data_8K6V
# 
_entry.id   8K6V 
# 
_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   8K6V         pdb_00008k6v 10.2210/pdb8k6v/pdb 
WWPDB D_1300039667 ?            ?                   
# 
_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                        8K6V 
_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 ADPR-Ub' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, T.T.' 1 ? 
primary 'Ouyang, S.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Actin gamma 1' 41838.766 1   ? ? ? ? 
2 polymer     man LnaB 40622.980 1   ? ? ? ? 
3 polymer     man Ubiquitin 8576.831  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    126 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
A ? 
2 'polypeptide(L)' no no 
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
;MSYQKIELSISLSLDSPKLDESDFILLSVKYLEKSLGKKKEFSGFFEDIEKLYFKQNYKEAIEKILDFCKKNESLLSEQV
VQRLAEVAPRLKSNPKDNESRRLYETLYADHLESVIKQESDLSVFNELRDSYNAVKPEYAVTHETEIKTLDEAKQFILSF
VMLNDNVELPLKAQSERYPKKDRSREELGNTPSANPGIMKPNSPNFTDNLVPVRDVPKIAINEKVAGGYSKTKPTTPFVA
SLSGTTYSLMVVLTDYIEKHKTDKDIEKKVNQIINLWISSYIKEGYHSYSEVVDVLTEPFLQSIFDKANIKLNYGVLDDT
HAEFRKAQDYVFGLTIQSAMHHELQERFKNKE
;
B ? 
3 'polypeptide(L)' no no MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
5 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
AR6 
6 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   GLU n 
1 4   GLU n 
1 5   ILE n 
1 6   ALA n 
1 7   ALA n 
1 8   LEU n 
1 9   VAL n 
1 10  ILE n 
1 11  ASP n 
1 12  ASN n 
1 13  GLY n 
1 14  SER n 
1 15  GLY n 
1 16  MET n 
1 17  CYS n 
1 18  LYS n 
1 19  ALA n 
1 20  GLY n 
1 21  PHE n 
1 22  ALA n 
1 23  GLY n 
1 24  ASP n 
1 25  ASP n 
1 26  ALA n 
1 27  PRO n 
1 28  ARG n 
1 29  ALA n 
1 30  VAL n 
1 31  PHE n 
1 32  PRO n 
1 33  SER n 
1 34  ILE n 
1 35  VAL n 
1 36  GLY n 
1 37  ARG n 
1 38  PRO n 
1 39  ARG n 
1 40  HIS n 
1 41  GLN n 
1 42  GLY n 
1 43  VAL n 
1 44  MET n 
1 45  VAL n 
1 46  GLY n 
1 47  MET n 
1 48  GLY n 
1 49  GLN n 
1 50  LYS n 
1 51  ASP n 
1 52  SER n 
1 53  TYR n 
1 54  VAL n 
1 55  GLY n 
1 56  ASP n 
1 57  GLU n 
1 58  ALA n 
1 59  GLN n 
1 60  SER n 
1 61  LYS n 
1 62  ARG n 
1 63  GLY n 
1 64  ILE n 
1 65  LEU n 
1 66  THR n 
1 67  LEU n 
1 68  LYS n 
1 69  TYR n 
1 70  PRO n 
1 71  ILE n 
1 72  GLU n 
1 73  HIS n 
1 74  GLY n 
1 75  ILE n 
1 76  VAL n 
1 77  THR n 
1 78  ASN n 
1 79  TRP n 
1 80  ASP n 
1 81  ASP n 
1 82  MET n 
1 83  GLU n 
1 84  LYS n 
1 85  ILE n 
1 86  TRP n 
1 87  HIS n 
1 88  HIS n 
1 89  THR n 
1 90  PHE n 
1 91  TYR n 
1 92  ASN n 
1 93  GLU n 
1 94  LEU n 
1 95  ARG n 
1 96  VAL n 
1 97  ALA n 
1 98  PRO n 
1 99  GLU n 
1 100 GLU n 
1 101 HIS n 
1 102 PRO n 
1 103 VAL n 
1 104 LEU n 
1 105 LEU n 
1 106 THR n 
1 107 GLU n 
1 108 ALA n 
1 109 PRO n 
1 110 LEU n 
1 111 ASN n 
1 112 PRO n 
1 113 LYS n 
1 114 ALA n 
1 115 ASN n 
1 116 ARG n 
1 117 GLU n 
1 118 LYS n 
1 119 MET n 
1 120 THR n 
1 121 GLN n 
1 122 ILE n 
1 123 MET n 
1 124 PHE n 
1 125 GLU n 
1 126 THR n 
1 127 PHE n 
1 128 ASN n 
1 129 THR n 
1 130 PRO n 
1 131 ALA n 
1 132 MET n 
1 133 TYR n 
1 134 VAL n 
1 135 ALA n 
1 136 ILE n 
1 137 GLN n 
1 138 ALA n 
1 139 VAL n 
1 140 LEU n 
1 141 SER n 
1 142 LEU n 
1 143 TYR n 
1 144 ALA n 
1 145 SER n 
1 146 GLY n 
1 147 ARG n 
1 148 THR n 
1 149 THR n 
1 150 GLY n 
1 151 ILE n 
1 152 VAL n 
1 153 MET n 
1 154 ASP n 
1 155 SER n 
1 156 GLY n 
1 157 ASP n 
1 158 GLY n 
1 159 VAL n 
1 160 THR n 
1 161 HIS n 
1 162 THR n 
1 163 VAL n 
1 164 PRO n 
1 165 ILE n 
1 166 TYR n 
1 167 GLU n 
1 168 GLY n 
1 169 TYR n 
1 170 ALA n 
1 171 LEU n 
1 172 PRO n 
1 173 HIS n 
1 174 ALA n 
1 175 ILE n 
1 176 LEU n 
1 177 ARG n 
1 178 LEU n 
1 179 ASP n 
1 180 LEU n 
1 181 ALA n 
1 182 GLY n 
1 183 ARG n 
1 184 ASP n 
1 185 LEU n 
1 186 THR n 
1 187 ASP n 
1 188 TYR n 
1 189 LEU n 
1 190 MET n 
1 191 LYS n 
1 192 ILE n 
1 193 LEU n 
1 194 THR n 
1 195 GLU n 
1 196 ARG n 
1 197 GLY n 
1 198 TYR n 
1 199 SER n 
1 200 PHE n 
1 201 THR n 
1 202 THR n 
1 203 THR n 
1 204 ALA n 
1 205 GLU n 
1 206 ARG n 
1 207 GLU n 
1 208 ILE n 
1 209 VAL n 
1 210 ARG n 
1 211 ASP n 
1 212 ILE n 
1 213 LYS n 
1 214 GLU n 
1 215 LYS n 
1 216 LEU n 
1 217 CYS n 
1 218 TYR n 
1 219 VAL n 
1 220 ALA n 
1 221 LEU n 
1 222 ASP n 
1 223 PHE n 
1 224 GLU n 
1 225 GLN n 
1 226 GLU n 
1 227 MET n 
1 228 ALA n 
1 229 THR n 
1 230 ALA n 
1 231 ALA n 
1 232 SER n 
1 233 SER n 
1 234 SER n 
1 235 SER n 
1 236 LEU n 
1 237 GLU n 
1 238 LYS n 
1 239 SER n 
1 240 TYR n 
1 241 GLU n 
1 242 LEU n 
1 243 PRO n 
1 244 ASP n 
1 245 GLY n 
1 246 GLN n 
1 247 VAL n 
1 248 ILE n 
1 249 THR n 
1 250 ILE n 
1 251 GLY n 
1 252 ASN n 
1 253 GLU n 
1 254 ARG n 
1 255 PHE n 
1 256 ARG n 
1 257 CYS n 
1 258 PRO n 
1 259 GLU n 
1 260 ALA n 
1 261 LEU n 
1 262 PHE n 
1 263 GLN n 
1 264 PRO n 
1 265 SER n 
1 266 PHE n 
1 267 LEU n 
1 268 GLY n 
1 269 MET n 
1 270 GLU n 
1 271 SER n 
1 272 CYS n 
1 273 GLY n 
1 274 ILE n 
1 275 HIS n 
1 276 GLU n 
1 277 THR n 
1 278 THR n 
1 279 PHE n 
1 280 ASN n 
1 281 SER n 
1 282 ILE n 
1 283 MET n 
1 284 LYS n 
1 285 CYS n 
1 286 ASP n 
1 287 VAL n 
1 288 ASP n 
1 289 ILE n 
1 290 ARG n 
1 291 LYS n 
1 292 ASP n 
1 293 LEU n 
1 294 TYR n 
1 295 ALA n 
1 296 ASN n 
1 297 THR n 
1 298 VAL n 
1 299 LEU n 
1 300 SER n 
1 301 GLY n 
1 302 GLY n 
1 303 THR n 
1 304 THR n 
1 305 MET n 
1 306 TYR n 
1 307 PRO n 
1 308 GLY n 
1 309 ILE n 
1 310 ALA n 
1 311 ASP n 
1 312 ARG n 
1 313 MET n 
1 314 GLN n 
1 315 LYS n 
1 316 GLU n 
1 317 ILE n 
1 318 THR n 
1 319 ALA n 
1 320 LEU n 
1 321 ALA n 
1 322 PRO n 
1 323 SER n 
1 324 THR n 
1 325 MET n 
1 326 LYS n 
1 327 ILE n 
1 328 LYS n 
1 329 ILE n 
1 330 ILE n 
1 331 ALA n 
1 332 PRO n 
1 333 PRO n 
1 334 GLU n 
1 335 ARG n 
1 336 LYS n 
1 337 TYR n 
1 338 SER n 
1 339 VAL n 
1 340 TRP n 
1 341 ILE n 
1 342 GLY n 
1 343 GLY n 
1 344 SER n 
1 345 ILE n 
1 346 LEU n 
1 347 ALA n 
1 348 SER n 
1 349 LEU n 
1 350 SER n 
1 351 THR n 
1 352 PHE n 
1 353 GLN n 
1 354 GLN n 
1 355 MET n 
1 356 TRP n 
1 357 ILE n 
1 358 SER n 
1 359 LYS n 
1 360 GLN n 
1 361 GLU n 
1 362 TYR n 
1 363 ASP n 
1 364 GLU n 
1 365 SER n 
1 366 GLY n 
1 367 PRO n 
1 368 SER n 
1 369 ILE n 
1 370 VAL n 
1 371 HIS n 
1 372 ARG n 
1 373 LYS n 
1 374 CYS n 
1 375 PHE n 
2 1   MET n 
2 2   SER n 
2 3   TYR n 
2 4   GLN n 
2 5   LYS n 
2 6   ILE n 
2 7   GLU n 
2 8   LEU n 
2 9   SER n 
2 10  ILE n 
2 11  SER n 
2 12  LEU n 
2 13  SER n 
2 14  LEU n 
2 15  ASP n 
2 16  SER n 
2 17  PRO n 
2 18  LYS n 
2 19  LEU n 
2 20  ASP n 
2 21  GLU n 
2 22  SER n 
2 23  ASP n 
2 24  PHE n 
2 25  ILE n 
2 26  LEU n 
2 27  LEU n 
2 28  SER n 
2 29  VAL n 
2 30  LYS n 
2 31  TYR n 
2 32  LEU n 
2 33  GLU n 
2 34  LYS n 
2 35  SER n 
2 36  LEU n 
2 37  GLY n 
2 38  LYS n 
2 39  LYS n 
2 40  LYS n 
2 41  GLU n 
2 42  PHE n 
2 43  SER n 
2 44  GLY n 
2 45  PHE n 
2 46  PHE n 
2 47  GLU n 
2 48  ASP n 
2 49  ILE n 
2 50  GLU n 
2 51  LYS n 
2 52  LEU n 
2 53  TYR n 
2 54  PHE n 
2 55  LYS n 
2 56  GLN n 
2 57  ASN n 
2 58  TYR n 
2 59  LYS n 
2 60  GLU n 
2 61  ALA n 
2 62  ILE n 
2 63  GLU n 
2 64  LYS n 
2 65  ILE n 
2 66  LEU n 
2 67  ASP n 
2 68  PHE n 
2 69  CYS n 
2 70  LYS n 
2 71  LYS n 
2 72  ASN n 
2 73  GLU n 
2 74  SER n 
2 75  LEU n 
2 76  LEU n 
2 77  SER n 
2 78  GLU n 
2 79  GLN n 
2 80  VAL n 
2 81  VAL n 
2 82  GLN n 
2 83  ARG n 
2 84  LEU n 
2 85  ALA n 
2 86  GLU n 
2 87  VAL n 
2 88  ALA n 
2 89  PRO n 
2 90  ARG n 
2 91  LEU n 
2 92  LYS n 
2 93  SER n 
2 94  ASN n 
2 95  PRO n 
2 96  LYS n 
2 97  ASP n 
2 98  ASN n 
2 99  GLU n 
2 100 SER n 
2 101 ARG n 
2 102 ARG n 
2 103 LEU n 
2 104 TYR n 
2 105 GLU n 
2 106 THR n 
2 107 LEU n 
2 108 TYR n 
2 109 ALA n 
2 110 ASP n 
2 111 HIS n 
2 112 LEU n 
2 113 GLU n 
2 114 SER n 
2 115 VAL n 
2 116 ILE n 
2 117 LYS n 
2 118 GLN n 
2 119 GLU n 
2 120 SER n 
2 121 ASP n 
2 122 LEU n 
2 123 SER n 
2 124 VAL n 
2 125 PHE n 
2 126 ASN n 
2 127 GLU n 
2 128 LEU n 
2 129 ARG n 
2 130 ASP n 
2 131 SER n 
2 132 TYR n 
2 133 ASN n 
2 134 ALA n 
2 135 VAL n 
2 136 LYS n 
2 137 PRO n 
2 138 GLU n 
2 139 TYR n 
2 140 ALA n 
2 141 VAL n 
2 142 THR n 
2 143 HIS n 
2 144 GLU n 
2 145 THR n 
2 146 GLU n 
2 147 ILE n 
2 148 LYS n 
2 149 THR n 
2 150 LEU n 
2 151 ASP n 
2 152 GLU n 
2 153 ALA n 
2 154 LYS n 
2 155 GLN n 
2 156 PHE n 
2 157 ILE n 
2 158 LEU n 
2 159 SER n 
2 160 PHE n 
2 161 VAL n 
2 162 MET n 
2 163 LEU n 
2 164 ASN n 
2 165 ASP n 
2 166 ASN n 
2 167 VAL n 
2 168 GLU n 
2 169 LEU n 
2 170 PRO n 
2 171 LEU n 
2 172 LYS n 
2 173 ALA n 
2 174 GLN n 
2 175 SER n 
2 176 GLU n 
2 177 ARG n 
2 178 TYR n 
2 179 PRO n 
2 180 LYS n 
2 181 LYS n 
2 182 ASP n 
2 183 ARG n 
2 184 SER n 
2 185 ARG n 
2 186 GLU n 
2 187 GLU n 
2 188 LEU n 
2 189 GLY n 
2 190 ASN n 
2 191 THR n 
2 192 PRO n 
2 193 SER n 
2 194 ALA n 
2 195 ASN n 
2 196 PRO n 
2 197 GLY n 
2 198 ILE n 
2 199 MET n 
2 200 LYS n 
2 201 PRO n 
2 202 ASN n 
2 203 SER n 
2 204 PRO n 
2 205 ASN n 
2 206 PHE n 
2 207 THR n 
2 208 ASP n 
2 209 ASN n 
2 210 LEU n 
2 211 VAL n 
2 212 PRO n 
2 213 VAL n 
2 214 ARG n 
2 215 ASP n 
2 216 VAL n 
2 217 PRO n 
2 218 LYS n 
2 219 ILE n 
2 220 ALA n 
2 221 ILE n 
2 222 ASN n 
2 223 GLU n 
2 224 LYS n 
2 225 VAL n 
2 226 ALA n 
2 227 GLY n 
2 228 GLY n 
2 229 TYR n 
2 230 SER n 
2 231 LYS n 
2 232 THR n 
2 233 LYS n 
2 234 PRO n 
2 235 THR n 
2 236 THR n 
2 237 PRO n 
2 238 PHE n 
2 239 VAL n 
2 240 ALA n 
2 241 SER n 
2 242 LEU n 
2 243 SER n 
2 244 GLY n 
2 245 THR n 
2 246 THR n 
2 247 TYR n 
2 248 SER n 
2 249 LEU n 
2 250 MET n 
2 251 VAL n 
2 252 VAL n 
2 253 LEU n 
2 254 THR n 
2 255 ASP n 
2 256 TYR n 
2 257 ILE n 
2 258 GLU n 
2 259 LYS n 
2 260 HIS n 
2 261 LYS n 
2 262 THR n 
2 263 ASP n 
2 264 LYS n 
2 265 ASP n 
2 266 ILE n 
2 267 GLU n 
2 268 LYS n 
2 269 LYS n 
2 270 VAL n 
2 271 ASN n 
2 272 GLN n 
2 273 ILE n 
2 274 ILE n 
2 275 ASN n 
2 276 LEU n 
2 277 TRP n 
2 278 ILE n 
2 279 SER n 
2 280 SER n 
2 281 TYR n 
2 282 ILE n 
2 283 LYS n 
2 284 GLU n 
2 285 GLY n 
2 286 TYR n 
2 287 HIS n 
2 288 SER n 
2 289 TYR n 
2 290 SER n 
2 291 GLU n 
2 292 VAL n 
2 293 VAL n 
2 294 ASP n 
2 295 VAL n 
2 296 LEU n 
2 297 THR n 
2 298 GLU n 
2 299 PRO n 
2 300 PHE n 
2 301 LEU n 
2 302 GLN n 
2 303 SER n 
2 304 ILE n 
2 305 PHE n 
2 306 ASP n 
2 307 LYS n 
2 308 ALA n 
2 309 ASN n 
2 310 ILE n 
2 311 LYS n 
2 312 LEU n 
2 313 ASN n 
2 314 TYR n 
2 315 GLY n 
2 316 VAL n 
2 317 LEU n 
2 318 ASP n 
2 319 ASP n 
2 320 THR n 
2 321 HIS n 
2 322 ALA n 
2 323 GLU n 
2 324 PHE n 
2 325 ARG n 
2 326 LYS n 
2 327 ALA n 
2 328 GLN n 
2 329 ASP n 
2 330 TYR n 
2 331 VAL n 
2 332 PHE n 
2 333 GLY n 
2 334 LEU n 
2 335 THR n 
2 336 ILE n 
2 337 GLN n 
2 338 SER n 
2 339 ALA n 
2 340 MET n 
2 341 HIS n 
2 342 HIS n 
2 343 GLU n 
2 344 LEU n 
2 345 GLN n 
2 346 GLU n 
2 347 ARG n 
2 348 PHE n 
2 349 LYS n 
2 350 ASN n 
2 351 LYS n 
2 352 GLU n 
3 1   MET n 
3 2   GLN n 
3 3   ILE n 
3 4   PHE n 
3 5   VAL n 
3 6   LYS n 
3 7   THR n 
3 8   LEU n 
3 9   THR n 
3 10  GLY n 
3 11  LYS n 
3 12  THR n 
3 13  ILE n 
3 14  THR n 
3 15  LEU n 
3 16  GLU n 
3 17  VAL n 
3 18  GLU n 
3 19  PRO n 
3 20  SER n 
3 21  ASP n 
3 22  THR n 
3 23  ILE n 
3 24  GLU n 
3 25  ASN n 
3 26  VAL n 
3 27  LYS n 
3 28  ALA n 
3 29  LYS n 
3 30  ILE n 
3 31  GLN n 
3 32  ASP n 
3 33  LYS n 
3 34  GLU n 
3 35  GLY n 
3 36  ILE n 
3 37  PRO n 
3 38  PRO n 
3 39  ASP n 
3 40  GLN n 
3 41  GLN n 
3 42  ARG n 
3 43  LEU n 
3 44  ILE n 
3 45  PHE n 
3 46  ALA n 
3 47  GLY n 
3 48  LYS n 
3 49  GLN n 
3 50  LEU n 
3 51  GLU n 
3 52  ASP n 
3 53  GLY n 
3 54  ARG n 
3 55  THR n 
3 56  LEU n 
3 57  SER n 
3 58  ASP n 
3 59  TYR n 
3 60  ASN n 
3 61  ILE n 
3 62  GLN n 
3 63  LYS n 
3 64  GLU n 
3 65  SER n 
3 66  THR n 
3 67  LEU n 
3 68  HIS n 
3 69  LEU n 
3 70  VAL n 
3 71  LEU n 
3 72  ARG n 
3 73  LEU n 
3 74  ARG n 
3 75  GLY n 
3 76  GLY n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
2 1 sample 'Biological sequence' 1 352 ?     ? ?   ? ? ? ? ? ? Legionella     445  ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 76  human ? UBB ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           375 
_entity_src_nat.common_name                rabbit 
_entity_src_nat.pdbx_organism_scientific   'Oryctolagus cuniculus' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9986 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                           'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                           'C10 H17 N6 O12 P3' 506.196 
AR6 non-polymer         . 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
Adenosine-5-Diphosphoribose 'C15 H23 N5 O14 P2' 559.316 
ARG 'L-peptide linking' y ARGININE ?                           'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                           'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                           'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                           'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                           'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                           'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                           'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?                           'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?                           'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                           'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                           'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                           'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                           'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                           'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                           'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                           'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                           'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                           'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                           'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                           'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   ILE 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  CYS 17  17  17  CYS CYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  MET 44  44  44  MET MET A . n 
A 1 45  VAL 45  45  45  VAL VAL A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  MET 47  47  ?   ?   ?   A . n 
A 1 48  GLY 48  48  ?   ?   ?   A . n 
A 1 49  GLN 49  49  ?   ?   ?   A . n 
A 1 50  LYS 50  50  ?   ?   ?   A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ARG 62  62  62  ARG ALA A . n 
A 1 63  GLY 63  63  63  GLY ALA A . n 
A 1 64  ILE 64  64  64  ILE ALA A . n 
A 1 65  LEU 65  65  65  LEU ALA A . n 
A 1 66  THR 66  66  66  THR ALA A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  HIS 73  73  73  HIS HIS A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 MET 132 132 132 MET MET A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 TYR 143 143 143 TYR TYR A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 ARG 147 147 147 ARG ARG A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 MET 153 153 153 MET MET A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 ARG 206 206 206 ARG ARG A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 CYS 217 217 217 CYS CYS A . n 
A 1 218 TYR 218 218 218 TYR TYR A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 GLN 225 225 225 GLN GLN A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 TYR 240 240 240 TYR TYR A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ILE 248 248 248 ILE ILE A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 PHE 255 255 255 PHE PHE A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 CYS 257 257 257 CYS CYS A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 GLU 259 259 259 GLU GLU A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 MET 269 269 269 MET MET A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 CYS 272 272 272 CYS CYS A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 HIS 275 275 275 HIS HIS A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 ASN 280 280 280 ASN ASN A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 MET 283 283 283 MET MET A . n 
A 1 284 LYS 284 284 284 LYS LYS A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 TYR 294 294 294 TYR TYR A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 THR 297 297 297 THR THR A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 MET 305 305 305 MET MET A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 ALA 310 310 310 ALA ALA A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 ARG 312 312 312 ARG ARG A . n 
A 1 313 MET 313 313 313 MET MET A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 GLU 316 316 316 GLU GLU A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 PRO 322 322 322 PRO PRO A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 THR 324 324 324 THR THR A . n 
A 1 325 MET 325 325 325 MET MET A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 LYS 328 328 328 LYS LYS A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 PRO 333 333 333 PRO PRO A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 ARG 335 335 335 ARG ARG A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 TYR 337 337 337 TYR TYR A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 TRP 340 340 340 TRP TRP A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLY 343 343 343 GLY GLY A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 PHE 352 352 352 PHE PHE A . n 
A 1 353 GLN 353 353 353 GLN GLN A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 MET 355 355 355 MET MET A . n 
A 1 356 TRP 356 356 356 TRP TRP A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 GLN 360 360 360 GLN GLN A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 TYR 362 362 362 TYR TYR A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 SER 365 365 365 SER SER A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 SER 368 368 368 SER SER A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 HIS 371 371 371 HIS HIS A . n 
A 1 372 ARG 372 372 372 ARG ARG A . n 
A 1 373 LYS 373 373 373 LYS LYS A . n 
A 1 374 CYS 374 374 374 CYS CYS A . n 
A 1 375 PHE 375 375 375 PHE PHE A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   ?   ?   ?   B . n 
B 2 3   TYR 3   3   ?   ?   ?   B . n 
B 2 4   GLN 4   4   ?   ?   ?   B . n 
B 2 5   LYS 5   5   ?   ?   ?   B . n 
B 2 6   ILE 6   6   ?   ?   ?   B . n 
B 2 7   GLU 7   7   7   GLU GLU B . n 
B 2 8   LEU 8   8   8   LEU LEU B . n 
B 2 9   SER 9   9   9   SER SER B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  SER 11  11  11  SER SER B . n 
B 2 12  LEU 12  12  12  LEU LEU B . n 
B 2 13  SER 13  13  13  SER SER B . n 
B 2 14  LEU 14  14  14  LEU LEU B . n 
B 2 15  ASP 15  15  15  ASP ASP B . n 
B 2 16  SER 16  16  16  SER SER B . n 
B 2 17  PRO 17  17  17  PRO PRO B . n 
B 2 18  LYS 18  18  18  LYS LYS B . n 
B 2 19  LEU 19  19  19  LEU LEU B . n 
B 2 20  ASP 20  20  20  ASP ASP B . n 
B 2 21  GLU 21  21  21  GLU GLU B . n 
B 2 22  SER 22  22  22  SER SER B . n 
B 2 23  ASP 23  23  23  ASP ASP B . n 
B 2 24  PHE 24  24  24  PHE PHE B . n 
B 2 25  ILE 25  25  25  ILE ILE B . n 
B 2 26  LEU 26  26  26  LEU LEU B . n 
B 2 27  LEU 27  27  27  LEU LEU B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  VAL 29  29  29  VAL VAL B . n 
B 2 30  LYS 30  30  30  LYS LYS B . n 
B 2 31  TYR 31  31  31  TYR TYR B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  GLU 33  33  33  GLU GLU B . n 
B 2 34  LYS 34  34  34  LYS LYS B . n 
B 2 35  SER 35  35  35  SER SER B . n 
B 2 36  LEU 36  36  36  LEU LEU B . n 
B 2 37  GLY 37  37  37  GLY GLY B . n 
B 2 38  LYS 38  38  38  LYS LYS B . n 
B 2 39  LYS 39  39  39  LYS LYS B . n 
B 2 40  LYS 40  40  40  LYS LYS B . n 
B 2 41  GLU 41  41  41  GLU GLU B . n 
B 2 42  PHE 42  42  42  PHE PHE B . n 
B 2 43  SER 43  43  43  SER SER B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  PHE 45  45  45  PHE PHE B . n 
B 2 46  PHE 46  46  46  PHE PHE B . n 
B 2 47  GLU 47  47  47  GLU GLU B . n 
B 2 48  ASP 48  48  48  ASP ASP B . n 
B 2 49  ILE 49  49  49  ILE ILE B . n 
B 2 50  GLU 50  50  50  GLU GLU B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  LEU 52  52  52  LEU LEU B . n 
B 2 53  TYR 53  53  53  TYR TYR B . n 
B 2 54  PHE 54  54  54  PHE PHE B . n 
B 2 55  LYS 55  55  55  LYS LYS B . n 
B 2 56  GLN 56  56  56  GLN GLN B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  TYR 58  58  58  TYR TYR B . n 
B 2 59  LYS 59  59  59  LYS LYS B . n 
B 2 60  GLU 60  60  60  GLU GLU B . n 
B 2 61  ALA 61  61  61  ALA ALA B . n 
B 2 62  ILE 62  62  62  ILE ILE B . n 
B 2 63  GLU 63  63  63  GLU GLU B . n 
B 2 64  LYS 64  64  64  LYS LYS B . n 
B 2 65  ILE 65  65  65  ILE ILE B . n 
B 2 66  LEU 66  66  66  LEU LEU B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  PHE 68  68  68  PHE PHE B . n 
B 2 69  CYS 69  69  69  CYS CYS B . n 
B 2 70  LYS 70  70  70  LYS LYS B . n 
B 2 71  LYS 71  71  71  LYS LYS B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  GLU 73  73  73  GLU GLU B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  LEU 75  75  75  LEU LEU B . n 
B 2 76  LEU 76  76  76  LEU LEU B . n 
B 2 77  SER 77  77  77  SER SER B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  GLN 79  79  79  GLN GLN B . n 
B 2 80  VAL 80  80  80  VAL VAL B . n 
B 2 81  VAL 81  81  81  VAL VAL B . n 
B 2 82  GLN 82  82  82  GLN GLN B . n 
B 2 83  ARG 83  83  83  ARG ARG B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  ALA 85  85  85  ALA ALA B . n 
B 2 86  GLU 86  86  86  GLU GLU B . n 
B 2 87  VAL 87  87  87  VAL VAL B . n 
B 2 88  ALA 88  88  88  ALA ALA B . n 
B 2 89  PRO 89  89  89  PRO PRO B . n 
B 2 90  ARG 90  90  90  ARG ARG B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  LYS 92  92  92  LYS LYS B . n 
B 2 93  SER 93  93  93  SER SER B . n 
B 2 94  ASN 94  94  94  ASN ASN B . n 
B 2 95  PRO 95  95  95  PRO PRO B . n 
B 2 96  LYS 96  96  96  LYS LYS B . n 
B 2 97  ASP 97  97  97  ASP ASP B . n 
B 2 98  ASN 98  98  98  ASN ASN B . n 
B 2 99  GLU 99  99  99  GLU GLU B . n 
B 2 100 SER 100 100 100 SER SER B . n 
B 2 101 ARG 101 101 101 ARG ARG B . n 
B 2 102 ARG 102 102 102 ARG ARG B . n 
B 2 103 LEU 103 103 103 LEU LEU B . n 
B 2 104 TYR 104 104 104 TYR TYR B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 THR 106 106 106 THR THR B . n 
B 2 107 LEU 107 107 107 LEU LEU B . n 
B 2 108 TYR 108 108 108 TYR TYR B . n 
B 2 109 ALA 109 109 109 ALA ALA B . n 
B 2 110 ASP 110 110 110 ASP ASP B . n 
B 2 111 HIS 111 111 111 HIS HIS B . n 
B 2 112 LEU 112 112 112 LEU LEU B . n 
B 2 113 GLU 113 113 113 GLU GLU B . n 
B 2 114 SER 114 114 114 SER SER B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 ILE 116 116 116 ILE ILE B . n 
B 2 117 LYS 117 117 117 LYS LYS B . n 
B 2 118 GLN 118 118 118 GLN GLN B . n 
B 2 119 GLU 119 119 119 GLU GLU B . n 
B 2 120 SER 120 120 120 SER SER B . n 
B 2 121 ASP 121 121 121 ASP ASP B . n 
B 2 122 LEU 122 122 122 LEU LEU B . n 
B 2 123 SER 123 123 123 SER SER B . n 
B 2 124 VAL 124 124 124 VAL VAL B . n 
B 2 125 PHE 125 125 125 PHE PHE B . n 
B 2 126 ASN 126 126 126 ASN ASN B . n 
B 2 127 GLU 127 127 127 GLU GLU B . n 
B 2 128 LEU 128 128 128 LEU LEU B . n 
B 2 129 ARG 129 129 129 ARG ARG B . n 
B 2 130 ASP 130 130 130 ASP ASP B . n 
B 2 131 SER 131 131 131 SER SER B . n 
B 2 132 TYR 132 132 132 TYR TYR B . n 
B 2 133 ASN 133 133 133 ASN ASN B . n 
B 2 134 ALA 134 134 134 ALA ALA B . n 
B 2 135 VAL 135 135 135 VAL VAL B . n 
B 2 136 LYS 136 136 136 LYS LYS B . n 
B 2 137 PRO 137 137 137 PRO PRO B . n 
B 2 138 GLU 138 138 138 GLU GLU B . n 
B 2 139 TYR 139 139 139 TYR TYR B . n 
B 2 140 ALA 140 140 140 ALA ALA B . n 
B 2 141 VAL 141 141 141 VAL VAL B . n 
B 2 142 THR 142 142 142 THR THR B . n 
B 2 143 HIS 143 143 143 HIS HIS B . n 
B 2 144 GLU 144 144 144 GLU GLU B . n 
B 2 145 THR 145 145 145 THR THR B . n 
B 2 146 GLU 146 146 146 GLU GLU B . n 
B 2 147 ILE 147 147 147 ILE ILE B . n 
B 2 148 LYS 148 148 148 LYS LYS B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 LEU 150 150 150 LEU LEU B . n 
B 2 151 ASP 151 151 151 ASP ASP B . n 
B 2 152 GLU 152 152 152 GLU GLU B . n 
B 2 153 ALA 153 153 153 ALA ALA B . n 
B 2 154 LYS 154 154 154 LYS LYS B . n 
B 2 155 GLN 155 155 155 GLN GLN B . n 
B 2 156 PHE 156 156 156 PHE PHE B . n 
B 2 157 ILE 157 157 157 ILE ILE B . n 
B 2 158 LEU 158 158 158 LEU LEU B . n 
B 2 159 SER 159 159 159 SER SER B . n 
B 2 160 PHE 160 160 160 PHE PHE B . n 
B 2 161 VAL 161 161 161 VAL VAL B . n 
B 2 162 MET 162 162 162 MET MET B . n 
B 2 163 LEU 163 163 163 LEU LEU B . n 
B 2 164 ASN 164 164 164 ASN ASN B . n 
B 2 165 ASP 165 165 165 ASP ASP B . n 
B 2 166 ASN 166 166 166 ASN ASN B . n 
B 2 167 VAL 167 167 167 VAL VAL B . n 
B 2 168 GLU 168 168 168 GLU GLU B . n 
B 2 169 LEU 169 169 169 LEU LEU B . n 
B 2 170 PRO 170 170 170 PRO PRO B . n 
B 2 171 LEU 171 171 171 LEU LEU B . n 
B 2 172 LYS 172 172 172 LYS LYS B . n 
B 2 173 ALA 173 173 173 ALA ALA B . n 
B 2 174 GLN 174 174 174 GLN GLN B . n 
B 2 175 SER 175 175 175 SER SER B . n 
B 2 176 GLU 176 176 176 GLU GLU B . n 
B 2 177 ARG 177 177 177 ARG ARG B . n 
B 2 178 TYR 178 178 178 TYR TYR B . n 
B 2 179 PRO 179 179 179 PRO PRO B . n 
B 2 180 LYS 180 180 180 LYS LYS B . n 
B 2 181 LYS 181 181 181 LYS LYS B . n 
B 2 182 ASP 182 182 182 ASP ASP B . n 
B 2 183 ARG 183 183 183 ARG ARG B . n 
B 2 184 SER 184 184 184 SER SER B . n 
B 2 185 ARG 185 185 185 ARG ARG B . n 
B 2 186 GLU 186 186 186 GLU GLU B . n 
B 2 187 GLU 187 187 187 GLU GLU B . n 
B 2 188 LEU 188 188 188 LEU LEU B . n 
B 2 189 GLY 189 189 189 GLY GLY B . n 
B 2 190 ASN 190 190 190 ASN ASN B . n 
B 2 191 THR 191 191 191 THR THR B . n 
B 2 192 PRO 192 192 192 PRO PRO B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 ALA 194 194 194 ALA ALA B . n 
B 2 195 ASN 195 195 195 ASN ASN B . n 
B 2 196 PRO 196 196 196 PRO PRO B . n 
B 2 197 GLY 197 197 197 GLY GLY B . n 
B 2 198 ILE 198 198 198 ILE ILE B . n 
B 2 199 MET 199 199 199 MET MET B . n 
B 2 200 LYS 200 200 200 LYS LYS B . n 
B 2 201 PRO 201 201 201 PRO PRO B . n 
B 2 202 ASN 202 202 202 ASN ASN B . n 
B 2 203 SER 203 203 203 SER SER B . n 
B 2 204 PRO 204 204 204 PRO PRO B . n 
B 2 205 ASN 205 205 205 ASN ASN B . n 
B 2 206 PHE 206 206 206 PHE PHE B . n 
B 2 207 THR 207 207 207 THR THR B . n 
B 2 208 ASP 208 208 208 ASP ASP B . n 
B 2 209 ASN 209 209 209 ASN ASN B . n 
B 2 210 LEU 210 210 210 LEU LEU B . n 
B 2 211 VAL 211 211 211 VAL VAL B . n 
B 2 212 PRO 212 212 212 PRO PRO B . n 
B 2 213 VAL 213 213 213 VAL VAL B . n 
B 2 214 ARG 214 214 214 ARG ARG B . n 
B 2 215 ASP 215 215 215 ASP ASP B . n 
B 2 216 VAL 216 216 216 VAL VAL B . n 
B 2 217 PRO 217 217 217 PRO PRO B . n 
B 2 218 LYS 218 218 218 LYS LYS B . n 
B 2 219 ILE 219 219 219 ILE ILE B . n 
B 2 220 ALA 220 220 220 ALA ALA B . n 
B 2 221 ILE 221 221 221 ILE ILE B . n 
B 2 222 ASN 222 222 222 ASN ASN B . n 
B 2 223 GLU 223 223 223 GLU GLU B . n 
B 2 224 LYS 224 224 224 LYS LYS B . n 
B 2 225 VAL 225 225 225 VAL VAL B . n 
B 2 226 ALA 226 226 226 ALA ALA B . n 
B 2 227 GLY 227 227 227 GLY GLY B . n 
B 2 228 GLY 228 228 228 GLY GLY B . n 
B 2 229 TYR 229 229 229 TYR TYR B . n 
B 2 230 SER 230 230 230 SER SER B . n 
B 2 231 LYS 231 231 231 LYS LYS B . n 
B 2 232 THR 232 232 232 THR THR B . n 
B 2 233 LYS 233 233 233 LYS LYS B . n 
B 2 234 PRO 234 234 234 PRO PRO B . n 
B 2 235 THR 235 235 235 THR THR B . n 
B 2 236 THR 236 236 236 THR THR B . n 
B 2 237 PRO 237 237 237 PRO PRO B . n 
B 2 238 PHE 238 238 238 PHE PHE B . n 
B 2 239 VAL 239 239 239 VAL VAL B . n 
B 2 240 ALA 240 240 240 ALA ALA B . n 
B 2 241 SER 241 241 241 SER SER B . n 
B 2 242 LEU 242 242 242 LEU LEU B . n 
B 2 243 SER 243 243 243 SER SER B . n 
B 2 244 GLY 244 244 244 GLY GLY B . n 
B 2 245 THR 245 245 245 THR THR B . n 
B 2 246 THR 246 246 246 THR THR B . n 
B 2 247 TYR 247 247 247 TYR TYR B . n 
B 2 248 SER 248 248 248 SER SER B . n 
B 2 249 LEU 249 249 249 LEU LEU B . n 
B 2 250 MET 250 250 250 MET MET B . n 
B 2 251 VAL 251 251 251 VAL VAL B . n 
B 2 252 VAL 252 252 252 VAL VAL B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 THR 254 254 254 THR THR B . n 
B 2 255 ASP 255 255 255 ASP ASP B . n 
B 2 256 TYR 256 256 256 TYR TYR B . n 
B 2 257 ILE 257 257 257 ILE ILE B . n 
B 2 258 GLU 258 258 258 GLU GLU B . n 
B 2 259 LYS 259 259 259 LYS LYS B . n 
B 2 260 HIS 260 260 260 HIS HIS B . n 
B 2 261 LYS 261 261 261 LYS LYS B . n 
B 2 262 THR 262 262 262 THR THR B . n 
B 2 263 ASP 263 263 263 ASP ASP B . n 
B 2 264 LYS 264 264 264 LYS LYS B . n 
B 2 265 ASP 265 265 265 ASP ASP B . n 
B 2 266 ILE 266 266 266 ILE ILE B . n 
B 2 267 GLU 267 267 267 GLU GLU B . n 
B 2 268 LYS 268 268 268 LYS LYS B . n 
B 2 269 LYS 269 269 269 LYS LYS B . n 
B 2 270 VAL 270 270 270 VAL VAL B . n 
B 2 271 ASN 271 271 271 ASN ASN B . n 
B 2 272 GLN 272 272 272 GLN GLN B . n 
B 2 273 ILE 273 273 273 ILE ILE B . n 
B 2 274 ILE 274 274 274 ILE ILE B . n 
B 2 275 ASN 275 275 275 ASN ASN B . n 
B 2 276 LEU 276 276 276 LEU LEU B . n 
B 2 277 TRP 277 277 277 TRP TRP B . n 
B 2 278 ILE 278 278 278 ILE ILE B . n 
B 2 279 SER 279 279 279 SER SER B . n 
B 2 280 SER 280 280 280 SER SER B . n 
B 2 281 TYR 281 281 281 TYR TYR B . n 
B 2 282 ILE 282 282 282 ILE ILE B . n 
B 2 283 LYS 283 283 283 LYS LYS B . n 
B 2 284 GLU 284 284 284 GLU GLU B . n 
B 2 285 GLY 285 285 285 GLY GLY B . n 
B 2 286 TYR 286 286 286 TYR TYR B . n 
B 2 287 HIS 287 287 287 HIS HIS B . n 
B 2 288 SER 288 288 288 SER SER B . n 
B 2 289 TYR 289 289 289 TYR TYR B . n 
B 2 290 SER 290 290 290 SER SER B . n 
B 2 291 GLU 291 291 291 GLU GLU B . n 
B 2 292 VAL 292 292 292 VAL VAL B . n 
B 2 293 VAL 293 293 293 VAL VAL B . n 
B 2 294 ASP 294 294 294 ASP ASP B . n 
B 2 295 VAL 295 295 295 VAL VAL B . n 
B 2 296 LEU 296 296 296 LEU LEU B . n 
B 2 297 THR 297 297 297 THR THR B . n 
B 2 298 GLU 298 298 298 GLU GLU B . n 
B 2 299 PRO 299 299 299 PRO PRO B . n 
B 2 300 PHE 300 300 300 PHE PHE B . n 
B 2 301 LEU 301 301 301 LEU LEU B . n 
B 2 302 GLN 302 302 302 GLN GLN B . n 
B 2 303 SER 303 303 303 SER SER B . n 
B 2 304 ILE 304 304 304 ILE ILE B . n 
B 2 305 PHE 305 305 305 PHE PHE B . n 
B 2 306 ASP 306 306 306 ASP ASP B . n 
B 2 307 LYS 307 307 307 LYS LYS B . n 
B 2 308 ALA 308 308 308 ALA ALA B . n 
B 2 309 ASN 309 309 309 ASN ASN B . n 
B 2 310 ILE 310 310 310 ILE ILE B . n 
B 2 311 LYS 311 311 311 LYS LYS B . n 
B 2 312 LEU 312 312 312 LEU LEU B . n 
B 2 313 ASN 313 313 313 ASN ASN B . n 
B 2 314 TYR 314 314 314 TYR TYR B . n 
B 2 315 GLY 315 315 315 GLY GLY B . n 
B 2 316 VAL 316 316 316 VAL VAL B . n 
B 2 317 LEU 317 317 317 LEU LEU B . n 
B 2 318 ASP 318 318 318 ASP ASP B . n 
B 2 319 ASP 319 319 319 ASP ASP B . n 
B 2 320 THR 320 320 320 THR THR B . n 
B 2 321 HIS 321 321 321 HIS HIS B . n 
B 2 322 ALA 322 322 322 ALA ALA B . n 
B 2 323 GLU 323 323 323 GLU GLU B . n 
B 2 324 PHE 324 324 324 PHE PHE B . n 
B 2 325 ARG 325 325 325 ARG ARG B . n 
B 2 326 LYS 326 326 326 LYS LYS B . n 
B 2 327 ALA 327 327 327 ALA ALA B . n 
B 2 328 GLN 328 328 328 GLN GLN B . n 
B 2 329 ASP 329 329 329 ASP ASP B . n 
B 2 330 TYR 330 330 330 TYR TYR B . n 
B 2 331 VAL 331 331 331 VAL VAL B . n 
B 2 332 PHE 332 332 332 PHE PHE B . n 
B 2 333 GLY 333 333 333 GLY GLY B . n 
B 2 334 LEU 334 334 334 LEU LEU B . n 
B 2 335 THR 335 335 335 THR THR B . n 
B 2 336 ILE 336 336 336 ILE ILE B . n 
B 2 337 GLN 337 337 337 GLN GLN B . n 
B 2 338 SER 338 338 338 SER SER B . n 
B 2 339 ALA 339 339 339 ALA ALA B . n 
B 2 340 MET 340 340 340 MET MET B . n 
B 2 341 HIS 341 341 341 HIS HIS B . n 
B 2 342 HIS 342 342 342 HIS HIS B . n 
B 2 343 GLU 343 343 343 GLU GLU B . n 
B 2 344 LEU 344 344 344 LEU LEU B . n 
B 2 345 GLN 345 345 345 GLN GLN B . n 
B 2 346 GLU 346 346 346 GLU GLU B . n 
B 2 347 ARG 347 347 347 ARG ARG B . n 
B 2 348 PHE 348 348 348 PHE PHE B . n 
B 2 349 LYS 349 349 349 LYS LYS B . n 
B 2 350 ASN 350 350 350 ASN ASN B . n 
B 2 351 LYS 351 351 351 LYS LYS B . n 
B 2 352 GLU 352 352 352 GLU GLU B . n 
C 3 1   MET 1   1   1   MET MET C . n 
C 3 2   GLN 2   2   2   GLN GLN C . n 
C 3 3   ILE 3   3   3   ILE ILE C . n 
C 3 4   PHE 4   4   4   PHE PHE C . n 
C 3 5   VAL 5   5   5   VAL VAL C . n 
C 3 6   LYS 6   6   6   LYS LYS C . n 
C 3 7   THR 7   7   7   THR THR C . n 
C 3 8   LEU 8   8   8   LEU LEU C . n 
C 3 9   THR 9   9   9   THR THR C . n 
C 3 10  GLY 10  10  10  GLY GLY C . n 
C 3 11  LYS 11  11  11  LYS LYS C . n 
C 3 12  THR 12  12  12  THR THR C . n 
C 3 13  ILE 13  13  13  ILE ILE C . n 
C 3 14  THR 14  14  14  THR THR C . n 
C 3 15  LEU 15  15  15  LEU LEU C . n 
C 3 16  GLU 16  16  16  GLU GLU C . n 
C 3 17  VAL 17  17  17  VAL VAL C . n 
C 3 18  GLU 18  18  18  GLU GLU C . n 
C 3 19  PRO 19  19  19  PRO PRO C . n 
C 3 20  SER 20  20  20  SER SER C . n 
C 3 21  ASP 21  21  21  ASP ASP C . n 
C 3 22  THR 22  22  22  THR THR C . n 
C 3 23  ILE 23  23  23  ILE ILE C . n 
C 3 24  GLU 24  24  24  GLU GLU C . n 
C 3 25  ASN 25  25  25  ASN ASN C . n 
C 3 26  VAL 26  26  26  VAL VAL C . n 
C 3 27  LYS 27  27  27  LYS LYS C . n 
C 3 28  ALA 28  28  28  ALA ALA C . n 
C 3 29  LYS 29  29  29  LYS LYS C . n 
C 3 30  ILE 30  30  30  ILE ILE C . n 
C 3 31  GLN 31  31  31  GLN GLN C . n 
C 3 32  ASP 32  32  32  ASP ASP C . n 
C 3 33  LYS 33  33  33  LYS LYS C . n 
C 3 34  GLU 34  34  34  GLU GLU C . n 
C 3 35  GLY 35  35  35  GLY GLY C . n 
C 3 36  ILE 36  36  36  ILE ILE C . n 
C 3 37  PRO 37  37  37  PRO PRO C . n 
C 3 38  PRO 38  38  38  PRO PRO C . n 
C 3 39  ASP 39  39  39  ASP ASP C . n 
C 3 40  GLN 40  40  40  GLN GLN C . n 
C 3 41  GLN 41  41  41  GLN GLN C . n 
C 3 42  ARG 42  42  42  ARG ARG C . n 
C 3 43  LEU 43  43  43  LEU LEU C . n 
C 3 44  ILE 44  44  44  ILE ILE C . n 
C 3 45  PHE 45  45  45  PHE PHE C . n 
C 3 46  ALA 46  46  46  ALA ALA C . n 
C 3 47  GLY 47  47  47  GLY GLY C . n 
C 3 48  LYS 48  48  48  LYS LYS C . n 
C 3 49  GLN 49  49  49  GLN GLN C . n 
C 3 50  LEU 50  50  50  LEU LEU C . n 
C 3 51  GLU 51  51  51  GLU GLU C . n 
C 3 52  ASP 52  52  52  ASP ASP C . n 
C 3 53  GLY 53  53  53  GLY GLY C . n 
C 3 54  ARG 54  54  54  ARG ARG C . n 
C 3 55  THR 55  55  55  THR THR C . n 
C 3 56  LEU 56  56  56  LEU LEU C . n 
C 3 57  SER 57  57  57  SER SER C . n 
C 3 58  ASP 58  58  58  ASP ASP C . n 
C 3 59  TYR 59  59  59  TYR TYR C . n 
C 3 60  ASN 60  60  60  ASN ASN C . n 
C 3 61  ILE 61  61  61  ILE ILE C . n 
C 3 62  GLN 62  62  62  GLN GLN C . n 
C 3 63  LYS 63  63  63  LYS LYS C . n 
C 3 64  GLU 64  64  64  GLU GLU C . n 
C 3 65  SER 65  65  65  SER SER C . n 
C 3 66  THR 66  66  66  THR THR C . n 
C 3 67  LEU 67  67  67  LEU LEU C . n 
C 3 68  HIS 68  68  68  HIS HIS C . n 
C 3 69  LEU 69  69  69  LEU LEU C . n 
C 3 70  VAL 70  70  70  VAL VAL C . n 
C 3 71  LEU 71  71  71  LEU LEU C . n 
C 3 72  ARG 72  72  72  ARG ARG C . n 
C 3 73  LEU 73  73  73  LEU LEU C . n 
C 3 74  ARG 74  74  74  ARG ARG C . n 
C 3 75  GLY 75  75  75  GLY GLY C . n 
C 3 76  GLY 76  76  76  GLY GLY C . 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 ANP ? ? ANP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 AR6 ? ? AR6 ? ? '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  401 383 AR6 AR6 B . 
F 6 HOH 1  501 33  HOH HOH A . 
F 6 HOH 2  502 26  HOH HOH A . 
F 6 HOH 3  503 46  HOH HOH A . 
F 6 HOH 4  504 115 HOH HOH A . 
F 6 HOH 5  505 89  HOH HOH A . 
F 6 HOH 6  506 5   HOH HOH A . 
F 6 HOH 7  507 12  HOH HOH A . 
F 6 HOH 8  508 107 HOH HOH A . 
F 6 HOH 9  509 97  HOH HOH A . 
F 6 HOH 10 510 37  HOH HOH A . 
F 6 HOH 11 511 1   HOH HOH A . 
F 6 HOH 12 512 54  HOH HOH A . 
F 6 HOH 13 513 11  HOH HOH A . 
F 6 HOH 14 514 74  HOH HOH A . 
F 6 HOH 15 515 56  HOH HOH A . 
F 6 HOH 16 516 92  HOH HOH A . 
F 6 HOH 17 517 95  HOH HOH A . 
F 6 HOH 18 518 31  HOH HOH A . 
F 6 HOH 19 519 38  HOH HOH A . 
F 6 HOH 20 520 24  HOH HOH A . 
F 6 HOH 21 521 20  HOH HOH A . 
F 6 HOH 22 522 66  HOH HOH A . 
F 6 HOH 23 523 91  HOH HOH A . 
F 6 HOH 24 524 65  HOH HOH A . 
F 6 HOH 25 525 111 HOH HOH A . 
F 6 HOH 26 526 41  HOH HOH A . 
F 6 HOH 27 527 57  HOH HOH A . 
F 6 HOH 28 528 61  HOH HOH A . 
F 6 HOH 29 529 96  HOH HOH A . 
F 6 HOH 30 530 67  HOH HOH A . 
F 6 HOH 31 531 122 HOH HOH A . 
F 6 HOH 32 532 121 HOH HOH A . 
F 6 HOH 33 533 51  HOH HOH A . 
F 6 HOH 34 534 87  HOH HOH A . 
F 6 HOH 35 535 49  HOH HOH A . 
F 6 HOH 36 536 129 HOH HOH A . 
F 6 HOH 37 537 119 HOH HOH A . 
F 6 HOH 38 538 22  HOH HOH A . 
F 6 HOH 39 539 72  HOH HOH A . 
F 6 HOH 40 540 53  HOH HOH A . 
F 6 HOH 41 541 130 HOH HOH A . 
F 6 HOH 42 542 70  HOH HOH A . 
F 6 HOH 43 543 60  HOH HOH A . 
F 6 HOH 44 544 100 HOH HOH A . 
F 6 HOH 45 545 125 HOH HOH A . 
F 6 HOH 46 546 124 HOH HOH A . 
F 6 HOH 47 547 79  HOH HOH A . 
F 6 HOH 48 548 64  HOH HOH A . 
F 6 HOH 49 549 68  HOH HOH A . 
F 6 HOH 50 550 55  HOH HOH A . 
G 6 HOH 1  501 36  HOH HOH B . 
G 6 HOH 2  502 39  HOH HOH B . 
G 6 HOH 3  503 52  HOH HOH B . 
G 6 HOH 4  504 86  HOH HOH B . 
G 6 HOH 5  505 8   HOH HOH B . 
G 6 HOH 6  506 93  HOH HOH B . 
G 6 HOH 7  507 28  HOH HOH B . 
G 6 HOH 8  508 114 HOH HOH B . 
G 6 HOH 9  509 16  HOH HOH B . 
G 6 HOH 10 510 45  HOH HOH B . 
G 6 HOH 11 511 29  HOH HOH B . 
G 6 HOH 12 512 15  HOH HOH B . 
G 6 HOH 13 513 25  HOH HOH B . 
G 6 HOH 14 514 88  HOH HOH B . 
G 6 HOH 15 515 18  HOH HOH B . 
G 6 HOH 16 516 98  HOH HOH B . 
G 6 HOH 17 517 27  HOH HOH B . 
G 6 HOH 18 518 32  HOH HOH B . 
G 6 HOH 19 519 21  HOH HOH B . 
G 6 HOH 20 520 102 HOH HOH B . 
G 6 HOH 21 521 90  HOH HOH B . 
G 6 HOH 22 522 2   HOH HOH B . 
G 6 HOH 23 523 99  HOH HOH B . 
G 6 HOH 24 524 109 HOH HOH B . 
G 6 HOH 25 525 82  HOH HOH B . 
G 6 HOH 26 526 63  HOH HOH B . 
G 6 HOH 27 527 40  HOH HOH B . 
G 6 HOH 28 528 113 HOH HOH B . 
G 6 HOH 29 529 69  HOH HOH B . 
G 6 HOH 30 530 83  HOH HOH B . 
G 6 HOH 31 531 110 HOH HOH B . 
G 6 HOH 32 532 78  HOH HOH B . 
G 6 HOH 33 533 84  HOH HOH B . 
G 6 HOH 34 534 30  HOH HOH B . 
G 6 HOH 35 535 4   HOH HOH B . 
G 6 HOH 36 536 81  HOH HOH B . 
G 6 HOH 37 537 17  HOH HOH B . 
G 6 HOH 38 538 42  HOH HOH B . 
G 6 HOH 39 539 106 HOH HOH B . 
G 6 HOH 40 540 104 HOH HOH B . 
G 6 HOH 41 541 103 HOH HOH B . 
G 6 HOH 42 542 101 HOH HOH B . 
G 6 HOH 43 543 123 HOH HOH B . 
G 6 HOH 44 544 50  HOH HOH B . 
G 6 HOH 45 545 112 HOH HOH B . 
G 6 HOH 46 546 10  HOH HOH B . 
G 6 HOH 47 547 19  HOH HOH B . 
G 6 HOH 48 548 43  HOH HOH B . 
G 6 HOH 49 549 127 HOH HOH B . 
G 6 HOH 50 550 73  HOH HOH B . 
G 6 HOH 51 551 118 HOH HOH B . 
G 6 HOH 52 552 76  HOH HOH B . 
G 6 HOH 53 553 35  HOH HOH B . 
G 6 HOH 54 554 71  HOH HOH B . 
G 6 HOH 55 555 48  HOH HOH B . 
G 6 HOH 56 556 75  HOH HOH B . 
G 6 HOH 57 557 62  HOH HOH B . 
G 6 HOH 58 558 105 HOH HOH B . 
G 6 HOH 59 559 108 HOH HOH B . 
G 6 HOH 60 560 126 HOH HOH B . 
G 6 HOH 61 561 7   HOH HOH B . 
G 6 HOH 62 562 44  HOH HOH B . 
G 6 HOH 63 563 80  HOH HOH B . 
G 6 HOH 64 564 77  HOH HOH B . 
G 6 HOH 65 565 58  HOH HOH B . 
G 6 HOH 66 566 128 HOH HOH B . 
G 6 HOH 67 567 34  HOH HOH B . 
G 6 HOH 68 568 47  HOH HOH B . 
G 6 HOH 69 569 120 HOH HOH B . 
H 6 HOH 1  101 116 HOH HOH C . 
H 6 HOH 2  102 6   HOH HOH C . 
H 6 HOH 3  103 117 HOH HOH C . 
H 6 HOH 4  104 23  HOH HOH C . 
H 6 HOH 5  105 9   HOH HOH C . 
H 6 HOH 6  106 59  HOH HOH C . 
H 6 HOH 7  107 13  HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 62 ? CG  ? A ARG 62 CG  
2  1 Y 1 A ARG 62 ? CD  ? A ARG 62 CD  
3  1 Y 1 A ARG 62 ? NE  ? A ARG 62 NE  
4  1 Y 1 A ARG 62 ? CZ  ? A ARG 62 CZ  
5  1 Y 1 A ARG 62 ? NH1 ? A ARG 62 NH1 
6  1 Y 1 A ARG 62 ? NH2 ? A ARG 62 NH2 
7  1 Y 1 A ILE 64 ? CG1 ? A ILE 64 CG1 
8  1 Y 1 A ILE 64 ? CG2 ? A ILE 64 CG2 
9  1 Y 1 A ILE 64 ? CD1 ? A ILE 64 CD1 
10 1 Y 1 A LEU 65 ? CG  ? A LEU 65 CG  
11 1 Y 1 A LEU 65 ? CD1 ? A LEU 65 CD1 
12 1 Y 1 A LEU 65 ? CD2 ? A LEU 65 CD2 
13 1 Y 1 A THR 66 ? OG1 ? A THR 66 OG1 
14 1 Y 1 A THR 66 ? CG2 ? A THR 66 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8K6V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     215.964 
_cell.length_a_esd                 ? 
_cell.length_b                     55.044 
_cell.length_b_esd                 ? 
_cell.length_c                     79.747 
_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                         8K6V 
_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                   8K6V 
_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             2.60 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.75 
_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    'Magnesium acetate, MOPS, 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                                       8K6V 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.6 
_reflns.d_resolution_low                               79.75 
_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                                     30202 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.7 
_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                                   0.915 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.6 
_reflns_shell.d_res_low                                     2.69 
_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                             2918 
_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                                  0.693 
_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                                 8K6V 
_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                            2.60 
_refine.ls_d_res_low                             79.75 
_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                     30085 
_refine.ls_number_reflns_R_free                  1511 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.73 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2555 
_refine.ls_R_factor_R_free                       0.3069 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2527 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.91 
_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                            0.48 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6252 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.number_atoms_solvent             126 
_refine_hist.number_atoms_total               6445 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        79.75 
# 
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' ? 0.016  ? 6447 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.598  ? 8728 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.309 ? 2445 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.115  ? 979  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1111 ? 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' 2.60 2.68  . . 137 2520 99.00  . . . . 0.3808 . . . . . . . . . . . 0.4159 
'X-RAY DIFFRACTION' 2.68 2.78  . . 136 2550 100.00 . . . . 0.3096 . . . . . . . . . . . 0.3537 
'X-RAY DIFFRACTION' 2.78 2.89  . . 142 2565 100.00 . . . . 0.2725 . . . . . . . . . . . 0.3424 
'X-RAY DIFFRACTION' 2.89 3.02  . . 119 2559 100.00 . . . . 0.3056 . . . . . . . . . . . 0.3522 
'X-RAY DIFFRACTION' 3.02 3.18  . . 137 2569 100.00 . . . . 0.2884 . . . . . . . . . . . 0.3769 
'X-RAY DIFFRACTION' 3.18 3.38  . . 125 2586 100.00 . . . . 0.2737 . . . . . . . . . . . 0.3053 
'X-RAY DIFFRACTION' 3.38 3.64  . . 126 2584 100.00 . . . . 0.2849 . . . . . . . . . . . 0.3713 
'X-RAY DIFFRACTION' 3.64 4.01  . . 136 2603 100.00 . . . . 0.2593 . . . . . . . . . . . 0.3457 
'X-RAY DIFFRACTION' 4.01 4.59  . . 146 2624 100.00 . . . . 0.1992 . . . . . . . . . . . 0.2656 
'X-RAY DIFFRACTION' 4.59 5.78  . . 146 2631 100.00 . . . . 0.2147 . . . . . . . . . . . 0.2563 
'X-RAY DIFFRACTION' 5.78 79.75 . . 161 2783 99.00  . . . . 0.2016 . . . . . . . . . . . 0.2315 
# 
_struct.entry_id                     8K6V 
_struct.title                        'LnaB-Actin-PRUb ternary complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8K6V 
_struct_keywords.text            'AMPylation, Legionella effector, TOXIN' 
_struct_keywords.pdbx_keywords   TOXIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A0A8C6VAB1_NAJNA A0A8C6VAB1 ? 1 
;MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD
DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVT
HTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITAL
APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
;
1 
2 PDB 8K6V             8K6V       ? 2 ? 1 
3 UNP UBB_HUMAN        P0CG47     ? 3 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8K6V A 1 ? 375 ? A0A8C6VAB1 1 ? 375 ? 1 375 
2 2 8K6V B 1 ? 352 ? 8K6V       1 ? 352 ? 1 352 
3 3 8K6V C 1 ? 76  ? P0CG47     1 ? 76  ? 1 76  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 55  ? LYS A 61  ? GLY A 55  LYS A 61  1 ? 7  
HELX_P HELX_P2  AA2 ASN A 78  ? ASN A 92  ? ASN A 78  ASN A 92  1 ? 15 
HELX_P HELX_P3  AA3 ALA A 97  ? HIS A 101 ? ALA A 97  HIS A 101 5 ? 5  
HELX_P HELX_P4  AA4 PRO A 112 ? THR A 126 ? PRO A 112 THR A 126 1 ? 15 
HELX_P HELX_P5  AA5 GLN A 137 ? SER A 145 ? GLN A 137 SER A 145 1 ? 9  
HELX_P HELX_P6  AA6 ALA A 181 ? ARG A 196 ? ALA A 181 ARG A 196 1 ? 16 
HELX_P HELX_P7  AA7 THR A 202 ? CYS A 217 ? THR A 202 CYS A 217 1 ? 16 
HELX_P HELX_P8  AA8 ASP A 222 ? ALA A 231 ? ASP A 222 ALA A 231 1 ? 10 
HELX_P HELX_P9  AA9 ASN A 252 ? GLN A 263 ? ASN A 252 GLN A 263 1 ? 12 
HELX_P HELX_P10 AB1 PRO A 264 ? GLY A 268 ? PRO A 264 GLY A 268 5 ? 5  
HELX_P HELX_P11 AB2 GLY A 273 ? LYS A 284 ? GLY A 273 LYS A 284 1 ? 12 
HELX_P HELX_P12 AB3 ASP A 286 ? ASP A 288 ? ASP A 286 ASP A 288 5 ? 3  
HELX_P HELX_P13 AB4 ILE A 289 ? ASN A 296 ? ILE A 289 ASN A 296 1 ? 8  
HELX_P HELX_P14 AB5 GLY A 301 ? MET A 305 ? GLY A 301 MET A 305 5 ? 5  
HELX_P HELX_P15 AB6 GLY A 308 ? ALA A 321 ? GLY A 308 ALA A 321 1 ? 14 
HELX_P HELX_P16 AB7 GLU A 334 ? LYS A 336 ? GLU A 334 LYS A 336 5 ? 3  
HELX_P HELX_P17 AB8 TYR A 337 ? LEU A 349 ? TYR A 337 LEU A 349 1 ? 13 
HELX_P HELX_P18 AB9 SER A 350 ? MET A 355 ? SER A 350 MET A 355 5 ? 6  
HELX_P HELX_P19 AC1 LYS A 359 ? GLY A 366 ? LYS A 359 GLY A 366 1 ? 8  
HELX_P HELX_P20 AC2 SER A 368 ? CYS A 374 ? SER A 368 CYS A 374 1 ? 7  
HELX_P HELX_P21 AC3 LEU B 8   ? LEU B 14  ? LEU B 8   LEU B 14  1 ? 7  
HELX_P HELX_P22 AC4 ASP B 20  ? LEU B 36  ? ASP B 20  LEU B 36  1 ? 17 
HELX_P HELX_P23 AC5 PHE B 42  ? GLN B 56  ? PHE B 42  GLN B 56  1 ? 15 
HELX_P HELX_P24 AC6 ASN B 57  ? ASN B 72  ? ASN B 57  ASN B 72  1 ? 16 
HELX_P HELX_P25 AC7 GLU B 73  ? LEU B 76  ? GLU B 73  LEU B 76  5 ? 4  
HELX_P HELX_P26 AC8 SER B 77  ? ALA B 88  ? SER B 77  ALA B 88  1 ? 12 
HELX_P HELX_P27 AC9 PRO B 89  ? LEU B 91  ? PRO B 89  LEU B 91  5 ? 3  
HELX_P HELX_P28 AD1 ASN B 98  ? SER B 120 ? ASN B 98  SER B 120 1 ? 23 
HELX_P HELX_P29 AD2 LEU B 122 ? LEU B 128 ? LEU B 122 LEU B 128 1 ? 7  
HELX_P HELX_P30 AD3 LEU B 128 ? LYS B 136 ? LEU B 128 LYS B 136 1 ? 9  
HELX_P HELX_P31 AD4 THR B 149 ? SER B 159 ? THR B 149 SER B 159 1 ? 11 
HELX_P HELX_P32 AD5 PHE B 160 ? ASN B 164 ? PHE B 160 ASN B 164 5 ? 5  
HELX_P HELX_P33 AD6 GLU B 168 ? GLN B 174 ? GLU B 168 GLN B 174 1 ? 7  
HELX_P HELX_P34 AD7 ARG B 177 ? LYS B 181 ? ARG B 177 LYS B 181 5 ? 5  
HELX_P HELX_P35 AD8 GLY B 228 ? LYS B 233 ? GLY B 228 LYS B 233 1 ? 6  
HELX_P HELX_P36 AD9 GLY B 244 ? HIS B 260 ? GLY B 244 HIS B 260 1 ? 17 
HELX_P HELX_P37 AE1 ASP B 265 ? GLU B 284 ? ASP B 265 GLU B 284 1 ? 20 
HELX_P HELX_P38 AE2 SER B 288 ? GLU B 291 ? SER B 288 GLU B 291 5 ? 4  
HELX_P HELX_P39 AE3 VAL B 292 ? THR B 297 ? VAL B 292 THR B 297 1 ? 6  
HELX_P HELX_P40 AE4 GLU B 298 ? LYS B 307 ? GLU B 298 LYS B 307 1 ? 10 
HELX_P HELX_P41 AE5 THR B 320 ? LYS B 349 ? THR B 320 LYS B 349 1 ? 30 
HELX_P HELX_P42 AE6 THR C 22  ? GLY C 35  ? THR C 22  GLY C 35  1 ? 14 
HELX_P HELX_P43 AE7 PRO C 37  ? ASP C 39  ? PRO C 37  ASP C 39  5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 29  ? PRO A 32  ? ALA A 29  PRO A 32  
AA1 2 MET A 16  ? PHE A 21  ? MET A 16  PHE A 21  
AA1 3 LEU A 8   ? ASP A 11  ? LEU A 8   ASP A 11  
AA1 4 VAL A 103 ? GLU A 107 ? VAL A 103 GLU A 107 
AA1 5 ALA A 131 ? ILE A 136 ? ALA A 131 ILE A 136 
AA1 6 ILE A 357 ? SER A 358 ? ILE A 357 SER A 358 
AA2 1 TYR A 53  ? VAL A 54  ? TYR A 53  VAL A 54  
AA2 2 VAL A 35  ? GLY A 36  ? VAL A 35  GLY A 36  
AA2 3 LEU A 67  ? LYS A 68  ? LEU A 67  LYS A 68  
AA3 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA3 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA3 3 LEU A 176 ? LEU A 178 ? LEU A 176 LEU A 178 
AA4 1 TYR A 169 ? ALA A 170 ? TYR A 169 ALA A 170 
AA4 2 THR A 160 ? TYR A 166 ? THR A 160 TYR A 166 
AA4 3 GLY A 150 ? SER A 155 ? GLY A 150 SER A 155 
AA4 4 THR A 297 ? SER A 300 ? THR A 297 SER A 300 
AA4 5 ILE A 329 ? ILE A 330 ? ILE A 329 ILE A 330 
AA5 1 LYS A 238 ? GLU A 241 ? LYS A 238 GLU A 241 
AA5 2 VAL A 247 ? ILE A 250 ? VAL A 247 ILE A 250 
AA6 1 ASN B 190 ? SER B 193 ? ASN B 190 SER B 193 
AA6 2 ARG B 214 ? PRO B 217 ? ARG B 214 PRO B 217 
AA7 1 THR C 12  ? LEU C 15  ? THR C 12  LEU C 15  
AA7 2 ILE C 3   ? LYS C 6   ? ILE C 3   LYS C 6   
AA7 3 SER C 65  ? LEU C 71  ? SER C 65  LEU C 71  
AA7 4 GLN C 41  ? PHE C 45  ? GLN C 41  PHE C 45  
AA7 5 LYS C 48  ? GLN C 49  ? LYS C 48  GLN C 49  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 29  ? O ALA A 29  N ALA A 19  ? N ALA A 19  
AA1 2 3 O LYS A 18  ? O LYS A 18  N ASP A 11  ? N ASP A 11  
AA1 3 4 N LEU A 8   ? N LEU A 8   O LEU A 104 ? O LEU A 104 
AA1 4 5 N LEU A 105 ? N LEU A 105 O TYR A 133 ? O TYR A 133 
AA1 5 6 N MET A 132 ? N MET A 132 O ILE A 357 ? O ILE A 357 
AA2 1 2 O TYR A 53  ? O TYR A 53  N GLY A 36  ? N GLY A 36  
AA2 2 3 N VAL A 35  ? N VAL A 35  O LYS A 68  ? O LYS A 68  
AA3 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA3 2 3 N THR A 160 ? N THR A 160 O LEU A 178 ? O LEU A 178 
AA4 1 2 O TYR A 169 ? O TYR A 169 N TYR A 166 ? N TYR A 166 
AA4 2 3 O VAL A 163 ? O VAL A 163 N VAL A 152 ? N VAL A 152 
AA4 3 4 N MET A 153 ? N MET A 153 O VAL A 298 ? O VAL A 298 
AA4 4 5 N THR A 297 ? N THR A 297 O ILE A 330 ? O ILE A 330 
AA5 1 2 N LYS A 238 ? N LYS A 238 O ILE A 250 ? O ILE A 250 
AA6 1 2 N THR B 191 ? N THR B 191 O VAL B 216 ? O VAL B 216 
AA7 1 2 O ILE C 13  ? O ILE C 13  N VAL C 5   ? N VAL C 5   
AA7 2 3 N LYS C 6   ? N LYS C 6   O LEU C 67  ? O LEU C 67  
AA7 3 4 O HIS C 68  ? O HIS C 68  N ILE C 44  ? N ILE C 44  
AA7 4 5 N PHE C 45  ? N PHE C 45  O LYS C 48  ? O LYS C 48  
# 
_pdbx_entry_details.entry_id                   8K6V 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ARG A 62  ? ? -56.04  -9.55   
2  1 HIS A 73  ? ? 81.74   9.77    
3  1 ALA A 181 ? ? -162.60 -160.75 
4  1 THR A 201 ? ? -135.20 -54.70  
5  1 LYS A 215 ? ? -95.26  -69.85  
6  1 THR A 303 ? ? -69.67  1.13    
7  1 LYS B 38  ? ? 75.77   -18.29  
8  1 GLN B 56  ? ? 70.11   30.57   
9  1 ASP B 165 ? ? 68.57   -0.28   
10 1 ASN B 166 ? ? -132.87 -80.18  
11 1 ALA B 240 ? ? -150.09 31.25   
12 1 SER B 241 ? ? 56.62   -149.52 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         28.5360 
_pdbx_refine_tls.origin_y         11.9357 
_pdbx_refine_tls.origin_z         38.7402 
_pdbx_refine_tls.T[1][1]          0.2436 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0150 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0422 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1994 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0179 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2456 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.2426 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0215 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0591 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.0366 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1443 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.5604 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0264 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0143 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0164 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0110 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0023 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0148 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0149 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0376 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0312 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 549 ? 6.47 . 
2 1 O ? A HOH 550 ? 6.55 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1  ? A MET 1  
2  1 Y 1 A GLU 2  ? A GLU 2  
3  1 Y 1 A GLU 3  ? A GLU 3  
4  1 Y 1 A GLU 4  ? A GLU 4  
5  1 Y 1 A ILE 5  ? A ILE 5  
6  1 Y 1 A MET 47 ? A MET 47 
7  1 Y 1 A GLY 48 ? A GLY 48 
8  1 Y 1 A GLN 49 ? A GLN 49 
9  1 Y 1 A LYS 50 ? A LYS 50 
10 1 Y 1 B MET 1  ? B MET 1  
11 1 Y 1 B SER 2  ? B SER 2  
12 1 Y 1 B TYR 3  ? B TYR 3  
13 1 Y 1 B GLN 4  ? B GLN 4  
14 1 Y 1 B LYS 5  ? B LYS 5  
15 1 Y 1 B ILE 6  ? B ILE 6  
# 
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                    8K6V 
_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]   0.004630 
_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]   0.018167 
_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]   0.012540 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . ALA A 1 6   ? 11.831 1.754   12.363 1.00 26.50  ?  6   ALA A N      1 
ATOM   2    C CA     . ALA A 1 6   ? 12.059 3.100   11.833 1.00 26.61  ?  6   ALA A CA     1 
ATOM   3    C C      . ALA A 1 6   ? 12.310 4.280   12.824 1.00 31.72  ?  6   ALA A C      1 
ATOM   4    O O      . ALA A 1 6   ? 11.594 5.255   12.753 1.00 36.73  ?  6   ALA A O      1 
ATOM   5    C CB     . ALA A 1 6   ? 10.884 3.455   10.973 1.00 28.59  ?  6   ALA A CB     1 
ATOM   6    N N      . ALA A 1 7   ? 13.341 4.267   13.673 1.00 31.91  ?  7   ALA A N      1 
ATOM   7    C CA     . ALA A 1 7   ? 13.480 5.320   14.686 1.00 33.63  ?  7   ALA A CA     1 
ATOM   8    C C      . ALA A 1 7   ? 14.017 6.653   14.133 1.00 30.87  ?  7   ALA A C      1 
ATOM   9    O O      . ALA A 1 7   ? 14.789 6.711   13.171 1.00 30.41  ?  7   ALA A O      1 
ATOM   10   C CB     . ALA A 1 7   ? 14.398 4.863   15.823 1.00 34.55  ?  7   ALA A CB     1 
ATOM   11   N N      . LEU A 1 8   ? 13.664 7.734   14.838 1.00 41.65  ?  8   LEU A N      1 
ATOM   12   C CA     . LEU A 1 8   ? 14.097 9.102   14.566 1.00 44.56  ?  8   LEU A CA     1 
ATOM   13   C C      . LEU A 1 8   ? 15.259 9.516   15.476 1.00 43.31  ?  8   LEU A C      1 
ATOM   14   O O      . LEU A 1 8   ? 15.376 9.054   16.612 1.00 41.68  ?  8   LEU A O      1 
ATOM   15   C CB     . LEU A 1 8   ? 12.940 10.082  14.765 1.00 42.58  ?  8   LEU A CB     1 
ATOM   16   C CG     . LEU A 1 8   ? 11.686 9.849   13.916 1.00 45.15  ?  8   LEU A CG     1 
ATOM   17   C CD1    . LEU A 1 8   ? 10.673 10.893  14.281 1.00 37.95  ?  8   LEU A CD1    1 
ATOM   18   C CD2    . LEU A 1 8   ? 11.982 9.856   12.389 1.00 43.29  ?  8   LEU A CD2    1 
ATOM   19   N N      . VAL A 1 9   ? 16.131 10.392  14.969 1.00 33.59  ?  9   VAL A N      1 
ATOM   20   C CA     . VAL A 1 9   ? 17.248 10.942  15.762 1.00 33.75  ?  9   VAL A CA     1 
ATOM   21   C C      . VAL A 1 9   ? 17.315 12.450  15.528 1.00 32.48  ?  9   VAL A C      1 
ATOM   22   O O      . VAL A 1 9   ? 17.323 12.889  14.403 1.00 27.65  ?  9   VAL A O      1 
ATOM   23   C CB     . VAL A 1 9   ? 18.634 10.285  15.500 1.00 26.19  ?  9   VAL A CB     1 
ATOM   24   C CG1    . VAL A 1 9   ? 19.679 10.814  16.462 1.00 26.61  ?  9   VAL A CG1    1 
ATOM   25   C CG2    . VAL A 1 9   ? 18.580 8.771   15.575 1.00 22.86  ?  9   VAL A CG2    1 
ATOM   26   N N      . ILE A 1 10  ? 17.317 13.237  16.583 1.00 20.04  ?  10  ILE A N      1 
ATOM   27   C CA     . ILE A 1 10  ? 17.390 14.670  16.482 1.00 20.00  ?  10  ILE A CA     1 
ATOM   28   C C      . ILE A 1 10  ? 18.402 15.293  17.400 1.00 21.80  ?  10  ILE A C      1 
ATOM   29   O O      . ILE A 1 10  ? 18.293 15.205  18.612 1.00 31.10  ?  10  ILE A O      1 
ATOM   30   C CB     . ILE A 1 10  ? 16.004 15.335  16.614 1.00 20.24  ?  10  ILE A CB     1 
ATOM   31   C CG1    . ILE A 1 10  ? 16.034 16.830  16.366 1.00 20.27  ?  10  ILE A CG1    1 
ATOM   32   C CG2    . ILE A 1 10  ? 15.291 14.880  17.871 1.00 25.92  ?  10  ILE A CG2    1 
ATOM   33   C CD1    . ILE A 1 10  ? 14.662 17.398  16.191 1.00 20.56  ?  10  ILE A CD1    1 
ATOM   34   N N      . ASP A 1 11  ? 19.433 15.872  16.822 1.00 28.74  ?  11  ASP A N      1 
ATOM   35   C CA     . ASP A 1 11  ? 20.436 16.595  17.587 1.00 22.11  ?  11  ASP A CA     1 
ATOM   36   C C      . ASP A 1 11  ? 19.935 18.025  17.768 1.00 28.91  ?  11  ASP A C      1 
ATOM   37   O O      . ASP A 1 11  ? 19.827 18.784  16.804 1.00 25.58  ?  11  ASP A O      1 
ATOM   38   C CB     . ASP A 1 11  ? 21.780 16.554  16.860 1.00 19.29  ?  11  ASP A CB     1 
ATOM   39   C CG     . ASP A 1 11  ? 22.927 17.183  17.656 1.00 27.23  ?  11  ASP A CG     1 
ATOM   40   O OD1    . ASP A 1 11  ? 22.844 17.232  18.886 1.00 33.19  ?  11  ASP A OD1    1 
ATOM   41   O OD2    . ASP A 1 11  ? 23.949 17.606  17.067 1.00 31.29  -1 11  ASP A OD2    1 
ATOM   42   N N      . ASN A 1 12  ? 19.664 18.410  18.999 1.00 39.49  ?  12  ASN A N      1 
ATOM   43   C CA     . ASN A 1 12  ? 19.145 19.734  19.271 1.00 36.23  ?  12  ASN A CA     1 
ATOM   44   C C      . ASN A 1 12  ? 20.349 20.554  19.675 1.00 37.59  ?  12  ASN A C      1 
ATOM   45   O O      . ASN A 1 12  ? 20.711 20.610  20.855 1.00 51.91  ?  12  ASN A O      1 
ATOM   46   C CB     . ASN A 1 12  ? 18.111 19.677  20.389 1.00 43.74  ?  12  ASN A CB     1 
ATOM   47   C CG     . ASN A 1 12  ? 17.050 18.585  20.172 1.00 47.83  ?  12  ASN A CG     1 
ATOM   48   O OD1    . ASN A 1 12  ? 16.040 18.825  19.499 1.00 48.68  ?  12  ASN A OD1    1 
ATOM   49   N ND2    . ASN A 1 12  ? 17.271 17.390  20.759 1.00 38.36  ?  12  ASN A ND2    1 
ATOM   50   N N      . GLY A 1 13  ? 20.904 21.271  18.701 1.00 26.05  ?  13  GLY A N      1 
ATOM   51   C CA     . GLY A 1 13  ? 22.146 21.989  18.860 1.00 19.39  ?  13  GLY A CA     1 
ATOM   52   C C      . GLY A 1 13  ? 21.929 23.490  18.955 1.00 22.47  ?  13  GLY A C      1 
ATOM   53   O O      . GLY A 1 13  ? 20.860 24.017  18.648 1.00 33.36  ?  13  GLY A O      1 
ATOM   54   N N      . SER A 1 14  ? 23.002 24.177  19.344 1.00 30.01  ?  14  SER A N      1 
ATOM   55   C CA     . SER A 1 14  ? 22.950 25.614  19.592 1.00 37.05  ?  14  SER A CA     1 
ATOM   56   C C      . SER A 1 14  ? 22.628 26.397  18.318 1.00 37.95  ?  14  SER A C      1 
ATOM   57   O O      . SER A 1 14  ? 21.798 27.312  18.333 1.00 42.99  ?  14  SER A O      1 
ATOM   58   C CB     . SER A 1 14  ? 24.289 26.071  20.184 1.00 43.04  ?  14  SER A CB     1 
ATOM   59   O OG     . SER A 1 14  ? 24.194 27.366  20.743 1.00 51.40  ?  14  SER A OG     1 
ATOM   60   N N      . GLY A 1 15  ? 23.360 26.135  17.240 1.00 27.39  ?  15  GLY A N      1 
ATOM   61   C CA     . GLY A 1 15  ? 23.121 26.799  15.976 1.00 33.62  ?  15  GLY A CA     1 
ATOM   62   C C      . GLY A 1 15  ? 22.082 26.186  15.068 1.00 32.23  ?  15  GLY A C      1 
ATOM   63   O O      . GLY A 1 15  ? 21.181 26.873  14.577 1.00 40.55  ?  15  GLY A O      1 
ATOM   64   N N      . MET A 1 16  ? 22.233 24.894  14.855 1.00 24.09  ?  16  MET A N      1 
ATOM   65   C CA     . MET A 1 16  ? 21.362 24.193  13.962 1.00 24.36  ?  16  MET A CA     1 
ATOM   66   C C      . MET A 1 16  ? 21.053 22.788  14.400 1.00 29.97  ?  16  MET A C      1 
ATOM   67   O O      . MET A 1 16  ? 21.837 22.184  15.089 1.00 26.09  ?  16  MET A O      1 
ATOM   68   C CB     . MET A 1 16  ? 22.048 24.114  12.634 1.00 35.23  ?  16  MET A CB     1 
ATOM   69   C CG     . MET A 1 16  ? 23.417 23.482  12.705 1.00 47.36  ?  16  MET A CG     1 
ATOM   70   S SD     . MET A 1 16  ? 24.647 24.454  11.837 1.00 57.34  ?  16  MET A SD     1 
ATOM   71   C CE     . MET A 1 16  ? 24.515 26.021  12.686 1.00 57.43  ?  16  MET A CE     1 
ATOM   72   N N      . CYS A 1 17  ? 19.945 22.283  13.923 1.00 37.25  ?  17  CYS A N      1 
ATOM   73   C CA     . CYS A 1 17  ? 19.516 20.956  14.243 1.00 38.49  ?  17  CYS A CA     1 
ATOM   74   C C      . CYS A 1 17  ? 19.830 19.943  13.169 1.00 36.17  ?  17  CYS A C      1 
ATOM   75   O O      . CYS A 1 17  ? 19.562 20.210  12.034 1.00 40.68  ?  17  CYS A O      1 
ATOM   76   C CB     . CYS A 1 17  ? 18.004 21.060  14.445 1.00 45.39  ?  17  CYS A CB     1 
ATOM   77   S SG     . CYS A 1 17  ? 17.089 19.526  14.340 1.00 63.35  ?  17  CYS A SG     1 
ATOM   78   N N      . LYS A 1 18  ? 20.307 18.784  13.553 1.00 30.76  ?  18  LYS A N      1 
ATOM   79   C CA     . LYS A 1 18  ? 20.581 17.730  12.625 1.00 24.63  ?  18  LYS A CA     1 
ATOM   80   C C      . LYS A 1 18  ? 19.569 16.663  12.872 1.00 24.93  ?  18  LYS A C      1 
ATOM   81   O O      . LYS A 1 18  ? 19.486 16.135  13.934 1.00 33.01  ?  18  LYS A O      1 
ATOM   82   C CB     . LYS A 1 18  ? 21.986 17.256  12.839 1.00 27.88  ?  18  LYS A CB     1 
ATOM   83   C CG     . LYS A 1 18  ? 22.990 18.359  12.673 1.00 22.99  ?  18  LYS A CG     1 
ATOM   84   C CD     . LYS A 1 18  ? 24.151 18.129  13.600 1.00 27.95  ?  18  LYS A CD     1 
ATOM   85   C CE     . LYS A 1 18  ? 24.655 19.452  14.121 1.00 30.21  ?  18  LYS A CE     1 
ATOM   86   N NZ     . LYS A 1 18  ? 23.760 20.051  15.135 1.00 26.61  ?  18  LYS A NZ     1 
ATOM   87   N N      . ALA A 1 19  ? 18.764 16.373  11.880 1.00 26.93  ?  19  ALA A N      1 
ATOM   88   C CA     . ALA A 1 19  ? 17.682 15.429  12.095 1.00 27.90  ?  19  ALA A CA     1 
ATOM   89   C C      . ALA A 1 19  ? 17.699 14.371  10.999 1.00 28.49  ?  19  ALA A C      1 
ATOM   90   O O      . ALA A 1 19  ? 18.100 14.639  9.870  1.00 27.07  ?  19  ALA A O      1 
ATOM   91   C CB     . ALA A 1 19  ? 16.332 16.155  12.153 1.00 32.83  ?  19  ALA A CB     1 
ATOM   92   N N      . GLY A 1 20  ? 17.273 13.161  11.337 1.00 20.55  ?  20  GLY A N      1 
ATOM   93   C CA     . GLY A 1 20  ? 17.323 12.094  10.368 1.00 20.70  ?  20  GLY A CA     1 
ATOM   94   C C      . GLY A 1 20  ? 16.841 10.801  10.969 1.00 20.80  ?  20  GLY A C      1 
ATOM   95   O O      . GLY A 1 20  ? 16.195 10.798  12.019 1.00 20.81  ?  20  GLY A O      1 
ATOM   96   N N      . PHE A 1 21  ? 17.172 9.690   10.296 1.00 28.20  ?  21  PHE A N      1 
ATOM   97   C CA     . PHE A 1 21  ? 16.650 8.380   10.656 1.00 28.24  ?  21  PHE A CA     1 
ATOM   98   C C      . PHE A 1 21  ? 17.768 7.446   11.077 1.00 33.74  ?  21  PHE A C      1 
ATOM   99   O O      . PHE A 1 21  ? 18.862 7.459   10.498 1.00 32.08  ?  21  PHE A O      1 
ATOM   100  C CB     . PHE A 1 21  ? 15.876 7.763   9.499  1.00 31.44  ?  21  PHE A CB     1 
ATOM   101  C CG     . PHE A 1 21  ? 14.889 8.699   8.889  1.00 39.51  ?  21  PHE A CG     1 
ATOM   102  C CD1    . PHE A 1 21  ? 15.323 9.732   8.067  1.00 42.66  ?  21  PHE A CD1    1 
ATOM   103  C CD2    . PHE A 1 21  ? 13.535 8.583   9.172  1.00 33.80  ?  21  PHE A CD2    1 
ATOM   104  C CE1    . PHE A 1 21  ? 14.432 10.610  7.520  1.00 41.15  ?  21  PHE A CE1    1 
ATOM   105  C CE2    . PHE A 1 21  ? 12.632 9.465   8.629  1.00 38.82  ?  21  PHE A CE2    1 
ATOM   106  C CZ     . PHE A 1 21  ? 13.083 10.483  7.803  1.00 44.70  ?  21  PHE A CZ     1 
ATOM   107  N N      . ALA A 1 22  ? 17.449 6.616   12.076 1.00 36.35  ?  22  ALA A N      1 
ATOM   108  C CA     . ALA A 1 22  ? 18.357 5.593   12.578 1.00 31.47  ?  22  ALA A CA     1 
ATOM   109  C C      . ALA A 1 22  ? 18.726 4.600   11.480 1.00 32.20  ?  22  ALA A C      1 
ATOM   110  O O      . ALA A 1 22  ? 17.855 4.026   10.813 1.00 39.81  ?  22  ALA A O      1 
ATOM   111  C CB     . ALA A 1 22  ? 17.713 4.867   13.767 1.00 30.92  ?  22  ALA A CB     1 
ATOM   112  N N      . GLY A 1 23  ? 20.025 4.361   11.334 1.00 24.76  ?  23  GLY A N      1 
ATOM   113  C CA     . GLY A 1 23  ? 20.569 3.617   10.230 1.00 23.06  ?  23  GLY A CA     1 
ATOM   114  C C      . GLY A 1 23  ? 21.259 4.456   9.166  1.00 30.32  ?  23  GLY A C      1 
ATOM   115  O O      . GLY A 1 23  ? 22.168 3.945   8.492  1.00 41.57  ?  23  GLY A O      1 
ATOM   116  N N      . ASP A 1 24  ? 20.912 5.733   9.040  1.00 29.39  ?  24  ASP A N      1 
ATOM   117  C CA     . ASP A 1 24  ? 21.563 6.594   8.065  1.00 33.08  ?  24  ASP A CA     1 
ATOM   118  C C      . ASP A 1 24  ? 22.879 7.157   8.583  1.00 40.96  ?  24  ASP A C      1 
ATOM   119  O O      . ASP A 1 24  ? 22.972 7.608   9.722  1.00 42.26  ?  24  ASP A O      1 
ATOM   120  C CB     . ASP A 1 24  ? 20.632 7.732   7.695  1.00 32.95  ?  24  ASP A CB     1 
ATOM   121  C CG     . ASP A 1 24  ? 19.410 7.235   7.039  1.00 39.49  ?  24  ASP A CG     1 
ATOM   122  O OD1    . ASP A 1 24  ? 19.486 6.103   6.522  1.00 46.65  ?  24  ASP A OD1    1 
ATOM   123  O OD2    . ASP A 1 24  ? 18.385 7.939   7.042  1.00 41.61  -1 24  ASP A OD2    1 
ATOM   124  N N      . ASP A 1 25  ? 23.884 7.182   7.708  1.00 57.55  ?  25  ASP A N      1 
ATOM   125  C CA     . ASP A 1 25  ? 25.204 7.738   8.015  1.00 59.50  ?  25  ASP A CA     1 
ATOM   126  C C      . ASP A 1 25  ? 25.215 9.255   8.189  1.00 48.78  ?  25  ASP A C      1 
ATOM   127  O O      . ASP A 1 25  ? 26.257 9.810   8.564  1.00 42.48  ?  25  ASP A O      1 
ATOM   128  C CB     . ASP A 1 25  ? 26.188 7.384   6.895  1.00 69.25  ?  25  ASP A CB     1 
ATOM   129  C CG     . ASP A 1 25  ? 26.554 5.919   6.880  1.00 75.44  ?  25  ASP A CG     1 
ATOM   130  O OD1    . ASP A 1 25  ? 26.285 5.226   7.888  1.00 75.42  ?  25  ASP A OD1    1 
ATOM   131  O OD2    . ASP A 1 25  ? 27.104 5.468   5.850  1.00 78.47  -1 25  ASP A OD2    1 
ATOM   132  N N      . ALA A 1 26  ? 24.130 9.947   7.865  1.00 27.89  ?  26  ALA A N      1 
ATOM   133  C CA     . ALA A 1 26  ? 24.113 11.396  7.974  1.00 25.35  ?  26  ALA A CA     1 
ATOM   134  C C      . ALA A 1 26  ? 22.713 11.832  8.351  1.00 27.92  ?  26  ALA A C      1 
ATOM   135  O O      . ALA A 1 26  ? 21.739 11.131  8.040  1.00 30.65  ?  26  ALA A O      1 
ATOM   136  C CB     . ALA A 1 26  ? 24.540 12.083  6.666  1.00 21.17  ?  26  ALA A CB     1 
ATOM   137  N N      . PRO A 1 27  ? 22.575 12.966  9.028  1.00 24.34  ?  27  PRO A N      1 
ATOM   138  C CA     . PRO A 1 27  ? 21.229 13.536  9.221  1.00 26.48  ?  27  PRO A CA     1 
ATOM   139  C C      . PRO A 1 27  ? 20.640 13.989  7.880  1.00 29.04  ?  27  PRO A C      1 
ATOM   140  O O      . PRO A 1 27  ? 21.342 14.547  7.032  1.00 29.03  ?  27  PRO A O      1 
ATOM   141  C CB     . PRO A 1 27  ? 21.464 14.719  10.181 1.00 19.93  ?  27  PRO A CB     1 
ATOM   142  C CG     . PRO A 1 27  ? 22.959 15.010  10.141 1.00 19.72  ?  27  PRO A CG     1 
ATOM   143  C CD     . PRO A 1 27  ? 23.639 13.699  9.749  1.00 19.72  ?  27  PRO A CD     1 
ATOM   144  N N      . ARG A 1 28  ? 19.335 13.736  7.684  1.00 32.74  ?  28  ARG A N      1 
ATOM   145  C CA     . ARG A 1 28  ? 18.662 14.201  6.474  1.00 28.20  ?  28  ARG A CA     1 
ATOM   146  C C      . ARG A 1 28  ? 18.356 15.695  6.482  1.00 27.09  ?  28  ARG A C      1 
ATOM   147  O O      . ARG A 1 28  ? 18.282 16.300  5.410  1.00 37.11  ?  28  ARG A O      1 
ATOM   148  C CB     . ARG A 1 28  ? 17.356 13.431  6.267  1.00 31.05  ?  28  ARG A CB     1 
ATOM   149  C CG     . ARG A 1 28  ? 16.953 13.211  4.831  1.00 27.99  ?  28  ARG A CG     1 
ATOM   150  C CD     . ARG A 1 28  ? 17.916 12.247  4.153  1.00 41.58  ?  28  ARG A CD     1 
ATOM   151  N NE     . ARG A 1 28  ? 17.825 10.876  4.658  1.00 37.36  ?  28  ARG A NE     1 
ATOM   152  C CZ     . ARG A 1 28  ? 16.881 10.028  4.271  1.00 43.22  ?  28  ARG A CZ     1 
ATOM   153  N NH1    . ARG A 1 28  ? 15.968 10.436  3.404  1.00 50.34  ?  28  ARG A NH1    1 
ATOM   154  N NH2    . ARG A 1 28  ? 16.835 8.788   4.736  1.00 42.36  ?  28  ARG A NH2    1 
ATOM   155  N N      . ALA A 1 29  ? 18.183 16.305  7.652  1.00 23.92  ?  29  ALA A N      1 
ATOM   156  C CA     . ALA A 1 29  ? 17.828 17.718  7.770  1.00 30.48  ?  29  ALA A CA     1 
ATOM   157  C C      . ALA A 1 29  ? 18.813 18.424  8.684  1.00 30.52  ?  29  ALA A C      1 
ATOM   158  O O      . ALA A 1 29  ? 19.061 17.972  9.805  1.00 38.62  ?  29  ALA A O      1 
ATOM   159  C CB     . ALA A 1 29  ? 16.399 17.927  8.309  1.00 25.30  ?  29  ALA A CB     1 
ATOM   160  N N      . VAL A 1 30  ? 19.360 19.540  8.212  1.00 22.65  ?  30  VAL A N      1 
ATOM   161  C CA     . VAL A 1 30  ? 20.191 20.402  9.037  1.00 22.25  ?  30  VAL A CA     1 
ATOM   162  C C      . VAL A 1 30  ? 19.733 21.828  8.761  1.00 25.16  ?  30  VAL A C      1 
ATOM   163  O O      . VAL A 1 30  ? 19.727 22.267  7.605  1.00 33.06  ?  30  VAL A O      1 
ATOM   164  C CB     . VAL A 1 30  ? 21.699 20.216  8.756  1.00 23.32  ?  30  VAL A CB     1 
ATOM   165  C CG1    . VAL A 1 30  ? 22.570 20.835  9.888  1.00 21.94  ?  30  VAL A CG1    1 
ATOM   166  C CG2    . VAL A 1 30  ? 22.047 18.728  8.542  1.00 20.01  ?  30  VAL A CG2    1 
ATOM   167  N N      . PHE A 1 31  ? 19.280 22.518  9.801  1.00 21.01  ?  31  PHE A N      1 
ATOM   168  C CA     . PHE A 1 31  ? 18.686 23.834  9.629  1.00 22.41  ?  31  PHE A CA     1 
ATOM   169  C C      . PHE A 1 31  ? 18.891 24.662  10.901 1.00 23.53  ?  31  PHE A C      1 
ATOM   170  O O      . PHE A 1 31  ? 19.047 24.102  11.994 1.00 27.65  ?  31  PHE A O      1 
ATOM   171  C CB     . PHE A 1 31  ? 17.208 23.680  9.278  1.00 21.19  ?  31  PHE A CB     1 
ATOM   172  C CG     . PHE A 1 31  ? 16.391 23.083  10.384 1.00 34.27  ?  31  PHE A CG     1 
ATOM   173  C CD1    . PHE A 1 31  ? 15.809 23.902  11.353 1.00 24.93  ?  31  PHE A CD1    1 
ATOM   174  C CD2    . PHE A 1 31  ? 16.209 21.701  10.465 1.00 28.08  ?  31  PHE A CD2    1 
ATOM   175  C CE1    . PHE A 1 31  ? 15.070 23.352  12.343 1.00 26.85  ?  31  PHE A CE1    1 
ATOM   176  C CE2    . PHE A 1 31  ? 15.465 21.156  11.461 1.00 23.46  ?  31  PHE A CE2    1 
ATOM   177  C CZ     . PHE A 1 31  ? 14.893 21.976  12.405 1.00 24.68  ?  31  PHE A CZ     1 
ATOM   178  N N      . PRO A 1 32  ? 18.877 26.002  10.800 1.00 33.59  ?  32  PRO A N      1 
ATOM   179  C CA     . PRO A 1 32  ? 19.142 26.837  11.984 1.00 33.73  ?  32  PRO A CA     1 
ATOM   180  C C      . PRO A 1 32  ? 18.153 26.605  13.113 1.00 36.19  ?  32  PRO A C      1 
ATOM   181  O O      . PRO A 1 32  ? 16.966 26.337  12.890 1.00 35.47  ?  32  PRO A O      1 
ATOM   182  C CB     . PRO A 1 32  ? 19.015 28.268  11.440 1.00 37.27  ?  32  PRO A CB     1 
ATOM   183  C CG     . PRO A 1 32  ? 19.359 28.146  9.980  1.00 32.32  ?  32  PRO A CG     1 
ATOM   184  C CD     . PRO A 1 32  ? 18.831 26.807  9.558  1.00 30.51  ?  32  PRO A CD     1 
ATOM   185  N N      . SER A 1 33  ? 18.642 26.788  14.346 1.00 35.66  ?  33  SER A N      1 
ATOM   186  C CA     . SER A 1 33  ? 17.753 26.781  15.506 1.00 33.10  ?  33  SER A CA     1 
ATOM   187  C C      . SER A 1 33  ? 17.281 28.215  15.625 1.00 35.02  ?  33  SER A C      1 
ATOM   188  O O      . SER A 1 33  ? 17.910 29.047  16.281 1.00 43.27  ?  33  SER A O      1 
ATOM   189  C CB     . SER A 1 33  ? 18.480 26.358  16.777 1.00 30.91  ?  33  SER A CB     1 
ATOM   190  O OG     . SER A 1 33  ? 19.274 25.199  16.603 1.00 32.89  ?  33  SER A OG     1 
ATOM   191  N N      . ILE A 1 34  ? 16.125 28.478  15.043 1.00 32.00  ?  34  ILE A N      1 
ATOM   192  C CA     . ILE A 1 34  ? 15.646 29.835  14.886 1.00 38.65  ?  34  ILE A CA     1 
ATOM   193  C C      . ILE A 1 34  ? 14.135 29.762  14.818 1.00 43.92  ?  34  ILE A C      1 
ATOM   194  O O      . ILE A 1 34  ? 13.572 28.849  14.200 1.00 45.28  ?  34  ILE A O      1 
ATOM   195  C CB     . ILE A 1 34  ? 16.259 30.508  13.635 1.00 46.88  ?  34  ILE A CB     1 
ATOM   196  C CG1    . ILE A 1 34  ? 17.755 30.769  13.832 1.00 50.66  ?  34  ILE A CG1    1 
ATOM   197  C CG2    . ILE A 1 34  ? 15.552 31.813  13.310 1.00 49.66  ?  34  ILE A CG2    1 
ATOM   198  C CD1    . ILE A 1 34  ? 18.397 31.525  12.670 1.00 52.63  ?  34  ILE A CD1    1 
ATOM   199  N N      . VAL A 1 35  ? 13.480 30.713  15.474 1.00 34.96  ?  35  VAL A N      1 
ATOM   200  C CA     . VAL A 1 35  ? 12.052 30.912  15.322 1.00 36.57  ?  35  VAL A CA     1 
ATOM   201  C C      . VAL A 1 35  ? 11.849 32.401  15.102 1.00 39.16  ?  35  VAL A C      1 
ATOM   202  O O      . VAL A 1 35  ? 12.122 33.210  16.000 1.00 40.11  ?  35  VAL A O      1 
ATOM   203  C CB     . VAL A 1 35  ? 11.261 30.391  16.534 1.00 30.41  ?  35  VAL A CB     1 
ATOM   204  C CG1    . VAL A 1 35  ? 9.747  30.658  16.374 1.00 26.41  ?  35  VAL A CG1    1 
ATOM   205  C CG2    . VAL A 1 35  ? 11.539 28.900  16.706 1.00 25.54  ?  35  VAL A CG2    1 
ATOM   206  N N      . GLY A 1 36  ? 11.456 32.769  13.884 1.00 52.36  ?  36  GLY A N      1 
ATOM   207  C CA     . GLY A 1 36  ? 10.926 34.089  13.594 1.00 55.12  ?  36  GLY A CA     1 
ATOM   208  C C      . GLY A 1 36  ? 9.494  34.283  14.047 1.00 56.08  ?  36  GLY A C      1 
ATOM   209  O O      . GLY A 1 36  ? 8.606  33.531  13.633 1.00 54.40  ?  36  GLY A O      1 
ATOM   210  N N      . ARG A 1 37  ? 9.239  35.299  14.864 1.00 69.08  ?  37  ARG A N      1 
ATOM   211  C CA     . ARG A 1 37  ? 7.879  35.758  15.110 1.00 69.09  ?  37  ARG A CA     1 
ATOM   212  C C      . ARG A 1 37  ? 7.756  37.171  14.554 1.00 62.20  ?  37  ARG A C      1 
ATOM   213  O O      . ARG A 1 37  ? 8.479  38.070  15.017 1.00 61.22  ?  37  ARG A O      1 
ATOM   214  C CB     . ARG A 1 37  ? 7.529  35.713  16.596 1.00 72.36  ?  37  ARG A CB     1 
ATOM   215  C CG     . ARG A 1 37  ? 6.097  35.243  16.851 1.00 77.18  ?  37  ARG A CG     1 
ATOM   216  C CD     . ARG A 1 37  ? 6.062  33.946  17.641 1.00 78.91  ?  37  ARG A CD     1 
ATOM   217  N NE     . ARG A 1 37  ? 6.625  34.114  18.978 1.00 79.53  ?  37  ARG A NE     1 
ATOM   218  C CZ     . ARG A 1 37  ? 6.995  33.110  19.764 1.00 82.20  ?  37  ARG A CZ     1 
ATOM   219  N NH1    . ARG A 1 37  ? 6.866  31.856  19.346 1.00 83.78  ?  37  ARG A NH1    1 
ATOM   220  N NH2    . ARG A 1 37  ? 7.506  33.361  20.964 1.00 82.27  ?  37  ARG A NH2    1 
ATOM   221  N N      . PRO A 1 38  ? 6.854  37.412  13.592 1.00 44.16  ?  38  PRO A N      1 
ATOM   222  C CA     . PRO A 1 38  ? 6.955  38.613  12.749 1.00 42.21  ?  38  PRO A CA     1 
ATOM   223  C C      . PRO A 1 38  ? 6.833  39.908  13.537 1.00 39.34  ?  38  PRO A C      1 
ATOM   224  O O      . PRO A 1 38  ? 6.006  40.038  14.440 1.00 38.02  ?  38  PRO A O      1 
ATOM   225  C CB     . PRO A 1 38  ? 5.791  38.449  11.757 1.00 41.06  ?  38  PRO A CB     1 
ATOM   226  C CG     . PRO A 1 38  ? 4.780  37.669  12.507 1.00 42.85  ?  38  PRO A CG     1 
ATOM   227  C CD     . PRO A 1 38  ? 5.592  36.686  13.355 1.00 43.83  ?  38  PRO A CD     1 
ATOM   228  N N      . ARG A 1 39  ? 7.657  40.886  13.154 1.00 43.45  ?  39  ARG A N      1 
ATOM   229  C CA     . ARG A 1 39  ? 7.751  42.115  13.919 1.00 51.48  ?  39  ARG A CA     1 
ATOM   230  C C      . ARG A 1 39  ? 6.438  42.878  13.937 1.00 53.81  ?  39  ARG A C      1 
ATOM   231  O O      . ARG A 1 39  ? 6.227  43.712  14.824 1.00 55.15  ?  39  ARG A O      1 
ATOM   232  C CB     . ARG A 1 39  ? 8.885  42.986  13.371 1.00 56.36  ?  39  ARG A CB     1 
ATOM   233  C CG     . ARG A 1 39  ? 9.971  43.282  14.399 1.00 55.76  ?  39  ARG A CG     1 
ATOM   234  C CD     . ARG A 1 39  ? 11.087 44.109  13.811 1.00 59.48  ?  39  ARG A CD     1 
ATOM   235  N NE     . ARG A 1 39  ? 11.932 43.326  12.916 1.00 64.28  ?  39  ARG A NE     1 
ATOM   236  C CZ     . ARG A 1 39  ? 12.742 43.865  12.010 1.00 65.60  ?  39  ARG A CZ     1 
ATOM   237  N NH1    . ARG A 1 39  ? 12.797 45.188  11.878 1.00 69.28  ?  39  ARG A NH1    1 
ATOM   238  N NH2    . ARG A 1 39  ? 13.487 43.088  11.227 1.00 56.79  ?  39  ARG A NH2    1 
ATOM   239  N N      . HIS A 1 40  ? 5.566  42.639  12.983 1.00 59.58  ?  40  HIS A N      1 
ATOM   240  C CA     . HIS A 1 40  ? 4.284  43.294  13.006 1.00 63.44  ?  40  HIS A CA     1 
ATOM   241  C C      . HIS A 1 40  ? 3.283  42.307  12.525 1.00 67.38  ?  40  HIS A C      1 
ATOM   242  O O      . HIS A 1 40  ? 3.649  41.347  11.878 1.00 72.56  ?  40  HIS A O      1 
ATOM   243  C CB     . HIS A 1 40  ? 4.268  44.500  12.072 1.00 62.98  ?  40  HIS A CB     1 
ATOM   244  C CG     . HIS A 1 40  ? 5.483  45.367  12.161 1.00 63.60  ?  40  HIS A CG     1 
ATOM   245  N ND1    . HIS A 1 40  ? 5.709  46.221  13.217 1.00 61.75  ?  40  HIS A ND1    1 
ATOM   246  C CD2    . HIS A 1 40  ? 6.544  45.503  11.333 1.00 65.40  ?  40  HIS A CD2    1 
ATOM   247  C CE1    . HIS A 1 40  ? 6.856  46.848  13.036 1.00 66.10  ?  40  HIS A CE1    1 
ATOM   248  N NE2    . HIS A 1 40  ? 7.383  46.429  11.900 1.00 67.90  ?  40  HIS A NE2    1 
ATOM   249  N N      . GLN A 1 41  ? 2.014  42.519  12.863 1.00 53.60  ?  41  GLN A N      1 
ATOM   250  C CA     . GLN A 1 41  ? 0.956  41.664  12.349 1.00 42.07  ?  41  GLN A CA     1 
ATOM   251  C C      . GLN A 1 41  ? 0.571  42.323  11.048 1.00 42.75  ?  41  GLN A C      1 
ATOM   252  O O      . GLN A 1 41  ? 0.664  43.547  10.929 1.00 42.26  ?  41  GLN A O      1 
ATOM   253  C CB     . GLN A 1 41  ? -0.230 41.642  13.304 1.00 45.63  ?  41  GLN A CB     1 
ATOM   254  C CG     . GLN A 1 41  ? 0.122  42.048  14.724 1.00 49.09  ?  41  GLN A CG     1 
ATOM   255  C CD     . GLN A 1 41  ? -1.099 42.161  15.612 1.00 56.23  ?  41  GLN A CD     1 
ATOM   256  O OE1    . GLN A 1 41  ? -2.226 41.942  15.168 1.00 58.77  ?  41  GLN A OE1    1 
ATOM   257  N NE2    . GLN A 1 41  ? -0.881 42.502  16.877 1.00 57.50  ?  41  GLN A NE2    1 
ATOM   258  N N      . GLY A 1 42  ? 0.136  41.546  10.065 1.00 35.85  ?  42  GLY A N      1 
ATOM   259  C CA     . GLY A 1 42  ? -0.140 42.128  8.779  1.00 43.26  ?  42  GLY A CA     1 
ATOM   260  C C      . GLY A 1 42  ? 0.554  41.259  7.790  1.00 50.60  ?  42  GLY A C      1 
ATOM   261  O O      . GLY A 1 42  ? 0.184  41.179  6.636  1.00 59.06  ?  42  GLY A O      1 
ATOM   262  N N      . VAL A 1 43  ? 1.586  40.581  8.245  1.00 58.79  ?  43  VAL A N      1 
ATOM   263  C CA     . VAL A 1 43  ? 2.259  39.629  7.410  1.00 54.72  ?  43  VAL A CA     1 
ATOM   264  C C      . VAL A 1 43  ? 1.648  38.293  7.814  1.00 55.81  ?  43  VAL A C      1 
ATOM   265  O O      . VAL A 1 43  ? 2.083  37.251  7.353  1.00 57.52  ?  43  VAL A O      1 
ATOM   266  C CB     . VAL A 1 43  ? 3.751  39.672  7.692  1.00 51.81  ?  43  VAL A CB     1 
ATOM   267  C CG1    . VAL A 1 43  ? 4.315  41.029  7.311  1.00 47.10  ?  43  VAL A CG1    1 
ATOM   268  C CG2    . VAL A 1 43  ? 4.025  39.387  9.152  1.00 51.17  ?  43  VAL A CG2    1 
ATOM   269  N N      . MET A 1 44  ? 0.634  38.325  8.680  1.00 52.67  ?  44  MET A N      1 
ATOM   270  C CA     . MET A 1 44  ? -0.049 37.126  9.098  1.00 50.21  ?  44  MET A CA     1 
ATOM   271  C C      . MET A 1 44  ? -1.390 37.023  8.406  1.00 52.06  ?  44  MET A C      1 
ATOM   272  O O      . MET A 1 44  ? -2.025 35.982  8.465  1.00 55.25  ?  44  MET A O      1 
ATOM   273  C CB     . MET A 1 44  ? -0.235 37.106  10.608 1.00 47.60  ?  44  MET A CB     1 
ATOM   274  C CG     . MET A 1 44  ? 1.019  36.845  11.409 1.00 47.46  ?  44  MET A CG     1 
ATOM   275  S SD     . MET A 1 44  ? 0.624  36.509  13.130 1.00 61.29  ?  44  MET A SD     1 
ATOM   276  C CE     . MET A 1 44  ? 1.137  38.027  13.911 1.00 63.19  ?  44  MET A CE     1 
ATOM   277  N N      . VAL A 1 45  ? -1.824 38.070  7.721  1.00 47.12  ?  45  VAL A N      1 
ATOM   278  C CA     . VAL A 1 45  ? -3.057 37.969  6.948  1.00 46.69  ?  45  VAL A CA     1 
ATOM   279  C C      . VAL A 1 45  ? -2.899 37.054  5.738  1.00 52.93  ?  45  VAL A C      1 
ATOM   280  O O      . VAL A 1 45  ? -1.881 37.097  5.053  1.00 60.86  ?  45  VAL A O      1 
ATOM   281  C CB     . VAL A 1 45  ? -3.629 39.347  6.562  1.00 51.96  ?  45  VAL A CB     1 
ATOM   282  C CG1    . VAL A 1 45  ? -3.686 40.254  7.779  1.00 55.11  ?  45  VAL A CG1    1 
ATOM   283  C CG2    . VAL A 1 45  ? -2.854 40.023  5.445  1.00 51.90  ?  45  VAL A CG2    1 
ATOM   284  N N      . GLY A 1 46  ? -3.863 36.176  5.496  1.00 45.77  ?  46  GLY A N      1 
ATOM   285  C CA     . GLY A 1 46  ? -3.739 35.233  4.386  1.00 45.90  ?  46  GLY A CA     1 
ATOM   286  C C      . GLY A 1 46  ? -3.471 33.779  4.755  1.00 47.49  ?  46  GLY A C      1 
ATOM   287  O O      . GLY A 1 46  ? -2.765 33.456  5.729  1.00 45.83  ?  46  GLY A O      1 
ATOM   288  N N      . ASP A 1 51  ? 2.030  30.916  12.248 1.00 47.84  ?  51  ASP A N      1 
ATOM   289  C CA     . ASP A 1 51  ? 2.295  32.338  12.413 1.00 57.61  ?  51  ASP A CA     1 
ATOM   290  C C      . ASP A 1 51  ? 3.644  32.589  13.121 1.00 57.10  ?  51  ASP A C      1 
ATOM   291  O O      . ASP A 1 51  ? 3.849  33.589  13.823 1.00 48.62  ?  51  ASP A O      1 
ATOM   292  C CB     . ASP A 1 51  ? 1.122  32.948  13.142 1.00 68.29  ?  51  ASP A CB     1 
ATOM   293  C CG     . ASP A 1 51  ? -0.192 32.402  12.613 1.00 83.82  ?  51  ASP A CG     1 
ATOM   294  O OD1    . ASP A 1 51  ? -0.178 31.909  11.456 1.00 86.78  ?  51  ASP A OD1    1 
ATOM   295  O OD2    . ASP A 1 51  ? -1.217 32.433  13.335 1.00 91.19  -1 51  ASP A OD2    1 
ATOM   296  N N      . SER A 1 52  ? 4.560  31.649  12.884 1.00 49.11  ?  52  SER A N      1 
ATOM   297  C CA     . SER A 1 52  ? 5.945  31.713  13.306 1.00 50.31  ?  52  SER A CA     1 
ATOM   298  C C      . SER A 1 52  ? 6.798  31.146  12.171 1.00 52.66  ?  52  SER A C      1 
ATOM   299  O O      . SER A 1 52  ? 6.287  30.732  11.125 1.00 51.58  ?  52  SER A O      1 
ATOM   300  C CB     . SER A 1 52  ? 6.164  30.949  14.621 1.00 54.15  ?  52  SER A CB     1 
ATOM   301  O OG     . SER A 1 52  ? 5.398  31.495  15.689 1.00 54.52  ?  52  SER A OG     1 
ATOM   302  N N      . TYR A 1 53  ? 8.108  31.113  12.370 1.00 54.88  ?  53  TYR A N      1 
ATOM   303  C CA     . TYR A 1 53  ? 8.998  30.633  11.325 1.00 53.17  ?  53  TYR A CA     1 
ATOM   304  C C      . TYR A 1 53  ? 10.129 29.835  11.949 1.00 46.06  ?  53  TYR A C      1 
ATOM   305  O O      . TYR A 1 53  ? 10.629 30.194  13.017 1.00 46.88  ?  53  TYR A O      1 
ATOM   306  C CB     . TYR A 1 53  ? 9.546  31.807  10.496 1.00 54.03  ?  53  TYR A CB     1 
ATOM   307  C CG     . TYR A 1 53  ? 8.561  32.304  9.466  1.00 51.61  ?  53  TYR A CG     1 
ATOM   308  C CD1    . TYR A 1 53  ? 8.342  31.589  8.306  1.00 55.29  ?  53  TYR A CD1    1 
ATOM   309  C CD2    . TYR A 1 53  ? 7.844  33.478  9.659  1.00 53.61  ?  53  TYR A CD2    1 
ATOM   310  C CE1    . TYR A 1 53  ? 7.443  32.016  7.362  1.00 59.80  ?  53  TYR A CE1    1 
ATOM   311  C CE2    . TYR A 1 53  ? 6.938  33.918  8.718  1.00 54.78  ?  53  TYR A CE2    1 
ATOM   312  C CZ     . TYR A 1 53  ? 6.740  33.178  7.567  1.00 59.56  ?  53  TYR A CZ     1 
ATOM   313  O OH     . TYR A 1 53  ? 5.841  33.582  6.601  1.00 62.10  ?  53  TYR A OH     1 
ATOM   314  N N      . VAL A 1 54  ? 10.531 28.754  11.281 1.00 26.87  ?  54  VAL A N      1 
ATOM   315  C CA     . VAL A 1 54  ? 11.566 27.878  11.804 1.00 26.45  ?  54  VAL A CA     1 
ATOM   316  C C      . VAL A 1 54  ? 12.756 27.866  10.861 1.00 36.18  ?  54  VAL A C      1 
ATOM   317  O O      . VAL A 1 54  ? 12.612 28.034  9.647  1.00 39.44  ?  54  VAL A O      1 
ATOM   318  C CB     . VAL A 1 54  ? 11.033 26.451  12.012 1.00 27.25  ?  54  VAL A CB     1 
ATOM   319  C CG1    . VAL A 1 54  ? 11.917 25.698  12.992 1.00 28.22  ?  54  VAL A CG1    1 
ATOM   320  C CG2    . VAL A 1 54  ? 9.602  26.472  12.458 1.00 22.99  ?  54  VAL A CG2    1 
ATOM   321  N N      . GLY A 1 55  ? 13.941 27.672  11.433 1.00 36.31  ?  55  GLY A N      1 
ATOM   322  C CA     . GLY A 1 55  ? 15.102 27.341  10.620 1.00 37.97  ?  55  GLY A CA     1 
ATOM   323  C C      . GLY A 1 55  ? 15.417 28.315  9.486  1.00 36.85  ?  55  GLY A C      1 
ATOM   324  O O      . GLY A 1 55  ? 15.604 29.521  9.693  1.00 29.68  ?  55  GLY A O      1 
ATOM   325  N N      . ASP A 1 56  ? 15.518 27.779  8.262  1.00 48.69  ?  56  ASP A N      1 
ATOM   326  C CA     . ASP A 1 56  ? 16.054 28.562  7.144  1.00 47.74  ?  56  ASP A CA     1 
ATOM   327  C C      . ASP A 1 56  ? 15.095 29.660  6.711  1.00 48.68  ?  56  ASP A C      1 
ATOM   328  O O      . ASP A 1 56  ? 15.528 30.763  6.352  1.00 44.57  ?  56  ASP A O      1 
ATOM   329  C CB     . ASP A 1 56  ? 16.365 27.662  5.954  1.00 46.60  ?  56  ASP A CB     1 
ATOM   330  C CG     . ASP A 1 56  ? 17.167 26.435  6.340  1.00 54.89  ?  56  ASP A CG     1 
ATOM   331  O OD1    . ASP A 1 56  ? 18.393 26.559  6.571  1.00 56.32  ?  56  ASP A OD1    1 
ATOM   332  O OD2    . ASP A 1 56  ? 16.567 25.339  6.404  1.00 59.82  -1 56  ASP A OD2    1 
ATOM   333  N N      . GLU A 1 57  ? 13.791 29.367  6.722  1.00 51.25  ?  57  GLU A N      1 
ATOM   334  C CA     . GLU A 1 57  ? 12.804 30.340  6.282  1.00 53.56  ?  57  GLU A CA     1 
ATOM   335  C C      . GLU A 1 57  ? 12.713 31.539  7.223  1.00 60.85  ?  57  GLU A C      1 
ATOM   336  O O      . GLU A 1 57  ? 12.459 32.664  6.767  1.00 63.44  ?  57  GLU A O      1 
ATOM   337  C CB     . GLU A 1 57  ? 11.465 29.643  6.147  1.00 56.75  ?  57  GLU A CB     1 
ATOM   338  C CG     . GLU A 1 57  ? 10.447 30.387  5.359  1.00 58.73  ?  57  GLU A CG     1 
ATOM   339  C CD     . GLU A 1 57  ? 9.377  29.450  4.883  1.00 66.16  ?  57  GLU A CD     1 
ATOM   340  O OE1    . GLU A 1 57  ? 9.740  28.436  4.250  1.00 70.39  ?  57  GLU A OE1    1 
ATOM   341  O OE2    . GLU A 1 57  ? 8.188  29.701  5.165  1.00 69.79  -1 57  GLU A OE2    1 
ATOM   342  N N      . ALA A 1 58  ? 12.911 31.331  8.533  1.00 54.78  ?  58  ALA A N      1 
ATOM   343  C CA     . ALA A 1 58  ? 13.074 32.475  9.427  1.00 49.66  ?  58  ALA A CA     1 
ATOM   344  C C      . ALA A 1 58  ? 14.343 33.248  9.097  1.00 48.80  ?  58  ALA A C      1 
ATOM   345  O O      . ALA A 1 58  ? 14.402 34.470  9.296  1.00 48.22  ?  58  ALA A O      1 
ATOM   346  C CB     . ALA A 1 58  ? 13.082 32.023  10.887 1.00 49.26  ?  58  ALA A CB     1 
ATOM   347  N N      . GLN A 1 59  ? 15.356 32.551  8.574  1.00 45.95  ?  59  GLN A N      1 
ATOM   348  C CA     . GLN A 1 59  ? 16.605 33.199  8.183  1.00 43.14  ?  59  GLN A CA     1 
ATOM   349  C C      . GLN A 1 59  ? 16.369 34.173  7.030  1.00 42.50  ?  59  GLN A C      1 
ATOM   350  O O      . GLN A 1 59  ? 16.799 35.333  7.077  1.00 44.23  ?  59  GLN A O      1 
ATOM   351  C CB     . GLN A 1 59  ? 17.634 32.121  7.811  1.00 44.69  ?  59  GLN A CB     1 
ATOM   352  C CG     . GLN A 1 59  ? 19.091 32.569  7.746  1.00 50.77  ?  59  GLN A CG     1 
ATOM   353  C CD     . GLN A 1 59  ? 19.473 33.517  8.872  1.00 58.25  ?  59  GLN A CD     1 
ATOM   354  O OE1    . GLN A 1 59  ? 19.652 34.720  8.645  1.00 59.36  ?  59  GLN A OE1    1 
ATOM   355  N NE2    . GLN A 1 59  ? 19.604 32.982  10.090 1.00 59.87  ?  59  GLN A NE2    1 
ATOM   356  N N      . SER A 1 60  ? 15.653 33.724  5.997  1.00 46.66  ?  60  SER A N      1 
ATOM   357  C CA     . SER A 1 60  ? 15.453 34.556  4.815  1.00 46.43  ?  60  SER A CA     1 
ATOM   358  C C      . SER A 1 60  ? 14.604 35.772  5.140  1.00 49.14  ?  60  SER A C      1 
ATOM   359  O O      . SER A 1 60  ? 14.894 36.883  4.682  1.00 54.47  ?  60  SER A O      1 
ATOM   360  C CB     . SER A 1 60  ? 14.812 33.735  3.699  1.00 50.45  ?  60  SER A CB     1 
ATOM   361  O OG     . SER A 1 60  ? 15.312 32.400  3.676  1.00 48.40  ?  60  SER A OG     1 
ATOM   362  N N      . LYS A 1 61  ? 13.563 35.588  5.942  1.00 43.30  ?  61  LYS A N      1 
ATOM   363  C CA     . LYS A 1 61  ? 12.582 36.626  6.216  1.00 42.34  ?  61  LYS A CA     1 
ATOM   364  C C      . LYS A 1 61  ? 12.881 37.405  7.486  1.00 54.75  ?  61  LYS A C      1 
ATOM   365  O O      . LYS A 1 61  ? 12.053 38.216  7.911  1.00 59.03  ?  61  LYS A O      1 
ATOM   366  C CB     . LYS A 1 61  ? 11.188 36.010  6.253  1.00 36.90  ?  61  LYS A CB     1 
ATOM   367  C CG     . LYS A 1 61  ? 10.822 35.404  4.890  1.00 43.09  ?  61  LYS A CG     1 
ATOM   368  C CD     . LYS A 1 61  ? 9.605  34.510  4.963  1.00 44.95  ?  61  LYS A CD     1 
ATOM   369  C CE     . LYS A 1 61  ? 9.080  34.173  3.579  1.00 49.26  ?  61  LYS A CE     1 
ATOM   370  N NZ     . LYS A 1 61  ? 8.167  32.984  3.597  1.00 48.34  ?  61  LYS A NZ     1 
ATOM   371  N N      . ARG A 1 62  ? 14.055 37.198  8.089  1.00 58.63  ?  62  ARG A N      1 
ATOM   372  C CA     . ARG A 1 62  ? 14.390 37.818  9.371  1.00 52.11  ?  62  ARG A CA     1 
ATOM   373  C C      . ARG A 1 62  ? 14.279 39.345  9.360  1.00 47.30  ?  62  ARG A C      1 
ATOM   374  O O      . ARG A 1 62  ? 14.388 39.956  10.427 1.00 45.10  ?  62  ARG A O      1 
ATOM   375  C CB     . ARG A 1 62  ? 15.801 37.399  9.797  1.00 47.74  ?  62  ARG A CB     1 
ATOM   376  N N      . GLY A 1 63  ? 14.093 39.984  8.201  1.00 47.77  ?  63  GLY A N      1 
ATOM   377  C CA     . GLY A 1 63  ? 13.718 41.398  8.206  1.00 49.35  ?  63  GLY A CA     1 
ATOM   378  C C      . GLY A 1 63  ? 12.307 41.584  8.748  1.00 55.49  ?  63  GLY A C      1 
ATOM   379  O O      . GLY A 1 63  ? 12.082 42.388  9.658  1.00 61.64  ?  63  GLY A O      1 
ATOM   380  N N      . ILE A 1 64  ? 11.342 40.834  8.215  1.00 37.57  ?  64  ILE A N      1 
ATOM   381  C CA     . ILE A 1 64  ? 9.976  40.942  8.714  1.00 30.54  ?  64  ILE A CA     1 
ATOM   382  C C      . ILE A 1 64  ? 9.818  40.304  10.102 1.00 30.73  ?  64  ILE A C      1 
ATOM   383  O O      . ILE A 1 64  ? 9.003  40.777  10.902 1.00 26.22  ?  64  ILE A O      1 
ATOM   384  C CB     . ILE A 1 64  ? 9.005  40.323  7.696  1.00 26.28  ?  64  ILE A CB     1 
ATOM   385  N N      . LEU A 1 65  ? 10.588 39.252  10.413 1.00 46.97  ?  65  LEU A N      1 
ATOM   386  C CA     . LEU A 1 65  ? 10.415 38.466  11.633 1.00 47.64  ?  65  LEU A CA     1 
ATOM   387  C C      . LEU A 1 65  ? 11.288 39.004  12.789 1.00 47.84  ?  65  LEU A C      1 
ATOM   388  O O      . LEU A 1 65  ? 12.068 39.944  12.625 1.00 46.64  ?  65  LEU A O      1 
ATOM   389  C CB     . LEU A 1 65  ? 10.706 36.986  11.334 1.00 37.13  ?  65  LEU A CB     1 
ATOM   390  N N      . THR A 1 66  ? 11.119 38.414  13.983 1.00 49.23  ?  66  THR A N      1 
ATOM   391  C CA     . THR A 1 66  ? 11.932 38.713  15.172 1.00 40.55  ?  66  THR A CA     1 
ATOM   392  C C      . THR A 1 66  ? 12.457 37.401  15.733 1.00 37.62  ?  66  THR A C      1 
ATOM   393  O O      . THR A 1 66  ? 11.710 36.669  16.387 1.00 43.06  ?  66  THR A O      1 
ATOM   394  C CB     . THR A 1 66  ? 11.118 39.457  16.238 1.00 41.21  ?  66  THR A CB     1 
ATOM   395  N N      . LEU A 1 67  ? 13.760 37.160  15.583 1.00 33.87  ?  67  LEU A N      1 
ATOM   396  C CA     . LEU A 1 67  ? 14.341 35.820  15.647 1.00 33.35  ?  67  LEU A CA     1 
ATOM   397  C C      . LEU A 1 67  ? 14.821 35.474  17.055 1.00 33.77  ?  67  LEU A C      1 
ATOM   398  O O      . LEU A 1 67  ? 15.682 36.159  17.599 1.00 35.80  ?  67  LEU A O      1 
ATOM   399  C CB     . LEU A 1 67  ? 15.522 35.723  14.674 1.00 35.89  ?  67  LEU A CB     1 
ATOM   400  C CG     . LEU A 1 67  ? 15.435 35.500  13.149 1.00 35.53  ?  67  LEU A CG     1 
ATOM   401  C CD1    . LEU A 1 67  ? 14.241 36.196  12.503 1.00 33.74  ?  67  LEU A CD1    1 
ATOM   402  C CD2    . LEU A 1 67  ? 16.790 35.895  12.435 1.00 23.34  ?  67  LEU A CD2    1 
ATOM   403  N N      . LYS A 1 68  ? 14.302 34.387  17.625 1.00 43.52  ?  68  LYS A N      1 
ATOM   404  C CA     . LYS A 1 68  ? 14.802 33.829  18.882 1.00 45.35  ?  68  LYS A CA     1 
ATOM   405  C C      . LYS A 1 68  ? 15.496 32.490  18.642 1.00 48.78  ?  68  LYS A C      1 
ATOM   406  O O      . LYS A 1 68  ? 14.930 31.609  17.992 1.00 53.96  ?  68  LYS A O      1 
ATOM   407  C CB     . LYS A 1 68  ? 13.661 33.628  19.884 1.00 44.08  ?  68  LYS A CB     1 
ATOM   408  C CG     . LYS A 1 68  ? 13.152 34.921  20.514 1.00 48.51  ?  68  LYS A CG     1 
ATOM   409  C CD     . LYS A 1 68  ? 12.435 34.688  21.834 1.00 48.30  ?  68  LYS A CD     1 
ATOM   410  C CE     . LYS A 1 68  ? 11.053 34.054  21.659 1.00 51.65  ?  68  LYS A CE     1 
ATOM   411  N NZ     . LYS A 1 68  ? 10.259 33.959  22.955 1.00 44.68  ?  68  LYS A NZ     1 
ATOM   412  N N      . TYR A 1 69  ? 16.631 32.332  19.307 1.00 64.07  ?  69  TYR A N      1 
ATOM   413  C CA     . TYR A 1 69  ? 17.344 31.078  19.290 1.00 63.84  ?  69  TYR A CA     1 
ATOM   414  C C      . TYR A 1 69  ? 17.063 30.407  20.667 1.00 52.93  ?  69  TYR A C      1 
ATOM   415  O O      . TYR A 1 69  ? 17.685 30.777  21.636 1.00 47.59  ?  69  TYR A O      1 
ATOM   416  C CB     . TYR A 1 69  ? 18.828 31.317  19.058 1.00 65.48  ?  69  TYR A CB     1 
ATOM   417  C CG     . TYR A 1 69  ? 19.068 32.547  18.214 1.00 73.66  ?  69  TYR A CG     1 
ATOM   418  C CD1    . TYR A 1 69  ? 18.889 32.513  16.842 1.00 71.85  ?  69  TYR A CD1    1 
ATOM   419  C CD2    . TYR A 1 69  ? 19.443 33.749  18.793 1.00 77.62  ?  69  TYR A CD2    1 
ATOM   420  C CE1    . TYR A 1 69  ? 19.088 33.637  16.070 1.00 72.00  ?  69  TYR A CE1    1 
ATOM   421  C CE2    . TYR A 1 69  ? 19.641 34.878  18.027 1.00 76.58  ?  69  TYR A CE2    1 
ATOM   422  C CZ     . TYR A 1 69  ? 19.464 34.816  16.666 1.00 76.83  ?  69  TYR A CZ     1 
ATOM   423  O OH     . TYR A 1 69  ? 19.665 35.940  15.894 1.00 80.98  ?  69  TYR A OH     1 
ATOM   424  N N      . PRO A 1 70  ? 16.099 29.443  20.745 1.00 38.67  ?  70  PRO A N      1 
ATOM   425  C CA     . PRO A 1 70  ? 15.829 28.842  22.057 1.00 41.06  ?  70  PRO A CA     1 
ATOM   426  C C      . PRO A 1 70  ? 16.900 27.887  22.541 1.00 41.77  ?  70  PRO A C      1 
ATOM   427  O O      . PRO A 1 70  ? 16.858 27.474  23.706 1.00 35.65  ?  70  PRO A O      1 
ATOM   428  C CB     . PRO A 1 70  ? 14.513 28.101  21.812 1.00 40.08  ?  70  PRO A CB     1 
ATOM   429  C CG     . PRO A 1 70  ? 14.677 27.646  20.388 1.00 36.45  ?  70  PRO A CG     1 
ATOM   430  C CD     . PRO A 1 70  ? 15.302 28.803  19.688 1.00 39.09  ?  70  PRO A CD     1 
ATOM   431  N N      . ILE A 1 71  ? 17.770 27.403  21.662 1.00 43.06  ?  71  ILE A N      1 
ATOM   432  C CA     . ILE A 1 71  ? 18.835 26.516  22.087 1.00 41.17  ?  71  ILE A CA     1 
ATOM   433  C C      . ILE A 1 71  ? 20.165 27.250  22.222 1.00 46.76  ?  71  ILE A C      1 
ATOM   434  O O      . ILE A 1 71  ? 21.202 26.614  22.458 1.00 48.23  ?  71  ILE A O      1 
ATOM   435  C CB     . ILE A 1 71  ? 18.931 25.301  21.168 1.00 38.53  ?  71  ILE A CB     1 
ATOM   436  C CG1    . ILE A 1 71  ? 17.799 24.353  21.500 1.00 38.09  ?  71  ILE A CG1    1 
ATOM   437  C CG2    . ILE A 1 71  ? 20.161 24.520  21.473 1.00 47.84  ?  71  ILE A CG2    1 
ATOM   438  C CD1    . ILE A 1 71  ? 18.193 23.353  22.531 1.00 42.63  ?  71  ILE A CD1    1 
ATOM   439  N N      . GLU A 1 72  ? 20.165 28.565  22.111 1.00 49.32  ?  72  GLU A N      1 
ATOM   440  C CA     . GLU A 1 72  ? 21.401 29.295  22.216 1.00 49.36  ?  72  GLU A CA     1 
ATOM   441  C C      . GLU A 1 72  ? 22.107 28.849  23.470 1.00 58.71  ?  72  GLU A C      1 
ATOM   442  O O      . GLU A 1 72  ? 21.487 28.850  24.524 1.00 70.41  ?  72  GLU A O      1 
ATOM   443  C CB     . GLU A 1 72  ? 21.158 30.785  22.205 1.00 49.39  ?  72  GLU A CB     1 
ATOM   444  C CG     . GLU A 1 72  ? 22.405 31.624  22.378 1.00 61.24  ?  72  GLU A CG     1 
ATOM   445  C CD     . GLU A 1 72  ? 22.087 33.058  22.728 1.00 67.49  ?  72  GLU A CD     1 
ATOM   446  O OE1    . GLU A 1 72  ? 21.494 33.283  23.798 1.00 68.69  ?  72  GLU A OE1    1 
ATOM   447  O OE2    . GLU A 1 72  ? 22.420 33.959  21.935 1.00 66.14  -1 72  GLU A OE2    1 
ATOM   448  N N      . HIS A 1 73  ? 23.364 28.438  23.367 1.00 51.98  ?  73  HIS A N      1 
ATOM   449  C CA     . HIS A 1 73  ? 24.152 27.934  24.498 1.00 50.76  ?  73  HIS A CA     1 
ATOM   450  C C      . HIS A 1 73  ? 23.918 26.472  24.867 1.00 51.13  ?  73  HIS A C      1 
ATOM   451  O O      . HIS A 1 73  ? 24.416 26.030  25.892 1.00 56.64  ?  73  HIS A O      1 
ATOM   452  C CB     . HIS A 1 73  ? 24.088 28.842  25.719 1.00 51.00  ?  73  HIS A CB     1 
ATOM   453  C CG     . HIS A 1 73  ? 24.483 30.255  25.456 1.00 50.03  ?  73  HIS A CG     1 
ATOM   454  N ND1    . HIS A 1 73  ? 23.718 31.322  25.869 1.00 48.66  ?  73  HIS A ND1    1 
ATOM   455  C CD2    . HIS A 1 73  ? 25.563 30.779  24.838 1.00 51.35  ?  73  HIS A CD2    1 
ATOM   456  C CE1    . HIS A 1 73  ? 24.309 32.445  25.511 1.00 52.46  ?  73  HIS A CE1    1 
ATOM   457  N NE2    . HIS A 1 73  ? 25.428 32.144  24.880 1.00 51.40  ?  73  HIS A NE2    1 
ATOM   458  N N      . GLY A 1 74  ? 23.196 25.713  24.051 1.00 27.89  ?  74  GLY A N      1 
ATOM   459  C CA     . GLY A 1 74  ? 23.009 24.289  24.268 1.00 21.21  ?  74  GLY A CA     1 
ATOM   460  C C      . GLY A 1 74  ? 21.839 23.804  25.087 1.00 27.99  ?  74  GLY A C      1 
ATOM   461  O O      . GLY A 1 74  ? 21.379 22.689  24.923 1.00 31.94  ?  74  GLY A O      1 
ATOM   462  N N      . ILE A 1 75  ? 21.377 24.613  26.012 1.00 33.59  ?  75  ILE A N      1 
ATOM   463  C CA     . ILE A 1 75  ? 20.244 24.257  26.830 1.00 36.31  ?  75  ILE A CA     1 
ATOM   464  C C      . ILE A 1 75  ? 18.994 24.939  26.324 1.00 34.76  ?  75  ILE A C      1 
ATOM   465  O O      . ILE A 1 75  ? 19.010 26.139  26.134 1.00 33.89  ?  75  ILE A O      1 
ATOM   466  C CB     . ILE A 1 75  ? 20.511 24.616  28.303 1.00 44.39  ?  75  ILE A CB     1 
ATOM   467  C CG1    . ILE A 1 75  ? 21.772 23.919  28.807 1.00 43.93  ?  75  ILE A CG1    1 
ATOM   468  C CG2    . ILE A 1 75  ? 19.341 24.251  29.191 1.00 42.12  ?  75  ILE A CG2    1 
ATOM   469  C CD1    . ILE A 1 75  ? 22.090 24.227  30.250 1.00 34.91  ?  75  ILE A CD1    1 
ATOM   470  N N      . VAL A 1 76  ? 17.939 24.176  26.070 1.00 27.32  ?  76  VAL A N      1 
ATOM   471  C CA     . VAL A 1 76  ? 16.650 24.703  25.591 1.00 28.55  ?  76  VAL A CA     1 
ATOM   472  C C      . VAL A 1 76  ? 16.143 25.765  26.557 1.00 36.61  ?  76  VAL A C      1 
ATOM   473  O O      . VAL A 1 76  ? 15.898 25.479  27.742 1.00 29.13  ?  76  VAL A O      1 
ATOM   474  C CB     . VAL A 1 76  ? 15.598 23.582  25.459 1.00 27.19  ?  76  VAL A CB     1 
ATOM   475  C CG1    . VAL A 1 76  ? 14.265 24.168  25.060 1.00 32.97  ?  76  VAL A CG1    1 
ATOM   476  C CG2    . VAL A 1 76  ? 16.022 22.444  24.478 1.00 24.81  ?  76  VAL A CG2    1 
ATOM   477  N N      . THR A 1 77  ? 15.908 26.977  26.032 1.00 46.20  ?  77  THR A N      1 
ATOM   478  C CA     . THR A 1 77  ? 15.516 28.146  26.821 1.00 45.04  ?  77  THR A CA     1 
ATOM   479  C C      . THR A 1 77  ? 14.016 28.400  26.728 1.00 51.64  ?  77  THR A C      1 
ATOM   480  O O      . THR A 1 77  ? 13.335 28.457  27.761 1.00 62.06  ?  77  THR A O      1 
ATOM   481  C CB     . THR A 1 77  ? 16.305 29.397  26.404 1.00 49.73  ?  77  THR A CB     1 
ATOM   482  O OG1    . THR A 1 77  ? 15.969 29.766  25.058 1.00 53.30  ?  77  THR A OG1    1 
ATOM   483  C CG2    . THR A 1 77  ? 17.799 29.137  26.492 1.00 53.80  ?  77  THR A CG2    1 
ATOM   484  N N      . ASN A 1 78  ? 13.485 28.605  25.516 1.00 37.79  ?  78  ASN A N      1 
ATOM   485  C CA     . ASN A 1 78  ? 12.039 28.693  25.339 1.00 38.18  ?  78  ASN A CA     1 
ATOM   486  C C      . ASN A 1 78  ? 11.464 27.388  24.809 1.00 35.73  ?  78  ASN A C      1 
ATOM   487  O O      . ASN A 1 78  ? 11.842 26.919  23.723 1.00 35.33  ?  78  ASN A O      1 
ATOM   488  C CB     . ASN A 1 78  ? 11.611 29.831  24.418 1.00 37.62  ?  78  ASN A CB     1 
ATOM   489  C CG     . ASN A 1 78  ? 10.108 29.939  24.353 1.00 39.23  ?  78  ASN A CG     1 
ATOM   490  O OD1    . ASN A 1 78  ? 9.508  29.693  23.322 1.00 44.97  ?  78  ASN A OD1    1 
ATOM   491  N ND2    . ASN A 1 78  ? 9.489  30.234  25.484 1.00 41.27  ?  78  ASN A ND2    1 
ATOM   492  N N      . TRP A 1 79  ? 10.498 26.846  25.552 1.00 31.92  ?  79  TRP A N      1 
ATOM   493  C CA     . TRP A 1 79  ? 9.792  25.641  25.128 1.00 36.82  ?  79  TRP A CA     1 
ATOM   494  C C      . TRP A 1 79  ? 8.695  25.914  24.094 1.00 38.90  ?  79  TRP A C      1 
ATOM   495  O O      . TRP A 1 79  ? 8.435  25.063  23.233 1.00 32.90  ?  79  TRP A O      1 
ATOM   496  C CB     . TRP A 1 79  ? 9.211  24.931  26.340 1.00 27.30  ?  79  TRP A CB     1 
ATOM   497  C CG     . TRP A 1 79  ? 10.272 24.416  27.243 1.00 37.12  ?  79  TRP A CG     1 
ATOM   498  C CD1    . TRP A 1 79  ? 10.694 24.985  28.413 1.00 36.39  ?  79  TRP A CD1    1 
ATOM   499  C CD2    . TRP A 1 79  ? 11.062 23.229  27.063 1.00 34.93  ?  79  TRP A CD2    1 
ATOM   500  N NE1    . TRP A 1 79  ? 11.689 24.231  28.967 1.00 38.11  ?  79  TRP A NE1    1 
ATOM   501  C CE2    . TRP A 1 79  ? 11.941 23.147  28.163 1.00 36.55  ?  79  TRP A CE2    1 
ATOM   502  C CE3    . TRP A 1 79  ? 11.112 22.230  26.079 1.00 35.12  ?  79  TRP A CE3    1 
ATOM   503  C CZ2    . TRP A 1 79  ? 12.876 22.103  28.311 1.00 34.97  ?  79  TRP A CZ2    1 
ATOM   504  C CZ3    . TRP A 1 79  ? 12.050 21.192  26.218 1.00 37.02  ?  79  TRP A CZ3    1 
ATOM   505  C CH2    . TRP A 1 79  ? 12.909 21.134  27.337 1.00 38.52  ?  79  TRP A CH2    1 
ATOM   506  N N      . ASP A 1 80  ? 8.008  27.059  24.180 1.00 56.55  ?  80  ASP A N      1 
ATOM   507  C CA     . ASP A 1 80  ? 7.060  27.397  23.119 1.00 61.91  ?  80  ASP A CA     1 
ATOM   508  C C      . ASP A 1 80  ? 7.762  27.410  21.757 1.00 59.22  ?  80  ASP A C      1 
ATOM   509  O O      . ASP A 1 80  ? 7.219  26.897  20.767 1.00 56.54  ?  80  ASP A O      1 
ATOM   510  C CB     . ASP A 1 80  ? 6.380  28.748  23.399 1.00 63.02  ?  80  ASP A CB     1 
ATOM   511  C CG     . ASP A 1 80  ? 5.477  28.726  24.634 1.00 68.57  ?  80  ASP A CG     1 
ATOM   512  O OD1    . ASP A 1 80  ? 4.690  27.772  24.799 1.00 68.22  ?  80  ASP A OD1    1 
ATOM   513  O OD2    . ASP A 1 80  ? 5.546  29.683  25.440 1.00 72.82  -1 80  ASP A OD2    1 
ATOM   514  N N      . ASP A 1 81  ? 8.983  27.984  21.699 1.00 35.06  ?  81  ASP A N      1 
ATOM   515  C CA     . ASP A 1 81  ? 9.784  27.966  20.475 1.00 34.86  ?  81  ASP A CA     1 
ATOM   516  C C      . ASP A 1 81  ? 10.418 26.607  20.223 1.00 39.05  ?  81  ASP A C      1 
ATOM   517  O O      . ASP A 1 81  ? 10.666 26.255  19.062 1.00 37.74  ?  81  ASP A O      1 
ATOM   518  C CB     . ASP A 1 81  ? 10.895 29.017  20.512 1.00 35.88  ?  81  ASP A CB     1 
ATOM   519  C CG     . ASP A 1 81  ? 10.366 30.421  20.601 1.00 42.20  ?  81  ASP A CG     1 
ATOM   520  O OD1    . ASP A 1 81  ? 9.143  30.598  20.440 1.00 35.91  ?  81  ASP A OD1    1 
ATOM   521  O OD2    . ASP A 1 81  ? 11.178 31.349  20.833 1.00 53.69  -1 81  ASP A OD2    1 
ATOM   522  N N      . MET A 1 82  ? 10.716 25.844  21.284 1.00 39.87  ?  82  MET A N      1 
ATOM   523  C CA     . MET A 1 82  ? 11.287 24.514  21.082 1.00 33.66  ?  82  MET A CA     1 
ATOM   524  C C      . MET A 1 82  ? 10.282 23.585  20.416 1.00 33.83  ?  82  MET A C      1 
ATOM   525  O O      . MET A 1 82  ? 10.642 22.837  19.496 1.00 32.14  ?  82  MET A O      1 
ATOM   526  C CB     . MET A 1 82  ? 11.752 23.937  22.413 1.00 38.49  ?  82  MET A CB     1 
ATOM   527  C CG     . MET A 1 82  ? 12.735 22.794  22.293 1.00 41.55  ?  82  MET A CG     1 
ATOM   528  S SD     . MET A 1 82  ? 14.209 23.290  21.378 1.00 44.43  ?  82  MET A SD     1 
ATOM   529  C CE     . MET A 1 82  ? 14.456 24.971  21.926 1.00 39.96  ?  82  MET A CE     1 
ATOM   530  N N      . GLU A 1 83  ? 9.020  23.630  20.866 1.00 40.23  ?  83  GLU A N      1 
ATOM   531  C CA     . GLU A 1 83  ? 7.943  22.857  20.245 1.00 38.99  ?  83  GLU A CA     1 
ATOM   532  C C      . GLU A 1 83  ? 7.844  23.141  18.758 1.00 35.10  ?  83  GLU A C      1 
ATOM   533  O O      . GLU A 1 83  ? 7.644  22.224  17.960 1.00 33.13  ?  83  GLU A O      1 
ATOM   534  C CB     . GLU A 1 83  ? 6.600  23.180  20.899 1.00 43.42  ?  83  GLU A CB     1 
ATOM   535  C CG     . GLU A 1 83  ? 6.333  22.568  22.243 1.00 46.44  ?  83  GLU A CG     1 
ATOM   536  C CD     . GLU A 1 83  ? 5.051  23.098  22.832 1.00 51.22  ?  83  GLU A CD     1 
ATOM   537  O OE1    . GLU A 1 83  ? 4.546  24.111  22.296 1.00 52.96  ?  83  GLU A OE1    1 
ATOM   538  O OE2    . GLU A 1 83  ? 4.554  22.516  23.826 1.00 51.65  -1 83  GLU A OE2    1 
ATOM   539  N N      . LYS A 1 84  ? 7.943  24.426  18.382 1.00 31.83  ?  84  LYS A N      1 
ATOM   540  C CA     . LYS A 1 84  ? 7.870  24.845  16.982 1.00 30.01  ?  84  LYS A CA     1 
ATOM   541  C C      . LYS A 1 84  ? 9.008  24.238  16.177 1.00 33.42  ?  84  LYS A C      1 
ATOM   542  O O      . LYS A 1 84  ? 8.777  23.504  15.209 1.00 33.56  ?  84  LYS A O      1 
ATOM   543  C CB     . LYS A 1 84  ? 7.884  26.378  16.893 1.00 29.73  ?  84  LYS A CB     1 
ATOM   544  C CG     . LYS A 1 84  ? 6.539  27.015  17.308 1.00 32.00  ?  84  LYS A CG     1 
ATOM   545  C CD     . LYS A 1 84  ? 6.636  28.446  17.855 1.00 33.26  ?  84  LYS A CD     1 
ATOM   546  C CE     . LYS A 1 84  ? 5.309  28.868  18.533 1.00 40.50  ?  84  LYS A CE     1 
ATOM   547  N NZ     . LYS A 1 84  ? 4.733  27.836  19.494 1.00 42.64  ?  84  LYS A NZ     1 
ATOM   548  N N      . ILE A 1 85  ? 10.253 24.499  16.596 1.00 35.23  ?  85  ILE A N      1 
ATOM   549  C CA     . ILE A 1 85  ? 11.407 23.837  15.995 1.00 31.29  ?  85  ILE A CA     1 
ATOM   550  C C      . ILE A 1 85  ? 11.151 22.336  15.879 1.00 31.10  ?  85  ILE A C      1 
ATOM   551  O O      . ILE A 1 85  ? 11.390 21.730  14.828 1.00 34.10  ?  85  ILE A O      1 
ATOM   552  C CB     . ILE A 1 85  ? 12.685 24.158  16.807 1.00 34.54  ?  85  ILE A CB     1 
ATOM   553  C CG1    . ILE A 1 85  ? 13.105 25.626  16.624 1.00 37.85  ?  85  ILE A CG1    1 
ATOM   554  C CG2    . ILE A 1 85  ? 13.876 23.241  16.455 1.00 21.07  ?  85  ILE A CG2    1 
ATOM   555  C CD1    . ILE A 1 85  ? 14.470 25.938  17.251 1.00 39.41  ?  85  ILE A CD1    1 
ATOM   556  N N      . TRP A 1 86  ? 10.606 21.720  16.931 1.00 32.53  ?  86  TRP A N      1 
ATOM   557  C CA     . TRP A 1 86  ? 10.363 20.282  16.896 1.00 28.99  ?  86  TRP A CA     1 
ATOM   558  C C      . TRP A 1 86  ? 9.237  19.916  15.937 1.00 34.36  ?  86  TRP A C      1 
ATOM   559  O O      . TRP A 1 86  ? 9.338  18.919  15.214 1.00 33.10  ?  86  TRP A O      1 
ATOM   560  C CB     . TRP A 1 86  ? 10.050 19.756  18.297 1.00 27.94  ?  86  TRP A CB     1 
ATOM   561  C CG     . TRP A 1 86  ? 11.277 19.365  19.033 1.00 36.05  ?  86  TRP A CG     1 
ATOM   562  C CD1    . TRP A 1 86  ? 12.487 19.056  18.490 1.00 31.66  ?  86  TRP A CD1    1 
ATOM   563  C CD2    . TRP A 1 86  ? 11.437 19.257  20.461 1.00 43.05  ?  86  TRP A CD2    1 
ATOM   564  N NE1    . TRP A 1 86  ? 13.387 18.748  19.483 1.00 32.31  ?  86  TRP A NE1    1 
ATOM   565  C CE2    . TRP A 1 86  ? 12.769 18.863  20.701 1.00 39.96  ?  86  TRP A CE2    1 
ATOM   566  C CE3    . TRP A 1 86  ? 10.582 19.441  21.552 1.00 40.10  ?  86  TRP A CE3    1 
ATOM   567  C CZ2    . TRP A 1 86  ? 13.267 18.663  21.987 1.00 38.47  ?  86  TRP A CZ2    1 
ATOM   568  C CZ3    . TRP A 1 86  ? 11.077 19.239  22.822 1.00 38.48  ?  86  TRP A CZ3    1 
ATOM   569  C CH2    . TRP A 1 86  ? 12.405 18.856  23.032 1.00 37.01  ?  86  TRP A CH2    1 
ATOM   570  N N      . HIS A 1 87  ? 8.136  20.672  15.941 1.00 45.74  ?  87  HIS A N      1 
ATOM   571  C CA     . HIS A 1 87  ? 7.068  20.379  14.989 1.00 46.01  ?  87  HIS A CA     1 
ATOM   572  C C      . HIS A 1 87  ? 7.582  20.519  13.569 1.00 42.98  ?  87  HIS A C      1 
ATOM   573  O O      . HIS A 1 87  ? 7.377  19.638  12.723 1.00 43.46  ?  87  HIS A O      1 
ATOM   574  C CB     . HIS A 1 87  ? 5.862  21.294  15.205 1.00 46.85  ?  87  HIS A CB     1 
ATOM   575  C CG     . HIS A 1 87  ? 4.828  21.175  14.129 1.00 47.98  ?  87  HIS A CG     1 
ATOM   576  N ND1    . HIS A 1 87  ? 3.731  20.351  14.236 1.00 50.49  ?  87  HIS A ND1    1 
ATOM   577  C CD2    . HIS A 1 87  ? 4.745  21.752  12.907 1.00 45.21  ?  87  HIS A CD2    1 
ATOM   578  C CE1    . HIS A 1 87  ? 3.013  20.428  13.129 1.00 45.95  ?  87  HIS A CE1    1 
ATOM   579  N NE2    . HIS A 1 87  ? 3.612  21.269  12.306 1.00 44.63  ?  87  HIS A NE2    1 
ATOM   580  N N      . HIS A 1 88  ? 8.267  21.634  13.301 1.00 33.97  ?  88  HIS A N      1 
ATOM   581  C CA     . HIS A 1 88  ? 8.901  21.845  12.011 1.00 32.53  ?  88  HIS A CA     1 
ATOM   582  C C      . HIS A 1 88  ? 9.789  20.670  11.640 1.00 34.93  ?  88  HIS A C      1 
ATOM   583  O O      . HIS A 1 88  ? 9.762  20.183  10.503 1.00 38.97  ?  88  HIS A O      1 
ATOM   584  C CB     . HIS A 1 88  ? 9.710  23.137  12.064 1.00 32.58  ?  88  HIS A CB     1 
ATOM   585  C CG     . HIS A 1 88  ? 10.326 23.526  10.758 1.00 38.26  ?  88  HIS A CG     1 
ATOM   586  N ND1    . HIS A 1 88  ? 9.636  24.220  9.789  1.00 44.40  ?  88  HIS A ND1    1 
ATOM   587  C CD2    . HIS A 1 88  ? 11.576 23.350  10.272 1.00 38.99  ?  88  HIS A CD2    1 
ATOM   588  C CE1    . HIS A 1 88  ? 10.431 24.450  8.760  1.00 42.50  ?  88  HIS A CE1    1 
ATOM   589  N NE2    . HIS A 1 88  ? 11.616 23.937  9.029  1.00 39.77  ?  88  HIS A NE2    1 
ATOM   590  N N      . THR A 1 89  ? 10.593 20.199  12.586 1.00 24.26  ?  89  THR A N      1 
ATOM   591  C CA     . THR A 1 89  ? 11.480 19.096  12.258 1.00 24.86  ?  89  THR A CA     1 
ATOM   592  C C      . THR A 1 89  ? 10.697 17.868  11.836 1.00 24.57  ?  89  THR A C      1 
ATOM   593  O O      . THR A 1 89  ? 11.051 17.220  10.851 1.00 25.58  ?  89  THR A O      1 
ATOM   594  C CB     . THR A 1 89  ? 12.396 18.772  13.434 1.00 24.40  ?  89  THR A CB     1 
ATOM   595  O OG1    . THR A 1 89  ? 13.315 19.844  13.598 1.00 21.15  ?  89  THR A OG1    1 
ATOM   596  C CG2    . THR A 1 89  ? 13.193 17.530  13.139 1.00 25.54  ?  89  THR A CG2    1 
ATOM   597  N N      . PHE A 1 90  ? 9.639  17.523  12.573 1.00 35.69  ?  90  PHE A N      1 
ATOM   598  C CA     . PHE A 1 90  ? 8.926  16.265  12.345 1.00 34.63  ?  90  PHE A CA     1 
ATOM   599  C C      . PHE A 1 90  ? 8.102  16.294  11.062 1.00 34.71  ?  90  PHE A C      1 
ATOM   600  O O      . PHE A 1 90  ? 8.222  15.402  10.220 1.00 36.12  ?  90  PHE A O      1 
ATOM   601  C CB     . PHE A 1 90  ? 8.004  15.954  13.528 1.00 31.98  ?  90  PHE A CB     1 
ATOM   602  C CG     . PHE A 1 90  ? 8.715  15.596  14.803 1.00 38.95  ?  90  PHE A CG     1 
ATOM   603  C CD1    . PHE A 1 90  ? 9.720  14.642  14.821 1.00 43.10  ?  90  PHE A CD1    1 
ATOM   604  C CD2    . PHE A 1 90  ? 8.336  16.188  15.998 1.00 40.03  ?  90  PHE A CD2    1 
ATOM   605  C CE1    . PHE A 1 90  ? 10.337 14.307  16.003 1.00 45.31  ?  90  PHE A CE1    1 
ATOM   606  C CE2    . PHE A 1 90  ? 8.939  15.853  17.179 1.00 40.87  ?  90  PHE A CE2    1 
ATOM   607  C CZ     . PHE A 1 90  ? 9.942  14.919  17.187 1.00 47.20  ?  90  PHE A CZ     1 
ATOM   608  N N      . TYR A 1 91  ? 7.205  17.278  10.931 1.00 36.06  ?  91  TYR A N      1 
ATOM   609  C CA     . TYR A 1 91  ? 6.222  17.280  9.850  1.00 33.34  ?  91  TYR A CA     1 
ATOM   610  C C      . TYR A 1 91  ? 6.762  17.849  8.546  1.00 41.22  ?  91  TYR A C      1 
ATOM   611  O O      . TYR A 1 91  ? 6.341  17.396  7.471  1.00 45.27  ?  91  TYR A O      1 
ATOM   612  C CB     . TYR A 1 91  ? 4.973  18.055  10.259 1.00 35.56  ?  91  TYR A CB     1 
ATOM   613  C CG     . TYR A 1 91  ? 4.258  17.424  11.423 1.00 45.29  ?  91  TYR A CG     1 
ATOM   614  C CD1    . TYR A 1 91  ? 3.296  16.439  11.226 1.00 45.59  ?  91  TYR A CD1    1 
ATOM   615  C CD2    . TYR A 1 91  ? 4.560  17.796  12.720 1.00 42.69  ?  91  TYR A CD2    1 
ATOM   616  C CE1    . TYR A 1 91  ? 2.663  15.857  12.287 1.00 39.51  ?  91  TYR A CE1    1 
ATOM   617  C CE2    . TYR A 1 91  ? 3.917  17.225  13.783 1.00 38.79  ?  91  TYR A CE2    1 
ATOM   618  C CZ     . TYR A 1 91  ? 2.969  16.257  13.562 1.00 39.04  ?  91  TYR A CZ     1 
ATOM   619  O OH     . TYR A 1 91  ? 2.343  15.670  14.637 1.00 44.54  ?  91  TYR A OH     1 
ATOM   620  N N      . ASN A 1 92  ? 7.686  18.815  8.618  1.00 45.23  ?  92  ASN A N      1 
ATOM   621  C CA     . ASN A 1 92  ? 8.228  19.506  7.447  1.00 38.04  ?  92  ASN A CA     1 
ATOM   622  C C      . ASN A 1 92  ? 9.589  18.976  6.991  1.00 47.31  ?  92  ASN A C      1 
ATOM   623  O O      . ASN A 1 92  ? 9.730  18.536  5.841  1.00 52.88  ?  92  ASN A O      1 
ATOM   624  C CB     . ASN A 1 92  ? 8.322  21.002  7.731  1.00 34.40  ?  92  ASN A CB     1 
ATOM   625  C CG     . ASN A 1 92  ? 6.980  21.633  7.814  1.00 45.10  ?  92  ASN A CG     1 
ATOM   626  O OD1    . ASN A 1 92  ? 5.979  20.943  7.977  1.00 47.96  ?  92  ASN A OD1    1 
ATOM   627  N ND2    . ASN A 1 92  ? 6.933  22.952  7.694  1.00 52.76  ?  92  ASN A ND2    1 
ATOM   628  N N      . GLU A 1 93  ? 10.606 18.987  7.827  1.00 35.74  ?  93  GLU A N      1 
ATOM   629  C CA     . GLU A 1 93  ? 11.906 18.549  7.372  1.00 28.04  ?  93  GLU A CA     1 
ATOM   630  C C      . GLU A 1 93  ? 11.944 17.064  7.196  1.00 36.70  ?  93  GLU A C      1 
ATOM   631  O O      . GLU A 1 93  ? 12.363 16.582  6.174  1.00 46.17  ?  93  GLU A O      1 
ATOM   632  C CB     . GLU A 1 93  ? 12.964 19.001  8.325  1.00 27.16  ?  93  GLU A CB     1 
ATOM   633  C CG     . GLU A 1 93  ? 12.853 20.448  8.736  1.00 33.68  ?  93  GLU A CG     1 
ATOM   634  C CD     . GLU A 1 93  ? 13.287 21.409  7.664  1.00 34.32  ?  93  GLU A CD     1 
ATOM   635  O OE1    . GLU A 1 93  ? 14.492 21.602  7.490  1.00 38.57  ?  93  GLU A OE1    1 
ATOM   636  O OE2    . GLU A 1 93  ? 12.416 21.998  7.008  1.00 43.64  -1 93  GLU A OE2    1 
ATOM   637  N N      . LEU A 1 94  ? 11.364 16.310  8.075  1.00 44.92  ?  94  LEU A N      1 
ATOM   638  C CA     . LEU A 1 94  ? 11.462 14.897  7.941  1.00 42.29  ?  94  LEU A CA     1 
ATOM   639  C C      . LEU A 1 94  ? 10.227 14.395  7.260  1.00 38.39  ?  94  LEU A C      1 
ATOM   640  O O      . LEU A 1 94  ? 10.253 13.326  6.693  1.00 37.76  ?  94  LEU A O      1 
ATOM   641  C CB     . LEU A 1 94  ? 11.710 14.274  9.308  1.00 44.44  ?  94  LEU A CB     1 
ATOM   642  C CG     . LEU A 1 94  ? 13.053 14.468  9.991  1.00 38.81  ?  94  LEU A CG     1 
ATOM   643  C CD1    . LEU A 1 94  ? 13.218 13.327  10.972 1.00 37.56  ?  94  LEU A CD1    1 
ATOM   644  C CD2    . LEU A 1 94  ? 14.177 14.438  8.973  1.00 39.31  ?  94  LEU A CD2    1 
ATOM   645  N N      . ARG A 1 95  ? 9.178  15.207  7.239  1.00 39.23  ?  95  ARG A N      1 
ATOM   646  C CA     . ARG A 1 95  ? 7.910  14.815  6.629  1.00 42.66  ?  95  ARG A CA     1 
ATOM   647  C C      . ARG A 1 95  ? 7.518  13.430  7.139  1.00 41.27  ?  95  ARG A C      1 
ATOM   648  O O      . ARG A 1 95  ? 7.454  12.447  6.397  1.00 48.23  ?  95  ARG A O      1 
ATOM   649  C CB     . ARG A 1 95  ? 7.985  14.870  5.095  1.00 44.99  ?  95  ARG A CB     1 
ATOM   650  C CG     . ARG A 1 95  ? 8.589  16.176  4.532  1.00 43.84  ?  95  ARG A CG     1 
ATOM   651  C CD     . ARG A 1 95  ? 8.419  16.268  3.020  1.00 47.93  ?  95  ARG A CD     1 
ATOM   652  N NE     . ARG A 1 95  ? 7.037  15.995  2.635  1.00 56.22  ?  95  ARG A NE     1 
ATOM   653  C CZ     . ARG A 1 95  ? 6.024  16.825  2.872  1.00 61.96  ?  95  ARG A CZ     1 
ATOM   654  N NH1    . ARG A 1 95  ? 6.243  17.981  3.495  1.00 61.91  ?  95  ARG A NH1    1 
ATOM   655  N NH2    . ARG A 1 95  ? 4.790  16.499  2.498  1.00 60.58  ?  95  ARG A NH2    1 
ATOM   656  N N      . VAL A 1 96  ? 7.271  13.388  8.449  1.00 30.80  ?  96  VAL A N      1 
ATOM   657  C CA     . VAL A 1 96  ? 7.054  12.167  9.226  1.00 28.98  ?  96  VAL A CA     1 
ATOM   658  C C      . VAL A 1 96  ? 6.008  12.465  10.285 1.00 31.57  ?  96  VAL A C      1 
ATOM   659  O O      . VAL A 1 96  ? 5.975  13.564  10.839 1.00 34.40  ?  96  VAL A O      1 
ATOM   660  C CB     . VAL A 1 96  ? 8.349  11.668  9.912  1.00 23.73  ?  96  VAL A CB     1 
ATOM   661  C CG1    . VAL A 1 96  ? 8.050  10.435  10.681 1.00 22.87  ?  96  VAL A CG1    1 
ATOM   662  C CG2    . VAL A 1 96  ? 9.427  11.390  8.914  1.00 23.74  ?  96  VAL A CG2    1 
ATOM   663  N N      . ALA A 1 97  ? 5.172  11.482  10.597 1.00 42.54  ?  97  ALA A N      1 
ATOM   664  C CA     . ALA A 1 97  ? 4.250  11.631  11.715 1.00 42.41  ?  97  ALA A CA     1 
ATOM   665  C C      . ALA A 1 97  ? 4.961  11.142  12.968 1.00 42.44  ?  97  ALA A C      1 
ATOM   666  O O      . ALA A 1 97  ? 5.250  9.943   13.067 1.00 44.78  ?  97  ALA A O      1 
ATOM   667  C CB     . ALA A 1 97  ? 2.964  10.842  11.478 1.00 41.95  ?  97  ALA A CB     1 
ATOM   668  N N      . PRO A 1 98  ? 5.270  12.015  13.943 1.00 35.39  ?  98  PRO A N      1 
ATOM   669  C CA     . PRO A 1 98  ? 6.108  11.573  15.068 1.00 30.54  ?  98  PRO A CA     1 
ATOM   670  C C      . PRO A 1 98  ? 5.436  10.507  15.890 1.00 31.07  ?  98  PRO A C      1 
ATOM   671  O O      . PRO A 1 98  ? 6.123  9.686   16.492 1.00 36.04  ?  98  PRO A O      1 
ATOM   672  C CB     . PRO A 1 98  ? 6.323  12.857  15.869 1.00 32.77  ?  98  PRO A CB     1 
ATOM   673  C CG     . PRO A 1 98  ? 5.050  13.582  15.660 1.00 36.30  ?  98  PRO A CG     1 
ATOM   674  C CD     . PRO A 1 98  ? 4.648  13.318  14.226 1.00 37.44  ?  98  PRO A CD     1 
ATOM   675  N N      . GLU A 1 99  ? 4.105  10.451  15.876 1.00 34.90  ?  99  GLU A N      1 
ATOM   676  C CA     . GLU A 1 99  ? 3.402  9.352   16.516 1.00 35.99  ?  99  GLU A CA     1 
ATOM   677  C C      . GLU A 1 99  ? 3.740  8.014   15.887 1.00 35.46  ?  99  GLU A C      1 
ATOM   678  O O      . GLU A 1 99  ? 3.282  6.977   16.383 1.00 42.24  ?  99  GLU A O      1 
ATOM   679  C CB     . GLU A 1 99  ? 1.899  9.593   16.458 1.00 41.06  ?  99  GLU A CB     1 
ATOM   680  C CG     . GLU A 1 99  ? 1.302  9.445   15.088 1.00 45.73  ?  99  GLU A CG     1 
ATOM   681  C CD     . GLU A 1 99  ? -0.097 10.015  15.036 1.00 53.59  ?  99  GLU A CD     1 
ATOM   682  O OE1    . GLU A 1 99  ? -0.379 10.905  15.861 1.00 54.91  ?  99  GLU A OE1    1 
ATOM   683  O OE2    . GLU A 1 99  ? -0.918 9.574   14.198 1.00 57.65  -1 99  GLU A OE2    1 
ATOM   684  N N      . GLU A 1 100 ? 4.463  8.018   14.774 1.00 31.64  ?  100 GLU A N      1 
ATOM   685  C CA     . GLU A 1 100 ? 4.920  6.807   14.107 1.00 41.96  ?  100 GLU A CA     1 
ATOM   686  C C      . GLU A 1 100 ? 6.249  6.282   14.648 1.00 39.81  ?  100 GLU A C      1 
ATOM   687  O O      . GLU A 1 100 ? 6.432  5.067   14.756 1.00 46.62  ?  100 GLU A O      1 
ATOM   688  C CB     . GLU A 1 100 ? 5.024  7.046   12.582 1.00 52.07  ?  100 GLU A CB     1 
ATOM   689  C CG     . GLU A 1 100 ? 3.755  7.664   11.884 1.00 54.31  ?  100 GLU A CG     1 
ATOM   690  C CD     . GLU A 1 100 ? 2.743  6.632   11.337 1.00 53.77  ?  100 GLU A CD     1 
ATOM   691  O OE1    . GLU A 1 100 ? 3.122  5.460   11.120 1.00 55.55  ?  100 GLU A OE1    1 
ATOM   692  O OE2    . GLU A 1 100 ? 1.562  7.003   11.108 1.00 51.54  -1 100 GLU A OE2    1 
ATOM   693  N N      . HIS A 1 101 ? 7.206  7.159   14.941 1.00 30.53  ?  101 HIS A N      1 
ATOM   694  C CA     . HIS A 1 101 ? 8.616  6.778   15.058 1.00 24.12  ?  101 HIS A CA     1 
ATOM   695  C C      . HIS A 1 101 ? 9.158  7.005   16.470 1.00 32.07  ?  101 HIS A C      1 
ATOM   696  O O      . HIS A 1 101 ? 9.084  8.140   16.977 1.00 33.52  ?  101 HIS A O      1 
ATOM   697  C CB     . HIS A 1 101 ? 9.416  7.577   14.013 1.00 28.77  ?  101 HIS A CB     1 
ATOM   698  C CG     . HIS A 1 101 ? 8.996  7.295   12.594 1.00 31.88  ?  101 HIS A CG     1 
ATOM   699  N ND1    . HIS A 1 101 ? 7.929  7.927   11.987 1.00 29.87  ?  101 HIS A ND1    1 
ATOM   700  C CD2    . HIS A 1 101 ? 9.478  6.418   11.681 1.00 31.85  ?  101 HIS A CD2    1 
ATOM   701  C CE1    . HIS A 1 101 ? 7.785  7.461   10.761 1.00 35.49  ?  101 HIS A CE1    1 
ATOM   702  N NE2    . HIS A 1 101 ? 8.716  6.548   10.548 1.00 36.94  ?  101 HIS A NE2    1 
ATOM   703  N N      . PRO A 1 102 ? 9.682  5.985   17.166 1.00 27.66  ?  102 PRO A N      1 
ATOM   704  C CA     . PRO A 1 102 ? 10.399 6.254   18.416 1.00 24.29  ?  102 PRO A CA     1 
ATOM   705  C C      . PRO A 1 102 ? 11.462 7.321   18.206 1.00 24.04  ?  102 PRO A C      1 
ATOM   706  O O      . PRO A 1 102 ? 12.105 7.382   17.162 1.00 26.79  ?  102 PRO A O      1 
ATOM   707  C CB     . PRO A 1 102 ? 11.022 4.895   18.776 1.00 24.81  ?  102 PRO A CB     1 
ATOM   708  C CG     . PRO A 1 102 ? 10.955 4.077   17.524 1.00 22.04  ?  102 PRO A CG     1 
ATOM   709  C CD     . PRO A 1 102 ? 9.695  4.545   16.857 1.00 25.69  ?  102 PRO A CD     1 
ATOM   710  N N      . VAL A 1 103 ? 11.640 8.183   19.200 1.00 38.27  ?  103 VAL A N      1 
ATOM   711  C CA     . VAL A 1 103 ? 12.488 9.355   19.039 1.00 40.15  ?  103 VAL A CA     1 
ATOM   712  C C      . VAL A 1 103 ? 13.581 9.355   20.102 1.00 33.99  ?  103 VAL A C      1 
ATOM   713  O O      . VAL A 1 103 ? 13.322 9.667   21.271 1.00 33.11  ?  103 VAL A O      1 
ATOM   714  C CB     . VAL A 1 103 ? 11.670 10.649  19.097 1.00 39.52  ?  103 VAL A CB     1 
ATOM   715  C CG1    . VAL A 1 103 ? 12.599 11.823  19.188 1.00 44.45  ?  103 VAL A CG1    1 
ATOM   716  C CG2    . VAL A 1 103 ? 10.752 10.754  17.860 1.00 31.14  ?  103 VAL A CG2    1 
ATOM   717  N N      . LEU A 1 104 ? 14.808 9.071   19.676 1.00 24.92  ?  104 LEU A N      1 
ATOM   718  C CA     . LEU A 1 104 ? 16.006 9.403   20.423 1.00 21.14  ?  104 LEU A CA     1 
ATOM   719  C C      . LEU A 1 104 ? 16.322 10.876  20.217 1.00 25.04  ?  104 LEU A C      1 
ATOM   720  O O      . LEU A 1 104 ? 16.417 11.332  19.077 1.00 27.84  ?  104 LEU A O      1 
ATOM   721  C CB     . LEU A 1 104 ? 17.183 8.548   19.960 1.00 21.59  ?  104 LEU A CB     1 
ATOM   722  C CG     . LEU A 1 104 ? 18.590 8.995   20.390 1.00 22.20  ?  104 LEU A CG     1 
ATOM   723  C CD1    . LEU A 1 104 ? 18.571 9.519   21.793 1.00 27.75  ?  104 LEU A CD1    1 
ATOM   724  C CD2    . LEU A 1 104 ? 19.562 7.854   20.309 1.00 19.69  ?  104 LEU A CD2    1 
ATOM   725  N N      . LEU A 1 105 ? 16.487 11.617  21.322 1.00 29.97  ?  105 LEU A N      1 
ATOM   726  C CA     . LEU A 1 105 ? 16.817 13.038  21.319 1.00 26.39  ?  105 LEU A CA     1 
ATOM   727  C C      . LEU A 1 105 ? 18.124 13.277  22.070 1.00 24.49  ?  105 LEU A C      1 
ATOM   728  O O      . LEU A 1 105 ? 18.500 12.507  22.946 1.00 28.25  ?  105 LEU A O      1 
ATOM   729  C CB     . LEU A 1 105 ? 15.699 13.856  21.963 1.00 34.39  ?  105 LEU A CB     1 
ATOM   730  C CG     . LEU A 1 105 ? 14.456 14.197  21.141 1.00 40.48  ?  105 LEU A CG     1 
ATOM   731  C CD1    . LEU A 1 105 ? 13.250 14.122  22.047 1.00 42.44  ?  105 LEU A CD1    1 
ATOM   732  C CD2    . LEU A 1 105 ? 14.560 15.590  20.541 1.00 42.29  ?  105 LEU A CD2    1 
ATOM   733  N N      . THR A 1 106 ? 18.834 14.344  21.721 1.00 19.40  ?  106 THR A N      1 
ATOM   734  C CA     . THR A 1 106 ? 20.104 14.656  22.370 1.00 25.03  ?  106 THR A CA     1 
ATOM   735  C C      . THR A 1 106 ? 19.995 15.917  23.224 1.00 28.74  ?  106 THR A C      1 
ATOM   736  O O      . THR A 1 106 ? 19.276 16.860  22.881 1.00 28.86  ?  106 THR A O      1 
ATOM   737  C CB     . THR A 1 106 ? 21.237 14.885  21.368 1.00 26.48  ?  106 THR A CB     1 
ATOM   738  O OG1    . THR A 1 106 ? 21.181 16.250  20.951 1.00 28.94  ?  106 THR A OG1    1 
ATOM   739  C CG2    . THR A 1 106 ? 21.133 13.971  20.149 1.00 25.36  ?  106 THR A CG2    1 
ATOM   740  N N      . GLU A 1 107 ? 20.780 15.941  24.314 1.00 35.80  ?  107 GLU A N      1 
ATOM   741  C CA     . GLU A 1 107 ? 20.817 17.027  25.289 1.00 25.31  ?  107 GLU A CA     1 
ATOM   742  C C      . GLU A 1 107 ? 22.256 17.496  25.537 1.00 20.89  ?  107 GLU A C      1 
ATOM   743  O O      . GLU A 1 107 ? 23.223 16.742  25.380 1.00 25.21  ?  107 GLU A O      1 
ATOM   744  C CB     . GLU A 1 107 ? 20.183 16.574  26.601 1.00 28.50  ?  107 GLU A CB     1 
ATOM   745  C CG     . GLU A 1 107 ? 20.997 15.455  27.273 1.00 33.81  ?  107 GLU A CG     1 
ATOM   746  C CD     . GLU A 1 107 ? 20.329 14.866  28.505 1.00 38.72  ?  107 GLU A CD     1 
ATOM   747  O OE1    . GLU A 1 107 ? 19.460 15.551  29.103 1.00 30.35  ?  107 GLU A OE1    1 
ATOM   748  O OE2    . GLU A 1 107 ? 20.676 13.710  28.860 1.00 43.53  -1 107 GLU A OE2    1 
ATOM   749  N N      . ALA A 1 108 ? 22.385 18.709  25.998 1.00 25.85  ?  108 ALA A N      1 
ATOM   750  C CA     . ALA A 1 108 ? 23.686 19.206  26.327 1.00 22.03  ?  108 ALA A CA     1 
ATOM   751  C C      . ALA A 1 108 ? 24.260 18.598  27.566 1.00 31.23  ?  108 ALA A C      1 
ATOM   752  O O      . ALA A 1 108 ? 23.575 18.020  28.406 1.00 18.64  ?  108 ALA A O      1 
ATOM   753  C CB     . ALA A 1 108 ? 23.619 20.688  26.494 1.00 18.85  ?  108 ALA A CB     1 
ATOM   754  N N      . PRO A 1 109 ? 25.574 18.686  27.654 1.00 50.40  ?  109 PRO A N      1 
ATOM   755  C CA     . PRO A 1 109 ? 26.190 18.260  28.880 1.00 43.80  ?  109 PRO A CA     1 
ATOM   756  C C      . PRO A 1 109 ? 25.749 19.223  29.938 1.00 48.81  ?  109 PRO A C      1 
ATOM   757  O O      . PRO A 1 109 ? 25.475 20.381  29.635 1.00 56.61  ?  109 PRO A O      1 
ATOM   758  C CB     . PRO A 1 109 ? 27.639 18.482  28.578 1.00 45.33  ?  109 PRO A CB     1 
ATOM   759  C CG     . PRO A 1 109 ? 27.766 18.193  27.134 1.00 44.49  ?  109 PRO A CG     1 
ATOM   760  C CD     . PRO A 1 109 ? 26.530 18.740  26.534 1.00 44.48  ?  109 PRO A CD     1 
ATOM   761  N N      . LEU A 1 110 ? 25.663 18.759  31.167 1.00 47.68  ?  110 LEU A N      1 
ATOM   762  C CA     . LEU A 1 110 ? 25.225 19.600  32.271 1.00 46.22  ?  110 LEU A CA     1 
ATOM   763  C C      . LEU A 1 110 ? 23.832 20.202  32.100 1.00 40.97  ?  110 LEU A C      1 
ATOM   764  O O      . LEU A 1 110 ? 23.642 21.380  32.353 1.00 41.90  ?  110 LEU A O      1 
ATOM   765  C CB     . LEU A 1 110 ? 26.293 20.655  32.608 1.00 51.18  ?  110 LEU A CB     1 
ATOM   766  C CG     . LEU A 1 110 ? 27.639 20.172  33.145 1.00 58.47  ?  110 LEU A CG     1 
ATOM   767  C CD1    . LEU A 1 110 ? 28.653 21.291  33.302 1.00 56.62  ?  110 LEU A CD1    1 
ATOM   768  C CD2    . LEU A 1 110 ? 27.465 19.401  34.443 1.00 60.11  ?  110 LEU A CD2    1 
ATOM   769  N N      . ASN A 1 111 ? 22.860 19.395  31.708 1.00 37.03  ?  111 ASN A N      1 
ATOM   770  C CA     . ASN A 1 111 ? 21.496 19.864  31.539 1.00 37.69  ?  111 ASN A CA     1 
ATOM   771  C C      . ASN A 1 111 ? 20.778 19.669  32.853 1.00 46.05  ?  111 ASN A C      1 
ATOM   772  O O      . ASN A 1 111 ? 20.909 18.622  33.471 1.00 48.35  ?  111 ASN A O      1 
ATOM   773  C CB     . ASN A 1 111 ? 20.804 19.067  30.449 1.00 35.81  ?  111 ASN A CB     1 
ATOM   774  C CG     . ASN A 1 111 ? 19.599 19.749  29.880 1.00 34.17  ?  111 ASN A CG     1 
ATOM   775  O OD1    . ASN A 1 111 ? 19.547 20.958  29.791 1.00 36.57  ?  111 ASN A OD1    1 
ATOM   776  N ND2    . ASN A 1 111 ? 18.626 18.962  29.466 1.00 37.59  ?  111 ASN A ND2    1 
ATOM   777  N N      . PRO A 1 112 ? 20.027 20.686  33.306 1.00 49.58  ?  112 PRO A N      1 
ATOM   778  C CA     . PRO A 1 112 ? 19.254 20.576  34.549 1.00 44.12  ?  112 PRO A CA     1 
ATOM   779  C C      . PRO A 1 112 ? 18.190 19.503  34.514 1.00 38.67  ?  112 PRO A C      1 
ATOM   780  O O      . PRO A 1 112 ? 17.572 19.332  33.479 1.00 45.79  ?  112 PRO A O      1 
ATOM   781  C CB     . PRO A 1 112 ? 18.628 21.943  34.672 1.00 41.00  ?  112 PRO A CB     1 
ATOM   782  C CG     . PRO A 1 112 ? 19.549 22.857  33.959 1.00 42.85  ?  112 PRO A CG     1 
ATOM   783  C CD     . PRO A 1 112 ? 20.064 22.067  32.806 1.00 48.57  ?  112 PRO A CD     1 
ATOM   784  N N      . LYS A 1 113 ? 17.985 18.797  35.613 1.00 30.83  ?  113 LYS A N      1 
ATOM   785  C CA     . LYS A 1 113 ? 17.047 17.680  35.625 1.00 33.05  ?  113 LYS A CA     1 
ATOM   786  C C      . LYS A 1 113 ? 15.632 18.112  35.247 1.00 33.68  ?  113 LYS A C      1 
ATOM   787  O O      . LYS A 1 113 ? 14.879 17.311  34.680 1.00 34.93  ?  113 LYS A O      1 
ATOM   788  C CB     . LYS A 1 113 ? 17.051 16.988  36.999 1.00 38.39  ?  113 LYS A CB     1 
ATOM   789  C CG     . LYS A 1 113 ? 16.108 17.592  38.062 1.00 39.93  ?  113 LYS A CG     1 
ATOM   790  C CD     . LYS A 1 113 ? 15.700 16.551  39.144 1.00 43.14  ?  113 LYS A CD     1 
ATOM   791  C CE     . LYS A 1 113 ? 14.446 16.982  39.970 1.00 43.54  ?  113 LYS A CE     1 
ATOM   792  N NZ     . LYS A 1 113 ? 13.670 15.859  40.646 1.00 38.52  ?  113 LYS A NZ     1 
ATOM   793  N N      . ALA A 1 114 ? 15.243 19.361  35.535 1.00 29.88  ?  114 ALA A N      1 
ATOM   794  C CA     . ALA A 1 114 ? 13.889 19.800  35.183 1.00 27.29  ?  114 ALA A CA     1 
ATOM   795  C C      . ALA A 1 114 ? 13.713 19.913  33.679 1.00 40.33  ?  114 ALA A C      1 
ATOM   796  O O      . ALA A 1 114 ? 12.606 19.714  33.164 1.00 45.58  ?  114 ALA A O      1 
ATOM   797  C CB     . ALA A 1 114 ? 13.554 21.141  35.839 1.00 23.33  ?  114 ALA A CB     1 
ATOM   798  N N      . ASN A 1 115 ? 14.785 20.236  32.959 1.00 48.96  ?  115 ASN A N      1 
ATOM   799  C CA     . ASN A 1 115 ? 14.688 20.311  31.508 1.00 40.17  ?  115 ASN A CA     1 
ATOM   800  C C      . ASN A 1 115 ? 14.488 18.936  30.900 1.00 29.77  ?  115 ASN A C      1 
ATOM   801  O O      . ASN A 1 115 ? 13.628 18.753  30.043 1.00 33.30  ?  115 ASN A O      1 
ATOM   802  C CB     . ASN A 1 115 ? 15.920 21.017  30.951 1.00 41.24  ?  115 ASN A CB     1 
ATOM   803  C CG     . ASN A 1 115 ? 15.964 22.478  31.381 1.00 55.32  ?  115 ASN A CG     1 
ATOM   804  O OD1    . ASN A 1 115 ? 15.700 22.810  32.547 1.00 62.11  ?  115 ASN A OD1    1 
ATOM   805  N ND2    . ASN A 1 115 ? 16.234 23.361  30.436 1.00 57.96  ?  115 ASN A ND2    1 
ATOM   806  N N      . ARG A 1 116 ? 15.235 17.944  31.350 1.00 24.95  ?  116 ARG A N      1 
ATOM   807  C CA     . ARG A 1 116 ? 15.044 16.643  30.753 1.00 21.96  ?  116 ARG A CA     1 
ATOM   808  C C      . ARG A 1 116 ? 13.624 16.136  30.921 1.00 24.12  ?  116 ARG A C      1 
ATOM   809  O O      . ARG A 1 116 ? 13.226 15.206  30.215 1.00 36.91  ?  116 ARG A O      1 
ATOM   810  C CB     . ARG A 1 116 ? 16.006 15.635  31.342 1.00 27.64  ?  116 ARG A CB     1 
ATOM   811  C CG     . ARG A 1 116 ? 17.254 16.199  31.960 1.00 32.37  ?  116 ARG A CG     1 
ATOM   812  C CD     . ARG A 1 116 ? 18.087 14.986  32.407 1.00 30.39  ?  116 ARG A CD     1 
ATOM   813  N NE     . ARG A 1 116 ? 18.432 14.170  31.247 1.00 30.95  ?  116 ARG A NE     1 
ATOM   814  C CZ     . ARG A 1 116 ? 18.533 12.849  31.255 1.00 31.70  ?  116 ARG A CZ     1 
ATOM   815  N NH1    . ARG A 1 116 ? 18.290 12.180  32.373 1.00 32.72  ?  116 ARG A NH1    1 
ATOM   816  N NH2    . ARG A 1 116 ? 18.866 12.198  30.140 1.00 30.97  ?  116 ARG A NH2    1 
ATOM   817  N N      . GLU A 1 117 ? 12.853 16.681  31.850 1.00 23.06  ?  117 GLU A N      1 
ATOM   818  C CA     . GLU A 1 117 ? 11.486 16.178  31.982 1.00 27.80  ?  117 GLU A CA     1 
ATOM   819  C C      . GLU A 1 117 ? 10.534 16.840  30.990 1.00 23.71  ?  117 GLU A C      1 
ATOM   820  O O      . GLU A 1 117 ? 9.597  16.193  30.497 1.00 23.88  ?  117 GLU A O      1 
ATOM   821  C CB     . GLU A 1 117 ? 10.984 16.358  33.414 1.00 34.36  ?  117 GLU A CB     1 
ATOM   822  C CG     . GLU A 1 117 ? 11.718 15.528  34.450 1.00 41.36  ?  117 GLU A CG     1 
ATOM   823  C CD     . GLU A 1 117 ? 11.475 16.025  35.878 1.00 45.73  ?  117 GLU A CD     1 
ATOM   824  O OE1    . GLU A 1 117 ? 10.552 16.858  36.052 1.00 48.25  ?  117 GLU A OE1    1 
ATOM   825  O OE2    . GLU A 1 117 ? 12.205 15.594  36.813 1.00 39.47  -1 117 GLU A OE2    1 
ATOM   826  N N      . LYS A 1 118 ? 10.741 18.126  30.705 1.00 30.73  ?  118 LYS A N      1 
ATOM   827  C CA     . LYS A 1 118 ? 9.929  18.799  29.688 1.00 41.04  ?  118 LYS A CA     1 
ATOM   828  C C      . LYS A 1 118 ? 10.173 18.221  28.286 1.00 47.47  ?  118 LYS A C      1 
ATOM   829  O O      . LYS A 1 118 ? 9.231  18.100  27.490 1.00 52.42  ?  118 LYS A O      1 
ATOM   830  C CB     . LYS A 1 118 ? 10.195 20.309  29.716 1.00 39.09  ?  118 LYS A CB     1 
ATOM   831  C CG     . LYS A 1 118 ? 9.128  21.162  28.994 1.00 48.50  ?  118 LYS A CG     1 
ATOM   832  C CD     . LYS A 1 118 ? 7.687  20.815  29.440 1.00 54.93  ?  118 LYS A CD     1 
ATOM   833  C CE     . LYS A 1 118 ? 6.621  21.685  28.751 1.00 55.85  ?  118 LYS A CE     1 
ATOM   834  N NZ     . LYS A 1 118 ? 5.226  21.166  28.950 1.00 54.32  ?  118 LYS A NZ     1 
ATOM   835  N N      . MET A 1 119 ? 11.418 17.860  27.954 1.00 39.26  ?  119 MET A N      1 
ATOM   836  C CA     . MET A 1 119 ? 11.659 17.158  26.698 1.00 32.98  ?  119 MET A CA     1 
ATOM   837  C C      . MET A 1 119 ? 10.850 15.863  26.641 1.00 32.50  ?  119 MET A C      1 
ATOM   838  O O      . MET A 1 119 ? 10.092 15.620  25.696 1.00 36.38  ?  119 MET A O      1 
ATOM   839  C CB     . MET A 1 119 ? 13.145 16.850  26.520 1.00 28.67  ?  119 MET A CB     1 
ATOM   840  C CG     . MET A 1 119 ? 14.138 17.965  26.753 1.00 36.64  ?  119 MET A CG     1 
ATOM   841  S SD     . MET A 1 119 ? 15.845 17.282  26.722 1.00 41.91  ?  119 MET A SD     1 
ATOM   842  C CE     . MET A 1 119 ? 15.917 16.547  25.098 1.00 34.63  ?  119 MET A CE     1 
ATOM   843  N N      . THR A 1 120 ? 11.029 15.001  27.636 1.00 33.95  ?  120 THR A N      1 
ATOM   844  C CA     . THR A 1 120 ? 10.233 13.783  27.733 1.00 34.34  ?  120 THR A CA     1 
ATOM   845  C C      . THR A 1 120 ? 8.737  14.079  27.683 1.00 34.51  ?  120 THR A C      1 
ATOM   846  O O      . THR A 1 120 ? 7.994  13.470  26.913 1.00 36.89  ?  120 THR A O      1 
ATOM   847  C CB     . THR A 1 120 ? 10.591 13.054  29.031 1.00 36.70  ?  120 THR A CB     1 
ATOM   848  O OG1    . THR A 1 120 ? 11.891 12.472  28.905 1.00 40.13  ?  120 THR A OG1    1 
ATOM   849  C CG2    . THR A 1 120 ? 9.571  11.966  29.365 1.00 38.55  ?  120 THR A CG2    1 
ATOM   850  N N      . GLN A 1 121 ? 8.272  14.997  28.528 1.00 35.34  ?  121 GLN A N      1 
ATOM   851  C CA     . GLN A 1 121 ? 6.840  15.279  28.609 1.00 35.10  ?  121 GLN A CA     1 
ATOM   852  C C      . GLN A 1 121 ? 6.291  15.787  27.276 1.00 35.35  ?  121 GLN A C      1 
ATOM   853  O O      . GLN A 1 121 ? 5.212  15.363  26.834 1.00 32.37  ?  121 GLN A O      1 
ATOM   854  C CB     . GLN A 1 121 ? 6.586  16.293  29.718 1.00 30.87  ?  121 GLN A CB     1 
ATOM   855  C CG     . GLN A 1 121 ? 5.275  17.045  29.592 1.00 31.88  ?  121 GLN A CG     1 
ATOM   856  C CD     . GLN A 1 121 ? 5.108  18.073  30.702 1.00 34.93  ?  121 GLN A CD     1 
ATOM   857  O OE1    . GLN A 1 121 ? 6.041  18.341  31.452 1.00 35.12  ?  121 GLN A OE1    1 
ATOM   858  N NE2    . GLN A 1 121 ? 3.916  18.631  30.818 1.00 34.59  ?  121 GLN A NE2    1 
ATOM   859  N N      . ILE A 1 122 ? 7.022  16.705  26.627 1.00 24.80  ?  122 ILE A N      1 
ATOM   860  C CA     . ILE A 1 122 ? 6.559  17.320  25.382 1.00 31.54  ?  122 ILE A CA     1 
ATOM   861  C C      . ILE A 1 122 ? 6.568  16.319  24.225 1.00 34.17  ?  122 ILE A C      1 
ATOM   862  O O      . ILE A 1 122 ? 5.682  16.339  23.362 1.00 29.75  ?  122 ILE A O      1 
ATOM   863  C CB     . ILE A 1 122 ? 7.414  18.555  25.064 1.00 31.56  ?  122 ILE A CB     1 
ATOM   864  C CG1    . ILE A 1 122 ? 7.095  19.682  26.052 1.00 21.90  ?  122 ILE A CG1    1 
ATOM   865  C CG2    . ILE A 1 122 ? 7.212  18.981  23.603 1.00 30.76  ?  122 ILE A CG2    1 
ATOM   866  C CD1    . ILE A 1 122 ? 7.980  20.860  25.898 1.00 21.78  ?  122 ILE A CD1    1 
ATOM   867  N N      . MET A 1 123 ? 7.565  15.436  24.188 1.00 41.93  ?  123 MET A N      1 
ATOM   868  C CA     . MET A 1 123 ? 7.645  14.427  23.137 1.00 42.71  ?  123 MET A CA     1 
ATOM   869  C C      . MET A 1 123 ? 6.455  13.472  23.186 1.00 45.57  ?  123 MET A C      1 
ATOM   870  O O      . MET A 1 123 ? 5.900  13.103  22.135 1.00 43.21  ?  123 MET A O      1 
ATOM   871  C CB     . MET A 1 123 ? 8.956  13.651  23.284 1.00 37.53  ?  123 MET A CB     1 
ATOM   872  C CG     . MET A 1 123 ? 9.745  13.456  22.016 1.00 38.71  ?  123 MET A CG     1 
ATOM   873  S SD     . MET A 1 123 ? 9.869  14.922  20.969 1.00 39.95  ?  123 MET A SD     1 
ATOM   874  C CE     . MET A 1 123 ? 10.982 15.988  21.884 1.00 40.62  ?  123 MET A CE     1 
ATOM   875  N N      . PHE A 1 124 ? 6.079  13.030  24.405 1.00 28.75  ?  124 PHE A N      1 
ATOM   876  C CA     . PHE A 1 124 ? 4.944  12.121  24.604 1.00 33.72  ?  124 PHE A CA     1 
ATOM   877  C C      . PHE A 1 124 ? 3.592  12.857  24.572 1.00 35.95  ?  124 PHE A C      1 
ATOM   878  O O      . PHE A 1 124 ? 2.650  12.403  23.909 1.00 37.65  ?  124 PHE A O      1 
ATOM   879  C CB     . PHE A 1 124 ? 5.095  11.335  25.929 1.00 25.28  ?  124 PHE A CB     1 
ATOM   880  C CG     . PHE A 1 124 ? 6.041  10.158  25.861 1.00 22.03  ?  124 PHE A CG     1 
ATOM   881  C CD1    . PHE A 1 124 ? 5.741  9.039   25.092 1.00 23.68  ?  124 PHE A CD1    1 
ATOM   882  C CD2    . PHE A 1 124 ? 7.218  10.150  26.607 1.00 21.67  ?  124 PHE A CD2    1 
ATOM   883  C CE1    . PHE A 1 124 ? 6.608  7.946   25.037 1.00 22.06  ?  124 PHE A CE1    1 
ATOM   884  C CE2    . PHE A 1 124 ? 8.087  9.072   26.550 1.00 21.50  ?  124 PHE A CE2    1 
ATOM   885  C CZ     . PHE A 1 124 ? 7.781  7.976   25.755 1.00 21.70  ?  124 PHE A CZ     1 
ATOM   886  N N      . GLU A 1 125 ? 3.460  13.979  25.293 1.00 45.60  ?  125 GLU A N      1 
ATOM   887  C CA     . GLU A 1 125 ? 2.170  14.672  25.328 1.00 44.06  ?  125 GLU A CA     1 
ATOM   888  C C      . GLU A 1 125 ? 1.911  15.511  24.077 1.00 39.21  ?  125 GLU A C      1 
ATOM   889  O O      . GLU A 1 125 ? 0.814  15.459  23.518 1.00 48.32  ?  125 GLU A O      1 
ATOM   890  C CB     . GLU A 1 125 ? 2.049  15.545  26.574 1.00 42.34  ?  125 GLU A CB     1 
ATOM   891  C CG     . GLU A 1 125 ? 2.285  14.784  27.848 1.00 47.18  ?  125 GLU A CG     1 
ATOM   892  C CD     . GLU A 1 125 ? 1.724  15.466  29.090 1.00 50.67  ?  125 GLU A CD     1 
ATOM   893  O OE1    . GLU A 1 125 ? 1.455  16.694  29.042 1.00 49.48  ?  125 GLU A OE1    1 
ATOM   894  O OE2    . GLU A 1 125 ? 1.558  14.751  30.111 1.00 50.28  -1 125 GLU A OE2    1 
ATOM   895  N N      . THR A 1 126 ? 2.876  16.311  23.626 1.00 24.77  ?  126 THR A N      1 
ATOM   896  C CA     . THR A 1 126 ? 2.576  17.143  22.454 1.00 30.87  ?  126 THR A CA     1 
ATOM   897  C C      . THR A 1 126 ? 2.651  16.368  21.138 1.00 31.87  ?  126 THR A C      1 
ATOM   898  O O      . THR A 1 126 ? 1.789  16.535  20.274 1.00 33.52  ?  126 THR A O      1 
ATOM   899  C CB     . THR A 1 126 ? 3.497  18.358  22.371 1.00 28.68  ?  126 THR A CB     1 
ATOM   900  O OG1    . THR A 1 126 ? 3.328  19.165  23.541 1.00 27.59  ?  126 THR A OG1    1 
ATOM   901  C CG2    . THR A 1 126 ? 3.136  19.174  21.127 1.00 23.59  ?  126 THR A CG2    1 
ATOM   902  N N      . PHE A 1 127 ? 3.698  15.571  20.927 1.00 31.54  ?  127 PHE A N      1 
ATOM   903  C CA     . PHE A 1 127 ? 3.830  14.854  19.669 1.00 35.50  ?  127 PHE A CA     1 
ATOM   904  C C      . PHE A 1 127 ? 3.400  13.395  19.738 1.00 35.76  ?  127 PHE A C      1 
ATOM   905  O O      . PHE A 1 127 ? 3.395  12.724  18.702 1.00 35.24  ?  127 PHE A O      1 
ATOM   906  C CB     . PHE A 1 127 ? 5.267  14.956  19.170 1.00 37.53  ?  127 PHE A CB     1 
ATOM   907  C CG     . PHE A 1 127 ? 5.756  16.360  19.076 1.00 28.19  ?  127 PHE A CG     1 
ATOM   908  C CD1    . PHE A 1 127 ? 5.384  17.154  18.004 1.00 24.31  ?  127 PHE A CD1    1 
ATOM   909  C CD2    . PHE A 1 127 ? 6.576  16.894  20.074 1.00 28.53  ?  127 PHE A CD2    1 
ATOM   910  C CE1    . PHE A 1 127 ? 5.836  18.484  17.908 1.00 28.25  ?  127 PHE A CE1    1 
ATOM   911  C CE2    . PHE A 1 127 ? 7.026  18.197  19.994 1.00 35.46  ?  127 PHE A CE2    1 
ATOM   912  C CZ     . PHE A 1 127 ? 6.656  19.002  18.900 1.00 34.53  ?  127 PHE A CZ     1 
ATOM   913  N N      . ASN A 1 128 ? 3.026  12.895  20.912 1.00 38.58  ?  128 ASN A N      1 
ATOM   914  C CA     . ASN A 1 128 ? 2.567  11.522  21.074 1.00 37.83  ?  128 ASN A CA     1 
ATOM   915  C C      . ASN A 1 128 ? 3.523  10.547  20.403 1.00 38.77  ?  128 ASN A C      1 
ATOM   916  O O      . ASN A 1 128 ? 3.161  9.863   19.445 1.00 38.37  ?  128 ASN A O      1 
ATOM   917  C CB     . ASN A 1 128 ? 1.155  11.324  20.506 1.00 46.97  ?  128 ASN A CB     1 
ATOM   918  C CG     . ASN A 1 128 ? 0.120  12.217  21.157 1.00 55.57  ?  128 ASN A CG     1 
ATOM   919  O OD1    . ASN A 1 128 ? -0.177 12.065  22.341 1.00 58.40  ?  128 ASN A OD1    1 
ATOM   920  N ND2    . ASN A 1 128 ? -0.442 13.157  20.384 1.00 57.25  ?  128 ASN A ND2    1 
ATOM   921  N N      . THR A 1 129 ? 4.765  10.481  20.915 1.00 28.95  ?  129 THR A N      1 
ATOM   922  C CA     . THR A 1 129 ? 5.624  9.464   20.308 1.00 26.10  ?  129 THR A CA     1 
ATOM   923  C C      . THR A 1 129 ? 5.438  8.107   20.994 1.00 26.35  ?  129 THR A C      1 
ATOM   924  O O      . THR A 1 129 ? 4.979  8.019   22.139 1.00 25.02  ?  129 THR A O      1 
ATOM   925  C CB     . THR A 1 129 ? 7.101  9.894   20.358 1.00 29.54  ?  129 THR A CB     1 
ATOM   926  O OG1    . THR A 1 129 ? 7.652  9.709   21.681 1.00 31.00  ?  129 THR A OG1    1 
ATOM   927  C CG2    . THR A 1 129 ? 7.248  11.345  19.949 1.00 26.84  ?  129 THR A CG2    1 
ATOM   928  N N      . PRO A 1 130 ? 5.721  7.019   20.277 1.00 30.14  ?  130 PRO A N      1 
ATOM   929  C CA     . PRO A 1 130 ? 5.597  5.676   20.888 1.00 24.61  ?  130 PRO A CA     1 
ATOM   930  C C      . PRO A 1 130 ? 6.652  5.361   21.934 1.00 28.67  ?  130 PRO A C      1 
ATOM   931  O O      . PRO A 1 130 ? 6.425  4.505   22.797 1.00 30.09  ?  130 PRO A O      1 
ATOM   932  C CB     . PRO A 1 130 ? 5.727  4.730   19.682 1.00 23.08  ?  130 PRO A CB     1 
ATOM   933  C CG     . PRO A 1 130 ? 6.316  5.604   18.504 1.00 22.93  ?  130 PRO A CG     1 
ATOM   934  C CD     . PRO A 1 130 ? 5.804  6.987   18.798 1.00 28.09  ?  130 PRO A CD     1 
ATOM   935  N N      . ALA A 1 131 ? 7.821  5.978   21.836 1.00 32.41  ?  131 ALA A N      1 
ATOM   936  C CA     . ALA A 1 131 ? 8.976  5.658   22.663 1.00 22.60  ?  131 ALA A CA     1 
ATOM   937  C C      . ALA A 1 131 ? 9.965  6.785   22.452 1.00 21.49  ?  131 ALA A C      1 
ATOM   938  O O      . ALA A 1 131 ? 9.748  7.663   21.621 1.00 23.73  ?  131 ALA A O      1 
ATOM   939  C CB     . ALA A 1 131 ? 9.570  4.296   22.297 1.00 21.88  ?  131 ALA A CB     1 
ATOM   940  N N      . MET A 1 132 ? 10.948 6.861   23.316 1.00 40.90  ?  132 MET A N      1 
ATOM   941  C CA     . MET A 1 132 ? 11.851 7.983   23.323 1.00 37.28  ?  132 MET A CA     1 
ATOM   942  C C      . MET A 1 132 ? 13.060 7.752   24.229 1.00 40.44  ?  132 MET A C      1 
ATOM   943  O O      . MET A 1 132 ? 12.996 6.948   25.125 1.00 38.00  ?  132 MET A O      1 
ATOM   944  C CB     . MET A 1 132 ? 11.045 9.178   23.793 1.00 37.76  ?  132 MET A CB     1 
ATOM   945  C CG     . MET A 1 132 ? 11.766 10.469  23.957 1.00 51.19  ?  132 MET A CG     1 
ATOM   946  S SD     . MET A 1 132 ? 11.887 10.794  25.703 1.00 53.92  ?  132 MET A SD     1 
ATOM   947  C CE     . MET A 1 132 ? 12.584 12.428  25.532 1.00 54.96  ?  132 MET A CE     1 
ATOM   948  N N      . TYR A 1 133 ? 14.172 8.434   23.962 1.00 33.51  ?  133 TYR A N      1 
ATOM   949  C CA     . TYR A 1 133 ? 15.365 8.327   24.793 1.00 31.40  ?  133 TYR A CA     1 
ATOM   950  C C      . TYR A 1 133 ? 16.097 9.653   24.729 1.00 36.20  ?  133 TYR A C      1 
ATOM   951  O O      . TYR A 1 133 ? 16.108 10.303  23.677 1.00 31.57  ?  133 TYR A O      1 
ATOM   952  C CB     . TYR A 1 133 ? 16.291 7.209   24.305 1.00 36.29  ?  133 TYR A CB     1 
ATOM   953  C CG     . TYR A 1 133 ? 17.286 6.680   25.318 1.00 40.06  ?  133 TYR A CG     1 
ATOM   954  C CD1    . TYR A 1 133 ? 16.915 5.689   26.231 1.00 40.19  ?  133 TYR A CD1    1 
ATOM   955  C CD2    . TYR A 1 133 ? 18.601 7.141   25.347 1.00 36.18  ?  133 TYR A CD2    1 
ATOM   956  C CE1    . TYR A 1 133 ? 17.816 5.180   27.149 1.00 38.91  ?  133 TYR A CE1    1 
ATOM   957  C CE2    . TYR A 1 133 ? 19.511 6.648   26.271 1.00 33.18  ?  133 TYR A CE2    1 
ATOM   958  C CZ     . TYR A 1 133 ? 19.112 5.651   27.168 1.00 40.32  ?  133 TYR A CZ     1 
ATOM   959  O OH     . TYR A 1 133 ? 20.000 5.118   28.097 1.00 45.20  ?  133 TYR A OH     1 
ATOM   960  N N      . VAL A 1 134 ? 16.731 10.037  25.847 1.00 37.32  ?  134 VAL A N      1 
ATOM   961  C CA     . VAL A 1 134 ? 17.587 11.225  25.902 1.00 37.81  ?  134 VAL A CA     1 
ATOM   962  C C      . VAL A 1 134 ? 19.035 10.786  26.067 1.00 34.93  ?  134 VAL A C      1 
ATOM   963  O O      . VAL A 1 134 ? 19.340 9.910   26.883 1.00 33.75  ?  134 VAL A O      1 
ATOM   964  C CB     . VAL A 1 134 ? 17.183 12.196  27.029 1.00 34.94  ?  134 VAL A CB     1 
ATOM   965  C CG1    . VAL A 1 134 ? 17.818 13.557  26.790 1.00 32.72  ?  134 VAL A CG1    1 
ATOM   966  C CG2    . VAL A 1 134 ? 15.694 12.338  27.097 1.00 32.58  ?  134 VAL A CG2    1 
ATOM   967  N N      . ALA A 1 135 ? 19.926 11.408  25.307 1.00 27.40  ?  135 ALA A N      1 
ATOM   968  C CA     . ALA A 1 135 ? 21.332 11.037  25.301 1.00 28.83  ?  135 ALA A CA     1 
ATOM   969  C C      . ALA A 1 135 ? 22.188 12.285  25.237 1.00 25.68  ?  135 ALA A C      1 
ATOM   970  O O      . ALA A 1 135 ? 21.843 13.239  24.535 1.00 27.47  ?  135 ALA A O      1 
ATOM   971  C CB     . ALA A 1 135 ? 21.665 10.133  24.105 1.00 32.08  ?  135 ALA A CB     1 
ATOM   972  N N      . ILE A 1 136 ? 23.322 12.260  25.935 1.00 35.06  ?  136 ILE A N      1 
ATOM   973  C CA     . ILE A 1 136 ? 24.202 13.424  25.962 1.00 33.87  ?  136 ILE A CA     1 
ATOM   974  C C      . ILE A 1 136 ? 24.973 13.534  24.649 1.00 37.12  ?  136 ILE A C      1 
ATOM   975  O O      . ILE A 1 136 ? 25.541 12.551  24.152 1.00 41.89  ?  136 ILE A O      1 
ATOM   976  C CB     . ILE A 1 136 ? 25.144 13.343  27.174 1.00 34.06  ?  136 ILE A CB     1 
ATOM   977  C CG1    . ILE A 1 136 ? 24.486 13.937  28.397 1.00 30.30  ?  136 ILE A CG1    1 
ATOM   978  C CG2    . ILE A 1 136 ? 26.491 14.048  26.908 1.00 37.05  ?  136 ILE A CG2    1 
ATOM   979  C CD1    . ILE A 1 136 ? 25.129 13.429  29.656 1.00 29.86  ?  136 ILE A CD1    1 
ATOM   980  N N      . GLN A 1 137 ? 25.010 14.745  24.082 1.00 25.29  ?  137 GLN A N      1 
ATOM   981  C CA     . GLN A 1 137 ? 25.659 14.932  22.784 1.00 24.00  ?  137 GLN A CA     1 
ATOM   982  C C      . GLN A 1 137 ? 27.090 14.422  22.783 1.00 25.21  ?  137 GLN A C      1 
ATOM   983  O O      . GLN A 1 137 ? 27.541 13.843  21.792 1.00 32.56  ?  137 GLN A O      1 
ATOM   984  C CB     . GLN A 1 137 ? 25.624 16.402  22.374 1.00 21.28  ?  137 GLN A CB     1 
ATOM   985  C CG     . GLN A 1 137 ? 24.236 16.816  21.919 1.00 18.71  ?  137 GLN A CG     1 
ATOM   986  C CD     . GLN A 1 137 ? 23.915 18.218  22.295 1.00 18.78  ?  137 GLN A CD     1 
ATOM   987  O OE1    . GLN A 1 137 ? 24.825 19.038  22.476 1.00 19.98  ?  137 GLN A OE1    1 
ATOM   988  N NE2    . GLN A 1 137 ? 22.608 18.523  22.434 1.00 18.94  ?  137 GLN A NE2    1 
ATOM   989  N N      . ALA A 1 138 ? 27.827 14.632  23.872 1.00 27.61  ?  138 ALA A N      1 
ATOM   990  C CA     . ALA A 1 138 ? 29.237 14.274  23.852 1.00 23.11  ?  138 ALA A CA     1 
ATOM   991  C C      . ALA A 1 138 ? 29.445 12.786  24.040 1.00 24.55  ?  138 ALA A C      1 
ATOM   992  O O      . ALA A 1 138 ? 30.488 12.264  23.642 1.00 28.78  ?  138 ALA A O      1 
ATOM   993  C CB     . ALA A 1 138 ? 30.004 15.076  24.908 1.00 18.11  ?  138 ALA A CB     1 
ATOM   994  N N      . VAL A 1 139 ? 28.476 12.092  24.635 1.00 24.03  ?  139 VAL A N      1 
ATOM   995  C CA     . VAL A 1 139 ? 28.608 10.654  24.842 1.00 18.28  ?  139 VAL A CA     1 
ATOM   996  C C      . VAL A 1 139 ? 28.401 9.913   23.529 1.00 18.39  ?  139 VAL A C      1 
ATOM   997  O O      . VAL A 1 139 ? 29.106 8.946   23.221 1.00 18.43  ?  139 VAL A O      1 
ATOM   998  C CB     . VAL A 1 139 ? 27.627 10.190  25.938 1.00 18.32  ?  139 VAL A CB     1 
ATOM   999  C CG1    . VAL A 1 139 ? 27.673 8.719   26.090 1.00 18.40  ?  139 VAL A CG1    1 
ATOM   1000 C CG2    . VAL A 1 139 ? 28.012 10.860  27.263 1.00 18.22  ?  139 VAL A CG2    1 
ATOM   1001 N N      . LEU A 1 140 ? 27.442 10.366  22.728 1.00 18.47  ?  140 LEU A N      1 
ATOM   1002 C CA     . LEU A 1 140 ? 27.228 9.772   21.418 1.00 18.60  ?  140 LEU A CA     1 
ATOM   1003 C C      . LEU A 1 140 ? 28.417 10.022  20.477 1.00 20.71  ?  140 LEU A C      1 
ATOM   1004 O O      . LEU A 1 140 ? 28.739 9.167   19.644 1.00 18.65  ?  140 LEU A O      1 
ATOM   1005 C CB     . LEU A 1 140 ? 25.926 10.309  20.819 1.00 18.71  ?  140 LEU A CB     1 
ATOM   1006 C CG     . LEU A 1 140 ? 24.588 10.065  21.516 1.00 18.81  ?  140 LEU A CG     1 
ATOM   1007 C CD1    . LEU A 1 140 ? 23.628 11.168  21.130 1.00 18.87  ?  140 LEU A CD1    1 
ATOM   1008 C CD2    . LEU A 1 140 ? 23.965 8.684   21.222 1.00 18.99  ?  140 LEU A CD2    1 
ATOM   1009 N N      . SER A 1 141 ? 29.064 11.196  20.566 1.00 28.27  ?  141 SER A N      1 
ATOM   1010 C CA     . SER A 1 141 ? 30.251 11.438  19.744 1.00 26.22  ?  141 SER A CA     1 
ATOM   1011 C C      . SER A 1 141 ? 31.335 10.401  20.037 1.00 34.70  ?  141 SER A C      1 
ATOM   1012 O O      . SER A 1 141 ? 31.939 9.837   19.115 1.00 39.32  ?  141 SER A O      1 
ATOM   1013 C CB     . SER A 1 141 ? 30.783 12.851  19.968 1.00 20.92  ?  141 SER A CB     1 
ATOM   1014 O OG     . SER A 1 141 ? 30.074 13.787  19.182 1.00 26.11  ?  141 SER A OG     1 
ATOM   1015 N N      . LEU A 1 142 ? 31.585 10.136  21.326 1.00 28.35  ?  142 LEU A N      1 
ATOM   1016 C CA     . LEU A 1 142 ? 32.516 9.090   21.731 1.00 26.83  ?  142 LEU A CA     1 
ATOM   1017 C C      . LEU A 1 142 ? 32.117 7.725   21.157 1.00 28.99  ?  142 LEU A C      1 
ATOM   1018 O O      . LEU A 1 142 ? 32.977 6.911   20.796 1.00 24.49  ?  142 LEU A O      1 
ATOM   1019 C CB     . LEU A 1 142 ? 32.573 9.047   23.255 1.00 24.68  ?  142 LEU A CB     1 
ATOM   1020 C CG     . LEU A 1 142 ? 33.897 8.478   23.759 1.00 27.83  ?  142 LEU A CG     1 
ATOM   1021 C CD1    . LEU A 1 142 ? 34.893 9.610   23.895 1.00 25.41  ?  142 LEU A CD1    1 
ATOM   1022 C CD2    . LEU A 1 142 ? 33.713 7.701   25.044 1.00 20.17  ?  142 LEU A CD2    1 
ATOM   1023 N N      . TYR A 1 143 ? 30.811 7.467   21.084 1.00 26.41  ?  143 TYR A N      1 
ATOM   1024 C CA     . TYR A 1 143 ? 30.249 6.213   20.603 1.00 23.41  ?  143 TYR A CA     1 
ATOM   1025 C C      . TYR A 1 143 ? 30.427 6.036   19.097 1.00 23.02  ?  143 TYR A C      1 
ATOM   1026 O O      . TYR A 1 143 ? 30.574 4.906   18.624 1.00 25.34  ?  143 TYR A O      1 
ATOM   1027 C CB     . TYR A 1 143 ? 28.754 6.184   20.940 1.00 27.12  ?  143 TYR A CB     1 
ATOM   1028 C CG     . TYR A 1 143 ? 28.367 5.770   22.351 1.00 29.83  ?  143 TYR A CG     1 
ATOM   1029 C CD1    . TYR A 1 143 ? 29.281 5.184   23.212 1.00 29.10  ?  143 TYR A CD1    1 
ATOM   1030 C CD2    . TYR A 1 143 ? 27.054 5.921   22.795 1.00 28.96  ?  143 TYR A CD2    1 
ATOM   1031 C CE1    . TYR A 1 143 ? 28.905 4.776   24.478 1.00 32.75  ?  143 TYR A CE1    1 
ATOM   1032 C CE2    . TYR A 1 143 ? 26.667 5.520   24.059 1.00 22.31  ?  143 TYR A CE2    1 
ATOM   1033 C CZ     . TYR A 1 143 ? 27.594 4.944   24.902 1.00 30.82  ?  143 TYR A CZ     1 
ATOM   1034 O OH     . TYR A 1 143 ? 27.223 4.538   26.180 1.00 28.86  ?  143 TYR A OH     1 
ATOM   1035 N N      . ALA A 1 144 ? 30.359 7.129   18.327 1.00 29.24  ?  144 ALA A N      1 
ATOM   1036 C CA     . ALA A 1 144 ? 30.617 7.066   16.886 1.00 31.50  ?  144 ALA A CA     1 
ATOM   1037 C C      . ALA A 1 144 ? 32.061 6.683   16.598 1.00 29.92  ?  144 ALA A C      1 
ATOM   1038 O O      . ALA A 1 144 ? 32.351 6.106   15.547 1.00 33.92  ?  144 ALA A O      1 
ATOM   1039 C CB     . ALA A 1 144 ? 30.289 8.408   16.219 1.00 28.69  ?  144 ALA A CB     1 
ATOM   1040 N N      . SER A 1 145 ? 32.945 6.905   17.545 1.00 33.88  ?  145 SER A N      1 
ATOM   1041 C CA     . SER A 1 145 ? 34.330 6.532   17.418 1.00 33.28  ?  145 SER A CA     1 
ATOM   1042 C C      . SER A 1 145 ? 34.560 5.179   18.008 1.00 38.60  ?  145 SER A C      1 
ATOM   1043 O O      . SER A 1 145 ? 35.677 4.721   18.050 1.00 45.66  ?  145 SER A O      1 
ATOM   1044 C CB     . SER A 1 145 ? 35.221 7.524   18.150 1.00 31.89  ?  145 SER A CB     1 
ATOM   1045 O OG     . SER A 1 145 ? 35.228 7.288   19.533 1.00 35.31  ?  145 SER A OG     1 
ATOM   1046 N N      . GLY A 1 146 ? 33.513 4.544   18.491 1.00 45.79  ?  146 GLY A N      1 
ATOM   1047 C CA     . GLY A 1 146 ? 33.634 3.200   19.017 1.00 48.58  ?  146 GLY A CA     1 
ATOM   1048 C C      . GLY A 1 146 ? 34.353 3.081   20.344 1.00 48.98  ?  146 GLY A C      1 
ATOM   1049 O O      . GLY A 1 146 ? 34.912 2.021   20.632 1.00 55.12  ?  146 GLY A O      1 
ATOM   1050 N N      . ARG A 1 147 ? 34.365 4.136   21.161 1.00 32.57  ?  147 ARG A N      1 
ATOM   1051 C CA     . ARG A 1 147 ? 34.904 4.080   22.511 1.00 32.72  ?  147 ARG A CA     1 
ATOM   1052 C C      . ARG A 1 147 ? 33.806 4.251   23.550 1.00 36.53  ?  147 ARG A C      1 
ATOM   1053 O O      . ARG A 1 147 ? 32.809 4.945   23.326 1.00 40.09  ?  147 ARG A O      1 
ATOM   1054 C CB     . ARG A 1 147 ? 35.943 5.178   22.750 1.00 35.31  ?  147 ARG A CB     1 
ATOM   1055 C CG     . ARG A 1 147 ? 37.206 5.079   21.946 1.00 31.80  ?  147 ARG A CG     1 
ATOM   1056 C CD     . ARG A 1 147 ? 37.530 6.444   21.386 1.00 32.25  ?  147 ARG A CD     1 
ATOM   1057 N NE     . ARG A 1 147 ? 38.952 6.593   21.122 1.00 33.43  ?  147 ARG A NE     1 
ATOM   1058 C CZ     . ARG A 1 147 ? 39.544 6.194   20.015 1.00 37.29  ?  147 ARG A CZ     1 
ATOM   1059 N NH1    . ARG A 1 147 ? 38.830 5.619   19.066 1.00 41.01  ?  147 ARG A NH1    1 
ATOM   1060 N NH2    . ARG A 1 147 ? 40.847 6.369   19.862 1.00 45.42  ?  147 ARG A NH2    1 
ATOM   1061 N N      . THR A 1 148 ? 34.088 3.782   24.758 1.00 42.74  ?  148 THR A N      1 
ATOM   1062 C CA     . THR A 1 148 ? 33.196 4.047   25.874 1.00 36.18  ?  148 THR A CA     1 
ATOM   1063 C C      . THR A 1 148 ? 33.923 5.013   26.825 1.00 39.73  ?  148 THR A C      1 
ATOM   1064 O O      . THR A 1 148 ? 33.263 5.733   27.532 1.00 37.18  ?  148 THR A O      1 
ATOM   1065 C CB     . THR A 1 148 ? 32.747 2.778   26.594 1.00 38.35  ?  148 THR A CB     1 
ATOM   1066 O OG1    . THR A 1 148 ? 33.890 1.990   26.941 1.00 46.42  ?  148 THR A OG1    1 
ATOM   1067 C CG2    . THR A 1 148 ? 31.849 1.970   25.704 1.00 40.15  ?  148 THR A CG2    1 
ATOM   1068 N N      . THR A 1 149 ? 35.270 5.070   26.807 1.00 42.08  ?  149 THR A N      1 
ATOM   1069 C CA     . THR A 1 149 ? 36.001 5.915   27.749 1.00 37.24  ?  149 THR A CA     1 
ATOM   1070 C C      . THR A 1 149 ? 36.895 6.909   27.013 1.00 34.45  ?  149 THR A C      1 
ATOM   1071 O O      . THR A 1 149 ? 37.616 6.539   26.079 1.00 38.05  ?  149 THR A O      1 
ATOM   1072 C CB     . THR A 1 149 ? 36.851 5.035   28.722 1.00 36.59  ?  149 THR A CB     1 
ATOM   1073 O OG1    . THR A 1 149 ? 35.977 4.193   29.487 1.00 26.04  ?  149 THR A OG1    1 
ATOM   1074 C CG2    . THR A 1 149 ? 37.801 5.890   29.682 1.00 26.55  ?  149 THR A CG2    1 
ATOM   1075 N N      . GLY A 1 150 ? 36.847 8.159   27.447 1.00 21.70  ?  150 GLY A N      1 
ATOM   1076 C CA     . GLY A 1 150 ? 37.715 9.201   26.927 1.00 20.27  ?  150 GLY A CA     1 
ATOM   1077 C C      . GLY A 1 150 ? 37.045 10.549  27.092 1.00 21.45  ?  150 GLY A C      1 
ATOM   1078 O O      . GLY A 1 150 ? 35.912 10.642  27.548 1.00 22.90  ?  150 GLY A O      1 
ATOM   1079 N N      . ILE A 1 151 ? 37.771 11.605  26.711 1.00 18.04  ?  151 ILE A N      1 
ATOM   1080 C CA     . ILE A 1 151 ? 37.312 12.975  26.960 1.00 17.98  ?  151 ILE A CA     1 
ATOM   1081 C C      . ILE A 1 151 ? 36.949 13.636  25.636 1.00 19.10  ?  151 ILE A C      1 
ATOM   1082 O O      . ILE A 1 151 ? 37.789 13.753  24.740 1.00 21.21  ?  151 ILE A O      1 
ATOM   1083 C CB     . ILE A 1 151 ? 38.348 13.818  27.721 1.00 17.99  ?  151 ILE A CB     1 
ATOM   1084 C CG1    . ILE A 1 151 ? 37.861 15.267  27.809 1.00 17.99  ?  151 ILE A CG1    1 
ATOM   1085 C CG2    . ILE A 1 151 ? 39.766 13.701  27.080 1.00 18.06  ?  151 ILE A CG2    1 
ATOM   1086 C CD1    . ILE A 1 151 ? 38.388 16.025  28.964 1.00 18.01  ?  151 ILE A CD1    1 
ATOM   1087 N N      . VAL A 1 152 ? 35.706 14.104  25.538 1.00 28.73  ?  152 VAL A N      1 
ATOM   1088 C CA     . VAL A 1 152 ? 35.174 14.654  24.302 1.00 26.83  ?  152 VAL A CA     1 
ATOM   1089 C C      . VAL A 1 152 ? 35.365 16.166  24.327 1.00 28.07  ?  152 VAL A C      1 
ATOM   1090 O O      . VAL A 1 152 ? 35.137 16.824  25.342 1.00 31.92  ?  152 VAL A O      1 
ATOM   1091 C CB     . VAL A 1 152 ? 33.694 14.253  24.111 1.00 22.63  ?  152 VAL A CB     1 
ATOM   1092 C CG1    . VAL A 1 152 ? 33.112 14.909  22.904 1.00 24.94  ?  152 VAL A CG1    1 
ATOM   1093 C CG2    . VAL A 1 152 ? 33.592 12.775  23.892 1.00 22.29  ?  152 VAL A CG2    1 
ATOM   1094 N N      . MET A 1 153 ? 35.843 16.709  23.227 1.00 35.21  ?  153 MET A N      1 
ATOM   1095 C CA     . MET A 1 153 ? 35.916 18.146  23.017 1.00 31.83  ?  153 MET A CA     1 
ATOM   1096 C C      . MET A 1 153 ? 34.876 18.452  21.935 1.00 31.86  ?  153 MET A C      1 
ATOM   1097 O O      . MET A 1 153 ? 35.088 18.138  20.761 1.00 31.96  ?  153 MET A O      1 
ATOM   1098 C CB     . MET A 1 153 ? 37.346 18.521  22.616 1.00 31.59  ?  153 MET A CB     1 
ATOM   1099 C CG     . MET A 1 153 ? 37.537 19.867  21.961 1.00 40.62  ?  153 MET A CG     1 
ATOM   1100 S SD     . MET A 1 153 ? 37.053 21.128  23.122 1.00 50.98  ?  153 MET A SD     1 
ATOM   1101 C CE     . MET A 1 153 ? 37.934 20.586  24.592 1.00 58.58  ?  153 MET A CE     1 
ATOM   1102 N N      . ASP A 1 154 ? 33.729 18.971  22.323 1.00 33.16  ?  154 ASP A N      1 
ATOM   1103 C CA     . ASP A 1 154 ? 32.686 19.340  21.388 1.00 35.63  ?  154 ASP A CA     1 
ATOM   1104 C C      . ASP A 1 154 ? 32.539 20.842  21.268 1.00 34.69  ?  154 ASP A C      1 
ATOM   1105 O O      . ASP A 1 154 ? 32.253 21.507  22.227 1.00 26.88  ?  154 ASP A O      1 
ATOM   1106 C CB     . ASP A 1 154 ? 31.377 18.678  21.793 1.00 43.28  ?  154 ASP A CB     1 
ATOM   1107 C CG     . ASP A 1 154 ? 30.226 18.971  20.845 1.00 48.87  ?  154 ASP A CG     1 
ATOM   1108 O OD1    . ASP A 1 154 ? 29.552 20.009  21.015 1.00 53.87  ?  154 ASP A OD1    1 
ATOM   1109 O OD2    . ASP A 1 154 ? 29.953 18.142  19.961 1.00 43.20  -1 154 ASP A OD2    1 
ATOM   1110 N N      . SER A 1 155 ? 32.763 21.362  20.074 1.00 38.05  ?  155 SER A N      1 
ATOM   1111 C CA     . SER A 1 155 ? 32.631 22.785  19.826 1.00 40.42  ?  155 SER A CA     1 
ATOM   1112 C C      . SER A 1 155 ? 31.597 23.014  18.791 1.00 42.74  ?  155 SER A C      1 
ATOM   1113 O O      . SER A 1 155 ? 31.713 22.551  17.676 1.00 48.81  ?  155 SER A O      1 
ATOM   1114 C CB     . SER A 1 155 ? 33.927 23.393  19.337 1.00 40.11  ?  155 SER A CB     1 
ATOM   1115 O OG     . SER A 1 155 ? 33.855 24.798  19.332 1.00 41.87  ?  155 SER A OG     1 
ATOM   1116 N N      . GLY A 1 156 ? 30.574 23.742  19.160 1.00 22.25  ?  156 GLY A N      1 
ATOM   1117 C CA     . GLY A 1 156 ? 29.538 24.050  18.230 1.00 18.91  ?  156 GLY A CA     1 
ATOM   1118 C C      . GLY A 1 156 ? 29.403 25.484  17.873 1.00 20.48  ?  156 GLY A C      1 
ATOM   1119 O O      . GLY A 1 156 ? 30.355 26.115  17.566 1.00 19.35  ?  156 GLY A O      1 
ATOM   1120 N N      . ASP A 1 157 ? 28.189 25.989  17.881 1.00 44.67  ?  157 ASP A N      1 
ATOM   1121 C CA     . ASP A 1 157 ? 27.928 27.351  17.483 1.00 46.05  ?  157 ASP A CA     1 
ATOM   1122 C C      . ASP A 1 157 ? 27.984 28.315  18.623 1.00 51.09  ?  157 ASP A C      1 
ATOM   1123 O O      . ASP A 1 157 ? 28.650 29.317  18.545 1.00 47.41  ?  157 ASP A O      1 
ATOM   1124 C CB     . ASP A 1 157 ? 26.573 27.432  16.811 1.00 39.25  ?  157 ASP A CB     1 
ATOM   1125 C CG     . ASP A 1 157 ? 26.466 28.586  15.874 1.00 52.89  ?  157 ASP A CG     1 
ATOM   1126 O OD1    . ASP A 1 157 ? 27.456 29.307  15.718 1.00 60.40  ?  157 ASP A OD1    1 
ATOM   1127 O OD2    . ASP A 1 157 ? 25.395 28.786  15.287 1.00 60.05  -1 157 ASP A OD2    1 
ATOM   1128 N N      . GLY A 1 158 ? 27.280 28.009  19.695 1.00 58.48  ?  158 GLY A N      1 
ATOM   1129 C CA     . GLY A 1 158 ? 27.269 28.868  20.855 1.00 53.49  ?  158 GLY A CA     1 
ATOM   1130 C C      . GLY A 1 158 ? 27.974 28.301  22.050 1.00 57.23  ?  158 GLY A C      1 
ATOM   1131 O O      . GLY A 1 158 ? 28.225 29.020  22.997 1.00 68.14  ?  158 GLY A O      1 
ATOM   1132 N N      . VAL A 1 159 ? 28.325 27.029  22.012 1.00 34.12  ?  159 VAL A N      1 
ATOM   1133 C CA     . VAL A 1 159 ? 28.908 26.431  23.178 1.00 29.40  ?  159 VAL A CA     1 
ATOM   1134 C C      . VAL A 1 159 ? 30.002 25.420  22.940 1.00 34.52  ?  159 VAL A C      1 
ATOM   1135 O O      . VAL A 1 159 ? 29.969 24.668  21.989 1.00 34.59  ?  159 VAL A O      1 
ATOM   1136 C CB     . VAL A 1 159 ? 27.802 25.866  24.093 1.00 29.93  ?  159 VAL A CB     1 
ATOM   1137 C CG1    . VAL A 1 159 ? 27.207 24.583  23.548 1.00 30.95  ?  159 VAL A CG1    1 
ATOM   1138 C CG2    . VAL A 1 159 ? 28.271 25.733  25.525 1.00 29.14  ?  159 VAL A CG2    1 
ATOM   1139 N N      . THR A 1 160 ? 30.998 25.439  23.790 1.00 36.06  ?  160 THR A N      1 
ATOM   1140 C CA     . THR A 1 160 ? 32.055 24.470  23.737 1.00 35.29  ?  160 THR A CA     1 
ATOM   1141 C C      . THR A 1 160 ? 31.989 23.676  25.047 1.00 37.33  ?  160 THR A C      1 
ATOM   1142 O O      . THR A 1 160 ? 31.712 24.211  26.097 1.00 33.88  ?  160 THR A O      1 
ATOM   1143 C CB     . THR A 1 160 ? 33.434 25.134  23.541 1.00 33.74  ?  160 THR A CB     1 
ATOM   1144 O OG1    . THR A 1 160 ? 33.733 25.216  22.155 1.00 37.48  ?  160 THR A OG1    1 
ATOM   1145 C CG2    . THR A 1 160 ? 34.528 24.345  24.218 1.00 31.65  ?  160 THR A CG2    1 
ATOM   1146 N N      . HIS A 1 161 ? 32.181 22.371  24.964 1.00 34.93  ?  161 HIS A N      1 
ATOM   1147 C CA     . HIS A 1 161 ? 32.160 21.530  26.139 1.00 36.14  ?  161 HIS A CA     1 
ATOM   1148 C C      . HIS A 1 161 ? 33.276 20.508  26.174 1.00 38.30  ?  161 HIS A C      1 
ATOM   1149 O O      . HIS A 1 161 ? 33.526 19.841  25.195 1.00 36.57  ?  161 HIS A O      1 
ATOM   1150 C CB     . HIS A 1 161 ? 30.849 20.784  26.216 1.00 36.89  ?  161 HIS A CB     1 
ATOM   1151 C CG     . HIS A 1 161 ? 29.758 21.518  26.919 1.00 42.91  ?  161 HIS A CG     1 
ATOM   1152 N ND1    . HIS A 1 161 ? 28.649 21.996  26.262 1.00 36.23  ?  161 HIS A ND1    1 
ATOM   1153 C CD2    . HIS A 1 161 ? 29.581 21.814  28.225 1.00 42.11  ?  161 HIS A CD2    1 
ATOM   1154 C CE1    . HIS A 1 161 ? 27.843 22.573  27.133 1.00 39.80  ?  161 HIS A CE1    1 
ATOM   1155 N NE2    . HIS A 1 161 ? 28.387 22.478  28.330 1.00 39.39  ?  161 HIS A NE2    1 
ATOM   1156 N N      . THR A 1 162 ? 33.950 20.387  27.307 1.00 36.91  ?  162 THR A N      1 
ATOM   1157 C CA     . THR A 1 162 ? 34.964 19.368  27.489 1.00 34.05  ?  162 THR A CA     1 
ATOM   1158 C C      . THR A 1 162 ? 34.364 18.352  28.415 1.00 29.62  ?  162 THR A C      1 
ATOM   1159 O O      . THR A 1 162 ? 34.170 18.621  29.568 1.00 36.59  ?  162 THR A O      1 
ATOM   1160 C CB     . THR A 1 162 ? 36.268 19.968  27.987 1.00 38.83  ?  162 THR A CB     1 
ATOM   1161 O OG1    . THR A 1 162 ? 36.473 21.231  27.357 1.00 32.91  ?  162 THR A OG1    1 
ATOM   1162 C CG2    . THR A 1 162 ? 37.377 19.079  27.638 1.00 38.52  ?  162 THR A CG2    1 
ATOM   1163 N N      . VAL A 1 163 ? 34.015 17.193  27.892 1.00 22.96  ?  163 VAL A N      1 
ATOM   1164 C CA     . VAL A 1 163 ? 33.289 16.212  28.659 1.00 23.47  ?  163 VAL A CA     1 
ATOM   1165 C C      . VAL A 1 163 ? 33.951 14.885  28.798 1.00 27.58  ?  163 VAL A C      1 
ATOM   1166 O O      . VAL A 1 163 ? 34.021 14.119  27.870 1.00 29.63  ?  163 VAL A O      1 
ATOM   1167 C CB     . VAL A 1 163 ? 31.892 15.998  28.066 1.00 25.73  ?  163 VAL A CB     1 
ATOM   1168 C CG1    . VAL A 1 163 ? 31.066 15.013  28.863 1.00 25.41  ?  163 VAL A CG1    1 
ATOM   1169 C CG2    . VAL A 1 163 ? 31.162 17.307  27.891 1.00 29.66  ?  163 VAL A CG2    1 
ATOM   1170 N N      . PRO A 1 164 ? 34.462 14.618  29.985 1.00 28.90  ?  164 PRO A N      1 
ATOM   1171 C CA     . PRO A 1 164 ? 35.063 13.328  30.258 1.00 26.04  ?  164 PRO A CA     1 
ATOM   1172 C C      . PRO A 1 164 ? 34.030 12.233  30.450 1.00 31.28  ?  164 PRO A C      1 
ATOM   1173 O O      . PRO A 1 164 ? 33.082 12.418  31.176 1.00 32.92  ?  164 PRO A O      1 
ATOM   1174 C CB     . PRO A 1 164 ? 35.823 13.579  31.530 1.00 24.61  ?  164 PRO A CB     1 
ATOM   1175 C CG     . PRO A 1 164 ? 35.795 15.019  31.779 1.00 22.96  ?  164 PRO A CG     1 
ATOM   1176 C CD     . PRO A 1 164 ? 34.580 15.533  31.119 1.00 24.38  ?  164 PRO A CD     1 
ATOM   1177 N N      . ILE A 1 165 ? 34.209 11.103  29.781 1.00 32.24  ?  165 ILE A N      1 
ATOM   1178 C CA     . ILE A 1 165 ? 33.260 10.003  29.854 1.00 30.58  ?  165 ILE A CA     1 
ATOM   1179 C C      . ILE A 1 165 ? 33.945 8.721   30.273 1.00 34.49  ?  165 ILE A C      1 
ATOM   1180 O O      . ILE A 1 165 ? 34.863 8.272   29.633 1.00 29.27  ?  165 ILE A O      1 
ATOM   1181 C CB     . ILE A 1 165 ? 32.501 9.803   28.529 1.00 26.29  ?  165 ILE A CB     1 
ATOM   1182 C CG1    . ILE A 1 165 ? 31.612 10.999  28.237 1.00 26.23  ?  165 ILE A CG1    1 
ATOM   1183 C CG2    . ILE A 1 165 ? 31.646 8.560   28.549 1.00 18.27  ?  165 ILE A CG2    1 
ATOM   1184 C CD1    . ILE A 1 165 ? 31.850 11.602  26.886 1.00 27.14  ?  165 ILE A CD1    1 
ATOM   1185 N N      . TYR A 1 166 ? 33.534 8.176   31.405 1.00 42.87  ?  166 TYR A N      1 
ATOM   1186 C CA     . TYR A 1 166 ? 34.072 6.925   31.868 1.00 42.23  ?  166 TYR A CA     1 
ATOM   1187 C C      . TYR A 1 166 ? 33.038 5.852   31.686 1.00 45.00  ?  166 TYR A C      1 
ATOM   1188 O O      . TYR A 1 166 ? 31.984 5.929   32.286 1.00 45.58  ?  166 TYR A O      1 
ATOM   1189 C CB     . TYR A 1 166 ? 34.460 7.032   33.335 1.00 33.66  ?  166 TYR A CB     1 
ATOM   1190 C CG     . TYR A 1 166 ? 35.033 5.772   33.906 1.00 45.41  ?  166 TYR A CG     1 
ATOM   1191 C CD1    . TYR A 1 166 ? 36.219 5.254   33.426 1.00 52.63  ?  166 TYR A CD1    1 
ATOM   1192 C CD2    . TYR A 1 166 ? 34.389 5.095   34.926 1.00 47.01  ?  166 TYR A CD2    1 
ATOM   1193 C CE1    . TYR A 1 166 ? 36.750 4.098   33.944 1.00 53.80  ?  166 TYR A CE1    1 
ATOM   1194 C CE2    . TYR A 1 166 ? 34.913 3.937   35.449 1.00 49.52  ?  166 TYR A CE2    1 
ATOM   1195 C CZ     . TYR A 1 166 ? 36.096 3.448   34.955 1.00 52.76  ?  166 TYR A CZ     1 
ATOM   1196 O OH     . TYR A 1 166 ? 36.627 2.293   35.469 1.00 59.23  ?  166 TYR A OH     1 
ATOM   1197 N N      . GLU A 1 167 ? 33.327 4.863   30.856 1.00 35.32  ?  167 GLU A N      1 
ATOM   1198 C CA     . GLU A 1 167 ? 32.431 3.746   30.621 1.00 34.71  ?  167 GLU A CA     1 
ATOM   1199 C C      . GLU A 1 167 ? 31.004 4.074   30.307 1.00 39.50  ?  167 GLU A C      1 
ATOM   1200 O O      . GLU A 1 167 ? 30.105 3.406   30.760 1.00 38.20  ?  167 GLU A O      1 
ATOM   1201 C CB     . GLU A 1 167 ? 32.503 2.770   31.773 1.00 41.59  ?  167 GLU A CB     1 
ATOM   1202 C CG     . GLU A 1 167 ? 33.864 2.122   31.922 1.00 52.11  ?  167 GLU A CG     1 
ATOM   1203 C CD     . GLU A 1 167 ? 33.884 1.061   32.993 1.00 47.50  ?  167 GLU A CD     1 
ATOM   1204 O OE1    . GLU A 1 167 ? 32.802 0.721   33.503 1.00 43.45  ?  167 GLU A OE1    1 
ATOM   1205 O OE2    . GLU A 1 167 ? 34.980 0.571   33.320 1.00 45.83  -1 167 GLU A OE2    1 
ATOM   1206 N N      . GLY A 1 168 ? 30.797 5.100   29.517 1.00 39.19  ?  168 GLY A N      1 
ATOM   1207 C CA     . GLY A 1 168 ? 29.462 5.527   29.193 1.00 38.99  ?  168 GLY A CA     1 
ATOM   1208 C C      . GLY A 1 168 ? 28.966 6.697   29.978 1.00 32.25  ?  168 GLY A C      1 
ATOM   1209 O O      . GLY A 1 168 ? 28.021 7.341   29.576 1.00 34.70  ?  168 GLY A O      1 
ATOM   1210 N N      . TYR A 1 169 ? 29.608 6.979   31.090 1.00 30.93  ?  169 TYR A N      1 
ATOM   1211 C CA     . TYR A 1 169 ? 29.135 8.033   31.953 1.00 31.50  ?  169 TYR A CA     1 
ATOM   1212 C C      . TYR A 1 169 ? 29.838 9.348   31.884 1.00 32.60  ?  169 TYR A C      1 
ATOM   1213 O O      . TYR A 1 169 ? 30.981 9.458   32.264 1.00 34.64  ?  169 TYR A O      1 
ATOM   1214 C CB     . TYR A 1 169 ? 29.054 7.540   33.400 1.00 36.48  ?  169 TYR A CB     1 
ATOM   1215 C CG     . TYR A 1 169 ? 28.261 8.421   34.315 1.00 43.85  ?  169 TYR A CG     1 
ATOM   1216 C CD1    . TYR A 1 169 ? 26.925 8.682   34.068 1.00 45.40  ?  169 TYR A CD1    1 
ATOM   1217 C CD2    . TYR A 1 169 ? 28.847 8.994   35.425 1.00 45.57  ?  169 TYR A CD2    1 
ATOM   1218 C CE1    . TYR A 1 169 ? 26.194 9.494   34.905 1.00 42.03  ?  169 TYR A CE1    1 
ATOM   1219 C CE2    . TYR A 1 169 ? 28.122 9.805   36.266 1.00 44.83  ?  169 TYR A CE2    1 
ATOM   1220 C CZ     . TYR A 1 169 ? 26.795 10.048  36.001 1.00 39.64  ?  169 TYR A CZ     1 
ATOM   1221 O OH     . TYR A 1 169 ? 26.064 10.854  36.831 1.00 40.25  ?  169 TYR A OH     1 
ATOM   1222 N N      . ALA A 1 170 ? 29.139 10.355  31.406 1.00 19.82  ?  170 ALA A N      1 
ATOM   1223 C CA     . ALA A 1 170 ? 29.689 11.673  31.405 1.00 21.87  ?  170 ALA A CA     1 
ATOM   1224 C C      . ALA A 1 170 ? 29.898 12.075  32.823 1.00 25.76  ?  170 ALA A C      1 
ATOM   1225 O O      . ALA A 1 170 ? 28.983 11.992  33.608 1.00 29.38  ?  170 ALA A O      1 
ATOM   1226 C CB     . ALA A 1 170 ? 28.766 12.628  30.715 1.00 18.06  ?  170 ALA A CB     1 
ATOM   1227 N N      . LEU A 1 171 ? 31.095 12.512  33.157 1.00 34.50  ?  171 LEU A N      1 
ATOM   1228 C CA     . LEU A 1 171 ? 31.428 12.841  34.529 1.00 34.61  ?  171 LEU A CA     1 
ATOM   1229 C C      . LEU A 1 171 ? 31.063 14.243  34.886 1.00 34.59  ?  171 LEU A C      1 
ATOM   1230 O O      . LEU A 1 171 ? 31.808 15.143  34.601 1.00 41.20  ?  171 LEU A O      1 
ATOM   1231 C CB     . LEU A 1 171 ? 32.899 12.566  34.796 1.00 31.71  ?  171 LEU A CB     1 
ATOM   1232 C CG     . LEU A 1 171 ? 33.309 11.117  34.607 1.00 33.49  ?  171 LEU A CG     1 
ATOM   1233 C CD1    . LEU A 1 171 ? 34.789 10.997  34.878 1.00 28.87  ?  171 LEU A CD1    1 
ATOM   1234 C CD2    . LEU A 1 171 ? 32.520 10.209  35.528 1.00 29.82  ?  171 LEU A CD2    1 
ATOM   1235 N N      . PRO A 1 172 ? 29.956 14.429  35.596 1.00 37.43  ?  172 PRO A N      1 
ATOM   1236 C CA     . PRO A 1 172 ? 29.432 15.750  35.909 1.00 37.45  ?  172 PRO A CA     1 
ATOM   1237 C C      . PRO A 1 172 ? 30.349 16.644  36.702 1.00 39.27  ?  172 PRO A C      1 
ATOM   1238 O O      . PRO A 1 172 ? 30.252 17.860  36.614 1.00 38.50  ?  172 PRO A O      1 
ATOM   1239 C CB     . PRO A 1 172 ? 28.202 15.395  36.734 1.00 35.60  ?  172 PRO A CB     1 
ATOM   1240 C CG     . PRO A 1 172 ? 27.900 13.975  36.444 1.00 35.89  ?  172 PRO A CG     1 
ATOM   1241 C CD     . PRO A 1 172 ? 29.262 13.402  36.374 1.00 35.68  ?  172 PRO A CD     1 
ATOM   1242 N N      . HIS A 1 173 ? 31.269 16.055  37.436 1.00 40.77  ?  173 HIS A N      1 
ATOM   1243 C CA     . HIS A 1 173 ? 32.167 16.806  38.263 1.00 36.59  ?  173 HIS A CA     1 
ATOM   1244 C C      . HIS A 1 173 ? 33.359 17.306  37.509 1.00 28.75  ?  173 HIS A C      1 
ATOM   1245 O O      . HIS A 1 173 ? 34.144 18.052  38.033 1.00 34.25  ?  173 HIS A O      1 
ATOM   1246 C CB     . HIS A 1 173 ? 32.557 15.937  39.453 1.00 36.64  ?  173 HIS A CB     1 
ATOM   1247 C CG     . HIS A 1 173 ? 33.000 14.561  39.089 1.00 36.22  ?  173 HIS A CG     1 
ATOM   1248 N ND1    . HIS A 1 173 ? 34.245 14.297  38.564 1.00 44.86  ?  173 HIS A ND1    1 
ATOM   1249 C CD2    . HIS A 1 173 ? 32.376 13.367  39.199 1.00 37.81  ?  173 HIS A CD2    1 
ATOM   1250 C CE1    . HIS A 1 173 ? 34.363 13.002  38.349 1.00 44.75  ?  173 HIS A CE1    1 
ATOM   1251 N NE2    . HIS A 1 173 ? 33.243 12.415  38.726 1.00 47.42  ?  173 HIS A NE2    1 
ATOM   1252 N N      . ALA A 1 174 ? 33.476 16.909  36.268 1.00 27.50  ?  174 ALA A N      1 
ATOM   1253 C CA     . ALA A 1 174 ? 34.576 17.344  35.445 1.00 35.34  ?  174 ALA A CA     1 
ATOM   1254 C C      . ALA A 1 174 ? 34.164 18.030  34.167 1.00 36.88  ?  174 ALA A C      1 
ATOM   1255 O O      . ALA A 1 174 ? 35.001 18.533  33.456 1.00 40.29  ?  174 ALA A O      1 
ATOM   1256 C CB     . ALA A 1 174 ? 35.445 16.181  35.125 1.00 31.26  ?  174 ALA A CB     1 
ATOM   1257 N N      . ILE A 1 175 ? 32.875 18.043  33.873 1.00 30.18  ?  175 ILE A N      1 
ATOM   1258 C CA     . ILE A 1 175 ? 32.382 18.654  32.646 1.00 34.34  ?  175 ILE A CA     1 
ATOM   1259 C C      . ILE A 1 175 ? 32.598 20.146  32.661 1.00 32.95  ?  175 ILE A C      1 
ATOM   1260 O O      . ILE A 1 175 ? 32.172 20.812  33.578 1.00 32.10  ?  175 ILE A O      1 
ATOM   1261 C CB     . ILE A 1 175 ? 30.925 18.265  32.303 1.00 32.32  ?  175 ILE A CB     1 
ATOM   1262 C CG1    . ILE A 1 175 ? 30.804 16.782  32.019 1.00 29.15  ?  175 ILE A CG1    1 
ATOM   1263 C CG2    . ILE A 1 175 ? 30.421 19.047  31.103 1.00 34.41  ?  175 ILE A CG2    1 
ATOM   1264 C CD1    . ILE A 1 175 ? 29.381 16.284  32.063 1.00 28.87  ?  175 ILE A CD1    1 
ATOM   1265 N N      . LEU A 1 176 ? 33.287 20.658  31.655 1.00 27.87  ?  176 LEU A N      1 
ATOM   1266 C CA     . LEU A 1 176 ? 33.623 22.055  31.596 1.00 29.10  ?  176 LEU A CA     1 
ATOM   1267 C C      . LEU A 1 176 ? 32.978 22.762  30.423 1.00 30.21  ?  176 LEU A C      1 
ATOM   1268 O O      . LEU A 1 176 ? 32.896 22.214  29.352 1.00 30.06  ?  176 LEU A O      1 
ATOM   1269 C CB     . LEU A 1 176 ? 35.140 22.189  31.569 1.00 32.15  ?  176 LEU A CB     1 
ATOM   1270 C CG     . LEU A 1 176 ? 35.988 21.942  32.822 1.00 31.11  ?  176 LEU A CG     1 
ATOM   1271 C CD1    . LEU A 1 176 ? 37.219 22.824  32.820 1.00 23.66  ?  176 LEU A CD1    1 
ATOM   1272 C CD2    . LEU A 1 176 ? 35.214 22.145  34.108 1.00 31.31  ?  176 LEU A CD2    1 
ATOM   1273 N N      . ARG A 1 177 ? 32.485 23.977  30.643 1.00 28.16  ?  177 ARG A N      1 
ATOM   1274 C CA     . ARG A 1 177 ? 31.796 24.741  29.598 1.00 27.64  ?  177 ARG A CA     1 
ATOM   1275 C C      . ARG A 1 177 ? 32.421 26.063  29.260 1.00 29.53  ?  177 ARG A C      1 
ATOM   1276 O O      . ARG A 1 177 ? 32.703 26.857  30.131 1.00 32.80  ?  177 ARG A O      1 
ATOM   1277 C CB     . ARG A 1 177 ? 30.338 24.975  29.965 1.00 30.03  ?  177 ARG A CB     1 
ATOM   1278 C CG     . ARG A 1 177 ? 29.587 25.935  29.064 1.00 32.64  ?  177 ARG A CG     1 
ATOM   1279 C CD     . ARG A 1 177 ? 28.107 25.939  29.364 1.00 36.61  ?  177 ARG A CD     1 
ATOM   1280 N NE     . ARG A 1 177 ? 27.474 27.155  28.879 1.00 40.37  ?  177 ARG A NE     1 
ATOM   1281 C CZ     . ARG A 1 177 ? 26.232 27.511  29.173 1.00 43.63  ?  177 ARG A CZ     1 
ATOM   1282 N NH1    . ARG A 1 177 ? 25.489 26.740  29.949 1.00 46.45  ?  177 ARG A NH1    1 
ATOM   1283 N NH2    . ARG A 1 177 ? 25.737 28.638  28.695 1.00 34.87  ?  177 ARG A NH2    1 
ATOM   1284 N N      . LEU A 1 178 ? 32.638 26.301  27.980 1.00 41.67  ?  178 LEU A N      1 
ATOM   1285 C CA     . LEU A 1 178 ? 33.205 27.533  27.515 1.00 38.50  ?  178 LEU A CA     1 
ATOM   1286 C C      . LEU A 1 178 ? 32.184 28.024  26.584 1.00 40.53  ?  178 LEU A C      1 
ATOM   1287 O O      . LEU A 1 178 ? 31.677 27.296  25.785 1.00 48.83  ?  178 LEU A O      1 
ATOM   1288 C CB     . LEU A 1 178 ? 34.496 27.258  26.758 1.00 34.30  ?  178 LEU A CB     1 
ATOM   1289 C CG     . LEU A 1 178 ? 35.097 28.341  25.868 1.00 41.23  ?  178 LEU A CG     1 
ATOM   1290 C CD1    . LEU A 1 178 ? 35.450 29.575  26.676 1.00 43.13  ?  178 LEU A CD1    1 
ATOM   1291 C CD2    . LEU A 1 178 ? 36.316 27.814  25.134 1.00 41.33  ?  178 LEU A CD2    1 
ATOM   1292 N N      . ASP A 1 179 ? 31.830 29.271  26.695 1.00 56.46  ?  179 ASP A N      1 
ATOM   1293 C CA     . ASP A 1 179 ? 30.903 29.811  25.750 1.00 62.95  ?  179 ASP A CA     1 
ATOM   1294 C C      . ASP A 1 179 ? 31.705 30.480  24.684 1.00 59.63  ?  179 ASP A C      1 
ATOM   1295 O O      . ASP A 1 179 ? 31.787 31.695  24.636 1.00 61.28  ?  179 ASP A O      1 
ATOM   1296 C CB     . ASP A 1 179 ? 29.926 30.786  26.413 1.00 66.97  ?  179 ASP A CB     1 
ATOM   1297 C CG     . ASP A 1 179 ? 29.550 30.377  27.818 1.00 65.39  ?  179 ASP A CG     1 
ATOM   1298 O OD1    . ASP A 1 179 ? 30.316 30.651  28.763 1.00 56.82  ?  179 ASP A OD1    1 
ATOM   1299 O OD2    . ASP A 1 179 ? 28.468 29.795  27.980 1.00 66.85  -1 179 ASP A OD2    1 
ATOM   1300 N N      . LEU A 1 180 ? 32.336 29.685  23.845 1.00 36.19  ?  180 LEU A N      1 
ATOM   1301 C CA     . LEU A 1 180 ? 33.072 30.223  22.739 1.00 35.42  ?  180 LEU A CA     1 
ATOM   1302 C C      . LEU A 1 180 ? 33.081 29.199  21.689 1.00 36.11  ?  180 LEU A C      1 
ATOM   1303 O O      . LEU A 1 180 ? 33.573 28.117  21.893 1.00 39.33  ?  180 LEU A O      1 
ATOM   1304 C CB     . LEU A 1 180 ? 34.522 30.498  23.076 1.00 39.32  ?  180 LEU A CB     1 
ATOM   1305 C CG     . LEU A 1 180 ? 35.523 30.579  21.926 1.00 40.09  ?  180 LEU A CG     1 
ATOM   1306 C CD1    . LEU A 1 180 ? 35.268 31.803  21.062 1.00 42.68  ?  180 LEU A CD1    1 
ATOM   1307 C CD2    . LEU A 1 180 ? 36.933 30.592  22.479 1.00 34.77  ?  180 LEU A CD2    1 
ATOM   1308 N N      . ALA A 1 181 ? 32.539 29.551  20.551 1.00 46.43  ?  181 ALA A N      1 
ATOM   1309 C CA     . ALA A 1 181 ? 32.446 28.613  19.493 1.00 49.02  ?  181 ALA A CA     1 
ATOM   1310 C C      . ALA A 1 181 ? 32.199 29.320  18.200 1.00 44.35  ?  181 ALA A C      1 
ATOM   1311 O O      . ALA A 1 181 ? 32.437 30.493  18.104 1.00 51.11  ?  181 ALA A O      1 
ATOM   1312 C CB     . ALA A 1 181 ? 31.230 27.809  19.805 1.00 52.51  ?  181 ALA A CB     1 
ATOM   1313 N N      . GLY A 1 182 ? 31.712 28.620  17.209 1.00 28.73  ?  182 GLY A N      1 
ATOM   1314 C CA     . GLY A 1 182 ? 31.528 29.197  15.901 1.00 39.85  ?  182 GLY A CA     1 
ATOM   1315 C C      . GLY A 1 182 ? 30.949 30.555  15.661 1.00 34.99  ?  182 GLY A C      1 
ATOM   1316 O O      . GLY A 1 182 ? 31.361 31.222  14.750 1.00 39.47  ?  182 GLY A O      1 
ATOM   1317 N N      . ARG A 1 183 ? 30.006 30.964  16.475 1.00 31.50  ?  183 ARG A N      1 
ATOM   1318 C CA     . ARG A 1 183 ? 29.388 32.238  16.347 1.00 29.52  ?  183 ARG A CA     1 
ATOM   1319 C C      . ARG A 1 183 ? 30.378 33.290  16.675 1.00 35.01  ?  183 ARG A C      1 
ATOM   1320 O O      . ARG A 1 183 ? 30.455 34.304  16.031 1.00 34.49  ?  183 ARG A O      1 
ATOM   1321 C CB     . ARG A 1 183 ? 28.213 32.295  17.308 1.00 30.56  ?  183 ARG A CB     1 
ATOM   1322 C CG     . ARG A 1 183 ? 26.887 32.697  16.711 1.00 39.35  ?  183 ARG A CG     1 
ATOM   1323 C CD     . ARG A 1 183 ? 25.822 31.645  16.961 1.00 46.77  ?  183 ARG A CD     1 
ATOM   1324 N NE     . ARG A 1 183 ? 25.511 31.457  18.371 1.00 50.42  ?  183 ARG A NE     1 
ATOM   1325 C CZ     . ARG A 1 183 ? 24.774 30.461  18.850 1.00 49.62  ?  183 ARG A CZ     1 
ATOM   1326 N NH1    . ARG A 1 183 ? 24.276 29.551  18.040 1.00 42.26  ?  183 ARG A NH1    1 
ATOM   1327 N NH2    . ARG A 1 183 ? 24.533 30.379  20.144 1.00 53.29  ?  183 ARG A NH2    1 
ATOM   1328 N N      . ASP A 1 184 ? 31.165 33.039  17.683 1.00 38.42  ?  184 ASP A N      1 
ATOM   1329 C CA     . ASP A 1 184 ? 32.137 34.000  18.105 1.00 36.82  ?  184 ASP A CA     1 
ATOM   1330 C C      . ASP A 1 184 ? 33.302 34.078  17.159 1.00 36.79  ?  184 ASP A C      1 
ATOM   1331 O O      . ASP A 1 184 ? 33.885 35.129  16.992 1.00 35.02  ?  184 ASP A O      1 
ATOM   1332 C CB     . ASP A 1 184 ? 32.605 33.645  19.501 1.00 39.32  ?  184 ASP A CB     1 
ATOM   1333 C CG     . ASP A 1 184 ? 31.460 33.431  20.468 1.00 45.63  ?  184 ASP A CG     1 
ATOM   1334 O OD1    . ASP A 1 184 ? 30.949 34.427  21.014 1.00 40.39  ?  184 ASP A OD1    1 
ATOM   1335 O OD2    . ASP A 1 184 ? 31.072 32.268  20.693 1.00 48.18  -1 184 ASP A OD2    1 
ATOM   1336 N N      . LEU A 1 185 ? 33.638 32.966  16.529 1.00 32.32  ?  185 LEU A N      1 
ATOM   1337 C CA     . LEU A 1 185 ? 34.728 32.929  15.592 1.00 31.44  ?  185 LEU A CA     1 
ATOM   1338 C C      . LEU A 1 185 ? 34.303 33.613  14.302 1.00 35.29  ?  185 LEU A C      1 
ATOM   1339 O O      . LEU A 1 185 ? 35.122 34.182  13.612 1.00 32.59  ?  185 LEU A O      1 
ATOM   1340 C CB     . LEU A 1 185 ? 35.170 31.479  15.403 1.00 30.47  ?  185 LEU A CB     1 
ATOM   1341 C CG     . LEU A 1 185 ? 35.767 30.722  16.584 1.00 27.64  ?  185 LEU A CG     1 
ATOM   1342 C CD1    . LEU A 1 185 ? 36.156 29.323  16.168 1.00 30.22  ?  185 LEU A CD1    1 
ATOM   1343 C CD2    . LEU A 1 185 ? 36.962 31.439  17.171 1.00 25.21  ?  185 LEU A CD2    1 
ATOM   1344 N N      . THR A 1 186 ? 33.016 33.581  13.993 1.00 38.61  ?  186 THR A N      1 
ATOM   1345 C CA     . THR A 1 186 ? 32.499 34.266  12.835 1.00 34.48  ?  186 THR A CA     1 
ATOM   1346 C C      . THR A 1 186 ? 32.432 35.739  13.095 1.00 36.47  ?  186 THR A C      1 
ATOM   1347 O O      . THR A 1 186 ? 32.735 36.496  12.214 1.00 40.77  ?  186 THR A O      1 
ATOM   1348 C CB     . THR A 1 186 ? 31.115 33.735  12.433 1.00 37.50  ?  186 THR A CB     1 
ATOM   1349 O OG1    . THR A 1 186 ? 31.230 32.888  11.297 1.00 36.28  ?  186 THR A OG1    1 
ATOM   1350 C CG2    . THR A 1 186 ? 30.197 34.867  12.042 1.00 39.74  ?  186 THR A CG2    1 
ATOM   1351 N N      . ASP A 1 187 ? 32.097 36.160  14.312 1.00 38.79  ?  187 ASP A N      1 
ATOM   1352 C CA     . ASP A 1 187 ? 32.128 37.590  14.596 1.00 38.38  ?  187 ASP A CA     1 
ATOM   1353 C C      . ASP A 1 187 ? 33.547 38.120  14.558 1.00 43.27  ?  187 ASP A C      1 
ATOM   1354 O O      . ASP A 1 187 ? 33.810 39.185  13.978 1.00 49.50  ?  187 ASP A O      1 
ATOM   1355 C CB     . ASP A 1 187 ? 31.519 37.881  15.964 1.00 50.51  ?  187 ASP A CB     1 
ATOM   1356 C CG     . ASP A 1 187 ? 30.018 38.065  15.914 1.00 59.85  ?  187 ASP A CG     1 
ATOM   1357 O OD1    . ASP A 1 187 ? 29.388 37.560  14.956 1.00 63.55  ?  187 ASP A OD1    1 
ATOM   1358 O OD2    . ASP A 1 187 ? 29.477 38.713  16.840 1.00 60.66  -1 187 ASP A OD2    1 
ATOM   1359 N N      . TYR A 1 188 ? 34.475 37.390  15.179 1.00 30.37  ?  188 TYR A N      1 
ATOM   1360 C CA     . TYR A 1 188 ? 35.858 37.844  15.218 1.00 29.83  ?  188 TYR A CA     1 
ATOM   1361 C C      . TYR A 1 188 ? 36.447 37.944  13.815 1.00 33.03  ?  188 TYR A C      1 
ATOM   1362 O O      . TYR A 1 188 ? 37.216 38.871  13.528 1.00 34.08  ?  188 TYR A O      1 
ATOM   1363 C CB     . TYR A 1 188 ? 36.686 36.910  16.086 1.00 21.36  ?  188 TYR A CB     1 
ATOM   1364 C CG     . TYR A 1 188 ? 38.111 37.365  16.260 1.00 26.38  ?  188 TYR A CG     1 
ATOM   1365 C CD1    . TYR A 1 188 ? 38.401 38.611  16.823 1.00 23.97  ?  188 TYR A CD1    1 
ATOM   1366 C CD2    . TYR A 1 188 ? 39.182 36.534  15.884 1.00 30.00  ?  188 TYR A CD2    1 
ATOM   1367 C CE1    . TYR A 1 188 ? 39.719 39.018  17.000 1.00 30.91  ?  188 TYR A CE1    1 
ATOM   1368 C CE2    . TYR A 1 188 ? 40.502 36.932  16.059 1.00 32.98  ?  188 TYR A CE2    1 
ATOM   1369 C CZ     . TYR A 1 188 ? 40.766 38.176  16.606 1.00 34.18  ?  188 TYR A CZ     1 
ATOM   1370 O OH     . TYR A 1 188 ? 42.075 38.572  16.776 1.00 36.81  ?  188 TYR A OH     1 
ATOM   1371 N N      . LEU A 1 189 ? 36.095 37.003  12.925 1.00 25.02  ?  189 LEU A N      1 
ATOM   1372 C CA     . LEU A 1 189 ? 36.573 37.074  11.552 1.00 22.70  ?  189 LEU A CA     1 
ATOM   1373 C C      . LEU A 1 189 ? 36.037 38.319  10.875 1.00 31.78  ?  189 LEU A C      1 
ATOM   1374 O O      . LEU A 1 189 ? 36.786 39.061  10.234 1.00 37.18  ?  189 LEU A O      1 
ATOM   1375 C CB     . LEU A 1 189 ? 36.167 35.823  10.791 1.00 21.03  ?  189 LEU A CB     1 
ATOM   1376 C CG     . LEU A 1 189 ? 36.801 35.700  9.407  1.00 21.05  ?  189 LEU A CG     1 
ATOM   1377 C CD1    . LEU A 1 189 ? 38.330 35.729  9.462  1.00 21.06  ?  189 LEU A CD1    1 
ATOM   1378 C CD2    . LEU A 1 189 ? 36.313 34.409  8.808  1.00 20.79  ?  189 LEU A CD2    1 
ATOM   1379 N N      . MET A 1 190 ? 34.740 38.589  11.053 1.00 47.58  ?  190 MET A N      1 
ATOM   1380 C CA     . MET A 1 190 ? 34.171 39.868  10.656 1.00 45.79  ?  190 MET A CA     1 
ATOM   1381 C C      . MET A 1 190 ? 35.047 41.020  11.119 1.00 46.20  ?  190 MET A C      1 
ATOM   1382 O O      . MET A 1 190 ? 35.383 41.915  10.338 1.00 43.05  ?  190 MET A O      1 
ATOM   1383 C CB     . MET A 1 190 ? 32.774 40.022  11.251 1.00 45.87  ?  190 MET A CB     1 
ATOM   1384 C CG     . MET A 1 190 ? 31.769 38.972  10.842 1.00 43.15  ?  190 MET A CG     1 
ATOM   1385 S SD     . MET A 1 190 ? 30.113 39.513  11.321 1.00 49.96  ?  190 MET A SD     1 
ATOM   1386 C CE     . MET A 1 190 ? 30.454 41.158  11.960 1.00 50.77  ?  190 MET A CE     1 
ATOM   1387 N N      . LYS A 1 191 ? 35.381 41.084  12.382 1.00 46.00  ?  191 LYS A N      1 
ATOM   1388 C CA     . LYS A 1 191 ? 36.233 42.160  12.810 1.00 47.05  ?  191 LYS A CA     1 
ATOM   1389 C C      . LYS A 1 191 ? 37.621 42.179  12.150 1.00 47.13  ?  191 LYS A C      1 
ATOM   1390 O O      . LYS A 1 191 ? 38.069 43.229  11.744 1.00 49.75  ?  191 LYS A O      1 
ATOM   1391 C CB     . LYS A 1 191 ? 36.312 42.231  14.335 1.00 42.55  ?  191 LYS A CB     1 
ATOM   1392 C CG     . LYS A 1 191 ? 36.606 43.607  14.893 1.00 42.72  ?  191 LYS A CG     1 
ATOM   1393 C CD     . LYS A 1 191 ? 37.876 43.626  15.723 1.00 47.50  ?  191 LYS A CD     1 
ATOM   1394 C CE     . LYS A 1 191 ? 37.764 42.747  16.954 1.00 48.43  ?  191 LYS A CE     1 
ATOM   1395 N NZ     . LYS A 1 191 ? 38.991 42.806  17.790 1.00 50.95  ?  191 LYS A NZ     1 
ATOM   1396 N N      . ILE A 1 192 ? 38.295 41.035  12.050 1.00 39.52  ?  192 ILE A N      1 
ATOM   1397 C CA     . ILE A 1 192 ? 39.642 41.008  11.467 1.00 34.76  ?  192 ILE A CA     1 
ATOM   1398 C C      . ILE A 1 192 ? 39.631 41.576  10.053 1.00 39.91  ?  192 ILE A C      1 
ATOM   1399 O O      . ILE A 1 192 ? 40.544 42.320  9.649  1.00 39.52  ?  192 ILE A O      1 
ATOM   1400 C CB     . ILE A 1 192 ? 40.213 39.579  11.446 1.00 34.18  ?  192 ILE A CB     1 
ATOM   1401 C CG1    . ILE A 1 192 ? 39.880 38.795  12.685 1.00 39.94  ?  192 ILE A CG1    1 
ATOM   1402 C CG2    . ILE A 1 192 ? 41.700 39.610  11.388 1.00 36.15  ?  192 ILE A CG2    1 
ATOM   1403 C CD1    . ILE A 1 192 ? 40.387 37.385  12.563 1.00 42.23  ?  192 ILE A CD1    1 
ATOM   1404 N N      . LEU A 1 193 ? 38.613 41.200  9.270  1.00 27.73  ?  193 LEU A N      1 
ATOM   1405 C CA     . LEU A 1 193 ? 38.520 41.549  7.859  1.00 30.80  ?  193 LEU A CA     1 
ATOM   1406 C C      . LEU A 1 193 ? 38.103 42.987  7.619  1.00 34.18  ?  193 LEU A C      1 
ATOM   1407 O O      . LEU A 1 193 ? 38.369 43.510  6.523  1.00 31.95  ?  193 LEU A O      1 
ATOM   1408 C CB     . LEU A 1 193 ? 37.520 40.645  7.154  1.00 24.49  ?  193 LEU A CB     1 
ATOM   1409 C CG     . LEU A 1 193 ? 37.914 39.199  7.107  1.00 22.16  ?  193 LEU A CG     1 
ATOM   1410 C CD1    . LEU A 1 193 ? 36.866 38.504  6.260  1.00 33.58  ?  193 LEU A CD1    1 
ATOM   1411 C CD2    . LEU A 1 193 ? 39.317 39.077  6.528  1.00 22.17  ?  193 LEU A CD2    1 
ATOM   1412 N N      . THR A 1 194 ? 37.406 43.606  8.588  1.00 32.28  ?  194 THR A N      1 
ATOM   1413 C CA     . THR A 1 194 ? 37.069 45.023  8.517  1.00 35.92  ?  194 THR A CA     1 
ATOM   1414 C C      . THR A 1 194 ? 38.216 45.908  8.978  1.00 41.49  ?  194 THR A C      1 
ATOM   1415 O O      . THR A 1 194 ? 38.215 47.112  8.690  1.00 41.23  ?  194 THR A O      1 
ATOM   1416 C CB     . THR A 1 194 ? 35.826 45.307  9.345  1.00 33.38  ?  194 THR A CB     1 
ATOM   1417 O OG1    . THR A 1 194 ? 34.845 44.307  9.070  1.00 27.50  ?  194 THR A OG1    1 
ATOM   1418 C CG2    . THR A 1 194 ? 35.270 46.690  9.004  1.00 36.82  ?  194 THR A CG2    1 
ATOM   1419 N N      . GLU A 1 195 ? 39.172 45.330  9.708  1.00 53.13  ?  195 GLU A N      1 
ATOM   1420 C CA     . GLU A 1 195 ? 40.437 45.999  9.969  1.00 46.90  ?  195 GLU A CA     1 
ATOM   1421 C C      . GLU A 1 195 ? 41.313 46.037  8.731  1.00 40.42  ?  195 GLU A C      1 
ATOM   1422 O O      . GLU A 1 195 ? 42.104 46.966  8.588  1.00 44.18  ?  195 GLU A O      1 
ATOM   1423 C CB     . GLU A 1 195 ? 41.180 45.294  11.104 1.00 51.87  ?  195 GLU A CB     1 
ATOM   1424 C CG     . GLU A 1 195 ? 40.626 45.527  12.501 1.00 57.53  ?  195 GLU A CG     1 
ATOM   1425 C CD     . GLU A 1 195 ? 41.218 44.547  13.520 1.00 65.40  ?  195 GLU A CD     1 
ATOM   1426 O OE1    . GLU A 1 195 ? 42.125 43.754  13.128 1.00 61.52  ?  195 GLU A OE1    1 
ATOM   1427 O OE2    . GLU A 1 195 ? 40.777 44.575  14.700 1.00 64.26  -1 195 GLU A OE2    1 
ATOM   1428 N N      . ARG A 1 196 ? 41.143 45.104  7.807  1.00 46.25  ?  196 ARG A N      1 
ATOM   1429 C CA     . ARG A 1 196 ? 41.930 45.036  6.560  1.00 49.13  ?  196 ARG A CA     1 
ATOM   1430 C C      . ARG A 1 196 ? 41.301 45.854  5.452  1.00 57.52  ?  196 ARG A C      1 
ATOM   1431 O O      . ARG A 1 196 ? 41.848 45.975  4.364  1.00 62.86  ?  196 ARG A O      1 
ATOM   1432 C CB     . ARG A 1 196 ? 42.152 43.587  6.097  1.00 44.37  ?  196 ARG A CB     1 
ATOM   1433 C CG     . ARG A 1 196 ? 43.200 43.383  5.012  1.00 43.96  ?  196 ARG A CG     1 
ATOM   1434 C CD     . ARG A 1 196 ? 44.280 42.403  5.426  1.00 52.90  ?  196 ARG A CD     1 
ATOM   1435 N NE     . ARG A 1 196 ? 45.021 42.851  6.602  1.00 55.90  ?  196 ARG A NE     1 
ATOM   1436 C CZ     . ARG A 1 196 ? 45.924 42.123  7.245  1.00 53.66  ?  196 ARG A CZ     1 
ATOM   1437 N NH1    . ARG A 1 196 ? 46.205 40.897  6.843  1.00 48.43  ?  196 ARG A NH1    1 
ATOM   1438 N NH2    . ARG A 1 196 ? 46.537 42.619  8.302  1.00 56.34  ?  196 ARG A NH2    1 
ATOM   1439 N N      . GLY A 1 197 ? 40.153 46.441  5.722  1.00 49.11  ?  197 GLY A N      1 
ATOM   1440 C CA     . GLY A 1 197 ? 39.505 47.294  4.760  1.00 44.42  ?  197 GLY A CA     1 
ATOM   1441 C C      . GLY A 1 197 ? 38.255 46.720  4.131  1.00 45.30  ?  197 GLY A C      1 
ATOM   1442 O O      . GLY A 1 197 ? 37.430 47.491  3.636  1.00 52.53  ?  197 GLY A O      1 
ATOM   1443 N N      . TYR A 1 198 ? 38.080 45.401  4.127  1.00 48.74  ?  198 TYR A N      1 
ATOM   1444 C CA     . TYR A 1 198 ? 36.808 44.867  3.654  1.00 53.06  ?  198 TYR A CA     1 
ATOM   1445 C C      . TYR A 1 198 ? 35.720 45.212  4.672  1.00 55.38  ?  198 TYR A C      1 
ATOM   1446 O O      . TYR A 1 198 ? 35.992 45.440  5.852  1.00 60.38  ?  198 TYR A O      1 
ATOM   1447 C CB     . TYR A 1 198 ? 36.921 43.354  3.393  1.00 51.57  ?  198 TYR A CB     1 
ATOM   1448 C CG     . TYR A 1 198 ? 38.125 43.038  2.522  1.00 49.68  ?  198 TYR A CG     1 
ATOM   1449 C CD1    . TYR A 1 198 ? 38.193 43.495  1.211  1.00 49.51  ?  198 TYR A CD1    1 
ATOM   1450 C CD2    . TYR A 1 198 ? 39.216 42.326  3.022  1.00 53.60  ?  198 TYR A CD2    1 
ATOM   1451 C CE1    . TYR A 1 198 ? 39.311 43.260  0.419  1.00 50.31  ?  198 TYR A CE1    1 
ATOM   1452 C CE2    . TYR A 1 198 ? 40.342 42.071  2.229  1.00 48.56  ?  198 TYR A CE2    1 
ATOM   1453 C CZ     . TYR A 1 198 ? 40.375 42.550  0.931  1.00 50.02  ?  198 TYR A CZ     1 
ATOM   1454 O OH     . TYR A 1 198 ? 41.467 42.333  0.129  1.00 48.88  ?  198 TYR A OH     1 
ATOM   1455 N N      . SER A 1 199 ? 34.491 45.329  4.208  1.00 46.00  ?  199 SER A N      1 
ATOM   1456 C CA     . SER A 1 199 ? 33.408 45.784  5.072  1.00 46.63  ?  199 SER A CA     1 
ATOM   1457 C C      . SER A 1 199 ? 32.405 44.658  5.290  1.00 49.28  ?  199 SER A C      1 
ATOM   1458 O O      . SER A 1 199 ? 31.624 44.332  4.385  1.00 40.88  ?  199 SER A O      1 
ATOM   1459 C CB     . SER A 1 199 ? 32.704 46.999  4.485  1.00 50.50  ?  199 SER A CB     1 
ATOM   1460 O OG     . SER A 1 199 ? 31.348 46.986  4.915  1.00 58.17  ?  199 SER A OG     1 
ATOM   1461 N N      . PHE A 1 200 ? 32.400 44.112  6.514  1.00 55.41  ?  200 PHE A N      1 
ATOM   1462 C CA     . PHE A 1 200 ? 31.435 43.108  6.955  1.00 50.24  ?  200 PHE A CA     1 
ATOM   1463 C C      . PHE A 1 200 ? 30.780 43.599  8.242  1.00 50.23  ?  200 PHE A C      1 
ATOM   1464 O O      . PHE A 1 200 ? 31.433 43.647  9.291  1.00 56.32  ?  200 PHE A O      1 
ATOM   1465 C CB     . PHE A 1 200 ? 32.113 41.762  7.202  1.00 49.43  ?  200 PHE A CB     1 
ATOM   1466 C CG     . PHE A 1 200 ? 32.797 41.183  6.010  1.00 48.21  ?  200 PHE A CG     1 
ATOM   1467 C CD1    . PHE A 1 200 ? 32.070 40.505  5.034  1.00 49.92  ?  200 PHE A CD1    1 
ATOM   1468 C CD2    . PHE A 1 200 ? 34.178 41.272  5.881  1.00 51.74  ?  200 PHE A CD2    1 
ATOM   1469 C CE1    . PHE A 1 200 ? 32.698 39.941  3.931  1.00 50.87  ?  200 PHE A CE1    1 
ATOM   1470 C CE2    . PHE A 1 200 ? 34.817 40.719  4.783  1.00 57.07  ?  200 PHE A CE2    1 
ATOM   1471 C CZ     . PHE A 1 200 ? 34.073 40.052  3.798  1.00 54.56  ?  200 PHE A CZ     1 
ATOM   1472 N N      . THR A 1 201 ? 29.497 43.955  8.164  1.00 38.89  ?  201 THR A N      1 
ATOM   1473 C CA     . THR A 1 201 ? 28.707 44.404  9.316  1.00 42.32  ?  201 THR A CA     1 
ATOM   1474 C C      . THR A 1 201 ? 27.321 43.758  9.359  1.00 41.59  ?  201 THR A C      1 
ATOM   1475 O O      . THR A 1 201 ? 26.904 43.229  10.393 1.00 37.79  ?  201 THR A O      1 
ATOM   1476 C CB     . THR A 1 201 ? 28.571 45.919  9.332  1.00 48.17  ?  201 THR A CB     1 
ATOM   1477 O OG1    . THR A 1 201 ? 29.844 46.509  9.041  1.00 53.35  ?  201 THR A OG1    1 
ATOM   1478 C CG2    . THR A 1 201 ? 28.105 46.368  10.713 1.00 47.76  ?  201 THR A CG2    1 
ATOM   1479 N N      . THR A 1 202 ? 26.584 43.907  8.249  1.00 53.20  ?  202 THR A N      1 
ATOM   1480 C CA     . THR A 1 202 ? 25.221 43.409  8.068  1.00 51.33  ?  202 THR A CA     1 
ATOM   1481 C C      . THR A 1 202 ? 25.151 41.888  8.228  1.00 51.10  ?  202 THR A C      1 
ATOM   1482 O O      . THR A 1 202 ? 26.149 41.175  8.086  1.00 54.60  ?  202 THR A O      1 
ATOM   1483 C CB     . THR A 1 202 ? 24.701 43.821  6.668  1.00 55.51  ?  202 THR A CB     1 
ATOM   1484 O OG1    . THR A 1 202 ? 25.352 43.065  5.628  1.00 56.00  ?  202 THR A OG1    1 
ATOM   1485 C CG2    . THR A 1 202 ? 24.923 45.328  6.402  1.00 52.15  ?  202 THR A CG2    1 
ATOM   1486 N N      . THR A 1 203 ? 23.952 41.389  8.560  1.00 47.50  ?  203 THR A N      1 
ATOM   1487 C CA     . THR A 1 203 ? 23.807 39.965  8.853  1.00 46.03  ?  203 THR A CA     1 
ATOM   1488 C C      . THR A 1 203 ? 24.053 39.115  7.611  1.00 55.73  ?  203 THR A C      1 
ATOM   1489 O O      . THR A 1 203 ? 24.604 38.011  7.709  1.00 61.78  ?  203 THR A O      1 
ATOM   1490 C CB     . THR A 1 203 ? 22.427 39.669  9.446  1.00 46.32  ?  203 THR A CB     1 
ATOM   1491 O OG1    . THR A 1 203 ? 21.408 40.179  8.576  1.00 50.86  ?  203 THR A OG1    1 
ATOM   1492 C CG2    . THR A 1 203 ? 22.289 40.308  10.826 1.00 44.07  ?  203 THR A CG2    1 
ATOM   1493 N N      . ALA A 1 204 ? 23.652 39.601  6.432  1.00 41.57  ?  204 ALA A N      1 
ATOM   1494 C CA     . ALA A 1 204 ? 24.108 38.954  5.205  1.00 35.65  ?  204 ALA A CA     1 
ATOM   1495 C C      . ALA A 1 204 ? 25.634 38.928  5.159  1.00 34.34  ?  204 ALA A C      1 
ATOM   1496 O O      . ALA A 1 204 ? 26.234 37.896  4.838  1.00 30.75  ?  204 ALA A O      1 
ATOM   1497 C CB     . ALA A 1 204 ? 23.527 39.664  3.970  1.00 25.61  ?  204 ALA A CB     1 
ATOM   1498 N N      . GLU A 1 205 ? 26.279 40.055  5.498  1.00 53.39  ?  205 GLU A N      1 
ATOM   1499 C CA     . GLU A 1 205 ? 27.740 40.104  5.546  1.00 55.11  ?  205 GLU A CA     1 
ATOM   1500 C C      . GLU A 1 205 ? 28.289 39.182  6.627  1.00 57.34  ?  205 GLU A C      1 
ATOM   1501 O O      . GLU A 1 205 ? 29.383 38.631  6.468  1.00 64.07  ?  205 GLU A O      1 
ATOM   1502 C CB     . GLU A 1 205 ? 28.226 41.550  5.747  1.00 53.08  ?  205 GLU A CB     1 
ATOM   1503 C CG     . GLU A 1 205 ? 27.914 42.444  4.525  1.00 59.77  ?  205 GLU A CG     1 
ATOM   1504 C CD     . GLU A 1 205 ? 28.430 43.883  4.620  1.00 64.64  ?  205 GLU A CD     1 
ATOM   1505 O OE1    . GLU A 1 205 ? 28.384 44.483  5.716  1.00 64.55  ?  205 GLU A OE1    1 
ATOM   1506 O OE2    . GLU A 1 205 ? 28.877 44.421  3.574  1.00 69.75  -1 205 GLU A OE2    1 
ATOM   1507 N N      . ARG A 1 206 ? 27.547 38.990  7.721  1.00 49.83  ?  206 ARG A N      1 
ATOM   1508 C CA     . ARG A 1 206 ? 27.835 37.885  8.635  1.00 47.03  ?  206 ARG A CA     1 
ATOM   1509 C C      . ARG A 1 206 ? 27.768 36.538  7.909  1.00 42.26  ?  206 ARG A C      1 
ATOM   1510 O O      . ARG A 1 206 ? 28.688 35.718  8.004  1.00 39.00  ?  206 ARG A O      1 
ATOM   1511 C CB     . ARG A 1 206 ? 26.856 37.918  9.816  1.00 46.43  ?  206 ARG A CB     1 
ATOM   1512 C CG     . ARG A 1 206 ? 27.196 36.985  10.967 1.00 43.95  ?  206 ARG A CG     1 
ATOM   1513 C CD     . ARG A 1 206 ? 26.415 37.321  12.250 1.00 48.65  ?  206 ARG A CD     1 
ATOM   1514 N NE     . ARG A 1 206 ? 27.078 36.803  13.457 1.00 54.92  ?  206 ARG A NE     1 
ATOM   1515 C CZ     . ARG A 1 206 ? 27.339 35.510  13.705 1.00 53.79  ?  206 ARG A CZ     1 
ATOM   1516 N NH1    . ARG A 1 206 ? 27.003 34.574  12.829 1.00 50.81  ?  206 ARG A NH1    1 
ATOM   1517 N NH2    . ARG A 1 206 ? 27.941 35.142  14.836 1.00 51.86  ?  206 ARG A NH2    1 
ATOM   1518 N N      . GLU A 1 207 ? 26.690 36.308  7.154  1.00 40.90  ?  207 GLU A N      1 
ATOM   1519 C CA     . GLU A 1 207 ? 26.485 35.024  6.483  1.00 40.90  ?  207 GLU A CA     1 
ATOM   1520 C C      . GLU A 1 207 ? 27.596 34.698  5.491  1.00 34.29  ?  207 GLU A C      1 
ATOM   1521 O O      . GLU A 1 207 ? 27.950 33.529  5.324  1.00 34.42  ?  207 GLU A O      1 
ATOM   1522 C CB     . GLU A 1 207 ? 25.123 35.011  5.776  1.00 46.70  ?  207 GLU A CB     1 
ATOM   1523 C CG     . GLU A 1 207 ? 23.945 34.877  6.728  1.00 51.82  ?  207 GLU A CG     1 
ATOM   1524 C CD     . GLU A 1 207 ? 23.983 33.587  7.569  1.00 59.76  ?  207 GLU A CD     1 
ATOM   1525 O OE1    . GLU A 1 207 ? 25.054 33.209  8.114  1.00 56.01  ?  207 GLU A OE1    1 
ATOM   1526 O OE2    . GLU A 1 207 ? 22.918 32.942  7.684  1.00 67.36  -1 207 GLU A OE2    1 
ATOM   1527 N N      . ILE A 1 208 ? 28.126 35.705  4.792  1.00 29.54  ?  208 ILE A N      1 
ATOM   1528 C CA     . ILE A 1 208 ? 29.240 35.476  3.875  1.00 30.23  ?  208 ILE A CA     1 
ATOM   1529 C C      . ILE A 1 208 ? 30.504 35.124  4.648  1.00 26.16  ?  208 ILE A C      1 
ATOM   1530 O O      . ILE A 1 208 ? 31.274 34.242  4.242  1.00 23.87  ?  208 ILE A O      1 
ATOM   1531 C CB     . ILE A 1 208 ? 29.477 36.720  3.004  1.00 37.10  ?  208 ILE A CB     1 
ATOM   1532 C CG1    . ILE A 1 208 ? 28.300 36.994  2.081  1.00 35.04  ?  208 ILE A CG1    1 
ATOM   1533 C CG2    . ILE A 1 208 ? 30.806 36.612  2.265  1.00 41.51  ?  208 ILE A CG2    1 
ATOM   1534 C CD1    . ILE A 1 208 ? 28.060 38.476  1.887  1.00 33.48  ?  208 ILE A CD1    1 
ATOM   1535 N N      . VAL A 1 209 ? 30.782 35.887  5.714  1.00 32.15  ?  209 VAL A N      1 
ATOM   1536 C CA     . VAL A 1 209 ? 31.967 35.670  6.547  1.00 38.39  ?  209 VAL A CA     1 
ATOM   1537 C C      . VAL A 1 209 ? 31.987 34.245  7.075  1.00 38.60  ?  209 VAL A C      1 
ATOM   1538 O O      . VAL A 1 209 ? 33.050 33.617  7.165  1.00 37.71  ?  209 VAL A O      1 
ATOM   1539 C CB     . VAL A 1 209 ? 32.031 36.696  7.706  1.00 34.16  ?  209 VAL A CB     1 
ATOM   1540 C CG1    . VAL A 1 209 ? 33.135 36.328  8.686  1.00 24.18  ?  209 VAL A CG1    1 
ATOM   1541 C CG2    . VAL A 1 209 ? 32.286 38.107  7.177  1.00 33.75  ?  209 VAL A CG2    1 
ATOM   1542 N N      . ARG A 1 210 ? 30.813 33.713  7.439  1.00 40.00  ?  210 ARG A N      1 
ATOM   1543 C CA     . ARG A 1 210 ? 30.730 32.342  7.930  1.00 41.96  ?  210 ARG A CA     1 
ATOM   1544 C C      . ARG A 1 210 ? 31.045 31.319  6.841  1.00 40.67  ?  210 ARG A C      1 
ATOM   1545 O O      . ARG A 1 210 ? 31.439 30.186  7.162  1.00 39.15  ?  210 ARG A O      1 
ATOM   1546 C CB     . ARG A 1 210 ? 29.349 32.076  8.540  1.00 47.61  ?  210 ARG A CB     1 
ATOM   1547 C CG     . ARG A 1 210 ? 29.222 30.683  9.144  1.00 55.82  ?  210 ARG A CG     1 
ATOM   1548 C CD     . ARG A 1 210 ? 28.237 30.608  10.321 1.00 63.37  ?  210 ARG A CD     1 
ATOM   1549 N NE     . ARG A 1 210 ? 28.569 31.507  11.433 1.00 62.77  ?  210 ARG A NE     1 
ATOM   1550 C CZ     . ARG A 1 210 ? 28.085 31.396  12.671 1.00 56.78  ?  210 ARG A CZ     1 
ATOM   1551 N NH1    . ARG A 1 210 ? 27.255 30.411  12.991 1.00 55.69  ?  210 ARG A NH1    1 
ATOM   1552 N NH2    . ARG A 1 210 ? 28.438 32.274  13.598 1.00 56.32  ?  210 ARG A NH2    1 
ATOM   1553 N N      . ASP A 1 211 ? 30.887 31.698  5.570  1.00 36.35  ?  211 ASP A N      1 
ATOM   1554 C CA     . ASP A 1 211 ? 31.387 30.883  4.468  1.00 40.66  ?  211 ASP A CA     1 
ATOM   1555 C C      . ASP A 1 211 ? 32.914 30.882  4.438  1.00 38.47  ?  211 ASP A C      1 
ATOM   1556 O O      . ASP A 1 211 ? 33.539 29.831  4.266  1.00 40.04  ?  211 ASP A O      1 
ATOM   1557 C CB     . ASP A 1 211 ? 30.817 31.406  3.138  1.00 44.71  ?  211 ASP A CB     1 
ATOM   1558 C CG     . ASP A 1 211 ? 31.111 30.478  1.960  1.00 48.73  ?  211 ASP A CG     1 
ATOM   1559 O OD1    . ASP A 1 211 ? 30.915 29.255  2.124  1.00 46.19  ?  211 ASP A OD1    1 
ATOM   1560 O OD2    . ASP A 1 211 ? 31.523 30.966  0.875  1.00 50.41  -1 211 ASP A OD2    1 
ATOM   1561 N N      . ILE A 1 212 ? 33.527 32.057  4.599  1.00 32.81  ?  212 ILE A N      1 
ATOM   1562 C CA     . ILE A 1 212 ? 34.981 32.160  4.542  1.00 27.58  ?  212 ILE A CA     1 
ATOM   1563 C C      . ILE A 1 212 ? 35.611 31.362  5.677  1.00 29.16  ?  212 ILE A C      1 
ATOM   1564 O O      . ILE A 1 212 ? 36.688 30.775  5.523  1.00 30.04  ?  212 ILE A O      1 
ATOM   1565 C CB     . ILE A 1 212 ? 35.412 33.640  4.584  1.00 23.73  ?  212 ILE A CB     1 
ATOM   1566 C CG1    . ILE A 1 212 ? 34.508 34.495  3.721  1.00 22.66  ?  212 ILE A CG1    1 
ATOM   1567 C CG2    . ILE A 1 212 ? 36.797 33.802  4.093  1.00 26.06  ?  212 ILE A CG2    1 
ATOM   1568 C CD1    . ILE A 1 212 ? 34.893 35.915  3.765  1.00 27.20  ?  212 ILE A CD1    1 
ATOM   1569 N N      . LYS A 1 213 ? 34.957 31.341  6.839  1.00 33.99  ?  213 LYS A N      1 
ATOM   1570 C CA     . LYS A 1 213 ? 35.446 30.540  7.961  1.00 37.77  ?  213 LYS A CA     1 
ATOM   1571 C C      . LYS A 1 213 ? 35.478 29.050  7.616  1.00 36.22  ?  213 LYS A C      1 
ATOM   1572 O O      . LYS A 1 213 ? 36.501 28.383  7.776  1.00 40.10  ?  213 LYS A O      1 
ATOM   1573 C CB     . LYS A 1 213 ? 34.575 30.799  9.195  1.00 34.09  ?  213 LYS A CB     1 
ATOM   1574 C CG     . LYS A 1 213 ? 35.032 30.111  10.468 1.00 30.29  ?  213 LYS A CG     1 
ATOM   1575 C CD     . LYS A 1 213 ? 34.315 30.694  11.697 1.00 39.26  ?  213 LYS A CD     1 
ATOM   1576 C CE     . LYS A 1 213 ? 32.796 30.478  11.626 1.00 40.33  ?  213 LYS A CE     1 
ATOM   1577 N NZ     . LYS A 1 213 ? 32.373 29.065  11.648 1.00 35.96  ?  213 LYS A NZ     1 
ATOM   1578 N N      . GLU A 1 214 ? 34.367 28.505  7.143  1.00 46.30  ?  214 GLU A N      1 
ATOM   1579 C CA     . GLU A 1 214 ? 34.300 27.064  6.969  1.00 44.00  ?  214 GLU A CA     1 
ATOM   1580 C C      . GLU A 1 214 ? 35.171 26.589  5.812  1.00 38.96  ?  214 GLU A C      1 
ATOM   1581 O O      . GLU A 1 214 ? 35.508 25.405  5.762  1.00 41.77  ?  214 GLU A O      1 
ATOM   1582 C CB     . GLU A 1 214 ? 32.832 26.647  6.806  1.00 44.50  ?  214 GLU A CB     1 
ATOM   1583 C CG     . GLU A 1 214 ? 31.954 27.070  8.015  1.00 42.20  ?  214 GLU A CG     1 
ATOM   1584 C CD     . GLU A 1 214 ? 30.468 26.884  7.769  1.00 50.25  ?  214 GLU A CD     1 
ATOM   1585 O OE1    . GLU A 1 214 ? 30.114 26.146  6.835  1.00 54.13  ?  214 GLU A OE1    1 
ATOM   1586 O OE2    . GLU A 1 214 ? 29.637 27.463  8.504  1.00 53.93  -1 214 GLU A OE2    1 
ATOM   1587 N N      . LYS A 1 215 ? 35.586 27.485  4.911  1.00 34.64  ?  215 LYS A N      1 
ATOM   1588 C CA     . LYS A 1 215 ? 36.514 27.130  3.820  1.00 36.85  ?  215 LYS A CA     1 
ATOM   1589 C C      . LYS A 1 215 ? 37.957 27.446  4.201  1.00 40.19  ?  215 LYS A C      1 
ATOM   1590 O O      . LYS A 1 215 ? 38.763 26.547  4.448  1.00 50.36  ?  215 LYS A O      1 
ATOM   1591 C CB     . LYS A 1 215 ? 36.138 27.869  2.527  1.00 32.17  ?  215 LYS A CB     1 
ATOM   1592 C CG     . LYS A 1 215 ? 35.090 27.220  1.609  1.00 33.00  ?  215 LYS A CG     1 
ATOM   1593 C CD     . LYS A 1 215 ? 33.646 27.352  2.101  1.00 34.08  ?  215 LYS A CD     1 
ATOM   1594 C CE     . LYS A 1 215 ? 32.656 27.207  0.956  1.00 37.17  ?  215 LYS A CE     1 
ATOM   1595 N NZ     . LYS A 1 215 ? 32.753 28.354  -0.032 1.00 46.09  ?  215 LYS A NZ     1 
ATOM   1596 N N      . LEU A 1 216 ? 38.276 28.731  4.284  1.00 39.32  ?  216 LEU A N      1 
ATOM   1597 C CA     . LEU A 1 216 ? 39.649 29.215  4.207  1.00 38.53  ?  216 LEU A CA     1 
ATOM   1598 C C      . LEU A 1 216 ? 40.416 29.132  5.523  1.00 35.12  ?  216 LEU A C      1 
ATOM   1599 O O      . LEU A 1 216 ? 41.649 29.000  5.503  1.00 32.84  ?  216 LEU A O      1 
ATOM   1600 C CB     . LEU A 1 216 ? 39.634 30.651  3.678  1.00 32.92  ?  216 LEU A CB     1 
ATOM   1601 C CG     . LEU A 1 216 ? 39.112 30.578  2.249  1.00 29.78  ?  216 LEU A CG     1 
ATOM   1602 C CD1    . LEU A 1 216 ? 39.245 31.911  1.523  1.00 34.61  ?  216 LEU A CD1    1 
ATOM   1603 C CD2    . LEU A 1 216 ? 39.907 29.489  1.550  1.00 31.05  ?  216 LEU A CD2    1 
ATOM   1604 N N      . CYS A 1 217 ? 39.721 29.235  6.652  1.00 30.84  ?  217 CYS A N      1 
ATOM   1605 C CA     . CYS A 1 217 ? 40.352 29.281  7.961  1.00 29.93  ?  217 CYS A CA     1 
ATOM   1606 C C      . CYS A 1 217 ? 40.966 27.940  8.320  1.00 30.05  ?  217 CYS A C      1 
ATOM   1607 O O      . CYS A 1 217 ? 40.441 26.895  7.946  1.00 27.00  ?  217 CYS A O      1 
ATOM   1608 C CB     . CYS A 1 217 ? 39.323 29.655  9.017  1.00 32.68  ?  217 CYS A CB     1 
ATOM   1609 S SG     . CYS A 1 217 ? 39.183 31.396  9.187  1.00 36.51  ?  217 CYS A SG     1 
ATOM   1610 N N      . TYR A 1 218 ? 42.094 27.987  9.048  1.00 29.65  ?  218 TYR A N      1 
ATOM   1611 C CA     . TYR A 1 218 ? 42.700 26.797  9.663  1.00 33.40  ?  218 TYR A CA     1 
ATOM   1612 C C      . TYR A 1 218 ? 43.405 27.167  10.966 1.00 29.97  ?  218 TYR A C      1 
ATOM   1613 O O      . TYR A 1 218 ? 43.473 28.344  11.360 1.00 26.09  ?  218 TYR A O      1 
ATOM   1614 C CB     . TYR A 1 218 ? 43.712 26.101  8.743  1.00 28.73  ?  218 TYR A CB     1 
ATOM   1615 C CG     . TYR A 1 218 ? 44.961 26.906  8.471  1.00 31.30  ?  218 TYR A CG     1 
ATOM   1616 C CD1    . TYR A 1 218 ? 44.890 28.131  7.806  1.00 36.39  ?  218 TYR A CD1    1 
ATOM   1617 C CD2    . TYR A 1 218 ? 46.213 26.433  8.843  1.00 30.84  ?  218 TYR A CD2    1 
ATOM   1618 C CE1    . TYR A 1 218 ? 46.030 28.874  7.531  1.00 36.46  ?  218 TYR A CE1    1 
ATOM   1619 C CE2    . TYR A 1 218 ? 47.359 27.169  8.577  1.00 28.79  ?  218 TYR A CE2    1 
ATOM   1620 C CZ     . TYR A 1 218 ? 47.263 28.384  7.916  1.00 32.52  ?  218 TYR A CZ     1 
ATOM   1621 O OH     . TYR A 1 218 ? 48.404 29.104  7.646  1.00 28.08  ?  218 TYR A OH     1 
ATOM   1622 N N      . VAL A 1 219 ? 43.968 26.137  11.616 1.00 20.79  ?  219 VAL A N      1 
ATOM   1623 C CA     . VAL A 1 219 ? 44.706 26.298  12.866 1.00 29.71  ?  219 VAL A CA     1 
ATOM   1624 C C      . VAL A 1 219 ? 46.202 26.183  12.608 1.00 36.10  ?  219 VAL A C      1 
ATOM   1625 O O      . VAL A 1 219 ? 46.670 25.215  11.987 1.00 33.02  ?  219 VAL A O      1 
ATOM   1626 C CB     . VAL A 1 219 ? 44.265 25.284  13.930 1.00 28.77  ?  219 VAL A CB     1 
ATOM   1627 C CG1    . VAL A 1 219 ? 45.340 25.180  15.026 1.00 29.15  ?  219 VAL A CG1    1 
ATOM   1628 C CG2    . VAL A 1 219 ? 42.944 25.733  14.515 1.00 25.76  ?  219 VAL A CG2    1 
ATOM   1629 N N      . ALA A 1 220 ? 46.944 27.184  13.081 1.00 32.21  ?  220 ALA A N      1 
ATOM   1630 C CA     . ALA A 1 220 ? 48.386 27.159  13.046 1.00 26.88  ?  220 ALA A CA     1 
ATOM   1631 C C      . ALA A 1 220 ? 48.885 26.204  14.117 1.00 31.12  ?  220 ALA A C      1 
ATOM   1632 O O      . ALA A 1 220 ? 48.218 25.992  15.137 1.00 33.96  ?  220 ALA A O      1 
ATOM   1633 C CB     . ALA A 1 220 ? 48.945 28.562  13.262 1.00 26.04  ?  220 ALA A CB     1 
ATOM   1634 N N      . LEU A 1 221 ? 50.031 25.564  13.830 1.00 22.60  ?  221 LEU A N      1 
ATOM   1635 C CA     . LEU A 1 221 ? 50.675 24.660  14.773 1.00 20.19  ?  221 LEU A CA     1 
ATOM   1636 C C      . LEU A 1 221 ? 51.490 25.457  15.775 1.00 29.30  ?  221 LEU A C      1 
ATOM   1637 O O      . LEU A 1 221 ? 51.406 25.237  16.991 1.00 30.67  ?  221 LEU A O      1 
ATOM   1638 C CB     . LEU A 1 221 ? 51.554 23.648  14.021 1.00 21.42  ?  221 LEU A CB     1 
ATOM   1639 C CG     . LEU A 1 221 ? 51.905 22.397  14.855 1.00 24.43  ?  221 LEU A CG     1 
ATOM   1640 C CD1    . LEU A 1 221 ? 50.632 21.633  15.199 1.00 19.61  ?  221 LEU A CD1    1 
ATOM   1641 C CD2    . LEU A 1 221 ? 52.952 21.496  14.228 1.00 19.99  ?  221 LEU A CD2    1 
ATOM   1642 N N      . ASP A 1 222 ? 52.288 26.384  15.255 1.00 43.47  ?  222 ASP A N      1 
ATOM   1643 C CA     . ASP A 1 222 ? 52.902 27.470  16.008 1.00 41.14  ?  222 ASP A CA     1 
ATOM   1644 C C      . ASP A 1 222 ? 52.365 28.752  15.386 1.00 38.25  ?  222 ASP A C      1 
ATOM   1645 O O      . ASP A 1 222 ? 52.624 29.052  14.207 1.00 36.55  ?  222 ASP A O      1 
ATOM   1646 C CB     . ASP A 1 222 ? 54.432 27.398  15.979 1.00 37.03  ?  222 ASP A CB     1 
ATOM   1647 C CG     . ASP A 1 222 ? 55.113 28.709  16.404 1.00 46.08  ?  222 ASP A CG     1 
ATOM   1648 O OD1    . ASP A 1 222 ? 54.507 29.522  17.133 1.00 43.64  ?  222 ASP A OD1    1 
ATOM   1649 O OD2    . ASP A 1 222 ? 56.290 28.920  16.008 1.00 57.49  -1 222 ASP A OD2    1 
ATOM   1650 N N      . PHE A 1 223 ? 51.587 29.478  16.181 1.00 27.11  ?  223 PHE A N      1 
ATOM   1651 C CA     . PHE A 1 223 ? 50.970 30.705  15.706 1.00 37.19  ?  223 PHE A CA     1 
ATOM   1652 C C      . PHE A 1 223 ? 52.029 31.720  15.247 1.00 44.44  ?  223 PHE A C      1 
ATOM   1653 O O      . PHE A 1 223 ? 51.898 32.326  14.175 1.00 42.83  ?  223 PHE A O      1 
ATOM   1654 C CB     . PHE A 1 223 ? 50.055 31.241  16.821 1.00 26.85  ?  223 PHE A CB     1 
ATOM   1655 C CG     . PHE A 1 223 ? 49.410 32.536  16.496 1.00 26.30  ?  223 PHE A CG     1 
ATOM   1656 C CD1    . PHE A 1 223 ? 48.287 32.582  15.684 1.00 26.40  ?  223 PHE A CD1    1 
ATOM   1657 C CD2    . PHE A 1 223 ? 49.941 33.726  16.979 1.00 28.30  ?  223 PHE A CD2    1 
ATOM   1658 C CE1    . PHE A 1 223 ? 47.692 33.788  15.367 1.00 33.37  ?  223 PHE A CE1    1 
ATOM   1659 C CE2    . PHE A 1 223 ? 49.342 34.934  16.671 1.00 33.44  ?  223 PHE A CE2    1 
ATOM   1660 C CZ     . PHE A 1 223 ? 48.210 34.967  15.869 1.00 31.37  ?  223 PHE A CZ     1 
ATOM   1661 N N      . GLU A 1 224 ? 53.106 31.874  16.028 1.00 49.70  ?  224 GLU A N      1 
ATOM   1662 C CA     . GLU A 1 224 ? 54.201 32.790  15.696 1.00 42.23  ?  224 GLU A CA     1 
ATOM   1663 C C      . GLU A 1 224 ? 54.807 32.506  14.317 1.00 42.22  ?  224 GLU A C      1 
ATOM   1664 O O      . GLU A 1 224 ? 54.993 33.426  13.506 1.00 39.35  ?  224 GLU A O      1 
ATOM   1665 C CB     . GLU A 1 224 ? 55.282 32.693  16.773 1.00 38.92  ?  224 GLU A CB     1 
ATOM   1666 C CG     . GLU A 1 224 ? 54.966 33.362  18.088 1.00 41.22  ?  224 GLU A CG     1 
ATOM   1667 C CD     . GLU A 1 224 ? 56.166 34.140  18.615 1.00 49.79  ?  224 GLU A CD     1 
ATOM   1668 O OE1    . GLU A 1 224 ? 57.257 34.069  17.998 1.00 53.23  ?  224 GLU A OE1    1 
ATOM   1669 O OE2    . GLU A 1 224 ? 56.022 34.831  19.642 1.00 50.37  -1 224 GLU A OE2    1 
ATOM   1670 N N      . GLN A 1 225 ? 55.174 31.245  14.049 1.00 43.47  ?  225 GLN A N      1 
ATOM   1671 C CA     . GLN A 1 225 ? 55.766 30.908  12.750 1.00 44.38  ?  225 GLN A CA     1 
ATOM   1672 C C      . GLN A 1 225 ? 54.782 31.162  11.608 1.00 43.67  ?  225 GLN A C      1 
ATOM   1673 O O      . GLN A 1 225 ? 55.152 31.706  10.563 1.00 38.25  ?  225 GLN A O      1 
ATOM   1674 C CB     . GLN A 1 225 ? 56.248 29.453  12.746 1.00 43.16  ?  225 GLN A CB     1 
ATOM   1675 C CG     . GLN A 1 225 ? 57.613 29.231  13.430 1.00 52.89  ?  225 GLN A CG     1 
ATOM   1676 C CD     . GLN A 1 225 ? 58.828 29.549  12.521 1.00 59.98  ?  225 GLN A CD     1 
ATOM   1677 O OE1    . GLN A 1 225 ? 58.776 30.453  11.678 1.00 61.60  ?  225 GLN A OE1    1 
ATOM   1678 N NE2    . GLN A 1 225 ? 59.916 28.797  12.697 1.00 59.40  ?  225 GLN A NE2    1 
ATOM   1679 N N      . GLU A 1 226 ? 53.512 30.845  11.762 1.00 49.62  ?  226 GLU A N      1 
ATOM   1680 C CA     . GLU A 1 226 ? 52.552 31.194  10.731 1.00 39.33  ?  226 GLU A CA     1 
ATOM   1681 C C      . GLU A 1 226 ? 52.444 32.684  10.626 1.00 37.77  ?  226 GLU A C      1 
ATOM   1682 O O      . GLU A 1 226 ? 52.378 33.187  9.532  1.00 36.23  ?  226 GLU A O      1 
ATOM   1683 C CB     . GLU A 1 226 ? 51.212 30.491  10.906 1.00 35.91  ?  226 GLU A CB     1 
ATOM   1684 C CG     . GLU A 1 226 ? 51.249 29.006  10.661 1.00 39.16  ?  226 GLU A CG     1 
ATOM   1685 C CD     . GLU A 1 226 ? 51.759 28.631  9.294  1.00 46.07  ?  226 GLU A CD     1 
ATOM   1686 O OE1    . GLU A 1 226 ? 52.990 28.526  9.122  1.00 53.53  ?  226 GLU A OE1    1 
ATOM   1687 O OE2    . GLU A 1 226 ? 50.929 28.413  8.399  1.00 44.43  -1 226 GLU A OE2    1 
ATOM   1688 N N      . MET A 1 227 ? 52.414 33.406  11.741 1.00 34.24  ?  227 MET A N      1 
ATOM   1689 C CA     . MET A 1 227 ? 52.468 34.861  11.607 1.00 40.14  ?  227 MET A CA     1 
ATOM   1690 C C      . MET A 1 227 ? 53.692 35.290  10.805 1.00 48.04  ?  227 MET A C      1 
ATOM   1691 O O      . MET A 1 227 ? 53.580 36.044  9.832  1.00 44.83  ?  227 MET A O      1 
ATOM   1692 C CB     . MET A 1 227 ? 52.477 35.532  12.984 1.00 40.71  ?  227 MET A CB     1 
ATOM   1693 C CG     . MET A 1 227 ? 51.133 35.519  13.701 1.00 51.36  ?  227 MET A CG     1 
ATOM   1694 S SD     . MET A 1 227 ? 49.778 36.218  12.710 1.00 52.38  ?  227 MET A SD     1 
ATOM   1695 C CE     . MET A 1 227 ? 49.811 37.910  13.276 1.00 53.23  ?  227 MET A CE     1 
ATOM   1696 N N      . ALA A 1 228 ? 54.876 34.814  11.208 1.00 50.55  ?  228 ALA A N      1 
ATOM   1697 C CA     . ALA A 1 228 ? 56.102 35.234  10.544 1.00 49.61  ?  228 ALA A CA     1 
ATOM   1698 C C      . ALA A 1 228 ? 56.095 34.859  9.067  1.00 46.84  ?  228 ALA A C      1 
ATOM   1699 O O      . ALA A 1 228 ? 56.697 35.564  8.249  1.00 51.36  ?  228 ALA A O      1 
ATOM   1700 C CB     . ALA A 1 228 ? 57.312 34.627  11.253 1.00 50.27  ?  228 ALA A CB     1 
ATOM   1701 N N      . THR A 1 229 ? 55.405 33.774  8.703  1.00 32.95  ?  229 THR A N      1 
ATOM   1702 C CA     . THR A 1 229 ? 55.332 33.374  7.304  1.00 35.06  ?  229 THR A CA     1 
ATOM   1703 C C      . THR A 1 229 ? 54.352 34.237  6.515  1.00 42.69  ?  229 THR A C      1 
ATOM   1704 O O      . THR A 1 229 ? 54.594 34.534  5.339  1.00 42.28  ?  229 THR A O      1 
ATOM   1705 C CB     . THR A 1 229 ? 54.927 31.909  7.199  1.00 33.76  ?  229 THR A CB     1 
ATOM   1706 O OG1    . THR A 1 229 ? 56.088 31.079  7.344  1.00 33.78  ?  229 THR A OG1    1 
ATOM   1707 C CG2    . THR A 1 229 ? 54.246 31.645  5.856  1.00 32.35  ?  229 THR A CG2    1 
ATOM   1708 N N      . ALA A 1 230 ? 53.230 34.627  7.135  1.00 37.75  ?  230 ALA A N      1 
ATOM   1709 C CA     . ALA A 1 230 ? 52.295 35.535  6.469  1.00 31.92  ?  230 ALA A CA     1 
ATOM   1710 C C      . ALA A 1 230 ? 52.923 36.913  6.234  1.00 36.36  ?  230 ALA A C      1 
ATOM   1711 O O      . ALA A 1 230 ? 52.594 37.590  5.254  1.00 39.12  ?  230 ALA A O      1 
ATOM   1712 C CB     . ALA A 1 230 ? 50.987 35.650  7.280  1.00 22.45  ?  230 ALA A CB     1 
ATOM   1713 N N      . ALA A 1 231 ? 53.826 37.349  7.117  1.00 35.47  ?  231 ALA A N      1 
ATOM   1714 C CA     . ALA A 1 231 ? 54.519 38.624  6.958  1.00 30.45  ?  231 ALA A CA     1 
ATOM   1715 C C      . ALA A 1 231 ? 55.718 38.523  6.029  1.00 32.85  ?  231 ALA A C      1 
ATOM   1716 O O      . ALA A 1 231 ? 56.354 39.547  5.758  1.00 29.22  ?  231 ALA A O      1 
ATOM   1717 C CB     . ALA A 1 231 ? 54.986 39.150  8.321  1.00 23.44  ?  231 ALA A CB     1 
ATOM   1718 N N      . SER A 1 232 ? 56.102 37.304  5.643  1.00 32.98  ?  232 SER A N      1 
ATOM   1719 C CA     . SER A 1 232 ? 57.215 37.055  4.755  1.00 24.45  ?  232 SER A CA     1 
ATOM   1720 C C      . SER A 1 232 ? 56.837 36.643  3.344  1.00 36.85  ?  232 SER A C      1 
ATOM   1721 O O      . SER A 1 232 ? 57.737 36.459  2.522  1.00 45.48  ?  232 SER A O      1 
ATOM   1722 C CB     . SER A 1 232 ? 58.103 35.988  5.368  1.00 25.77  ?  232 SER A CB     1 
ATOM   1723 O OG     . SER A 1 232 ? 58.941 36.627  6.312  1.00 39.07  ?  232 SER A OG     1 
ATOM   1724 N N      . SER A 1 233 ? 55.562 36.404  3.084  1.00 54.25  ?  233 SER A N      1 
ATOM   1725 C CA     . SER A 1 233 ? 55.134 35.914  1.782  1.00 50.45  ?  233 SER A CA     1 
ATOM   1726 C C      . SER A 1 233 ? 53.667 35.775  1.573  1.00 49.53  ?  233 SER A C      1 
ATOM   1727 O O      . SER A 1 233 ? 52.899 35.756  2.516  1.00 51.38  ?  233 SER A O      1 
ATOM   1728 C CB     . SER A 1 233 ? 55.717 34.539  1.503  1.00 51.27  ?  233 SER A CB     1 
ATOM   1729 O OG     . SER A 1 233 ? 55.039 33.526  2.215  1.00 53.14  ?  233 SER A OG     1 
ATOM   1730 N N      . SER A 1 234 ? 53.281 35.630  0.334  1.00 41.49  ?  234 SER A N      1 
ATOM   1731 C CA     . SER A 1 234 ? 51.889 35.435  -0.047 1.00 46.03  ?  234 SER A CA     1 
ATOM   1732 C C      . SER A 1 234 ? 51.431 33.975  0.023  1.00 50.83  ?  234 SER A C      1 
ATOM   1733 O O      . SER A 1 234 ? 50.269 33.691  -0.297 1.00 48.31  ?  234 SER A O      1 
ATOM   1734 C CB     . SER A 1 234 ? 51.700 35.944  -1.467 1.00 40.70  ?  234 SER A CB     1 
ATOM   1735 O OG     . SER A 1 234 ? 52.577 35.213  -2.311 1.00 46.06  ?  234 SER A OG     1 
ATOM   1736 N N      . SER A 1 235 ? 52.302 33.046  0.419  1.00 60.65  ?  235 SER A N      1 
ATOM   1737 C CA     . SER A 1 235 ? 51.977 31.629  0.299  1.00 62.63  ?  235 SER A CA     1 
ATOM   1738 C C      . SER A 1 235 ? 50.635 31.292  0.946  1.00 62.09  ?  235 SER A C      1 
ATOM   1739 O O      . SER A 1 235 ? 49.840 30.541  0.374  1.00 66.62  ?  235 SER A O      1 
ATOM   1740 C CB     . SER A 1 235 ? 53.106 30.799  0.911  1.00 67.87  ?  235 SER A CB     1 
ATOM   1741 O OG     . SER A 1 235 ? 54.372 31.198  0.408  1.00 67.98  ?  235 SER A OG     1 
ATOM   1742 N N      . LEU A 1 236 ? 50.382 31.843  2.124  1.00 53.62  ?  236 LEU A N      1 
ATOM   1743 C CA     . LEU A 1 236 ? 49.159 31.560  2.859  1.00 53.77  ?  236 LEU A CA     1 
ATOM   1744 C C      . LEU A 1 236 ? 47.922 32.363  2.462  1.00 57.44  ?  236 LEU A C      1 
ATOM   1745 O O      . LEU A 1 236 ? 46.826 32.038  2.873  1.00 52.83  ?  236 LEU A O      1 
ATOM   1746 C CB     . LEU A 1 236 ? 49.412 31.747  4.347  1.00 49.97  ?  236 LEU A CB     1 
ATOM   1747 C CG     . LEU A 1 236 ? 50.618 31.049  4.953  1.00 50.33  ?  236 LEU A CG     1 
ATOM   1748 C CD1    . LEU A 1 236 ? 50.714 31.413  6.424  1.00 51.89  ?  236 LEU A CD1    1 
ATOM   1749 C CD2    . LEU A 1 236 ? 50.518 29.544  4.757  1.00 43.87  ?  236 LEU A CD2    1 
ATOM   1750 N N      . GLU A 1 237 ? 48.092 33.402  1.657  1.00 76.80  ?  237 GLU A N      1 
ATOM   1751 C CA     . GLU A 1 237 ? 46.948 34.173  1.192  1.00 73.38  ?  237 GLU A CA     1 
ATOM   1752 C C      . GLU A 1 237 ? 46.135 33.361  0.192  1.00 70.08  ?  237 GLU A C      1 
ATOM   1753 O O      . GLU A 1 237 ? 46.695 32.647  -0.644 1.00 69.50  ?  237 GLU A O      1 
ATOM   1754 C CB     . GLU A 1 237 ? 47.419 35.480  0.563  1.00 75.60  ?  237 GLU A CB     1 
ATOM   1755 C CG     . GLU A 1 237 ? 48.194 36.366  1.516  1.00 80.27  ?  237 GLU A CG     1 
ATOM   1756 C CD     . GLU A 1 237 ? 48.633 37.665  0.873  1.00 86.37  ?  237 GLU A CD     1 
ATOM   1757 O OE1    . GLU A 1 237 ? 48.829 37.679  -0.360 1.00 88.35  ?  237 GLU A OE1    1 
ATOM   1758 O OE2    . GLU A 1 237 ? 48.778 38.677  1.599  1.00 89.53  -1 237 GLU A OE2    1 
ATOM   1759 N N      . LYS A 1 238 ? 44.805 33.450  0.305  1.00 33.67  ?  238 LYS A N      1 
ATOM   1760 C CA     . LYS A 1 238 ? 43.868 32.848  -0.634 1.00 27.88  ?  238 LYS A CA     1 
ATOM   1761 C C      . LYS A 1 238 ? 42.838 33.892  -1.023 1.00 31.38  ?  238 LYS A C      1 
ATOM   1762 O O      . LYS A 1 238 ? 42.601 34.864  -0.297 1.00 29.62  ?  238 LYS A O      1 
ATOM   1763 C CB     . LYS A 1 238 ? 43.160 31.628  -0.052 1.00 26.12  ?  238 LYS A CB     1 
ATOM   1764 C CG     . LYS A 1 238 ? 44.086 30.470  0.229  1.00 29.41  ?  238 LYS A CG     1 
ATOM   1765 C CD     . LYS A 1 238 ? 43.635 29.205  -0.482 1.00 27.04  ?  238 LYS A CD     1 
ATOM   1766 C CE     . LYS A 1 238 ? 44.704 28.129  -0.298 1.00 29.63  ?  238 LYS A CE     1 
ATOM   1767 N NZ     . LYS A 1 238 ? 44.174 26.747  -0.517 1.00 31.92  ?  238 LYS A NZ     1 
ATOM   1768 N N      . SER A 1 239 ? 42.260 33.738  -2.199 1.00 46.76  ?  239 SER A N      1 
ATOM   1769 C CA     . SER A 1 239 ? 41.222 34.688  -2.553 1.00 50.60  ?  239 SER A CA     1 
ATOM   1770 C C      . SER A 1 239 ? 39.866 34.012  -2.413 1.00 41.19  ?  239 SER A C      1 
ATOM   1771 O O      . SER A 1 239 ? 39.748 32.794  -2.242 1.00 35.86  ?  239 SER A O      1 
ATOM   1772 C CB     . SER A 1 239 ? 41.457 35.290  -3.965 1.00 51.25  ?  239 SER A CB     1 
ATOM   1773 O OG     . SER A 1 239 ? 41.197 34.404  -5.054 1.00 46.60  ?  239 SER A OG     1 
ATOM   1774 N N      . TYR A 1 240 ? 38.832 34.829  -2.507 1.00 29.78  ?  240 TYR A N      1 
ATOM   1775 C CA     . TYR A 1 240 ? 37.486 34.354  -2.250 1.00 36.16  ?  240 TYR A CA     1 
ATOM   1776 C C      . TYR A 1 240 ? 36.564 35.228  -3.088 1.00 39.06  ?  240 TYR A C      1 
ATOM   1777 O O      . TYR A 1 240 ? 36.818 36.426  -3.226 1.00 43.71  ?  240 TYR A O      1 
ATOM   1778 C CB     . TYR A 1 240 ? 37.168 34.403  -0.734 1.00 34.75  ?  240 TYR A CB     1 
ATOM   1779 C CG     . TYR A 1 240 ? 35.733 34.064  -0.416 1.00 34.06  ?  240 TYR A CG     1 
ATOM   1780 C CD1    . TYR A 1 240 ? 35.274 32.753  -0.499 1.00 33.67  ?  240 TYR A CD1    1 
ATOM   1781 C CD2    . TYR A 1 240 ? 34.827 35.060  -0.073 1.00 32.10  ?  240 TYR A CD2    1 
ATOM   1782 C CE1    . TYR A 1 240 ? 33.953 32.446  -0.248 1.00 36.98  ?  240 TYR A CE1    1 
ATOM   1783 C CE2    . TYR A 1 240 ? 33.496 34.763  0.174  1.00 32.41  ?  240 TYR A CE2    1 
ATOM   1784 C CZ     . TYR A 1 240 ? 33.073 33.454  0.090  1.00 37.27  ?  240 TYR A CZ     1 
ATOM   1785 O OH     . TYR A 1 240 ? 31.765 33.142  0.349  1.00 42.00  ?  240 TYR A OH     1 
ATOM   1786 N N      . GLU A 1 241 ? 35.524 34.626  -3.673 1.00 55.74  ?  241 GLU A N      1 
ATOM   1787 C CA     . GLU A 1 241 ? 34.634 35.323  -4.606 1.00 62.22  ?  241 GLU A CA     1 
ATOM   1788 C C      . GLU A 1 241 ? 33.345 35.642  -3.874 1.00 53.72  ?  241 GLU A C      1 
ATOM   1789 O O      . GLU A 1 241 ? 32.565 34.738  -3.568 1.00 53.80  ?  241 GLU A O      1 
ATOM   1790 C CB     . GLU A 1 241 ? 34.342 34.488  -5.855 1.00 69.69  ?  241 GLU A CB     1 
ATOM   1791 C CG     . GLU A 1 241 ? 35.533 34.295  -6.797 1.00 77.02  ?  241 GLU A CG     1 
ATOM   1792 C CD     . GLU A 1 241 ? 36.633 33.424  -6.192 1.00 79.54  ?  241 GLU A CD     1 
ATOM   1793 O OE1    . GLU A 1 241 ? 36.282 32.477  -5.447 1.00 82.51  ?  241 GLU A OE1    1 
ATOM   1794 O OE2    . GLU A 1 241 ? 37.837 33.690  -6.451 1.00 74.63  -1 241 GLU A OE2    1 
ATOM   1795 N N      . LEU A 1 242 ? 33.115 36.919  -3.620 1.00 41.05  ?  242 LEU A N      1 
ATOM   1796 C CA     . LEU A 1 242 ? 31.931 37.344  -2.893 1.00 42.01  ?  242 LEU A CA     1 
ATOM   1797 C C      . LEU A 1 242 ? 30.705 36.996  -3.712 1.00 38.00  ?  242 LEU A C      1 
ATOM   1798 O O      . LEU A 1 242 ? 30.834 36.676  -4.899 1.00 37.82  ?  242 LEU A O      1 
ATOM   1799 C CB     . LEU A 1 242 ? 31.940 38.848  -2.643 1.00 45.35  ?  242 LEU A CB     1 
ATOM   1800 C CG     . LEU A 1 242 ? 32.982 39.453  -1.738 1.00 44.40  ?  242 LEU A CG     1 
ATOM   1801 C CD1    . LEU A 1 242 ? 32.477 40.848  -1.445 1.00 39.70  ?  242 LEU A CD1    1 
ATOM   1802 C CD2    . LEU A 1 242 ? 33.098 38.578  -0.479 1.00 44.24  ?  242 LEU A CD2    1 
ATOM   1803 N N      . PRO A 1 243 ? 29.506 37.050  -3.138 1.00 37.64  ?  243 PRO A N      1 
ATOM   1804 C CA     . PRO A 1 243 ? 28.330 36.816  -3.977 1.00 36.15  ?  243 PRO A CA     1 
ATOM   1805 C C      . PRO A 1 243 ? 28.381 37.701  -5.188 1.00 39.02  ?  243 PRO A C      1 
ATOM   1806 O O      . PRO A 1 243 ? 28.279 37.193  -6.305 1.00 51.23  ?  243 PRO A O      1 
ATOM   1807 C CB     . PRO A 1 243 ? 27.144 37.137  -3.055 1.00 36.36  ?  243 PRO A CB     1 
ATOM   1808 C CG     . PRO A 1 243 ? 27.740 37.928  -1.899 1.00 42.94  ?  243 PRO A CG     1 
ATOM   1809 C CD     . PRO A 1 243 ? 29.140 37.388  -1.749 1.00 44.59  ?  243 PRO A CD     1 
ATOM   1810 N N      . ASP A 1 244 ? 28.664 38.990  -5.011 1.00 46.18  ?  244 ASP A N      1 
ATOM   1811 C CA     . ASP A 1 244 ? 28.408 39.971  -6.071 1.00 52.25  ?  244 ASP A CA     1 
ATOM   1812 C C      . ASP A 1 244 ? 29.529 40.041  -7.106 1.00 50.50  ?  244 ASP A C      1 
ATOM   1813 O O      . ASP A 1 244 ? 29.477 40.891  -7.999 1.00 44.37  ?  244 ASP A O      1 
ATOM   1814 C CB     . ASP A 1 244 ? 28.103 41.363  -5.477 1.00 50.27  ?  244 ASP A CB     1 
ATOM   1815 C CG     . ASP A 1 244 ? 29.339 42.095  -4.933 1.00 53.51  ?  244 ASP A CG     1 
ATOM   1816 O OD1    . ASP A 1 244 ? 30.480 41.578  -5.052 1.00 49.79  ?  244 ASP A OD1    1 
ATOM   1817 O OD2    . ASP A 1 244 ? 29.152 43.227  -4.405 1.00 53.60  -1 244 ASP A OD2    1 
ATOM   1818 N N      . GLY A 1 245 ? 30.522 39.163  -7.010 1.00 72.18  ?  245 GLY A N      1 
ATOM   1819 C CA     . GLY A 1 245 ? 31.567 39.038  -8.003 1.00 70.89  ?  245 GLY A CA     1 
ATOM   1820 C C      . GLY A 1 245 ? 32.937 39.512  -7.559 1.00 64.23  ?  245 GLY A C      1 
ATOM   1821 O O      . GLY A 1 245 ? 33.931 39.130  -8.190 1.00 67.82  ?  245 GLY A O      1 
ATOM   1822 N N      . GLN A 1 246 ? 33.033 40.284  -6.473 1.00 40.36  ?  246 GLN A N      1 
ATOM   1823 C CA     . GLN A 1 246 ? 34.340 40.748  -6.018 1.00 44.19  ?  246 GLN A CA     1 
ATOM   1824 C C      . GLN A 1 246 ? 35.130 39.631  -5.339 1.00 48.39  ?  246 GLN A C      1 
ATOM   1825 O O      . GLN A 1 246 ? 34.570 38.753  -4.672 1.00 51.96  ?  246 GLN A O      1 
ATOM   1826 C CB     . GLN A 1 246 ? 34.194 41.924  -5.072 1.00 38.57  ?  246 GLN A CB     1 
ATOM   1827 C CG     . GLN A 1 246 ? 33.094 42.858  -5.487 1.00 44.26  ?  246 GLN A CG     1 
ATOM   1828 C CD     . GLN A 1 246 ? 32.876 43.981  -4.500 1.00 47.00  ?  246 GLN A CD     1 
ATOM   1829 O OE1    . GLN A 1 246 ? 33.833 44.572  -3.992 1.00 52.48  ?  246 GLN A OE1    1 
ATOM   1830 N NE2    . GLN A 1 246 ? 31.614 44.280  -4.221 1.00 43.29  ?  246 GLN A NE2    1 
ATOM   1831 N N      . VAL A 1 247 ? 36.442 39.666  -5.540 1.00 33.90  ?  247 VAL A N      1 
ATOM   1832 C CA     . VAL A 1 247 ? 37.365 38.666  -5.022 1.00 34.84  ?  247 VAL A CA     1 
ATOM   1833 C C      . VAL A 1 247 ? 38.269 39.354  -4.017 1.00 37.65  ?  247 VAL A C      1 
ATOM   1834 O O      . VAL A 1 247 ? 39.106 40.186  -4.397 1.00 34.65  ?  247 VAL A O      1 
ATOM   1835 C CB     . VAL A 1 247 ? 38.200 38.026  -6.130 1.00 45.72  ?  247 VAL A CB     1 
ATOM   1836 C CG1    . VAL A 1 247 ? 39.499 37.471  -5.534 1.00 50.06  ?  247 VAL A CG1    1 
ATOM   1837 C CG2    . VAL A 1 247 ? 37.396 36.952  -6.864 1.00 46.82  ?  247 VAL A CG2    1 
ATOM   1838 N N      . ILE A 1 248 ? 38.114 38.977  -2.740 1.00 35.58  ?  248 ILE A N      1 
ATOM   1839 C CA     . ILE A 1 248 ? 38.841 39.557  -1.621 1.00 30.42  ?  248 ILE A CA     1 
ATOM   1840 C C      . ILE A 1 248 ? 39.911 38.565  -1.189 1.00 30.69  ?  248 ILE A C      1 
ATOM   1841 O O      . ILE A 1 248 ? 39.726 37.348  -1.298 1.00 35.88  ?  248 ILE A O      1 
ATOM   1842 C CB     . ILE A 1 248 ? 37.865 39.910  -0.473 1.00 33.93  ?  248 ILE A CB     1 
ATOM   1843 C CG1    . ILE A 1 248 ? 37.649 38.724  0.467  1.00 26.99  ?  248 ILE A CG1    1 
ATOM   1844 C CG2    . ILE A 1 248 ? 36.497 40.341  -1.028 1.00 29.89  ?  248 ILE A CG2    1 
ATOM   1845 C CD1    . ILE A 1 248 ? 36.591 38.985  1.421  1.00 23.22  ?  248 ILE A CD1    1 
ATOM   1846 N N      . THR A 1 249 ? 41.052 39.074  -0.720 1.00 36.76  ?  249 THR A N      1 
ATOM   1847 C CA     . THR A 1 249 ? 42.169 38.208  -0.340 1.00 37.41  ?  249 THR A CA     1 
ATOM   1848 C C      . THR A 1 249 ? 42.274 38.038  1.172  1.00 41.59  ?  249 THR A C      1 
ATOM   1849 O O      . THR A 1 249 ? 42.142 38.996  1.935  1.00 42.27  ?  249 THR A O      1 
ATOM   1850 C CB     . THR A 1 249 ? 43.490 38.738  -0.873 1.00 38.33  ?  249 THR A CB     1 
ATOM   1851 O OG1    . THR A 1 249 ? 43.416 38.826  -2.303 1.00 50.36  ?  249 THR A OG1    1 
ATOM   1852 C CG2    . THR A 1 249 ? 44.611 37.780  -0.486 1.00 37.38  ?  249 THR A CG2    1 
ATOM   1853 N N      . ILE A 1 250 ? 42.544 36.810  1.595  1.00 39.63  ?  250 ILE A N      1 
ATOM   1854 C CA     . ILE A 1 250 ? 42.546 36.431  2.998  1.00 34.36  ?  250 ILE A CA     1 
ATOM   1855 C C      . ILE A 1 250 ? 43.961 35.969  3.365  1.00 43.23  ?  250 ILE A C      1 
ATOM   1856 O O      . ILE A 1 250 ? 44.476 34.995  2.805  1.00 38.69  ?  250 ILE A O      1 
ATOM   1857 C CB     . ILE A 1 250 ? 41.495 35.342  3.290  1.00 33.18  ?  250 ILE A CB     1 
ATOM   1858 C CG1    . ILE A 1 250 ? 40.141 35.747  2.737  1.00 39.41  ?  250 ILE A CG1    1 
ATOM   1859 C CG2    . ILE A 1 250 ? 41.299 35.155  4.783  1.00 35.50  ?  250 ILE A CG2    1 
ATOM   1860 C CD1    . ILE A 1 250 ? 39.498 36.913  3.515  1.00 47.20  ?  250 ILE A CD1    1 
ATOM   1861 N N      . GLY A 1 251 ? 44.570 36.663  4.315  1.00 52.54  ?  251 GLY A N      1 
ATOM   1862 C CA     . GLY A 1 251 ? 45.911 36.469  4.835  1.00 46.85  ?  251 GLY A CA     1 
ATOM   1863 C C      . GLY A 1 251 ? 45.915 35.704  6.140  1.00 48.84  ?  251 GLY A C      1 
ATOM   1864 O O      . GLY A 1 251 ? 45.274 34.653  6.274  1.00 45.76  ?  251 GLY A O      1 
ATOM   1865 N N      . ASN A 1 252 ? 46.731 36.191  7.081  1.00 44.95  ?  252 ASN A N      1 
ATOM   1866 C CA     . ASN A 1 252 ? 46.796 35.679  8.441  1.00 40.41  ?  252 ASN A CA     1 
ATOM   1867 C C      . ASN A 1 252 ? 45.466 35.739  9.186  1.00 45.17  ?  252 ASN A C      1 
ATOM   1868 O O      . ASN A 1 252 ? 45.385 35.218  10.306 1.00 45.98  ?  252 ASN A O      1 
ATOM   1869 C CB     . ASN A 1 252 ? 47.834 36.467  9.207  1.00 37.24  ?  252 ASN A CB     1 
ATOM   1870 C CG     . ASN A 1 252 ? 47.607 37.938  9.110  1.00 34.26  ?  252 ASN A CG     1 
ATOM   1871 O OD1    . ASN A 1 252 ? 46.465 38.413  9.092  1.00 33.67  ?  252 ASN A OD1    1 
ATOM   1872 N ND2    . ASN A 1 252 ? 48.699 38.687  9.037  1.00 38.34  ?  252 ASN A ND2    1 
ATOM   1873 N N      . GLU A 1 253 ? 44.451 36.424  8.640  1.00 40.09  ?  253 GLU A N      1 
ATOM   1874 C CA     . GLU A 1 253 ? 43.094 36.242  9.139  1.00 31.76  ?  253 GLU A CA     1 
ATOM   1875 C C      . GLU A 1 253 ? 42.696 34.775  9.113  1.00 31.24  ?  253 GLU A C      1 
ATOM   1876 O O      . GLU A 1 253 ? 41.878 34.343  9.926  1.00 33.09  ?  253 GLU A O      1 
ATOM   1877 C CB     . GLU A 1 253 ? 42.101 37.056  8.313  1.00 33.80  ?  253 GLU A CB     1 
ATOM   1878 C CG     . GLU A 1 253 ? 42.139 38.553  8.550  1.00 39.22  ?  253 GLU A CG     1 
ATOM   1879 C CD     . GLU A 1 253 ? 43.153 39.281  7.689  1.00 43.24  ?  253 GLU A CD     1 
ATOM   1880 O OE1    . GLU A 1 253 ? 43.854 38.613  6.899  1.00 42.53  ?  253 GLU A OE1    1 
ATOM   1881 O OE2    . GLU A 1 253 ? 43.230 40.529  7.799  1.00 44.74  -1 253 GLU A OE2    1 
ATOM   1882 N N      . ARG A 1 254 ? 43.290 33.994  8.200  1.00 37.81  ?  254 ARG A N      1 
ATOM   1883 C CA     . ARG A 1 254 ? 42.920 32.591  8.019  1.00 34.95  ?  254 ARG A CA     1 
ATOM   1884 C C      . ARG A 1 254 ? 43.126 31.776  9.289  1.00 32.46  ?  254 ARG A C      1 
ATOM   1885 O O      . ARG A 1 254 ? 42.288 30.939  9.630  1.00 34.01  ?  254 ARG A O      1 
ATOM   1886 C CB     . ARG A 1 254 ? 43.717 31.979  6.863  1.00 35.71  ?  254 ARG A CB     1 
ATOM   1887 C CG     . ARG A 1 254 ? 43.359 32.533  5.504  1.00 32.69  ?  254 ARG A CG     1 
ATOM   1888 C CD     . ARG A 1 254 ? 44.008 31.773  4.346  1.00 30.67  ?  254 ARG A CD     1 
ATOM   1889 N NE     . ARG A 1 254 ? 43.581 30.385  4.243  1.00 25.46  ?  254 ARG A NE     1 
ATOM   1890 C CZ     . ARG A 1 254 ? 44.427 29.370  4.232  1.00 30.08  ?  254 ARG A CZ     1 
ATOM   1891 N NH1    . ARG A 1 254 ? 45.727 29.597  4.320  1.00 37.93  ?  254 ARG A NH1    1 
ATOM   1892 N NH2    . ARG A 1 254 ? 43.990 28.136  4.141  1.00 25.15  ?  254 ARG A NH2    1 
ATOM   1893 N N      . PHE A 1 255 ? 44.285 31.909  9.939  1.00 40.02  ?  255 PHE A N      1 
ATOM   1894 C CA     . PHE A 1 255 ? 44.518 31.206  11.203 1.00 45.28  ?  255 PHE A CA     1 
ATOM   1895 C C      . PHE A 1 255 ? 44.338 32.058  12.467 1.00 38.59  ?  255 PHE A C      1 
ATOM   1896 O O      . PHE A 1 255 ? 44.261 31.493  13.567 1.00 31.40  ?  255 PHE A O      1 
ATOM   1897 C CB     . PHE A 1 255 ? 45.921 30.584  11.205 1.00 50.38  ?  255 PHE A CB     1 
ATOM   1898 C CG     . PHE A 1 255 ? 46.995 31.532  10.761 1.00 50.61  ?  255 PHE A CG     1 
ATOM   1899 C CD1    . PHE A 1 255 ? 47.276 31.702  9.414  1.00 43.32  ?  255 PHE A CD1    1 
ATOM   1900 C CD2    . PHE A 1 255 ? 47.713 32.264  11.690 1.00 48.52  ?  255 PHE A CD2    1 
ATOM   1901 C CE1    . PHE A 1 255 ? 48.254 32.575  9.012  1.00 38.79  ?  255 PHE A CE1    1 
ATOM   1902 C CE2    . PHE A 1 255 ? 48.689 33.119  11.298 1.00 47.09  ?  255 PHE A CE2    1 
ATOM   1903 C CZ     . PHE A 1 255 ? 48.961 33.284  9.957  1.00 45.89  ?  255 PHE A CZ     1 
ATOM   1904 N N      . ARG A 1 256 ? 44.250 33.384  12.361 1.00 28.02  ?  256 ARG A N      1 
ATOM   1905 C CA     . ARG A 1 256 ? 43.948 34.146  13.567 1.00 29.64  ?  256 ARG A CA     1 
ATOM   1906 C C      . ARG A 1 256 ? 42.518 33.940  14.030 1.00 35.05  ?  256 ARG A C      1 
ATOM   1907 O O      . ARG A 1 256 ? 42.224 34.164  15.204 1.00 40.24  ?  256 ARG A O      1 
ATOM   1908 C CB     . ARG A 1 256 ? 44.176 35.633  13.357 1.00 29.63  ?  256 ARG A CB     1 
ATOM   1909 C CG     . ARG A 1 256 ? 45.612 36.006  13.199 1.00 29.33  ?  256 ARG A CG     1 
ATOM   1910 C CD     . ARG A 1 256 ? 45.694 37.330  12.476 1.00 35.83  ?  256 ARG A CD     1 
ATOM   1911 N NE     . ARG A 1 256 ? 45.011 38.396  13.209 1.00 37.31  ?  256 ARG A NE     1 
ATOM   1912 C CZ     . ARG A 1 256 ? 44.614 39.531  12.653 1.00 28.06  ?  256 ARG A CZ     1 
ATOM   1913 N NH1    . ARG A 1 256 ? 44.827 39.732  11.361 1.00 30.62  ?  256 ARG A NH1    1 
ATOM   1914 N NH2    . ARG A 1 256 ? 44.013 40.457  13.388 1.00 23.41  ?  256 ARG A NH2    1 
ATOM   1915 N N      . CYS A 1 257 ? 41.618 33.559  13.133 1.00 43.65  ?  257 CYS A N      1 
ATOM   1916 C CA     . CYS A 1 257 ? 40.254 33.244  13.552 1.00 42.56  ?  257 CYS A CA     1 
ATOM   1917 C C      . CYS A 1 257 ? 40.216 32.042  14.492 1.00 44.71  ?  257 CYS A C      1 
ATOM   1918 O O      . CYS A 1 257 ? 39.773 32.190  15.649 1.00 50.01  ?  257 CYS A O      1 
ATOM   1919 C CB     . CYS A 1 257 ? 39.392 33.058  12.303 1.00 45.87  ?  257 CYS A CB     1 
ATOM   1920 S SG     . CYS A 1 257 ? 37.699 32.436  12.577 1.00 40.02  ?  257 CYS A SG     1 
ATOM   1921 N N      . PRO A 1 258 ? 40.682 30.853  14.099 1.00 31.35  ?  258 PRO A N      1 
ATOM   1922 C CA     . PRO A 1 258 ? 40.579 29.697  15.007 1.00 34.34  ?  258 PRO A CA     1 
ATOM   1923 C C      . PRO A 1 258 ? 41.473 29.801  16.235 1.00 33.58  ?  258 PRO A C      1 
ATOM   1924 O O      . PRO A 1 258 ? 41.212 29.089  17.210 1.00 25.14  ?  258 PRO A O      1 
ATOM   1925 C CB     . PRO A 1 258 ? 40.980 28.511  14.117 1.00 36.57  ?  258 PRO A CB     1 
ATOM   1926 C CG     . PRO A 1 258 ? 40.849 29.012  12.722 1.00 35.48  ?  258 PRO A CG     1 
ATOM   1927 C CD     . PRO A 1 258 ? 41.201 30.461  12.786 1.00 32.54  ?  258 PRO A CD     1 
ATOM   1928 N N      . GLU A 1 259 ? 42.514 30.649  16.190 1.00 38.87  ?  259 GLU A N      1 
ATOM   1929 C CA     . GLU A 1 259 ? 43.379 30.954  17.329 1.00 33.88  ?  259 GLU A CA     1 
ATOM   1930 C C      . GLU A 1 259 ? 42.596 31.470  18.533 1.00 45.92  ?  259 GLU A C      1 
ATOM   1931 O O      . GLU A 1 259 ? 43.034 31.281  19.674 1.00 54.06  ?  259 GLU A O      1 
ATOM   1932 C CB     . GLU A 1 259 ? 44.416 31.998  16.912 1.00 29.32  ?  259 GLU A CB     1 
ATOM   1933 C CG     . GLU A 1 259 ? 45.673 32.068  17.744 1.00 29.01  ?  259 GLU A CG     1 
ATOM   1934 C CD     . GLU A 1 259 ? 46.306 30.694  17.999 1.00 36.62  ?  259 GLU A CD     1 
ATOM   1935 O OE1    . GLU A 1 259 ? 46.391 29.827  17.061 1.00 26.39  ?  259 GLU A OE1    1 
ATOM   1936 O OE2    . GLU A 1 259 ? 46.705 30.485  19.175 1.00 42.65  -1 259 GLU A OE2    1 
ATOM   1937 N N      . ALA A 1 260 ? 41.451 32.135  18.310 1.00 44.07  ?  260 ALA A N      1 
ATOM   1938 C CA     . ALA A 1 260 ? 40.596 32.531  19.431 1.00 37.30  ?  260 ALA A CA     1 
ATOM   1939 C C      . ALA A 1 260 ? 40.169 31.331  20.274 1.00 38.19  ?  260 ALA A C      1 
ATOM   1940 O O      . ALA A 1 260 ? 39.784 31.513  21.437 1.00 34.38  ?  260 ALA A O      1 
ATOM   1941 C CB     . ALA A 1 260 ? 39.357 33.305  18.935 1.00 26.91  ?  260 ALA A CB     1 
ATOM   1942 N N      . LEU A 1 261 ? 40.239 30.106  19.728 1.00 28.19  ?  261 LEU A N      1 
ATOM   1943 C CA     . LEU A 1 261 ? 39.922 28.928  20.536 1.00 26.37  ?  261 LEU A CA     1 
ATOM   1944 C C      . LEU A 1 261 ? 41.015 28.675  21.562 1.00 24.78  ?  261 LEU A C      1 
ATOM   1945 O O      . LEU A 1 261 ? 40.731 28.445  22.744 1.00 25.38  ?  261 LEU A O      1 
ATOM   1946 C CB     . LEU A 1 261 ? 39.700 27.698  19.639 1.00 28.18  ?  261 LEU A CB     1 
ATOM   1947 C CG     . LEU A 1 261 ? 38.479 27.831  18.701 1.00 29.07  ?  261 LEU A CG     1 
ATOM   1948 C CD1    . LEU A 1 261 ? 38.376 26.787  17.633 1.00 19.09  ?  261 LEU A CD1    1 
ATOM   1949 C CD2    . LEU A 1 261 ? 37.183 27.913  19.492 1.00 22.14  ?  261 LEU A CD2    1 
ATOM   1950 N N      . PHE A 1 262 ? 42.273 28.773  21.135 1.00 29.25  ?  262 PHE A N      1 
ATOM   1951 C CA     . PHE A 1 262 ? 43.398 28.594  22.045 1.00 31.40  ?  262 PHE A CA     1 
ATOM   1952 C C      . PHE A 1 262 ? 43.731 29.858  22.815 1.00 30.20  ?  262 PHE A C      1 
ATOM   1953 O O      . PHE A 1 262 ? 44.230 29.771  23.940 1.00 38.78  ?  262 PHE A O      1 
ATOM   1954 C CB     . PHE A 1 262 ? 44.607 28.082  21.254 1.00 26.73  ?  262 PHE A CB     1 
ATOM   1955 C CG     . PHE A 1 262 ? 44.314 26.819  20.518 1.00 26.90  ?  262 PHE A CG     1 
ATOM   1956 C CD1    . PHE A 1 262 ? 43.732 26.857  19.270 1.00 26.91  ?  262 PHE A CD1    1 
ATOM   1957 C CD2    . PHE A 1 262 ? 44.550 25.592  21.109 1.00 25.52  ?  262 PHE A CD2    1 
ATOM   1958 C CE1    . PHE A 1 262 ? 43.428 25.693  18.612 1.00 29.55  ?  262 PHE A CE1    1 
ATOM   1959 C CE2    . PHE A 1 262 ? 44.253 24.424  20.445 1.00 30.35  ?  262 PHE A CE2    1 
ATOM   1960 C CZ     . PHE A 1 262 ? 43.689 24.468  19.200 1.00 29.51  ?  262 PHE A CZ     1 
ATOM   1961 N N      . GLN A 1 263 ? 43.467 31.004  22.215 1.00 20.78  ?  263 GLN A N      1 
ATOM   1962 C CA     . GLN A 1 263 ? 43.736 32.280  22.826 1.00 20.30  ?  263 GLN A CA     1 
ATOM   1963 C C      . GLN A 1 263 ? 42.495 33.100  22.816 1.00 21.95  ?  263 GLN A C      1 
ATOM   1964 O O      . GLN A 1 263 ? 42.259 33.829  21.891 1.00 26.59  ?  263 GLN A O      1 
ATOM   1965 C CB     . GLN A 1 263 ? 44.810 33.004  22.060 1.00 26.96  ?  263 GLN A CB     1 
ATOM   1966 C CG     . GLN A 1 263 ? 46.171 32.334  22.075 1.00 25.64  ?  263 GLN A CG     1 
ATOM   1967 C CD     . GLN A 1 263 ? 47.280 33.259  21.633 1.00 25.08  ?  263 GLN A CD     1 
ATOM   1968 O OE1    . GLN A 1 263 ? 48.055 32.934  20.745 1.00 31.59  ?  263 GLN A OE1    1 
ATOM   1969 N NE2    . GLN A 1 263 ? 47.356 34.420  22.248 1.00 24.93  ?  263 GLN A NE2    1 
ATOM   1970 N N      . PRO A 1 264 ? 41.679 33.028  23.943 1.00 37.23  ?  264 PRO A N      1 
ATOM   1971 C CA     . PRO A 1 264 ? 40.397 33.740  23.912 1.00 31.47  ?  264 PRO A CA     1 
ATOM   1972 C C      . PRO A 1 264 ? 40.509 35.211  24.144 1.00 35.68  ?  264 PRO A C      1 
ATOM   1973 O O      . PRO A 1 264 ? 39.515 35.896  24.035 1.00 31.04  ?  264 PRO A O      1 
ATOM   1974 C CB     . PRO A 1 264 ? 39.616 33.073  25.043 1.00 30.37  ?  264 PRO A CB     1 
ATOM   1975 C CG     . PRO A 1 264 ? 40.324 31.811  25.352 1.00 28.93  ?  264 PRO A CG     1 
ATOM   1976 C CD     . PRO A 1 264 ? 41.725 32.256  25.219 1.00 31.06  ?  264 PRO A CD     1 
ATOM   1977 N N      . SER A 1 265 ? 41.709 35.686  24.432 1.00 52.23  ?  265 SER A N      1 
ATOM   1978 C CA     . SER A 1 265 ? 41.957 37.101  24.633 1.00 52.02  ?  265 SER A CA     1 
ATOM   1979 C C      . SER A 1 265 ? 41.714 37.866  23.398 1.00 47.72  ?  265 SER A C      1 
ATOM   1980 O O      . SER A 1 265 ? 41.588 39.072  23.423 1.00 48.92  ?  265 SER A O      1 
ATOM   1981 C CB     . SER A 1 265 ? 43.424 37.269  25.015 1.00 50.25  ?  265 SER A CB     1 
ATOM   1982 O OG     . SER A 1 265 ? 44.287 36.727  24.041 1.00 47.75  ?  265 SER A OG     1 
ATOM   1983 N N      . PHE A 1 266 ? 41.667 37.155  22.304 1.00 39.23  ?  266 PHE A N      1 
ATOM   1984 C CA     . PHE A 1 266 ? 41.507 37.810  21.012 1.00 30.18  ?  266 PHE A CA     1 
ATOM   1985 C C      . PHE A 1 266 ? 40.185 38.540  20.912 1.00 28.98  ?  266 PHE A C      1 
ATOM   1986 O O      . PHE A 1 266 ? 40.119 39.620  20.322 1.00 39.60  ?  266 PHE A O      1 
ATOM   1987 C CB     . PHE A 1 266 ? 41.643 36.779  19.901 1.00 31.45  ?  266 PHE A CB     1 
ATOM   1988 C CG     . PHE A 1 266 ? 43.064 36.381  19.628 1.00 30.39  ?  266 PHE A CG     1 
ATOM   1989 C CD1    . PHE A 1 266 ? 44.087 36.820  20.457 1.00 28.64  ?  266 PHE A CD1    1 
ATOM   1990 C CD2    . PHE A 1 266 ? 43.385 35.614  18.518 1.00 33.31  ?  266 PHE A CD2    1 
ATOM   1991 C CE1    . PHE A 1 266 ? 45.411 36.459  20.216 1.00 28.73  ?  266 PHE A CE1    1 
ATOM   1992 C CE2    . PHE A 1 266 ? 44.702 35.272  18.254 1.00 34.17  ?  266 PHE A CE2    1 
ATOM   1993 C CZ     . PHE A 1 266 ? 45.719 35.697  19.112 1.00 30.29  ?  266 PHE A CZ     1 
ATOM   1994 N N      . LEU A 1 267 ? 39.157 38.002  21.536 1.00 41.12  ?  267 LEU A N      1 
ATOM   1995 C CA     . LEU A 1 267 ? 37.857 38.641  21.581 1.00 37.98  ?  267 LEU A CA     1 
ATOM   1996 C C      . LEU A 1 267 ? 37.624 39.308  22.936 1.00 43.18  ?  267 LEU A C      1 
ATOM   1997 O O      . LEU A 1 267 ? 36.500 39.658  23.250 1.00 46.10  ?  267 LEU A O      1 
ATOM   1998 C CB     . LEU A 1 267 ? 36.778 37.617  21.307 1.00 35.37  ?  267 LEU A CB     1 
ATOM   1999 C CG     . LEU A 1 267 ? 36.476 37.202  19.885 1.00 38.56  ?  267 LEU A CG     1 
ATOM   2000 C CD1    . LEU A 1 267 ? 36.073 35.744  19.880 1.00 40.07  ?  267 LEU A CD1    1 
ATOM   2001 C CD2    . LEU A 1 267 ? 35.351 38.066  19.351 1.00 46.98  ?  267 LEU A CD2    1 
ATOM   2002 N N      . GLY A 1 268 ? 38.636 39.371  23.768 1.00 30.49  ?  268 GLY A N      1 
ATOM   2003 C CA     . GLY A 1 268 ? 38.489 40.031  25.035 1.00 35.53  ?  268 GLY A CA     1 
ATOM   2004 C C      . GLY A 1 268 ? 37.877 39.232  26.137 1.00 37.39  ?  268 GLY A C      1 
ATOM   2005 O O      . GLY A 1 268 ? 37.119 39.753  26.934 1.00 39.97  ?  268 GLY A O      1 
ATOM   2006 N N      . MET A 1 269 ? 38.236 37.977  26.217 1.00 47.42  ?  269 MET A N      1 
ATOM   2007 C CA     . MET A 1 269 ? 37.673 37.118  27.212 1.00 50.57  ?  269 MET A CA     1 
ATOM   2008 C C      . MET A 1 269 ? 38.776 36.491  27.998 1.00 49.59  ?  269 MET A C      1 
ATOM   2009 O O      . MET A 1 269 ? 39.690 35.948  27.431 1.00 39.73  ?  269 MET A O      1 
ATOM   2010 C CB     . MET A 1 269 ? 36.803 36.066  26.518 1.00 54.62  ?  269 MET A CB     1 
ATOM   2011 C CG     . MET A 1 269 ? 36.551 34.763  27.243 1.00 58.48  ?  269 MET A CG     1 
ATOM   2012 S SD     . MET A 1 269 ? 35.253 33.867  26.362 1.00 58.41  ?  269 MET A SD     1 
ATOM   2013 C CE     . MET A 1 269 ? 35.975 33.711  24.737 1.00 56.94  ?  269 MET A CE     1 
ATOM   2014 N N      . GLU A 1 270 ? 38.719 36.618  29.309 1.00 60.90  ?  270 GLU A N      1 
ATOM   2015 C CA     . GLU A 1 270 ? 39.690 35.953  30.144 1.00 64.77  ?  270 GLU A CA     1 
ATOM   2016 C C      . GLU A 1 270 ? 39.089 34.629  30.419 1.00 67.90  ?  270 GLU A C      1 
ATOM   2017 O O      . GLU A 1 270 ? 38.249 34.467  31.294 1.00 71.09  ?  270 GLU A O      1 
ATOM   2018 C CB     . GLU A 1 270 ? 40.023 36.717  31.420 1.00 66.42  ?  270 GLU A CB     1 
ATOM   2019 C CG     . GLU A 1 270 ? 40.686 35.904  32.528 1.00 70.34  ?  270 GLU A CG     1 
ATOM   2020 C CD     . GLU A 1 270 ? 41.917 35.138  32.080 1.00 75.22  ?  270 GLU A CD     1 
ATOM   2021 O OE1    . GLU A 1 270 ? 42.938 35.779  31.755 1.00 73.71  ?  270 GLU A OE1    1 
ATOM   2022 O OE2    . GLU A 1 270 ? 41.866 33.888  32.070 1.00 77.84  -1 270 GLU A OE2    1 
ATOM   2023 N N      . SER A 1 271 ? 39.480 33.679  29.607 1.00 90.64  ?  271 SER A N      1 
ATOM   2024 C CA     . SER A 1 271 ? 39.018 32.349  29.778 1.00 87.79  ?  271 SER A CA     1 
ATOM   2025 C C      . SER A 1 271 ? 40.240 31.620  29.500 1.00 84.13  ?  271 SER A C      1 
ATOM   2026 O O      . SER A 1 271 ? 41.294 32.188  29.310 1.00 92.36  ?  271 SER A O      1 
ATOM   2027 C CB     . SER A 1 271 ? 38.038 31.951  28.704 1.00 86.10  ?  271 SER A CB     1 
ATOM   2028 O OG     . SER A 1 271 ? 37.334 30.793  29.099 1.00 84.24  ?  271 SER A OG     1 
ATOM   2029 N N      . CYS A 1 272 ? 40.099 30.341  29.428 1.00 53.46  ?  272 CYS A N      1 
ATOM   2030 C CA     . CYS A 1 272 ? 41.211 29.555  29.192 1.00 52.82  ?  272 CYS A CA     1 
ATOM   2031 C C      . CYS A 1 272 ? 40.904 28.977  27.879 1.00 49.32  ?  272 CYS A C      1 
ATOM   2032 O O      . CYS A 1 272 ? 39.760 28.873  27.485 1.00 44.96  ?  272 CYS A O      1 
ATOM   2033 C CB     . CYS A 1 272 ? 41.279 28.477  30.260 1.00 68.86  ?  272 CYS A CB     1 
ATOM   2034 S SG     . CYS A 1 272 ? 41.553 29.112  31.930 1.00 79.63  ?  272 CYS A SG     1 
ATOM   2035 N N      . GLY A 1 273 ? 41.944 28.592  27.190 1.00 48.66  ?  273 GLY A N      1 
ATOM   2036 C CA     . GLY A 1 273 ? 41.784 28.030  25.892 1.00 51.54  ?  273 GLY A CA     1 
ATOM   2037 C C      . GLY A 1 273 ? 41.364 26.622  25.942 1.00 49.64  ?  273 GLY A C      1 
ATOM   2038 O O      . GLY A 1 273 ? 41.522 25.992  26.951 1.00 54.33  ?  273 GLY A O      1 
ATOM   2039 N N      . ILE A 1 274 ? 40.875 26.121  24.840 1.00 32.82  ?  274 ILE A N      1 
ATOM   2040 C CA     . ILE A 1 274 ? 40.340 24.775  24.762 1.00 27.96  ?  274 ILE A CA     1 
ATOM   2041 C C      . ILE A 1 274 ? 41.308 23.720  25.232 1.00 24.21  ?  274 ILE A C      1 
ATOM   2042 O O      . ILE A 1 274 ? 40.875 22.710  25.710 1.00 22.65  ?  274 ILE A O      1 
ATOM   2043 C CB     . ILE A 1 274 ? 39.760 24.538  23.352 1.00 29.10  ?  274 ILE A CB     1 
ATOM   2044 C CG1    . ILE A 1 274 ? 40.818 24.688  22.268 1.00 28.32  ?  274 ILE A CG1    1 
ATOM   2045 C CG2    . ILE A 1 274 ? 38.603 25.480  23.088 1.00 29.64  ?  274 ILE A CG2    1 
ATOM   2046 C CD1    . ILE A 1 274 ? 40.320 24.245  20.915 1.00 24.67  ?  274 ILE A CD1    1 
ATOM   2047 N N      . HIS A 1 275 ? 42.600 23.905  25.019 1.00 19.61  ?  275 HIS A N      1 
ATOM   2048 C CA     . HIS A 1 275 ? 43.612 23.029  25.569 1.00 18.79  ?  275 HIS A CA     1 
ATOM   2049 C C      . HIS A 1 275 ? 43.721 23.052  27.055 1.00 32.41  ?  275 HIS A C      1 
ATOM   2050 O O      . HIS A 1 275 ? 43.775 22.010  27.675 1.00 36.29  ?  275 HIS A O      1 
ATOM   2051 C CB     . HIS A 1 275 ? 44.968 23.350  24.954 1.00 20.16  ?  275 HIS A CB     1 
ATOM   2052 C CG     . HIS A 1 275 ? 45.414 24.774  25.075 1.00 23.89  ?  275 HIS A CG     1 
ATOM   2053 N ND1    . HIS A 1 275 ? 44.619 25.847  24.742 1.00 24.94  ?  275 HIS A ND1    1 
ATOM   2054 C CD2    . HIS A 1 275 ? 46.608 25.293  25.435 1.00 25.62  ?  275 HIS A CD2    1 
ATOM   2055 C CE1    . HIS A 1 275 ? 45.292 26.965  24.927 1.00 21.67  ?  275 HIS A CE1    1 
ATOM   2056 N NE2    . HIS A 1 275 ? 46.504 26.657  25.341 1.00 27.11  ?  275 HIS A NE2    1 
ATOM   2057 N N      . GLU A 1 276 ? 43.737 24.239  27.642 1.00 40.40  ?  276 GLU A N      1 
ATOM   2058 C CA     . GLU A 1 276 ? 43.793 24.398  29.051 1.00 35.01  ?  276 GLU A CA     1 
ATOM   2059 C C      . GLU A 1 276 ? 42.508 23.898  29.643 1.00 39.94  ?  276 GLU A C      1 
ATOM   2060 O O      . GLU A 1 276 ? 42.536 23.351  30.705 1.00 45.50  ?  276 GLU A O      1 
ATOM   2061 C CB     . GLU A 1 276 ? 44.078 25.857  29.357 1.00 45.33  ?  276 GLU A CB     1 
ATOM   2062 C CG     . GLU A 1 276 ? 45.402 26.372  28.813 1.00 53.63  ?  276 GLU A CG     1 
ATOM   2063 C CD     . GLU A 1 276 ? 45.385 27.852  28.452 1.00 51.32  ?  276 GLU A CD     1 
ATOM   2064 O OE1    . GLU A 1 276 ? 44.317 28.383  28.129 1.00 45.06  ?  276 GLU A OE1    1 
ATOM   2065 O OE2    . GLU A 1 276 ? 46.449 28.492  28.467 1.00 53.04  -1 276 GLU A OE2    1 
ATOM   2066 N N      . THR A 1 277 ? 41.380 24.098  28.981 1.00 26.53  ?  277 THR A N      1 
ATOM   2067 C CA     . THR A 1 277 ? 40.096 23.575  29.420 1.00 22.17  ?  277 THR A CA     1 
ATOM   2068 C C      . THR A 1 277 ? 40.084 22.058  29.429 1.00 27.42  ?  277 THR A C      1 
ATOM   2069 O O      . THR A 1 277 ? 39.547 21.460  30.332 1.00 29.69  ?  277 THR A O      1 
ATOM   2070 C CB     . THR A 1 277 ? 38.968 24.133  28.560 1.00 23.75  ?  277 THR A CB     1 
ATOM   2071 O OG1    . THR A 1 277 ? 38.991 25.559  28.610 1.00 29.11  ?  277 THR A OG1    1 
ATOM   2072 C CG2    . THR A 1 277 ? 37.638 23.666  29.055 1.00 34.35  ?  277 THR A CG2    1 
ATOM   2073 N N      . THR A 1 278 ? 40.694 21.428  28.440 1.00 22.34  ?  278 THR A N      1 
ATOM   2074 C CA     . THR A 1 278 ? 40.807 19.989  28.399 1.00 19.88  ?  278 THR A CA     1 
ATOM   2075 C C      . THR A 1 278 ? 41.716 19.514  29.490 1.00 26.66  ?  278 THR A C      1 
ATOM   2076 O O      . THR A 1 278 ? 41.393 18.582  30.154 1.00 31.24  ?  278 THR A O      1 
ATOM   2077 C CB     . THR A 1 278 ? 41.321 19.484  27.041 1.00 20.27  ?  278 THR A CB     1 
ATOM   2078 O OG1    . THR A 1 278 ? 40.498 19.993  26.007 1.00 27.74  ?  278 THR A OG1    1 
ATOM   2079 C CG2    . THR A 1 278 ? 41.319 17.987  26.968 1.00 22.51  ?  278 THR A CG2    1 
ATOM   2080 N N      . PHE A 1 279 ? 42.838 20.167  29.693 1.00 18.78  ?  279 PHE A N      1 
ATOM   2081 C CA     . PHE A 1 279 ? 43.720 19.805  30.802 1.00 26.90  ?  279 PHE A CA     1 
ATOM   2082 C C      . PHE A 1 279 ? 43.000 19.973  32.137 1.00 24.70  ?  279 PHE A C      1 
ATOM   2083 O O      . PHE A 1 279 ? 43.047 19.081  32.989 1.00 23.75  ?  279 PHE A O      1 
ATOM   2084 C CB     . PHE A 1 279 ? 45.029 20.628  30.765 1.00 31.86  ?  279 PHE A CB     1 
ATOM   2085 C CG     . PHE A 1 279 ? 45.975 20.394  31.970 1.00 30.54  ?  279 PHE A CG     1 
ATOM   2086 C CD1    . PHE A 1 279 ? 46.639 19.174  32.139 1.00 26.20  ?  279 PHE A CD1    1 
ATOM   2087 C CD2    . PHE A 1 279 ? 46.208 21.413  32.909 1.00 27.94  ?  279 PHE A CD2    1 
ATOM   2088 C CE1    . PHE A 1 279 ? 47.493 18.961  33.216 1.00 24.43  ?  279 PHE A CE1    1 
ATOM   2089 C CE2    . PHE A 1 279 ? 47.079 21.214  34.000 1.00 24.67  ?  279 PHE A CE2    1 
ATOM   2090 C CZ     . PHE A 1 279 ? 47.720 19.987  34.163 1.00 23.30  ?  279 PHE A CZ     1 
ATOM   2091 N N      . ASN A 1 280 ? 42.306 21.107  32.322 1.00 24.40  ?  280 ASN A N      1 
ATOM   2092 C CA     . ASN A 1 280 ? 41.623 21.371  33.585 1.00 24.23  ?  280 ASN A CA     1 
ATOM   2093 C C      . ASN A 1 280 ? 40.490 20.383  33.833 1.00 28.83  ?  280 ASN A C      1 
ATOM   2094 O O      . ASN A 1 280 ? 40.277 19.953  34.975 1.00 27.57  ?  280 ASN A O      1 
ATOM   2095 C CB     . ASN A 1 280 ? 41.084 22.798  33.603 1.00 24.50  ?  280 ASN A CB     1 
ATOM   2096 C CG     . ASN A 1 280 ? 42.190 23.849  33.615 1.00 24.15  ?  280 ASN A CG     1 
ATOM   2097 O OD1    . ASN A 1 280 ? 43.340 23.587  33.991 1.00 26.16  ?  280 ASN A OD1    1 
ATOM   2098 N ND2    . ASN A 1 280 ? 41.843 25.042  33.166 1.00 27.53  ?  280 ASN A ND2    1 
ATOM   2099 N N      . SER A 1 281 ? 39.746 20.024  32.778 1.00 28.51  ?  281 SER A N      1 
ATOM   2100 C CA     . SER A 1 281 ? 38.731 18.980  32.886 1.00 24.18  ?  281 SER A CA     1 
ATOM   2101 C C      . SER A 1 281 ? 39.341 17.619  33.242 1.00 28.01  ?  281 SER A C      1 
ATOM   2102 O O      . SER A 1 281 ? 38.799 16.884  34.079 1.00 29.19  ?  281 SER A O      1 
ATOM   2103 C CB     . SER A 1 281 ? 37.955 18.898  31.582 1.00 26.21  ?  281 SER A CB     1 
ATOM   2104 O OG     . SER A 1 281 ? 37.419 17.609  31.413 1.00 29.71  ?  281 SER A OG     1 
ATOM   2105 N N      . ILE A 1 282 ? 40.465 17.261  32.617 1.00 25.24  ?  282 ILE A N      1 
ATOM   2106 C CA     . ILE A 1 282 ? 41.135 16.004  32.937 1.00 28.25  ?  282 ILE A CA     1 
ATOM   2107 C C      . ILE A 1 282 ? 41.655 16.009  34.377 1.00 29.07  ?  282 ILE A C      1 
ATOM   2108 O O      . ILE A 1 282 ? 41.680 14.969  35.043 1.00 21.61  ?  282 ILE A O      1 
ATOM   2109 C CB     . ILE A 1 282 ? 42.267 15.748  31.925 1.00 27.81  ?  282 ILE A CB     1 
ATOM   2110 C CG1    . ILE A 1 282 ? 41.703 15.707  30.492 1.00 24.20  ?  282 ILE A CG1    1 
ATOM   2111 C CG2    . ILE A 1 282 ? 43.000 14.461  32.255 1.00 30.59  ?  282 ILE A CG2    1 
ATOM   2112 C CD1    . ILE A 1 282 ? 42.768 15.583  29.405 1.00 22.92  ?  282 ILE A CD1    1 
ATOM   2113 N N      . MET A 1 283 ? 42.062 17.169  34.886 1.00 23.32  ?  283 MET A N      1 
ATOM   2114 C CA     . MET A 1 283 ? 42.633 17.229  36.224 1.00 26.50  ?  283 MET A CA     1 
ATOM   2115 C C      . MET A 1 283 ? 41.569 17.082  37.298 1.00 33.84  ?  283 MET A C      1 
ATOM   2116 O O      . MET A 1 283 ? 41.883 16.699  38.428 1.00 39.03  ?  283 MET A O      1 
ATOM   2117 C CB     . MET A 1 283 ? 43.397 18.550  36.415 1.00 19.61  ?  283 MET A CB     1 
ATOM   2118 C CG     . MET A 1 283 ? 44.771 18.583  35.801 1.00 23.85  ?  283 MET A CG     1 
ATOM   2119 S SD     . MET A 1 283 ? 45.903 17.363  36.441 1.00 28.86  ?  283 MET A SD     1 
ATOM   2120 C CE     . MET A 1 283 ? 45.269 15.923  35.606 1.00 33.25  ?  283 MET A CE     1 
ATOM   2121 N N      . LYS A 1 284 ? 40.316 17.357  36.950 1.00 37.43  ?  284 LYS A N      1 
ATOM   2122 C CA     . LYS A 1 284 ? 39.197 17.205  37.864 1.00 34.12  ?  284 LYS A CA     1 
ATOM   2123 C C      . LYS A 1 284 ? 38.626 15.819  37.902 1.00 28.73  ?  284 LYS A C      1 
ATOM   2124 O O      . LYS A 1 284 ? 37.569 15.616  38.449 1.00 34.73  ?  284 LYS A O      1 
ATOM   2125 C CB     . LYS A 1 284 ? 38.138 18.254  37.602 1.00 35.71  ?  284 LYS A CB     1 
ATOM   2126 C CG     . LYS A 1 284 ? 38.196 19.398  38.580 1.00 32.51  ?  284 LYS A CG     1 
ATOM   2127 C CD     . LYS A 1 284 ? 37.386 20.577  38.103 1.00 32.01  ?  284 LYS A CD     1 
ATOM   2128 C CE     . LYS A 1 284 ? 37.679 21.737  39.017 1.00 38.88  ?  284 LYS A CE     1 
ATOM   2129 N NZ     . LYS A 1 284 ? 39.102 21.652  39.432 1.00 39.26  ?  284 LYS A NZ     1 
ATOM   2130 N N      . CYS A 1 285 ? 39.285 14.875  37.274 1.00 25.90  ?  285 CYS A N      1 
ATOM   2131 C CA     . CYS A 1 285 ? 38.927 13.476  37.409 1.00 26.24  ?  285 CYS A CA     1 
ATOM   2132 C C      . CYS A 1 285 ? 39.948 12.772  38.273 1.00 27.77  ?  285 CYS A C      1 
ATOM   2133 O O      . CYS A 1 285 ? 41.057 13.265  38.519 1.00 29.46  ?  285 CYS A O      1 
ATOM   2134 C CB     . CYS A 1 285 ? 38.872 12.768  36.048 1.00 33.96  ?  285 CYS A CB     1 
ATOM   2135 S SG     . CYS A 1 285 ? 37.747 13.501  34.804 1.00 22.84  ?  285 CYS A SG     1 
ATOM   2136 N N      . ASP A 1 286 ? 39.587 11.548  38.626 1.00 30.47  ?  286 ASP A N      1 
ATOM   2137 C CA     . ASP A 1 286 ? 40.490 10.686  39.353 1.00 25.33  ?  286 ASP A CA     1 
ATOM   2138 C C      . ASP A 1 286 ? 41.805 10.572  38.589 1.00 26.80  ?  286 ASP A C      1 
ATOM   2139 O O      . ASP A 1 286 ? 41.806 10.309  37.387 1.00 30.65  ?  286 ASP A O      1 
ATOM   2140 C CB     . ASP A 1 286 ? 39.815 9.328   39.523 1.00 34.27  ?  286 ASP A CB     1 
ATOM   2141 C CG     . ASP A 1 286 ? 40.577 8.376   40.439 1.00 43.75  ?  286 ASP A CG     1 
ATOM   2142 O OD1    . ASP A 1 286 ? 41.808 8.562   40.622 1.00 42.99  ?  286 ASP A OD1    1 
ATOM   2143 O OD2    . ASP A 1 286 ? 39.927 7.417   40.948 1.00 45.12  -1 286 ASP A OD2    1 
ATOM   2144 N N      . VAL A 1 287 ? 42.930 10.755  39.294 1.00 37.06  ?  287 VAL A N      1 
ATOM   2145 C CA     . VAL A 1 287 ? 44.239 10.479  38.704 1.00 40.66  ?  287 VAL A CA     1 
ATOM   2146 C C      . VAL A 1 287 ? 44.219 9.130   37.980 1.00 43.20  ?  287 VAL A C      1 
ATOM   2147 O O      . VAL A 1 287 ? 44.847 8.973   36.924 1.00 45.19  ?  287 VAL A O      1 
ATOM   2148 C CB     . VAL A 1 287 ? 45.320 10.522  39.815 1.00 42.98  ?  287 VAL A CB     1 
ATOM   2149 C CG1    . VAL A 1 287 ? 45.263 9.244   40.625 1.00 41.54  ?  287 VAL A CG1    1 
ATOM   2150 C CG2    . VAL A 1 287 ? 46.784 10.800  39.266 1.00 36.15  ?  287 VAL A CG2    1 
ATOM   2151 N N      . ASP A 1 288 ? 43.440 8.161   38.499 1.00 34.27  ?  288 ASP A N      1 
ATOM   2152 C CA     . ASP A 1 288 ? 43.438 6.770   38.017 1.00 28.62  ?  288 ASP A CA     1 
ATOM   2153 C C      . ASP A 1 288 ? 42.881 6.609   36.602 1.00 28.77  ?  288 ASP A C      1 
ATOM   2154 O O      . ASP A 1 288 ? 43.111 5.569   35.975 1.00 27.59  ?  288 ASP A O      1 
ATOM   2155 C CB     . ASP A 1 288 ? 42.583 5.867   38.928 1.00 28.28  ?  288 ASP A CB     1 
ATOM   2156 C CG     . ASP A 1 288 ? 43.281 5.420   40.222 1.00 33.25  ?  288 ASP A CG     1 
ATOM   2157 O OD1    . ASP A 1 288 ? 44.529 5.381   40.291 1.00 31.30  ?  288 ASP A OD1    1 
ATOM   2158 O OD2    . ASP A 1 288 ? 42.540 5.064   41.179 1.00 40.19  -1 288 ASP A OD2    1 
ATOM   2159 N N      . ILE A 1 289 ? 42.007 7.517   36.154 1.00 29.21  ?  289 ILE A N      1 
ATOM   2160 C CA     . ILE A 1 289 ? 41.404 7.395   34.833 1.00 29.48  ?  289 ILE A CA     1 
ATOM   2161 C C      . ILE A 1 289 ? 42.041 8.325   33.808 1.00 32.44  ?  289 ILE A C      1 
ATOM   2162 O O      . ILE A 1 289 ? 41.609 8.340   32.634 1.00 23.03  ?  289 ILE A O      1 
ATOM   2163 C CB     . ILE A 1 289 ? 39.881 7.618   34.892 1.00 30.24  ?  289 ILE A CB     1 
ATOM   2164 C CG1    . ILE A 1 289 ? 39.558 9.000   35.458 1.00 27.91  ?  289 ILE A CG1    1 
ATOM   2165 C CG2    . ILE A 1 289 ? 39.203 6.480   35.661 1.00 24.90  ?  289 ILE A CG2    1 
ATOM   2166 C CD1    . ILE A 1 289 ? 38.134 9.367   35.357 1.00 28.59  ?  289 ILE A CD1    1 
ATOM   2167 N N      . ARG A 1 290 ? 43.054 9.099   34.212 1.00 33.53  ?  290 ARG A N      1 
ATOM   2168 C CA     . ARG A 1 290 ? 43.548 10.182  33.373 1.00 28.80  ?  290 ARG A CA     1 
ATOM   2169 C C      . ARG A 1 290 ? 44.362 9.672   32.197 1.00 31.41  ?  290 ARG A C      1 
ATOM   2170 O O      . ARG A 1 290 ? 44.280 10.242  31.103 1.00 37.75  ?  290 ARG A O      1 
ATOM   2171 C CB     . ARG A 1 290 ? 44.385 11.143  34.193 1.00 31.85  ?  290 ARG A CB     1 
ATOM   2172 C CG     . ARG A 1 290 ? 43.583 12.021  35.098 1.00 26.79  ?  290 ARG A CG     1 
ATOM   2173 C CD     . ARG A 1 290 ? 44.515 12.853  35.890 1.00 25.46  ?  290 ARG A CD     1 
ATOM   2174 N NE     . ARG A 1 290 ? 43.881 13.245  37.122 1.00 36.03  ?  290 ARG A NE     1 
ATOM   2175 C CZ     . ARG A 1 290 ? 44.512 13.837  38.123 1.00 37.80  ?  290 ARG A CZ     1 
ATOM   2176 N NH1    . ARG A 1 290 ? 45.816 14.090  38.027 1.00 39.85  ?  290 ARG A NH1    1 
ATOM   2177 N NH2    . ARG A 1 290 ? 43.833 14.170  39.208 1.00 25.71  ?  290 ARG A NH2    1 
ATOM   2178 N N      . LYS A 1 291 ? 45.192 8.644   32.394 1.00 22.33  ?  291 LYS A N      1 
ATOM   2179 C CA     . LYS A 1 291 ? 45.887 8.107   31.227 1.00 32.13  ?  291 LYS A CA     1 
ATOM   2180 C C      . LYS A 1 291 ? 44.874 7.800   30.125 1.00 37.42  ?  291 LYS A C      1 
ATOM   2181 O O      . LYS A 1 291 ? 45.090 8.132   28.950 1.00 39.40  ?  291 LYS A O      1 
ATOM   2182 C CB     . LYS A 1 291 ? 46.721 6.863   31.572 1.00 29.08  ?  291 LYS A CB     1 
ATOM   2183 C CG     . LYS A 1 291 ? 47.588 6.961   32.834 1.00 36.11  ?  291 LYS A CG     1 
ATOM   2184 C CD     . LYS A 1 291 ? 48.976 6.328   32.611 1.00 42.22  ?  291 LYS A CD     1 
ATOM   2185 C CE     . LYS A 1 291 ? 49.558 5.627   33.849 1.00 39.43  ?  291 LYS A CE     1 
ATOM   2186 N NZ     . LYS A 1 291 ? 49.108 4.202   33.992 1.00 39.52  ?  291 LYS A NZ     1 
ATOM   2187 N N      . ASP A 1 292 ? 43.749 7.218   30.485 1.00 48.65  ?  292 ASP A N      1 
ATOM   2188 C CA     . ASP A 1 292 ? 42.711 6.876   29.522 1.00 49.65  ?  292 ASP A CA     1 
ATOM   2189 C C      . ASP A 1 292 ? 42.053 8.052   28.840 1.00 48.73  ?  292 ASP A C      1 
ATOM   2190 O O      . ASP A 1 292 ? 41.690 7.941   27.689 1.00 46.97  ?  292 ASP A O      1 
ATOM   2191 C CB     . ASP A 1 292 ? 41.684 5.980   30.171 1.00 53.07  ?  292 ASP A CB     1 
ATOM   2192 C CG     . ASP A 1 292 ? 42.291 4.772   30.845 1.00 58.64  ?  292 ASP A CG     1 
ATOM   2193 O OD1    . ASP A 1 292 ? 43.176 4.939   31.706 1.00 67.16  ?  292 ASP A OD1    1 
ATOM   2194 O OD2    . ASP A 1 292 ? 41.846 3.651   30.540 1.00 54.03  -1 292 ASP A OD2    1 
ATOM   2195 N N      . LEU A 1 293 ? 41.853 9.158   29.526 1.00 31.05  ?  293 LEU A N      1 
ATOM   2196 C CA     . LEU A 1 293 ? 41.370 10.371  28.884 1.00 24.08  ?  293 LEU A CA     1 
ATOM   2197 C C      . LEU A 1 293 ? 42.446 10.976  28.004 1.00 25.77  ?  293 LEU A C      1 
ATOM   2198 O O      . LEU A 1 293 ? 42.147 11.542  26.947 1.00 24.66  ?  293 LEU A O      1 
ATOM   2199 C CB     . LEU A 1 293 ? 40.941 11.389  29.939 1.00 21.38  ?  293 LEU A CB     1 
ATOM   2200 C CG     . LEU A 1 293 ? 39.920 10.929  30.957 1.00 22.12  ?  293 LEU A CG     1 
ATOM   2201 C CD1    . LEU A 1 293 ? 39.470 12.141  31.662 1.00 26.66  ?  293 LEU A CD1    1 
ATOM   2202 C CD2    . LEU A 1 293 ? 38.748 10.204  30.314 1.00 25.19  ?  293 LEU A CD2    1 
ATOM   2203 N N      . TYR A 1 294 ? 43.698 10.935  28.470 1.00 35.00  ?  294 TYR A N      1 
ATOM   2204 C CA     . TYR A 1 294 ? 44.800 11.504  27.706 1.00 28.36  ?  294 TYR A CA     1 
ATOM   2205 C C      . TYR A 1 294 ? 45.016 10.721  26.422 1.00 33.06  ?  294 TYR A C      1 
ATOM   2206 O O      . TYR A 1 294 ? 45.487 11.276  25.424 1.00 33.41  ?  294 TYR A O      1 
ATOM   2207 C CB     . TYR A 1 294 ? 46.087 11.504  28.541 1.00 24.75  ?  294 TYR A CB     1 
ATOM   2208 C CG     . TYR A 1 294 ? 46.319 12.671  29.478 1.00 26.29  ?  294 TYR A CG     1 
ATOM   2209 C CD1    . TYR A 1 294 ? 46.409 13.974  28.990 1.00 30.40  ?  294 TYR A CD1    1 
ATOM   2210 C CD2    . TYR A 1 294 ? 46.507 12.473  30.844 1.00 28.84  ?  294 TYR A CD2    1 
ATOM   2211 C CE1    . TYR A 1 294 ? 46.646 15.061  29.829 1.00 35.92  ?  294 TYR A CE1    1 
ATOM   2212 C CE2    . TYR A 1 294 ? 46.756 13.561  31.701 1.00 36.82  ?  294 TYR A CE2    1 
ATOM   2213 C CZ     . TYR A 1 294 ? 46.824 14.855  31.180 1.00 40.21  ?  294 TYR A CZ     1 
ATOM   2214 O OH     . TYR A 1 294 ? 47.056 15.951  31.996 1.00 40.17  ?  294 TYR A OH     1 
ATOM   2215 N N      . ALA A 1 295 ? 44.690 9.426   26.441 1.00 33.97  ?  295 ALA A N      1 
ATOM   2216 C CA     . ALA A 1 295 ? 44.837 8.567   25.279 1.00 30.83  ?  295 ALA A CA     1 
ATOM   2217 C C      . ALA A 1 295 ? 43.598 8.512   24.386 1.00 32.31  ?  295 ALA A C      1 
ATOM   2218 O O      . ALA A 1 295 ? 43.703 7.995   23.256 1.00 31.44  ?  295 ALA A O      1 
ATOM   2219 C CB     . ALA A 1 295 ? 45.208 7.160   25.730 1.00 30.84  ?  295 ALA A CB     1 
ATOM   2220 N N      . ASN A 1 296 ? 42.477 9.074   24.829 1.00 24.80  ?  296 ASN A N      1 
ATOM   2221 C CA     . ASN A 1 296 ? 41.289 9.141   23.999 1.00 21.63  ?  296 ASN A CA     1 
ATOM   2222 C C      . ASN A 1 296 ? 40.539 10.475  23.970 1.00 27.16  ?  296 ASN A C      1 
ATOM   2223 O O      . ASN A 1 296 ? 39.417 10.524  24.406 1.00 31.94  ?  296 ASN A O      1 
ATOM   2224 C CB     . ASN A 1 296 ? 40.325 7.998   24.290 1.00 28.89  ?  296 ASN A CB     1 
ATOM   2225 C CG     . ASN A 1 296 ? 40.999 6.638   24.353 1.00 35.37  ?  296 ASN A CG     1 
ATOM   2226 O OD1    . ASN A 1 296 ? 41.495 6.228   25.394 1.00 30.91  ?  296 ASN A OD1    1 
ATOM   2227 N ND2    . ASN A 1 296 ? 40.999 5.929   23.247 1.00 36.64  ?  296 ASN A ND2    1 
ATOM   2228 N N      . THR A 1 297 ? 41.123 11.535  23.395 1.00 23.43  ?  297 THR A N      1 
ATOM   2229 C CA     . THR A 1 297 ? 40.494 12.854  23.378 1.00 23.85  ?  297 THR A CA     1 
ATOM   2230 C C      . THR A 1 297 ? 39.873 12.939  21.995 1.00 27.54  ?  297 THR A C      1 
ATOM   2231 O O      . THR A 1 297 ? 40.584 13.011  20.990 1.00 29.91  ?  297 THR A O      1 
ATOM   2232 C CB     . THR A 1 297 ? 41.469 14.016  23.644 1.00 28.03  ?  297 THR A CB     1 
ATOM   2233 O OG1    . THR A 1 297 ? 42.443 13.637  24.623 1.00 34.98  ?  297 THR A OG1    1 
ATOM   2234 C CG2    . THR A 1 297 ? 40.731 15.304  24.137 1.00 18.17  ?  297 THR A CG2    1 
ATOM   2235 N N      . VAL A 1 298 ? 38.552 12.877  21.956 1.00 37.66  ?  298 VAL A N      1 
ATOM   2236 C CA     . VAL A 1 298 ? 37.779 12.764  20.732 1.00 32.51  ?  298 VAL A CA     1 
ATOM   2237 C C      . VAL A 1 298 ? 37.214 14.139  20.418 1.00 25.04  ?  298 VAL A C      1 
ATOM   2238 O O      . VAL A 1 298 ? 36.513 14.717  21.252 1.00 31.38  ?  298 VAL A O      1 
ATOM   2239 C CB     . VAL A 1 298 ? 36.674 11.715  20.900 1.00 27.75  ?  298 VAL A CB     1 
ATOM   2240 C CG1    . VAL A 1 298 ? 35.693 11.761  19.745 1.00 29.37  ?  298 VAL A CG1    1 
ATOM   2241 C CG2    . VAL A 1 298 ? 37.310 10.349  21.025 1.00 27.69  ?  298 VAL A CG2    1 
ATOM   2242 N N      . LEU A 1 299 ? 37.558 14.686  19.248 1.00 25.67  ?  299 LEU A N      1 
ATOM   2243 C CA     . LEU A 1 299 ? 37.084 16.009  18.818 1.00 27.46  ?  299 LEU A CA     1 
ATOM   2244 C C      . LEU A 1 299 ? 35.740 15.866  18.086 1.00 25.12  ?  299 LEU A C      1 
ATOM   2245 O O      . LEU A 1 299 ? 35.466 14.841  17.463 1.00 31.34  ?  299 LEU A O      1 
ATOM   2246 C CB     . LEU A 1 299 ? 38.146 16.711  17.947 1.00 23.67  ?  299 LEU A CB     1 
ATOM   2247 C CG     . LEU A 1 299 ? 39.377 17.392  18.598 1.00 24.59  ?  299 LEU A CG     1 
ATOM   2248 C CD1    . LEU A 1 299 ? 40.531 17.677  17.629 1.00 26.75  ?  299 LEU A CD1    1 
ATOM   2249 C CD2    . LEU A 1 299 ? 38.992 18.679  19.256 1.00 24.43  ?  299 LEU A CD2    1 
ATOM   2250 N N      . SER A 1 300 ? 34.861 16.851  18.256 1.00 28.98  ?  300 SER A N      1 
ATOM   2251 C CA     . SER A 1 300 ? 33.483 16.724  17.794 1.00 31.07  ?  300 SER A CA     1 
ATOM   2252 C C      . SER A 1 300 ? 32.878 18.096  17.539 1.00 27.67  ?  300 SER A C      1 
ATOM   2253 O O      . SER A 1 300 ? 33.131 19.046  18.283 1.00 25.27  ?  300 SER A O      1 
ATOM   2254 C CB     . SER A 1 300 ? 32.641 15.971  18.834 1.00 32.07  ?  300 SER A CB     1 
ATOM   2255 O OG     . SER A 1 300 ? 31.295 15.887  18.430 1.00 35.44  ?  300 SER A OG     1 
ATOM   2256 N N      . GLY A 1 301 ? 32.027 18.176  16.528 1.00 30.99  ?  301 GLY A N      1 
ATOM   2257 C CA     . GLY A 1 301 ? 31.300 19.414  16.249 1.00 32.21  ?  301 GLY A CA     1 
ATOM   2258 C C      . GLY A 1 301 ? 31.954 20.300  15.205 1.00 34.52  ?  301 GLY A C      1 
ATOM   2259 O O      . GLY A 1 301 ? 33.176 20.362  15.068 1.00 36.50  ?  301 GLY A O      1 
ATOM   2260 N N      . GLY A 1 302 ? 31.190 21.039  14.438 1.00 33.33  ?  302 GLY A N      1 
ATOM   2261 C CA     . GLY A 1 302 ? 31.761 21.867  13.389 1.00 26.47  ?  302 GLY A CA     1 
ATOM   2262 C C      . GLY A 1 302 ? 32.952 22.749  13.666 1.00 23.72  ?  302 GLY A C      1 
ATOM   2263 O O      . GLY A 1 302 ? 33.780 22.874  12.817 1.00 39.31  ?  302 GLY A O      1 
ATOM   2264 N N      . THR A 1 303 ? 33.041 23.372  14.829 1.00 19.67  ?  303 THR A N      1 
ATOM   2265 C CA     . THR A 1 303 ? 34.168 24.227  15.207 1.00 21.59  ?  303 THR A CA     1 
ATOM   2266 C C      . THR A 1 303 ? 35.495 23.471  15.453 1.00 28.20  ?  303 THR A C      1 
ATOM   2267 O O      . THR A 1 303 ? 36.500 24.052  15.774 1.00 22.92  ?  303 THR A O      1 
ATOM   2268 C CB     . THR A 1 303 ? 33.749 25.193  16.335 1.00 19.73  ?  303 THR A CB     1 
ATOM   2269 O OG1    . THR A 1 303 ? 32.534 25.803  15.957 1.00 21.23  ?  303 THR A OG1    1 
ATOM   2270 C CG2    . THR A 1 303 ? 34.760 26.281  16.576 1.00 20.01  ?  303 THR A CG2    1 
ATOM   2271 N N      . THR A 1 304 ? 35.494 22.170  15.282 1.00 31.57  ?  304 THR A N      1 
ATOM   2272 C CA     . THR A 1 304 ? 36.703 21.381  15.386 1.00 29.72  ?  304 THR A CA     1 
ATOM   2273 C C      . THR A 1 304 ? 37.115 21.008  13.998 1.00 28.68  ?  304 THR A C      1 
ATOM   2274 O O      . THR A 1 304 ? 38.107 20.359  13.813 1.00 31.98  ?  304 THR A O      1 
ATOM   2275 C CB     . THR A 1 304 ? 36.496 20.065  16.216 1.00 29.21  ?  304 THR A CB     1 
ATOM   2276 O OG1    . THR A 1 304 ? 35.702 19.118  15.500 1.00 21.24  ?  304 THR A OG1    1 
ATOM   2277 C CG2    . THR A 1 304 ? 35.869 20.370  17.550 1.00 23.00  ?  304 THR A CG2    1 
ATOM   2278 N N      . MET A 1 305 ? 36.359 21.416  13.010 1.00 30.82  ?  305 MET A N      1 
ATOM   2279 C CA     . MET A 1 305 ? 36.673 20.968  11.655 1.00 39.08  ?  305 MET A CA     1 
ATOM   2280 C C      . MET A 1 305 ? 37.841 21.706  11.005 1.00 42.62  ?  305 MET A C      1 
ATOM   2281 O O      . MET A 1 305 ? 38.285 21.278  9.935  1.00 45.21  ?  305 MET A O      1 
ATOM   2282 C CB     . MET A 1 305 ? 35.433 21.086  10.770 1.00 37.72  ?  305 MET A CB     1 
ATOM   2283 C CG     . MET A 1 305 ? 34.341 20.113  11.187 1.00 39.23  ?  305 MET A CG     1 
ATOM   2284 S SD     . MET A 1 305 ? 34.902 18.424  10.981 1.00 38.95  ?  305 MET A SD     1 
ATOM   2285 C CE     . MET A 1 305 ? 34.259 18.104  9.337  1.00 43.31  ?  305 MET A CE     1 
ATOM   2286 N N      . TYR A 1 306 ? 38.348 22.780  11.612 1.00 33.19  ?  306 TYR A N      1 
ATOM   2287 C CA     . TYR A 1 306 ? 39.462 23.530  11.047 1.00 29.58  ?  306 TYR A CA     1 
ATOM   2288 C C      . TYR A 1 306 ? 40.612 22.588  10.672 1.00 34.97  ?  306 TYR A C      1 
ATOM   2289 O O      . TYR A 1 306 ? 40.959 21.699  11.462 1.00 36.07  ?  306 TYR A O      1 
ATOM   2290 C CB     . TYR A 1 306 ? 39.936 24.568  12.064 1.00 30.88  ?  306 TYR A CB     1 
ATOM   2291 C CG     . TYR A 1 306 ? 38.881 25.590  12.349 1.00 25.84  ?  306 TYR A CG     1 
ATOM   2292 C CD1    . TYR A 1 306 ? 38.726 26.686  11.514 1.00 35.11  ?  306 TYR A CD1    1 
ATOM   2293 C CD2    . TYR A 1 306 ? 38.005 25.440  13.403 1.00 23.78  ?  306 TYR A CD2    1 
ATOM   2294 C CE1    . TYR A 1 306 ? 37.737 27.620  11.730 1.00 35.21  ?  306 TYR A CE1    1 
ATOM   2295 C CE2    . TYR A 1 306 ? 36.995 26.390  13.642 1.00 27.54  ?  306 TYR A CE2    1 
ATOM   2296 C CZ     . TYR A 1 306 ? 36.873 27.476  12.797 1.00 27.72  ?  306 TYR A CZ     1 
ATOM   2297 O OH     . TYR A 1 306 ? 35.894 28.420  12.977 1.00 24.79  ?  306 TYR A OH     1 
ATOM   2298 N N      . PRO A 1 307 ? 41.194 22.716  9.475  1.00 33.73  ?  307 PRO A N      1 
ATOM   2299 C CA     . PRO A 1 307 ? 42.412 21.950  9.185  1.00 29.07  ?  307 PRO A CA     1 
ATOM   2300 C C      . PRO A 1 307 ? 43.459 22.206  10.257 1.00 27.19  ?  307 PRO A C      1 
ATOM   2301 O O      . PRO A 1 307 ? 43.657 23.338  10.691 1.00 25.19  ?  307 PRO A O      1 
ATOM   2302 C CB     . PRO A 1 307 ? 42.856 22.478  7.815  1.00 25.84  ?  307 PRO A CB     1 
ATOM   2303 C CG     . PRO A 1 307 ? 41.557 22.938  7.152  1.00 22.66  ?  307 PRO A CG     1 
ATOM   2304 C CD     . PRO A 1 307 ? 40.655 23.390  8.270  1.00 26.60  ?  307 PRO A CD     1 
ATOM   2305 N N      . GLY A 1 308 ? 44.108 21.122  10.702 1.00 26.56  ?  308 GLY A N      1 
ATOM   2306 C CA     . GLY A 1 308 ? 45.183 21.194  11.656 1.00 19.16  ?  308 GLY A CA     1 
ATOM   2307 C C      . GLY A 1 308 ? 44.803 21.426  13.105 1.00 24.86  ?  308 GLY A C      1 
ATOM   2308 O O      . GLY A 1 308 ? 45.695 21.756  13.901 1.00 23.25  ?  308 GLY A O      1 
ATOM   2309 N N      . ILE A 1 309 ? 43.519 21.246  13.477 1.00 18.94  ?  309 ILE A N      1 
ATOM   2310 C CA     . ILE A 1 309 ? 43.095 21.433  14.865 1.00 25.40  ?  309 ILE A CA     1 
ATOM   2311 C C      . ILE A 1 309 ? 43.650 20.329  15.762 1.00 23.93  ?  309 ILE A C      1 
ATOM   2312 O O      . ILE A 1 309 ? 44.043 20.598  16.905 1.00 31.37  ?  309 ILE A O      1 
ATOM   2313 C CB     . ILE A 1 309 ? 41.556 21.530  14.999 1.00 30.84  ?  309 ILE A CB     1 
ATOM   2314 C CG1    . ILE A 1 309 ? 41.207 22.139  16.359 1.00 27.36  ?  309 ILE A CG1    1 
ATOM   2315 C CG2    . ILE A 1 309 ? 40.864 20.165  14.912 1.00 18.65  ?  309 ILE A CG2    1 
ATOM   2316 C CD1    . ILE A 1 309 ? 39.754 22.080  16.680 1.00 34.38  ?  309 ILE A CD1    1 
ATOM   2317 N N      . ALA A 1 310 ? 43.734 19.094  15.253 1.00 22.39  ?  310 ALA A N      1 
ATOM   2318 C CA     . ALA A 1 310 ? 44.149 17.947  16.053 1.00 27.54  ?  310 ALA A CA     1 
ATOM   2319 C C      . ALA A 1 310 ? 45.655 17.923  16.346 1.00 31.29  ?  310 ALA A C      1 
ATOM   2320 O O      . ALA A 1 310 ? 46.083 17.359  17.360 1.00 33.51  ?  310 ALA A O      1 
ATOM   2321 C CB     . ALA A 1 310 ? 43.726 16.660  15.341 1.00 30.83  ?  310 ALA A CB     1 
ATOM   2322 N N      . ASP A 1 311 ? 46.479 18.493  15.475 1.00 31.29  ?  311 ASP A N      1 
ATOM   2323 C CA     . ASP A 1 311 ? 47.909 18.474  15.744 1.00 30.26  ?  311 ASP A CA     1 
ATOM   2324 C C      . ASP A 1 311 ? 48.279 19.508  16.792 1.00 33.81  ?  311 ASP A C      1 
ATOM   2325 O O      . ASP A 1 311 ? 49.109 19.237  17.673 1.00 30.41  ?  311 ASP A O      1 
ATOM   2326 C CB     . ASP A 1 311 ? 48.691 18.736  14.455 1.00 31.84  ?  311 ASP A CB     1 
ATOM   2327 C CG     . ASP A 1 311 ? 48.789 17.519  13.557 1.00 40.64  ?  311 ASP A CG     1 
ATOM   2328 O OD1    . ASP A 1 311 ? 48.797 16.381  14.080 1.00 47.04  ?  311 ASP A OD1    1 
ATOM   2329 O OD2    . ASP A 1 311 ? 48.865 17.705  12.318 1.00 41.27  -1 311 ASP A OD2    1 
ATOM   2330 N N      . ARG A 1 312 ? 47.686 20.709  16.662 1.00 27.61  ?  312 ARG A N      1 
ATOM   2331 C CA     . ARG A 1 312 ? 47.899 21.808  17.598 1.00 24.12  ?  312 ARG A CA     1 
ATOM   2332 C C      . ARG A 1 312 ? 47.534 21.401  19.013 1.00 25.77  ?  312 ARG A C      1 
ATOM   2333 O O      . ARG A 1 312 ? 48.227 21.753  19.969 1.00 26.32  ?  312 ARG A O      1 
ATOM   2334 C CB     . ARG A 1 312 ? 47.053 22.996  17.160 1.00 19.21  ?  312 ARG A CB     1 
ATOM   2335 C CG     . ARG A 1 312 ? 47.101 24.175  18.098 1.00 22.15  ?  312 ARG A CG     1 
ATOM   2336 C CD     . ARG A 1 312 ? 48.472 24.799  18.215 1.00 19.53  ?  312 ARG A CD     1 
ATOM   2337 N NE     . ARG A 1 312 ? 48.388 25.769  19.289 1.00 20.42  ?  312 ARG A NE     1 
ATOM   2338 C CZ     . ARG A 1 312 ? 47.969 27.018  19.161 1.00 23.82  ?  312 ARG A CZ     1 
ATOM   2339 N NH1    . ARG A 1 312 ? 47.623 27.521  17.980 1.00 23.98  ?  312 ARG A NH1    1 
ATOM   2340 N NH2    . ARG A 1 312 ? 47.925 27.781  20.234 1.00 33.42  ?  312 ARG A NH2    1 
ATOM   2341 N N      . MET A 1 313 ? 46.419 20.682  19.147 1.00 28.43  ?  313 MET A N      1 
ATOM   2342 C CA     . MET A 1 313 ? 45.944 20.143  20.408 1.00 30.26  ?  313 MET A CA     1 
ATOM   2343 C C      . MET A 1 313 ? 46.847 19.030  20.919 1.00 29.36  ?  313 MET A C      1 
ATOM   2344 O O      . MET A 1 313 ? 47.013 18.863  22.130 1.00 31.51  ?  313 MET A O      1 
ATOM   2345 C CB     . MET A 1 313 ? 44.507 19.637  20.214 1.00 33.77  ?  313 MET A CB     1 
ATOM   2346 C CG     . MET A 1 313 ? 43.701 19.518  21.496 1.00 38.88  ?  313 MET A CG     1 
ATOM   2347 S SD     . MET A 1 313 ? 43.142 21.097  22.187 1.00 42.38  ?  313 MET A SD     1 
ATOM   2348 C CE     . MET A 1 313 ? 42.559 20.567  23.797 1.00 44.95  ?  313 MET A CE     1 
ATOM   2349 N N      . GLN A 1 314 ? 47.398 18.227  20.018 1.00 35.51  ?  314 GLN A N      1 
ATOM   2350 C CA     . GLN A 1 314 ? 48.426 17.279  20.413 1.00 29.39  ?  314 GLN A CA     1 
ATOM   2351 C C      . GLN A 1 314 ? 49.666 18.019  20.888 1.00 33.52  ?  314 GLN A C      1 
ATOM   2352 O O      . GLN A 1 314 ? 50.315 17.601  21.850 1.00 40.12  ?  314 GLN A O      1 
ATOM   2353 C CB     . GLN A 1 314 ? 48.746 16.350  19.237 1.00 33.48  ?  314 GLN A CB     1 
ATOM   2354 C CG     . GLN A 1 314 ? 49.919 15.409  19.458 1.00 35.82  ?  314 GLN A CG     1 
ATOM   2355 C CD     . GLN A 1 314 ? 49.599 14.312  20.468 1.00 43.88  ?  314 GLN A CD     1 
ATOM   2356 O OE1    . GLN A 1 314 ? 48.448 14.166  20.940 1.00 40.42  ?  314 GLN A OE1    1 
ATOM   2357 N NE2    . GLN A 1 314 ? 50.621 13.533  20.815 1.00 42.61  ?  314 GLN A NE2    1 
ATOM   2358 N N      . LYS A 1 315 ? 49.986 19.143  20.246 1.00 20.47  ?  315 LYS A N      1 
ATOM   2359 C CA     . LYS A 1 315 ? 51.113 19.951  20.693 1.00 21.07  ?  315 LYS A CA     1 
ATOM   2360 C C      . LYS A 1 315 ? 50.857 20.513  22.090 1.00 25.25  ?  315 LYS A C      1 
ATOM   2361 O O      . LYS A 1 315 ? 51.716 20.417  22.974 1.00 28.97  ?  315 LYS A O      1 
ATOM   2362 C CB     . LYS A 1 315 ? 51.387 21.075  19.677 1.00 20.50  ?  315 LYS A CB     1 
ATOM   2363 C CG     . LYS A 1 315 ? 52.783 21.704  19.779 1.00 19.81  ?  315 LYS A CG     1 
ATOM   2364 C CD     . LYS A 1 315 ? 53.066 22.738  18.676 1.00 19.96  ?  315 LYS A CD     1 
ATOM   2365 C CE     . LYS A 1 315 ? 54.546 22.597  18.160 1.00 27.03  ?  315 LYS A CE     1 
ATOM   2366 N NZ     . LYS A 1 315 ? 55.035 23.535  17.029 1.00 27.54  ?  315 LYS A NZ     1 
ATOM   2367 N N      . GLU A 1 316 ? 49.655 21.077  22.312 1.00 28.02  ?  316 GLU A N      1 
ATOM   2368 C CA     . GLU A 1 316 ? 49.336 21.855  23.516 1.00 32.11  ?  316 GLU A CA     1 
ATOM   2369 C C      . GLU A 1 316 ? 49.053 20.979  24.735 1.00 31.12  ?  316 GLU A C      1 
ATOM   2370 O O      . GLU A 1 316 ? 49.468 21.328  25.842 1.00 27.38  ?  316 GLU A O      1 
ATOM   2371 C CB     . GLU A 1 316 ? 48.130 22.766  23.266 1.00 34.68  ?  316 GLU A CB     1 
ATOM   2372 C CG     . GLU A 1 316 ? 48.388 23.933  22.336 1.00 34.83  ?  316 GLU A CG     1 
ATOM   2373 C CD     . GLU A 1 316 ? 49.486 24.840  22.841 1.00 42.77  ?  316 GLU A CD     1 
ATOM   2374 O OE1    . GLU A 1 316 ? 49.971 24.601  23.978 1.00 39.39  ?  316 GLU A OE1    1 
ATOM   2375 O OE2    . GLU A 1 316 ? 49.862 25.781  22.096 1.00 49.61  -1 316 GLU A OE2    1 
ATOM   2376 N N      . ILE A 1 317 ? 48.332 19.860  24.558 1.00 32.88  ?  317 ILE A N      1 
ATOM   2377 C CA     . ILE A 1 317 ? 48.121 18.934  25.665 1.00 34.57  ?  317 ILE A CA     1 
ATOM   2378 C C      . ILE A 1 317 ? 49.430 18.239  26.045 1.00 36.05  ?  317 ILE A C      1 
ATOM   2379 O O      . ILE A 1 317 ? 49.669 17.951  27.219 1.00 35.03  ?  317 ILE A O      1 
ATOM   2380 C CB     . ILE A 1 317 ? 47.024 17.900  25.339 1.00 35.28  ?  317 ILE A CB     1 
ATOM   2381 C CG1    . ILE A 1 317 ? 45.637 18.546  25.319 1.00 34.85  ?  317 ILE A CG1    1 
ATOM   2382 C CG2    . ILE A 1 317 ? 47.041 16.789  26.371 1.00 37.35  ?  317 ILE A CG2    1 
ATOM   2383 C CD1    . ILE A 1 317 ? 45.548 19.802  26.146 1.00 39.33  ?  317 ILE A CD1    1 
ATOM   2384 N N      . THR A 1 318 ? 50.293 17.944  25.078 1.00 25.79  ?  318 THR A N      1 
ATOM   2385 C CA     . THR A 1 318 ? 51.595 17.410  25.442 1.00 21.06  ?  318 THR A CA     1 
ATOM   2386 C C      . THR A 1 318 ? 52.414 18.431  26.232 1.00 26.70  ?  318 THR A C      1 
ATOM   2387 O O      . THR A 1 318 ? 53.150 18.067  27.151 1.00 26.03  ?  318 THR A O      1 
ATOM   2388 C CB     . THR A 1 318 ? 52.351 16.963  24.199 1.00 22.56  ?  318 THR A CB     1 
ATOM   2389 O OG1    . THR A 1 318 ? 51.883 15.667  23.799 1.00 30.82  ?  318 THR A OG1    1 
ATOM   2390 C CG2    . THR A 1 318 ? 53.832 16.879  24.503 1.00 23.78  ?  318 THR A CG2    1 
ATOM   2391 N N      . ALA A 1 319 ? 52.299 19.713  25.889 1.00 30.91  ?  319 ALA A N      1 
ATOM   2392 C CA     . ALA A 1 319 ? 53.019 20.743  26.619 1.00 29.95  ?  319 ALA A CA     1 
ATOM   2393 C C      . ALA A 1 319 ? 52.494 20.908  28.033 1.00 34.17  ?  319 ALA A C      1 
ATOM   2394 O O      . ALA A 1 319 ? 53.215 21.420  28.887 1.00 36.97  ?  319 ALA A O      1 
ATOM   2395 C CB     . ALA A 1 319 ? 52.910 22.085  25.891 1.00 27.48  ?  319 ALA A CB     1 
ATOM   2396 N N      . LEU A 1 320 ? 51.205 20.615  28.249 1.00 38.24  ?  320 LEU A N      1 
ATOM   2397 C CA     . LEU A 1 320 ? 50.490 20.647  29.526 1.00 37.37  ?  320 LEU A CA     1 
ATOM   2398 C C      . LEU A 1 320 ? 50.572 19.344  30.340 1.00 36.56  ?  320 LEU A C      1 
ATOM   2399 O O      . LEU A 1 320 ? 50.587 19.379  31.582 1.00 29.41  ?  320 LEU A O      1 
ATOM   2400 C CB     . LEU A 1 320 ? 49.019 21.008  29.275 1.00 31.92  ?  320 LEU A CB     1 
ATOM   2401 C CG     . LEU A 1 320 ? 48.692 22.350  28.615 1.00 26.90  ?  320 LEU A CG     1 
ATOM   2402 C CD1    . LEU A 1 320 ? 47.214 22.567  28.595 1.00 25.61  ?  320 LEU A CD1    1 
ATOM   2403 C CD2    . LEU A 1 320 ? 49.380 23.526  29.306 1.00 31.69  ?  320 LEU A CD2    1 
ATOM   2404 N N      . ALA A 1 321 ? 50.544 18.190  29.682 1.00 30.71  ?  321 ALA A N      1 
ATOM   2405 C CA     . ALA A 1 321 ? 50.490 16.928  30.393 1.00 26.99  ?  321 ALA A CA     1 
ATOM   2406 C C      . ALA A 1 321 ? 51.892 16.589  30.831 1.00 32.95  ?  321 ALA A C      1 
ATOM   2407 O O      . ALA A 1 321 ? 52.841 17.303  30.502 1.00 32.90  ?  321 ALA A O      1 
ATOM   2408 C CB     . ALA A 1 321 ? 49.906 15.829  29.512 1.00 23.59  ?  321 ALA A CB     1 
ATOM   2409 N N      . PRO A 1 322 ? 52.053 15.510  31.588 1.00 49.95  ?  322 PRO A N      1 
ATOM   2410 C CA     . PRO A 1 322 ? 53.403 15.053  31.935 1.00 48.24  ?  322 PRO A CA     1 
ATOM   2411 C C      . PRO A 1 322 ? 54.179 14.625  30.699 1.00 49.74  ?  322 PRO A C      1 
ATOM   2412 O O      . PRO A 1 322 ? 53.650 14.474  29.589 1.00 49.25  ?  322 PRO A O      1 
ATOM   2413 C CB     . PRO A 1 322 ? 53.143 13.884  32.895 1.00 44.55  ?  322 PRO A CB     1 
ATOM   2414 C CG     . PRO A 1 322 ? 51.854 14.336  33.612 1.00 40.87  ?  322 PRO A CG     1 
ATOM   2415 C CD     . PRO A 1 322 ? 51.029 14.985  32.516 1.00 43.80  ?  322 PRO A CD     1 
ATOM   2416 N N      . SER A 1 323 ? 55.490 14.491  30.910 1.00 48.66  ?  323 SER A N      1 
ATOM   2417 C CA     . SER A 1 323 ? 56.373 14.020  29.859 1.00 49.89  ?  323 SER A CA     1 
ATOM   2418 C C      . SER A 1 323 ? 56.088 12.574  29.503 1.00 48.62  ?  323 SER A C      1 
ATOM   2419 O O      . SER A 1 323 ? 56.221 12.184  28.338 1.00 57.45  ?  323 SER A O      1 
ATOM   2420 C CB     . SER A 1 323 ? 57.828 14.176  30.292 1.00 60.67  ?  323 SER A CB     1 
ATOM   2421 O OG     . SER A 1 323 ? 58.169 13.197  31.260 1.00 66.01  ?  323 SER A OG     1 
ATOM   2422 N N      . THR A 1 324 ? 55.676 11.798  30.457 1.00 45.88  ?  324 THR A N      1 
ATOM   2423 C CA     . THR A 1 324 ? 55.469 10.416  30.161 1.00 55.09  ?  324 THR A CA     1 
ATOM   2424 C C      . THR A 1 324 ? 54.086 10.084  29.574 1.00 60.28  ?  324 THR A C      1 
ATOM   2425 O O      . THR A 1 324 ? 53.911 8.995   29.062 1.00 61.55  ?  324 THR A O      1 
ATOM   2426 C CB     . THR A 1 324 ? 55.836 9.598   31.414 1.00 54.29  ?  324 THR A CB     1 
ATOM   2427 O OG1    . THR A 1 324 ? 55.610 8.206   31.174 1.00 51.92  ?  324 THR A OG1    1 
ATOM   2428 C CG2    . THR A 1 324 ? 55.037 10.062  32.613 1.00 52.69  ?  324 THR A CG2    1 
ATOM   2429 N N      . MET A 1 325 ? 53.134 11.018  29.577 1.00 55.13  ?  325 MET A N      1 
ATOM   2430 C CA     . MET A 1 325 ? 51.766 10.731  29.151 1.00 48.73  ?  325 MET A CA     1 
ATOM   2431 C C      . MET A 1 325 ? 51.676 10.343  27.680 1.00 47.66  ?  325 MET A C      1 
ATOM   2432 O O      . MET A 1 325 ? 52.139 11.073  26.799 1.00 54.91  ?  325 MET A O      1 
ATOM   2433 C CB     . MET A 1 325 ? 50.881 11.947  29.393 1.00 49.78  ?  325 MET A CB     1 
ATOM   2434 C CG     . MET A 1 325 ? 50.055 11.850  30.626 1.00 53.20  ?  325 MET A CG     1 
ATOM   2435 S SD     . MET A 1 325 ? 49.023 10.384  30.628 1.00 53.61  ?  325 MET A SD     1 
ATOM   2436 C CE     . MET A 1 325 ? 48.588 10.385  32.371 1.00 53.75  ?  325 MET A CE     1 
ATOM   2437 N N      . LYS A 1 326 ? 51.046 9.206   27.412 1.00 27.92  ?  326 LYS A N      1 
ATOM   2438 C CA     . LYS A 1 326 ? 50.577 8.939   26.067 1.00 31.16  ?  326 LYS A CA     1 
ATOM   2439 C C      . LYS A 1 326 ? 49.392 9.864   25.770 1.00 31.70  ?  326 LYS A C      1 
ATOM   2440 O O      . LYS A 1 326 ? 48.435 9.932   26.546 1.00 33.20  ?  326 LYS A O      1 
ATOM   2441 C CB     . LYS A 1 326 ? 50.202 7.461   25.922 1.00 34.85  ?  326 LYS A CB     1 
ATOM   2442 C CG     . LYS A 1 326 ? 50.355 6.899   24.505 1.00 34.73  ?  326 LYS A CG     1 
ATOM   2443 C CD     . LYS A 1 326 ? 49.471 5.665   24.301 1.00 40.48  ?  326 LYS A CD     1 
ATOM   2444 C CE     . LYS A 1 326 ? 49.841 4.865   23.046 1.00 43.12  ?  326 LYS A CE     1 
ATOM   2445 N NZ     . LYS A 1 326 ? 51.069 4.019   23.201 1.00 42.62  ?  326 LYS A NZ     1 
ATOM   2446 N N      . ILE A 1 327 ? 49.477 10.605  24.669 1.00 21.76  ?  327 ILE A N      1 
ATOM   2447 C CA     . ILE A 1 327 ? 48.505 11.634  24.315 1.00 27.10  ?  327 ILE A CA     1 
ATOM   2448 C C      . ILE A 1 327 ? 47.988 11.310  22.910 1.00 31.48  ?  327 ILE A C      1 
ATOM   2449 O O      . ILE A 1 327 ? 48.734 11.393  21.925 1.00 23.68  ?  327 ILE A O      1 
ATOM   2450 C CB     . ILE A 1 327 ? 49.117 13.047  24.369 1.00 26.06  ?  327 ILE A CB     1 
ATOM   2451 C CG1    . ILE A 1 327 ? 49.700 13.337  25.744 1.00 22.76  ?  327 ILE A CG1    1 
ATOM   2452 C CG2    . ILE A 1 327 ? 48.093 14.158  23.925 1.00 20.18  ?  327 ILE A CG2    1 
ATOM   2453 C CD1    . ILE A 1 327 ? 48.671 13.824  26.678 1.00 28.05  ?  327 ILE A CD1    1 
ATOM   2454 N N      . LYS A 1 328 ? 46.715 10.951  22.807 1.00 35.74  ?  328 LYS A N      1 
ATOM   2455 C CA     . LYS A 1 328 ? 46.096 10.739  21.510 1.00 35.83  ?  328 LYS A CA     1 
ATOM   2456 C C      . LYS A 1 328 ? 44.949 11.724  21.366 1.00 32.88  ?  328 LYS A C      1 
ATOM   2457 O O      . LYS A 1 328 ? 44.043 11.752  22.207 1.00 36.49  ?  328 LYS A O      1 
ATOM   2458 C CB     . LYS A 1 328 ? 45.620 9.292   21.352 1.00 39.85  ?  328 LYS A CB     1 
ATOM   2459 C CG     . LYS A 1 328 ? 45.362 8.897   19.912 1.00 38.38  ?  328 LYS A CG     1 
ATOM   2460 C CD     . LYS A 1 328 ? 45.428 7.399   19.743 1.00 39.11  ?  328 LYS A CD     1 
ATOM   2461 C CE     . LYS A 1 328 ? 44.988 6.995   18.341 1.00 44.74  ?  328 LYS A CE     1 
ATOM   2462 N NZ     . LYS A 1 328 ? 45.061 5.521   18.098 1.00 41.87  ?  328 LYS A NZ     1 
ATOM   2463 N N      . ILE A 1 329 ? 45.023 12.565  20.338 1.00 26.84  ?  329 ILE A N      1 
ATOM   2464 C CA     . ILE A 1 329 ? 43.868 13.305  19.831 1.00 33.47  ?  329 ILE A CA     1 
ATOM   2465 C C      . ILE A 1 329 ? 43.224 12.457  18.737 1.00 31.32  ?  329 ILE A C      1 
ATOM   2466 O O      . ILE A 1 329 ? 43.904 12.004  17.816 1.00 34.67  ?  329 ILE A O      1 
ATOM   2467 C CB     . ILE A 1 329 ? 44.264 14.688  19.281 1.00 31.69  ?  329 ILE A CB     1 
ATOM   2468 C CG1    . ILE A 1 329 ? 45.098 15.478  20.293 1.00 19.19  ?  329 ILE A CG1    1 
ATOM   2469 C CG2    . ILE A 1 329 ? 43.014 15.441  18.827 1.00 32.81  ?  329 ILE A CG2    1 
ATOM   2470 C CD1    . ILE A 1 329 ? 44.754 15.137  21.724 1.00 18.68  ?  329 ILE A CD1    1 
ATOM   2471 N N      . ILE A 1 330 ? 41.927 12.212  18.848 1.00 36.13  ?  330 ILE A N      1 
ATOM   2472 C CA     . ILE A 1 330 ? 41.178 11.511  17.820 1.00 37.10  ?  330 ILE A CA     1 
ATOM   2473 C C      . ILE A 1 330 ? 40.231 12.526  17.206 1.00 41.96  ?  330 ILE A C      1 
ATOM   2474 O O      . ILE A 1 330 ? 39.394 13.108  17.907 1.00 51.09  ?  330 ILE A O      1 
ATOM   2475 C CB     . ILE A 1 330 ? 40.432 10.299  18.385 1.00 33.54  ?  330 ILE A CB     1 
ATOM   2476 C CG1    . ILE A 1 330 ? 41.420 9.242   18.900 1.00 34.78  ?  330 ILE A CG1    1 
ATOM   2477 C CG2    . ILE A 1 330 ? 39.576 9.670   17.326 1.00 32.70  ?  330 ILE A CG2    1 
ATOM   2478 C CD1    . ILE A 1 330 ? 42.114 9.605   20.182 1.00 36.66  ?  330 ILE A CD1    1 
ATOM   2479 N N      . ALA A 1 331 ? 40.410 12.794  15.912 1.00 25.90  ?  331 ALA A N      1 
ATOM   2480 C CA     . ALA A 1 331 ? 39.653 13.827  15.201 1.00 27.54  ?  331 ALA A CA     1 
ATOM   2481 C C      . ALA A 1 331 ? 39.096 13.163  13.953 1.00 29.33  ?  331 ALA A C      1 
ATOM   2482 O O      . ALA A 1 331 ? 39.704 13.217  12.878 1.00 27.65  ?  331 ALA A O      1 
ATOM   2483 C CB     . ALA A 1 331 ? 40.516 15.051  14.881 1.00 18.91  ?  331 ALA A CB     1 
ATOM   2484 N N      . PRO A 1 332 ? 37.950 12.498  14.070 1.00 28.81  ?  332 PRO A N      1 
ATOM   2485 C CA     . PRO A 1 332 ? 37.426 11.678  12.975 1.00 28.35  ?  332 PRO A CA     1 
ATOM   2486 C C      . PRO A 1 332 ? 36.917 12.551  11.842 1.00 36.28  ?  332 PRO A C      1 
ATOM   2487 O O      . PRO A 1 332 ? 36.301 13.593  12.100 1.00 35.73  ?  332 PRO A O      1 
ATOM   2488 C CB     . PRO A 1 332 ? 36.276 10.922  13.650 1.00 21.06  ?  332 PRO A CB     1 
ATOM   2489 C CG     . PRO A 1 332 ? 36.579 11.036  15.102 1.00 18.62  ?  332 PRO A CG     1 
ATOM   2490 C CD     . PRO A 1 332 ? 37.106 12.395  15.258 1.00 18.75  ?  332 PRO A CD     1 
ATOM   2491 N N      . PRO A 1 333 ? 37.145 12.177  10.577 1.00 50.23  ?  333 PRO A N      1 
ATOM   2492 C CA     . PRO A 1 333 ? 36.714 13.065  9.480  1.00 51.02  ?  333 PRO A CA     1 
ATOM   2493 C C      . PRO A 1 333 ? 35.227 13.404  9.534  1.00 47.84  ?  333 PRO A C      1 
ATOM   2494 O O      . PRO A 1 333 ? 34.815 14.479  9.060  1.00 47.43  ?  333 PRO A O      1 
ATOM   2495 C CB     . PRO A 1 333 ? 37.087 12.269  8.219  1.00 51.81  ?  333 PRO A CB     1 
ATOM   2496 C CG     . PRO A 1 333 ? 38.198 11.380  8.653  1.00 49.78  ?  333 PRO A CG     1 
ATOM   2497 C CD     . PRO A 1 333 ? 37.851 10.985  10.074 1.00 50.59  ?  333 PRO A CD     1 
ATOM   2498 N N      . GLU A 1 334 ? 34.419 12.539  10.149 1.00 31.43  ?  334 GLU A N      1 
ATOM   2499 C CA     . GLU A 1 334 ? 32.971 12.704  10.224 1.00 32.45  ?  334 GLU A CA     1 
ATOM   2500 C C      . GLU A 1 334 ? 32.503 13.461  11.467 1.00 31.63  ?  334 GLU A C      1 
ATOM   2501 O O      . GLU A 1 334 ? 31.295 13.537  11.707 1.00 36.18  ?  334 GLU A O      1 
ATOM   2502 C CB     . GLU A 1 334 ? 32.287 11.336  10.161 1.00 39.87  ?  334 GLU A CB     1 
ATOM   2503 C CG     . GLU A 1 334 ? 32.609 10.411  11.342 1.00 49.42  ?  334 GLU A CG     1 
ATOM   2504 C CD     . GLU A 1 334 ? 33.732 9.414   11.054 1.00 53.77  ?  334 GLU A CD     1 
ATOM   2505 O OE1    . GLU A 1 334 ? 34.443 9.571   10.031 1.00 56.39  ?  334 GLU A OE1    1 
ATOM   2506 O OE2    . GLU A 1 334 ? 33.902 8.469   11.858 1.00 49.10  -1 334 GLU A OE2    1 
ATOM   2507 N N      . ARG A 1 335 ? 33.426 14.016  12.258 1.00 31.06  ?  335 ARG A N      1 
ATOM   2508 C CA     . ARG A 1 335 ? 33.111 14.576  13.566 1.00 33.21  ?  335 ARG A CA     1 
ATOM   2509 C C      . ARG A 1 335 ? 32.130 15.753  13.514 1.00 37.67  ?  335 ARG A C      1 
ATOM   2510 O O      . ARG A 1 335 ? 31.571 16.100  14.558 1.00 31.91  ?  335 ARG A O      1 
ATOM   2511 C CB     . ARG A 1 335 ? 34.418 14.956  14.299 1.00 30.79  ?  335 ARG A CB     1 
ATOM   2512 C CG     . ARG A 1 335 ? 35.154 16.240  13.900 1.00 19.58  ?  335 ARG A CG     1 
ATOM   2513 C CD     . ARG A 1 335 ? 36.670 16.059  14.159 1.00 26.67  ?  335 ARG A CD     1 
ATOM   2514 N NE     . ARG A 1 335 ? 37.494 17.155  13.627 1.00 36.30  ?  335 ARG A NE     1 
ATOM   2515 C CZ     . ARG A 1 335 ? 38.137 17.149  12.446 1.00 36.35  ?  335 ARG A CZ     1 
ATOM   2516 N NH1    . ARG A 1 335 ? 38.072 16.111  11.633 1.00 26.96  ?  335 ARG A NH1    1 
ATOM   2517 N NH2    . ARG A 1 335 ? 38.851 18.203  12.061 1.00 38.06  ?  335 ARG A NH2    1 
ATOM   2518 N N      . LYS A 1 336 ? 31.855 16.335  12.343 1.00 44.46  ?  336 LYS A N      1 
ATOM   2519 C CA     . LYS A 1 336 ? 30.849 17.398  12.282 1.00 44.58  ?  336 LYS A CA     1 
ATOM   2520 C C      . LYS A 1 336 ? 29.488 16.915  12.782 1.00 39.81  ?  336 LYS A C      1 
ATOM   2521 O O      . LYS A 1 336 ? 28.808 17.609  13.542 1.00 46.18  ?  336 LYS A O      1 
ATOM   2522 C CB     . LYS A 1 336 ? 30.736 17.940  10.858 1.00 41.80  ?  336 LYS A CB     1 
ATOM   2523 C CG     . LYS A 1 336 ? 30.021 19.279  10.804 1.00 40.10  ?  336 LYS A CG     1 
ATOM   2524 C CD     . LYS A 1 336 ? 30.362 20.043  9.534  1.00 35.44  ?  336 LYS A CD     1 
ATOM   2525 C CE     . LYS A 1 336 ? 29.185 20.116  8.595  1.00 33.19  ?  336 LYS A CE     1 
ATOM   2526 N NZ     . LYS A 1 336 ? 29.672 20.272  7.198  1.00 41.51  ?  336 LYS A NZ     1 
ATOM   2527 N N      . TYR A 1 337 ? 29.045 15.759  12.298 1.00 38.16  ?  337 TYR A N      1 
ATOM   2528 C CA     . TYR A 1 337 ? 27.809 15.087  12.694 1.00 40.50  ?  337 TYR A CA     1 
ATOM   2529 C C      . TYR A 1 337 ? 28.038 13.950  13.682 1.00 33.57  ?  337 TYR A C      1 
ATOM   2530 O O      . TYR A 1 337 ? 27.213 13.036  13.733 1.00 30.30  ?  337 TYR A O      1 
ATOM   2531 C CB     . TYR A 1 337 ? 27.050 14.594  11.460 1.00 41.91  ?  337 TYR A CB     1 
ATOM   2532 C CG     . TYR A 1 337 ? 26.788 15.757  10.552 1.00 38.21  ?  337 TYR A CG     1 
ATOM   2533 C CD1    . TYR A 1 337 ? 26.380 16.974  11.095 1.00 26.43  ?  337 TYR A CD1    1 
ATOM   2534 C CD2    . TYR A 1 337 ? 27.055 15.686  9.173  1.00 39.18  ?  337 TYR A CD2    1 
ATOM   2535 C CE1    . TYR A 1 337 ? 26.186 18.062  10.306 1.00 31.48  ?  337 TYR A CE1    1 
ATOM   2536 C CE2    . TYR A 1 337 ? 26.852 16.789  8.356  1.00 32.74  ?  337 TYR A CE2    1 
ATOM   2537 C CZ     . TYR A 1 337 ? 26.407 17.972  8.937  1.00 36.37  ?  337 TYR A CZ     1 
ATOM   2538 O OH     . TYR A 1 337 ? 26.189 19.100  8.186  1.00 45.92  ?  337 TYR A OH     1 
ATOM   2539 N N      . SER A 1 338 ? 29.214 13.904  14.322 1.00 32.17  ?  338 SER A N      1 
ATOM   2540 C CA     . SER A 1 338 ? 29.520 12.860  15.305 1.00 35.38  ?  338 SER A CA     1 
ATOM   2541 C C      . SER A 1 338 ? 28.377 12.645  16.299 1.00 33.98  ?  338 SER A C      1 
ATOM   2542 O O      . SER A 1 338 ? 28.032 11.502  16.610 1.00 37.29  ?  338 SER A O      1 
ATOM   2543 C CB     . SER A 1 338 ? 30.796 13.202  16.079 1.00 38.00  ?  338 SER A CB     1 
ATOM   2544 O OG     . SER A 1 338 ? 31.957 12.855  15.358 1.00 49.27  ?  338 SER A OG     1 
ATOM   2545 N N      . VAL A 1 339 ? 27.811 13.722  16.852 1.00 19.81  ?  339 VAL A N      1 
ATOM   2546 C CA     . VAL A 1 339 ? 26.762 13.522  17.846 1.00 18.69  ?  339 VAL A CA     1 
ATOM   2547 C C      . VAL A 1 339 ? 25.627 12.736  17.212 1.00 21.61  ?  339 VAL A C      1 
ATOM   2548 O O      . VAL A 1 339 ? 25.224 11.673  17.702 1.00 25.50  ?  339 VAL A O      1 
ATOM   2549 C CB     . VAL A 1 339 ? 26.256 14.865  18.424 1.00 19.93  ?  339 VAL A CB     1 
ATOM   2550 C CG1    . VAL A 1 339 ? 25.193 14.625  19.463 1.00 18.71  ?  339 VAL A CG1    1 
ATOM   2551 C CG2    . VAL A 1 339 ? 27.349 15.724  19.000 1.00 18.55  ?  339 VAL A CG2    1 
ATOM   2552 N N      . TRP A 1 340 ? 25.129 13.237  16.075 1.00 24.62  ?  340 TRP A N      1 
ATOM   2553 C CA     . TRP A 1 340 ? 24.013 12.602  15.379 1.00 22.74  ?  340 TRP A CA     1 
ATOM   2554 C C      . TRP A 1 340 ? 24.341 11.165  14.967 1.00 23.11  ?  340 TRP A C      1 
ATOM   2555 O O      . TRP A 1 340 ? 23.496 10.265  15.093 1.00 25.09  ?  340 TRP A O      1 
ATOM   2556 C CB     . TRP A 1 340 ? 23.615 13.439  14.156 1.00 25.22  ?  340 TRP A CB     1 
ATOM   2557 C CG     . TRP A 1 340 ? 22.335 12.972  13.611 1.00 30.52  ?  340 TRP A CG     1 
ATOM   2558 C CD1    . TRP A 1 340 ? 21.090 13.404  13.958 1.00 29.96  ?  340 TRP A CD1    1 
ATOM   2559 C CD2    . TRP A 1 340 ? 22.146 11.916  12.671 1.00 28.79  ?  340 TRP A CD2    1 
ATOM   2560 N NE1    . TRP A 1 340 ? 20.137 12.689  13.290 1.00 28.36  ?  340 TRP A NE1    1 
ATOM   2561 C CE2    . TRP A 1 340 ? 20.756 11.774  12.482 1.00 26.88  ?  340 TRP A CE2    1 
ATOM   2562 C CE3    . TRP A 1 340 ? 23.016 11.094  11.959 1.00 22.81  ?  340 TRP A CE3    1 
ATOM   2563 C CZ2    . TRP A 1 340 ? 20.216 10.844  11.622 1.00 20.16  ?  340 TRP A CZ2    1 
ATOM   2564 C CZ3    . TRP A 1 340 ? 22.475 10.157  11.109 1.00 27.08  ?  340 TRP A CZ3    1 
ATOM   2565 C CH2    . TRP A 1 340 ? 21.089 10.044  10.939 1.00 24.83  ?  340 TRP A CH2    1 
ATOM   2566 N N      . ILE A 1 341 ? 25.543 10.934  14.436 1.00 19.32  ?  341 ILE A N      1 
ATOM   2567 C CA     . ILE A 1 341 ? 25.899 9.593   13.966 1.00 26.76  ?  341 ILE A CA     1 
ATOM   2568 C C      . ILE A 1 341 ? 25.961 8.618   15.142 1.00 23.21  ?  341 ILE A C      1 
ATOM   2569 O O      . ILE A 1 341 ? 25.471 7.482   15.057 1.00 21.79  ?  341 ILE A O      1 
ATOM   2570 C CB     . ILE A 1 341 ? 27.229 9.625   13.178 1.00 26.89  ?  341 ILE A CB     1 
ATOM   2571 C CG1    . ILE A 1 341 ? 27.172 10.655  12.058 1.00 27.87  ?  341 ILE A CG1    1 
ATOM   2572 C CG2    . ILE A 1 341 ? 27.578 8.248   12.586 1.00 20.81  ?  341 ILE A CG2    1 
ATOM   2573 C CD1    . ILE A 1 341 ? 28.494 10.797  11.342 1.00 23.32  ?  341 ILE A CD1    1 
ATOM   2574 N N      . GLY A 1 342 ? 26.596 9.029   16.240 1.00 19.09  ?  342 GLY A N      1 
ATOM   2575 C CA     . GLY A 1 342 ? 26.483 8.263   17.468 1.00 19.06  ?  342 GLY A CA     1 
ATOM   2576 C C      . GLY A 1 342 ? 25.038 8.078   17.877 1.00 20.93  ?  342 GLY A C      1 
ATOM   2577 O O      . GLY A 1 342 ? 24.646 7.015   18.353 1.00 21.29  ?  342 GLY A O      1 
ATOM   2578 N N      . GLY A 1 343 ? 24.215 9.097   17.654 1.00 27.52  ?  343 GLY A N      1 
ATOM   2579 C CA     . GLY A 1 343 ? 22.789 8.918   17.834 1.00 26.41  ?  343 GLY A CA     1 
ATOM   2580 C C      . GLY A 1 343 ? 22.258 7.776   16.998 1.00 28.97  ?  343 GLY A C      1 
ATOM   2581 O O      . GLY A 1 343 ? 21.591 6.869   17.504 1.00 33.16  ?  343 GLY A O      1 
ATOM   2582 N N      . SER A 1 344 ? 22.563 7.796   15.704 1.00 29.51  ?  344 SER A N      1 
ATOM   2583 C CA     . SER A 1 344 ? 21.966 6.832   14.785 1.00 30.89  ?  344 SER A CA     1 
ATOM   2584 C C      . SER A 1 344 ? 22.450 5.411   15.057 1.00 28.23  ?  344 SER A C      1 
ATOM   2585 O O      . SER A 1 344 ? 21.680 4.458   14.909 1.00 29.70  ?  344 SER A O      1 
ATOM   2586 C CB     . SER A 1 344 ? 22.262 7.237   13.337 1.00 29.22  ?  344 SER A CB     1 
ATOM   2587 O OG     . SER A 1 344 ? 21.773 6.272   12.437 1.00 21.39  ?  344 SER A OG     1 
ATOM   2588 N N      . ILE A 1 345 ? 23.727 5.246   15.426 1.00 36.26  ?  345 ILE A N      1 
ATOM   2589 C CA     . ILE A 1 345 ? 24.256 3.928   15.793 1.00 35.26  ?  345 ILE A CA     1 
ATOM   2590 C C      . ILE A 1 345 ? 23.478 3.362   16.970 1.00 34.10  ?  345 ILE A C      1 
ATOM   2591 O O      . ILE A 1 345 ? 22.946 2.249   16.921 1.00 40.41  ?  345 ILE A O      1 
ATOM   2592 C CB     . ILE A 1 345 ? 25.755 4.018   16.142 1.00 35.73  ?  345 ILE A CB     1 
ATOM   2593 C CG1    . ILE A 1 345 ? 26.592 4.548   14.968 1.00 36.94  ?  345 ILE A CG1    1 
ATOM   2594 C CG2    . ILE A 1 345 ? 26.265 2.664   16.649 1.00 29.54  ?  345 ILE A CG2    1 
ATOM   2595 C CD1    . ILE A 1 345 ? 28.074 4.863   15.324 1.00 28.97  ?  345 ILE A CD1    1 
ATOM   2596 N N      . LEU A 1 346 ? 23.435 4.121   18.061 1.00 31.75  ?  346 LEU A N      1 
ATOM   2597 C CA     . LEU A 1 346 ? 22.721 3.679   19.243 1.00 35.44  ?  346 LEU A CA     1 
ATOM   2598 C C      . LEU A 1 346 ? 21.292 3.284   18.892 1.00 39.71  ?  346 LEU A C      1 
ATOM   2599 O O      . LEU A 1 346 ? 20.843 2.184   19.229 1.00 47.53  ?  346 LEU A O      1 
ATOM   2600 C CB     . LEU A 1 346 ? 22.757 4.781   20.304 1.00 33.42  ?  346 LEU A CB     1 
ATOM   2601 C CG     . LEU A 1 346 ? 22.059 4.463   21.626 1.00 35.16  ?  346 LEU A CG     1 
ATOM   2602 C CD1    . LEU A 1 346 ? 22.657 3.205   22.188 1.00 35.01  ?  346 LEU A CD1    1 
ATOM   2603 C CD2    . LEU A 1 346 ? 22.118 5.630   22.646 1.00 31.54  ?  346 LEU A CD2    1 
ATOM   2604 N N      . ALA A 1 347 ? 20.576 4.149   18.171 1.00 48.64  ?  347 ALA A N      1 
ATOM   2605 C CA     . ALA A 1 347 ? 19.168 3.886   17.884 1.00 49.33  ?  347 ALA A CA     1 
ATOM   2606 C C      . ALA A 1 347 ? 18.978 2.585   17.124 1.00 50.87  ?  347 ALA A C      1 
ATOM   2607 O O      . ALA A 1 347 ? 17.924 1.945   17.251 1.00 54.80  ?  347 ALA A O      1 
ATOM   2608 C CB     . ALA A 1 347 ? 18.553 5.046   17.101 1.00 51.37  ?  347 ALA A CB     1 
ATOM   2609 N N      . SER A 1 348 ? 19.991 2.164   16.348 1.00 35.50  ?  348 SER A N      1 
ATOM   2610 C CA     . SER A 1 348 ? 19.903 0.992   15.473 1.00 31.82  ?  348 SER A CA     1 
ATOM   2611 C C      . SER A 1 348 ? 20.346 -0.300  16.134 1.00 35.29  ?  348 SER A C      1 
ATOM   2612 O O      . SER A 1 348 ? 20.178 -1.370  15.534 1.00 40.06  ?  348 SER A O      1 
ATOM   2613 C CB     . SER A 1 348 ? 20.751 1.184   14.205 1.00 21.06  ?  348 SER A CB     1 
ATOM   2614 O OG     . SER A 1 348 ? 20.390 2.353   13.478 1.00 31.31  ?  348 SER A OG     1 
ATOM   2615 N N      . LEU A 1 349 ? 20.947 -0.227  17.314 1.00 33.50  ?  349 LEU A N      1 
ATOM   2616 C CA     . LEU A 1 349 ? 21.321 -1.437  18.023 1.00 33.00  ?  349 LEU A CA     1 
ATOM   2617 C C      . LEU A 1 349 ? 20.075 -2.159  18.519 1.00 33.72  ?  349 LEU A C      1 
ATOM   2618 O O      . LEU A 1 349 ? 19.054 -1.543  18.825 1.00 34.31  ?  349 LEU A O      1 
ATOM   2619 C CB     . LEU A 1 349 ? 22.242 -1.102  19.185 1.00 30.59  ?  349 LEU A CB     1 
ATOM   2620 C CG     . LEU A 1 349 ? 23.582 -0.508  18.760 1.00 30.62  ?  349 LEU A CG     1 
ATOM   2621 C CD1    . LEU A 1 349 ? 24.554 -0.506  19.931 1.00 29.37  ?  349 LEU A CD1    1 
ATOM   2622 C CD2    . LEU A 1 349 ? 24.150 -1.298  17.601 1.00 32.87  ?  349 LEU A CD2    1 
ATOM   2623 N N      . SER A 1 350 ? 20.158 -3.476  18.592 1.00 39.06  ?  350 SER A N      1 
ATOM   2624 C CA     . SER A 1 350 ? 19.043 -4.301  19.039 1.00 42.69  ?  350 SER A CA     1 
ATOM   2625 C C      . SER A 1 350 ? 18.948 -4.201  20.535 1.00 42.32  ?  350 SER A C      1 
ATOM   2626 O O      . SER A 1 350 ? 17.875 -4.133  21.076 1.00 44.12  ?  350 SER A O      1 
ATOM   2627 C CB     . SER A 1 350 ? 19.263 -5.717  18.523 1.00 42.78  ?  350 SER A CB     1 
ATOM   2628 O OG     . SER A 1 350 ? 20.598 -6.128  18.703 1.00 43.29  ?  350 SER A OG     1 
ATOM   2629 N N      . THR A 1 351 ? 20.061 -4.304  21.216 1.00 41.29  ?  351 THR A N      1 
ATOM   2630 C CA     . THR A 1 351 ? 20.101 -3.987  22.637 1.00 41.32  ?  351 THR A CA     1 
ATOM   2631 C C      . THR A 1 351 ? 19.352 -2.685  22.929 1.00 44.13  ?  351 THR A C      1 
ATOM   2632 O O      . THR A 1 351 ? 18.485 -2.637  23.813 1.00 42.96  ?  351 THR A O      1 
ATOM   2633 C CB     . THR A 1 351 ? 21.558 -3.918  23.103 1.00 42.06  ?  351 THR A CB     1 
ATOM   2634 O OG1    . THR A 1 351 ? 22.345 -3.217  22.127 1.00 42.85  ?  351 THR A OG1    1 
ATOM   2635 C CG2    . THR A 1 351 ? 22.140 -5.304  23.236 1.00 39.47  ?  351 THR A CG2    1 
ATOM   2636 N N      . PHE A 1 352 ? 19.616 -1.629  22.148 1.00 38.29  ?  352 PHE A N      1 
ATOM   2637 C CA     . PHE A 1 352 ? 18.887 -0.380  22.380 1.00 33.42  ?  352 PHE A CA     1 
ATOM   2638 C C      . PHE A 1 352 ? 17.390 -0.531  22.156 1.00 31.22  ?  352 PHE A C      1 
ATOM   2639 O O      . PHE A 1 352 ? 16.634 0.406   22.435 1.00 37.44  ?  352 PHE A O      1 
ATOM   2640 C CB     . PHE A 1 352 ? 19.428 0.761   21.498 1.00 33.92  ?  352 PHE A CB     1 
ATOM   2641 C CG     . PHE A 1 352 ? 18.953 2.167   21.909 1.00 30.08  ?  352 PHE A CG     1 
ATOM   2642 C CD1    . PHE A 1 352 ? 19.527 2.828   22.980 1.00 31.66  ?  352 PHE A CD1    1 
ATOM   2643 C CD2    . PHE A 1 352 ? 17.949 2.833   21.193 1.00 32.01  ?  352 PHE A CD2    1 
ATOM   2644 C CE1    . PHE A 1 352 ? 19.098 4.118   23.356 1.00 31.92  ?  352 PHE A CE1    1 
ATOM   2645 C CE2    . PHE A 1 352 ? 17.518 4.119   21.559 1.00 31.46  ?  352 PHE A CE2    1 
ATOM   2646 C CZ     . PHE A 1 352 ? 18.100 4.765   22.640 1.00 34.44  ?  352 PHE A CZ     1 
ATOM   2647 N N      . GLN A 1 353 ? 16.893 -1.666  21.764 1.00 33.10  ?  353 GLN A N      1 
ATOM   2648 C CA     . GLN A 1 353 ? 15.452 -1.765  21.626 1.00 39.42  ?  353 GLN A CA     1 
ATOM   2649 C C      . GLN A 1 353 ? 14.823 -1.982  22.985 1.00 40.17  ?  353 GLN A C      1 
ATOM   2650 O O      . GLN A 1 353 ? 13.637 -1.767  23.138 1.00 43.11  ?  353 GLN A O      1 
ATOM   2651 C CB     . GLN A 1 353 ? 15.048 -2.783  20.552 1.00 32.01  ?  353 GLN A CB     1 
ATOM   2652 C CG     . GLN A 1 353 ? 15.536 -2.453  19.150 1.00 36.65  ?  353 GLN A CG     1 
ATOM   2653 C CD     . GLN A 1 353 ? 15.404 -0.986  18.786 1.00 45.69  ?  353 GLN A CD     1 
ATOM   2654 O OE1    . GLN A 1 353 ? 14.316 -0.414  18.834 1.00 53.29  ?  353 GLN A OE1    1 
ATOM   2655 N NE2    . GLN A 1 353 ? 16.513 -0.374  18.402 1.00 37.34  ?  353 GLN A NE2    1 
ATOM   2656 N N      . GLN A 1 354 ? 15.620 -2.283  24.003 1.00 48.13  ?  354 GLN A N      1 
ATOM   2657 C CA     . GLN A 1 354 ? 15.131 -2.495  25.376 1.00 48.38  ?  354 GLN A CA     1 
ATOM   2658 C C      . GLN A 1 354 ? 15.400 -1.289  26.233 1.00 44.36  ?  354 GLN A C      1 
ATOM   2659 O O      . GLN A 1 354 ? 15.016 -1.247  27.385 1.00 39.58  ?  354 GLN A O      1 
ATOM   2660 C CB     . GLN A 1 354 ? 15.826 -3.692  26.032 1.00 43.41  ?  354 GLN A CB     1 
ATOM   2661 C CG     . GLN A 1 354 ? 15.994 -4.894  25.126 1.00 53.22  ?  354 GLN A CG     1 
ATOM   2662 C CD     . GLN A 1 354 ? 14.681 -5.549  24.769 1.00 56.64  ?  354 GLN A CD     1 
ATOM   2663 O OE1    . GLN A 1 354 ? 14.254 -5.518  23.620 1.00 52.24  ?  354 GLN A OE1    1 
ATOM   2664 N NE2    . GLN A 1 354 ? 14.033 -6.144  25.755 1.00 62.05  ?  354 GLN A NE2    1 
ATOM   2665 N N      . MET A 1 355 ? 16.066 -0.310  25.663 1.00 30.33  ?  355 MET A N      1 
ATOM   2666 C CA     . MET A 1 355 ? 16.422 0.861   26.422 1.00 24.15  ?  355 MET A CA     1 
ATOM   2667 C C      . MET A 1 355 ? 15.471 2.031   26.241 1.00 30.01  ?  355 MET A C      1 
ATOM   2668 O O      . MET A 1 355 ? 15.516 2.959   27.051 1.00 34.45  ?  355 MET A O      1 
ATOM   2669 C CB     . MET A 1 355 ? 17.860 1.230   26.060 1.00 27.79  ?  355 MET A CB     1 
ATOM   2670 C CG     . MET A 1 355 ? 18.724 -0.001  26.327 1.00 32.24  ?  355 MET A CG     1 
ATOM   2671 S SD     . MET A 1 355 ? 20.455 0.022   25.901 1.00 39.67  ?  355 MET A SD     1 
ATOM   2672 C CE     . MET A 1 355 ? 20.885 1.710   26.317 1.00 36.97  ?  355 MET A CE     1 
ATOM   2673 N N      . TRP A 1 356 ? 14.566 1.984   25.257 1.00 26.64  ?  356 TRP A N      1 
ATOM   2674 C CA     . TRP A 1 356 ? 13.596 3.065   25.070 1.00 28.75  ?  356 TRP A CA     1 
ATOM   2675 C C      . TRP A 1 356 ? 12.684 3.217   26.289 1.00 29.63  ?  356 TRP A C      1 
ATOM   2676 O O      . TRP A 1 356 ? 12.193 2.229   26.834 1.00 24.21  ?  356 TRP A O      1 
ATOM   2677 C CB     . TRP A 1 356 ? 12.689 2.809   23.860 1.00 22.84  ?  356 TRP A CB     1 
ATOM   2678 C CG     . TRP A 1 356 ? 13.272 2.828   22.518 1.00 21.23  ?  356 TRP A CG     1 
ATOM   2679 C CD1    . TRP A 1 356 ? 13.441 1.749   21.692 1.00 22.17  ?  356 TRP A CD1    1 
ATOM   2680 C CD2    . TRP A 1 356 ? 13.744 3.971   21.789 1.00 26.20  ?  356 TRP A CD2    1 
ATOM   2681 N NE1    . TRP A 1 356 ? 14.006 2.139   20.497 1.00 24.41  ?  356 TRP A NE1    1 
ATOM   2682 C CE2    . TRP A 1 356 ? 14.193 3.499   20.516 1.00 24.96  ?  356 TRP A CE2    1 
ATOM   2683 C CE3    . TRP A 1 356 ? 13.836 5.346   22.078 1.00 24.72  ?  356 TRP A CE3    1 
ATOM   2684 C CZ2    . TRP A 1 356 ? 14.729 4.360   19.526 1.00 20.99  ?  356 TRP A CZ2    1 
ATOM   2685 C CZ3    . TRP A 1 356 ? 14.371 6.210   21.092 1.00 24.50  ?  356 TRP A CZ3    1 
ATOM   2686 C CH2    . TRP A 1 356 ? 14.818 5.703   19.834 1.00 20.77  ?  356 TRP A CH2    1 
ATOM   2687 N N      . ILE A 1 357 ? 12.254 4.457   26.550 1.00 32.05  ?  357 ILE A N      1 
ATOM   2688 C CA     . ILE A 1 357 ? 11.240 4.718   27.541 1.00 24.18  ?  357 ILE A CA     1 
ATOM   2689 C C      . ILE A 1 357 ? 10.010 4.628   26.692 1.00 29.24  ?  357 ILE A C      1 
ATOM   2690 O O      . ILE A 1 357 ? 9.938  5.259   25.671 1.00 29.05  ?  357 ILE A O      1 
ATOM   2691 C CB     . ILE A 1 357 ? 11.228 6.163   27.974 1.00 24.14  ?  357 ILE A CB     1 
ATOM   2692 C CG1    . ILE A 1 357 ? 12.463 6.509   28.784 1.00 30.40  ?  357 ILE A CG1    1 
ATOM   2693 C CG2    . ILE A 1 357 ? 9.971  6.477   28.760 1.00 27.86  ?  357 ILE A CG2    1 
ATOM   2694 C CD1    . ILE A 1 357 ? 12.532 7.967   29.162 1.00 23.50  ?  357 ILE A CD1    1 
ATOM   2695 N N      . SER A 1 358 ? 9.044  3.823   27.091 1.00 40.59  ?  358 SER A N      1 
ATOM   2696 C CA     . SER A 1 358 ? 7.779  3.705   26.370 1.00 40.20  ?  358 SER A CA     1 
ATOM   2697 C C      . SER A 1 358 ? 6.593  4.504   26.869 1.00 34.62  ?  358 SER A C      1 
ATOM   2698 O O      . SER A 1 358 ? 6.572  4.953   27.976 1.00 35.71  ?  358 SER A O      1 
ATOM   2699 C CB     . SER A 1 358 ? 7.399  2.254   26.239 1.00 45.19  ?  358 SER A CB     1 
ATOM   2700 O OG     . SER A 1 358 ? 6.893  1.725   27.446 1.00 52.80  ?  358 SER A OG     1 
ATOM   2701 N N      . LYS A 1 359 ? 5.597  4.657   26.035 1.00 33.12  ?  359 LYS A N      1 
ATOM   2702 C CA     . LYS A 1 359 ? 4.425  5.441   26.360 1.00 34.66  ?  359 LYS A CA     1 
ATOM   2703 C C      . LYS A 1 359 ? 3.720  4.862   27.552 1.00 38.69  ?  359 LYS A C      1 
ATOM   2704 O O      . LYS A 1 359 ? 3.213  5.586   28.386 1.00 33.81  ?  359 LYS A O      1 
ATOM   2705 C CB     . LYS A 1 359 ? 3.528  5.505   25.114 1.00 32.01  ?  359 LYS A CB     1 
ATOM   2706 C CG     . LYS A 1 359 ? 2.196  6.217   25.257 1.00 32.05  ?  359 LYS A CG     1 
ATOM   2707 C CD     . LYS A 1 359 ? 2.347  7.711   25.471 1.00 37.98  ?  359 LYS A CD     1 
ATOM   2708 C CE     . LYS A 1 359 ? 0.986  8.357   25.657 1.00 41.81  ?  359 LYS A CE     1 
ATOM   2709 N NZ     . LYS A 1 359 ? 1.086  9.772   26.092 1.00 45.02  ?  359 LYS A NZ     1 
ATOM   2710 N N      . GLN A 1 360 ? 3.705  3.549   27.630 1.00 61.01  ?  360 GLN A N      1 
ATOM   2711 C CA     . GLN A 1 360 ? 3.095  2.871   28.745 1.00 65.07  ?  360 GLN A CA     1 
ATOM   2712 C C      . GLN A 1 360 ? 3.801  3.356   29.967 1.00 70.38  ?  360 GLN A C      1 
ATOM   2713 O O      . GLN A 1 360 ? 3.161  3.819   30.886 1.00 73.14  ?  360 GLN A O      1 
ATOM   2714 C CB     . GLN A 1 360 ? 3.286  1.378   28.580 1.00 61.20  ?  360 GLN A CB     1 
ATOM   2715 C CG     . GLN A 1 360 ? 2.579  0.511   29.597 1.00 65.31  ?  360 GLN A CG     1 
ATOM   2716 C CD     . GLN A 1 360 ? 2.693  -0.955  29.242 1.00 75.74  ?  360 GLN A CD     1 
ATOM   2717 O OE1    . GLN A 1 360 ? 3.221  -1.318  28.192 1.00 78.67  ?  360 GLN A OE1    1 
ATOM   2718 N NE2    . GLN A 1 360 ? 2.197  -1.812  30.126 1.00 77.40  ?  360 GLN A NE2    1 
ATOM   2719 N N      . GLU A 1 361 ? 5.125  3.314   29.952 1.00 58.56  ?  361 GLU A N      1 
ATOM   2720 C CA     . GLU A 1 361 ? 5.927  3.758   31.084 1.00 57.97  ?  361 GLU A CA     1 
ATOM   2721 C C      . GLU A 1 361 ? 5.768  5.212   31.484 1.00 49.91  ?  361 GLU A C      1 
ATOM   2722 O O      . GLU A 1 361 ? 5.701  5.515   32.647 1.00 48.72  ?  361 GLU A O      1 
ATOM   2723 C CB     . GLU A 1 361 ? 7.383  3.463   30.785 1.00 60.52  ?  361 GLU A CB     1 
ATOM   2724 C CG     . GLU A 1 361 ? 7.697  1.986   30.638 1.00 64.20  ?  361 GLU A CG     1 
ATOM   2725 C CD     . GLU A 1 361 ? 9.072  1.741   30.052 1.00 67.02  ?  361 GLU A CD     1 
ATOM   2726 O OE1    . GLU A 1 361 ? 9.803  2.719   29.839 1.00 71.85  ?  361 GLU A OE1    1 
ATOM   2727 O OE2    . GLU A 1 361 ? 9.419  0.574   29.802 1.00 66.76  -1 361 GLU A OE2    1 
ATOM   2728 N N      . TYR A 1 362 ? 5.691  6.101   30.526 1.00 32.73  ?  362 TYR A N      1 
ATOM   2729 C CA     . TYR A 1 362 ? 5.523  7.484   30.822 1.00 34.31  ?  362 TYR A CA     1 
ATOM   2730 C C      . TYR A 1 362 ? 4.214  7.714   31.541 1.00 44.38  ?  362 TYR A C      1 
ATOM   2731 O O      . TYR A 1 362 ? 4.131  8.467   32.446 1.00 42.79  ?  362 TYR A O      1 
ATOM   2732 C CB     . TYR A 1 362 ? 5.552  8.293   29.530 1.00 33.14  ?  362 TYR A CB     1 
ATOM   2733 C CG     . TYR A 1 362 ? 5.217  9.740   29.698 1.00 33.08  ?  362 TYR A CG     1 
ATOM   2734 C CD1    . TYR A 1 362 ? 6.178  10.640  30.083 1.00 37.20  ?  362 TYR A CD1    1 
ATOM   2735 C CD2    . TYR A 1 362 ? 3.941  10.207  29.465 1.00 33.48  ?  362 TYR A CD2    1 
ATOM   2736 C CE1    . TYR A 1 362 ? 5.878  11.969  30.241 1.00 36.35  ?  362 TYR A CE1    1 
ATOM   2737 C CE2    . TYR A 1 362 ? 3.632  11.532  29.631 1.00 31.21  ?  362 TYR A CE2    1 
ATOM   2738 C CZ     . TYR A 1 362 ? 4.609  12.403  30.020 1.00 33.18  ?  362 TYR A CZ     1 
ATOM   2739 O OH     . TYR A 1 362 ? 4.315  13.720  30.187 1.00 37.25  ?  362 TYR A OH     1 
ATOM   2740 N N      . ASP A 1 363 ? 3.154  7.077   31.100 1.00 74.11  ?  363 ASP A N      1 
ATOM   2741 C CA     . ASP A 1 363 ? 1.873  7.262   31.730 1.00 74.92  ?  363 ASP A CA     1 
ATOM   2742 C C      . ASP A 1 363 ? 1.926  6.714   33.145 1.00 69.24  ?  363 ASP A C      1 
ATOM   2743 O O      . ASP A 1 363 ? 1.435  7.344   34.073 1.00 63.47  ?  363 ASP A O      1 
ATOM   2744 C CB     . ASP A 1 363 ? 0.805  6.614   30.874 1.00 74.61  ?  363 ASP A CB     1 
ATOM   2745 C CG     . ASP A 1 363 ? 0.607  7.328   29.574 1.00 78.21  ?  363 ASP A CG     1 
ATOM   2746 O OD1    . ASP A 1 363 ? 0.949  8.521   29.506 1.00 74.79  ?  363 ASP A OD1    1 
ATOM   2747 O OD2    . ASP A 1 363 ? 0.099  6.698   28.626 1.00 83.09  -1 363 ASP A OD2    1 
ATOM   2748 N N      . GLU A 1 364 ? 2.569  5.572   33.308 1.00 48.29  ?  364 GLU A N      1 
ATOM   2749 C CA     . GLU A 1 364 ? 2.732  4.971   34.603 1.00 40.32  ?  364 GLU A CA     1 
ATOM   2750 C C      . GLU A 1 364 ? 3.584  5.829   35.507 1.00 46.50  ?  364 GLU A C      1 
ATOM   2751 O O      . GLU A 1 364 ? 3.502  5.719   36.719 1.00 50.55  ?  364 GLU A O      1 
ATOM   2752 C CB     . GLU A 1 364 ? 3.361  3.594   34.452 1.00 36.94  ?  364 GLU A CB     1 
ATOM   2753 C CG     . GLU A 1 364 ? 2.533  2.558   33.724 1.00 40.19  ?  364 GLU A CG     1 
ATOM   2754 C CD     . GLU A 1 364 ? 3.375  1.378   33.298 1.00 49.11  ?  364 GLU A CD     1 
ATOM   2755 O OE1    . GLU A 1 364 ? 4.574  1.360   33.632 1.00 50.30  ?  364 GLU A OE1    1 
ATOM   2756 O OE2    . GLU A 1 364 ? 2.847  0.471   32.630 1.00 49.83  -1 364 GLU A OE2    1 
ATOM   2757 N N      . SER A 1 365 ? 4.456  6.632   34.925 1.00 45.06  ?  365 SER A N      1 
ATOM   2758 C CA     . SER A 1 365 ? 5.343  7.486   35.721 1.00 44.96  ?  365 SER A CA     1 
ATOM   2759 C C      . SER A 1 365 ? 5.295  8.999   35.498 1.00 36.06  ?  365 SER A C      1 
ATOM   2760 O O      . SER A 1 365 ? 5.257  9.739   36.449 1.00 29.20  ?  365 SER A O      1 
ATOM   2761 C CB     . SER A 1 365 ? 6.793  6.988   35.618 1.00 51.08  ?  365 SER A CB     1 
ATOM   2762 O OG     . SER A 1 365 ? 7.052  5.933   36.520 1.00 53.85  ?  365 SER A OG     1 
ATOM   2763 N N      . GLY A 1 366 ? 5.286  9.453   34.248 1.00 43.77  ?  366 GLY A N      1 
ATOM   2764 C CA     . GLY A 1 366 ? 5.346  10.869  33.981 1.00 38.68  ?  366 GLY A CA     1 
ATOM   2765 C C      . GLY A 1 366 ? 6.738  11.227  33.514 1.00 39.99  ?  366 GLY A C      1 
ATOM   2766 O O      . GLY A 1 366 ? 7.574  10.360  33.242 1.00 47.49  ?  366 GLY A O      1 
ATOM   2767 N N      . PRO A 1 367 ? 7.023  12.517  33.413 1.00 23.95  ?  367 PRO A N      1 
ATOM   2768 C CA     . PRO A 1 367 ? 8.359  12.936  32.944 1.00 28.22  ?  367 PRO A CA     1 
ATOM   2769 C C      . PRO A 1 367 ? 9.544  12.433  33.799 1.00 34.89  ?  367 PRO A C      1 
ATOM   2770 O O      . PRO A 1 367 ? 10.690 12.513  33.336 1.00 39.83  ?  367 PRO A O      1 
ATOM   2771 C CB     . PRO A 1 367 ? 8.268  14.467  32.955 1.00 26.17  ?  367 PRO A CB     1 
ATOM   2772 C CG     . PRO A 1 367 ? 6.755  14.755  32.866 1.00 27.82  ?  367 PRO A CG     1 
ATOM   2773 C CD     . PRO A 1 367 ? 6.061  13.621  33.541 1.00 21.69  ?  367 PRO A CD     1 
ATOM   2774 N N      . SER A 1 368 ? 9.325  11.936  35.018 1.00 40.28  ?  368 SER A N      1 
ATOM   2775 C CA     . SER A 1 368 ? 10.425 11.526  35.894 1.00 33.32  ?  368 SER A CA     1 
ATOM   2776 C C      . SER A 1 368 ? 11.011 10.164  35.539 1.00 32.72  ?  368 SER A C      1 
ATOM   2777 O O      . SER A 1 368 ? 12.046 9.785   36.116 1.00 30.54  ?  368 SER A O      1 
ATOM   2778 C CB     . SER A 1 368 ? 9.933  11.514  37.339 1.00 32.63  ?  368 SER A CB     1 
ATOM   2779 O OG     . SER A 1 368 ? 8.657  10.911  37.398 1.00 33.39  ?  368 SER A OG     1 
ATOM   2780 N N      . ILE A 1 369 ? 10.401 9.456   34.601 1.00 40.05  ?  369 ILE A N      1 
ATOM   2781 C CA     . ILE A 1 369 ? 10.882 8.166   34.114 1.00 38.91  ?  369 ILE A CA     1 
ATOM   2782 C C      . ILE A 1 369 ? 12.215 8.322   33.426 1.00 40.67  ?  369 ILE A C      1 
ATOM   2783 O O      . ILE A 1 369 ? 12.990 7.403   33.366 1.00 43.58  ?  369 ILE A O      1 
ATOM   2784 C CB     . ILE A 1 369 ? 9.858  7.566   33.105 1.00 33.23  ?  369 ILE A CB     1 
ATOM   2785 C CG1    . ILE A 1 369 ? 10.172 6.123   32.733 1.00 30.08  ?  369 ILE A CG1    1 
ATOM   2786 C CG2    . ILE A 1 369 ? 9.704  8.433   31.867 1.00 28.00  ?  369 ILE A CG2    1 
ATOM   2787 C CD1    . ILE A 1 369 ? 9.430  5.110   33.560 1.00 32.38  ?  369 ILE A CD1    1 
ATOM   2788 N N      . VAL A 1 370 ? 12.512 9.509   32.954 1.00 32.59  ?  370 VAL A N      1 
ATOM   2789 C CA     . VAL A 1 370 ? 13.728 9.713   32.192 1.00 30.78  ?  370 VAL A CA     1 
ATOM   2790 C C      . VAL A 1 370 ? 14.959 9.646   33.096 1.00 29.66  ?  370 VAL A C      1 
ATOM   2791 O O      . VAL A 1 370 ? 16.048 9.288   32.635 1.00 31.11  ?  370 VAL A O      1 
ATOM   2792 C CB     . VAL A 1 370 ? 13.632 11.050  31.421 1.00 34.41  ?  370 VAL A CB     1 
ATOM   2793 C CG1    . VAL A 1 370 ? 13.397 12.233  32.379 1.00 29.54  ?  370 VAL A CG1    1 
ATOM   2794 C CG2    . VAL A 1 370 ? 14.883 11.283  30.569 1.00 37.22  ?  370 VAL A CG2    1 
ATOM   2795 N N      . HIS A 1 371 ? 14.818 9.982   34.384 1.00 25.15  ?  371 HIS A N      1 
ATOM   2796 C CA     . HIS A 1 371 ? 15.944 9.887   35.319 1.00 23.64  ?  371 HIS A CA     1 
ATOM   2797 C C      . HIS A 1 371 ? 16.358 8.452   35.600 1.00 22.61  ?  371 HIS A C      1 
ATOM   2798 O O      . HIS A 1 371 ? 17.545 8.185   35.789 1.00 26.18  ?  371 HIS A O      1 
ATOM   2799 C CB     . HIS A 1 371 ? 15.605 10.535  36.629 1.00 22.57  ?  371 HIS A CB     1 
ATOM   2800 C CG     . HIS A 1 371 ? 15.167 11.942  36.494 1.00 24.81  ?  371 HIS A CG     1 
ATOM   2801 N ND1    . HIS A 1 371 ? 16.025 12.944  36.107 1.00 24.40  ?  371 HIS A ND1    1 
ATOM   2802 C CD2    . HIS A 1 371 ? 13.959 12.522  36.687 1.00 28.51  ?  371 HIS A CD2    1 
ATOM   2803 C CE1    . HIS A 1 371 ? 15.369 14.088  36.077 1.00 27.01  ?  371 HIS A CE1    1 
ATOM   2804 N NE2    . HIS A 1 371 ? 14.114 13.859  36.426 1.00 31.15  ?  371 HIS A NE2    1 
ATOM   2805 N N      . ARG A 1 372 ? 15.447 7.514   35.581 1.00 28.02  ?  372 ARG A N      1 
ATOM   2806 C CA     . ARG A 1 372 ? 15.781 6.147   35.883 1.00 32.12  ?  372 ARG A CA     1 
ATOM   2807 C C      . ARG A 1 372 ? 16.042 5.336   34.658 1.00 31.20  ?  372 ARG A C      1 
ATOM   2808 O O      . ARG A 1 372 ? 16.641 4.288   34.727 1.00 37.46  ?  372 ARG A O      1 
ATOM   2809 C CB     . ARG A 1 372 ? 14.679 5.512   36.724 1.00 40.49  ?  372 ARG A CB     1 
ATOM   2810 C CG     . ARG A 1 372 ? 13.299 5.484   36.102 1.00 47.38  ?  372 ARG A CG     1 
ATOM   2811 C CD     . ARG A 1 372 ? 12.274 4.930   37.077 1.00 52.40  ?  372 ARG A CD     1 
ATOM   2812 N NE     . ARG A 1 372 ? 10.992 5.614   36.958 1.00 58.98  ?  372 ARG A NE     1 
ATOM   2813 C CZ     . ARG A 1 372 ? 10.681 6.729   37.610 1.00 67.53  ?  372 ARG A CZ     1 
ATOM   2814 N NH1    . ARG A 1 372 ? 11.559 7.289   38.430 1.00 72.07  ?  372 ARG A NH1    1 
ATOM   2815 N NH2    . ARG A 1 372 ? 9.497  7.294   37.442 1.00 65.31  ?  372 ARG A NH2    1 
ATOM   2816 N N      . LYS A 1 373 ? 15.593 5.821   33.538 1.00 34.59  ?  373 LYS A N      1 
ATOM   2817 C CA     . LYS A 1 373 ? 15.776 5.141   32.255 1.00 39.00  ?  373 LYS A CA     1 
ATOM   2818 C C      . LYS A 1 373 ? 17.014 5.639   31.504 1.00 48.54  ?  373 LYS A C      1 
ATOM   2819 O O      . LYS A 1 373 ? 17.919 4.851   31.200 1.00 57.20  ?  373 LYS A O      1 
ATOM   2820 C CB     . LYS A 1 373 ? 14.500 5.297   31.407 1.00 40.23  ?  373 LYS A CB     1 
ATOM   2821 C CG     . LYS A 1 373 ? 13.270 4.608   31.999 1.00 42.83  ?  373 LYS A CG     1 
ATOM   2822 C CD     . LYS A 1 373 ? 13.493 3.104   32.111 1.00 49.74  ?  373 LYS A CD     1 
ATOM   2823 C CE     . LYS A 1 373 ? 12.595 2.458   33.169 1.00 51.71  ?  373 LYS A CE     1 
ATOM   2824 N NZ     . LYS A 1 373 ? 13.075 1.094   33.564 1.00 48.80  ?  373 LYS A NZ     1 
ATOM   2825 N N      . CYS A 1 374 ? 17.069 6.924   31.223 1.00 47.13  ?  374 CYS A N      1 
ATOM   2826 C CA     . CYS A 1 374 ? 18.180 7.493   30.497 1.00 46.78  ?  374 CYS A CA     1 
ATOM   2827 C C      . CYS A 1 374 ? 19.114 8.142   31.473 1.00 50.46  ?  374 CYS A C      1 
ATOM   2828 O O      . CYS A 1 374 ? 18.842 9.207   31.971 1.00 54.18  ?  374 CYS A O      1 
ATOM   2829 C CB     . CYS A 1 374 ? 17.695 8.528   29.487 1.00 46.13  ?  374 CYS A CB     1 
ATOM   2830 S SG     . CYS A 1 374 ? 16.194 8.184   28.579 1.00 51.36  ?  374 CYS A SG     1 
ATOM   2831 N N      . PHE A 1 375 ? 20.221 7.491   31.750 1.00 49.59  ?  375 PHE A N      1 
ATOM   2832 C CA     . PHE A 1 375 ? 21.210 8.036   32.647 1.00 49.15  ?  375 PHE A CA     1 
ATOM   2833 C C      . PHE A 1 375 ? 22.608 7.540   32.258 1.00 43.91  ?  375 PHE A C      1 
ATOM   2834 O O      . PHE A 1 375 ? 22.816 6.990   31.187 1.00 39.78  ?  375 PHE A O      1 
ATOM   2835 C CB     . PHE A 1 375 ? 20.868 7.724   34.118 1.00 53.86  ?  375 PHE A CB     1 
ATOM   2836 C CG     . PHE A 1 375 ? 20.921 6.267   34.490 1.00 50.79  ?  375 PHE A CG     1 
ATOM   2837 C CD1    . PHE A 1 375 ? 19.935 5.387   34.082 1.00 41.04  ?  375 PHE A CD1    1 
ATOM   2838 C CD2    . PHE A 1 375 ? 21.936 5.789   35.288 1.00 53.44  ?  375 PHE A CD2    1 
ATOM   2839 C CE1    . PHE A 1 375 ? 19.986 4.055   34.425 1.00 46.79  ?  375 PHE A CE1    1 
ATOM   2840 C CE2    . PHE A 1 375 ? 21.986 4.464   35.643 1.00 49.56  ?  375 PHE A CE2    1 
ATOM   2841 C CZ     . PHE A 1 375 ? 21.011 3.592   35.212 1.00 50.14  ?  375 PHE A CZ     1 
ATOM   2842 N N      . GLU B 2 7   ? 9.807  -10.338 29.381 1.00 64.01  ?  7   GLU B N      1 
ATOM   2843 C CA     . GLU B 2 7   ? 10.917 -9.410  29.396 1.00 61.73  ?  7   GLU B CA     1 
ATOM   2844 C C      . GLU B 2 7   ? 12.242 -10.077 29.036 1.00 63.84  ?  7   GLU B C      1 
ATOM   2845 O O      . GLU B 2 7   ? 12.844 -10.740 29.855 1.00 57.98  ?  7   GLU B O      1 
ATOM   2846 C CB     . GLU B 2 7   ? 10.956 -8.668  30.735 1.00 61.97  ?  7   GLU B CB     1 
ATOM   2847 C CG     . GLU B 2 7   ? 11.033 -9.506  32.002 1.00 68.01  ?  7   GLU B CG     1 
ATOM   2848 C CD     . GLU B 2 7   ? 9.682  -9.903  32.546 1.00 68.67  ?  7   GLU B CD     1 
ATOM   2849 O OE1    . GLU B 2 7   ? 8.670  -9.711  31.853 1.00 69.94  ?  7   GLU B OE1    1 
ATOM   2850 O OE2    . GLU B 2 7   ? 9.626  -10.405 33.676 1.00 61.65  -1 7   GLU B OE2    1 
ATOM   2851 N N      . LEU B 2 8   ? 12.685 -9.918  27.786 1.00 65.97  ?  8   LEU B N      1 
ATOM   2852 C CA     . LEU B 2 8   ? 13.964 -10.460 27.361 1.00 64.96  ?  8   LEU B CA     1 
ATOM   2853 C C      . LEU B 2 8   ? 15.115 -9.672  27.970 1.00 60.62  ?  8   LEU B C      1 
ATOM   2854 O O      . LEU B 2 8   ? 16.240 -10.177 28.059 1.00 54.69  ?  8   LEU B O      1 
ATOM   2855 C CB     . LEU B 2 8   ? 14.082 -10.470 25.833 1.00 62.01  ?  8   LEU B CB     1 
ATOM   2856 C CG     . LEU B 2 8   ? 15.318 -11.311 25.521 1.00 58.75  ?  8   LEU B CG     1 
ATOM   2857 C CD1    . LEU B 2 8   ? 14.943 -12.784 25.250 1.00 57.61  ?  8   LEU B CD1    1 
ATOM   2858 C CD2    . LEU B 2 8   ? 16.210 -10.689 24.449 1.00 55.51  ?  8   LEU B CD2    1 
ATOM   2859 N N      . SER B 2 9   ? 14.820 -8.476  28.409 1.00 71.66  ?  9   SER B N      1 
ATOM   2860 C CA     . SER B 2 9   ? 15.803 -7.655  29.047 1.00 72.22  ?  9   SER B CA     1 
ATOM   2861 C C      . SER B 2 9   ? 16.590 -8.334  30.138 1.00 71.47  ?  9   SER B C      1 
ATOM   2862 O O      . SER B 2 9   ? 17.775 -8.077  30.288 1.00 71.84  ?  9   SER B O      1 
ATOM   2863 C CB     . SER B 2 9   ? 15.045 -6.497  29.630 1.00 74.21  ?  9   SER B CB     1 
ATOM   2864 O OG     . SER B 2 9   ? 13.777 -6.906  30.093 1.00 73.45  ?  9   SER B OG     1 
ATOM   2865 N N      . ILE B 2 10  ? 15.936 -9.182  30.917 1.00 68.08  ?  10  ILE B N      1 
ATOM   2866 C CA     . ILE B 2 10  ? 16.613 -9.846  32.034 1.00 66.49  ?  10  ILE B CA     1 
ATOM   2867 C C      . ILE B 2 10  ? 17.731 -10.767 31.536 1.00 64.12  ?  10  ILE B C      1 
ATOM   2868 O O      . ILE B 2 10  ? 18.759 -10.917 32.207 1.00 69.07  ?  10  ILE B O      1 
ATOM   2869 C CB     . ILE B 2 10  ? 15.605 -10.609 32.923 1.00 68.98  ?  10  ILE B CB     1 
ATOM   2870 C CG1    . ILE B 2 10  ? 14.586 -9.657  33.554 1.00 68.24  ?  10  ILE B CG1    1 
ATOM   2871 C CG2    . ILE B 2 10  ? 16.325 -11.323 34.060 1.00 72.01  ?  10  ILE B CG2    1 
ATOM   2872 C CD1    . ILE B 2 10  ? 15.184 -8.688  34.569 1.00 69.57  ?  10  ILE B CD1    1 
ATOM   2873 N N      . SER B 2 11  ? 17.569 -11.385 30.356 1.00 43.78  ?  11  SER B N      1 
ATOM   2874 C CA     . SER B 2 11  ? 18.593 -12.291 29.846 1.00 41.25  ?  11  SER B CA     1 
ATOM   2875 C C      . SER B 2 11  ? 19.763 -11.547 29.235 1.00 36.96  ?  11  SER B C      1 
ATOM   2876 O O      . SER B 2 11  ? 20.868 -12.094 29.171 1.00 34.25  ?  11  SER B O      1 
ATOM   2877 C CB     . SER B 2 11  ? 18.000 -13.245 28.822 1.00 51.11  ?  11  SER B CB     1 
ATOM   2878 O OG     . SER B 2 11  ? 17.507 -12.530 27.710 1.00 60.47  ?  11  SER B OG     1 
ATOM   2879 N N      . LEU B 2 12  ? 19.537 -10.308 28.799 1.00 56.53  ?  12  LEU B N      1 
ATOM   2880 C CA     . LEU B 2 12  ? 20.616 -9.429  28.357 1.00 59.89  ?  12  LEU B CA     1 
ATOM   2881 C C      . LEU B 2 12  ? 21.351 -8.787  29.531 1.00 63.01  ?  12  LEU B C      1 
ATOM   2882 O O      . LEU B 2 12  ? 22.551 -8.504  29.426 1.00 63.79  ?  12  LEU B O      1 
ATOM   2883 C CB     . LEU B 2 12  ? 20.056 -8.346  27.431 1.00 56.24  ?  12  LEU B CB     1 
ATOM   2884 C CG     . LEU B 2 12  ? 19.966 -8.676  25.934 1.00 66.63  ?  12  LEU B CG     1 
ATOM   2885 C CD1    . LEU B 2 12  ? 18.912 -7.842  25.198 1.00 61.51  ?  12  LEU B CD1    1 
ATOM   2886 C CD2    . LEU B 2 12  ? 21.340 -8.537  25.256 1.00 70.58  ?  12  LEU B CD2    1 
ATOM   2887 N N      . SER B 2 13  ? 20.653 -8.531  30.641 1.00 56.85  ?  13  SER B N      1 
ATOM   2888 C CA     . SER B 2 13  ? 21.344 -8.087  31.848 1.00 57.14  ?  13  SER B CA     1 
ATOM   2889 C C      . SER B 2 13  ? 22.230 -9.190  32.414 1.00 53.45  ?  13  SER B C      1 
ATOM   2890 O O      . SER B 2 13  ? 23.346 -8.922  32.875 1.00 53.68  ?  13  SER B O      1 
ATOM   2891 C CB     . SER B 2 13  ? 20.337 -7.619  32.897 1.00 58.79  ?  13  SER B CB     1 
ATOM   2892 O OG     . SER B 2 13  ? 19.801 -6.357  32.551 1.00 63.47  ?  13  SER B OG     1 
ATOM   2893 N N      . LEU B 2 14  ? 21.769 -10.417 32.334 1.00 46.63  ?  14  LEU B N      1 
ATOM   2894 C CA     . LEU B 2 14  ? 22.519 -11.516 32.901 1.00 51.20  ?  14  LEU B CA     1 
ATOM   2895 C C      . LEU B 2 14  ? 23.776 -11.845 32.136 1.00 55.61  ?  14  LEU B C      1 
ATOM   2896 O O      . LEU B 2 14  ? 24.563 -12.642 32.597 1.00 55.69  ?  14  LEU B O      1 
ATOM   2897 C CB     . LEU B 2 14  ? 21.630 -12.723 33.076 1.00 46.96  ?  14  LEU B CB     1 
ATOM   2898 C CG     . LEU B 2 14  ? 20.506 -12.601 34.083 1.00 39.24  ?  14  LEU B CG     1 
ATOM   2899 C CD1    . LEU B 2 14  ? 19.617 -13.818 33.947 1.00 35.43  ?  14  LEU B CD1    1 
ATOM   2900 C CD2    . LEU B 2 14  ? 21.048 -12.435 35.484 1.00 37.28  ?  14  LEU B CD2    1 
ATOM   2901 N N      . ASP B 2 15  ? 23.967 -11.255 30.972 1.00 70.45  ?  15  ASP B N      1 
ATOM   2902 C CA     . ASP B 2 15  ? 25.217 -11.414 30.235 1.00 69.34  ?  15  ASP B CA     1 
ATOM   2903 C C      . ASP B 2 15  ? 26.402 -10.746 30.936 1.00 69.20  ?  15  ASP B C      1 
ATOM   2904 O O      . ASP B 2 15  ? 27.529 -11.248 30.847 1.00 73.79  ?  15  ASP B O      1 
ATOM   2905 C CB     . ASP B 2 15  ? 25.088 -10.832 28.826 1.00 72.22  ?  15  ASP B CB     1 
ATOM   2906 C CG     . ASP B 2 15  ? 24.234 -11.679 27.899 1.00 78.93  ?  15  ASP B CG     1 
ATOM   2907 O OD1    . ASP B 2 15  ? 24.249 -12.926 28.006 1.00 80.74  ?  15  ASP B OD1    1 
ATOM   2908 O OD2    . ASP B 2 15  ? 23.556 -11.081 27.035 1.00 81.44  -1 15  ASP B OD2    1 
ATOM   2909 N N      . SER B 2 16  ? 26.176 -9.626  31.626 1.00 51.73  ?  16  SER B N      1 
ATOM   2910 C CA     . SER B 2 16  ? 27.274 -8.768  32.042 1.00 48.53  ?  16  SER B CA     1 
ATOM   2911 C C      . SER B 2 16  ? 28.356 -9.577  32.759 1.00 52.72  ?  16  SER B C      1 
ATOM   2912 O O      . SER B 2 16  ? 28.034 -10.382 33.649 1.00 43.17  ?  16  SER B O      1 
ATOM   2913 C CB     . SER B 2 16  ? 26.777 -7.655  32.961 1.00 51.93  ?  16  SER B CB     1 
ATOM   2914 O OG     . SER B 2 16  ? 27.877 -6.902  33.439 1.00 56.15  ?  16  SER B OG     1 
ATOM   2915 N N      . PRO B 2 17  ? 29.637 -9.394  32.412 1.00 63.05  ?  17  PRO B N      1 
ATOM   2916 C CA     . PRO B 2 17  ? 30.682 -10.117 33.142 1.00 60.52  ?  17  PRO B CA     1 
ATOM   2917 C C      . PRO B 2 17  ? 30.760 -9.691  34.591 1.00 60.09  ?  17  PRO B C      1 
ATOM   2918 O O      . PRO B 2 17  ? 31.208 -10.476 35.438 1.00 59.11  ?  17  PRO B O      1 
ATOM   2919 C CB     . PRO B 2 17  ? 31.960 -9.755  32.373 1.00 56.57  ?  17  PRO B CB     1 
ATOM   2920 C CG     . PRO B 2 17  ? 31.683 -8.400  31.840 1.00 55.06  ?  17  PRO B CG     1 
ATOM   2921 C CD     . PRO B 2 17  ? 30.215 -8.432  31.455 1.00 63.71  ?  17  PRO B CD     1 
ATOM   2922 N N      . LYS B 2 18  ? 30.324 -8.480  34.885 1.00 57.16  ?  18  LYS B N      1 
ATOM   2923 C CA     . LYS B 2 18  ? 30.472 -7.951  36.230 1.00 53.38  ?  18  LYS B CA     1 
ATOM   2924 C C      . LYS B 2 18  ? 29.310 -8.102  37.167 1.00 50.95  ?  18  LYS B C      1 
ATOM   2925 O O      . LYS B 2 18  ? 29.306 -7.503  38.226 1.00 56.95  ?  18  LYS B O      1 
ATOM   2926 C CB     . LYS B 2 18  ? 30.966 -6.506  36.179 1.00 53.76  ?  18  LYS B CB     1 
ATOM   2927 C CG     . LYS B 2 18  ? 32.454 -6.372  35.906 1.00 60.55  ?  18  LYS B CG     1 
ATOM   2928 C CD     . LYS B 2 18  ? 33.259 -7.515  36.517 1.00 64.68  ?  18  LYS B CD     1 
ATOM   2929 C CE     . LYS B 2 18  ? 33.300 -7.492  38.039 1.00 61.04  ?  18  LYS B CE     1 
ATOM   2930 N NZ     . LYS B 2 18  ? 33.264 -8.885  38.569 1.00 56.24  ?  18  LYS B NZ     1 
ATOM   2931 N N      . LEU B 2 19  ? 28.348 -8.909  36.808 1.00 40.31  ?  19  LEU B N      1 
ATOM   2932 C CA     . LEU B 2 19  ? 27.244 -9.185  37.683 1.00 41.81  ?  19  LEU B CA     1 
ATOM   2933 C C      . LEU B 2 19  ? 27.767 -9.681  38.957 1.00 47.51  ?  19  LEU B C      1 
ATOM   2934 O O      . LEU B 2 19  ? 28.587 -10.594 38.982 1.00 48.89  ?  19  LEU B O      1 
ATOM   2935 C CB     . LEU B 2 19  ? 26.348 -10.256 37.122 1.00 40.68  ?  19  LEU B CB     1 
ATOM   2936 C CG     . LEU B 2 19  ? 24.896 -10.318 37.564 1.00 42.57  ?  19  LEU B CG     1 
ATOM   2937 C CD1    . LEU B 2 19  ? 24.150 -9.203  36.868 1.00 31.93  ?  19  LEU B CD1    1 
ATOM   2938 C CD2    . LEU B 2 19  ? 24.323 -11.659 37.155 1.00 49.18  ?  19  LEU B CD2    1 
ATOM   2939 N N      . ASP B 2 20  ? 27.293 -9.094  40.040 1.00 52.88  ?  20  ASP B N      1 
ATOM   2940 C CA     . ASP B 2 20  ? 27.683 -9.543  41.341 1.00 44.99  ?  20  ASP B CA     1 
ATOM   2941 C C      . ASP B 2 20  ? 26.489 -10.166 42.007 1.00 48.68  ?  20  ASP B C      1 
ATOM   2942 O O      . ASP B 2 20  ? 25.437 -10.242 41.421 1.00 47.56  ?  20  ASP B O      1 
ATOM   2943 C CB     . ASP B 2 20  ? 28.341 -8.424  42.151 1.00 45.56  ?  20  ASP B CB     1 
ATOM   2944 C CG     . ASP B 2 20  ? 27.480 -7.181  42.299 1.00 53.91  ?  20  ASP B CG     1 
ATOM   2945 O OD1    . ASP B 2 20  ? 26.315 -7.274  42.699 1.00 52.43  ?  20  ASP B OD1    1 
ATOM   2946 O OD2    . ASP B 2 20  ? 28.002 -6.077  42.069 1.00 55.13  -1 20  ASP B OD2    1 
ATOM   2947 N N      . GLU B 2 21  ? 26.659 -10.641 43.213 1.00 49.62  ?  21  GLU B N      1 
ATOM   2948 C CA     . GLU B 2 21  ? 25.571 -11.234 43.963 1.00 45.04  ?  21  GLU B CA     1 
ATOM   2949 C C      . GLU B 2 21  ? 24.427 -10.278 44.230 1.00 39.40  ?  21  GLU B C      1 
ATOM   2950 O O      . GLU B 2 21  ? 23.289 -10.668 44.159 1.00 38.97  ?  21  GLU B O      1 
ATOM   2951 C CB     . GLU B 2 21  ? 26.130 -11.800 45.262 1.00 46.62  ?  21  GLU B CB     1 
ATOM   2952 C CG     . GLU B 2 21  ? 27.296 -12.754 45.099 1.00 49.33  ?  21  GLU B CG     1 
ATOM   2953 C CD     . GLU B 2 21  ? 27.758 -13.339 46.420 1.00 53.43  ?  21  GLU B CD     1 
ATOM   2954 O OE1    . GLU B 2 21  ? 27.628 -12.669 47.460 1.00 52.17  ?  21  GLU B OE1    1 
ATOM   2955 O OE2    . GLU B 2 21  ? 28.257 -14.478 46.422 1.00 57.19  -1 21  GLU B OE2    1 
ATOM   2956 N N      . SER B 2 22  ? 24.719 -9.029  44.534 1.00 39.43  ?  22  SER B N      1 
ATOM   2957 C CA     . SER B 2 22  ? 23.672 -8.024  44.710 1.00 42.13  ?  22  SER B CA     1 
ATOM   2958 C C      . SER B 2 22  ? 22.895 -7.787  43.446 1.00 42.44  ?  22  SER B C      1 
ATOM   2959 O O      . SER B 2 22  ? 21.679 -7.762  43.463 1.00 43.86  ?  22  SER B O      1 
ATOM   2960 C CB     . SER B 2 22  ? 24.245 -6.703  45.237 1.00 42.89  ?  22  SER B CB     1 
ATOM   2961 O OG     . SER B 2 22  ? 23.282 -5.682  45.313 1.00 38.57  ?  22  SER B OG     1 
ATOM   2962 N N      . ASP B 2 23  ? 23.594 -7.629  42.343 1.00 55.91  ?  23  ASP B N      1 
ATOM   2963 C CA     . ASP B 2 23  ? 22.951 -7.419  41.057 1.00 61.71  ?  23  ASP B CA     1 
ATOM   2964 C C      . ASP B 2 23  ? 22.037 -8.568  40.730 1.00 58.95  ?  23  ASP B C      1 
ATOM   2965 O O      . ASP B 2 23  ? 20.979 -8.354  40.186 1.00 58.87  ?  23  ASP B O      1 
ATOM   2966 C CB     . ASP B 2 23  ? 23.986 -7.249  39.955 1.00 66.34  ?  23  ASP B CB     1 
ATOM   2967 C CG     . ASP B 2 23  ? 24.798 -6.012  40.099 1.00 78.21  ?  23  ASP B CG     1 
ATOM   2968 O OD1    . ASP B 2 23  ? 24.395 -5.143  40.880 1.00 83.22  ?  23  ASP B OD1    1 
ATOM   2969 O OD2    . ASP B 2 23  ? 25.844 -5.906  39.425 1.00 79.80  -1 23  ASP B OD2    1 
ATOM   2970 N N      . PHE B 2 24  ? 22.435 -9.777  41.063 1.00 32.38  ?  24  PHE B N      1 
ATOM   2971 C CA     . PHE B 2 24  ? 21.592 -10.926 40.864 1.00 30.52  ?  24  PHE B CA     1 
ATOM   2972 C C      . PHE B 2 24  ? 20.315 -10.839 41.638 1.00 35.90  ?  24  PHE B C      1 
ATOM   2973 O O      . PHE B 2 24  ? 19.265 -10.993 41.076 1.00 30.58  ?  24  PHE B O      1 
ATOM   2974 C CB     . PHE B 2 24  ? 22.360 -12.150 41.294 1.00 24.38  ?  24  PHE B CB     1 
ATOM   2975 C CG     . PHE B 2 24  ? 21.690 -13.450 41.001 1.00 32.29  ?  24  PHE B CG     1 
ATOM   2976 C CD1    . PHE B 2 24  ? 21.706 -13.976 39.730 1.00 38.99  ?  24  PHE B CD1    1 
ATOM   2977 C CD2    . PHE B 2 24  ? 21.113 -14.185 42.014 1.00 32.67  ?  24  PHE B CD2    1 
ATOM   2978 C CE1    . PHE B 2 24  ? 21.123 -15.190 39.468 1.00 36.01  ?  24  PHE B CE1    1 
ATOM   2979 C CE2    . PHE B 2 24  ? 20.524 -15.399 41.755 1.00 33.50  ?  24  PHE B CE2    1 
ATOM   2980 C CZ     . PHE B 2 24  ? 20.530 -15.903 40.480 1.00 35.03  ?  24  PHE B CZ     1 
ATOM   2981 N N      . ILE B 2 25  ? 20.385 -10.555 42.923 1.00 41.22  ?  25  ILE B N      1 
ATOM   2982 C CA     . ILE B 2 25  ? 19.204 -10.588 43.757 1.00 36.09  ?  25  ILE B CA     1 
ATOM   2983 C C      . ILE B 2 25  ? 18.257 -9.577  43.227 1.00 33.72  ?  25  ILE B C      1 
ATOM   2984 O O      . ILE B 2 25  ? 17.095 -9.825  43.115 1.00 40.11  ?  25  ILE B O      1 
ATOM   2985 C CB     . ILE B 2 25  ? 19.540 -10.365 45.250 1.00 31.90  ?  25  ILE B CB     1 
ATOM   2986 C CG1    . ILE B 2 25  ? 20.363 -11.541 45.758 1.00 34.98  ?  25  ILE B CG1    1 
ATOM   2987 C CG2    . ILE B 2 25  ? 18.294 -10.212 46.093 1.00 25.45  ?  25  ILE B CG2    1 
ATOM   2988 C CD1    . ILE B 2 25  ? 21.142 -11.247 47.010 1.00 31.07  ?  25  ILE B CD1    1 
ATOM   2989 N N      . LEU B 2 26  ? 18.771 -8.428  42.870 1.00 34.84  ?  26  LEU B N      1 
ATOM   2990 C CA     . LEU B 2 26  ? 17.942 -7.407  42.320 1.00 35.39  ?  26  LEU B CA     1 
ATOM   2991 C C      . LEU B 2 26  ? 17.354 -7.716  40.955 1.00 33.98  ?  26  LEU B C      1 
ATOM   2992 O O      . LEU B 2 26  ? 16.197 -7.482  40.715 1.00 39.17  ?  26  LEU B O      1 
ATOM   2993 C CB     . LEU B 2 26  ? 18.712 -6.111  42.358 1.00 38.92  ?  26  LEU B CB     1 
ATOM   2994 C CG     . LEU B 2 26  ? 18.956 -5.501  43.730 1.00 39.11  ?  26  LEU B CG     1 
ATOM   2995 C CD1    . LEU B 2 26  ? 20.003 -4.411  43.638 1.00 37.04  ?  26  LEU B CD1    1 
ATOM   2996 C CD2    . LEU B 2 26  ? 17.667 -4.952  44.298 1.00 34.40  ?  26  LEU B CD2    1 
ATOM   2997 N N      . LEU B 2 27  ? 18.141 -8.298  40.085 1.00 32.44  ?  27  LEU B N      1 
ATOM   2998 C CA     . LEU B 2 27  ? 17.662 -8.663  38.778 1.00 36.94  ?  27  LEU B CA     1 
ATOM   2999 C C      . LEU B 2 27  ? 16.765 -9.879  38.782 1.00 37.81  ?  27  LEU B C      1 
ATOM   3000 O O      . LEU B 2 27  ? 15.807 -9.933  38.033 1.00 33.15  ?  27  LEU B O      1 
ATOM   3001 C CB     . LEU B 2 27  ? 18.826 -8.900  37.820 1.00 35.39  ?  27  LEU B CB     1 
ATOM   3002 C CG     . LEU B 2 27  ? 19.517 -7.670  37.265 1.00 39.23  ?  27  LEU B CG     1 
ATOM   3003 C CD1    . LEU B 2 27  ? 20.803 -8.076  36.580 1.00 36.28  ?  27  LEU B CD1    1 
ATOM   3004 C CD2    . LEU B 2 27  ? 18.605 -6.916  36.316 1.00 45.49  ?  27  LEU B CD2    1 
ATOM   3005 N N      . SER B 2 28  ? 17.068 -10.843 39.638 1.00 41.13  ?  28  SER B N      1 
ATOM   3006 C CA     . SER B 2 28  ? 16.181 -11.996 39.720 1.00 39.33  ?  28  SER B CA     1 
ATOM   3007 C C      . SER B 2 28  ? 14.845 -11.621 40.330 1.00 44.76  ?  28  SER B C      1 
ATOM   3008 O O      . SER B 2 28  ? 13.791 -12.029 39.825 1.00 46.44  ?  28  SER B O      1 
ATOM   3009 C CB     . SER B 2 28  ? 16.834 -13.108 40.526 1.00 44.30  ?  28  SER B CB     1 
ATOM   3010 O OG     . SER B 2 28  ? 17.859 -13.709 39.762 1.00 52.84  ?  28  SER B OG     1 
ATOM   3011 N N      . VAL B 2 29  ? 14.865 -10.831 41.414 1.00 38.77  ?  29  VAL B N      1 
ATOM   3012 C CA     . VAL B 2 29  ? 13.630 -10.516 42.124 1.00 35.04  ?  29  VAL B CA     1 
ATOM   3013 C C      . VAL B 2 29  ? 12.726 -9.650  41.260 1.00 40.75  ?  29  VAL B C      1 
ATOM   3014 O O      . VAL B 2 29  ? 11.503 -9.826  41.240 1.00 38.06  ?  29  VAL B O      1 
ATOM   3015 C CB     . VAL B 2 29  ? 13.944 -9.857  43.482 1.00 36.86  ?  29  VAL B CB     1 
ATOM   3016 C CG1    . VAL B 2 29  ? 12.704 -9.160  44.059 1.00 35.41  ?  29  VAL B CG1    1 
ATOM   3017 C CG2    . VAL B 2 29  ? 14.472 -10.910 44.458 1.00 32.07  ?  29  VAL B CG2    1 
ATOM   3018 N N      . LYS B 2 30  ? 13.309 -8.702  40.524 1.00 61.71  ?  30  LYS B N      1 
ATOM   3019 C CA     . LYS B 2 30  ? 12.502 -7.904  39.603 1.00 68.12  ?  30  LYS B CA     1 
ATOM   3020 C C      . LYS B 2 30  ? 11.914 -8.774  38.491 1.00 67.07  ?  30  LYS B C      1 
ATOM   3021 O O      . LYS B 2 30  ? 10.781 -8.549  38.049 1.00 66.30  ?  30  LYS B O      1 
ATOM   3022 C CB     . LYS B 2 30  ? 13.339 -6.765  39.022 1.00 67.85  ?  30  LYS B CB     1 
ATOM   3023 C CG     . LYS B 2 30  ? 12.555 -5.514  38.649 1.00 66.95  ?  30  LYS B CG     1 
ATOM   3024 C CD     . LYS B 2 30  ? 13.464 -4.530  37.919 1.00 64.28  ?  30  LYS B CD     1 
ATOM   3025 C CE     . LYS B 2 30  ? 12.781 -3.195  37.663 1.00 61.44  ?  30  LYS B CE     1 
ATOM   3026 N NZ     . LYS B 2 30  ? 13.672 -2.233  36.928 1.00 54.61  ?  30  LYS B NZ     1 
ATOM   3027 N N      . TYR B 2 31  ? 12.629 -9.746  37.973 1.00 60.08  ?  31  TYR B N      1 
ATOM   3028 C CA     . TYR B 2 31  ? 12.031 -10.614 36.979 1.00 56.43  ?  31  TYR B CA     1 
ATOM   3029 C C      . TYR B 2 31  ? 10.864 -11.377 37.556 1.00 57.81  ?  31  TYR B C      1 
ATOM   3030 O O      . TYR B 2 31  ? 9.795  -11.415 36.969 1.00 61.20  ?  31  TYR B O      1 
ATOM   3031 C CB     . TYR B 2 31  ? 13.069 -11.574 36.394 1.00 51.17  ?  31  TYR B CB     1 
ATOM   3032 C CG     . TYR B 2 31  ? 12.498 -12.812 35.793 1.00 47.54  ?  31  TYR B CG     1 
ATOM   3033 C CD1    . TYR B 2 31  ? 11.788 -12.761 34.612 1.00 45.80  ?  31  TYR B CD1    1 
ATOM   3034 C CD2    . TYR B 2 31  ? 12.668 -14.036 36.408 1.00 49.29  ?  31  TYR B CD2    1 
ATOM   3035 C CE1    . TYR B 2 31  ? 11.252 -13.895 34.064 1.00 41.90  ?  31  TYR B CE1    1 
ATOM   3036 C CE2    . TYR B 2 31  ? 12.140 -15.177 35.865 1.00 42.24  ?  31  TYR B CE2    1 
ATOM   3037 C CZ     . TYR B 2 31  ? 11.436 -15.090 34.696 1.00 42.98  ?  31  TYR B CZ     1 
ATOM   3038 O OH     . TYR B 2 31  ? 10.915 -16.215 34.156 1.00 56.04  ?  31  TYR B OH     1 
ATOM   3039 N N      . LEU B 2 32  ? 11.049 -11.976 38.710 1.00 50.22  ?  32  LEU B N      1 
ATOM   3040 C CA     . LEU B 2 32  ? 10.010 -12.792 39.276 1.00 47.39  ?  32  LEU B CA     1 
ATOM   3041 C C      . LEU B 2 32  ? 8.794  -11.993 39.638 1.00 55.73  ?  32  LEU B C      1 
ATOM   3042 O O      . LEU B 2 32  ? 7.693  -12.468 39.462 1.00 59.25  ?  32  LEU B O      1 
ATOM   3043 C CB     . LEU B 2 32  ? 10.547 -13.568 40.463 1.00 42.03  ?  32  LEU B CB     1 
ATOM   3044 C CG     . LEU B 2 32  ? 11.583 -14.618 40.098 1.00 40.32  ?  32  LEU B CG     1 
ATOM   3045 C CD1    . LEU B 2 32  ? 12.339 -15.071 41.330 1.00 39.99  ?  32  LEU B CD1    1 
ATOM   3046 C CD2    . LEU B 2 32  ? 10.890 -15.781 39.422 1.00 36.35  ?  32  LEU B CD2    1 
ATOM   3047 N N      . GLU B 2 33  ? 8.972  -10.762 40.086 1.00 69.14  ?  33  GLU B N      1 
ATOM   3048 C CA     . GLU B 2 33  ? 7.859  -9.923  40.506 1.00 73.13  ?  33  GLU B CA     1 
ATOM   3049 C C      . GLU B 2 33  ? 7.041  -9.323  39.396 1.00 72.25  ?  33  GLU B C      1 
ATOM   3050 O O      . GLU B 2 33  ? 6.038  -8.690  39.667 1.00 75.42  ?  33  GLU B O      1 
ATOM   3051 C CB     . GLU B 2 33  ? 8.343  -8.803  41.400 1.00 76.62  ?  33  GLU B CB     1 
ATOM   3052 C CG     . GLU B 2 33  ? 7.877  -8.942  42.838 1.00 83.26  ?  33  GLU B CG     1 
ATOM   3053 C CD     . GLU B 2 33  ? 7.564  -7.613  43.497 1.00 86.53  ?  33  GLU B CD     1 
ATOM   3054 O OE1    . GLU B 2 33  ? 8.322  -6.642  43.271 1.00 82.75  ?  33  GLU B OE1    1 
ATOM   3055 O OE2    . GLU B 2 33  ? 6.560  -7.544  44.244 1.00 84.74  -1 33  GLU B OE2    1 
ATOM   3056 N N      . LYS B 2 34  ? 7.455  -9.512  38.149 1.00 52.35  ?  34  LYS B N      1 
ATOM   3057 C CA     . LYS B 2 34  ? 6.720  -9.012  37.009 1.00 44.46  ?  34  LYS B CA     1 
ATOM   3058 C C      . LYS B 2 34  ? 5.915  -10.147 36.524 1.00 45.92  ?  34  LYS B C      1 
ATOM   3059 O O      . LYS B 2 34  ? 4.715  -10.033 36.348 1.00 41.16  ?  34  LYS B O      1 
ATOM   3060 C CB     . LYS B 2 34  ? 7.695  -8.651  35.921 1.00 40.56  ?  34  LYS B CB     1 
ATOM   3061 C CG     . LYS B 2 34  ? 7.068  -8.009  34.703 1.00 41.31  ?  34  LYS B CG     1 
ATOM   3062 C CD     . LYS B 2 34  ? 7.261  -6.505  34.717 1.00 38.93  ?  34  LYS B CD     1 
ATOM   3063 C CE     . LYS B 2 34  ? 6.515  -5.853  33.569 1.00 41.07  ?  34  LYS B CE     1 
ATOM   3064 N NZ     . LYS B 2 34  ? 5.986  -4.515  33.936 1.00 42.81  ?  34  LYS B NZ     1 
ATOM   3065 N N      . SER B 2 35  ? 6.586  -11.264 36.320 1.00 57.12  ?  35  SER B N      1 
ATOM   3066 C CA     . SER B 2 35  ? 5.933  -12.456 35.834 1.00 57.61  ?  35  SER B CA     1 
ATOM   3067 C C      . SER B 2 35  ? 4.857  -12.897 36.792 1.00 63.62  ?  35  SER B C      1 
ATOM   3068 O O      . SER B 2 35  ? 3.679  -12.862 36.459 1.00 64.16  ?  35  SER B O      1 
ATOM   3069 C CB     . SER B 2 35  ? 6.981  -13.540 35.683 1.00 52.98  ?  35  SER B CB     1 
ATOM   3070 O OG     . SER B 2 35  ? 8.078  -13.084 34.923 1.00 52.01  ?  35  SER B OG     1 
ATOM   3071 N N      . LEU B 2 36  ? 5.250  -13.308 37.984 1.00 81.39  ?  36  LEU B N      1 
ATOM   3072 C CA     . LEU B 2 36  ? 4.293  -13.706 38.991 1.00 80.98  ?  36  LEU B CA     1 
ATOM   3073 C C      . LEU B 2 36  ? 4.249  -12.527 39.882 1.00 82.87  ?  36  LEU B C      1 
ATOM   3074 O O      . LEU B 2 36  ? 5.101  -12.375 40.735 1.00 87.70  ?  36  LEU B O      1 
ATOM   3075 C CB     . LEU B 2 36  ? 4.800  -14.893 39.818 1.00 75.59  ?  36  LEU B CB     1 
ATOM   3076 C CG     . LEU B 2 36  ? 5.013  -16.294 39.266 1.00 73.09  ?  36  LEU B CG     1 
ATOM   3077 C CD1    . LEU B 2 36  ? 4.967  -16.308 37.752 1.00 67.06  ?  36  LEU B CD1    1 
ATOM   3078 C CD2    . LEU B 2 36  ? 6.338  -16.831 39.778 1.00 71.76  ?  36  LEU B CD2    1 
ATOM   3079 N N      . GLY B 2 37  ? 3.266  -11.677 39.712 1.00 79.32  ?  37  GLY B N      1 
ATOM   3080 C CA     . GLY B 2 37  ? 3.259  -10.466 40.491 1.00 81.90  ?  37  GLY B CA     1 
ATOM   3081 C C      . GLY B 2 37  ? 1.906  -10.150 41.041 1.00 83.44  ?  37  GLY B C      1 
ATOM   3082 O O      . GLY B 2 37  ? 0.907  -10.481 40.401 1.00 80.43  ?  37  GLY B O      1 
ATOM   3083 N N      . LYS B 2 38  ? 1.856  -9.518  42.210 1.00 118.20 ?  38  LYS B N      1 
ATOM   3084 C CA     . LYS B 2 38  ? 0.593  -9.161  42.880 1.00 118.76 ?  38  LYS B CA     1 
ATOM   3085 C C      . LYS B 2 38  ? -0.058 -10.358 43.520 1.00 114.20 ?  38  LYS B C      1 
ATOM   3086 O O      . LYS B 2 38  ? -0.917 -10.189 44.362 1.00 115.50 ?  38  LYS B O      1 
ATOM   3087 C CB     . LYS B 2 38  ? -0.397 -8.356  42.006 1.00 119.08 ?  38  LYS B CB     1 
ATOM   3088 C CG     . LYS B 2 38  ? -1.674 -7.915  42.690 1.00 117.88 ?  38  LYS B CG     1 
ATOM   3089 C CD     . LYS B 2 38  ? -2.519 -7.099  41.728 1.00 113.45 ?  38  LYS B CD     1 
ATOM   3090 C CE     . LYS B 2 38  ? -3.819 -6.658  42.372 1.00 111.08 ?  38  LYS B CE     1 
ATOM   3091 N NZ     . LYS B 2 38  ? -4.644 -5.858  41.425 1.00 109.23 ?  38  LYS B NZ     1 
ATOM   3092 N N      . LYS B 2 39  ? 0.313  -11.563 43.128 1.00 67.99  ?  39  LYS B N      1 
ATOM   3093 C CA     . LYS B 2 39  ? -0.195 -12.723 43.808 1.00 70.63  ?  39  LYS B CA     1 
ATOM   3094 C C      . LYS B 2 39  ? 0.264  -12.571 45.238 1.00 74.68  ?  39  LYS B C      1 
ATOM   3095 O O      . LYS B 2 39  ? 1.464  -12.492 45.500 1.00 76.17  ?  39  LYS B O      1 
ATOM   3096 C CB     . LYS B 2 39  ? 0.390  -13.985 43.203 1.00 68.84  ?  39  LYS B CB     1 
ATOM   3097 C CG     . LYS B 2 39  ? -0.505 -15.200 43.309 1.00 67.44  ?  39  LYS B CG     1 
ATOM   3098 C CD     . LYS B 2 39  ? -0.659 -15.863 41.952 1.00 68.02  ?  39  LYS B CD     1 
ATOM   3099 C CE     . LYS B 2 39  ? -0.772 -17.369 42.094 1.00 70.00  ?  39  LYS B CE     1 
ATOM   3100 N NZ     . LYS B 2 39  ? -1.671 -17.739 43.218 1.00 72.96  ?  39  LYS B NZ     1 
ATOM   3101 N N      . LYS B 2 40  ? -0.667 -12.503 46.166 1.00 72.93  ?  40  LYS B N      1 
ATOM   3102 C CA     . LYS B 2 40  ? -0.271 -12.275 47.531 1.00 76.71  ?  40  LYS B CA     1 
ATOM   3103 C C      . LYS B 2 40  ? 0.213  -13.563 48.141 1.00 73.95  ?  40  LYS B C      1 
ATOM   3104 O O      . LYS B 2 40  ? 0.645  -13.585 49.278 1.00 69.24  ?  40  LYS B O      1 
ATOM   3105 C CB     . LYS B 2 40  ? -1.416 -11.646 48.317 1.00 79.24  ?  40  LYS B CB     1 
ATOM   3106 C CG     . LYS B 2 40  ? -2.318 -10.768 47.470 1.00 78.38  ?  40  LYS B CG     1 
ATOM   3107 C CD     . LYS B 2 40  ? -1.785 -9.352  47.390 1.00 78.74  ?  40  LYS B CD     1 
ATOM   3108 C CE     . LYS B 2 40  ? -2.815 -8.412  46.790 1.00 82.45  ?  40  LYS B CE     1 
ATOM   3109 N NZ     . LYS B 2 40  ? -4.015 -8.281  47.662 1.00 84.47  ?  40  LYS B NZ     1 
ATOM   3110 N N      . GLU B 2 41  ? 0.120  -14.645 47.393 1.00 89.34  ?  41  GLU B N      1 
ATOM   3111 C CA     . GLU B 2 41  ? 0.659  -15.895 47.858 1.00 88.90  ?  41  GLU B CA     1 
ATOM   3112 C C      . GLU B 2 41  ? 2.145  -15.692 47.845 1.00 93.71  ?  41  GLU B C      1 
ATOM   3113 O O      . GLU B 2 41  ? 2.857  -16.133 48.740 1.00 94.66  ?  41  GLU B O      1 
ATOM   3114 C CB     . GLU B 2 41  ? 0.287  -16.999 46.892 1.00 89.13  ?  41  GLU B CB     1 
ATOM   3115 C CG     . GLU B 2 41  ? 0.891  -18.346 47.228 1.00 94.23  ?  41  GLU B CG     1 
ATOM   3116 C CD     . GLU B 2 41  ? 0.945  -19.263 46.029 1.00 99.76  ?  41  GLU B CD     1 
ATOM   3117 O OE1    . GLU B 2 41  ? 0.788  -18.759 44.903 1.00 102.85 ?  41  GLU B OE1    1 
ATOM   3118 O OE2    . GLU B 2 41  ? 1.149  -20.481 46.208 1.00 99.66  -1 41  GLU B OE2    1 
ATOM   3119 N N      . PHE B 2 42  ? 2.624  -14.998 46.833 1.00 75.00  ?  42  PHE B N      1 
ATOM   3120 C CA     . PHE B 2 42  ? 4.041  -14.775 46.683 1.00 69.74  ?  42  PHE B CA     1 
ATOM   3121 C C      . PHE B 2 42  ? 4.500  -13.531 47.413 1.00 70.40  ?  42  PHE B C      1 
ATOM   3122 O O      . PHE B 2 42  ? 5.661  -13.188 47.346 1.00 73.24  ?  42  PHE B O      1 
ATOM   3123 C CB     . PHE B 2 42  ? 4.351  -14.664 45.199 1.00 67.27  ?  42  PHE B CB     1 
ATOM   3124 C CG     . PHE B 2 42  ? 3.990  -15.881 44.412 1.00 65.28  ?  42  PHE B CG     1 
ATOM   3125 C CD1    . PHE B 2 42  ? 4.509  -17.113 44.748 1.00 63.09  ?  42  PHE B CD1    1 
ATOM   3126 C CD2    . PHE B 2 42  ? 3.146  -15.790 43.328 1.00 64.45  ?  42  PHE B CD2    1 
ATOM   3127 C CE1    . PHE B 2 42  ? 4.187  -18.234 44.023 1.00 60.88  ?  42  PHE B CE1    1 
ATOM   3128 C CE2    . PHE B 2 42  ? 2.821  -16.906 42.595 1.00 64.22  ?  42  PHE B CE2    1 
ATOM   3129 C CZ     . PHE B 2 42  ? 3.342  -18.131 42.942 1.00 63.32  ?  42  PHE B CZ     1 
ATOM   3130 N N      . SER B 2 43  ? 3.591  -12.843 48.082 1.00 63.31  ?  43  SER B N      1 
ATOM   3131 C CA     . SER B 2 43  ? 3.928  -11.652 48.846 1.00 57.84  ?  43  SER B CA     1 
ATOM   3132 C C      . SER B 2 43  ? 5.004  -11.973 49.825 1.00 56.65  ?  43  SER B C      1 
ATOM   3133 O O      . SER B 2 43  ? 5.949  -11.221 49.989 1.00 58.46  ?  43  SER B O      1 
ATOM   3134 C CB     . SER B 2 43  ? 2.692  -11.140 49.589 1.00 56.32  ?  43  SER B CB     1 
ATOM   3135 O OG     . SER B 2 43  ? 2.501  -11.742 50.843 1.00 50.52  ?  43  SER B OG     1 
ATOM   3136 N N      . GLY B 2 44  ? 4.866  -13.112 50.463 1.00 62.13  ?  44  GLY B N      1 
ATOM   3137 C CA     . GLY B 2 44  ? 5.845  -13.528 51.442 1.00 58.97  ?  44  GLY B CA     1 
ATOM   3138 C C      . GLY B 2 44  ? 7.240  -13.615 50.863 1.00 54.11  ?  44  GLY B C      1 
ATOM   3139 O O      . GLY B 2 44  ? 8.180  -13.026 51.389 1.00 59.16  ?  44  GLY B O      1 
ATOM   3140 N N      . PHE B 2 45  ? 7.387  -14.355 49.768 1.00 39.50  ?  45  PHE B N      1 
ATOM   3141 C CA     . PHE B 2 45  ? 8.714  -14.639 49.228 1.00 38.36  ?  45  PHE B CA     1 
ATOM   3142 C C      . PHE B 2 45  ? 9.514  -13.360 48.972 1.00 39.08  ?  45  PHE B C      1 
ATOM   3143 O O      . PHE B 2 45  ? 10.689 -13.274 49.337 1.00 31.85  ?  45  PHE B O      1 
ATOM   3144 C CB     . PHE B 2 45  ? 8.584  -15.463 47.944 1.00 39.67  ?  45  PHE B CB     1 
ATOM   3145 C CG     . PHE B 2 45  ? 9.871  -15.597 47.191 1.00 43.38  ?  45  PHE B CG     1 
ATOM   3146 C CD1    . PHE B 2 45  ? 10.816 -16.536 47.578 1.00 41.69  ?  45  PHE B CD1    1 
ATOM   3147 C CD2    . PHE B 2 45  ? 10.148 -14.760 46.110 1.00 44.74  ?  45  PHE B CD2    1 
ATOM   3148 C CE1    . PHE B 2 45  ? 11.997 -16.639 46.908 1.00 39.96  ?  45  PHE B CE1    1 
ATOM   3149 C CE2    . PHE B 2 45  ? 11.330 -14.867 45.423 1.00 36.95  ?  45  PHE B CE2    1 
ATOM   3150 C CZ     . PHE B 2 45  ? 12.251 -15.806 45.825 1.00 43.06  ?  45  PHE B CZ     1 
ATOM   3151 N N      . PHE B 2 46  ? 8.939  -12.354 48.370 1.00 64.48  ?  46  PHE B N      1 
ATOM   3152 C CA     . PHE B 2 46  ? 9.678  -11.151 48.120 1.00 65.74  ?  46  PHE B CA     1 
ATOM   3153 C C      . PHE B 2 46  ? 9.838  -10.349 49.402 1.00 69.96  ?  46  PHE B C      1 
ATOM   3154 O O      . PHE B 2 46  ? 10.886 -9.790  49.653 1.00 76.45  ?  46  PHE B O      1 
ATOM   3155 C CB     . PHE B 2 46  ? 9.010  -10.303 47.034 1.00 68.84  ?  46  PHE B CB     1 
ATOM   3156 C CG     . PHE B 2 46  ? 8.682  -11.052 45.779 1.00 75.28  ?  46  PHE B CG     1 
ATOM   3157 C CD1    . PHE B 2 46  ? 9.664  -11.333 44.848 1.00 79.40  ?  46  PHE B CD1    1 
ATOM   3158 C CD2    . PHE B 2 46  ? 7.388  -11.452 45.516 1.00 77.86  ?  46  PHE B CD2    1 
ATOM   3159 C CE1    . PHE B 2 46  ? 9.363  -12.022 43.689 1.00 80.24  ?  46  PHE B CE1    1 
ATOM   3160 C CE2    . PHE B 2 46  ? 7.080  -12.141 44.361 1.00 81.10  ?  46  PHE B CE2    1 
ATOM   3161 C CZ     . PHE B 2 46  ? 8.070  -12.426 43.445 1.00 81.46  ?  46  PHE B CZ     1 
ATOM   3162 N N      . GLU B 2 47  ? 8.808  -10.273 50.217 1.00 75.03  ?  47  GLU B N      1 
ATOM   3163 C CA     . GLU B 2 47  ? 8.967  -9.586  51.493 1.00 77.08  ?  47  GLU B CA     1 
ATOM   3164 C C      . GLU B 2 47  ? 10.179 -10.107 52.268 1.00 82.15  ?  47  GLU B C      1 
ATOM   3165 O O      . GLU B 2 47  ? 10.893 -9.333  52.917 1.00 83.95  ?  47  GLU B O      1 
ATOM   3166 C CB     . GLU B 2 47  ? 7.682  -9.735  52.308 1.00 76.68  ?  47  GLU B CB     1 
ATOM   3167 C CG     . GLU B 2 47  ? 7.874  -9.635  53.804 1.00 84.03  ?  47  GLU B CG     1 
ATOM   3168 C CD     . GLU B 2 47  ? 7.931  -8.199  54.297 1.00 90.28  ?  47  GLU B CD     1 
ATOM   3169 O OE1    . GLU B 2 47  ? 8.059  -7.275  53.465 1.00 91.72  ?  47  GLU B OE1    1 
ATOM   3170 O OE2    . GLU B 2 47  ? 7.841  -7.991  55.524 1.00 92.00  -1 47  GLU B OE2    1 
ATOM   3171 N N      . ASP B 2 48  ? 10.419 -11.423 52.225 1.00 73.93  ?  48  ASP B N      1 
ATOM   3172 C CA     . ASP B 2 48  ? 11.514 -12.010 52.995 1.00 70.65  ?  48  ASP B CA     1 
ATOM   3173 C C      . ASP B 2 48  ? 12.850 -11.884 52.290 1.00 66.16  ?  48  ASP B C      1 
ATOM   3174 O O      . ASP B 2 48  ? 13.885 -11.774 52.951 1.00 66.70  ?  48  ASP B O      1 
ATOM   3175 C CB     . ASP B 2 48  ? 11.222 -13.476 53.308 1.00 71.99  ?  48  ASP B CB     1 
ATOM   3176 C CG     . ASP B 2 48  ? 10.075 -13.631 54.307 1.00 80.82  ?  48  ASP B CG     1 
ATOM   3177 O OD1    . ASP B 2 48  ? 9.884  -12.711 55.141 1.00 82.56  ?  48  ASP B OD1    1 
ATOM   3178 O OD2    . ASP B 2 48  ? 9.360  -14.656 54.250 1.00 82.25  -1 48  ASP B OD2    1 
ATOM   3179 N N      . ILE B 2 49  ? 12.852 -11.908 50.958 1.00 51.99  ?  49  ILE B N      1 
ATOM   3180 C CA     . ILE B 2 49  ? 14.091 -11.683 50.228 1.00 42.08  ?  49  ILE B CA     1 
ATOM   3181 C C      . ILE B 2 49  ? 14.567 -10.250 50.444 1.00 50.07  ?  49  ILE B C      1 
ATOM   3182 O O      . ILE B 2 49  ? 15.773 -9.988  50.558 1.00 50.71  ?  49  ILE B O      1 
ATOM   3183 C CB     . ILE B 2 49  ? 13.895 -12.025 48.738 1.00 43.23  ?  49  ILE B CB     1 
ATOM   3184 C CG1    . ILE B 2 49  ? 13.598 -13.520 48.580 1.00 52.06  ?  49  ILE B CG1    1 
ATOM   3185 C CG2    . ILE B 2 49  ? 15.107 -11.624 47.893 1.00 41.05  ?  49  ILE B CG2    1 
ATOM   3186 C CD1    . ILE B 2 49  ? 14.728 -14.438 49.033 1.00 58.03  ?  49  ILE B CD1    1 
ATOM   3187 N N      . GLU B 2 50  ? 13.660 -9.293  50.539 1.00 53.43  ?  50  GLU B N      1 
ATOM   3188 C CA     . GLU B 2 50  ? 14.053 -7.903  50.662 1.00 48.57  ?  50  GLU B CA     1 
ATOM   3189 C C      . GLU B 2 50  ? 14.801 -7.663  51.947 1.00 48.06  ?  50  GLU B C      1 
ATOM   3190 O O      . GLU B 2 50  ? 15.715 -6.867  51.983 1.00 42.65  ?  50  GLU B O      1 
ATOM   3191 C CB     . GLU B 2 50  ? 12.839 -7.018  50.486 1.00 50.90  ?  50  GLU B CB     1 
ATOM   3192 C CG     . GLU B 2 50  ? 12.344 -6.887  49.057 1.00 51.98  ?  50  GLU B CG     1 
ATOM   3193 C CD     . GLU B 2 50  ? 11.474 -5.659  48.851 1.00 53.77  ?  50  GLU B CD     1 
ATOM   3194 O OE1    . GLU B 2 50  ? 11.524 -4.750  49.693 1.00 62.81  ?  50  GLU B OE1    1 
ATOM   3195 O OE2    . GLU B 2 50  ? 10.751 -5.595  47.844 1.00 43.98  -1 50  GLU B OE2    1 
ATOM   3196 N N      . LYS B 2 51  ? 14.382 -8.309  53.013 1.00 49.74  ?  51  LYS B N      1 
ATOM   3197 C CA     . LYS B 2 51  ? 15.106 -8.280  54.284 1.00 46.66  ?  51  LYS B CA     1 
ATOM   3198 C C      . LYS B 2 51  ? 16.408 -9.055  54.243 1.00 45.94  ?  51  LYS B C      1 
ATOM   3199 O O      . LYS B 2 51  ? 17.330 -8.722  54.945 1.00 47.76  ?  51  LYS B O      1 
ATOM   3200 C CB     . LYS B 2 51  ? 14.217 -8.789  55.411 1.00 42.11  ?  51  LYS B CB     1 
ATOM   3201 C CG     . LYS B 2 51  ? 12.875 -8.106  55.530 1.00 35.87  ?  51  LYS B CG     1 
ATOM   3202 C CD     . LYS B 2 51  ? 12.059 -8.814  56.585 1.00 38.32  ?  51  LYS B CD     1 
ATOM   3203 C CE     . LYS B 2 51  ? 10.651 -8.272  56.670 1.00 46.11  ?  51  LYS B CE     1 
ATOM   3204 N NZ     . LYS B 2 51  ? 10.542 -6.883  57.193 1.00 45.33  ?  51  LYS B NZ     1 
ATOM   3205 N N      . LEU B 2 52  ? 16.471 -10.111 53.450 1.00 49.10  ?  52  LEU B N      1 
ATOM   3206 C CA     . LEU B 2 52  ? 17.674 -10.924 53.347 1.00 49.16  ?  52  LEU B CA     1 
ATOM   3207 C C      . LEU B 2 52  ? 18.736 -10.181 52.583 1.00 53.28  ?  52  LEU B C      1 
ATOM   3208 O O      . LEU B 2 52  ? 19.913 -10.287 52.879 1.00 56.39  ?  52  LEU B O      1 
ATOM   3209 C CB     . LEU B 2 52  ? 17.383 -12.266 52.686 1.00 43.01  ?  52  LEU B CB     1 
ATOM   3210 C CG     . LEU B 2 52  ? 17.024 -13.450 53.572 1.00 45.74  ?  52  LEU B CG     1 
ATOM   3211 C CD1    . LEU B 2 52  ? 16.774 -14.682 52.722 1.00 45.24  ?  52  LEU B CD1    1 
ATOM   3212 C CD2    . LEU B 2 52  ? 18.117 -13.713 54.587 1.00 39.51  ?  52  LEU B CD2    1 
ATOM   3213 N N      . TYR B 2 53  ? 18.327 -9.440  51.575 1.00 41.19  ?  53  TYR B N      1 
ATOM   3214 C CA     . TYR B 2 53  ? 19.261 -8.629  50.864 1.00 38.12  ?  53  TYR B CA     1 
ATOM   3215 C C      . TYR B 2 53  ? 19.809 -7.547  51.734 1.00 38.20  ?  53  TYR B C      1 
ATOM   3216 O O      . TYR B 2 53  ? 20.983 -7.233  51.653 1.00 49.51  ?  53  TYR B O      1 
ATOM   3217 C CB     . TYR B 2 53  ? 18.616 -8.064  49.612 1.00 37.32  ?  53  TYR B CB     1 
ATOM   3218 C CG     . TYR B 2 53  ? 19.410 -7.024  48.882 1.00 33.95  ?  53  TYR B CG     1 
ATOM   3219 C CD1    . TYR B 2 53  ? 20.393 -7.383  47.986 1.00 40.06  ?  53  TYR B CD1    1 
ATOM   3220 C CD2    . TYR B 2 53  ? 19.150 -5.682  49.065 1.00 24.38  ?  53  TYR B CD2    1 
ATOM   3221 C CE1    . TYR B 2 53  ? 21.110 -6.430  47.307 1.00 36.03  ?  53  TYR B CE1    1 
ATOM   3222 C CE2    . TYR B 2 53  ? 19.862 -4.729  48.391 1.00 30.46  ?  53  TYR B CE2    1 
ATOM   3223 C CZ     . TYR B 2 53  ? 20.840 -5.103  47.516 1.00 36.55  ?  53  TYR B CZ     1 
ATOM   3224 O OH     . TYR B 2 53  ? 21.541 -4.136  46.851 1.00 37.76  ?  53  TYR B OH     1 
ATOM   3225 N N      . PHE B 2 54  ? 18.963 -6.952  52.551 1.00 32.95  ?  54  PHE B N      1 
ATOM   3226 C CA     . PHE B 2 54  ? 19.408 -5.903  53.411 1.00 28.85  ?  54  PHE B CA     1 
ATOM   3227 C C      . PHE B 2 54  ? 20.411 -6.424  54.389 1.00 30.62  ?  54  PHE B C      1 
ATOM   3228 O O      . PHE B 2 54  ? 21.456 -5.844  54.582 1.00 37.92  ?  54  PHE B O      1 
ATOM   3229 C CB     . PHE B 2 54  ? 18.266 -5.228  54.146 1.00 25.09  ?  54  PHE B CB     1 
ATOM   3230 C CG     . PHE B 2 54  ? 18.713 -4.127  55.058 1.00 29.37  ?  54  PHE B CG     1 
ATOM   3231 C CD1    . PHE B 2 54  ? 18.856 -2.847  54.584 1.00 34.59  ?  54  PHE B CD1    1 
ATOM   3232 C CD2    . PHE B 2 54  ? 19.014 -4.379  56.380 1.00 29.45  ?  54  PHE B CD2    1 
ATOM   3233 C CE1    . PHE B 2 54  ? 19.292 -1.841  55.405 1.00 34.86  ?  54  PHE B CE1    1 
ATOM   3234 C CE2    . PHE B 2 54  ? 19.450 -3.378  57.206 1.00 31.90  ?  54  PHE B CE2    1 
ATOM   3235 C CZ     . PHE B 2 54  ? 19.586 -2.105  56.720 1.00 37.20  ?  54  PHE B CZ     1 
ATOM   3236 N N      . LYS B 2 55  ? 20.070 -7.516  55.026 1.00 40.47  ?  55  LYS B N      1 
ATOM   3237 C CA     . LYS B 2 55  ? 21.024 -8.103  55.965 1.00 47.01  ?  55  LYS B CA     1 
ATOM   3238 C C      . LYS B 2 55  ? 22.364 -8.417  55.309 1.00 52.85  ?  55  LYS B C      1 
ATOM   3239 O O      . LYS B 2 55  ? 23.356 -8.619  56.028 1.00 56.32  ?  55  LYS B O      1 
ATOM   3240 C CB     . LYS B 2 55  ? 20.448 -9.381  56.585 1.00 49.36  ?  55  LYS B CB     1 
ATOM   3241 C CG     . LYS B 2 55  ? 19.224 -9.165  57.474 1.00 52.62  ?  55  LYS B CG     1 
ATOM   3242 C CD     . LYS B 2 55  ? 19.551 -8.425  58.760 1.00 50.59  ?  55  LYS B CD     1 
ATOM   3243 C CE     . LYS B 2 55  ? 18.285 -8.250  59.586 1.00 56.13  ?  55  LYS B CE     1 
ATOM   3244 N NZ     . LYS B 2 55  ? 18.510 -7.456  60.835 1.00 65.02  ?  55  LYS B NZ     1 
ATOM   3245 N N      . GLN B 2 56  ? 22.430 -8.397  53.971 1.00 39.65  ?  56  GLN B N      1 
ATOM   3246 C CA     . GLN B 2 56  ? 23.581 -8.873  53.213 1.00 36.10  ?  56  GLN B CA     1 
ATOM   3247 C C      . GLN B 2 56  ? 23.732 -10.393 53.276 1.00 38.75  ?  56  GLN B C      1 
ATOM   3248 O O      . GLN B 2 56  ? 24.842 -10.905 53.153 1.00 46.76  ?  56  GLN B O      1 
ATOM   3249 C CB     . GLN B 2 56  ? 24.889 -8.211  53.679 1.00 30.05  ?  56  GLN B CB     1 
ATOM   3250 C CG     . GLN B 2 56  ? 25.163 -6.793  53.170 1.00 33.22  ?  56  GLN B CG     1 
ATOM   3251 C CD     . GLN B 2 56  ? 26.415 -6.148  53.834 1.00 33.06  ?  56  GLN B CD     1 
ATOM   3252 O OE1    . GLN B 2 56  ? 26.339 -5.058  54.419 1.00 33.10  ?  56  GLN B OE1    1 
ATOM   3253 N NE2    . GLN B 2 56  ? 27.561 -6.830  53.743 1.00 30.23  ?  56  GLN B NE2    1 
ATOM   3254 N N      . ASN B 2 57  ? 22.630 -11.101 53.400 1.00 40.69  ?  57  ASN B N      1 
ATOM   3255 C CA     . ASN B 2 57  ? 22.685 -12.547 53.369 1.00 49.56  ?  57  ASN B CA     1 
ATOM   3256 C C      . ASN B 2 57  ? 22.316 -12.969 51.967 1.00 50.89  ?  57  ASN B C      1 
ATOM   3257 O O      . ASN B 2 57  ? 21.202 -13.391 51.714 1.00 49.79  ?  57  ASN B O      1 
ATOM   3258 C CB     . ASN B 2 57  ? 21.777 -13.184 54.423 1.00 52.56  ?  57  ASN B CB     1 
ATOM   3259 C CG     . ASN B 2 57  ? 22.036 -14.674 54.603 1.00 58.33  ?  57  ASN B CG     1 
ATOM   3260 O OD1    . ASN B 2 57  ? 23.156 -15.141 54.431 1.00 60.46  ?  57  ASN B OD1    1 
ATOM   3261 N ND2    . ASN B 2 57  ? 21.003 -15.425 54.955 1.00 62.74  ?  57  ASN B ND2    1 
ATOM   3262 N N      . TYR B 2 58  ? 23.253 -12.820 51.050 1.00 51.16  ?  58  TYR B N      1 
ATOM   3263 C CA     . TYR B 2 58  ? 23.028 -13.157 49.670 1.00 47.54  ?  58  TYR B CA     1 
ATOM   3264 C C      . TYR B 2 58  ? 22.951 -14.618 49.380 1.00 47.89  ?  58  TYR B C      1 
ATOM   3265 O O      . TYR B 2 58  ? 22.092 -15.053 48.651 1.00 47.63  ?  58  TYR B O      1 
ATOM   3266 C CB     . TYR B 2 58  ? 24.107 -12.484 48.826 1.00 48.56  ?  58  TYR B CB     1 
ATOM   3267 C CG     . TYR B 2 58  ? 24.160 -10.980 48.930 1.00 51.99  ?  58  TYR B CG     1 
ATOM   3268 C CD1    . TYR B 2 58  ? 23.159 -10.263 49.564 1.00 50.05  ?  58  TYR B CD1    1 
ATOM   3269 C CD2    . TYR B 2 58  ? 25.212 -10.276 48.377 1.00 55.68  ?  58  TYR B CD2    1 
ATOM   3270 C CE1    . TYR B 2 58  ? 23.213 -8.893  49.652 1.00 50.32  ?  58  TYR B CE1    1 
ATOM   3271 C CE2    . TYR B 2 58  ? 25.272 -8.904  48.460 1.00 54.26  ?  58  TYR B CE2    1 
ATOM   3272 C CZ     . TYR B 2 58  ? 24.269 -8.224  49.099 1.00 48.67  ?  58  TYR B CZ     1 
ATOM   3273 O OH     . TYR B 2 58  ? 24.328 -6.865  49.176 1.00 45.75  ?  58  TYR B OH     1 
ATOM   3274 N N      . LYS B 2 59  ? 23.835 -15.390 49.978 1.00 38.81  ?  59  LYS B N      1 
ATOM   3275 C CA     . LYS B 2 59  ? 23.830 -16.819 49.780 1.00 33.30  ?  59  LYS B CA     1 
ATOM   3276 C C      . LYS B 2 59  ? 22.468 -17.421 50.024 1.00 34.20  ?  59  LYS B C      1 
ATOM   3277 O O      . LYS B 2 59  ? 21.974 -18.159 49.208 1.00 42.57  ?  59  LYS B O      1 
ATOM   3278 C CB     . LYS B 2 59  ? 24.872 -17.465 50.676 1.00 34.05  ?  59  LYS B CB     1 
ATOM   3279 C CG     . LYS B 2 59  ? 25.133 -18.934 50.388 1.00 42.99  ?  59  LYS B CG     1 
ATOM   3280 C CD     . LYS B 2 59  ? 25.948 -19.122 49.117 1.00 44.11  ?  59  LYS B CD     1 
ATOM   3281 C CE     . LYS B 2 59  ? 26.234 -20.589 48.848 1.00 42.00  ?  59  LYS B CE     1 
ATOM   3282 N NZ     . LYS B 2 59  ? 27.272 -20.793 47.803 1.00 37.30  ?  59  LYS B NZ     1 
ATOM   3283 N N      . GLU B 2 60  ? 21.877 -17.125 51.160 1.00 44.32  ?  60  GLU B N      1 
ATOM   3284 C CA     . GLU B 2 60  ? 20.560 -17.648 51.497 1.00 51.25  ?  60  GLU B CA     1 
ATOM   3285 C C      . GLU B 2 60  ? 19.531 -17.222 50.457 1.00 52.73  ?  60  GLU B C      1 
ATOM   3286 O O      . GLU B 2 60  ? 18.742 -18.046 49.967 1.00 52.85  ?  60  GLU B O      1 
ATOM   3287 C CB     . GLU B 2 60  ? 20.143 -17.198 52.902 1.00 51.47  ?  60  GLU B CB     1 
ATOM   3288 C CG     . GLU B 2 60  ? 18.875 -17.904 53.402 1.00 61.31  ?  60  GLU B CG     1 
ATOM   3289 C CD     . GLU B 2 60  ? 18.626 -17.751 54.900 1.00 69.94  ?  60  GLU B CD     1 
ATOM   3290 O OE1    . GLU B 2 60  ? 19.545 -18.040 55.705 1.00 75.31  ?  60  GLU B OE1    1 
ATOM   3291 O OE2    . GLU B 2 60  ? 17.500 -17.350 55.271 1.00 67.90  -1 60  GLU B OE2    1 
ATOM   3292 N N      . ALA B 2 61  ? 19.540 -15.937 50.094 1.00 42.30  ?  61  ALA B N      1 
ATOM   3293 C CA     . ALA B 2 61  ? 18.534 -15.432 49.173 1.00 40.25  ?  61  ALA B CA     1 
ATOM   3294 C C      . ALA B 2 61  ? 18.673 -16.106 47.820 1.00 48.63  ?  61  ALA B C      1 
ATOM   3295 O O      . ALA B 2 61  ? 17.687 -16.587 47.249 1.00 55.17  ?  61  ALA B O      1 
ATOM   3296 C CB     . ALA B 2 61  ? 18.662 -13.918 49.053 1.00 43.52  ?  61  ALA B CB     1 
ATOM   3297 N N      . ILE B 2 62  ? 19.904 -16.186 47.309 1.00 41.37  ?  62  ILE B N      1 
ATOM   3298 C CA     . ILE B 2 62  ? 20.160 -16.893 46.057 1.00 35.72  ?  62  ILE B CA     1 
ATOM   3299 C C      . ILE B 2 62  ? 19.512 -18.275 46.077 1.00 36.24  ?  62  ILE B C      1 
ATOM   3300 O O      . ILE B 2 62  ? 18.770 -18.655 45.156 1.00 37.05  ?  62  ILE B O      1 
ATOM   3301 C CB     . ILE B 2 62  ? 21.671 -16.981 45.802 1.00 31.35  ?  62  ILE B CB     1 
ATOM   3302 C CG1    . ILE B 2 62  ? 22.261 -15.569 45.698 1.00 33.24  ?  62  ILE B CG1    1 
ATOM   3303 C CG2    . ILE B 2 62  ? 21.930 -17.809 44.558 1.00 29.59  ?  62  ILE B CG2    1 
ATOM   3304 C CD1    . ILE B 2 62  ? 23.794 -15.511 45.586 1.00 34.87  ?  62  ILE B CD1    1 
ATOM   3305 N N      . GLU B 2 63  ? 19.771 -19.047 47.135 1.00 40.13  ?  63  GLU B N      1 
ATOM   3306 C CA     . GLU B 2 63  ? 19.149 -20.361 47.258 1.00 47.20  ?  63  GLU B CA     1 
ATOM   3307 C C      . GLU B 2 63  ? 17.626 -20.276 47.187 1.00 47.85  ?  63  GLU B C      1 
ATOM   3308 O O      . GLU B 2 63  ? 16.980 -20.996 46.409 1.00 41.38  ?  63  GLU B O      1 
ATOM   3309 C CB     . GLU B 2 63  ? 19.581 -21.011 48.561 1.00 49.85  ?  63  GLU B CB     1 
ATOM   3310 C CG     . GLU B 2 63  ? 21.073 -21.162 48.667 1.00 54.88  ?  63  GLU B CG     1 
ATOM   3311 C CD     . GLU B 2 63  ? 21.446 -21.756 49.994 1.00 58.20  ?  63  GLU B CD     1 
ATOM   3312 O OE1    . GLU B 2 63  ? 20.508 -22.269 50.649 1.00 60.85  ?  63  GLU B OE1    1 
ATOM   3313 O OE2    . GLU B 2 63  ? 22.642 -21.697 50.382 1.00 52.64  -1 63  GLU B OE2    1 
ATOM   3314 N N      . LYS B 2 64  ? 17.028 -19.423 48.020 1.00 40.54  ?  64  LYS B N      1 
ATOM   3315 C CA     . LYS B 2 64  ? 15.589 -19.231 47.942 1.00 42.46  ?  64  LYS B CA     1 
ATOM   3316 C C      . LYS B 2 64  ? 15.150 -18.883 46.521 1.00 51.90  ?  64  LYS B C      1 
ATOM   3317 O O      . LYS B 2 64  ? 14.210 -19.485 45.993 1.00 51.13  ?  64  LYS B O      1 
ATOM   3318 C CB     . LYS B 2 64  ? 15.162 -18.149 48.923 1.00 40.22  ?  64  LYS B CB     1 
ATOM   3319 C CG     . LYS B 2 64  ? 15.171 -18.619 50.348 1.00 47.89  ?  64  LYS B CG     1 
ATOM   3320 C CD     . LYS B 2 64  ? 14.017 -17.982 51.119 1.00 51.06  ?  64  LYS B CD     1 
ATOM   3321 C CE     . LYS B 2 64  ? 13.913 -18.528 52.530 1.00 43.20  ?  64  LYS B CE     1 
ATOM   3322 N NZ     . LYS B 2 64  ? 15.157 -18.264 53.306 1.00 40.23  ?  64  LYS B NZ     1 
ATOM   3323 N N      . ILE B 2 65  ? 15.843 -17.926 45.881 1.00 60.61  ?  65  ILE B N      1 
ATOM   3324 C CA     . ILE B 2 65  ? 15.436 -17.427 44.559 1.00 59.25  ?  65  ILE B CA     1 
ATOM   3325 C C      . ILE B 2 65  ? 15.390 -18.563 43.531 1.00 59.97  ?  65  ILE B C      1 
ATOM   3326 O O      . ILE B 2 65  ? 14.442 -18.678 42.742 1.00 54.88  ?  65  ILE B O      1 
ATOM   3327 C CB     . ILE B 2 65  ? 16.376 -16.296 44.084 1.00 52.10  ?  65  ILE B CB     1 
ATOM   3328 C CG1    . ILE B 2 65  ? 16.514 -15.190 45.118 1.00 50.91  ?  65  ILE B CG1    1 
ATOM   3329 C CG2    . ILE B 2 65  ? 15.868 -15.696 42.793 1.00 49.65  ?  65  ILE B CG2    1 
ATOM   3330 C CD1    . ILE B 2 65  ? 15.200 -14.678 45.623 1.00 53.38  ?  65  ILE B CD1    1 
ATOM   3331 N N      . LEU B 2 66  ? 16.438 -19.391 43.489 1.00 46.63  ?  66  LEU B N      1 
ATOM   3332 C CA     . LEU B 2 66  ? 16.420 -20.523 42.573 1.00 44.14  ?  66  LEU B CA     1 
ATOM   3333 C C      . LEU B 2 66  ? 15.360 -21.536 42.984 1.00 52.78  ?  66  LEU B C      1 
ATOM   3334 O O      . LEU B 2 66  ? 14.631 -22.066 42.135 1.00 51.68  ?  66  LEU B O      1 
ATOM   3335 C CB     . LEU B 2 66  ? 17.802 -21.168 42.525 1.00 41.00  ?  66  LEU B CB     1 
ATOM   3336 C CG     . LEU B 2 66  ? 18.976 -20.215 42.304 1.00 35.14  ?  66  LEU B CG     1 
ATOM   3337 C CD1    . LEU B 2 66  ? 20.232 -20.946 42.682 1.00 35.58  ?  66  LEU B CD1    1 
ATOM   3338 C CD2    . LEU B 2 66  ? 19.051 -19.701 40.850 1.00 29.04  ?  66  LEU B CD2    1 
ATOM   3339 N N      . ASP B 2 67  ? 15.142 -21.775 44.270 1.00 82.10  ?  67  ASP B N      1 
ATOM   3340 C CA     . ASP B 2 67  ? 14.038 -22.647 44.707 1.00 84.83  ?  67  ASP B CA     1 
ATOM   3341 C C      . ASP B 2 67  ? 12.670 -22.135 44.328 1.00 82.14  ?  67  ASP B C      1 
ATOM   3342 O O      . ASP B 2 67  ? 11.745 -22.911 44.197 1.00 87.54  ?  67  ASP B O      1 
ATOM   3343 C CB     . ASP B 2 67  ? 14.016 -22.817 46.216 1.00 89.23  ?  67  ASP B CB     1 
ATOM   3344 C CG     . ASP B 2 67  ? 14.447 -24.197 46.663 1.00 91.10  ?  67  ASP B CG     1 
ATOM   3345 O OD1    . ASP B 2 67  ? 14.529 -25.107 45.819 1.00 92.83  ?  67  ASP B OD1    1 
ATOM   3346 O OD2    . ASP B 2 67  ? 14.700 -24.373 47.871 1.00 90.89  -1 67  ASP B OD2    1 
ATOM   3347 N N      . PHE B 2 68  ? 12.504 -20.837 44.207 1.00 71.95  ?  68  PHE B N      1 
ATOM   3348 C CA     . PHE B 2 68  ? 11.236 -20.280 43.785 1.00 69.53  ?  68  PHE B CA     1 
ATOM   3349 C C      . PHE B 2 68  ? 10.997 -20.743 42.395 1.00 70.97  ?  68  PHE B C      1 
ATOM   3350 O O      . PHE B 2 68  ? 9.905  -21.121 42.046 1.00 70.65  ?  68  PHE B O      1 
ATOM   3351 C CB     . PHE B 2 68  ? 11.343 -18.774 43.791 1.00 65.96  ?  68  PHE B CB     1 
ATOM   3352 C CG     . PHE B 2 68  ? 10.042 -18.046 43.749 1.00 61.84  ?  68  PHE B CG     1 
ATOM   3353 C CD1    . PHE B 2 68  ? 9.250  -17.961 44.868 1.00 55.21  ?  68  PHE B CD1    1 
ATOM   3354 C CD2    . PHE B 2 68  ? 9.654  -17.380 42.607 1.00 64.39  ?  68  PHE B CD2    1 
ATOM   3355 C CE1    . PHE B 2 68  ? 8.068  -17.259 44.840 1.00 52.94  ?  68  PHE B CE1    1 
ATOM   3356 C CE2    . PHE B 2 68  ? 8.474  -16.676 42.569 1.00 62.75  ?  68  PHE B CE2    1 
ATOM   3357 C CZ     . PHE B 2 68  ? 7.679  -16.614 43.689 1.00 58.86  ?  68  PHE B CZ     1 
ATOM   3358 N N      . CYS B 2 69  ? 12.040 -20.730 41.593 1.00 69.07  ?  69  CYS B N      1 
ATOM   3359 C CA     . CYS B 2 69  ? 11.911 -21.112 40.210 1.00 65.04  ?  69  CYS B CA     1 
ATOM   3360 C C      . CYS B 2 69  ? 11.922 -22.602 40.164 1.00 74.81  ?  69  CYS B C      1 
ATOM   3361 O O      . CYS B 2 69  ? 11.687 -23.177 39.116 1.00 83.11  ?  69  CYS B O      1 
ATOM   3362 C CB     . CYS B 2 69  ? 13.030 -20.521 39.387 1.00 59.26  ?  69  CYS B CB     1 
ATOM   3363 S SG     . CYS B 2 69  ? 13.311 -18.742 39.599 1.00 58.12  ?  69  CYS B SG     1 
ATOM   3364 N N      . LYS B 2 70  ? 12.231 -23.259 41.280 1.00 86.15  ?  70  LYS B N      1 
ATOM   3365 C CA     . LYS B 2 70  ? 12.083 -24.710 41.291 1.00 85.16  ?  70  LYS B CA     1 
ATOM   3366 C C      . LYS B 2 70  ? 10.641 -25.116 41.589 1.00 87.68  ?  70  LYS B C      1 
ATOM   3367 O O      . LYS B 2 70  ? 10.085 -25.985 40.908 1.00 97.05  ?  70  LYS B O      1 
ATOM   3368 C CB     . LYS B 2 70  ? 13.051 -25.328 42.310 1.00 83.67  ?  70  LYS B CB     1 
ATOM   3369 C CG     . LYS B 2 70  ? 13.773 -26.579 41.818 1.00 83.41  ?  70  LYS B CG     1 
ATOM   3370 C CD     . LYS B 2 70  ? 14.889 -27.013 42.758 1.00 81.97  ?  70  LYS B CD     1 
ATOM   3371 C CE     . LYS B 2 70  ? 15.925 -25.904 42.988 1.00 82.85  ?  70  LYS B CE     1 
ATOM   3372 N NZ     . LYS B 2 70  ? 16.772 -25.577 41.802 1.00 80.90  ?  70  LYS B NZ     1 
ATOM   3373 N N      . LYS B 2 71  ? 10.014 -24.500 42.599 1.00 64.66  ?  71  LYS B N      1 
ATOM   3374 C CA     . LYS B 2 71  ? 8.621  -24.812 42.912 1.00 64.12  ?  71  LYS B CA     1 
ATOM   3375 C C      . LYS B 2 71  ? 7.648  -24.143 41.955 1.00 60.44  ?  71  LYS B C      1 
ATOM   3376 O O      . LYS B 2 71  ? 6.485  -24.566 41.875 1.00 56.58  ?  71  LYS B O      1 
ATOM   3377 C CB     . LYS B 2 71  ? 8.257  -24.375 44.341 1.00 63.86  ?  71  LYS B CB     1 
ATOM   3378 C CG     . LYS B 2 71  ? 9.299  -24.683 45.395 1.00 63.49  ?  71  LYS B CG     1 
ATOM   3379 C CD     . LYS B 2 71  ? 9.068  -23.849 46.649 1.00 60.35  ?  71  LYS B CD     1 
ATOM   3380 C CE     . LYS B 2 71  ? 10.296 -23.857 47.549 1.00 58.13  ?  71  LYS B CE     1 
ATOM   3381 N NZ     . LYS B 2 71  ? 10.773 -25.249 47.789 1.00 57.81  ?  71  LYS B NZ     1 
ATOM   3382 N N      . ASN B 2 72  ? 8.120  -23.113 41.267 1.00 64.94  ?  72  ASN B N      1 
ATOM   3383 C CA     . ASN B 2 72  ? 7.251  -22.355 40.373 1.00 66.46  ?  72  ASN B CA     1 
ATOM   3384 C C      . ASN B 2 72  ? 7.743  -22.345 38.940 1.00 70.12  ?  72  ASN B C      1 
ATOM   3385 O O      . ASN B 2 72  ? 7.444  -21.419 38.211 1.00 72.25  ?  72  ASN B O      1 
ATOM   3386 C CB     . ASN B 2 72  ? 7.112  -20.917 40.863 1.00 62.44  ?  72  ASN B CB     1 
ATOM   3387 C CG     . ASN B 2 72  ? 6.540  -20.827 42.250 1.00 62.09  ?  72  ASN B CG     1 
ATOM   3388 O OD1    . ASN B 2 72  ? 5.732  -21.650 42.662 1.00 65.29  ?  72  ASN B OD1    1 
ATOM   3389 N ND2    . ASN B 2 72  ? 6.953  -19.821 42.974 1.00 62.35  ?  72  ASN B ND2    1 
ATOM   3390 N N      . GLU B 2 73  ? 8.495  -23.353 38.528 1.00 76.13  ?  73  GLU B N      1 
ATOM   3391 C CA     . GLU B 2 73  ? 9.058  -23.295 37.179 1.00 77.80  ?  73  GLU B CA     1 
ATOM   3392 C C      . GLU B 2 73  ? 7.986  -23.054 36.123 1.00 82.96  ?  73  GLU B C      1 
ATOM   3393 O O      . GLU B 2 73  ? 8.188  -22.249 35.203 1.00 86.26  ?  73  GLU B O      1 
ATOM   3394 C CB     . GLU B 2 73  ? 9.819  -24.577 36.814 1.00 79.76  ?  73  GLU B CB     1 
ATOM   3395 C CG     . GLU B 2 73  ? 10.549 -24.458 35.440 1.00 89.01  ?  73  GLU B CG     1 
ATOM   3396 C CD     . GLU B 2 73  ? 10.473 -25.716 34.542 1.00 93.86  ?  73  GLU B CD     1 
ATOM   3397 O OE1    . GLU B 2 73  ? 11.244 -26.677 34.775 1.00 98.64  ?  73  GLU B OE1    1 
ATOM   3398 O OE2    . GLU B 2 73  ? 9.655  -25.731 33.584 1.00 89.07  -1 73  GLU B OE2    1 
ATOM   3399 N N      . SER B 2 74  ? 6.835  -23.671 36.311 1.00 70.96  ?  74  SER B N      1 
ATOM   3400 C CA     . SER B 2 74  ? 5.759  -23.571 35.333 1.00 63.78  ?  74  SER B CA     1 
ATOM   3401 C C      . SER B 2 74  ? 5.279  -22.177 34.978 1.00 60.55  ?  74  SER B C      1 
ATOM   3402 O O      . SER B 2 74  ? 4.703  -21.968 33.933 1.00 53.89  ?  74  SER B O      1 
ATOM   3403 C CB     . SER B 2 74  ? 4.617  -24.475 35.791 1.00 55.53  ?  74  SER B CB     1 
ATOM   3404 O OG     . SER B 2 74  ? 4.550  -24.532 37.201 1.00 59.60  ?  74  SER B OG     1 
ATOM   3405 N N      . LEU B 2 75  ? 5.529  -21.227 35.845 1.00 69.29  ?  75  LEU B N      1 
ATOM   3406 C CA     . LEU B 2 75  ? 5.031  -19.896 35.625 1.00 73.55  ?  75  LEU B CA     1 
ATOM   3407 C C      . LEU B 2 75  ? 6.092  -18.975 35.105 1.00 75.06  ?  75  LEU B C      1 
ATOM   3408 O O      . LEU B 2 75  ? 5.836  -17.799 34.925 1.00 76.35  ?  75  LEU B O      1 
ATOM   3409 C CB     . LEU B 2 75  ? 4.556  -19.358 36.957 1.00 75.99  ?  75  LEU B CB     1 
ATOM   3410 C CG     . LEU B 2 75  ? 3.479  -20.139 37.708 1.00 74.88  ?  75  LEU B CG     1 
ATOM   3411 C CD1    . LEU B 2 75  ? 3.731  -20.132 39.209 1.00 71.80  ?  75  LEU B CD1    1 
ATOM   3412 C CD2    . LEU B 2 75  ? 2.107  -19.572 37.386 1.00 73.59  ?  75  LEU B CD2    1 
ATOM   3413 N N      . LEU B 2 76  ? 7.275  -19.496 34.836 1.00 65.93  ?  76  LEU B N      1 
ATOM   3414 C CA     . LEU B 2 76  ? 8.380  -18.655 34.464 1.00 60.91  ?  76  LEU B CA     1 
ATOM   3415 C C      . LEU B 2 76  ? 9.060  -19.141 33.206 1.00 61.21  ?  76  LEU B C      1 
ATOM   3416 O O      . LEU B 2 76  ? 8.838  -20.260 32.805 1.00 66.88  ?  76  LEU B O      1 
ATOM   3417 C CB     . LEU B 2 76  ? 9.347  -18.596 35.643 1.00 56.58  ?  76  LEU B CB     1 
ATOM   3418 C CG     . LEU B 2 76  ? 8.685  -18.191 36.953 1.00 51.75  ?  76  LEU B CG     1 
ATOM   3419 C CD1    . LEU B 2 76  ? 9.506  -18.604 38.159 1.00 54.30  ?  76  LEU B CD1    1 
ATOM   3420 C CD2    . LEU B 2 76  ? 8.404  -16.704 36.949 1.00 50.37  ?  76  LEU B CD2    1 
ATOM   3421 N N      . SER B 2 77  ? 9.829  -18.288 32.553 1.00 61.96  ?  77  SER B N      1 
ATOM   3422 C CA     . SER B 2 77  ? 10.522 -18.642 31.331 1.00 68.22  ?  77  SER B CA     1 
ATOM   3423 C C      . SER B 2 77  ? 11.754 -19.482 31.515 1.00 71.62  ?  77  SER B C      1 
ATOM   3424 O O      . SER B 2 77  ? 12.647 -19.107 32.246 1.00 75.56  ?  77  SER B O      1 
ATOM   3425 C CB     . SER B 2 77  ? 10.899 -17.387 30.564 1.00 71.92  ?  77  SER B CB     1 
ATOM   3426 O OG     . SER B 2 77  ? 11.224 -17.694 29.226 1.00 73.29  ?  77  SER B OG     1 
ATOM   3427 N N      . GLU B 2 78  ? 11.836 -20.585 30.804 1.00 73.10  ?  78  GLU B N      1 
ATOM   3428 C CA     . GLU B 2 78  ? 12.913 -21.518 30.933 1.00 71.13  ?  78  GLU B CA     1 
ATOM   3429 C C      . GLU B 2 78  ? 14.335 -21.067 30.694 1.00 75.73  ?  78  GLU B C      1 
ATOM   3430 O O      . GLU B 2 78  ? 15.206 -21.376 31.478 1.00 84.71  ?  78  GLU B O      1 
ATOM   3431 C CB     . GLU B 2 78  ? 12.621 -22.532 29.861 1.00 72.29  ?  78  GLU B CB     1 
ATOM   3432 C CG     . GLU B 2 78  ? 12.121 -21.915 28.568 1.00 68.59  ?  78  GLU B CG     1 
ATOM   3433 C CD     . GLU B 2 78  ? 12.068 -22.899 27.430 1.00 77.31  ?  78  GLU B CD     1 
ATOM   3434 O OE1    . GLU B 2 78  ? 11.419 -23.951 27.582 1.00 79.47  ?  78  GLU B OE1    1 
ATOM   3435 O OE2    . GLU B 2 78  ? 12.665 -22.607 26.376 1.00 81.83  -1 78  GLU B OE2    1 
ATOM   3436 N N      . GLN B 2 79  ? 14.599 -20.321 29.646 1.00 87.81  ?  79  GLN B N      1 
ATOM   3437 C CA     . GLN B 2 79  ? 15.942 -19.858 29.448 1.00 89.86  ?  79  GLN B CA     1 
ATOM   3438 C C      . GLN B 2 79  ? 16.378 -18.952 30.592 1.00 93.00  ?  79  GLN B C      1 
ATOM   3439 O O      . GLN B 2 79  ? 17.516 -19.010 30.970 1.00 94.13  ?  79  GLN B O      1 
ATOM   3440 C CB     . GLN B 2 79  ? 16.124 -19.201 28.077 1.00 89.25  ?  79  GLN B CB     1 
ATOM   3441 C CG     . GLN B 2 79  ? 15.682 -17.756 27.954 1.00 91.40  ?  79  GLN B CG     1 
ATOM   3442 C CD     . GLN B 2 79  ? 14.183 -17.600 27.830 1.00 99.63  ?  79  GLN B CD     1 
ATOM   3443 O OE1    . GLN B 2 79  ? 13.450 -18.578 27.712 1.00 103.41 ?  79  GLN B OE1    1 
ATOM   3444 N NE2    . GLN B 2 79  ? 13.719 -16.357 27.846 1.00 103.69 ?  79  GLN B NE2    1 
ATOM   3445 N N      . VAL B 2 80  ? 15.498 -18.097 31.108 1.00 72.93  ?  80  VAL B N      1 
ATOM   3446 C CA     . VAL B 2 80  ? 15.811 -17.246 32.235 1.00 67.02  ?  80  VAL B CA     1 
ATOM   3447 C C      . VAL B 2 80  ? 16.080 -18.015 33.516 1.00 63.63  ?  80  VAL B C      1 
ATOM   3448 O O      . VAL B 2 80  ? 17.060 -17.789 34.195 1.00 56.61  ?  80  VAL B O      1 
ATOM   3449 C CB     . VAL B 2 80  ? 14.654 -16.277 32.482 1.00 67.10  ?  80  VAL B CB     1 
ATOM   3450 C CG1    . VAL B 2 80  ? 15.006 -15.290 33.583 1.00 61.20  ?  80  VAL B CG1    1 
ATOM   3451 C CG2    . VAL B 2 80  ? 14.304 -15.537 31.209 1.00 64.89  ?  80  VAL B CG2    1 
ATOM   3452 N N      . VAL B 2 81  ? 15.242 -18.980 33.809 1.00 56.23  ?  81  VAL B N      1 
ATOM   3453 C CA     . VAL B 2 81  ? 15.443 -19.780 34.993 1.00 59.35  ?  81  VAL B CA     1 
ATOM   3454 C C      . VAL B 2 81  ? 16.732 -20.546 34.905 1.00 62.20  ?  81  VAL B C      1 
ATOM   3455 O O      . VAL B 2 81  ? 17.401 -20.721 35.901 1.00 67.27  ?  81  VAL B O      1 
ATOM   3456 C CB     . VAL B 2 81  ? 14.247 -20.691 35.340 1.00 58.54  ?  81  VAL B CB     1 
ATOM   3457 C CG1    . VAL B 2 81  ? 12.949 -19.906 35.328 1.00 54.64  ?  81  VAL B CG1    1 
ATOM   3458 C CG2    . VAL B 2 81  ? 14.156 -21.917 34.458 1.00 61.97  ?  81  VAL B CG2    1 
ATOM   3459 N N      . GLN B 2 82  ? 17.083 -21.016 33.725 1.00 67.95  ?  82  GLN B N      1 
ATOM   3460 C CA     . GLN B 2 82  ? 18.267 -21.819 33.594 1.00 70.70  ?  82  GLN B CA     1 
ATOM   3461 C C      . GLN B 2 82  ? 19.470 -20.941 33.494 1.00 68.69  ?  82  GLN B C      1 
ATOM   3462 O O      . GLN B 2 82  ? 20.550 -21.312 33.920 1.00 68.95  ?  82  GLN B O      1 
ATOM   3463 C CB     . GLN B 2 82  ? 18.156 -22.764 32.393 1.00 70.35  ?  82  GLN B CB     1 
ATOM   3464 C CG     . GLN B 2 82  ? 18.785 -24.129 32.606 1.00 71.61  ?  82  GLN B CG     1 
ATOM   3465 C CD     . GLN B 2 82  ? 20.247 -24.162 32.225 1.00 78.39  ?  82  GLN B CD     1 
ATOM   3466 O OE1    . GLN B 2 82  ? 20.652 -23.579 31.218 1.00 82.12  ?  82  GLN B OE1    1 
ATOM   3467 N NE2    . GLN B 2 82  ? 21.051 -24.856 33.022 1.00 75.31  ?  82  GLN B NE2    1 
ATOM   3468 N N      . ARG B 2 83  ? 19.355 -19.758 32.923 1.00 47.54  ?  83  ARG B N      1 
ATOM   3469 C CA     . ARG B 2 83  ? 20.489 -18.851 32.880 1.00 41.37  ?  83  ARG B CA     1 
ATOM   3470 C C      . ARG B 2 83  ? 20.831 -18.336 34.263 1.00 48.31  ?  83  ARG B C      1 
ATOM   3471 O O      . ARG B 2 83  ? 21.992 -18.239 34.614 1.00 48.05  ?  83  ARG B O      1 
ATOM   3472 C CB     . ARG B 2 83  ? 20.219 -17.692 31.947 1.00 39.14  ?  83  ARG B CB     1 
ATOM   3473 C CG     . ARG B 2 83  ? 21.346 -16.700 31.854 1.00 38.02  ?  83  ARG B CG     1 
ATOM   3474 C CD     . ARG B 2 83  ? 22.426 -17.240 30.953 1.00 44.14  ?  83  ARG B CD     1 
ATOM   3475 N NE     . ARG B 2 83  ? 23.687 -16.543 31.132 1.00 47.17  ?  83  ARG B NE     1 
ATOM   3476 C CZ     . ARG B 2 83  ? 23.956 -15.350 30.624 1.00 44.30  ?  83  ARG B CZ     1 
ATOM   3477 N NH1    . ARG B 2 83  ? 23.043 -14.699 29.919 1.00 33.86  ?  83  ARG B NH1    1 
ATOM   3478 N NH2    . ARG B 2 83  ? 25.143 -14.807 30.833 1.00 46.90  ?  83  ARG B NH2    1 
ATOM   3479 N N      . LEU B 2 84  ? 19.821 -18.013 35.056 1.00 52.79  ?  84  LEU B N      1 
ATOM   3480 C CA     . LEU B 2 84  ? 20.041 -17.565 36.410 1.00 48.80  ?  84  LEU B CA     1 
ATOM   3481 C C      . LEU B 2 84  ? 20.712 -18.660 37.175 1.00 52.20  ?  84  LEU B C      1 
ATOM   3482 O O      . LEU B 2 84  ? 21.629 -18.415 37.930 1.00 61.38  ?  84  LEU B O      1 
ATOM   3483 C CB     . LEU B 2 84  ? 18.715 -17.265 37.097 1.00 43.98  ?  84  LEU B CB     1 
ATOM   3484 C CG     . LEU B 2 84  ? 17.851 -16.073 36.711 1.00 45.42  ?  84  LEU B CG     1 
ATOM   3485 C CD1    . LEU B 2 84  ? 16.497 -16.152 37.393 1.00 43.35  ?  84  LEU B CD1    1 
ATOM   3486 C CD2    . LEU B 2 84  ? 18.546 -14.776 37.040 1.00 35.88  ?  84  LEU B CD2    1 
ATOM   3487 N N      . ALA B 2 85  ? 20.276 -19.880 36.972 1.00 43.51  ?  85  ALA B N      1 
ATOM   3488 C CA     . ALA B 2 85  ? 20.882 -20.997 37.651 1.00 48.27  ?  85  ALA B CA     1 
ATOM   3489 C C      . ALA B 2 85  ? 22.320 -21.169 37.262 1.00 52.31  ?  85  ALA B C      1 
ATOM   3490 O O      . ALA B 2 85  ? 23.117 -21.602 38.061 1.00 52.64  ?  85  ALA B O      1 
ATOM   3491 C CB     . ALA B 2 85  ? 20.117 -22.259 37.354 1.00 46.02  ?  85  ALA B CB     1 
ATOM   3492 N N      . GLU B 2 86  ? 22.656 -20.802 36.050 1.00 59.83  ?  86  GLU B N      1 
ATOM   3493 C CA     . GLU B 2 86  ? 23.997 -20.966 35.555 1.00 60.24  ?  86  GLU B CA     1 
ATOM   3494 C C      . GLU B 2 86  ? 24.920 -19.905 36.070 1.00 56.51  ?  86  GLU B C      1 
ATOM   3495 O O      . GLU B 2 86  ? 26.061 -20.177 36.396 1.00 60.19  ?  86  GLU B O      1 
ATOM   3496 C CB     . GLU B 2 86  ? 23.945 -20.917 34.031 1.00 64.44  ?  86  GLU B CB     1 
ATOM   3497 C CG     . GLU B 2 86  ? 25.267 -20.708 33.328 1.00 71.20  ?  86  GLU B CG     1 
ATOM   3498 C CD     . GLU B 2 86  ? 25.087 -20.526 31.839 1.00 78.85  ?  86  GLU B CD     1 
ATOM   3499 O OE1    . GLU B 2 86  ? 23.943 -20.266 31.415 1.00 81.30  ?  86  GLU B OE1    1 
ATOM   3500 O OE2    . GLU B 2 86  ? 26.085 -20.649 31.097 1.00 81.55  -1 86  GLU B OE2    1 
ATOM   3501 N N      . VAL B 2 87  ? 24.441 -18.680 36.158 1.00 56.43  ?  87  VAL B N      1 
ATOM   3502 C CA     . VAL B 2 87  ? 25.318 -17.599 36.544 1.00 56.50  ?  87  VAL B CA     1 
ATOM   3503 C C      . VAL B 2 87  ? 25.557 -17.681 38.031 1.00 61.04  ?  87  VAL B C      1 
ATOM   3504 O O      . VAL B 2 87  ? 26.654 -17.436 38.506 1.00 63.59  ?  87  VAL B O      1 
ATOM   3505 C CB     . VAL B 2 87  ? 24.751 -16.241 36.109 1.00 55.59  ?  87  VAL B CB     1 
ATOM   3506 C CG1    . VAL B 2 87  ? 25.682 -15.123 36.525 1.00 53.70  ?  87  VAL B CG1    1 
ATOM   3507 C CG2    . VAL B 2 87  ? 24.574 -16.200 34.607 1.00 57.83  ?  87  VAL B CG2    1 
ATOM   3508 N N      . ALA B 2 88  ? 24.541 -18.070 38.760 1.00 44.28  ?  88  ALA B N      1 
ATOM   3509 C CA     . ALA B 2 88  ? 24.656 -18.184 40.200 1.00 44.00  ?  88  ALA B CA     1 
ATOM   3510 C C      . ALA B 2 88  ? 25.896 -18.864 40.832 1.00 48.77  ?  88  ALA B C      1 
ATOM   3511 O O      . ALA B 2 88  ? 26.483 -18.291 41.735 1.00 50.94  ?  88  ALA B O      1 
ATOM   3512 C CB     . ALA B 2 88  ? 23.352 -18.763 40.762 1.00 31.72  ?  88  ALA B CB     1 
ATOM   3513 N N      . PRO B 2 89  ? 26.292 -20.085 40.399 1.00 44.33  ?  89  PRO B N      1 
ATOM   3514 C CA     . PRO B 2 89  ? 27.432 -20.675 41.088 1.00 44.43  ?  89  PRO B CA     1 
ATOM   3515 C C      . PRO B 2 89  ? 28.685 -19.810 41.085 1.00 48.00  ?  89  PRO B C      1 
ATOM   3516 O O      . PRO B 2 89  ? 29.436 -19.837 42.046 1.00 47.78  ?  89  PRO B O      1 
ATOM   3517 C CB     . PRO B 2 89  ? 27.630 -21.980 40.340 1.00 39.16  ?  89  PRO B CB     1 
ATOM   3518 C CG     . PRO B 2 89  ? 26.266 -22.362 39.939 1.00 39.41  ?  89  PRO B CG     1 
ATOM   3519 C CD     . PRO B 2 89  ? 25.631 -21.076 39.540 1.00 38.58  ?  89  PRO B CD     1 
ATOM   3520 N N      . ARG B 2 90  ? 28.915 -19.072 40.020 1.00 61.07  ?  90  ARG B N      1 
ATOM   3521 C CA     . ARG B 2 90  ? 30.091 -18.217 39.895 1.00 61.88  ?  90  ARG B CA     1 
ATOM   3522 C C      . ARG B 2 90  ? 30.059 -16.788 40.493 1.00 54.27  ?  90  ARG B C      1 
ATOM   3523 O O      . ARG B 2 90  ? 31.038 -16.066 40.414 1.00 52.09  ?  90  ARG B O      1 
ATOM   3524 C CB     . ARG B 2 90  ? 30.399 -18.100 38.411 1.00 63.73  ?  90  ARG B CB     1 
ATOM   3525 C CG     . ARG B 2 90  ? 31.043 -19.321 37.791 1.00 65.58  ?  90  ARG B CG     1 
ATOM   3526 C CD     . ARG B 2 90  ? 31.233 -19.148 36.289 1.00 68.16  ?  90  ARG B CD     1 
ATOM   3527 N NE     . ARG B 2 90  ? 29.972 -19.055 35.550 1.00 67.65  ?  90  ARG B NE     1 
ATOM   3528 C CZ     . ARG B 2 90  ? 29.447 -17.925 35.081 1.00 66.67  ?  90  ARG B CZ     1 
ATOM   3529 N NH1    . ARG B 2 90  ? 30.064 -16.769 35.268 1.00 67.31  ?  90  ARG B NH1    1 
ATOM   3530 N NH2    . ARG B 2 90  ? 28.305 -17.952 34.418 1.00 64.62  ?  90  ARG B NH2    1 
ATOM   3531 N N      . LEU B 2 91  ? 28.947 -16.373 41.062 1.00 33.86  ?  91  LEU B N      1 
ATOM   3532 C CA     . LEU B 2 91  ? 28.821 -15.015 41.560 1.00 29.91  ?  91  LEU B CA     1 
ATOM   3533 C C      . LEU B 2 91  ? 29.775 -14.674 42.665 1.00 30.65  ?  91  LEU B C      1 
ATOM   3534 O O      . LEU B 2 91  ? 30.096 -15.510 43.485 1.00 33.34  ?  91  LEU B O      1 
ATOM   3535 C CB     . LEU B 2 91  ? 27.375 -14.700 41.927 1.00 24.97  ?  91  LEU B CB     1 
ATOM   3536 C CG     . LEU B 2 91  ? 26.277 -14.683 40.893 1.00 25.35  ?  91  LEU B CG     1 
ATOM   3537 C CD1    . LEU B 2 91  ? 24.959 -14.730 41.626 1.00 22.76  ?  91  LEU B CD1    1 
ATOM   3538 C CD2    . LEU B 2 91  ? 26.377 -13.439 40.037 1.00 30.36  ?  91  LEU B CD2    1 
ATOM   3539 N N      . LYS B 2 92  ? 30.228 -13.436 42.685 1.00 42.39  ?  92  LYS B N      1 
ATOM   3540 C CA     . LYS B 2 92  ? 31.204 -13.008 43.657 1.00 42.08  ?  92  LYS B CA     1 
ATOM   3541 C C      . LYS B 2 92  ? 30.825 -11.614 44.075 1.00 50.25  ?  92  LYS B C      1 
ATOM   3542 O O      . LYS B 2 92  ? 29.948 -11.018 43.468 1.00 51.63  ?  92  LYS B O      1 
ATOM   3543 C CB     . LYS B 2 92  ? 32.610 -12.986 43.048 1.00 37.68  ?  92  LYS B CB     1 
ATOM   3544 C CG     . LYS B 2 92  ? 33.157 -14.325 42.596 1.00 41.82  ?  92  LYS B CG     1 
ATOM   3545 C CD     . LYS B 2 92  ? 33.829 -15.075 43.733 1.00 48.90  ?  92  LYS B CD     1 
ATOM   3546 C CE     . LYS B 2 92  ? 34.254 -16.473 43.313 1.00 52.14  ?  92  LYS B CE     1 
ATOM   3547 N NZ     . LYS B 2 92  ? 33.115 -17.431 43.292 1.00 48.04  ?  92  LYS B NZ     1 
ATOM   3548 N N      . SER B 2 93  ? 31.393 -11.109 45.151 1.00 43.00  ?  93  SER B N      1 
ATOM   3549 C CA     . SER B 2 93  ? 31.174 -9.722  45.534 1.00 33.69  ?  93  SER B CA     1 
ATOM   3550 C C      . SER B 2 93  ? 32.531 -9.102  45.759 1.00 38.51  ?  93  SER B C      1 
ATOM   3551 O O      . SER B 2 93  ? 33.425 -9.748  46.248 1.00 43.88  ?  93  SER B O      1 
ATOM   3552 C CB     . SER B 2 93  ? 30.268 -9.582  46.742 1.00 34.79  ?  93  SER B CB     1 
ATOM   3553 O OG     . SER B 2 93  ? 28.912 -9.573  46.370 1.00 37.31  ?  93  SER B OG     1 
ATOM   3554 N N      . ASN B 2 94  ? 32.707 -7.869  45.352 1.00 44.93  ?  94  ASN B N      1 
ATOM   3555 C CA     . ASN B 2 94  ? 33.966 -7.185  45.505 1.00 52.77  ?  94  ASN B CA     1 
ATOM   3556 C C      . ASN B 2 94  ? 33.754 -5.880  46.203 1.00 55.15  ?  94  ASN B C      1 
ATOM   3557 O O      . ASN B 2 94  ? 33.014 -5.047  45.741 1.00 50.45  ?  94  ASN B O      1 
ATOM   3558 C CB     . ASN B 2 94  ? 34.578 -6.926  44.130 1.00 61.39  ?  94  ASN B CB     1 
ATOM   3559 C CG     . ASN B 2 94  ? 35.902 -6.187  44.188 1.00 67.03  ?  94  ASN B CG     1 
ATOM   3560 O OD1    . ASN B 2 94  ? 36.593 -6.182  45.203 1.00 68.38  ?  94  ASN B OD1    1 
ATOM   3561 N ND2    . ASN B 2 94  ? 36.271 -5.571  43.074 1.00 64.99  ?  94  ASN B ND2    1 
ATOM   3562 N N      . PRO B 2 95  ? 34.470 -5.675  47.289 1.00 49.76  ?  95  PRO B N      1 
ATOM   3563 C CA     . PRO B 2 95  ? 34.307 -4.457  48.056 1.00 48.54  ?  95  PRO B CA     1 
ATOM   3564 C C      . PRO B 2 95  ? 34.633 -3.176  47.285 1.00 49.40  ?  95  PRO B C      1 
ATOM   3565 O O      . PRO B 2 95  ? 33.964 -2.191  47.494 1.00 51.17  ?  95  PRO B O      1 
ATOM   3566 C CB     . PRO B 2 95  ? 35.221 -4.682  49.255 1.00 45.63  ?  95  PRO B CB     1 
ATOM   3567 C CG     . PRO B 2 95  ? 35.993 -5.920  48.988 1.00 44.63  ?  95  PRO B CG     1 
ATOM   3568 C CD     . PRO B 2 95  ? 35.170 -6.716  48.046 1.00 49.74  ?  95  PRO B CD     1 
ATOM   3569 N N      . LYS B 2 96  ? 35.640 -3.180  46.429 1.00 42.94  ?  96  LYS B N      1 
ATOM   3570 C CA     . LYS B 2 96  ? 36.011 -2.016  45.653 1.00 40.90  ?  96  LYS B CA     1 
ATOM   3571 C C      . LYS B 2 96  ? 34.886 -1.587  44.752 1.00 38.81  ?  96  LYS B C      1 
ATOM   3572 O O      . LYS B 2 96  ? 34.700 -0.419  44.504 1.00 34.56  ?  96  LYS B O      1 
ATOM   3573 C CB     . LYS B 2 96  ? 37.245 -2.330  44.829 1.00 40.98  ?  96  LYS B CB     1 
ATOM   3574 C CG     . LYS B 2 96  ? 38.562 -2.274  45.571 1.00 41.10  ?  96  LYS B CG     1 
ATOM   3575 C CD     . LYS B 2 96  ? 39.695 -2.672  44.641 1.00 37.00  ?  96  LYS B CD     1 
ATOM   3576 C CE     . LYS B 2 96  ? 41.051 -2.263  45.186 1.00 36.20  ?  96  LYS B CE     1 
ATOM   3577 N NZ     . LYS B 2 96  ? 42.148 -2.669  44.269 1.00 33.49  ?  96  LYS B NZ     1 
ATOM   3578 N N      . ASP B 2 97  ? 34.160 -2.543  44.223 1.00 69.12  ?  97  ASP B N      1 
ATOM   3579 C CA     . ASP B 2 97  ? 33.055 -2.264  43.354 1.00 77.20  ?  97  ASP B CA     1 
ATOM   3580 C C      . ASP B 2 97  ? 31.763 -2.912  43.814 1.00 77.12  ?  97  ASP B C      1 
ATOM   3581 O O      . ASP B 2 97  ? 31.500 -4.030  43.407 1.00 85.47  ?  97  ASP B O      1 
ATOM   3582 C CB     . ASP B 2 97  ? 33.355 -2.937  42.000 1.00 84.77  ?  97  ASP B CB     1 
ATOM   3583 C CG     . ASP B 2 97  ? 34.318 -2.172  41.120 1.00 83.58  ?  97  ASP B CG     1 
ATOM   3584 O OD1    . ASP B 2 97  ? 35.115 -1.354  41.605 1.00 87.75  ?  97  ASP B OD1    1 
ATOM   3585 O OD2    . ASP B 2 97  ? 34.293 -2.430  39.901 1.00 80.71  -1 97  ASP B OD2    1 
ATOM   3586 N N      . ASN B 2 98  ? 30.920 -2.270  44.605 1.00 45.05  ?  98  ASN B N      1 
ATOM   3587 C CA     . ASN B 2 98  ? 29.603 -2.861  44.912 1.00 38.00  ?  98  ASN B CA     1 
ATOM   3588 C C      . ASN B 2 98  ? 28.621 -1.779  44.664 1.00 38.76  ?  98  ASN B C      1 
ATOM   3589 O O      . ASN B 2 98  ? 28.011 -1.309  45.590 1.00 34.28  ?  98  ASN B O      1 
ATOM   3590 C CB     . ASN B 2 98  ? 29.491 -3.351  46.334 1.00 42.08  ?  98  ASN B CB     1 
ATOM   3591 C CG     . ASN B 2 98  ? 30.037 -4.752  46.525 1.00 41.62  ?  98  ASN B CG     1 
ATOM   3592 O OD1    . ASN B 2 98  ? 29.947 -5.590  45.641 1.00 44.04  ?  98  ASN B OD1    1 
ATOM   3593 N ND2    . ASN B 2 98  ? 30.591 -5.009  47.692 1.00 36.56  ?  98  ASN B ND2    1 
ATOM   3594 N N      . GLU B 2 99  ? 28.395 -1.445  43.414 1.00 29.81  ?  99  GLU B N      1 
ATOM   3595 C CA     . GLU B 2 99  ? 27.599 -0.290  43.076 1.00 37.19  ?  99  GLU B CA     1 
ATOM   3596 C C      . GLU B 2 99  ? 26.100 -0.287  43.260 1.00 39.66  ?  99  GLU B C      1 
ATOM   3597 O O      . GLU B 2 99  ? 25.519 0.735   43.555 1.00 38.97  ?  99  GLU B O      1 
ATOM   3598 C CB     . GLU B 2 99  ? 28.010 0.173   41.678 1.00 41.40  ?  99  GLU B CB     1 
ATOM   3599 C CG     . GLU B 2 99  ? 29.498 0.421   41.533 1.00 46.65  ?  99  GLU B CG     1 
ATOM   3600 C CD     . GLU B 2 99  ? 30.153 -0.487  40.514 1.00 55.79  ?  99  GLU B CD     1 
ATOM   3601 O OE1    . GLU B 2 99  ? 30.075 -1.722  40.669 1.00 47.07  ?  99  GLU B OE1    1 
ATOM   3602 O OE2    . GLU B 2 99  ? 30.757 0.041   39.558 1.00 64.04  -1 99  GLU B OE2    1 
ATOM   3603 N N      . SER B 2 100 ? 25.469 -1.404  43.039 1.00 39.90  ?  100 SER B N      1 
ATOM   3604 C CA     . SER B 2 100 ? 24.080 -1.500  43.308 1.00 40.08  ?  100 SER B CA     1 
ATOM   3605 C C      . SER B 2 100 ? 23.823 -1.315  44.778 1.00 41.29  ?  100 SER B C      1 
ATOM   3606 O O      . SER B 2 100 ? 22.916 -0.588  45.127 1.00 34.91  ?  100 SER B O      1 
ATOM   3607 C CB     . SER B 2 100 ? 23.688 -2.893  42.909 1.00 39.42  ?  100 SER B CB     1 
ATOM   3608 O OG     . SER B 2 100 ? 24.761 -3.788  43.086 1.00 43.56  ?  100 SER B OG     1 
ATOM   3609 N N      . ARG B 2 101 ? 24.610 -1.968  45.634 1.00 31.93  ?  101 ARG B N      1 
ATOM   3610 C CA     . ARG B 2 101 ? 24.494 -1.821  47.079 1.00 27.64  ?  101 ARG B CA     1 
ATOM   3611 C C      . ARG B 2 101 ? 24.935 -0.458  47.560 1.00 29.78  ?  101 ARG B C      1 
ATOM   3612 O O      . ARG B 2 101 ? 24.419 0.038   48.532 1.00 33.70  ?  101 ARG B O      1 
ATOM   3613 C CB     . ARG B 2 101 ? 25.081 -2.997  47.865 1.00 25.20  ?  101 ARG B CB     1 
ATOM   3614 C CG     . ARG B 2 101 ? 24.943 -2.829  49.359 1.00 33.78  ?  101 ARG B CG     1 
ATOM   3615 C CD     . ARG B 2 101 ? 24.996 -4.121  50.132 1.00 42.60  ?  101 ARG B CD     1 
ATOM   3616 N NE     . ARG B 2 101 ? 24.523 -3.911  51.493 1.00 49.33  ?  101 ARG B NE     1 
ATOM   3617 C CZ     . ARG B 2 101 ? 23.262 -4.049  51.885 1.00 44.45  ?  101 ARG B CZ     1 
ATOM   3618 N NH1    . ARG B 2 101 ? 22.332 -4.409  51.022 1.00 37.18  ?  101 ARG B NH1    1 
ATOM   3619 N NH2    . ARG B 2 101 ? 22.940 -3.832  53.149 1.00 38.27  ?  101 ARG B NH2    1 
ATOM   3620 N N      . ARG B 2 102 ? 25.869 0.162   46.873 1.00 26.32  ?  102 ARG B N      1 
ATOM   3621 C CA     . ARG B 2 102 ? 26.251 1.515   47.206 1.00 19.53  ?  102 ARG B CA     1 
ATOM   3622 C C      . ARG B 2 102 ? 25.106 2.474   47.046 1.00 20.94  ?  102 ARG B C      1 
ATOM   3623 O O      . ARG B 2 102 ? 24.861 3.273   47.911 1.00 27.20  ?  102 ARG B O      1 
ATOM   3624 C CB     . ARG B 2 102 ? 27.467 1.953   46.384 1.00 20.36  ?  102 ARG B CB     1 
ATOM   3625 C CG     . ARG B 2 102 ? 28.768 1.327   46.810 1.00 18.96  ?  102 ARG B CG     1 
ATOM   3626 C CD     . ARG B 2 102 ? 29.906 1.743   45.911 1.00 22.65  ?  102 ARG B CD     1 
ATOM   3627 N NE     . ARG B 2 102 ? 31.130 1.010   46.195 1.00 30.92  ?  102 ARG B NE     1 
ATOM   3628 C CZ     . ARG B 2 102 ? 32.000 1.337   47.141 1.00 29.56  ?  102 ARG B CZ     1 
ATOM   3629 N NH1    . ARG B 2 102 ? 31.783 2.383   47.915 1.00 22.17  ?  102 ARG B NH1    1 
ATOM   3630 N NH2    . ARG B 2 102 ? 33.085 0.610   47.318 1.00 29.53  ?  102 ARG B NH2    1 
ATOM   3631 N N      . LEU B 2 103 ? 24.381 2.380   45.959 1.00 25.80  ?  103 LEU B N      1 
ATOM   3632 C CA     . LEU B 2 103 ? 23.210 3.199   45.755 1.00 28.17  ?  103 LEU B CA     1 
ATOM   3633 C C      . LEU B 2 103 ? 22.123 2.850   46.719 1.00 27.49  ?  103 LEU B C      1 
ATOM   3634 O O      . LEU B 2 103 ? 21.513 3.726   47.250 1.00 34.47  ?  103 LEU B O      1 
ATOM   3635 C CB     . LEU B 2 103 ? 22.720 3.064   44.319 1.00 25.36  ?  103 LEU B CB     1 
ATOM   3636 C CG     . LEU B 2 103 ? 21.386 3.700   43.966 1.00 34.22  ?  103 LEU B CG     1 
ATOM   3637 C CD1    . LEU B 2 103 ? 21.562 4.981   43.177 1.00 42.88  ?  103 LEU B CD1    1 
ATOM   3638 C CD2    . LEU B 2 103 ? 20.531 2.724   43.194 1.00 34.42  ?  103 LEU B CD2    1 
ATOM   3639 N N      . TYR B 2 104 ? 21.909 1.574   46.995 1.00 35.76  ?  104 TYR B N      1 
ATOM   3640 C CA     . TYR B 2 104 ? 20.842 1.111   47.854 1.00 30.39  ?  104 TYR B CA     1 
ATOM   3641 C C      . TYR B 2 104 ? 20.945 1.642   49.236 1.00 34.47  ?  104 TYR B C      1 
ATOM   3642 O O      . TYR B 2 104 ? 19.972 2.055   49.807 1.00 30.98  ?  104 TYR B O      1 
ATOM   3643 C CB     . TYR B 2 104 ? 20.911 -0.421  47.904 1.00 29.02  ?  104 TYR B CB     1 
ATOM   3644 C CG     . TYR B 2 104 ? 19.957 -1.097  48.851 1.00 32.17  ?  104 TYR B CG     1 
ATOM   3645 C CD1    . TYR B 2 104 ? 18.633 -1.290  48.508 1.00 37.60  ?  104 TYR B CD1    1 
ATOM   3646 C CD2    . TYR B 2 104 ? 20.390 -1.561  50.077 1.00 35.83  ?  104 TYR B CD2    1 
ATOM   3647 C CE1    . TYR B 2 104 ? 17.765 -1.913  49.372 1.00 39.80  ?  104 TYR B CE1    1 
ATOM   3648 C CE2    . TYR B 2 104 ? 19.530 -2.183  50.945 1.00 38.20  ?  104 TYR B CE2    1 
ATOM   3649 C CZ     . TYR B 2 104 ? 18.220 -2.356  50.587 1.00 39.94  ?  104 TYR B CZ     1 
ATOM   3650 O OH     . TYR B 2 104 ? 17.372 -2.981  51.450 1.00 35.38  ?  104 TYR B OH     1 
ATOM   3651 N N      . GLU B 2 105 ? 22.145 1.653   49.765 1.00 43.40  ?  105 GLU B N      1 
ATOM   3652 C CA     . GLU B 2 105 ? 22.344 2.083   51.111 1.00 45.81  ?  105 GLU B CA     1 
ATOM   3653 C C      . GLU B 2 105 ? 22.332 3.548   51.148 1.00 44.38  ?  105 GLU B C      1 
ATOM   3654 O O      . GLU B 2 105 ? 21.876 4.118   52.114 1.00 50.42  ?  105 GLU B O      1 
ATOM   3655 C CB     . GLU B 2 105 ? 23.670 1.595   51.660 1.00 45.95  ?  105 GLU B CB     1 
ATOM   3656 C CG     . GLU B 2 105 ? 23.821 0.088   51.807 1.00 41.83  ?  105 GLU B CG     1 
ATOM   3657 C CD     . GLU B 2 105 ? 25.128 -0.286  52.479 1.00 45.24  ?  105 GLU B CD     1 
ATOM   3658 O OE1    . GLU B 2 105 ? 25.858 0.627   52.896 1.00 47.90  ?  105 GLU B OE1    1 
ATOM   3659 O OE2    . GLU B 2 105 ? 25.428 -1.482  52.605 1.00 40.66  -1 105 GLU B OE2    1 
ATOM   3660 N N      . THR B 2 106 ? 22.806 4.187   50.094 1.00 25.14  ?  106 THR B N      1 
ATOM   3661 C CA     . THR B 2 106 ? 22.712 5.641   50.098 1.00 19.12  ?  106 THR B CA     1 
ATOM   3662 C C      . THR B 2 106 ? 21.261 6.087   50.093 1.00 20.06  ?  106 THR B C      1 
ATOM   3663 O O      . THR B 2 106 ? 20.916 7.113   50.690 1.00 20.86  ?  106 THR B O      1 
ATOM   3664 C CB     . THR B 2 106 ? 23.434 6.237   48.903 1.00 18.97  ?  106 THR B CB     1 
ATOM   3665 O OG1    . THR B 2 106 ? 24.753 5.689   48.808 1.00 20.39  ?  106 THR B OG1    1 
ATOM   3666 C CG2    . THR B 2 106 ? 23.495 7.739   49.046 1.00 18.91  ?  106 THR B CG2    1 
ATOM   3667 N N      . LEU B 2 107 ? 20.398 5.334   49.409 1.00 19.34  ?  107 LEU B N      1 
ATOM   3668 C CA     . LEU B 2 107 ? 18.971 5.615   49.458 1.00 19.50  ?  107 LEU B CA     1 
ATOM   3669 C C      . LEU B 2 107 ? 18.384 5.207   50.802 1.00 23.98  ?  107 LEU B C      1 
ATOM   3670 O O      . LEU B 2 107 ? 17.569 5.931   51.383 1.00 24.36  ?  107 LEU B O      1 
ATOM   3671 C CB     . LEU B 2 107 ? 18.273 4.887   48.314 1.00 19.58  ?  107 LEU B CB     1 
ATOM   3672 C CG     . LEU B 2 107 ? 18.645 5.483   46.955 1.00 19.75  ?  107 LEU B CG     1 
ATOM   3673 C CD1    . LEU B 2 107 ? 18.115 4.653   45.769 1.00 19.53  ?  107 LEU B CD1    1 
ATOM   3674 C CD2    . LEU B 2 107 ? 18.230 6.963   46.870 1.00 19.61  ?  107 LEU B CD2    1 
ATOM   3675 N N      . TYR B 2 108 ? 18.791 4.078   51.337 1.00 35.54  ?  108 TYR B N      1 
ATOM   3676 C CA     . TYR B 2 108 ? 18.265 3.604   52.587 1.00 36.99  ?  108 TYR B CA     1 
ATOM   3677 C C      . TYR B 2 108 ? 18.462 4.570   53.706 1.00 37.98  ?  108 TYR B C      1 
ATOM   3678 O O      . TYR B 2 108 ? 17.669 4.624   54.607 1.00 47.18  ?  108 TYR B O      1 
ATOM   3679 C CB     . TYR B 2 108 ? 18.801 2.206   52.934 1.00 34.03  ?  108 TYR B CB     1 
ATOM   3680 C CG     . TYR B 2 108 ? 18.997 1.930   54.391 1.00 40.63  ?  108 TYR B CG     1 
ATOM   3681 C CD1    . TYR B 2 108 ? 17.938 1.531   55.188 1.00 43.04  ?  108 TYR B CD1    1 
ATOM   3682 C CD2    . TYR B 2 108 ? 20.247 2.050   54.970 1.00 41.05  ?  108 TYR B CD2    1 
ATOM   3683 C CE1    . TYR B 2 108 ? 18.116 1.286   56.527 1.00 41.47  ?  108 TYR B CE1    1 
ATOM   3684 C CE2    . TYR B 2 108 ? 20.433 1.801   56.306 1.00 40.55  ?  108 TYR B CE2    1 
ATOM   3685 C CZ     . TYR B 2 108 ? 19.362 1.417   57.073 1.00 38.25  ?  108 TYR B CZ     1 
ATOM   3686 O OH     . TYR B 2 108 ? 19.550 1.158   58.392 1.00 38.40  ?  108 TYR B OH     1 
ATOM   3687 N N      . ALA B 2 109 ? 19.513 5.338   53.661 1.00 30.45  ?  109 ALA B N      1 
ATOM   3688 C CA     . ALA B 2 109 ? 19.785 6.232   54.777 1.00 26.41  ?  109 ALA B CA     1 
ATOM   3689 C C      . ALA B 2 109 ? 19.078 7.577   54.633 1.00 34.12  ?  109 ALA B C      1 
ATOM   3690 O O      . ALA B 2 109 ? 19.139 8.395   55.556 1.00 36.12  ?  109 ALA B O      1 
ATOM   3691 C CB     . ALA B 2 109 ? 21.294 6.419   54.933 1.00 25.21  ?  109 ALA B CB     1 
ATOM   3692 N N      . ASP B 2 110 ? 18.443 7.824   53.477 1.00 42.51  ?  110 ASP B N      1 
ATOM   3693 C CA     . ASP B 2 110 ? 17.434 8.876   53.335 1.00 42.90  ?  110 ASP B CA     1 
ATOM   3694 C C      . ASP B 2 110 ? 16.138 8.477   54.020 1.00 43.72  ?  110 ASP B C      1 
ATOM   3695 O O      . ASP B 2 110 ? 15.478 9.303   54.660 1.00 43.69  ?  110 ASP B O      1 
ATOM   3696 C CB     . ASP B 2 110 ? 17.143 9.127   51.847 1.00 46.50  ?  110 ASP B CB     1 
ATOM   3697 C CG     . ASP B 2 110 ? 17.939 10.279  51.246 1.00 51.68  ?  110 ASP B CG     1 
ATOM   3698 O OD1    . ASP B 2 110 ? 19.089 10.562  51.678 1.00 47.36  ?  110 ASP B OD1    1 
ATOM   3699 O OD2    . ASP B 2 110 ? 17.391 10.897  50.305 1.00 57.35  -1 110 ASP B OD2    1 
ATOM   3700 N N      . HIS B 2 111 ? 15.739 7.215   53.834 1.00 46.54  ?  111 HIS B N      1 
ATOM   3701 C CA     . HIS B 2 111 ? 14.554 6.661   54.477 1.00 47.19  ?  111 HIS B CA     1 
ATOM   3702 C C      . HIS B 2 111 ? 14.766 6.530   55.979 1.00 41.21  ?  111 HIS B C      1 
ATOM   3703 O O      . HIS B 2 111 ? 13.861 6.825   56.766 1.00 48.46  ?  111 HIS B O      1 
ATOM   3704 C CB     . HIS B 2 111 ? 14.229 5.302   53.837 1.00 48.48  ?  111 HIS B CB     1 
ATOM   3705 C CG     . HIS B 2 111 ? 12.917 4.709   54.257 1.00 50.70  ?  111 HIS B CG     1 
ATOM   3706 N ND1    . HIS B 2 111 ? 12.594 3.387   54.023 1.00 51.97  ?  111 HIS B ND1    1 
ATOM   3707 C CD2    . HIS B 2 111 ? 11.846 5.254   54.882 1.00 52.32  ?  111 HIS B CD2    1 
ATOM   3708 C CE1    . HIS B 2 111 ? 11.384 3.141   54.496 1.00 55.26  ?  111 HIS B CE1    1 
ATOM   3709 N NE2    . HIS B 2 111 ? 10.909 4.257   55.026 1.00 58.42  ?  111 HIS B NE2    1 
ATOM   3710 N N      . LEU B 2 112 ? 15.960 6.092   56.392 1.00 32.29  ?  112 LEU B N      1 
ATOM   3711 C CA     . LEU B 2 112 ? 16.314 6.042   57.804 1.00 34.96  ?  112 LEU B CA     1 
ATOM   3712 C C      . LEU B 2 112 ? 16.404 7.430   58.423 1.00 34.79  ?  112 LEU B C      1 
ATOM   3713 O O      . LEU B 2 112 ? 16.210 7.567   59.630 1.00 39.93  ?  112 LEU B O      1 
ATOM   3714 C CB     . LEU B 2 112 ? 17.633 5.302   57.994 1.00 28.31  ?  112 LEU B CB     1 
ATOM   3715 C CG     . LEU B 2 112 ? 18.047 4.884   59.409 1.00 27.47  ?  112 LEU B CG     1 
ATOM   3716 C CD1    . LEU B 2 112 ? 17.018 4.014   60.115 1.00 22.26  ?  112 LEU B CD1    1 
ATOM   3717 C CD2    . LEU B 2 112 ? 19.384 4.160   59.364 1.00 32.86  ?  112 LEU B CD2    1 
ATOM   3718 N N      . GLU B 2 113 ? 16.663 8.470   57.627 1.00 30.08  ?  113 GLU B N      1 
ATOM   3719 C CA     . GLU B 2 113 ? 16.646 9.811   58.200 1.00 32.97  ?  113 GLU B CA     1 
ATOM   3720 C C      . GLU B 2 113 ? 15.220 10.339  58.339 1.00 30.36  ?  113 GLU B C      1 
ATOM   3721 O O      . GLU B 2 113 ? 14.895 11.009  59.322 1.00 33.47  ?  113 GLU B O      1 
ATOM   3722 C CB     . GLU B 2 113 ? 17.505 10.749  57.361 1.00 39.04  ?  113 GLU B CB     1 
ATOM   3723 C CG     . GLU B 2 113 ? 18.149 11.849  58.160 1.00 44.21  ?  113 GLU B CG     1 
ATOM   3724 C CD     . GLU B 2 113 ? 19.349 12.436  57.455 1.00 51.93  ?  113 GLU B CD     1 
ATOM   3725 O OE1    . GLU B 2 113 ? 19.136 13.376  56.659 1.00 55.15  ?  113 GLU B OE1    1 
ATOM   3726 O OE2    . GLU B 2 113 ? 20.495 11.948  57.683 1.00 51.98  -1 113 GLU B OE2    1 
ATOM   3727 N N      . SER B 2 114 ? 14.350 10.030  57.384 1.00 32.64  ?  114 SER B N      1 
ATOM   3728 C CA     . SER B 2 114 ? 12.929 10.338  57.534 1.00 33.14  ?  114 SER B CA     1 
ATOM   3729 C C      . SER B 2 114 ? 12.321 9.621   58.732 1.00 40.88  ?  114 SER B C      1 
ATOM   3730 O O      . SER B 2 114 ? 11.538 10.215  59.483 1.00 46.32  ?  114 SER B O      1 
ATOM   3731 C CB     . SER B 2 114 ? 12.172 9.963   56.268 1.00 28.50  ?  114 SER B CB     1 
ATOM   3732 O OG     . SER B 2 114 ? 12.703 10.679  55.173 1.00 37.81  ?  114 SER B OG     1 
ATOM   3733 N N      . VAL B 2 115 ? 12.661 8.346   58.929 1.00 40.45  ?  115 VAL B N      1 
ATOM   3734 C CA     . VAL B 2 115 ? 12.034 7.590   60.006 1.00 42.59  ?  115 VAL B CA     1 
ATOM   3735 C C      . VAL B 2 115 ? 12.489 8.107   61.368 1.00 47.96  ?  115 VAL B C      1 
ATOM   3736 O O      . VAL B 2 115 ? 11.691 8.179   62.312 1.00 48.69  ?  115 VAL B O      1 
ATOM   3737 C CB     . VAL B 2 115 ? 12.315 6.088   59.831 1.00 39.75  ?  115 VAL B CB     1 
ATOM   3738 C CG1    . VAL B 2 115 ? 11.736 5.294   60.986 1.00 36.43  ?  115 VAL B CG1    1 
ATOM   3739 C CG2    . VAL B 2 115 ? 11.745 5.609   58.504 1.00 36.70  ?  115 VAL B CG2    1 
ATOM   3740 N N      . ILE B 2 116 ? 13.771 8.473   61.501 1.00 57.19  ?  116 ILE B N      1 
ATOM   3741 C CA     . ILE B 2 116 ? 14.214 9.099   62.748 1.00 53.39  ?  116 ILE B CA     1 
ATOM   3742 C C      . ILE B 2 116 ? 13.540 10.446  62.923 1.00 49.49  ?  116 ILE B C      1 
ATOM   3743 O O      . ILE B 2 116 ? 13.365 10.924  64.048 1.00 48.28  ?  116 ILE B O      1 
ATOM   3744 C CB     . ILE B 2 116 ? 15.745 9.278   62.811 1.00 45.67  ?  116 ILE B CB     1 
ATOM   3745 C CG1    . ILE B 2 116 ? 16.499 8.095   62.183 1.00 49.64  ?  116 ILE B CG1    1 
ATOM   3746 C CG2    . ILE B 2 116 ? 16.160 9.524   64.277 1.00 40.00  ?  116 ILE B CG2    1 
ATOM   3747 C CD1    . ILE B 2 116 ? 16.389 6.759   62.934 1.00 54.80  ?  116 ILE B CD1    1 
ATOM   3748 N N      . LYS B 2 117 ? 13.196 11.100  61.818 1.00 45.94  ?  117 LYS B N      1 
ATOM   3749 C CA     . LYS B 2 117 ? 12.638 12.439  61.901 1.00 43.87  ?  117 LYS B CA     1 
ATOM   3750 C C      . LYS B 2 117 ? 11.175 12.388  62.338 1.00 46.93  ?  117 LYS B C      1 
ATOM   3751 O O      . LYS B 2 117 ? 10.752 13.172  63.197 1.00 45.89  ?  117 LYS B O      1 
ATOM   3752 C CB     . LYS B 2 117 ? 12.801 13.147  60.553 1.00 39.00  ?  117 LYS B CB     1 
ATOM   3753 C CG     . LYS B 2 117 ? 13.315 14.570  60.643 1.00 33.98  ?  117 LYS B CG     1 
ATOM   3754 C CD     . LYS B 2 117 ? 12.922 15.352  59.429 1.00 37.16  ?  117 LYS B CD     1 
ATOM   3755 C CE     . LYS B 2 117 ? 13.059 16.858  59.664 1.00 48.48  ?  117 LYS B CE     1 
ATOM   3756 N NZ     . LYS B 2 117 ? 12.614 17.646  58.473 1.00 48.06  ?  117 LYS B NZ     1 
ATOM   3757 N N      . GLN B 2 118 ? 10.395 11.461  61.768 1.00 49.24  ?  118 GLN B N      1 
ATOM   3758 C CA     . GLN B 2 118 ? 9.020  11.268  62.226 1.00 49.43  ?  118 GLN B CA     1 
ATOM   3759 C C      . GLN B 2 118 ? 8.990  10.884  63.701 1.00 50.67  ?  118 GLN B C      1 
ATOM   3760 O O      . GLN B 2 118 ? 8.137  11.358  64.454 1.00 50.29  ?  118 GLN B O      1 
ATOM   3761 C CB     . GLN B 2 118 ? 8.309  10.210  61.365 1.00 46.69  ?  118 GLN B CB     1 
ATOM   3762 C CG     . GLN B 2 118 ? 8.027  10.635  59.891 1.00 52.23  ?  118 GLN B CG     1 
ATOM   3763 C CD     . GLN B 2 118 ? 8.174  9.488   58.830 1.00 55.89  ?  118 GLN B CD     1 
ATOM   3764 O OE1    . GLN B 2 118 ? 7.619  8.388   58.978 1.00 59.02  ?  118 GLN B OE1    1 
ATOM   3765 N NE2    . GLN B 2 118 ? 8.924  9.767   57.759 1.00 50.28  ?  118 GLN B NE2    1 
ATOM   3766 N N      . GLU B 2 119 ? 9.928  10.041  64.136 1.00 59.06  ?  119 GLU B N      1 
ATOM   3767 C CA     . GLU B 2 119 ? 9.856  9.424   65.458 1.00 61.15  ?  119 GLU B CA     1 
ATOM   3768 C C      . GLU B 2 119 ? 10.407 10.302  66.584 1.00 57.24  ?  119 GLU B C      1 
ATOM   3769 O O      . GLU B 2 119 ? 9.835  10.350  67.678 1.00 52.16  ?  119 GLU B O      1 
ATOM   3770 C CB     . GLU B 2 119 ? 10.590 8.089   65.423 1.00 67.55  ?  119 GLU B CB     1 
ATOM   3771 C CG     . GLU B 2 119 ? 10.683 7.423   66.769 1.00 75.71  ?  119 GLU B CG     1 
ATOM   3772 C CD     . GLU B 2 119 ? 11.319 6.059   66.686 1.00 81.46  ?  119 GLU B CD     1 
ATOM   3773 O OE1    . GLU B 2 119 ? 11.563 5.595   65.538 1.00 81.82  ?  119 GLU B OE1    1 
ATOM   3774 O OE2    . GLU B 2 119 ? 11.572 5.464   67.764 1.00 82.34  -1 119 GLU B OE2    1 
ATOM   3775 N N      . SER B 2 120 ? 11.534 10.963  66.374 1.00 53.69  ?  120 SER B N      1 
ATOM   3776 C CA     . SER B 2 120 ? 12.253 11.579  67.478 1.00 52.01  ?  120 SER B CA     1 
ATOM   3777 C C      . SER B 2 120 ? 11.847 13.033  67.606 1.00 58.04  ?  120 SER B C      1 
ATOM   3778 O O      . SER B 2 120 ? 11.616 13.719  66.606 1.00 60.57  ?  120 SER B O      1 
ATOM   3779 C CB     . SER B 2 120 ? 13.769 11.484  67.293 1.00 46.82  ?  120 SER B CB     1 
ATOM   3780 O OG     . SER B 2 120 ? 14.452 12.100  68.366 1.00 44.67  ?  120 SER B OG     1 
ATOM   3781 N N      . ASP B 2 121 ? 11.736 13.485  68.848 1.00 65.09  ?  121 ASP B N      1 
ATOM   3782 C CA     . ASP B 2 121 ? 11.601 14.897  69.156 1.00 69.37  ?  121 ASP B CA     1 
ATOM   3783 C C      . ASP B 2 121 ? 12.950 15.545  69.455 1.00 69.09  ?  121 ASP B C      1 
ATOM   3784 O O      . ASP B 2 121 ? 12.992 16.698  69.902 1.00 70.84  ?  121 ASP B O      1 
ATOM   3785 C CB     . ASP B 2 121 ? 10.633 15.097  70.323 1.00 73.58  ?  121 ASP B CB     1 
ATOM   3786 C CG     . ASP B 2 121 ? 11.204 14.618  71.643 1.00 80.28  ?  121 ASP B CG     1 
ATOM   3787 O OD1    . ASP B 2 121 ? 11.144 13.394  71.920 1.00 85.96  ?  121 ASP B OD1    1 
ATOM   3788 O OD2    . ASP B 2 121 ? 11.726 15.473  72.396 1.00 74.87  -1 121 ASP B OD2    1 
ATOM   3789 N N      . LEU B 2 122 ? 14.032 14.811  69.235 1.00 55.91  ?  122 LEU B N      1 
ATOM   3790 C CA     . LEU B 2 122 ? 15.359 15.336  69.461 1.00 53.85  ?  122 LEU B CA     1 
ATOM   3791 C C      . LEU B 2 122 ? 15.697 15.579  70.920 1.00 56.92  ?  122 LEU B C      1 
ATOM   3792 O O      . LEU B 2 122 ? 16.624 16.300  71.221 1.00 57.54  ?  122 LEU B O      1 
ATOM   3793 C CB     . LEU B 2 122 ? 15.586 16.568  68.604 1.00 50.40  ?  122 LEU B CB     1 
ATOM   3794 C CG     . LEU B 2 122 ? 15.397 16.260  67.134 1.00 52.48  ?  122 LEU B CG     1 
ATOM   3795 C CD1    . LEU B 2 122 ? 14.610 17.342  66.434 1.00 52.35  ?  122 LEU B CD1    1 
ATOM   3796 C CD2    . LEU B 2 122 ? 16.771 16.118  66.541 1.00 53.65  ?  122 LEU B CD2    1 
ATOM   3797 N N      . SER B 2 123 ? 14.943 14.980  71.829 1.00 46.52  ?  123 SER B N      1 
ATOM   3798 C CA     . SER B 2 123 ? 15.188 15.239  73.236 1.00 42.60  ?  123 SER B CA     1 
ATOM   3799 C C      . SER B 2 123 ? 16.333 14.393  73.756 1.00 36.44  ?  123 SER B C      1 
ATOM   3800 O O      . SER B 2 123 ? 17.021 14.797  74.693 1.00 34.03  ?  123 SER B O      1 
ATOM   3801 C CB     . SER B 2 123 ? 13.928 14.981  74.045 1.00 40.38  ?  123 SER B CB     1 
ATOM   3802 O OG     . SER B 2 123 ? 13.654 13.599  74.036 1.00 42.89  ?  123 SER B OG     1 
ATOM   3803 N N      . VAL B 2 124 ? 16.548 13.221  73.162 1.00 34.98  ?  124 VAL B N      1 
ATOM   3804 C CA     . VAL B 2 124 ? 17.718 12.421  73.511 1.00 33.58  ?  124 VAL B CA     1 
ATOM   3805 C C      . VAL B 2 124 ? 19.015 13.107  73.066 1.00 35.67  ?  124 VAL B C      1 
ATOM   3806 O O      . VAL B 2 124 ? 20.045 12.984  73.737 1.00 30.83  ?  124 VAL B O      1 
ATOM   3807 C CB     . VAL B 2 124 ? 17.584 11.022  72.893 1.00 29.37  ?  124 VAL B CB     1 
ATOM   3808 C CG1    . VAL B 2 124 ? 17.647 11.118  71.343 1.00 31.11  ?  124 VAL B CG1    1 
ATOM   3809 C CG2    . VAL B 2 124 ? 18.646 10.128  73.436 1.00 23.27  ?  124 VAL B CG2    1 
ATOM   3810 N N      . PHE B 2 125 ? 18.993 13.825  71.926 1.00 39.08  ?  125 PHE B N      1 
ATOM   3811 C CA     . PHE B 2 125 ? 20.197 14.510  71.459 1.00 36.14  ?  125 PHE B CA     1 
ATOM   3812 C C      . PHE B 2 125 ? 20.519 15.686  72.344 1.00 45.78  ?  125 PHE B C      1 
ATOM   3813 O O      . PHE B 2 125 ? 21.680 16.097  72.424 1.00 53.86  ?  125 PHE B O      1 
ATOM   3814 C CB     . PHE B 2 125 ? 20.053 14.957  69.997 1.00 34.58  ?  125 PHE B CB     1 
ATOM   3815 C CG     . PHE B 2 125 ? 19.718 13.833  69.079 1.00 41.65  ?  125 PHE B CG     1 
ATOM   3816 C CD1    . PHE B 2 125 ? 20.711 12.954  68.656 1.00 37.94  ?  125 PHE B CD1    1 
ATOM   3817 C CD2    . PHE B 2 125 ? 18.398 13.599  68.701 1.00 42.03  ?  125 PHE B CD2    1 
ATOM   3818 C CE1    . PHE B 2 125 ? 20.406 11.903  67.848 1.00 39.06  ?  125 PHE B CE1    1 
ATOM   3819 C CE2    . PHE B 2 125 ? 18.076 12.540  67.886 1.00 39.44  ?  125 PHE B CE2    1 
ATOM   3820 C CZ     . PHE B 2 125 ? 19.074 11.690  67.459 1.00 44.00  ?  125 PHE B CZ     1 
ATOM   3821 N N      . ASN B 2 126 ? 19.505 16.239  73.012 1.00 50.93  ?  126 ASN B N      1 
ATOM   3822 C CA     . ASN B 2 126 ? 19.733 17.265  74.023 1.00 48.93  ?  126 ASN B CA     1 
ATOM   3823 C C      . ASN B 2 126 ? 20.228 16.657  75.326 1.00 38.20  ?  126 ASN B C      1 
ATOM   3824 O O      . ASN B 2 126 ? 21.088 17.242  76.000 1.00 31.80  ?  126 ASN B O      1 
ATOM   3825 C CB     . ASN B 2 126 ? 18.453 18.057  74.250 1.00 43.08  ?  126 ASN B CB     1 
ATOM   3826 C CG     . ASN B 2 126 ? 18.304 19.173  73.280 1.00 41.13  ?  126 ASN B CG     1 
ATOM   3827 O OD1    . ASN B 2 126 ? 18.659 20.309  73.578 1.00 37.50  ?  126 ASN B OD1    1 
ATOM   3828 N ND2    . ASN B 2 126 ? 17.805 18.863  72.095 1.00 44.27  ?  126 ASN B ND2    1 
ATOM   3829 N N      . GLU B 2 127 ? 19.702 15.472  75.660 1.00 34.53  ?  127 GLU B N      1 
ATOM   3830 C CA     . GLU B 2 127 ? 20.132 14.731  76.842 1.00 39.13  ?  127 GLU B CA     1 
ATOM   3831 C C      . GLU B 2 127 ? 21.539 14.169  76.668 1.00 43.35  ?  127 GLU B C      1 
ATOM   3832 O O      . GLU B 2 127 ? 22.280 14.053  77.653 1.00 45.10  ?  127 GLU B O      1 
ATOM   3833 C CB     . GLU B 2 127 ? 19.145 13.595  77.154 1.00 38.33  ?  127 GLU B CB     1 
ATOM   3834 C CG     . GLU B 2 127 ? 17.711 14.015  77.516 1.00 33.91  ?  127 GLU B CG     1 
ATOM   3835 C CD     . GLU B 2 127 ? 16.743 12.839  77.596 1.00 43.53  ?  127 GLU B CD     1 
ATOM   3836 O OE1    . GLU B 2 127 ? 17.207 11.686  77.555 1.00 47.49  ?  127 GLU B OE1    1 
ATOM   3837 O OE2    . GLU B 2 127 ? 15.513 13.063  77.698 1.00 47.40  -1 127 GLU B OE2    1 
ATOM   3838 N N      . LEU B 2 128 ? 21.926 13.828  75.428 1.00 38.42  ?  128 LEU B N      1 
ATOM   3839 C CA     . LEU B 2 128 ? 23.257 13.299  75.137 1.00 30.33  ?  128 LEU B CA     1 
ATOM   3840 C C      . LEU B 2 128 ? 24.333 14.393  75.073 1.00 26.30  ?  128 LEU B C      1 
ATOM   3841 O O      . LEU B 2 128 ? 25.524 14.064  75.014 1.00 24.31  ?  128 LEU B O      1 
ATOM   3842 C CB     . LEU B 2 128 ? 23.207 12.475  73.836 1.00 27.70  ?  128 LEU B CB     1 
ATOM   3843 C CG     . LEU B 2 128 ? 24.335 11.520  73.390 1.00 28.54  ?  128 LEU B CG     1 
ATOM   3844 C CD1    . LEU B 2 128 ? 24.689 10.486  74.435 1.00 29.69  ?  128 LEU B CD1    1 
ATOM   3845 C CD2    . LEU B 2 128 ? 23.969 10.811  72.097 1.00 26.93  ?  128 LEU B CD2    1 
ATOM   3846 N N      . ARG B 2 129 ? 23.953 15.677  75.137 1.00 25.57  ?  129 ARG B N      1 
ATOM   3847 C CA     . ARG B 2 129 ? 24.949 16.754  75.192 1.00 22.62  ?  129 ARG B CA     1 
ATOM   3848 C C      . ARG B 2 129 ? 25.889 16.600  76.388 1.00 29.86  ?  129 ARG B C      1 
ATOM   3849 O O      . ARG B 2 129 ? 27.113 16.752  76.265 1.00 33.06  ?  129 ARG B O      1 
ATOM   3850 C CB     . ARG B 2 129 ? 24.250 18.110  75.238 1.00 24.37  ?  129 ARG B CB     1 
ATOM   3851 C CG     . ARG B 2 129 ? 23.696 18.552  73.905 1.00 35.24  ?  129 ARG B CG     1 
ATOM   3852 C CD     . ARG B 2 129 ? 23.456 20.050  73.873 1.00 38.85  ?  129 ARG B CD     1 
ATOM   3853 N NE     . ARG B 2 129 ? 22.125 20.377  74.358 1.00 45.91  ?  129 ARG B NE     1 
ATOM   3854 C CZ     . ARG B 2 129 ? 21.887 21.106  75.439 1.00 47.24  ?  129 ARG B CZ     1 
ATOM   3855 N NH1    . ARG B 2 129 ? 22.907 21.602  76.128 1.00 49.32  ?  129 ARG B NH1    1 
ATOM   3856 N NH2    . ARG B 2 129 ? 20.633 21.353  75.814 1.00 41.32  ?  129 ARG B NH2    1 
ATOM   3857 N N      . ASP B 2 130 ? 25.328 16.297  77.555 1.00 43.37  ?  130 ASP B N      1 
ATOM   3858 C CA     . ASP B 2 130 ? 26.079 16.258  78.796 1.00 47.12  ?  130 ASP B CA     1 
ATOM   3859 C C      . ASP B 2 130 ? 26.829 14.951  78.979 1.00 52.51  ?  130 ASP B C      1 
ATOM   3860 O O      . ASP B 2 130 ? 27.695 14.876  79.857 1.00 57.66  ?  130 ASP B O      1 
ATOM   3861 C CB     . ASP B 2 130 ? 25.111 16.530  79.944 1.00 55.81  ?  130 ASP B CB     1 
ATOM   3862 C CG     . ASP B 2 130 ? 24.090 17.628  79.578 1.00 64.96  ?  130 ASP B CG     1 
ATOM   3863 O OD1    . ASP B 2 130 ? 24.463 18.829  79.603 1.00 68.67  ?  130 ASP B OD1    1 
ATOM   3864 O OD2    . ASP B 2 130 ? 22.929 17.295  79.227 1.00 62.63  -1 130 ASP B OD2    1 
ATOM   3865 N N      . SER B 2 131 ? 26.531 13.925  78.172 1.00 44.08  ?  131 SER B N      1 
ATOM   3866 C CA     . SER B 2 131 ? 27.447 12.797  78.054 1.00 40.37  ?  131 SER B CA     1 
ATOM   3867 C C      . SER B 2 131 ? 28.657 13.164  77.200 1.00 40.77  ?  131 SER B C      1 
ATOM   3868 O O      . SER B 2 131 ? 29.795 12.793  77.522 1.00 35.24  ?  131 SER B O      1 
ATOM   3869 C CB     . SER B 2 131 ? 26.733 11.588  77.467 1.00 44.13  ?  131 SER B CB     1 
ATOM   3870 O OG     . SER B 2 131 ? 25.800 11.052  78.388 1.00 52.61  ?  131 SER B OG     1 
ATOM   3871 N N      . TYR B 2 132 ? 28.428 13.907  76.118 1.00 47.62  ?  132 TYR B N      1 
ATOM   3872 C CA     . TYR B 2 132 ? 29.537 14.378  75.303 1.00 48.68  ?  132 TYR B CA     1 
ATOM   3873 C C      . TYR B 2 132 ? 30.478 15.249  76.123 1.00 47.45  ?  132 TYR B C      1 
ATOM   3874 O O      . TYR B 2 132 ? 31.672 14.949  76.244 1.00 50.80  ?  132 TYR B O      1 
ATOM   3875 C CB     . TYR B 2 132 ? 29.007 15.140  74.090 1.00 47.19  ?  132 TYR B CB     1 
ATOM   3876 C CG     . TYR B 2 132 ? 30.094 15.832  73.320 1.00 46.43  ?  132 TYR B CG     1 
ATOM   3877 C CD1    . TYR B 2 132 ? 30.974 15.098  72.532 1.00 43.24  ?  132 TYR B CD1    1 
ATOM   3878 C CD2    . TYR B 2 132 ? 30.248 17.214  73.388 1.00 45.95  ?  132 TYR B CD2    1 
ATOM   3879 C CE1    . TYR B 2 132 ? 31.961 15.713  71.822 1.00 48.68  ?  132 TYR B CE1    1 
ATOM   3880 C CE2    . TYR B 2 132 ? 31.244 17.842  72.679 1.00 46.67  ?  132 TYR B CE2    1 
ATOM   3881 C CZ     . TYR B 2 132 ? 32.106 17.086  71.902 1.00 49.44  ?  132 TYR B CZ     1 
ATOM   3882 O OH     . TYR B 2 132 ? 33.121 17.688  71.191 1.00 52.26  ?  132 TYR B OH     1 
ATOM   3883 N N      . ASN B 2 133 ? 29.944 16.328  76.714 1.00 39.47  ?  133 ASN B N      1 
ATOM   3884 C CA     . ASN B 2 133 ? 30.771 17.286  77.454 1.00 37.13  ?  133 ASN B CA     1 
ATOM   3885 C C      . ASN B 2 133 ? 31.507 16.642  78.629 1.00 34.73  ?  133 ASN B C      1 
ATOM   3886 O O      . ASN B 2 133 ? 32.634 17.047  78.943 1.00 34.57  ?  133 ASN B O      1 
ATOM   3887 C CB     . ASN B 2 133 ? 29.906 18.449  77.945 1.00 37.84  ?  133 ASN B CB     1 
ATOM   3888 C CG     . ASN B 2 133 ? 29.298 19.231  76.812 1.00 46.49  ?  133 ASN B CG     1 
ATOM   3889 O OD1    . ASN B 2 133 ? 29.746 20.330  76.498 1.00 46.15  ?  133 ASN B OD1    1 
ATOM   3890 N ND2    . ASN B 2 133 ? 28.285 18.659  76.172 1.00 54.67  ?  133 ASN B ND2    1 
ATOM   3891 N N      . ALA B 2 134 ? 30.884 15.646  79.277 1.00 23.18  ?  134 ALA B N      1 
ATOM   3892 C CA     . ALA B 2 134 ? 31.544 14.792  80.271 1.00 23.29  ?  134 ALA B CA     1 
ATOM   3893 C C      . ALA B 2 134 ? 32.800 14.092  79.738 1.00 23.64  ?  134 ALA B C      1 
ATOM   3894 O O      . ALA B 2 134 ? 33.854 14.134  80.379 1.00 23.84  ?  134 ALA B O      1 
ATOM   3895 C CB     . ALA B 2 134 ? 30.561 13.737  80.758 1.00 23.25  ?  134 ALA B CB     1 
ATOM   3896 N N      . VAL B 2 135 ? 32.699 13.377  78.597 1.00 26.98  ?  135 VAL B N      1 
ATOM   3897 C CA     . VAL B 2 135 ? 33.799 12.495  78.186 1.00 22.65  ?  135 VAL B CA     1 
ATOM   3898 C C      . VAL B 2 135 ? 34.839 13.159  77.282 1.00 23.59  ?  135 VAL B C      1 
ATOM   3899 O O      . VAL B 2 135 ? 35.960 12.631  77.166 1.00 22.56  ?  135 VAL B O      1 
ATOM   3900 C CB     . VAL B 2 135 ? 33.274 11.211  77.502 1.00 22.38  ?  135 VAL B CB     1 
ATOM   3901 C CG1    . VAL B 2 135 ? 32.349 10.464  78.417 1.00 22.47  ?  135 VAL B CG1    1 
ATOM   3902 C CG2    . VAL B 2 135 ? 32.611 11.509  76.136 1.00 22.11  ?  135 VAL B CG2    1 
ATOM   3903 N N      . LYS B 2 136 ? 34.536 14.331  76.712 1.00 29.36  ?  136 LYS B N      1 
ATOM   3904 C CA     . LYS B 2 136 ? 35.359 14.912  75.656 1.00 34.24  ?  136 LYS B CA     1 
ATOM   3905 C C      . LYS B 2 136 ? 36.781 15.210  76.135 1.00 41.40  ?  136 LYS B C      1 
ATOM   3906 O O      . LYS B 2 136 ? 37.007 15.512  77.309 1.00 43.23  ?  136 LYS B O      1 
ATOM   3907 C CB     . LYS B 2 136 ? 34.722 16.202  75.136 1.00 33.94  ?  136 LYS B CB     1 
ATOM   3908 C CG     . LYS B 2 136 ? 34.523 17.285  76.193 1.00 32.75  ?  136 LYS B CG     1 
ATOM   3909 C CD     . LYS B 2 136 ? 33.501 18.342  75.761 1.00 35.29  ?  136 LYS B CD     1 
ATOM   3910 C CE     . LYS B 2 136 ? 34.150 19.646  75.342 1.00 30.38  ?  136 LYS B CE     1 
ATOM   3911 N NZ     . LYS B 2 136 ? 35.412 19.868  76.089 1.00 28.63  ?  136 LYS B NZ     1 
ATOM   3912 N N      . PRO B 2 137 ? 37.713 15.245  75.178 1.00 46.47  ?  137 PRO B N      1 
ATOM   3913 C CA     . PRO B 2 137 ? 39.031 15.688  75.589 1.00 46.10  ?  137 PRO B CA     1 
ATOM   3914 C C      . PRO B 2 137 ? 38.940 17.199  75.821 1.00 45.92  ?  137 PRO B C      1 
ATOM   3915 O O      . PRO B 2 137 ? 37.986 17.816  75.396 1.00 42.30  ?  137 PRO B O      1 
ATOM   3916 C CB     . PRO B 2 137 ? 39.877 15.396  74.363 1.00 42.84  ?  137 PRO B CB     1 
ATOM   3917 C CG     . PRO B 2 137 ? 39.162 14.335  73.619 1.00 43.82  ?  137 PRO B CG     1 
ATOM   3918 C CD     . PRO B 2 137 ? 37.731 14.670  73.818 1.00 45.58  ?  137 PRO B CD     1 
ATOM   3919 N N      . GLU B 2 138 ? 39.929 17.787  76.486 1.00 58.37  ?  138 GLU B N      1 
ATOM   3920 C CA     . GLU B 2 138 ? 39.890 19.211  76.759 1.00 54.98  ?  138 GLU B CA     1 
ATOM   3921 C C      . GLU B 2 138 ? 39.975 20.019  75.495 1.00 56.39  ?  138 GLU B C      1 
ATOM   3922 O O      . GLU B 2 138 ? 39.459 21.120  75.427 1.00 58.64  ?  138 GLU B O      1 
ATOM   3923 C CB     . GLU B 2 138 ? 41.012 19.573  77.701 1.00 58.62  ?  138 GLU B CB     1 
ATOM   3924 C CG     . GLU B 2 138 ? 42.251 18.708  77.559 1.00 68.76  ?  138 GLU B CG     1 
ATOM   3925 C CD     . GLU B 2 138 ? 43.261 19.303  76.609 1.00 73.14  ?  138 GLU B CD     1 
ATOM   3926 O OE1    . GLU B 2 138 ? 43.366 20.544  76.564 1.00 71.14  ?  138 GLU B OE1    1 
ATOM   3927 O OE2    . GLU B 2 138 ? 43.951 18.533  75.914 1.00 76.19  -1 138 GLU B OE2    1 
ATOM   3928 N N      . TYR B 2 139 ? 40.604 19.479  74.478 1.00 49.86  ?  139 TYR B N      1 
ATOM   3929 C CA     . TYR B 2 139 ? 40.692 20.155  73.210 1.00 43.49  ?  139 TYR B CA     1 
ATOM   3930 C C      . TYR B 2 139 ? 39.390 20.115  72.436 1.00 45.05  ?  139 TYR B C      1 
ATOM   3931 O O      . TYR B 2 139 ? 39.224 20.835  71.476 1.00 54.27  ?  139 TYR B O      1 
ATOM   3932 C CB     . TYR B 2 139 ? 41.843 19.586  72.387 1.00 38.79  ?  139 TYR B CB     1 
ATOM   3933 C CG     . TYR B 2 139 ? 41.799 18.117  72.044 1.00 40.81  ?  139 TYR B CG     1 
ATOM   3934 C CD1    . TYR B 2 139 ? 41.005 17.648  71.016 1.00 47.70  ?  139 TYR B CD1    1 
ATOM   3935 C CD2    . TYR B 2 139 ? 42.599 17.210  72.712 1.00 42.11  ?  139 TYR B CD2    1 
ATOM   3936 C CE1    . TYR B 2 139 ? 40.976 16.314  70.688 1.00 49.65  ?  139 TYR B CE1    1 
ATOM   3937 C CE2    . TYR B 2 139 ? 42.579 15.871  72.387 1.00 45.03  ?  139 TYR B CE2    1 
ATOM   3938 C CZ     . TYR B 2 139 ? 41.763 15.432  71.373 1.00 49.51  ?  139 TYR B CZ     1 
ATOM   3939 O OH     . TYR B 2 139 ? 41.731 14.104  71.042 1.00 55.49  ?  139 TYR B OH     1 
ATOM   3940 N N      . ALA B 2 140 ? 38.462 19.279  72.852 1.00 35.48  ?  140 ALA B N      1 
ATOM   3941 C CA     . ALA B 2 140 ? 37.182 19.200  72.162 1.00 35.08  ?  140 ALA B CA     1 
ATOM   3942 C C      . ALA B 2 140 ? 36.250 20.311  72.633 1.00 37.65  ?  140 ALA B C      1 
ATOM   3943 O O      . ALA B 2 140 ? 36.273 20.711  73.802 1.00 36.80  ?  140 ALA B O      1 
ATOM   3944 C CB     . ALA B 2 140 ? 36.536 17.831  72.373 1.00 35.98  ?  140 ALA B CB     1 
ATOM   3945 N N      . VAL B 2 141 ? 35.463 20.849  71.726 1.00 39.47  ?  141 VAL B N      1 
ATOM   3946 C CA     . VAL B 2 141 ? 34.654 21.985  72.095 1.00 43.84  ?  141 VAL B CA     1 
ATOM   3947 C C      . VAL B 2 141 ? 33.361 21.648  72.794 1.00 49.51  ?  141 VAL B C      1 
ATOM   3948 O O      . VAL B 2 141 ? 32.560 20.877  72.284 1.00 52.14  ?  141 VAL B O      1 
ATOM   3949 C CB     . VAL B 2 141 ? 34.476 22.983  70.936 1.00 43.26  ?  141 VAL B CB     1 
ATOM   3950 C CG1    . VAL B 2 141 ? 33.950 22.303  69.685 1.00 32.91  ?  141 VAL B CG1    1 
ATOM   3951 C CG2    . VAL B 2 141 ? 33.633 24.177  71.334 1.00 48.39  ?  141 VAL B CG2    1 
ATOM   3952 N N      . THR B 2 142 ? 33.200 22.169  73.994 1.00 49.52  ?  142 THR B N      1 
ATOM   3953 C CA     . THR B 2 142 ? 31.969 22.012  74.764 1.00 51.95  ?  142 THR B CA     1 
ATOM   3954 C C      . THR B 2 142 ? 30.767 22.397  73.902 1.00 49.27  ?  142 THR B C      1 
ATOM   3955 O O      . THR B 2 142 ? 30.741 23.485  73.319 1.00 46.28  ?  142 THR B O      1 
ATOM   3956 C CB     . THR B 2 142 ? 32.019 22.893  76.024 1.00 54.73  ?  142 THR B CB     1 
ATOM   3957 O OG1    . THR B 2 142 ? 32.974 22.373  76.957 1.00 57.35  ?  142 THR B OG1    1 
ATOM   3958 C CG2    . THR B 2 142 ? 30.655 22.975  76.698 1.00 52.24  ?  142 THR B CG2    1 
ATOM   3959 N N      . HIS B 2 143 ? 29.769 21.502  73.814 1.00 40.16  ?  143 HIS B N      1 
ATOM   3960 C CA     . HIS B 2 143 ? 28.551 21.771  73.043 1.00 41.85  ?  143 HIS B CA     1 
ATOM   3961 C C      . HIS B 2 143 ? 27.499 22.375  73.966 1.00 47.17  ?  143 HIS B C      1 
ATOM   3962 O O      . HIS B 2 143 ? 26.995 21.697  74.866 1.00 46.21  ?  143 HIS B O      1 
ATOM   3963 C CB     . HIS B 2 143 ? 28.017 20.503  72.385 1.00 43.90  ?  143 HIS B CB     1 
ATOM   3964 C CG     . HIS B 2 143 ? 26.883 20.736  71.430 1.00 36.83  ?  143 HIS B CG     1 
ATOM   3965 N ND1    . HIS B 2 143 ? 25.696 21.330  71.800 1.00 36.02  ?  143 HIS B ND1    1 
ATOM   3966 C CD2    . HIS B 2 143 ? 26.751 20.432  70.118 1.00 38.03  ?  143 HIS B CD2    1 
ATOM   3967 C CE1    . HIS B 2 143 ? 24.887 21.388  70.760 1.00 37.39  ?  143 HIS B CE1    1 
ATOM   3968 N NE2    . HIS B 2 143 ? 25.500 20.842  69.726 1.00 39.93  ?  143 HIS B NE2    1 
ATOM   3969 N N      . GLU B 2 144 ? 27.191 23.662  73.757 1.00 72.36  ?  144 GLU B N      1 
ATOM   3970 C CA     . GLU B 2 144 ? 26.244 24.410  74.577 1.00 72.86  ?  144 GLU B CA     1 
ATOM   3971 C C      . GLU B 2 144 ? 24.865 24.648  73.954 1.00 63.48  ?  144 GLU B C      1 
ATOM   3972 O O      . GLU B 2 144 ? 23.987 25.133  74.666 1.00 63.43  ?  144 GLU B O      1 
ATOM   3973 C CB     . GLU B 2 144 ? 26.849 25.774  74.929 1.00 81.74  ?  144 GLU B CB     1 
ATOM   3974 C CG     . GLU B 2 144 ? 26.980 26.721  73.717 1.00 82.75  ?  144 GLU B CG     1 
ATOM   3975 C CD     . GLU B 2 144 ? 28.348 26.671  73.035 1.00 78.93  ?  144 GLU B CD     1 
ATOM   3976 O OE1    . GLU B 2 144 ? 28.598 25.716  72.259 1.00 73.31  ?  144 GLU B OE1    1 
ATOM   3977 O OE2    . GLU B 2 144 ? 29.165 27.598  73.267 1.00 79.11  -1 144 GLU B OE2    1 
ATOM   3978 N N      . THR B 2 145 ? 24.646 24.338  72.672 1.00 49.53  ?  145 THR B N      1 
ATOM   3979 C CA     . THR B 2 145 ? 23.406 24.739  72.001 1.00 48.91  ?  145 THR B CA     1 
ATOM   3980 C C      . THR B 2 145 ? 22.253 23.768  72.306 1.00 46.62  ?  145 THR B C      1 
ATOM   3981 O O      . THR B 2 145 ? 22.449 22.603  72.661 1.00 47.08  ?  145 THR B O      1 
ATOM   3982 C CB     . THR B 2 145 ? 23.601 24.848  70.473 1.00 48.95  ?  145 THR B CB     1 
ATOM   3983 O OG1    . THR B 2 145 ? 24.815 25.552  70.169 1.00 49.03  ?  145 THR B OG1    1 
ATOM   3984 C CG2    . THR B 2 145 ? 22.428 25.602  69.818 1.00 40.84  ?  145 THR B CG2    1 
ATOM   3985 N N      . GLU B 2 146 ? 21.027 24.269  72.173 1.00 48.30  ?  146 GLU B N      1 
ATOM   3986 C CA     . GLU B 2 146 ? 19.872 23.379  72.134 1.00 46.26  ?  146 GLU B CA     1 
ATOM   3987 C C      . GLU B 2 146 ? 19.707 22.797  70.737 1.00 50.51  ?  146 GLU B C      1 
ATOM   3988 O O      . GLU B 2 146 ? 19.888 23.491  69.729 1.00 45.50  ?  146 GLU B O      1 
ATOM   3989 C CB     . GLU B 2 146 ? 18.587 24.097  72.527 1.00 44.68  ?  146 GLU B CB     1 
ATOM   3990 C CG     . GLU B 2 146 ? 17.404 23.134  72.591 1.00 53.65  ?  146 GLU B CG     1 
ATOM   3991 C CD     . GLU B 2 146 ? 16.046 23.816  72.770 1.00 62.11  ?  146 GLU B CD     1 
ATOM   3992 O OE1    . GLU B 2 146 ? 15.696 24.676  71.931 1.00 68.69  ?  146 GLU B OE1    1 
ATOM   3993 O OE2    . GLU B 2 146 ? 15.324 23.485  73.744 1.00 61.29  -1 146 GLU B OE2    1 
ATOM   3994 N N      . ILE B 2 147 ? 19.341 21.522  70.686 1.00 47.87  ?  147 ILE B N      1 
ATOM   3995 C CA     . ILE B 2 147 ? 19.177 20.803  69.433 1.00 41.44  ?  147 ILE B CA     1 
ATOM   3996 C C      . ILE B 2 147 ? 17.679 20.748  69.167 1.00 44.93  ?  147 ILE B C      1 
ATOM   3997 O O      . ILE B 2 147 ? 16.943 20.021  69.842 1.00 41.04  ?  147 ILE B O      1 
ATOM   3998 C CB     . ILE B 2 147 ? 19.816 19.420  69.519 1.00 37.97  ?  147 ILE B CB     1 
ATOM   3999 C CG1    . ILE B 2 147 ? 21.311 19.603  69.845 1.00 35.07  ?  147 ILE B CG1    1 
ATOM   4000 C CG2    . ILE B 2 147 ? 19.549 18.629  68.244 1.00 42.73  ?  147 ILE B CG2    1 
ATOM   4001 C CD1    . ILE B 2 147 ? 22.074 18.332  70.089 1.00 33.04  ?  147 ILE B CD1    1 
ATOM   4002 N N      . LYS B 2 148 ? 17.216 21.579  68.228 1.00 55.76  ?  148 LYS B N      1 
ATOM   4003 C CA     . LYS B 2 148 ? 15.812 21.632  67.845 1.00 58.93  ?  148 LYS B CA     1 
ATOM   4004 C C      . LYS B 2 148 ? 15.511 20.959  66.517 1.00 55.77  ?  148 LYS B C      1 
ATOM   4005 O O      . LYS B 2 148 ? 14.331 20.774  66.191 1.00 52.97  ?  148 LYS B O      1 
ATOM   4006 C CB     . LYS B 2 148 ? 15.341 23.092  67.784 1.00 65.44  ?  148 LYS B CB     1 
ATOM   4007 C CG     . LYS B 2 148 ? 15.471 23.855  69.100 1.00 66.20  ?  148 LYS B CG     1 
ATOM   4008 C CD     . LYS B 2 148 ? 14.112 24.368  69.611 1.00 66.32  ?  148 LYS B CD     1 
ATOM   4009 C CE     . LYS B 2 148 ? 13.159 23.237  70.037 1.00 62.05  ?  148 LYS B CE     1 
ATOM   4010 N NZ     . LYS B 2 148 ? 11.885 23.760  70.648 1.00 60.06  ?  148 LYS B NZ     1 
ATOM   4011 N N      . THR B 2 149 ? 16.528 20.711  65.709 1.00 57.81  ?  149 THR B N      1 
ATOM   4012 C CA     . THR B 2 149 ? 16.313 20.019  64.450 1.00 57.21  ?  149 THR B CA     1 
ATOM   4013 C C      . THR B 2 149 ? 17.219 18.844  64.241 1.00 53.46  ?  149 THR B C      1 
ATOM   4014 O O      . THR B 2 149 ? 18.255 18.730  64.865 1.00 55.67  ?  149 THR B O      1 
ATOM   4015 C CB     . THR B 2 149 ? 16.630 20.880  63.292 1.00 62.18  ?  149 THR B CB     1 
ATOM   4016 O OG1    . THR B 2 149 ? 18.009 20.678  62.997 1.00 62.18  ?  149 THR B OG1    1 
ATOM   4017 C CG2    . THR B 2 149 ? 16.306 22.341  63.607 1.00 65.57  ?  149 THR B CG2    1 
ATOM   4018 N N      . LEU B 2 150 ? 16.819 17.965  63.346 1.00 40.63  ?  150 LEU B N      1 
ATOM   4019 C CA     . LEU B 2 150 ? 17.614 16.764  63.122 1.00 41.53  ?  150 LEU B CA     1 
ATOM   4020 C C      . LEU B 2 150 ? 19.005 17.081  62.568 1.00 48.30  ?  150 LEU B C      1 
ATOM   4021 O O      . LEU B 2 150 ? 19.927 16.271  62.738 1.00 51.68  ?  150 LEU B O      1 
ATOM   4022 C CB     . LEU B 2 150 ? 16.865 15.801  62.193 1.00 45.59  ?  150 LEU B CB     1 
ATOM   4023 C CG     . LEU B 2 150 ? 17.293 14.341  62.366 1.00 50.16  ?  150 LEU B CG     1 
ATOM   4024 C CD1    . LEU B 2 150 ? 17.096 13.895  63.811 1.00 56.71  ?  150 LEU B CD1    1 
ATOM   4025 C CD2    . LEU B 2 150 ? 16.569 13.413  61.407 1.00 50.13  ?  150 LEU B CD2    1 
ATOM   4026 N N      . ASP B 2 151 ? 19.172 18.233  61.954 1.00 55.31  ?  151 ASP B N      1 
ATOM   4027 C CA     . ASP B 2 151 ? 20.465 18.587  61.461 1.00 58.50  ?  151 ASP B CA     1 
ATOM   4028 C C      . ASP B 2 151 ? 21.396 19.100  62.528 1.00 63.97  ?  151 ASP B C      1 
ATOM   4029 O O      . ASP B 2 151 ? 22.585 19.094  62.318 1.00 68.15  ?  151 ASP B O      1 
ATOM   4030 C CB     . ASP B 2 151 ? 20.372 19.516  60.273 1.00 68.80  ?  151 ASP B CB     1 
ATOM   4031 C CG     . ASP B 2 151 ? 19.676 18.886  59.096 1.00 79.14  ?  151 ASP B CG     1 
ATOM   4032 O OD1    . ASP B 2 151 ? 18.434 18.784  59.131 1.00 81.42  ?  151 ASP B OD1    1 
ATOM   4033 O OD2    . ASP B 2 151 ? 20.363 18.503  58.131 1.00 84.25  -1 151 ASP B OD2    1 
ATOM   4034 N N      . GLU B 2 152 ? 20.897 19.596  63.654 1.00 60.34  ?  152 GLU B N      1 
ATOM   4035 C CA     . GLU B 2 152 ? 21.809 19.914  64.744 1.00 60.67  ?  152 GLU B CA     1 
ATOM   4036 C C      . GLU B 2 152 ? 22.205 18.661  65.520 1.00 58.85  ?  152 GLU B C      1 
ATOM   4037 O O      . GLU B 2 152 ? 23.372 18.513  65.894 1.00 58.88  ?  152 GLU B O      1 
ATOM   4038 C CB     . GLU B 2 152 ? 21.197 20.944  65.675 1.00 63.64  ?  152 GLU B CB     1 
ATOM   4039 C CG     . GLU B 2 152 ? 20.535 22.080  64.972 1.00 70.53  ?  152 GLU B CG     1 
ATOM   4040 C CD     . GLU B 2 152 ? 19.907 23.030  65.955 1.00 78.14  ?  152 GLU B CD     1 
ATOM   4041 O OE1    . GLU B 2 152 ? 20.643 23.891  66.479 1.00 82.44  ?  152 GLU B OE1    1 
ATOM   4042 O OE2    . GLU B 2 152 ? 18.693 22.893  66.228 1.00 82.39  -1 152 GLU B OE2    1 
ATOM   4043 N N      . ALA B 2 153 ? 21.251 17.756  65.782 1.00 37.28  ?  153 ALA B N      1 
ATOM   4044 C CA     . ALA B 2 153 ? 21.623 16.438  66.283 1.00 33.53  ?  153 ALA B CA     1 
ATOM   4045 C C      . ALA B 2 153 ? 22.659 15.787  65.368 1.00 36.23  ?  153 ALA B C      1 
ATOM   4046 O O      . ALA B 2 153 ? 23.535 15.051  65.841 1.00 26.28  ?  153 ALA B O      1 
ATOM   4047 C CB     . ALA B 2 153 ? 20.387 15.538  66.429 1.00 21.31  ?  153 ALA B CB     1 
ATOM   4048 N N      . LYS B 2 154 ? 22.589 16.082  64.062 1.00 47.39  ?  154 LYS B N      1 
ATOM   4049 C CA     . LYS B 2 154 ? 23.523 15.541  63.076 1.00 45.82  ?  154 LYS B CA     1 
ATOM   4050 C C      . LYS B 2 154 ? 24.866 16.257  63.110 1.00 45.75  ?  154 LYS B C      1 
ATOM   4051 O O      . LYS B 2 154 ? 25.909 15.617  62.948 1.00 53.22  ?  154 LYS B O      1 
ATOM   4052 C CB     . LYS B 2 154 ? 22.917 15.645  61.679 1.00 46.08  ?  154 LYS B CB     1 
ATOM   4053 C CG     . LYS B 2 154 ? 23.284 14.559  60.709 1.00 39.47  ?  154 LYS B CG     1 
ATOM   4054 C CD     . LYS B 2 154 ? 22.146 14.454  59.737 1.00 41.95  ?  154 LYS B CD     1 
ATOM   4055 C CE     . LYS B 2 154 ? 20.827 14.438  60.510 1.00 50.26  ?  154 LYS B CE     1 
ATOM   4056 N NZ     . LYS B 2 154 ? 19.581 14.534  59.676 1.00 54.62  ?  154 LYS B NZ     1 
ATOM   4057 N N      . GLN B 2 155 ? 24.871 17.580  63.274 1.00 43.82  ?  155 GLN B N      1 
ATOM   4058 C CA     . GLN B 2 155 ? 26.133 18.270  63.530 1.00 44.83  ?  155 GLN B CA     1 
ATOM   4059 C C      . GLN B 2 155 ? 26.750 17.774  64.827 1.00 46.46  ?  155 GLN B C      1 
ATOM   4060 O O      . GLN B 2 155 ? 27.937 17.436  64.889 1.00 45.84  ?  155 GLN B O      1 
ATOM   4061 C CB     . GLN B 2 155 ? 25.903 19.778  63.596 1.00 46.50  ?  155 GLN B CB     1 
ATOM   4062 C CG     . GLN B 2 155 ? 25.413 20.364  62.305 1.00 54.12  ?  155 GLN B CG     1 
ATOM   4063 C CD     . GLN B 2 155 ? 26.537 21.005  61.513 1.00 61.26  ?  155 GLN B CD     1 
ATOM   4064 O OE1    . GLN B 2 155 ? 27.586 21.362  62.072 1.00 62.56  ?  155 GLN B OE1    1 
ATOM   4065 N NE2    . GLN B 2 155 ? 26.324 21.165  60.207 1.00 61.44  ?  155 GLN B NE2    1 
ATOM   4066 N N      . PHE B 2 156 ? 25.936 17.711  65.874 1.00 45.61  ?  156 PHE B N      1 
ATOM   4067 C CA     . PHE B 2 156 ? 26.388 17.242  67.174 1.00 40.90  ?  156 PHE B CA     1 
ATOM   4068 C C      . PHE B 2 156 ? 26.924 15.818  67.105 1.00 38.45  ?  156 PHE B C      1 
ATOM   4069 O O      . PHE B 2 156 ? 28.092 15.566  67.407 1.00 42.00  ?  156 PHE B O      1 
ATOM   4070 C CB     . PHE B 2 156 ? 25.220 17.309  68.145 1.00 34.23  ?  156 PHE B CB     1 
ATOM   4071 C CG     . PHE B 2 156 ? 25.558 16.816  69.455 1.00 31.68  ?  156 PHE B CG     1 
ATOM   4072 C CD1    . PHE B 2 156 ? 26.650 17.363  70.132 1.00 34.48  ?  156 PHE B CD1    1 
ATOM   4073 C CD2    . PHE B 2 156 ? 24.832 15.801  70.020 1.00 29.49  ?  156 PHE B CD2    1 
ATOM   4074 C CE1    . PHE B 2 156 ? 27.005 16.935  71.373 1.00 30.90  ?  156 PHE B CE1    1 
ATOM   4075 C CE2    . PHE B 2 156 ? 25.173 15.354  71.281 1.00 39.12  ?  156 PHE B CE2    1 
ATOM   4076 C CZ     . PHE B 2 156 ? 26.268 15.923  71.962 1.00 38.22  ?  156 PHE B CZ     1 
ATOM   4077 N N      . ILE B 2 157 ? 26.070 14.878  66.689 1.00 38.65  ?  157 ILE B N      1 
ATOM   4078 C CA     . ILE B 2 157 ? 26.416 13.460  66.687 1.00 39.95  ?  157 ILE B CA     1 
ATOM   4079 C C      . ILE B 2 157 ? 27.801 13.261  66.092 1.00 42.81  ?  157 ILE B C      1 
ATOM   4080 O O      . ILE B 2 157 ? 28.632 12.530  66.646 1.00 44.85  ?  157 ILE B O      1 
ATOM   4081 C CB     . ILE B 2 157 ? 25.343 12.662  65.910 1.00 45.55  ?  157 ILE B CB     1 
ATOM   4082 C CG1    . ILE B 2 157 ? 25.400 11.169  66.184 1.00 51.02  ?  157 ILE B CG1    1 
ATOM   4083 C CG2    . ILE B 2 157 ? 25.516 12.812  64.407 1.00 40.59  ?  157 ILE B CG2    1 
ATOM   4084 C CD1    . ILE B 2 157 ? 24.538 10.376  65.200 1.00 54.84  ?  157 ILE B CD1    1 
ATOM   4085 N N      . LEU B 2 158 ? 28.093 13.953  64.983 1.00 30.51  ?  158 LEU B N      1 
ATOM   4086 C CA     . LEU B 2 158 ? 29.277 13.640  64.197 1.00 34.51  ?  158 LEU B CA     1 
ATOM   4087 C C      . LEU B 2 158 ? 30.555 14.160  64.834 1.00 37.14  ?  158 LEU B C      1 
ATOM   4088 O O      . LEU B 2 158 ? 31.635 13.639  64.523 1.00 40.18  ?  158 LEU B O      1 
ATOM   4089 C CB     . LEU B 2 158 ? 29.142 14.187  62.750 1.00 32.33  ?  158 LEU B CB     1 
ATOM   4090 C CG     . LEU B 2 158 ? 28.162 13.488  61.774 1.00 33.44  ?  158 LEU B CG     1 
ATOM   4091 C CD1    . LEU B 2 158 ? 28.259 13.951  60.355 1.00 31.12  ?  158 LEU B CD1    1 
ATOM   4092 C CD2    . LEU B 2 158 ? 28.298 11.971  61.800 1.00 41.24  ?  158 LEU B CD2    1 
ATOM   4093 N N      . SER B 2 159 ? 30.452 15.167  65.713 1.00 30.39  ?  159 SER B N      1 
ATOM   4094 C CA     . SER B 2 159 ? 31.622 15.734  66.375 1.00 30.51  ?  159 SER B CA     1 
ATOM   4095 C C      . SER B 2 159 ? 32.281 14.763  67.350 1.00 35.37  ?  159 SER B C      1 
ATOM   4096 O O      . SER B 2 159 ? 33.413 15.026  67.780 1.00 33.63  ?  159 SER B O      1 
ATOM   4097 C CB     . SER B 2 159 ? 31.252 17.039  67.092 1.00 28.94  ?  159 SER B CB     1 
ATOM   4098 O OG     . SER B 2 159 ? 30.032 16.931  67.814 1.00 34.86  ?  159 SER B OG     1 
ATOM   4099 N N      . PHE B 2 160 ? 31.614 13.649  67.688 1.00 29.51  ?  160 PHE B N      1 
ATOM   4100 C CA     . PHE B 2 160 ? 32.221 12.644  68.543 1.00 23.38  ?  160 PHE B CA     1 
ATOM   4101 C C      . PHE B 2 160 ? 33.564 12.217  67.997 1.00 31.33  ?  160 PHE B C      1 
ATOM   4102 O O      . PHE B 2 160 ? 34.407 11.704  68.756 1.00 26.35  ?  160 PHE B O      1 
ATOM   4103 C CB     . PHE B 2 160 ? 31.323 11.421  68.663 1.00 20.77  ?  160 PHE B CB     1 
ATOM   4104 C CG     . PHE B 2 160 ? 29.986 11.720  69.236 1.00 25.52  ?  160 PHE B CG     1 
ATOM   4105 C CD1    . PHE B 2 160 ? 29.708 12.984  69.766 1.00 30.16  ?  160 PHE B CD1    1 
ATOM   4106 C CD2    . PHE B 2 160 ? 28.995 10.736  69.260 1.00 25.19  ?  160 PHE B CD2    1 
ATOM   4107 C CE1    . PHE B 2 160 ? 28.452 13.281  70.297 1.00 27.11  ?  160 PHE B CE1    1 
ATOM   4108 C CE2    . PHE B 2 160 ? 27.735 11.009  69.784 1.00 27.13  ?  160 PHE B CE2    1 
ATOM   4109 C CZ     . PHE B 2 160 ? 27.461 12.288  70.298 1.00 31.74  ?  160 PHE B CZ     1 
ATOM   4110 N N      . VAL B 2 161 ? 33.764 12.410  66.684 1.00 32.29  ?  161 VAL B N      1 
ATOM   4111 C CA     . VAL B 2 161 ? 35.033 12.114  66.036 1.00 31.45  ?  161 VAL B CA     1 
ATOM   4112 C C      . VAL B 2 161 ? 36.167 12.835  66.753 1.00 37.68  ?  161 VAL B C      1 
ATOM   4113 O O      . VAL B 2 161 ? 37.310 12.362  66.757 1.00 42.15  ?  161 VAL B O      1 
ATOM   4114 C CB     . VAL B 2 161 ? 34.951 12.467  64.526 1.00 28.87  ?  161 VAL B CB     1 
ATOM   4115 C CG1    . VAL B 2 161 ? 34.895 13.975  64.295 1.00 26.24  ?  161 VAL B CG1    1 
ATOM   4116 C CG2    . VAL B 2 161 ? 36.077 11.821  63.745 1.00 23.98  ?  161 VAL B CG2    1 
ATOM   4117 N N      . MET B 2 162 ? 35.875 13.957  67.419 1.00 46.31  ?  162 MET B N      1 
ATOM   4118 C CA     . MET B 2 162 ? 36.935 14.623  68.174 1.00 45.52  ?  162 MET B CA     1 
ATOM   4119 C C      . MET B 2 162 ? 37.503 13.739  69.273 1.00 44.51  ?  162 MET B C      1 
ATOM   4120 O O      . MET B 2 162 ? 38.666 13.921  69.660 1.00 49.26  ?  162 MET B O      1 
ATOM   4121 C CB     . MET B 2 162 ? 36.442 15.952  68.751 1.00 46.87  ?  162 MET B CB     1 
ATOM   4122 C CG     . MET B 2 162 ? 36.453 17.097  67.729 1.00 44.94  ?  162 MET B CG     1 
ATOM   4123 S SD     . MET B 2 162 ? 38.099 17.341  67.027 1.00 54.08  ?  162 MET B SD     1 
ATOM   4124 C CE     . MET B 2 162 ? 37.710 17.513  65.270 1.00 57.80  ?  162 MET B CE     1 
ATOM   4125 N N      . LEU B 2 163 ? 36.757 12.762  69.753 1.00 31.15  ?  163 LEU B N      1 
ATOM   4126 C CA     . LEU B 2 163 ? 37.209 11.894  70.839 1.00 41.12  ?  163 LEU B CA     1 
ATOM   4127 C C      . LEU B 2 163 ? 38.136 10.830  70.324 1.00 38.00  ?  163 LEU B C      1 
ATOM   4128 O O      . LEU B 2 163 ? 38.627 10.001  71.076 1.00 34.42  ?  163 LEU B O      1 
ATOM   4129 C CB     . LEU B 2 163 ? 36.026 11.261  71.574 1.00 22.17  ?  163 LEU B CB     1 
ATOM   4130 C CG     . LEU B 2 163 ? 35.179 11.981  72.610 1.00 27.89  ?  163 LEU B CG     1 
ATOM   4131 C CD1    . LEU B 2 163 ? 34.948 13.441  72.273 1.00 32.99  ?  163 LEU B CD1    1 
ATOM   4132 C CD2    . LEU B 2 163 ? 33.860 11.244  72.662 1.00 27.28  ?  163 LEU B CD2    1 
ATOM   4133 N N      . ASN B 2 164 ? 38.396 10.865  69.037 1.00 39.78  ?  164 ASN B N      1 
ATOM   4134 C CA     . ASN B 2 164 ? 39.220 9.849   68.427 1.00 39.49  ?  164 ASN B CA     1 
ATOM   4135 C C      . ASN B 2 164 ? 40.689 9.894   68.785 1.00 45.07  ?  164 ASN B C      1 
ATOM   4136 O O      . ASN B 2 164 ? 41.212 10.941  69.133 1.00 44.11  ?  164 ASN B O      1 
ATOM   4137 C CB     . ASN B 2 164 ? 39.036 9.853   66.910 1.00 32.27  ?  164 ASN B CB     1 
ATOM   4138 C CG     . ASN B 2 164 ? 37.883 8.988   66.446 1.00 41.63  ?  164 ASN B CG     1 
ATOM   4139 O OD1    . ASN B 2 164 ? 36.770 9.092   66.942 1.00 36.84  ?  164 ASN B OD1    1 
ATOM   4140 N ND2    . ASN B 2 164 ? 38.149 8.139   65.467 1.00 39.98  ?  164 ASN B ND2    1 
ATOM   4141 N N      . ASP B 2 165 ? 41.344 8.755   68.704 1.00 55.96  ?  165 ASP B N      1 
ATOM   4142 C CA     . ASP B 2 165 ? 42.752 8.626   69.034 1.00 55.98  ?  165 ASP B CA     1 
ATOM   4143 C C      . ASP B 2 165 ? 43.151 8.783   70.481 1.00 50.70  ?  165 ASP B C      1 
ATOM   4144 O O      . ASP B 2 165 ? 44.294 8.650   70.806 1.00 48.22  ?  165 ASP B O      1 
ATOM   4145 C CB     . ASP B 2 165 ? 43.634 9.224   67.939 1.00 53.34  ?  165 ASP B CB     1 
ATOM   4146 C CG     . ASP B 2 165 ? 43.383 8.605   66.591 1.00 52.60  ?  165 ASP B CG     1 
ATOM   4147 O OD1    . ASP B 2 165 ? 43.386 7.366   66.498 1.00 58.18  ?  165 ASP B OD1    1 
ATOM   4148 O OD2    . ASP B 2 165 ? 43.184 9.355   65.623 1.00 48.09  -1 165 ASP B OD2    1 
ATOM   4149 N N      . ASN B 2 166 ? 42.158 9.036   71.339 1.00 54.46  ?  166 ASN B N      1 
ATOM   4150 C CA     . ASN B 2 166 ? 42.418 9.267   72.759 1.00 49.48  ?  166 ASN B CA     1 
ATOM   4151 C C      . ASN B 2 166 ? 41.488 8.472   73.672 1.00 49.82  ?  166 ASN B C      1 
ATOM   4152 O O      . ASN B 2 166 ? 41.877 7.425   74.187 1.00 52.87  ?  166 ASN B O      1 
ATOM   4153 C CB     . ASN B 2 166 ? 42.259 10.766  73.051 1.00 46.03  ?  166 ASN B CB     1 
ATOM   4154 C CG     . ASN B 2 166 ? 42.579 11.130  74.492 1.00 48.29  ?  166 ASN B CG     1 
ATOM   4155 O OD1    . ASN B 2 166 ? 43.424 10.509  75.136 1.00 53.98  ?  166 ASN B OD1    1 
ATOM   4156 N ND2    . ASN B 2 166 ? 41.903 12.152  75.001 1.00 47.55  ?  166 ASN B ND2    1 
ATOM   4157 N N      . VAL B 2 167 ? 40.264 8.953   73.875 1.00 37.05  ?  167 VAL B N      1 
ATOM   4158 C CA     . VAL B 2 167 ? 39.345 8.303   74.818 1.00 36.39  ?  167 VAL B CA     1 
ATOM   4159 C C      . VAL B 2 167 ? 38.768 6.973   74.353 1.00 42.22  ?  167 VAL B C      1 
ATOM   4160 O O      . VAL B 2 167 ? 38.349 6.155   75.169 1.00 44.01  ?  167 VAL B O      1 
ATOM   4161 C CB     . VAL B 2 167 ? 38.173 9.241   75.179 1.00 36.61  ?  167 VAL B CB     1 
ATOM   4162 C CG1    . VAL B 2 167 ? 37.948 9.265   76.683 1.00 36.55  ?  167 VAL B CG1    1 
ATOM   4163 C CG2    . VAL B 2 167 ? 38.443 10.645  74.669 1.00 36.86  ?  167 VAL B CG2    1 
ATOM   4164 N N      . GLU B 2 168 ? 38.735 6.752   73.049 1.00 57.77  ?  168 GLU B N      1 
ATOM   4165 C CA     . GLU B 2 168 ? 38.140 5.534   72.524 1.00 56.15  ?  168 GLU B CA     1 
ATOM   4166 C C      . GLU B 2 168 ? 39.114 4.376   72.511 1.00 52.95  ?  168 GLU B C      1 
ATOM   4167 O O      . GLU B 2 168 ? 38.720 3.262   72.182 1.00 52.51  ?  168 GLU B O      1 
ATOM   4168 C CB     . GLU B 2 168 ? 37.688 5.793   71.098 1.00 59.44  ?  168 GLU B CB     1 
ATOM   4169 C CG     . GLU B 2 168 ? 38.738 6.501   70.262 1.00 67.86  ?  168 GLU B CG     1 
ATOM   4170 C CD     . GLU B 2 168 ? 39.110 5.711   69.031 1.00 69.29  ?  168 GLU B CD     1 
ATOM   4171 O OE1    . GLU B 2 168 ? 38.495 4.651   68.817 1.00 74.84  ?  168 GLU B OE1    1 
ATOM   4172 O OE2    . GLU B 2 168 ? 40.012 6.142   68.282 1.00 64.84  -1 168 GLU B OE2    1 
ATOM   4173 N N      . LEU B 2 169 ? 40.368 4.612   72.881 1.00 24.95  ?  169 LEU B N      1 
ATOM   4174 C CA     . LEU B 2 169 ? 41.374 3.584   72.785 1.00 26.93  ?  169 LEU B CA     1 
ATOM   4175 C C      . LEU B 2 169 ? 41.243 2.380   73.729 1.00 29.15  ?  169 LEU B C      1 
ATOM   4176 O O      . LEU B 2 169 ? 41.476 1.267   73.310 1.00 31.67  ?  169 LEU B O      1 
ATOM   4177 C CB     . LEU B 2 169 ? 42.748 4.221   72.946 1.00 27.71  ?  169 LEU B CB     1 
ATOM   4178 C CG     . LEU B 2 169 ? 43.626 4.529   71.742 1.00 34.57  ?  169 LEU B CG     1 
ATOM   4179 C CD1    . LEU B 2 169 ? 42.916 5.440   70.757 1.00 40.03  ?  169 LEU B CD1    1 
ATOM   4180 C CD2    . LEU B 2 169 ? 44.909 5.171   72.235 1.00 29.72  ?  169 LEU B CD2    1 
ATOM   4181 N N      . PRO B 2 170 ? 40.916 2.600   75.011 1.00 35.31  ?  170 PRO B N      1 
ATOM   4182 C CA     . PRO B 2 170 ? 40.705 1.448   75.894 1.00 41.16  ?  170 PRO B CA     1 
ATOM   4183 C C      . PRO B 2 170 ? 39.663 0.495   75.364 1.00 40.53  ?  170 PRO B C      1 
ATOM   4184 O O      . PRO B 2 170 ? 39.856 -0.692  75.515 1.00 48.55  ?  170 PRO B O      1 
ATOM   4185 C CB     . PRO B 2 170 ? 40.298 2.093   77.213 1.00 36.70  ?  170 PRO B CB     1 
ATOM   4186 C CG     . PRO B 2 170 ? 40.018 3.525   76.908 1.00 38.71  ?  170 PRO B CG     1 
ATOM   4187 C CD     . PRO B 2 170 ? 40.922 3.853   75.775 1.00 34.33  ?  170 PRO B CD     1 
ATOM   4188 N N      . LEU B 2 171 ? 38.592 0.990   74.775 1.00 36.06  ?  171 LEU B N      1 
ATOM   4189 C CA     . LEU B 2 171 ? 37.586 0.159   74.112 1.00 37.76  ?  171 LEU B CA     1 
ATOM   4190 C C      . LEU B 2 171 ? 38.133 -0.476  72.840 1.00 41.86  ?  171 LEU B C      1 
ATOM   4191 O O      . LEU B 2 171 ? 37.941 -1.677  72.599 1.00 45.11  ?  171 LEU B O      1 
ATOM   4192 C CB     . LEU B 2 171 ? 36.360 0.995   73.762 1.00 38.13  ?  171 LEU B CB     1 
ATOM   4193 C CG     . LEU B 2 171 ? 35.311 1.163   74.843 1.00 34.94  ?  171 LEU B CG     1 
ATOM   4194 C CD1    . LEU B 2 171 ? 34.011 1.741   74.238 1.00 23.28  ?  171 LEU B CD1    1 
ATOM   4195 C CD2    . LEU B 2 171 ? 35.100 -0.181  75.520 1.00 38.66  ?  171 LEU B CD2    1 
ATOM   4196 N N      . LYS B 2 172 ? 38.770 0.345   71.984 1.00 39.78  ?  172 LYS B N      1 
ATOM   4197 C CA     . LYS B 2 172 ? 39.317 -0.096  70.701 1.00 29.14  ?  172 LYS B CA     1 
ATOM   4198 C C      . LYS B 2 172 ? 40.255 -1.289  70.870 1.00 35.63  ?  172 LYS B C      1 
ATOM   4199 O O      . LYS B 2 172 ? 40.279 -2.205  70.041 1.00 31.76  ?  172 LYS B O      1 
ATOM   4200 C CB     . LYS B 2 172 ? 40.030 1.091   70.059 1.00 26.41  ?  172 LYS B CB     1 
ATOM   4201 C CG     . LYS B 2 172 ? 40.287 1.002   68.561 1.00 32.10  ?  172 LYS B CG     1 
ATOM   4202 C CD     . LYS B 2 172 ? 40.719 2.377   67.973 1.00 32.38  ?  172 LYS B CD     1 
ATOM   4203 C CE     . LYS B 2 172 ? 42.273 2.534   67.919 1.00 36.67  ?  172 LYS B CE     1 
ATOM   4204 N NZ     . LYS B 2 172 ? 42.717 3.917   67.544 1.00 37.96  ?  172 LYS B NZ     1 
ATOM   4205 N N      . ALA B 2 173 ? 40.987 -1.328  71.980 1.00 44.96  ?  173 ALA B N      1 
ATOM   4206 C CA     . ALA B 2 173 ? 41.946 -2.400  72.203 1.00 43.45  ?  173 ALA B CA     1 
ATOM   4207 C C      . ALA B 2 173 ? 41.274 -3.747  72.476 1.00 40.33  ?  173 ALA B C      1 
ATOM   4208 O O      . ALA B 2 173 ? 41.861 -4.793  72.177 1.00 42.54  ?  173 ALA B O      1 
ATOM   4209 C CB     . ALA B 2 173 ? 42.876 -2.008  73.354 1.00 39.62  ?  173 ALA B CB     1 
ATOM   4210 N N      . GLN B 2 174 ? 40.069 -3.761  73.056 1.00 39.76  ?  174 GLN B N      1 
ATOM   4211 C CA     . GLN B 2 174 ? 39.434 -5.052  73.349 1.00 41.68  ?  174 GLN B CA     1 
ATOM   4212 C C      . GLN B 2 174 ? 39.017 -5.810  72.092 1.00 40.57  ?  174 GLN B C      1 
ATOM   4213 O O      . GLN B 2 174 ? 38.672 -6.988  72.201 1.00 39.88  ?  174 GLN B O      1 
ATOM   4214 C CB     . GLN B 2 174 ? 38.207 -4.881  74.263 1.00 29.89  ?  174 GLN B CB     1 
ATOM   4215 C CG     . GLN B 2 174 ? 38.559 -4.699  75.734 1.00 33.39  ?  174 GLN B CG     1 
ATOM   4216 C CD     . GLN B 2 174 ? 37.590 -3.779  76.501 1.00 38.48  ?  174 GLN B CD     1 
ATOM   4217 O OE1    . GLN B 2 174 ? 36.403 -4.073  76.632 1.00 42.46  ?  174 GLN B OE1    1 
ATOM   4218 N NE2    . GLN B 2 174 ? 38.108 -2.660  77.012 1.00 41.06  ?  174 GLN B NE2    1 
ATOM   4219 N N      . SER B 2 175 ? 39.089 -5.189  70.915 1.00 39.48  ?  175 SER B N      1 
ATOM   4220 C CA     . SER B 2 175 ? 38.440 -5.725  69.724 1.00 32.98  ?  175 SER B CA     1 
ATOM   4221 C C      . SER B 2 175 ? 39.297 -6.750  68.989 1.00 35.60  ?  175 SER B C      1 
ATOM   4222 O O      . SER B 2 175 ? 40.481 -6.512  68.709 1.00 34.00  ?  175 SER B O      1 
ATOM   4223 C CB     . SER B 2 175 ? 38.097 -4.605  68.758 1.00 29.47  ?  175 SER B CB     1 
ATOM   4224 O OG     . SER B 2 175 ? 37.523 -5.188  67.619 1.00 35.06  ?  175 SER B OG     1 
ATOM   4225 N N      . GLU B 2 176 ? 38.677 -7.889  68.664 1.00 54.01  ?  176 GLU B N      1 
ATOM   4226 C CA     . GLU B 2 176 ? 39.238 -8.825  67.694 1.00 61.88  ?  176 GLU B CA     1 
ATOM   4227 C C      . GLU B 2 176 ? 39.028 -8.373  66.245 1.00 59.80  ?  176 GLU B C      1 
ATOM   4228 O O      . GLU B 2 176 ? 39.845 -8.701  65.379 1.00 58.59  ?  176 GLU B O      1 
ATOM   4229 C CB     . GLU B 2 176 ? 38.628 -10.219 67.896 1.00 68.69  ?  176 GLU B CB     1 
ATOM   4230 C CG     . GLU B 2 176 ? 39.477 -11.193 68.715 1.00 73.44  ?  176 GLU B CG     1 
ATOM   4231 C CD     . GLU B 2 176 ? 39.282 -11.037 70.214 1.00 78.95  ?  176 GLU B CD     1 
ATOM   4232 O OE1    . GLU B 2 176 ? 38.121 -11.174 70.666 1.00 79.94  ?  176 GLU B OE1    1 
ATOM   4233 O OE2    . GLU B 2 176 ? 40.280 -10.776 70.936 1.00 80.75  -1 176 GLU B OE2    1 
ATOM   4234 N N      . ARG B 2 177 ? 37.969 -7.650  65.930 1.00 55.46  ?  177 ARG B N      1 
ATOM   4235 C CA     . ARG B 2 177 ? 37.691 -7.293  64.547 1.00 52.00  ?  177 ARG B CA     1 
ATOM   4236 C C      . ARG B 2 177 ? 38.487 -6.143  64.036 1.00 50.51  ?  177 ARG B C      1 
ATOM   4237 O O      . ARG B 2 177 ? 39.071 -6.228  62.982 1.00 52.10  ?  177 ARG B O      1 
ATOM   4238 C CB     . ARG B 2 177 ? 36.212 -6.981  64.371 1.00 51.52  ?  177 ARG B CB     1 
ATOM   4239 C CG     . ARG B 2 177 ? 35.784 -6.469  63.007 1.00 55.87  ?  177 ARG B CG     1 
ATOM   4240 C CD     . ARG B 2 177 ? 34.980 -7.472  62.198 1.00 63.31  ?  177 ARG B CD     1 
ATOM   4241 N NE     . ARG B 2 177 ? 33.710 -7.824  62.827 1.00 70.26  ?  177 ARG B NE     1 
ATOM   4242 C CZ     . ARG B 2 177 ? 32.739 -8.508  62.227 1.00 67.48  ?  177 ARG B CZ     1 
ATOM   4243 N NH1    . ARG B 2 177 ? 32.876 -8.903  60.971 1.00 61.64  ?  177 ARG B NH1    1 
ATOM   4244 N NH2    . ARG B 2 177 ? 31.625 -8.793  62.882 1.00 63.70  ?  177 ARG B NH2    1 
ATOM   4245 N N      . TYR B 2 178 ? 38.525 -5.060  64.788 1.00 44.48  ?  178 TYR B N      1 
ATOM   4246 C CA     . TYR B 2 178 ? 39.207 -3.858  64.299 1.00 43.73  ?  178 TYR B CA     1 
ATOM   4247 C C      . TYR B 2 178 ? 40.629 -4.087  63.787 1.00 48.21  ?  178 TYR B C      1 
ATOM   4248 O O      . TYR B 2 178 ? 40.998 -3.445  62.783 1.00 43.29  ?  178 TYR B O      1 
ATOM   4249 C CB     . TYR B 2 178 ? 39.235 -2.769  65.388 1.00 39.74  ?  178 TYR B CB     1 
ATOM   4250 C CG     . TYR B 2 178 ? 39.278 -1.402  64.761 1.00 36.44  ?  178 TYR B CG     1 
ATOM   4251 C CD1    . TYR B 2 178 ? 38.165 -0.890  64.104 1.00 38.32  ?  178 TYR B CD1    1 
ATOM   4252 C CD2    . TYR B 2 178 ? 40.429 -0.648  64.781 1.00 33.01  ?  178 TYR B CD2    1 
ATOM   4253 C CE1    . TYR B 2 178 ? 38.211 0.340   63.496 1.00 41.20  ?  178 TYR B CE1    1 
ATOM   4254 C CE2    . TYR B 2 178 ? 40.476 0.589   64.178 1.00 34.02  ?  178 TYR B CE2    1 
ATOM   4255 C CZ     . TYR B 2 178 ? 39.375 1.070   63.526 1.00 38.01  ?  178 TYR B CZ     1 
ATOM   4256 O OH     . TYR B 2 178 ? 39.429 2.303   62.927 1.00 46.95  ?  178 TYR B OH     1 
ATOM   4257 N N      . PRO B 2 179 ? 41.473 -4.924  64.401 1.00 37.37  ?  179 PRO B N      1 
ATOM   4258 C CA     . PRO B 2 179 ? 42.838 -5.094  63.866 1.00 33.94  ?  179 PRO B CA     1 
ATOM   4259 C C      . PRO B 2 179 ? 42.876 -5.723  62.473 1.00 35.90  ?  179 PRO B C      1 
ATOM   4260 O O      . PRO B 2 179 ? 43.896 -5.601  61.785 1.00 35.71  ?  179 PRO B O      1 
ATOM   4261 C CB     . PRO B 2 179 ? 43.528 -5.977  64.920 1.00 26.72  ?  179 PRO B CB     1 
ATOM   4262 C CG     . PRO B 2 179 ? 42.712 -5.770  66.167 1.00 24.59  ?  179 PRO B CG     1 
ATOM   4263 C CD     . PRO B 2 179 ? 41.304 -5.632  65.686 1.00 28.71  ?  179 PRO B CD     1 
ATOM   4264 N N      . LYS B 2 180 ? 41.790 -6.362  62.036 1.00 46.58  ?  180 LYS B N      1 
ATOM   4265 C CA     . LYS B 2 180 ? 41.585 -6.846  60.675 1.00 44.70  ?  180 LYS B CA     1 
ATOM   4266 C C      . LYS B 2 180 ? 41.063 -5.761  59.746 1.00 39.76  ?  180 LYS B C      1 
ATOM   4267 O O      . LYS B 2 180 ? 40.580 -6.094  58.661 1.00 42.89  ?  180 LYS B O      1 
ATOM   4268 C CB     . LYS B 2 180 ? 40.632 -8.044  60.664 1.00 46.52  ?  180 LYS B CB     1 
ATOM   4269 C CG     . LYS B 2 180 ? 41.089 -9.196  61.555 1.00 50.74  ?  180 LYS B CG     1 
ATOM   4270 C CD     . LYS B 2 180 ? 40.334 -10.476 61.218 1.00 50.65  ?  180 LYS B CD     1 
ATOM   4271 C CE     . LYS B 2 180 ? 41.103 -11.710 61.662 1.00 45.92  ?  180 LYS B CE     1 
ATOM   4272 N NZ     . LYS B 2 180 ? 42.551 -11.627 61.316 1.00 40.64  ?  180 LYS B NZ     1 
ATOM   4273 N N      . LYS B 2 181 ? 41.222 -4.504  60.113 1.00 33.96  ?  181 LYS B N      1 
ATOM   4274 C CA     . LYS B 2 181 ? 40.885 -3.384  59.251 1.00 29.93  ?  181 LYS B CA     1 
ATOM   4275 C C      . LYS B 2 181 ? 41.893 -3.302  58.164 1.00 31.10  ?  181 LYS B C      1 
ATOM   4276 O O      . LYS B 2 181 ? 43.047 -3.607  58.369 1.00 41.98  ?  181 LYS B O      1 
ATOM   4277 C CB     . LYS B 2 181 ? 40.949 -2.081  60.027 1.00 20.64  ?  181 LYS B CB     1 
ATOM   4278 C CG     . LYS B 2 181 ? 39.909 -1.046  59.683 1.00 22.79  ?  181 LYS B CG     1 
ATOM   4279 C CD     . LYS B 2 181 ? 40.326 0.303   60.216 1.00 24.38  ?  181 LYS B CD     1 
ATOM   4280 C CE     . LYS B 2 181 ? 40.025 1.402   59.223 1.00 24.02  ?  181 LYS B CE     1 
ATOM   4281 N NZ     . LYS B 2 181 ? 39.769 2.697   59.903 1.00 20.86  ?  181 LYS B NZ     1 
ATOM   4282 N N      . ASP B 2 182 ? 41.479 -2.851  57.001 1.00 48.64  ?  182 ASP B N      1 
ATOM   4283 C CA     . ASP B 2 182 ? 42.358 -2.750  55.858 1.00 44.12  ?  182 ASP B CA     1 
ATOM   4284 C C      . ASP B 2 182 ? 42.194 -1.476  55.077 1.00 37.58  ?  182 ASP B C      1 
ATOM   4285 O O      . ASP B 2 182 ? 41.755 -1.480  53.956 1.00 46.31  ?  182 ASP B O      1 
ATOM   4286 C CB     . ASP B 2 182 ? 42.278 -4.001  54.979 1.00 51.60  ?  182 ASP B CB     1 
ATOM   4287 C CG     . ASP B 2 182 ? 40.861 -4.444  54.653 1.00 60.94  ?  182 ASP B CG     1 
ATOM   4288 O OD1    . ASP B 2 182 ? 40.075 -4.733  55.561 1.00 60.97  ?  182 ASP B OD1    1 
ATOM   4289 O OD2    . ASP B 2 182 ? 40.549 -4.558  53.458 1.00 64.08  -1 182 ASP B OD2    1 
ATOM   4290 N N      . ARG B 2 183 ? 42.552 -0.369  55.685 1.00 38.28  ?  183 ARG B N      1 
ATOM   4291 C CA     . ARG B 2 183 ? 42.526 0.896   54.995 1.00 36.58  ?  183 ARG B CA     1 
ATOM   4292 C C      . ARG B 2 183 ? 43.943 1.225   54.706 1.00 31.29  ?  183 ARG B C      1 
ATOM   4293 O O      . ARG B 2 183 ? 44.739 1.301   55.613 1.00 39.98  ?  183 ARG B O      1 
ATOM   4294 C CB     . ARG B 2 183 ? 41.928 1.967   55.878 1.00 37.40  ?  183 ARG B CB     1 
ATOM   4295 C CG     . ARG B 2 183 ? 42.110 3.375   55.375 1.00 38.63  ?  183 ARG B CG     1 
ATOM   4296 C CD     . ARG B 2 183 ? 41.387 4.353   56.271 1.00 32.44  ?  183 ARG B CD     1 
ATOM   4297 N NE     . ARG B 2 183 ? 41.586 5.719   55.814 1.00 39.62  ?  183 ARG B NE     1 
ATOM   4298 C CZ     . ARG B 2 183 ? 40.741 6.714   56.031 1.00 38.18  ?  183 ARG B CZ     1 
ATOM   4299 N NH1    . ARG B 2 183 ? 39.623 6.499   56.700 1.00 37.33  ?  183 ARG B NH1    1 
ATOM   4300 N NH2    . ARG B 2 183 ? 41.017 7.920   55.573 1.00 33.78  ?  183 ARG B NH2    1 
ATOM   4301 N N      . SER B 2 184 ? 44.269 1.392   53.439 1.00 25.84  ?  184 SER B N      1 
ATOM   4302 C CA     . SER B 2 184 ? 45.634 1.704   53.034 1.00 29.88  ?  184 SER B CA     1 
ATOM   4303 C C      . SER B 2 184 ? 46.088 3.021   53.648 1.00 27.60  ?  184 SER B C      1 
ATOM   4304 O O      . SER B 2 184 ? 45.324 3.990   53.743 1.00 26.56  ?  184 SER B O      1 
ATOM   4305 C CB     . SER B 2 184 ? 45.753 1.761   51.511 1.00 30.74  ?  184 SER B CB     1 
ATOM   4306 O OG     . SER B 2 184 ? 47.046 2.208   51.136 1.00 32.99  ?  184 SER B OG     1 
ATOM   4307 N N      . ARG B 2 185 ? 47.339 3.037   54.094 1.00 35.54  ?  185 ARG B N      1 
ATOM   4308 C CA     . ARG B 2 185 ? 47.882 4.229   54.722 1.00 42.00  ?  185 ARG B CA     1 
ATOM   4309 C C      . ARG B 2 185 ? 48.289 5.271   53.690 1.00 40.86  ?  185 ARG B C      1 
ATOM   4310 O O      . ARG B 2 185 ? 48.640 6.396   54.064 1.00 42.82  ?  185 ARG B O      1 
ATOM   4311 C CB     . ARG B 2 185 ? 49.061 3.842   55.619 1.00 43.46  ?  185 ARG B CB     1 
ATOM   4312 C CG     . ARG B 2 185 ? 48.688 3.079   56.873 1.00 48.56  ?  185 ARG B CG     1 
ATOM   4313 C CD     . ARG B 2 185 ? 49.864 2.258   57.420 1.00 53.04  ?  185 ARG B CD     1 
ATOM   4314 N NE     . ARG B 2 185 ? 49.829 2.176   58.877 1.00 49.54  ?  185 ARG B NE     1 
ATOM   4315 C CZ     . ARG B 2 185 ? 50.774 2.652   59.678 1.00 41.31  ?  185 ARG B CZ     1 
ATOM   4316 N NH1    . ARG B 2 185 ? 51.854 3.232   59.168 1.00 43.18  ?  185 ARG B NH1    1 
ATOM   4317 N NH2    . ARG B 2 185 ? 50.639 2.532   60.994 1.00 39.89  ?  185 ARG B NH2    1 
ATOM   4318 N N      . GLU B 2 186 ? 48.234 4.921   52.409 1.00 47.93  ?  186 GLU B N      1 
ATOM   4319 C CA     . GLU B 2 186 ? 48.440 5.886   51.344 1.00 42.22  ?  186 GLU B CA     1 
ATOM   4320 C C      . GLU B 2 186 ? 47.576 7.109   51.582 1.00 44.90  ?  186 GLU B C      1 
ATOM   4321 O O      . GLU B 2 186 ? 46.366 6.992   51.805 1.00 48.75  ?  186 GLU B O      1 
ATOM   4322 C CB     . GLU B 2 186 ? 48.051 5.268   49.997 1.00 38.84  ?  186 GLU B CB     1 
ATOM   4323 C CG     . GLU B 2 186 ? 49.073 4.400   49.314 1.00 51.10  ?  186 GLU B CG     1 
ATOM   4324 C CD     . GLU B 2 186 ? 48.719 4.184   47.831 1.00 65.30  ?  186 GLU B CD     1 
ATOM   4325 O OE1    . GLU B 2 186 ? 48.998 5.099   47.019 1.00 72.05  ?  186 GLU B OE1    1 
ATOM   4326 O OE2    . GLU B 2 186 ? 48.144 3.120   47.480 1.00 61.85  -1 186 GLU B OE2    1 
ATOM   4327 N N      . GLU B 2 187 ? 48.179 8.286   51.460 1.00 49.03  ?  187 GLU B N      1 
ATOM   4328 C CA     . GLU B 2 187 ? 47.406 9.511   51.312 1.00 58.76  ?  187 GLU B CA     1 
ATOM   4329 C C      . GLU B 2 187 ? 47.105 9.676   49.819 1.00 62.65  ?  187 GLU B C      1 
ATOM   4330 O O      . GLU B 2 187 ? 48.018 9.872   49.009 1.00 58.51  ?  187 GLU B O      1 
ATOM   4331 C CB     . GLU B 2 187 ? 48.169 10.711  51.873 1.00 60.69  ?  187 GLU B CB     1 
ATOM   4332 C CG     . GLU B 2 187 ? 47.289 11.936  52.013 1.00 65.28  ?  187 GLU B CG     1 
ATOM   4333 C CD     . GLU B 2 187 ? 45.837 11.558  52.298 1.00 72.11  ?  187 GLU B CD     1 
ATOM   4334 O OE1    . GLU B 2 187 ? 45.578 10.968  53.373 1.00 79.37  ?  187 GLU B OE1    1 
ATOM   4335 O OE2    . GLU B 2 187 ? 44.958 11.826  51.447 1.00 67.07  -1 187 GLU B OE2    1 
ATOM   4336 N N      . LEU B 2 188 ? 45.826 9.521   49.448 1.00 57.27  ?  188 LEU B N      1 
ATOM   4337 C CA     . LEU B 2 188 ? 45.374 9.726   48.078 1.00 45.63  ?  188 LEU B CA     1 
ATOM   4338 C C      . LEU B 2 188 ? 44.657 11.058  47.839 1.00 48.79  ?  188 LEU B C      1 
ATOM   4339 O O      . LEU B 2 188 ? 44.357 11.380  46.684 1.00 51.21  ?  188 LEU B O      1 
ATOM   4340 C CB     . LEU B 2 188 ? 44.469 8.567   47.674 1.00 47.28  ?  188 LEU B CB     1 
ATOM   4341 C CG     . LEU B 2 188 ? 45.215 7.242   47.797 1.00 54.78  ?  188 LEU B CG     1 
ATOM   4342 C CD1    . LEU B 2 188 ? 44.402 6.091   47.195 1.00 57.86  ?  188 LEU B CD1    1 
ATOM   4343 C CD2    . LEU B 2 188 ? 46.586 7.358   47.130 1.00 52.78  ?  188 LEU B CD2    1 
ATOM   4344 N N      . GLY B 2 189 ? 44.389 11.844  48.888 1.00 44.29  ?  189 GLY B N      1 
ATOM   4345 C CA     . GLY B 2 189 ? 43.703 13.126  48.756 1.00 37.14  ?  189 GLY B CA     1 
ATOM   4346 C C      . GLY B 2 189 ? 42.211 13.003  48.468 1.00 34.52  ?  189 GLY B C      1 
ATOM   4347 O O      . GLY B 2 189 ? 41.542 12.027  48.829 1.00 29.07  ?  189 GLY B O      1 
ATOM   4348 N N      . ASN B 2 190 ? 41.747 14.070  47.850 1.00 44.34  ?  190 ASN B N      1 
ATOM   4349 C CA     . ASN B 2 190 ? 40.370 14.166  47.552 1.00 45.02  ?  190 ASN B CA     1 
ATOM   4350 C C      . ASN B 2 190 ? 40.167 14.298  46.081 1.00 44.64  ?  190 ASN B C      1 
ATOM   4351 O O      . ASN B 2 190 ? 40.905 14.983  45.412 1.00 43.74  ?  190 ASN B O      1 
ATOM   4352 C CB     . ASN B 2 190 ? 39.810 15.408  48.249 1.00 48.31  ?  190 ASN B CB     1 
ATOM   4353 C CG     . ASN B 2 190 ? 40.331 15.583  49.645 1.00 51.92  ?  190 ASN B CG     1 
ATOM   4354 O OD1    . ASN B 2 190 ? 39.951 14.860  50.557 1.00 53.13  ?  190 ASN B OD1    1 
ATOM   4355 N ND2    . ASN B 2 190 ? 41.197 16.563  49.825 1.00 57.29  ?  190 ASN B ND2    1 
ATOM   4356 N N      . THR B 2 191 ? 39.168 13.615  45.562 1.00 43.27  ?  191 THR B N      1 
ATOM   4357 C CA     . THR B 2 191 ? 38.821 13.714  44.166 1.00 42.89  ?  191 THR B CA     1 
ATOM   4358 C C      . THR B 2 191 ? 37.430 14.350  44.106 1.00 42.25  ?  191 THR B C      1 
ATOM   4359 O O      . THR B 2 191 ? 36.662 14.244  45.028 1.00 37.68  ?  191 THR B O      1 
ATOM   4360 C CB     . THR B 2 191 ? 38.905 12.332  43.477 1.00 47.76  ?  191 THR B CB     1 
ATOM   4361 O OG1    . THR B 2 191 ? 38.867 12.483  42.056 1.00 50.75  ?  191 THR B OG1    1 
ATOM   4362 C CG2    . THR B 2 191 ? 37.794 11.418  43.913 1.00 54.08  ?  191 THR B CG2    1 
ATOM   4363 N N      . PRO B 2 192 ? 37.125 15.072  43.027 1.00 48.79  ?  192 PRO B N      1 
ATOM   4364 C CA     . PRO B 2 192 ? 35.773 15.610  42.920 1.00 45.41  ?  192 PRO B CA     1 
ATOM   4365 C C      . PRO B 2 192 ? 34.653 14.590  42.670 1.00 42.39  ?  192 PRO B C      1 
ATOM   4366 O O      . PRO B 2 192 ? 34.892 13.602  41.999 1.00 40.21  ?  192 PRO B O      1 
ATOM   4367 C CB     . PRO B 2 192 ? 35.907 16.639  41.793 1.00 39.44  ?  192 PRO B CB     1 
ATOM   4368 C CG     . PRO B 2 192 ? 37.337 17.000  41.767 1.00 33.15  ?  192 PRO B CG     1 
ATOM   4369 C CD     . PRO B 2 192 ? 38.047 15.729  42.087 1.00 39.10  ?  192 PRO B CD     1 
ATOM   4370 N N      . SER B 2 193 ? 33.462 14.846  43.195 1.00 28.65  ?  193 SER B N      1 
ATOM   4371 C CA     . SER B 2 193 ? 32.311 13.955  43.016 1.00 28.09  ?  193 SER B CA     1 
ATOM   4372 C C      . SER B 2 193 ? 30.969 14.639  43.039 1.00 25.41  ?  193 SER B C      1 
ATOM   4373 O O      . SER B 2 193 ? 30.786 15.594  43.745 1.00 31.83  ?  193 SER B O      1 
ATOM   4374 C CB     . SER B 2 193 ? 32.284 12.894  44.102 1.00 31.46  ?  193 SER B CB     1 
ATOM   4375 O OG     . SER B 2 193 ? 31.109 12.116  44.076 1.00 36.47  ?  193 SER B OG     1 
ATOM   4376 N N      . ALA B 2 194 ? 30.023 14.140  42.277 1.00 26.58  ?  194 ALA B N      1 
ATOM   4377 C CA     . ALA B 2 194 ? 28.671 14.654  42.284 1.00 29.32  ?  194 ALA B CA     1 
ATOM   4378 C C      . ALA B 2 194 ? 27.736 13.575  42.742 1.00 28.09  ?  194 ALA B C      1 
ATOM   4379 O O      . ALA B 2 194 ? 26.535 13.728  42.704 1.00 28.23  ?  194 ALA B O      1 
ATOM   4380 C CB     . ALA B 2 194 ? 28.284 15.084  40.907 1.00 30.83  ?  194 ALA B CB     1 
ATOM   4381 N N      . ASN B 2 195 ? 28.296 12.453  43.124 1.00 31.63  ?  195 ASN B N      1 
ATOM   4382 C CA     . ASN B 2 195 ? 27.489 11.361  43.592 1.00 35.29  ?  195 ASN B CA     1 
ATOM   4383 C C      . ASN B 2 195 ? 27.350 11.357  45.101 1.00 32.21  ?  195 ASN B C      1 
ATOM   4384 O O      . ASN B 2 195 ? 28.249 11.727  45.816 1.00 31.77  ?  195 ASN B O      1 
ATOM   4385 C CB     . ASN B 2 195 ? 28.021 10.044  43.051 1.00 35.60  ?  195 ASN B CB     1 
ATOM   4386 C CG     . ASN B 2 195 ? 27.647 9.821   41.631 1.00 34.25  ?  195 ASN B CG     1 
ATOM   4387 O OD1    . ASN B 2 195 ? 26.679 10.376  41.149 1.00 32.73  ?  195 ASN B OD1    1 
ATOM   4388 N ND2    . ASN B 2 195 ? 28.425 9.021   40.943 1.00 30.69  ?  195 ASN B ND2    1 
ATOM   4389 N N      . PRO B 2 196 ? 26.186 10.962  45.570 1.00 34.56  ?  196 PRO B N      1 
ATOM   4390 C CA     . PRO B 2 196 ? 25.940 10.929  46.999 1.00 33.16  ?  196 PRO B CA     1 
ATOM   4391 C C      . PRO B 2 196 ? 26.297 9.676   47.760 1.00 29.12  ?  196 PRO B C      1 
ATOM   4392 O O      . PRO B 2 196 ? 26.414 8.614   47.211 1.00 32.49  ?  196 PRO B O      1 
ATOM   4393 C CB     . PRO B 2 196 ? 24.443 11.087  47.058 1.00 29.94  ?  196 PRO B CB     1 
ATOM   4394 C CG     . PRO B 2 196 ? 23.952 10.407  45.841 1.00 31.51  ?  196 PRO B CG     1 
ATOM   4395 C CD     . PRO B 2 196 ? 24.953 10.779  44.798 1.00 31.19  ?  196 PRO B CD     1 
ATOM   4396 N N      . GLY B 2 197 ? 26.477 9.824   49.049 1.00 31.87  ?  197 GLY B N      1 
ATOM   4397 C CA     . GLY B 2 197 ? 26.730 8.695   49.899 1.00 33.34  ?  197 GLY B CA     1 
ATOM   4398 C C      . GLY B 2 197 ? 27.933 7.844   49.757 1.00 33.55  ?  197 GLY B C      1 
ATOM   4399 O O      . GLY B 2 197 ? 29.039 8.334   49.661 1.00 29.51  ?  197 GLY B O      1 
ATOM   4400 N N      . ILE B 2 198 ? 27.705 6.541   49.755 1.00 34.85  ?  198 ILE B N      1 
ATOM   4401 C CA     . ILE B 2 198 ? 28.838 5.669   49.531 1.00 33.93  ?  198 ILE B CA     1 
ATOM   4402 C C      . ILE B 2 198 ? 28.983 5.276   48.063 1.00 30.91  ?  198 ILE B C      1 
ATOM   4403 O O      . ILE B 2 198 ? 29.666 4.290   47.764 1.00 30.09  ?  198 ILE B O      1 
ATOM   4404 C CB     . ILE B 2 198 ? 28.781 4.444   50.448 1.00 33.32  ?  198 ILE B CB     1 
ATOM   4405 C CG1    . ILE B 2 198 ? 27.540 3.613   50.154 1.00 25.88  ?  198 ILE B CG1    1 
ATOM   4406 C CG2    . ILE B 2 198 ? 28.853 4.888   51.892 1.00 32.68  ?  198 ILE B CG2    1 
ATOM   4407 C CD1    . ILE B 2 198 ? 27.791 2.163   50.439 1.00 27.34  ?  198 ILE B CD1    1 
ATOM   4408 N N      . MET B 2 199 ? 28.260 5.945   47.158 1.00 27.51  ?  199 MET B N      1 
ATOM   4409 C CA     . MET B 2 199 ? 28.459 5.766   45.717 1.00 28.77  ?  199 MET B CA     1 
ATOM   4410 C C      . MET B 2 199 ? 29.832 6.267   45.308 1.00 26.10  ?  199 MET B C      1 
ATOM   4411 O O      . MET B 2 199 ? 30.378 7.195   45.903 1.00 30.39  ?  199 MET B O      1 
ATOM   4412 C CB     . MET B 2 199 ? 27.410 6.530   44.902 1.00 26.66  ?  199 MET B CB     1 
ATOM   4413 C CG     . MET B 2 199 ? 25.982 6.062   45.100 1.00 30.57  ?  199 MET B CG     1 
ATOM   4414 S SD     . MET B 2 199 ? 24.879 6.944   43.971 1.00 27.19  ?  199 MET B SD     1 
ATOM   4415 C CE     . MET B 2 199 ? 25.245 6.119   42.402 1.00 26.45  ?  199 MET B CE     1 
ATOM   4416 N N      . LYS B 2 200 ? 30.365 5.683   44.323 1.00 21.32  ?  200 LYS B N      1 
ATOM   4417 C CA     . LYS B 2 200 ? 31.691 6.206   43.988 1.00 24.87  ?  200 LYS B CA     1 
ATOM   4418 C C      . LYS B 2 200 ? 31.577 7.380   43.014 1.00 32.30  ?  200 LYS B C      1 
ATOM   4419 O O      . LYS B 2 200 ? 30.623 7.446   42.219 1.00 31.14  ?  200 LYS B O      1 
ATOM   4420 C CB     . LYS B 2 200 ? 32.570 5.109   43.362 1.00 23.50  ?  200 LYS B CB     1 
ATOM   4421 C CG     . LYS B 2 200 ? 32.904 3.941   44.275 1.00 25.84  ?  200 LYS B CG     1 
ATOM   4422 C CD     . LYS B 2 200 ? 32.763 2.606   43.543 1.00 24.67  ?  200 LYS B CD     1 
ATOM   4423 C CE     . LYS B 2 200 ? 33.970 2.320   42.646 1.00 25.65  ?  200 LYS B CE     1 
ATOM   4424 N NZ     . LYS B 2 200 ? 33.719 1.146   41.765 1.00 24.15  ?  200 LYS B NZ     1 
ATOM   4425 N N      . PRO B 2 201 ? 32.562 8.295   43.048 1.00 34.42  ?  201 PRO B N      1 
ATOM   4426 C CA     . PRO B 2 201 ? 32.489 9.501   42.194 1.00 34.79  ?  201 PRO B CA     1 
ATOM   4427 C C      . PRO B 2 201 ? 32.277 9.219   40.706 1.00 37.88  ?  201 PRO B C      1 
ATOM   4428 O O      . PRO B 2 201 ? 31.430 9.864   40.072 1.00 42.90  ?  201 PRO B O      1 
ATOM   4429 C CB     . PRO B 2 201 ? 33.837 10.189  42.449 1.00 32.97  ?  201 PRO B CB     1 
ATOM   4430 C CG     . PRO B 2 201 ? 34.360 9.588   43.722 1.00 26.93  ?  201 PRO B CG     1 
ATOM   4431 C CD     . PRO B 2 201 ? 33.818 8.221   43.812 1.00 26.30  ?  201 PRO B CD     1 
ATOM   4432 N N      . ASN B 2 202 ? 33.001 8.263   40.133 1.00 37.98  ?  202 ASN B N      1 
ATOM   4433 C CA     . ASN B 2 202 ? 32.930 7.991   38.702 1.00 34.75  ?  202 ASN B CA     1 
ATOM   4434 C C      . ASN B 2 202 ? 31.834 6.963   38.343 1.00 31.16  ?  202 ASN B C      1 
ATOM   4435 O O      . ASN B 2 202 ? 31.740 6.540   37.188 1.00 32.55  ?  202 ASN B O      1 
ATOM   4436 C CB     . ASN B 2 202 ? 34.320 7.558   38.178 1.00 31.05  ?  202 ASN B CB     1 
ATOM   4437 C CG     . ASN B 2 202 ? 35.467 8.606   38.465 1.00 34.33  ?  202 ASN B CG     1 
ATOM   4438 O OD1    . ASN B 2 202 ? 35.251 9.819   38.611 1.00 30.82  ?  202 ASN B OD1    1 
ATOM   4439 N ND2    . ASN B 2 202 ? 36.697 8.108   38.504 1.00 38.60  ?  202 ASN B ND2    1 
ATOM   4440 N N      . SER B 2 203 ? 31.006 6.574   39.285 1.00 34.42  ?  203 SER B N      1 
ATOM   4441 C CA     . SER B 2 203 ? 29.957 5.631   38.995 1.00 31.91  ?  203 SER B CA     1 
ATOM   4442 C C      . SER B 2 203 ? 28.718 6.304   38.461 1.00 33.71  ?  203 SER B C      1 
ATOM   4443 O O      . SER B 2 203 ? 28.392 7.407   38.828 1.00 33.63  ?  203 SER B O      1 
ATOM   4444 C CB     . SER B 2 203 ? 29.658 4.763   40.199 1.00 32.42  ?  203 SER B CB     1 
ATOM   4445 O OG     . SER B 2 203 ? 30.636 3.763   40.360 1.00 30.24  ?  203 SER B OG     1 
ATOM   4446 N N      . PRO B 2 204 ? 28.037 5.643   37.538 1.00 40.83  ?  204 PRO B N      1 
ATOM   4447 C CA     . PRO B 2 204 ? 26.800 6.188   36.988 1.00 41.27  ?  204 PRO B CA     1 
ATOM   4448 C C      . PRO B 2 204 ? 25.714 6.451   38.016 1.00 42.50  ?  204 PRO B C      1 
ATOM   4449 O O      . PRO B 2 204 ? 25.698 5.834   39.055 1.00 43.32  ?  204 PRO B O      1 
ATOM   4450 C CB     . PRO B 2 204 ? 26.359 5.104   36.018 1.00 36.48  ?  204 PRO B CB     1 
ATOM   4451 C CG     . PRO B 2 204 ? 27.314 3.972   36.158 1.00 34.90  ?  204 PRO B CG     1 
ATOM   4452 C CD     . PRO B 2 204 ? 28.553 4.532   36.735 1.00 32.41  ?  204 PRO B CD     1 
ATOM   4453 N N      . ASN B 2 205 ? 24.793 7.333   37.714 1.00 41.86  ?  205 ASN B N      1 
ATOM   4454 C CA     . ASN B 2 205 ? 23.756 7.667   38.668 1.00 43.34  ?  205 ASN B CA     1 
ATOM   4455 C C      . ASN B 2 205 ? 22.536 8.284   38.024 1.00 44.63  ?  205 ASN B C      1 
ATOM   4456 O O      . ASN B 2 205 ? 22.614 8.768   36.904 1.00 39.61  ?  205 ASN B O      1 
ATOM   4457 C CB     . ASN B 2 205 ? 24.318 8.666   39.684 1.00 42.29  ?  205 ASN B CB     1 
ATOM   4458 C CG     . ASN B 2 205 ? 23.477 8.812   40.932 1.00 41.53  ?  205 ASN B CG     1 
ATOM   4459 O OD1    . ASN B 2 205 ? 22.629 7.986   41.232 1.00 53.82  ?  205 ASN B OD1    1 
ATOM   4460 N ND2    . ASN B 2 205 ? 23.726 9.871   41.672 1.00 34.69  ?  205 ASN B ND2    1 
ATOM   4461 N N      . PHE B 2 206 ? 21.414 8.258   38.722 1.00 34.74  ?  206 PHE B N      1 
ATOM   4462 C CA     . PHE B 2 206 ? 20.214 8.944   38.268 1.00 34.25  ?  206 PHE B CA     1 
ATOM   4463 C C      . PHE B 2 206 ? 20.398 10.458  38.362 1.00 37.44  ?  206 PHE B C      1 
ATOM   4464 O O      . PHE B 2 206 ? 21.188 10.975  39.166 1.00 35.48  ?  206 PHE B O      1 
ATOM   4465 C CB     . PHE B 2 206 ? 18.990 8.522   39.089 1.00 28.33  ?  206 PHE B CB     1 
ATOM   4466 C CG     . PHE B 2 206 ? 18.748 7.039   39.109 1.00 28.72  ?  206 PHE B CG     1 
ATOM   4467 C CD1    . PHE B 2 206 ? 18.771 6.296   37.949 1.00 29.24  ?  206 PHE B CD1    1 
ATOM   4468 C CD2    . PHE B 2 206 ? 18.510 6.383   40.306 1.00 31.70  ?  206 PHE B CD2    1 
ATOM   4469 C CE1    . PHE B 2 206 ? 18.544 4.918   37.982 1.00 32.25  ?  206 PHE B CE1    1 
ATOM   4470 C CE2    . PHE B 2 206 ? 18.286 5.015   40.339 1.00 34.79  ?  206 PHE B CE2    1 
ATOM   4471 C CZ     . PHE B 2 206 ? 18.303 4.279   39.176 1.00 25.89  ?  206 PHE B CZ     1 
ATOM   4472 N N      . THR B 2 207 ? 19.667 11.175  37.512 1.00 46.05  ?  207 THR B N      1 
ATOM   4473 C CA     . THR B 2 207 ? 19.797 12.624  37.479 1.00 50.88  ?  207 THR B CA     1 
ATOM   4474 C C      . THR B 2 207 ? 19.028 13.303  38.605 1.00 52.16  ?  207 THR B C      1 
ATOM   4475 O O      . THR B 2 207 ? 19.395 14.410  39.022 1.00 53.31  ?  207 THR B O      1 
ATOM   4476 C CB     . THR B 2 207 ? 19.326 13.158  36.136 1.00 47.84  ?  207 THR B CB     1 
ATOM   4477 O OG1    . THR B 2 207 ? 19.931 12.384  35.103 1.00 42.41  ?  207 THR B OG1    1 
ATOM   4478 C CG2    . THR B 2 207 ? 19.727 14.623  35.990 1.00 50.29  ?  207 THR B CG2    1 
ATOM   4479 N N      . ASP B 2 208 ? 17.950 12.683  39.091 1.00 52.11  ?  208 ASP B N      1 
ATOM   4480 C CA     . ASP B 2 208 ? 17.330 13.195  40.305 1.00 51.92  ?  208 ASP B CA     1 
ATOM   4481 C C      . ASP B 2 208 ? 18.259 13.034  41.505 1.00 46.02  ?  208 ASP B C      1 
ATOM   4482 O O      . ASP B 2 208 ? 18.095 13.746  42.495 1.00 56.69  ?  208 ASP B O      1 
ATOM   4483 C CB     . ASP B 2 208 ? 15.972 12.516  40.551 1.00 56.69  ?  208 ASP B CB     1 
ATOM   4484 C CG     . ASP B 2 208 ? 15.957 11.025  40.186 1.00 64.12  ?  208 ASP B CG     1 
ATOM   4485 O OD1    . ASP B 2 208 ? 17.020 10.453  39.883 1.00 69.12  ?  208 ASP B OD1    1 
ATOM   4486 O OD2    . ASP B 2 208 ? 14.867 10.412  40.218 1.00 66.62  -1 208 ASP B OD2    1 
ATOM   4487 N N      . ASN B 2 209 ? 19.264 12.164  41.393 1.00 23.53  ?  209 ASN B N      1 
ATOM   4488 C CA     . ASN B 2 209 ? 20.109 11.688  42.479 1.00 30.99  ?  209 ASN B CA     1 
ATOM   4489 C C      . ASN B 2 209 ? 21.481 12.349  42.567 1.00 33.05  ?  209 ASN B C      1 
ATOM   4490 O O      . ASN B 2 209 ? 22.295 11.924  43.393 1.00 36.61  ?  209 ASN B O      1 
ATOM   4491 C CB     . ASN B 2 209 ? 20.289 10.169  42.365 1.00 34.07  ?  209 ASN B CB     1 
ATOM   4492 C CG     . ASN B 2 209 ? 20.074 9.460   43.683 1.00 35.87  ?  209 ASN B CG     1 
ATOM   4493 O OD1    . ASN B 2 209 ? 19.122 9.758   44.422 1.00 37.57  ?  209 ASN B OD1    1 
ATOM   4494 N ND2    . ASN B 2 209 ? 20.957 8.512   43.987 1.00 31.89  ?  209 ASN B ND2    1 
ATOM   4495 N N      . LEU B 2 210 ? 21.752 13.350  41.772 1.00 36.69  ?  210 LEU B N      1 
ATOM   4496 C CA     . LEU B 2 210 ? 23.005 14.056  41.887 1.00 31.40  ?  210 LEU B CA     1 
ATOM   4497 C C      . LEU B 2 210 ? 22.986 15.005  43.062 1.00 28.09  ?  210 LEU B C      1 
ATOM   4498 O O      . LEU B 2 210 ? 21.946 15.311  43.591 1.00 30.82  ?  210 LEU B O      1 
ATOM   4499 C CB     . LEU B 2 210 ? 23.357 14.740  40.582 1.00 21.28  ?  210 LEU B CB     1 
ATOM   4500 C CG     . LEU B 2 210 ? 23.486 13.886  39.337 1.00 28.48  ?  210 LEU B CG     1 
ATOM   4501 C CD1    . LEU B 2 210 ? 23.889 14.777  38.180 1.00 34.77  ?  210 LEU B CD1    1 
ATOM   4502 C CD2    . LEU B 2 210 ? 24.524 12.808  39.562 1.00 32.04  ?  210 LEU B CD2    1 
ATOM   4503 N N      . VAL B 2 211 ? 24.152 15.435  43.493 1.00 21.55  ?  211 VAL B N      1 
ATOM   4504 C CA     . VAL B 2 211 ? 24.278 16.322  44.628 1.00 20.96  ?  211 VAL B CA     1 
ATOM   4505 C C      . VAL B 2 211 ? 25.227 17.391  44.194 1.00 21.72  ?  211 VAL B C      1 
ATOM   4506 O O      . VAL B 2 211 ? 25.936 17.239  43.222 1.00 23.55  ?  211 VAL B O      1 
ATOM   4507 C CB     . VAL B 2 211 ? 24.817 15.618  45.911 1.00 18.78  ?  211 VAL B CB     1 
ATOM   4508 C CG1    . VAL B 2 211 ? 23.781 14.718  46.547 1.00 20.86  ?  211 VAL B CG1    1 
ATOM   4509 C CG2    . VAL B 2 211 ? 26.153 14.940  45.715 1.00 18.63  ?  211 VAL B CG2    1 
ATOM   4510 N N      . PRO B 2 212 ? 25.228 18.498  44.905 1.00 29.20  ?  212 PRO B N      1 
ATOM   4511 C CA     . PRO B 2 212 ? 26.207 19.507  44.576 1.00 33.46  ?  212 PRO B CA     1 
ATOM   4512 C C      . PRO B 2 212 ? 27.674 19.029  44.600 1.00 37.46  ?  212 PRO B C      1 
ATOM   4513 O O      . PRO B 2 212 ? 28.102 18.479  45.600 1.00 39.93  ?  212 PRO B O      1 
ATOM   4514 C CB     . PRO B 2 212 ? 25.922 20.557  45.621 1.00 26.56  ?  212 PRO B CB     1 
ATOM   4515 C CG     . PRO B 2 212 ? 24.462 20.498  45.797 1.00 26.91  ?  212 PRO B CG     1 
ATOM   4516 C CD     . PRO B 2 212 ? 24.169 19.037  45.775 1.00 26.91  ?  212 PRO B CD     1 
ATOM   4517 N N      . VAL B 2 213 ? 28.432 19.275  43.538 1.00 35.19  ?  213 VAL B N      1 
ATOM   4518 C CA     . VAL B 2 213 ? 29.812 18.804  43.424 1.00 43.39  ?  213 VAL B CA     1 
ATOM   4519 C C      . VAL B 2 213 ? 30.763 19.225  44.519 1.00 45.42  ?  213 VAL B C      1 
ATOM   4520 O O      . VAL B 2 213 ? 30.916 20.408  44.804 1.00 43.64  ?  213 VAL B O      1 
ATOM   4521 C CB     . VAL B 2 213 ? 30.405 19.183  42.054 1.00 43.57  ?  213 VAL B CB     1 
ATOM   4522 C CG1    . VAL B 2 213 ? 31.848 18.719  41.913 1.00 37.24  ?  213 VAL B CG1    1 
ATOM   4523 C CG2    . VAL B 2 213 ? 29.557 18.626  40.929 1.00 44.70  ?  213 VAL B CG2    1 
ATOM   4524 N N      . ARG B 2 214 ? 31.427 18.252  45.112 1.00 43.67  ?  214 ARG B N      1 
ATOM   4525 C CA     . ARG B 2 214 ? 32.325 18.539  46.197 1.00 44.05  ?  214 ARG B CA     1 
ATOM   4526 C C      . ARG B 2 214 ? 33.501 17.603  46.193 1.00 41.19  ?  214 ARG B C      1 
ATOM   4527 O O      . ARG B 2 214 ? 33.545 16.651  45.452 1.00 37.53  ?  214 ARG B O      1 
ATOM   4528 C CB     . ARG B 2 214 ? 31.583 18.412  47.526 1.00 42.04  ?  214 ARG B CB     1 
ATOM   4529 C CG     . ARG B 2 214 ? 31.350 16.990  48.008 1.00 38.65  ?  214 ARG B CG     1 
ATOM   4530 C CD     . ARG B 2 214 ? 29.956 16.533  47.668 1.00 35.49  ?  214 ARG B CD     1 
ATOM   4531 N NE     . ARG B 2 214 ? 29.622 15.264  48.285 1.00 41.37  ?  214 ARG B NE     1 
ATOM   4532 C CZ     . ARG B 2 214 ? 29.490 14.139  47.608 1.00 41.85  ?  214 ARG B CZ     1 
ATOM   4533 N NH1    . ARG B 2 214 ? 29.682 14.140  46.302 1.00 45.61  ?  214 ARG B NH1    1 
ATOM   4534 N NH2    . ARG B 2 214 ? 29.177 13.019  48.235 1.00 40.69  ?  214 ARG B NH2    1 
ATOM   4535 N N      . ASP B 2 215 ? 34.450 17.880  47.050 1.00 50.46  ?  215 ASP B N      1 
ATOM   4536 C CA     . ASP B 2 215 ? 35.594 17.028  47.136 1.00 46.99  ?  215 ASP B CA     1 
ATOM   4537 C C      . ASP B 2 215 ? 35.358 15.859  48.045 1.00 39.51  ?  215 ASP B C      1 
ATOM   4538 O O      . ASP B 2 215 ? 34.819 15.986  49.125 1.00 43.89  ?  215 ASP B O      1 
ATOM   4539 C CB     . ASP B 2 215 ? 36.836 17.832  47.514 1.00 51.10  ?  215 ASP B CB     1 
ATOM   4540 C CG     . ASP B 2 215 ? 37.570 18.365  46.304 1.00 51.28  ?  215 ASP B CG     1 
ATOM   4541 O OD1    . ASP B 2 215 ? 37.294 17.900  45.189 1.00 47.85  ?  215 ASP B OD1    1 
ATOM   4542 O OD2    . ASP B 2 215 ? 38.422 19.255  46.464 1.00 55.42  -1 215 ASP B OD2    1 
ATOM   4543 N N      . VAL B 2 216 ? 35.716 14.703  47.563 1.00 34.24  ?  216 VAL B N      1 
ATOM   4544 C CA     . VAL B 2 216 ? 35.526 13.525  48.328 1.00 40.59  ?  216 VAL B CA     1 
ATOM   4545 C C      . VAL B 2 216 ? 36.836 12.745  48.572 1.00 43.22  ?  216 VAL B C      1 
ATOM   4546 O O      . VAL B 2 216 ? 37.644 12.652  47.684 1.00 47.72  ?  216 VAL B O      1 
ATOM   4547 C CB     . VAL B 2 216 ? 34.426 12.555  47.830 1.00 42.43  ?  216 VAL B CB     1 
ATOM   4548 C CG1    . VAL B 2 216 ? 33.067 13.215  47.765 1.00 33.75  ?  216 VAL B CG1    1 
ATOM   4549 C CG2    . VAL B 2 216 ? 34.804 11.844  46.551 1.00 38.73  ?  216 VAL B CG2    1 
ATOM   4550 N N      . PRO B 2 217 ? 37.036 12.165  49.774 1.00 33.97  ?  217 PRO B N      1 
ATOM   4551 C CA     . PRO B 2 217 ? 38.304 11.491  49.993 1.00 31.76  ?  217 PRO B CA     1 
ATOM   4552 C C      . PRO B 2 217 ? 38.519 10.180  49.279 1.00 35.14  ?  217 PRO B C      1 
ATOM   4553 O O      . PRO B 2 217 ? 37.593 9.415   49.118 1.00 43.85  ?  217 PRO B O      1 
ATOM   4554 C CB     . PRO B 2 217 ? 38.294 11.248  51.491 1.00 32.80  ?  217 PRO B CB     1 
ATOM   4555 C CG     . PRO B 2 217 ? 37.296 12.194  52.058 1.00 29.24  ?  217 PRO B CG     1 
ATOM   4556 C CD     . PRO B 2 217 ? 36.250 12.287  51.007 1.00 30.73  ?  217 PRO B CD     1 
ATOM   4557 N N      . LYS B 2 218 ? 39.740 9.922   48.855 1.00 34.16  ?  218 LYS B N      1 
ATOM   4558 C CA     . LYS B 2 218 ? 40.080 8.649   48.230 1.00 32.05  ?  218 LYS B CA     1 
ATOM   4559 C C      . LYS B 2 218 ? 40.793 7.767   49.255 1.00 32.31  ?  218 LYS B C      1 
ATOM   4560 O O      . LYS B 2 218 ? 41.852 8.137   49.778 1.00 32.63  ?  218 LYS B O      1 
ATOM   4561 C CB     . LYS B 2 218 ? 40.965 8.864   47.001 1.00 34.85  ?  218 LYS B CB     1 
ATOM   4562 C CG     . LYS B 2 218 ? 40.210 9.046   45.682 1.00 33.76  ?  218 LYS B CG     1 
ATOM   4563 C CD     . LYS B 2 218 ? 40.874 8.218   44.576 1.00 29.90  ?  218 LYS B CD     1 
ATOM   4564 C CE     . LYS B 2 218 ? 42.180 8.842   44.119 1.00 25.05  ?  218 LYS B CE     1 
ATOM   4565 N NZ     . LYS B 2 218 ? 42.016 10.186  43.506 1.00 28.51  ?  218 LYS B NZ     1 
ATOM   4566 N N      . ILE B 2 219 ? 40.215 6.610   49.548 1.00 21.13  ?  219 ILE B N      1 
ATOM   4567 C CA     . ILE B 2 219 ? 40.833 5.662   50.456 1.00 24.36  ?  219 ILE B CA     1 
ATOM   4568 C C      . ILE B 2 219 ? 41.121 4.403   49.654 1.00 23.50  ?  219 ILE B C      1 
ATOM   4569 O O      . ILE B 2 219 ? 40.258 3.962   48.891 1.00 21.94  ?  219 ILE B O      1 
ATOM   4570 C CB     . ILE B 2 219 ? 39.934 5.400   51.685 1.00 26.82  ?  219 ILE B CB     1 
ATOM   4571 C CG1    . ILE B 2 219 ? 39.733 6.711   52.459 1.00 27.54  ?  219 ILE B CG1    1 
ATOM   4572 C CG2    . ILE B 2 219 ? 40.586 4.396   52.639 1.00 28.51  ?  219 ILE B CG2    1 
ATOM   4573 C CD1    . ILE B 2 219 ? 38.348 7.273   52.441 1.00 24.98  ?  219 ILE B CD1    1 
ATOM   4574 N N      . ALA B 2 220 ? 42.351 3.865   49.777 1.00 22.88  ?  220 ALA B N      1 
ATOM   4575 C CA     . ALA B 2 220 ? 42.758 2.602   49.158 1.00 29.83  ?  220 ALA B CA     1 
ATOM   4576 C C      . ALA B 2 220 ? 42.619 1.410   50.116 1.00 31.09  ?  220 ALA B C      1 
ATOM   4577 O O      . ALA B 2 220 ? 42.824 1.537   51.322 1.00 29.77  ?  220 ALA B O      1 
ATOM   4578 C CB     . ALA B 2 220 ? 44.206 2.683   48.671 1.00 38.26  ?  220 ALA B CB     1 
ATOM   4579 N N      . ILE B 2 221 ? 42.260 0.232   49.568 1.00 33.90  ?  221 ILE B N      1 
ATOM   4580 C CA     . ILE B 2 221 ? 42.225 -0.998  50.363 1.00 31.83  ?  221 ILE B CA     1 
ATOM   4581 C C      . ILE B 2 221 ? 43.637 -1.544  50.492 1.00 39.62  ?  221 ILE B C      1 
ATOM   4582 O O      . ILE B 2 221 ? 44.384 -1.592  49.509 1.00 41.97  ?  221 ILE B O      1 
ATOM   4583 C CB     . ILE B 2 221 ? 41.317 -2.074  49.735 1.00 23.21  ?  221 ILE B CB     1 
ATOM   4584 C CG1    . ILE B 2 221 ? 39.867 -1.638  49.666 1.00 30.62  ?  221 ILE B CG1    1 
ATOM   4585 C CG2    . ILE B 2 221 ? 41.419 -3.352  50.514 1.00 25.59  ?  221 ILE B CG2    1 
ATOM   4586 C CD1    . ILE B 2 221 ? 38.940 -2.664  48.991 1.00 28.79  ?  221 ILE B CD1    1 
ATOM   4587 N N      . ASN B 2 222 ? 43.995 -1.993  51.695 1.00 51.97  ?  222 ASN B N      1 
ATOM   4588 C CA     . ASN B 2 222 ? 45.247 -2.711  51.915 1.00 47.77  ?  222 ASN B CA     1 
ATOM   4589 C C      . ASN B 2 222 ? 44.919 -4.188  51.758 1.00 49.12  ?  222 ASN B C      1 
ATOM   4590 O O      . ASN B 2 222 ? 44.213 -4.766  52.591 1.00 56.51  ?  222 ASN B O      1 
ATOM   4591 C CB     . ASN B 2 222 ? 45.826 -2.393  53.300 1.00 46.41  ?  222 ASN B CB     1 
ATOM   4592 C CG     . ASN B 2 222 ? 47.197 -3.035  53.543 1.00 46.04  ?  222 ASN B CG     1 
ATOM   4593 O OD1    . ASN B 2 222 ? 47.839 -3.563  52.636 1.00 49.13  ?  222 ASN B OD1    1 
ATOM   4594 N ND2    . ASN B 2 222 ? 47.637 -2.989  54.778 1.00 47.24  ?  222 ASN B ND2    1 
ATOM   4595 N N      . GLU B 2 223 ? 45.389 -4.789  50.670 1.00 44.55  ?  223 GLU B N      1 
ATOM   4596 C CA     . GLU B 2 223 ? 45.051 -6.180  50.402 1.00 44.65  ?  223 GLU B CA     1 
ATOM   4597 C C      . GLU B 2 223 ? 46.009 -7.149  51.065 1.00 45.53  ?  223 GLU B C      1 
ATOM   4598 O O      . GLU B 2 223 ? 45.657 -8.319  51.264 1.00 40.05  ?  223 GLU B O      1 
ATOM   4599 C CB     . GLU B 2 223 ? 45.026 -6.420  48.899 1.00 45.09  ?  223 GLU B CB     1 
ATOM   4600 C CG     . GLU B 2 223 ? 44.585 -5.192  48.119 1.00 50.39  ?  223 GLU B CG     1 
ATOM   4601 C CD     . GLU B 2 223 ? 44.744 -5.374  46.615 1.00 57.00  ?  223 GLU B CD     1 
ATOM   4602 O OE1    . GLU B 2 223 ? 45.512 -6.280  46.186 1.00 51.76  ?  223 GLU B OE1    1 
ATOM   4603 O OE2    . GLU B 2 223 ? 44.092 -4.609  45.870 1.00 58.67  -1 223 GLU B OE2    1 
ATOM   4604 N N      . LYS B 2 224 ? 47.191 -6.668  51.455 1.00 53.00  ?  224 LYS B N      1 
ATOM   4605 C CA     . LYS B 2 224 ? 48.205 -7.495  52.086 1.00 52.63  ?  224 LYS B CA     1 
ATOM   4606 C C      . LYS B 2 224 ? 47.826 -7.916  53.505 1.00 63.77  ?  224 LYS B C      1 
ATOM   4607 O O      . LYS B 2 224 ? 48.533 -8.741  54.094 1.00 72.56  ?  224 LYS B O      1 
ATOM   4608 C CB     . LYS B 2 224 ? 49.528 -6.735  52.095 1.00 46.69  ?  224 LYS B CB     1 
ATOM   4609 C CG     . LYS B 2 224 ? 50.196 -6.566  50.738 1.00 42.75  ?  224 LYS B CG     1 
ATOM   4610 C CD     . LYS B 2 224 ? 51.451 -5.699  50.856 1.00 44.86  ?  224 LYS B CD     1 
ATOM   4611 C CE     . LYS B 2 224 ? 51.106 -4.362  51.518 1.00 44.29  ?  224 LYS B CE     1 
ATOM   4612 N NZ     . LYS B 2 224 ? 52.216 -3.372  51.469 1.00 46.22  ?  224 LYS B NZ     1 
ATOM   4613 N N      . VAL B 2 225 ? 46.737 -7.373  54.059 1.00 54.07  ?  225 VAL B N      1 
ATOM   4614 C CA     . VAL B 2 225 ? 46.277 -7.736  55.395 1.00 43.48  ?  225 VAL B CA     1 
ATOM   4615 C C      . VAL B 2 225 ? 45.712 -9.151  55.384 1.00 41.89  ?  225 VAL B C      1 
ATOM   4616 O O      . VAL B 2 225 ? 44.831 -9.480  54.580 1.00 46.71  ?  225 VAL B O      1 
ATOM   4617 C CB     . VAL B 2 225 ? 45.233 -6.719  55.880 1.00 39.32  ?  225 VAL B CB     1 
ATOM   4618 C CG1    . VAL B 2 225 ? 44.877 -6.976  57.353 1.00 40.75  ?  225 VAL B CG1    1 
ATOM   4619 C CG2    . VAL B 2 225 ? 45.754 -5.307  55.678 1.00 32.00  ?  225 VAL B CG2    1 
ATOM   4620 N N      . ALA B 2 226 ? 46.220 -9.998  56.277 1.00 41.39  ?  226 ALA B N      1 
ATOM   4621 C CA     . ALA B 2 226 ? 45.652 -11.330 56.474 1.00 43.04  ?  226 ALA B CA     1 
ATOM   4622 C C      . ALA B 2 226 ? 44.307 -11.244 57.190 1.00 44.87  ?  226 ALA B C      1 
ATOM   4623 O O      . ALA B 2 226 ? 44.148 -10.499 58.163 1.00 50.94  ?  226 ALA B O      1 
ATOM   4624 C CB     . ALA B 2 226 ? 46.603 -12.213 57.280 1.00 43.26  ?  226 ALA B CB     1 
ATOM   4625 N N      . GLY B 2 227 ? 43.340 -12.016 56.702 1.00 37.98  ?  227 GLY B N      1 
ATOM   4626 C CA     . GLY B 2 227 ? 41.991 -11.968 57.227 1.00 40.63  ?  227 GLY B CA     1 
ATOM   4627 C C      . GLY B 2 227 ? 41.318 -10.622 57.119 1.00 39.29  ?  227 GLY B C      1 
ATOM   4628 O O      . GLY B 2 227 ? 40.376 -10.348 57.866 1.00 39.77  ?  227 GLY B O      1 
ATOM   4629 N N      . GLY B 2 228 ? 41.777 -9.775  56.195 1.00 31.41  ?  228 GLY B N      1 
ATOM   4630 C CA     . GLY B 2 228 ? 41.291 -8.420  56.067 1.00 24.62  ?  228 GLY B CA     1 
ATOM   4631 C C      . GLY B 2 228 ? 39.797 -8.339  55.857 1.00 27.76  ?  228 GLY B C      1 
ATOM   4632 O O      . GLY B 2 228 ? 39.190 -9.246  55.273 1.00 29.79  ?  228 GLY B O      1 
ATOM   4633 N N      . TYR B 2 229 ? 39.162 -7.302  56.349 1.00 30.26  ?  229 TYR B N      1 
ATOM   4634 C CA     . TYR B 2 229 ? 37.717 -7.226  56.317 1.00 35.51  ?  229 TYR B CA     1 
ATOM   4635 C C      . TYR B 2 229 ? 37.049 -7.238  54.979 1.00 41.73  ?  229 TYR B C      1 
ATOM   4636 O O      . TYR B 2 229 ? 35.986 -7.797  54.805 1.00 44.09  ?  229 TYR B O      1 
ATOM   4637 C CB     . TYR B 2 229 ? 37.237 -6.042  57.148 1.00 37.00  ?  229 TYR B CB     1 
ATOM   4638 C CG     . TYR B 2 229 ? 35.744 -5.867  57.183 1.00 35.20  ?  229 TYR B CG     1 
ATOM   4639 C CD1    . TYR B 2 229 ? 34.961 -6.586  58.063 1.00 30.95  ?  229 TYR B CD1    1 
ATOM   4640 C CD2    . TYR B 2 229 ? 35.120 -4.985  56.323 1.00 33.45  ?  229 TYR B CD2    1 
ATOM   4641 C CE1    . TYR B 2 229 ? 33.595 -6.427  58.081 1.00 43.91  ?  229 TYR B CE1    1 
ATOM   4642 C CE2    . TYR B 2 229 ? 33.763 -4.823  56.329 1.00 38.82  ?  229 TYR B CE2    1 
ATOM   4643 C CZ     . TYR B 2 229 ? 33.007 -5.542  57.208 1.00 49.06  ?  229 TYR B CZ     1 
ATOM   4644 O OH     . TYR B 2 229 ? 31.655 -5.362  57.187 1.00 52.06  ?  229 TYR B OH     1 
ATOM   4645 N N      . SER B 2 230 ? 37.667 -6.594  54.029 1.00 50.47  ?  230 SER B N      1 
ATOM   4646 C CA     . SER B 2 230 ? 37.109 -6.623  52.676 1.00 47.93  ?  230 SER B CA     1 
ATOM   4647 C C      . SER B 2 230 ? 37.209 -8.004  52.051 1.00 44.69  ?  230 SER B C      1 
ATOM   4648 O O      . SER B 2 230 ? 36.481 -8.295  51.092 1.00 39.47  ?  230 SER B O      1 
ATOM   4649 C CB     . SER B 2 230 ? 37.821 -5.607  51.778 1.00 46.10  ?  230 SER B CB     1 
ATOM   4650 O OG     . SER B 2 230 ? 38.799 -6.233  50.952 1.00 54.07  ?  230 SER B OG     1 
ATOM   4651 N N      . LYS B 2 231 ? 38.134 -8.829  52.559 1.00 43.52  ?  231 LYS B N      1 
ATOM   4652 C CA     . LYS B 2 231 ? 38.282 -10.219 52.153 1.00 40.86  ?  231 LYS B CA     1 
ATOM   4653 C C      . LYS B 2 231 ? 37.306 -11.138 52.865 1.00 40.12  ?  231 LYS B C      1 
ATOM   4654 O O      . LYS B 2 231 ? 36.849 -12.119 52.270 1.00 45.75  ?  231 LYS B O      1 
ATOM   4655 C CB     . LYS B 2 231 ? 39.709 -10.681 52.415 1.00 38.54  ?  231 LYS B CB     1 
ATOM   4656 C CG     . LYS B 2 231 ? 40.788 -9.728  51.912 1.00 31.21  ?  231 LYS B CG     1 
ATOM   4657 C CD     . LYS B 2 231 ? 42.147 -10.450 51.967 1.00 35.08  ?  231 LYS B CD     1 
ATOM   4658 C CE     . LYS B 2 231 ? 43.254 -9.481  51.892 1.00 34.79  ?  231 LYS B CE     1 
ATOM   4659 N NZ     . LYS B 2 231 ? 42.639 -8.136  52.126 1.00 44.32  ?  231 LYS B NZ     1 
ATOM   4660 N N      . THR B 2 232 ? 36.991 -10.849 54.128 1.00 31.65  ?  232 THR B N      1 
ATOM   4661 C CA     . THR B 2 232 ? 36.038 -11.662 54.881 1.00 34.06  ?  232 THR B CA     1 
ATOM   4662 C C      . THR B 2 232 ? 34.592 -11.365 54.489 1.00 35.41  ?  232 THR B C      1 
ATOM   4663 O O      . THR B 2 232 ? 33.796 -12.291 54.279 1.00 37.92  ?  232 THR B O      1 
ATOM   4664 C CB     . THR B 2 232 ? 36.222 -11.444 56.392 1.00 31.34  ?  232 THR B CB     1 
ATOM   4665 O OG1    . THR B 2 232 ? 36.214 -10.035 56.689 1.00 35.42  ?  232 THR B OG1    1 
ATOM   4666 C CG2    . THR B 2 232 ? 37.533 -12.057 56.847 1.00 25.87  ?  232 THR B CG2    1 
ATOM   4667 N N      . LYS B 2 233 ? 34.248 -10.077 54.402 1.00 28.37  ?  233 LYS B N      1 
ATOM   4668 C CA     . LYS B 2 233 ? 32.906 -9.641  54.040 1.00 25.12  ?  233 LYS B CA     1 
ATOM   4669 C C      . LYS B 2 233 ? 32.963 -8.803  52.797 1.00 26.44  ?  233 LYS B C      1 
ATOM   4670 O O      . LYS B 2 233 ? 32.901 -7.600  52.873 1.00 28.86  ?  233 LYS B O      1 
ATOM   4671 C CB     . LYS B 2 233 ? 32.278 -8.846  55.173 1.00 28.68  ?  233 LYS B CB     1 
ATOM   4672 C CG     . LYS B 2 233 ? 30.769 -8.752  55.117 1.00 34.00  ?  233 LYS B CG     1 
ATOM   4673 C CD     . LYS B 2 233 ? 30.190 -8.377  56.470 1.00 39.26  ?  233 LYS B CD     1 
ATOM   4674 C CE     . LYS B 2 233 ? 28.677 -8.538  56.483 1.00 33.24  ?  233 LYS B CE     1 
ATOM   4675 N NZ     . LYS B 2 233 ? 28.094 -8.486  57.847 1.00 30.82  ?  233 LYS B NZ     1 
ATOM   4676 N N      . PRO B 2 234 ? 33.081 -9.441  51.640 1.00 43.33  ?  234 PRO B N      1 
ATOM   4677 C CA     . PRO B 2 234 ? 33.181 -8.766  50.360 1.00 39.58  ?  234 PRO B CA     1 
ATOM   4678 C C      . PRO B 2 234 ? 31.909 -8.116  49.918 1.00 48.99  ?  234 PRO B C      1 
ATOM   4679 O O      . PRO B 2 234 ? 31.971 -7.223  49.103 1.00 57.22  ?  234 PRO B O      1 
ATOM   4680 C CB     . PRO B 2 234 ? 33.601 -9.882  49.433 1.00 40.52  ?  234 PRO B CB     1 
ATOM   4681 C CG     . PRO B 2 234 ? 33.018 -11.106 50.018 1.00 48.73  ?  234 PRO B CG     1 
ATOM   4682 C CD     . PRO B 2 234 ? 33.085 -10.905 51.495 1.00 50.37  ?  234 PRO B CD     1 
ATOM   4683 N N      . THR B 2 235 ? 30.785 -8.540  50.437 1.00 29.21  ?  235 THR B N      1 
ATOM   4684 C CA     . THR B 2 235 ? 29.505 -7.964  50.118 1.00 29.69  ?  235 THR B CA     1 
ATOM   4685 C C      . THR B 2 235 ? 29.442 -6.508  50.518 1.00 30.56  ?  235 THR B C      1 
ATOM   4686 O O      . THR B 2 235 ? 28.724 -5.735  49.918 1.00 29.04  ?  235 THR B O      1 
ATOM   4687 C CB     . THR B 2 235 ? 28.396 -8.758  50.828 1.00 32.80  ?  235 THR B CB     1 
ATOM   4688 O OG1    . THR B 2 235 ? 28.703 -8.883  52.217 1.00 29.97  ?  235 THR B OG1    1 
ATOM   4689 C CG2    . THR B 2 235 ? 28.286 -10.134 50.237 1.00 21.21  ?  235 THR B CG2    1 
ATOM   4690 N N      . THR B 2 236 ? 30.159 -6.146  51.562 1.00 45.17  ?  236 THR B N      1 
ATOM   4691 C CA     . THR B 2 236 ? 30.162 -4.782  52.056 1.00 44.82  ?  236 THR B CA     1 
ATOM   4692 C C      . THR B 2 236 ? 30.977 -3.854  51.174 1.00 45.77  ?  236 THR B C      1 
ATOM   4693 O O      . THR B 2 236 ? 32.122 -4.128  50.905 1.00 46.53  ?  236 THR B O      1 
ATOM   4694 C CB     . THR B 2 236 ? 30.679 -4.709  53.512 1.00 45.83  ?  236 THR B CB     1 
ATOM   4695 O OG1    . THR B 2 236 ? 29.973 -5.619  54.349 1.00 45.99  ?  236 THR B OG1    1 
ATOM   4696 C CG2    . THR B 2 236 ? 30.535 -3.321  54.059 1.00 45.75  ?  236 THR B CG2    1 
ATOM   4697 N N      . PRO B 2 237 ? 30.370 -2.769  50.672 1.00 39.75  ?  237 PRO B N      1 
ATOM   4698 C CA     . PRO B 2 237 ? 31.156 -1.780  49.899 1.00 39.99  ?  237 PRO B CA     1 
ATOM   4699 C C      . PRO B 2 237 ? 32.235 -1.067  50.723 1.00 43.36  ?  237 PRO B C      1 
ATOM   4700 O O      . PRO B 2 237 ? 31.989 -0.558  51.824 1.00 43.96  ?  237 PRO B O      1 
ATOM   4701 C CB     . PRO B 2 237 ? 30.093 -0.800  49.400 1.00 33.72  ?  237 PRO B CB     1 
ATOM   4702 C CG     . PRO B 2 237 ? 28.847 -1.117  50.200 1.00 37.13  ?  237 PRO B CG     1 
ATOM   4703 C CD     . PRO B 2 237 ? 28.923 -2.576  50.516 1.00 35.04  ?  237 PRO B CD     1 
ATOM   4704 N N      . PHE B 2 238 ? 33.435 -0.955  50.157 1.00 37.00  ?  238 PHE B N      1 
ATOM   4705 C CA     . PHE B 2 238 ? 34.542 -0.272  50.826 1.00 30.38  ?  238 PHE B CA     1 
ATOM   4706 C C      . PHE B 2 238 ? 34.521 1.203   50.682 1.00 27.35  ?  238 PHE B C      1 
ATOM   4707 O O      . PHE B 2 238 ? 34.588 1.736   49.609 1.00 33.03  ?  238 PHE B O      1 
ATOM   4708 C CB     . PHE B 2 238 ? 35.902 -0.801  50.365 1.00 29.50  ?  238 PHE B CB     1 
ATOM   4709 C CG     . PHE B 2 238 ? 37.081 -0.253  51.133 1.00 33.59  ?  238 PHE B CG     1 
ATOM   4710 C CD1    . PHE B 2 238 ? 37.683 0.941   50.770 1.00 33.86  ?  238 PHE B CD1    1 
ATOM   4711 C CD2    . PHE B 2 238 ? 37.621 -0.963  52.184 1.00 37.32  ?  238 PHE B CD2    1 
ATOM   4712 C CE1    . PHE B 2 238 ? 38.768 1.429   51.461 1.00 32.64  ?  238 PHE B CE1    1 
ATOM   4713 C CE2    . PHE B 2 238 ? 38.715 -0.484  52.874 1.00 36.26  ?  238 PHE B CE2    1 
ATOM   4714 C CZ     . PHE B 2 238 ? 39.287 0.716   52.516 1.00 33.28  ?  238 PHE B CZ     1 
ATOM   4715 N N      . VAL B 2 239 ? 34.415 1.888   51.813 1.00 20.52  ?  239 VAL B N      1 
ATOM   4716 C CA     . VAL B 2 239 ? 34.495 3.336   51.782 1.00 24.32  ?  239 VAL B CA     1 
ATOM   4717 C C      . VAL B 2 239 ? 35.688 3.730   52.637 1.00 25.19  ?  239 VAL B C      1 
ATOM   4718 O O      . VAL B 2 239 ? 36.570 4.433   52.153 1.00 25.34  ?  239 VAL B O      1 
ATOM   4719 C CB     . VAL B 2 239 ? 33.197 4.014   52.236 1.00 21.38  ?  239 VAL B CB     1 
ATOM   4720 C CG1    . VAL B 2 239 ? 32.880 5.158   51.293 1.00 18.80  ?  239 VAL B CG1    1 
ATOM   4721 C CG2    . VAL B 2 239 ? 32.060 3.016   52.192 1.00 30.17  ?  239 VAL B CG2    1 
ATOM   4722 N N      . ALA B 2 240 ? 35.747 3.244   53.879 1.00 28.48  ?  240 ALA B N      1 
ATOM   4723 C CA     . ALA B 2 240 ? 36.912 3.519   54.726 1.00 24.47  ?  240 ALA B CA     1 
ATOM   4724 C C      . ALA B 2 240 ? 37.183 2.400   55.723 1.00 28.69  ?  240 ALA B C      1 
ATOM   4725 O O      . ALA B 2 240 ? 37.717 2.661   56.804 1.00 34.43  ?  240 ALA B O      1 
ATOM   4726 C CB     . ALA B 2 240 ? 36.740 4.846   55.452 1.00 19.25  ?  240 ALA B CB     1 
ATOM   4727 N N      . SER B 2 241 ? 36.868 1.164   55.373 1.00 25.96  ?  241 SER B N      1 
ATOM   4728 C CA     . SER B 2 241 ? 37.006 0.011   56.288 1.00 24.27  ?  241 SER B CA     1 
ATOM   4729 C C      . SER B 2 241 ? 36.274 0.104   57.595 1.00 30.50  ?  241 SER B C      1 
ATOM   4730 O O      . SER B 2 241 ? 35.277 0.761   57.678 1.00 39.26  ?  241 SER B O      1 
ATOM   4731 C CB     . SER B 2 241 ? 38.424 -0.460  56.488 1.00 24.69  ?  241 SER B CB     1 
ATOM   4732 O OG     . SER B 2 241 ? 38.463 -1.836  56.801 1.00 27.54  ?  241 SER B OG     1 
ATOM   4733 N N      . LEU B 2 242 ? 36.784 -0.505  58.644 1.00 36.11  ?  242 LEU B N      1 
ATOM   4734 C CA     . LEU B 2 242 ? 36.052 -0.537  59.907 1.00 31.34  ?  242 LEU B CA     1 
ATOM   4735 C C      . LEU B 2 242 ? 36.069 0.842   60.557 1.00 31.46  ?  242 LEU B C      1 
ATOM   4736 O O      . LEU B 2 242 ? 37.107 1.490   60.602 1.00 20.01  ?  242 LEU B O      1 
ATOM   4737 C CB     . LEU B 2 242 ? 36.647 -1.579  60.853 1.00 31.72  ?  242 LEU B CB     1 
ATOM   4738 C CG     . LEU B 2 242 ? 36.161 -3.021  60.691 1.00 36.96  ?  242 LEU B CG     1 
ATOM   4739 C CD1    . LEU B 2 242 ? 34.651 -3.116  60.861 1.00 37.48  ?  242 LEU B CD1    1 
ATOM   4740 C CD2    . LEU B 2 242 ? 36.598 -3.592  59.350 1.00 38.35  ?  242 LEU B CD2    1 
ATOM   4741 N N      . SER B 2 243 ? 34.925 1.297   61.057 1.00 23.53  ?  243 SER B N      1 
ATOM   4742 C CA     . SER B 2 243 ? 34.893 2.583   61.737 1.00 23.74  ?  243 SER B CA     1 
ATOM   4743 C C      . SER B 2 243 ? 35.265 2.546   63.179 1.00 23.46  ?  243 SER B C      1 
ATOM   4744 O O      . SER B 2 243 ? 34.749 1.760   63.927 1.00 20.24  ?  243 SER B O      1 
ATOM   4745 C CB     . SER B 2 243 ? 33.569 3.292   61.572 1.00 22.25  ?  243 SER B CB     1 
ATOM   4746 O OG     . SER B 2 243 ? 33.653 4.627   61.983 1.00 21.79  ?  243 SER B OG     1 
ATOM   4747 N N      . GLY B 2 244 ? 36.191 3.407   63.549 1.00 48.51  ?  244 GLY B N      1 
ATOM   4748 C CA     . GLY B 2 244 ? 36.635 3.514   64.917 1.00 46.31  ?  244 GLY B CA     1 
ATOM   4749 C C      . GLY B 2 244 ? 36.026 4.673   65.609 1.00 46.85  ?  244 GLY B C      1 
ATOM   4750 O O      . GLY B 2 244 ? 36.312 4.874   66.762 1.00 55.26  ?  244 GLY B O      1 
ATOM   4751 N N      . THR B 2 245 ? 35.209 5.456   64.922 1.00 37.45  ?  245 THR B N      1 
ATOM   4752 C CA     . THR B 2 245 ? 34.490 6.520   65.575 1.00 33.03  ?  245 THR B CA     1 
ATOM   4753 C C      . THR B 2 245 ? 33.324 5.884   66.239 1.00 28.99  ?  245 THR B C      1 
ATOM   4754 O O      . THR B 2 245 ? 32.678 6.503   67.045 1.00 43.66  ?  245 THR B O      1 
ATOM   4755 C CB     . THR B 2 245 ? 34.071 7.680   64.662 1.00 30.22  ?  245 THR B CB     1 
ATOM   4756 O OG1    . THR B 2 245 ? 33.115 7.209   63.718 1.00 39.41  ?  245 THR B OG1    1 
ATOM   4757 C CG2    . THR B 2 245 ? 35.235 8.266   63.947 1.00 32.22  ?  245 THR B CG2    1 
ATOM   4758 N N      . THR B 2 246 ? 33.041 4.645   65.910 1.00 25.33  ?  246 THR B N      1 
ATOM   4759 C CA     . THR B 2 246 ? 31.998 3.919   66.591 1.00 28.24  ?  246 THR B CA     1 
ATOM   4760 C C      . THR B 2 246 ? 32.407 3.757   68.040 1.00 28.05  ?  246 THR B C      1 
ATOM   4761 O O      . THR B 2 246 ? 31.571 3.760   68.904 1.00 29.85  ?  246 THR B O      1 
ATOM   4762 C CB     . THR B 2 246 ? 31.726 2.538   65.989 1.00 33.26  ?  246 THR B CB     1 
ATOM   4763 O OG1    . THR B 2 246 ? 31.950 2.554   64.588 1.00 36.53  ?  246 THR B OG1    1 
ATOM   4764 C CG2    . THR B 2 246 ? 30.310 2.091   66.267 1.00 33.62  ?  246 THR B CG2    1 
ATOM   4765 N N      . TYR B 2 247 ? 33.687 3.562   68.285 1.00 23.31  ?  247 TYR B N      1 
ATOM   4766 C CA     . TYR B 2 247 ? 34.194 3.449   69.629 1.00 33.19  ?  247 TYR B CA     1 
ATOM   4767 C C      . TYR B 2 247 ? 34.012 4.732   70.425 1.00 38.38  ?  247 TYR B C      1 
ATOM   4768 O O      . TYR B 2 247 ? 33.802 4.691   71.618 1.00 38.05  ?  247 TYR B O      1 
ATOM   4769 C CB     . TYR B 2 247 ? 35.638 2.922   69.673 1.00 29.67  ?  247 TYR B CB     1 
ATOM   4770 C CG     . TYR B 2 247 ? 35.853 1.577   69.048 1.00 36.89  ?  247 TYR B CG     1 
ATOM   4771 C CD1    . TYR B 2 247 ? 35.324 0.433   69.618 1.00 36.18  ?  247 TYR B CD1    1 
ATOM   4772 C CD2    . TYR B 2 247 ? 36.602 1.444   67.896 1.00 40.22  ?  247 TYR B CD2    1 
ATOM   4773 C CE1    . TYR B 2 247 ? 35.526 -0.800  69.045 1.00 28.76  ?  247 TYR B CE1    1 
ATOM   4774 C CE2    . TYR B 2 247 ? 36.810 0.214   67.321 1.00 35.10  ?  247 TYR B CE2    1 
ATOM   4775 C CZ     . TYR B 2 247 ? 36.271 -0.901  67.900 1.00 29.11  ?  247 TYR B CZ     1 
ATOM   4776 O OH     . TYR B 2 247 ? 36.480 -2.122  67.326 1.00 32.88  ?  247 TYR B OH     1 
ATOM   4777 N N      . SER B 2 248 ? 34.174 5.871   69.791 1.00 38.65  ?  248 SER B N      1 
ATOM   4778 C CA     . SER B 2 248 ? 33.909 7.129   70.467 1.00 33.66  ?  248 SER B CA     1 
ATOM   4779 C C      . SER B 2 248 ? 32.440 7.352   70.816 1.00 37.82  ?  248 SER B C      1 
ATOM   4780 O O      . SER B 2 248 ? 32.164 7.765   71.911 1.00 40.97  ?  248 SER B O      1 
ATOM   4781 C CB     . SER B 2 248 ? 34.492 8.280   69.686 1.00 29.32  ?  248 SER B CB     1 
ATOM   4782 O OG     . SER B 2 248 ? 35.887 8.283   69.712 1.00 29.83  ?  248 SER B OG     1 
ATOM   4783 N N      . LEU B 2 249 ? 31.502 7.035   69.922 1.00 35.44  ?  249 LEU B N      1 
ATOM   4784 C CA     . LEU B 2 249 ? 30.064 7.124   70.222 1.00 30.76  ?  249 LEU B CA     1 
ATOM   4785 C C      . LEU B 2 249 ? 29.784 6.161   71.331 1.00 30.12  ?  249 LEU B C      1 
ATOM   4786 O O      . LEU B 2 249 ? 28.881 6.371   72.091 1.00 22.38  ?  249 LEU B O      1 
ATOM   4787 C CB     . LEU B 2 249 ? 29.200 6.822   68.983 1.00 24.50  ?  249 LEU B CB     1 
ATOM   4788 C CG     . LEU B 2 249 ? 27.778 6.311   69.074 1.00 20.70  ?  249 LEU B CG     1 
ATOM   4789 C CD1    . LEU B 2 249 ? 26.835 7.489   69.126 1.00 31.37  ?  249 LEU B CD1    1 
ATOM   4790 C CD2    . LEU B 2 249 ? 27.501 5.481   67.841 1.00 20.54  ?  249 LEU B CD2    1 
ATOM   4791 N N      . MET B 2 250 ? 30.515 5.062   71.358 1.00 35.55  ?  250 MET B N      1 
ATOM   4792 C CA     . MET B 2 250 ? 30.408 4.081   72.396 1.00 28.23  ?  250 MET B CA     1 
ATOM   4793 C C      . MET B 2 250 ? 30.803 4.635   73.732 1.00 35.58  ?  250 MET B C      1 
ATOM   4794 O O      . MET B 2 250 ? 30.202 4.289   74.726 1.00 32.34  ?  250 MET B O      1 
ATOM   4795 C CB     . MET B 2 250 ? 31.241 2.883   72.027 1.00 29.02  ?  250 MET B CB     1 
ATOM   4796 C CG     . MET B 2 250 ? 30.547 1.922   71.078 1.00 37.82  ?  250 MET B CG     1 
ATOM   4797 S SD     . MET B 2 250 ? 28.824 1.621   71.492 1.00 36.64  ?  250 MET B SD     1 
ATOM   4798 C CE     . MET B 2 250 ? 28.972 0.471   72.843 1.00 30.00  ?  250 MET B CE     1 
ATOM   4799 N N      . VAL B 2 251 ? 31.827 5.464   73.773 1.00 28.67  ?  251 VAL B N      1 
ATOM   4800 C CA     . VAL B 2 251 ? 32.158 6.118   75.014 1.00 32.54  ?  251 VAL B CA     1 
ATOM   4801 C C      . VAL B 2 251 ? 31.070 7.104   75.453 1.00 35.02  ?  251 VAL B C      1 
ATOM   4802 O O      . VAL B 2 251 ? 30.640 7.094   76.580 1.00 30.04  ?  251 VAL B O      1 
ATOM   4803 C CB     . VAL B 2 251 ? 33.561 6.778   74.961 1.00 29.72  ?  251 VAL B CB     1 
ATOM   4804 C CG1    . VAL B 2 251 ? 33.830 7.605   76.199 1.00 23.84  ?  251 VAL B CG1    1 
ATOM   4805 C CG2    . VAL B 2 251 ? 34.636 5.732   74.764 1.00 36.15  ?  251 VAL B CG2    1 
ATOM   4806 N N      . VAL B 2 252 ? 30.591 7.906   74.534 1.00 32.43  ?  252 VAL B N      1 
ATOM   4807 C CA     . VAL B 2 252 ? 29.565 8.866   74.839 1.00 31.03  ?  252 VAL B CA     1 
ATOM   4808 C C      . VAL B 2 252 ? 28.280 8.165   75.245 1.00 41.27  ?  252 VAL B C      1 
ATOM   4809 O O      . VAL B 2 252 ? 27.650 8.533   76.224 1.00 42.44  ?  252 VAL B O      1 
ATOM   4810 C CB     . VAL B 2 252 ? 29.354 9.794   73.627 1.00 21.77  ?  252 VAL B CB     1 
ATOM   4811 C CG1    . VAL B 2 252 ? 28.202 10.748  73.866 1.00 22.82  ?  252 VAL B CG1    1 
ATOM   4812 C CG2    . VAL B 2 252 ? 30.628 10.529  73.289 1.00 21.82  ?  252 VAL B CG2    1 
ATOM   4813 N N      . LEU B 2 253 ? 27.912 7.130   74.523 1.00 42.42  ?  253 LEU B N      1 
ATOM   4814 C CA     . LEU B 2 253 ? 26.715 6.404   74.806 1.00 38.66  ?  253 LEU B CA     1 
ATOM   4815 C C      . LEU B 2 253 ? 26.776 5.693   76.129 1.00 39.09  ?  253 LEU B C      1 
ATOM   4816 O O      . LEU B 2 253 ? 25.780 5.599   76.797 1.00 36.48  ?  253 LEU B O      1 
ATOM   4817 C CB     . LEU B 2 253 ? 26.385 5.466   73.648 1.00 33.06  ?  253 LEU B CB     1 
ATOM   4818 C CG     . LEU B 2 253 ? 25.384 5.887   72.589 1.00 31.96  ?  253 LEU B CG     1 
ATOM   4819 C CD1    . LEU B 2 253 ? 25.203 4.716   71.654 1.00 29.58  ?  253 LEU B CD1    1 
ATOM   4820 C CD2    . LEU B 2 253 ? 24.063 6.226   73.247 1.00 38.01  ?  253 LEU B CD2    1 
ATOM   4821 N N      . THR B 2 254 ? 27.937 5.164   76.489 1.00 44.78  ?  254 THR B N      1 
ATOM   4822 C CA     . THR B 2 254 ? 28.096 4.432   77.749 1.00 45.20  ?  254 THR B CA     1 
ATOM   4823 C C      . THR B 2 254 ? 27.832 5.370   78.886 1.00 43.06  ?  254 THR B C      1 
ATOM   4824 O O      . THR B 2 254 ? 27.153 4.999   79.822 1.00 43.50  ?  254 THR B O      1 
ATOM   4825 C CB     . THR B 2 254 ? 29.442 3.678   77.868 1.00 42.88  ?  254 THR B CB     1 
ATOM   4826 O OG1    . THR B 2 254 ? 29.448 2.580   76.954 1.00 48.82  ?  254 THR B OG1    1 
ATOM   4827 C CG2    . THR B 2 254 ? 29.654 3.154   79.260 1.00 30.80  ?  254 THR B CG2    1 
ATOM   4828 N N      . ASP B 2 255 ? 28.295 6.600   78.786 1.00 57.37  ?  255 ASP B N      1 
ATOM   4829 C CA     . ASP B 2 255 ? 27.975 7.593   79.787 1.00 60.87  ?  255 ASP B CA     1 
ATOM   4830 C C      . ASP B 2 255 ? 26.468 7.860   79.823 1.00 63.32  ?  255 ASP B C      1 
ATOM   4831 O O      . ASP B 2 255 ? 25.928 8.076   80.878 1.00 66.84  ?  255 ASP B O      1 
ATOM   4832 C CB     . ASP B 2 255 ? 28.763 8.871   79.556 1.00 59.55  ?  255 ASP B CB     1 
ATOM   4833 C CG     . ASP B 2 255 ? 28.829 9.737   80.761 1.00 66.39  ?  255 ASP B CG     1 
ATOM   4834 O OD1    . ASP B 2 255 ? 29.353 9.279   81.793 1.00 70.38  ?  255 ASP B OD1    1 
ATOM   4835 O OD2    . ASP B 2 255 ? 28.376 10.889  80.664 1.00 71.23  -1 255 ASP B OD2    1 
ATOM   4836 N N      . TYR B 2 256 ? 25.793 7.876   78.685 1.00 43.06  ?  256 TYR B N      1 
ATOM   4837 C CA     . TYR B 2 256 ? 24.339 8.038   78.650 1.00 43.92  ?  256 TYR B CA     1 
ATOM   4838 C C      . TYR B 2 256 ? 23.565 6.908   79.308 1.00 43.92  ?  256 TYR B C      1 
ATOM   4839 O O      . TYR B 2 256 ? 22.614 7.143   80.003 1.00 33.73  ?  256 TYR B O      1 
ATOM   4840 C CB     . TYR B 2 256 ? 23.869 8.229   77.210 1.00 38.88  ?  256 TYR B CB     1 
ATOM   4841 C CG     . TYR B 2 256 ? 22.406 8.504   77.061 1.00 35.33  ?  256 TYR B CG     1 
ATOM   4842 C CD1    . TYR B 2 256 ? 21.895 9.765   77.297 1.00 35.93  ?  256 TYR B CD1    1 
ATOM   4843 C CD2    . TYR B 2 256 ? 21.534 7.507   76.670 1.00 36.64  ?  256 TYR B CD2    1 
ATOM   4844 C CE1    . TYR B 2 256 ? 20.554 10.023  77.159 1.00 39.91  ?  256 TYR B CE1    1 
ATOM   4845 C CE2    . TYR B 2 256 ? 20.189 7.755   76.533 1.00 37.97  ?  256 TYR B CE2    1 
ATOM   4846 C CZ     . TYR B 2 256 ? 19.709 9.013   76.784 1.00 41.05  ?  256 TYR B CZ     1 
ATOM   4847 O OH     . TYR B 2 256 ? 18.376 9.256   76.645 1.00 39.52  ?  256 TYR B OH     1 
ATOM   4848 N N      . ILE B 2 257 ? 23.979 5.682   79.079 1.00 46.84  ?  257 ILE B N      1 
ATOM   4849 C CA     . ILE B 2 257 ? 23.324 4.548   79.671 1.00 43.92  ?  257 ILE B CA     1 
ATOM   4850 C C      . ILE B 2 257 ? 23.463 4.623   81.176 1.00 49.23  ?  257 ILE B C      1 
ATOM   4851 O O      . ILE B 2 257 ? 22.534 4.283   81.882 1.00 52.97  ?  257 ILE B O      1 
ATOM   4852 C CB     . ILE B 2 257 ? 23.811 3.206   79.083 1.00 32.21  ?  257 ILE B CB     1 
ATOM   4853 C CG1    . ILE B 2 257 ? 23.558 3.174   77.581 1.00 34.94  ?  257 ILE B CG1    1 
ATOM   4854 C CG2    . ILE B 2 257 ? 23.129 2.037   79.765 1.00 24.68  ?  257 ILE B CG2    1 
ATOM   4855 C CD1    . ILE B 2 257 ? 24.134 1.962   76.885 1.00 32.77  ?  257 ILE B CD1    1 
ATOM   4856 N N      . GLU B 2 258 ? 24.613 5.040   81.681 1.00 50.54  ?  258 GLU B N      1 
ATOM   4857 C CA     . GLU B 2 258 ? 24.776 5.223   83.105 1.00 39.67  ?  258 GLU B CA     1 
ATOM   4858 C C      . GLU B 2 258 ? 23.896 6.297   83.674 1.00 37.50  ?  258 GLU B C      1 
ATOM   4859 O O      . GLU B 2 258 ? 23.214 6.076   84.651 1.00 34.66  ?  258 GLU B O      1 
ATOM   4860 C CB     . GLU B 2 258 ? 26.194 5.633   83.363 1.00 43.13  ?  258 GLU B CB     1 
ATOM   4861 C CG     . GLU B 2 258 ? 27.275 4.654   82.952 1.00 51.79  ?  258 GLU B CG     1 
ATOM   4862 C CD     . GLU B 2 258 ? 28.670 5.248   83.111 1.00 58.97  ?  258 GLU B CD     1 
ATOM   4863 O OE1    . GLU B 2 258 ? 28.781 6.410   83.549 1.00 54.10  ?  258 GLU B OE1    1 
ATOM   4864 O OE2    . GLU B 2 258 ? 29.660 4.559   82.795 1.00 62.90  -1 258 GLU B OE2    1 
ATOM   4865 N N      . LYS B 2 259 ? 23.866 7.438   83.029 1.00 23.53  ?  259 LYS B N      1 
ATOM   4866 C CA     . LYS B 2 259 ? 23.087 8.556   83.502 1.00 27.53  ?  259 LYS B CA     1 
ATOM   4867 C C      . LYS B 2 259 ? 21.603 8.415   83.333 1.00 26.74  ?  259 LYS B C      1 
ATOM   4868 O O      . LYS B 2 259 ? 20.855 9.117   83.963 1.00 31.07  ?  259 LYS B O      1 
ATOM   4869 C CB     . LYS B 2 259 ? 23.632 9.864   82.942 1.00 23.48  ?  259 LYS B CB     1 
ATOM   4870 C CG     . LYS B 2 259 ? 25.093 10.094  83.281 1.00 30.76  ?  259 LYS B CG     1 
ATOM   4871 C CD     . LYS B 2 259 ? 25.589 11.467  82.868 1.00 32.21  ?  259 LYS B CD     1 
ATOM   4872 C CE     . LYS B 2 259 ? 27.003 11.681  83.376 1.00 40.61  ?  259 LYS B CE     1 
ATOM   4873 N NZ     . LYS B 2 259 ? 27.493 13.081  83.246 1.00 40.07  ?  259 LYS B NZ     1 
ATOM   4874 N N      . HIS B 2 260 ? 21.183 7.526   82.463 1.00 48.66  ?  260 HIS B N      1 
ATOM   4875 C CA     . HIS B 2 260 ? 19.787 7.308   82.183 1.00 49.18  ?  260 HIS B CA     1 
ATOM   4876 C C      . HIS B 2 260 ? 19.337 5.874   82.391 1.00 47.55  ?  260 HIS B C      1 
ATOM   4877 O O      . HIS B 2 260 ? 18.395 5.458   81.749 1.00 44.77  ?  260 HIS B O      1 
ATOM   4878 C CB     . HIS B 2 260 ? 19.477 7.762   80.751 1.00 44.23  ?  260 HIS B CB     1 
ATOM   4879 C CG     . HIS B 2 260 ? 19.496 9.242   80.553 1.00 50.41  ?  260 HIS B CG     1 
ATOM   4880 N ND1    . HIS B 2 260 ? 20.662 9.973   80.508 1.00 55.25  ?  260 HIS B ND1    1 
ATOM   4881 C CD2    . HIS B 2 260 ? 18.491 10.125  80.350 1.00 55.91  ?  260 HIS B CD2    1 
ATOM   4882 C CE1    . HIS B 2 260 ? 20.372 11.246  80.307 1.00 59.24  ?  260 HIS B CE1    1 
ATOM   4883 N NE2    . HIS B 2 260 ? 19.061 11.363  80.205 1.00 57.88  ?  260 HIS B NE2    1 
ATOM   4884 N N      . LYS B 2 261 ? 19.975 5.113   83.272 1.00 32.10  ?  261 LYS B N      1 
ATOM   4885 C CA     . LYS B 2 261 ? 19.634 3.682   83.411 1.00 38.10  ?  261 LYS B CA     1 
ATOM   4886 C C      . LYS B 2 261 ? 18.218 3.356   83.856 1.00 38.08  ?  261 LYS B C      1 
ATOM   4887 O O      . LYS B 2 261 ? 17.737 2.273   83.611 1.00 40.03  ?  261 LYS B O      1 
ATOM   4888 C CB     . LYS B 2 261 ? 20.659 2.907   84.253 1.00 38.86  ?  261 LYS B CB     1 
ATOM   4889 C CG     . LYS B 2 261 ? 20.796 3.354   85.690 1.00 46.55  ?  261 LYS B CG     1 
ATOM   4890 C CD     . LYS B 2 261 ? 22.033 2.745   86.323 1.00 51.98  ?  261 LYS B CD     1 
ATOM   4891 C CE     . LYS B 2 261 ? 23.279 3.070   85.514 1.00 44.88  ?  261 LYS B CE     1 
ATOM   4892 N NZ     . LYS B 2 261 ? 24.531 2.953   86.305 1.00 37.95  ?  261 LYS B NZ     1 
ATOM   4893 N N      . THR B 2 262 ? 17.581 4.264   84.552 1.00 24.47  ?  262 THR B N      1 
ATOM   4894 C CA     . THR B 2 262 ? 16.260 4.058   85.036 1.00 24.28  ?  262 THR B CA     1 
ATOM   4895 C C      . THR B 2 262 ? 15.159 4.366   84.033 1.00 24.31  ?  262 THR B C      1 
ATOM   4896 O O      . THR B 2 262 ? 14.018 3.980   84.209 1.00 25.88  ?  262 THR B O      1 
ATOM   4897 C CB     . THR B 2 262 ? 16.118 4.844   86.350 1.00 29.38  ?  262 THR B CB     1 
ATOM   4898 O OG1    . THR B 2 262 ? 16.511 6.203   86.139 1.00 33.75  ?  262 THR B OG1    1 
ATOM   4899 C CG2    . THR B 2 262 ? 16.988 4.239   87.419 1.00 24.69  ?  262 THR B CG2    1 
ATOM   4900 N N      . ASP B 2 263 ? 15.504 5.032   82.965 1.00 42.95  ?  263 ASP B N      1 
ATOM   4901 C CA     . ASP B 2 263 ? 14.552 5.374   81.945 1.00 50.60  ?  263 ASP B CA     1 
ATOM   4902 C C      . ASP B 2 263 ? 13.943 4.191   81.238 1.00 46.47  ?  263 ASP B C      1 
ATOM   4903 O O      . ASP B 2 263 ? 14.603 3.220   80.940 1.00 48.02  ?  263 ASP B O      1 
ATOM   4904 C CB     . ASP B 2 263 ? 15.214 6.285   80.928 1.00 54.24  ?  263 ASP B CB     1 
ATOM   4905 C CG     . ASP B 2 263 ? 15.174 7.731   81.319 1.00 60.03  ?  263 ASP B CG     1 
ATOM   4906 O OD1    . ASP B 2 263 ? 14.611 8.042   82.379 1.00 66.52  ?  263 ASP B OD1    1 
ATOM   4907 O OD2    . ASP B 2 263 ? 15.706 8.562   80.562 1.00 58.87  -1 263 ASP B OD2    1 
ATOM   4908 N N      . LYS B 2 264 ? 12.658 4.278   80.977 1.00 47.90  ?  264 LYS B N      1 
ATOM   4909 C CA     . LYS B 2 264 ? 11.968 3.174   80.354 1.00 56.76  ?  264 LYS B CA     1 
ATOM   4910 C C      . LYS B 2 264 ? 11.918 3.289   78.861 1.00 53.63  ?  264 LYS B C      1 
ATOM   4911 O O      . LYS B 2 264 ? 11.588 2.345   78.182 1.00 56.84  ?  264 LYS B O      1 
ATOM   4912 C CB     . LYS B 2 264 ? 10.573 3.033   80.969 1.00 62.09  ?  264 LYS B CB     1 
ATOM   4913 C CG     . LYS B 2 264 ? 9.916  1.690   80.685 1.00 67.99  ?  264 LYS B CG     1 
ATOM   4914 C CD     . LYS B 2 264 ? 10.898 0.538   80.857 1.00 68.05  ?  264 LYS B CD     1 
ATOM   4915 C CE     . LYS B 2 264 ? 10.332 -0.764  80.318 1.00 69.11  ?  264 LYS B CE     1 
ATOM   4916 N NZ     . LYS B 2 264 ? 10.017 -0.688  78.864 1.00 72.72  ?  264 LYS B NZ     1 
ATOM   4917 N N      . ASP B 2 265 ? 12.294 4.435   78.354 1.00 42.55  ?  265 ASP B N      1 
ATOM   4918 C CA     . ASP B 2 265 ? 12.320 4.657   76.938 1.00 46.19  ?  265 ASP B CA     1 
ATOM   4919 C C      . ASP B 2 265 ? 13.739 4.605   76.413 1.00 47.71  ?  265 ASP B C      1 
ATOM   4920 O O      . ASP B 2 265 ? 13.974 4.980   75.286 1.00 43.38  ?  265 ASP B O      1 
ATOM   4921 C CB     . ASP B 2 265 ? 11.613 5.986   76.600 1.00 50.55  ?  265 ASP B CB     1 
ATOM   4922 C CG     . ASP B 2 265 ? 12.177 7.191   77.335 1.00 55.47  ?  265 ASP B CG     1 
ATOM   4923 O OD1    . ASP B 2 265 ? 12.485 7.119   78.537 1.00 58.39  ?  265 ASP B OD1    1 
ATOM   4924 O OD2    . ASP B 2 265 ? 12.263 8.251   76.695 1.00 56.03  -1 265 ASP B OD2    1 
ATOM   4925 N N      . ILE B 2 266 ? 14.677 4.122   77.214 1.00 38.02  ?  266 ILE B N      1 
ATOM   4926 C CA     . ILE B 2 266 ? 16.097 4.118   76.845 1.00 39.07  ?  266 ILE B CA     1 
ATOM   4927 C C      . ILE B 2 266 ? 16.486 3.316   75.595 1.00 38.05  ?  266 ILE B C      1 
ATOM   4928 O O      . ILE B 2 266 ? 17.307 3.756   74.829 1.00 34.71  ?  266 ILE B O      1 
ATOM   4929 C CB     . ILE B 2 266 ? 17.012 3.854   78.091 1.00 37.40  ?  266 ILE B CB     1 
ATOM   4930 C CG1    . ILE B 2 266 ? 18.375 4.515   77.896 1.00 36.34  ?  266 ILE B CG1    1 
ATOM   4931 C CG2    . ILE B 2 266 ? 17.142 2.376   78.404 1.00 38.26  ?  266 ILE B CG2    1 
ATOM   4932 C CD1    . ILE B 2 266 ? 19.482 3.914   78.721 1.00 33.54  ?  266 ILE B CD1    1 
ATOM   4933 N N      . GLU B 2 267 ? 15.889 2.163   75.375 1.00 39.30  ?  267 GLU B N      1 
ATOM   4934 C CA     . GLU B 2 267 ? 16.136 1.414   74.154 1.00 42.61  ?  267 GLU B CA     1 
ATOM   4935 C C      . GLU B 2 267 ? 15.662 2.178   72.924 1.00 48.33  ?  267 GLU B C      1 
ATOM   4936 O O      . GLU B 2 267 ? 16.313 2.147   71.906 1.00 45.25  ?  267 GLU B O      1 
ATOM   4937 C CB     . GLU B 2 267 ? 15.460 0.075   74.242 1.00 41.56  ?  267 GLU B CB     1 
ATOM   4938 C CG     . GLU B 2 267 ? 15.951 -1.031  73.351 1.00 39.76  ?  267 GLU B CG     1 
ATOM   4939 C CD     . GLU B 2 267 ? 14.955 -2.157  73.364 1.00 46.08  ?  267 GLU B CD     1 
ATOM   4940 O OE1    . GLU B 2 267 ? 13.754 -1.858  73.296 1.00 47.07  ?  267 GLU B OE1    1 
ATOM   4941 O OE2    . GLU B 2 267 ? 15.346 -3.326  73.464 1.00 44.53  -1 267 GLU B OE2    1 
ATOM   4942 N N      . LYS B 2 268 ? 14.523 2.839   73.005 1.00 36.86  ?  268 LYS B N      1 
ATOM   4943 C CA     . LYS B 2 268 ? 14.056 3.641   71.916 1.00 34.06  ?  268 LYS B CA     1 
ATOM   4944 C C      . LYS B 2 268 ? 14.972 4.780   71.655 1.00 40.04  ?  268 LYS B C      1 
ATOM   4945 O O      . LYS B 2 268 ? 15.255 5.086   70.514 1.00 42.05  ?  268 LYS B O      1 
ATOM   4946 C CB     . LYS B 2 268 ? 12.674 4.174   72.256 1.00 33.24  ?  268 LYS B CB     1 
ATOM   4947 C CG     . LYS B 2 268 ? 12.120 5.220   71.319 1.00 35.07  ?  268 LYS B CG     1 
ATOM   4948 C CD     . LYS B 2 268 ? 10.771 5.679   71.831 1.00 39.70  ?  268 LYS B CD     1 
ATOM   4949 C CE     . LYS B 2 268 ? 10.281 6.911   71.099 1.00 41.96  ?  268 LYS B CE     1 
ATOM   4950 N NZ     . LYS B 2 268 ? 9.008  7.405   71.687 1.00 43.36  ?  268 LYS B NZ     1 
ATOM   4951 N N      . LYS B 2 269 ? 15.405 5.441   72.711 1.00 46.11  ?  269 LYS B N      1 
ATOM   4952 C CA     . LYS B 2 269 ? 16.318 6.562   72.598 1.00 42.64  ?  269 LYS B CA     1 
ATOM   4953 C C      . LYS B 2 269 ? 17.721 6.215   72.150 1.00 42.65  ?  269 LYS B C      1 
ATOM   4954 O O      . LYS B 2 269 ? 18.277 6.900   71.328 1.00 43.99  ?  269 LYS B O      1 
ATOM   4955 C CB     . LYS B 2 269 ? 16.282 7.365   73.887 1.00 37.64  ?  269 LYS B CB     1 
ATOM   4956 C CG     . LYS B 2 269 ? 14.989 8.126   74.076 1.00 33.72  ?  269 LYS B CG     1 
ATOM   4957 C CD     . LYS B 2 269 ? 15.073 9.060   75.261 1.00 27.80  ?  269 LYS B CD     1 
ATOM   4958 C CE     . LYS B 2 269 ? 15.335 8.281   76.529 1.00 37.31  ?  269 LYS B CE     1 
ATOM   4959 N NZ     . LYS B 2 269 ? 15.225 9.159   77.718 1.00 47.42  ?  269 LYS B NZ     1 
ATOM   4960 N N      . VAL B 2 270 ? 18.285 5.148   72.668 1.00 32.26  ?  270 VAL B N      1 
ATOM   4961 C CA     . VAL B 2 270 ? 19.590 4.690   72.226 1.00 28.52  ?  270 VAL B CA     1 
ATOM   4962 C C      . VAL B 2 270 ? 19.504 4.233   70.790 1.00 29.04  ?  270 VAL B C      1 
ATOM   4963 O O      . VAL B 2 270 ? 20.447 4.382   70.055 1.00 21.58  ?  270 VAL B O      1 
ATOM   4964 C CB     . VAL B 2 270 ? 20.225 3.689   73.212 1.00 25.91  ?  270 VAL B CB     1 
ATOM   4965 C CG1    . VAL B 2 270 ? 21.386 2.944   72.580 1.00 21.61  ?  270 VAL B CG1    1 
ATOM   4966 C CG2    . VAL B 2 270 ? 20.661 4.393   74.478 1.00 23.63  ?  270 VAL B CG2    1 
ATOM   4967 N N      . ASN B 2 271 ? 18.386 3.636   70.410 1.00 39.26  ?  271 ASN B N      1 
ATOM   4968 C CA     . ASN B 2 271 ? 18.144 3.250   69.018 1.00 38.23  ?  271 ASN B CA     1 
ATOM   4969 C C      . ASN B 2 271 ? 18.061 4.420   68.077 1.00 38.43  ?  271 ASN B C      1 
ATOM   4970 O O      . ASN B 2 271 ? 18.510 4.330   66.971 1.00 38.66  ?  271 ASN B O      1 
ATOM   4971 C CB     . ASN B 2 271 ? 16.917 2.348   68.903 1.00 40.77  ?  271 ASN B CB     1 
ATOM   4972 C CG     . ASN B 2 271 ? 17.266 0.891   68.750 1.00 39.83  ?  271 ASN B CG     1 
ATOM   4973 O OD1    . ASN B 2 271 ? 18.016 0.518   67.863 1.00 37.68  ?  271 ASN B OD1    1 
ATOM   4974 N ND2    . ASN B 2 271 ? 16.701 0.059   69.605 1.00 34.83  ?  271 ASN B ND2    1 
ATOM   4975 N N      . GLN B 2 272 ? 17.468 5.509   68.504 1.00 26.91  ?  272 GLN B N      1 
ATOM   4976 C CA     . GLN B 2 272 ? 17.444 6.687   67.711 1.00 21.29  ?  272 GLN B CA     1 
ATOM   4977 C C      . GLN B 2 272 ? 18.835 7.246   67.490 1.00 29.99  ?  272 GLN B C      1 
ATOM   4978 O O      . GLN B 2 272 ? 19.178 7.672   66.402 1.00 29.78  ?  272 GLN B O      1 
ATOM   4979 C CB     . GLN B 2 272 ? 16.569 7.708   68.382 1.00 21.50  ?  272 GLN B CB     1 
ATOM   4980 C CG     . GLN B 2 272 ? 15.087 7.534   68.184 1.00 23.45  ?  272 GLN B CG     1 
ATOM   4981 C CD     . GLN B 2 272 ? 14.320 8.600   68.922 1.00 31.37  ?  272 GLN B CD     1 
ATOM   4982 O OE1    . GLN B 2 272 ? 14.903 9.429   69.604 1.00 30.12  ?  272 GLN B OE1    1 
ATOM   4983 N NE2    . GLN B 2 272 ? 13.010 8.581   68.791 1.00 36.43  ?  272 GLN B NE2    1 
ATOM   4984 N N      . ILE B 2 273 ? 19.647 7.258   68.518 1.00 25.59  ?  273 ILE B N      1 
ATOM   4985 C CA     . ILE B 2 273 ? 20.986 7.730   68.360 1.00 24.84  ?  273 ILE B CA     1 
ATOM   4986 C C      . ILE B 2 273 ? 21.809 6.836   67.448 1.00 29.89  ?  273 ILE B C      1 
ATOM   4987 O O      . ILE B 2 273 ? 22.501 7.306   66.561 1.00 24.89  ?  273 ILE B O      1 
ATOM   4988 C CB     . ILE B 2 273 ? 21.670 7.937   69.721 1.00 21.14  ?  273 ILE B CB     1 
ATOM   4989 C CG1    . ILE B 2 273 ? 20.743 8.640   70.693 1.00 23.79  ?  273 ILE B CG1    1 
ATOM   4990 C CG2    . ILE B 2 273 ? 22.964 8.703   69.557 1.00 25.88  ?  273 ILE B CG2    1 
ATOM   4991 C CD1    . ILE B 2 273 ? 20.706 10.133  70.518 1.00 36.24  ?  273 ILE B CD1    1 
ATOM   4992 N N      . ILE B 2 274 ? 21.700 5.542   67.642 1.00 31.35  ?  274 ILE B N      1 
ATOM   4993 C CA     . ILE B 2 274 ? 22.464 4.619   66.855 1.00 34.17  ?  274 ILE B CA     1 
ATOM   4994 C C      . ILE B 2 274 ? 22.053 4.668   65.414 1.00 37.66  ?  274 ILE B C      1 
ATOM   4995 O O      . ILE B 2 274 ? 22.877 4.641   64.528 1.00 40.41  ?  274 ILE B O      1 
ATOM   4996 C CB     . ILE B 2 274 ? 22.374 3.199   67.434 1.00 31.66  ?  274 ILE B CB     1 
ATOM   4997 C CG1    . ILE B 2 274 ? 23.087 3.135   68.778 1.00 27.93  ?  274 ILE B CG1    1 
ATOM   4998 C CG2    . ILE B 2 274 ? 22.985 2.185   66.484 1.00 26.35  ?  274 ILE B CG2    1 
ATOM   4999 C CD1    . ILE B 2 274 ? 24.542 3.515   68.698 1.00 20.83  ?  274 ILE B CD1    1 
ATOM   5000 N N      . ASN B 2 275 ? 20.765 4.739   65.181 1.00 39.70  ?  275 ASN B N      1 
ATOM   5001 C CA     . ASN B 2 275 ? 20.261 4.797   63.844 1.00 35.03  ?  275 ASN B CA     1 
ATOM   5002 C C      . ASN B 2 275 ? 20.599 6.084   63.103 1.00 34.20  ?  275 ASN B C      1 
ATOM   5003 O O      . ASN B 2 275 ? 20.869 6.039   61.922 1.00 32.34  ?  275 ASN B O      1 
ATOM   5004 C CB     . ASN B 2 275 ? 18.781 4.405   63.809 1.00 30.47  ?  275 ASN B CB     1 
ATOM   5005 C CG     . ASN B 2 275 ? 18.535 2.995   64.274 1.00 26.57  ?  275 ASN B CG     1 
ATOM   5006 O OD1    . ASN B 2 275 ? 19.451 2.241   64.556 1.00 36.12  ?  275 ASN B OD1    1 
ATOM   5007 N ND2    . ASN B 2 275 ? 17.277 2.645   64.366 1.00 25.34  ?  275 ASN B ND2    1 
ATOM   5008 N N      . LEU B 2 276 ? 20.567 7.227   63.766 1.00 29.97  ?  276 LEU B N      1 
ATOM   5009 C CA     . LEU B 2 276 ? 20.980 8.472   63.143 1.00 25.54  ?  276 LEU B CA     1 
ATOM   5010 C C      . LEU B 2 276 ? 22.435 8.443   62.789 1.00 28.22  ?  276 LEU B C      1 
ATOM   5011 O O      . LEU B 2 276 ? 22.831 9.063   61.846 1.00 30.07  ?  276 LEU B O      1 
ATOM   5012 C CB     . LEU B 2 276 ? 20.647 9.703   63.981 1.00 31.07  ?  276 LEU B CB     1 
ATOM   5013 C CG     . LEU B 2 276 ? 20.845 11.030  63.262 1.00 29.37  ?  276 LEU B CG     1 
ATOM   5014 C CD1    . LEU B 2 276 ? 19.944 11.098  62.044 1.00 31.95  ?  276 LEU B CD1    1 
ATOM   5015 C CD2    . LEU B 2 276 ? 20.585 12.196  64.186 1.00 28.83  ?  276 LEU B CD2    1 
ATOM   5016 N N      . TRP B 2 277 ? 23.247 7.785   63.581 1.00 28.77  ?  277 TRP B N      1 
ATOM   5017 C CA     . TRP B 2 277 ? 24.642 7.636   63.269 1.00 31.18  ?  277 TRP B CA     1 
ATOM   5018 C C      . TRP B 2 277 ? 24.827 6.890   62.002 1.00 27.94  ?  277 TRP B C      1 
ATOM   5019 O O      . TRP B 2 277 ? 25.596 7.303   61.169 1.00 27.96  ?  277 TRP B O      1 
ATOM   5020 C CB     . TRP B 2 277 ? 25.304 6.849   64.382 1.00 30.15  ?  277 TRP B CB     1 
ATOM   5021 C CG     . TRP B 2 277 ? 26.773 6.723   64.319 1.00 31.35  ?  277 TRP B CG     1 
ATOM   5022 C CD1    . TRP B 2 277 ? 27.474 5.720   63.752 1.00 33.85  ?  277 TRP B CD1    1 
ATOM   5023 C CD2    . TRP B 2 277 ? 27.733 7.613   64.884 1.00 33.92  ?  277 TRP B CD2    1 
ATOM   5024 N NE1    . TRP B 2 277 ? 28.813 5.929   63.907 1.00 30.17  ?  277 TRP B NE1    1 
ATOM   5025 C CE2    . TRP B 2 277 ? 29.000 7.088   64.603 1.00 29.15  ?  277 TRP B CE2    1 
ATOM   5026 C CE3    . TRP B 2 277 ? 27.644 8.805   65.595 1.00 35.14  ?  277 TRP B CE3    1 
ATOM   5027 C CZ2    . TRP B 2 277 ? 30.165 7.711   65.003 1.00 30.15  ?  277 TRP B CZ2    1 
ATOM   5028 C CZ3    . TRP B 2 277 ? 28.798 9.421   65.986 1.00 38.17  ?  277 TRP B CZ3    1 
ATOM   5029 C CH2    . TRP B 2 277 ? 30.044 8.877   65.691 1.00 35.04  ?  277 TRP B CH2    1 
ATOM   5030 N N      . ILE B 2 278 ? 24.088 5.812   61.838 1.00 32.52  ?  278 ILE B N      1 
ATOM   5031 C CA     . ILE B 2 278 ? 24.165 4.997   60.637 1.00 35.90  ?  278 ILE B CA     1 
ATOM   5032 C C      . ILE B 2 278 ? 23.737 5.765   59.412 1.00 36.94  ?  278 ILE B C      1 
ATOM   5033 O O      . ILE B 2 278 ? 24.399 5.713   58.390 1.00 33.25  ?  278 ILE B O      1 
ATOM   5034 C CB     . ILE B 2 278 ? 23.343 3.709   60.819 1.00 35.32  ?  278 ILE B CB     1 
ATOM   5035 C CG1    . ILE B 2 278 ? 23.919 2.888   61.973 1.00 30.55  ?  278 ILE B CG1    1 
ATOM   5036 C CG2    . ILE B 2 278 ? 23.276 2.897   59.536 1.00 20.41  ?  278 ILE B CG2    1 
ATOM   5037 C CD1    . ILE B 2 278 ? 23.049 1.730   62.395 1.00 35.39  ?  278 ILE B CD1    1 
ATOM   5038 N N      . SER B 2 279 ? 22.674 6.523   59.544 1.00 34.50  ?  279 SER B N      1 
ATOM   5039 C CA     . SER B 2 279 ? 22.190 7.309   58.465 1.00 25.67  ?  279 SER B CA     1 
ATOM   5040 C C      . SER B 2 279 ? 23.214 8.300   58.095 1.00 29.53  ?  279 SER B C      1 
ATOM   5041 O O      . SER B 2 279 ? 23.463 8.509   56.934 1.00 31.91  ?  279 SER B O      1 
ATOM   5042 C CB     . SER B 2 279 ? 20.975 8.067   58.966 1.00 26.66  ?  279 SER B CB     1 
ATOM   5043 O OG     . SER B 2 279 ? 19.990 7.220   59.481 1.00 35.31  ?  279 SER B OG     1 
ATOM   5044 N N      . SER B 2 280 ? 23.802 8.930   59.081 1.00 31.01  ?  280 SER B N      1 
ATOM   5045 C CA     . SER B 2 280 ? 24.776 9.970   58.865 1.00 31.75  ?  280 SER B CA     1 
ATOM   5046 C C      . SER B 2 280 ? 26.099 9.574   58.270 1.00 39.12  ?  280 SER B C      1 
ATOM   5047 O O      . SER B 2 280 ? 26.632 10.272  57.435 1.00 43.17  ?  280 SER B O      1 
ATOM   5048 C CB     . SER B 2 280 ? 24.935 10.790  60.139 1.00 28.82  ?  280 SER B CB     1 
ATOM   5049 O OG     . SER B 2 280 ? 23.697 11.300  60.565 1.00 29.75  ?  280 SER B OG     1 
ATOM   5050 N N      . TYR B 2 281 ? 26.645 8.467   58.690 1.00 33.98  ?  281 TYR B N      1 
ATOM   5051 C CA     . TYR B 2 281 ? 27.870 8.004   58.104 1.00 31.54  ?  281 TYR B CA     1 
ATOM   5052 C C      . TYR B 2 281 ? 27.693 7.601   56.654 1.00 34.63  ?  281 TYR B C      1 
ATOM   5053 O O      . TYR B 2 281 ? 28.581 7.817   55.855 1.00 31.94  ?  281 TYR B O      1 
ATOM   5054 C CB     . TYR B 2 281 ? 28.591 6.997   58.998 1.00 24.60  ?  281 TYR B CB     1 
ATOM   5055 C CG     . TYR B 2 281 ? 29.429 7.652   60.045 1.00 35.30  ?  281 TYR B CG     1 
ATOM   5056 C CD1    . TYR B 2 281 ? 28.872 8.544   60.937 1.00 38.34  ?  281 TYR B CD1    1 
ATOM   5057 C CD2    . TYR B 2 281 ? 30.784 7.396   60.134 1.00 44.16  ?  281 TYR B CD2    1 
ATOM   5058 C CE1    . TYR B 2 281 ? 29.643 9.163   61.892 1.00 42.17  ?  281 TYR B CE1    1 
ATOM   5059 C CE2    . TYR B 2 281 ? 31.562 8.015   61.090 1.00 42.21  ?  281 TYR B CE2    1 
ATOM   5060 C CZ     . TYR B 2 281 ? 30.981 8.898   61.958 1.00 42.28  ?  281 TYR B CZ     1 
ATOM   5061 O OH     . TYR B 2 281 ? 31.738 9.520   62.908 1.00 45.96  ?  281 TYR B OH     1 
ATOM   5062 N N      . ILE B 2 282 ? 26.572 6.970   56.327 1.00 25.06  ?  282 ILE B N      1 
ATOM   5063 C CA     . ILE B 2 282 ? 26.284 6.642   54.955 1.00 23.67  ?  282 ILE B CA     1 
ATOM   5064 C C      . ILE B 2 282 ? 26.058 7.865   54.088 1.00 29.69  ?  282 ILE B C      1 
ATOM   5065 O O      . ILE B 2 282 ? 26.579 7.952   53.000 1.00 31.05  ?  282 ILE B O      1 
ATOM   5066 C CB     . ILE B 2 282 ? 25.129 5.669   54.819 1.00 27.37  ?  282 ILE B CB     1 
ATOM   5067 C CG1    . ILE B 2 282 ? 25.415 4.395   55.614 1.00 27.70  ?  282 ILE B CG1    1 
ATOM   5068 C CG2    . ILE B 2 282 ? 24.883 5.342   53.357 1.00 22.87  ?  282 ILE B CG2    1 
ATOM   5069 C CD1    . ILE B 2 282 ? 24.264 3.418   55.662 1.00 19.49  ?  282 ILE B CD1    1 
ATOM   5070 N N      . LYS B 2 283 ? 25.329 8.829   54.590 1.00 41.03  ?  283 LYS B N      1 
ATOM   5071 C CA     . LYS B 2 283 ? 25.053 10.008  53.829 1.00 42.72  ?  283 LYS B CA     1 
ATOM   5072 C C      . LYS B 2 283 ? 26.257 10.841  53.535 1.00 44.49  ?  283 LYS B C      1 
ATOM   5073 O O      . LYS B 2 283 ? 26.319 11.485  52.501 1.00 48.78  ?  283 LYS B O      1 
ATOM   5074 C CB     . LYS B 2 283 ? 23.944 10.821  54.462 1.00 43.20  ?  283 LYS B CB     1 
ATOM   5075 C CG     . LYS B 2 283 ? 22.562 10.250  54.202 1.00 45.40  ?  283 LYS B CG     1 
ATOM   5076 C CD     . LYS B 2 283 ? 21.472 11.270  54.471 1.00 40.99  ?  283 LYS B CD     1 
ATOM   5077 C CE     . LYS B 2 283 ? 21.646 12.500  53.600 1.00 46.15  ?  283 LYS B CE     1 
ATOM   5078 N NZ     . LYS B 2 283 ? 20.443 13.377  53.620 1.00 49.76  ?  283 LYS B NZ     1 
ATOM   5079 N N      . GLU B 2 284 ? 27.179 10.887  54.470 1.00 42.63  ?  284 GLU B N      1 
ATOM   5080 C CA     . GLU B 2 284 ? 28.364 11.682  54.332 1.00 37.87  ?  284 GLU B CA     1 
ATOM   5081 C C      . GLU B 2 284 ? 29.488 10.986  53.624 1.00 32.31  ?  284 GLU B C      1 
ATOM   5082 O O      . GLU B 2 284 ? 30.508 11.593  53.367 1.00 36.82  ?  284 GLU B O      1 
ATOM   5083 C CB     . GLU B 2 284 ? 28.801 12.145  55.723 1.00 43.47  ?  284 GLU B CB     1 
ATOM   5084 C CG     . GLU B 2 284 ? 27.769 12.964  56.464 1.00 43.80  ?  284 GLU B CG     1 
ATOM   5085 C CD     . GLU B 2 284 ? 27.517 14.298  55.810 1.00 51.63  ?  284 GLU B CD     1 
ATOM   5086 O OE1    . GLU B 2 284 ? 28.498 15.016  55.539 1.00 47.99  ?  284 GLU B OE1    1 
ATOM   5087 O OE2    . GLU B 2 284 ? 26.337 14.633  55.582 1.00 58.32  -1 284 GLU B OE2    1 
ATOM   5088 N N      . GLY B 2 285 ? 29.317 9.717   53.317 1.00 18.97  ?  285 GLY B N      1 
ATOM   5089 C CA     . GLY B 2 285 ? 30.327 8.972   52.611 1.00 18.79  ?  285 GLY B CA     1 
ATOM   5090 C C      . GLY B 2 285 ? 31.455 8.457   53.432 1.00 22.18  ?  285 GLY B C      1 
ATOM   5091 O O      . GLY B 2 285 ? 32.415 7.963   52.882 1.00 24.52  ?  285 GLY B O      1 
ATOM   5092 N N      . TYR B 2 286 ? 31.372 8.617   54.732 1.00 18.96  ?  286 TYR B N      1 
ATOM   5093 C CA     . TYR B 2 286 ? 32.363 8.145   55.627 1.00 19.04  ?  286 TYR B CA     1 
ATOM   5094 C C      . TYR B 2 286 ? 32.445 6.666   55.649 1.00 25.10  ?  286 TYR B C      1 
ATOM   5095 O O      . TYR B 2 286 ? 33.529 6.132   55.675 1.00 34.23  ?  286 TYR B O      1 
ATOM   5096 C CB     . TYR B 2 286 ? 32.007 8.586   57.031 1.00 26.23  ?  286 TYR B CB     1 
ATOM   5097 C CG     . TYR B 2 286 ? 31.884 10.068  57.269 1.00 29.57  ?  286 TYR B CG     1 
ATOM   5098 C CD1    . TYR B 2 286 ? 32.576 10.981  56.498 1.00 28.52  ?  286 TYR B CD1    1 
ATOM   5099 C CD2    . TYR B 2 286 ? 31.101 10.549  58.298 1.00 34.64  ?  286 TYR B CD2    1 
ATOM   5100 C CE1    . TYR B 2 286 ? 32.472 12.335  56.730 1.00 29.94  ?  286 TYR B CE1    1 
ATOM   5101 C CE2    . TYR B 2 286 ? 30.990 11.901  58.540 1.00 39.05  ?  286 TYR B CE2    1 
ATOM   5102 C CZ     . TYR B 2 286 ? 31.680 12.789  57.751 1.00 36.11  ?  286 TYR B CZ     1 
ATOM   5103 O OH     . TYR B 2 286 ? 31.580 14.135  57.981 1.00 37.68  ?  286 TYR B OH     1 
ATOM   5104 N N      . HIS B 2 287 ? 31.307 5.989   55.686 1.00 23.48  ?  287 HIS B N      1 
ATOM   5105 C CA     . HIS B 2 287 ? 31.298 4.549   55.794 1.00 22.88  ?  287 HIS B CA     1 
ATOM   5106 C C      . HIS B 2 287 ? 30.112 3.824   55.254 1.00 23.11  ?  287 HIS B C      1 
ATOM   5107 O O      . HIS B 2 287 ? 29.076 4.409   55.030 1.00 21.85  ?  287 HIS B O      1 
ATOM   5108 C CB     . HIS B 2 287 ? 31.411 4.107   57.258 1.00 20.20  ?  287 HIS B CB     1 
ATOM   5109 C CG     . HIS B 2 287 ? 32.775 4.249   57.855 1.00 24.46  ?  287 HIS B CG     1 
ATOM   5110 N ND1    . HIS B 2 287 ? 33.802 3.374   57.589 1.00 23.63  ?  287 HIS B ND1    1 
ATOM   5111 C CD2    . HIS B 2 287 ? 33.278 5.167   58.709 1.00 19.88  ?  287 HIS B CD2    1 
ATOM   5112 C CE1    . HIS B 2 287 ? 34.879 3.748   58.248 1.00 19.50  ?  287 HIS B CE1    1 
ATOM   5113 N NE2    . HIS B 2 287 ? 34.585 4.830   58.938 1.00 19.69  ?  287 HIS B NE2    1 
ATOM   5114 N N      . SER B 2 288 ? 30.277 2.533   55.023 1.00 46.84  ?  288 SER B N      1 
ATOM   5115 C CA     . SER B 2 288 ? 29.186 1.673   54.656 1.00 52.39  ?  288 SER B CA     1 
ATOM   5116 C C      . SER B 2 288 ? 28.492 1.220   55.946 1.00 53.24  ?  288 SER B C      1 
ATOM   5117 O O      . SER B 2 288 ? 29.051 1.365   57.006 1.00 53.45  ?  288 SER B O      1 
ATOM   5118 C CB     . SER B 2 288 ? 29.722 0.488   53.904 1.00 50.83  ?  288 SER B CB     1 
ATOM   5119 O OG     . SER B 2 288 ? 30.141 -0.491  54.805 1.00 50.83  ?  288 SER B OG     1 
ATOM   5120 N N      . TYR B 2 289 ? 27.290 0.672   55.868 1.00 35.33  ?  289 TYR B N      1 
ATOM   5121 C CA     . TYR B 2 289 ? 26.530 0.250   57.039 1.00 28.31  ?  289 TYR B CA     1 
ATOM   5122 C C      . TYR B 2 289 ? 27.228 -0.792  57.826 1.00 27.13  ?  289 TYR B C      1 
ATOM   5123 O O      . TYR B 2 289 ? 27.274 -0.716  59.027 1.00 30.93  ?  289 TYR B O      1 
ATOM   5124 C CB     . TYR B 2 289 ? 25.201 -0.309  56.543 1.00 29.41  ?  289 TYR B CB     1 
ATOM   5125 C CG     . TYR B 2 289 ? 24.370 -1.151  57.477 1.00 25.37  ?  289 TYR B CG     1 
ATOM   5126 C CD1    . TYR B 2 289 ? 24.574 -2.515  57.581 1.00 26.12  ?  289 TYR B CD1    1 
ATOM   5127 C CD2    . TYR B 2 289 ? 23.328 -0.595  58.192 1.00 23.99  ?  289 TYR B CD2    1 
ATOM   5128 C CE1    . TYR B 2 289 ? 23.803 -3.290  58.412 1.00 25.77  ?  289 TYR B CE1    1 
ATOM   5129 C CE2    . TYR B 2 289 ? 22.549 -1.363  59.023 1.00 27.21  ?  289 TYR B CE2    1 
ATOM   5130 C CZ     . TYR B 2 289 ? 22.793 -2.709  59.128 1.00 30.71  ?  289 TYR B CZ     1 
ATOM   5131 O OH     . TYR B 2 289 ? 22.020 -3.479  59.951 1.00 35.64  ?  289 TYR B OH     1 
ATOM   5132 N N      . SER B 2 290 ? 27.825 -1.743  57.153 1.00 37.09  ?  290 SER B N      1 
ATOM   5133 C CA     . SER B 2 290 ? 28.454 -2.853  57.827 1.00 38.08  ?  290 SER B CA     1 
ATOM   5134 C C      . SER B 2 290 ? 29.828 -2.493  58.261 1.00 33.69  ?  290 SER B C      1 
ATOM   5135 O O      . SER B 2 290 ? 30.520 -3.283  58.832 1.00 33.22  ?  290 SER B O      1 
ATOM   5136 C CB     . SER B 2 290 ? 28.382 -4.102  56.965 1.00 42.65  ?  290 SER B CB     1 
ATOM   5137 O OG     . SER B 2 290 ? 27.096 -4.663  57.007 1.00 42.54  ?  290 SER B OG     1 
ATOM   5138 N N      . GLU B 2 291 ? 30.221 -1.271  57.987 1.00 30.60  ?  291 GLU B N      1 
ATOM   5139 C CA     . GLU B 2 291 ? 31.504 -0.786  58.440 1.00 30.59  ?  291 GLU B CA     1 
ATOM   5140 C C      . GLU B 2 291 ? 31.253 -0.116  59.760 1.00 27.78  ?  291 GLU B C      1 
ATOM   5141 O O      . GLU B 2 291 ? 32.167 0.178   60.486 1.00 29.10  ?  291 GLU B O      1 
ATOM   5142 C CB     . GLU B 2 291 ? 32.145 0.133   57.409 1.00 28.39  ?  291 GLU B CB     1 
ATOM   5143 C CG     . GLU B 2 291 ? 32.827 -0.563  56.244 1.00 28.39  ?  291 GLU B CG     1 
ATOM   5144 C CD     . GLU B 2 291 ? 33.280 0.414   55.174 1.00 29.72  ?  291 GLU B CD     1 
ATOM   5145 O OE1    . GLU B 2 291 ? 33.082 1.618   55.343 1.00 36.06  ?  291 GLU B OE1    1 
ATOM   5146 O OE2    . GLU B 2 291 ? 33.848 -0.008  54.166 1.00 25.30  -1 291 GLU B OE2    1 
ATOM   5147 N N      . VAL B 2 292 ? 30.002 0.094   60.076 1.00 19.91  ?  292 VAL B N      1 
ATOM   5148 C CA     . VAL B 2 292 ? 29.648 0.637   61.378 1.00 31.77  ?  292 VAL B CA     1 
ATOM   5149 C C      . VAL B 2 292 ? 29.050 -0.446  62.271 1.00 36.72  ?  292 VAL B C      1 
ATOM   5150 O O      . VAL B 2 292 ? 29.506 -0.673  63.400 1.00 25.87  ?  292 VAL B O      1 
ATOM   5151 C CB     . VAL B 2 292 ? 28.670 1.806   61.231 1.00 33.36  ?  292 VAL B CB     1 
ATOM   5152 C CG1    . VAL B 2 292 ? 28.414 2.441   62.614 1.00 26.04  ?  292 VAL B CG1    1 
ATOM   5153 C CG2    . VAL B 2 292 ? 29.203 2.803   60.193 1.00 36.20  ?  292 VAL B CG2    1 
ATOM   5154 N N      . VAL B 2 293 ? 27.954 -1.043  61.796 1.00 32.69  ?  293 VAL B N      1 
ATOM   5155 C CA     . VAL B 2 293 ? 27.259 -2.081  62.551 1.00 25.36  ?  293 VAL B CA     1 
ATOM   5156 C C      . VAL B 2 293 ? 28.218 -3.185  62.966 1.00 25.89  ?  293 VAL B C      1 
ATOM   5157 O O      . VAL B 2 293 ? 28.191 -3.659  64.109 1.00 25.32  ?  293 VAL B O      1 
ATOM   5158 C CB     . VAL B 2 293 ? 26.084 -2.633  61.724 1.00 24.05  ?  293 VAL B CB     1 
ATOM   5159 C CG1    . VAL B 2 293 ? 25.464 -3.808  62.439 1.00 25.85  ?  293 VAL B CG1    1 
ATOM   5160 C CG2    . VAL B 2 293 ? 25.052 -1.521  61.462 1.00 20.38  ?  293 VAL B CG2    1 
ATOM   5161 N N      . ASP B 2 294 ? 29.071 -3.620  62.036 1.00 37.00  ?  294 ASP B N      1 
ATOM   5162 C CA     . ASP B 2 294 ? 30.014 -4.691  62.323 1.00 32.87  ?  294 ASP B CA     1 
ATOM   5163 C C      . ASP B 2 294 ? 31.024 -4.288  63.392 1.00 32.67  ?  294 ASP B C      1 
ATOM   5164 O O      . ASP B 2 294 ? 31.716 -5.160  63.919 1.00 35.42  ?  294 ASP B O      1 
ATOM   5165 C CB     . ASP B 2 294 ? 30.724 -5.137  61.033 1.00 33.61  ?  294 ASP B CB     1 
ATOM   5166 C CG     . ASP B 2 294 ? 29.891 -6.139  60.199 1.00 43.27  ?  294 ASP B CG     1 
ATOM   5167 O OD1    . ASP B 2 294 ? 28.661 -6.241  60.400 1.00 49.78  ?  294 ASP B OD1    1 
ATOM   5168 O OD2    . ASP B 2 294 ? 30.468 -6.837  59.340 1.00 48.66  -1 294 ASP B OD2    1 
ATOM   5169 N N      . VAL B 2 295 ? 31.131 -2.997  63.724 1.00 25.58  ?  295 VAL B N      1 
ATOM   5170 C CA     . VAL B 2 295 ? 31.859 -2.587  64.925 1.00 25.31  ?  295 VAL B CA     1 
ATOM   5171 C C      . VAL B 2 295 ? 30.993 -2.813  66.162 1.00 28.44  ?  295 VAL B C      1 
ATOM   5172 O O      . VAL B 2 295 ? 31.396 -3.499  67.104 1.00 32.46  ?  295 VAL B O      1 
ATOM   5173 C CB     . VAL B 2 295 ? 32.312 -1.111  64.802 1.00 26.58  ?  295 VAL B CB     1 
ATOM   5174 C CG1    . VAL B 2 295 ? 32.891 -0.582  66.100 1.00 26.61  ?  295 VAL B CG1    1 
ATOM   5175 C CG2    . VAL B 2 295 ? 33.337 -0.932  63.680 1.00 31.92  ?  295 VAL B CG2    1 
ATOM   5176 N N      . LEU B 2 296 ? 29.750 -2.321  66.114 1.00 32.92  ?  296 LEU B N      1 
ATOM   5177 C CA     . LEU B 2 296 ? 28.843 -2.343  67.257 1.00 35.00  ?  296 LEU B CA     1 
ATOM   5178 C C      . LEU B 2 296 ? 28.544 -3.751  67.751 1.00 34.39  ?  296 LEU B C      1 
ATOM   5179 O O      . LEU B 2 296 ? 28.451 -3.982  68.959 1.00 45.24  ?  296 LEU B O      1 
ATOM   5180 C CB     . LEU B 2 296 ? 27.533 -1.670  66.869 1.00 35.17  ?  296 LEU B CB     1 
ATOM   5181 C CG     . LEU B 2 296 ? 27.659 -0.174  66.887 1.00 34.54  ?  296 LEU B CG     1 
ATOM   5182 C CD1    . LEU B 2 296 ? 26.461 0.380   66.183 1.00 28.30  ?  296 LEU B CD1    1 
ATOM   5183 C CD2    . LEU B 2 296 ? 27.748 0.263   68.353 1.00 35.02  ?  296 LEU B CD2    1 
ATOM   5184 N N      . THR B 2 297 ? 28.314 -4.682  66.835 1.00 21.22  ?  297 THR B N      1 
ATOM   5185 C CA     . THR B 2 297 ? 27.823 -6.013  67.149 1.00 22.03  ?  297 THR B CA     1 
ATOM   5186 C C      . THR B 2 297 ? 28.901 -6.955  67.669 1.00 26.81  ?  297 THR B C      1 
ATOM   5187 O O      . THR B 2 297 ? 28.572 -8.085  68.048 1.00 34.63  ?  297 THR B O      1 
ATOM   5188 C CB     . THR B 2 297 ? 27.172 -6.636  65.897 1.00 29.48  ?  297 THR B CB     1 
ATOM   5189 O OG1    . THR B 2 297 ? 28.161 -6.856  64.874 1.00 27.52  ?  297 THR B OG1    1 
ATOM   5190 C CG2    . THR B 2 297 ? 26.075 -5.732  65.353 1.00 26.55  ?  297 THR B CG2    1 
ATOM   5191 N N      . GLU B 2 298 ? 30.169 -6.559  67.665 1.00 26.57  ?  298 GLU B N      1 
ATOM   5192 C CA     . GLU B 2 298 ? 31.144 -7.402  68.322 1.00 25.42  ?  298 GLU B CA     1 
ATOM   5193 C C      . GLU B 2 298 ? 30.667 -7.653  69.746 1.00 26.31  ?  298 GLU B C      1 
ATOM   5194 O O      . GLU B 2 298 ? 30.212 -6.719  70.420 1.00 27.77  ?  298 GLU B O      1 
ATOM   5195 C CB     . GLU B 2 298 ? 32.540 -6.776  68.334 1.00 25.23  ?  298 GLU B CB     1 
ATOM   5196 C CG     . GLU B 2 298 ? 33.582 -7.785  68.798 1.00 29.79  ?  298 GLU B CG     1 
ATOM   5197 C CD     . GLU B 2 298 ? 35.023 -7.384  68.507 1.00 36.72  ?  298 GLU B CD     1 
ATOM   5198 O OE1    . GLU B 2 298 ? 35.256 -6.373  67.821 1.00 35.61  ?  298 GLU B OE1    1 
ATOM   5199 O OE2    . GLU B 2 298 ? 35.936 -8.099  68.965 1.00 43.57  -1 298 GLU B OE2    1 
ATOM   5200 N N      . PRO B 2 299 ? 30.769 -8.885  70.230 1.00 28.50  ?  299 PRO B N      1 
ATOM   5201 C CA     . PRO B 2 299 ? 30.152 -9.236  71.535 1.00 35.64  ?  299 PRO B CA     1 
ATOM   5202 C C      . PRO B 2 299 ? 30.484 -8.318  72.717 1.00 37.54  ?  299 PRO B C      1 
ATOM   5203 O O      . PRO B 2 299 ? 29.560 -7.913  73.440 1.00 33.59  ?  299 PRO B O      1 
ATOM   5204 C CB     . PRO B 2 299 ? 30.664 -10.668 71.768 1.00 31.77  ?  299 PRO B CB     1 
ATOM   5205 C CG     . PRO B 2 299 ? 30.916 -11.202 70.351 1.00 29.83  ?  299 PRO B CG     1 
ATOM   5206 C CD     . PRO B 2 299 ? 31.443 -10.015 69.581 1.00 25.85  ?  299 PRO B CD     1 
ATOM   5207 N N      . PHE B 2 300 ? 31.765 -7.965  72.932 1.00 28.10  ?  300 PHE B N      1 
ATOM   5208 C CA     . PHE B 2 300 ? 32.136 -7.196  74.122 1.00 22.54  ?  300 PHE B CA     1 
ATOM   5209 C C      . PHE B 2 300 ? 31.364 -5.882  74.206 1.00 25.66  ?  300 PHE B C      1 
ATOM   5210 O O      . PHE B 2 300 ? 30.984 -5.452  75.302 1.00 32.17  ?  300 PHE B O      1 
ATOM   5211 C CB     . PHE B 2 300 ? 33.656 -6.959  74.155 1.00 22.56  ?  300 PHE B CB     1 
ATOM   5212 C CG     . PHE B 2 300 ? 34.129 -5.802  73.319 1.00 25.92  ?  300 PHE B CG     1 
ATOM   5213 C CD1    . PHE B 2 300 ? 34.436 -5.975  71.964 1.00 25.73  ?  300 PHE B CD1    1 
ATOM   5214 C CD2    . PHE B 2 300 ? 34.296 -4.533  73.891 1.00 24.24  ?  300 PHE B CD2    1 
ATOM   5215 C CE1    . PHE B 2 300 ? 34.901 -4.886  71.184 1.00 23.69  ?  300 PHE B CE1    1 
ATOM   5216 C CE2    . PHE B 2 300 ? 34.730 -3.456  73.137 1.00 21.97  ?  300 PHE B CE2    1 
ATOM   5217 C CZ     . PHE B 2 300 ? 35.046 -3.632  71.767 1.00 21.81  ?  300 PHE B CZ     1 
ATOM   5218 N N      . LEU B 2 301 ? 31.152 -5.222  73.057 1.00 42.07  ?  301 LEU B N      1 
ATOM   5219 C CA     . LEU B 2 301 ? 30.305 -4.032  72.959 1.00 37.63  ?  301 LEU B CA     1 
ATOM   5220 C C      . LEU B 2 301 ? 28.823 -4.364  73.059 1.00 42.12  ?  301 LEU B C      1 
ATOM   5221 O O      . LEU B 2 301 ? 28.032 -3.507  73.463 1.00 45.88  ?  301 LEU B O      1 
ATOM   5222 C CB     . LEU B 2 301 ? 30.536 -3.325  71.630 1.00 39.22  ?  301 LEU B CB     1 
ATOM   5223 C CG     . LEU B 2 301 ? 31.884 -2.690  71.343 1.00 47.88  ?  301 LEU B CG     1 
ATOM   5224 C CD1    . LEU B 2 301 ? 32.054 -2.546  69.835 1.00 48.82  ?  301 LEU B CD1    1 
ATOM   5225 C CD2    . LEU B 2 301 ? 31.951 -1.331  72.030 1.00 47.33  ?  301 LEU B CD2    1 
ATOM   5226 N N      . GLN B 2 302 ? 28.390 -5.537  72.643 1.00 53.17  ?  302 GLN B N      1 
ATOM   5227 C CA     . GLN B 2 302 ? 26.993 -5.912  72.782 1.00 54.49  ?  302 GLN B CA     1 
ATOM   5228 C C      . GLN B 2 302 ? 26.630 -6.041  74.211 1.00 49.74  ?  302 GLN B C      1 
ATOM   5229 O O      . GLN B 2 302 ? 25.516 -5.808  74.598 1.00 51.58  ?  302 GLN B O      1 
ATOM   5230 C CB     . GLN B 2 302 ? 26.690 -7.211  72.050 1.00 56.01  ?  302 GLN B CB     1 
ATOM   5231 C CG     . GLN B 2 302 ? 26.390 -6.989  70.597 1.00 64.80  ?  302 GLN B CG     1 
ATOM   5232 C CD     . GLN B 2 302 ? 25.372 -5.902  70.438 1.00 68.33  ?  302 GLN B CD     1 
ATOM   5233 O OE1    . GLN B 2 302 ? 25.646 -4.868  69.838 1.00 70.28  ?  302 GLN B OE1    1 
ATOM   5234 N NE2    . GLN B 2 302 ? 24.192 -6.111  71.008 1.00 65.68  ?  302 GLN B NE2    1 
ATOM   5235 N N      . SER B 2 303 ? 27.604 -6.334  75.007 1.00 31.22  ?  303 SER B N      1 
ATOM   5236 C CA     . SER B 2 303 ? 27.378 -6.488  76.377 1.00 38.23  ?  303 SER B CA     1 
ATOM   5237 C C      . SER B 2 303 ? 26.848 -5.225  76.977 1.00 47.27  ?  303 SER B C      1 
ATOM   5238 O O      . SER B 2 303 ? 25.973 -5.281  77.823 1.00 48.68  ?  303 SER B O      1 
ATOM   5239 C CB     . SER B 2 303 ? 28.695 -6.826  77.029 1.00 41.12  ?  303 SER B CB     1 
ATOM   5240 O OG     . SER B 2 303 ? 29.200 -8.062  76.580 1.00 43.78  ?  303 SER B OG     1 
ATOM   5241 N N      . ILE B 2 304 ? 27.344 -4.074  76.557 1.00 48.21  ?  304 ILE B N      1 
ATOM   5242 C CA     . ILE B 2 304 ? 26.945 -2.836  77.190 1.00 42.89  ?  304 ILE B CA     1 
ATOM   5243 C C      . ILE B 2 304 ? 25.480 -2.656  77.053 1.00 43.70  ?  304 ILE B C      1 
ATOM   5244 O O      . ILE B 2 304 ? 24.813 -2.284  78.002 1.00 48.78  ?  304 ILE B O      1 
ATOM   5245 C CB     . ILE B 2 304 ? 27.696 -1.627  76.595 1.00 40.41  ?  304 ILE B CB     1 
ATOM   5246 C CG1    . ILE B 2 304 ? 29.145 -1.620  77.072 1.00 40.32  ?  304 ILE B CG1    1 
ATOM   5247 C CG2    . ILE B 2 304 ? 27.071 -0.312  77.002 1.00 33.62  ?  304 ILE B CG2    1 
ATOM   5248 C CD1    . ILE B 2 304 ? 30.137 -2.213  76.105 1.00 34.63  ?  304 ILE B CD1    1 
ATOM   5249 N N      . PHE B 2 305 ? 24.971 -2.903  75.872 1.00 42.13  ?  305 PHE B N      1 
ATOM   5250 C CA     . PHE B 2 305 ? 23.554 -2.806  75.628 1.00 41.29  ?  305 PHE B CA     1 
ATOM   5251 C C      . PHE B 2 305 ? 22.744 -3.904  76.315 1.00 39.89  ?  305 PHE B C      1 
ATOM   5252 O O      . PHE B 2 305 ? 21.791 -3.638  77.006 1.00 37.94  ?  305 PHE B O      1 
ATOM   5253 C CB     . PHE B 2 305 ? 23.328 -2.829  74.112 1.00 36.23  ?  305 PHE B CB     1 
ATOM   5254 C CG     . PHE B 2 305 ? 24.100 -1.802  73.363 1.00 30.35  ?  305 PHE B CG     1 
ATOM   5255 C CD1    . PHE B 2 305 ? 23.690 -0.495  73.347 1.00 25.92  ?  305 PHE B CD1    1 
ATOM   5256 C CD2    . PHE B 2 305 ? 25.224 -2.152  72.652 1.00 32.79  ?  305 PHE B CD2    1 
ATOM   5257 C CE1    . PHE B 2 305 ? 24.396 0.454   72.653 1.00 27.93  ?  305 PHE B CE1    1 
ATOM   5258 C CE2    . PHE B 2 305 ? 25.936 -1.210  71.955 1.00 29.34  ?  305 PHE B CE2    1 
ATOM   5259 C CZ     . PHE B 2 305 ? 25.516 0.096   71.951 1.00 28.48  ?  305 PHE B CZ     1 
ATOM   5260 N N      . ASP B 2 306 ? 23.194 -5.130  76.204 1.00 56.76  ?  306 ASP B N      1 
ATOM   5261 C CA     . ASP B 2 306 ? 22.457 -6.246  76.750 1.00 61.31  ?  306 ASP B CA     1 
ATOM   5262 C C      . ASP B 2 306 ? 22.288 -6.199  78.243 1.00 58.92  ?  306 ASP B C      1 
ATOM   5263 O O      . ASP B 2 306 ? 21.215 -6.465  78.753 1.00 66.01  ?  306 ASP B O      1 
ATOM   5264 C CB     . ASP B 2 306 ? 23.142 -7.579  76.398 1.00 64.26  ?  306 ASP B CB     1 
ATOM   5265 C CG     . ASP B 2 306 ? 23.166 -7.874  74.923 1.00 68.78  ?  306 ASP B CG     1 
ATOM   5266 O OD1    . ASP B 2 306 ? 22.901 -6.968  74.113 1.00 70.42  ?  306 ASP B OD1    1 
ATOM   5267 O OD2    . ASP B 2 306 ? 23.476 -9.029  74.571 1.00 65.56  -1 306 ASP B OD2    1 
ATOM   5268 N N      . LYS B 2 307 ? 23.329 -5.864  78.959 1.00 54.12  ?  307 LYS B N      1 
ATOM   5269 C CA     . LYS B 2 307 ? 23.243 -5.869  80.400 1.00 55.47  ?  307 LYS B CA     1 
ATOM   5270 C C      . LYS B 2 307 ? 22.379 -4.746  80.859 1.00 60.49  ?  307 LYS B C      1 
ATOM   5271 O O      . LYS B 2 307 ? 21.985 -4.711  82.007 1.00 66.37  ?  307 LYS B O      1 
ATOM   5272 C CB     . LYS B 2 307 ? 24.612 -5.853  81.066 1.00 56.14  ?  307 LYS B CB     1 
ATOM   5273 C CG     . LYS B 2 307 ? 25.516 -7.005  80.646 1.00 54.84  ?  307 LYS B CG     1 
ATOM   5274 C CD     . LYS B 2 307 ? 26.868 -6.957  81.337 1.00 58.23  ?  307 LYS B CD     1 
ATOM   5275 C CE     . LYS B 2 307 ? 26.764 -7.384  82.794 1.00 62.66  ?  307 LYS B CE     1 
ATOM   5276 N NZ     . LYS B 2 307 ? 28.049 -7.242  83.534 1.00 60.88  ?  307 LYS B NZ     1 
ATOM   5277 N N      . ALA B 2 308 ? 22.120 -3.783  79.996 1.00 56.12  ?  308 ALA B N      1 
ATOM   5278 C CA     . ALA B 2 308 ? 21.198 -2.723  80.335 1.00 54.41  ?  308 ALA B CA     1 
ATOM   5279 C C      . ALA B 2 308 ? 19.846 -2.966  79.672 1.00 56.94  ?  308 ALA B C      1 
ATOM   5280 O O      . ALA B 2 308 ? 18.960 -2.127  79.769 1.00 52.68  ?  308 ALA B O      1 
ATOM   5281 C CB     . ALA B 2 308 ? 21.768 -1.400  79.910 1.00 48.76  ?  308 ALA B CB     1 
ATOM   5282 N N      . ASN B 2 309 ? 19.674 -4.116  79.037 1.00 54.18  ?  309 ASN B N      1 
ATOM   5283 C CA     . ASN B 2 309 ? 18.441 -4.438  78.296 1.00 52.88  ?  309 ASN B CA     1 
ATOM   5284 C C      . ASN B 2 309 ? 18.093 -3.568  77.122 1.00 43.42  ?  309 ASN B C      1 
ATOM   5285 O O      . ASN B 2 309 ? 16.945 -3.199  76.938 1.00 42.16  ?  309 ASN B O      1 
ATOM   5286 C CB     . ASN B 2 309 ? 17.245 -4.705  79.225 1.00 58.93  ?  309 ASN B CB     1 
ATOM   5287 C CG     . ASN B 2 309 ? 17.343 -6.033  79.938 1.00 61.27  ?  309 ASN B CG     1 
ATOM   5288 O OD1    . ASN B 2 309 ? 16.605 -6.959  79.630 1.00 63.25  ?  309 ASN B OD1    1 
ATOM   5289 N ND2    . ASN B 2 309 ? 18.255 -6.133  80.895 1.00 61.45  ?  309 ASN B ND2    1 
ATOM   5290 N N      . ILE B 2 310 ? 19.100 -3.218  76.343 1.00 41.17  ?  310 ILE B N      1 
ATOM   5291 C CA     . ILE B 2 310 ? 18.868 -2.488  75.112 1.00 41.08  ?  310 ILE B CA     1 
ATOM   5292 C C      . ILE B 2 310 ? 19.097 -3.394  73.905 1.00 40.58  ?  310 ILE B C      1 
ATOM   5293 O O      . ILE B 2 310 ? 20.208 -3.799  73.644 1.00 43.63  ?  310 ILE B O      1 
ATOM   5294 C CB     . ILE B 2 310 ? 19.723 -1.220  75.035 1.00 40.94  ?  310 ILE B CB     1 
ATOM   5295 C CG1    . ILE B 2 310 ? 19.453 -0.319  76.225 1.00 38.09  ?  310 ILE B CG1    1 
ATOM   5296 C CG2    . ILE B 2 310 ? 19.475 -0.468  73.741 1.00 37.86  ?  310 ILE B CG2    1 
ATOM   5297 C CD1    . ILE B 2 310 ? 20.327 0.907   76.230 1.00 42.04  ?  310 ILE B CD1    1 
ATOM   5298 N N      . LYS B 2 311 ? 18.041 -3.756  73.200 1.00 33.04  ?  311 LYS B N      1 
ATOM   5299 C CA     . LYS B 2 311 ? 18.120 -4.568  71.987 1.00 38.05  ?  311 LYS B CA     1 
ATOM   5300 C C      . LYS B 2 311 ? 18.063 -3.623  70.785 1.00 42.19  ?  311 LYS B C      1 
ATOM   5301 O O      . LYS B 2 311 ? 17.034 -2.993  70.517 1.00 38.94  ?  311 LYS B O      1 
ATOM   5302 C CB     . LYS B 2 311 ? 17.004 -5.612  71.930 1.00 33.83  ?  311 LYS B CB     1 
ATOM   5303 C CG     . LYS B 2 311 ? 17.052 -6.419  70.650 1.00 37.14  ?  311 LYS B CG     1 
ATOM   5304 C CD     . LYS B 2 311 ? 16.007 -7.527  70.617 1.00 39.25  ?  311 LYS B CD     1 
ATOM   5305 C CE     . LYS B 2 311 ? 16.218 -8.418  69.419 1.00 33.69  ?  311 LYS B CE     1 
ATOM   5306 N NZ     . LYS B 2 311 ? 17.674 -8.706  69.225 1.00 33.81  ?  311 LYS B NZ     1 
ATOM   5307 N N      . LEU B 2 312 ? 19.176 -3.521  70.072 1.00 32.12  ?  312 LEU B N      1 
ATOM   5308 C CA     . LEU B 2 312 ? 19.316 -2.557  68.994 1.00 31.57  ?  312 LEU B CA     1 
ATOM   5309 C C      . LEU B 2 312 ? 18.784 -3.138  67.678 1.00 36.61  ?  312 LEU B C      1 
ATOM   5310 O O      . LEU B 2 312 ? 19.010 -4.312  67.361 1.00 39.43  ?  312 LEU B O      1 
ATOM   5311 C CB     . LEU B 2 312 ? 20.788 -2.139  68.863 1.00 27.78  ?  312 LEU B CB     1 
ATOM   5312 C CG     . LEU B 2 312 ? 21.255 -1.007  69.775 1.00 23.51  ?  312 LEU B CG     1 
ATOM   5313 C CD1    . LEU B 2 312 ? 22.612 -0.458  69.334 1.00 21.28  ?  312 LEU B CD1    1 
ATOM   5314 C CD2    . LEU B 2 312 ? 20.173 0.104   69.841 1.00 21.50  ?  312 LEU B CD2    1 
ATOM   5315 N N      . ASN B 2 313 ? 18.046 -2.319  66.926 1.00 43.17  ?  313 ASN B N      1 
ATOM   5316 C CA     . ASN B 2 313 ? 17.563 -2.760  65.625 1.00 39.02  ?  313 ASN B CA     1 
ATOM   5317 C C      . ASN B 2 313 ? 18.551 -2.454  64.503 1.00 37.09  ?  313 ASN B C      1 
ATOM   5318 O O      . ASN B 2 313 ? 18.378 -2.974  63.399 1.00 39.51  ?  313 ASN B O      1 
ATOM   5319 C CB     . ASN B 2 313 ? 16.161 -2.165  65.326 1.00 34.54  ?  313 ASN B CB     1 
ATOM   5320 C CG     . ASN B 2 313 ? 16.121 -0.619  65.306 1.00 37.03  ?  313 ASN B CG     1 
ATOM   5321 O OD1    . ASN B 2 313 ? 17.097 0.049   64.979 1.00 43.96  ?  313 ASN B OD1    1 
ATOM   5322 N ND2    . ASN B 2 313 ? 14.960 -0.064  65.628 1.00 33.39  ?  313 ASN B ND2    1 
ATOM   5323 N N      . TYR B 2 314 ? 19.590 -1.659  64.773 1.00 31.59  ?  314 TYR B N      1 
ATOM   5324 C CA     . TYR B 2 314 ? 20.643 -1.373  63.799 1.00 34.81  ?  314 TYR B CA     1 
ATOM   5325 C C      . TYR B 2 314 ? 20.080 -0.900  62.469 1.00 32.06  ?  314 TYR B C      1 
ATOM   5326 O O      . TYR B 2 314 ? 20.469 -1.384  61.407 1.00 35.33  ?  314 TYR B O      1 
ATOM   5327 C CB     . TYR B 2 314 ? 21.524 -2.597  63.551 1.00 40.53  ?  314 TYR B CB     1 
ATOM   5328 C CG     . TYR B 2 314 ? 22.071 -3.241  64.776 1.00 37.95  ?  314 TYR B CG     1 
ATOM   5329 C CD1    . TYR B 2 314 ? 23.142 -2.680  65.444 1.00 36.54  ?  314 TYR B CD1    1 
ATOM   5330 C CD2    . TYR B 2 314 ? 21.536 -4.435  65.250 1.00 38.91  ?  314 TYR B CD2    1 
ATOM   5331 C CE1    . TYR B 2 314 ? 23.666 -3.272  66.569 1.00 38.01  ?  314 TYR B CE1    1 
ATOM   5332 C CE2    . TYR B 2 314 ? 22.040 -5.035  66.373 1.00 36.27  ?  314 TYR B CE2    1 
ATOM   5333 C CZ     . TYR B 2 314 ? 23.111 -4.443  67.036 1.00 43.62  ?  314 TYR B CZ     1 
ATOM   5334 O OH     . TYR B 2 314 ? 23.641 -5.021  68.168 1.00 52.40  ?  314 TYR B OH     1 
ATOM   5335 N N      . GLY B 2 315 ? 19.114 -0.037  62.520 1.00 36.62  ?  315 GLY B N      1 
ATOM   5336 C CA     . GLY B 2 315 ? 18.499 0.474   61.324 1.00 41.41  ?  315 GLY B CA     1 
ATOM   5337 C C      . GLY B 2 315 ? 17.586 -0.411  60.523 1.00 48.75  ?  315 GLY B C      1 
ATOM   5338 O O      . GLY B 2 315 ? 17.254 -0.070  59.403 1.00 53.11  ?  315 GLY B O      1 
ATOM   5339 N N      . VAL B 2 316 ? 17.157 -1.536  61.056 1.00 32.06  ?  316 VAL B N      1 
ATOM   5340 C CA     . VAL B 2 316 ? 16.364 -2.398  60.220 1.00 31.15  ?  316 VAL B CA     1 
ATOM   5341 C C      . VAL B 2 316 ? 14.972 -1.880  60.201 1.00 34.29  ?  316 VAL B C      1 
ATOM   5342 O O      . VAL B 2 316 ? 14.284 -1.885  61.196 1.00 33.82  ?  316 VAL B O      1 
ATOM   5343 C CB     . VAL B 2 316 ? 16.472 -3.872  60.586 1.00 26.18  ?  316 VAL B CB     1 
ATOM   5344 C CG1    . VAL B 2 316 ? 15.497 -4.708  59.786 1.00 22.86  ?  316 VAL B CG1    1 
ATOM   5345 C CG2    . VAL B 2 316 ? 17.893 -4.334  60.369 1.00 22.89  ?  316 VAL B CG2    1 
ATOM   5346 N N      . LEU B 2 317 ? 14.545 -1.437  59.043 1.00 31.59  ?  317 LEU B N      1 
ATOM   5347 C CA     . LEU B 2 317 ? 13.259 -0.852  58.918 1.00 27.41  ?  317 LEU B CA     1 
ATOM   5348 C C      . LEU B 2 317 ? 12.217 -1.842  58.487 1.00 30.39  ?  317 LEU B C      1 
ATOM   5349 O O      . LEU B 2 317 ? 12.511 -2.970  58.152 1.00 26.71  ?  317 LEU B O      1 
ATOM   5350 C CB     . LEU B 2 317 ? 13.362 0.327   57.946 1.00 27.77  ?  317 LEU B CB     1 
ATOM   5351 C CG     . LEU B 2 317 ? 14.269 1.517   58.217 1.00 26.77  ?  317 LEU B CG     1 
ATOM   5352 C CD1    . LEU B 2 317 ? 14.340 2.396   56.986 1.00 20.82  ?  317 LEU B CD1    1 
ATOM   5353 C CD2    . LEU B 2 317 ? 13.745 2.298   59.404 1.00 29.17  ?  317 LEU B CD2    1 
ATOM   5354 N N      . ASP B 2 318 ? 10.974 -1.423  58.551 1.00 51.92  ?  318 ASP B N      1 
ATOM   5355 C CA     . ASP B 2 318 ? 9.893  -2.282  58.155 1.00 57.40  ?  318 ASP B CA     1 
ATOM   5356 C C      . ASP B 2 318 ? 9.884  -2.607  56.687 1.00 59.64  ?  318 ASP B C      1 
ATOM   5357 O O      . ASP B 2 318 ? 9.722  -3.752  56.309 1.00 61.37  ?  318 ASP B O      1 
ATOM   5358 C CB     . ASP B 2 318 ? 8.587  -1.575  58.491 1.00 65.81  ?  318 ASP B CB     1 
ATOM   5359 C CG     . ASP B 2 318 ? 8.309  -1.500  59.991 1.00 76.96  ?  318 ASP B CG     1 
ATOM   5360 O OD1    . ASP B 2 318 ? 8.975  -2.236  60.748 1.00 79.31  ?  318 ASP B OD1    1 
ATOM   5361 O OD2    . ASP B 2 318 ? 7.445  -0.714  60.431 1.00 79.97  -1 318 ASP B OD2    1 
ATOM   5362 N N      . ASP B 2 319 ? 10.102 -1.611  55.859 1.00 50.49  ?  319 ASP B N      1 
ATOM   5363 C CA     . ASP B 2 319 ? 10.044 -1.774  54.433 1.00 52.07  ?  319 ASP B CA     1 
ATOM   5364 C C      . ASP B 2 319 ? 11.289 -1.178  53.825 1.00 54.09  ?  319 ASP B C      1 
ATOM   5365 O O      . ASP B 2 319 ? 11.706 -0.104  54.211 1.00 56.60  ?  319 ASP B O      1 
ATOM   5366 C CB     . ASP B 2 319 ? 8.822  -0.995  53.968 1.00 54.25  ?  319 ASP B CB     1 
ATOM   5367 C CG     . ASP B 2 319 ? 8.703  -0.885  52.486 1.00 62.95  ?  319 ASP B CG     1 
ATOM   5368 O OD1    . ASP B 2 319 ? 9.242  0.079   51.917 1.00 68.80  ?  319 ASP B OD1    1 
ATOM   5369 O OD2    . ASP B 2 319 ? 8.017  -1.733  51.892 1.00 66.64  -1 319 ASP B OD2    1 
ATOM   5370 N N      . THR B 2 320 ? 11.913 -1.880  52.909 1.00 40.38  ?  320 THR B N      1 
ATOM   5371 C CA     . THR B 2 320 ? 13.046 -1.349  52.200 1.00 36.32  ?  320 THR B CA     1 
ATOM   5372 C C      . THR B 2 320 ? 12.663 -1.296  50.757 1.00 38.41  ?  320 THR B C      1 
ATOM   5373 O O      . THR B 2 320 ? 13.518 -1.174  49.922 1.00 41.85  ?  320 THR B O      1 
ATOM   5374 C CB     . THR B 2 320 ? 14.277 -2.225  52.361 1.00 39.06  ?  320 THR B CB     1 
ATOM   5375 O OG1    . THR B 2 320 ? 13.910 -3.605  52.286 1.00 39.11  ?  320 THR B OG1    1 
ATOM   5376 C CG2    . THR B 2 320 ? 14.946 -1.945  53.697 1.00 35.74  ?  320 THR B CG2    1 
ATOM   5377 N N      . HIS B 2 321 ? 11.385 -1.393  50.457 1.00 38.85  ?  321 HIS B N      1 
ATOM   5378 C CA     . HIS B 2 321 ? 10.912 -1.476  49.075 1.00 44.40  ?  321 HIS B CA     1 
ATOM   5379 C C      . HIS B 2 321 ? 11.241 -0.378  48.062 1.00 37.34  ?  321 HIS B C      1 
ATOM   5380 O O      . HIS B 2 321 ? 11.728 -0.641  46.990 1.00 30.60  ?  321 HIS B O      1 
ATOM   5381 C CB     . HIS B 2 321 ? 9.407  -1.753  49.083 1.00 45.62  ?  321 HIS B CB     1 
ATOM   5382 C CG     . HIS B 2 321 ? 8.849  -2.144  47.751 1.00 53.78  ?  321 HIS B CG     1 
ATOM   5383 N ND1    . HIS B 2 321 ? 9.090  -3.370  47.177 1.00 55.18  ?  321 HIS B ND1    1 
ATOM   5384 C CD2    . HIS B 2 321 ? 8.042  -1.478  46.893 1.00 58.69  ?  321 HIS B CD2    1 
ATOM   5385 C CE1    . HIS B 2 321 ? 8.465  -3.442  46.016 1.00 58.67  ?  321 HIS B CE1    1 
ATOM   5386 N NE2    . HIS B 2 321 ? 7.823  -2.306  45.821 1.00 62.21  ?  321 HIS B NE2    1 
ATOM   5387 N N      . ALA B 2 322 ? 10.915 0.842   48.410 1.00 26.33  ?  322 ALA B N      1 
ATOM   5388 C CA     . ALA B 2 322 ? 11.210 1.950   47.503 1.00 25.82  ?  322 ALA B CA     1 
ATOM   5389 C C      . ALA B 2 322 ? 12.683 1.966   47.098 1.00 33.74  ?  322 ALA B C      1 
ATOM   5390 O O      . ALA B 2 322 ? 13.015 2.251   45.937 1.00 39.87  ?  322 ALA B O      1 
ATOM   5391 C CB     . ALA B 2 322 ? 10.815 3.290   48.132 1.00 20.96  ?  322 ALA B CB     1 
ATOM   5392 N N      . GLU B 2 323 ? 13.590 1.685   48.042 1.00 33.08  ?  323 GLU B N      1 
ATOM   5393 C CA     . GLU B 2 323 ? 15.000 1.682   47.670 1.00 26.09  ?  323 GLU B CA     1 
ATOM   5394 C C      . GLU B 2 323 ? 15.369 0.379   46.986 1.00 27.17  ?  323 GLU B C      1 
ATOM   5395 O O      . GLU B 2 323 ? 16.210 0.381   46.086 1.00 40.75  ?  323 GLU B O      1 
ATOM   5396 C CB     . GLU B 2 323 ? 15.910 1.970   48.886 1.00 23.82  ?  323 GLU B CB     1 
ATOM   5397 C CG     . GLU B 2 323 ? 15.710 1.077   50.129 1.00 32.54  ?  323 GLU B CG     1 
ATOM   5398 C CD     . GLU B 2 323 ? 14.812 1.710   51.234 1.00 36.61  ?  323 GLU B CD     1 
ATOM   5399 O OE1    . GLU B 2 323 ? 13.572 1.814   51.059 1.00 38.51  ?  323 GLU B OE1    1 
ATOM   5400 O OE2    . GLU B 2 323 ? 15.354 2.104   52.292 1.00 30.16  -1 323 GLU B OE2    1 
ATOM   5401 N N      . PHE B 2 324 ? 14.731 -0.730  47.364 1.00 23.21  ?  324 PHE B N      1 
ATOM   5402 C CA     . PHE B 2 324 ? 14.955 -1.983  46.655 1.00 25.86  ?  324 PHE B CA     1 
ATOM   5403 C C      . PHE B 2 324 ? 14.579 -1.820  45.194 1.00 31.83  ?  324 PHE B C      1 
ATOM   5404 O O      . PHE B 2 324 ? 15.383 -2.105  44.301 1.00 40.36  ?  324 PHE B O      1 
ATOM   5405 C CB     . PHE B 2 324 ? 14.152 -3.106  47.315 1.00 23.94  ?  324 PHE B CB     1 
ATOM   5406 C CG     . PHE B 2 324 ? 14.620 -4.525  46.977 1.00 31.55  ?  324 PHE B CG     1 
ATOM   5407 C CD1    . PHE B 2 324 ? 15.712 -5.092  47.612 1.00 26.72  ?  324 PHE B CD1    1 
ATOM   5408 C CD2    . PHE B 2 324 ? 13.911 -5.317  46.076 1.00 37.07  ?  324 PHE B CD2    1 
ATOM   5409 C CE1    . PHE B 2 324 ? 16.108 -6.405  47.339 1.00 27.15  ?  324 PHE B CE1    1 
ATOM   5410 C CE2    . PHE B 2 324 ? 14.307 -6.631  45.797 1.00 36.60  ?  324 PHE B CE2    1 
ATOM   5411 C CZ     . PHE B 2 324 ? 15.403 -7.175  46.433 1.00 32.03  ?  324 PHE B CZ     1 
ATOM   5412 N N      . ARG B 2 325 ? 13.375 -1.302  44.930 1.00 41.30  ?  325 ARG B N      1 
ATOM   5413 C CA     . ARG B 2 325 ? 12.944 -1.111  43.550 1.00 46.49  ?  325 ARG B CA     1 
ATOM   5414 C C      . ARG B 2 325 ? 13.797 -0.081  42.822 1.00 44.58  ?  325 ARG B C      1 
ATOM   5415 O O      . ARG B 2 325 ? 14.004 -0.213  41.604 1.00 44.32  ?  325 ARG B O      1 
ATOM   5416 C CB     . ARG B 2 325 ? 11.469 -0.717  43.498 1.00 47.75  ?  325 ARG B CB     1 
ATOM   5417 C CG     . ARG B 2 325 ? 10.506 -1.902  43.413 1.00 52.56  ?  325 ARG B CG     1 
ATOM   5418 C CD     . ARG B 2 325 ? 10.559 -2.617  42.065 1.00 57.34  ?  325 ARG B CD     1 
ATOM   5419 N NE     . ARG B 2 325 ? 10.167 -1.749  40.957 1.00 62.77  ?  325 ARG B NE     1 
ATOM   5420 C CZ     . ARG B 2 325 ? 11.020 -1.008  40.256 1.00 66.49  ?  325 ARG B CZ     1 
ATOM   5421 N NH1    . ARG B 2 325 ? 12.311 -1.035  40.551 1.00 64.91  ?  325 ARG B NH1    1 
ATOM   5422 N NH2    . ARG B 2 325 ? 10.586 -0.241  39.265 1.00 67.91  ?  325 ARG B NH2    1 
ATOM   5423 N N      . LYS B 2 326 ? 14.377 0.886   43.509 1.00 35.13  ?  326 LYS B N      1 
ATOM   5424 C CA     . LYS B 2 326 ? 15.159 1.876   42.796 1.00 38.32  ?  326 LYS B CA     1 
ATOM   5425 C C      . LYS B 2 326 ? 16.522 1.341   42.452 1.00 39.10  ?  326 LYS B C      1 
ATOM   5426 O O      . LYS B 2 326 ? 17.069 1.664   41.421 1.00 35.56  ?  326 LYS B O      1 
ATOM   5427 C CB     . LYS B 2 326 ? 15.191 3.204   43.511 1.00 37.53  ?  326 LYS B CB     1 
ATOM   5428 C CG     . LYS B 2 326 ? 13.886 3.964   43.442 1.00 35.43  ?  326 LYS B CG     1 
ATOM   5429 C CD     . LYS B 2 326 ? 14.065 5.360   43.991 1.00 37.84  ?  326 LYS B CD     1 
ATOM   5430 C CE     . LYS B 2 326 ? 15.195 6.054   43.259 1.00 43.14  ?  326 LYS B CE     1 
ATOM   5431 N NZ     . LYS B 2 326 ? 15.206 7.515   43.519 1.00 49.16  ?  326 LYS B NZ     1 
ATOM   5432 N N      . ALA B 2 327 ? 17.079 0.516   43.304 1.00 38.40  ?  327 ALA B N      1 
ATOM   5433 C CA     . ALA B 2 327 ? 18.316 -0.168  42.983 1.00 38.24  ?  327 ALA B CA     1 
ATOM   5434 C C      . ALA B 2 327 ? 18.124 -1.146  41.835 1.00 41.67  ?  327 ALA B C      1 
ATOM   5435 O O      . ALA B 2 327 ? 19.042 -1.417  41.115 1.00 36.21  ?  327 ALA B O      1 
ATOM   5436 C CB     . ALA B 2 327 ? 18.821 -0.867  44.196 1.00 36.54  ?  327 ALA B CB     1 
ATOM   5437 N N      . GLN B 2 328 ? 16.947 -1.727  41.718 1.00 52.53  ?  328 GLN B N      1 
ATOM   5438 C CA     . GLN B 2 328 ? 16.618 -2.603  40.617 1.00 49.59  ?  328 GLN B CA     1 
ATOM   5439 C C      . GLN B 2 328 ? 16.637 -1.918  39.275 1.00 53.19  ?  328 GLN B C      1 
ATOM   5440 O O      . GLN B 2 328 ? 17.103 -2.486  38.315 1.00 50.80  ?  328 GLN B O      1 
ATOM   5441 C CB     . GLN B 2 328 ? 15.240 -3.147  40.881 1.00 53.90  ?  328 GLN B CB     1 
ATOM   5442 C CG     . GLN B 2 328 ? 15.219 -4.293  41.870 1.00 64.28  ?  328 GLN B CG     1 
ATOM   5443 C CD     . GLN B 2 328 ? 13.845 -4.883  42.073 1.00 67.11  ?  328 GLN B CD     1 
ATOM   5444 O OE1    . GLN B 2 328 ? 12.867 -4.335  41.614 1.00 73.10  ?  328 GLN B OE1    1 
ATOM   5445 N NE2    . GLN B 2 328 ? 13.771 -6.012  42.752 1.00 59.32  ?  328 GLN B NE2    1 
ATOM   5446 N N      . ASP B 2 329 ? 16.164 -0.685  39.209 1.00 48.01  ?  329 ASP B N      1 
ATOM   5447 C CA     . ASP B 2 329 ? 16.205 0.089   37.974 1.00 41.74  ?  329 ASP B CA     1 
ATOM   5448 C C      . ASP B 2 329 ? 17.628 0.455   37.580 1.00 39.92  ?  329 ASP B C      1 
ATOM   5449 O O      . ASP B 2 329 ? 17.955 0.502   36.411 1.00 46.20  ?  329 ASP B O      1 
ATOM   5450 C CB     . ASP B 2 329 ? 15.366 1.360   38.142 1.00 40.97  ?  329 ASP B CB     1 
ATOM   5451 C CG     . ASP B 2 329 ? 13.900 1.121   38.004 1.00 50.26  ?  329 ASP B CG     1 
ATOM   5452 O OD1    . ASP B 2 329 ? 13.491 0.503   37.009 1.00 48.12  ?  329 ASP B OD1    1 
ATOM   5453 O OD2    . ASP B 2 329 ? 13.146 1.578   38.882 1.00 54.66  -1 329 ASP B OD2    1 
ATOM   5454 N N      . TYR B 2 330 ? 18.472 0.687   38.549 1.00 26.09  ?  330 TYR B N      1 
ATOM   5455 C CA     . TYR B 2 330 ? 19.836 1.053   38.314 1.00 25.97  ?  330 TYR B CA     1 
ATOM   5456 C C      . TYR B 2 330 ? 20.633 -0.095  37.824 1.00 25.73  ?  330 TYR B C      1 
ATOM   5457 O O      . TYR B 2 330 ? 21.451 0.037   36.961 1.00 26.40  ?  330 TYR B O      1 
ATOM   5458 C CB     . TYR B 2 330 ? 20.384 1.496   39.657 1.00 31.70  ?  330 TYR B CB     1 
ATOM   5459 C CG     . TYR B 2 330 ? 21.810 1.964   39.717 1.00 32.23  ?  330 TYR B CG     1 
ATOM   5460 C CD1    . TYR B 2 330 ? 22.197 3.140   39.113 1.00 28.93  ?  330 TYR B CD1    1 
ATOM   5461 C CD2    . TYR B 2 330 ? 22.757 1.252   40.432 1.00 31.09  ?  330 TYR B CD2    1 
ATOM   5462 C CE1    . TYR B 2 330 ? 23.494 3.575   39.188 1.00 26.01  ?  330 TYR B CE1    1 
ATOM   5463 C CE2    . TYR B 2 330 ? 24.056 1.687   40.516 1.00 29.61  ?  330 TYR B CE2    1 
ATOM   5464 C CZ     . TYR B 2 330 ? 24.418 2.849   39.891 1.00 30.59  ?  330 TYR B CZ     1 
ATOM   5465 O OH     . TYR B 2 330 ? 25.721 3.278   39.968 1.00 30.67  ?  330 TYR B OH     1 
ATOM   5466 N N      . VAL B 2 331 ? 20.373 -1.242  38.384 1.00 28.04  ?  331 VAL B N      1 
ATOM   5467 C CA     . VAL B 2 331 ? 21.109 -2.390  38.009 1.00 33.34  ?  331 VAL B CA     1 
ATOM   5468 C C      . VAL B 2 331 ? 20.684 -2.761  36.622 1.00 37.50  ?  331 VAL B C      1 
ATOM   5469 O O      . VAL B 2 331 ? 21.510 -3.042  35.775 1.00 36.50  ?  331 VAL B O      1 
ATOM   5470 C CB     . VAL B 2 331 ? 20.906 -3.521  39.022 1.00 30.72  ?  331 VAL B CB     1 
ATOM   5471 C CG1    . VAL B 2 331 ? 21.518 -4.798  38.509 1.00 40.13  ?  331 VAL B CG1    1 
ATOM   5472 C CG2    . VAL B 2 331 ? 21.558 -3.164  40.310 1.00 23.74  ?  331 VAL B CG2    1 
ATOM   5473 N N      . PHE B 2 332 ? 19.398 -2.695  36.372 1.00 37.78  ?  332 PHE B N      1 
ATOM   5474 C CA     . PHE B 2 332 ? 18.878 -3.004  35.077 1.00 37.96  ?  332 PHE B CA     1 
ATOM   5475 C C      . PHE B 2 332 ? 19.504 -2.135  34.030 1.00 32.25  ?  332 PHE B C      1 
ATOM   5476 O O      . PHE B 2 332 ? 20.032 -2.629  33.073 1.00 38.43  ?  332 PHE B O      1 
ATOM   5477 C CB     . PHE B 2 332 ? 17.372 -2.836  35.150 1.00 41.89  ?  332 PHE B CB     1 
ATOM   5478 C CG     . PHE B 2 332 ? 16.650 -3.126  33.892 1.00 43.73  ?  332 PHE B CG     1 
ATOM   5479 C CD1    . PHE B 2 332 ? 16.231 -4.400  33.624 1.00 49.51  ?  332 PHE B CD1    1 
ATOM   5480 C CD2    . PHE B 2 332 ? 16.335 -2.110  33.010 1.00 46.26  ?  332 PHE B CD2    1 
ATOM   5481 C CE1    . PHE B 2 332 ? 15.543 -4.672  32.478 1.00 56.10  ?  332 PHE B CE1    1 
ATOM   5482 C CE2    . PHE B 2 332 ? 15.654 -2.372  31.852 1.00 53.72  ?  332 PHE B CE2    1 
ATOM   5483 C CZ     . PHE B 2 332 ? 15.250 -3.657  31.590 1.00 57.21  ?  332 PHE B CZ     1 
ATOM   5484 N N      . GLY B 2 333 ? 19.463 -0.842  34.216 1.00 39.15  ?  333 GLY B N      1 
ATOM   5485 C CA     . GLY B 2 333 ? 19.992 0.068   33.232 1.00 40.30  ?  333 GLY B CA     1 
ATOM   5486 C C      . GLY B 2 333 ? 21.479 0.073   33.036 1.00 44.01  ?  333 GLY B C      1 
ATOM   5487 O O      . GLY B 2 333 ? 21.951 0.706   32.130 1.00 51.83  ?  333 GLY B O      1 
ATOM   5488 N N      . LEU B 2 334 ? 22.216 -0.623  33.872 1.00 37.30  ?  334 LEU B N      1 
ATOM   5489 C CA     . LEU B 2 334 ? 23.638 -0.616  33.768 1.00 41.74  ?  334 LEU B CA     1 
ATOM   5490 C C      . LEU B 2 334 ? 24.078 -1.855  33.117 1.00 48.68  ?  334 LEU B C      1 
ATOM   5491 O O      . LEU B 2 334 ? 25.108 -1.898  32.472 1.00 53.50  ?  334 LEU B O      1 
ATOM   5492 C CB     . LEU B 2 334 ? 24.262 -0.589  35.132 1.00 47.78  ?  334 LEU B CB     1 
ATOM   5493 C CG     . LEU B 2 334 ? 24.306 0.754   35.838 1.00 48.41  ?  334 LEU B CG     1 
ATOM   5494 C CD1    . LEU B 2 334 ? 25.305 0.708   36.975 1.00 53.21  ?  334 LEU B CD1    1 
ATOM   5495 C CD2    . LEU B 2 334 ? 24.600 1.853   34.834 1.00 44.98  ?  334 LEU B CD2    1 
ATOM   5496 N N      . THR B 2 335 ? 23.311 -2.894  33.306 1.00 44.94  ?  335 THR B N      1 
ATOM   5497 C CA     . THR B 2 335 ? 23.633 -4.146  32.717 1.00 40.17  ?  335 THR B CA     1 
ATOM   5498 C C      . THR B 2 335 ? 23.150 -4.186  31.262 1.00 43.47  ?  335 THR B C      1 
ATOM   5499 O O      . THR B 2 335 ? 23.743 -4.866  30.442 1.00 45.36  ?  335 THR B O      1 
ATOM   5500 C CB     . THR B 2 335 ? 23.027 -5.251  33.568 1.00 34.71  ?  335 THR B CB     1 
ATOM   5501 O OG1    . THR B 2 335 ? 21.710 -4.873  33.950 1.00 42.44  ?  335 THR B OG1    1 
ATOM   5502 C CG2    . THR B 2 335 ? 23.852 -5.482  34.804 1.00 35.79  ?  335 THR B CG2    1 
ATOM   5503 N N      . ILE B 2 336 ? 22.092 -3.463  30.933 1.00 36.40  ?  336 ILE B N      1 
ATOM   5504 C CA     . ILE B 2 336 ? 21.657 -3.413  29.560 1.00 43.31  ?  336 ILE B CA     1 
ATOM   5505 C C      . ILE B 2 336 ? 22.594 -2.488  28.834 1.00 47.00  ?  336 ILE B C      1 
ATOM   5506 O O      . ILE B 2 336 ? 22.826 -2.672  27.676 1.00 51.61  ?  336 ILE B O      1 
ATOM   5507 C CB     . ILE B 2 336 ? 20.205 -2.959  29.417 1.00 44.89  ?  336 ILE B CB     1 
ATOM   5508 C CG1    . ILE B 2 336 ? 19.295 -3.843  30.237 1.00 48.19  ?  336 ILE B CG1    1 
ATOM   5509 C CG2    . ILE B 2 336 ? 19.714 -3.143  27.996 1.00 44.34  ?  336 ILE B CG2    1 
ATOM   5510 C CD1    . ILE B 2 336 ? 18.501 -4.794  29.385 1.00 54.02  ?  336 ILE B CD1    1 
ATOM   5511 N N      . GLN B 2 337 ? 23.167 -1.513  29.526 1.00 50.50  ?  337 GLN B N      1 
ATOM   5512 C CA     . GLN B 2 337 ? 24.139 -0.613  28.945 1.00 46.34  ?  337 GLN B CA     1 
ATOM   5513 C C      . GLN B 2 337 ? 25.436 -1.327  28.721 1.00 47.11  ?  337 GLN B C      1 
ATOM   5514 O O      . GLN B 2 337 ? 26.179 -0.943  27.875 1.00 49.42  ?  337 GLN B O      1 
ATOM   5515 C CB     . GLN B 2 337 ? 24.317 0.591   29.867 1.00 39.24  ?  337 GLN B CB     1 
ATOM   5516 C CG     . GLN B 2 337 ? 25.561 1.434   29.733 1.00 41.14  ?  337 GLN B CG     1 
ATOM   5517 C CD     . GLN B 2 337 ? 25.232 2.837   29.316 1.00 50.71  ?  337 GLN B CD     1 
ATOM   5518 O OE1    . GLN B 2 337 ? 24.208 3.069   28.699 1.00 49.87  ?  337 GLN B OE1    1 
ATOM   5519 N NE2    . GLN B 2 337 ? 26.093 3.785   29.659 1.00 49.97  ?  337 GLN B NE2    1 
ATOM   5520 N N      . SER B 2 338 ? 25.678 -2.414  29.439 1.00 45.20  ?  338 SER B N      1 
ATOM   5521 C CA     . SER B 2 338 ? 26.881 -3.190  29.281 1.00 37.85  ?  338 SER B CA     1 
ATOM   5522 C C      . SER B 2 338 ? 26.715 -4.057  28.064 1.00 38.86  ?  338 SER B C      1 
ATOM   5523 O O      . SER B 2 338 ? 27.668 -4.354  27.392 1.00 37.82  ?  338 SER B O      1 
ATOM   5524 C CB     . SER B 2 338 ? 27.148 -4.005  30.555 1.00 31.55  ?  338 SER B CB     1 
ATOM   5525 O OG     . SER B 2 338 ? 28.506 -4.348  30.694 1.00 32.40  ?  338 SER B OG     1 
ATOM   5526 N N      . ALA B 2 339 ? 25.496 -4.463  27.790 1.00 38.61  ?  339 ALA B N      1 
ATOM   5527 C CA     . ALA B 2 339 ? 25.213 -5.261  26.626 1.00 32.82  ?  339 ALA B CA     1 
ATOM   5528 C C      . ALA B 2 339 ? 25.118 -4.307  25.497 1.00 35.86  ?  339 ALA B C      1 
ATOM   5529 O O      . ALA B 2 339 ? 25.494 -4.630  24.392 1.00 37.64  ?  339 ALA B O      1 
ATOM   5530 C CB     . ALA B 2 339 ? 23.914 -5.974  26.811 1.00 27.95  ?  339 ALA B CB     1 
ATOM   5531 N N      . MET B 2 340 ? 24.563 -3.136  25.757 1.00 45.54  ?  340 MET B N      1 
ATOM   5532 C CA     . MET B 2 340 ? 24.574 -2.096  24.737 1.00 43.32  ?  340 MET B CA     1 
ATOM   5533 C C      . MET B 2 340 ? 26.004 -1.770  24.321 1.00 44.13  ?  340 MET B C      1 
ATOM   5534 O O      . MET B 2 340 ? 26.339 -1.751  23.129 1.00 43.53  ?  340 MET B O      1 
ATOM   5535 C CB     . MET B 2 340 ? 23.856 -0.849  25.245 1.00 36.91  ?  340 MET B CB     1 
ATOM   5536 C CG     . MET B 2 340 ? 23.585 0.137   24.136 1.00 41.39  ?  340 MET B CG     1 
ATOM   5537 S SD     . MET B 2 340 ? 24.899 1.362   23.917 1.00 40.71  ?  340 MET B SD     1 
ATOM   5538 C CE     . MET B 2 340 ? 24.474 2.466   25.255 1.00 42.01  ?  340 MET B CE     1 
ATOM   5539 N N      . HIS B 2 341 ? 26.876 -1.554  25.303 1.00 31.76  ?  341 HIS B N      1 
ATOM   5540 C CA     . HIS B 2 341 ? 28.278 -1.321  24.989 1.00 30.24  ?  341 HIS B CA     1 
ATOM   5541 C C      . HIS B 2 341 ? 28.918 -2.524  24.313 1.00 26.65  ?  341 HIS B C      1 
ATOM   5542 O O      . HIS B 2 341 ? 29.742 -2.358  23.417 1.00 25.01  ?  341 HIS B O      1 
ATOM   5543 C CB     . HIS B 2 341 ? 29.029 -0.935  26.251 1.00 19.58  ?  341 HIS B CB     1 
ATOM   5544 C CG     . HIS B 2 341 ? 28.665 0.433   26.729 1.00 19.31  ?  341 HIS B CG     1 
ATOM   5545 N ND1    . HIS B 2 341 ? 29.071 0.944   27.943 1.00 21.08  ?  341 HIS B ND1    1 
ATOM   5546 C CD2    . HIS B 2 341 ? 27.894 1.389   26.156 1.00 20.83  ?  341 HIS B CD2    1 
ATOM   5547 C CE1    . HIS B 2 341 ? 28.585 2.164   28.083 1.00 30.56  ?  341 HIS B CE1    1 
ATOM   5548 N NE2    . HIS B 2 341 ? 27.871 2.458   27.011 1.00 27.75  ?  341 HIS B NE2    1 
ATOM   5549 N N      . HIS B 2 342 ? 28.551 -3.740  24.712 1.00 34.13  ?  342 HIS B N      1 
ATOM   5550 C CA     . HIS B 2 342 ? 29.187 -4.900  24.094 1.00 37.23  ?  342 HIS B CA     1 
ATOM   5551 C C      . HIS B 2 342 ? 28.841 -5.013  22.607 1.00 35.04  ?  342 HIS B C      1 
ATOM   5552 O O      . HIS B 2 342 ? 29.737 -5.209  21.777 1.00 31.50  ?  342 HIS B O      1 
ATOM   5553 C CB     . HIS B 2 342 ? 28.812 -6.182  24.829 1.00 40.39  ?  342 HIS B CB     1 
ATOM   5554 C CG     . HIS B 2 342 ? 29.253 -7.432  24.119 1.00 45.65  ?  342 HIS B CG     1 
ATOM   5555 N ND1    . HIS B 2 342 ? 28.379 -8.443  23.766 1.00 46.22  ?  342 HIS B ND1    1 
ATOM   5556 C CD2    . HIS B 2 342 ? 30.475 -7.829  23.686 1.00 45.34  ?  342 HIS B CD2    1 
ATOM   5557 C CE1    . HIS B 2 342 ? 29.043 -9.410  23.160 1.00 43.33  ?  342 HIS B CE1    1 
ATOM   5558 N NE2    . HIS B 2 342 ? 30.317 -9.063  23.099 1.00 46.12  ?  342 HIS B NE2    1 
ATOM   5559 N N      . GLU B 2 343 ? 27.550 -4.935  22.250 1.00 25.49  ?  343 GLU B N      1 
ATOM   5560 C CA     . GLU B 2 343 ? 27.192 -5.014  20.841 1.00 39.27  ?  343 GLU B CA     1 
ATOM   5561 C C      . GLU B 2 343 ? 27.844 -3.887  20.047 1.00 49.38  ?  343 GLU B C      1 
ATOM   5562 O O      . GLU B 2 343 ? 28.305 -4.093  18.913 1.00 51.87  ?  343 GLU B O      1 
ATOM   5563 C CB     . GLU B 2 343 ? 25.676 -4.956  20.654 1.00 40.06  ?  343 GLU B CB     1 
ATOM   5564 C CG     . GLU B 2 343 ? 25.308 -4.856  19.168 1.00 43.29  ?  343 GLU B CG     1 
ATOM   5565 C CD     . GLU B 2 343 ? 23.833 -4.676  18.925 1.00 46.85  ?  343 GLU B CD     1 
ATOM   5566 O OE1    . GLU B 2 343 ? 23.100 -4.557  19.929 1.00 54.11  ?  343 GLU B OE1    1 
ATOM   5567 O OE2    . GLU B 2 343 ? 23.412 -4.652  17.740 1.00 42.44  -1 343 GLU B OE2    1 
ATOM   5568 N N      . LEU B 2 344 ? 27.871 -2.682  20.629 1.00 38.31  ?  344 LEU B N      1 
ATOM   5569 C CA     . LEU B 2 344 ? 28.413 -1.516  19.948 1.00 31.74  ?  344 LEU B CA     1 
ATOM   5570 C C      . LEU B 2 344 ? 29.868 -1.732  19.535 1.00 30.45  ?  344 LEU B C      1 
ATOM   5571 O O      . LEU B 2 344 ? 30.230 -1.591  18.361 1.00 27.15  ?  344 LEU B O      1 
ATOM   5572 C CB     . LEU B 2 344 ? 28.272 -0.295  20.855 1.00 28.16  ?  344 LEU B CB     1 
ATOM   5573 C CG     . LEU B 2 344 ? 28.977 0.979   20.395 1.00 30.42  ?  344 LEU B CG     1 
ATOM   5574 C CD1    . LEU B 2 344 ? 28.557 1.401   18.966 1.00 30.24  ?  344 LEU B CD1    1 
ATOM   5575 C CD2    . LEU B 2 344 ? 28.729 2.085   21.390 1.00 27.92  ?  344 LEU B CD2    1 
ATOM   5576 N N      . GLN B 2 345 ? 30.728 -2.038  20.501 1.00 40.74  ?  345 GLN B N      1 
ATOM   5577 C CA     . GLN B 2 345 ? 32.127 -2.280  20.187 1.00 44.72  ?  345 GLN B CA     1 
ATOM   5578 C C      . GLN B 2 345 ? 32.285 -3.462  19.233 1.00 44.89  ?  345 GLN B C      1 
ATOM   5579 O O      . GLN B 2 345 ? 33.178 -3.459  18.381 1.00 45.72  ?  345 GLN B O      1 
ATOM   5580 C CB     . GLN B 2 345 ? 32.918 -2.487  21.492 1.00 47.88  ?  345 GLN B CB     1 
ATOM   5581 C CG     . GLN B 2 345 ? 33.041 -1.210  22.348 1.00 48.51  ?  345 GLN B CG     1 
ATOM   5582 C CD     . GLN B 2 345 ? 33.445 -1.460  23.799 1.00 53.76  ?  345 GLN B CD     1 
ATOM   5583 O OE1    . GLN B 2 345 ? 32.904 -2.342  24.469 1.00 53.09  ?  345 GLN B OE1    1 
ATOM   5584 N NE2    . GLN B 2 345 ? 34.385 -0.660  24.297 1.00 57.91  ?  345 GLN B NE2    1 
ATOM   5585 N N      . GLU B 2 346 ? 31.427 -4.469  19.343 1.00 51.36  ?  346 GLU B N      1 
ATOM   5586 C CA     . GLU B 2 346 ? 31.461 -5.549  18.375 1.00 54.84  ?  346 GLU B CA     1 
ATOM   5587 C C      . GLU B 2 346 ? 30.861 -5.159  17.033 1.00 57.31  ?  346 GLU B C      1 
ATOM   5588 O O      . GLU B 2 346 ? 31.076 -5.884  16.059 1.00 61.97  ?  346 GLU B O      1 
ATOM   5589 C CB     . GLU B 2 346 ? 30.774 -6.800  18.932 1.00 57.27  ?  346 GLU B CB     1 
ATOM   5590 C CG     . GLU B 2 346 ? 31.698 -7.611  19.842 1.00 61.95  ?  346 GLU B CG     1 
ATOM   5591 C CD     . GLU B 2 346 ? 31.339 -9.088  19.926 1.00 67.29  ?  346 GLU B CD     1 
ATOM   5592 O OE1    . GLU B 2 346 ? 30.230 -9.467  19.478 1.00 67.79  ?  346 GLU B OE1    1 
ATOM   5593 O OE2    . GLU B 2 346 ? 32.176 -9.870  20.449 1.00 67.08  -1 346 GLU B OE2    1 
ATOM   5594 N N      . ARG B 2 347 ? 30.293 -3.979  16.891 1.00 52.82  ?  347 ARG B N      1 
ATOM   5595 C CA     . ARG B 2 347 ? 29.857 -3.496  15.583 1.00 47.73  ?  347 ARG B CA     1 
ATOM   5596 C C      . ARG B 2 347 ? 30.988 -2.669  15.012 1.00 44.92  ?  347 ARG B C      1 
ATOM   5597 O O      . ARG B 2 347 ? 31.205 -2.637  13.821 1.00 53.70  ?  347 ARG B O      1 
ATOM   5598 C CB     . ARG B 2 347 ? 28.605 -2.630  15.684 1.00 49.24  ?  347 ARG B CB     1 
ATOM   5599 C CG     . ARG B 2 347 ? 28.034 -2.202  14.342 1.00 53.49  ?  347 ARG B CG     1 
ATOM   5600 C CD     . ARG B 2 347 ? 26.931 -1.166  14.464 1.00 56.78  ?  347 ARG B CD     1 
ATOM   5601 N NE     . ARG B 2 347 ? 25.597 -1.735  14.286 1.00 65.70  ?  347 ARG B NE     1 
ATOM   5602 C CZ     . ARG B 2 347 ? 24.477 -1.018  14.211 1.00 67.56  ?  347 ARG B CZ     1 
ATOM   5603 N NH1    . ARG B 2 347 ? 24.522 0.304   14.290 1.00 66.23  ?  347 ARG B NH1    1 
ATOM   5604 N NH2    . ARG B 2 347 ? 23.306 -1.623  14.051 1.00 66.28  ?  347 ARG B NH2    1 
ATOM   5605 N N      . PHE B 2 348 ? 31.724 -2.004  15.879 1.00 44.69  ?  348 PHE B N      1 
ATOM   5606 C CA     . PHE B 2 348 ? 32.827 -1.182  15.404 1.00 52.11  ?  348 PHE B CA     1 
ATOM   5607 C C      . PHE B 2 348 ? 34.070 -1.997  15.086 1.00 52.49  ?  348 PHE B C      1 
ATOM   5608 O O      . PHE B 2 348 ? 34.953 -1.514  14.370 1.00 53.69  ?  348 PHE B O      1 
ATOM   5609 C CB     . PHE B 2 348 ? 33.159 -0.112  16.444 1.00 56.68  ?  348 PHE B CB     1 
ATOM   5610 C CG     . PHE B 2 348 ? 33.501 1.202   15.844 1.00 61.14  ?  348 PHE B CG     1 
ATOM   5611 C CD1    . PHE B 2 348 ? 32.503 2.104   15.522 1.00 56.59  ?  348 PHE B CD1    1 
ATOM   5612 C CD2    . PHE B 2 348 ? 34.828 1.528   15.575 1.00 66.11  ?  348 PHE B CD2    1 
ATOM   5613 C CE1    . PHE B 2 348 ? 32.817 3.303   14.951 1.00 59.50  ?  348 PHE B CE1    1 
ATOM   5614 C CE2    . PHE B 2 348 ? 35.161 2.733   15.008 1.00 63.21  ?  348 PHE B CE2    1 
ATOM   5615 C CZ     . PHE B 2 348 ? 34.152 3.627   14.694 1.00 65.56  ?  348 PHE B CZ     1 
ATOM   5616 N N      . LYS B 2 349 ? 34.162 -3.217  15.616 1.00 60.25  ?  349 LYS B N      1 
ATOM   5617 C CA     . LYS B 2 349 ? 35.223 -4.143  15.241 1.00 61.23  ?  349 LYS B CA     1 
ATOM   5618 C C      . LYS B 2 349 ? 35.121 -4.570  13.786 1.00 66.44  ?  349 LYS B C      1 
ATOM   5619 O O      . LYS B 2 349 ? 36.079 -5.132  13.241 1.00 69.15  ?  349 LYS B O      1 
ATOM   5620 C CB     . LYS B 2 349 ? 35.168 -5.387  16.131 1.00 60.52  ?  349 LYS B CB     1 
ATOM   5621 C CG     . LYS B 2 349 ? 35.565 -5.165  17.571 1.00 61.03  ?  349 LYS B CG     1 
ATOM   5622 C CD     . LYS B 2 349 ? 35.833 -6.496  18.250 1.00 64.60  ?  349 LYS B CD     1 
ATOM   5623 C CE     . LYS B 2 349 ? 36.957 -7.236  17.557 1.00 66.22  ?  349 LYS B CE     1 
ATOM   5624 N NZ     . LYS B 2 349 ? 37.205 -8.572  18.162 1.00 69.27  ?  349 LYS B NZ     1 
ATOM   5625 N N      . ASN B 2 350 ? 33.956 -4.389  13.176 1.00 73.26  ?  350 ASN B N      1 
ATOM   5626 C CA     . ASN B 2 350 ? 33.674 -4.872  11.834 1.00 75.39  ?  350 ASN B CA     1 
ATOM   5627 C C      . ASN B 2 350 ? 33.749 -3.793  10.750 1.00 75.90  ?  350 ASN B C      1 
ATOM   5628 O O      . ASN B 2 350 ? 33.463 -4.088  9.583  1.00 76.04  ?  350 ASN B O      1 
ATOM   5629 C CB     . ASN B 2 350 ? 32.310 -5.568  11.836 1.00 74.45  ?  350 ASN B CB     1 
ATOM   5630 C CG     . ASN B 2 350 ? 32.295 -6.805  12.727 1.00 66.60  ?  350 ASN B CG     1 
ATOM   5631 O OD1    . ASN B 2 350 ? 33.352 -7.336  13.087 1.00 67.06  ?  350 ASN B OD1    1 
ATOM   5632 N ND2    . ASN B 2 350 ? 31.103 -7.271  13.079 1.00 60.30  ?  350 ASN B ND2    1 
ATOM   5633 N N      . LYS B 2 351 ? 34.131 -2.576  11.086 1.00 69.87  ?  351 LYS B N      1 
ATOM   5634 C CA     . LYS B 2 351 ? 34.292 -1.515  10.102 1.00 67.34  ?  351 LYS B CA     1 
ATOM   5635 C C      . LYS B 2 351 ? 35.656 -1.540  9.435  1.00 76.63  ?  351 LYS B C      1 
ATOM   5636 O O      . LYS B 2 351 ? 35.934 -0.698  8.588  1.00 80.19  ?  351 LYS B O      1 
ATOM   5637 C CB     . LYS B 2 351 ? 34.065 -0.154  10.745 1.00 58.42  ?  351 LYS B CB     1 
ATOM   5638 C CG     . LYS B 2 351 ? 32.668 0.018   11.305 1.00 59.26  ?  351 LYS B CG     1 
ATOM   5639 C CD     . LYS B 2 351 ? 31.625 -0.172  10.219 1.00 59.01  ?  351 LYS B CD     1 
ATOM   5640 C CE     . LYS B 2 351 ? 30.563 -1.168  10.648 1.00 67.52  ?  351 LYS B CE     1 
ATOM   5641 N NZ     . LYS B 2 351 ? 29.540 -1.363  9.586  1.00 71.86  ?  351 LYS B NZ     1 
ATOM   5642 N N      . GLU B 2 352 ? 36.524 -2.470  9.804  1.00 84.36  ?  352 GLU B N      1 
ATOM   5643 C CA     . GLU B 2 352 ? 37.823 -2.626  9.145  1.00 85.32  ?  352 GLU B CA     1 
ATOM   5644 C C      . GLU B 2 352 ? 37.714 -3.486  7.886  1.00 84.37  ?  352 GLU B C      1 
ATOM   5645 O O      . GLU B 2 352 ? 37.240 -4.622  7.937  1.00 85.32  ?  352 GLU B O      1 
ATOM   5646 C CB     . GLU B 2 352 ? 38.844 -3.237  10.106 1.00 82.12  ?  352 GLU B CB     1 
ATOM   5647 C CG     . GLU B 2 352 ? 38.478 -4.610  10.645 1.00 80.08  ?  352 GLU B CG     1 
ATOM   5648 C CD     . GLU B 2 352 ? 38.908 -4.787  12.096 1.00 77.48  ?  352 GLU B CD     1 
ATOM   5649 O OE1    . GLU B 2 352 ? 39.691 -3.943  12.594 1.00 73.81  ?  352 GLU B OE1    1 
ATOM   5650 O OE2    . GLU B 2 352 ? 38.450 -5.761  12.741 1.00 76.77  -1 352 GLU B OE2    1 
ATOM   5651 N N      . MET C 3 1   ? 57.130 35.001  65.355 1.00 58.71  ?  1   MET C N      1 
ATOM   5652 C CA     . MET C 3 1   ? 56.329 34.624  66.533 1.00 66.84  ?  1   MET C CA     1 
ATOM   5653 C C      . MET C 3 1   ? 56.661 33.245  67.127 1.00 68.95  ?  1   MET C C      1 
ATOM   5654 O O      . MET C 3 1   ? 57.753 32.714  66.940 1.00 75.09  ?  1   MET C O      1 
ATOM   5655 C CB     . MET C 3 1   ? 54.820 34.670  66.209 1.00 64.41  ?  1   MET C CB     1 
ATOM   5656 C CG     . MET C 3 1   ? 54.419 33.961  64.930 1.00 62.44  ?  1   MET C CG     1 
ATOM   5657 S SD     . MET C 3 1   ? 52.657 33.564  64.829 1.00 62.70  ?  1   MET C SD     1 
ATOM   5658 C CE     . MET C 3 1   ? 51.879 35.132  65.209 1.00 66.19  ?  1   MET C CE     1 
ATOM   5659 N N      . GLN C 3 2   ? 55.689 32.688  67.846 1.00 72.11  ?  2   GLN C N      1 
ATOM   5660 C CA     . GLN C 3 2   ? 55.865 31.498  68.669 1.00 74.41  ?  2   GLN C CA     1 
ATOM   5661 C C      . GLN C 3 2   ? 54.514 30.811  68.840 1.00 76.41  ?  2   GLN C C      1 
ATOM   5662 O O      . GLN C 3 2   ? 53.460 31.443  68.705 1.00 76.63  ?  2   GLN C O      1 
ATOM   5663 C CB     . GLN C 3 2   ? 56.452 31.872  70.041 1.00 79.14  ?  2   GLN C CB     1 
ATOM   5664 C CG     . GLN C 3 2   ? 56.965 30.710  70.867 1.00 79.66  ?  2   GLN C CG     1 
ATOM   5665 C CD     . GLN C 3 2   ? 58.310 30.216  70.386 1.00 81.29  ?  2   GLN C CD     1 
ATOM   5666 O OE1    . GLN C 3 2   ? 58.389 29.320  69.539 1.00 84.18  ?  2   GLN C OE1    1 
ATOM   5667 N NE2    . GLN C 3 2   ? 59.381 30.802  70.918 1.00 77.60  ?  2   GLN C NE2    1 
ATOM   5668 N N      . ILE C 3 3   ? 54.553 29.500  69.129 1.00 65.88  ?  3   ILE C N      1 
ATOM   5669 C CA     . ILE C 3 3   ? 53.376 28.708  69.511 1.00 61.02  ?  3   ILE C CA     1 
ATOM   5670 C C      . ILE C 3 3   ? 53.847 27.497  70.318 1.00 56.95  ?  3   ILE C C      1 
ATOM   5671 O O      . ILE C 3 3   ? 55.030 27.156  70.331 1.00 59.59  ?  3   ILE C O      1 
ATOM   5672 C CB     . ILE C 3 3   ? 52.527 28.242  68.296 1.00 60.12  ?  3   ILE C CB     1 
ATOM   5673 C CG1    . ILE C 3 3   ? 53.254 27.164  67.499 1.00 59.56  ?  3   ILE C CG1    1 
ATOM   5674 C CG2    . ILE C 3 3   ? 52.148 29.404  67.380 1.00 60.64  ?  3   ILE C CG2    1 
ATOM   5675 C CD1    . ILE C 3 3   ? 52.439 26.614  66.370 1.00 58.21  ?  3   ILE C CD1    1 
ATOM   5676 N N      . PHE C 3 4   ? 52.908 26.839  71.002 1.00 54.76  ?  4   PHE C N      1 
ATOM   5677 C CA     . PHE C 3 4   ? 53.188 25.628  71.779 1.00 51.00  ?  4   PHE C CA     1 
ATOM   5678 C C      . PHE C 3 4   ? 52.203 24.539  71.388 1.00 46.93  ?  4   PHE C C      1 
ATOM   5679 O O      . PHE C 3 4   ? 50.987 24.739  71.479 1.00 50.36  ?  4   PHE C O      1 
ATOM   5680 C CB     . PHE C 3 4   ? 53.095 25.877  73.287 1.00 45.89  ?  4   PHE C CB     1 
ATOM   5681 C CG     . PHE C 3 4   ? 53.691 27.161  73.722 1.00 51.50  ?  4   PHE C CG     1 
ATOM   5682 C CD1    . PHE C 3 4   ? 52.929 28.319  73.746 1.00 58.02  ?  4   PHE C CD1    1 
ATOM   5683 C CD2    . PHE C 3 4   ? 55.008 27.224  74.117 1.00 57.76  ?  4   PHE C CD2    1 
ATOM   5684 C CE1    . PHE C 3 4   ? 53.472 29.520  74.153 1.00 66.94  ?  4   PHE C CE1    1 
ATOM   5685 C CE2    . PHE C 3 4   ? 55.563 28.425  74.533 1.00 62.52  ?  4   PHE C CE2    1 
ATOM   5686 C CZ     . PHE C 3 4   ? 54.789 29.577  74.549 1.00 65.91  ?  4   PHE C CZ     1 
ATOM   5687 N N      . VAL C 3 5   ? 52.733 23.389  71.014 1.00 36.50  ?  5   VAL C N      1 
ATOM   5688 C CA     . VAL C 3 5   ? 51.934 22.267  70.617 1.00 36.73  ?  5   VAL C CA     1 
ATOM   5689 C C      . VAL C 3 5   ? 51.951 21.267  71.731 1.00 42.05  ?  5   VAL C C      1 
ATOM   5690 O O      . VAL C 3 5   ? 52.975 20.690  72.024 1.00 47.05  ?  5   VAL C O      1 
ATOM   5691 C CB     . VAL C 3 5   ? 52.499 21.649  69.346 1.00 43.65  ?  5   VAL C CB     1 
ATOM   5692 C CG1    . VAL C 3 5   ? 51.738 20.396  68.976 1.00 46.58  ?  5   VAL C CG1    1 
ATOM   5693 C CG2    . VAL C 3 5   ? 52.459 22.657  68.215 1.00 45.25  ?  5   VAL C CG2    1 
ATOM   5694 N N      . LYS C 3 6   ? 50.797 21.043  72.335 1.00 48.88  ?  6   LYS C N      1 
ATOM   5695 C CA     . LYS C 3 6   ? 50.694 20.111  73.438 1.00 52.24  ?  6   LYS C CA     1 
ATOM   5696 C C      . LYS C 3 6   ? 50.253 18.731  73.030 1.00 55.99  ?  6   LYS C C      1 
ATOM   5697 O O      . LYS C 3 6   ? 49.403 18.575  72.185 1.00 62.45  ?  6   LYS C O      1 
ATOM   5698 C CB     . LYS C 3 6   ? 49.773 20.649  74.519 1.00 57.93  ?  6   LYS C CB     1 
ATOM   5699 C CG     . LYS C 3 6   ? 50.461 21.560  75.512 1.00 67.83  ?  6   LYS C CG     1 
ATOM   5700 C CD     . LYS C 3 6   ? 50.133 21.153  76.936 1.00 73.35  ?  6   LYS C CD     1 
ATOM   5701 C CE     . LYS C 3 6   ? 50.569 22.218  77.933 1.00 68.72  ?  6   LYS C CE     1 
ATOM   5702 N NZ     . LYS C 3 6   ? 50.363 21.792  79.345 1.00 62.48  ?  6   LYS C NZ     1 
ATOM   5703 N N      . THR C 3 7   ? 50.860 17.748  73.669 1.00 46.51  ?  7   THR C N      1 
ATOM   5704 C CA     . THR C 3 7   ? 50.570 16.371  73.375 1.00 49.26  ?  7   THR C CA     1 
ATOM   5705 C C      . THR C 3 7   ? 49.558 15.806  74.336 1.00 51.51  ?  7   THR C C      1 
ATOM   5706 O O      . THR C 3 7   ? 49.115 16.466  75.257 1.00 52.39  ?  7   THR C O      1 
ATOM   5707 C CB     . THR C 3 7   ? 51.853 15.521  73.472 1.00 44.28  ?  7   THR C CB     1 
ATOM   5708 O OG1    . THR C 3 7   ? 52.495 15.759  74.722 1.00 42.19  ?  7   THR C OG1    1 
ATOM   5709 C CG2    . THR C 3 7   ? 52.799 15.855  72.354 1.00 40.26  ?  7   THR C CG2    1 
ATOM   5710 N N      . LEU C 3 8   ? 49.200 14.557  74.140 1.00 46.04  ?  8   LEU C N      1 
ATOM   5711 C CA     . LEU C 3 8   ? 48.246 13.916  74.988 1.00 43.84  ?  8   LEU C CA     1 
ATOM   5712 C C      . LEU C 3 8   ? 48.995 13.490  76.217 1.00 49.86  ?  8   LEU C C      1 
ATOM   5713 O O      . LEU C 3 8   ? 48.450 12.795  77.062 1.00 55.53  ?  8   LEU C O      1 
ATOM   5714 C CB     . LEU C 3 8   ? 47.641 12.699  74.282 1.00 38.86  ?  8   LEU C CB     1 
ATOM   5715 C CG     . LEU C 3 8   ? 46.581 12.817  73.203 1.00 30.73  ?  8   LEU C CG     1 
ATOM   5716 C CD1    . LEU C 3 8   ? 45.959 11.447  73.035 1.00 22.70  ?  8   LEU C CD1    1 
ATOM   5717 C CD2    . LEU C 3 8   ? 45.545 13.852  73.589 1.00 28.64  ?  8   LEU C CD2    1 
ATOM   5718 N N      . THR C 3 9   ? 50.252 13.890  76.325 1.00 81.04  ?  9   THR C N      1 
ATOM   5719 C CA     . THR C 3 9   ? 51.039 13.573  77.502 1.00 82.27  ?  9   THR C CA     1 
ATOM   5720 C C      . THR C 3 9   ? 51.113 14.826  78.310 1.00 78.46  ?  9   THR C C      1 
ATOM   5721 O O      . THR C 3 9   ? 51.397 14.782  79.501 1.00 78.26  ?  9   THR C O      1 
ATOM   5722 C CB     . THR C 3 9   ? 52.463 13.125  77.153 1.00 83.88  ?  9   THR C CB     1 
ATOM   5723 O OG1    . THR C 3 9   ? 53.127 14.160  76.426 1.00 85.83  ?  9   THR C OG1    1 
ATOM   5724 C CG2    . THR C 3 9   ? 52.431 11.872  76.325 1.00 84.47  ?  9   THR C CG2    1 
ATOM   5725 N N      . GLY C 3 10  ? 50.840 15.943  77.663 1.00 47.28  ?  10  GLY C N      1 
ATOM   5726 C CA     . GLY C 3 10  ? 50.921 17.214  78.325 1.00 43.00  ?  10  GLY C CA     1 
ATOM   5727 C C      . GLY C 3 10  ? 52.287 17.817  78.164 1.00 52.03  ?  10  GLY C C      1 
ATOM   5728 O O      . GLY C 3 10  ? 52.541 18.887  78.683 1.00 62.70  ?  10  GLY C O      1 
ATOM   5729 N N      . LYS C 3 11  ? 53.172 17.152  77.446 1.00 45.80  ?  11  LYS C N      1 
ATOM   5730 C CA     . LYS C 3 11  ? 54.485 17.692  77.170 1.00 47.87  ?  11  LYS C CA     1 
ATOM   5731 C C      . LYS C 3 11  ? 54.304 18.835  76.225 1.00 51.89  ?  11  LYS C C      1 
ATOM   5732 O O      . LYS C 3 11  ? 53.380 18.821  75.427 1.00 53.07  ?  11  LYS C O      1 
ATOM   5733 C CB     . LYS C 3 11  ? 55.363 16.652  76.523 1.00 49.08  ?  11  LYS C CB     1 
ATOM   5734 C CG     . LYS C 3 11  ? 55.581 15.393  77.341 1.00 52.95  ?  11  LYS C CG     1 
ATOM   5735 C CD     . LYS C 3 11  ? 56.199 15.687  78.699 1.00 48.72  ?  11  LYS C CD     1 
ATOM   5736 C CE     . LYS C 3 11  ? 56.915 14.467  79.248 1.00 42.82  ?  11  LYS C CE     1 
ATOM   5737 N NZ     . LYS C 3 11  ? 56.089 13.240  79.132 1.00 39.19  ?  11  LYS C NZ     1 
ATOM   5738 N N      . THR C 3 12  ? 55.184 19.829  76.274 1.00 62.18  ?  12  THR C N      1 
ATOM   5739 C CA     . THR C 3 12  ? 54.963 21.028  75.460 1.00 59.91  ?  12  THR C CA     1 
ATOM   5740 C C      . THR C 3 12  ? 56.087 21.225  74.445 1.00 60.52  ?  12  THR C C      1 
ATOM   5741 O O      . THR C 3 12  ? 57.205 21.609  74.807 1.00 64.81  ?  12  THR C O      1 
ATOM   5742 C CB     . THR C 3 12  ? 54.816 22.266  76.339 1.00 52.45  ?  12  THR C CB     1 
ATOM   5743 O OG1    . THR C 3 12  ? 53.807 22.028  77.338 1.00 47.94  ?  12  THR C OG1    1 
ATOM   5744 C CG2    . THR C 3 12  ? 54.424 23.473  75.471 1.00 48.79  ?  12  THR C CG2    1 
ATOM   5745 N N      . ILE C 3 13  ? 55.766 21.002  73.173 1.00 45.39  ?  13  ILE C N      1 
ATOM   5746 C CA     . ILE C 3 13  ? 56.656 21.320  72.058 1.00 37.44  ?  13  ILE C CA     1 
ATOM   5747 C C      . ILE C 3 13  ? 56.531 22.806  71.743 1.00 37.03  ?  13  ILE C C      1 
ATOM   5748 O O      . ILE C 3 13  ? 55.422 23.342  71.631 1.00 49.26  ?  13  ILE C O      1 
ATOM   5749 C CB     . ILE C 3 13  ? 56.297 20.462  70.829 1.00 39.90  ?  13  ILE C CB     1 
ATOM   5750 C CG1    . ILE C 3 13  ? 55.959 19.025  71.248 1.00 37.08  ?  13  ILE C CG1    1 
ATOM   5751 C CG2    . ILE C 3 13  ? 57.404 20.458  69.804 1.00 42.70  ?  13  ILE C CG2    1 
ATOM   5752 C CD1    . ILE C 3 13  ? 55.377 18.157  70.131 1.00 31.75  ?  13  ILE C CD1    1 
ATOM   5753 N N      . THR C 3 14  ? 57.654 23.491  71.616 1.00 32.32  ?  14  THR C N      1 
ATOM   5754 C CA     . THR C 3 14  ? 57.648 24.904  71.242 1.00 38.59  ?  14  THR C CA     1 
ATOM   5755 C C      . THR C 3 14  ? 58.215 25.055  69.830 1.00 40.61  ?  14  THR C C      1 
ATOM   5756 O O      . THR C 3 14  ? 59.410 24.835  69.610 1.00 50.62  ?  14  THR C O      1 
ATOM   5757 C CB     . THR C 3 14  ? 58.438 25.736  72.252 1.00 49.36  ?  14  THR C CB     1 
ATOM   5758 O OG1    . THR C 3 14  ? 58.093 25.339  73.591 1.00 57.20  ?  14  THR C OG1    1 
ATOM   5759 C CG2    . THR C 3 14  ? 58.124 27.219  72.082 1.00 48.78  ?  14  THR C CG2    1 
ATOM   5760 N N      . LEU C 3 15  ? 57.374 25.470  68.917 1.00 54.02  ?  15  LEU C N      1 
ATOM   5761 C CA     . LEU C 3 15  ? 57.779 25.652  67.553 1.00 59.17  ?  15  LEU C CA     1 
ATOM   5762 C C      . LEU C 3 15  ? 57.704 27.096  67.161 1.00 67.41  ?  15  LEU C C      1 
ATOM   5763 O O      . LEU C 3 15  ? 56.625 27.659  67.166 1.00 73.44  ?  15  LEU C O      1 
ATOM   5764 C CB     . LEU C 3 15  ? 56.829 24.922  66.629 1.00 57.42  ?  15  LEU C CB     1 
ATOM   5765 C CG     . LEU C 3 15  ? 56.842 23.437  66.333 1.00 51.47  ?  15  LEU C CG     1 
ATOM   5766 C CD1    . LEU C 3 15  ? 56.232 22.692  67.496 1.00 51.71  ?  15  LEU C CD1    1 
ATOM   5767 C CD2    . LEU C 3 15  ? 55.943 23.287  65.129 1.00 50.81  ?  15  LEU C CD2    1 
ATOM   5768 N N      . GLU C 3 16  ? 58.828 27.710  66.837 1.00 60.61  ?  16  GLU C N      1 
ATOM   5769 C CA     . GLU C 3 16  ? 58.836 29.083  66.337 1.00 60.21  ?  16  GLU C CA     1 
ATOM   5770 C C      . GLU C 3 16  ? 58.374 29.090  64.886 1.00 56.60  ?  16  GLU C C      1 
ATOM   5771 O O      . GLU C 3 16  ? 58.889 28.334  64.058 1.00 50.17  ?  16  GLU C O      1 
ATOM   5772 C CB     . GLU C 3 16  ? 60.222 29.724  66.435 1.00 67.54  ?  16  GLU C CB     1 
ATOM   5773 C CG     . GLU C 3 16  ? 60.658 30.166  67.819 1.00 71.02  ?  16  GLU C CG     1 
ATOM   5774 C CD     . GLU C 3 16  ? 61.794 29.306  68.342 1.00 72.23  ?  16  GLU C CD     1 
ATOM   5775 O OE1    . GLU C 3 16  ? 62.867 29.276  67.702 1.00 70.91  ?  16  GLU C OE1    1 
ATOM   5776 O OE2    . GLU C 3 16  ? 61.605 28.636  69.380 1.00 72.14  -1 16  GLU C OE2    1 
ATOM   5777 N N      . VAL C 3 17  ? 57.397 29.944  64.586 1.00 49.39  ?  17  VAL C N      1 
ATOM   5778 C CA     . VAL C 3 17  ? 56.745 29.984  63.289 1.00 45.15  ?  17  VAL C CA     1 
ATOM   5779 C C      . VAL C 3 17  ? 56.565 31.440  62.885 1.00 45.16  ?  17  VAL C C      1 
ATOM   5780 O O      . VAL C 3 17  ? 56.717 32.362  63.690 1.00 44.76  ?  17  VAL C O      1 
ATOM   5781 C CB     . VAL C 3 17  ? 55.386 29.261  63.306 1.00 46.43  ?  17  VAL C CB     1 
ATOM   5782 C CG1    . VAL C 3 17  ? 55.518 27.894  63.975 1.00 51.05  ?  17  VAL C CG1    1 
ATOM   5783 C CG2    . VAL C 3 17  ? 54.361 30.116  64.018 1.00 47.35  ?  17  VAL C CG2    1 
ATOM   5784 N N      . GLU C 3 18  ? 56.230 31.638  61.613 1.00 63.26  ?  18  GLU C N      1 
ATOM   5785 C CA     . GLU C 3 18  ? 55.851 32.942  61.114 1.00 66.53  ?  18  GLU C CA     1 
ATOM   5786 C C      . GLU C 3 18  ? 54.438 32.830  60.561 1.00 66.22  ?  18  GLU C C      1 
ATOM   5787 O O      . GLU C 3 18  ? 54.137 31.879  59.835 1.00 68.51  ?  18  GLU C O      1 
ATOM   5788 C CB     . GLU C 3 18  ? 56.809 33.421  60.008 1.00 67.97  ?  18  GLU C CB     1 
ATOM   5789 C CG     . GLU C 3 18  ? 58.285 33.518  60.400 1.00 67.82  ?  18  GLU C CG     1 
ATOM   5790 C CD     . GLU C 3 18  ? 58.670 34.902  60.923 1.00 75.22  ?  18  GLU C CD     1 
ATOM   5791 O OE1    . GLU C 3 18  ? 57.763 35.694  61.266 1.00 71.52  ?  18  GLU C OE1    1 
ATOM   5792 O OE2    . GLU C 3 18  ? 59.887 35.204  60.989 1.00 80.36  -1 18  GLU C OE2    1 
ATOM   5793 N N      . PRO C 3 19  ? 53.570 33.805  60.825 1.00 57.53  ?  19  PRO C N      1 
ATOM   5794 C CA     . PRO C 3 19  ? 52.122 33.527  60.776 1.00 51.99  ?  19  PRO C CA     1 
ATOM   5795 C C      . PRO C 3 19  ? 51.630 33.023  59.433 1.00 49.03  ?  19  PRO C C      1 
ATOM   5796 O O      . PRO C 3 19  ? 50.512 32.491  59.363 1.00 48.64  ?  19  PRO C O      1 
ATOM   5797 C CB     . PRO C 3 19  ? 51.487 34.873  61.147 1.00 52.77  ?  19  PRO C CB     1 
ATOM   5798 C CG     . PRO C 3 19  ? 52.554 35.886  60.899 1.00 56.38  ?  19  PRO C CG     1 
ATOM   5799 C CD     . PRO C 3 19  ? 53.870 35.212  61.133 1.00 57.57  ?  19  PRO C CD     1 
ATOM   5800 N N      . SER C 3 20  ? 52.414 33.162  58.366 1.00 52.35  ?  20  SER C N      1 
ATOM   5801 C CA     . SER C 3 20  ? 52.050 32.577  57.083 1.00 59.49  ?  20  SER C CA     1 
ATOM   5802 C C      . SER C 3 20  ? 52.507 31.128  56.939 1.00 59.14  ?  20  SER C C      1 
ATOM   5803 O O      . SER C 3 20  ? 52.223 30.508  55.910 1.00 63.68  ?  20  SER C O      1 
ATOM   5804 C CB     . SER C 3 20  ? 52.609 33.415  55.926 1.00 61.27  ?  20  SER C CB     1 
ATOM   5805 O OG     . SER C 3 20  ? 51.773 33.312  54.782 1.00 60.51  ?  20  SER C OG     1 
ATOM   5806 N N      . ASP C 3 21  ? 53.198 30.575  57.935 1.00 69.08  ?  21  ASP C N      1 
ATOM   5807 C CA     . ASP C 3 21  ? 53.505 29.150  57.928 1.00 68.20  ?  21  ASP C CA     1 
ATOM   5808 C C      . ASP C 3 21  ? 52.210 28.342  57.859 1.00 72.30  ?  21  ASP C C      1 
ATOM   5809 O O      . ASP C 3 21  ? 51.296 28.540  58.664 1.00 77.41  ?  21  ASP C O      1 
ATOM   5810 C CB     . ASP C 3 21  ? 54.318 28.770  59.175 1.00 67.40  ?  21  ASP C CB     1 
ATOM   5811 C CG     . ASP C 3 21  ? 55.788 29.226  59.096 1.00 72.06  ?  21  ASP C CG     1 
ATOM   5812 O OD1    . ASP C 3 21  ? 56.082 30.240  58.424 1.00 70.25  ?  21  ASP C OD1    1 
ATOM   5813 O OD2    . ASP C 3 21  ? 56.660 28.568  59.713 1.00 74.05  -1 21  ASP C OD2    1 
ATOM   5814 N N      . THR C 3 22  ? 52.132 27.440  56.880 1.00 66.07  ?  22  THR C N      1 
ATOM   5815 C CA     . THR C 3 22  ? 50.970 26.577  56.691 1.00 61.96  ?  22  THR C CA     1 
ATOM   5816 C C      . THR C 3 22  ? 50.917 25.483  57.757 1.00 59.66  ?  22  THR C C      1 
ATOM   5817 O O      . THR C 3 22  ? 51.905 25.189  58.434 1.00 62.97  ?  22  THR C O      1 
ATOM   5818 C CB     . THR C 3 22  ? 50.994 25.937  55.298 1.00 61.66  ?  22  THR C CB     1 
ATOM   5819 O OG1    . THR C 3 22  ? 52.172 25.125  55.149 1.00 55.78  ?  22  THR C OG1    1 
ATOM   5820 C CG2    . THR C 3 22  ? 50.962 27.017  54.214 1.00 61.82  ?  22  THR C CG2    1 
ATOM   5821 N N      . ILE C 3 23  ? 49.736 24.883  57.922 1.00 51.08  ?  23  ILE C N      1 
ATOM   5822 C CA     . ILE C 3 23  ? 49.635 23.747  58.835 1.00 49.57  ?  23  ILE C CA     1 
ATOM   5823 C C      . ILE C 3 23  ? 50.543 22.611  58.358 1.00 49.80  ?  23  ILE C C      1 
ATOM   5824 O O      . ILE C 3 23  ? 51.231 21.968  59.163 1.00 55.03  ?  23  ILE C O      1 
ATOM   5825 C CB     . ILE C 3 23  ? 48.157 23.324  58.998 1.00 48.60  ?  23  ILE C CB     1 
ATOM   5826 C CG1    . ILE C 3 23  ? 47.320 24.522  59.463 1.00 47.63  ?  23  ILE C CG1    1 
ATOM   5827 C CG2    . ILE C 3 23  ? 47.985 22.221  60.043 1.00 45.29  ?  23  ILE C CG2    1 
ATOM   5828 C CD1    . ILE C 3 23  ? 47.873 25.239  60.664 1.00 45.21  ?  23  ILE C CD1    1 
ATOM   5829 N N      . GLU C 3 24  ? 50.598 22.381  57.039 1.00 44.11  ?  24  GLU C N      1 
ATOM   5830 C CA     . GLU C 3 24  ? 51.629 21.527  56.433 1.00 39.19  ?  24  GLU C CA     1 
ATOM   5831 C C      . GLU C 3 24  ? 53.037 21.885  56.910 1.00 38.32  ?  24  GLU C C      1 
ATOM   5832 O O      . GLU C 3 24  ? 53.888 21.007  57.077 1.00 36.94  ?  24  GLU C O      1 
ATOM   5833 C CB     . GLU C 3 24  ? 51.568 21.667  54.911 1.00 45.53  ?  24  GLU C CB     1 
ATOM   5834 C CG     . GLU C 3 24  ? 51.457 20.393  54.088 1.00 52.91  ?  24  GLU C CG     1 
ATOM   5835 C CD     . GLU C 3 24  ? 51.487 20.688  52.572 1.00 59.71  ?  24  GLU C CD     1 
ATOM   5836 O OE1    . GLU C 3 24  ? 51.998 21.771  52.194 1.00 60.80  ?  24  GLU C OE1    1 
ATOM   5837 O OE2    . GLU C 3 24  ? 50.999 19.852  51.762 1.00 60.65  -1 24  GLU C OE2    1 
ATOM   5838 N N      . ASN C 3 25  ? 53.318 23.182  57.065 1.00 54.44  ?  25  ASN C N      1 
ATOM   5839 C CA     . ASN C 3 25  ? 54.647 23.624  57.496 1.00 56.00  ?  25  ASN C CA     1 
ATOM   5840 C C      . ASN C 3 25  ? 54.922 23.263  58.953 1.00 53.20  ?  25  ASN C C      1 
ATOM   5841 O O      . ASN C 3 25  ? 56.036 22.850  59.292 1.00 51.06  ?  25  ASN C O      1 
ATOM   5842 C CB     . ASN C 3 25  ? 54.799 25.137  57.310 1.00 56.74  ?  25  ASN C CB     1 
ATOM   5843 C CG     . ASN C 3 25  ? 55.472 25.496  56.022 1.00 67.51  ?  25  ASN C CG     1 
ATOM   5844 O OD1    . ASN C 3 25  ? 54.969 26.318  55.253 1.00 74.72  ?  25  ASN C OD1    1 
ATOM   5845 N ND2    . ASN C 3 25  ? 56.627 24.882  55.769 1.00 72.54  ?  25  ASN C ND2    1 
ATOM   5846 N N      . VAL C 3 26  ? 53.940 23.433  59.813 1.00 41.70  ?  26  VAL C N      1 
ATOM   5847 C CA     . VAL C 3 26  ? 54.164 23.225  61.224 1.00 38.60  ?  26  VAL C CA     1 
ATOM   5848 C C      . VAL C 3 26  ? 54.289 21.780  61.582 1.00 46.15  ?  26  VAL C C      1 
ATOM   5849 O O      . VAL C 3 26  ? 55.048 21.432  62.449 1.00 55.03  ?  26  VAL C O      1 
ATOM   5850 C CB     . VAL C 3 26  ? 53.176 24.016  62.092 1.00 36.95  ?  26  VAL C CB     1 
ATOM   5851 C CG1    . VAL C 3 26  ? 53.351 25.501  61.857 1.00 38.61  ?  26  VAL C CG1    1 
ATOM   5852 C CG2    . VAL C 3 26  ? 51.744 23.602  61.856 1.00 42.07  ?  26  VAL C CG2    1 
ATOM   5853 N N      . LYS C 3 27  ? 53.581 20.922  60.895 1.00 29.95  ?  27  LYS C N      1 
ATOM   5854 C CA     . LYS C 3 27  ? 53.716 19.528  61.116 1.00 23.51  ?  27  LYS C CA     1 
ATOM   5855 C C      . LYS C 3 27  ? 55.109 19.070  60.745 1.00 27.83  ?  27  LYS C C      1 
ATOM   5856 O O      . LYS C 3 27  ? 55.616 18.149  61.343 1.00 36.78  ?  27  LYS C O      1 
ATOM   5857 C CB     . LYS C 3 27  ? 52.606 18.807  60.405 1.00 22.38  ?  27  LYS C CB     1 
ATOM   5858 C CG     . LYS C 3 27  ? 51.234 19.140  60.915 1.00 22.24  ?  27  LYS C CG     1 
ATOM   5859 C CD     . LYS C 3 27  ? 50.196 18.430  60.090 1.00 21.83  ?  27  LYS C CD     1 
ATOM   5860 C CE     . LYS C 3 27  ? 48.815 18.586  60.685 1.00 22.99  ?  27  LYS C CE     1 
ATOM   5861 N NZ     . LYS C 3 27  ? 47.798 17.877  59.875 1.00 24.64  ?  27  LYS C NZ     1 
ATOM   5862 N N      . ALA C 3 28  ? 55.712 19.644  59.719 1.00 37.16  ?  28  ALA C N      1 
ATOM   5863 C CA     . ALA C 3 28  ? 57.097 19.331  59.318 1.00 35.36  ?  28  ALA C CA     1 
ATOM   5864 C C      . ALA C 3 28  ? 58.125 19.719  60.316 1.00 32.00  ?  28  ALA C C      1 
ATOM   5865 O O      . ALA C 3 28  ? 59.089 19.022  60.503 1.00 40.30  ?  28  ALA C O      1 
ATOM   5866 C CB     . ALA C 3 28  ? 57.408 19.974  57.982 1.00 28.55  ?  28  ALA C CB     1 
ATOM   5867 N N      . LYS C 3 29  ? 57.953 20.859  60.926 1.00 41.39  ?  29  LYS C N      1 
ATOM   5868 C CA     . LYS C 3 29  ? 58.835 21.276  61.995 1.00 46.39  ?  29  LYS C CA     1 
ATOM   5869 C C      . LYS C 3 29  ? 58.679 20.330  63.144 1.00 45.50  ?  29  LYS C C      1 
ATOM   5870 O O      . LYS C 3 29  ? 59.640 19.987  63.796 1.00 47.89  ?  29  LYS C O      1 
ATOM   5871 C CB     . LYS C 3 29  ? 58.482 22.673  62.472 1.00 43.05  ?  29  LYS C CB     1 
ATOM   5872 C CG     . LYS C 3 29  ? 58.473 23.745  61.417 1.00 47.16  ?  29  LYS C CG     1 
ATOM   5873 C CD     . LYS C 3 29  ? 58.121 25.068  62.057 1.00 50.02  ?  29  LYS C CD     1 
ATOM   5874 C CE     . LYS C 3 29  ? 58.064 26.157  61.018 1.00 52.16  ?  29  LYS C CE     1 
ATOM   5875 N NZ     . LYS C 3 29  ? 59.315 26.228  60.222 1.00 54.63  ?  29  LYS C NZ     1 
ATOM   5876 N N      . ILE C 3 30  ? 57.455 19.916  63.392 1.00 29.83  ?  30  ILE C N      1 
ATOM   5877 C CA     . ILE C 3 30  ? 57.213 19.020  64.465 1.00 33.37  ?  30  ILE C CA     1 
ATOM   5878 C C      . ILE C 3 30  ? 57.968 17.725  64.228 1.00 31.96  ?  30  ILE C C      1 
ATOM   5879 O O      . ILE C 3 30  ? 58.647 17.251  65.107 1.00 35.45  ?  30  ILE C O      1 
ATOM   5880 C CB     . ILE C 3 30  ? 55.688 18.769  64.635 1.00 32.72  ?  30  ILE C CB     1 
ATOM   5881 C CG1    . ILE C 3 30  ? 54.983 19.956  65.257 1.00 24.27  ?  30  ILE C CG1    1 
ATOM   5882 C CG2    . ILE C 3 30  ? 55.432 17.545  65.498 1.00 31.58  ?  30  ILE C CG2    1 
ATOM   5883 C CD1    . ILE C 3 30  ? 53.484 19.837  65.204 1.00 24.34  ?  30  ILE C CD1    1 
ATOM   5884 N N      . GLN C 3 31  ? 57.921 17.199  63.028 1.00 31.58  ?  31  GLN C N      1 
ATOM   5885 C CA     . GLN C 3 31  ? 58.664 16.003  62.711 1.00 37.13  ?  31  GLN C CA     1 
ATOM   5886 C C      . GLN C 3 31  ? 60.154 16.176  62.847 1.00 35.37  ?  31  GLN C C      1 
ATOM   5887 O O      . GLN C 3 31  ? 60.837 15.324  63.342 1.00 35.68  ?  31  GLN C O      1 
ATOM   5888 C CB     . GLN C 3 31  ? 58.349 15.556  61.300 1.00 36.98  ?  31  GLN C CB     1 
ATOM   5889 C CG     . GLN C 3 31  ? 59.105 14.335  60.828 1.00 36.76  ?  31  GLN C CG     1 
ATOM   5890 C CD     . GLN C 3 31  ? 59.031 14.174  59.333 1.00 44.34  ?  31  GLN C CD     1 
ATOM   5891 O OE1    . GLN C 3 31  ? 59.044 15.151  58.591 1.00 41.16  ?  31  GLN C OE1    1 
ATOM   5892 N NE2    . GLN C 3 31  ? 58.959 12.936  58.883 1.00 53.62  ?  31  GLN C NE2    1 
ATOM   5893 N N      . ASP C 3 32  ? 60.664 17.304  62.437 1.00 37.85  ?  32  ASP C N      1 
ATOM   5894 C CA     . ASP C 3 32  ? 62.058 17.520  62.613 1.00 42.88  ?  32  ASP C CA     1 
ATOM   5895 C C      . ASP C 3 32  ? 62.501 17.526  64.046 1.00 37.61  ?  32  ASP C C      1 
ATOM   5896 O O      . ASP C 3 32  ? 63.511 16.939  64.340 1.00 49.72  ?  32  ASP C O      1 
ATOM   5897 C CB     . ASP C 3 32  ? 62.479 18.798  61.917 1.00 58.95  ?  32  ASP C CB     1 
ATOM   5898 C CG     . ASP C 3 32  ? 62.450 18.682  60.405 1.00 69.16  ?  32  ASP C CG     1 
ATOM   5899 O OD1    . ASP C 3 32  ? 62.446 17.547  59.885 1.00 69.00  ?  32  ASP C OD1    1 
ATOM   5900 O OD2    . ASP C 3 32  ? 62.445 19.733  59.734 1.00 72.74  -1 32  ASP C OD2    1 
ATOM   5901 N N      . LYS C 3 33  ? 61.804 18.199  64.938 1.00 38.81  ?  33  LYS C N      1 
ATOM   5902 C CA     . LYS C 3 33  ? 62.116 18.106  66.365 1.00 46.92  ?  33  LYS C CA     1 
ATOM   5903 C C      . LYS C 3 33  ? 61.817 16.776  67.023 1.00 53.55  ?  33  LYS C C      1 
ATOM   5904 O O      . LYS C 3 33  ? 62.627 16.275  67.773 1.00 56.66  ?  33  LYS C O      1 
ATOM   5905 C CB     . LYS C 3 33  ? 61.343 19.160  67.146 1.00 49.77  ?  33  LYS C CB     1 
ATOM   5906 C CG     . LYS C 3 33  ? 61.837 19.363  68.565 1.00 53.26  ?  33  LYS C CG     1 
ATOM   5907 C CD     . LYS C 3 33  ? 60.853 20.169  69.388 1.00 56.46  ?  33  LYS C CD     1 
ATOM   5908 C CE     . LYS C 3 33  ? 60.735 21.604  68.913 1.00 51.85  ?  33  LYS C CE     1 
ATOM   5909 N NZ     . LYS C 3 33  ? 61.569 22.517  69.730 1.00 48.86  ?  33  LYS C NZ     1 
ATOM   5910 N N      . GLU C 3 34  ? 60.663 16.191  66.730 1.00 55.43  ?  34  GLU C N      1 
ATOM   5911 C CA     . GLU C 3 34  ? 60.218 14.976  67.396 1.00 50.20  ?  34  GLU C CA     1 
ATOM   5912 C C      . GLU C 3 34  ? 60.133 13.672  66.617 1.00 48.41  ?  34  GLU C C      1 
ATOM   5913 O O      . GLU C 3 34  ? 59.872 12.628  67.192 1.00 48.90  ?  34  GLU C O      1 
ATOM   5914 C CB     . GLU C 3 34  ? 58.849 15.272  67.981 1.00 50.77  ?  34  GLU C CB     1 
ATOM   5915 C CG     . GLU C 3 34  ? 58.783 16.450  68.923 1.00 51.16  ?  34  GLU C CG     1 
ATOM   5916 C CD     . GLU C 3 34  ? 59.075 16.031  70.333 1.00 52.00  ?  34  GLU C CD     1 
ATOM   5917 O OE1    . GLU C 3 34  ? 59.090 14.811  70.569 1.00 46.94  ?  34  GLU C OE1    1 
ATOM   5918 O OE2    . GLU C 3 34  ? 59.281 16.905  71.193 1.00 56.76  -1 34  GLU C OE2    1 
ATOM   5919 N N      . GLY C 3 35  ? 60.328 13.724  65.317 1.00 36.91  ?  35  GLY C N      1 
ATOM   5920 C CA     . GLY C 3 35  ? 60.304 12.524  64.512 1.00 40.60  ?  35  GLY C CA     1 
ATOM   5921 C C      . GLY C 3 35  ? 58.955 12.002  64.115 1.00 45.96  ?  35  GLY C C      1 
ATOM   5922 O O      . GLY C 3 35  ? 58.847 11.021  63.409 1.00 48.40  ?  35  GLY C O      1 
ATOM   5923 N N      . ILE C 3 36  ? 57.898 12.629  64.561 1.00 37.95  ?  36  ILE C N      1 
ATOM   5924 C CA     . ILE C 3 36  ? 56.587 12.123  64.301 1.00 32.57  ?  36  ILE C CA     1 
ATOM   5925 C C      . ILE C 3 36  ? 56.254 12.293  62.840 1.00 38.57  ?  36  ILE C C      1 
ATOM   5926 O O      . ILE C 3 36  ? 56.365 13.371  62.300 1.00 43.95  ?  36  ILE C O      1 
ATOM   5927 C CB     . ILE C 3 36  ? 55.550 12.847  65.193 1.00 31.25  ?  36  ILE C CB     1 
ATOM   5928 C CG1    . ILE C 3 36  ? 55.899 12.681  66.664 1.00 23.55  ?  36  ILE C CG1    1 
ATOM   5929 C CG2    . ILE C 3 36  ? 54.143 12.401  64.865 1.00 26.90  ?  36  ILE C CG2    1 
ATOM   5930 C CD1    . ILE C 3 36  ? 55.430 13.833  67.510 1.00 26.92  ?  36  ILE C CD1    1 
ATOM   5931 N N      . PRO C 3 37  ? 55.802 11.232  62.204 1.00 39.66  ?  37  PRO C N      1 
ATOM   5932 C CA     . PRO C 3 37  ? 55.408 11.344  60.826 1.00 40.22  ?  37  PRO C CA     1 
ATOM   5933 C C      . PRO C 3 37  ? 54.286 12.342  60.667 1.00 45.31  ?  37  PRO C C      1 
ATOM   5934 O O      . PRO C 3 37  ? 53.315 12.324  61.399 1.00 48.75  ?  37  PRO C O      1 
ATOM   5935 C CB     . PRO C 3 37  ? 54.931 9.938   60.513 1.00 38.30  ?  37  PRO C CB     1 
ATOM   5936 C CG     . PRO C 3 37  ? 55.676 9.059   61.428 1.00 40.76  ?  37  PRO C CG     1 
ATOM   5937 C CD     . PRO C 3 37  ? 55.774 9.846   62.687 1.00 43.64  ?  37  PRO C CD     1 
ATOM   5938 N N      . PRO C 3 38  ? 54.392 13.207  59.680 1.00 49.57  ?  38  PRO C N      1 
ATOM   5939 C CA     . PRO C 3 38  ? 53.393 14.258  59.543 1.00 52.01  ?  38  PRO C CA     1 
ATOM   5940 C C      . PRO C 3 38  ? 51.990 13.703  59.278 1.00 56.90  ?  38  PRO C C      1 
ATOM   5941 O O      . PRO C 3 38  ? 51.022 14.364  59.584 1.00 57.94  ?  38  PRO C O      1 
ATOM   5942 C CB     . PRO C 3 38  ? 53.945 15.105  58.394 1.00 43.70  ?  38  PRO C CB     1 
ATOM   5943 C CG     . PRO C 3 38  ? 54.921 14.248  57.689 1.00 40.91  ?  38  PRO C CG     1 
ATOM   5944 C CD     . PRO C 3 38  ? 55.510 13.378  58.747 1.00 48.28  ?  38  PRO C CD     1 
ATOM   5945 N N      . ASP C 3 39  ? 51.884 12.481  58.787 1.00 70.67  ?  39  ASP C N      1 
ATOM   5946 C CA     . ASP C 3 39  ? 50.604 11.869  58.439 1.00 65.82  ?  39  ASP C CA     1 
ATOM   5947 C C      . ASP C 3 39  ? 49.842 11.250  59.601 1.00 56.17  ?  39  ASP C C      1 
ATOM   5948 O O      . ASP C 3 39  ? 48.720 10.823  59.461 1.00 51.16  ?  39  ASP C O      1 
ATOM   5949 C CB     . ASP C 3 39  ? 50.838 10.869  57.319 1.00 68.44  ?  39  ASP C CB     1 
ATOM   5950 C CG     . ASP C 3 39  ? 51.160 11.538  56.002 1.00 78.57  ?  39  ASP C CG     1 
ATOM   5951 O OD1    . ASP C 3 39  ? 50.929 12.759  55.877 1.00 75.62  ?  39  ASP C OD1    1 
ATOM   5952 O OD2    . ASP C 3 39  ? 51.660 10.844  55.094 1.00 84.47  -1 39  ASP C OD2    1 
ATOM   5953 N N      . GLN C 3 40  ? 50.468 11.165  60.738 1.00 47.06  ?  40  GLN C N      1 
ATOM   5954 C CA     . GLN C 3 40  ? 49.753 10.728  61.925 1.00 48.01  ?  40  GLN C CA     1 
ATOM   5955 C C      . GLN C 3 40  ? 49.323 11.930  62.710 1.00 40.99  ?  40  GLN C C      1 
ATOM   5956 O O      . GLN C 3 40  ? 48.594 11.828  63.649 1.00 41.75  ?  40  GLN C O      1 
ATOM   5957 C CB     . GLN C 3 40  ? 50.558 9.713   62.771 1.00 41.31  ?  40  GLN C CB     1 
ATOM   5958 C CG     . GLN C 3 40  ? 51.870 10.151  63.370 1.00 42.73  ?  40  GLN C CG     1 
ATOM   5959 C CD     . GLN C 3 40  ? 52.390 9.105   64.328 1.00 46.60  ?  40  GLN C CD     1 
ATOM   5960 O OE1    . GLN C 3 40  ? 51.764 8.078   64.522 1.00 51.03  ?  40  GLN C OE1    1 
ATOM   5961 N NE2    . GLN C 3 40  ? 53.527 9.362   64.934 1.00 52.48  ?  40  GLN C NE2    1 
ATOM   5962 N N      . GLN C 3 41  ? 49.732 13.086  62.268 1.00 32.20  ?  41  GLN C N      1 
ATOM   5963 C CA     . GLN C 3 41  ? 49.434 14.295  62.979 1.00 33.14  ?  41  GLN C CA     1 
ATOM   5964 C C      . GLN C 3 41  ? 48.108 14.964  62.793 1.00 33.51  ?  41  GLN C C      1 
ATOM   5965 O O      . GLN C 3 41  ? 47.631 15.175  61.706 1.00 21.79  ?  41  GLN C O      1 
ATOM   5966 C CB     . GLN C 3 41  ? 50.554 15.304  62.767 1.00 38.98  ?  41  GLN C CB     1 
ATOM   5967 C CG     . GLN C 3 41  ? 51.946 14.789  63.043 1.00 44.27  ?  41  GLN C CG     1 
ATOM   5968 C CD     . GLN C 3 41  ? 52.949 15.909  63.098 1.00 43.20  ?  41  GLN C CD     1 
ATOM   5969 O OE1    . GLN C 3 41  ? 52.637 17.002  63.545 1.00 36.90  ?  41  GLN C OE1    1 
ATOM   5970 N NE2    . GLN C 3 41  ? 54.160 15.640  62.649 1.00 44.03  ?  41  GLN C NE2    1 
ATOM   5971 N N      . ARG C 3 42  ? 47.495 15.252  63.913 1.00 61.30  ?  42  ARG C N      1 
ATOM   5972 C CA     . ARG C 3 42  ? 46.247 15.961  63.909 1.00 66.71  ?  42  ARG C CA     1 
ATOM   5973 C C      . ARG C 3 42  ? 46.453 17.064  64.889 1.00 67.26  ?  42  ARG C C      1 
ATOM   5974 O O      . ARG C 3 42  ? 46.738 16.817  66.038 1.00 69.27  ?  42  ARG C O      1 
ATOM   5975 C CB     . ARG C 3 42  ? 45.092 15.082  64.336 1.00 68.64  ?  42  ARG C CB     1 
ATOM   5976 C CG     . ARG C 3 42  ? 44.619 14.111  63.281 1.00 71.84  ?  42  ARG C CG     1 
ATOM   5977 C CD     . ARG C 3 42  ? 43.562 13.202  63.872 1.00 78.14  ?  42  ARG C CD     1 
ATOM   5978 N NE     . ARG C 3 42  ? 42.637 13.932  64.729 1.00 80.59  ?  42  ARG C NE     1 
ATOM   5979 C CZ     . ARG C 3 42  ? 42.309 13.551  65.953 1.00 73.82  ?  42  ARG C CZ     1 
ATOM   5980 N NH1    . ARG C 3 42  ? 42.822 12.443  66.451 1.00 73.53  ?  42  ARG C NH1    1 
ATOM   5981 N NH2    . ARG C 3 42  ? 41.459 14.268  66.672 1.00 67.56  ?  42  ARG C NH2    1 
ATOM   5982 N N      . LEU C 3 43  ? 46.340 18.276  64.431 1.00 38.96  ?  43  LEU C N      1 
ATOM   5983 C CA     . LEU C 3 43  ? 46.487 19.445  65.239 1.00 34.29  ?  43  LEU C CA     1 
ATOM   5984 C C      . LEU C 3 43  ? 45.138 20.065  65.421 1.00 36.67  ?  43  LEU C C      1 
ATOM   5985 O O      . LEU C 3 43  ? 44.434 20.281  64.462 1.00 34.62  ?  43  LEU C O      1 
ATOM   5986 C CB     . LEU C 3 43  ? 47.498 20.408  64.631 1.00 32.35  ?  43  LEU C CB     1 
ATOM   5987 C CG     . LEU C 3 43  ? 48.965 20.018  64.726 1.00 32.12  ?  43  LEU C CG     1 
ATOM   5988 C CD1    . LEU C 3 43  ? 49.785 20.889  63.805 1.00 33.70  ?  43  LEU C CD1    1 
ATOM   5989 C CD2    . LEU C 3 43  ? 49.458 20.163  66.148 1.00 30.46  ?  43  LEU C CD2    1 
ATOM   5990 N N      . ILE C 3 44  ? 44.763 20.306  66.663 1.00 39.29  ?  44  ILE C N      1 
ATOM   5991 C CA     . ILE C 3 44  ? 43.481 20.921  67.006 1.00 38.96  ?  44  ILE C CA     1 
ATOM   5992 C C      . ILE C 3 44  ? 43.739 22.309  67.583 1.00 34.26  ?  44  ILE C C      1 
ATOM   5993 O O      . ILE C 3 44  ? 44.704 22.517  68.326 1.00 30.58  ?  44  ILE C O      1 
ATOM   5994 C CB     . ILE C 3 44  ? 42.697 20.048  68.007 1.00 37.82  ?  44  ILE C CB     1 
ATOM   5995 C CG1    . ILE C 3 44  ? 42.211 18.774  67.332 1.00 38.42  ?  44  ILE C CG1    1 
ATOM   5996 C CG2    . ILE C 3 44  ? 41.566 20.817  68.649 1.00 37.32  ?  44  ILE C CG2    1 
ATOM   5997 C CD1    . ILE C 3 44  ? 43.186 17.630  67.510 1.00 36.42  ?  44  ILE C CD1    1 
ATOM   5998 N N      . PHE C 3 45  ? 42.890 23.265  67.202 1.00 37.36  ?  45  PHE C N      1 
ATOM   5999 C CA     . PHE C 3 45  ? 42.866 24.623  67.737 1.00 34.86  ?  45  PHE C CA     1 
ATOM   6000 C C      . PHE C 3 45  ? 41.416 25.089  67.800 1.00 41.51  ?  45  PHE C C      1 
ATOM   6001 O O      . PHE C 3 45  ? 40.694 24.997  66.804 1.00 42.25  ?  45  PHE C O      1 
ATOM   6002 C CB     . PHE C 3 45  ? 43.685 25.581  66.868 1.00 30.49  ?  45  PHE C CB     1 
ATOM   6003 C CG     . PHE C 3 45  ? 43.814 26.964  67.437 1.00 36.98  ?  45  PHE C CG     1 
ATOM   6004 C CD1    . PHE C 3 45  ? 44.710 27.222  68.462 1.00 31.36  ?  45  PHE C CD1    1 
ATOM   6005 C CD2    . PHE C 3 45  ? 43.056 28.023  66.927 1.00 44.81  ?  45  PHE C CD2    1 
ATOM   6006 C CE1    . PHE C 3 45  ? 44.841 28.509  68.973 1.00 39.81  ?  45  PHE C CE1    1 
ATOM   6007 C CE2    . PHE C 3 45  ? 43.179 29.316  67.443 1.00 42.79  ?  45  PHE C CE2    1 
ATOM   6008 C CZ     . PHE C 3 45  ? 44.069 29.558  68.462 1.00 40.06  ?  45  PHE C CZ     1 
ATOM   6009 N N      . ALA C 3 46  ? 40.999 25.625  68.948 1.00 56.60  ?  46  ALA C N      1 
ATOM   6010 C CA     . ALA C 3 46  ? 39.611 26.049  69.118 1.00 60.42  ?  46  ALA C CA     1 
ATOM   6011 C C      . ALA C 3 46  ? 38.635 24.934  68.731 1.00 55.75  ?  46  ALA C C      1 
ATOM   6012 O O      . ALA C 3 46  ? 37.552 25.186  68.191 1.00 54.52  ?  46  ALA C O      1 
ATOM   6013 C CB     . ALA C 3 46  ? 39.316 27.326  68.323 1.00 63.23  ?  46  ALA C CB     1 
ATOM   6014 N N      . GLY C 3 47  ? 39.004 23.691  69.022 1.00 33.43  ?  47  GLY C N      1 
ATOM   6015 C CA     . GLY C 3 47  ? 38.058 22.606  68.898 1.00 35.01  ?  47  GLY C CA     1 
ATOM   6016 C C      . GLY C 3 47  ? 37.868 22.081  67.498 1.00 39.53  ?  47  GLY C C      1 
ATOM   6017 O O      . GLY C 3 47  ? 36.949 21.283  67.271 1.00 46.51  ?  47  GLY C O      1 
ATOM   6018 N N      . LYS C 3 48  ? 38.705 22.505  66.554 1.00 42.45  ?  48  LYS C N      1 
ATOM   6019 C CA     . LYS C 3 48  ? 38.578 22.148  65.145 1.00 47.04  ?  48  LYS C CA     1 
ATOM   6020 C C      . LYS C 3 48  ? 39.897 21.570  64.657 1.00 44.40  ?  48  LYS C C      1 
ATOM   6021 O O      . LYS C 3 48  ? 40.944 22.210  64.789 1.00 41.11  ?  48  LYS C O      1 
ATOM   6022 C CB     . LYS C 3 48  ? 38.181 23.372  64.280 1.00 47.97  ?  48  LYS C CB     1 
ATOM   6023 C CG     . LYS C 3 48  ? 39.306 24.396  64.017 1.00 44.24  ?  48  LYS C CG     1 
ATOM   6024 C CD     . LYS C 3 48  ? 38.779 25.711  63.423 1.00 47.44  ?  48  LYS C CD     1 
ATOM   6025 C CE     . LYS C 3 48  ? 38.454 25.599  61.919 1.00 48.42  ?  48  LYS C CE     1 
ATOM   6026 N NZ     . LYS C 3 48  ? 38.194 26.910  61.198 1.00 42.07  ?  48  LYS C NZ     1 
ATOM   6027 N N      . GLN C 3 49  ? 39.817 20.449  63.944 1.00 61.77  ?  49  GLN C N      1 
ATOM   6028 C CA     . GLN C 3 49  ? 41.013 19.882  63.328 1.00 67.62  ?  49  GLN C CA     1 
ATOM   6029 C C      . GLN C 3 49  ? 41.512 20.856  62.270 1.00 65.67  ?  49  GLN C C      1 
ATOM   6030 O O      . GLN C 3 49  ? 40.767 21.210  61.355 1.00 71.72  ?  49  GLN C O      1 
ATOM   6031 C CB     . GLN C 3 49  ? 40.686 18.539  62.682 1.00 68.69  ?  49  GLN C CB     1 
ATOM   6032 C CG     . GLN C 3 49  ? 41.890 17.794  62.135 1.00 72.64  ?  49  GLN C CG     1 
ATOM   6033 C CD     . GLN C 3 49  ? 41.534 16.402  61.661 1.00 77.61  ?  49  GLN C CD     1 
ATOM   6034 O OE1    . GLN C 3 49  ? 40.400 15.947  61.821 1.00 81.00  ?  49  GLN C OE1    1 
ATOM   6035 N NE2    . GLN C 3 49  ? 42.502 15.716  61.066 1.00 76.21  ?  49  GLN C NE2    1 
ATOM   6036 N N      . LEU C 3 50  ? 42.758 21.288  62.381 1.00 45.50  ?  50  LEU C N      1 
ATOM   6037 C CA     . LEU C 3 50  ? 43.345 22.257  61.458 1.00 39.27  ?  50  LEU C CA     1 
ATOM   6038 C C      . LEU C 3 50  ? 43.713 21.584  60.126 1.00 39.21  ?  50  LEU C C      1 
ATOM   6039 O O      . LEU C 3 50  ? 44.388 20.542  60.117 1.00 36.65  ?  50  LEU C O      1 
ATOM   6040 C CB     . LEU C 3 50  ? 44.589 22.890  62.088 1.00 39.36  ?  50  LEU C CB     1 
ATOM   6041 C CG     . LEU C 3 50  ? 44.540 23.534  63.485 1.00 36.19  ?  50  LEU C CG     1 
ATOM   6042 C CD1    . LEU C 3 50  ? 45.808 24.419  63.795 1.00 26.33  ?  50  LEU C CD1    1 
ATOM   6043 C CD2    . LEU C 3 50  ? 43.265 24.327  63.661 1.00 37.29  ?  50  LEU C CD2    1 
ATOM   6044 N N      . GLU C 3 51  ? 43.229 22.143  59.005 1.00 49.37  ?  51  GLU C N      1 
ATOM   6045 C CA     . GLU C 3 51  ? 43.543 21.646  57.658 1.00 50.73  ?  51  GLU C CA     1 
ATOM   6046 C C      . GLU C 3 51  ? 44.901 22.121  57.241 1.00 53.67  ?  51  GLU C C      1 
ATOM   6047 O O      . GLU C 3 51  ? 45.200 23.296  57.321 1.00 59.84  ?  51  GLU C O      1 
ATOM   6048 C CB     . GLU C 3 51  ? 42.511 22.069  56.651 1.00 52.52  ?  51  GLU C CB     1 
ATOM   6049 C CG     . GLU C 3 51  ? 41.149 21.447  56.852 1.00 64.25  ?  51  GLU C CG     1 
ATOM   6050 C CD     . GLU C 3 51  ? 40.292 21.567  55.617 1.00 73.17  ?  51  GLU C CD     1 
ATOM   6051 O OE1    . GLU C 3 51  ? 40.861 21.746  54.524 1.00 72.80  ?  51  GLU C OE1    1 
ATOM   6052 O OE2    . GLU C 3 51  ? 39.055 21.487  55.738 1.00 74.90  -1 51  GLU C OE2    1 
ATOM   6053 N N      . ASP C 3 52  ? 45.723 21.224  56.754 1.00 62.15  ?  52  ASP C N      1 
ATOM   6054 C CA     . ASP C 3 52  ? 47.123 21.578  56.532 1.00 72.21  ?  52  ASP C CA     1 
ATOM   6055 C C      . ASP C 3 52  ? 47.329 22.526  55.352 1.00 73.01  ?  52  ASP C C      1 
ATOM   6056 O O      . ASP C 3 52  ? 48.419 23.091  55.222 1.00 71.95  ?  52  ASP C O      1 
ATOM   6057 C CB     . ASP C 3 52  ? 47.952 20.305  56.357 1.00 74.85  ?  52  ASP C CB     1 
ATOM   6058 C CG     . ASP C 3 52  ? 47.287 19.304  55.445 1.00 80.80  ?  52  ASP C CG     1 
ATOM   6059 O OD1    . ASP C 3 52  ? 46.084 19.494  55.141 1.00 80.79  ?  52  ASP C OD1    1 
ATOM   6060 O OD2    . ASP C 3 52  ? 47.963 18.331  55.033 1.00 82.31  -1 52  ASP C OD2    1 
ATOM   6061 N N      . GLY C 3 53  ? 46.315 22.730  54.510 1.00 70.89  ?  53  GLY C N      1 
ATOM   6062 C CA     . GLY C 3 53  ? 46.403 23.682  53.423 1.00 67.49  ?  53  GLY C CA     1 
ATOM   6063 C C      . GLY C 3 53  ? 46.130 25.129  53.773 1.00 66.95  ?  53  GLY C C      1 
ATOM   6064 O O      . GLY C 3 53  ? 46.303 25.997  52.923 1.00 67.47  ?  53  GLY C O      1 
ATOM   6065 N N      . ARG C 3 54  ? 45.694 25.429  54.991 1.00 62.73  ?  54  ARG C N      1 
ATOM   6066 C CA     . ARG C 3 54  ? 45.534 26.804  55.425 1.00 61.56  ?  54  ARG C CA     1 
ATOM   6067 C C      . ARG C 3 54  ? 46.737 27.209  56.276 1.00 59.74  ?  54  ARG C C      1 
ATOM   6068 O O      . ARG C 3 54  ? 47.668 26.430  56.494 1.00 56.89  ?  54  ARG C O      1 
ATOM   6069 C CB     . ARG C 3 54  ? 44.214 26.982  56.180 1.00 65.45  ?  54  ARG C CB     1 
ATOM   6070 C CG     . ARG C 3 54  ? 42.945 26.926  55.308 1.00 71.64  ?  54  ARG C CG     1 
ATOM   6071 C CD     . ARG C 3 54  ? 42.200 25.591  55.472 1.00 76.54  ?  54  ARG C CD     1 
ATOM   6072 N NE     . ARG C 3 54  ? 40.864 25.578  54.866 1.00 74.65  ?  54  ARG C NE     1 
ATOM   6073 C CZ     . ARG C 3 54  ? 40.629 25.379  53.571 1.00 69.63  ?  54  ARG C CZ     1 
ATOM   6074 N NH1    . ARG C 3 54  ? 41.642 25.186  52.733 1.00 68.81  ?  54  ARG C NH1    1 
ATOM   6075 N NH2    . ARG C 3 54  ? 39.381 25.373  53.115 1.00 66.65  ?  54  ARG C NH2    1 
ATOM   6076 N N      . THR C 3 55  ? 46.694 28.451  56.740 1.00 67.88  ?  55  THR C N      1 
ATOM   6077 C CA     . THR C 3 55  ? 47.798 28.991  57.504 1.00 72.97  ?  55  THR C CA     1 
ATOM   6078 C C      . THR C 3 55  ? 47.404 29.370  58.895 1.00 73.61  ?  55  THR C C      1 
ATOM   6079 O O      . THR C 3 55  ? 46.244 29.365  59.238 1.00 70.10  ?  55  THR C O      1 
ATOM   6080 C CB     . THR C 3 55  ? 48.290 30.282  56.851 1.00 78.01  ?  55  THR C CB     1 
ATOM   6081 O OG1    . THR C 3 55  ? 47.214 31.222  56.801 1.00 80.66  ?  55  THR C OG1    1 
ATOM   6082 C CG2    . THR C 3 55  ? 48.771 30.035  55.445 1.00 79.06  ?  55  THR C CG2    1 
ATOM   6083 N N      . LEU C 3 56  ? 48.388 29.738  59.699 1.00 66.86  ?  56  LEU C N      1 
ATOM   6084 C CA     . LEU C 3 56  ? 48.124 30.115  61.067 1.00 60.51  ?  56  LEU C CA     1 
ATOM   6085 C C      . LEU C 3 56  ? 47.449 31.447  61.096 1.00 63.34  ?  56  LEU C C      1 
ATOM   6086 O O      . LEU C 3 56  ? 46.756 31.759  62.031 1.00 66.62  ?  56  LEU C O      1 
ATOM   6087 C CB     . LEU C 3 56  ? 49.416 30.166  61.854 1.00 52.10  ?  56  LEU C CB     1 
ATOM   6088 C CG     . LEU C 3 56  ? 50.400 29.024  61.721 1.00 46.10  ?  56  LEU C CG     1 
ATOM   6089 C CD1    . LEU C 3 56  ? 51.759 29.661  61.783 1.00 47.83  ?  56  LEU C CD1    1 
ATOM   6090 C CD2    . LEU C 3 56  ? 50.264 27.984  62.812 1.00 47.28  ?  56  LEU C CD2    1 
ATOM   6091 N N      . SER C 3 57  ? 47.624 32.244  60.060 1.00 81.26  ?  57  SER C N      1 
ATOM   6092 C CA     . SER C 3 57  ? 46.922 33.516  59.978 1.00 82.02  ?  57  SER C CA     1 
ATOM   6093 C C      . SER C 3 57  ? 45.465 33.302  59.683 1.00 76.42  ?  57  SER C C      1 
ATOM   6094 O O      . SER C 3 57  ? 44.624 34.070  60.101 1.00 78.40  ?  57  SER C O      1 
ATOM   6095 C CB     . SER C 3 57  ? 47.538 34.384  58.897 1.00 82.62  ?  57  SER C CB     1 
ATOM   6096 O OG     . SER C 3 57  ? 48.864 34.741  59.221 1.00 81.20  ?  57  SER C OG     1 
ATOM   6097 N N      . ASP C 3 58  ? 45.164 32.235  58.978 1.00 67.12  ?  58  ASP C N      1 
ATOM   6098 C CA     . ASP C 3 58  ? 43.789 31.907  58.672 1.00 68.39  ?  58  ASP C CA     1 
ATOM   6099 C C      . ASP C 3 58  ? 43.005 31.360  59.865 1.00 61.97  ?  58  ASP C C      1 
ATOM   6100 O O      . ASP C 3 58  ? 41.789 31.467  59.892 1.00 61.84  ?  58  ASP C O      1 
ATOM   6101 C CB     . ASP C 3 58  ? 43.768 30.899  57.518 1.00 72.72  ?  58  ASP C CB     1 
ATOM   6102 C CG     . ASP C 3 58  ? 43.907 31.546  56.177 1.00 73.56  ?  58  ASP C CG     1 
ATOM   6103 O OD1    . ASP C 3 58  ? 43.187 32.528  55.918 1.00 74.14  ?  58  ASP C OD1    1 
ATOM   6104 O OD2    . ASP C 3 58  ? 44.731 31.066  55.378 1.00 74.82  -1 58  ASP C OD2    1 
ATOM   6105 N N      . TYR C 3 59  ? 43.679 30.757  60.834 1.00 47.82  ?  59  TYR C N      1 
ATOM   6106 C CA     . TYR C 3 59  ? 43.012 30.278  62.044 1.00 52.87  ?  59  TYR C CA     1 
ATOM   6107 C C      . TYR C 3 59  ? 43.057 31.287  63.187 1.00 49.70  ?  59  TYR C C      1 
ATOM   6108 O O      . TYR C 3 59  ? 42.675 30.950  64.312 1.00 48.87  ?  59  TYR C O      1 
ATOM   6109 C CB     . TYR C 3 59  ? 43.618 28.940  62.498 1.00 53.86  ?  59  TYR C CB     1 
ATOM   6110 C CG     . TYR C 3 59  ? 43.279 27.824  61.548 1.00 49.85  ?  59  TYR C CG     1 
ATOM   6111 C CD1    . TYR C 3 59  ? 41.991 27.311  61.496 1.00 48.20  ?  59  TYR C CD1    1 
ATOM   6112 C CD2    . TYR C 3 59  ? 44.232 27.307  60.671 1.00 47.71  ?  59  TYR C CD2    1 
ATOM   6113 C CE1    . TYR C 3 59  ? 41.652 26.304  60.605 1.00 44.14  ?  59  TYR C CE1    1 
ATOM   6114 C CE2    . TYR C 3 59  ? 43.903 26.296  59.783 1.00 45.60  ?  59  TYR C CE2    1 
ATOM   6115 C CZ     . TYR C 3 59  ? 42.605 25.801  59.755 1.00 42.88  ?  59  TYR C CZ     1 
ATOM   6116 O OH     . TYR C 3 59  ? 42.254 24.811  58.871 1.00 41.58  ?  59  TYR C OH     1 
ATOM   6117 N N      . ASN C 3 60  ? 43.554 32.495  62.939 1.00 49.58  ?  60  ASN C N      1 
ATOM   6118 C CA     . ASN C 3 60  ? 43.811 33.453  63.996 1.00 52.93  ?  60  ASN C CA     1 
ATOM   6119 C C      . ASN C 3 60  ? 44.763 32.875  65.025 1.00 57.38  ?  60  ASN C C      1 
ATOM   6120 O O      . ASN C 3 60  ? 44.803 33.312  66.180 1.00 53.55  ?  60  ASN C O      1 
ATOM   6121 C CB     . ASN C 3 60  ? 42.507 33.901  64.657 1.00 54.81  ?  60  ASN C CB     1 
ATOM   6122 C CG     . ASN C 3 60  ? 42.546 35.340  65.049 1.00 56.83  ?  60  ASN C CG     1 
ATOM   6123 O OD1    . ASN C 3 60  ? 43.454 36.062  64.634 1.00 59.10  ?  60  ASN C OD1    1 
ATOM   6124 N ND2    . ASN C 3 60  ? 41.574 35.781  65.844 1.00 53.07  ?  60  ASN C ND2    1 
ATOM   6125 N N      . ILE C 3 61  ? 45.524 31.869  64.609 1.00 69.05  ?  61  ILE C N      1 
ATOM   6126 C CA     . ILE C 3 61  ? 46.542 31.309  65.471 1.00 69.72  ?  61  ILE C CA     1 
ATOM   6127 C C      . ILE C 3 61  ? 47.650 32.339  65.608 1.00 72.64  ?  61  ILE C C      1 
ATOM   6128 O O      . ILE C 3 61  ? 48.178 32.843  64.607 1.00 72.39  ?  61  ILE C O      1 
ATOM   6129 C CB     . ILE C 3 61  ? 47.031 29.966  64.911 1.00 61.97  ?  61  ILE C CB     1 
ATOM   6130 C CG1    . ILE C 3 61  ? 45.925 28.925  65.086 1.00 55.23  ?  61  ILE C CG1    1 
ATOM   6131 C CG2    . ILE C 3 61  ? 48.304 29.517  65.600 1.00 64.69  ?  61  ILE C CG2    1 
ATOM   6132 C CD1    . ILE C 3 61  ? 46.372 27.535  64.793 1.00 56.16  ?  61  ILE C CD1    1 
ATOM   6133 N N      . GLN C 3 62  ? 47.960 32.704  66.854 1.00 71.64  ?  62  GLN C N      1 
ATOM   6134 C CA     . GLN C 3 62  ? 48.820 33.850  67.119 1.00 71.73  ?  62  GLN C CA     1 
ATOM   6135 C C      . GLN C 3 62  ? 49.923 33.524  68.120 1.00 71.88  ?  62  GLN C C      1 
ATOM   6136 O O      . GLN C 3 62  ? 50.103 32.363  68.505 1.00 69.33  ?  62  GLN C O      1 
ATOM   6137 C CB     . GLN C 3 62  ? 47.978 35.028  67.614 1.00 72.51  ?  62  GLN C CB     1 
ATOM   6138 C CG     . GLN C 3 62  ? 48.101 36.277  66.743 1.00 78.16  ?  62  GLN C CG     1 
ATOM   6139 C CD     . GLN C 3 62  ? 47.659 36.044  65.303 1.00 79.11  ?  62  GLN C CD     1 
ATOM   6140 O OE1    . GLN C 3 62  ? 48.425 35.545  64.470 1.00 83.06  ?  62  GLN C OE1    1 
ATOM   6141 N NE2    . GLN C 3 62  ? 46.414 36.402  65.010 1.00 77.35  ?  62  GLN C NE2    1 
ATOM   6142 N N      . LYS C 3 63  ? 50.674 34.546  68.531 1.00 72.31  ?  63  LYS C N      1 
ATOM   6143 C CA     . LYS C 3 63  ? 51.808 34.342  69.421 1.00 72.31  ?  63  LYS C CA     1 
ATOM   6144 C C      . LYS C 3 63  ? 51.336 33.807  70.769 1.00 75.12  ?  63  LYS C C      1 
ATOM   6145 O O      . LYS C 3 63  ? 50.256 34.149  71.250 1.00 79.90  ?  63  LYS C O      1 
ATOM   6146 C CB     . LYS C 3 63  ? 52.574 35.650  69.609 1.00 75.64  ?  63  LYS C CB     1 
ATOM   6147 C CG     . LYS C 3 63  ? 53.878 35.526  70.396 1.00 82.00  ?  63  LYS C CG     1 
ATOM   6148 C CD     . LYS C 3 63  ? 54.982 34.895  69.556 1.00 82.62  ?  63  LYS C CD     1 
ATOM   6149 C CE     . LYS C 3 63  ? 56.370 35.055  70.190 1.00 81.70  ?  63  LYS C CE     1 
ATOM   6150 N NZ     . LYS C 3 63  ? 56.865 36.472  70.159 1.00 78.77  ?  63  LYS C NZ     1 
ATOM   6151 N N      . GLU C 3 64  ? 52.139 32.935  71.362 1.00 73.29  ?  64  GLU C N      1 
ATOM   6152 C CA     . GLU C 3 64  ? 51.814 32.300  72.640 1.00 69.71  ?  64  GLU C CA     1 
ATOM   6153 C C      . GLU C 3 64  ? 50.581 31.420  72.609 1.00 65.52  ?  64  GLU C C      1 
ATOM   6154 O O      . GLU C 3 64  ? 50.084 31.040  73.650 1.00 71.79  ?  64  GLU C O      1 
ATOM   6155 C CB     . GLU C 3 64  ? 51.793 33.274  73.823 1.00 68.54  ?  64  GLU C CB     1 
ATOM   6156 C CG     . GLU C 3 64  ? 52.815 34.400  73.788 1.00 70.29  ?  64  GLU C CG     1 
ATOM   6157 C CD     . GLU C 3 64  ? 54.128 34.055  74.452 1.00 73.13  ?  64  GLU C CD     1 
ATOM   6158 O OE1    . GLU C 3 64  ? 54.314 32.896  74.859 1.00 73.12  ?  64  GLU C OE1    1 
ATOM   6159 O OE2    . GLU C 3 64  ? 54.979 34.954  74.569 1.00 73.69  -1 64  GLU C OE2    1 
ATOM   6160 N N      . SER C 3 65  ? 50.117 31.062  71.423 1.00 44.58  ?  65  SER C N      1 
ATOM   6161 C CA     . SER C 3 65  ? 48.930 30.230  71.305 1.00 40.06  ?  65  SER C CA     1 
ATOM   6162 C C      . SER C 3 65  ? 49.311 28.765  71.447 1.00 47.07  ?  65  SER C C      1 
ATOM   6163 O O      . SER C 3 65  ? 50.388 28.336  71.029 1.00 48.96  ?  65  SER C O      1 
ATOM   6164 C CB     . SER C 3 65  ? 48.240 30.438  69.956 1.00 44.93  ?  65  SER C CB     1 
ATOM   6165 O OG     . SER C 3 65  ? 47.730 31.750  69.808 1.00 49.97  ?  65  SER C OG     1 
ATOM   6166 N N      . THR C 3 66  ? 48.417 27.989  72.028 1.00 56.68  ?  66  THR C N      1 
ATOM   6167 C CA     . THR C 3 66  ? 48.655 26.570  72.190 1.00 58.86  ?  66  THR C CA     1 
ATOM   6168 C C      . THR C 3 66  ? 47.793 25.795  71.212 1.00 55.75  ?  66  THR C C      1 
ATOM   6169 O O      . THR C 3 66  ? 46.595 26.070  71.076 1.00 53.91  ?  66  THR C O      1 
ATOM   6170 C CB     . THR C 3 66  ? 48.359 26.109  73.613 1.00 63.52  ?  66  THR C CB     1 
ATOM   6171 O OG1    . THR C 3 66  ? 49.216 26.810  74.527 1.00 63.68  ?  66  THR C OG1    1 
ATOM   6172 C CG2    . THR C 3 66  ? 48.597 24.601  73.729 1.00 64.32  ?  66  THR C CG2    1 
ATOM   6173 N N      . LEU C 3 67  ? 48.415 24.822  70.550 1.00 47.79  ?  67  LEU C N      1 
ATOM   6174 C CA     . LEU C 3 67  ? 47.737 23.864  69.691 1.00 46.03  ?  67  LEU C CA     1 
ATOM   6175 C C      . LEU C 3 67  ? 47.815 22.490  70.335 1.00 45.38  ?  67  LEU C C      1 
ATOM   6176 O O      . LEU C 3 67  ? 48.654 22.232  71.207 1.00 47.15  ?  67  LEU C O      1 
ATOM   6177 C CB     . LEU C 3 67  ? 48.345 23.815  68.287 1.00 43.85  ?  67  LEU C CB     1 
ATOM   6178 C CG     . LEU C 3 67  ? 48.196 25.101  67.478 1.00 51.15  ?  67  LEU C CG     1 
ATOM   6179 C CD1    . LEU C 3 67  ? 48.932 26.271  68.165 1.00 51.70  ?  67  LEU C CD1    1 
ATOM   6180 C CD2    . LEU C 3 67  ? 48.676 24.903  66.041 1.00 49.14  ?  67  LEU C CD2    1 
ATOM   6181 N N      . HIS C 3 68  ? 46.896 21.616  69.940 1.00 29.56  ?  68  HIS C N      1 
ATOM   6182 C CA     . HIS C 3 68  ? 46.881 20.268  70.473 1.00 31.54  ?  68  HIS C CA     1 
ATOM   6183 C C      . HIS C 3 68  ? 47.204 19.266  69.386 1.00 31.13  ?  68  HIS C C      1 
ATOM   6184 O O      . HIS C 3 68  ? 46.726 19.381  68.243 1.00 28.40  ?  68  HIS C O      1 
ATOM   6185 C CB     . HIS C 3 68  ? 45.552 19.947  71.139 1.00 35.47  ?  68  HIS C CB     1 
ATOM   6186 C CG     . HIS C 3 68  ? 45.446 20.521  72.509 1.00 32.83  ?  68  HIS C CG     1 
ATOM   6187 N ND1    . HIS C 3 68  ? 45.058 21.825  72.742 1.00 32.44  ?  68  HIS C ND1    1 
ATOM   6188 C CD2    . HIS C 3 68  ? 45.763 20.000  73.717 1.00 32.85  ?  68  HIS C CD2    1 
ATOM   6189 C CE1    . HIS C 3 68  ? 45.093 22.063  74.043 1.00 31.95  ?  68  HIS C CE1    1 
ATOM   6190 N NE2    . HIS C 3 68  ? 45.515 20.970  74.657 1.00 30.93  ?  68  HIS C NE2    1 
ATOM   6191 N N      . LEU C 3 69  ? 48.031 18.310  69.786 1.00 34.49  ?  69  LEU C N      1 
ATOM   6192 C CA     . LEU C 3 69  ? 48.445 17.279  68.884 1.00 35.97  ?  69  LEU C CA     1 
ATOM   6193 C C      . LEU C 3 69  ? 47.936 15.956  69.320 1.00 35.53  ?  69  LEU C C      1 
ATOM   6194 O O      . LEU C 3 69  ? 48.068 15.615  70.477 1.00 38.73  ?  69  LEU C O      1 
ATOM   6195 C CB     . LEU C 3 69  ? 49.967 17.245  68.769 1.00 33.84  ?  69  LEU C CB     1 
ATOM   6196 C CG     . LEU C 3 69  ? 50.628 16.303  67.777 1.00 32.16  ?  69  LEU C CG     1 
ATOM   6197 C CD1    . LEU C 3 69  ? 50.171 16.556  66.359 1.00 28.43  ?  69  LEU C CD1    1 
ATOM   6198 C CD2    . LEU C 3 69  ? 52.135 16.406  67.883 1.00 36.20  ?  69  LEU C CD2    1 
ATOM   6199 N N      . VAL C 3 70  ? 47.324 15.233  68.411 1.00 33.41  ?  70  VAL C N      1 
ATOM   6200 C CA     . VAL C 3 70  ? 46.784 13.898  68.643 1.00 35.81  ?  70  VAL C CA     1 
ATOM   6201 C C      . VAL C 3 70  ? 47.278 13.012  67.504 1.00 42.44  ?  70  VAL C C      1 
ATOM   6202 O O      . VAL C 3 70  ? 46.936 13.242  66.335 1.00 36.57  ?  70  VAL C O      1 
ATOM   6203 C CB     . VAL C 3 70  ? 45.243 13.894  68.716 1.00 33.61  ?  70  VAL C CB     1 
ATOM   6204 C CG1    . VAL C 3 70  ? 44.721 12.518  69.113 1.00 27.55  ?  70  VAL C CG1    1 
ATOM   6205 C CG2    . VAL C 3 70  ? 44.735 14.969  69.687 1.00 30.75  ?  70  VAL C CG2    1 
ATOM   6206 N N      . LEU C 3 71  ? 48.075 12.019  67.838 1.00 50.98  ?  71  LEU C N      1 
ATOM   6207 C CA     . LEU C 3 71  ? 48.619 11.121  66.852 1.00 43.94  ?  71  LEU C CA     1 
ATOM   6208 C C      . LEU C 3 71  ? 47.713 10.006  66.413 1.00 40.31  ?  71  LEU C C      1 
ATOM   6209 O O      . LEU C 3 71  ? 47.199 9.251   67.201 1.00 34.12  ?  71  LEU C O      1 
ATOM   6210 C CB     . LEU C 3 71  ? 49.946 10.588  67.367 1.00 46.58  ?  71  LEU C CB     1 
ATOM   6211 C CG     . LEU C 3 71  ? 51.112 11.569  67.225 1.00 47.58  ?  71  LEU C CG     1 
ATOM   6212 C CD1    . LEU C 3 71  ? 51.074 12.181  65.841 1.00 48.25  ?  71  LEU C CD1    1 
ATOM   6213 C CD2    . LEU C 3 71  ? 51.059 12.674  68.260 1.00 43.57  ?  71  LEU C CD2    1 
ATOM   6214 N N      . ARG C 3 72  ? 47.524 9.921   65.119 1.00 42.32  ?  72  ARG C N      1 
ATOM   6215 C CA     . ARG C 3 72  ? 46.661 8.922   64.575 1.00 45.59  ?  72  ARG C CA     1 
ATOM   6216 C C      . ARG C 3 72  ? 47.284 7.571   64.707 1.00 47.31  ?  72  ARG C C      1 
ATOM   6217 O O      . ARG C 3 72  ? 48.494 7.417   64.649 1.00 47.55  ?  72  ARG C O      1 
ATOM   6218 C CB     . ARG C 3 72  ? 46.243 9.256   63.151 1.00 36.72  ?  72  ARG C CB     1 
ATOM   6219 C CG     . ARG C 3 72  ? 45.411 10.503  63.029 1.00 34.62  ?  72  ARG C CG     1 
ATOM   6220 C CD     . ARG C 3 72  ? 45.479 11.062  61.623 1.00 39.90  ?  72  ARG C CD     1 
ATOM   6221 N NE     . ARG C 3 72  ? 45.201 10.043  60.629 1.00 43.49  ?  72  ARG C NE     1 
ATOM   6222 C CZ     . ARG C 3 72  ? 44.650 10.290  59.448 1.00 54.95  ?  72  ARG C CZ     1 
ATOM   6223 N NH1    . ARG C 3 72  ? 44.295 11.521  59.127 1.00 61.06  ?  72  ARG C NH1    1 
ATOM   6224 N NH2    . ARG C 3 72  ? 44.429 9.303   58.597 1.00 55.16  ?  72  ARG C NH2    1 
ATOM   6225 N N      . LEU C 3 73  ? 46.436 6.584   64.907 1.00 45.33  ?  73  LEU C N      1 
ATOM   6226 C CA     . LEU C 3 73  ? 46.896 5.252   65.106 1.00 51.05  ?  73  LEU C CA     1 
ATOM   6227 C C      . LEU C 3 73  ? 46.217 4.209   64.209 1.00 50.95  ?  73  LEU C C      1 
ATOM   6228 O O      . LEU C 3 73  ? 45.117 3.781   64.508 1.00 48.31  ?  73  LEU C O      1 
ATOM   6229 C CB     . LEU C 3 73  ? 46.593 4.917   66.560 1.00 52.44  ?  73  LEU C CB     1 
ATOM   6230 C CG     . LEU C 3 73  ? 47.184 5.757   67.681 1.00 48.72  ?  73  LEU C CG     1 
ATOM   6231 C CD1    . LEU C 3 73  ? 46.480 5.448   68.982 1.00 52.53  ?  73  LEU C CD1    1 
ATOM   6232 C CD2    . LEU C 3 73  ? 48.675 5.495   67.803 1.00 47.55  ?  73  LEU C CD2    1 
ATOM   6233 N N      . ARG C 3 74  ? 46.844 3.812   63.099 1.00 54.48  ?  74  ARG C N      1 
ATOM   6234 C CA     . ARG C 3 74  ? 46.279 2.717   62.339 1.00 55.00  ?  74  ARG C CA     1 
ATOM   6235 C C      . ARG C 3 74  ? 47.152 1.485   62.289 1.00 62.70  ?  74  ARG C C      1 
ATOM   6236 O O      . ARG C 3 74  ? 47.864 1.284   61.327 1.00 65.30  ?  74  ARG C O      1 
ATOM   6237 C CB     . ARG C 3 74  ? 45.888 3.140   60.946 1.00 60.16  ?  74  ARG C CB     1 
ATOM   6238 C CG     . ARG C 3 74  ? 44.694 2.363   60.413 1.00 67.12  ?  74  ARG C CG     1 
ATOM   6239 C CD     . ARG C 3 74  ? 43.523 2.430   61.389 1.00 68.66  ?  74  ARG C CD     1 
ATOM   6240 N NE     . ARG C 3 74  ? 42.756 3.664   61.257 1.00 68.01  ?  74  ARG C NE     1 
ATOM   6241 C CZ     . ARG C 3 74  ? 41.979 4.166   62.211 1.00 62.83  ?  74  ARG C CZ     1 
ATOM   6242 N NH1    . ARG C 3 74  ? 41.887 3.551   63.378 1.00 57.80  ?  74  ARG C NH1    1 
ATOM   6243 N NH2    . ARG C 3 74  ? 41.311 5.293   62.001 1.00 58.30  ?  74  ARG C NH2    1 
ATOM   6244 N N      . GLY C 3 75  ? 47.100 0.657   63.316 1.00 76.03  ?  75  GLY C N      1 
ATOM   6245 C CA     . GLY C 3 75  ? 47.823 -0.599  63.349 1.00 80.21  ?  75  GLY C CA     1 
ATOM   6246 C C      . GLY C 3 75  ? 46.909 -1.764  63.033 1.00 84.20  ?  75  GLY C C      1 
ATOM   6247 O O      . GLY C 3 75  ? 47.340 -2.922  62.984 1.00 91.49  ?  75  GLY C O      1 
ATOM   6248 N N      . GLY C 3 76  ? 45.628 -1.461  62.845 1.00 62.24  ?  76  GLY C N      1 
ATOM   6249 C CA     . GLY C 3 76  ? 44.592 -2.460  62.641 1.00 51.71  ?  76  GLY C CA     1 
ATOM   6250 C C      . GLY C 3 76  ? 43.232 -1.878  63.000 1.00 43.88  ?  76  GLY C C      1 
ATOM   6251 O O      . GLY C 3 76  ? 43.077 -0.656  63.107 1.00 37.50  ?  76  GLY C O      1 
HETATM 6252 P PG     . ANP D 4 .   ? 26.616 20.254  18.430 1.00 45.99  ?  401 ANP A PG     1 
HETATM 6253 O O1G    . ANP D 4 .   ? 28.074 20.618  18.155 1.00 39.06  ?  401 ANP A O1G    1 
HETATM 6254 O O2G    . ANP D 4 .   ? 26.129 19.209  17.456 1.00 43.45  ?  401 ANP A O2G    1 
HETATM 6255 O O3G    . ANP D 4 .   ? 26.511 19.583  19.777 1.00 45.28  ?  401 ANP A O3G    1 
HETATM 6256 P PB     . ANP D 4 .   ? 25.680 23.048  17.456 1.00 28.19  ?  401 ANP A PB     1 
HETATM 6257 O O1B    . ANP D 4 .   ? 24.507 23.190  16.530 1.00 38.42  ?  401 ANP A O1B    1 
HETATM 6258 O O2B    . ANP D 4 .   ? 25.657 24.271  18.335 1.00 28.60  ?  401 ANP A O2B    1 
HETATM 6259 N N3B    . ANP D 4 .   ? 25.559 21.612  18.394 1.00 35.88  ?  401 ANP A N3B    1 
HETATM 6260 P PA     . ANP D 4 .   ? 27.409 22.392  15.101 1.00 36.74  ?  401 ANP A PA     1 
HETATM 6261 O O1A    . ANP D 4 .   ? 28.457 21.351  15.317 1.00 27.84  -1 401 ANP A O1A    1 
HETATM 6262 O O2A    . ANP D 4 .   ? 26.209 21.833  14.396 1.00 29.62  ?  401 ANP A O2A    1 
HETATM 6263 O O3A    . ANP D 4 .   ? 27.074 23.104  16.564 1.00 41.24  ?  401 ANP A O3A    1 
HETATM 6264 O "O5'"  . ANP D 4 .   ? 28.067 23.557  14.180 1.00 35.05  ?  401 ANP A "O5'"  1 
HETATM 6265 C "C5'"  . ANP D 4 .   ? 28.903 24.303  14.992 1.00 41.88  ?  401 ANP A "C5'"  1 
HETATM 6266 C "C4'"  . ANP D 4 .   ? 29.779 25.302  14.215 1.00 39.90  ?  401 ANP A "C4'"  1 
HETATM 6267 O "O4'"  . ANP D 4 .   ? 30.640 24.684  13.465 1.00 40.25  ?  401 ANP A "O4'"  1 
HETATM 6268 C "C3'"  . ANP D 4 .   ? 28.877 26.081  13.263 1.00 28.11  ?  401 ANP A "C3'"  1 
HETATM 6269 O "O3'"  . ANP D 4 .   ? 28.550 27.250  13.856 1.00 32.71  ?  401 ANP A "O3'"  1 
HETATM 6270 C "C2'"  . ANP D 4 .   ? 29.760 26.325  12.029 1.00 30.76  ?  401 ANP A "C2'"  1 
HETATM 6271 O "O2'"  . ANP D 4 .   ? 29.843 27.814  11.797 1.00 29.31  ?  401 ANP A "O2'"  1 
HETATM 6272 C "C1'"  . ANP D 4 .   ? 30.925 25.730  12.283 1.00 32.38  ?  401 ANP A "C1'"  1 
HETATM 6273 N N9     . ANP D 4 .   ? 31.445 24.942  11.177 1.00 33.37  ?  401 ANP A N9     1 
HETATM 6274 C C8     . ANP D 4 .   ? 30.744 24.102  10.402 1.00 28.46  ?  401 ANP A C8     1 
HETATM 6275 N N7     . ANP D 4 .   ? 31.556 23.558  9.499  1.00 30.39  ?  401 ANP A N7     1 
HETATM 6276 C C5     . ANP D 4 .   ? 32.780 24.053  9.707  1.00 34.43  ?  401 ANP A C5     1 
HETATM 6277 C C6     . ANP D 4 .   ? 33.972 23.826  9.071  1.00 33.89  ?  401 ANP A C6     1 
HETATM 6278 N N6     . ANP D 4 .   ? 34.468 23.041  7.968  1.00 44.30  ?  401 ANP A N6     1 
HETATM 6279 N N1     . ANP D 4 .   ? 35.054 24.431  9.497  1.00 37.65  ?  401 ANP A N1     1 
HETATM 6280 C C2     . ANP D 4 .   ? 34.995 25.292  10.542 1.00 33.27  ?  401 ANP A C2     1 
HETATM 6281 N N3     . ANP D 4 .   ? 33.826 25.536  11.179 1.00 28.26  ?  401 ANP A N3     1 
HETATM 6282 C C4     . ANP D 4 .   ? 32.717 24.904  10.750 1.00 34.20  ?  401 ANP A C4     1 
HETATM 6283 H HNB1   . ANP D 4 .   ? 24.879 21.567  18.918 1.00 47.94  ?  401 ANP A HNB1   1 
HETATM 6284 H "H5'1" . ANP D 4 .   ? 29.482 23.698  15.482 1.00 61.15  ?  401 ANP A "H5'1" 1 
HETATM 6285 H "H5'2" . ANP D 4 .   ? 28.360 24.796  15.627 1.00 61.15  ?  401 ANP A "H5'2" 1 
HETATM 6286 H "H4'"  . ANP D 4 .   ? 30.234 25.907  14.821 1.00 56.99  ?  401 ANP A "H4'"  1 
HETATM 6287 H "H3'"  . ANP D 4 .   ? 28.088 25.566  13.031 1.00 31.66  ?  401 ANP A "H3'"  1 
HETATM 6288 H "HO3'" . ANP D 4 .   ? 29.211 27.532  14.311 1.00 41.49  ?  401 ANP A "HO3'" 1 
HETATM 6289 H "H2'"  . ANP D 4 .   ? 29.352 25.900  11.259 1.00 37.29  ?  401 ANP A "H2'"  1 
HETATM 6290 H "HO2'" . ANP D 4 .   ? 30.124 28.195  12.503 1.00 34.17  ?  401 ANP A "HO2'" 1 
HETATM 6291 H "H1'"  . ANP D 4 .   ? 31.578 26.386  12.570 1.00 40.86  ?  401 ANP A "H1'"  1 
HETATM 6292 H H8     . ANP D 4 .   ? 29.830 23.942  10.470 1.00 32.23  ?  401 ANP A H8     1 
HETATM 6293 H HN61   . ANP D 4 .   ? 35.275 22.745  7.980  1.00 65.80  ?  401 ANP A HN61   1 
HETATM 6294 H HN62   . ANP D 4 .   ? 33.956 22.868  7.299  1.00 65.80  ?  401 ANP A HN62   1 
HETATM 6295 H H2     . ANP D 4 .   ? 35.793 25.702  10.788 1.00 42.71  ?  401 ANP A H2     1 
HETATM 6296 N N1     . AR6 E 5 .   ? 38.443 17.337  60.178 1.00 94.15  ?  401 AR6 B N1     1 
HETATM 6297 C C2     . AR6 E 5 .   ? 37.223 17.003  60.664 1.00 94.78  ?  401 AR6 B C2     1 
HETATM 6298 N N3     . AR6 E 5 .   ? 36.846 15.700  60.704 1.00 97.12  ?  401 AR6 B N3     1 
HETATM 6299 C C4     . AR6 E 5 .   ? 37.669 14.716  60.269 1.00 97.04  ?  401 AR6 B C4     1 
HETATM 6300 C C5     . AR6 E 5 .   ? 38.882 15.047  59.789 1.00 97.86  ?  401 AR6 B C5     1 
HETATM 6301 C C6     . AR6 E 5 .   ? 39.260 16.384  59.747 1.00 96.19  ?  401 AR6 B C6     1 
HETATM 6302 N N6     . AR6 E 5 .   ? 40.497 16.947  59.276 1.00 95.61  ?  401 AR6 B N6     1 
HETATM 6303 N N7     . AR6 E 5 .   ? 39.521 13.908  59.423 1.00 96.94  ?  401 AR6 B N7     1 
HETATM 6304 C C8     . AR6 E 5 .   ? 38.723 12.861  59.665 1.00 94.45  ?  401 AR6 B C8     1 
HETATM 6305 N N9     . AR6 E 5 .   ? 37.599 13.371  60.168 1.00 94.16  ?  401 AR6 B N9     1 
HETATM 6306 P PA     . AR6 E 5 .   ? 36.510 7.665   58.983 1.00 104.59 ?  401 AR6 B PA     1 
HETATM 6307 P PB     . AR6 E 5 .   ? 37.256 6.112   61.340 1.00 57.64  ?  401 AR6 B PB     1 
HETATM 6308 C "C1'"  . AR6 E 5 .   ? 36.307 12.906  60.680 1.00 92.84  ?  401 AR6 B "C1'"  1 
HETATM 6309 O O1A    . AR6 E 5 .   ? 37.640 8.519   58.429 1.00 107.36 -1 401 AR6 B O1A    1 
HETATM 6310 O O1B    . AR6 E 5 .   ? 37.680 4.706   61.718 1.00 50.08  -1 401 AR6 B O1B    1 
HETATM 6311 C C1D    . AR6 E 5 .   ? 41.157 10.205  60.300 1.00 74.43  ?  401 AR6 B C1D    1 
HETATM 6312 O O1D    . AR6 E 5 .   ? 42.119 9.199   60.561 1.00 74.72  ?  401 AR6 B O1D    1 
HETATM 6313 C "C2'"  . AR6 E 5 .   ? 35.246 13.075  59.877 1.00 85.41  ?  401 AR6 B "C2'"  1 
HETATM 6314 O "O2'"  . AR6 E 5 .   ? 34.562 14.329  60.117 1.00 75.76  ?  401 AR6 B "O2'"  1 
HETATM 6315 O O2A    . AR6 E 5 .   ? 35.594 7.240   57.859 1.00 110.70 ?  401 AR6 B O2A    1 
HETATM 6316 O O2B    . AR6 E 5 .   ? 35.847 6.295   61.878 1.00 59.29  ?  401 AR6 B O2B    1 
HETATM 6317 C C2D    . AR6 E 5 .   ? 40.932 11.047  61.611 1.00 74.08  ?  401 AR6 B C2D    1 
HETATM 6318 O O2D    . AR6 E 5 .   ? 42.098 11.224  62.296 1.00 70.72  ?  401 AR6 B O2D    1 
HETATM 6319 C "C3'"  . AR6 E 5 .   ? 34.183 11.878  60.215 1.00 93.67  ?  401 AR6 B "C3'"  1 
HETATM 6320 O "O3'"  . AR6 E 5 .   ? 33.222 12.305  61.199 1.00 95.07  ?  401 AR6 B "O3'"  1 
HETATM 6321 O O3A    . AR6 E 5 .   ? 37.200 6.314   59.680 1.00 81.84  ?  401 AR6 B O3A    1 
HETATM 6322 C C3D    . AR6 E 5 .   ? 40.007 10.167  62.405 1.00 71.56  ?  401 AR6 B C3D    1 
HETATM 6323 O O3D    . AR6 E 5 .   ? 40.781 9.718   63.592 1.00 70.78  ?  401 AR6 B O3D    1 
HETATM 6324 C "C4'"  . AR6 E 5 .   ? 34.906 10.803  60.679 1.00 99.02  ?  401 AR6 B "C4'"  1 
HETATM 6325 O "O4'"  . AR6 E 5 .   ? 36.359 11.314  60.810 1.00 98.84  ?  401 AR6 B "O4'"  1 
HETATM 6326 C C4D    . AR6 E 5 .   ? 39.724 9.116   61.603 1.00 71.56  ?  401 AR6 B C4D    1 
HETATM 6327 O O4D    . AR6 E 5 .   ? 40.018 9.642   60.110 1.00 71.44  ?  401 AR6 B O4D    1 
HETATM 6328 C "C5'"  . AR6 E 5 .   ? 34.797 9.608   59.711 1.00 99.91  ?  401 AR6 B "C5'"  1 
HETATM 6329 O "O5'"  . AR6 E 5 .   ? 35.611 8.524   60.114 1.00 103.10 ?  401 AR6 B "O5'"  1 
HETATM 6330 C C5D    . AR6 E 5 .   ? 38.307 8.613   61.716 1.00 66.53  ?  401 AR6 B C5D    1 
HETATM 6331 O O5D    . AR6 E 5 .   ? 38.344 7.209   61.958 1.00 61.92  ?  401 AR6 B O5D    1 
HETATM 6332 H H2     . AR6 E 5 .   ? 36.644 17.665  60.964 1.00 132.13 ?  401 AR6 B H2     1 
HETATM 6333 H HN6    . AR6 E 5 .   ? 40.523 17.764  59.010 1.00 133.96 ?  401 AR6 B HN6    1 
HETATM 6334 H HN6A   . AR6 E 5 .   ? 41.210 16.466  59.262 1.00 133.96 ?  401 AR6 B HN6A   1 
HETATM 6335 H H8     . AR6 E 5 .   ? 38.909 11.965  59.502 1.00 131.36 ?  401 AR6 B H8     1 
HETATM 6336 H "H1'"  . AR6 E 5 .   ? 36.129 13.302  61.548 1.00 127.85 ?  401 AR6 B "H1'"  1 
HETATM 6337 H H1D    . AR6 E 5 .   ? 41.408 10.769  59.551 1.00 88.13  ?  401 AR6 B H1D    1 
HETATM 6338 H "H2'"  . AR6 E 5 .   ? 35.525 13.017  58.950 1.00 112.11 ?  401 AR6 B "H2'"  1 
HETATM 6339 H "HO2'" . AR6 E 5 .   ? 33.729 14.184  60.201 1.00 91.57  ?  401 AR6 B "HO2'" 1 
HETATM 6340 H H2D    . AR6 E 5 .   ? 40.510 11.895  61.408 1.00 87.35  ?  401 AR6 B H2D    1 
HETATM 6341 H HO2D   . AR6 E 5 .   ? 42.206 10.581  62.842 1.00 80.04  ?  401 AR6 B HO2D   1 
HETATM 6342 H "H3'"  . AR6 E 5 .   ? 33.723 11.624  59.401 1.00 129.53 ?  401 AR6 B "H3'"  1 
HETATM 6343 H "HO3'" . AR6 E 5 .   ? 32.446 12.046  60.967 1.00 132.36 ?  401 AR6 B "HO3'" 1 
HETATM 6344 H H3D    . AR6 E 5 .   ? 39.201 10.643  62.660 1.00 81.83  ?  401 AR6 B H3D    1 
HETATM 6345 H HO3D   . AR6 E 5 .   ? 40.858 10.363  64.141 1.00 79.90  ?  401 AR6 B HO3D   1 
HETATM 6346 H "H4'"  . AR6 E 5 .   ? 34.574 10.547  61.554 1.00 140.77 ?  401 AR6 B "H4'"  1 
HETATM 6347 H H4D    . AR6 E 5 .   ? 40.338 8.392   61.807 1.00 81.75  ?  401 AR6 B H4D    1 
HETATM 6348 H "H5'"  . AR6 E 5 .   ? 35.070 9.896   58.824 1.00 142.63 ?  401 AR6 B "H5'"  1 
HETATM 6349 H "H5'A" . AR6 E 5 .   ? 33.874 9.314   59.675 1.00 142.63 ?  401 AR6 B "H5'A" 1 
HETATM 6350 H H5D    . AR6 E 5 .   ? 37.832 8.790   60.888 1.00 70.97  ?  401 AR6 B H5D    1 
HETATM 6351 H H5DA   . AR6 E 5 .   ? 37.859 9.061   62.451 1.00 70.97  ?  401 AR6 B H5DA   1 
HETATM 6352 H HD1    . AR6 E 5 .   ? 42.350 9.234   61.378 1.00 88.51  ?  401 AR6 B HD1    1 
HETATM 6353 O O      . HOH F 6 .   ? 46.026 29.016  14.086 1.00 34.53  ?  501 HOH A O      1 
HETATM 6354 O O      . HOH F 6 .   ? 45.786 7.722   35.241 1.00 33.14  ?  502 HOH A O      1 
HETATM 6355 O O      . HOH F 6 .   ? 52.314 24.686  23.786 1.00 45.58  ?  503 HOH A O      1 
HETATM 6356 O O      . HOH F 6 .   ? 46.868 4.781   40.116 1.00 58.80  ?  504 HOH A O      1 
HETATM 6357 O O      . HOH F 6 .   ? 6.676  12.174  36.639 1.00 21.47  ?  505 HOH A O      1 
HETATM 6358 O O      . HOH F 6 .   ? 23.736 19.497  19.523 1.00 18.99  ?  506 HOH A O      1 
HETATM 6359 O O      . HOH F 6 .   ? 47.980 7.937   28.026 1.00 21.93  ?  507 HOH A O      1 
HETATM 6360 O O      . HOH F 6 .   ? 31.110 44.750  1.887  1.00 37.63  ?  508 HOH A O      1 
HETATM 6361 O O      . HOH F 6 .   ? 2.493  7.338   19.551 1.00 35.43  ?  509 HOH A O      1 
HETATM 6362 O O      . HOH F 6 .   ? 4.603  22.274  26.653 1.00 43.60  ?  510 HOH A O      1 
HETATM 6363 O O      . HOH F 6 .   ? 33.715 27.095  13.617 1.00 20.27  ?  511 HOH A O      1 
HETATM 6364 O O      . HOH F 6 .   ? 41.233 19.118  11.031 1.00 18.87  ?  512 HOH A O      1 
HETATM 6365 O O      . HOH F 6 .   ? 26.234 21.295  9.651  1.00 35.46  ?  513 HOH A O      1 
HETATM 6366 O O      . HOH F 6 .   ? 54.002 13.056  26.290 1.00 21.54  ?  514 HOH A O      1 
HETATM 6367 O O      . HOH F 6 .   ? 49.727 30.758  21.160 1.00 34.20  ?  515 HOH A O      1 
HETATM 6368 O O      . HOH F 6 .   ? 20.336 2.972   29.842 1.00 19.54  ?  516 HOH A O      1 
HETATM 6369 O O      . HOH F 6 .   ? 33.532 10.897  17.079 1.00 19.25  ?  517 HOH A O      1 
HETATM 6370 O O      . HOH F 6 .   ? 42.178 34.800  28.010 1.00 23.38  ?  518 HOH A O      1 
HETATM 6371 O O      . HOH F 6 .   ? 38.599 4.104   25.074 1.00 33.10  ?  519 HOH A O      1 
HETATM 6372 O O      . HOH F 6 .   ? 0.455  9.612   35.475 1.00 50.86  ?  520 HOH A O      1 
HETATM 6373 O O      . HOH F 6 .   ? 51.446 26.144  11.383 1.00 33.31  ?  521 HOH A O      1 
HETATM 6374 O O      . HOH F 6 .   ? 27.561 34.141  24.807 1.00 29.48  ?  522 HOH A O      1 
HETATM 6375 O O      . HOH F 6 .   ? 25.485 33.182  20.762 1.00 37.04  ?  523 HOH A O      1 
HETATM 6376 O O      . HOH F 6 .   ? 16.925 21.639  5.813  1.00 39.11  ?  524 HOH A O      1 
HETATM 6377 O O      . HOH F 6 .   ? 4.482  13.655  1.745  1.00 40.52  ?  525 HOH A O      1 
HETATM 6378 O O      . HOH F 6 .   ? 20.371 38.569  6.293  1.00 23.36  ?  526 HOH A O      1 
HETATM 6379 O O      . HOH F 6 .   ? 35.360 15.764  6.385  1.00 38.85  ?  527 HOH A O      1 
HETATM 6380 O O      . HOH F 6 .   ? 55.788 11.230  25.486 1.00 37.18  ?  528 HOH A O      1 
HETATM 6381 O O      . HOH F 6 .   ? 36.761 1.761   25.893 1.00 31.15  ?  529 HOH A O      1 
HETATM 6382 O O      . HOH F 6 .   ? 39.626 15.807  8.997  1.00 40.17  ?  530 HOH A O      1 
HETATM 6383 O O      . HOH F 6 .   ? 52.437 25.694  19.867 1.00 32.12  ?  531 HOH A O      1 
HETATM 6384 O O      . HOH F 6 .   ? 44.765 45.529  9.224  1.00 42.92  ?  532 HOH A O      1 
HETATM 6385 O O      . HOH F 6 .   ? 26.828 26.514  9.406  1.00 21.22  ?  533 HOH A O      1 
HETATM 6386 O O      . HOH F 6 .   ? 27.038 29.143  8.173  1.00 34.48  ?  534 HOH A O      1 
HETATM 6387 O O      . HOH F 6 .   ? 12.442 23.820  32.036 1.00 44.55  ?  535 HOH A O      1 
HETATM 6388 O O      . HOH F 6 .   ? 46.574 14.224  16.543 1.00 26.37  ?  536 HOH A O      1 
HETATM 6389 O O      . HOH F 6 .   ? 32.111 37.409  20.278 1.00 57.94  ?  537 HOH A O      1 
HETATM 6390 O O      . HOH F 6 .   ? 55.585 29.076  -1.807 1.00 36.99  ?  538 HOH A O      1 
HETATM 6391 O O      . HOH F 6 .   ? 49.629 24.859  10.517 1.00 22.04  ?  539 HOH A O      1 
HETATM 6392 O O      . HOH F 6 .   ? 9.121  -2.759  29.899 1.00 49.68  ?  540 HOH A O      1 
HETATM 6393 O O      . HOH F 6 .   ? 23.305 36.763  23.598 1.00 40.15  ?  541 HOH A O      1 
HETATM 6394 O O      . HOH F 6 .   ? 48.091 9.324   35.988 1.00 26.26  ?  542 HOH A O      1 
HETATM 6395 O O      . HOH F 6 .   ? 22.890 36.607  19.756 1.00 39.17  ?  543 HOH A O      1 
HETATM 6396 O O      . HOH F 6 .   ? 26.816 17.942  38.134 1.00 37.86  ?  544 HOH A O      1 
HETATM 6397 O O      . HOH F 6 .   ? 12.746 7.768   5.074  1.00 30.55  ?  545 HOH A O      1 
HETATM 6398 O O      . HOH F 6 .   ? 9.913  0.729   21.076 1.00 26.25  ?  546 HOH A O      1 
HETATM 6399 O O      . HOH F 6 .   ? 51.188 4.641   27.676 1.00 35.33  ?  547 HOH A O      1 
HETATM 6400 O O      . HOH F 6 .   ? 11.614 25.157  34.400 1.00 34.81  ?  548 HOH A O      1 
HETATM 6401 O O      . HOH F 6 .   ? 10.339 45.905  4.325  1.00 43.04  ?  549 HOH A O      1 
HETATM 6402 O O      . HOH F 6 .   ? 8.372  44.336  3.550  1.00 34.30  ?  550 HOH A O      1 
HETATM 6403 O O      . HOH G 6 .   ? 19.520 10.087  35.594 1.00 46.17  ?  501 HOH B O      1 
HETATM 6404 O O      . HOH G 6 .   ? 42.853 11.904  42.330 1.00 27.35  ?  502 HOH B O      1 
HETATM 6405 O O      . HOH G 6 .   ? 18.850 22.646  62.155 1.00 40.17  ?  503 HOH B O      1 
HETATM 6406 O O      . HOH G 6 .   ? 41.022 -4.270  69.161 1.00 48.95  ?  504 HOH B O      1 
HETATM 6407 O O      . HOH G 6 .   ? 30.644 -7.058  64.804 1.00 44.35  ?  505 HOH B O      1 
HETATM 6408 O O      . HOH G 6 .   ? 27.744 -7.635  62.068 1.00 37.92  ?  506 HOH B O      1 
HETATM 6409 O O      . HOH G 6 .   ? 14.138 0.191   62.310 1.00 34.05  ?  507 HOH B O      1 
HETATM 6410 O O      . HOH G 6 .   ? 26.677 -12.293 34.068 1.00 30.13  ?  508 HOH B O      1 
HETATM 6411 O O      . HOH G 6 .   ? 12.292 11.325  72.222 1.00 62.93  ?  509 HOH B O      1 
HETATM 6412 O O      . HOH G 6 .   ? 34.786 -1.821  19.145 1.00 28.16  ?  510 HOH B O      1 
HETATM 6413 O O      . HOH G 6 .   ? 27.350 -2.819  54.370 1.00 40.38  ?  511 HOH B O      1 
HETATM 6414 O O      . HOH G 6 .   ? 14.609 8.110   39.165 1.00 20.38  ?  512 HOH B O      1 
HETATM 6415 O O      . HOH G 6 .   ? 31.019 4.224   62.885 1.00 26.50  ?  513 HOH B O      1 
HETATM 6416 O O      . HOH G 6 .   ? 34.319 -3.958  67.997 1.00 37.70  ?  514 HOH B O      1 
HETATM 6417 O O      . HOH G 6 .   ? 21.982 9.470   50.996 1.00 27.01  ?  515 HOH B O      1 
HETATM 6418 O O      . HOH G 6 .   ? 39.420 12.677  65.237 1.00 35.08  ?  516 HOH B O      1 
HETATM 6419 O O      . HOH G 6 .   ? 22.510 4.303   27.130 1.00 28.58  ?  517 HOH B O      1 
HETATM 6420 O O      . HOH G 6 .   ? 32.234 6.517   78.589 1.00 33.24  ?  518 HOH B O      1 
HETATM 6421 O O      . HOH G 6 .   ? 29.454 3.475   43.223 1.00 18.60  ?  519 HOH B O      1 
HETATM 6422 O O      . HOH G 6 .   ? 17.738 -23.542 46.564 1.00 52.57  ?  520 HOH B O      1 
HETATM 6423 O O      . HOH G 6 .   ? 34.100 -4.914  52.512 1.00 29.21  ?  521 HOH B O      1 
HETATM 6424 O O      . HOH G 6 .   ? 14.865 -12.324 28.879 1.00 23.99  ?  522 HOH B O      1 
HETATM 6425 O O      . HOH G 6 .   ? 20.304 -6.473  73.436 1.00 60.35  ?  523 HOH B O      1 
HETATM 6426 O O      . HOH G 6 .   ? 28.521 -21.064 37.024 1.00 34.68  ?  524 HOH B O      1 
HETATM 6427 O O      . HOH G 6 .   ? 23.543 12.298  79.268 1.00 28.63  ?  525 HOH B O      1 
HETATM 6428 O O      . HOH G 6 .   ? 9.384  -22.770 31.917 1.00 51.28  ?  526 HOH B O      1 
HETATM 6429 O O      . HOH G 6 .   ? 9.634  15.580  63.856 1.00 22.61  ?  527 HOH B O      1 
HETATM 6430 O O      . HOH G 6 .   ? 24.209 -7.737  58.476 1.00 26.19  ?  528 HOH B O      1 
HETATM 6431 O O      . HOH G 6 .   ? 34.970 -2.523  54.156 1.00 39.94  ?  529 HOH B O      1 
HETATM 6432 O O      . HOH G 6 .   ? 1.289  -13.761 52.284 1.00 54.46  ?  530 HOH B O      1 
HETATM 6433 O O      . HOH G 6 .   ? 29.495 -11.691 20.965 1.00 56.26  ?  531 HOH B O      1 
HETATM 6434 O O      . HOH G 6 .   ? 21.637 -5.235  70.365 1.00 42.84  ?  532 HOH B O      1 
HETATM 6435 O O      . HOH G 6 .   ? 34.835 6.333   40.974 1.00 19.82  ?  533 HOH B O      1 
HETATM 6436 O O      . HOH G 6 .   ? 33.849 -8.441  65.580 1.00 43.57  ?  534 HOH B O      1 
HETATM 6437 O O      . HOH G 6 .   ? 16.124 10.006  44.501 1.00 24.40  ?  535 HOH B O      1 
HETATM 6438 O O      . HOH G 6 .   ? 26.135 -6.343  59.124 1.00 22.05  ?  536 HOH B O      1 
HETATM 6439 O O      . HOH G 6 .   ? 27.834 11.670  38.904 1.00 24.40  ?  537 HOH B O      1 
HETATM 6440 O O      . HOH G 6 .   ? 32.673 -3.769  6.869  1.00 37.73  ?  538 HOH B O      1 
HETATM 6441 O O      . HOH G 6 .   ? 41.023 19.159  47.661 1.00 29.32  ?  539 HOH B O      1 
HETATM 6442 O O      . HOH G 6 .   ? 36.283 -10.009 46.196 1.00 34.08  ?  540 HOH B O      1 
HETATM 6443 O O      . HOH G 6 .   ? 20.129 -7.184  69.170 1.00 22.33  ?  541 HOH B O      1 
HETATM 6444 O O      . HOH G 6 .   ? 44.598 5.954   55.743 1.00 19.90  ?  542 HOH B O      1 
HETATM 6445 O O      . HOH G 6 .   ? 27.128 -3.571  40.598 1.00 19.70  ?  543 HOH B O      1 
HETATM 6446 O O      . HOH G 6 .   ? 3.274  -12.404 43.004 1.00 58.34  ?  544 HOH B O      1 
HETATM 6447 O O      . HOH G 6 .   ? 25.399 -7.469  29.815 1.00 32.14  ?  545 HOH B O      1 
HETATM 6448 O O      . HOH G 6 .   ? 27.354 -6.913  46.043 1.00 37.71  ?  546 HOH B O      1 
HETATM 6449 O O      . HOH G 6 .   ? 37.654 -3.429  54.467 1.00 20.12  ?  547 HOH B O      1 
HETATM 6450 O O      . HOH G 6 .   ? 43.743 8.352   52.018 1.00 23.73  ?  548 HOH B O      1 
HETATM 6451 O O      . HOH G 6 .   ? 42.166 10.827  51.769 1.00 41.08  ?  549 HOH B O      1 
HETATM 6452 O O      . HOH G 6 .   ? 43.369 13.369  44.692 1.00 46.44  ?  550 HOH B O      1 
HETATM 6453 O O      . HOH G 6 .   ? 6.884  -24.665 33.071 1.00 30.25  ?  551 HOH B O      1 
HETATM 6454 O O      . HOH G 6 .   ? 12.235 -13.690 29.092 1.00 38.37  ?  552 HOH B O      1 
HETATM 6455 O O      . HOH G 6 .   ? 26.114 18.600  40.432 1.00 29.05  ?  553 HOH B O      1 
HETATM 6456 O O      . HOH G 6 .   ? 41.160 -1.955  10.704 1.00 48.18  ?  554 HOH B O      1 
HETATM 6457 O O      . HOH G 6 .   ? 14.655 5.198   65.076 1.00 35.53  ?  555 HOH B O      1 
HETATM 6458 O O      . HOH G 6 .   ? 25.254 -14.160 56.707 1.00 37.93  ?  556 HOH B O      1 
HETATM 6459 O O      . HOH G 6 .   ? 3.883  -15.291 52.726 1.00 27.35  ?  557 HOH B O      1 
HETATM 6460 O O      . HOH G 6 .   ? 13.614 0.012   76.944 1.00 48.31  ?  558 HOH B O      1 
HETATM 6461 O O      . HOH G 6 .   ? 38.931 12.907  78.675 1.00 46.69  ?  559 HOH B O      1 
HETATM 6462 O O      . HOH G 6 .   ? 41.652 -8.455  72.960 1.00 31.62  ?  560 HOH B O      1 
HETATM 6463 O O      . HOH G 6 .   ? 42.806 -8.637  70.189 1.00 38.63  ?  561 HOH B O      1 
HETATM 6464 O O      . HOH G 6 .   ? 45.252 -0.451  46.430 1.00 37.28  ?  562 HOH B O      1 
HETATM 6465 O O      . HOH G 6 .   ? 6.042  -4.100  43.416 1.00 42.49  ?  563 HOH B O      1 
HETATM 6466 O O      . HOH G 6 .   ? 7.083  12.295  68.489 1.00 45.16  ?  564 HOH B O      1 
HETATM 6467 O O      . HOH G 6 .   ? 38.567 15.508  56.297 1.00 44.43  ?  565 HOH B O      1 
HETATM 6468 O O      . HOH G 6 .   ? 19.593 13.466  45.999 1.00 42.06  ?  566 HOH B O      1 
HETATM 6469 O O      . HOH G 6 .   ? 8.616  -5.043  30.434 1.00 46.38  ?  567 HOH B O      1 
HETATM 6470 O O      . HOH G 6 .   ? 7.782  17.351  63.719 1.00 23.21  ?  568 HOH B O      1 
HETATM 6471 O O      . HOH G 6 .   ? 5.362  16.176  64.724 1.00 42.64  ?  569 HOH B O      1 
HETATM 6472 O O      . HOH H 6 .   ? 48.542 -4.921  62.299 1.00 27.59  ?  101 HOH C O      1 
HETATM 6473 O O      . HOH H 6 .   ? 49.287 15.788  58.215 1.00 62.16  ?  102 HOH C O      1 
HETATM 6474 O O      . HOH H 6 .   ? 39.038 27.544  54.639 1.00 44.29  ?  103 HOH C O      1 
HETATM 6475 O O      . HOH H 6 .   ? 54.966 27.591  52.859 1.00 31.43  ?  104 HOH C O      1 
HETATM 6476 O O      . HOH H 6 .   ? 59.299 36.186  63.906 1.00 39.38  ?  105 HOH C O      1 
HETATM 6477 O O      . HOH H 6 .   ? 49.539 13.070  71.703 1.00 32.39  ?  106 HOH C O      1 
HETATM 6478 O O      . HOH H 6 .   ? 46.869 9.903   70.064 1.00 22.20  ?  107 HOH C O      1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . ALA A 6   ? 0.3342 0.3695 0.3033 -0.0406 0.0208  -0.0093 6   ALA A N     
2    C CA    . ALA A 6   ? 0.3307 0.3740 0.3065 -0.0350 0.0222  -0.0071 6   ALA A CA    
3    C C     . ALA A 6   ? 0.3926 0.4375 0.3752 -0.0289 0.0241  -0.0050 6   ALA A C     
4    O O     . ALA A 6   ? 0.4505 0.5064 0.4385 -0.0270 0.0249  -0.0018 6   ALA A O     
5    C CB    . ALA A 6   ? 0.3504 0.4080 0.3281 -0.0376 0.0217  -0.0044 6   ALA A CB    
6    N N     . ALA A 7   ? 0.3985 0.4330 0.3810 -0.0256 0.0248  -0.0067 7   ALA A N     
7    C CA    . ALA A 7   ? 0.4179 0.4538 0.4062 -0.0208 0.0265  -0.0049 7   ALA A CA    
8    C C     . ALA A 7   ? 0.3797 0.4197 0.3733 -0.0150 0.0280  -0.0034 7   ALA A C     
9    O O     . ALA A 7   ? 0.3750 0.4127 0.3677 -0.0136 0.0279  -0.0047 7   ALA A O     
10   C CB    . ALA A 7   ? 0.4341 0.4581 0.4204 -0.0195 0.0267  -0.0071 7   ALA A CB    
11   N N     . LEU A 8   ? 0.5129 0.5578 0.5118 -0.0115 0.0294  -0.0009 8   LEU A N     
12   C CA    . LEU A 8   ? 0.5470 0.5950 0.5511 -0.0059 0.0311  0.0008  8   LEU A CA    
13   C C     . LEU A 8   ? 0.5340 0.5725 0.5391 -0.0020 0.0322  -0.0006 8   LEU A C     
14   O O     . LEU A 8   ? 0.5158 0.5486 0.5194 -0.0029 0.0321  -0.0018 8   LEU A O     
15   C CB    . LEU A 8   ? 0.5166 0.5758 0.5255 -0.0042 0.0323  0.0046  8   LEU A CB    
16   C CG    . LEU A 8   ? 0.5453 0.6162 0.5541 -0.0077 0.0314  0.0068  8   LEU A CG    
17   C CD1   . LEU A 8   ? 0.4489 0.5302 0.4627 -0.0048 0.0329  0.0108  8   LEU A CD1   
18   C CD2   . LEU A 8   ? 0.5210 0.5949 0.5289 -0.0081 0.0308  0.0066  8   LEU A CD2   
19   N N     . VAL A 9   ? 0.4106 0.4478 0.4181 0.0021  0.0332  -0.0004 9   VAL A N     
20   C CA    . VAL A 9   ? 0.4147 0.4442 0.4235 0.0057  0.0343  -0.0014 9   VAL A CA    
21   C C     . VAL A 9   ? 0.3955 0.4293 0.4092 0.0103  0.0361  0.0011  9   VAL A C     
22   O O     . VAL A 9   ? 0.3323 0.3709 0.3474 0.0113  0.0362  0.0023  9   VAL A O     
23   C CB    . VAL A 9   ? 0.3231 0.3434 0.3285 0.0058  0.0337  -0.0044 9   VAL A CB    
24   C CG1   . VAL A 9   ? 0.3302 0.3438 0.3370 0.0090  0.0347  -0.0052 9   VAL A CG1   
25   C CG2   . VAL A 9   ? 0.2845 0.2998 0.2843 0.0016  0.0320  -0.0069 9   VAL A CG2   
26   N N     . ILE A 10  ? 0.2376 0.2698 0.2538 0.0129  0.0375  0.0019  10  ILE A N     
27   C CA    . ILE A 10  ? 0.2351 0.2697 0.2552 0.0172  0.0393  0.0041  10  ILE A CA    
28   C C     . ILE A 10  ? 0.2603 0.2869 0.2810 0.0199  0.0404  0.0030  10  ILE A C     
29   O O     . ILE A 10  ? 0.3792 0.4026 0.3996 0.0197  0.0408  0.0023  10  ILE A O     
30   C CB    . ILE A 10  ? 0.2341 0.2778 0.2571 0.0183  0.0404  0.0073  10  ILE A CB    
31   C CG1   . ILE A 10  ? 0.2325 0.2784 0.2591 0.0230  0.0424  0.0099  10  ILE A CG1   
32   C CG2   . ILE A 10  ? 0.3064 0.3499 0.3286 0.0167  0.0403  0.0071  10  ILE A CG2   
33   C CD1   . ILE A 10  ? 0.2320 0.2881 0.2612 0.0243  0.0434  0.0134  10  ILE A CD1   
34   N N     . ASP A 11  ? 0.3490 0.3727 0.3705 0.0220  0.0408  0.0028  11  ASP A N     
35   C CA    . ASP A 11  ? 0.2670 0.2838 0.2891 0.0243  0.0419  0.0020  11  ASP A CA    
36   C C     . ASP A 11  ? 0.3512 0.3707 0.3766 0.0277  0.0439  0.0046  11  ASP A C     
37   O O     . ASP A 11  ? 0.3071 0.3306 0.3344 0.0296  0.0446  0.0067  11  ASP A O     
38   C CB    . ASP A 11  ? 0.2329 0.2458 0.2542 0.0247  0.0413  0.0007  11  ASP A CB    
39   C CG    . ASP A 11  ? 0.3356 0.3417 0.3572 0.0265  0.0422  -0.0002 11  ASP A CG    
40   O OD1   . ASP A 11  ? 0.4124 0.4150 0.4336 0.0264  0.0427  -0.0009 11  ASP A OD1   
41   O OD2   . ASP A 11  ? 0.3876 0.3919 0.4095 0.0276  0.0423  -0.0003 11  ASP A OD2   
42   N N     . ASN A 12  ? 0.4860 0.5029 0.5117 0.0287  0.0450  0.0045  12  ASN A N     
43   C CA    . ASN A 12  ? 0.4434 0.4617 0.4714 0.0321  0.0471  0.0069  12  ASN A CA    
44   C C     . ASN A 12  ? 0.4633 0.4738 0.4911 0.0338  0.0481  0.0059  12  ASN A C     
45   O O     . ASN A 12  ? 0.6470 0.6519 0.6737 0.0338  0.0485  0.0043  12  ASN A O     
46   C CB    . ASN A 12  ? 0.5378 0.5581 0.5659 0.0323  0.0478  0.0073  12  ASN A CB    
47   C CG    . ASN A 12  ? 0.5874 0.6148 0.6149 0.0293  0.0464  0.0078  12  ASN A CG    
48   O OD1   . ASN A 12  ? 0.5950 0.6307 0.6241 0.0300  0.0468  0.0104  12  ASN A OD1   
49   N ND2   . ASN A 12  ? 0.4695 0.4936 0.4945 0.0259  0.0448  0.0054  12  ASN A ND2   
50   N N     . GLY A 13  ? 0.3168 0.3274 0.3457 0.0354  0.0485  0.0070  13  GLY A N     
51   C CA    . GLY A 13  ? 0.2348 0.2386 0.2634 0.0363  0.0491  0.0062  13  GLY A CA    
52   C C     . GLY A 13  ? 0.2738 0.2761 0.3037 0.0396  0.0513  0.0084  13  GLY A C     
53   O O     . GLY A 13  ? 0.4096 0.4168 0.4410 0.0418  0.0525  0.0109  13  GLY A O     
54   N N     . SER A 14  ? 0.3720 0.3672 0.4011 0.0400  0.0520  0.0075  14  SER A N     
55   C CA    . SER A 14  ? 0.4623 0.4536 0.4916 0.0428  0.0542  0.0090  14  SER A CA    
56   C C     . SER A 14  ? 0.4718 0.4672 0.5030 0.0451  0.0550  0.0122  14  SER A C     
57   O O     . SER A 14  ? 0.5350 0.5314 0.5670 0.0481  0.0570  0.0146  14  SER A O     
58   C CB    . SER A 14  ? 0.5416 0.5247 0.5692 0.0417  0.0543  0.0072  14  SER A CB    
59   O OG    . SER A 14  ? 0.6495 0.6271 0.6763 0.0439  0.0565  0.0081  14  SER A OG    
60   N N     . GLY A 15  ? 0.3371 0.3347 0.3690 0.0439  0.0538  0.0124  15  GLY A N     
61   C CA    . GLY A 15  ? 0.4139 0.4159 0.4476 0.0458  0.0544  0.0155  15  GLY A CA    
62   C C     . GLY A 15  ? 0.3925 0.4043 0.4279 0.0459  0.0537  0.0171  15  GLY A C     
63   O O     . GLY A 15  ? 0.4957 0.5121 0.5328 0.0486  0.0550  0.0202  15  GLY A O     
64   N N     . MET A 16  ? 0.2887 0.3034 0.3234 0.0430  0.0516  0.0151  16  MET A N     
65   C CA    . MET A 16  ? 0.2888 0.3123 0.3244 0.0422  0.0506  0.0163  16  MET A CA    
66   C C     . MET A 16  ? 0.3599 0.3848 0.3939 0.0391  0.0488  0.0138  16  MET A C     
67   O O     . MET A 16  ? 0.3134 0.3325 0.3454 0.0373  0.0480  0.0110  16  MET A O     
68   C CB    . MET A 16  ? 0.4253 0.4517 0.4615 0.0417  0.0496  0.0168  16  MET A CB    
69   C CG    . MET A 16  ? 0.5815 0.6025 0.6157 0.0395  0.0482  0.0139  16  MET A CG    
70   S SD    . MET A 16  ? 0.7081 0.7271 0.7433 0.0407  0.0486  0.0152  16  MET A SD    
71   C CE    . MET A 16  ? 0.7110 0.7240 0.7469 0.0435  0.0511  0.0171  16  MET A CE    
72   N N     . CYS A 17  ? 0.4493 0.4821 0.4839 0.0384  0.0483  0.0151  17  CYS A N     
73   C CA    . CYS A 17  ? 0.4651 0.4996 0.4978 0.0351  0.0467  0.0131  17  CYS A CA    
74   C C     . CYS A 17  ? 0.4351 0.4726 0.4664 0.0323  0.0447  0.0119  17  CYS A C     
75   O O     . CYS A 17  ? 0.4898 0.5335 0.5224 0.0329  0.0447  0.0138  17  CYS A O     
76   C CB    . CYS A 17  ? 0.5495 0.5915 0.5835 0.0357  0.0474  0.0154  17  CYS A CB    
77   S SG    . CYS A 17  ? 0.7756 0.8238 0.8078 0.0312  0.0453  0.0143  17  CYS A SG    
78   N N     . LYS A 18  ? 0.3691 0.4023 0.3975 0.0294  0.0432  0.0088  18  LYS A N     
79   C CA    . LYS A 18  ? 0.2916 0.3265 0.3178 0.0268  0.0414  0.0073  18  LYS A CA    
80   C C     . LYS A 18  ? 0.2950 0.3330 0.3192 0.0236  0.0403  0.0065  18  LYS A C     
81   O O     . LYS A 18  ? 0.3992 0.4331 0.4220 0.0223  0.0400  0.0050  18  LYS A O     
82   C CB    . LYS A 18  ? 0.3361 0.3631 0.3600 0.0263  0.0407  0.0044  18  LYS A CB    
83   C CG    . LYS A 18  ? 0.2745 0.2987 0.3003 0.0291  0.0418  0.0053  18  LYS A CG    
84   C CD    . LYS A 18  ? 0.3406 0.3566 0.3648 0.0290  0.0416  0.0029  18  LYS A CD    
85   C CE    . LYS A 18  ? 0.3696 0.3822 0.3958 0.0314  0.0432  0.0042  18  LYS A CE    
86   N NZ    . LYS A 18  ? 0.3238 0.3359 0.3512 0.0324  0.0445  0.0052  18  LYS A NZ    
87   N N     . ALA A 19  ? 0.3176 0.3636 0.3419 0.0221  0.0396  0.0079  19  ALA A N     
88   C CA    . ALA A 19  ? 0.3291 0.3791 0.3517 0.0186  0.0385  0.0076  19  ALA A CA    
89   C C     . ALA A 19  ? 0.3370 0.3892 0.3563 0.0151  0.0367  0.0061  19  ALA A C     
90   O O     . ALA A 19  ? 0.3179 0.3729 0.3378 0.0160  0.0366  0.0066  19  ALA A O     
91   C CB    . ALA A 19  ? 0.3875 0.4468 0.4132 0.0198  0.0396  0.0111  19  ALA A CB    
92   N N     . GLY A 20  ? 0.2381 0.2888 0.2538 0.0111  0.0353  0.0042  20  GLY A N     
93   C CA    . GLY A 20  ? 0.2412 0.2924 0.2529 0.0075  0.0337  0.0024  20  GLY A CA    
94   C C     . GLY A 20  ? 0.2451 0.2929 0.2524 0.0030  0.0323  0.0003  20  GLY A C     
95   O O     . GLY A 20  ? 0.2448 0.2929 0.2529 0.0023  0.0326  0.0010  20  GLY A O     
96   N N     . PHE A 21  ? 0.3417 0.3859 0.3440 -0.0002 0.0308  -0.0023 21  PHE A N     
97   C CA    . PHE A 21  ? 0.3449 0.3859 0.3421 -0.0052 0.0294  -0.0043 21  PHE A CA    
98   C C     . PHE A 21  ? 0.4202 0.4488 0.4127 -0.0055 0.0289  -0.0078 21  PHE A C     
99   O O     . PHE A 21  ? 0.4010 0.4253 0.3925 -0.0032 0.0290  -0.0093 21  PHE A O     
100  C CB    . PHE A 21  ? 0.3842 0.4317 0.3785 -0.0095 0.0281  -0.0042 21  PHE A CB    
101  C CG    . PHE A 21  ? 0.4805 0.5412 0.4795 -0.0087 0.0286  -0.0005 21  PHE A CG    
102  C CD1   . PHE A 21  ? 0.5176 0.5828 0.5205 -0.0047 0.0296  0.0012  21  PHE A CD1   
103  C CD2   . PHE A 21  ? 0.4052 0.4741 0.4049 -0.0119 0.0282  0.0016  21  PHE A CD2   
104  C CE1   . PHE A 21  ? 0.4931 0.5701 0.5001 -0.0036 0.0302  0.0049  21  PHE A CE1   
105  C CE2   . PHE A 21  ? 0.4630 0.5447 0.4671 -0.0107 0.0288  0.0054  21  PHE A CE2   
106  C CZ    . PHE A 21  ? 0.5351 0.6206 0.5429 -0.0064 0.0299  0.0070  21  PHE A CZ    
107  N N     . ALA A 22  ? 0.4560 0.4795 0.4456 -0.0083 0.0283  -0.0090 22  ALA A N     
108  C CA    . ALA A 22  ? 0.3998 0.4115 0.3844 -0.0089 0.0278  -0.0121 22  ALA A CA    
109  C C     . ALA A 22  ? 0.4124 0.4200 0.3909 -0.0112 0.0267  -0.0147 22  ALA A C     
110  O O     . ALA A 22  ? 0.5085 0.5200 0.4840 -0.0156 0.0256  -0.0148 22  ALA A O     
111  C CB    . ALA A 22  ? 0.3947 0.4030 0.3772 -0.0122 0.0273  -0.0124 22  ALA A CB    
112  N N     . GLY A 23  ? 0.3215 0.3213 0.2979 -0.0084 0.0270  -0.0168 23  GLY A N     
113  C CA    . GLY A 23  ? 0.3030 0.2990 0.2742 -0.0091 0.0264  -0.0191 23  GLY A CA    
114  C C     . GLY A 23  ? 0.3924 0.3931 0.3665 -0.0055 0.0270  -0.0184 23  GLY A C     
115  O O     . GLY A 23  ? 0.5378 0.5335 0.5081 -0.0042 0.0269  -0.0206 23  GLY A O     
116  N N     . ASP A 24  ? 0.3754 0.3852 0.3562 -0.0033 0.0278  -0.0154 24  ASP A N     
117  C CA    . ASP A 24  ? 0.4195 0.4340 0.4034 0.0002  0.0285  -0.0144 24  ASP A CA    
118  C C     . ASP A 24  ? 0.5203 0.5296 0.5065 0.0048  0.0295  -0.0146 24  ASP A C     
119  O O     . ASP A 24  ? 0.5365 0.5437 0.5256 0.0063  0.0303  -0.0137 24  ASP A O     
120  C CB    . ASP A 24  ? 0.4121 0.4380 0.4018 0.0006  0.0290  -0.0109 24  ASP A CB    
121  C CG    . ASP A 24  ? 0.4935 0.5260 0.4811 -0.0039 0.0279  -0.0105 24  ASP A CG    
122  O OD1   . ASP A 24  ? 0.5876 0.6158 0.5690 -0.0071 0.0267  -0.0132 24  ASP A OD1   
123  O OD2   . ASP A 24  ? 0.5158 0.5576 0.5076 -0.0043 0.0282  -0.0075 24  ASP A OD2   
124  N N     . ASP A 25  ? 0.7311 0.7394 0.7162 0.0071  0.0297  -0.0155 25  ASP A N     
125  C CA    . ASP A 25  ? 0.7562 0.7612 0.7435 0.0114  0.0306  -0.0155 25  ASP A CA    
126  C C     . ASP A 25  ? 0.6161 0.6270 0.6103 0.0141  0.0317  -0.0123 25  ASP A C     
127  O O     . ASP A 25  ? 0.5366 0.5449 0.5327 0.0172  0.0325  -0.0121 25  ASP A O     
128  C CB    . ASP A 25  ? 0.8810 0.8848 0.8653 0.0130  0.0304  -0.0170 25  ASP A CB    
129  C CG    . ASP A 25  ? 0.9648 0.9600 0.9416 0.0116  0.0297  -0.0204 25  ASP A CG    
130  O OD1   . ASP A 25  ? 0.9675 0.9564 0.9418 0.0099  0.0295  -0.0215 25  ASP A OD1   
131  O OD2   . ASP A 25  ? 1.0045 0.9991 0.9779 0.0123  0.0295  -0.0219 25  ASP A OD2   
132  N N     . ALA A 26  ? 0.3477 0.3667 0.3453 0.0132  0.0319  -0.0099 26  ALA A N     
133  C CA    . ALA A 26  ? 0.3118 0.3358 0.3155 0.0160  0.0331  -0.0068 26  ALA A CA    
134  C C     . ALA A 26  ? 0.3416 0.3713 0.3479 0.0147  0.0334  -0.0046 26  ALA A C     
135  O O     . ALA A 26  ? 0.3758 0.4089 0.3799 0.0114  0.0325  -0.0049 26  ALA A O     
136  C CB    . ALA A 26  ? 0.2563 0.2860 0.2619 0.0179  0.0334  -0.0054 26  ALA A CB    
137  N N     . PRO A 27  ? 0.2943 0.3254 0.3051 0.0170  0.0347  -0.0023 27  PRO A N     
138  C CA    . PRO A 27  ? 0.3180 0.3561 0.3318 0.0166  0.0352  0.0003  27  PRO A CA    
139  C C     . PRO A 27  ? 0.3467 0.3944 0.3623 0.0167  0.0352  0.0027  27  PRO A C     
140  O O     . PRO A 27  ? 0.3456 0.3948 0.3625 0.0188  0.0355  0.0034  27  PRO A O     
141  C CB    . PRO A 27  ? 0.2346 0.2705 0.2522 0.0199  0.0369  0.0020  27  PRO A CB    
142  C CG    . PRO A 27  ? 0.2340 0.2639 0.2515 0.0220  0.0372  0.0008  27  PRO A CG    
143  C CD    . PRO A 27  ? 0.2370 0.2627 0.2497 0.0201  0.0357  -0.0023 27  PRO A CD    
144  N N     . ARG A 28  ? 0.3911 0.4460 0.4068 0.0143  0.0348  0.0040  28  ARG A N     
145  C CA    . ARG A 28  ? 0.3296 0.3948 0.3472 0.0144  0.0348  0.0066  28  ARG A CA    
146  C C     . ARG A 28  ? 0.3119 0.3824 0.3350 0.0184  0.0366  0.0106  28  ARG A C     
147  O O     . ARG A 28  ? 0.4359 0.5131 0.4611 0.0199  0.0369  0.0128  28  ARG A O     
148  C CB    . ARG A 28  ? 0.3640 0.4360 0.3798 0.0102  0.0337  0.0070  28  ARG A CB    
149  C CG    . ARG A 28  ? 0.3227 0.4032 0.3375 0.0083  0.0328  0.0078  28  ARG A CG    
150  C CD    . ARG A 28  ? 0.4985 0.5729 0.5085 0.0065  0.0316  0.0041  28  ARG A CD    
151  N NE    . ARG A 28  ? 0.4492 0.5168 0.4535 0.0023  0.0302  0.0007  28  ARG A NE    
152  C CZ    . ARG A 28  ? 0.5231 0.5951 0.5241 -0.0024 0.0289  0.0002  28  ARG A CZ    
153  N NH1   . ARG A 28  ? 0.6087 0.6924 0.6118 -0.0034 0.0288  0.0029  28  ARG A NH1   
154  N NH2   . ARG A 28  ? 0.5165 0.5812 0.5119 -0.0064 0.0277  -0.0029 28  ARG A NH2   
155  N N     . ALA A 29  ? 0.2721 0.3394 0.2973 0.0204  0.0379  0.0115  29  ALA A N     
156  C CA    . ALA A 29  ? 0.3525 0.4235 0.3821 0.0245  0.0398  0.0151  29  ALA A CA    
157  C C     . ALA A 29  ? 0.3558 0.4176 0.3863 0.0273  0.0410  0.0143  29  ALA A C     
158  O O     . ALA A 29  ? 0.4612 0.5161 0.4900 0.0264  0.0408  0.0121  29  ALA A O     
159  C CB    . ALA A 29  ? 0.2840 0.3619 0.3153 0.0244  0.0405  0.0176  29  ALA A CB    
160  N N     . VAL A 30  ? 0.2552 0.3170 0.2882 0.0306  0.0422  0.0163  30  VAL A N     
161  C CA    . VAL A 30  ? 0.2525 0.3063 0.2865 0.0332  0.0436  0.0161  30  VAL A CA    
162  C C     . VAL A 30  ? 0.2870 0.3445 0.3244 0.0369  0.0456  0.0201  30  VAL A C     
163  O O     . VAL A 30  ? 0.3847 0.4479 0.4237 0.0380  0.0457  0.0223  30  VAL A O     
164  C CB    . VAL A 30  ? 0.2686 0.3162 0.3011 0.0329  0.0429  0.0139  30  VAL A CB    
165  C CG1   . VAL A 30  ? 0.2542 0.2927 0.2868 0.0344  0.0439  0.0130  30  VAL A CG1   
166  C CG2   . VAL A 30  ? 0.2285 0.2745 0.2573 0.0295  0.0409  0.0105  30  VAL A CG2   
167  N N     . PHE A 31  ? 0.2350 0.2898 0.2734 0.0390  0.0471  0.0211  31  PHE A N     
168  C CA    . PHE A 31  ? 0.2508 0.3088 0.2920 0.0429  0.0493  0.0250  31  PHE A CA    
169  C C     . PHE A 31  ? 0.2678 0.3174 0.3088 0.0452  0.0511  0.0247  31  PHE A C     
170  O O     . PHE A 31  ? 0.3224 0.3667 0.3617 0.0436  0.0506  0.0220  31  PHE A O     
171  C CB    . PHE A 31  ? 0.2313 0.2999 0.2738 0.0431  0.0494  0.0276  31  PHE A CB    
172  C CG    . PHE A 31  ? 0.3973 0.4662 0.4388 0.0418  0.0493  0.0265  31  PHE A CG    
173  C CD1   . PHE A 31  ? 0.2792 0.3465 0.3217 0.0449  0.0513  0.0281  31  PHE A CD1   
174  C CD2   . PHE A 31  ? 0.3190 0.3895 0.3583 0.0373  0.0472  0.0239  31  PHE A CD2   
175  C CE1   . PHE A 31  ? 0.3034 0.3716 0.3451 0.0437  0.0512  0.0272  31  PHE A CE1   
176  C CE2   . PHE A 31  ? 0.2607 0.3316 0.2990 0.0359  0.0470  0.0231  31  PHE A CE2   
177  C CZ    . PHE A 31  ? 0.2760 0.3462 0.3157 0.0390  0.0490  0.0248  31  PHE A CZ    
178  N N     . PRO A 32  ? 0.3953 0.4433 0.4379 0.0490  0.0532  0.0276  32  PRO A N     
179  C CA    . PRO A 32  ? 0.4002 0.4392 0.4420 0.0511  0.0550  0.0271  32  PRO A CA    
180  C C     . PRO A 32  ? 0.4314 0.4711 0.4727 0.0515  0.0556  0.0267  32  PRO A C     
181  O O     . PRO A 32  ? 0.4189 0.4673 0.4614 0.0520  0.0557  0.0286  32  PRO A O     
182  C CB    . PRO A 32  ? 0.4446 0.4835 0.4879 0.0552  0.0572  0.0308  32  PRO A CB    
183  C CG    . PRO A 32  ? 0.3795 0.4244 0.4241 0.0544  0.0561  0.0323  32  PRO A CG    
184  C CD    . PRO A 32  ? 0.3538 0.4069 0.3984 0.0513  0.0539  0.0310  32  PRO A CD    
185  N N     . SER A 33  ? 0.4282 0.4589 0.4678 0.0515  0.0562  0.0244  33  SER A N     
186  C CA    . SER A 33  ? 0.3960 0.4265 0.4351 0.0526  0.0573  0.0242  33  SER A CA    
187  C C     . SER A 33  ? 0.4207 0.4495 0.4605 0.0575  0.0602  0.0273  33  SER A C     
188  O O     . SER A 33  ? 0.5288 0.5482 0.5670 0.0589  0.0616  0.0264  33  SER A O     
189  C CB    . SER A 33  ? 0.3719 0.3937 0.4086 0.0504  0.0567  0.0205  33  SER A CB    
190  O OG    . SER A 33  ? 0.3977 0.4186 0.4333 0.0464  0.0543  0.0176  33  SER A OG    
191  N N     . ILE A 34  ? 0.3788 0.4167 0.4205 0.0600  0.0611  0.0308  34  ILE A N     
192  C CA    . ILE A 34  ? 0.4629 0.5002 0.5053 0.0652  0.0640  0.0343  34  ILE A CA    
193  C C     . ILE A 34  ? 0.5255 0.5738 0.5696 0.0675  0.0649  0.0374  34  ILE A C     
194  O O     . ILE A 34  ? 0.5388 0.5972 0.5843 0.0651  0.0631  0.0380  34  ILE A O     
195  C CB    . ILE A 34  ? 0.5668 0.6040 0.6103 0.0662  0.0642  0.0365  34  ILE A CB    
196  C CG1   . ILE A 34  ? 0.6191 0.6451 0.6607 0.0643  0.0637  0.0338  34  ILE A CG1   
197  C CG2   . ILE A 34  ? 0.6013 0.6398 0.6457 0.0718  0.0671  0.0409  34  ILE A CG2   
198  C CD1   . ILE A 34  ? 0.6440 0.6694 0.6865 0.0653  0.0640  0.0360  34  ILE A CD1   
199  N N     . VAL A 35  ? 0.4128 0.4590 0.4565 0.0722  0.0676  0.0394  35  VAL A N     
200  C CA    . VAL A 35  ? 0.4290 0.4860 0.4745 0.0757  0.0690  0.0432  35  VAL A CA    
201  C C     . VAL A 35  ? 0.4631 0.5166 0.5084 0.0819  0.0723  0.0468  35  VAL A C     
202  O O     . VAL A 35  ? 0.4794 0.5224 0.5223 0.0846  0.0744  0.0458  35  VAL A O     
203  C CB    . VAL A 35  ? 0.3506 0.4097 0.3952 0.0754  0.0692  0.0420  35  VAL A CB    
204  C CG1   . VAL A 35  ? 0.2952 0.3666 0.3418 0.0794  0.0709  0.0465  35  VAL A CG1   
205  C CG2   . VAL A 35  ? 0.2882 0.3497 0.3326 0.0691  0.0659  0.0386  35  VAL A CG2   
206  N N     . GLY A 36  ? 0.6267 0.6882 0.6743 0.0840  0.0727  0.0507  36  GLY A N     
207  C CA    . GLY A 36  ? 0.6617 0.7231 0.7096 0.0906  0.0760  0.0551  36  GLY A CA    
208  C C     . GLY A 36  ? 0.6707 0.7407 0.7194 0.0950  0.0780  0.0582  36  GLY A C     
209  O O     . GLY A 36  ? 0.6441 0.7279 0.6952 0.0937  0.0767  0.0600  36  GLY A O     
210  N N     . ARG A 37  ? 0.8387 0.9010 0.8852 0.1003  0.0812  0.0591  37  ARG A N     
211  C CA    . ARG A 37  ? 0.8358 0.9065 0.8830 0.1061  0.0838  0.0631  37  ARG A CA    
212  C C     . ARG A 37  ? 0.7499 0.8168 0.7967 0.1129  0.0871  0.0674  37  ARG A C     
213  O O     . ARG A 37  ? 0.7435 0.7955 0.7869 0.1149  0.0889  0.0660  37  ARG A O     
214  C CB    . ARG A 37  ? 0.8795 0.9454 0.9244 0.1073  0.0850  0.0608  37  ARG A CB    
215  C CG    . ARG A 37  ? 0.9350 1.0157 0.9818 0.1092  0.0853  0.0635  37  ARG A CG    
216  C CD    . ARG A 37  ? 0.9558 1.0396 1.0026 0.1032  0.0826  0.0597  37  ARG A CD    
217  N NE    . ARG A 37  ? 0.9692 1.0397 1.0126 0.1030  0.0834  0.0556  37  ARG A NE    
218  C CZ    . ARG A 37  ? 1.0041 1.0724 1.0467 0.0976  0.0810  0.0514  37  ARG A CZ    
219  N NH1   . ARG A 37  ? 1.0204 1.0979 1.0650 0.0919  0.0778  0.0506  37  ARG A NH1   
220  N NH2   . ARG A 37  ? 1.0100 1.0664 1.0494 0.0978  0.0819  0.0479  37  ARG A NH2   
221  N N     . PRO A 38  ? 0.5162 0.5960 0.5658 0.1164  0.0880  0.0727  38  PRO A N     
222  C CA    . PRO A 38  ? 0.4925 0.5691 0.5420 0.1216  0.0905  0.0768  38  PRO A CA    
223  C C     . PRO A 38  ? 0.4615 0.5259 0.5073 0.1285  0.0946  0.0779  38  PRO A C     
224  O O     . PRO A 38  ? 0.4447 0.5106 0.4893 0.1322  0.0965  0.0783  38  PRO A O     
225  C CB    . PRO A 38  ? 0.4704 0.5658 0.5239 0.1241  0.0906  0.0823  38  PRO A CB    
226  C CG    . PRO A 38  ? 0.4894 0.5951 0.5437 0.1235  0.0901  0.0820  38  PRO A CG    
227  C CD    . PRO A 38  ? 0.5050 0.6028 0.5577 0.1164  0.0872  0.0755  38  PRO A CD    
228  N N     . ARG A 39  ? 0.5184 0.5705 0.5620 0.1301  0.0960  0.0784  39  ARG A N     
229  C CA    . ARG A 39  ? 0.6265 0.6639 0.6656 0.1357  0.0997  0.0785  39  ARG A CA    
230  C C     . ARG A 39  ? 0.6538 0.6977 0.6929 0.1444  0.1035  0.0839  39  ARG A C     
231  O O     . ARG A 39  ? 0.6758 0.7092 0.7107 0.1495  0.1067  0.0837  39  ARG A O     
232  C CB    . ARG A 39  ? 0.6936 0.7174 0.7304 0.1352  0.1002  0.0785  39  ARG A CB    
233  C CG    . ARG A 39  ? 0.6937 0.6991 0.7257 0.1323  0.1003  0.0732  39  ARG A CG    
234  C CD    . ARG A 39  ? 0.7457 0.7388 0.7755 0.1312  0.1007  0.0734  39  ARG A CD    
235  N NE    . ARG A 39  ? 0.8036 0.8020 0.8367 0.1246  0.0969  0.0721  39  ARG A NE    
236  C CZ    . ARG A 39  ? 0.8219 0.8156 0.8549 0.1235  0.0967  0.0736  39  ARG A CZ    
237  N NH1   . ARG A 39  ? 0.8731 0.8564 0.9030 0.1283  0.0999  0.0765  39  ARG A NH1   
238  N NH2   . ARG A 39  ? 0.7075 0.7069 0.7434 0.1176  0.0933  0.0723  39  ARG A NH2   
239  N N     . HIS A 40  ? 0.7199 0.7805 0.7632 0.1464  0.1032  0.0887  40  HIS A N     
240  C CA    . HIS A 40  ? 0.7662 0.8347 0.8097 0.1547  0.1067  0.0941  40  HIS A CA    
241  C C     . HIS A 40  ? 0.8071 0.8973 0.8556 0.1532  0.1048  0.0966  40  HIS A C     
242  O O     . HIS A 40  ? 0.8693 0.9669 0.9208 0.1463  0.1011  0.0950  40  HIS A O     
243  C CB    . HIS A 40  ? 0.7615 0.8269 0.8045 0.1608  0.1096  0.0993  40  HIS A CB    
244  C CG    . HIS A 40  ? 0.7777 0.8226 0.8164 0.1603  0.1106  0.0970  40  HIS A CG    
245  N ND1   . HIS A 40  ? 0.7618 0.7896 0.7948 0.1638  0.1135  0.0950  40  HIS A ND1   
246  C CD2   . HIS A 40  ? 0.8023 0.8413 0.8414 0.1562  0.1089  0.0964  40  HIS A CD2   
247  C CE1   . HIS A 40  ? 0.8232 0.8353 0.8531 0.1617  0.1136  0.0932  40  HIS A CE1   
248  N NE2   . HIS A 40  ? 0.8425 0.8613 0.8762 0.1571  0.1108  0.0941  40  HIS A NE2   
249  N N     . GLN A 41  ? 0.6290 0.7293 0.6781 0.1593  0.1072  0.1004  41  GLN A N     
250  C CA    . GLN A 41  ? 0.4741 0.5965 0.5279 0.1581  0.1056  0.1036  41  GLN A CA    
251  C C     . GLN A 41  ? 0.4791 0.6101 0.5352 0.1627  0.1070  0.1100  41  GLN A C     
252  O O     . GLN A 41  ? 0.4768 0.5982 0.5305 0.1695  0.1105  0.1128  41  GLN A O     
253  C CB    . GLN A 41  ? 0.5167 0.6469 0.5700 0.1628  0.1077  0.1053  41  GLN A CB    
254  C CG    . GLN A 41  ? 0.5678 0.6812 0.6161 0.1647  0.1096  0.1010  41  GLN A CG    
255  C CD    . GLN A 41  ? 0.6557 0.7772 0.7035 0.1706  0.1121  0.1033  41  GLN A CD    
256  O OE1   . GLN A 41  ? 0.6806 0.8207 0.7317 0.1733  0.1125  0.1082  41  GLN A OE1   
257  N NE2   . GLN A 41  ? 0.6778 0.7858 0.7211 0.1725  0.1139  0.0997  41  GLN A NE2   
258  N N     . GLY A 42  ? 0.3843 0.5331 0.4449 0.1591  0.1044  0.1123  42  GLY A N     
259  C CA    . GLY A 42  ? 0.4744 0.6318 0.5375 0.1628  0.1055  0.1182  42  GLY A CA    
260  C C     . GLY A 42  ? 0.5649 0.7272 0.6306 0.1545  0.1014  0.1162  42  GLY A C     
261  O O     . GLY A 42  ? 0.6665 0.8423 0.7354 0.1546  0.1007  0.1203  42  GLY A O     
262  N N     . VAL A 43  ? 0.6728 0.8240 0.7369 0.1474  0.0986  0.1096  43  VAL A N     
263  C CA    . VAL A 43  ? 0.6191 0.7748 0.6853 0.1393  0.0945  0.1071  43  VAL A CA    
264  C C     . VAL A 43  ? 0.6284 0.7961 0.6960 0.1336  0.0916  0.1048  43  VAL A C     
265  O O     . VAL A 43  ? 0.6484 0.8201 0.7171 0.1261  0.0880  0.1017  43  VAL A O     
266  C CB    . VAL A 43  ? 0.5895 0.7262 0.6528 0.1350  0.0932  0.1015  43  VAL A CB    
267  C CG1   . VAL A 43  ? 0.5344 0.6590 0.5960 0.1404  0.0961  0.1040  43  VAL A CG1   
268  C CG2   . VAL A 43  ? 0.5863 0.7116 0.6465 0.1333  0.0932  0.0963  43  VAL A CG2   
269  N N     . MET A 44  ? 0.5868 0.7602 0.6542 0.1373  0.0934  0.1063  44  MET A N     
270  C CA    . MET A 44  ? 0.5512 0.7367 0.6198 0.1323  0.0910  0.1047  44  MET A CA    
271  C C     . MET A 44  ? 0.5661 0.7736 0.6382 0.1348  0.0914  0.1109  44  MET A C     
272  O O     . MET A 44  ? 0.6017 0.8222 0.6752 0.1299  0.0891  0.1105  44  MET A O     
273  C CB    . MET A 44  ? 0.5216 0.6993 0.5875 0.1337  0.0922  0.1018  44  MET A CB    
274  C CG    . MET A 44  ? 0.5272 0.6861 0.5900 0.1292  0.0908  0.0950  44  MET A CG    
275  S SD    . MET A 44  ? 0.7046 0.8591 0.7649 0.1294  0.0915  0.0916  44  MET A SD    
276  C CE    . MET A 44  ? 0.7368 0.8714 0.7929 0.1372  0.0959  0.0913  44  MET A CE    
277  N N     . VAL A 45  ? 0.5017 0.7137 0.5749 0.1421  0.0944  0.1168  45  VAL A N     
278  C CA    . VAL A 45  ? 0.4877 0.7219 0.5644 0.1443  0.0947  0.1231  45  VAL A CA    
279  C C     . VAL A 45  ? 0.5620 0.8079 0.6413 0.1368  0.0909  0.1229  45  VAL A C     
280  O O     . VAL A 45  ? 0.6653 0.9027 0.7443 0.1339  0.0896  0.1208  45  VAL A O     
281  C CB    . VAL A 45  ? 0.5534 0.7902 0.6307 0.1548  0.0992  0.1300  45  VAL A CB    
282  C CG1   . VAL A 45  ? 0.5991 0.8220 0.6729 0.1621  0.1030  0.1295  45  VAL A CG1   
283  C CG2   . VAL A 45  ? 0.5545 0.7853 0.6322 0.1561  0.0996  0.1316  45  VAL A CG2   
284  N N     . GLY A 46  ? 0.4641 0.7291 0.5457 0.1331  0.0890  0.1247  46  GLY A N     
285  C CA    . GLY A 46  ? 0.4616 0.7375 0.5450 0.1254  0.0853  0.1241  46  GLY A CA    
286  C C     . GLY A 46  ? 0.4822 0.7578 0.5644 0.1154  0.0811  0.1181  46  GLY A C     
287  O O     . GLY A 46  ? 0.4671 0.7276 0.5466 0.1127  0.0804  0.1125  46  GLY A O     
288  N N     . ASP A 51  ? 0.5286 0.6980 0.5911 0.0933  0.0746  0.0767  51  ASP A N     
289  C CA    . ASP A 51  ? 0.6558 0.8157 0.7176 0.1009  0.0782  0.0786  51  ASP A CA    
290  C C     . ASP A 51  ? 0.6570 0.7969 0.7158 0.0999  0.0783  0.0735  51  ASP A C     
291  O O     . ASP A 51  ? 0.5538 0.6830 0.6107 0.1051  0.0811  0.0735  51  ASP A O     
292  C CB    . ASP A 51  ? 0.7888 0.9552 0.8509 0.1074  0.0813  0.0823  51  ASP A CB    
293  C CG    . ASP A 51  ? 0.9775 1.1649 1.0424 0.1066  0.0805  0.0866  51  ASP A CG    
294  O OD1   . ASP A 51  ? 1.0114 1.2077 1.0782 0.1027  0.0783  0.0878  51  ASP A OD1   
295  O OD2   . ASP A 51  ? 1.0680 1.2635 1.1332 0.1095  0.0819  0.0888  51  ASP A OD2   
296  N N     . SER A 52  ? 0.5574 0.6929 0.6156 0.0929  0.0750  0.0692  52  SER A N     
297  C CA    . SER A 52  ? 0.5791 0.6978 0.6348 0.0907  0.0744  0.0644  52  SER A CA    
298  C C     . SER A 52  ? 0.6085 0.7275 0.6649 0.0857  0.0716  0.0629  52  SER A C     
299  O O     . SER A 52  ? 0.5900 0.7214 0.6485 0.0841  0.0704  0.0654  52  SER A O     
300  C CB    . SER A 52  ? 0.6305 0.7428 0.6841 0.0871  0.0732  0.0598  52  SER A CB    
301  O OG    . SER A 52  ? 0.6356 0.7476 0.6884 0.0918  0.0758  0.0611  52  SER A OG    
302  N N     . TYR A 53  ? 0.6417 0.7472 0.6962 0.0832  0.0707  0.0589  53  TYR A N     
303  C CA    . TYR A 53  ? 0.6201 0.7252 0.6750 0.0790  0.0684  0.0574  53  TYR A CA    
304  C C     . TYR A 53  ? 0.5344 0.6287 0.5869 0.0739  0.0662  0.0517  53  TYR A C     
305  O O     . TYR A 53  ? 0.5492 0.6323 0.5997 0.0749  0.0672  0.0494  53  TYR A O     
306  C CB    . TYR A 53  ? 0.6323 0.7330 0.6878 0.0830  0.0701  0.0600  53  TYR A CB    
307  C CG    . TYR A 53  ? 0.5963 0.7102 0.6546 0.0867  0.0713  0.0657  53  TYR A CG    
308  C CD1   . TYR A 53  ? 0.6383 0.7639 0.6985 0.0833  0.0692  0.0668  53  TYR A CD1   
309  C CD2   . TYR A 53  ? 0.6212 0.7358 0.6799 0.0937  0.0748  0.0699  53  TYR A CD2   
310  C CE1   . TYR A 53  ? 0.6903 0.8288 0.7530 0.0865  0.0702  0.0721  53  TYR A CE1   
311  C CE2   . TYR A 53  ? 0.6309 0.7581 0.6922 0.0974  0.0760  0.0754  53  TYR A CE2   
312  C CZ    . TYR A 53  ? 0.6867 0.8263 0.7501 0.0936  0.0736  0.0766  53  TYR A CZ    
313  O OH    . TYR A 53  ? 0.7134 0.8668 0.7795 0.0970  0.0747  0.0821  53  TYR A OH    
314  N N     . VAL A 54  ? 0.2902 0.3880 0.3428 0.0684  0.0632  0.0496  54  VAL A N     
315  C CA    . VAL A 54  ? 0.2887 0.3775 0.3390 0.0636  0.0611  0.0445  54  VAL A CA    
316  C C     . VAL A 54  ? 0.4134 0.4978 0.4635 0.0618  0.0599  0.0432  54  VAL A C     
317  O O     . VAL A 54  ? 0.4516 0.5434 0.5034 0.0623  0.0596  0.0458  54  VAL A O     
318  C CB    . VAL A 54  ? 0.2968 0.3921 0.3464 0.0585  0.0586  0.0425  54  VAL A CB    
319  C CG1   . VAL A 54  ? 0.3135 0.3983 0.3604 0.0549  0.0572  0.0376  54  VAL A CG1   
320  C CG2   . VAL A 54  ? 0.2392 0.3444 0.2899 0.0602  0.0597  0.0453  54  VAL A CG2   
321  N N     . GLY A 55  ? 0.4195 0.4925 0.4675 0.0598  0.0591  0.0394  55  GLY A N     
322  C CA    . GLY A 55  ? 0.4418 0.5116 0.4893 0.0570  0.0574  0.0375  55  GLY A CA    
323  C C     . GLY A 55  ? 0.4264 0.4979 0.4757 0.0598  0.0584  0.0407  55  GLY A C     
324  O O     . GLY A 55  ? 0.3375 0.4032 0.3869 0.0637  0.0607  0.0425  55  GLY A O     
325  N N     . ASP A 56  ? 0.5737 0.6524 0.6238 0.0577  0.0568  0.0412  56  ASP A N     
326  C CA    . ASP A 56  ? 0.5609 0.6405 0.6123 0.0595  0.0573  0.0437  56  ASP A CA    
327  C C     . ASP A 56  ? 0.5699 0.6559 0.6237 0.0644  0.0597  0.0489  56  ASP A C     
328  O O     . ASP A 56  ? 0.5191 0.6010 0.5735 0.0676  0.0614  0.0512  56  ASP A O     
329  C CB    . ASP A 56  ? 0.5441 0.6306 0.5957 0.0560  0.0550  0.0428  56  ASP A CB    
330  C CG    . ASP A 56  ? 0.6518 0.7329 0.7007 0.0513  0.0526  0.0378  56  ASP A CG    
331  O OD1   . ASP A 56  ? 0.6734 0.7455 0.7211 0.0507  0.0524  0.0356  56  ASP A OD1   
332  O OD2   . ASP A 56  ? 0.7129 0.7992 0.7609 0.0482  0.0511  0.0363  56  ASP A OD2   
333  N N     . GLU A 57  ? 0.5988 0.6950 0.6537 0.0651  0.0600  0.0510  57  GLU A N     
334  C CA    . GLU A 57  ? 0.6246 0.7284 0.6818 0.0701  0.0623  0.0563  57  GLU A CA    
335  C C     . GLU A 57  ? 0.7202 0.8151 0.7768 0.0752  0.0653  0.0577  57  GLU A C     
336  O O     . GLU A 57  ? 0.7523 0.8480 0.8100 0.0800  0.0676  0.0618  57  GLU A O     
337  C CB    . GLU A 57  ? 0.6602 0.7775 0.7186 0.0691  0.0616  0.0580  57  GLU A CB    
338  C CG    . GLU A 57  ? 0.6805 0.8094 0.7416 0.0734  0.0633  0.0637  57  GLU A CG    
339  C CD    . GLU A 57  ? 0.7692 0.9131 0.8314 0.0704  0.0617  0.0649  57  GLU A CD    
340  O OE1   . GLU A 57  ? 0.8221 0.9691 0.8834 0.0651  0.0590  0.0624  57  GLU A OE1   
341  O OE2   . GLU A 57  ? 0.8119 0.9644 0.8754 0.0732  0.0631  0.0682  57  GLU A OE2   
342  N N     . ALA A 58  ? 0.6469 0.7331 0.7014 0.0744  0.0655  0.0544  58  ALA A N     
343  C CA    . ALA A 58  ? 0.5861 0.6615 0.6391 0.0786  0.0682  0.0549  58  ALA A CA    
344  C C     . ALA A 58  ? 0.5791 0.6440 0.6311 0.0789  0.0687  0.0544  58  ALA A C     
345  O O     . ALA A 58  ? 0.5744 0.6322 0.6255 0.0832  0.0713  0.0565  58  ALA A O     
346  C CB    . ALA A 58  ? 0.5841 0.6527 0.6349 0.0772  0.0681  0.0511  58  ALA A CB    
347  N N     . GLN A 59  ? 0.5436 0.6072 0.5953 0.0744  0.0662  0.0516  59  GLN A N     
348  C CA    . GLN A 59  ? 0.5111 0.5661 0.5620 0.0740  0.0663  0.0513  59  GLN A CA    
349  C C     . GLN A 59  ? 0.5008 0.5603 0.5536 0.0777  0.0678  0.0562  59  GLN A C     
350  O O     . GLN A 59  ? 0.5258 0.5770 0.5776 0.0805  0.0698  0.0579  59  GLN A O     
351  C CB    . GLN A 59  ? 0.5308 0.5857 0.5814 0.0686  0.0632  0.0475  59  GLN A CB    
352  C CG    . GLN A 59  ? 0.6116 0.6566 0.6608 0.0672  0.0630  0.0460  59  GLN A CG    
353  C CD    . GLN A 59  ? 0.7113 0.7437 0.7581 0.0690  0.0650  0.0452  59  GLN A CD    
354  O OE1   . GLN A 59  ? 0.7272 0.7547 0.7736 0.0719  0.0670  0.0479  59  GLN A OE1   
355  N NE2   . GLN A 59  ? 0.7343 0.7612 0.7792 0.0672  0.0645  0.0415  59  GLN A NE2   
356  N N     . SER A 60  ? 0.5483 0.6211 0.6036 0.0775  0.0669  0.0587  60  SER A N     
357  C CA    . SER A 60  ? 0.5428 0.6212 0.6002 0.0807  0.0681  0.0636  60  SER A CA    
358  C C     . SER A 60  ? 0.5776 0.6545 0.6350 0.0870  0.0716  0.0678  60  SER A C     
359  O O     . SER A 60  ? 0.6465 0.7190 0.7039 0.0903  0.0734  0.0709  60  SER A O     
360  C CB    . SER A 60  ? 0.5878 0.6815 0.6476 0.0789  0.0663  0.0651  60  SER A CB    
361  O OG    . SER A 60  ? 0.5616 0.6567 0.6206 0.0732  0.0633  0.0606  60  SER A OG    
362  N N     . LYS A 61  ? 0.5026 0.5828 0.5599 0.0888  0.0725  0.0680  61  LYS A N     
363  C CA    . LYS A 61  ? 0.4901 0.5710 0.5476 0.0953  0.0759  0.0723  61  LYS A CA    
364  C C     . LYS A 61  ? 0.6534 0.7195 0.7076 0.0978  0.0781  0.0706  61  LYS A C     
365  O O     . LYS A 61  ? 0.7081 0.7733 0.7616 0.1034  0.0811  0.0735  61  LYS A O     
366  C CB    . LYS A 61  ? 0.4159 0.5110 0.4753 0.0963  0.0757  0.0742  61  LYS A CB    
367  C CG    . LYS A 61  ? 0.4882 0.5985 0.5507 0.0942  0.0738  0.0765  61  LYS A CG    
368  C CD    . LYS A 61  ? 0.5065 0.6309 0.5705 0.0929  0.0728  0.0773  61  LYS A CD    
369  C CE    . LYS A 61  ? 0.5549 0.6950 0.6217 0.0919  0.0716  0.0806  61  LYS A CE    
370  N NZ    . LYS A 61  ? 0.5387 0.6917 0.6063 0.0881  0.0696  0.0799  61  LYS A NZ    
371  N N     . ARG A 62  ? 0.7072 0.7615 0.7590 0.0939  0.0769  0.0660  62  ARG A N     
372  C CA    . ARG A 62  ? 0.6305 0.6707 0.6787 0.0953  0.0787  0.0637  62  ARG A CA    
373  C C     . ARG A 62  ? 0.5729 0.6048 0.6193 0.1011  0.0823  0.0673  62  ARG A C     
374  O O     . ARG A 62  ? 0.5501 0.5704 0.5931 0.1030  0.0842  0.0657  62  ARG A O     
375  C CB    . ARG A 62  ? 0.5792 0.6093 0.6254 0.0898  0.0766  0.0587  62  ARG A CB    
376  N N     . GLY A 63  ? 0.5766 0.6135 0.6248 0.1040  0.0832  0.0719  63  GLY A N     
377  C CA    . GLY A 63  ? 0.5994 0.6297 0.6458 0.1105  0.0870  0.0760  63  GLY A CA    
378  C C     . GLY A 63  ? 0.6752 0.7114 0.7218 0.1161  0.0894  0.0785  63  GLY A C     
379  O O     . GLY A 63  ? 0.7577 0.7837 0.8008 0.1202  0.0923  0.0785  63  GLY A O     
380  N N     . ILE A 64  ? 0.4415 0.4942 0.4917 0.1163  0.0883  0.0807  64  ILE A N     
381  C CA    . ILE A 64  ? 0.3498 0.4100 0.4005 0.1214  0.0905  0.0833  64  ILE A CA    
382  C C     . ILE A 64  ? 0.3540 0.4105 0.4029 0.1194  0.0899  0.0788  64  ILE A C     
383  O O     . ILE A 64  ? 0.2979 0.3531 0.3452 0.1244  0.0926  0.0801  64  ILE A O     
384  C CB    . ILE A 64  ? 0.2877 0.3677 0.3429 0.1216  0.0893  0.0871  64  ILE A CB    
385  N N     . LEU A 65  ? 0.5604 0.6151 0.6093 0.1125  0.0866  0.0737  65  LEU A N     
386  C CA    . LEU A 65  ? 0.5698 0.6230 0.6174 0.1099  0.0857  0.0695  65  LEU A CA    
387  C C     . LEU A 65  ? 0.5798 0.6152 0.6229 0.1095  0.0868  0.0656  65  LEU A C     
388  O O     . LEU A 65  ? 0.5690 0.5930 0.6100 0.1107  0.0881  0.0659  65  LEU A O     
389  C CB    . LEU A 65  ? 0.4333 0.4946 0.4830 0.1027  0.0816  0.0664  65  LEU A CB    
390  N N     . THR A 66  ? 0.5985 0.6318 0.6402 0.1078  0.0863  0.0621  66  THR A N     
391  C CA    . THR A 66  ? 0.4950 0.5130 0.5326 0.1065  0.0868  0.0578  66  THR A CA    
392  C C     . THR A 66  ? 0.4574 0.4765 0.4955 0.0998  0.0835  0.0528  66  THR A C     
393  O O     . THR A 66  ? 0.5240 0.5496 0.5626 0.0992  0.0829  0.0519  66  THR A O     
394  C CB    . THR A 66  ? 0.5059 0.5191 0.5407 0.1122  0.0903  0.0585  66  THR A CB    
395  N N     . LEU A 67  ? 0.4128 0.4244 0.4499 0.0949  0.0815  0.0497  67  LEU A N     
396  C CA    . LEU A 67  ? 0.4046 0.4196 0.4429 0.0885  0.0779  0.0460  67  LEU A CA    
397  C C     . LEU A 67  ? 0.4138 0.4200 0.4492 0.0859  0.0775  0.0413  67  LEU A C     
398  O O     . LEU A 67  ? 0.4447 0.4385 0.4771 0.0856  0.0784  0.0394  67  LEU A O     
399  C CB    . LEU A 67  ? 0.4373 0.4501 0.4763 0.0849  0.0760  0.0453  67  LEU A CB    
400  C CG    . LEU A 67  ? 0.4282 0.4513 0.4705 0.0844  0.0747  0.0483  67  LEU A CG    
401  C CD1   . LEU A 67  ? 0.4022 0.4335 0.4463 0.0900  0.0770  0.0537  67  LEU A CD1   
402  C CD2   . LEU A 67  ? 0.2763 0.2925 0.3180 0.0821  0.0739  0.0478  67  LEU A CD2   
403  N N     . LYS A 68  ? 0.5348 0.5476 0.5712 0.0836  0.0759  0.0396  68  LYS A N     
404  C CA    . LYS A 68  ? 0.5609 0.5671 0.5950 0.0803  0.0749  0.0351  68  LYS A CA    
405  C C     . LYS A 68  ? 0.6030 0.6123 0.6382 0.0742  0.0714  0.0322  68  LYS A C     
406  O O     . LYS A 68  ? 0.6642 0.6843 0.7019 0.0726  0.0697  0.0332  68  LYS A O     
407  C CB    . LYS A 68  ? 0.5436 0.5539 0.5773 0.0826  0.0761  0.0353  68  LYS A CB    
408  C CG    . LYS A 68  ? 0.6027 0.6066 0.6340 0.0886  0.0799  0.0369  68  LYS A CG    
409  C CD    . LYS A 68  ? 0.6004 0.6047 0.6302 0.0898  0.0808  0.0355  68  LYS A CD    
410  C CE    . LYS A 68  ? 0.6368 0.6560 0.6696 0.0913  0.0806  0.0383  68  LYS A CE    
411  N NZ    . LYS A 68  ? 0.5486 0.5689 0.5800 0.0933  0.0820  0.0375  68  LYS A NZ    
412  N N     . TYR A 69  ? 0.8005 0.8004 0.8335 0.0710  0.0704  0.0285  69  TYR A N     
413  C CA    . TYR A 69  ? 0.7969 0.7983 0.8303 0.0656  0.0673  0.0254  69  TYR A CA    
414  C C     . TYR A 69  ? 0.6597 0.6597 0.6917 0.0641  0.0670  0.0226  69  TYR A C     
415  O O     . TYR A 69  ? 0.5960 0.5868 0.6255 0.0637  0.0677  0.0203  69  TYR A O     
416  C CB    . TYR A 69  ? 0.8210 0.8141 0.8531 0.0631  0.0665  0.0235  69  TYR A CB    
417  C CG    . TYR A 69  ? 0.9255 0.9155 0.9577 0.0660  0.0682  0.0264  69  TYR A CG    
418  C CD1   . TYR A 69  ? 0.8993 0.8969 0.9340 0.0665  0.0676  0.0292  69  TYR A CD1   
419  C CD2   . TYR A 69  ? 0.9802 0.9596 1.0096 0.0681  0.0704  0.0263  69  TYR A CD2   
420  C CE1   . TYR A 69  ? 0.9019 0.8969 0.9368 0.0692  0.0692  0.0321  69  TYR A CE1   
421  C CE2   . TYR A 69  ? 0.9682 0.9442 0.9974 0.0706  0.0720  0.0291  69  TYR A CE2   
422  C CZ    . TYR A 69  ? 0.9677 0.9517 0.9998 0.0713  0.0714  0.0321  69  TYR A CZ    
423  O OH    . TYR A 69  ? 1.0215 1.0022 1.0533 0.0738  0.0730  0.0351  69  TYR A OH    
424  N N     . PRO A 70  ? 0.4755 0.4848 0.5089 0.0632  0.0659  0.0230  70  PRO A N     
425  C CA    . PRO A 70  ? 0.5066 0.5147 0.5387 0.0618  0.0656  0.0206  70  PRO A CA    
426  C C     . PRO A 70  ? 0.5177 0.5209 0.5485 0.0569  0.0632  0.0168  70  PRO A C     
427  O O     . PRO A 70  ? 0.4416 0.4422 0.4709 0.0557  0.0631  0.0146  70  PRO A O     
428  C CB    . PRO A 70  ? 0.4895 0.5097 0.5236 0.0618  0.0650  0.0227  70  PRO A CB    
429  C CG    . PRO A 70  ? 0.4408 0.4672 0.4768 0.0599  0.0632  0.0240  70  PRO A CG    
430  C CD    . PRO A 70  ? 0.4760 0.4972 0.5121 0.0626  0.0647  0.0254  70  PRO A CD    
431  N N     . ILE A 71  ? 0.5339 0.5370 0.5652 0.0541  0.0613  0.0160  71  ILE A N     
432  C CA    . ILE A 71  ? 0.5119 0.5105 0.5418 0.0500  0.0593  0.0126  71  ILE A CA    
433  C C     . ILE A 71  ? 0.5864 0.5756 0.6148 0.0497  0.0597  0.0111  71  ILE A C     
434  O O     . ILE A 71  ? 0.6066 0.5921 0.6338 0.0466  0.0580  0.0086  71  ILE A O     
435  C CB    . ILE A 71  ? 0.4761 0.4808 0.5070 0.0468  0.0567  0.0122  71  ILE A CB    
436  C CG1   . ILE A 71  ? 0.4681 0.4799 0.4994 0.0455  0.0559  0.0125  71  ILE A CG1   
437  C CG2   . ILE A 71  ? 0.5964 0.5958 0.6257 0.0433  0.0549  0.0090  71  ILE A CG2   
438  C CD1   . ILE A 71  ? 0.5274 0.5357 0.5569 0.0423  0.0545  0.0094  71  ILE A CD1   
439  N N     . GLU A 72  ? 0.6204 0.6054 0.6483 0.0529  0.0619  0.0128  72  GLU A N     
440  C CA    . GLU A 72  ? 0.6244 0.6006 0.6506 0.0522  0.0623  0.0116  72  GLU A CA    
441  C C     . GLU A 72  ? 0.7454 0.7158 0.7693 0.0495  0.0615  0.0082  72  GLU A C     
442  O O     . GLU A 72  ? 0.8944 0.8637 0.9173 0.0503  0.0625  0.0073  72  GLU A O     
443  C CB    . GLU A 72  ? 0.6268 0.5978 0.6519 0.0559  0.0651  0.0136  72  GLU A CB    
444  C CG    . GLU A 72  ? 0.7810 0.7422 0.8037 0.0548  0.0655  0.0124  72  GLU A CG    
445  C CD    . GLU A 72  ? 0.8633 0.8173 0.8838 0.0583  0.0686  0.0138  72  GLU A CD    
446  O OE1   . GLU A 72  ? 0.8801 0.8311 0.8987 0.0600  0.0700  0.0128  72  GLU A OE1   
447  O OE2   . GLU A 72  ? 0.8473 0.7982 0.8676 0.0596  0.0695  0.0158  72  GLU A OE2   
448  N N     . HIS A 73  ? 0.6614 0.6289 0.6847 0.0463  0.0599  0.0063  73  HIS A N     
449  C CA    . HIS A 73  ? 0.6481 0.6110 0.6695 0.0435  0.0590  0.0032  73  HIS A CA    
450  C C     . HIS A 73  ? 0.6511 0.6187 0.6729 0.0413  0.0570  0.0016  73  HIS A C     
451  O O     . HIS A 73  ? 0.7225 0.6867 0.7427 0.0394  0.0564  -0.0007 73  HIS A O     
452  C CB    . HIS A 73  ? 0.6545 0.6101 0.6732 0.0446  0.0609  0.0021  73  HIS A CB    
453  C CG    . HIS A 73  ? 0.6449 0.5940 0.6622 0.0462  0.0628  0.0032  73  HIS A CG    
454  N ND1   . HIS A 73  ? 0.6293 0.5745 0.6451 0.0495  0.0654  0.0043  73  HIS A ND1   
455  C CD2   . HIS A 73  ? 0.6630 0.6085 0.6798 0.0448  0.0625  0.0035  73  HIS A CD2   
456  C CE1   . HIS A 73  ? 0.6802 0.6188 0.6944 0.0501  0.0666  0.0051  73  HIS A CE1   
457  N NE2   . HIS A 73  ? 0.6664 0.6054 0.6813 0.0470  0.0648  0.0047  73  HIS A NE2   
458  N N     . GLY A 74  ? 0.3536 0.3286 0.3773 0.0414  0.0560  0.0029  74  GLY A N     
459  C CA    . GLY A 74  ? 0.2678 0.2466 0.2916 0.0389  0.0541  0.0015  74  GLY A CA    
460  C C     . GLY A 74  ? 0.3526 0.3347 0.3763 0.0391  0.0544  0.0015  74  GLY A C     
461  O O     . GLY A 74  ? 0.4008 0.3877 0.4249 0.0373  0.0529  0.0013  74  GLY A O     
462  N N     . ILE A 75  ? 0.4247 0.4040 0.4477 0.0412  0.0563  0.0017  75  ILE A N     
463  C CA    . ILE A 75  ? 0.4579 0.4408 0.4809 0.0417  0.0567  0.0019  75  ILE A CA    
464  C C     . ILE A 75  ? 0.4358 0.4243 0.4605 0.0451  0.0584  0.0049  75  ILE A C     
465  O O     . ILE A 75  ? 0.4259 0.4113 0.4504 0.0482  0.0603  0.0062  75  ILE A O     
466  C CB    . ILE A 75  ? 0.5629 0.5397 0.5838 0.0418  0.0578  -0.0001 75  ILE A CB    
467  C CG1   . ILE A 75  ? 0.5592 0.5313 0.5786 0.0385  0.0561  -0.0028 75  ILE A CG1   
468  C CG2   . ILE A 75  ? 0.5328 0.5138 0.5537 0.0425  0.0583  0.0002  75  ILE A CG2   
469  C CD1   . ILE A 75  ? 0.4475 0.4141 0.4647 0.0382  0.0570  -0.0048 75  ILE A CD1   
470  N N     . VAL A 76  ? 0.3385 0.3352 0.3644 0.0446  0.0576  0.0063  76  VAL A N     
471  C CA    . VAL A 76  ? 0.3509 0.3550 0.3787 0.0478  0.0591  0.0095  76  VAL A CA    
472  C C     . VAL A 76  ? 0.4544 0.4554 0.4812 0.0516  0.0618  0.0101  76  VAL A C     
473  O O     . VAL A 76  ? 0.3604 0.3603 0.3860 0.0511  0.0620  0.0086  76  VAL A O     
474  C CB    . VAL A 76  ? 0.3302 0.3438 0.3590 0.0457  0.0576  0.0105  76  VAL A CB    
475  C CG1   . VAL A 76  ? 0.4000 0.4221 0.4307 0.0492  0.0593  0.0141  76  VAL A CG1   
476  C CG2   . VAL A 76  ? 0.2991 0.3155 0.3282 0.0418  0.0550  0.0098  76  VAL A CG2   
477  N N     . THR A 77  ? 0.5760 0.5761 0.6032 0.0557  0.0640  0.0123  77  THR A N     
478  C CA    . THR A 77  ? 0.5634 0.5589 0.5890 0.0600  0.0669  0.0129  77  THR A CA    
479  C C     . THR A 77  ? 0.6434 0.6480 0.6705 0.0638  0.0685  0.0162  77  THR A C     
480  O O     . THR A 77  ? 0.7754 0.7809 0.8016 0.0654  0.0697  0.0160  77  THR A O     
481  C CB    . THR A 77  ? 0.6261 0.6130 0.6504 0.0622  0.0685  0.0132  77  THR A CB    
482  O OG1   . THR A 77  ? 0.6688 0.6609 0.6953 0.0641  0.0688  0.0164  77  THR A OG1   
483  C CG2   . THR A 77  ? 0.6806 0.6599 0.7035 0.0582  0.0668  0.0102  77  THR A CG2   
484  N N     . ASN A 78  ? 0.4650 0.4765 0.4944 0.0656  0.0687  0.0195  78  ASN A N     
485  C CA    . ASN A 78  ? 0.4658 0.4880 0.4970 0.0688  0.0699  0.0230  78  ASN A CA    
486  C C     . ASN A 78  ? 0.4303 0.4636 0.4637 0.0649  0.0673  0.0237  78  ASN A C     
487  O O     . ASN A 78  ? 0.4239 0.4599 0.4585 0.0623  0.0655  0.0240  78  ASN A O     
488  C CB    . ASN A 78  ? 0.4577 0.4817 0.4898 0.0738  0.0722  0.0267  78  ASN A CB    
489  C CG    . ASN A 78  ? 0.4736 0.5093 0.5075 0.0775  0.0736  0.0305  78  ASN A CG    
490  O OD1   . ASN A 78  ? 0.5421 0.5879 0.5786 0.0776  0.0730  0.0334  78  ASN A OD1   
491  N ND2   . ASN A 78  ? 0.5002 0.5353 0.5327 0.0803  0.0755  0.0303  78  ASN A ND2   
492  N N     . TRP A 79  ? 0.3796 0.4198 0.4133 0.0646  0.0673  0.0242  79  TRP A N     
493  C CA    . TRP A 79  ? 0.4375 0.4886 0.4728 0.0607  0.0650  0.0252  79  TRP A CA    
494  C C     . TRP A 79  ? 0.4589 0.5222 0.4968 0.0632  0.0657  0.0296  79  TRP A C     
495  O O     . TRP A 79  ? 0.3800 0.4510 0.4192 0.0596  0.0635  0.0305  79  TRP A O     
496  C CB    . TRP A 79  ? 0.3163 0.3702 0.3508 0.0589  0.0645  0.0241  79  TRP A CB    
497  C CG    . TRP A 79  ? 0.4448 0.4886 0.4771 0.0556  0.0633  0.0199  79  TRP A CG    
498  C CD1   . TRP A 79  ? 0.4391 0.4744 0.4693 0.0575  0.0648  0.0179  79  TRP A CD1   
499  C CD2   . TRP A 79  ? 0.4182 0.4593 0.4497 0.0499  0.0603  0.0173  79  TRP A CD2   
500  N NE1   . TRP A 79  ? 0.4636 0.4920 0.4922 0.0532  0.0629  0.0144  79  TRP A NE1   
501  C CE2   . TRP A 79  ? 0.4427 0.4742 0.4720 0.0488  0.0602  0.0140  79  TRP A CE2   
502  C CE3   . TRP A 79  ? 0.4188 0.4646 0.4510 0.0458  0.0578  0.0174  79  TRP A CE3   
503  C CZ2   . TRP A 79  ? 0.4247 0.4514 0.4528 0.0440  0.0578  0.0110  79  TRP A CZ2   
504  C CZ3   . TRP A 79  ? 0.4453 0.4853 0.4759 0.0411  0.0555  0.0142  79  TRP A CZ3   
505  C CH2   . TRP A 79  ? 0.4680 0.4988 0.4966 0.0404  0.0555  0.0112  79  TRP A CH2   
506  N N     . ASP A 80  ? 0.6817 0.7470 0.7200 0.0693  0.0687  0.0326  80  ASP A N     
507  C CA    . ASP A 80  ? 0.7449 0.8217 0.7857 0.0721  0.0695  0.0371  80  ASP A CA    
508  C C     . ASP A 80  ? 0.7108 0.7867 0.7526 0.0705  0.0682  0.0374  80  ASP A C     
509  O O     . ASP A 80  ? 0.6726 0.7592 0.7165 0.0686  0.0668  0.0397  80  ASP A O     
510  C CB    . ASP A 80  ? 0.7589 0.8360 0.7996 0.0797  0.0733  0.0402  80  ASP A CB    
511  C CG    . ASP A 80  ? 0.8282 0.9091 0.8682 0.0818  0.0747  0.0406  80  ASP A CG    
512  O OD1   . ASP A 80  ? 0.8198 0.9114 0.8609 0.0787  0.0731  0.0414  80  ASP A OD1   
513  O OD2   . ASP A 80  ? 0.8853 0.9584 0.9232 0.0866  0.0775  0.0402  80  ASP A OD2   
514  N N     . ASP A 81  ? 0.4094 0.4728 0.4498 0.0709  0.0686  0.0352  81  ASP A N     
515  C CA    . ASP A 81  ? 0.4072 0.4691 0.4484 0.0691  0.0673  0.0352  81  ASP A CA    
516  C C     . ASP A 81  ? 0.4604 0.5223 0.5012 0.0625  0.0639  0.0321  81  ASP A C     
517  O O     . ASP A 81  ? 0.4421 0.5078 0.4841 0.0604  0.0623  0.0327  81  ASP A O     
518  C CB    . ASP A 81  ? 0.4249 0.4738 0.4645 0.0715  0.0688  0.0339  81  ASP A CB    
519  C CG    . ASP A 81  ? 0.5056 0.5529 0.5450 0.0782  0.0723  0.0370  81  ASP A CG    
520  O OD1   . ASP A 81  ? 0.4220 0.4794 0.4629 0.0815  0.0736  0.0406  81  ASP A OD1   
521  O OD2   . ASP A 81  ? 0.6557 0.6913 0.6930 0.0802  0.0739  0.0360  81  ASP A OD2   
522  N N     . MET A 82  ? 0.4728 0.5301 0.5119 0.0592  0.0627  0.0288  82  MET A N     
523  C CA    . MET A 82  ? 0.3945 0.4514 0.4328 0.0532  0.0596  0.0259  82  MET A CA    
524  C C     . MET A 82  ? 0.3922 0.4616 0.4318 0.0503  0.0579  0.0278  82  MET A C     
525  O O     . MET A 82  ? 0.3701 0.4414 0.4096 0.0467  0.0558  0.0270  82  MET A O     
526  C CB    . MET A 82  ? 0.4590 0.5085 0.4951 0.0508  0.0589  0.0224  82  MET A CB    
527  C CG    . MET A 82  ? 0.4997 0.5445 0.5343 0.0456  0.0561  0.0190  82  MET A CG    
528  S SD    . MET A 82  ? 0.5390 0.5757 0.5733 0.0458  0.0559  0.0178  82  MET A SD    
529  C CE    . MET A 82  ? 0.4848 0.5143 0.5190 0.0513  0.0591  0.0187  82  MET A CE    
530  N N     . GLU A 83  ? 0.4700 0.5482 0.5105 0.0518  0.0589  0.0303  83  GLU A N     
531  C CA    . GLU A 83  ? 0.4494 0.5408 0.4911 0.0491  0.0575  0.0326  83  GLU A CA    
532  C C     . GLU A 83  ? 0.3975 0.4953 0.4409 0.0498  0.0572  0.0351  83  GLU A C     
533  O O     . GLU A 83  ? 0.3704 0.4746 0.4138 0.0454  0.0550  0.0351  83  GLU A O     
534  C CB    . GLU A 83  ? 0.5021 0.6028 0.5450 0.0520  0.0591  0.0357  83  GLU A CB    
535  C CG    . GLU A 83  ? 0.5413 0.6404 0.5827 0.0500  0.0587  0.0338  83  GLU A CG    
536  C CD    . GLU A 83  ? 0.5984 0.7068 0.6411 0.0540  0.0609  0.0373  83  GLU A CD    
537  O OE1   . GLU A 83  ? 0.6181 0.7316 0.6626 0.0593  0.0631  0.0408  83  GLU A OE1   
538  O OE2   . GLU A 83  ? 0.6033 0.7142 0.6452 0.0521  0.0604  0.0367  83  GLU A OE2   
539  N N     . LYS A 84  ? 0.3561 0.4523 0.4009 0.0554  0.0597  0.0374  84  LYS A N     
540  C CA    . LYS A 84  ? 0.3305 0.4327 0.3771 0.0567  0.0598  0.0402  84  LYS A CA    
541  C C     . LYS A 84  ? 0.3758 0.4726 0.4215 0.0526  0.0575  0.0374  84  LYS A C     
542  O O     . LYS A 84  ? 0.3749 0.4792 0.4209 0.0491  0.0556  0.0379  84  LYS A O     
543  C CB    . LYS A 84  ? 0.3276 0.4266 0.3753 0.0637  0.0630  0.0429  84  LYS A CB    
544  C CG    . LYS A 84  ? 0.3528 0.4609 0.4019 0.0686  0.0655  0.0470  84  LYS A CG    
545  C CD    . LYS A 84  ? 0.3717 0.4719 0.4201 0.0756  0.0690  0.0483  84  LYS A CD    
546  C CE    . LYS A 84  ? 0.4603 0.5689 0.5095 0.0802  0.0713  0.0516  84  LYS A CE    
547  N NZ    . LYS A 84  ? 0.4860 0.5994 0.5346 0.0764  0.0699  0.0500  84  LYS A NZ    
548  N N     . ILE A 85  ? 0.4036 0.4874 0.4477 0.0528  0.0577  0.0342  85  ILE A N     
549  C CA    . ILE A 85  ? 0.3560 0.4340 0.3988 0.0489  0.0555  0.0312  85  ILE A CA    
550  C C     . ILE A 85  ? 0.3526 0.4352 0.3940 0.0430  0.0527  0.0293  85  ILE A C     
551  O O     . ILE A 85  ? 0.3897 0.4754 0.4308 0.0401  0.0509  0.0289  85  ILE A O     
552  C CB    . ILE A 85  ? 0.4024 0.4665 0.4434 0.0493  0.0559  0.0279  85  ILE A CB    
553  C CG1   . ILE A 85  ? 0.4458 0.5047 0.4877 0.0544  0.0584  0.0297  85  ILE A CG1   
554  C CG2   . ILE A 85  ? 0.2343 0.2927 0.2736 0.0450  0.0535  0.0244  85  ILE A CG2   
555  C CD1   . ILE A 85  ? 0.4706 0.5163 0.5105 0.0540  0.0585  0.0265  85  ILE A CD1   
556  N N     . TRP A 86  ? 0.3708 0.4540 0.4112 0.0412  0.0523  0.0283  86  TRP A N     
557  C CA    . TRP A 86  ? 0.3255 0.4118 0.3640 0.0353  0.0497  0.0265  86  TRP A CA    
558  C C     . TRP A 86  ? 0.3886 0.4885 0.4283 0.0335  0.0489  0.0294  86  TRP A C     
559  O O     . TRP A 86  ? 0.3726 0.4746 0.4106 0.0287  0.0466  0.0281  86  TRP A O     
560  C CB    . TRP A 86  ? 0.3137 0.3973 0.3508 0.0338  0.0495  0.0249  86  TRP A CB    
561  C CG    . TRP A 86  ? 0.4213 0.4923 0.4561 0.0323  0.0488  0.0208  86  TRP A CG    
562  C CD1   . TRP A 86  ? 0.3686 0.4323 0.4020 0.0308  0.0477  0.0183  86  TRP A CD1   
563  C CD2   . TRP A 86  ? 0.5125 0.5772 0.5461 0.0324  0.0493  0.0190  86  TRP A CD2   
564  N NE1   . TRP A 86  ? 0.3809 0.4345 0.4124 0.0299  0.0474  0.0152  86  TRP A NE1   
565  C CE2   . TRP A 86  ? 0.4776 0.5315 0.5091 0.0307  0.0483  0.0155  86  TRP A CE2   
566  C CE3   . TRP A 86  ? 0.4739 0.5416 0.5079 0.0337  0.0505  0.0201  86  TRP A CE3   
567  C CZ2   . TRP A 86  ? 0.4618 0.5080 0.4918 0.0303  0.0485  0.0131  86  TRP A CZ2   
568  C CZ3   . TRP A 86  ? 0.4566 0.5164 0.4890 0.0332  0.0506  0.0175  86  TRP A CZ3   
569  C CH2   . TRP A 86  ? 0.4422 0.4914 0.4726 0.0315  0.0496  0.0141  86  TRP A CH2   
570  N N     . HIS A 87  ? 0.5287 0.6382 0.5709 0.0370  0.0506  0.0334  87  HIS A N     
571  C CA    . HIS A 87  ? 0.5271 0.6506 0.5704 0.0353  0.0499  0.0366  87  HIS A CA    
572  C C     . HIS A 87  ? 0.4881 0.6131 0.5319 0.0350  0.0492  0.0370  87  HIS A C     
573  O O     . HIS A 87  ? 0.4926 0.6235 0.5354 0.0304  0.0471  0.0366  87  HIS A O     
574  C CB    . HIS A 87  ? 0.5334 0.6673 0.5796 0.0401  0.0522  0.0413  87  HIS A CB    
575  C CG    . HIS A 87  ? 0.5419 0.6912 0.5898 0.0391  0.0517  0.0451  87  HIS A CG    
576  N ND1   . HIS A 87  ? 0.5701 0.7307 0.6177 0.0350  0.0504  0.0464  87  HIS A ND1   
577  C CD2   . HIS A 87  ? 0.5041 0.6598 0.5539 0.0412  0.0522  0.0479  87  HIS A CD2   
578  C CE1   . HIS A 87  ? 0.5077 0.6812 0.5569 0.0346  0.0501  0.0499  87  HIS A CE1   
579  N NE2   . HIS A 87  ? 0.4914 0.6622 0.5420 0.0385  0.0512  0.0508  87  HIS A NE2   
580  N N     . HIS A 88  ? 0.3752 0.4947 0.4206 0.0399  0.0510  0.0378  88  HIS A N     
581  C CA    . HIS A 88  ? 0.3568 0.4765 0.4026 0.0400  0.0505  0.0382  88  HIS A CA    
582  C C     . HIS A 88  ? 0.3901 0.5041 0.4330 0.0345  0.0478  0.0340  88  HIS A C     
583  O O     . HIS A 88  ? 0.4395 0.5592 0.4820 0.0318  0.0464  0.0342  88  HIS A O     
584  C CB    . HIS A 88  ? 0.3598 0.4712 0.4069 0.0455  0.0528  0.0388  88  HIS A CB    
585  C CG    . HIS A 88  ? 0.4312 0.5434 0.4792 0.0462  0.0526  0.0398  88  HIS A CG    
586  N ND1   . HIS A 88  ? 0.5046 0.6271 0.5552 0.0491  0.0537  0.0442  88  HIS A ND1   
587  C CD2   . HIS A 88  ? 0.4434 0.5478 0.4902 0.0447  0.0515  0.0371  88  HIS A CD2   
588  C CE1   . HIS A 88  ? 0.4811 0.6019 0.5320 0.0492  0.0532  0.0442  88  HIS A CE1   
589  N NE2   . HIS A 88  ? 0.4508 0.5608 0.4995 0.0466  0.0519  0.0399  88  HIS A NE2   
590  N N     . THR A 89  ? 0.2594 0.3622 0.3000 0.0329  0.0473  0.0302  89  THR A N     
591  C CA    . THR A 89  ? 0.2702 0.3669 0.3077 0.0283  0.0449  0.0263  89  THR A CA    
592  C C     . THR A 89  ? 0.2646 0.3688 0.3001 0.0228  0.0428  0.0259  89  THR A C     
593  O O     . THR A 89  ? 0.2777 0.3828 0.3114 0.0198  0.0412  0.0245  89  THR A O     
594  C CB    . THR A 89  ? 0.2691 0.3534 0.3045 0.0278  0.0448  0.0226  89  THR A CB    
595  O OG1   . THR A 89  ? 0.2301 0.3069 0.2667 0.0320  0.0464  0.0226  89  THR A OG1   
596  C CG2   . THR A 89  ? 0.2866 0.3653 0.3185 0.0232  0.0425  0.0189  89  THR A CG2   
597  N N     . PHE A 90  ? 0.4036 0.5133 0.4390 0.0213  0.0427  0.0270  90  PHE A N     
598  C CA    . PHE A 90  ? 0.3891 0.5047 0.4219 0.0152  0.0405  0.0262  90  PHE A CA    
599  C C     . PHE A 90  ? 0.3853 0.5141 0.4193 0.0139  0.0400  0.0292  90  PHE A C     
600  O O     . PHE A 90  ? 0.4038 0.5337 0.4349 0.0093  0.0380  0.0276  90  PHE A O     
601  C CB    . PHE A 90  ? 0.3546 0.4732 0.3873 0.0139  0.0406  0.0270  90  PHE A CB    
602  C CG    . PHE A 90  ? 0.4476 0.5541 0.4783 0.0136  0.0406  0.0237  90  PHE A CG    
603  C CD1   . PHE A 90  ? 0.5048 0.6009 0.5318 0.0102  0.0389  0.0196  90  PHE A CD1   
604  C CD2   . PHE A 90  ? 0.4608 0.5668 0.4932 0.0167  0.0423  0.0248  90  PHE A CD2   
605  C CE1   . PHE A 90  ? 0.5367 0.6227 0.5621 0.0100  0.0389  0.0169  90  PHE A CE1   
606  C CE2   . PHE A 90  ? 0.4755 0.5713 0.5062 0.0163  0.0422  0.0220  90  PHE A CE2   
607  C CZ    . PHE A 90  ? 0.5600 0.6460 0.5873 0.0129  0.0405  0.0181  90  PHE A CZ    
608  N N     . TYR A 91  ? 0.3977 0.5369 0.4355 0.0179  0.0417  0.0337  91  TYR A N     
609  C CA    . TYR A 91  ? 0.3580 0.5118 0.3970 0.0165  0.0413  0.0371  91  TYR A CA    
610  C C     . TYR A 91  ? 0.4567 0.6123 0.4971 0.0187  0.0416  0.0382  91  TYR A C     
611  O O     . TYR A 91  ? 0.5052 0.6698 0.5449 0.0153  0.0402  0.0391  91  TYR A O     
612  C CB    . TYR A 91  ? 0.3811 0.5465 0.4236 0.0201  0.0431  0.0419  91  TYR A CB    
613  C CG    . TYR A 91  ? 0.5043 0.6710 0.5455 0.0174  0.0427  0.0415  91  TYR A CG    
614  C CD1   . TYR A 91  ? 0.5052 0.6820 0.5448 0.0113  0.0407  0.0422  91  TYR A CD1   
615  C CD2   . TYR A 91  ? 0.4742 0.6322 0.5157 0.0205  0.0441  0.0403  91  TYR A CD2   
616  C CE1   . TYR A 91  ? 0.4282 0.6063 0.4666 0.0086  0.0402  0.0419  91  TYR A CE1   
617  C CE2   . TYR A 91  ? 0.4247 0.5842 0.4651 0.0181  0.0436  0.0400  91  TYR A CE2   
618  C CZ    . TYR A 91  ? 0.4249 0.5946 0.4639 0.0122  0.0417  0.0409  91  TYR A CZ    
619  O OH    . TYR A 91  ? 0.4945 0.6657 0.5323 0.0095  0.0412  0.0407  91  TYR A OH    
620  N N     . ASN A 92  ? 0.5097 0.6569 0.5518 0.0238  0.0433  0.0380  92  ASN A N     
621  C CA    . ASN A 92  ? 0.4177 0.5663 0.4614 0.0265  0.0438  0.0394  92  ASN A CA    
622  C C     . ASN A 92  ? 0.5395 0.6775 0.5805 0.0243  0.0424  0.0352  92  ASN A C     
623  O O     . ASN A 92  ? 0.6089 0.7513 0.6488 0.0217  0.0410  0.0348  92  ASN A O     
624  C CB    . ASN A 92  ? 0.3710 0.5179 0.4183 0.0337  0.0468  0.0425  92  ASN A CB    
625  C CG    . ASN A 92  ? 0.5014 0.6607 0.5515 0.0368  0.0484  0.0474  92  ASN A CG    
626  O OD1   . ASN A 92  ? 0.5348 0.7031 0.5843 0.0334  0.0474  0.0482  92  ASN A OD1   
627  N ND2   . ASN A 92  ? 0.5972 0.7572 0.6502 0.0431  0.0510  0.0509  92  ASN A ND2   
628  N N     . GLU A 93  ? 0.3977 0.5227 0.4375 0.0253  0.0427  0.0321  93  GLU A N     
629  C CA    . GLU A 93  ? 0.3040 0.4200 0.3414 0.0239  0.0416  0.0286  93  GLU A CA    
630  C C     . GLU A 93  ? 0.4156 0.5303 0.4486 0.0178  0.0391  0.0251  93  GLU A C     
631  O O     . GLU A 93  ? 0.5358 0.6513 0.5670 0.0156  0.0378  0.0238  93  GLU A O     
632  C CB    . GLU A 93  ? 0.2971 0.4004 0.3344 0.0266  0.0426  0.0265  93  GLU A CB    
633  C CG    . GLU A 93  ? 0.3786 0.4815 0.4194 0.0323  0.0452  0.0296  93  GLU A CG    
634  C CD    . GLU A 93  ? 0.3853 0.4904 0.4283 0.0356  0.0462  0.0321  93  GLU A CD    
635  O OE1   . GLU A 93  ? 0.4420 0.5391 0.4844 0.0363  0.0461  0.0302  93  GLU A OE1   
636  O OE2   . GLU A 93  ? 0.4991 0.6144 0.5446 0.0377  0.0471  0.0360  93  GLU A OE2   
637  N N     . LEU A 94  ? 0.5206 0.6346 0.5517 0.0147  0.0383  0.0239  94  LEU A N     
638  C CA    . LEU A 94  ? 0.4899 0.6008 0.5162 0.0089  0.0360  0.0205  94  LEU A CA    
639  C C     . LEU A 94  ? 0.4365 0.5599 0.4622 0.0049  0.0349  0.0224  94  LEU A C     
640  O O     . LEU A 94  ? 0.4300 0.5530 0.4516 -0.0001 0.0330  0.0201  94  LEU A O     
641  C CB    . LEU A 94  ? 0.5210 0.6223 0.5450 0.0074  0.0357  0.0178  94  LEU A CB    
642  C CG    . LEU A 94  ? 0.4543 0.5426 0.4778 0.0101  0.0364  0.0151  94  LEU A CG    
643  C CD1   . LEU A 94  ? 0.4425 0.5227 0.4620 0.0064  0.0352  0.0118  94  LEU A CD1   
644  C CD2   . LEU A 94  ? 0.4623 0.5465 0.4847 0.0107  0.0359  0.0134  94  LEU A CD2   
645  N N     . ARG A 95  ? 0.4421 0.5769 0.4717 0.0072  0.0362  0.0268  95  ARG A N     
646  C CA    . ARG A 95  ? 0.4809 0.6295 0.5104 0.0035  0.0352  0.0293  95  ARG A CA    
647  C C     . ARG A 95  ? 0.4657 0.6120 0.4905 -0.0032 0.0331  0.0265  95  ARG A C     
648  O O     . ARG A 95  ? 0.5548 0.7023 0.5755 -0.0086 0.0311  0.0246  95  ARG A O     
649  C CB    . ARG A 95  ? 0.5081 0.6638 0.5375 0.0027  0.0345  0.0302  95  ARG A CB    
650  C CG    . ARG A 95  ? 0.4921 0.6480 0.5257 0.0091  0.0364  0.0326  95  ARG A CG    
651  C CD    . ARG A 95  ? 0.5404 0.7062 0.5745 0.0082  0.0358  0.0343  95  ARG A CD    
652  N NE    . ARG A 95  ? 0.6404 0.8211 0.6748 0.0050  0.0351  0.0373  95  ARG A NE    
653  C CZ    . ARG A 95  ? 0.7081 0.8995 0.7467 0.0083  0.0367  0.0422  95  ARG A CZ    
654  N NH1   . ARG A 95  ? 0.7075 0.8952 0.7497 0.0150  0.0391  0.0443  95  ARG A NH1   
655  N NH2   . ARG A 95  ? 0.6857 0.8916 0.7244 0.0050  0.0359  0.0449  95  ARG A NH2   
656  N N     . VAL A 96  ? 0.3343 0.4767 0.3593 -0.0027 0.0337  0.0263  96  VAL A N     
657  C CA    . VAL A 96  ? 0.3142 0.4518 0.3350 -0.0083 0.0320  0.0236  96  VAL A CA    
658  C C     . VAL A 96  ? 0.3441 0.4883 0.3672 -0.0074 0.0329  0.0265  96  VAL A C     
659  O O     . VAL A 96  ? 0.3782 0.5233 0.4056 -0.0015 0.0351  0.0287  96  VAL A O     
660  C CB    . VAL A 96  ? 0.2543 0.3752 0.2720 -0.0081 0.0317  0.0191  96  VAL A CB    
661  C CG1   . VAL A 96  ? 0.2465 0.3628 0.2597 -0.0137 0.0301  0.0168  96  VAL A CG1   
662  C CG2   . VAL A 96  ? 0.2575 0.3719 0.2728 -0.0083 0.0310  0.0164  96  VAL A CG2   
663  N N     . ALA A 97  ? 0.4825 0.6309 0.5028 -0.0134 0.0313  0.0263  97  ALA A N     
664  C CA    . ALA A 97  ? 0.4785 0.6323 0.5006 -0.0130 0.0320  0.0286  97  ALA A CA    
665  C C     . ALA A 97  ? 0.4843 0.6242 0.5042 -0.0134 0.0319  0.0251  97  ALA A C     
666  O O     . ALA A 97  ? 0.5180 0.6507 0.5329 -0.0189 0.0300  0.0219  97  ALA A O     
667  C CB    . ALA A 97  ? 0.4691 0.6353 0.4894 -0.0195 0.0303  0.0305  97  ALA A CB    
668  N N     . PRO A 98  ? 0.3954 0.5309 0.4184 -0.0076 0.0340  0.0257  98  PRO A N     
669  C CA    . PRO A 98  ? 0.3393 0.4610 0.3600 -0.0078 0.0338  0.0223  98  PRO A CA    
670  C C     . PRO A 98  ? 0.3468 0.4693 0.3646 -0.0134 0.0324  0.0216  98  PRO A C     
671  O O     . PRO A 98  ? 0.4147 0.5257 0.4289 -0.0158 0.0314  0.0182  98  PRO A O     
672  C CB    . PRO A 98  ? 0.3668 0.4867 0.3918 -0.0006 0.0365  0.0238  98  PRO A CB    
673  C CG    . PRO A 98  ? 0.4052 0.5401 0.4338 0.0015  0.0376  0.0285  98  PRO A CG    
674  C CD    . PRO A 98  ? 0.4169 0.5608 0.4450 -0.0015 0.0364  0.0298  98  PRO A CD    
675  N N     . GLU A 99  ? 0.3904 0.5263 0.4093 -0.0157 0.0321  0.0250  99  GLU A N     
676  C CA    . GLU A 99  ? 0.4047 0.5424 0.4203 -0.0220 0.0304  0.0246  99  GLU A CA    
677  C C     . GLU A 99  ? 0.4022 0.5335 0.4118 -0.0291 0.0279  0.0214  99  GLU A C     
678  O O     . GLU A 99  ? 0.4895 0.6200 0.4955 -0.0351 0.0263  0.0206  99  GLU A O     
679  C CB    . GLU A 99  ? 0.4623 0.6174 0.4804 -0.0233 0.0306  0.0292  99  GLU A CB    
680  C CG    . GLU A 99  ? 0.5178 0.6840 0.5356 -0.0265 0.0294  0.0310  99  GLU A CG    
681  C CD    . GLU A 99  ? 0.6100 0.7947 0.6316 -0.0256 0.0302  0.0363  99  GLU A CD    
682  O OE1   . GLU A 99  ? 0.6243 0.8121 0.6498 -0.0198 0.0324  0.0387  99  GLU A OE1   
683  O OE2   . GLU A 99  ? 0.6580 0.8542 0.6784 -0.0306 0.0288  0.0382  99  GLU A OE2   
684  N N     . GLU A 100 ? 0.3555 0.4829 0.3639 -0.0288 0.0275  0.0197  100 GLU A N     
685  C CA    . GLU A 100 ? 0.4907 0.6107 0.4929 -0.0347 0.0253  0.0162  100 GLU A CA    
686  C C     . GLU A 100 ? 0.4705 0.5729 0.4694 -0.0338 0.0252  0.0118  100 GLU A C     
687  O O     . GLU A 100 ? 0.5612 0.6558 0.5543 -0.0392 0.0235  0.0091  100 GLU A O     
688  C CB    . GLU A 100 ? 0.6170 0.7422 0.6192 -0.0347 0.0250  0.0165  100 GLU A CB    
689  C CG    . GLU A 100 ? 0.6378 0.7817 0.6438 -0.0349 0.0253  0.0212  100 GLU A CG    
690  C CD    . GLU A 100 ? 0.6297 0.7820 0.6315 -0.0434 0.0230  0.0217  100 GLU A CD    
691  O OE1   . GLU A 100 ? 0.6573 0.8005 0.6527 -0.0492 0.0211  0.0180  100 GLU A OE1   
692  O OE2   . GLU A 100 ? 0.5951 0.7634 0.5997 -0.0444 0.0231  0.0258  100 GLU A OE2   
693  N N     . HIS A 101 ? 0.3539 0.4501 0.3561 -0.0272 0.0269  0.0113  101 HIS A N     
694  C CA    . HIS A 101 ? 0.2787 0.3599 0.2779 -0.0259 0.0269  0.0073  101 HIS A CA    
695  C C     . HIS A 101 ? 0.3817 0.4547 0.3822 -0.0226 0.0280  0.0065  101 HIS A C     
696  O O     . HIS A 101 ? 0.3971 0.4738 0.4026 -0.0175 0.0298  0.0086  101 HIS A O     
697  C CB    . HIS A 101 ? 0.3369 0.4178 0.3383 -0.0214 0.0277  0.0072  101 HIS A CB    
698  C CG    . HIS A 101 ? 0.3745 0.4626 0.3742 -0.0246 0.0266  0.0076  101 HIS A CG    
699  N ND1   . HIS A 101 ? 0.3430 0.4458 0.3462 -0.0246 0.0269  0.0114  101 HIS A ND1   
700  C CD2   . HIS A 101 ? 0.3776 0.4606 0.3722 -0.0281 0.0252  0.0048  101 HIS A CD2   
701  C CE1   . HIS A 101 ? 0.4138 0.5204 0.4143 -0.0281 0.0256  0.0109  101 HIS A CE1   
702  N NE2   . HIS A 101 ? 0.4380 0.5325 0.4331 -0.0303 0.0246  0.0068  101 HIS A NE2   
703  N N     . PRO A 102 ? 0.3309 0.3931 0.3270 -0.0254 0.0270  0.0037  102 PRO A N     
704  C CA    . PRO A 102 ? 0.2905 0.3445 0.2879 -0.0219 0.0281  0.0027  102 PRO A CA    
705  C C     . PRO A 102 ? 0.2874 0.3378 0.2882 -0.0155 0.0297  0.0023  102 PRO A C     
706  O O     . PRO A 102 ? 0.3232 0.3716 0.3231 -0.0146 0.0295  0.0012  102 PRO A O     
707  C CB    . PRO A 102 ? 0.3031 0.3451 0.2943 -0.0257 0.0267  -0.0007 102 PRO A CB    
708  C CG    . PRO A 102 ? 0.2698 0.3114 0.2563 -0.0300 0.0251  -0.0020 102 PRO A CG    
709  C CD    . PRO A 102 ? 0.3103 0.3664 0.2996 -0.0317 0.0250  0.0012  102 PRO A CD    
710  N N     . VAL A 103 ? 0.4668 0.5163 0.4712 -0.0112 0.0313  0.0032  103 VAL A N     
711  C CA    . VAL A 103 ? 0.4901 0.5375 0.4980 -0.0054 0.0330  0.0033  103 VAL A CA    
712  C C     . VAL A 103 ? 0.4158 0.4524 0.4231 -0.0032 0.0336  0.0011  103 VAL A C     
713  O O     . VAL A 103 ? 0.4042 0.4407 0.4130 -0.0020 0.0345  0.0018  103 VAL A O     
714  C CB    . VAL A 103 ? 0.4771 0.5343 0.4901 -0.0016 0.0348  0.0068  103 VAL A CB    
715  C CG1   . VAL A 103 ? 0.5400 0.5928 0.5559 0.0040  0.0366  0.0067  103 VAL A CG1   
716  C CG2   . VAL A 103 ? 0.3669 0.4354 0.3809 -0.0032 0.0343  0.0092  103 VAL A CG2   
717  N N     . LEU A 104 ? 0.3045 0.3328 0.3096 -0.0025 0.0332  -0.0013 104 LEU A N     
718  C CA    . LEU A 104 ? 0.2593 0.2791 0.2649 0.0007  0.0341  -0.0029 104 LEU A CA    
719  C C     . LEU A 104 ? 0.3063 0.3287 0.3164 0.0056  0.0359  -0.0014 104 LEU A C     
720  O O     . LEU A 104 ? 0.3402 0.3662 0.3515 0.0068  0.0360  -0.0006 104 LEU A O     
721  C CB    . LEU A 104 ? 0.2693 0.2803 0.2709 -0.0002 0.0331  -0.0057 104 LEU A CB    
722  C CG    . LEU A 104 ? 0.2792 0.2828 0.2815 0.0035  0.0340  -0.0072 104 LEU A CG    
723  C CD1   . LEU A 104 ? 0.3493 0.3515 0.3537 0.0052  0.0350  -0.0067 104 LEU A CD1   
724  C CD2   . LEU A 104 ? 0.2519 0.2468 0.2495 0.0021  0.0329  -0.0098 104 LEU A CD2   
725  N N     . LEU A 105 ? 0.3688 0.3891 0.3810 0.0084  0.0373  -0.0010 105 LEU A N     
726  C CA    . LEU A 105 ? 0.3220 0.3431 0.3378 0.0130  0.0391  0.0002  105 LEU A CA    
727  C C     . LEU A 105 ? 0.3011 0.3132 0.3164 0.0149  0.0396  -0.0017 105 LEU A C     
728  O O     . LEU A 105 ? 0.3512 0.3579 0.3642 0.0132  0.0390  -0.0035 105 LEU A O     
729  C CB    . LEU A 105 ? 0.4202 0.4477 0.4389 0.0148  0.0405  0.0027  105 LEU A CB    
730  C CG    . LEU A 105 ? 0.4930 0.5313 0.5137 0.0149  0.0408  0.0057  105 LEU A CG    
731  C CD1   . LEU A 105 ? 0.5158 0.5598 0.5371 0.0141  0.0412  0.0073  105 LEU A CD1   
732  C CD2   . LEU A 105 ? 0.5141 0.5549 0.5380 0.0194  0.0426  0.0077  105 LEU A CD2   
733  N N     . THR A 106 ? 0.2364 0.2471 0.2537 0.0182  0.0408  -0.0013 106 THR A N     
734  C CA    . THR A 106 ? 0.3104 0.3134 0.3273 0.0197  0.0413  -0.0030 106 THR A CA    
735  C C     . THR A 106 ? 0.3568 0.3592 0.3760 0.0227  0.0432  -0.0020 106 THR A C     
736  O O     . THR A 106 ? 0.3560 0.3632 0.3775 0.0249  0.0445  0.0002  106 THR A O     
737  C CB    . THR A 106 ? 0.3295 0.3301 0.3463 0.0208  0.0411  -0.0036 106 THR A CB    
738  O OG1   . THR A 106 ? 0.3589 0.3620 0.3787 0.0238  0.0426  -0.0017 106 THR A OG1   
739  C CG2   . THR A 106 ? 0.3151 0.3182 0.3302 0.0187  0.0396  -0.0039 106 THR A CG2   
740  N N     . GLU A 107 ? 0.4486 0.4447 0.4668 0.0229  0.0435  -0.0037 107 GLU A N     
741  C CA    . GLU A 107 ? 0.3161 0.3100 0.3355 0.0253  0.0453  -0.0034 107 GLU A CA    
742  C C     . GLU A 107 ? 0.2626 0.2498 0.2814 0.0261  0.0456  -0.0048 107 GLU A C     
743  O O     . GLU A 107 ? 0.3189 0.3029 0.3361 0.0247  0.0443  -0.0064 107 GLU A O     
744  C CB    . GLU A 107 ? 0.3568 0.3507 0.3753 0.0242  0.0453  -0.0039 107 GLU A CB    
745  C CG    . GLU A 107 ? 0.4267 0.4154 0.4427 0.0217  0.0439  -0.0062 107 GLU A CG    
746  C CD    . GLU A 107 ? 0.4890 0.4782 0.5041 0.0202  0.0438  -0.0065 107 GLU A CD    
747  O OE1   . GLU A 107 ? 0.3815 0.3739 0.3979 0.0216  0.0451  -0.0053 107 GLU A OE1   
748  O OE2   . GLU A 107 ? 0.5516 0.5380 0.5644 0.0177  0.0424  -0.0078 107 GLU A OE2   
749  N N     . ALA A 108 ? 0.3258 0.3110 0.3456 0.0284  0.0473  -0.0043 108 ALA A N     
750  C CA    . ALA A 108 ? 0.2796 0.2589 0.2986 0.0287  0.0476  -0.0056 108 ALA A CA    
751  C C     . ALA A 108 ? 0.3980 0.3733 0.4152 0.0271  0.0470  -0.0077 108 ALA A C     
752  O O     . ALA A 108 ? 0.2384 0.2147 0.2550 0.0262  0.0468  -0.0080 108 ALA A O     
753  C CB    . ALA A 108 ? 0.2397 0.2171 0.2596 0.0312  0.0496  -0.0046 108 ALA A CB    
754  N N     . PRO A 109 ? 0.6425 0.6137 0.6588 0.0267  0.0467  -0.0088 109 PRO A N     
755  C CA    . PRO A 109 ? 0.5606 0.5282 0.5753 0.0255  0.0464  -0.0105 109 PRO A CA    
756  C C     . PRO A 109 ? 0.6246 0.5905 0.6394 0.0265  0.0480  -0.0106 109 PRO A C     
757  O O     . PRO A 109 ? 0.7232 0.6888 0.7389 0.0283  0.0495  -0.0095 109 PRO A O     
758  C CB    . PRO A 109 ? 0.5811 0.5458 0.5953 0.0253  0.0460  -0.0112 109 PRO A CB    
759  C CG    . PRO A 109 ? 0.5694 0.5368 0.5843 0.0256  0.0452  -0.0104 109 PRO A CG    
760  C CD    . PRO A 109 ? 0.5676 0.5385 0.5841 0.0268  0.0460  -0.0087 109 PRO A CD    
761  N N     . LEU A 110 ? 0.6111 0.5758 0.6247 0.0255  0.0479  -0.0117 110 LEU A N     
762  C CA    . LEU A 110 ? 0.5933 0.5563 0.6065 0.0264  0.0495  -0.0120 110 LEU A CA    
763  C C     . LEU A 110 ? 0.5253 0.4916 0.5398 0.0285  0.0509  -0.0104 110 LEU A C     
764  O O     . LEU A 110 ? 0.5377 0.5020 0.5521 0.0305  0.0527  -0.0101 110 LEU A O     
765  C CB    . LEU A 110 ? 0.6581 0.6161 0.6704 0.0267  0.0504  -0.0129 110 LEU A CB    
766  C CG    . LEU A 110 ? 0.7517 0.7071 0.7626 0.0246  0.0494  -0.0144 110 LEU A CG    
767  C CD1   . LEU A 110 ? 0.7301 0.6814 0.7400 0.0245  0.0502  -0.0150 110 LEU A CD1   
768  C CD2   . LEU A 110 ? 0.7729 0.7283 0.7826 0.0234  0.0490  -0.0156 110 LEU A CD2   
769  N N     . ASN A 111 ? 0.4734 0.4449 0.4887 0.0280  0.0501  -0.0093 111 ASN A N     
770  C CA    . ASN A 111 ? 0.4797 0.4559 0.4964 0.0300  0.0513  -0.0075 111 ASN A CA    
771  C C     . ASN A 111 ? 0.5855 0.5627 0.6015 0.0298  0.0519  -0.0079 111 ASN A C     
772  O O     . ASN A 111 ? 0.6149 0.5922 0.6299 0.0274  0.0506  -0.0089 111 ASN A O     
773  C CB    . ASN A 111 ? 0.4536 0.4356 0.4714 0.0290  0.0501  -0.0060 111 ASN A CB    
774  C CG    . ASN A 111 ? 0.4304 0.4180 0.4500 0.0314  0.0513  -0.0036 111 ASN A CG    
775  O OD1   . ASN A 111 ? 0.4611 0.4473 0.4813 0.0343  0.0532  -0.0027 111 ASN A OD1   
776  N ND2   . ASN A 111 ? 0.4713 0.4655 0.4916 0.0301  0.0504  -0.0023 111 ASN A ND2   
777  N N     . PRO A 112 ? 0.6299 0.6078 0.6461 0.0326  0.0540  -0.0070 112 PRO A N     
778  C CA    . PRO A 112 ? 0.5604 0.5401 0.5760 0.0329  0.0547  -0.0072 112 PRO A CA    
779  C C     . PRO A 112 ? 0.4887 0.4755 0.5052 0.0313  0.0535  -0.0059 112 PRO A C     
780  O O     . PRO A 112 ? 0.5767 0.5685 0.5946 0.0315  0.0531  -0.0041 112 PRO A O     
781  C CB    . PRO A 112 ? 0.5210 0.5003 0.5367 0.0368  0.0573  -0.0061 112 PRO A CB    
782  C CG    . PRO A 112 ? 0.5463 0.5200 0.5616 0.0379  0.0579  -0.0064 112 PRO A CG    
783  C CD    . PRO A 112 ? 0.6178 0.5933 0.6344 0.0357  0.0559  -0.0061 112 PRO A CD    
784  N N     . LYS A 113 ? 0.3894 0.3770 0.4050 0.0296  0.0530  -0.0068 113 LYS A N     
785  C CA    . LYS A 113 ? 0.4153 0.4092 0.4313 0.0273  0.0516  -0.0056 113 LYS A CA    
786  C C     . LYS A 113 ? 0.4201 0.4218 0.4378 0.0294  0.0528  -0.0029 113 LYS A C     
787  O O     . LYS A 113 ? 0.4335 0.4415 0.4520 0.0274  0.0515  -0.0014 113 LYS A O     
788  C CB    . LYS A 113 ? 0.4836 0.4768 0.4982 0.0254  0.0511  -0.0067 113 LYS A CB    
789  C CG    . LYS A 113 ? 0.5020 0.4986 0.5167 0.0275  0.0529  -0.0060 113 LYS A CG    
790  C CD    . LYS A 113 ? 0.5420 0.5413 0.5559 0.0248  0.0519  -0.0062 113 LYS A CD    
791  C CE    . LYS A 113 ? 0.5448 0.5504 0.5592 0.0268  0.0535  -0.0048 113 LYS A CE    
792  N NZ    . LYS A 113 ? 0.4794 0.4907 0.4937 0.0238  0.0522  -0.0038 113 LYS A NZ    
793  N N     . ALA A 114 ? 0.3718 0.3736 0.3899 0.0334  0.0552  -0.0022 114 ALA A N     
794  C CA    . ALA A 114 ? 0.3357 0.3456 0.3555 0.0359  0.0564  0.0006  114 ALA A CA    
795  C C     . ALA A 114 ? 0.4992 0.5126 0.5206 0.0364  0.0560  0.0024  114 ALA A C     
796  O O     . ALA A 114 ? 0.5623 0.5844 0.5852 0.0366  0.0559  0.0049  114 ALA A O     
797  C CB    . ALA A 114 ? 0.2864 0.2946 0.3056 0.0407  0.0594  0.0009  114 ALA A CB    
798  N N     . ASN A 115 ? 0.6106 0.6179 0.6318 0.0364  0.0557  0.0013  115 ASN A N     
799  C CA    . ASN A 115 ? 0.4977 0.5082 0.5204 0.0367  0.0552  0.0030  115 ASN A CA    
800  C C     . ASN A 115 ? 0.3645 0.3794 0.3872 0.0324  0.0526  0.0031  115 ASN A C     
801  O O     . ASN A 115 ? 0.4062 0.4288 0.4304 0.0322  0.0523  0.0053  115 ASN A O     
802  C CB    . ASN A 115 ? 0.5140 0.5168 0.5362 0.0377  0.0556  0.0017  115 ASN A CB    
803  C CG    . ASN A 115 ? 0.6938 0.6924 0.7156 0.0419  0.0583  0.0020  115 ASN A CG    
804  O OD1   . ASN A 115 ? 0.7808 0.7776 0.8014 0.0432  0.0596  0.0012  115 ASN A OD1   
805  N ND2   . ASN A 115 ? 0.7276 0.7245 0.7501 0.0442  0.0592  0.0031  115 ASN A ND2   
806  N N     . ARG A 116 ? 0.3055 0.3159 0.3265 0.0289  0.0509  0.0009  116 ARG A N     
807  C CA    . ARG A 116 ? 0.2668 0.2804 0.2873 0.0249  0.0486  0.0009  116 ARG A CA    
808  C C     . ARG A 116 ? 0.2910 0.3135 0.3120 0.0236  0.0483  0.0030  116 ARG A C     
809  O O     . ARG A 116 ? 0.4518 0.4783 0.4724 0.0203  0.0466  0.0036  116 ARG A O     
810  C CB    . ARG A 116 ? 0.3417 0.3487 0.3599 0.0218  0.0470  -0.0016 116 ARG A CB    
811  C CG    . ARG A 116 ? 0.4046 0.4035 0.4220 0.0233  0.0478  -0.0037 116 ARG A CG    
812  C CD    . ARG A 116 ? 0.3818 0.3758 0.3969 0.0201  0.0460  -0.0057 116 ARG A CD    
813  N NE    . ARG A 116 ? 0.3893 0.3830 0.4037 0.0181  0.0443  -0.0059 116 ARG A NE    
814  C CZ    . ARG A 116 ? 0.4000 0.3923 0.4122 0.0148  0.0425  -0.0067 116 ARG A CZ    
815  N NH1   . ARG A 116 ? 0.4135 0.4051 0.4244 0.0130  0.0421  -0.0071 116 ARG A NH1   
816  N NH2   . ARG A 116 ? 0.3914 0.3828 0.4024 0.0133  0.0412  -0.0070 116 ARG A NH2   
817  N N     . GLU A 117 ? 0.2761 0.3021 0.2979 0.0257  0.0499  0.0041  117 GLU A N     
818  C CA    . GLU A 117 ? 0.3326 0.3684 0.3551 0.0242  0.0495  0.0064  117 GLU A CA    
819  C C     . GLU A 117 ? 0.2772 0.3217 0.3019 0.0266  0.0505  0.0095  117 GLU A C     
820  O O     . GLU A 117 ? 0.2763 0.3294 0.3015 0.0241  0.0493  0.0114  117 GLU A O     
821  C CB    . GLU A 117 ? 0.4154 0.4524 0.4376 0.0254  0.0506  0.0064  117 GLU A CB    
822  C CG    . GLU A 117 ? 0.5070 0.5374 0.5271 0.0224  0.0495  0.0039  117 GLU A CG    
823  C CD    . GLU A 117 ? 0.5625 0.5926 0.5823 0.0246  0.0511  0.0036  117 GLU A CD    
824  O OE1   . GLU A 117 ? 0.5920 0.6281 0.6132 0.0281  0.0530  0.0055  117 GLU A OE1   
825  O OE2   . GLU A 117 ? 0.4858 0.5100 0.5040 0.0230  0.0505  0.0014  117 GLU A OE2   
826  N N     . LYS A 118 ? 0.3664 0.4090 0.3924 0.0314  0.0526  0.0101  118 LYS A N     
827  C CA    . LYS A 118 ? 0.4935 0.5440 0.5216 0.0342  0.0536  0.0132  118 LYS A CA    
828  C C     . LYS A 118 ? 0.5743 0.6266 0.6026 0.0313  0.0518  0.0135  118 LYS A C     
829  O O     . LYS A 118 ? 0.6333 0.6954 0.6631 0.0308  0.0515  0.0161  118 LYS A O     
830  C CB    . LYS A 118 ? 0.4700 0.5164 0.4987 0.0400  0.0564  0.0137  118 LYS A CB    
831  C CG    . LYS A 118 ? 0.5855 0.6409 0.6164 0.0441  0.0582  0.0176  118 LYS A CG    
832  C CD    . LYS A 118 ? 0.6627 0.7298 0.6946 0.0441  0.0585  0.0202  118 LYS A CD    
833  C CE    . LYS A 118 ? 0.6703 0.7473 0.7045 0.0486  0.0604  0.0244  118 LYS A CE    
834  N NZ    . LYS A 118 ? 0.6460 0.7365 0.6814 0.0476  0.0601  0.0273  118 LYS A NZ    
835  N N     . MET A 119 ? 0.4737 0.5174 0.5006 0.0294  0.0505  0.0108  119 MET A N     
836  C CA    . MET A 119 ? 0.3937 0.4389 0.4203 0.0264  0.0486  0.0107  119 MET A CA    
837  C C     . MET A 119 ? 0.3859 0.4374 0.4114 0.0214  0.0466  0.0112  119 MET A C     
838  O O     . MET A 119 ? 0.4321 0.4919 0.4583 0.0199  0.0458  0.0132  119 MET A O     
839  C CB    . MET A 119 ? 0.3431 0.3780 0.3680 0.0251  0.0476  0.0076  119 MET A CB    
840  C CG    . MET A 119 ? 0.4466 0.4738 0.4719 0.0288  0.0492  0.0066  119 MET A CG    
841  S SD    . MET A 119 ? 0.5176 0.5343 0.5405 0.0263  0.0476  0.0030  119 MET A SD    
842  C CE    . MET A 119 ? 0.4243 0.4445 0.4470 0.0239  0.0458  0.0034  119 MET A CE    
843  N N     . THR A 120 ? 0.4063 0.4539 0.4298 0.0184  0.0455  0.0094  120 THR A N     
844  C CA    . THR A 120 ? 0.4100 0.4628 0.4320 0.0134  0.0437  0.0099  120 THR A CA    
845  C C     . THR A 120 ? 0.4073 0.4727 0.4313 0.0140  0.0444  0.0134  120 THR A C     
846  O O     . THR A 120 ? 0.4350 0.5079 0.4587 0.0107  0.0430  0.0149  120 THR A O     
847  C CB    . THR A 120 ? 0.4426 0.4893 0.4624 0.0113  0.0430  0.0078  120 THR A CB    
848  O OG1   . THR A 120 ? 0.4903 0.5268 0.5078 0.0097  0.0419  0.0049  120 THR A OG1   
849  C CG2   . THR A 120 ? 0.4645 0.5175 0.4829 0.0065  0.0415  0.0089  120 THR A CG2   
850  N N     . GLN A 121 ? 0.4163 0.4844 0.4421 0.0182  0.0465  0.0148  121 GLN A N     
851  C CA    . GLN A 121 ? 0.4085 0.4891 0.4361 0.0193  0.0474  0.0183  121 GLN A CA    
852  C C     . GLN A 121 ? 0.4082 0.4971 0.4378 0.0208  0.0478  0.0211  121 GLN A C     
853  O O     . GLN A 121 ? 0.3665 0.4667 0.3968 0.0184  0.0470  0.0237  121 GLN A O     
854  C CB    . GLN A 121 ? 0.3545 0.4351 0.3834 0.0245  0.0500  0.0190  121 GLN A CB    
855  C CG    . GLN A 121 ? 0.3623 0.4552 0.3937 0.0281  0.0518  0.0230  121 GLN A CG    
856  C CD    . GLN A 121 ? 0.4014 0.4927 0.4332 0.0337  0.0546  0.0233  121 GLN A CD    
857  O OE1   . GLN A 121 ? 0.4078 0.4884 0.4383 0.0349  0.0552  0.0205  121 GLN A OE1   
858  N NE2   . GLN A 121 ? 0.3929 0.4950 0.4265 0.0371  0.0563  0.0268  121 GLN A NE2   
859  N N     . ILE A 122 ? 0.2759 0.3598 0.3066 0.0247  0.0490  0.0207  122 ILE A N     
860  C CA    . ILE A 122 ? 0.3580 0.4496 0.3908 0.0269  0.0497  0.0235  122 ILE A CA    
861  C C     . ILE A 122 ? 0.3906 0.4853 0.4223 0.0216  0.0471  0.0232  122 ILE A C     
862  O O     . ILE A 122 ? 0.3306 0.4362 0.3637 0.0210  0.0469  0.0261  122 ILE A O     
863  C CB    . ILE A 122 ? 0.3604 0.4446 0.3942 0.0323  0.0517  0.0231  122 ILE A CB    
864  C CG1   . ILE A 122 ? 0.2381 0.3214 0.2728 0.0380  0.0546  0.0241  122 ILE A CG1   
865  C CG2   . ILE A 122 ? 0.3476 0.4379 0.3832 0.0335  0.0518  0.0254  122 ILE A CG2   
866  C CD1   . ILE A 122 ? 0.2394 0.3138 0.2743 0.0426  0.0565  0.0234  122 ILE A CD1   
867  N N     . MET A 123 ? 0.4930 0.5782 0.5220 0.0178  0.0452  0.0197  123 MET A N     
868  C CA    . MET A 123 ? 0.5030 0.5896 0.5301 0.0127  0.0429  0.0190  123 MET A CA    
869  C C     . MET A 123 ? 0.5364 0.6327 0.5625 0.0076  0.0413  0.0206  123 MET A C     
870  O O     . MET A 123 ? 0.5039 0.6079 0.5298 0.0047  0.0401  0.0220  123 MET A O     
871  C CB    . MET A 123 ? 0.4428 0.5165 0.4667 0.0101  0.0414  0.0149  123 MET A CB    
872  C CG    . MET A 123 ? 0.4592 0.5295 0.4822 0.0092  0.0404  0.0136  123 MET A CG    
873  S SD    . MET A 123 ? 0.4723 0.5466 0.4989 0.0148  0.0424  0.0159  123 MET A SD    
874  C CE    . MET A 123 ? 0.4842 0.5475 0.5118 0.0200  0.0445  0.0144  123 MET A CE    
875  N N     . PHE A 124 ? 0.3237 0.4197 0.3489 0.0060  0.0412  0.0203  124 PHE A N     
876  C CA    . PHE A 124 ? 0.3840 0.4890 0.4080 0.0009  0.0397  0.0219  124 PHE A CA    
877  C C     . PHE A 124 ? 0.4062 0.5262 0.4336 0.0035  0.0411  0.0264  124 PHE A C     
878  O O     . PHE A 124 ? 0.4241 0.5550 0.4514 -0.0001 0.0399  0.0287  124 PHE A O     
879  C CB    . PHE A 124 ? 0.2800 0.3790 0.3017 -0.0019 0.0389  0.0201  124 PHE A CB    
880  C CG    . PHE A 124 ? 0.2440 0.3316 0.2615 -0.0066 0.0368  0.0165  124 PHE A CG    
881  C CD1   . PHE A 124 ? 0.2653 0.3547 0.2797 -0.0129 0.0345  0.0161  124 PHE A CD1   
882  C CD2   . PHE A 124 ? 0.2440 0.3191 0.2604 -0.0049 0.0372  0.0135  124 PHE A CD2   
883  C CE1   . PHE A 124 ? 0.2500 0.3281 0.2600 -0.0168 0.0328  0.0128  124 PHE A CE1   
884  C CE2   . PHE A 124 ? 0.2465 0.3115 0.2590 -0.0087 0.0355  0.0104  124 PHE A CE2   
885  C CZ    . PHE A 124 ? 0.2497 0.3159 0.2589 -0.0144 0.0333  0.0101  124 PHE A CZ    
886  N N     . GLU A 125 ? 0.5273 0.6481 0.5573 0.0098  0.0437  0.0277  125 GLU A N     
887  C CA    . GLU A 125 ? 0.5020 0.6370 0.5350 0.0129  0.0453  0.0321  125 GLU A CA    
888  C C     . GLU A 125 ? 0.4375 0.5794 0.4729 0.0164  0.0464  0.0348  125 GLU A C     
889  O O     . GLU A 125 ? 0.5478 0.7036 0.5845 0.0153  0.0461  0.0383  125 GLU A O     
890  C CB    . GLU A 125 ? 0.4803 0.6137 0.5146 0.0185  0.0479  0.0326  125 GLU A CB    
891  C CG    . GLU A 125 ? 0.5445 0.6717 0.5766 0.0155  0.0470  0.0302  125 GLU A CG    
892  C CD    . GLU A 125 ? 0.5871 0.7175 0.6204 0.0200  0.0492  0.0316  125 GLU A CD    
893  O OE1   . GLU A 125 ? 0.5703 0.7038 0.6059 0.0266  0.0519  0.0336  125 GLU A OE1   
894  O OE2   . GLU A 125 ? 0.5829 0.7127 0.6149 0.0168  0.0483  0.0308  125 GLU A OE2   
895  N N     . THR A 126 ? 0.2573 0.3906 0.2933 0.0206  0.0476  0.0334  126 THR A N     
896  C CA    . THR A 126 ? 0.3313 0.4717 0.3697 0.0241  0.0487  0.0364  126 THR A CA    
897  C C     . THR A 126 ? 0.3432 0.4870 0.3806 0.0189  0.0463  0.0361  126 THR A C     
898  O O     . THR A 126 ? 0.3594 0.5157 0.3985 0.0189  0.0463  0.0395  126 THR A O     
899  C CB    . THR A 126 ? 0.3065 0.4374 0.3460 0.0305  0.0510  0.0356  126 THR A CB    
900  O OG1   . THR A 126 ? 0.2933 0.4217 0.3335 0.0355  0.0534  0.0360  126 THR A OG1   
901  C CG2   . THR A 126 ? 0.2384 0.3773 0.2804 0.0339  0.0521  0.0390  126 THR A CG2   
902  N N     . PHE A 127 ? 0.3437 0.4766 0.3782 0.0149  0.0444  0.0321  127 PHE A N     
903  C CA    . PHE A 127 ? 0.3936 0.5286 0.4266 0.0102  0.0423  0.0315  127 PHE A CA    
904  C C     . PHE A 127 ? 0.3973 0.5345 0.4269 0.0023  0.0395  0.0303  127 PHE A C     
905  O O     . PHE A 127 ? 0.3907 0.5301 0.4183 -0.0021 0.0377  0.0298  127 PHE A O     
906  C CB    . PHE A 127 ? 0.4240 0.5462 0.4558 0.0113  0.0420  0.0282  127 PHE A CB    
907  C CG    . PHE A 127 ? 0.3057 0.4248 0.3404 0.0184  0.0446  0.0292  127 PHE A CG    
908  C CD1   . PHE A 127 ? 0.2531 0.3802 0.2903 0.0214  0.0456  0.0324  127 PHE A CD1   
909  C CD2   . PHE A 127 ? 0.3138 0.4218 0.3484 0.0218  0.0460  0.0272  127 PHE A CD2   
910  C CE1   . PHE A 127 ? 0.3035 0.4270 0.3430 0.0280  0.0481  0.0335  127 PHE A CE1   
911  C CE2   . PHE A 127 ? 0.4021 0.5064 0.4388 0.0280  0.0484  0.0281  127 PHE A CE2   
912  C CZ    . PHE A 127 ? 0.3870 0.4988 0.4261 0.0311  0.0494  0.0313  127 PHE A CZ    
913  N N     . ASN A 128 ? 0.4336 0.5701 0.4621 0.0003  0.0392  0.0299  128 ASN A N     
914  C CA    . ASN A 128 ? 0.4247 0.5629 0.4497 -0.0074 0.0367  0.0290  128 ASN A CA    
915  C C     . ASN A 128 ? 0.4415 0.5692 0.4623 -0.0120 0.0346  0.0252  128 ASN A C     
916  O O     . ASN A 128 ? 0.4357 0.5681 0.4543 -0.0170 0.0328  0.0253  128 ASN A O     
917  C CB    . ASN A 128 ? 0.5345 0.6897 0.5604 -0.0106 0.0360  0.0329  128 ASN A CB    
918  C CG    . ASN A 128 ? 0.6382 0.8051 0.6680 -0.0059 0.0381  0.0371  128 ASN A CG    
919  O OD1   . ASN A 128 ? 0.6743 0.8407 0.7039 -0.0060 0.0385  0.0372  128 ASN A OD1   
920  N ND2   . ASN A 128 ? 0.6548 0.8325 0.6880 -0.0017 0.0396  0.0407  128 ASN A ND2   
921  N N     . THR A 129 ? 0.3225 0.4357 0.3418 -0.0103 0.0348  0.0216  129 THR A N     
922  C CA    . THR A 129 ? 0.2911 0.3947 0.3060 -0.0146 0.0329  0.0181  129 THR A CA    
923  C C     . THR A 129 ? 0.2971 0.3963 0.3075 -0.0210 0.0309  0.0164  129 THR A C     
924  O O     . THR A 129 ? 0.2798 0.3803 0.2907 -0.0213 0.0313  0.0172  129 THR A O     
925  C CB    . THR A 129 ? 0.3390 0.4296 0.3539 -0.0104 0.0338  0.0152  129 THR A CB    
926  O OG1   . THR A 129 ? 0.3607 0.4422 0.3748 -0.0095 0.0341  0.0133  129 THR A OG1   
927  C CG2   . THR A 129 ? 0.3020 0.3962 0.3215 -0.0038 0.0360  0.0172  129 THR A CG2   
928  N N     . PRO A 130 ? 0.3483 0.4427 0.3540 -0.0265 0.0289  0.0141  130 PRO A N     
929  C CA    . PRO A 130 ? 0.2819 0.3705 0.2825 -0.0328 0.0270  0.0124  130 PRO A CA    
930  C C     . PRO A 130 ? 0.3385 0.4133 0.3374 -0.0312 0.0273  0.0095  130 PRO A C     
931  O O     . PRO A 130 ? 0.3585 0.4299 0.3546 -0.0350 0.0264  0.0090  130 PRO A O     
932  C CB    . PRO A 130 ? 0.2650 0.3511 0.2607 -0.0381 0.0251  0.0106  130 PRO A CB    
933  C CG    . PRO A 130 ? 0.2618 0.3492 0.2600 -0.0336 0.0260  0.0105  130 PRO A CG    
934  C CD    . PRO A 130 ? 0.3217 0.4192 0.3265 -0.0277 0.0281  0.0140  130 PRO A CD    
935  N N     . ALA A 131 ? 0.3881 0.4550 0.3885 -0.0260 0.0285  0.0077  131 ALA A N     
936  C CA    . ALA A 131 ? 0.2689 0.3225 0.2673 -0.0245 0.0287  0.0049  131 ALA A CA    
937  C C     . ALA A 131 ? 0.2549 0.3050 0.2568 -0.0179 0.0305  0.0043  131 ALA A C     
938  O O     . ALA A 131 ? 0.2799 0.3369 0.2849 -0.0152 0.0313  0.0059  131 ALA A O     
939  C CB    . ALA A 131 ? 0.2653 0.3087 0.2574 -0.0292 0.0269  0.0018  131 ALA A CB    
940  N N     . MET A 132 ? 0.5039 0.5446 0.5056 -0.0153 0.0311  0.0024  132 MET A N     
941  C CA    . MET A 132 ? 0.4579 0.4955 0.4629 -0.0094 0.0328  0.0020  132 MET A CA    
942  C C     . MET A 132 ? 0.5023 0.5285 0.5057 -0.0079 0.0331  -0.0005 132 MET A C     
943  O O     . MET A 132 ? 0.4735 0.4958 0.4745 -0.0105 0.0324  -0.0013 132 MET A O     
944  C CB    . MET A 132 ? 0.4596 0.5060 0.4693 -0.0058 0.0346  0.0049  132 MET A CB    
945  C CG    . MET A 132 ? 0.6295 0.6732 0.6425 0.0002  0.0366  0.0050  132 MET A CG    
946  S SD    . MET A 132 ? 0.6650 0.7048 0.6788 0.0023  0.0379  0.0046  132 MET A SD    
947  C CE    . MET A 132 ? 0.6776 0.7156 0.6950 0.0088  0.0402  0.0050  132 MET A CE    
948  N N     . TYR A 133 ? 0.4159 0.4369 0.4206 -0.0039 0.0340  -0.0017 133 TYR A N     
949  C CA    . TYR A 133 ? 0.3927 0.4041 0.3963 -0.0022 0.0344  -0.0038 133 TYR A CA    
950  C C     . TYR A 133 ? 0.4525 0.4631 0.4596 0.0029  0.0361  -0.0036 133 TYR A C     
951  O O     . TYR A 133 ? 0.3922 0.4064 0.4011 0.0046  0.0365  -0.0027 133 TYR A O     
952  C CB    . TYR A 133 ? 0.4590 0.4620 0.4581 -0.0043 0.0330  -0.0063 133 TYR A CB    
953  C CG    . TYR A 133 ? 0.5105 0.5043 0.5075 -0.0038 0.0329  -0.0082 133 TYR A CG    
954  C CD1   . TYR A 133 ? 0.5140 0.5049 0.5081 -0.0071 0.0321  -0.0086 133 TYR A CD1   
955  C CD2   . TYR A 133 ? 0.4630 0.4512 0.4606 -0.0003 0.0337  -0.0095 133 TYR A CD2   
956  C CE1   . TYR A 133 ? 0.5011 0.4840 0.4932 -0.0065 0.0321  -0.0101 133 TYR A CE1   
957  C CE2   . TYR A 133 ? 0.4281 0.4087 0.4238 0.0001  0.0336  -0.0110 133 TYR A CE2   
958  C CZ    . TYR A 133 ? 0.5204 0.4983 0.5133 -0.0029 0.0328  -0.0113 133 TYR A CZ    
959  O OH    . TYR A 133 ? 0.5852 0.5560 0.5762 -0.0023 0.0328  -0.0126 133 TYR A OH    
960  N N     . VAL A 134 ? 0.4682 0.4740 0.4760 0.0051  0.0370  -0.0044 134 VAL A N     
961  C CA    . VAL A 134 ? 0.4743 0.4776 0.4846 0.0094  0.0385  -0.0046 134 VAL A CA    
962  C C     . VAL A 134 ? 0.4415 0.4361 0.4497 0.0096  0.0380  -0.0069 134 VAL A C     
963  O O     . VAL A 134 ? 0.4289 0.4187 0.4346 0.0079  0.0373  -0.0082 134 VAL A O     
964  C CB    . VAL A 134 ? 0.4366 0.4417 0.4494 0.0119  0.0402  -0.0035 134 VAL A CB    
965  C CG1   . VAL A 134 ? 0.4080 0.4118 0.4232 0.0160  0.0418  -0.0032 134 VAL A CG1   
966  C CG2   . VAL A 134 ? 0.4032 0.4172 0.4175 0.0113  0.0405  -0.0012 134 VAL A CG2   
967  N N     . ALA A 135 ? 0.3464 0.3392 0.3555 0.0120  0.0385  -0.0073 135 ALA A N     
968  C CA    . ALA A 135 ? 0.3675 0.3532 0.3747 0.0125  0.0380  -0.0092 135 ALA A CA    
969  C C     . ALA A 135 ? 0.3271 0.3117 0.3368 0.0158  0.0393  -0.0090 135 ALA A C     
970  O O     . ALA A 135 ? 0.3476 0.3363 0.3598 0.0176  0.0402  -0.0075 135 ALA A O     
971  C CB    . ALA A 135 ? 0.4100 0.3945 0.4145 0.0109  0.0367  -0.0101 135 ALA A CB    
972  N N     . ILE A 136 ? 0.4481 0.4272 0.4569 0.0166  0.0395  -0.0104 136 ILE A N     
973  C CA    . ILE A 136 ? 0.4329 0.4105 0.4436 0.0192  0.0406  -0.0103 136 ILE A CA    
974  C C     . ILE A 136 ? 0.4739 0.4516 0.4846 0.0201  0.0402  -0.0103 136 ILE A C     
975  O O     . ILE A 136 ? 0.5359 0.5115 0.5442 0.0191  0.0391  -0.0114 136 ILE A O     
976  C CB    . ILE A 136 ? 0.4373 0.4099 0.4470 0.0193  0.0408  -0.0116 136 ILE A CB    
977  C CG1   . ILE A 136 ? 0.3891 0.3623 0.3999 0.0197  0.0419  -0.0113 136 ILE A CG1   
978  C CG2   . ILE A 136 ? 0.4758 0.4459 0.4860 0.0210  0.0412  -0.0120 136 ILE A CG2   
979  C CD1   . ILE A 136 ? 0.3854 0.3545 0.3945 0.0189  0.0416  -0.0126 136 ILE A CD1   
980  N N     . GLN A 137 ? 0.3226 0.3026 0.3359 0.0220  0.0413  -0.0090 137 GLN A N     
981  C CA    . GLN A 137 ? 0.3058 0.2868 0.3193 0.0229  0.0410  -0.0087 137 GLN A CA    
982  C C     . GLN A 137 ? 0.3231 0.2999 0.3348 0.0229  0.0403  -0.0102 137 GLN A C     
983  O O     . GLN A 137 ? 0.4166 0.3938 0.4270 0.0228  0.0394  -0.0106 137 GLN A O     
984  C CB    . GLN A 137 ? 0.2697 0.2528 0.2861 0.0251  0.0424  -0.0069 137 GLN A CB    
985  C CG    . GLN A 137 ? 0.2346 0.2233 0.2528 0.0255  0.0430  -0.0050 137 GLN A CG    
986  C CD    . GLN A 137 ? 0.2347 0.2236 0.2551 0.0279  0.0448  -0.0035 137 GLN A CD    
987  O OE1   . GLN A 137 ? 0.2510 0.2362 0.2718 0.0290  0.0456  -0.0036 137 GLN A OE1   
988  N NE2   . GLN A 137 ? 0.2348 0.2282 0.2565 0.0286  0.0456  -0.0019 137 GLN A NE2   
989  N N     . ALA A 138 ? 0.3549 0.3279 0.3663 0.0232  0.0407  -0.0110 138 ALA A N     
990  C CA    . ALA A 138 ? 0.2994 0.2695 0.3093 0.0235  0.0402  -0.0120 138 ALA A CA    
991  C C     . ALA A 138 ? 0.3195 0.2871 0.3262 0.0224  0.0390  -0.0134 138 ALA A C     
992  O O     . ALA A 138 ? 0.3742 0.3402 0.3792 0.0231  0.0385  -0.0141 138 ALA A O     
993  C CB    . ALA A 138 ? 0.2366 0.2043 0.2473 0.0240  0.0410  -0.0122 138 ALA A CB    
994  N N     . VAL A 139 ? 0.3135 0.2805 0.3190 0.0209  0.0387  -0.0138 139 VAL A N     
995  C CA    . VAL A 139 ? 0.2429 0.2066 0.2449 0.0196  0.0376  -0.0150 139 VAL A CA    
996  C C     . VAL A 139 ? 0.2448 0.2092 0.2448 0.0191  0.0367  -0.0153 139 VAL A C     
997  O O     . VAL A 139 ? 0.2475 0.2084 0.2442 0.0192  0.0361  -0.0164 139 VAL A O     
998  C CB    . VAL A 139 ? 0.2439 0.2069 0.2452 0.0178  0.0375  -0.0151 139 VAL A CB    
999  C CG1   . VAL A 139 ? 0.2475 0.2066 0.2449 0.0163  0.0365  -0.0161 139 VAL A CG1   
1000 C CG2   . VAL A 139 ? 0.2425 0.2044 0.2453 0.0185  0.0384  -0.0151 139 VAL A CG2   
1001 N N     . LEU A 140 ? 0.2438 0.2126 0.2454 0.0185  0.0368  -0.0143 140 LEU A N     
1002 C CA    . LEU A 140 ? 0.2455 0.2158 0.2453 0.0178  0.0360  -0.0145 140 LEU A CA    
1003 C C     . LEU A 140 ? 0.2724 0.2425 0.2722 0.0199  0.0361  -0.0148 140 LEU A C     
1004 O O     . LEU A 140 ? 0.2477 0.2164 0.2444 0.0197  0.0353  -0.0158 140 LEU A O     
1005 C CB    . LEU A 140 ? 0.2442 0.2205 0.2462 0.0168  0.0362  -0.0130 140 LEU A CB    
1006 C CG    . LEU A 140 ? 0.2447 0.2230 0.2469 0.0146  0.0360  -0.0124 140 LEU A CG    
1007 C CD1   . LEU A 140 ? 0.2420 0.2272 0.2479 0.0153  0.0369  -0.0103 140 LEU A CD1   
1008 C CD2   . LEU A 140 ? 0.2488 0.2258 0.2469 0.0114  0.0347  -0.0134 140 LEU A CD2   
1009 N N     . SER A 141 ? 0.3664 0.3382 0.3694 0.0218  0.0370  -0.0138 141 SER A N     
1010 C CA    . SER A 141 ? 0.3404 0.3126 0.3434 0.0237  0.0370  -0.0138 141 SER A CA    
1011 C C     . SER A 141 ? 0.4505 0.4181 0.4500 0.0243  0.0365  -0.0153 141 SER A C     
1012 O O     . SER A 141 ? 0.5098 0.4771 0.5071 0.0252  0.0360  -0.0159 141 SER A O     
1013 C CB    . SER A 141 ? 0.2715 0.2455 0.2780 0.0251  0.0380  -0.0125 141 SER A CB    
1014 O OG    . SER A 141 ? 0.3348 0.3132 0.3441 0.0254  0.0385  -0.0109 141 SER A OG    
1015 N N     . LEU A 142 ? 0.3714 0.3356 0.3702 0.0241  0.0366  -0.0158 142 LEU A N     
1016 C CA    . LEU A 142 ? 0.3547 0.3147 0.3501 0.0248  0.0362  -0.0170 142 LEU A CA    
1017 C C     . LEU A 142 ? 0.3846 0.3413 0.3756 0.0240  0.0354  -0.0183 142 LEU A C     
1018 O O     . LEU A 142 ? 0.3296 0.2834 0.3173 0.0254  0.0352  -0.0192 142 LEU A O     
1019 C CB    . LEU A 142 ? 0.3282 0.2857 0.3238 0.0243  0.0365  -0.0171 142 LEU A CB    
1020 C CG    . LEU A 142 ? 0.3698 0.3245 0.3633 0.0259  0.0365  -0.0176 142 LEU A CG    
1021 C CD1   . LEU A 142 ? 0.3371 0.2950 0.3335 0.0272  0.0371  -0.0167 142 LEU A CD1   
1022 C CD2   . LEU A 142 ? 0.2746 0.2255 0.2662 0.0250  0.0364  -0.0181 142 LEU A CD2   
1023 N N     . TYR A 143 ? 0.3519 0.3090 0.3424 0.0215  0.0350  -0.0183 143 TYR A N     
1024 C CA    . TYR A 143 ? 0.3166 0.2704 0.3026 0.0198  0.0342  -0.0195 143 TYR A CA    
1025 C C     . TYR A 143 ? 0.3117 0.2670 0.2961 0.0204  0.0338  -0.0200 143 TYR A C     
1026 O O     . TYR A 143 ? 0.3441 0.2950 0.3236 0.0201  0.0333  -0.0215 143 TYR A O     
1027 C CB    . TYR A 143 ? 0.3627 0.3183 0.3494 0.0167  0.0339  -0.0191 143 TYR A CB    
1028 C CG    . TYR A 143 ? 0.3983 0.3508 0.3843 0.0152  0.0338  -0.0191 143 TYR A CG    
1029 C CD1   . TYR A 143 ? 0.3914 0.3388 0.3754 0.0164  0.0339  -0.0198 143 TYR A CD1   
1030 C CD2   . TYR A 143 ? 0.3859 0.3412 0.3733 0.0127  0.0337  -0.0183 143 TYR A CD2   
1031 C CE1   . TYR A 143 ? 0.4388 0.3836 0.4220 0.0151  0.0339  -0.0197 143 TYR A CE1   
1032 C CE2   . TYR A 143 ? 0.3026 0.2556 0.2893 0.0113  0.0336  -0.0183 143 TYR A CE2   
1033 C CZ    . TYR A 143 ? 0.4129 0.3604 0.3975 0.0124  0.0337  -0.0190 143 TYR A CZ    
1034 O OH    . TYR A 143 ? 0.3890 0.3345 0.3730 0.0110  0.0337  -0.0189 143 TYR A OH    
1035 N N     . ALA A 144 ? 0.3871 0.3484 0.3753 0.0212  0.0342  -0.0188 144 ALA A N     
1036 C CA    . ALA A 144 ? 0.4153 0.3790 0.4025 0.0220  0.0339  -0.0191 144 ALA A CA    
1037 C C     . ALA A 144 ? 0.3970 0.3580 0.3819 0.0249  0.0341  -0.0199 144 ALA A C     
1038 O O     . ALA A 144 ? 0.4488 0.4092 0.4306 0.0255  0.0338  -0.0208 144 ALA A O     
1039 C CB    . ALA A 144 ? 0.3756 0.3465 0.3678 0.0225  0.0344  -0.0172 144 ALA A CB    
1040 N N     . SER A 145 ? 0.4473 0.4067 0.4333 0.0265  0.0346  -0.0195 145 SER A N     
1041 C CA    . SER A 145 ? 0.4410 0.3986 0.4250 0.0294  0.0348  -0.0200 145 SER A CA    
1042 C C     . SER A 145 ? 0.5125 0.4630 0.4913 0.0296  0.0347  -0.0215 145 SER A C     
1043 O O     . SER A 145 ? 0.6032 0.5517 0.5798 0.0323  0.0350  -0.0218 145 SER A O     
1044 C CB    . SER A 145 ? 0.4212 0.3815 0.4091 0.0308  0.0355  -0.0186 145 SER A CB    
1045 O OG    . SER A 145 ? 0.4657 0.4227 0.4534 0.0303  0.0356  -0.0187 145 SER A OG    
1046 N N     . GLY A 146 ? 0.6053 0.5522 0.5821 0.0269  0.0342  -0.0222 146 GLY A N     
1047 C CA    . GLY A 146 ? 0.6450 0.5844 0.6164 0.0269  0.0340  -0.0235 146 GLY A CA    
1048 C C     . GLY A 146 ? 0.6508 0.5877 0.6225 0.0283  0.0345  -0.0230 146 GLY A C     
1049 O O     . GLY A 146 ? 0.7321 0.6631 0.6992 0.0297  0.0346  -0.0238 146 GLY A O     
1050 N N     . ARG A 147 ? 0.4399 0.3810 0.4167 0.0280  0.0348  -0.0217 147 ARG A N     
1051 C CA    . ARG A 147 ? 0.4421 0.3816 0.4194 0.0287  0.0352  -0.0212 147 ARG A CA    
1052 C C     . ARG A 147 ? 0.4899 0.4290 0.4689 0.0258  0.0350  -0.0209 147 ARG A C     
1053 O O     . ARG A 147 ? 0.5330 0.4756 0.5147 0.0238  0.0349  -0.0205 147 ARG A O     
1054 C CB    . ARG A 147 ? 0.4719 0.4165 0.4533 0.0306  0.0357  -0.0199 147 ARG A CB    
1055 C CG    . ARG A 147 ? 0.4274 0.3734 0.4076 0.0338  0.0360  -0.0198 147 ARG A CG    
1056 C CD    . ARG A 147 ? 0.4293 0.3820 0.4142 0.0340  0.0362  -0.0186 147 ARG A CD    
1057 N NE    . ARG A 147 ? 0.4432 0.3988 0.4281 0.0369  0.0366  -0.0179 147 ARG A NE    
1058 C CZ    . ARG A 147 ? 0.4925 0.4489 0.4754 0.0391  0.0366  -0.0182 147 ARG A CZ    
1059 N NH1   . ARG A 147 ? 0.5413 0.4954 0.5215 0.0386  0.0362  -0.0193 147 ARG A NH1   
1060 N NH2   . ARG A 147 ? 0.5942 0.5541 0.5773 0.0417  0.0369  -0.0172 147 ARG A NH2   
1061 N N     . THR A 148 ? 0.5701 0.5061 0.5479 0.0259  0.0351  -0.0208 148 THR A N     
1062 C CA    . THR A 148 ? 0.4861 0.4226 0.4659 0.0235  0.0351  -0.0203 148 THR A CA    
1063 C C     . THR A 148 ? 0.5288 0.4686 0.5123 0.0246  0.0357  -0.0194 148 THR A C     
1064 O O     . THR A 148 ? 0.4947 0.4369 0.4811 0.0230  0.0360  -0.0190 148 THR A O     
1065 C CB    . THR A 148 ? 0.5170 0.4474 0.4926 0.0220  0.0347  -0.0209 148 THR A CB    
1066 O OG1   . THR A 148 ? 0.6216 0.5480 0.5940 0.0246  0.0350  -0.0210 148 THR A OG1   
1067 C CG2   . THR A 148 ? 0.5421 0.4695 0.5141 0.0199  0.0340  -0.0218 148 THR A CG2   
1068 N N     . THR A 149 ? 0.5584 0.4989 0.5417 0.0273  0.0361  -0.0191 149 THR A N     
1069 C CA    . THR A 149 ? 0.4950 0.4388 0.4813 0.0278  0.0366  -0.0183 149 THR A CA    
1070 C C     . THR A 149 ? 0.4572 0.4056 0.4460 0.0293  0.0369  -0.0177 149 THR A C     
1071 O O     . THR A 149 ? 0.5033 0.4520 0.4905 0.0313  0.0368  -0.0177 149 THR A O     
1072 C CB    . THR A 149 ? 0.4886 0.4296 0.4723 0.0292  0.0367  -0.0181 149 THR A CB    
1073 O OG1   . THR A 149 ? 0.3571 0.2938 0.3386 0.0275  0.0364  -0.0185 149 THR A OG1   
1074 C CG2   . THR A 149 ? 0.3591 0.3043 0.3456 0.0297  0.0372  -0.0172 149 THR A CG2   
1075 N N     . GLY A 150 ? 0.2934 0.2453 0.2860 0.0282  0.0373  -0.0171 150 GLY A N     
1076 C CA    . GLY A 150 ? 0.2730 0.2291 0.2680 0.0291  0.0376  -0.0163 150 GLY A CA    
1077 C C     . GLY A 150 ? 0.2861 0.2443 0.2845 0.0273  0.0381  -0.0159 150 GLY A C     
1078 O O     . GLY A 150 ? 0.3048 0.2616 0.3038 0.0259  0.0382  -0.0163 150 GLY A O     
1079 N N     . ILE A 151 ? 0.2411 0.2025 0.2416 0.0276  0.0384  -0.0151 151 ILE A N     
1080 C CA    . ILE A 151 ? 0.2392 0.2017 0.2424 0.0262  0.0391  -0.0147 151 ILE A CA    
1081 C C     . ILE A 151 ? 0.2522 0.2167 0.2570 0.0266  0.0392  -0.0140 151 ILE A C     
1082 O O     . ILE A 151 ? 0.2780 0.2449 0.2830 0.0276  0.0390  -0.0134 151 ILE A O     
1083 C CB    . ILE A 151 ? 0.2385 0.2025 0.2427 0.0255  0.0394  -0.0143 151 ILE A CB    
1084 C CG1   . ILE A 151 ? 0.2377 0.2017 0.2440 0.0241  0.0402  -0.0139 151 ILE A CG1   
1085 C CG2   . ILE A 151 ? 0.2384 0.2057 0.2421 0.0268  0.0391  -0.0135 151 ILE A CG2   
1086 C CD1   . ILE A 151 ? 0.2381 0.2018 0.2446 0.0226  0.0407  -0.0140 151 ILE A CD1   
1087 N N     . VAL A 152 ? 0.3738 0.3378 0.3800 0.0258  0.0396  -0.0140 152 VAL A N     
1088 C CA    . VAL A 152 ? 0.3485 0.3146 0.3562 0.0262  0.0397  -0.0131 152 VAL A CA    
1089 C C     . VAL A 152 ? 0.3631 0.3303 0.3732 0.0259  0.0406  -0.0121 152 VAL A C     
1090 O O     . VAL A 152 ? 0.4123 0.3776 0.4228 0.0250  0.0413  -0.0122 152 VAL A O     
1091 C CB    . VAL A 152 ? 0.2954 0.2613 0.3031 0.0257  0.0397  -0.0133 152 VAL A CB    
1092 C CG1   . VAL A 152 ? 0.3231 0.2920 0.3326 0.0262  0.0399  -0.0122 152 VAL A CG1   
1093 C CG2   . VAL A 152 ? 0.2925 0.2569 0.2973 0.0257  0.0387  -0.0144 152 VAL A CG2   
1094 N N     . MET A 153 ? 0.4523 0.4220 0.4634 0.0266  0.0406  -0.0110 153 MET A N     
1095 C CA    . MET A 153 ? 0.4087 0.3789 0.4218 0.0263  0.0415  -0.0098 153 MET A CA    
1096 C C     . MET A 153 ? 0.4080 0.3800 0.4225 0.0271  0.0418  -0.0088 153 MET A C     
1097 O O     . MET A 153 ? 0.4082 0.3832 0.4229 0.0279  0.0412  -0.0082 153 MET A O     
1098 C CB    . MET A 153 ? 0.4050 0.3772 0.4182 0.0263  0.0413  -0.0090 153 MET A CB    
1099 C CG    . MET A 153 ? 0.5185 0.4917 0.5334 0.0260  0.0419  -0.0074 153 MET A CG    
1100 S SD    . MET A 153 ? 0.6511 0.6198 0.6662 0.0246  0.0432  -0.0075 153 MET A SD    
1101 C CE    . MET A 153 ? 0.7484 0.7156 0.7616 0.0231  0.0428  -0.0090 153 MET A CE    
1102 N N     . ASP A 154 ? 0.4245 0.3955 0.4400 0.0270  0.0426  -0.0085 154 ASP A N     
1103 C CA    . ASP A 154 ? 0.4544 0.4279 0.4715 0.0279  0.0430  -0.0072 154 ASP A CA    
1104 C C     . ASP A 154 ? 0.4422 0.4149 0.4609 0.0284  0.0444  -0.0056 154 ASP A C     
1105 O O     . ASP A 154 ? 0.3444 0.3139 0.3629 0.0282  0.0454  -0.0058 154 ASP A O     
1106 C CB    . ASP A 154 ? 0.5514 0.5250 0.5681 0.0277  0.0430  -0.0077 154 ASP A CB    
1107 C CG    . ASP A 154 ? 0.6204 0.5977 0.6387 0.0285  0.0433  -0.0062 154 ASP A CG    
1108 O OD1   . ASP A 154 ? 0.6833 0.6606 0.7030 0.0294  0.0446  -0.0049 154 ASP A OD1   
1109 O OD2   . ASP A 154 ? 0.5478 0.5280 0.5655 0.0283  0.0424  -0.0063 154 ASP A OD2   
1110 N N     . SER A 155 ? 0.4835 0.4589 0.5034 0.0292  0.0444  -0.0040 155 SER A N     
1111 C CA    . SER A 155 ? 0.5134 0.4878 0.5347 0.0298  0.0458  -0.0022 155 SER A CA    
1112 C C     . SER A 155 ? 0.5409 0.5190 0.5638 0.0313  0.0462  -0.0004 155 SER A C     
1113 O O     . SER A 155 ? 0.6163 0.5986 0.6398 0.0317  0.0453  0.0001  155 SER A O     
1114 C CB    . SER A 155 ? 0.5095 0.4839 0.5308 0.0292  0.0456  -0.0014 155 SER A CB    
1115 O OG    . SER A 155 ? 0.5324 0.5041 0.5542 0.0294  0.0470  0.0002  155 SER A OG    
1116 N N     . GLY A 156 ? 0.2816 0.2585 0.3052 0.0324  0.0475  0.0005  156 GLY A N     
1117 C CA    . GLY A 156 ? 0.2373 0.2184 0.2627 0.0340  0.0481  0.0026  156 GLY A CA    
1118 C C     . GLY A 156 ? 0.2574 0.2371 0.2838 0.0356  0.0497  0.0049  156 GLY A C     
1119 O O     . GLY A 156 ? 0.2438 0.2215 0.2701 0.0352  0.0498  0.0055  156 GLY A O     
1120 N N     . ASP A 157 ? 0.5630 0.5439 0.5904 0.0375  0.0510  0.0065  157 ASP A N     
1121 C CA    . ASP A 157 ? 0.5807 0.5600 0.6089 0.0396  0.0528  0.0090  157 ASP A CA    
1122 C C     . ASP A 157 ? 0.6476 0.6194 0.6741 0.0400  0.0545  0.0085  157 ASP A C     
1123 O O     . ASP A 157 ? 0.6028 0.5700 0.6285 0.0400  0.0553  0.0093  157 ASP A O     
1124 C CB    . ASP A 157 ? 0.4920 0.4772 0.5221 0.0419  0.0535  0.0113  157 ASP A CB    
1125 C CG    . ASP A 157 ? 0.6641 0.6500 0.6954 0.0441  0.0548  0.0145  157 ASP A CG    
1126 O OD1   . ASP A 157 ? 0.7609 0.7426 0.7916 0.0435  0.0551  0.0148  157 ASP A OD1   
1127 O OD2   . ASP A 157 ? 0.7525 0.7436 0.7854 0.0463  0.0556  0.0168  157 ASP A OD2   
1128 N N     . GLY A 158 ? 0.7420 0.7124 0.7677 0.0403  0.0549  0.0072  158 GLY A N     
1129 C CA    . GLY A 158 ? 0.6819 0.6450 0.7055 0.0408  0.0566  0.0064  158 GLY A CA    
1130 C C     . GLY A 158 ? 0.7311 0.6904 0.7528 0.0382  0.0557  0.0034  158 GLY A C     
1131 O O     . GLY A 158 ? 0.8722 0.8251 0.8918 0.0379  0.0569  0.0024  158 GLY A O     
1132 N N     . VAL A 159 ? 0.4371 0.4002 0.4592 0.0363  0.0538  0.0019  159 VAL A N     
1133 C CA    . VAL A 159 ? 0.3789 0.3390 0.3993 0.0342  0.0530  -0.0007 159 VAL A CA    
1134 C C     . VAL A 159 ? 0.4432 0.4052 0.4633 0.0320  0.0510  -0.0020 159 VAL A C     
1135 O O     . VAL A 159 ? 0.4421 0.4089 0.4633 0.0321  0.0498  -0.0015 159 VAL A O     
1136 C CB    . VAL A 159 ? 0.3853 0.3464 0.4054 0.0348  0.0533  -0.0016 159 VAL A CB    
1137 C CG1   . VAL A 159 ? 0.3956 0.3631 0.4170 0.0345  0.0518  -0.0015 159 VAL A CG1   
1138 C CG2   . VAL A 159 ? 0.3776 0.3341 0.3956 0.0332  0.0533  -0.0039 159 VAL A CG2   
1139 N N     . THR A 160 ? 0.4645 0.4228 0.4829 0.0301  0.0507  -0.0036 160 THR A N     
1140 C CA    . THR A 160 ? 0.4542 0.4143 0.4722 0.0284  0.0489  -0.0048 160 THR A CA    
1141 C C     . THR A 160 ? 0.4811 0.4396 0.4977 0.0273  0.0485  -0.0069 160 THR A C     
1142 O O     . THR A 160 ? 0.4390 0.3939 0.4545 0.0271  0.0496  -0.0076 160 THR A O     
1143 C CB    . THR A 160 ? 0.4355 0.3938 0.4528 0.0269  0.0488  -0.0045 160 THR A CB    
1144 O OG1   . THR A 160 ? 0.4811 0.4431 0.4999 0.0276  0.0483  -0.0028 160 THR A OG1   
1145 C CG2   . THR A 160 ? 0.4093 0.3679 0.4254 0.0250  0.0475  -0.0062 160 THR A CG2   
1146 N N     . HIS A 161 ? 0.4498 0.4111 0.4663 0.0268  0.0470  -0.0078 161 HIS A N     
1147 C CA    . HIS A 161 ? 0.4660 0.4261 0.4811 0.0258  0.0465  -0.0095 161 HIS A CA    
1148 C C     . HIS A 161 ? 0.4933 0.4544 0.5073 0.0247  0.0451  -0.0105 161 HIS A C     
1149 O O     . HIS A 161 ? 0.4705 0.4344 0.4848 0.0252  0.0441  -0.0101 161 HIS A O     
1150 C CB    . HIS A 161 ? 0.4747 0.4368 0.4902 0.0264  0.0464  -0.0096 161 HIS A CB    
1151 C CG    . HIS A 161 ? 0.5513 0.5119 0.5670 0.0273  0.0479  -0.0093 161 HIS A CG    
1152 N ND1   . HIS A 161 ? 0.4654 0.4284 0.4826 0.0290  0.0488  -0.0077 161 HIS A ND1   
1153 C CD2   . HIS A 161 ? 0.5426 0.5002 0.5572 0.0269  0.0487  -0.0103 161 HIS A CD2   
1154 C CE1   . HIS A 161 ? 0.5114 0.4727 0.5283 0.0299  0.0502  -0.0077 161 HIS A CE1   
1155 N NE2   . HIS A 161 ? 0.5078 0.4656 0.5231 0.0286  0.0502  -0.0094 161 HIS A NE2   
1156 N N     . THR A 162 ? 0.4769 0.4360 0.4896 0.0235  0.0450  -0.0116 162 THR A N     
1157 C CA    . THR A 162 ? 0.4407 0.4010 0.4522 0.0229  0.0438  -0.0124 162 THR A CA    
1158 C C     . THR A 162 ? 0.3852 0.3446 0.3957 0.0227  0.0434  -0.0135 162 THR A C     
1159 O O     . THR A 162 ? 0.4743 0.4317 0.4842 0.0219  0.0440  -0.0142 162 THR A O     
1160 C CB    . THR A 162 ? 0.5016 0.4613 0.5124 0.0215  0.0438  -0.0125 162 THR A CB    
1161 O OG1   . THR A 162 ? 0.4266 0.3857 0.4382 0.0213  0.0445  -0.0114 162 THR A OG1   
1162 C CG2   . THR A 162 ? 0.4970 0.4594 0.5071 0.0217  0.0426  -0.0124 162 THR A CG2   
1163 N N     . VAL A 163 ? 0.3005 0.2613 0.3105 0.0233  0.0425  -0.0136 163 VAL A N     
1164 C CA    . VAL A 163 ? 0.3077 0.2675 0.3166 0.0228  0.0421  -0.0144 163 VAL A CA    
1165 C C     . VAL A 163 ? 0.3605 0.3200 0.3675 0.0229  0.0410  -0.0151 163 VAL A C     
1166 O O     . VAL A 163 ? 0.3865 0.3467 0.3927 0.0235  0.0403  -0.0150 163 VAL A O     
1167 C CB    . VAL A 163 ? 0.3356 0.2967 0.3453 0.0232  0.0422  -0.0140 163 VAL A CB    
1168 C CG1   . VAL A 163 ? 0.3323 0.2926 0.3407 0.0223  0.0418  -0.0146 163 VAL A CG1   
1169 C CG2   . VAL A 163 ? 0.3846 0.3462 0.3961 0.0238  0.0435  -0.0130 163 VAL A CG2   
1170 N N     . PRO A 164 ? 0.3780 0.3362 0.3839 0.0222  0.0410  -0.0157 164 PRO A N     
1171 C CA    . PRO A 164 ? 0.3427 0.3002 0.3465 0.0225  0.0402  -0.0161 164 PRO A CA    
1172 C C     . PRO A 164 ? 0.4101 0.3659 0.4125 0.0221  0.0397  -0.0166 164 PRO A C     
1173 O O     . PRO A 164 ? 0.4309 0.3862 0.4338 0.0211  0.0401  -0.0167 164 PRO A O     
1174 C CB    . PRO A 164 ? 0.3247 0.2820 0.3282 0.0217  0.0404  -0.0164 164 PRO A CB    
1175 C CG    . PRO A 164 ? 0.3032 0.2608 0.3082 0.0209  0.0413  -0.0163 164 PRO A CG    
1176 C CD    . PRO A 164 ? 0.3208 0.2781 0.3272 0.0212  0.0418  -0.0160 164 PRO A CD    
1177 N N     . ILE A 165 ? 0.4233 0.3781 0.4237 0.0228  0.0389  -0.0167 165 ILE A N     
1178 C CA    . ILE A 165 ? 0.4036 0.3563 0.4021 0.0220  0.0383  -0.0171 165 ILE A CA    
1179 C C     . ILE A 165 ? 0.4551 0.4049 0.4504 0.0226  0.0378  -0.0175 165 ILE A C     
1180 O O     . ILE A 165 ? 0.3897 0.3390 0.3835 0.0242  0.0375  -0.0175 165 ILE A O     
1181 C CB    . ILE A 165 ? 0.3491 0.3025 0.3474 0.0219  0.0380  -0.0170 165 ILE A CB    
1182 C CG1   . ILE A 165 ? 0.3463 0.3027 0.3476 0.0215  0.0386  -0.0163 165 ILE A CG1   
1183 C CG2   . ILE A 165 ? 0.2493 0.2001 0.2448 0.0206  0.0372  -0.0175 165 ILE A CG2   
1184 C CD1   . ILE A 165 ? 0.3565 0.3153 0.3592 0.0225  0.0387  -0.0158 165 ILE A CD1   
1185 N N     . TYR A 166 ? 0.5622 0.5101 0.5564 0.0215  0.0377  -0.0176 166 TYR A N     
1186 C CA    . TYR A 166 ? 0.5563 0.5010 0.5473 0.0221  0.0373  -0.0178 166 TYR A CA    
1187 C C     . TYR A 166 ? 0.5934 0.5347 0.5818 0.0207  0.0367  -0.0181 166 TYR A C     
1188 O O     . TYR A 166 ? 0.6003 0.5420 0.5894 0.0187  0.0366  -0.0180 166 TYR A O     
1189 C CB    . TYR A 166 ? 0.4475 0.3926 0.4389 0.0217  0.0376  -0.0175 166 TYR A CB    
1190 C CG    . TYR A 166 ? 0.5984 0.5404 0.5866 0.0226  0.0373  -0.0173 166 TYR A CG    
1191 C CD1   . TYR A 166 ? 0.6907 0.6319 0.6770 0.0250  0.0372  -0.0170 166 TYR A CD1   
1192 C CD2   . TYR A 166 ? 0.6198 0.5596 0.6067 0.0212  0.0371  -0.0172 166 TYR A CD2   
1193 C CE1   . TYR A 166 ? 0.7076 0.6458 0.6907 0.0263  0.0371  -0.0166 166 TYR A CE1   
1194 C CE2   . TYR A 166 ? 0.6537 0.5903 0.6374 0.0222  0.0369  -0.0168 166 TYR A CE2   
1195 C CZ    . TYR A 166 ? 0.6958 0.6313 0.6775 0.0248  0.0369  -0.0165 166 TYR A CZ    
1196 O OH    . TYR A 166 ? 0.7800 0.7121 0.7584 0.0263  0.0369  -0.0159 166 TYR A OH    
1197 N N     . GLU A 167 ? 0.4730 0.4109 0.4580 0.0216  0.0362  -0.0185 167 GLU A N     
1198 C CA    . GLU A 167 ? 0.4678 0.4016 0.4495 0.0199  0.0355  -0.0189 167 GLU A CA    
1199 C C     . GLU A 167 ? 0.5273 0.4632 0.5104 0.0173  0.0352  -0.0189 167 GLU A C     
1200 O O     . GLU A 167 ? 0.5121 0.4460 0.4934 0.0150  0.0348  -0.0189 167 GLU A O     
1201 C CB    . GLU A 167 ? 0.5572 0.4870 0.5362 0.0195  0.0354  -0.0187 167 GLU A CB    
1202 C CG    . GLU A 167 ? 0.6922 0.6192 0.6685 0.0224  0.0356  -0.0186 167 GLU A CG    
1203 C CD    . GLU A 167 ? 0.6363 0.5590 0.6096 0.0221  0.0355  -0.0181 167 GLU A CD    
1204 O OE1   . GLU A 167 ? 0.5857 0.5069 0.5584 0.0193  0.0351  -0.0181 167 GLU A OE1   
1205 O OE2   . GLU A 167 ? 0.6163 0.5373 0.5878 0.0247  0.0359  -0.0176 167 GLU A OE2   
1206 N N     . GLY A 168 ? 0.5209 0.4610 0.5070 0.0176  0.0355  -0.0188 168 GLY A N     
1207 C CA    . GLY A 168 ? 0.5167 0.4600 0.5046 0.0155  0.0354  -0.0184 168 GLY A CA    
1208 C C     . GLY A 168 ? 0.4286 0.3761 0.4205 0.0153  0.0362  -0.0177 168 GLY A C     
1209 O O     . GLY A 168 ? 0.4577 0.4090 0.4518 0.0145  0.0364  -0.0171 168 GLY A O     
1210 N N     . TYR A 169 ? 0.4119 0.3588 0.4045 0.0161  0.0367  -0.0176 169 TYR A N     
1211 C CA    . TYR A 169 ? 0.4170 0.3671 0.4127 0.0158  0.0375  -0.0172 169 TYR A CA    
1212 C C     . TYR A 169 ? 0.4294 0.3816 0.4278 0.0174  0.0384  -0.0171 169 TYR A C     
1213 O O     . TYR A 169 ? 0.4556 0.4068 0.4538 0.0184  0.0385  -0.0173 169 TYR A O     
1214 C CB    . TYR A 169 ? 0.4810 0.4296 0.4757 0.0148  0.0375  -0.0172 169 TYR A CB    
1215 C CG    . TYR A 169 ? 0.5724 0.5241 0.5696 0.0142  0.0383  -0.0169 169 TYR A CG    
1216 C CD1   . TYR A 169 ? 0.5906 0.5453 0.5890 0.0131  0.0384  -0.0162 169 TYR A CD1   
1217 C CD2   . TYR A 169 ? 0.5939 0.5457 0.5920 0.0148  0.0390  -0.0171 169 TYR A CD2   
1218 C CE1   . TYR A 169 ? 0.5464 0.5039 0.5468 0.0131  0.0393  -0.0158 169 TYR A CE1   
1219 C CE2   . TYR A 169 ? 0.5832 0.5373 0.5830 0.0144  0.0398  -0.0169 169 TYR A CE2   
1220 C CZ    . TYR A 169 ? 0.5161 0.4730 0.5170 0.0138  0.0401  -0.0163 169 TYR A CZ    
1221 O OH    . TYR A 169 ? 0.5225 0.4819 0.5251 0.0139  0.0411  -0.0161 169 TYR A OH    
1222 N N     . ALA A 170 ? 0.2657 0.2209 0.2666 0.0176  0.0390  -0.0165 170 ALA A N     
1223 C CA    . ALA A 170 ? 0.2905 0.2469 0.2936 0.0188  0.0400  -0.0164 170 ALA A CA    
1224 C C     . ALA A 170 ? 0.3399 0.2956 0.3433 0.0185  0.0406  -0.0167 170 ALA A C     
1225 O O     . ALA A 170 ? 0.3855 0.3418 0.3891 0.0177  0.0409  -0.0166 170 ALA A O     
1226 C CB    . ALA A 170 ? 0.2405 0.1998 0.2459 0.0193  0.0407  -0.0155 170 ALA A CB    
1227 N N     . LEU A 171 ? 0.4508 0.4057 0.4542 0.0191  0.0408  -0.0171 171 LEU A N     
1228 C CA    . LEU A 171 ? 0.4525 0.4068 0.4557 0.0185  0.0414  -0.0175 171 LEU A CA    
1229 C C     . LEU A 171 ? 0.4515 0.4063 0.4563 0.0186  0.0426  -0.0176 171 LEU A C     
1230 O O     . LEU A 171 ? 0.5351 0.4897 0.5405 0.0190  0.0431  -0.0176 171 LEU A O     
1231 C CB    . LEU A 171 ? 0.4163 0.3700 0.4184 0.0188  0.0410  -0.0178 171 LEU A CB    
1232 C CG    . LEU A 171 ? 0.4400 0.3925 0.4399 0.0191  0.0399  -0.0177 171 LEU A CG    
1233 C CD1   . LEU A 171 ? 0.3816 0.3345 0.3807 0.0199  0.0397  -0.0176 171 LEU A CD1   
1234 C CD2   . LEU A 171 ? 0.3944 0.3456 0.3930 0.0181  0.0396  -0.0178 171 LEU A CD2   
1235 N N     . PRO A 172 ? 0.4873 0.4426 0.4924 0.0183  0.0433  -0.0176 172 PRO A N     
1236 C CA    . PRO A 172 ? 0.4872 0.4425 0.4934 0.0188  0.0447  -0.0177 172 PRO A CA    
1237 C C     . PRO A 172 ? 0.5110 0.4644 0.5166 0.0184  0.0455  -0.0185 172 PRO A C     
1238 O O     . PRO A 172 ? 0.5016 0.4538 0.5075 0.0190  0.0467  -0.0186 172 PRO A O     
1239 C CB    . PRO A 172 ? 0.4632 0.4199 0.4694 0.0185  0.0450  -0.0176 172 PRO A CB    
1240 C CG    . PRO A 172 ? 0.4668 0.4244 0.4722 0.0175  0.0436  -0.0172 172 PRO A CG    
1241 C CD    . PRO A 172 ? 0.4652 0.4209 0.4694 0.0173  0.0427  -0.0177 172 PRO A CD    
1242 N N     . HIS A 173 ? 0.5306 0.4836 0.5349 0.0174  0.0448  -0.0191 173 HIS A N     
1243 C CA    . HIS A 173 ? 0.4783 0.4302 0.4817 0.0165  0.0453  -0.0200 173 HIS A CA    
1244 C C     . HIS A 173 ? 0.3791 0.3308 0.3826 0.0164  0.0451  -0.0198 173 HIS A C     
1245 O O     . HIS A 173 ? 0.4492 0.4000 0.4519 0.0152  0.0455  -0.0203 173 HIS A O     
1246 C CB    . HIS A 173 ? 0.4791 0.4318 0.4813 0.0154  0.0447  -0.0204 173 HIS A CB    
1247 C CG    . HIS A 173 ? 0.4737 0.4273 0.4754 0.0156  0.0433  -0.0198 173 HIS A CG    
1248 N ND1   . HIS A 173 ? 0.5830 0.5372 0.5844 0.0159  0.0427  -0.0194 173 HIS A ND1   
1249 C CD2   . HIS A 173 ? 0.4939 0.4476 0.4951 0.0157  0.0426  -0.0194 173 HIS A CD2   
1250 C CE1   . HIS A 173 ? 0.5819 0.5362 0.5824 0.0165  0.0417  -0.0189 173 HIS A CE1   
1251 N NE2   . HIS A 173 ? 0.6159 0.5696 0.6162 0.0162  0.0416  -0.0189 173 HIS A NE2   
1252 N N     . ALA A 174 ? 0.3626 0.3152 0.3670 0.0173  0.0444  -0.0189 174 ALA A N     
1253 C CA    . ALA A 174 ? 0.4617 0.4148 0.4664 0.0173  0.0441  -0.0184 174 ALA A CA    
1254 C C     . ALA A 174 ? 0.4807 0.4337 0.4867 0.0184  0.0446  -0.0176 174 ALA A C     
1255 O O     . ALA A 174 ? 0.5236 0.4771 0.5300 0.0183  0.0445  -0.0171 174 ALA A O     
1256 C CB    . ALA A 174 ? 0.4096 0.3644 0.4136 0.0177  0.0429  -0.0181 174 ALA A CB    
1257 N N     . ILE A 175 ? 0.3956 0.3485 0.4025 0.0194  0.0450  -0.0173 175 ILE A N     
1258 C CA    . ILE A 175 ? 0.4477 0.4011 0.4560 0.0206  0.0455  -0.0163 175 ILE A CA    
1259 C C     . ILE A 175 ? 0.4308 0.3820 0.4392 0.0205  0.0468  -0.0161 175 ILE A C     
1260 O O     . ILE A 175 ? 0.4210 0.3699 0.4286 0.0203  0.0479  -0.0168 175 ILE A O     
1261 C CB    . ILE A 175 ? 0.4212 0.3762 0.4304 0.0216  0.0456  -0.0157 175 ILE A CB    
1262 C CG1   . ILE A 175 ? 0.3808 0.3374 0.3895 0.0212  0.0442  -0.0158 175 ILE A CG1   
1263 C CG2   . ILE A 175 ? 0.4468 0.4029 0.4576 0.0229  0.0462  -0.0144 175 ILE A CG2   
1264 C CD1   . ILE A 175 ? 0.3765 0.3348 0.3856 0.0213  0.0442  -0.0154 175 ILE A CD1   
1265 N N     . LEU A 176 ? 0.3661 0.3176 0.3751 0.0207  0.0467  -0.0153 176 LEU A N     
1266 C CA    . LEU A 176 ? 0.3827 0.3315 0.3914 0.0203  0.0478  -0.0150 176 LEU A CA    
1267 C C     . LEU A 176 ? 0.3963 0.3452 0.4064 0.0220  0.0485  -0.0135 176 LEU A C     
1268 O O     . LEU A 176 ? 0.3928 0.3450 0.4043 0.0229  0.0477  -0.0126 176 LEU A O     
1269 C CB    . LEU A 176 ? 0.4216 0.3707 0.4294 0.0186  0.0471  -0.0151 176 LEU A CB    
1270 C CG    . LEU A 176 ? 0.4091 0.3578 0.4152 0.0165  0.0467  -0.0164 176 LEU A CG    
1271 C CD1   . LEU A 176 ? 0.3153 0.2633 0.3203 0.0144  0.0467  -0.0162 176 LEU A CD1   
1272 C CD2   . LEU A 176 ? 0.4129 0.3589 0.4178 0.0162  0.0476  -0.0177 176 LEU A CD2   
1273 N N     . ARG A 177 ? 0.3717 0.3171 0.3812 0.0226  0.0502  -0.0133 177 ARG A N     
1274 C CA    . ARG A 177 ? 0.3646 0.3100 0.3755 0.0246  0.0512  -0.0116 177 ARG A CA    
1275 C C     . ARG A 177 ? 0.3902 0.3318 0.4002 0.0241  0.0522  -0.0109 177 ARG A C     
1276 O O     . ARG A 177 ? 0.4339 0.3707 0.4417 0.0230  0.0531  -0.0119 177 ARG A O     
1277 C CB    . ARG A 177 ? 0.3949 0.3400 0.4061 0.0267  0.0525  -0.0113 177 ARG A CB    
1278 C CG    . ARG A 177 ? 0.4277 0.3725 0.4399 0.0291  0.0539  -0.0093 177 ARG A CG    
1279 C CD    . ARG A 177 ? 0.4773 0.4237 0.4901 0.0314  0.0551  -0.0087 177 ARG A CD    
1280 N NE    . ARG A 177 ? 0.5255 0.4699 0.5384 0.0340  0.0570  -0.0070 177 ARG A NE    
1281 C CZ    . ARG A 177 ? 0.5666 0.5116 0.5796 0.0367  0.0586  -0.0062 177 ARG A CZ    
1282 N NH1   . ARG A 177 ? 0.6012 0.5491 0.6144 0.0367  0.0583  -0.0070 177 ARG A NH1   
1283 N NH2   . ARG A 177 ? 0.4564 0.3993 0.4693 0.0394  0.0605  -0.0044 177 ARG A NH2   
1284 N N     . LEU A 178 ? 0.5427 0.4863 0.5542 0.0248  0.0519  -0.0092 178 LEU A N     
1285 C CA    . LEU A 178 ? 0.5040 0.4441 0.5147 0.0243  0.0528  -0.0082 178 LEU A CA    
1286 C C     . LEU A 178 ? 0.5290 0.4699 0.5412 0.0271  0.0538  -0.0062 178 LEU A C     
1287 O O     . LEU A 178 ? 0.6315 0.5777 0.6459 0.0284  0.0531  -0.0053 178 LEU A O     
1288 C CB    . LEU A 178 ? 0.4497 0.3928 0.4609 0.0225  0.0513  -0.0076 178 LEU A CB    
1289 C CG    . LEU A 178 ? 0.5380 0.4796 0.5492 0.0220  0.0517  -0.0058 178 LEU A CG    
1290 C CD1   . LEU A 178 ? 0.5653 0.4997 0.5735 0.0202  0.0531  -0.0064 178 LEU A CD1   
1291 C CD2   . LEU A 178 ? 0.5373 0.4837 0.5494 0.0205  0.0500  -0.0053 178 LEU A CD2   
1292 N N     . ASP A 179 ? 0.7329 0.6687 0.7438 0.0281  0.0557  -0.0055 179 ASP A N     
1293 C CA    . ASP A 179 ? 0.8142 0.7510 0.8266 0.0311  0.0568  -0.0031 179 ASP A CA    
1294 C C     . ASP A 179 ? 0.7722 0.7086 0.7849 0.0304  0.0567  -0.0014 179 ASP A C     
1295 O O     . ASP A 179 ? 0.7956 0.7263 0.8066 0.0307  0.0582  -0.0005 179 ASP A O     
1296 C CB    . ASP A 179 ? 0.8675 0.7989 0.8781 0.0334  0.0593  -0.0030 179 ASP A CB    
1297 C CG    . ASP A 179 ? 0.8486 0.7784 0.8577 0.0330  0.0595  -0.0053 179 ASP A CG    
1298 O OD1   . ASP A 179 ? 0.7426 0.6675 0.7490 0.0306  0.0596  -0.0072 179 ASP A OD1   
1299 O OD2   . ASP A 179 ? 0.8654 0.7991 0.8758 0.0350  0.0597  -0.0051 179 ASP A OD2   
1300 N N     . LEU A 180 ? 0.4727 0.4149 0.4874 0.0294  0.0549  -0.0010 180 LEU A N     
1301 C CA    . LEU A 180 ? 0.4624 0.4055 0.4778 0.0288  0.0546  0.0009  180 LEU A CA    
1302 C C     . LEU A 180 ? 0.4677 0.4186 0.4858 0.0295  0.0530  0.0016  180 LEU A C     
1303 O O     . LEU A 180 ? 0.5074 0.4614 0.5256 0.0282  0.0514  0.0002  180 LEU A O     
1304 C CB    . LEU A 180 ? 0.5133 0.4540 0.5269 0.0254  0.0538  0.0001  180 LEU A CB    
1305 C CG    . LEU A 180 ? 0.5213 0.4657 0.5360 0.0242  0.0527  0.0018  180 LEU A CG    
1306 C CD1   . LEU A 180 ? 0.5550 0.4968 0.5699 0.0253  0.0541  0.0044  180 LEU A CD1   
1307 C CD2   . LEU A 180 ? 0.4548 0.3984 0.4678 0.0206  0.0517  0.0007  180 LEU A CD2   
1308 N N     . ALA A 181 ? 0.5969 0.5506 0.6167 0.0315  0.0534  0.0040  181 ALA A N     
1309 C CA    . ALA A 181 ? 0.6265 0.5875 0.6485 0.0321  0.0520  0.0046  181 ALA A CA    
1310 C C     . ALA A 181 ? 0.5660 0.5295 0.5897 0.0338  0.0526  0.0075  181 ALA A C     
1311 O O     . ALA A 181 ? 0.6533 0.6126 0.6762 0.0338  0.0539  0.0090  181 ALA A O     
1312 C CB    . ALA A 181 ? 0.6695 0.6332 0.6923 0.0336  0.0520  0.0039  181 ALA A CB    
1313 N N     . GLY A 182 ? 0.3652 0.3355 0.3910 0.0350  0.0518  0.0084  182 GLY A N     
1314 C CA    . GLY A 182 ? 0.5042 0.4781 0.5317 0.0364  0.0522  0.0113  182 GLY A CA    
1315 C C     . GLY A 182 ? 0.4437 0.4144 0.4714 0.0384  0.0542  0.0139  182 GLY A C     
1316 O O     . GLY A 182 ? 0.4998 0.4715 0.5283 0.0387  0.0545  0.0161  182 GLY A O     
1317 N N     . ARG A 183 ? 0.4010 0.3680 0.4279 0.0401  0.0558  0.0138  183 ARG A N     
1318 C CA    . ARG A 183 ? 0.3773 0.3405 0.4039 0.0426  0.0580  0.0163  183 ARG A CA    
1319 C C     . ARG A 183 ? 0.4502 0.4054 0.4744 0.0409  0.0588  0.0163  183 ARG A C     
1320 O O     . ARG A 183 ? 0.4444 0.3974 0.4685 0.0419  0.0599  0.0189  183 ARG A O     
1321 C CB    . ARG A 183 ? 0.3914 0.3525 0.4173 0.0447  0.0595  0.0156  183 ARG A CB    
1322 C CG    . ARG A 183 ? 0.5008 0.4659 0.5283 0.0485  0.0610  0.0186  183 ARG A CG    
1323 C CD    . ARG A 183 ? 0.5922 0.5639 0.6211 0.0493  0.0603  0.0178  183 ARG A CD    
1324 N NE    . ARG A 183 ? 0.6405 0.6078 0.6675 0.0490  0.0609  0.0154  183 ARG A NE    
1325 C CZ    . ARG A 183 ? 0.6286 0.6005 0.6562 0.0488  0.0601  0.0141  183 ARG A CZ    
1326 N NH1   . ARG A 183 ? 0.5318 0.5122 0.5616 0.0485  0.0587  0.0149  183 ARG A NH1   
1327 N NH2   . ARG A 183 ? 0.6770 0.6448 0.7029 0.0486  0.0607  0.0122  183 ARG A NH2   
1328 N N     . ASP A 184 ? 0.4956 0.4466 0.5177 0.0382  0.0581  0.0136  184 ASP A N     
1329 C CA    . ASP A 184 ? 0.4787 0.4221 0.4981 0.0359  0.0587  0.0134  184 ASP A CA    
1330 C C     . ASP A 184 ? 0.4771 0.4235 0.4974 0.0337  0.0574  0.0146  184 ASP A C     
1331 O O     . ASP A 184 ? 0.4569 0.3981 0.4755 0.0324  0.0582  0.0160  184 ASP A O     
1332 C CB    . ASP A 184 ? 0.5126 0.4517 0.5296 0.0334  0.0583  0.0101  184 ASP A CB    
1333 C CG    . ASP A 184 ? 0.5933 0.5306 0.6097 0.0355  0.0594  0.0087  184 ASP A CG    
1334 O OD1   . ASP A 184 ? 0.5301 0.4603 0.5442 0.0370  0.0616  0.0091  184 ASP A OD1   
1335 O OD2   . ASP A 184 ? 0.6234 0.5659 0.6412 0.0357  0.0582  0.0074  184 ASP A OD2   
1336 N N     . LEU A 185 ? 0.4171 0.3715 0.4395 0.0331  0.0555  0.0142  185 LEU A N     
1337 C CA    . LEU A 185 ? 0.4043 0.3627 0.4277 0.0313  0.0542  0.0154  185 LEU A CA    
1338 C C     . LEU A 185 ? 0.4514 0.4126 0.4767 0.0335  0.0549  0.0189  185 LEU A C     
1339 O O     . LEU A 185 ? 0.4171 0.3787 0.4424 0.0321  0.0547  0.0207  185 LEU A O     
1340 C CB    . LEU A 185 ? 0.3892 0.3548 0.4139 0.0306  0.0520  0.0136  185 LEU A CB    
1341 C CG    . LEU A 185 ? 0.3545 0.3183 0.3775 0.0285  0.0511  0.0105  185 LEU A CG    
1342 C CD1   . LEU A 185 ? 0.3844 0.3552 0.4085 0.0284  0.0492  0.0093  185 LEU A CD1   
1343 C CD2   . LEU A 185 ? 0.3259 0.2852 0.3468 0.0253  0.0511  0.0102  185 LEU A CD2   
1344 N N     . THR A 186 ? 0.4923 0.4557 0.5190 0.0367  0.0559  0.0200  186 THR A N     
1345 C CA    . THR A 186 ? 0.4385 0.4046 0.4669 0.0391  0.0569  0.0236  186 THR A CA    
1346 C C     . THR A 186 ? 0.4673 0.4247 0.4936 0.0397  0.0590  0.0254  186 THR A C     
1347 O O     . THR A 186 ? 0.5216 0.4791 0.5483 0.0399  0.0595  0.0283  186 THR A O     
1348 C CB    . THR A 186 ? 0.4740 0.4462 0.5046 0.0423  0.0572  0.0244  186 THR A CB    
1349 O OG1   . THR A 186 ? 0.4547 0.4361 0.4877 0.0422  0.0555  0.0250  186 THR A OG1   
1350 C CG2   . THR A 186 ? 0.5030 0.4731 0.5339 0.0457  0.0595  0.0277  186 THR A CG2   
1351 N N     . ASP A 187 ? 0.5003 0.4496 0.5239 0.0399  0.0604  0.0238  187 ASP A N     
1352 C CA    . ASP A 187 ? 0.4994 0.4388 0.5200 0.0403  0.0626  0.0253  187 ASP A CA    
1353 C C     . ASP A 187 ? 0.5633 0.4987 0.5820 0.0361  0.0618  0.0253  187 ASP A C     
1354 O O     . ASP A 187 ? 0.6440 0.5753 0.6616 0.0360  0.0629  0.0280  187 ASP A O     
1355 C CB    . ASP A 187 ? 0.6566 0.5881 0.6743 0.0412  0.0642  0.0232  187 ASP A CB    
1356 C CG    . ASP A 187 ? 0.7743 0.7068 0.7928 0.0462  0.0661  0.0248  187 ASP A CG    
1357 O OD1   . ASP A 187 ? 0.8169 0.7586 0.8390 0.0484  0.0656  0.0267  187 ASP A OD1   
1358 O OD2   . ASP A 187 ? 0.7882 0.7128 0.8038 0.0478  0.0681  0.0241  187 ASP A OD2   
1359 N N     . TYR A 188 ? 0.3998 0.3363 0.4178 0.0326  0.0600  0.0224  188 TYR A N     
1360 C CA    . TYR A 188 ? 0.3946 0.3282 0.4107 0.0282  0.0592  0.0224  188 TYR A CA    
1361 C C     . TYR A 188 ? 0.4321 0.3723 0.4506 0.0278  0.0582  0.0253  188 TYR A C     
1362 O O     . TYR A 188 ? 0.4473 0.3835 0.4640 0.0254  0.0585  0.0271  188 TYR A O     
1363 C CB    . TYR A 188 ? 0.2868 0.2225 0.3022 0.0251  0.0574  0.0191  188 TYR A CB    
1364 C CG    . TYR A 188 ? 0.3518 0.2852 0.3651 0.0203  0.0565  0.0190  188 TYR A CG    
1365 C CD1   . TYR A 188 ? 0.3261 0.2492 0.3353 0.0180  0.0580  0.0192  188 TYR A CD1   
1366 C CD2   . TYR A 188 ? 0.3944 0.3360 0.4094 0.0181  0.0543  0.0186  188 TYR A CD2   
1367 C CE1   . TYR A 188 ? 0.4153 0.3369 0.4224 0.0131  0.0570  0.0192  188 TYR A CE1   
1368 C CE2   . TYR A 188 ? 0.4331 0.3737 0.4462 0.0136  0.0535  0.0188  188 TYR A CE2   
1369 C CZ    . TYR A 188 ? 0.4529 0.3838 0.4621 0.0109  0.0548  0.0191  188 TYR A CZ    
1370 O OH    . TYR A 188 ? 0.4870 0.4175 0.4942 0.0059  0.0538  0.0194  188 TYR A OH    
1371 N N     . LEU A 189 ? 0.3261 0.2762 0.3483 0.0299  0.0571  0.0260  189 LEU A N     
1372 C CA    . LEU A 189 ? 0.2937 0.2507 0.3182 0.0298  0.0562  0.0288  189 LEU A CA    
1373 C C     . LEU A 189 ? 0.4100 0.3631 0.4342 0.0318  0.0582  0.0325  189 LEU A C     
1374 O O     . LEU A 189 ? 0.4788 0.4312 0.5026 0.0300  0.0581  0.0349  189 LEU A O     
1375 C CB    . LEU A 189 ? 0.2678 0.2354 0.2957 0.0318  0.0548  0.0284  189 LEU A CB    
1376 C CG    . LEU A 189 ? 0.2647 0.2404 0.2948 0.0315  0.0536  0.0308  189 LEU A CG    
1377 C CD1   . LEU A 189 ? 0.2649 0.2413 0.2940 0.0276  0.0523  0.0304  189 LEU A CD1   
1378 C CD2   . LEU A 189 ? 0.2574 0.2424 0.2901 0.0334  0.0524  0.0297  189 LEU A CD2   
1379 N N     . MET A 190 ? 0.6110 0.5615 0.6354 0.0356  0.0599  0.0331  190 MET A N     
1380 C CA    . MET A 190 ? 0.5906 0.5353 0.6139 0.0379  0.0622  0.0365  190 MET A CA    
1381 C C     . MET A 190 ? 0.6007 0.5348 0.6199 0.0347  0.0631  0.0369  190 MET A C     
1382 O O     . MET A 190 ? 0.5616 0.4938 0.5804 0.0343  0.0637  0.0401  190 MET A O     
1383 C CB    . MET A 190 ? 0.5929 0.5342 0.6157 0.0421  0.0642  0.0362  190 MET A CB    
1384 C CG    . MET A 190 ? 0.5539 0.5053 0.5803 0.0451  0.0636  0.0361  190 MET A CG    
1385 S SD    . MET A 190 ? 0.6416 0.5893 0.6674 0.0504  0.0664  0.0373  190 MET A SD    
1386 C CE    . MET A 190 ? 0.6587 0.5909 0.6793 0.0502  0.0690  0.0383  190 MET A CE    
1387 N N     . LYS A 191 ? 0.6018 0.5284 0.6177 0.0323  0.0633  0.0338  191 LYS A N     
1388 C CA    . LYS A 191 ? 0.6199 0.5365 0.6315 0.0286  0.0640  0.0340  191 LYS A CA    
1389 C C     . LYS A 191 ? 0.6192 0.5401 0.6313 0.0241  0.0620  0.0352  191 LYS A C     
1390 O O     . LYS A 191 ? 0.6548 0.5704 0.6649 0.0224  0.0628  0.0377  191 LYS A O     
1391 C CB    . LYS A 191 ? 0.5672 0.4750 0.5747 0.0267  0.0645  0.0303  191 LYS A CB    
1392 C CG    . LYS A 191 ? 0.5757 0.4697 0.5776 0.0245  0.0664  0.0307  191 LYS A CG    
1393 C CD    . LYS A 191 ? 0.6385 0.5290 0.6372 0.0184  0.0651  0.0282  191 LYS A CD    
1394 C CE    . LYS A 191 ? 0.6502 0.5415 0.6485 0.0178  0.0644  0.0240  191 LYS A CE    
1395 N NZ    . LYS A 191 ? 0.6842 0.5724 0.6792 0.0118  0.0632  0.0217  191 LYS A NZ    
1396 N N     . ILE A 192 ? 0.5188 0.4492 0.5335 0.0223  0.0596  0.0335  192 ILE A N     
1397 C CA    . ILE A 192 ? 0.4567 0.3922 0.4719 0.0183  0.0578  0.0346  192 ILE A CA    
1398 C C     . ILE A 192 ? 0.5200 0.4593 0.5372 0.0195  0.0581  0.0389  192 ILE A C     
1399 O O     . ILE A 192 ? 0.5159 0.4537 0.5318 0.0161  0.0578  0.0410  192 ILE A O     
1400 C CB    . ILE A 192 ? 0.4448 0.3910 0.4628 0.0175  0.0554  0.0324  192 ILE A CB    
1401 C CG1   . ILE A 192 ? 0.5188 0.4630 0.5358 0.0178  0.0553  0.0284  192 ILE A CG1   
1402 C CG2   . ILE A 192 ? 0.4691 0.4183 0.4863 0.0127  0.0538  0.0326  192 ILE A CG2   
1403 C CD1   . ILE A 192 ? 0.5436 0.4979 0.5631 0.0176  0.0531  0.0266  192 ILE A CD1   
1404 N N     . LEU A 193 ? 0.3627 0.3079 0.3832 0.0242  0.0586  0.0403  193 LEU A N     
1405 C CA    . LEU A 193 ? 0.3987 0.3498 0.4219 0.0258  0.0586  0.0443  193 LEU A CA    
1406 C C     . LEU A 193 ? 0.4453 0.3872 0.4662 0.0269  0.0610  0.0477  193 LEU A C     
1407 O O     . LEU A 193 ? 0.4156 0.3607 0.4377 0.0269  0.0610  0.0514  193 LEU A O     
1408 C CB    . LEU A 193 ? 0.3142 0.2748 0.3414 0.0303  0.0583  0.0446  193 LEU A CB    
1409 C CG    . LEU A 193 ? 0.2808 0.2509 0.3102 0.0296  0.0560  0.0418  193 LEU A CG    
1410 C CD1   . LEU A 193 ? 0.4214 0.4001 0.4543 0.0336  0.0560  0.0426  193 LEU A CD1   
1411 C CD2   . LEU A 193 ? 0.2789 0.2545 0.3088 0.0260  0.0543  0.0426  193 LEU A CD2   
1412 N N     . THR A 194 ? 0.4260 0.3568 0.4435 0.0283  0.0630  0.0466  194 THR A N     
1413 C CA    . THR A 194 ? 0.4769 0.3968 0.4911 0.0293  0.0655  0.0495  194 THR A CA    
1414 C C     . THR A 194 ? 0.5522 0.4626 0.5617 0.0237  0.0655  0.0494  194 THR A C     
1415 O O     . THR A 194 ? 0.5527 0.4545 0.5593 0.0235  0.0672  0.0524  194 THR A O     
1416 C CB    . THR A 194 ? 0.4481 0.3600 0.4603 0.0334  0.0679  0.0484  194 THR A CB    
1417 O OG1   . THR A 194 ? 0.3689 0.2908 0.3854 0.0377  0.0675  0.0479  194 THR A OG1   
1418 C CG2   . THR A 194 ? 0.4957 0.3980 0.5051 0.0361  0.0708  0.0522  194 THR A CG2   
1419 N N     . GLU A 195 ? 0.6994 0.6112 0.7080 0.0191  0.0636  0.0462  195 GLU A N     
1420 C CA    . GLU A 195 ? 0.6236 0.5301 0.6285 0.0130  0.0630  0.0464  195 GLU A CA    
1421 C C     . GLU A 195 ? 0.5376 0.4530 0.5452 0.0108  0.0614  0.0497  195 GLU A C     
1422 O O     . GLU A 195 ? 0.5881 0.4980 0.5926 0.0066  0.0615  0.0517  195 GLU A O     
1423 C CB    . GLU A 195 ? 0.6867 0.5939 0.6903 0.0090  0.0614  0.0421  195 GLU A CB    
1424 C CG    . GLU A 195 ? 0.7635 0.6595 0.7629 0.0093  0.0629  0.0388  195 GLU A CG    
1425 C CD    . GLU A 195 ? 0.8619 0.7618 0.8613 0.0065  0.0611  0.0346  195 GLU A CD    
1426 O OE1   . GLU A 195 ? 0.8082 0.7188 0.8105 0.0041  0.0588  0.0346  195 GLU A OE1   
1427 O OE2   . GLU A 195 ? 0.8510 0.7433 0.8474 0.0067  0.0622  0.0316  195 GLU A OE2   
1428 N N     . ARG A 196 ? 0.6053 0.5338 0.6182 0.0135  0.0601  0.0506  196 ARG A N     
1429 C CA    . ARG A 196 ? 0.6374 0.5759 0.6532 0.0120  0.0585  0.0537  196 ARG A CA    
1430 C C     . ARG A 196 ? 0.7436 0.6814 0.7605 0.0151  0.0601  0.0583  196 ARG A C     
1431 O O     . ARG A 196 ? 0.8081 0.7532 0.8272 0.0141  0.0591  0.0614  196 ARG A O     
1432 C CB    . ARG A 196 ? 0.5708 0.5238 0.5912 0.0133  0.0563  0.0521  196 ARG A CB    
1433 C CG    . ARG A 196 ? 0.5612 0.5250 0.5841 0.0110  0.0545  0.0546  196 ARG A CG    
1434 C CD    . ARG A 196 ? 0.6718 0.6428 0.6952 0.0080  0.0522  0.0518  196 ARG A CD    
1435 N NE    . ARG A 196 ? 0.7140 0.6769 0.7332 0.0031  0.0522  0.0500  196 ARG A NE    
1436 C CZ    . ARG A 196 ? 0.6843 0.6515 0.7031 0.0002  0.0505  0.0474  196 ARG A CZ    
1437 N NH1   . ARG A 196 ? 0.6130 0.5919 0.6352 0.0020  0.0489  0.0463  196 ARG A NH1   
1438 N NH2   . ARG A 196 ? 0.7219 0.6817 0.7368 -0.0044 0.0506  0.0460  196 ARG A NH2   
1439 N N     . GLY A 197 ? 0.6404 0.5697 0.6557 0.0190  0.0625  0.0589  197 GLY A N     
1440 C CA    . GLY A 197 ? 0.5813 0.5090 0.5973 0.0223  0.0642  0.0634  197 GLY A CA    
1441 C C     . GLY A 197 ? 0.5884 0.5241 0.6087 0.0286  0.0648  0.0644  197 GLY A C     
1442 O O     . GLY A 197 ? 0.6812 0.6134 0.7013 0.0324  0.0669  0.0678  197 GLY A O     
1443 N N     . TYR A 198 ? 0.6273 0.5735 0.6511 0.0298  0.0631  0.0617  198 TYR A N     
1444 C CA    . TYR A 198 ? 0.6786 0.6316 0.7058 0.0354  0.0638  0.0623  198 TYR A CA    
1445 C C     . TYR A 198 ? 0.7121 0.6553 0.7368 0.0386  0.0661  0.0609  198 TYR A C     
1446 O O     . TYR A 198 ? 0.7799 0.7134 0.8007 0.0363  0.0665  0.0580  198 TYR A O     
1447 C CB    . TYR A 198 ? 0.6541 0.6201 0.6851 0.0354  0.0614  0.0596  198 TYR A CB    
1448 C CG    . TYR A 198 ? 0.6267 0.6013 0.6595 0.0321  0.0592  0.0606  198 TYR A CG    
1449 C CD1   . TYR A 198 ? 0.6219 0.6025 0.6569 0.0331  0.0593  0.0650  198 TYR A CD1   
1450 C CD2   . TYR A 198 ? 0.6757 0.6528 0.7079 0.0282  0.0572  0.0575  198 TYR A CD2   
1451 C CE1   . TYR A 198 ? 0.6288 0.6175 0.6652 0.0301  0.0574  0.0661  198 TYR A CE1   
1452 C CE2   . TYR A 198 ? 0.6087 0.5941 0.6423 0.0255  0.0554  0.0587  198 TYR A CE2   
1453 C CZ    . TYR A 198 ? 0.6245 0.6157 0.6602 0.0264  0.0555  0.0630  198 TYR A CZ    
1454 O OH    . TYR A 198 ? 0.6067 0.6065 0.6439 0.0239  0.0538  0.0643  198 TYR A OH    
1455 N N     . SER A 199 ? 0.5917 0.5376 0.6183 0.0438  0.0676  0.0632  199 SER A N     
1456 C CA    . SER A 199 ? 0.6035 0.5406 0.6276 0.0475  0.0701  0.0626  199 SER A CA    
1457 C C     . SER A 199 ? 0.6332 0.5787 0.6604 0.0507  0.0696  0.0604  199 SER A C     
1458 O O     . SER A 199 ? 0.5224 0.4776 0.5532 0.0542  0.0697  0.0628  199 SER A O     
1459 C CB    . SER A 199 ? 0.6546 0.5865 0.6777 0.0515  0.0729  0.0675  199 SER A CB    
1460 O OG    . SER A 199 ? 0.7521 0.6828 0.7752 0.0569  0.0749  0.0675  199 SER A OG    
1461 N N     . PHE A 200 ? 0.7128 0.6542 0.7382 0.0494  0.0693  0.0560  200 PHE A N     
1462 C CA    . PHE A 200 ? 0.6447 0.5920 0.6721 0.0520  0.0690  0.0536  200 PHE A CA    
1463 C C     . PHE A 200 ? 0.6495 0.5859 0.6733 0.0538  0.0712  0.0519  200 PHE A C     
1464 O O     . PHE A 200 ? 0.7304 0.6587 0.7508 0.0505  0.0709  0.0486  200 PHE A O     
1465 C CB    . PHE A 200 ? 0.6316 0.5860 0.6606 0.0485  0.0661  0.0497  200 PHE A CB    
1466 C CG    . PHE A 200 ? 0.6114 0.5765 0.6437 0.0468  0.0639  0.0509  200 PHE A CG    
1467 C CD1   . PHE A 200 ? 0.6280 0.6047 0.6641 0.0495  0.0633  0.0523  200 PHE A CD1   
1468 C CD2   . PHE A 200 ? 0.6567 0.6210 0.6880 0.0424  0.0624  0.0504  200 PHE A CD2   
1469 C CE1   . PHE A 200 ? 0.6358 0.6224 0.6746 0.0480  0.0613  0.0532  200 PHE A CE1   
1470 C CE2   . PHE A 200 ? 0.7198 0.6944 0.7540 0.0411  0.0605  0.0515  200 PHE A CE2   
1471 C CZ    . PHE A 200 ? 0.6833 0.6688 0.7211 0.0440  0.0600  0.0528  200 PHE A CZ    
1472 N N     . THR A 201 ? 0.5056 0.4422 0.5299 0.0591  0.0733  0.0541  201 THR A N     
1473 C CA    . THR A 201 ? 0.5532 0.4805 0.5741 0.0619  0.0757  0.0528  201 THR A CA    
1474 C C     . THR A 201 ? 0.5403 0.4760 0.5640 0.0665  0.0763  0.0531  201 THR A C     
1475 O O     . THR A 201 ? 0.4928 0.4272 0.5157 0.0667  0.0763  0.0499  201 THR A O     
1476 C CB    . THR A 201 ? 0.6327 0.5478 0.6495 0.0642  0.0787  0.0558  201 THR A CB    
1477 O OG1   . THR A 201 ? 0.7011 0.6103 0.7158 0.0596  0.0780  0.0563  201 THR A OG1   
1478 C CG2   . THR A 201 ? 0.6331 0.5364 0.6452 0.0658  0.0809  0.0533  201 THR A CG2   
1479 N N     . THR A 202 ? 0.6835 0.6274 0.7104 0.0703  0.0770  0.0573  202 THR A N     
1480 C CA    . THR A 202 ? 0.6558 0.6091 0.6856 0.0747  0.0776  0.0586  202 THR A CA    
1481 C C     . THR A 202 ? 0.6484 0.6120 0.6811 0.0722  0.0748  0.0551  202 THR A C     
1482 O O     . THR A 202 ? 0.6917 0.6578 0.7252 0.0676  0.0723  0.0527  202 THR A O     
1483 C CB    . THR A 202 ? 0.7049 0.6665 0.7378 0.0781  0.0784  0.0639  202 THR A CB    
1484 O OG1   . THR A 202 ? 0.7065 0.6784 0.7429 0.0749  0.0756  0.0641  202 THR A OG1   
1485 C CG2   . THR A 202 ? 0.6670 0.6179 0.6968 0.0802  0.0810  0.0677  202 THR A CG2   
1486 N N     . THR A 203 ? 0.6004 0.5699 0.6345 0.0753  0.0754  0.0550  203 THR A N     
1487 C CA    . THR A 203 ? 0.5784 0.5561 0.6145 0.0728  0.0730  0.0516  203 THR A CA    
1488 C C     . THR A 203 ? 0.6959 0.6857 0.7357 0.0708  0.0705  0.0524  203 THR A C     
1489 O O     . THR A 203 ? 0.7711 0.7646 0.8116 0.0670  0.0680  0.0490  203 THR A O     
1490 C CB    . THR A 203 ? 0.5805 0.5622 0.6172 0.0764  0.0742  0.0517  203 THR A CB    
1491 O OG1   . THR A 203 ? 0.6350 0.6236 0.6738 0.0811  0.0759  0.0566  203 THR A OG1   
1492 C CG2   . THR A 203 ? 0.5574 0.5270 0.5901 0.0777  0.0763  0.0499  203 THR A CG2   
1493 N N     . ALA A 204 ? 0.5137 0.5098 0.5558 0.0735  0.0713  0.0568  204 ALA A N     
1494 C CA    . ALA A 204 ? 0.4346 0.4407 0.4795 0.0712  0.0690  0.0575  204 ALA A CA    
1495 C C     . ALA A 204 ? 0.4201 0.4210 0.4637 0.0668  0.0674  0.0554  204 ALA A C     
1496 O O     . ALA A 204 ? 0.3723 0.3789 0.4170 0.0635  0.0649  0.0530  204 ALA A O     
1497 C CB    . ALA A 204 ? 0.3044 0.3172 0.3516 0.0748  0.0703  0.0630  204 ALA A CB    
1498 N N     . GLU A 205 ? 0.6660 0.6557 0.7069 0.0667  0.0689  0.0563  205 GLU A N     
1499 C CA    . GLU A 205 ? 0.6900 0.6747 0.7293 0.0622  0.0674  0.0545  205 GLU A CA    
1500 C C     . GLU A 205 ? 0.7196 0.7014 0.7575 0.0587  0.0658  0.0494  205 GLU A C     
1501 O O     . GLU A 205 ? 0.8043 0.7878 0.8422 0.0550  0.0637  0.0474  205 GLU A O     
1502 C CB    . GLU A 205 ? 0.6693 0.6420 0.7054 0.0625  0.0695  0.0567  205 GLU A CB    
1503 C CG    . GLU A 205 ? 0.7525 0.7283 0.7902 0.0654  0.0709  0.0621  205 GLU A CG    
1504 C CD    . GLU A 205 ? 0.8195 0.7830 0.8537 0.0655  0.0729  0.0645  205 GLU A CD    
1505 O OE1   . GLU A 205 ? 0.8237 0.7751 0.8538 0.0657  0.0746  0.0630  205 GLU A OE1   
1506 O OE2   . GLU A 205 ? 0.8831 0.8488 0.9182 0.0651  0.0728  0.0680  205 GLU A OE2   
1507 N N     . ARG A 206 ? 0.6262 0.6043 0.6627 0.0601  0.0667  0.0473  206 ARG A N     
1508 C CA    . ARG A 206 ? 0.5910 0.5692 0.6269 0.0572  0.0650  0.0427  206 ARG A CA    
1509 C C     . ARG A 206 ? 0.5256 0.5157 0.5644 0.0560  0.0626  0.0416  206 ARG A C     
1510 O O     . ARG A 206 ? 0.4840 0.4752 0.5226 0.0526  0.0605  0.0388  206 ARG A O     
1511 C CB    . ARG A 206 ? 0.5853 0.5591 0.6197 0.0595  0.0665  0.0412  206 ARG A CB    
1512 C CG    . ARG A 206 ? 0.5551 0.5266 0.5881 0.0566  0.0651  0.0366  206 ARG A CG    
1513 C CD    . ARG A 206 ? 0.6178 0.5825 0.6484 0.0586  0.0671  0.0353  206 ARG A CD    
1514 N NE    . ARG A 206 ? 0.6997 0.6590 0.7281 0.0553  0.0661  0.0311  206 ARG A NE    
1515 C CZ    . ARG A 206 ? 0.6833 0.6478 0.7128 0.0527  0.0638  0.0282  206 ARG A CZ    
1516 N NH1   . ARG A 206 ? 0.6412 0.6159 0.6736 0.0528  0.0622  0.0287  206 ARG A NH1   
1517 N NH2   . ARG A 206 ? 0.6614 0.6206 0.6886 0.0500  0.0631  0.0247  206 ARG A NH2   
1518 N N     . GLU A 207 ? 0.5046 0.5034 0.5459 0.0588  0.0628  0.0439  207 GLU A N     
1519 C CA    . GLU A 207 ? 0.5002 0.5099 0.5438 0.0576  0.0607  0.0428  207 GLU A CA    
1520 C C     . GLU A 207 ? 0.4148 0.4286 0.4593 0.0550  0.0588  0.0428  207 GLU A C     
1521 O O     . GLU A 207 ? 0.4148 0.4335 0.4596 0.0527  0.0567  0.0401  207 GLU A O     
1522 C CB    . GLU A 207 ? 0.5699 0.5886 0.6159 0.0609  0.0615  0.0459  207 GLU A CB    
1523 C CG    . GLU A 207 ? 0.6352 0.6532 0.6807 0.0629  0.0627  0.0453  207 GLU A CG    
1524 C CD    . GLU A 207 ? 0.7359 0.7543 0.7805 0.0600  0.0609  0.0408  207 GLU A CD    
1525 O OE1   . GLU A 207 ? 0.6908 0.7036 0.7337 0.0570  0.0596  0.0375  207 GLU A OE1   
1526 O OE2   . GLU A 207 ? 0.8296 0.8544 0.8752 0.0608  0.0607  0.0407  207 GLU A OE2   
1527 N N     . ILE A 208 ? 0.3552 0.3673 0.3999 0.0555  0.0596  0.0459  208 ILE A N     
1528 C CA    . ILE A 208 ? 0.3623 0.3785 0.4078 0.0532  0.0579  0.0461  208 ILE A CA    
1529 C C     . ILE A 208 ? 0.3135 0.3237 0.3568 0.0496  0.0567  0.0426  208 ILE A C     
1530 O O     . ILE A 208 ? 0.2828 0.2979 0.3264 0.0474  0.0547  0.0408  208 ILE A O     
1531 C CB    . ILE A 208 ? 0.4494 0.4649 0.4956 0.0545  0.0592  0.0506  208 ILE A CB    
1532 C CG1   . ILE A 208 ? 0.4199 0.4431 0.4685 0.0581  0.0603  0.0544  208 ILE A CG1   
1533 C CG2   . ILE A 208 ? 0.5042 0.5223 0.5507 0.0516  0.0576  0.0507  208 ILE A CG2   
1534 C CD1   . ILE A 208 ? 0.4021 0.4197 0.4503 0.0609  0.0628  0.0588  208 ILE A CD1   
1535 N N     . VAL A 209 ? 0.3936 0.3934 0.4345 0.0490  0.0579  0.0419  209 VAL A N     
1536 C CA    . VAL A 209 ? 0.4753 0.4694 0.5140 0.0455  0.0569  0.0388  209 VAL A CA    
1537 C C     . VAL A 209 ? 0.4768 0.4742 0.5154 0.0442  0.0552  0.0349  209 VAL A C     
1538 O O     . VAL A 209 ? 0.4654 0.4638 0.5034 0.0416  0.0535  0.0327  209 VAL A O     
1539 C CB    . VAL A 209 ? 0.4268 0.4088 0.4624 0.0452  0.0587  0.0385  209 VAL A CB    
1540 C CG1   . VAL A 209 ? 0.3027 0.2799 0.3361 0.0415  0.0576  0.0350  209 VAL A CG1   
1541 C CG2   . VAL A 209 ? 0.4234 0.4006 0.4582 0.0458  0.0603  0.0422  209 VAL A CG2   
1542 N N     . ARG A 210 ? 0.4937 0.4931 0.5329 0.0461  0.0555  0.0339  210 ARG A N     
1543 C CA    . ARG A 210 ? 0.5178 0.5200 0.5566 0.0448  0.0540  0.0304  210 ARG A CA    
1544 C C     . ARG A 210 ? 0.4980 0.5092 0.5382 0.0441  0.0520  0.0300  210 ARG A C     
1545 O O     . ARG A 210 ? 0.4787 0.4911 0.5179 0.0424  0.0505  0.0268  210 ARG A O     
1546 C CB    . ARG A 210 ? 0.5892 0.5916 0.6282 0.0468  0.0549  0.0299  210 ARG A CB    
1547 C CG    . ARG A 210 ? 0.6927 0.6971 0.7310 0.0453  0.0533  0.0262  210 ARG A CG    
1548 C CD    . ARG A 210 ? 0.7898 0.7906 0.8272 0.0463  0.0543  0.0250  210 ARG A CD    
1549 N NE    . ARG A 210 ? 0.7861 0.7773 0.8215 0.0462  0.0558  0.0244  210 ARG A NE    
1550 C CZ    . ARG A 210 ? 0.7123 0.6989 0.7463 0.0464  0.0564  0.0226  210 ARG A CZ    
1551 N NH1   . ARG A 210 ? 0.6970 0.6878 0.7314 0.0465  0.0558  0.0212  210 ARG A NH1   
1552 N NH2   . ARG A 210 ? 0.7101 0.6878 0.7419 0.0462  0.0578  0.0220  210 ARG A NH2   
1553 N N     . ASP A 211 ? 0.4406 0.4579 0.4827 0.0453  0.0522  0.0331  211 ASP A N     
1554 C CA    . ASP A 211 ? 0.4922 0.5176 0.5352 0.0444  0.0504  0.0328  211 ASP A CA    
1555 C C     . ASP A 211 ? 0.4654 0.4889 0.5074 0.0422  0.0494  0.0319  211 ASP A C     
1556 O O     . ASP A 211 ? 0.4844 0.5112 0.5257 0.0410  0.0478  0.0295  211 ASP A O     
1557 C CB    . ASP A 211 ? 0.5403 0.5729 0.5856 0.0464  0.0510  0.0366  211 ASP A CB    
1558 C CG    . ASP A 211 ? 0.5880 0.6297 0.6340 0.0457  0.0492  0.0362  211 ASP A CG    
1559 O OD1   . ASP A 211 ? 0.5553 0.5994 0.6004 0.0448  0.0479  0.0331  211 ASP A OD1   
1560 O OD2   . ASP A 211 ? 0.6071 0.6535 0.6546 0.0461  0.0492  0.0389  211 ASP A OD2   
1561 N N     . ILE A 212 ? 0.3955 0.4139 0.4372 0.0417  0.0504  0.0338  212 ILE A N     
1562 C CA    . ILE A 212 ? 0.3299 0.3474 0.3707 0.0393  0.0495  0.0335  212 ILE A CA    
1563 C C     . ILE A 212 ? 0.3518 0.3654 0.3906 0.0374  0.0486  0.0296  212 ILE A C     
1564 O O     . ILE A 212 ? 0.3623 0.3787 0.4005 0.0359  0.0472  0.0284  212 ILE A O     
1565 C CB    . ILE A 212 ? 0.2832 0.2949 0.3236 0.0387  0.0509  0.0364  212 ILE A CB    
1566 C CG1   . ILE A 212 ? 0.2683 0.2821 0.3104 0.0413  0.0523  0.0403  212 ILE A CG1   
1567 C CG2   . ILE A 212 ? 0.3120 0.3260 0.3522 0.0364  0.0498  0.0372  212 ILE A CG2   
1568 C CD1   . ILE A 212 ? 0.3284 0.3356 0.3696 0.0408  0.0537  0.0432  212 ILE A CD1   
1569 N N     . LYS A 213 ? 0.4154 0.4229 0.4530 0.0376  0.0493  0.0279  213 LYS A N     
1570 C CA    . LYS A 213 ? 0.4651 0.4692 0.5008 0.0360  0.0485  0.0243  213 LYS A CA    
1571 C C     . LYS A 213 ? 0.4434 0.4535 0.4791 0.0361  0.0469  0.0220  213 LYS A C     
1572 O O     . LYS A 213 ? 0.4927 0.5037 0.5273 0.0348  0.0457  0.0202  213 LYS A O     
1573 C CB    . LYS A 213 ? 0.4212 0.4184 0.4558 0.0365  0.0498  0.0231  213 LYS A CB    
1574 C CG    . LYS A 213 ? 0.3750 0.3681 0.4076 0.0347  0.0491  0.0196  213 LYS A CG    
1575 C CD    . LYS A 213 ? 0.4917 0.4771 0.5229 0.0351  0.0506  0.0189  213 LYS A CD    
1576 C CE    . LYS A 213 ? 0.5042 0.4915 0.5365 0.0377  0.0514  0.0193  213 LYS A CE    
1577 N NZ    . LYS A 213 ? 0.4472 0.4393 0.4799 0.0377  0.0501  0.0171  213 LYS A NZ    
1578 N N     . GLU A 214 ? 0.5695 0.5836 0.6061 0.0377  0.0468  0.0220  214 GLU A N     
1579 C CA    . GLU A 214 ? 0.5393 0.5574 0.5751 0.0376  0.0454  0.0194  214 GLU A CA    
1580 C C     . GLU A 214 ? 0.4733 0.4977 0.5093 0.0374  0.0442  0.0197  214 GLU A C     
1581 O O     . GLU A 214 ? 0.5088 0.5350 0.5432 0.0371  0.0430  0.0172  214 GLU A O     
1582 C CB    . GLU A 214 ? 0.5445 0.5652 0.5810 0.0388  0.0457  0.0194  214 GLU A CB    
1583 C CG    . GLU A 214 ? 0.5174 0.5323 0.5536 0.0392  0.0469  0.0190  214 GLU A CG    
1584 C CD    . GLU A 214 ? 0.6178 0.6365 0.6550 0.0406  0.0474  0.0199  214 GLU A CD    
1585 O OE1   . GLU A 214 ? 0.6646 0.6899 0.7022 0.0406  0.0464  0.0199  214 GLU A OE1   
1586 O OE2   . GLU A 214 ? 0.6654 0.6808 0.7029 0.0416  0.0487  0.0206  214 GLU A OE2   
1587 N N     . LYS A 215 ? 0.4171 0.4445 0.4546 0.0377  0.0445  0.0227  215 LYS A N     
1588 C CA    . LYS A 215 ? 0.4429 0.4767 0.4805 0.0377  0.0435  0.0232  215 LYS A CA    
1589 C C     . LYS A 215 ? 0.4860 0.5179 0.5229 0.0361  0.0432  0.0232  215 LYS A C     
1590 O O     . LYS A 215 ? 0.6151 0.6478 0.6504 0.0357  0.0421  0.0210  215 LYS A O     
1591 C CB    . LYS A 215 ? 0.3809 0.4205 0.4209 0.0388  0.0440  0.0267  215 LYS A CB    
1592 C CG    . LYS A 215 ? 0.3890 0.4350 0.4297 0.0401  0.0436  0.0268  215 LYS A CG    
1593 C CD    . LYS A 215 ? 0.4032 0.4472 0.4444 0.0410  0.0445  0.0270  215 LYS A CD    
1594 C CE    . LYS A 215 ? 0.4392 0.4910 0.4819 0.0422  0.0445  0.0287  215 LYS A CE    
1595 N NZ    . LYS A 215 ? 0.5501 0.6059 0.5952 0.0433  0.0453  0.0329  215 LYS A NZ    
1596 N N     . LEU A 216 ? 0.4757 0.5049 0.5135 0.0353  0.0441  0.0258  216 LEU A N     
1597 C CA    . LEU A 216 ? 0.4656 0.4954 0.5031 0.0336  0.0437  0.0269  216 LEU A CA    
1598 C C     . LEU A 216 ? 0.4249 0.4491 0.4604 0.0316  0.0435  0.0249  216 LEU A C     
1599 O O     . LEU A 216 ? 0.3954 0.4222 0.4303 0.0302  0.0427  0.0249  216 LEU A O     
1600 C CB    . LEU A 216 ? 0.3943 0.4233 0.4332 0.0332  0.0447  0.0308  216 LEU A CB    
1601 C CG    . LEU A 216 ? 0.3513 0.3879 0.3921 0.0351  0.0446  0.0329  216 LEU A CG    
1602 C CD1   . LEU A 216 ? 0.4118 0.4491 0.4542 0.0349  0.0455  0.0372  216 LEU A CD1   
1603 C CD2   . LEU A 216 ? 0.3650 0.4092 0.4056 0.0353  0.0431  0.0316  216 LEU A CD2   
1604 N N     . CYS A 217 ? 0.3733 0.3905 0.4079 0.0314  0.0442  0.0233  217 CYS A N     
1605 C CA    . CYS A 217 ? 0.3642 0.3758 0.3970 0.0293  0.0442  0.0216  217 CYS A CA    
1606 C C     . CYS A 217 ? 0.3654 0.3796 0.3969 0.0294  0.0429  0.0187  217 CYS A C     
1607 O O     . CYS A 217 ? 0.3257 0.3429 0.3572 0.0312  0.0424  0.0173  217 CYS A O     
1608 C CB    . CYS A 217 ? 0.4019 0.4058 0.4339 0.0295  0.0454  0.0205  217 CYS A CB    
1609 S SG    . CYS A 217 ? 0.4527 0.4500 0.4845 0.0285  0.0471  0.0233  217 CYS A SG    
1610 N N     . TYR A 218 ? 0.3611 0.3742 0.3913 0.0273  0.0425  0.0181  218 TYR A N     
1611 C CA    . TYR A 218 ? 0.4087 0.4230 0.4374 0.0274  0.0415  0.0155  218 TYR A CA    
1612 C C     . TYR A 218 ? 0.3672 0.3771 0.3945 0.0249  0.0416  0.0147  218 TYR A C     
1613 O O     . TYR A 218 ? 0.3196 0.3251 0.3466 0.0227  0.0424  0.0160  218 TYR A O     
1614 C CB    . TYR A 218 ? 0.3469 0.3692 0.3757 0.0284  0.0405  0.0160  218 TYR A CB    
1615 C CG    . TYR A 218 ? 0.3781 0.4039 0.4073 0.0263  0.0402  0.0184  218 TYR A CG    
1616 C CD1   . TYR A 218 ? 0.4421 0.4680 0.4727 0.0252  0.0408  0.0213  218 TYR A CD1   
1617 C CD2   . TYR A 218 ? 0.3715 0.4009 0.3996 0.0255  0.0394  0.0180  218 TYR A CD2   
1618 C CE1   . TYR A 218 ? 0.4418 0.4711 0.4726 0.0229  0.0405  0.0237  218 TYR A CE1   
1619 C CE2   . TYR A 218 ? 0.3440 0.3774 0.3724 0.0233  0.0391  0.0204  218 TYR A CE2   
1620 C CZ    . TYR A 218 ? 0.3908 0.4241 0.4206 0.0218  0.0396  0.0232  218 TYR A CZ    
1621 O OH    . TYR A 218 ? 0.3331 0.3706 0.3631 0.0192  0.0392  0.0257  218 TYR A OH    
1622 N N     . VAL A 219 ? 0.2511 0.2621 0.2769 0.0250  0.0409  0.0127  219 VAL A N     
1623 C CA    . VAL A 219 ? 0.3655 0.3736 0.3898 0.0227  0.0408  0.0118  219 VAL A CA    
1624 C C     . VAL A 219 ? 0.4443 0.4589 0.4684 0.0216  0.0399  0.0129  219 VAL A C     
1625 O O     . VAL A 219 ? 0.4034 0.4239 0.4275 0.0238  0.0392  0.0127  219 VAL A O     
1626 C CB    . VAL A 219 ? 0.3551 0.3599 0.3781 0.0235  0.0407  0.0089  219 VAL A CB    
1627 C CG1   . VAL A 219 ? 0.3604 0.3651 0.3819 0.0215  0.0403  0.0082  219 VAL A CG1   
1628 C CG2   . VAL A 219 ? 0.3192 0.3171 0.3423 0.0235  0.0417  0.0080  219 VAL A CG2   
1629 N N     . ALA A 220 ? 0.3955 0.4090 0.4191 0.0182  0.0400  0.0143  220 ALA A N     
1630 C CA    . ALA A 220 ? 0.3260 0.3459 0.3493 0.0166  0.0392  0.0155  220 ALA A CA    
1631 C C     . ALA A 220 ? 0.3800 0.4006 0.4018 0.0168  0.0387  0.0135  220 ALA A C     
1632 O O     . ALA A 220 ? 0.4184 0.4328 0.4391 0.0167  0.0391  0.0113  220 ALA A O     
1633 C CB    . ALA A 220 ? 0.3162 0.3342 0.3391 0.0123  0.0394  0.0175  220 ALA A CB    
1634 N N     . LEU A 221 ? 0.2696 0.2981 0.2912 0.0176  0.0379  0.0142  221 LEU A N     
1635 C CA    . LEU A 221 ? 0.2388 0.2692 0.2590 0.0181  0.0374  0.0129  221 LEU A CA    
1636 C C     . LEU A 221 ? 0.3545 0.3848 0.3738 0.0137  0.0373  0.0136  221 LEU A C     
1637 O O     . LEU A 221 ? 0.3736 0.4001 0.3915 0.0126  0.0374  0.0119  221 LEU A O     
1638 C CB    . LEU A 221 ? 0.2515 0.2907 0.2716 0.0213  0.0368  0.0136  221 LEU A CB    
1639 C CG    . LEU A 221 ? 0.2900 0.3300 0.3084 0.0235  0.0366  0.0118  221 LEU A CG    
1640 C CD1   . LEU A 221 ? 0.2317 0.2642 0.2493 0.0257  0.0370  0.0090  221 LEU A CD1   
1641 C CD2   . LEU A 221 ? 0.2309 0.2797 0.2487 0.0267  0.0361  0.0128  221 LEU A CD2   
1642 N N     . ASP A 222 ? 0.5324 0.5669 0.5522 0.0109  0.0370  0.0162  222 ASP A N     
1643 C CA    . ASP A 222 ? 0.5038 0.5368 0.5224 0.0056  0.0369  0.0172  222 ASP A CA    
1644 C C     . ASP A 222 ? 0.4687 0.4967 0.4879 0.0035  0.0375  0.0186  222 ASP A C     
1645 O O     . ASP A 222 ? 0.4451 0.4778 0.4657 0.0040  0.0373  0.0209  222 ASP A O     
1646 C CB    . ASP A 222 ? 0.4485 0.4916 0.4669 0.0038  0.0359  0.0193  222 ASP A CB    
1647 C CG    . ASP A 222 ? 0.5637 0.6062 0.5810 -0.0024 0.0357  0.0210  222 ASP A CG    
1648 O OD1   . ASP A 222 ? 0.5363 0.5696 0.5522 -0.0054 0.0364  0.0198  222 ASP A OD1   
1649 O OD2   . ASP A 222 ? 0.7051 0.7566 0.7227 -0.0044 0.0349  0.0235  222 ASP A OD2   
1650 N N     . PHE A 223 ? 0.3314 0.3496 0.3492 0.0015  0.0384  0.0173  223 PHE A N     
1651 C CA    . PHE A 223 ? 0.4611 0.4731 0.4789 -0.0001 0.0392  0.0185  223 PHE A CA    
1652 C C     . PHE A 223 ? 0.5519 0.5675 0.5693 -0.0044 0.0388  0.0215  223 PHE A C     
1653 O O     . PHE A 223 ? 0.5308 0.5472 0.5494 -0.0042 0.0390  0.0238  223 PHE A O     
1654 C CB    . PHE A 223 ? 0.3344 0.3353 0.3503 -0.0014 0.0403  0.0164  223 PHE A CB    
1655 C CG    . PHE A 223 ? 0.3303 0.3234 0.3454 -0.0029 0.0415  0.0176  223 PHE A CG    
1656 C CD1   . PHE A 223 ? 0.3319 0.3225 0.3488 0.0008  0.0423  0.0180  223 PHE A CD1   
1657 C CD2   . PHE A 223 ? 0.3581 0.3465 0.3707 -0.0079 0.0418  0.0184  223 PHE A CD2   
1658 C CE1   . PHE A 223 ? 0.4227 0.4063 0.4388 -0.0001 0.0436  0.0194  223 PHE A CE1   
1659 C CE2   . PHE A 223 ? 0.4263 0.4065 0.4376 -0.0090 0.0430  0.0196  223 PHE A CE2   
1660 C CZ    . PHE A 223 ? 0.4003 0.3781 0.4135 -0.0048 0.0440  0.0202  223 PHE A CZ    
1661 N N     . GLU A 224 ? 0.6181 0.6367 0.6338 -0.0084 0.0381  0.0218  224 GLU A N     
1662 C CA    . GLU A 224 ? 0.5223 0.5451 0.5372 -0.0133 0.0374  0.0247  224 GLU A CA    
1663 C C     . GLU A 224 ? 0.5178 0.5511 0.5352 -0.0113 0.0367  0.0275  224 GLU A C     
1664 O O     . GLU A 224 ? 0.4812 0.5149 0.4989 -0.0135 0.0367  0.0301  224 GLU A O     
1665 C CB    . GLU A 224 ? 0.4797 0.5064 0.4926 -0.0173 0.0366  0.0243  224 GLU A CB    
1666 C CG    . GLU A 224 ? 0.5132 0.5300 0.5229 -0.0212 0.0372  0.0222  224 GLU A CG    
1667 C CD    . GLU A 224 ? 0.6216 0.6413 0.6288 -0.0280 0.0364  0.0237  224 GLU A CD    
1668 O OE1   . GLU A 224 ? 0.6613 0.6917 0.6696 -0.0295 0.0353  0.0264  224 GLU A OE1   
1669 O OE2   . GLU A 224 ? 0.6329 0.6442 0.6368 -0.0321 0.0369  0.0221  224 GLU A OE2   
1670 N N     . GLN A 225 ? 0.5302 0.5723 0.5492 -0.0073 0.0360  0.0270  225 GLN A N     
1671 C CA    . GLN A 225 ? 0.5376 0.5899 0.5587 -0.0050 0.0354  0.0295  225 GLN A CA    
1672 C C     . GLN A 225 ? 0.5291 0.5782 0.5519 -0.0022 0.0361  0.0301  225 GLN A C     
1673 O O     . GLN A 225 ? 0.4585 0.5124 0.4824 -0.0030 0.0358  0.0330  225 GLN A O     
1674 C CB    . GLN A 225 ? 0.5191 0.5798 0.5409 -0.0007 0.0348  0.0285  225 GLN A CB    
1675 C CG    . GLN A 225 ? 0.6398 0.7090 0.6606 -0.0032 0.0339  0.0296  225 GLN A CG    
1676 C CD    . GLN A 225 ? 0.7253 0.8064 0.7471 -0.0048 0.0331  0.0333  225 GLN A CD    
1677 O OE1   . GLN A 225 ? 0.7457 0.8265 0.7682 -0.0068 0.0331  0.0355  225 GLN A OE1   
1678 N NE2   . GLN A 225 ? 0.7145 0.8062 0.7362 -0.0036 0.0324  0.0342  225 GLN A NE2   
1679 N N     . GLU A 226 ? 0.6069 0.6484 0.6299 0.0009  0.0369  0.0278  226 GLU A N     
1680 C CA    . GLU A 226 ? 0.4770 0.5157 0.5015 0.0031  0.0376  0.0286  226 GLU A CA    
1681 C C     . GLU A 226 ? 0.4595 0.4923 0.4833 -0.0009 0.0382  0.0307  226 GLU A C     
1682 O O     . GLU A 226 ? 0.4388 0.4740 0.4639 -0.0005 0.0384  0.0332  226 GLU A O     
1683 C CB    . GLU A 226 ? 0.4356 0.4684 0.4605 0.0072  0.0384  0.0258  226 GLU A CB    
1684 C CG    . GLU A 226 ? 0.4746 0.5132 0.5001 0.0115  0.0378  0.0241  226 GLU A CG    
1685 C CD    . GLU A 226 ? 0.5585 0.6066 0.5855 0.0138  0.0372  0.0261  226 GLU A CD    
1686 O OE1   . GLU A 226 ? 0.6503 0.7065 0.6773 0.0128  0.0364  0.0276  226 GLU A OE1   
1687 O OE2   . GLU A 226 ? 0.5373 0.5853 0.5655 0.0167  0.0375  0.0260  226 GLU A OE2   
1688 N N     . MET A 227 ? 0.4184 0.4430 0.4397 -0.0047 0.0387  0.0298  227 MET A N     
1689 C CA    . MET A 227 ? 0.4955 0.5142 0.5153 -0.0088 0.0393  0.0320  227 MET A CA    
1690 C C     . MET A 227 ? 0.5924 0.6201 0.6128 -0.0119 0.0383  0.0355  227 MET A C     
1691 O O     . MET A 227 ? 0.5515 0.5791 0.5727 -0.0123 0.0386  0.0383  227 MET A O     
1692 C CB    . MET A 227 ? 0.5070 0.5163 0.5234 -0.0131 0.0398  0.0303  227 MET A CB    
1693 C CG    . MET A 227 ? 0.6457 0.6444 0.6612 -0.0107 0.0412  0.0275  227 MET A CG    
1694 S SD    . MET A 227 ? 0.6604 0.6526 0.6772 -0.0073 0.0428  0.0290  227 MET A SD    
1695 C CE    . MET A 227 ? 0.6766 0.6566 0.6892 -0.0125 0.0440  0.0300  227 MET A CE    
1696 N N     . ALA A 228 ? 0.6216 0.6575 0.6417 -0.0139 0.0371  0.0357  228 ALA A N     
1697 C CA    . ALA A 228 ? 0.6065 0.6517 0.6269 -0.0172 0.0360  0.0391  228 ALA A CA    
1698 C C     . ALA A 228 ? 0.5675 0.6213 0.5910 -0.0133 0.0358  0.0413  228 ALA A C     
1699 O O     . ALA A 228 ? 0.6230 0.6815 0.6470 -0.0158 0.0354  0.0447  228 ALA A O     
1700 C CB    . ALA A 228 ? 0.6122 0.6661 0.6319 -0.0192 0.0349  0.0389  228 ALA A CB    
1701 N N     . THR A 229 ? 0.3904 0.4459 0.4156 -0.0074 0.0360  0.0393  229 THR A N     
1702 C CA    . THR A 229 ? 0.4137 0.4769 0.4415 -0.0036 0.0358  0.0410  229 THR A CA    
1703 C C     . THR A 229 ? 0.5121 0.5692 0.5408 -0.0031 0.0368  0.0425  229 THR A C     
1704 O O     . THR A 229 ? 0.5043 0.5676 0.5347 -0.0026 0.0365  0.0454  229 THR A O     
1705 C CB    . THR A 229 ? 0.3958 0.4623 0.4246 0.0022  0.0357  0.0383  229 THR A CB    
1706 O OG1   . THR A 229 ? 0.3928 0.4693 0.4214 0.0028  0.0348  0.0384  229 THR A OG1   
1707 C CG2   . THR A 229 ? 0.3763 0.4457 0.4072 0.0064  0.0360  0.0391  229 THR A CG2   
1708 N N     . ALA A 230 ? 0.4537 0.4991 0.4814 -0.0028 0.0379  0.0407  230 ALA A N     
1709 C CA    . ALA A 230 ? 0.3818 0.4210 0.4100 -0.0023 0.0390  0.0423  230 ALA A CA    
1710 C C     . ALA A 230 ? 0.4391 0.4764 0.4661 -0.0074 0.0391  0.0458  230 ALA A C     
1711 O O     . ALA A 230 ? 0.4737 0.5107 0.5018 -0.0069 0.0396  0.0486  230 ALA A O     
1712 C CB    . ALA A 230 ? 0.2661 0.2935 0.2933 -0.0007 0.0404  0.0397  230 ALA A CB    
1713 N N     . ALA A 231 ? 0.4291 0.4649 0.4537 -0.0125 0.0386  0.0458  231 ALA A N     
1714 C CA    . ALA A 231 ? 0.3668 0.4006 0.3895 -0.0182 0.0385  0.0491  231 ALA A CA    
1715 C C     . ALA A 231 ? 0.3922 0.4395 0.4166 -0.0197 0.0371  0.0524  231 ALA A C     
1716 O O     . ALA A 231 ? 0.3467 0.3938 0.3698 -0.0246 0.0369  0.0555  231 ALA A O     
1717 C CB    . ALA A 231 ? 0.2817 0.3083 0.3006 -0.0237 0.0385  0.0476  231 ALA A CB    
1718 N N     . SER A 232 ? 0.3892 0.4478 0.4160 -0.0159 0.0362  0.0516  232 SER A N     
1719 C CA    . SER A 232 ? 0.2760 0.3485 0.3045 -0.0163 0.0350  0.0545  232 SER A CA    
1720 C C     . SER A 232 ? 0.4298 0.5092 0.4613 -0.0115 0.0351  0.0559  232 SER A C     
1721 O O     . SER A 232 ? 0.5346 0.6259 0.5676 -0.0115 0.0342  0.0585  232 SER A O     
1722 C CB    . SER A 232 ? 0.2899 0.3710 0.3182 -0.0156 0.0340  0.0528  232 SER A CB    
1723 O OG    . SER A 232 ? 0.4597 0.5393 0.4855 -0.0219 0.0335  0.0535  232 SER A OG    
1724 N N     . SER A 233 ? 0.6519 0.7251 0.6843 -0.0072 0.0361  0.0542  233 SER A N     
1725 C CA    . SER A 233 ? 0.6006 0.6805 0.6357 -0.0024 0.0361  0.0552  233 SER A CA    
1726 C C     . SER A 233 ? 0.5911 0.6638 0.6270 0.0015  0.0373  0.0535  233 SER A C     
1727 O O     . SER A 233 ? 0.6182 0.6811 0.6528 0.0018  0.0380  0.0508  233 SER A O     
1728 C CB    . SER A 233 ? 0.6070 0.6981 0.6432 0.0013  0.0352  0.0537  233 SER A CB    
1729 O OG    . SER A 233 ? 0.6323 0.7188 0.6678 0.0047  0.0356  0.0496  233 SER A OG    
1730 N N     . SER A 234 ? 0.4866 0.5649 0.5248 0.0047  0.0374  0.0551  234 SER A N     
1731 C CA    . SER A 234 ? 0.5453 0.6190 0.5846 0.0086  0.0383  0.0539  234 SER A CA    
1732 C C     . SER A 234 ? 0.6050 0.6815 0.6446 0.0132  0.0381  0.0501  234 SER A C     
1733 O O     . SER A 234 ? 0.5738 0.6475 0.6142 0.0164  0.0387  0.0490  234 SER A O     
1734 C CB    . SER A 234 ? 0.4752 0.5545 0.5167 0.0098  0.0385  0.0576  234 SER A CB    
1735 O OG    . SER A 234 ? 0.5385 0.6305 0.5811 0.0111  0.0374  0.0583  234 SER A OG    
1736 N N     . SER A 235 ? 0.7278 0.8099 0.7667 0.0136  0.0372  0.0483  235 SER A N     
1737 C CA    . SER A 235 ? 0.7519 0.8372 0.7907 0.0181  0.0369  0.0451  235 SER A CA    
1738 C C     . SER A 235 ? 0.7484 0.8242 0.7866 0.0199  0.0377  0.0420  235 SER A C     
1739 O O     . SER A 235 ? 0.8050 0.8822 0.8438 0.0235  0.0378  0.0405  235 SER A O     
1740 C CB    . SER A 235 ? 0.8170 0.9074 0.8544 0.0180  0.0360  0.0437  235 SER A CB    
1741 O OG    . SER A 235 ? 0.8151 0.9147 0.8531 0.0158  0.0353  0.0469  235 SER A OG    
1742 N N     . LEU A 236 ? 0.6446 0.7112 0.6815 0.0174  0.0382  0.0410  236 LEU A N     
1743 C CA    . LEU A 236 ? 0.6497 0.7074 0.6859 0.0189  0.0390  0.0382  236 LEU A CA    
1744 C C     . LEU A 236 ? 0.6976 0.7498 0.7349 0.0197  0.0402  0.0395  236 LEU A C     
1745 O O     . LEU A 236 ? 0.6412 0.6879 0.6783 0.0216  0.0408  0.0374  236 LEU A O     
1746 C CB    . LEU A 236 ? 0.6047 0.6551 0.6389 0.0162  0.0392  0.0364  236 LEU A CB    
1747 C CG    . LEU A 236 ? 0.6080 0.6633 0.6410 0.0151  0.0382  0.0352  236 LEU A CG    
1748 C CD1   . LEU A 236 ? 0.6311 0.6785 0.6621 0.0120  0.0385  0.0337  236 LEU A CD1   
1749 C CD2   . LEU A 236 ? 0.5247 0.5846 0.5576 0.0193  0.0377  0.0326  236 LEU A CD2   
1750 N N     . GLU A 237 ? 0.9420 0.9958 0.9804 0.0183  0.0405  0.0432  237 GLU A N     
1751 C CA    . GLU A 237 ? 0.8997 0.9491 0.9392 0.0195  0.0417  0.0450  237 GLU A CA    
1752 C C     . GLU A 237 ? 0.8554 0.9108 0.8966 0.0236  0.0416  0.0445  237 GLU A C     
1753 O O     . GLU A 237 ? 0.8447 0.9093 0.8867 0.0248  0.0406  0.0446  237 GLU A O     
1754 C CB    . GLU A 237 ? 0.9276 0.9773 0.9675 0.0169  0.0420  0.0493  237 GLU A CB    
1755 C CG    . GLU A 237 ? 0.9897 1.0328 1.0273 0.0123  0.0422  0.0499  237 GLU A CG    
1756 C CD    . GLU A 237 ? 1.0672 1.1098 1.1047 0.0094  0.0425  0.0543  237 GLU A CD    
1757 O OE1   . GLU A 237 ? 1.0887 1.1398 1.1284 0.0106  0.0421  0.0570  237 GLU A OE1   
1758 O OE2   . GLU A 237 ? 1.1110 1.1445 1.1462 0.0059  0.0432  0.0550  237 GLU A OE2   
1759 N N     . LYS A 238 ? 0.3958 0.4461 0.4375 0.0256  0.0426  0.0438  238 LYS A N     
1760 C CA    . LYS A 238 ? 0.3202 0.3756 0.3634 0.0289  0.0426  0.0437  238 LYS A CA    
1761 C C     . LYS A 238 ? 0.3653 0.4173 0.4098 0.0298  0.0440  0.0466  238 LYS A C     
1762 O O     . LYS A 238 ? 0.3461 0.3895 0.3897 0.0285  0.0452  0.0476  238 LYS A O     
1763 C CB    . LYS A 238 ? 0.2988 0.3526 0.3411 0.0309  0.0424  0.0396  238 LYS A CB    
1764 C CG    . LYS A 238 ? 0.3397 0.3972 0.3806 0.0308  0.0411  0.0368  238 LYS A CG    
1765 C CD    . LYS A 238 ? 0.3078 0.3710 0.3485 0.0336  0.0404  0.0347  238 LYS A CD    
1766 C CE    . LYS A 238 ? 0.3399 0.4068 0.3789 0.0339  0.0394  0.0324  238 LYS A CE    
1767 N NZ    . LYS A 238 ? 0.3690 0.4375 0.4065 0.0363  0.0389  0.0292  238 LYS A NZ    
1768 N N     . SER A 239 ? 0.5572 0.6160 0.6035 0.0321  0.0440  0.0483  239 SER A N     
1769 C CA    . SER A 239 ? 0.6063 0.6624 0.6539 0.0334  0.0455  0.0512  239 SER A CA    
1770 C C     . SER A 239 ? 0.4871 0.5429 0.5351 0.0361  0.0459  0.0492  239 SER A C     
1771 O O     . SER A 239 ? 0.4189 0.4773 0.4662 0.0368  0.0449  0.0458  239 SER A O     
1772 C CB    . SER A 239 ? 0.6113 0.6750 0.6610 0.0339  0.0454  0.0555  239 SER A CB    
1773 O OG    . SER A 239 ? 0.5485 0.6225 0.5997 0.0360  0.0446  0.0552  239 SER A OG    
1774 N N     . TYR A 240 ? 0.3433 0.3959 0.3922 0.0377  0.0474  0.0516  240 TYR A N     
1775 C CA    . TYR A 240 ? 0.4242 0.4761 0.4735 0.0400  0.0479  0.0502  240 TYR A CA    
1776 C C     . TYR A 240 ? 0.4596 0.5139 0.5108 0.0423  0.0493  0.0544  240 TYR A C     
1777 O O     . TYR A 240 ? 0.5196 0.5701 0.5709 0.0419  0.0504  0.0578  240 TYR A O     
1778 C CB    . TYR A 240 ? 0.4105 0.4522 0.4578 0.0394  0.0487  0.0475  240 TYR A CB    
1779 C CG    . TYR A 240 ? 0.4019 0.4428 0.4496 0.0418  0.0495  0.0466  240 TYR A CG    
1780 C CD1   . TYR A 240 ? 0.3952 0.4411 0.4428 0.0424  0.0483  0.0436  240 TYR A CD1   
1781 C CD2   . TYR A 240 ? 0.3789 0.4142 0.4267 0.0435  0.0514  0.0488  240 TYR A CD2   
1782 C CE1   . TYR A 240 ? 0.4370 0.4832 0.4850 0.0442  0.0490  0.0430  240 TYR A CE1   
1783 C CE2   . TYR A 240 ? 0.3824 0.4183 0.4308 0.0458  0.0522  0.0483  240 TYR A CE2   
1784 C CZ    . TYR A 240 ? 0.4419 0.4835 0.4905 0.0459  0.0509  0.0455  240 TYR A CZ    
1785 O OH    . TYR A 240 ? 0.5013 0.5441 0.5504 0.0478  0.0515  0.0451  240 TYR A OH    
1786 N N     . GLU A 241 ? 0.6681 0.7290 0.7208 0.0445  0.0492  0.0543  241 GLU A N     
1787 C CA    . GLU A 241 ? 0.7479 0.8134 0.8027 0.0469  0.0503  0.0585  241 GLU A CA    
1788 C C     . GLU A 241 ? 0.6421 0.7024 0.6968 0.0490  0.0519  0.0588  241 GLU A C     
1789 O O     . GLU A 241 ? 0.6423 0.7048 0.6969 0.0497  0.0515  0.0562  241 GLU A O     
1790 C CB    . GLU A 241 ? 0.8379 0.9156 0.8944 0.0478  0.0491  0.0587  241 GLU A CB    
1791 C CG    . GLU A 241 ? 0.9284 1.0126 0.9852 0.0464  0.0478  0.0593  241 GLU A CG    
1792 C CD    . GLU A 241 ? 0.9619 1.0439 1.0165 0.0442  0.0464  0.0552  241 GLU A CD    
1793 O OE1   . GLU A 241 ? 1.0008 1.0803 1.0540 0.0441  0.0459  0.0512  241 GLU A OE1   
1794 O OE2   . GLU A 241 ? 0.8993 0.9825 0.9538 0.0426  0.0458  0.0561  241 GLU A OE2   
1795 N N     . LEU A 242 ? 0.4839 0.5375 0.5384 0.0501  0.0538  0.0620  242 LEU A N     
1796 C CA    . LEU A 242 ? 0.4980 0.5462 0.5521 0.0526  0.0557  0.0625  242 LEU A CA    
1797 C C     . LEU A 242 ? 0.4431 0.5012 0.4997 0.0554  0.0559  0.0644  242 LEU A C     
1798 O O     . LEU A 242 ? 0.4370 0.5049 0.4953 0.0554  0.0548  0.0658  242 LEU A O     
1799 C CB    . LEU A 242 ? 0.5436 0.5828 0.5967 0.0537  0.0579  0.0661  242 LEU A CB    
1800 C CG    . LEU A 242 ? 0.5362 0.5642 0.5865 0.0509  0.0581  0.0649  242 LEU A CG    
1801 C CD1   . LEU A 242 ? 0.4803 0.4991 0.5291 0.0530  0.0607  0.0683  242 LEU A CD1   
1802 C CD2   . LEU A 242 ? 0.5364 0.5599 0.5848 0.0492  0.0572  0.0597  242 LEU A CD2   
1803 N N     . PRO A 243 ? 0.4391 0.4955 0.4957 0.0578  0.0572  0.0645  243 PRO A N     
1804 C CA    . PRO A 243 ? 0.4160 0.4827 0.4749 0.0604  0.0574  0.0668  243 PRO A CA    
1805 C C     . PRO A 243 ? 0.4499 0.5219 0.5108 0.0620  0.0582  0.0720  243 PRO A C     
1806 O O     . PRO A 243 ? 0.6003 0.6833 0.6630 0.0619  0.0571  0.0730  243 PRO A O     
1807 C CB    . PRO A 243 ? 0.4203 0.4825 0.4787 0.0631  0.0593  0.0672  243 PRO A CB    
1808 C CG    . PRO A 243 ? 0.5092 0.5574 0.5649 0.0625  0.0605  0.0662  243 PRO A CG    
1809 C CD    . PRO A 243 ? 0.5314 0.5771 0.5858 0.0584  0.0586  0.0628  243 PRO A CD    
1810 N N     . ASP A 244 ? 0.5436 0.6074 0.6037 0.0632  0.0600  0.0751  244 ASP A N     
1811 C CA    . ASP A 244 ? 0.6184 0.6864 0.6803 0.0657  0.0614  0.0809  244 ASP A CA    
1812 C C     . ASP A 244 ? 0.5944 0.6671 0.6572 0.0634  0.0600  0.0822  244 ASP A C     
1813 O O     . ASP A 244 ? 0.5153 0.5911 0.5795 0.0650  0.0610  0.0871  244 ASP A O     
1814 C CB    . ASP A 244 ? 0.5977 0.6543 0.6580 0.0683  0.0642  0.0840  244 ASP A CB    
1815 C CG    . ASP A 244 ? 0.6437 0.6882 0.7012 0.0655  0.0644  0.0834  244 ASP A CG    
1816 O OD1   . ASP A 244 ? 0.5963 0.6420 0.6535 0.0616  0.0624  0.0809  244 ASP A OD1   
1817 O OD2   . ASP A 244 ? 0.6491 0.6830 0.7045 0.0673  0.0667  0.0856  244 ASP A OD2   
1818 N N     . GLY A 245 ? 0.8689 0.9428 0.9310 0.0598  0.0578  0.0782  245 GLY A N     
1819 C CA    . GLY A 245 ? 0.8502 0.9303 0.9131 0.0577  0.0563  0.0791  245 GLY A CA    
1820 C C     . GLY A 245 ? 0.7691 0.8411 0.8301 0.0546  0.0560  0.0784  245 GLY A C     
1821 O O     . GLY A 245 ? 0.8127 0.8902 0.8741 0.0524  0.0543  0.0779  245 GLY A O     
1822 N N     . GLN A 246 ? 0.4718 0.5312 0.5304 0.0543  0.0574  0.0782  246 GLN A N     
1823 C CA    . GLN A 246 ? 0.5235 0.5753 0.5800 0.0508  0.0570  0.0775  246 GLN A CA    
1824 C C     . GLN A 246 ? 0.5772 0.6290 0.6325 0.0479  0.0550  0.0722  246 GLN A C     
1825 O O     . GLN A 246 ? 0.6226 0.6741 0.6775 0.0484  0.0546  0.0685  246 GLN A O     
1826 C CB    . GLN A 246 ? 0.4579 0.4959 0.5118 0.0511  0.0591  0.0788  246 GLN A CB    
1827 C CG    . GLN A 246 ? 0.5300 0.5669 0.5847 0.0553  0.0615  0.0834  246 GLN A CG    
1828 C CD    . GLN A 246 ? 0.5708 0.5930 0.6221 0.0561  0.0638  0.0843  246 GLN A CD    
1829 O OE1   . GLN A 246 ? 0.6442 0.6572 0.6927 0.0528  0.0639  0.0838  246 GLN A OE1   
1830 N NE2   . GLN A 246 ? 0.5245 0.5444 0.5759 0.0603  0.0658  0.0855  246 GLN A NE2   
1831 N N     . VAL A 247 ? 0.3936 0.4462 0.4483 0.0447  0.0537  0.0720  247 VAL A N     
1832 C CA    . VAL A 247 ? 0.4056 0.4592 0.4591 0.0420  0.0519  0.0676  247 VAL A CA    
1833 C C     . VAL A 247 ? 0.4456 0.4886 0.4964 0.0388  0.0522  0.0670  247 VAL A C     
1834 O O     . VAL A 247 ? 0.4080 0.4500 0.4584 0.0367  0.0523  0.0699  247 VAL A O     
1835 C CB    . VAL A 247 ? 0.5390 0.6040 0.5941 0.0410  0.0501  0.0679  247 VAL A CB    
1836 C CG1   . VAL A 247 ? 0.5949 0.6587 0.6483 0.0379  0.0486  0.0648  247 VAL A CG1   
1837 C CG2   . VAL A 247 ? 0.5492 0.6240 0.6060 0.0434  0.0493  0.0666  247 VAL A CG2   
1838 N N     . ILE A 248 ? 0.4224 0.4581 0.4712 0.0382  0.0523  0.0632  248 ILE A N     
1839 C CA    . ILE A 248 ? 0.3617 0.3868 0.4075 0.0351  0.0527  0.0620  248 ILE A CA    
1840 C C     . ILE A 248 ? 0.3642 0.3926 0.4093 0.0324  0.0507  0.0583  248 ILE A C     
1841 O O     . ILE A 248 ? 0.4275 0.4623 0.4736 0.0336  0.0495  0.0555  248 ILE A O     
1842 C CB    . ILE A 248 ? 0.4102 0.4248 0.4541 0.0367  0.0544  0.0605  248 ILE A CB    
1843 C CG1   . ILE A 248 ? 0.3226 0.3372 0.3659 0.0367  0.0535  0.0556  248 ILE A CG1   
1844 C CG2   . ILE A 248 ? 0.3581 0.3739 0.4036 0.0410  0.0561  0.0634  248 ILE A CG2   
1845 C CD1   . ILE A 248 ? 0.2780 0.2845 0.3199 0.0386  0.0552  0.0545  248 ILE A CD1   
1846 N N     . THR A 249 ? 0.4432 0.4673 0.4863 0.0287  0.0503  0.0585  249 THR A N     
1847 C CA    . THR A 249 ? 0.4504 0.4783 0.4928 0.0262  0.0485  0.0556  249 THR A CA    
1848 C C     . THR A 249 ? 0.5071 0.5263 0.5469 0.0244  0.0487  0.0520  249 THR A C     
1849 O O     . THR A 249 ? 0.5199 0.5289 0.5574 0.0230  0.0500  0.0525  249 THR A O     
1850 C CB    . THR A 249 ? 0.4608 0.4924 0.5031 0.0228  0.0477  0.0582  249 THR A CB    
1851 O OG1   . THR A 249 ? 0.6093 0.6500 0.6542 0.0245  0.0474  0.0615  249 THR A OG1   
1852 C CG2   . THR A 249 ? 0.4472 0.4839 0.4889 0.0208  0.0459  0.0554  249 THR A CG2   
1853 N N     . ILE A 250 ? 0.4809 0.5040 0.5207 0.0246  0.0474  0.0484  250 ILE A N     
1854 C CA    . ILE A 250 ? 0.4172 0.4335 0.4548 0.0235  0.0474  0.0447  250 ILE A CA    
1855 C C     . ILE A 250 ? 0.5288 0.5484 0.5653 0.0203  0.0459  0.0433  250 ILE A C     
1856 O O     . ILE A 250 ? 0.4679 0.4965 0.5056 0.0212  0.0445  0.0426  250 ILE A O     
1857 C CB    . ILE A 250 ? 0.4017 0.4190 0.4400 0.0266  0.0474  0.0417  250 ILE A CB    
1858 C CG1   . ILE A 250 ? 0.4804 0.4971 0.5201 0.0298  0.0487  0.0436  250 ILE A CG1   
1859 C CG2   . ILE A 250 ? 0.4346 0.4437 0.4706 0.0257  0.0478  0.0384  250 ILE A CG2   
1860 C CD1   . ILE A 250 ? 0.5832 0.5889 0.6212 0.0299  0.0507  0.0446  250 ILE A CD1   
1861 N N     . GLY A 251 ? 0.6499 0.6625 0.6840 0.0168  0.0462  0.0431  251 GLY A N     
1862 C CA    . GLY A 251 ? 0.5776 0.5923 0.6102 0.0132  0.0449  0.0422  251 GLY A CA    
1863 C C     . GLY A 251 ? 0.6045 0.6156 0.6355 0.0129  0.0446  0.0382  251 GLY A C     
1864 O O     . GLY A 251 ? 0.5645 0.5776 0.5964 0.0159  0.0444  0.0357  251 GLY A O     
1865 N N     . ASN A 252 ? 0.5575 0.5642 0.5861 0.0088  0.0445  0.0377  252 ASN A N     
1866 C CA    . ASN A 252 ? 0.5022 0.5045 0.5288 0.0078  0.0443  0.0342  252 ASN A CA    
1867 C C     . ASN A 252 ? 0.5656 0.5591 0.5914 0.0100  0.0457  0.0322  252 ASN A C     
1868 O O     . ASN A 252 ? 0.5775 0.5676 0.6018 0.0096  0.0456  0.0292  252 ASN A O     
1869 C CB    . ASN A 252 ? 0.4642 0.4628 0.4880 0.0025  0.0441  0.0347  252 ASN A CB    
1870 C CG    . ASN A 252 ? 0.4299 0.4199 0.4518 0.0002  0.0454  0.0371  252 ASN A CG    
1871 O OD1   . ASN A 252 ? 0.4248 0.4077 0.4466 0.0026  0.0470  0.0372  252 ASN A OD1   
1872 N ND2   . ASN A 252 ? 0.4819 0.4726 0.5023 -0.0045 0.0449  0.0392  252 ASN A ND2   
1873 N N     . GLU A 253 ? 0.5025 0.4919 0.5289 0.0122  0.0471  0.0340  253 GLU A N     
1874 C CA    . GLU A 253 ? 0.3988 0.3828 0.4252 0.0153  0.0483  0.0322  253 GLU A CA    
1875 C C     . GLU A 253 ? 0.3895 0.3798 0.4177 0.0182  0.0474  0.0297  253 GLU A C     
1876 O O     . GLU A 253 ? 0.4144 0.4008 0.4420 0.0197  0.0479  0.0273  253 GLU A O     
1877 C CB    . GLU A 253 ? 0.4250 0.4067 0.4525 0.0179  0.0498  0.0351  253 GLU A CB    
1878 C CG    . GLU A 253 ? 0.4977 0.4697 0.5225 0.0159  0.0514  0.0372  253 GLU A CG    
1879 C CD    . GLU A 253 ? 0.5477 0.5227 0.5726 0.0130  0.0509  0.0405  253 GLU A CD    
1880 O OE1   . GLU A 253 ? 0.5345 0.5197 0.5617 0.0128  0.0493  0.0412  253 GLU A OE1   
1881 O OE2   . GLU A 253 ? 0.5703 0.5370 0.5927 0.0110  0.0521  0.0425  253 GLU A OE2   
1882 N N     . ARG A 254 ? 0.4688 0.4689 0.4989 0.0189  0.0460  0.0302  254 ARG A N     
1883 C CA    . ARG A 254 ? 0.4302 0.4360 0.4615 0.0217  0.0451  0.0280  254 ARG A CA    
1884 C C     . ARG A 254 ? 0.4002 0.4033 0.4298 0.0209  0.0446  0.0245  254 ARG A C     
1885 O O     . ARG A 254 ? 0.4200 0.4224 0.4497 0.0230  0.0446  0.0223  254 ARG A O     
1886 C CB    . ARG A 254 ? 0.4360 0.4519 0.4688 0.0223  0.0438  0.0291  254 ARG A CB    
1887 C CG    . ARG A 254 ? 0.3957 0.4158 0.4305 0.0237  0.0441  0.0323  254 ARG A CG    
1888 C CD    . ARG A 254 ? 0.3662 0.3968 0.4024 0.0248  0.0429  0.0330  254 ARG A CD    
1889 N NE    . ARG A 254 ? 0.2990 0.3332 0.3352 0.0274  0.0422  0.0302  254 ARG A NE    
1890 C CZ    . ARG A 254 ? 0.3561 0.3952 0.3915 0.0277  0.0411  0.0285  254 ARG A CZ    
1891 N NH1   . ARG A 254 ? 0.4547 0.4968 0.4896 0.0257  0.0404  0.0295  254 ARG A NH1   
1892 N NH2   . ARG A 254 ? 0.2932 0.3343 0.3281 0.0300  0.0406  0.0259  254 ARG A NH2   
1893 N N     . PHE A 255 ? 0.4966 0.4993 0.5247 0.0178  0.0440  0.0241  255 PHE A N     
1894 C CA    . PHE A 255 ? 0.5646 0.5649 0.5910 0.0170  0.0436  0.0211  255 PHE A CA    
1895 C C     . PHE A 255 ? 0.4837 0.4746 0.5078 0.0145  0.0446  0.0201  255 PHE A C     
1896 O O     . PHE A 255 ? 0.3940 0.3822 0.4169 0.0142  0.0445  0.0175  255 PHE A O     
1897 C CB    . PHE A 255 ? 0.6270 0.6342 0.6530 0.0156  0.0422  0.0209  255 PHE A CB    
1898 C CG    . PHE A 255 ? 0.6291 0.6390 0.6550 0.0124  0.0419  0.0238  255 PHE A CG    
1899 C CD1   . PHE A 255 ? 0.5339 0.5504 0.5617 0.0133  0.0415  0.0264  255 PHE A CD1   
1900 C CD2   . PHE A 255 ? 0.6046 0.6105 0.6284 0.0083  0.0419  0.0238  255 PHE A CD2   
1901 C CE1   . PHE A 255 ? 0.4757 0.4949 0.5033 0.0101  0.0412  0.0292  255 PHE A CE1   
1902 C CE2   . PHE A 255 ? 0.5858 0.5942 0.6093 0.0049  0.0416  0.0265  255 PHE A CE2   
1903 C CZ    . PHE A 255 ? 0.5677 0.5827 0.5931 0.0058  0.0412  0.0292  255 PHE A CZ    
1904 N N     . ARG A 256 ? 0.3520 0.3375 0.3753 0.0127  0.0456  0.0222  256 ARG A N     
1905 C CA    . ARG A 256 ? 0.3768 0.3523 0.3972 0.0108  0.0468  0.0209  256 ARG A CA    
1906 C C     . ARG A 256 ? 0.4469 0.4174 0.4674 0.0139  0.0480  0.0193  256 ARG A C     
1907 O O     . ARG A 256 ? 0.5157 0.4792 0.5341 0.0130  0.0488  0.0173  256 ARG A O     
1908 C CB    . ARG A 256 ? 0.3792 0.3488 0.3979 0.0081  0.0478  0.0234  256 ARG A CB    
1909 C CG    . ARG A 256 ? 0.3744 0.3476 0.3922 0.0039  0.0467  0.0249  256 ARG A CG    
1910 C CD    . ARG A 256 ? 0.4583 0.4276 0.4753 0.0022  0.0476  0.0281  256 ARG A CD    
1911 N NE    . ARG A 256 ? 0.4822 0.4392 0.4961 0.0014  0.0495  0.0277  256 ARG A NE    
1912 C CZ    . ARG A 256 ? 0.3674 0.3186 0.3803 0.0016  0.0509  0.0303  256 ARG A CZ    
1913 N NH1   . ARG A 256 ? 0.3971 0.3542 0.4123 0.0023  0.0505  0.0336  256 ARG A NH1   
1914 N NH2   . ARG A 256 ? 0.3136 0.2529 0.3230 0.0012  0.0527  0.0298  256 ARG A NH2   
1915 N N     . CYS A 257 ? 0.5538 0.5279 0.5768 0.0175  0.0482  0.0202  257 CYS A N     
1916 C CA    . CYS A 257 ? 0.5409 0.5119 0.5642 0.0205  0.0492  0.0188  257 CYS A CA    
1917 C C     . CYS A 257 ? 0.5679 0.5399 0.5908 0.0207  0.0483  0.0155  257 CYS A C     
1918 O O     . CYS A 257 ? 0.6378 0.6035 0.6588 0.0203  0.0491  0.0137  257 CYS A O     
1919 C CB    . CYS A 257 ? 0.5802 0.5563 0.6062 0.0239  0.0494  0.0207  257 CYS A CB    
1920 S SG    . CYS A 257 ? 0.5060 0.4815 0.5330 0.0276  0.0502  0.0193  257 CYS A SG    
1921 N N     . PRO A 258 ? 0.3959 0.3752 0.4199 0.0213  0.0468  0.0146  258 PRO A N     
1922 C CA    . PRO A 258 ? 0.4339 0.4135 0.4572 0.0216  0.0461  0.0116  258 PRO A CA    
1923 C C     . PRO A 258 ? 0.4261 0.4024 0.4472 0.0186  0.0458  0.0101  258 PRO A C     
1924 O O     . PRO A 258 ? 0.3202 0.2948 0.3404 0.0188  0.0457  0.0078  258 PRO A O     
1925 C CB    . PRO A 258 ? 0.4590 0.4467 0.4836 0.0231  0.0447  0.0115  258 PRO A CB    
1926 C CG    . PRO A 258 ? 0.4433 0.4350 0.4698 0.0242  0.0448  0.0142  258 PRO A CG    
1927 C CD    . PRO A 258 ? 0.4077 0.3950 0.4336 0.0221  0.0458  0.0162  258 PRO A CD    
1928 N N     . GLU A 259 ? 0.4937 0.4695 0.5138 0.0157  0.0457  0.0115  259 GLU A N     
1929 C CA    . GLU A 259 ? 0.4322 0.4050 0.4499 0.0122  0.0455  0.0104  259 GLU A CA    
1930 C C     . GLU A 259 ? 0.5885 0.5524 0.6041 0.0117  0.0469  0.0087  259 GLU A C     
1931 O O     . GLU A 259 ? 0.6928 0.6548 0.7066 0.0096  0.0466  0.0068  259 GLU A O     
1932 C CB    . GLU A 259 ? 0.3747 0.3478 0.3916 0.0089  0.0454  0.0127  259 GLU A CB    
1933 C CG    . GLU A 259 ? 0.3710 0.3452 0.3860 0.0049  0.0446  0.0121  259 GLU A CG    
1934 C CD    . GLU A 259 ? 0.4646 0.4462 0.4804 0.0058  0.0432  0.0108  259 GLU A CD    
1935 O OE1   . GLU A 259 ? 0.3321 0.3208 0.3500 0.0087  0.0424  0.0114  259 GLU A OE1   
1936 O OE2   . GLU A 259 ? 0.5421 0.5222 0.5561 0.0038  0.0430  0.0091  259 GLU A OE2   
1937 N N     . ALA A 260 ? 0.5666 0.5254 0.5824 0.0136  0.0484  0.0094  260 ALA A N     
1938 C CA    . ALA A 260 ? 0.4841 0.4350 0.4979 0.0139  0.0497  0.0076  260 ALA A CA    
1939 C C     . ALA A 260 ? 0.4949 0.4474 0.5089 0.0152  0.0492  0.0050  260 ALA A C     
1940 O O     . ALA A 260 ? 0.4490 0.3960 0.4611 0.0146  0.0500  0.0032  260 ALA A O     
1941 C CB    . ALA A 260 ? 0.3539 0.3005 0.3682 0.0168  0.0515  0.0091  260 ALA A CB    
1942 N N     . LEU A 261 ? 0.3651 0.3249 0.3813 0.0168  0.0479  0.0048  261 LEU A N     
1943 C CA    . LEU A 261 ? 0.3416 0.3026 0.3577 0.0177  0.0473  0.0024  261 LEU A CA    
1944 C C     . LEU A 261 ? 0.3221 0.2831 0.3364 0.0149  0.0465  0.0010  261 LEU A C     
1945 O O     . LEU A 261 ? 0.3313 0.2890 0.3441 0.0143  0.0468  -0.0010 261 LEU A O     
1946 C CB    . LEU A 261 ? 0.3616 0.3293 0.3798 0.0202  0.0461  0.0025  261 LEU A CB    
1947 C CG    . LEU A 261 ? 0.3720 0.3405 0.3920 0.0230  0.0469  0.0038  261 LEU A CG    
1948 C CD1   . LEU A 261 ? 0.2428 0.2179 0.2644 0.0248  0.0457  0.0041  261 LEU A CD1   
1949 C CD2   . LEU A 261 ? 0.2859 0.2499 0.3055 0.0242  0.0480  0.0027  261 LEU A CD2   
1950 N N     . PHE A 262 ? 0.3774 0.3425 0.3916 0.0129  0.0455  0.0021  262 PHE A N     
1951 C CA    . PHE A 262 ? 0.4047 0.3711 0.4173 0.0100  0.0448  0.0012  262 PHE A CA    
1952 C C     . PHE A 262 ? 0.3924 0.3527 0.4024 0.0063  0.0456  0.0011  262 PHE A C     
1953 O O     . PHE A 262 ? 0.5021 0.4612 0.5102 0.0040  0.0454  -0.0004 262 PHE A O     
1954 C CB    . PHE A 262 ? 0.3425 0.3171 0.3562 0.0097  0.0434  0.0026  262 PHE A CB    
1955 C CG    . PHE A 262 ? 0.3423 0.3221 0.3578 0.0133  0.0427  0.0024  262 PHE A CG    
1956 C CD1   . PHE A 262 ? 0.3412 0.3227 0.3585 0.0156  0.0428  0.0037  262 PHE A CD1   
1957 C CD2   . PHE A 262 ? 0.3241 0.3064 0.3391 0.0144  0.0419  0.0009  262 PHE A CD2   
1958 C CE1   . PHE A 262 ? 0.3729 0.3585 0.3912 0.0185  0.0422  0.0033  262 PHE A CE1   
1959 C CE2   . PHE A 262 ? 0.3838 0.3697 0.3998 0.0175  0.0413  0.0005  262 PHE A CE2   
1960 C CZ    . PHE A 262 ? 0.3721 0.3595 0.3896 0.0195  0.0415  0.0016  262 PHE A CZ    
1961 N N     . GLN A 263 ? 0.2745 0.2307 0.2842 0.0058  0.0466  0.0027  263 GLN A N     
1962 C CA    . GLN A 263 ? 0.2719 0.2210 0.2785 0.0023  0.0475  0.0027  263 GLN A CA    
1963 C C     . GLN A 263 ? 0.2958 0.2368 0.3015 0.0043  0.0494  0.0027  263 GLN A C     
1964 O O     . GLN A 263 ? 0.3548 0.2943 0.3611 0.0050  0.0501  0.0048  263 GLN A O     
1965 C CB    . GLN A 263 ? 0.3555 0.3071 0.3618 -0.0007 0.0470  0.0050  263 GLN A CB    
1966 C CG    . GLN A 263 ? 0.3357 0.2959 0.3425 -0.0028 0.0452  0.0054  263 GLN A CG    
1967 C CD    . GLN A 263 ? 0.3285 0.2901 0.3342 -0.0070 0.0448  0.0076  263 GLN A CD    
1968 O OE1   . GLN A 263 ? 0.4077 0.3774 0.4152 -0.0070 0.0437  0.0095  263 GLN A OE1   
1969 N NE2   . GLN A 263 ? 0.3305 0.2841 0.3327 -0.0108 0.0457  0.0073  263 GLN A NE2   
1970 N N     . PRO A 264 ? 0.4916 0.4272 0.4958 0.0051  0.0504  0.0004  264 PRO A N     
1971 C CA    . PRO A 264 ? 0.4212 0.3498 0.4247 0.0078  0.0523  0.0006  264 PRO A CA    
1972 C C     . PRO A 264 ? 0.4788 0.3983 0.4786 0.0055  0.0539  0.0011  264 PRO A C     
1973 O O     . PRO A 264 ? 0.4223 0.3358 0.4213 0.0081  0.0557  0.0017  264 PRO A O     
1974 C CB    . PRO A 264 ? 0.4079 0.3350 0.4109 0.0093  0.0527  -0.0019 264 PRO A CB    
1975 C CG    . PRO A 264 ? 0.3868 0.3212 0.3912 0.0084  0.0508  -0.0030 264 PRO A CG    
1976 C CD    . PRO A 264 ? 0.4136 0.3496 0.4168 0.0044  0.0499  -0.0022 264 PRO A CD    
1977 N N     . SER A 265 ? 0.6895 0.6080 0.6869 0.0009  0.0532  0.0011  265 SER A N     
1978 C CA    . SER A 265 ? 0.6913 0.6005 0.6846 -0.0022 0.0545  0.0015  265 SER A CA    
1979 C C     . SER A 265 ? 0.6372 0.5448 0.6313 -0.0007 0.0553  0.0045  265 SER A C     
1980 O O     . SER A 265 ? 0.6565 0.5550 0.6472 -0.0018 0.0568  0.0052  265 SER A O     
1981 C CB    . SER A 265 ? 0.6690 0.5802 0.6601 -0.0080 0.0531  0.0013  265 SER A CB    
1982 O OG    . SER A 265 ? 0.6330 0.5540 0.6273 -0.0086 0.0513  0.0034  265 SER A OG    
1983 N N     . PHE A 266 ? 0.5252 0.4415 0.5237 0.0019  0.0542  0.0063  266 PHE A N     
1984 C CA    . PHE A 266 ? 0.4101 0.3265 0.4099 0.0033  0.0548  0.0095  266 PHE A CA    
1985 C C     . PHE A 266 ? 0.3978 0.3066 0.3968 0.0071  0.0571  0.0102  266 PHE A C     
1986 O O     . PHE A 266 ? 0.5346 0.4380 0.5321 0.0070  0.0583  0.0124  266 PHE A O     
1987 C CB    . PHE A 266 ? 0.4208 0.3487 0.4255 0.0055  0.0532  0.0109  266 PHE A CB    
1988 C CG    . PHE A 266 ? 0.4047 0.3400 0.4101 0.0020  0.0512  0.0115  266 PHE A CG    
1989 C CD1   . PHE A 266 ? 0.3846 0.3171 0.3867 -0.0030 0.0507  0.0106  266 PHE A CD1   
1990 C CD2   . PHE A 266 ? 0.4371 0.3823 0.4461 0.0037  0.0498  0.0131  266 PHE A CD2   
1991 C CE1   . PHE A 266 ? 0.3827 0.3232 0.3855 -0.0062 0.0489  0.0114  266 PHE A CE1   
1992 C CE2   . PHE A 266 ? 0.4454 0.3979 0.4550 0.0008  0.0481  0.0138  266 PHE A CE2   
1993 C CZ    . PHE A 266 ? 0.3979 0.3483 0.4045 -0.0041 0.0477  0.0131  266 PHE A CZ    
1994 N N     . LEU A 267 ? 0.5515 0.4597 0.5511 0.0104  0.0578  0.0084  267 LEU A N     
1995 C CA    . LEU A 267 ? 0.5142 0.4158 0.5128 0.0144  0.0602  0.0089  267 LEU A CA    
1996 C C     . LEU A 267 ? 0.5853 0.4763 0.5789 0.0133  0.0618  0.0065  267 LEU A C     
1997 O O     . LEU A 267 ? 0.6244 0.5104 0.6170 0.0169  0.0638  0.0063  267 LEU A O     
1998 C CB    . LEU A 267 ? 0.4776 0.3862 0.4801 0.0190  0.0600  0.0088  267 LEU A CB    
1999 C CG    . LEU A 267 ? 0.5138 0.4307 0.5207 0.0217  0.0593  0.0115  267 LEU A CG    
2000 C CD1   . LEU A 267 ? 0.5288 0.4546 0.5391 0.0234  0.0578  0.0102  267 LEU A CD1   
2001 C CD2   . LEU A 267 ? 0.6217 0.5347 0.6286 0.0257  0.0615  0.0139  267 LEU A CD2   
2002 N N     . GLY A 268 ? 0.4263 0.3151 0.4170 0.0084  0.0609  0.0045  268 GLY A N     
2003 C CA    . GLY A 268 ? 0.4952 0.3739 0.4808 0.0069  0.0624  0.0021  268 GLY A CA    
2004 C C     . GLY A 268 ? 0.5183 0.3983 0.5041 0.0085  0.0625  -0.0008 268 GLY A C     
2005 O O     . GLY A 268 ? 0.5547 0.4269 0.5373 0.0101  0.0644  -0.0022 268 GLY A O     
2006 N N     . MET A 269 ? 0.6409 0.5306 0.6302 0.0080  0.0604  -0.0017 269 MET A N     
2007 C CA    . MET A 269 ? 0.6800 0.5717 0.6698 0.0094  0.0602  -0.0041 269 MET A CA    
2008 C C     . MET A 269 ? 0.6666 0.5620 0.6557 0.0051  0.0584  -0.0060 269 MET A C     
2009 O O     . MET A 269 ? 0.5386 0.4411 0.5299 0.0032  0.0565  -0.0051 269 MET A O     
2010 C CB    . MET A 269 ? 0.7269 0.6269 0.7217 0.0138  0.0596  -0.0031 269 MET A CB    
2011 C CG    . MET A 269 ? 0.7732 0.6791 0.7698 0.0145  0.0584  -0.0051 269 MET A CG    
2012 S SD    . MET A 269 ? 0.7682 0.6813 0.7696 0.0197  0.0584  -0.0036 269 MET A SD    
2013 C CE    . MET A 269 ? 0.7464 0.6660 0.7509 0.0194  0.0569  -0.0008 269 MET A CE    
2014 N N     . GLU A 270 ? 0.8126 0.7031 0.7983 0.0035  0.0590  -0.0087 270 GLU A N     
2015 C CA    . GLU A 270 ? 0.8604 0.7552 0.8455 -0.0003 0.0573  -0.0104 270 GLU A CA    
2016 C C     . GLU A 270 ? 0.8965 0.7982 0.8851 0.0027  0.0565  -0.0113 270 GLU A C     
2017 O O     . GLU A 270 ? 0.9381 0.8371 0.9257 0.0045  0.0575  -0.0130 270 GLU A O     
2018 C CB    . GLU A 270 ? 0.8857 0.7725 0.8653 -0.0041 0.0582  -0.0129 270 GLU A CB    
2019 C CG    . GLU A 270 ? 0.9340 0.8256 0.9132 -0.0070 0.0568  -0.0150 270 GLU A CG    
2020 C CD    . GLU A 270 ? 0.9916 0.8930 0.9735 -0.0095 0.0544  -0.0138 270 GLU A CD    
2021 O OE1   . GLU A 270 ? 0.9732 0.8742 0.9534 -0.0136 0.0538  -0.0128 270 GLU A OE1   
2022 O OE2   . GLU A 270 ? 1.0208 0.9304 1.0064 -0.0075 0.0531  -0.0138 270 GLU A OE2   
2023 N N     . SER A 271 ? 1.1802 1.0908 1.1728 0.0035  0.0548  -0.0099 271 SER A N     
2024 C CA    . SER A 271 ? 1.1410 1.0580 1.1365 0.0060  0.0538  -0.0106 271 SER A CA    
2025 C C     . SER A 271 ? 1.0917 1.0161 1.0888 0.0037  0.0518  -0.0101 271 SER A C     
2026 O O     . SER A 271 ? 1.1964 1.1207 1.1920 0.0004  0.0513  -0.0093 271 SER A O     
2027 C CB    . SER A 271 ? 1.1174 1.0376 1.1165 0.0103  0.0540  -0.0089 271 SER A CB    
2028 O OG    . SER A 271 ? 1.0918 1.0161 1.0928 0.0126  0.0535  -0.0099 271 SER A OG    
2029 N N     . CYS A 272 ? 0.7003 0.6310 0.7000 0.0057  0.0506  -0.0103 272 CYS A N     
2030 C CA    . CYS A 272 ? 0.6894 0.6272 0.6903 0.0043  0.0488  -0.0097 272 CYS A CA    
2031 C C     . CYS A 272 ? 0.6425 0.5850 0.6466 0.0073  0.0483  -0.0081 272 CYS A C     
2032 O O     . CYS A 272 ? 0.5872 0.5285 0.5927 0.0104  0.0490  -0.0078 272 CYS A O     
2033 C CB    . CYS A 272 ? 0.8916 0.8323 0.8924 0.0043  0.0481  -0.0115 272 CYS A CB    
2034 S SG    . CYS A 272 ? 1.0310 0.9665 1.0279 0.0006  0.0488  -0.0137 272 CYS A SG    
2035 N N     . GLY A 273 ? 0.6316 0.5802 0.6369 0.0065  0.0470  -0.0068 273 GLY A N     
2036 C CA    . GLY A 273 ? 0.6656 0.6191 0.6737 0.0092  0.0463  -0.0053 273 GLY A CA    
2037 C C     . GLY A 273 ? 0.6397 0.5970 0.6492 0.0118  0.0456  -0.0062 273 GLY A C     
2038 O O     . GLY A 273 ? 0.6994 0.6570 0.7079 0.0112  0.0452  -0.0076 273 GLY A O     
2039 N N     . ILE A 274 ? 0.4250 0.3853 0.4365 0.0144  0.0453  -0.0052 274 ILE A N     
2040 C CA    . ILE A 274 ? 0.3622 0.3253 0.3747 0.0168  0.0446  -0.0061 274 ILE A CA    
2041 C C     . ILE A 274 ? 0.3137 0.2807 0.3255 0.0164  0.0434  -0.0068 274 ILE A C     
2042 O O     . ILE A 274 ? 0.2939 0.2610 0.3055 0.0176  0.0431  -0.0080 274 ILE A O     
2043 C CB    . ILE A 274 ? 0.3752 0.3411 0.3896 0.0193  0.0445  -0.0048 274 ILE A CB    
2044 C CG1   . ILE A 274 ? 0.3634 0.3341 0.3786 0.0190  0.0437  -0.0031 274 ILE A CG1   
2045 C CG2   . ILE A 274 ? 0.3830 0.3452 0.3981 0.0202  0.0458  -0.0040 274 ILE A CG2   
2046 C CD1   . ILE A 274 ? 0.3154 0.2896 0.3323 0.0214  0.0434  -0.0021 274 ILE A CD1   
2047 N N     . HIS A 275 ? 0.2543 0.2249 0.2658 0.0149  0.0428  -0.0058 275 HIS A N     
2048 C CA    . HIS A 275 ? 0.2428 0.2175 0.2536 0.0145  0.0418  -0.0062 275 HIS A CA    
2049 C C     . HIS A 275 ? 0.4167 0.3889 0.4258 0.0125  0.0420  -0.0076 275 HIS A C     
2050 O O     . HIS A 275 ? 0.4656 0.4391 0.4741 0.0135  0.0415  -0.0085 275 HIS A O     
2051 C CB    . HIS A 275 ? 0.2583 0.2384 0.2692 0.0132  0.0411  -0.0045 275 HIS A CB    
2052 C CG    . HIS A 275 ? 0.3065 0.2846 0.3167 0.0098  0.0416  -0.0036 275 HIS A CG    
2053 N ND1   . HIS A 275 ? 0.3215 0.2943 0.3319 0.0093  0.0426  -0.0033 275 HIS A ND1   
2054 C CD2   . HIS A 275 ? 0.3278 0.3087 0.3370 0.0066  0.0412  -0.0028 275 HIS A CD2   
2055 C CE1   . HIS A 275 ? 0.2810 0.2523 0.2901 0.0058  0.0429  -0.0025 275 HIS A CE1   
2056 N NE2   . HIS A 275 ? 0.3485 0.3249 0.3569 0.0039  0.0419  -0.0022 275 HIS A NE2   
2057 N N     . GLU A 276 ? 0.5197 0.4879 0.5276 0.0097  0.0427  -0.0078 276 GLU A N     
2058 C CA    . GLU A 276 ? 0.4529 0.4185 0.4590 0.0076  0.0430  -0.0093 276 GLU A CA    
2059 C C     . GLU A 276 ? 0.5166 0.4783 0.5227 0.0095  0.0436  -0.0109 276 GLU A C     
2060 O O     . GLU A 276 ? 0.5873 0.5491 0.5924 0.0091  0.0435  -0.0120 276 GLU A O     
2061 C CB    . GLU A 276 ? 0.5855 0.5470 0.5899 0.0041  0.0438  -0.0092 276 GLU A CB    
2062 C CG    . GLU A 276 ? 0.6892 0.6550 0.6934 0.0016  0.0431  -0.0075 276 GLU A CG    
2063 C CD    . GLU A 276 ? 0.6620 0.6229 0.6650 -0.0009 0.0440  -0.0068 276 GLU A CD    
2064 O OE1   . GLU A 276 ? 0.5846 0.5398 0.5877 0.0007  0.0451  -0.0069 276 GLU A OE1   
2065 O OE2   . GLU A 276 ? 0.6836 0.6463 0.6853 -0.0045 0.0435  -0.0058 276 GLU A OE2   
2066 N N     . THR A 277 ? 0.3473 0.3062 0.3545 0.0116  0.0443  -0.0107 277 THR A N     
2067 C CA    . THR A 277 ? 0.2928 0.2492 0.3002 0.0135  0.0448  -0.0118 277 THR A CA    
2068 C C     . THR A 277 ? 0.3580 0.3180 0.3660 0.0152  0.0438  -0.0122 277 THR A C     
2069 O O     . THR A 277 ? 0.3873 0.3460 0.3946 0.0155  0.0438  -0.0133 277 THR A O     
2070 C CB    . THR A 277 ? 0.3133 0.2673 0.3220 0.0153  0.0458  -0.0111 277 THR A CB    
2071 O OG1   . THR A 277 ? 0.3829 0.3327 0.3906 0.0139  0.0469  -0.0107 277 THR A OG1   
2072 C CG2   . THR A 277 ? 0.4480 0.4002 0.4569 0.0170  0.0463  -0.0120 277 THR A CG2   
2073 N N     . THR A 278 ? 0.2919 0.2561 0.3007 0.0164  0.0429  -0.0112 278 THR A N     
2074 C CA    . THR A 278 ? 0.2599 0.2267 0.2686 0.0182  0.0420  -0.0115 278 THR A CA    
2075 C C     . THR A 278 ? 0.3457 0.3141 0.3530 0.0171  0.0415  -0.0120 278 THR A C     
2076 O O     . THR A 278 ? 0.4042 0.3719 0.4107 0.0178  0.0413  -0.0128 278 THR A O     
2077 C CB    . THR A 278 ? 0.2634 0.2341 0.2727 0.0199  0.0412  -0.0103 278 THR A CB    
2078 O OG1   . THR A 278 ? 0.3577 0.3276 0.3685 0.0208  0.0417  -0.0097 278 THR A OG1   
2079 C CG2   . THR A 278 ? 0.2916 0.2636 0.3001 0.0220  0.0405  -0.0109 278 THR A CG2   
2080 N N     . PHE A 279 ? 0.2454 0.2161 0.2523 0.0151  0.0414  -0.0113 279 PHE A N     
2081 C CA    . PHE A 279 ? 0.3478 0.3208 0.3534 0.0137  0.0410  -0.0116 279 PHE A CA    
2082 C C     . PHE A 279 ? 0.3217 0.2906 0.3263 0.0124  0.0416  -0.0132 279 PHE A C     
2083 O O     . PHE A 279 ? 0.3096 0.2793 0.3134 0.0128  0.0412  -0.0137 279 PHE A O     
2084 C CB    . PHE A 279 ? 0.4095 0.3862 0.4147 0.0111  0.0407  -0.0105 279 PHE A CB    
2085 C CG    . PHE A 279 ? 0.3922 0.3721 0.3960 0.0092  0.0403  -0.0106 279 PHE A CG    
2086 C CD1   . PHE A 279 ? 0.3358 0.3205 0.3394 0.0112  0.0396  -0.0099 279 PHE A CD1   
2087 C CD2   . PHE A 279 ? 0.3603 0.3385 0.3629 0.0055  0.0407  -0.0112 279 PHE A CD2   
2088 C CE1   . PHE A 279 ? 0.3124 0.3009 0.3150 0.0097  0.0393  -0.0097 279 PHE A CE1   
2089 C CE2   . PHE A 279 ? 0.3180 0.2999 0.3193 0.0034  0.0403  -0.0113 279 PHE A CE2   
2090 C CZ    . PHE A 279 ? 0.2988 0.2863 0.3003 0.0056  0.0395  -0.0104 279 PHE A CZ    
2091 N N     . ASN A 280 ? 0.3195 0.2839 0.3239 0.0109  0.0425  -0.0138 280 ASN A N     
2092 C CA    . ASN A 280 ? 0.3189 0.2795 0.3221 0.0098  0.0433  -0.0153 280 ASN A CA    
2093 C C     . ASN A 280 ? 0.3775 0.3367 0.3812 0.0121  0.0433  -0.0160 280 ASN A C     
2094 O O     . ASN A 280 ? 0.3621 0.3207 0.3648 0.0115  0.0433  -0.0170 280 ASN A O     
2095 C CB    . ASN A 280 ? 0.3243 0.2797 0.3268 0.0084  0.0445  -0.0158 280 ASN A CB    
2096 C CG    . ASN A 280 ? 0.3203 0.2759 0.3215 0.0052  0.0445  -0.0153 280 ASN A CG    
2097 O OD1   . ASN A 280 ? 0.3444 0.3043 0.3450 0.0034  0.0437  -0.0150 280 ASN A OD1   
2098 N ND2   . ASN A 280 ? 0.3647 0.3158 0.3654 0.0045  0.0455  -0.0151 280 ASN A ND2   
2099 N N     . SER A 281 ? 0.3731 0.3320 0.3781 0.0143  0.0433  -0.0155 281 SER A N     
2100 C CA    . SER A 281 ? 0.3183 0.2767 0.3236 0.0161  0.0431  -0.0160 281 SER A CA    
2101 C C     . SER A 281 ? 0.3663 0.3272 0.3708 0.0168  0.0420  -0.0159 281 SER A C     
2102 O O     . SER A 281 ? 0.3818 0.3417 0.3856 0.0170  0.0420  -0.0166 281 SER A O     
2103 C CB    . SER A 281 ? 0.3436 0.3019 0.3504 0.0179  0.0431  -0.0153 281 SER A CB    
2104 O OG    . SER A 281 ? 0.3877 0.3467 0.3943 0.0194  0.0424  -0.0154 281 SER A OG    
2105 N N     . ILE A 282 ? 0.3301 0.2944 0.3345 0.0174  0.0413  -0.0150 282 ILE A N     
2106 C CA    . ILE A 282 ? 0.3678 0.3344 0.3711 0.0185  0.0406  -0.0148 282 ILE A CA    
2107 C C     . ILE A 282 ? 0.3782 0.3457 0.3805 0.0169  0.0406  -0.0152 282 ILE A C     
2108 O O     . ILE A 282 ? 0.2840 0.2517 0.2852 0.0177  0.0403  -0.0152 282 ILE A O     
2109 C CB    . ILE A 282 ? 0.3609 0.3315 0.3644 0.0198  0.0400  -0.0135 282 ILE A CB    
2110 C CG1   . ILE A 282 ? 0.3151 0.2849 0.3194 0.0215  0.0399  -0.0132 282 ILE A CG1   
2111 C CG2   . ILE A 282 ? 0.3958 0.3685 0.3978 0.0216  0.0394  -0.0131 282 ILE A CG2   
2112 C CD1   . ILE A 282 ? 0.2975 0.2714 0.3020 0.0228  0.0395  -0.0120 282 ILE A CD1   
2113 N N     . MET A 283 ? 0.3053 0.2731 0.3076 0.0144  0.0410  -0.0154 283 MET A N     
2114 C CA    . MET A 283 ? 0.3456 0.3148 0.3467 0.0124  0.0410  -0.0158 283 MET A CA    
2115 C C     . MET A 283 ? 0.4399 0.4057 0.4404 0.0120  0.0415  -0.0171 283 MET A C     
2116 O O     . MET A 283 ? 0.5053 0.4726 0.5048 0.0111  0.0414  -0.0173 283 MET A O     
2117 C CB    . MET A 283 ? 0.2581 0.2283 0.2588 0.0094  0.0413  -0.0157 283 MET A CB    
2118 C CG    . MET A 283 ? 0.3099 0.2855 0.3107 0.0090  0.0406  -0.0142 283 MET A CG    
2119 S SD    . MET A 283 ? 0.3715 0.3535 0.3716 0.0101  0.0398  -0.0130 283 MET A SD    
2120 C CE    . MET A 283 ? 0.4275 0.4080 0.4281 0.0146  0.0395  -0.0127 283 MET A CE    
2121 N N     . LYS A 284 ? 0.4864 0.4483 0.4875 0.0127  0.0421  -0.0177 284 LYS A N     
2122 C CA    . LYS A 284 ? 0.4455 0.4048 0.4463 0.0126  0.0427  -0.0188 284 LYS A CA    
2123 C C     . LYS A 284 ? 0.3772 0.3365 0.3780 0.0143  0.0421  -0.0186 284 LYS A C     
2124 O O     . LYS A 284 ? 0.4538 0.4113 0.4545 0.0144  0.0424  -0.0192 284 LYS A O     
2125 C CB    . LYS A 284 ? 0.4666 0.4222 0.4679 0.0125  0.0438  -0.0194 284 LYS A CB    
2126 C CG    . LYS A 284 ? 0.4272 0.3807 0.4273 0.0103  0.0447  -0.0205 284 LYS A CG    
2127 C CD    . LYS A 284 ? 0.4222 0.3717 0.4224 0.0106  0.0460  -0.0208 284 LYS A CD    
2128 C CE    . LYS A 284 ? 0.5109 0.4576 0.5089 0.0082  0.0469  -0.0221 284 LYS A CE    
2129 N NZ    . LYS A 284 ? 0.5149 0.4647 0.5120 0.0058  0.0461  -0.0220 284 LYS A NZ    
2130 N N     . CYS A 285 ? 0.3408 0.3021 0.3414 0.0158  0.0413  -0.0176 285 CYS A N     
2131 C CA    . CYS A 285 ? 0.3455 0.3062 0.3453 0.0173  0.0407  -0.0174 285 CYS A CA    
2132 C C     . CYS A 285 ? 0.3644 0.3276 0.3629 0.0174  0.0403  -0.0168 285 CYS A C     
2133 O O     . CYS A 285 ? 0.3848 0.3513 0.3832 0.0165  0.0402  -0.0164 285 CYS A O     
2134 C CB    . CYS A 285 ? 0.4434 0.4036 0.4432 0.0193  0.0402  -0.0168 285 CYS A CB    
2135 S SG    . CYS A 285 ? 0.3027 0.2610 0.3040 0.0195  0.0406  -0.0170 285 CYS A SG    
2136 N N     . ASP A 286 ? 0.3995 0.3614 0.3968 0.0185  0.0399  -0.0166 286 ASP A N     
2137 C CA    . ASP A 286 ? 0.3342 0.2982 0.3301 0.0192  0.0396  -0.0157 286 ASP A CA    
2138 C C     . ASP A 286 ? 0.3517 0.3191 0.3474 0.0208  0.0393  -0.0146 286 ASP A C     
2139 O O     . ASP A 286 ? 0.4008 0.3671 0.3965 0.0225  0.0391  -0.0143 286 ASP A O     
2140 C CB    . ASP A 286 ? 0.4490 0.4098 0.4433 0.0205  0.0392  -0.0155 286 ASP A CB    
2141 C CG    . ASP A 286 ? 0.5691 0.5315 0.5617 0.0215  0.0390  -0.0144 286 ASP A CG    
2142 O OD1   . ASP A 286 ? 0.5580 0.5247 0.5507 0.0219  0.0390  -0.0135 286 ASP A OD1   
2143 O OD2   . ASP A 286 ? 0.5878 0.5473 0.5791 0.0217  0.0389  -0.0142 286 ASP A OD2   
2144 N N     . VAL A 287 ? 0.4803 0.4522 0.4758 0.0203  0.0392  -0.0138 287 VAL A N     
2145 C CA    . VAL A 287 ? 0.5246 0.5008 0.5197 0.0221  0.0389  -0.0123 287 VAL A CA    
2146 C C     . VAL A 287 ? 0.5580 0.5318 0.5515 0.0256  0.0387  -0.0116 287 VAL A C     
2147 O O     . VAL A 287 ? 0.5829 0.5581 0.5761 0.0277  0.0386  -0.0109 287 VAL A O     
2148 C CB    . VAL A 287 ? 0.5521 0.5339 0.5469 0.0212  0.0389  -0.0112 287 VAL A CB    
2149 C CG1   . VAL A 287 ? 0.5348 0.5158 0.5279 0.0230  0.0388  -0.0105 287 VAL A CG1   
2150 C CG2   . VAL A 287 ? 0.4634 0.4517 0.4584 0.0219  0.0387  -0.0096 287 VAL A CG2   
2151 N N     . ASP A 288 ? 0.4469 0.4164 0.4389 0.0263  0.0387  -0.0119 288 ASP A N     
2152 C CA    . ASP A 288 ? 0.3773 0.3434 0.3668 0.0294  0.0386  -0.0113 288 ASP A CA    
2153 C C     . ASP A 288 ? 0.3805 0.3429 0.3695 0.0305  0.0385  -0.0121 288 ASP A C     
2154 O O     . ASP A 288 ? 0.3673 0.3271 0.3538 0.0333  0.0385  -0.0117 288 ASP A O     
2155 C CB    . ASP A 288 ? 0.3749 0.3368 0.3628 0.0290  0.0386  -0.0115 288 ASP A CB    
2156 C CG    . ASP A 288 ? 0.4372 0.4021 0.4242 0.0294  0.0387  -0.0102 288 ASP A CG    
2157 O OD1   . ASP A 288 ? 0.4108 0.3807 0.3977 0.0311  0.0388  -0.0088 288 ASP A OD1   
2158 O OD2   . ASP A 288 ? 0.5259 0.4886 0.5125 0.0281  0.0387  -0.0104 288 ASP A OD2   
2159 N N     . ILE A 289 ? 0.3858 0.3471 0.3768 0.0284  0.0385  -0.0132 289 ILE A N     
2160 C CA    . ILE A 289 ? 0.3904 0.3488 0.3811 0.0291  0.0383  -0.0139 289 ILE A CA    
2161 C C     . ILE A 289 ? 0.4260 0.3881 0.4185 0.0294  0.0384  -0.0136 289 ILE A C     
2162 O O     . ILE A 289 ? 0.3073 0.2679 0.2998 0.0300  0.0383  -0.0141 289 ILE A O     
2163 C CB    . ILE A 289 ? 0.4008 0.3557 0.3923 0.0269  0.0383  -0.0150 289 ILE A CB    
2164 C CG1   . ILE A 289 ? 0.3696 0.3268 0.3639 0.0245  0.0387  -0.0155 289 ILE A CG1   
2165 C CG2   . ILE A 289 ? 0.3353 0.2862 0.3246 0.0268  0.0381  -0.0152 289 ILE A CG2   
2166 C CD1   . ILE A 289 ? 0.3787 0.3336 0.3741 0.0229  0.0388  -0.0163 289 ILE A CD1   
2167 N N     . ARG A 290 ? 0.4377 0.4049 0.4316 0.0287  0.0385  -0.0128 290 ARG A N     
2168 C CA    . ARG A 290 ? 0.3759 0.3466 0.3717 0.0281  0.0386  -0.0125 290 ARG A CA    
2169 C C     . ARG A 290 ? 0.4086 0.3813 0.4034 0.0310  0.0384  -0.0116 290 ARG A C     
2170 O O     . ARG A 290 ? 0.4884 0.4618 0.4843 0.0310  0.0384  -0.0117 290 ARG A O     
2171 C CB    . ARG A 290 ? 0.4126 0.3879 0.4097 0.0260  0.0387  -0.0119 290 ARG A CB    
2172 C CG    . ARG A 290 ? 0.3489 0.3221 0.3470 0.0229  0.0390  -0.0130 290 ARG A CG    
2173 C CD    . ARG A 290 ? 0.3304 0.3079 0.3289 0.0207  0.0391  -0.0126 290 ARG A CD    
2174 N NE    . ARG A 290 ? 0.4650 0.4405 0.4635 0.0184  0.0394  -0.0137 290 ARG A NE    
2175 C CZ    . ARG A 290 ? 0.4865 0.4650 0.4847 0.0160  0.0395  -0.0136 290 ARG A CZ    
2176 N NH1   . ARG A 290 ? 0.5106 0.4947 0.5088 0.0155  0.0392  -0.0124 290 ARG A NH1   
2177 N NH2   . ARG A 290 ? 0.3342 0.3105 0.3321 0.0141  0.0399  -0.0148 290 ARG A NH2   
2178 N N     . LYS A 291 ? 0.2939 0.2679 0.2866 0.0337  0.0384  -0.0107 291 LYS A N     
2179 C CA    . LYS A 291 ? 0.4180 0.3933 0.4093 0.0370  0.0384  -0.0100 291 LYS A CA    
2180 C C     . LYS A 291 ? 0.4870 0.4573 0.4775 0.0375  0.0383  -0.0113 291 LYS A C     
2181 O O     . LYS A 291 ? 0.5112 0.4834 0.5024 0.0383  0.0382  -0.0111 291 LYS A O     
2182 C CB    . LYS A 291 ? 0.3803 0.3561 0.3687 0.0405  0.0386  -0.0089 291 LYS A CB    
2183 C CG    . LYS A 291 ? 0.4675 0.4483 0.4563 0.0400  0.0387  -0.0075 291 LYS A CG    
2184 C CD    . LYS A 291 ? 0.5435 0.5297 0.5309 0.0439  0.0390  -0.0055 291 LYS A CD    
2185 C CE    . LYS A 291 ? 0.5080 0.4961 0.4940 0.0452  0.0392  -0.0041 291 LYS A CE    
2186 N NZ    . LYS A 291 ? 0.5129 0.4938 0.4951 0.0483  0.0396  -0.0044 291 LYS A NZ    
2187 N N     . ASP A 292 ? 0.6315 0.5960 0.6208 0.0366  0.0382  -0.0124 292 ASP A N     
2188 C CA    . ASP A 292 ? 0.6460 0.6060 0.6343 0.0366  0.0380  -0.0136 292 ASP A CA    
2189 C C     . ASP A 292 ? 0.6328 0.5943 0.6242 0.0344  0.0379  -0.0140 292 ASP A C     
2190 O O     . ASP A 292 ? 0.6111 0.5717 0.6020 0.0351  0.0378  -0.0144 292 ASP A O     
2191 C CB    . ASP A 292 ? 0.6921 0.6461 0.6782 0.0357  0.0379  -0.0145 292 ASP A CB    
2192 C CG    . ASP A 292 ? 0.7645 0.7162 0.7473 0.0380  0.0380  -0.0139 292 ASP A CG    
2193 O OD1   . ASP A 292 ? 0.8709 0.8263 0.8544 0.0386  0.0383  -0.0128 292 ASP A OD1   
2194 O OD2   . ASP A 292 ? 0.7092 0.6551 0.6884 0.0391  0.0380  -0.0145 292 ASP A OD2   
2195 N N     . LEU A 293 ? 0.4074 0.3709 0.4016 0.0320  0.0381  -0.0139 293 LEU A N     
2196 C CA    . LEU A 293 ? 0.3178 0.2827 0.3146 0.0303  0.0382  -0.0140 293 LEU A CA    
2197 C C     . LEU A 293 ? 0.3371 0.3068 0.3350 0.0313  0.0382  -0.0129 293 LEU A C     
2198 O O     . LEU A 293 ? 0.3224 0.2929 0.3216 0.0312  0.0382  -0.0128 293 LEU A O     
2199 C CB    . LEU A 293 ? 0.2829 0.2478 0.2817 0.0277  0.0386  -0.0142 293 LEU A CB    
2200 C CG    . LEU A 293 ? 0.2937 0.2550 0.2918 0.0265  0.0387  -0.0150 293 LEU A CG    
2201 C CD1   . LEU A 293 ? 0.3504 0.3120 0.3505 0.0243  0.0392  -0.0153 293 LEU A CD1   
2202 C CD2   . LEU A 293 ? 0.3341 0.2920 0.3312 0.0268  0.0384  -0.0157 293 LEU A CD2   
2203 N N     . TYR A 294 ? 0.4529 0.4263 0.4505 0.0320  0.0382  -0.0119 294 TYR A N     
2204 C CA    . TYR A 294 ? 0.3667 0.3455 0.3653 0.0327  0.0382  -0.0106 294 TYR A CA    
2205 C C     . TYR A 294 ? 0.4266 0.4058 0.4236 0.0358  0.0381  -0.0105 294 TYR A C     
2206 O O     . TYR A 294 ? 0.4294 0.4123 0.4276 0.0362  0.0380  -0.0097 294 TYR A O     
2207 C CB    . TYR A 294 ? 0.3195 0.3031 0.3178 0.0328  0.0382  -0.0094 294 TYR A CB    
2208 C CG    . TYR A 294 ? 0.3377 0.3234 0.3378 0.0293  0.0383  -0.0091 294 TYR A CG    
2209 C CD1   . TYR A 294 ? 0.3885 0.3760 0.3906 0.0271  0.0383  -0.0087 294 TYR A CD1   
2210 C CD2   . TYR A 294 ? 0.3702 0.3560 0.3696 0.0283  0.0383  -0.0092 294 TYR A CD2   
2211 C CE1   . TYR A 294 ? 0.4577 0.4463 0.4607 0.0237  0.0385  -0.0087 294 TYR A CE1   
2212 C CE2   . TYR A 294 ? 0.4703 0.4580 0.4709 0.0248  0.0384  -0.0092 294 TYR A CE2   
2213 C CZ    . TYR A 294 ? 0.5123 0.5010 0.5144 0.0225  0.0385  -0.0090 294 TYR A CZ    
2214 O OH    . TYR A 294 ? 0.5115 0.5009 0.5141 0.0188  0.0387  -0.0091 294 TYR A OH    
2215 N N     . ALA A 295 ? 0.4405 0.4155 0.4346 0.0378  0.0380  -0.0113 295 ALA A N     
2216 C CA    . ALA A 295 ? 0.4019 0.3759 0.3935 0.0408  0.0380  -0.0116 295 ALA A CA    
2217 C C     . ALA A 295 ? 0.4221 0.3922 0.4135 0.0399  0.0378  -0.0129 295 ALA A C     
2218 O O     . ALA A 295 ? 0.4117 0.3816 0.4013 0.0420  0.0377  -0.0132 295 ALA A O     
2219 C CB    . ALA A 295 ? 0.4045 0.3753 0.3922 0.0436  0.0382  -0.0117 295 ALA A CB    
2220 N N     . ASN A 296 ? 0.3271 0.2949 0.3203 0.0371  0.0377  -0.0135 296 ASN A N     
2221 C CA    . ASN A 296 ? 0.2875 0.2531 0.2810 0.0361  0.0376  -0.0144 296 ASN A CA    
2222 C C     . ASN A 296 ? 0.3558 0.3230 0.3529 0.0335  0.0377  -0.0140 296 ASN A C     
2223 O O     . ASN A 296 ? 0.4172 0.3817 0.4148 0.0319  0.0377  -0.0147 296 ASN A O     
2224 C CB    . ASN A 296 ? 0.3826 0.3422 0.3730 0.0358  0.0373  -0.0157 296 ASN A CB    
2225 C CG    . ASN A 296 ? 0.4671 0.4237 0.4532 0.0384  0.0373  -0.0160 296 ASN A CG    
2226 O OD1   . ASN A 296 ? 0.4113 0.3669 0.3964 0.0390  0.0375  -0.0157 296 ASN A OD1   
2227 N ND2   . ASN A 296 ? 0.4847 0.4396 0.4680 0.0401  0.0372  -0.0167 296 ASN A ND2   
2228 N N     . THR A 297 ? 0.3063 0.2779 0.3059 0.0334  0.0379  -0.0129 297 THR A N     
2229 C CA    . THR A 297 ? 0.3103 0.2828 0.3130 0.0313  0.0382  -0.0124 297 THR A CA    
2230 C C     . THR A 297 ? 0.3565 0.3300 0.3597 0.0319  0.0381  -0.0123 297 THR A C     
2231 O O     . THR A 297 ? 0.3854 0.3623 0.3886 0.0332  0.0380  -0.0116 297 THR A O     
2232 C CB    . THR A 297 ? 0.3614 0.3374 0.3661 0.0304  0.0385  -0.0111 297 THR A CB    
2233 O OG1   . THR A 297 ? 0.4496 0.4265 0.4531 0.0305  0.0384  -0.0110 297 THR A OG1   
2234 C CG2   . THR A 297 ? 0.2362 0.2108 0.2431 0.0280  0.0391  -0.0110 297 THR A CG2   
2235 N N     . VAL A 298 ? 0.4854 0.4566 0.4888 0.0309  0.0381  -0.0129 298 VAL A N     
2236 C CA    . VAL A 298 ? 0.4199 0.3920 0.4234 0.0311  0.0379  -0.0129 298 VAL A CA    
2237 C C     . VAL A 298 ? 0.3235 0.2978 0.3303 0.0301  0.0385  -0.0116 298 VAL A C     
2238 O O     . VAL A 298 ? 0.4038 0.3766 0.4119 0.0289  0.0390  -0.0116 298 VAL A O     
2239 C CB    . VAL A 298 ? 0.3615 0.3301 0.3627 0.0305  0.0376  -0.0142 298 VAL A CB    
2240 C CG1   . VAL A 298 ? 0.3813 0.3517 0.3830 0.0300  0.0374  -0.0140 298 VAL A CG1   
2241 C CG2   . VAL A 298 ? 0.3630 0.3288 0.3603 0.0318  0.0371  -0.0153 298 VAL A CG2   
2242 N N     . LEU A 299 ? 0.3298 0.3078 0.3379 0.0309  0.0385  -0.0105 299 LEU A N     
2243 C CA    . LEU A 299 ? 0.3508 0.3307 0.3619 0.0303  0.0391  -0.0090 299 LEU A CA    
2244 C C     . LEU A 299 ? 0.3207 0.3015 0.3322 0.0302  0.0391  -0.0090 299 LEU A C     
2245 O O     . LEU A 299 ? 0.4001 0.3812 0.4097 0.0306  0.0384  -0.0099 299 LEU A O     
2246 C CB    . LEU A 299 ? 0.3010 0.2848 0.3133 0.0310  0.0392  -0.0076 299 LEU A CB    
2247 C CG    . LEU A 299 ? 0.3123 0.2967 0.3252 0.0303  0.0394  -0.0069 299 LEU A CG    
2248 C CD1   . LEU A 299 ? 0.3380 0.3271 0.3513 0.0311  0.0391  -0.0055 299 LEU A CD1   
2249 C CD2   . LEU A 299 ? 0.3104 0.2927 0.3250 0.0287  0.0402  -0.0061 299 LEU A CD2   
2250 N N     . SER A 300 ? 0.3688 0.3497 0.3826 0.0296  0.0399  -0.0079 300 SER A N     
2251 C CA    . SER A 300 ? 0.3946 0.3769 0.4090 0.0294  0.0399  -0.0076 300 SER A CA    
2252 C C     . SER A 300 ? 0.3501 0.3341 0.3673 0.0297  0.0410  -0.0057 300 SER A C     
2253 O O     . SER A 300 ? 0.3200 0.3018 0.3383 0.0296  0.0419  -0.0051 300 SER A O     
2254 C CB    . SER A 300 ? 0.4088 0.3881 0.4217 0.0283  0.0398  -0.0090 300 SER A CB    
2255 O OG    . SER A 300 ? 0.4505 0.4320 0.4641 0.0278  0.0398  -0.0085 300 SER A OG    
2256 N N     . GLY A 301 ? 0.3905 0.3782 0.4088 0.0301  0.0410  -0.0046 301 GLY A N     
2257 C CA    . GLY A 301 ? 0.4045 0.3940 0.4254 0.0308  0.0421  -0.0024 301 GLY A CA    
2258 C C     . GLY A 301 ? 0.4323 0.4245 0.4548 0.0317  0.0424  -0.0006 301 GLY A C     
2259 O O     . GLY A 301 ? 0.4577 0.4493 0.4797 0.0317  0.0421  -0.0008 301 GLY A O     
2260 N N     . GLY A 302 ? 0.4154 0.4109 0.4399 0.0327  0.0431  0.0015  302 GLY A N     
2261 C CA    . GLY A 302 ? 0.3271 0.3254 0.3531 0.0335  0.0434  0.0036  302 GLY A CA    
2262 C C     . GLY A 302 ? 0.2933 0.2887 0.3195 0.0333  0.0439  0.0042  302 GLY A C     
2263 O O     . GLY A 302 ? 0.4896 0.4877 0.5162 0.0334  0.0434  0.0050  302 GLY A O     
2264 N N     . THR A 303 ? 0.2437 0.2340 0.2696 0.0328  0.0447  0.0038  303 THR A N     
2265 C CA    . THR A 303 ? 0.2692 0.2563 0.2948 0.0319  0.0451  0.0042  303 THR A CA    
2266 C C     . THR A 303 ? 0.3533 0.3407 0.3774 0.0308  0.0439  0.0027  303 THR A C     
2267 O O     . THR A 303 ? 0.2871 0.2729 0.3109 0.0297  0.0440  0.0030  303 THR A O     
2268 C CB    . THR A 303 ? 0.2477 0.2291 0.2730 0.0317  0.0466  0.0043  303 THR A CB    
2269 O OG1   . THR A 303 ? 0.2659 0.2481 0.2926 0.0334  0.0477  0.0060  303 THR A OG1   
2270 C CG2   . THR A 303 ? 0.2525 0.2304 0.2773 0.0305  0.0471  0.0051  303 THR A CG2   
2271 N N     . THR A 304 ? 0.3957 0.3852 0.4187 0.0310  0.0428  0.0011  304 THR A N     
2272 C CA    . THR A 304 ? 0.3725 0.3627 0.3939 0.0307  0.0418  -0.0001 304 THR A CA    
2273 C C     . THR A 304 ? 0.3575 0.3529 0.3792 0.0317  0.0411  0.0006  304 THR A C     
2274 O O     . THR A 304 ? 0.3991 0.3963 0.4196 0.0320  0.0404  0.0000  304 THR A O     
2275 C CB    . THR A 304 ? 0.3675 0.3555 0.3868 0.0305  0.0412  -0.0026 304 THR A CB    
2276 O OG1   . THR A 304 ? 0.2662 0.2562 0.2848 0.0312  0.0406  -0.0032 304 THR A OG1   
2277 C CG2   . THR A 304 ? 0.2905 0.2739 0.3096 0.0296  0.0419  -0.0033 304 THR A CG2   
2278 N N     . MET A 305 ? 0.3831 0.3815 0.4063 0.0324  0.0414  0.0021  305 MET A N     
2279 C CA    . MET A 305 ? 0.4860 0.4897 0.5092 0.0334  0.0407  0.0027  305 MET A CA    
2280 C C     . MET A 305 ? 0.5295 0.5362 0.5537 0.0334  0.0407  0.0045  305 MET A C     
2281 O O     . MET A 305 ? 0.5608 0.5722 0.5848 0.0343  0.0400  0.0048  305 MET A O     
2282 C CB    . MET A 305 ? 0.4674 0.4741 0.4919 0.0340  0.0409  0.0038  305 MET A CB    
2283 C CG    . MET A 305 ? 0.4873 0.4926 0.5105 0.0337  0.0406  0.0019  305 MET A CG    
2284 S SD    . MET A 305 ? 0.4851 0.4903 0.5046 0.0337  0.0392  -0.0009 305 MET A SD    
2285 C CE    . MET A 305 ? 0.5382 0.5496 0.5578 0.0343  0.0388  -0.0001 305 MET A CE    
2286 N N     . TYR A 306 ? 0.4106 0.4149 0.4357 0.0323  0.0413  0.0057  306 TYR A N     
2287 C CA    . TYR A 306 ? 0.3636 0.3708 0.3896 0.0318  0.0413  0.0076  306 TYR A CA    
2288 C C     . TYR A 306 ? 0.4310 0.4423 0.4556 0.0324  0.0402  0.0068  306 TYR A C     
2289 O O     . TYR A 306 ? 0.4461 0.4555 0.4688 0.0324  0.0398  0.0048  306 TYR A O     
2290 C CB    . TYR A 306 ? 0.3815 0.3842 0.4075 0.0298  0.0420  0.0082  306 TYR A CB    
2291 C CG    . TYR A 306 ? 0.3189 0.3172 0.3458 0.0297  0.0433  0.0093  306 TYR A CG    
2292 C CD1   . TYR A 306 ? 0.4354 0.4348 0.4639 0.0299  0.0440  0.0120  306 TYR A CD1   
2293 C CD2   . TYR A 306 ? 0.2947 0.2881 0.3208 0.0297  0.0438  0.0077  306 TYR A CD2   
2294 C CE1   . TYR A 306 ? 0.4378 0.4332 0.4669 0.0304  0.0453  0.0132  306 TYR A CE1   
2295 C CE2   . TYR A 306 ? 0.3432 0.3329 0.3701 0.0301  0.0452  0.0088  306 TYR A CE2   
2296 C CZ    . TYR A 306 ? 0.3448 0.3353 0.3730 0.0306  0.0460  0.0115  306 TYR A CZ    
2297 O OH    . TYR A 306 ? 0.3089 0.2957 0.3376 0.0316  0.0475  0.0129  306 TYR A OH    
2298 N N     . PRO A 307 ? 0.4131 0.4302 0.4385 0.0331  0.0399  0.0084  307 PRO A N     
2299 C CA    . PRO A 307 ? 0.3532 0.3744 0.3771 0.0339  0.0390  0.0079  307 PRO A CA    
2300 C C     . PRO A 307 ? 0.3301 0.3497 0.3534 0.0324  0.0390  0.0078  307 PRO A C     
2301 O O     . PRO A 307 ? 0.3050 0.3228 0.3295 0.0303  0.0395  0.0093  307 PRO A O     
2302 C CB    . PRO A 307 ? 0.3095 0.3372 0.3350 0.0345  0.0389  0.0103  307 PRO A CB    
2303 C CG    . PRO A 307 ? 0.2689 0.2963 0.2960 0.0348  0.0394  0.0113  307 PRO A CG    
2304 C CD    . PRO A 307 ? 0.3209 0.3416 0.3483 0.0337  0.0402  0.0106  307 PRO A CD    
2305 N N     . GLY A 308 ? 0.3226 0.3428 0.3439 0.0334  0.0385  0.0061  308 GLY A N     
2306 C CA    . GLY A 308 ? 0.2291 0.2493 0.2497 0.0322  0.0383  0.0062  308 GLY A CA    
2307 C C     . GLY A 308 ? 0.3036 0.3174 0.3236 0.0304  0.0387  0.0049  308 GLY A C     
2308 O O     . GLY A 308 ? 0.2832 0.2973 0.3029 0.0287  0.0386  0.0053  308 GLY A O     
2309 N N     . ILE A 309 ? 0.2303 0.2390 0.2502 0.0306  0.0391  0.0035  309 ILE A N     
2310 C CA    . ILE A 309 ? 0.3142 0.3171 0.3336 0.0290  0.0395  0.0023  309 ILE A CA    
2311 C C     . ILE A 309 ? 0.2965 0.2988 0.3138 0.0296  0.0391  0.0005  309 ILE A C     
2312 O O     . ILE A 309 ? 0.3916 0.3917 0.4084 0.0279  0.0392  0.0002  309 ILE A O     
2313 C CB    . ILE A 309 ? 0.3845 0.3830 0.4044 0.0293  0.0401  0.0015  309 ILE A CB    
2314 C CG1   . ILE A 309 ? 0.3424 0.3352 0.3621 0.0274  0.0408  0.0008  309 ILE A CG1   
2315 C CG2   . ILE A 309 ? 0.2308 0.2286 0.2493 0.0310  0.0397  -0.0004 309 ILE A CG2   
2316 C CD1   . ILE A 309 ? 0.4324 0.4214 0.4523 0.0279  0.0414  0.0000  309 ILE A CD1   
2317 N N     . ALA A 310 ? 0.2770 0.2811 0.2928 0.0320  0.0385  -0.0005 310 ALA A N     
2318 C CA    . ALA A 310 ? 0.3434 0.3462 0.3568 0.0330  0.0382  -0.0021 310 ALA A CA    
2319 C C     . ALA A 310 ? 0.3896 0.3968 0.4025 0.0331  0.0379  -0.0011 310 ALA A C     
2320 O O     . ALA A 310 ? 0.4186 0.4246 0.4300 0.0332  0.0379  -0.0019 310 ALA A O     
2321 C CB    . ALA A 310 ? 0.3858 0.3883 0.3972 0.0356  0.0379  -0.0035 310 ALA A CB    
2322 N N     . ASP A 311 ? 0.3873 0.4002 0.4013 0.0331  0.0378  0.0008  311 ASP A N     
2323 C CA    . ASP A 311 ? 0.3727 0.3909 0.3863 0.0331  0.0375  0.0021  311 ASP A CA    
2324 C C     . ASP A 311 ? 0.4176 0.4349 0.4321 0.0295  0.0376  0.0028  311 ASP A C     
2325 O O     . ASP A 311 ? 0.3743 0.3934 0.3878 0.0290  0.0374  0.0029  311 ASP A O     
2326 C CB    . ASP A 311 ? 0.3899 0.4154 0.4044 0.0341  0.0372  0.0040  311 ASP A CB    
2327 C CG    . ASP A 311 ? 0.5013 0.5290 0.5140 0.0381  0.0371  0.0032  311 ASP A CG    
2328 O OD1   . ASP A 311 ? 0.5840 0.6092 0.5942 0.0401  0.0371  0.0016  311 ASP A OD1   
2329 O OD2   . ASP A 311 ? 0.5076 0.5394 0.5209 0.0391  0.0370  0.0043  311 ASP A OD2   
2330 N N     . ARG A 312 ? 0.3394 0.3540 0.3556 0.0270  0.0380  0.0035  312 ARG A N     
2331 C CA    . ARG A 312 ? 0.2960 0.3081 0.3124 0.0233  0.0383  0.0041  312 ARG A CA    
2332 C C     . ARG A 312 ? 0.3190 0.3262 0.3341 0.0226  0.0385  0.0021  312 ARG A C     
2333 O O     . ARG A 312 ? 0.3260 0.3336 0.3405 0.0202  0.0384  0.0023  312 ARG A O     
2334 C CB    . ARG A 312 ? 0.2346 0.2429 0.2525 0.0218  0.0389  0.0048  312 ARG A CB    
2335 C CG    . ARG A 312 ? 0.2734 0.2773 0.2909 0.0180  0.0394  0.0051  312 ARG A CG    
2336 C CD    . ARG A 312 ? 0.2387 0.2472 0.2559 0.0151  0.0389  0.0068  312 ARG A CD    
2337 N NE    . ARG A 312 ? 0.2524 0.2552 0.2684 0.0115  0.0395  0.0064  312 ARG A NE    
2338 C CZ    . ARG A 312 ? 0.2971 0.2950 0.3131 0.0093  0.0402  0.0072  312 ARG A CZ    
2339 N NH1   . ARG A 312 ? 0.2984 0.2969 0.3158 0.0103  0.0405  0.0088  312 ARG A NH1   
2340 N NH2   . ARG A 312 ? 0.4211 0.4133 0.4353 0.0061  0.0407  0.0063  312 ARG A NH2   
2341 N N     . MET A 313 ? 0.3543 0.3570 0.3690 0.0245  0.0387  0.0003  313 MET A N     
2342 C CA    . MET A 313 ? 0.3794 0.3776 0.3929 0.0243  0.0389  -0.0016 313 MET A CA    
2343 C C     . MET A 313 ? 0.3675 0.3688 0.3793 0.0257  0.0383  -0.0020 313 MET A C     
2344 O O     . MET A 313 ? 0.3955 0.3952 0.4064 0.0246  0.0384  -0.0027 313 MET A O     
2345 C CB    . MET A 313 ? 0.4254 0.4190 0.4388 0.0258  0.0392  -0.0030 313 MET A CB    
2346 C CG    . MET A 313 ? 0.4921 0.4802 0.5048 0.0248  0.0395  -0.0047 313 MET A CG    
2347 S SD    . MET A 313 ? 0.5378 0.5212 0.5513 0.0218  0.0405  -0.0045 313 MET A SD    
2348 C CE    . MET A 313 ? 0.5723 0.5511 0.5844 0.0212  0.0408  -0.0065 313 MET A CE    
2349 N N     . GLN A 314 ? 0.4440 0.4498 0.4553 0.0285  0.0379  -0.0014 314 GLN A N     
2350 C CA    . GLN A 314 ? 0.3658 0.3754 0.3755 0.0303  0.0376  -0.0013 314 GLN A CA    
2351 C C     . GLN A 314 ? 0.4161 0.4311 0.4263 0.0280  0.0374  0.0005  314 GLN A C     
2352 O O     . GLN A 314 ? 0.4995 0.5162 0.5086 0.0278  0.0373  0.0005  314 GLN A O     
2353 C CB    . GLN A 314 ? 0.4169 0.4299 0.4255 0.0341  0.0374  -0.0010 314 GLN A CB    
2354 C CG    . GLN A 314 ? 0.4455 0.4632 0.4523 0.0367  0.0373  -0.0004 314 GLN A CG    
2355 C CD    . GLN A 314 ? 0.5499 0.5629 0.5544 0.0382  0.0374  -0.0020 314 GLN A CD    
2356 O OE1   . GLN A 314 ? 0.5084 0.5146 0.5126 0.0372  0.0376  -0.0037 314 GLN A OE1   
2357 N NE2   . GLN A 314 ? 0.5331 0.5500 0.5360 0.0406  0.0375  -0.0013 314 GLN A NE2   
2358 N N     . LYS A 315 ? 0.2493 0.2672 0.2612 0.0258  0.0373  0.0021  315 LYS A N     
2359 C CA    . LYS A 315 ? 0.2552 0.2780 0.2674 0.0227  0.0371  0.0038  315 LYS A CA    
2360 C C     . LYS A 315 ? 0.3099 0.3281 0.3215 0.0192  0.0373  0.0028  315 LYS A C     
2361 O O     . LYS A 315 ? 0.3561 0.3777 0.3669 0.0178  0.0370  0.0032  315 LYS A O     
2362 C CB    . LYS A 315 ? 0.2464 0.2721 0.2602 0.0208  0.0370  0.0058  315 LYS A CB    
2363 C CG    . LYS A 315 ? 0.2352 0.2685 0.2491 0.0180  0.0365  0.0081  315 LYS A CG    
2364 C CD    . LYS A 315 ? 0.2356 0.2719 0.2509 0.0162  0.0363  0.0103  315 LYS A CD    
2365 C CE    . LYS A 315 ? 0.3213 0.3689 0.3369 0.0165  0.0357  0.0129  315 LYS A CE    
2366 N NZ    . LYS A 315 ? 0.3257 0.3782 0.3426 0.0147  0.0354  0.0155  315 LYS A NZ    
2367 N N     . GLU A 316 ? 0.3474 0.3578 0.3593 0.0180  0.0379  0.0014  316 GLU A N     
2368 C CA    . GLU A 316 ? 0.4011 0.4065 0.4123 0.0145  0.0383  0.0004  316 GLU A CA    
2369 C C     . GLU A 316 ? 0.3899 0.3929 0.3998 0.0153  0.0383  -0.0013 316 GLU A C     
2370 O O     . GLU A 316 ? 0.3428 0.3456 0.3517 0.0125  0.0383  -0.0016 316 GLU A O     
2371 C CB    . GLU A 316 ? 0.4358 0.4341 0.4476 0.0135  0.0390  -0.0002 316 GLU A CB    
2372 C CG    . GLU A 316 ? 0.4371 0.4363 0.4498 0.0117  0.0392  0.0017  316 GLU A CG    
2373 C CD    . GLU A 316 ? 0.5373 0.5389 0.5491 0.0074  0.0389  0.0028  316 GLU A CD    
2374 O OE1   . GLU A 316 ? 0.4946 0.4969 0.5050 0.0058  0.0387  0.0020  316 GLU A OE1   
2375 O OE2   . GLU A 316 ? 0.6232 0.6261 0.6355 0.0055  0.0389  0.0046  316 GLU A OE2   
2376 N N     . ILE A 317 ? 0.4129 0.4137 0.4226 0.0187  0.0383  -0.0025 317 ILE A N     
2377 C CA    . ILE A 317 ? 0.4353 0.4343 0.4437 0.0196  0.0383  -0.0039 317 ILE A CA    
2378 C C     . ILE A 317 ? 0.4522 0.4578 0.4597 0.0205  0.0378  -0.0028 317 ILE A C     
2379 O O     . ILE A 317 ? 0.4396 0.4452 0.4461 0.0196  0.0378  -0.0033 317 ILE A O     
2380 C CB    . ILE A 317 ? 0.4459 0.4407 0.4540 0.0228  0.0385  -0.0053 317 ILE A CB    
2381 C CG1   . ILE A 317 ? 0.4423 0.4309 0.4511 0.0217  0.0391  -0.0064 317 ILE A CG1   
2382 C CG2   . ILE A 317 ? 0.4730 0.4667 0.4793 0.0240  0.0384  -0.0063 317 ILE A CG2   
2383 C CD1   . ILE A 317 ? 0.4998 0.4857 0.5088 0.0182  0.0396  -0.0065 317 ILE A CD1   
2384 N N     . THR A 318 ? 0.3201 0.3318 0.3279 0.0225  0.0375  -0.0012 318 THR A N     
2385 C CA    . THR A 318 ? 0.2581 0.2770 0.2650 0.0234  0.0371  0.0002  318 THR A CA    
2386 C C     . THR A 318 ? 0.3282 0.3510 0.3354 0.0188  0.0368  0.0013  318 THR A C     
2387 O O     . THR A 318 ? 0.3186 0.3454 0.3249 0.0184  0.0366  0.0018  318 THR A O     
2388 C CB    . THR A 318 ? 0.2749 0.3001 0.2820 0.0265  0.0369  0.0018  318 THR A CB    
2389 O OG1   . THR A 318 ? 0.3809 0.4033 0.3866 0.0310  0.0371  0.0008  318 THR A OG1   
2390 C CG2   . THR A 318 ? 0.2874 0.3220 0.2943 0.0264  0.0365  0.0040  318 THR A CG2   
2391 N N     . ALA A 319 ? 0.3816 0.4030 0.3897 0.0153  0.0369  0.0016  319 ALA A N     
2392 C CA    . ALA A 319 ? 0.3688 0.3927 0.3765 0.0104  0.0367  0.0024  319 ALA A CA    
2393 C C     . ALA A 319 ? 0.4245 0.4429 0.4310 0.0081  0.0370  0.0006  319 ALA A C     
2394 O O     . ALA A 319 ? 0.4593 0.4807 0.4648 0.0044  0.0367  0.0010  319 ALA A O     
2395 C CB    . ALA A 319 ? 0.3379 0.3599 0.3464 0.0073  0.0368  0.0032  319 ALA A CB    
2396 N N     . LEU A 320 ? 0.4786 0.4892 0.4850 0.0097  0.0375  -0.0015 320 LEU A N     
2397 C CA    . LEU A 320 ? 0.4699 0.4748 0.4753 0.0082  0.0380  -0.0035 320 LEU A CA    
2398 C C     . LEU A 320 ? 0.4593 0.4659 0.4639 0.0107  0.0378  -0.0040 320 LEU A C     
2399 O O     . LEU A 320 ? 0.3694 0.3751 0.3729 0.0088  0.0379  -0.0048 320 LEU A O     
2400 C CB    . LEU A 320 ? 0.4036 0.3999 0.4093 0.0088  0.0387  -0.0051 320 LEU A CB    
2401 C CG    . LEU A 320 ? 0.3410 0.3338 0.3472 0.0065  0.0392  -0.0048 320 LEU A CG    
2402 C CD1   . LEU A 320 ? 0.3272 0.3123 0.3337 0.0076  0.0401  -0.0063 320 LEU A CD1   
2403 C CD2   . LEU A 320 ? 0.4021 0.3949 0.4069 0.0016  0.0392  -0.0045 320 LEU A CD2   
2404 N N     . ALA A 321 ? 0.3846 0.3927 0.3894 0.0151  0.0377  -0.0036 321 ALA A N     
2405 C CA    . ALA A 321 ? 0.3380 0.3461 0.3417 0.0178  0.0376  -0.0040 321 ALA A CA    
2406 C C     . ALA A 321 ? 0.4107 0.4273 0.4138 0.0179  0.0372  -0.0022 321 ALA A C     
2407 O O     . ALA A 321 ? 0.4079 0.4305 0.4115 0.0159  0.0369  -0.0006 321 ALA A O     
2408 C CB    . ALA A 321 ? 0.2958 0.3013 0.2993 0.0223  0.0377  -0.0045 321 ALA A CB    
2409 N N     . PRO A 322 ? 0.6261 0.6437 0.6281 0.0202  0.0372  -0.0021 322 PRO A N     
2410 C CA    . PRO A 322 ? 0.6016 0.6282 0.6030 0.0212  0.0369  0.0000  322 PRO A CA    
2411 C C     . PRO A 322 ? 0.6187 0.6509 0.6204 0.0247  0.0368  0.0019  322 PRO A C     
2412 O O     . PRO A 322 ? 0.6136 0.6423 0.6155 0.0269  0.0370  0.0013  322 PRO A O     
2413 C CB    . PRO A 322 ? 0.5561 0.5807 0.5561 0.0237  0.0372  -0.0005 322 PRO A CB    
2414 C CG    . PRO A 322 ? 0.5123 0.5284 0.5123 0.0210  0.0374  -0.0029 322 PRO A CG    
2415 C CD    . PRO A 322 ? 0.5506 0.5616 0.5518 0.0205  0.0376  -0.0040 322 PRO A CD    
2416 N N     . SER A 323 ? 0.6018 0.6436 0.6033 0.0251  0.0366  0.0042  323 SER A N     
2417 C CA    . SER A 323 ? 0.6152 0.6637 0.6167 0.0289  0.0366  0.0063  323 SER A CA    
2418 C C     . SER A 323 ? 0.6008 0.6459 0.6005 0.0350  0.0371  0.0059  323 SER A C     
2419 O O     . SER A 323 ? 0.7126 0.7584 0.7119 0.0384  0.0373  0.0063  323 SER A O     
2420 C CB    . SER A 323 ? 0.7478 0.8082 0.7494 0.0279  0.0362  0.0091  323 SER A CB    
2421 O OG    . SER A 323 ? 0.8150 0.8777 0.8153 0.0305  0.0365  0.0098  323 SER A OG    
2422 N N     . THR A 324 ? 0.5680 0.6090 0.5663 0.0362  0.0374  0.0050  324 THR A N     
2423 C CA    . THR A 324 ? 0.6866 0.7239 0.6828 0.0418  0.0380  0.0048  324 THR A CA    
2424 C C     . THR A 324 ? 0.7562 0.7827 0.7516 0.0426  0.0382  0.0022  324 THR A C     
2425 O O     . THR A 324 ? 0.7742 0.7971 0.7673 0.0469  0.0386  0.0019  324 THR A O     
2426 C CB    . THR A 324 ? 0.6764 0.7153 0.6710 0.0433  0.0383  0.0057  324 THR A CB    
2427 O OG1   . THR A 324 ? 0.6490 0.6830 0.6408 0.0488  0.0389  0.0055  324 THR A OG1   
2428 C CG2   . THR A 324 ? 0.6575 0.6916 0.6528 0.0389  0.0380  0.0041  324 THR A CG2   
2429 N N     . MET A 325 ? 0.6921 0.7136 0.6891 0.0385  0.0379  0.0005  325 MET A N     
2430 C CA    . MET A 325 ? 0.6143 0.6265 0.6108 0.0388  0.0380  -0.0018 325 MET A CA    
2431 C C     . MET A 325 ? 0.6013 0.6125 0.5971 0.0420  0.0381  -0.0019 325 MET A C     
2432 O O     . MET A 325 ? 0.6910 0.7069 0.6883 0.0413  0.0379  -0.0010 325 MET A O     
2433 C CB    . MET A 325 ? 0.6281 0.6367 0.6267 0.0341  0.0378  -0.0032 325 MET A CB    
2434 C CG    . MET A 325 ? 0.6732 0.6766 0.6714 0.0322  0.0379  -0.0046 325 MET A CG    
2435 S SD    . MET A 325 ? 0.6819 0.6774 0.6777 0.0355  0.0382  -0.0060 325 MET A SD    
2436 C CE    . MET A 325 ? 0.6844 0.6777 0.6801 0.0329  0.0382  -0.0067 325 MET A CE    
2437 N N     . LYS A 326 ? 0.3542 0.3592 0.3475 0.0451  0.0384  -0.0031 326 LYS A N     
2438 C CA    . LYS A 326 ? 0.3965 0.3985 0.3890 0.0470  0.0385  -0.0040 326 LYS A CA    
2439 C C     . LYS A 326 ? 0.4040 0.4018 0.3987 0.0433  0.0382  -0.0055 326 LYS A C     
2440 O O     . LYS A 326 ? 0.4246 0.4172 0.4195 0.0410  0.0382  -0.0068 326 LYS A O     
2441 C CB    . LYS A 326 ? 0.4467 0.4423 0.4352 0.0508  0.0389  -0.0051 326 LYS A CB    
2442 C CG    . LYS A 326 ? 0.4460 0.4411 0.4324 0.0543  0.0391  -0.0053 326 LYS A CG    
2443 C CD    . LYS A 326 ? 0.5233 0.5090 0.5056 0.0563  0.0394  -0.0072 326 LYS A CD    
2444 C CE    . LYS A 326 ? 0.5582 0.5431 0.5371 0.0606  0.0398  -0.0075 326 LYS A CE    
2445 N NZ    . LYS A 326 ? 0.5517 0.5397 0.5278 0.0655  0.0406  -0.0059 326 LYS A NZ    
2446 N N     . ILE A 327 ? 0.2766 0.2774 0.2730 0.0427  0.0380  -0.0051 327 ILE A N     
2447 C CA    . ILE A 327 ? 0.3443 0.3424 0.3429 0.0395  0.0379  -0.0059 327 ILE A CA    
2448 C C     . ILE A 327 ? 0.4006 0.3970 0.3986 0.0414  0.0379  -0.0065 327 ILE A C     
2449 O O     . ILE A 327 ? 0.3001 0.3015 0.2982 0.0431  0.0378  -0.0054 327 ILE A O     
2450 C CB    . ILE A 327 ? 0.3284 0.3319 0.3299 0.0363  0.0377  -0.0045 327 ILE A CB    
2451 C CG1   . ILE A 327 ? 0.2858 0.2915 0.2875 0.0342  0.0377  -0.0039 327 ILE A CG1   
2452 C CG2   . ILE A 327 ? 0.2543 0.2546 0.2579 0.0335  0.0378  -0.0051 327 ILE A CG2   
2453 C CD1   . ILE A 327 ? 0.3544 0.3544 0.3568 0.0312  0.0378  -0.0054 327 ILE A CD1   
2454 N N     . LYS A 328 ? 0.4569 0.4469 0.4542 0.0409  0.0379  -0.0083 328 LYS A N     
2455 C CA    . LYS A 328 ? 0.4587 0.4472 0.4554 0.0420  0.0378  -0.0090 328 LYS A CA    
2456 C C     . LYS A 328 ? 0.4211 0.4076 0.4204 0.0389  0.0377  -0.0094 328 LYS A C     
2457 O O     . LYS A 328 ? 0.4682 0.4504 0.4677 0.0371  0.0378  -0.0103 328 LYS A O     
2458 C CB    . LYS A 328 ? 0.5128 0.4957 0.5055 0.0444  0.0378  -0.0105 328 LYS A CB    
2459 C CG    . LYS A 328 ? 0.4948 0.4774 0.4860 0.0461  0.0377  -0.0111 328 LYS A CG    
2460 C CD    . LYS A 328 ? 0.5073 0.4851 0.4935 0.0492  0.0379  -0.0123 328 LYS A CD    
2461 C CE    . LYS A 328 ? 0.5798 0.5563 0.5639 0.0504  0.0378  -0.0134 328 LYS A CE    
2462 N NZ    . LYS A 328 ? 0.5473 0.5181 0.5256 0.0534  0.0381  -0.0148 328 LYS A NZ    
2463 N N     . ILE A 329 ? 0.3428 0.3329 0.3441 0.0385  0.0377  -0.0085 329 ILE A N     
2464 C CA    . ILE A 329 ? 0.4268 0.4151 0.4300 0.0367  0.0377  -0.0087 329 ILE A CA    
2465 C C     . ILE A 329 ? 0.4007 0.3874 0.4021 0.0384  0.0375  -0.0097 329 ILE A C     
2466 O O     . ILE A 329 ? 0.4426 0.4322 0.4426 0.0407  0.0374  -0.0095 329 ILE A O     
2467 C CB    . ILE A 329 ? 0.4017 0.3944 0.4079 0.0352  0.0379  -0.0070 329 ILE A CB    
2468 C CG1   . ILE A 329 ? 0.2424 0.2370 0.2498 0.0333  0.0380  -0.0060 329 ILE A CG1   
2469 C CG2   . ILE A 329 ? 0.4159 0.4066 0.4241 0.0337  0.0381  -0.0071 329 ILE A CG2   
2470 C CD1   . ILE A 329 ? 0.2377 0.2281 0.2441 0.0322  0.0381  -0.0072 329 ILE A CD1   
2471 N N     . ILE A 330 ? 0.4631 0.4455 0.4641 0.0372  0.0375  -0.0109 330 ILE A N     
2472 C CA    . ILE A 330 ? 0.4765 0.4574 0.4756 0.0380  0.0372  -0.0119 330 ILE A CA    
2473 C C     . ILE A 330 ? 0.5365 0.5192 0.5387 0.0363  0.0373  -0.0112 330 ILE A C     
2474 O O     . ILE A 330 ? 0.6521 0.6330 0.6560 0.0344  0.0376  -0.0111 330 ILE A O     
2475 C CB    . ILE A 330 ? 0.4345 0.4095 0.4303 0.0379  0.0370  -0.0137 330 ILE A CB    
2476 C CG1   . ILE A 330 ? 0.4520 0.4251 0.4445 0.0402  0.0371  -0.0142 330 ILE A CG1   
2477 C CG2   . ILE A 330 ? 0.4250 0.3986 0.4188 0.0379  0.0367  -0.0148 330 ILE A CG2   
2478 C CD1   . ILE A 330 ? 0.4751 0.4490 0.4689 0.0398  0.0373  -0.0134 330 ILE A CD1   
2479 N N     . ALA A 331 ? 0.3315 0.3182 0.3343 0.0372  0.0372  -0.0105 331 ALA A N     
2480 C CA    . ALA A 331 ? 0.3505 0.3397 0.3563 0.0360  0.0374  -0.0093 331 ALA A CA    
2481 C C     . ALA A 331 ? 0.3733 0.3636 0.3775 0.0368  0.0370  -0.0100 331 ALA A C     
2482 O O     . ALA A 331 ? 0.3508 0.3451 0.3548 0.0382  0.0369  -0.0093 331 ALA A O     
2483 C CB    . ALA A 331 ? 0.2387 0.2324 0.2474 0.0359  0.0377  -0.0072 331 ALA A CB    
2484 N N     . PRO A 332 ? 0.3683 0.3554 0.3709 0.0358  0.0368  -0.0113 332 PRO A N     
2485 C CA    . PRO A 332 ? 0.3633 0.3506 0.3632 0.0361  0.0363  -0.0124 332 PRO A CA    
2486 C C     . PRO A 332 ? 0.4610 0.4537 0.4637 0.0357  0.0364  -0.0108 332 PRO A C     
2487 O O     . PRO A 332 ? 0.4524 0.4466 0.4586 0.0345  0.0368  -0.0094 332 PRO A O     
2488 C CB    . PRO A 332 ? 0.2732 0.2557 0.2711 0.0342  0.0360  -0.0138 332 PRO A CB    
2489 C CG    . PRO A 332 ? 0.2432 0.2225 0.2418 0.0339  0.0363  -0.0139 332 PRO A CG    
2490 C CD    . PRO A 332 ? 0.2423 0.2252 0.2449 0.0341  0.0369  -0.0120 332 PRO A CD    
2491 N N     . PRO A 333 ? 0.6372 0.6329 0.6384 0.0367  0.0360  -0.0111 333 PRO A N     
2492 C CA    . PRO A 333 ? 0.6443 0.6458 0.6484 0.0365  0.0361  -0.0093 333 PRO A CA    
2493 C C     . PRO A 333 ? 0.6033 0.6052 0.6090 0.0344  0.0362  -0.0088 333 PRO A C     
2494 O O     . PRO A 333 ? 0.5955 0.6018 0.6048 0.0342  0.0366  -0.0067 333 PRO A O     
2495 C CB    . PRO A 333 ? 0.6547 0.6584 0.6556 0.0378  0.0357  -0.0103 333 PRO A CB    
2496 C CG    . PRO A 333 ? 0.6313 0.6314 0.6287 0.0397  0.0357  -0.0118 333 PRO A CG    
2497 C CD    . PRO A 333 ? 0.6438 0.6378 0.6404 0.0385  0.0357  -0.0128 333 PRO A CD    
2498 N N     . GLU A 334 ? 0.3978 0.3955 0.4010 0.0330  0.0358  -0.0105 334 GLU A N     
2499 C CA    . GLU A 334 ? 0.4099 0.4086 0.4143 0.0310  0.0358  -0.0101 334 GLU A CA    
2500 C C     . GLU A 334 ? 0.3992 0.3961 0.4065 0.0303  0.0364  -0.0091 334 GLU A C     
2501 O O     . GLU A 334 ? 0.4562 0.4540 0.4643 0.0288  0.0365  -0.0087 334 GLU A O     
2502 C CB    . GLU A 334 ? 0.5066 0.5021 0.5064 0.0293  0.0350  -0.0124 334 GLU A CB    
2503 C CG    . GLU A 334 ? 0.6309 0.6192 0.6276 0.0291  0.0348  -0.0143 334 GLU A CG    
2504 C CD    . GLU A 334 ? 0.6887 0.6735 0.6810 0.0309  0.0346  -0.0160 334 GLU A CD    
2505 O OE1   . GLU A 334 ? 0.7207 0.7088 0.7129 0.0326  0.0346  -0.0157 334 GLU A OE1   
2506 O OE2   . GLU A 334 ? 0.6327 0.6114 0.6216 0.0307  0.0344  -0.0177 334 GLU A OE2   
2507 N N     . ARG A 335 ? 0.3922 0.3871 0.4008 0.0313  0.0370  -0.0087 335 ARG A N     
2508 C CA    . ARG A 335 ? 0.4198 0.4119 0.4301 0.0306  0.0376  -0.0083 335 ARG A CA    
2509 C C     . ARG A 335 ? 0.4741 0.4691 0.4880 0.0303  0.0384  -0.0062 335 ARG A C     
2510 O O     . ARG A 335 ? 0.4017 0.3944 0.4165 0.0297  0.0389  -0.0061 335 ARG A O     
2511 C CB    . ARG A 335 ? 0.3897 0.3797 0.4004 0.0315  0.0379  -0.0082 335 ARG A CB    
2512 C CG    . ARG A 335 ? 0.2457 0.2388 0.2594 0.0322  0.0385  -0.0062 335 ARG A CG    
2513 C CD    . ARG A 335 ? 0.3362 0.3286 0.3487 0.0331  0.0383  -0.0065 335 ARG A CD    
2514 N NE    . ARG A 335 ? 0.4561 0.4521 0.4710 0.0335  0.0387  -0.0046 335 ARG A NE    
2515 C CZ    . ARG A 335 ? 0.4552 0.4556 0.4701 0.0346  0.0384  -0.0037 335 ARG A CZ    
2516 N NH1   . ARG A 335 ? 0.3367 0.3384 0.3493 0.0356  0.0377  -0.0049 335 ARG A NH1   
2517 N NH2   . ARG A 335 ? 0.4753 0.4786 0.4923 0.0346  0.0387  -0.0017 335 ARG A NH2   
2518 N N     . LYS A 336 ? 0.5578 0.5579 0.5735 0.0309  0.0385  -0.0045 336 LYS A N     
2519 C CA    . LYS A 336 ? 0.5574 0.5602 0.5762 0.0310  0.0394  -0.0023 336 LYS A CA    
2520 C C     . LYS A 336 ? 0.4972 0.5000 0.5155 0.0297  0.0394  -0.0028 336 LYS A C     
2521 O O     . LYS A 336 ? 0.5775 0.5797 0.5975 0.0299  0.0403  -0.0018 336 LYS A O     
2522 C CB    . LYS A 336 ? 0.5196 0.5284 0.5402 0.0319  0.0395  -0.0004 336 LYS A CB    
2523 C CG    . LYS A 336 ? 0.4962 0.5074 0.5202 0.0328  0.0408  0.0024  336 LYS A CG    
2524 C CD    . LYS A 336 ? 0.4349 0.4509 0.4607 0.0339  0.0410  0.0047  336 LYS A CD    
2525 C CE    . LYS A 336 ? 0.4038 0.4262 0.4310 0.0341  0.0411  0.0064  336 LYS A CE    
2526 N NZ    . LYS A 336 ? 0.5073 0.5349 0.5350 0.0348  0.0407  0.0076  336 LYS A NZ    
2527 N N     . TYR A 337 ? 0.4767 0.4806 0.4924 0.0284  0.0383  -0.0042 337 TYR A N     
2528 C CA    . TYR A 337 ? 0.5066 0.5109 0.5212 0.0265  0.0379  -0.0048 337 TYR A CA    
2529 C C     . TYR A 337 ? 0.4221 0.4204 0.4332 0.0252  0.0372  -0.0072 337 TYR A C     
2530 O O     . TYR A 337 ? 0.3814 0.3796 0.3902 0.0231  0.0365  -0.0082 337 TYR A O     
2531 C CB    . TYR A 337 ? 0.5231 0.5328 0.5367 0.0254  0.0371  -0.0044 337 TYR A CB    
2532 C CG    . TYR A 337 ? 0.4729 0.4889 0.4901 0.0269  0.0379  -0.0016 337 TYR A CG    
2533 C CD1   . TYR A 337 ? 0.3222 0.3391 0.3429 0.0283  0.0393  0.0006  337 TYR A CD1   
2534 C CD2   . TYR A 337 ? 0.4838 0.5043 0.5007 0.0272  0.0374  -0.0012 337 TYR A CD2   
2535 C CE1   . TYR A 337 ? 0.3836 0.4054 0.4073 0.0300  0.0401  0.0034  337 TYR A CE1   
2536 C CE2   . TYR A 337 ? 0.3991 0.4254 0.4195 0.0287  0.0382  0.0017  337 TYR A CE2   
2537 C CZ    . TYR A 337 ? 0.4438 0.4705 0.4675 0.0302  0.0396  0.0040  337 TYR A CZ    
2538 O OH    . TYR A 337 ? 0.5621 0.5938 0.5890 0.0319  0.0405  0.0071  337 TYR A OH    
2539 N N     . SER A 338 ? 0.4061 0.3997 0.4164 0.0262  0.0374  -0.0083 338 SER A N     
2540 C CA    . SER A 338 ? 0.4498 0.4376 0.4569 0.0253  0.0369  -0.0104 338 SER A CA    
2541 C C     . SER A 338 ? 0.4323 0.4192 0.4395 0.0235  0.0369  -0.0104 338 SER A C     
2542 O O     . SER A 338 ? 0.4763 0.4603 0.4802 0.0218  0.0361  -0.0119 338 SER A O     
2543 C CB    . SER A 338 ? 0.4839 0.4683 0.4915 0.0267  0.0373  -0.0107 338 SER A CB    
2544 O OG    . SER A 338 ? 0.6273 0.6116 0.6333 0.0280  0.0369  -0.0113 338 SER A OG    
2545 N N     . VAL A 339 ? 0.2511 0.2399 0.2616 0.0240  0.0379  -0.0088 339 VAL A N     
2546 C CA    . VAL A 339 ? 0.2371 0.2254 0.2476 0.0226  0.0381  -0.0088 339 VAL A CA    
2547 C C     . VAL A 339 ? 0.2735 0.2652 0.2825 0.0205  0.0372  -0.0088 339 VAL A C     
2548 O O     . VAL A 339 ? 0.3245 0.3138 0.3307 0.0183  0.0364  -0.0101 339 VAL A O     
2549 C CB    . VAL A 339 ? 0.2510 0.2412 0.2651 0.0240  0.0395  -0.0069 339 VAL A CB    
2550 C CG1   . VAL A 339 ? 0.2356 0.2259 0.2496 0.0228  0.0397  -0.0069 339 VAL A CG1   
2551 C CG2   . VAL A 339 ? 0.2343 0.2210 0.2495 0.0256  0.0404  -0.0070 339 VAL A CG2   
2552 N N     . TRP A 340 ? 0.3090 0.3067 0.3198 0.0209  0.0373  -0.0072 340 TRP A N     
2553 C CA    . TRP A 340 ? 0.2841 0.2863 0.2936 0.0185  0.0365  -0.0069 340 TRP A CA    
2554 C C     . TRP A 340 ? 0.2916 0.2901 0.2962 0.0163  0.0351  -0.0093 340 TRP A C     
2555 O O     . TRP A 340 ? 0.3176 0.3162 0.3196 0.0134  0.0342  -0.0100 340 TRP A O     
2556 C CB    . TRP A 340 ? 0.3122 0.3217 0.3245 0.0197  0.0369  -0.0047 340 TRP A CB    
2557 C CG    . TRP A 340 ? 0.3775 0.3930 0.3891 0.0172  0.0362  -0.0039 340 TRP A CG    
2558 C CD1   . TRP A 340 ? 0.3678 0.3888 0.3816 0.0168  0.0367  -0.0019 340 TRP A CD1   
2559 C CD2   . TRP A 340 ? 0.3563 0.3731 0.3644 0.0146  0.0348  -0.0052 340 TRP A CD2   
2560 N NE1   . TRP A 340 ? 0.3464 0.3727 0.3586 0.0138  0.0357  -0.0016 340 TRP A NE1   
2561 C CE2   . TRP A 340 ? 0.3297 0.3532 0.3382 0.0122  0.0345  -0.0038 340 TRP A CE2   
2562 C CE3   . TRP A 340 ? 0.2831 0.2961 0.2875 0.0140  0.0339  -0.0074 340 TRP A CE3   
2563 C CZ2   . TRP A 340 ? 0.2448 0.2711 0.2500 0.0089  0.0331  -0.0046 340 TRP A CZ2   
2564 C CZ3   . TRP A 340 ? 0.3376 0.3526 0.3385 0.0110  0.0327  -0.0084 340 TRP A CZ3   
2565 C CH2   . TRP A 340 ? 0.3069 0.3285 0.3082 0.0082  0.0323  -0.0070 340 TRP A CH2   
2566 N N     . ILE A 341 ? 0.2453 0.2406 0.2483 0.0177  0.0348  -0.0106 341 ILE A N     
2567 C CA    . ILE A 341 ? 0.3426 0.3338 0.3404 0.0162  0.0337  -0.0129 341 ILE A CA    
2568 C C     . ILE A 341 ? 0.3010 0.2852 0.2955 0.0148  0.0333  -0.0146 341 ILE A C     
2569 O O     . ILE A 341 ? 0.2854 0.2670 0.2757 0.0121  0.0324  -0.0160 341 ILE A O     
2570 C CB    . ILE A 341 ? 0.3450 0.3348 0.3420 0.0186  0.0338  -0.0137 341 ILE A CB    
2571 C CG1   . ILE A 341 ? 0.3539 0.3507 0.3543 0.0200  0.0342  -0.0117 341 ILE A CG1   
2572 C CG2   . ILE A 341 ? 0.2714 0.2567 0.2624 0.0175  0.0328  -0.0162 341 ILE A CG2   
2573 C CD1   . ILE A 341 ? 0.2966 0.2928 0.2966 0.0224  0.0343  -0.0121 341 ILE A CD1   
2574 N N     . GLY A 342 ? 0.2493 0.2303 0.2455 0.0165  0.0340  -0.0145 342 GLY A N     
2575 C CA    . GLY A 342 ? 0.2516 0.2272 0.2455 0.0151  0.0338  -0.0156 342 GLY A CA    
2576 C C     . GLY A 342 ? 0.2742 0.2526 0.2683 0.0122  0.0335  -0.0149 342 GLY A C     
2577 O O     . GLY A 342 ? 0.2812 0.2558 0.2718 0.0097  0.0327  -0.0160 342 GLY A O     
2578 N N     . GLY A 343 ? 0.3540 0.3393 0.3522 0.0125  0.0341  -0.0128 343 GLY A N     
2579 C CA    . GLY A 343 ? 0.3385 0.3281 0.3370 0.0098  0.0337  -0.0118 343 GLY A CA    
2580 C C     . GLY A 343 ? 0.3723 0.3621 0.3665 0.0063  0.0323  -0.0128 343 GLY A C     
2581 O O     . GLY A 343 ? 0.4270 0.4148 0.4183 0.0031  0.0316  -0.0135 343 GLY A O     
2582 N N     . SER A 344 ? 0.3786 0.3705 0.3721 0.0068  0.0321  -0.0131 344 SER A N     
2583 C CA    . SER A 344 ? 0.3971 0.3900 0.3865 0.0033  0.0308  -0.0140 344 SER A CA    
2584 C C     . SER A 344 ? 0.3687 0.3522 0.3517 0.0014  0.0299  -0.0168 344 SER A C     
2585 O O     . SER A 344 ? 0.3890 0.3715 0.3679 -0.0026 0.0289  -0.0176 344 SER A O     
2586 C CB    . SER A 344 ? 0.3743 0.3717 0.3644 0.0046  0.0308  -0.0137 344 SER A CB    
2587 O OG    . SER A 344 ? 0.2766 0.2743 0.2620 0.0011  0.0296  -0.0150 344 SER A OG    
2588 N N     . ILE A 345 ? 0.4731 0.4497 0.4549 0.0043  0.0304  -0.0181 345 ILE A N     
2589 C CA    . ILE A 345 ? 0.4656 0.4328 0.4414 0.0032  0.0298  -0.0205 345 ILE A CA    
2590 C C     . ILE A 345 ? 0.4522 0.4168 0.4267 0.0003  0.0294  -0.0204 345 ILE A C     
2591 O O     . ILE A 345 ? 0.5351 0.4957 0.5044 -0.0034 0.0284  -0.0216 345 ILE A O     
2592 C CB    . ILE A 345 ? 0.4733 0.4353 0.4491 0.0073  0.0305  -0.0213 345 ILE A CB    
2593 C CG1   . ILE A 345 ? 0.4873 0.4521 0.4641 0.0102  0.0309  -0.0213 345 ILE A CG1   
2594 C CG2   . ILE A 345 ? 0.4003 0.3524 0.3698 0.0067  0.0302  -0.0234 345 ILE A CG2   
2595 C CD1   . ILE A 345 ? 0.3871 0.3488 0.3650 0.0144  0.0317  -0.0215 345 ILE A CD1   
2596 N N     . LEU A 346 ? 0.4203 0.3868 0.3992 0.0018  0.0302  -0.0190 346 LEU A N     
2597 C CA    . LEU A 346 ? 0.4678 0.4326 0.4460 -0.0007 0.0299  -0.0186 346 LEU A CA    
2598 C C     . LEU A 346 ? 0.5208 0.4903 0.4977 -0.0053 0.0289  -0.0179 346 LEU A C     
2599 O O     . LEU A 346 ? 0.6228 0.5879 0.5951 -0.0090 0.0280  -0.0188 346 LEU A O     
2600 C CB    . LEU A 346 ? 0.4394 0.4074 0.4231 0.0017  0.0310  -0.0170 346 LEU A CB    
2601 C CG    . LEU A 346 ? 0.4617 0.4289 0.4453 -0.0004 0.0309  -0.0165 346 LEU A CG    
2602 C CD1   . LEU A 346 ? 0.4647 0.4226 0.4431 -0.0014 0.0303  -0.0182 346 LEU A CD1   
2603 C CD2   . LEU A 346 ? 0.4131 0.3835 0.4019 0.0023  0.0322  -0.0151 346 LEU A CD2   
2604 N N     . ALA A 347 ? 0.6296 0.6083 0.6103 -0.0053 0.0291  -0.0162 347 ALA A N     
2605 C CA    . ALA A 347 ? 0.6364 0.6214 0.6165 -0.0096 0.0283  -0.0150 347 ALA A CA    
2606 C C     . ALA A 347 ? 0.6596 0.6403 0.6330 -0.0138 0.0269  -0.0170 347 ALA A C     
2607 O O     . ALA A 347 ? 0.7096 0.6921 0.6805 -0.0186 0.0259  -0.0166 347 ALA A O     
2608 C CB    . ALA A 347 ? 0.6569 0.6527 0.6421 -0.0083 0.0288  -0.0127 347 ALA A CB    
2609 N N     . SER A 348 ? 0.4681 0.4428 0.4381 -0.0123 0.0268  -0.0191 348 SER A N     
2610 C CA    . SER A 348 ? 0.4254 0.3953 0.3884 -0.0159 0.0256  -0.0212 348 SER A CA    
2611 C C     . SER A 348 ? 0.4756 0.4334 0.4320 -0.0174 0.0252  -0.0234 348 SER A C     
2612 O O     . SER A 348 ? 0.5399 0.4924 0.4896 -0.0209 0.0242  -0.0253 348 SER A O     
2613 C CB    . SER A 348 ? 0.2894 0.2591 0.2516 -0.0132 0.0259  -0.0224 348 SER A CB    
2614 O OG    . SER A 348 ? 0.4138 0.3942 0.3816 -0.0117 0.0263  -0.0203 348 SER A OG    
2615 N N     . LEU A 349 ? 0.4539 0.4072 0.4118 -0.0148 0.0259  -0.0232 349 LEU A N     
2616 C CA    . LEU A 349 ? 0.4532 0.3955 0.4051 -0.0161 0.0256  -0.0249 349 LEU A CA    
2617 C C     . LEU A 349 ? 0.4632 0.4055 0.4123 -0.0220 0.0245  -0.0244 349 LEU A C     
2618 O O     . LEU A 349 ? 0.4662 0.4176 0.4197 -0.0239 0.0243  -0.0222 349 LEU A O     
2619 C CB    . LEU A 349 ? 0.4229 0.3617 0.3776 -0.0119 0.0266  -0.0245 349 LEU A CB    
2620 C CG    . LEU A 349 ? 0.4229 0.3609 0.3797 -0.0064 0.0276  -0.0250 349 LEU A CG    
2621 C CD1   . LEU A 349 ? 0.4084 0.3414 0.3660 -0.0031 0.0284  -0.0249 349 LEU A CD1   
2622 C CD2   . LEU A 349 ? 0.4552 0.3876 0.4060 -0.0062 0.0273  -0.0272 349 LEU A CD2   
2623 N N     . SER A 350 ? 0.5368 0.4689 0.4783 -0.0249 0.0238  -0.0262 350 SER A N     
2624 C CA    . SER A 350 ? 0.5845 0.5154 0.5222 -0.0311 0.0226  -0.0259 350 SER A CA    
2625 C C     . SER A 350 ? 0.5791 0.5094 0.5196 -0.0305 0.0230  -0.0244 350 SER A C     
2626 O O     . SER A 350 ? 0.5993 0.5355 0.5416 -0.0341 0.0224  -0.0227 350 SER A O     
2627 C CB    . SER A 350 ? 0.5928 0.5118 0.5208 -0.0342 0.0219  -0.0285 350 SER A CB    
2628 O OG    . SER A 350 ? 0.6037 0.5124 0.5287 -0.0295 0.0228  -0.0302 350 SER A OG    
2629 N N     . THR A 351 ? 0.5684 0.4917 0.5087 -0.0262 0.0239  -0.0250 351 THR A N     
2630 C CA    . THR A 351 ? 0.5672 0.4914 0.5113 -0.0248 0.0244  -0.0235 351 THR A CA    
2631 C C     . THR A 351 ? 0.5959 0.5328 0.5481 -0.0242 0.0248  -0.0211 351 THR A C     
2632 O O     . THR A 351 ? 0.5791 0.5201 0.5332 -0.0267 0.0246  -0.0195 351 THR A O     
2633 C CB    . THR A 351 ? 0.5786 0.4964 0.5231 -0.0191 0.0256  -0.0243 351 THR A CB    
2634 O OG1   . THR A 351 ? 0.5870 0.5073 0.5337 -0.0151 0.0263  -0.0250 351 THR A OG1   
2635 C CG2   . THR A 351 ? 0.5528 0.4577 0.4893 -0.0198 0.0254  -0.0261 351 THR A CG2   
2636 N N     . PHE A 352 ? 0.5182 0.4617 0.4750 -0.0209 0.0255  -0.0208 352 PHE A N     
2637 C CA    . PHE A 352 ? 0.4504 0.4053 0.4143 -0.0200 0.0260  -0.0184 352 PHE A CA    
2638 C C     . PHE A 352 ? 0.4201 0.3825 0.3838 -0.0251 0.0250  -0.0170 352 PHE A C     
2639 O O     . PHE A 352 ? 0.4938 0.4660 0.4630 -0.0246 0.0255  -0.0147 352 PHE A O     
2640 C CB    . PHE A 352 ? 0.4534 0.4136 0.4218 -0.0158 0.0269  -0.0182 352 PHE A CB    
2641 C CG    . PHE A 352 ? 0.3992 0.3690 0.3748 -0.0134 0.0280  -0.0158 352 PHE A CG    
2642 C CD1   . PHE A 352 ? 0.4183 0.3872 0.3974 -0.0099 0.0291  -0.0153 352 PHE A CD1   
2643 C CD2   . PHE A 352 ? 0.4192 0.3991 0.3979 -0.0144 0.0279  -0.0140 352 PHE A CD2   
2644 C CE1   . PHE A 352 ? 0.4171 0.3937 0.4022 -0.0076 0.0302  -0.0134 352 PHE A CE1   
2645 C CE2   . PHE A 352 ? 0.4075 0.3955 0.3924 -0.0118 0.0291  -0.0118 352 PHE A CE2   
2646 C CZ    . PHE A 352 ? 0.4449 0.4308 0.4328 -0.0083 0.0302  -0.0116 352 PHE A CZ    
2647 N N     . GLN A 353 ? 0.4472 0.4057 0.4048 -0.0302 0.0237  -0.0179 353 GLN A N     
2648 C CA    . GLN A 353 ? 0.5244 0.4913 0.4822 -0.0354 0.0227  -0.0162 353 GLN A CA    
2649 C C     . GLN A 353 ? 0.5332 0.5011 0.4919 -0.0375 0.0226  -0.0147 353 GLN A C     
2650 O O     . GLN A 353 ? 0.5666 0.5438 0.5274 -0.0406 0.0222  -0.0126 353 GLN A O     
2651 C CB    . GLN A 353 ? 0.4337 0.3976 0.3848 -0.0407 0.0213  -0.0177 353 GLN A CB    
2652 C CG    . GLN A 353 ? 0.4922 0.4573 0.4430 -0.0387 0.0215  -0.0189 353 GLN A CG    
2653 C CD    . GLN A 353 ? 0.6001 0.5768 0.5589 -0.0346 0.0225  -0.0168 353 GLN A CD    
2654 O OE1   . GLN A 353 ? 0.6915 0.6791 0.6541 -0.0363 0.0224  -0.0144 353 GLN A OE1   
2655 N NE2   . GLN A 353 ? 0.4945 0.4689 0.4554 -0.0293 0.0235  -0.0177 353 GLN A NE2   
2656 N N     . GLN A 354 ? 0.6371 0.5968 0.5949 -0.0352 0.0232  -0.0155 354 GLN A N     
2657 C CA    . GLN A 354 ? 0.6399 0.6000 0.5985 -0.0368 0.0231  -0.0141 354 GLN A CA    
2658 C C     . GLN A 354 ? 0.5848 0.5503 0.5503 -0.0317 0.0246  -0.0128 354 GLN A C     
2659 O O     . GLN A 354 ? 0.5231 0.4905 0.4903 -0.0322 0.0248  -0.0115 354 GLN A O     
2660 C CB    . GLN A 354 ? 0.5832 0.5305 0.5358 -0.0378 0.0227  -0.0157 354 GLN A CB    
2661 C CG    . GLN A 354 ? 0.7131 0.6512 0.6578 -0.0414 0.0217  -0.0178 354 GLN A CG    
2662 C CD    . GLN A 354 ? 0.7564 0.6980 0.6975 -0.0486 0.0201  -0.0170 354 GLN A CD    
2663 O OE1   . GLN A 354 ? 0.6998 0.6453 0.6396 -0.0509 0.0195  -0.0174 354 GLN A OE1   
2664 N NE2   . GLN A 354 ? 0.8259 0.7666 0.7653 -0.0525 0.0195  -0.0158 354 GLN A NE2   
2665 N N     . MET A 355 ? 0.4052 0.3729 0.3745 -0.0270 0.0256  -0.0131 355 MET A N     
2666 C CA    . MET A 355 ? 0.3236 0.2951 0.2987 -0.0222 0.0271  -0.0121 355 MET A CA    
2667 C C     . MET A 355 ? 0.3920 0.3755 0.3728 -0.0212 0.0278  -0.0098 355 MET A C     
2668 O O     . MET A 355 ? 0.4456 0.4325 0.4308 -0.0179 0.0291  -0.0088 355 MET A O     
2669 C CB    . MET A 355 ? 0.3715 0.3372 0.3471 -0.0174 0.0280  -0.0138 355 MET A CB    
2670 C CG    . MET A 355 ? 0.4336 0.3878 0.4034 -0.0182 0.0274  -0.0157 355 MET A CG    
2671 S SD    . MET A 355 ? 0.5308 0.4771 0.4993 -0.0133 0.0281  -0.0177 355 MET A SD    
2672 C CE    . MET A 355 ? 0.4918 0.4450 0.4679 -0.0083 0.0297  -0.0165 355 MET A CE    
2673 N N     . TRP A 356 ? 0.3471 0.3374 0.3276 -0.0240 0.0271  -0.0089 356 TRP A N     
2674 C CA    . TRP A 356 ? 0.3682 0.3705 0.3538 -0.0229 0.0278  -0.0063 356 TRP A CA    
2675 C C     . TRP A 356 ? 0.3768 0.3846 0.3645 -0.0239 0.0281  -0.0044 356 TRP A C     
2676 O O     . TRP A 356 ? 0.3098 0.3159 0.2942 -0.0283 0.0270  -0.0043 356 TRP A O     
2677 C CB    . TRP A 356 ? 0.2914 0.3006 0.2757 -0.0266 0.0267  -0.0054 356 TRP A CB    
2678 C CG    . TRP A 356 ? 0.2722 0.2795 0.2551 -0.0258 0.0265  -0.0068 356 TRP A CG    
2679 C CD1   . TRP A 356 ? 0.2879 0.2896 0.2650 -0.0297 0.0251  -0.0087 356 TRP A CD1   
2680 C CD2   . TRP A 356 ? 0.3325 0.3434 0.3196 -0.0210 0.0277  -0.0063 356 TRP A CD2   
2681 N NE1   . TRP A 356 ? 0.3160 0.3181 0.2936 -0.0274 0.0253  -0.0095 356 TRP A NE1   
2682 C CE2   . TRP A 356 ? 0.3189 0.3268 0.3027 -0.0222 0.0269  -0.0080 356 TRP A CE2   
2683 C CE3   . TRP A 356 ? 0.3102 0.3260 0.3031 -0.0159 0.0294  -0.0047 356 TRP A CE3   
2684 C CZ2   . TRP A 356 ? 0.2669 0.2773 0.2534 -0.0185 0.0276  -0.0078 356 TRP A CZ2   
2685 C CZ3   . TRP A 356 ? 0.3059 0.3236 0.3013 -0.0123 0.0302  -0.0046 356 TRP A CZ3   
2686 C CH2   . TRP A 356 ? 0.2606 0.2759 0.2529 -0.0137 0.0293  -0.0060 356 TRP A CH2   
2687 N N     . ILE A 357 ? 0.4028 0.4188 0.3960 -0.0202 0.0296  -0.0024 357 ILE A N     
2688 C CA    . ILE A 357 ? 0.3000 0.3234 0.2955 -0.0207 0.0301  -0.0002 357 ILE A CA    
2689 C C     . ILE A 357 ? 0.3605 0.3943 0.3562 -0.0240 0.0293  0.0020  357 ILE A C     
2690 O O     . ILE A 357 ? 0.3558 0.3943 0.3535 -0.0223 0.0297  0.0026  357 ILE A O     
2691 C CB    . ILE A 357 ? 0.2961 0.3244 0.2969 -0.0150 0.0322  0.0012  357 ILE A CB    
2692 C CG1   . ILE A 357 ? 0.3782 0.3975 0.3794 -0.0113 0.0332  -0.0008 357 ILE A CG1   
2693 C CG2   . ILE A 357 ? 0.3391 0.3772 0.3423 -0.0155 0.0327  0.0038  357 ILE A CG2   
2694 C CD1   . ILE A 357 ? 0.2882 0.3108 0.2939 -0.0058 0.0353  0.0002  357 ILE A CD1   
2695 N N     . SER A 358 ? 0.5036 0.5414 0.4972 -0.0291 0.0281  0.0032  358 SER A N     
2696 C CA    . SER A 358 ? 0.4948 0.5441 0.4886 -0.0329 0.0272  0.0056  358 SER A CA    
2697 C C     . SER A 358 ? 0.4182 0.4808 0.4165 -0.0314 0.0283  0.0091  358 SER A C     
2698 O O     . SER A 358 ? 0.4311 0.4940 0.4316 -0.0286 0.0295  0.0097  358 SER A O     
2699 C CB    . SER A 358 ? 0.5610 0.6070 0.5489 -0.0404 0.0250  0.0048  358 SER A CB    
2700 O OG    . SER A 358 ? 0.6576 0.7041 0.6446 -0.0431 0.0246  0.0058  358 SER A OG    
2701 N N     . LYS A 359 ? 0.3950 0.4689 0.3944 -0.0334 0.0279  0.0114  359 LYS A N     
2702 C CA    . LYS A 359 ? 0.4084 0.4964 0.4120 -0.0316 0.0290  0.0151  359 LYS A CA    
2703 C C     . LYS A 359 ? 0.4588 0.5497 0.4615 -0.0349 0.0284  0.0163  359 LYS A C     
2704 O O     . LYS A 359 ? 0.3936 0.4912 0.3999 -0.0314 0.0299  0.0184  359 LYS A O     
2705 C CB    . LYS A 359 ? 0.3708 0.4704 0.3750 -0.0341 0.0282  0.0174  359 LYS A CB    
2706 C CG    . LYS A 359 ? 0.3644 0.4806 0.3727 -0.0328 0.0292  0.0218  359 LYS A CG    
2707 C CD    . LYS A 359 ? 0.4368 0.5560 0.4504 -0.0243 0.0320  0.0232  359 LYS A CD    
2708 C CE    . LYS A 359 ? 0.4787 0.6142 0.4959 -0.0226 0.0331  0.0277  359 LYS A CE    
2709 N NZ    . LYS A 359 ? 0.5172 0.6544 0.5388 -0.0142 0.0361  0.0290  359 LYS A NZ    
2710 N N     . GLN A 360 ? 0.7450 0.8305 0.7427 -0.0416 0.0263  0.0150  360 GLN A N     
2711 C CA    . GLN A 360 ? 0.7963 0.8835 0.7925 -0.0454 0.0256  0.0161  360 GLN A CA    
2712 C C     . GLN A 360 ? 0.8651 0.9458 0.8633 -0.0403 0.0272  0.0150  360 GLN A C     
2713 O O     . GLN A 360 ? 0.8967 0.9848 0.8977 -0.0385 0.0282  0.0172  360 GLN A O     
2714 C CB    . GLN A 360 ? 0.7524 0.8308 0.7420 -0.0528 0.0232  0.0142  360 GLN A CB    
2715 C CG    . GLN A 360 ? 0.8047 0.8849 0.7919 -0.0582 0.0221  0.0155  360 GLN A CG    
2716 C CD    . GLN A 360 ? 0.9422 1.0135 0.9223 -0.0659 0.0197  0.0137  360 GLN A CD    
2717 O OE1   . GLN A 360 ? 0.9825 1.0472 0.9593 -0.0673 0.0190  0.0116  360 GLN A OE1   
2718 N NE2   . GLN A 360 ? 0.9642 1.0350 0.9415 -0.0710 0.0186  0.0147  360 GLN A NE2   
2719 N N     . GLU A 361 ? 0.7202 0.7877 0.7170 -0.0377 0.0275  0.0118  361 GLU A N     
2720 C CA    . GLU A 361 ? 0.7146 0.7752 0.7129 -0.0331 0.0289  0.0105  361 GLU A CA    
2721 C C     . GLU A 361 ? 0.6085 0.6756 0.6122 -0.0263 0.0313  0.0120  361 GLU A C     
2722 O O     . GLU A 361 ? 0.5928 0.6604 0.5980 -0.0242 0.0323  0.0124  361 GLU A O     
2723 C CB    . GLU A 361 ? 0.7525 0.7990 0.7482 -0.0317 0.0287  0.0071  361 GLU A CB    
2724 C CG    . GLU A 361 ? 0.8040 0.8414 0.7937 -0.0376 0.0266  0.0053  361 GLU A CG    
2725 C CD    . GLU A 361 ? 0.8448 0.8698 0.8319 -0.0358 0.0265  0.0021  361 GLU A CD    
2726 O OE1   . GLU A 361 ? 0.9054 0.9291 0.8957 -0.0303 0.0280  0.0014  361 GLU A OE1   
2727 O OE2   . GLU A 361 ? 0.8461 0.8627 0.8279 -0.0399 0.0251  0.0005  361 GLU A OE2   
2728 N N     . TYR A 362 ? 0.3884 0.4603 0.3948 -0.0230 0.0323  0.0128  362 TYR A N     
2729 C CA    . TYR A 362 ? 0.4051 0.4823 0.4160 -0.0165 0.0347  0.0142  362 TYR A CA    
2730 C C     . TYR A 362 ? 0.5279 0.6175 0.5409 -0.0166 0.0353  0.0175  362 TYR A C     
2731 O O     . TYR A 362 ? 0.5065 0.5975 0.5217 -0.0123 0.0371  0.0181  362 TYR A O     
2732 C CB    . TYR A 362 ? 0.3885 0.4694 0.4015 -0.0135 0.0354  0.0150  362 TYR A CB    
2733 C CG    . TYR A 362 ? 0.3841 0.4713 0.4015 -0.0069 0.0380  0.0170  362 TYR A CG    
2734 C CD1   . TYR A 362 ? 0.4385 0.5178 0.4572 -0.0015 0.0398  0.0152  362 TYR A CD1   
2735 C CD2   . TYR A 362 ? 0.3837 0.4847 0.4035 -0.0060 0.0387  0.0206  362 TYR A CD2   
2736 C CE1   . TYR A 362 ? 0.4251 0.5089 0.4471 0.0046  0.0423  0.0170  362 TYR A CE1   
2737 C CE2   . TYR A 362 ? 0.3520 0.4582 0.3754 0.0005  0.0413  0.0225  362 TYR A CE2   
2738 C CZ    . TYR A 362 ? 0.3799 0.4767 0.4041 0.0058  0.0431  0.0206  362 TYR A CZ    
2739 O OH    . TYR A 362 ? 0.4292 0.5298 0.4563 0.0122  0.0457  0.0223  362 TYR A OH    
2740 N N     . ASP A 363 ? 0.9015 1.0006 0.9136 -0.0216 0.0339  0.0197  363 ASP A N     
2741 C CA    . ASP A 363 ? 0.9069 1.0190 0.9209 -0.0219 0.0344  0.0232  363 ASP A CA    
2742 C C     . ASP A 363 ? 0.8366 0.9450 0.8493 -0.0236 0.0342  0.0225  363 ASP A C     
2743 O O     . ASP A 363 ? 0.7607 0.8750 0.7759 -0.0201 0.0358  0.0241  363 ASP A O     
2744 C CB    . ASP A 363 ? 0.8996 1.0226 0.9126 -0.0277 0.0326  0.0257  363 ASP A CB    
2745 C CG    . ASP A 363 ? 0.9424 1.0717 0.9576 -0.0252 0.0333  0.0270  363 ASP A CG    
2746 O OD1   . ASP A 363 ? 0.8981 1.0270 0.9166 -0.0182 0.0355  0.0271  363 ASP A OD1   
2747 O OD2   . ASP A 363 ? 1.0029 1.1377 1.0164 -0.0305 0.0315  0.0279  363 ASP A OD2   
2748 N N     . GLU A 364 ? 0.5760 0.6741 0.5846 -0.0284 0.0323  0.0201  364 GLU A N     
2749 C CA    . GLU A 364 ? 0.4772 0.5706 0.4842 -0.0302 0.0319  0.0194  364 GLU A CA    
2750 C C     . GLU A 364 ? 0.5570 0.6438 0.5659 -0.0239 0.0340  0.0177  364 GLU A C     
2751 O O     . GLU A 364 ? 0.6084 0.6950 0.6174 -0.0236 0.0344  0.0179  364 GLU A O     
2752 C CB    . GLU A 364 ? 0.4398 0.5220 0.4415 -0.0362 0.0296  0.0171  364 GLU A CB    
2753 C CG    . GLU A 364 ? 0.4805 0.5676 0.4790 -0.0438 0.0273  0.0184  364 GLU A CG    
2754 C CD    . GLU A 364 ? 0.5998 0.6733 0.5927 -0.0484 0.0255  0.0155  364 GLU A CD    
2755 O OE1   . GLU A 364 ? 0.6192 0.6806 0.6112 -0.0454 0.0260  0.0128  364 GLU A OE1   
2756 O OE2   . GLU A 364 ? 0.6097 0.6846 0.5989 -0.0548 0.0236  0.0160  364 GLU A OE2   
2757 N N     . SER A 365 ? 0.5404 0.6212 0.5506 -0.0191 0.0351  0.0159  365 SER A N     
2758 C CA    . SER A 365 ? 0.5408 0.6148 0.5525 -0.0134 0.0371  0.0141  365 SER A CA    
2759 C C     . SER A 365 ? 0.4257 0.5033 0.4410 -0.0066 0.0396  0.0149  365 SER A C     
2760 O O     . SER A 365 ? 0.3381 0.4165 0.3550 -0.0026 0.0414  0.0150  365 SER A O     
2761 C CB    . SER A 365 ? 0.6240 0.6837 0.6331 -0.0140 0.0362  0.0106  365 SER A CB    
2762 O OG    . SER A 365 ? 0.6619 0.7161 0.6680 -0.0178 0.0350  0.0097  365 SER A OG    
2763 N N     . GLY A 366 ? 0.5222 0.6020 0.5387 -0.0052 0.0398  0.0154  366 GLY A N     
2764 C CA    . GLY A 366 ? 0.4562 0.5379 0.4757 0.0013  0.0422  0.0160  366 GLY A CA    
2765 C C     . GLY A 366 ? 0.4769 0.5468 0.4958 0.0036  0.0425  0.0131  366 GLY A C     
2766 O O     . GLY A 366 ? 0.5754 0.6372 0.5917 0.0002  0.0408  0.0108  366 GLY A O     
2767 N N     . PRO A 367 ? 0.2734 0.3422 0.2944 0.0094  0.0447  0.0132  367 PRO A N     
2768 C CA    . PRO A 367 ? 0.3311 0.3894 0.3517 0.0115  0.0450  0.0106  367 PRO A CA    
2769 C C     . PRO A 367 ? 0.4201 0.4672 0.4384 0.0102  0.0443  0.0074  367 PRO A C     
2770 O O     . PRO A 367 ? 0.4857 0.5245 0.5032 0.0108  0.0441  0.0053  367 PRO A O     
2771 C CB    . PRO A 367 ? 0.3039 0.3636 0.3269 0.0179  0.0478  0.0116  367 PRO A CB    
2772 C CG    . PRO A 367 ? 0.3197 0.3928 0.3447 0.0191  0.0486  0.0153  367 PRO A CG    
2773 C CD    . PRO A 367 ? 0.2407 0.3187 0.2645 0.0142  0.0470  0.0160  367 PRO A CD    
2774 N N     . SER A 368 ? 0.4887 0.5357 0.5060 0.0086  0.0441  0.0071  368 SER A N     
2775 C CA    . SER A 368 ? 0.4044 0.4417 0.4198 0.0078  0.0437  0.0044  368 SER A CA    
2776 C C     . SER A 368 ? 0.3997 0.4313 0.4121 0.0029  0.0413  0.0030  368 SER A C     
2777 O O     . SER A 368 ? 0.3755 0.3986 0.3862 0.0025  0.0409  0.0008  368 SER A O     
2778 C CB    . SER A 368 ? 0.3949 0.4348 0.4102 0.0081  0.0444  0.0048  368 SER A CB    
2779 O OG    . SER A 368 ? 0.4013 0.4507 0.4168 0.0051  0.0436  0.0073  368 SER A OG    
2780 N N     . ILE A 369 ? 0.4915 0.5273 0.5031 -0.0005 0.0398  0.0041  369 ILE A N     
2781 C CA    . ILE A 369 ? 0.4801 0.5101 0.4883 -0.0052 0.0376  0.0028  369 ILE A CA    
2782 C C     . ILE A 369 ? 0.5056 0.5268 0.5130 -0.0034 0.0376  0.0005  369 ILE A C     
2783 O O     . ILE A 369 ? 0.5460 0.5596 0.5504 -0.0057 0.0363  -0.0013 369 ILE A O     
2784 C CB    . ILE A 369 ? 0.4060 0.4433 0.4135 -0.0091 0.0362  0.0046  369 ILE A CB    
2785 C CG1   . ILE A 369 ? 0.3696 0.4008 0.3726 -0.0145 0.0340  0.0033  369 ILE A CG1   
2786 C CG2   . ILE A 369 ? 0.3374 0.3793 0.3472 -0.0065 0.0370  0.0055  369 ILE A CG2   
2787 C CD1   . ILE A 369 ? 0.3987 0.4320 0.3995 -0.0193 0.0327  0.0042  369 ILE A CD1   
2788 N N     . VAL A 370 ? 0.4021 0.4241 0.4121 0.0009  0.0391  0.0006  370 VAL A N     
2789 C CA    . VAL A 370 ? 0.3817 0.3966 0.3912 0.0025  0.0390  -0.0013 370 VAL A CA    
2790 C C     . VAL A 370 ? 0.3708 0.3768 0.3791 0.0037  0.0393  -0.0035 370 VAL A C     
2791 O O     . VAL A 370 ? 0.3920 0.3913 0.3987 0.0035  0.0386  -0.0052 370 VAL A O     
2792 C CB    . VAL A 370 ? 0.4254 0.4440 0.4380 0.0067  0.0406  -0.0002 370 VAL A CB    
2793 C CG1   . VAL A 370 ? 0.3623 0.3827 0.3772 0.0107  0.0428  0.0005  370 VAL A CG1   
2794 C CG2   . VAL A 370 ? 0.4634 0.4753 0.4755 0.0082  0.0405  -0.0019 370 VAL A CG2   
2795 N N     . HIS A 371 ? 0.3134 0.3198 0.3225 0.0049  0.0403  -0.0034 371 HIS A N     
2796 C CA    . HIS A 371 ? 0.2972 0.2961 0.3050 0.0056  0.0404  -0.0054 371 HIS A CA    
2797 C C     . HIS A 371 ? 0.2868 0.2807 0.2914 0.0019  0.0386  -0.0063 371 HIS A C     
2798 O O     . HIS A 371 ? 0.3349 0.3218 0.3380 0.0024  0.0384  -0.0080 371 HIS A O     
2799 C CB    . HIS A 371 ? 0.2824 0.2835 0.2915 0.0074  0.0418  -0.0051 371 HIS A CB    
2800 C CG    . HIS A 371 ? 0.3086 0.3136 0.3203 0.0113  0.0438  -0.0042 371 HIS A CG    
2801 N ND1   . HIS A 371 ? 0.3046 0.3055 0.3171 0.0144  0.0450  -0.0052 371 HIS A ND1   
2802 C CD2   . HIS A 371 ? 0.3523 0.3650 0.3658 0.0128  0.0450  -0.0022 371 HIS A CD2   
2803 C CE1   . HIS A 371 ? 0.3356 0.3406 0.3501 0.0177  0.0468  -0.0039 371 HIS A CE1   
2804 N NE2   . HIS A 371 ? 0.3854 0.3976 0.4004 0.0170  0.0469  -0.0021 371 HIS A NE2   
2805 N N     . ARG A 372 ? 0.3548 0.3519 0.3579 -0.0017 0.0374  -0.0052 372 ARG A N     
2806 C CA    . ARG A 372 ? 0.4098 0.4015 0.4092 -0.0052 0.0359  -0.0060 372 ARG A CA    
2807 C C     . ARG A 372 ? 0.4003 0.3883 0.3970 -0.0074 0.0345  -0.0067 372 ARG A C     
2808 O O     . ARG A 372 ? 0.4830 0.4642 0.4762 -0.0094 0.0334  -0.0077 372 ARG A O     
2809 C CB    . ARG A 372 ? 0.5145 0.5108 0.5132 -0.0085 0.0353  -0.0044 372 ARG A CB    
2810 C CG    . ARG A 372 ? 0.5985 0.6036 0.5980 -0.0108 0.0348  -0.0023 372 ARG A CG    
2811 C CD    . ARG A 372 ? 0.6605 0.6707 0.6595 -0.0139 0.0344  -0.0006 372 ARG A CD    
2812 N NE    . ARG A 372 ? 0.7393 0.7607 0.7412 -0.0134 0.0351  0.0017  372 ARG A NE    
2813 C CZ    . ARG A 372 ? 0.8447 0.8712 0.8499 -0.0094 0.0369  0.0025  372 ARG A CZ    
2814 N NH1   . ARG A 372 ? 0.9037 0.9250 0.9095 -0.0060 0.0381  0.0009  372 ARG A NH1   
2815 N NH2   . ARG A 372 ? 0.8123 0.8492 0.8198 -0.0086 0.0377  0.0049  372 ARG A NH2   
2816 N N     . LYS A 373 ? 0.4412 0.4337 0.4392 -0.0070 0.0346  -0.0060 373 LYS A N     
2817 C CA    . LYS A 373 ? 0.4988 0.4887 0.4943 -0.0090 0.0334  -0.0067 373 LYS A CA    
2818 C C     . LYS A 373 ? 0.6211 0.6061 0.6170 -0.0057 0.0339  -0.0082 373 LYS A C     
2819 O O     . LYS A 373 ? 0.7344 0.7120 0.7271 -0.0063 0.0331  -0.0098 373 LYS A O     
2820 C CB    . LYS A 373 ? 0.5111 0.5099 0.5077 -0.0110 0.0330  -0.0048 373 LYS A CB    
2821 C CG    . LYS A 373 ? 0.5426 0.5467 0.5381 -0.0152 0.0321  -0.0031 373 LYS A CG    
2822 C CD    . LYS A 373 ? 0.6343 0.6310 0.6245 -0.0198 0.0304  -0.0042 373 LYS A CD    
2823 C CE    . LYS A 373 ? 0.6586 0.6583 0.6478 -0.0234 0.0298  -0.0028 373 LYS A CE    
2824 N NZ    . LYS A 373 ? 0.6266 0.6169 0.6106 -0.0269 0.0285  -0.0040 373 LYS A NZ    
2825 N N     . CYS A 374 ? 0.6007 0.5896 0.6004 -0.0022 0.0352  -0.0077 374 CYS A N     
2826 C CA    . CYS A 374 ? 0.5973 0.5825 0.5976 0.0008  0.0358  -0.0088 374 CYS A CA    
2827 C C     . CYS A 374 ? 0.6447 0.6261 0.6463 0.0037  0.0369  -0.0097 374 CYS A C     
2828 O O     . CYS A 374 ? 0.6899 0.6746 0.6943 0.0060  0.0383  -0.0089 374 CYS A O     
2829 C CB    . CYS A 374 ? 0.5859 0.5774 0.5893 0.0027  0.0366  -0.0075 374 CYS A CB    
2830 S SG    . CYS A 374 ? 0.6493 0.6494 0.6527 -0.0004 0.0357  -0.0055 374 CYS A SG    
2831 N N     . PHE A 375 ? 0.6369 0.6114 0.6361 0.0037  0.0364  -0.0112 375 PHE A N     
2832 C CA    . PHE A 375 ? 0.6321 0.6032 0.6322 0.0061  0.0373  -0.0121 375 PHE A CA    
2833 C C     . PHE A 375 ? 0.5686 0.5333 0.5665 0.0069  0.0367  -0.0135 375 PHE A C     
2834 O O     . PHE A 375 ? 0.5173 0.4805 0.5135 0.0063  0.0359  -0.0139 375 PHE A O     
2835 C CB    . PHE A 375 ? 0.6919 0.6629 0.6915 0.0050  0.0374  -0.0119 375 PHE A CB    
2836 C CG    . PHE A 375 ? 0.6556 0.6225 0.6516 0.0021  0.0360  -0.0122 375 PHE A CG    
2837 C CD1   . PHE A 375 ? 0.5322 0.5008 0.5263 -0.0013 0.0349  -0.0115 375 PHE A CD1   
2838 C CD2   . PHE A 375 ? 0.6915 0.6531 0.6858 0.0026  0.0359  -0.0131 375 PHE A CD2   
2839 C CE1   . PHE A 375 ? 0.6080 0.5718 0.5982 -0.0041 0.0337  -0.0118 375 PHE A CE1   
2840 C CE2   . PHE A 375 ? 0.6450 0.6023 0.6357 0.0002  0.0348  -0.0133 375 PHE A CE2   
2841 C CZ    . PHE A 375 ? 0.6529 0.6108 0.6413 -0.0032 0.0338  -0.0126 375 PHE A CZ    
2842 N N     . GLU B 7   ? 0.8579 0.7943 0.7799 -0.0831 0.0137  -0.0089 7   GLU B N     
2843 C CA    . GLU B 7   ? 0.8275 0.7633 0.7547 -0.0745 0.0155  -0.0100 7   GLU B CA    
2844 C C     . GLU B 7   ? 0.8614 0.7814 0.7830 -0.0715 0.0160  -0.0130 7   GLU B C     
2845 O O     . GLU B 7   ? 0.7914 0.7015 0.7098 -0.0705 0.0163  -0.0133 7   GLU B O     
2846 C CB    . GLU B 7   ? 0.8261 0.7682 0.7601 -0.0705 0.0166  -0.0080 7   GLU B CB    
2847 C CG    . GLU B 7   ? 0.9060 0.8410 0.8369 -0.0724 0.0163  -0.0072 7   GLU B CG    
2848 C CD    . GLU B 7   ? 0.9122 0.8546 0.8425 -0.0793 0.0150  -0.0046 7   GLU B CD    
2849 O OE1   . GLU B 7   ? 0.9249 0.8769 0.8559 -0.0833 0.0141  -0.0035 7   GLU B OE1   
2850 O OE2   . GLU B 7   ? 0.8246 0.7639 0.7538 -0.0806 0.0149  -0.0034 7   GLU B OE2   
2851 N N     . LEU B 8   ? 0.8895 0.8075 0.8096 -0.0698 0.0162  -0.0151 8   LEU B N     
2852 C CA    . LEU B 8   ? 0.8830 0.7873 0.7981 -0.0662 0.0168  -0.0179 8   LEU B CA    
2853 C C     . LEU B 8   ? 0.8262 0.7302 0.7469 -0.0581 0.0185  -0.0179 8   LEU B C     
2854 O O     . LEU B 8   ? 0.7561 0.6488 0.6731 -0.0545 0.0192  -0.0195 8   LEU B O     
2855 C CB    . LEU B 8   ? 0.8469 0.7502 0.7590 -0.0668 0.0165  -0.0200 8   LEU B CB    
2856 C CG    . LEU B 8   ? 0.8133 0.7006 0.7184 -0.0639 0.0171  -0.0228 8   LEU B CG    
2857 C CD1   . LEU B 8   ? 0.8064 0.6816 0.7007 -0.0706 0.0159  -0.0241 8   LEU B CD1   
2858 C CD2   . LEU B 8   ? 0.7715 0.6593 0.6784 -0.0584 0.0180  -0.0246 8   LEU B CD2   
2859 N N     . SER B 9   ? 0.9591 0.8754 0.8882 -0.0553 0.0192  -0.0161 9   SER B N     
2860 C CA    . SER B 9   ? 0.9641 0.8811 0.8986 -0.0484 0.0207  -0.0160 9   SER B CA    
2861 C C     . SER B 9   ? 0.9589 0.8661 0.8907 -0.0466 0.0212  -0.0162 9   SER B C     
2862 O O     . SER B 9   ? 0.9646 0.8675 0.8976 -0.0410 0.0223  -0.0171 9   SER B O     
2863 C CB    . SER B 9   ? 0.9822 0.9130 0.9246 -0.0475 0.0211  -0.0137 9   SER B CB    
2864 O OG    . SER B 9   ? 0.9711 0.9070 0.9127 -0.0534 0.0200  -0.0118 9   SER B OG    
2865 N N     . ILE B 10  ? 0.9181 0.8224 0.8464 -0.0514 0.0203  -0.0150 10  ILE B N     
2866 C CA    . ILE B 10  ? 0.9016 0.7971 0.8274 -0.0498 0.0208  -0.0148 10  ILE B CA    
2867 C C     . ILE B 10  ? 0.8789 0.7599 0.7977 -0.0477 0.0211  -0.0170 10  ILE B C     
2868 O O     . ILE B 10  ? 0.9436 0.8186 0.8622 -0.0432 0.0221  -0.0171 10  ILE B O     
2869 C CB    . ILE B 10  ? 0.9341 0.8296 0.8573 -0.0559 0.0197  -0.0128 10  ILE B CB    
2870 C CG1   . ILE B 10  ? 0.9173 0.8276 0.8478 -0.0570 0.0196  -0.0104 10  ILE B CG1   
2871 C CG2   . ILE B 10  ? 0.9764 0.8626 0.8968 -0.0542 0.0202  -0.0124 10  ILE B CG2   
2872 C CD1   . ILE B 10  ? 0.9301 0.8456 0.8675 -0.0510 0.0210  -0.0096 10  ILE B CD1   
2873 N N     . SER B 11  ? 0.6251 0.5004 0.5379 -0.0506 0.0204  -0.0187 11  SER B N     
2874 C CA    . SER B 11  ? 0.6002 0.4613 0.5056 -0.0484 0.0209  -0.0209 11  SER B CA    
2875 C C     . SER B 11  ? 0.5445 0.4066 0.4532 -0.0414 0.0221  -0.0223 11  SER B C     
2876 O O     . SER B 11  ? 0.5150 0.3669 0.4195 -0.0374 0.0230  -0.0235 11  SER B O     
2877 C CB    . SER B 11  ? 0.7302 0.5843 0.6273 -0.0543 0.0197  -0.0225 11  SER B CB    
2878 O OG    . SER B 11  ? 0.8449 0.7080 0.7448 -0.0555 0.0192  -0.0232 11  SER B OG    
2879 N N     . LEU B 12  ? 0.7858 0.6601 0.7018 -0.0397 0.0223  -0.0219 12  LEU B N     
2880 C CA    . LEU B 12  ? 0.8262 0.7030 0.7464 -0.0331 0.0235  -0.0228 12  LEU B CA    
2881 C C     . LEU B 12  ? 0.8627 0.7426 0.7886 -0.0282 0.0246  -0.0215 12  LEU B C     
2882 O O     . LEU B 12  ? 0.8731 0.7505 0.8000 -0.0226 0.0257  -0.0222 12  LEU B O     
2883 C CB    . LEU B 12  ? 0.7742 0.6627 0.6999 -0.0334 0.0233  -0.0227 12  LEU B CB    
2884 C CG    . LEU B 12  ? 0.9082 0.7941 0.8293 -0.0351 0.0228  -0.0246 12  LEU B CG    
2885 C CD1   . LEU B 12  ? 0.8378 0.7360 0.7634 -0.0379 0.0221  -0.0238 12  LEU B CD1   
2886 C CD2   . LEU B 12  ? 0.9602 0.8412 0.8805 -0.0291 0.0239  -0.0264 12  LEU B CD2   
2887 N N     . SER B 13  ? 0.7817 0.6672 0.7112 -0.0302 0.0244  -0.0195 13  SER B N     
2888 C CA    . SER B 13  ? 0.7835 0.6705 0.7171 -0.0261 0.0254  -0.0184 13  SER B CA    
2889 C C     . SER B 13  ? 0.7427 0.6178 0.6705 -0.0245 0.0258  -0.0187 13  SER B C     
2890 O O     . SER B 13  ? 0.7454 0.6193 0.6751 -0.0193 0.0268  -0.0187 13  SER B O     
2891 C CB    . SER B 13  ? 0.7999 0.6956 0.7382 -0.0288 0.0251  -0.0163 13  SER B CB    
2892 O OG    . SER B 13  ? 0.8531 0.7605 0.7980 -0.0281 0.0253  -0.0158 13  SER B OG    
2893 N N     . LEU B 14  ? 0.6616 0.5280 0.5822 -0.0288 0.0249  -0.0190 14  LEU B N     
2894 C CA    . LEU B 14  ? 0.7255 0.5800 0.6401 -0.0273 0.0254  -0.0190 14  LEU B CA    
2895 C C     . LEU B 14  ? 0.7854 0.6317 0.6961 -0.0224 0.0263  -0.0208 14  LEU B C     
2896 O O     . LEU B 14  ? 0.7909 0.6280 0.6971 -0.0198 0.0270  -0.0206 14  LEU B O     
2897 C CB    . LEU B 14  ? 0.6766 0.5235 0.5842 -0.0337 0.0243  -0.0186 14  LEU B CB    
2898 C CG    . LEU B 14  ? 0.5755 0.4294 0.4861 -0.0383 0.0234  -0.0164 14  LEU B CG    
2899 C CD1   . LEU B 14  ? 0.5324 0.3785 0.4353 -0.0453 0.0222  -0.0162 14  LEU B CD1   
2900 C CD2   . LEU B 14  ? 0.5491 0.4044 0.4632 -0.0350 0.0242  -0.0146 14  LEU B CD2   
2901 N N     . ASP B 15  ? 0.9716 0.8214 0.8838 -0.0208 0.0264  -0.0223 15  ASP B N     
2902 C CA    . ASP B 15  ? 0.9604 0.8043 0.8699 -0.0154 0.0275  -0.0238 15  ASP B CA    
2903 C C     . ASP B 15  ? 0.9557 0.8034 0.8703 -0.0091 0.0287  -0.0229 15  ASP B C     
2904 O O     . ASP B 15  ? 1.0173 0.8580 0.9284 -0.0046 0.0297  -0.0234 15  ASP B O     
2905 C CB    . ASP B 15  ? 0.9950 0.8434 0.9056 -0.0155 0.0272  -0.0255 15  ASP B CB    
2906 C CG    . ASP B 15  ? 1.0844 0.9268 0.9880 -0.0210 0.0262  -0.0269 15  ASP B CG    
2907 O OD1   . ASP B 15  ? 1.1140 0.9443 1.0093 -0.0228 0.0260  -0.0276 15  ASP B OD1   
2908 O OD2   . ASP B 15  ? 1.1128 0.9626 1.0190 -0.0234 0.0255  -0.0275 15  ASP B OD2   
2909 N N     . SER B 16  ? 0.7280 0.5867 0.6507 -0.0087 0.0288  -0.0215 16  SER B N     
2910 C CA    . SER B 16  ? 0.6839 0.5479 0.6120 -0.0032 0.0299  -0.0210 16  SER B CA    
2911 C C     . SER B 16  ? 0.7409 0.5971 0.6652 0.0006  0.0307  -0.0204 16  SER B C     
2912 O O     . SER B 16  ? 0.6228 0.4738 0.5439 -0.0015 0.0305  -0.0193 16  SER B O     
2913 C CB    . SER B 16  ? 0.7209 0.5956 0.6567 -0.0040 0.0298  -0.0195 16  SER B CB    
2914 O OG    . SER B 16  ? 0.7715 0.6504 0.7116 0.0009  0.0308  -0.0190 16  SER B OG    
2915 N N     . PRO B 17  ? 0.8719 0.7273 0.7964 0.0061  0.0317  -0.0208 17  PRO B N     
2916 C CA    . PRO B 17  ? 0.8429 0.6922 0.7642 0.0101  0.0327  -0.0198 17  PRO B CA    
2917 C C     . PRO B 17  ? 0.8340 0.6890 0.7601 0.0104  0.0329  -0.0178 17  PRO B C     
2918 O O     . PRO B 17  ? 0.8245 0.6741 0.7475 0.0119  0.0334  -0.0166 17  PRO B O     
2919 C CB    . PRO B 17  ? 0.7923 0.6429 0.7142 0.0157  0.0337  -0.0205 17  PRO B CB    
2920 C CG    . PRO B 17  ? 0.7673 0.6285 0.6961 0.0150  0.0333  -0.0210 17  PRO B CG    
2921 C CD    . PRO B 17  ? 0.8769 0.7386 0.8052 0.0091  0.0321  -0.0217 17  PRO B CD    
2922 N N     . LYS B 18  ? 0.7910 0.6566 0.7243 0.0090  0.0326  -0.0175 18  LYS B N     
2923 C CA    . LYS B 18  ? 0.7395 0.6111 0.6775 0.0096  0.0329  -0.0159 18  LYS B CA    
2924 C C     . LYS B 18  ? 0.7080 0.5811 0.6468 0.0050  0.0321  -0.0148 18  LYS B C     
2925 O O     . LYS B 18  ? 0.7804 0.6597 0.7237 0.0051  0.0323  -0.0137 18  LYS B O     
2926 C CB    . LYS B 18  ? 0.7386 0.6204 0.6837 0.0118  0.0333  -0.0160 18  LYS B CB    
2927 C CG    . LYS B 18  ? 0.8246 0.7063 0.7696 0.0172  0.0342  -0.0160 18  LYS B CG    
2928 C CD    . LYS B 18  ? 0.8809 0.7555 0.8210 0.0199  0.0348  -0.0149 18  LYS B CD    
2929 C CE    . LYS B 18  ? 0.8332 0.7107 0.7755 0.0195  0.0350  -0.0131 18  LYS B CE    
2930 N NZ    . LYS B 18  ? 0.7775 0.6458 0.7136 0.0194  0.0351  -0.0120 18  LYS B NZ    
2931 N N     . LEU B 19  ? 0.5766 0.4441 0.5109 0.0008  0.0313  -0.0152 19  LEU B N     
2932 C CA    . LEU B 19  ? 0.5951 0.4638 0.5296 -0.0038 0.0305  -0.0139 19  LEU B CA    
2933 C C     . LEU B 19  ? 0.6684 0.5347 0.6020 -0.0022 0.0310  -0.0122 19  LEU B C     
2934 O O     . LEU B 19  ? 0.6904 0.5483 0.6190 0.0004  0.0316  -0.0120 19  LEU B O     
2935 C CB    . LEU B 19  ? 0.5855 0.4464 0.5136 -0.0084 0.0296  -0.0144 19  LEU B CB    
2936 C CG    . LEU B 19  ? 0.6080 0.4725 0.5368 -0.0145 0.0285  -0.0135 19  LEU B CG    
2937 C CD1   . LEU B 19  ? 0.4682 0.3426 0.4023 -0.0160 0.0281  -0.0142 19  LEU B CD1   
2938 C CD2   . LEU B 19  ? 0.6980 0.5520 0.6186 -0.0187 0.0276  -0.0137 19  LEU B CD2   
2939 N N     . ASP B 20  ? 0.7324 0.6062 0.6707 -0.0037 0.0309  -0.0110 20  ASP B N     
2940 C CA    . ASP B 20  ? 0.6330 0.5057 0.5709 -0.0027 0.0313  -0.0092 20  ASP B CA    
2941 C C     . ASP B 20  ? 0.6807 0.5522 0.6168 -0.0079 0.0304  -0.0079 20  ASP B C     
2942 O O     . ASP B 20  ? 0.6668 0.5385 0.6019 -0.0120 0.0295  -0.0085 20  ASP B O     
2943 C CB    . ASP B 20  ? 0.6349 0.5168 0.5792 0.0004  0.0320  -0.0087 20  ASP B CB    
2944 C CG    . ASP B 20  ? 0.7352 0.6273 0.6857 -0.0017 0.0318  -0.0091 20  ASP B CG    
2945 O OD1   . ASP B 20  ? 0.7156 0.6100 0.6665 -0.0058 0.0311  -0.0084 20  ASP B OD1   
2946 O OD2   . ASP B 20  ? 0.7473 0.6454 0.7022 0.0008  0.0323  -0.0099 20  ASP B OD2   
2947 N N     . GLU B 21  ? 0.6932 0.5636 0.6285 -0.0077 0.0306  -0.0061 21  GLU B N     
2948 C CA    . GLU B 21  ? 0.6359 0.5058 0.5697 -0.0126 0.0297  -0.0045 21  GLU B CA    
2949 C C     . GLU B 21  ? 0.5589 0.4397 0.4983 -0.0160 0.0292  -0.0044 21  GLU B C     
2950 O O     . GLU B 21  ? 0.5542 0.4348 0.4918 -0.0209 0.0282  -0.0039 21  GLU B O     
2951 C CB    . GLU B 21  ? 0.6570 0.5248 0.5896 -0.0110 0.0302  -0.0024 21  GLU B CB    
2952 C CG    . GLU B 21  ? 0.6966 0.5542 0.6237 -0.0070 0.0310  -0.0021 21  GLU B CG    
2953 C CD    . GLU B 21  ? 0.7493 0.6055 0.6754 -0.0056 0.0315  0.0004  21  GLU B CD    
2954 O OE1   . GLU B 21  ? 0.7286 0.5939 0.6599 -0.0058 0.0316  0.0015  21  GLU B OE1   
2955 O OE2   . GLU B 21  ? 0.8025 0.6482 0.7223 -0.0041 0.0319  0.0014  21  GLU B OE2   
2956 N N     . SER B 22  ? 0.5541 0.4442 0.4998 -0.0134 0.0298  -0.0049 22  SER B N     
2957 C CA    . SER B 22  ? 0.5833 0.4835 0.5342 -0.0157 0.0295  -0.0049 22  SER B CA    
2958 C C     . SER B 22  ? 0.5869 0.4881 0.5376 -0.0181 0.0289  -0.0061 22  SER B C     
2959 O O     . SER B 22  ? 0.6033 0.5086 0.5546 -0.0222 0.0282  -0.0055 22  SER B O     
2960 C CB    . SER B 22  ? 0.5879 0.4965 0.5450 -0.0121 0.0305  -0.0054 22  SER B CB    
2961 O OG    . SER B 22  ? 0.5287 0.4463 0.4903 -0.0137 0.0305  -0.0056 22  SER B OG    
2962 N N     . ASP B 23  ? 0.7590 0.6567 0.7088 -0.0155 0.0292  -0.0078 23  ASP B N     
2963 C CA    . ASP B 23  ? 0.8323 0.7308 0.7816 -0.0174 0.0287  -0.0090 23  ASP B CA    
2964 C C     . ASP B 23  ? 0.8012 0.6939 0.7449 -0.0226 0.0275  -0.0085 23  ASP B C     
2965 O O     . ASP B 23  ? 0.7984 0.6955 0.7429 -0.0262 0.0267  -0.0086 23  ASP B O     
2966 C CB    . ASP B 23  ? 0.8925 0.7871 0.8409 -0.0136 0.0292  -0.0108 23  ASP B CB    
2967 C CG    . ASP B 23  ? 1.0388 0.9399 0.9928 -0.0092 0.0302  -0.0113 23  ASP B CG    
2968 O OD1   . ASP B 23  ? 1.0981 1.0070 1.0569 -0.0094 0.0305  -0.0106 23  ASP B OD1   
2969 O OD2   . ASP B 23  ? 1.0602 0.9582 1.0135 -0.0056 0.0307  -0.0123 23  ASP B OD2   
2970 N N     . PHE B 24  ? 0.4698 0.3527 0.4077 -0.0231 0.0273  -0.0080 24  PHE B N     
2971 C CA    . PHE B 24  ? 0.4505 0.3268 0.3823 -0.0285 0.0262  -0.0075 24  PHE B CA    
2972 C C     . PHE B 24  ? 0.5155 0.3991 0.4495 -0.0333 0.0254  -0.0056 24  PHE B C     
2973 O O     . PHE B 24  ? 0.4478 0.3333 0.3806 -0.0380 0.0244  -0.0056 24  PHE B O     
2974 C CB    . PHE B 24  ? 0.3788 0.2432 0.3043 -0.0273 0.0265  -0.0069 24  PHE B CB    
2975 C CG    . PHE B 24  ? 0.4849 0.3395 0.4026 -0.0326 0.0255  -0.0066 24  PHE B CG    
2976 C CD1   . PHE B 24  ? 0.5742 0.4210 0.4864 -0.0337 0.0252  -0.0085 24  PHE B CD1   
2977 C CD2   . PHE B 24  ? 0.4911 0.3437 0.4066 -0.0363 0.0249  -0.0045 24  PHE B CD2   
2978 C CE1   . PHE B 24  ? 0.5423 0.3792 0.4467 -0.0388 0.0243  -0.0083 24  PHE B CE1   
2979 C CE2   . PHE B 24  ? 0.5075 0.3503 0.4152 -0.0414 0.0240  -0.0041 24  PHE B CE2   
2980 C CZ    . PHE B 24  ? 0.5314 0.3660 0.4334 -0.0428 0.0237  -0.0062 24  PHE B CZ    
2981 N N     . ILE B 25  ? 0.5802 0.4686 0.5176 -0.0322 0.0258  -0.0041 25  ILE B N     
2982 C CA    . ILE B 25  ? 0.5125 0.4075 0.4515 -0.0367 0.0251  -0.0021 25  ILE B CA    
2983 C C     . ILE B 25  ? 0.4772 0.3830 0.4210 -0.0382 0.0249  -0.0025 25  ILE B C     
2984 O O     . ILE B 25  ? 0.5573 0.4666 0.5003 -0.0432 0.0239  -0.0014 25  ILE B O     
2985 C CB    . ILE B 25  ? 0.4569 0.3559 0.3991 -0.0346 0.0258  -0.0005 25  ILE B CB    
2986 C CG1   . ILE B 25  ? 0.5015 0.3894 0.4381 -0.0336 0.0259  0.0003  25  ILE B CG1   
2987 C CG2   . ILE B 25  ? 0.3715 0.2793 0.3162 -0.0387 0.0252  0.0014  25  ILE B CG2   
2988 C CD1   . ILE B 25  ? 0.4499 0.3409 0.3897 -0.0298 0.0269  0.0014  25  ILE B CD1   
2989 N N     . LEU B 26  ? 0.4881 0.3991 0.4368 -0.0337 0.0258  -0.0038 26  LEU B N     
2990 C CA    . LEU B 26  ? 0.4901 0.4110 0.4434 -0.0344 0.0258  -0.0040 26  LEU B CA    
2991 C C     . LEU B 26  ? 0.4739 0.3931 0.4242 -0.0376 0.0249  -0.0048 26  LEU B C     
2992 O O     . LEU B 26  ? 0.5366 0.4631 0.4884 -0.0411 0.0242  -0.0039 26  LEU B O     
2993 C CB    . LEU B 26  ? 0.5314 0.4573 0.4902 -0.0288 0.0272  -0.0051 26  LEU B CB    
2994 C CG    . LEU B 26  ? 0.5307 0.4618 0.4934 -0.0264 0.0281  -0.0042 26  LEU B CG    
2995 C CD1   . LEU B 26  ? 0.5027 0.4356 0.4692 -0.0211 0.0293  -0.0057 26  LEU B CD1   
2996 C CD2   . LEU B 26  ? 0.4665 0.4079 0.4327 -0.0289 0.0280  -0.0028 26  LEU B CD2   
2997 N N     . LEU B 27  ? 0.4590 0.3686 0.4049 -0.0365 0.0248  -0.0064 27  LEU B N     
2998 C CA    . LEU B 27  ? 0.5180 0.4251 0.4604 -0.0396 0.0239  -0.0075 27  LEU B CA    
2999 C C     . LEU B 27  ? 0.5326 0.4349 0.4690 -0.0462 0.0225  -0.0065 27  LEU B C     
3000 O O     . LEU B 27  ? 0.4727 0.3788 0.4081 -0.0505 0.0216  -0.0064 27  LEU B O     
3001 C CB    . LEU B 27  ? 0.5024 0.4007 0.4416 -0.0360 0.0244  -0.0096 27  LEU B CB    
3002 C CG    . LEU B 27  ? 0.5474 0.4510 0.4920 -0.0308 0.0255  -0.0109 27  LEU B CG    
3003 C CD1   . LEU B 27  ? 0.5144 0.4086 0.4553 -0.0270 0.0260  -0.0126 27  LEU B CD1   
3004 C CD2   . LEU B 27  ? 0.6229 0.5350 0.5705 -0.0326 0.0251  -0.0110 27  LEU B CD2   
3005 N N     . SER B 28  ? 0.5787 0.4731 0.5109 -0.0472 0.0224  -0.0056 28  SER B N     
3006 C CA    . SER B 28  ? 0.5594 0.4491 0.4857 -0.0539 0.0210  -0.0045 28  SER B CA    
3007 C C     . SER B 28  ? 0.6230 0.5246 0.5531 -0.0583 0.0203  -0.0023 28  SER B C     
3008 O O     . SER B 28  ? 0.6444 0.5481 0.5719 -0.0643 0.0190  -0.0017 28  SER B O     
3009 C CB    . SER B 28  ? 0.6281 0.5061 0.5489 -0.0537 0.0212  -0.0038 28  SER B CB    
3010 O OG    . SER B 28  ? 0.7422 0.6079 0.6576 -0.0509 0.0217  -0.0058 28  SER B OG    
3011 N N     . VAL B 29  ? 0.5422 0.4524 0.4785 -0.0553 0.0211  -0.0010 29  VAL B N     
3012 C CA    . VAL B 29  ? 0.4901 0.4116 0.4298 -0.0589 0.0206  0.0014  29  VAL B CA    
3013 C C     . VAL B 29  ? 0.5574 0.4899 0.5009 -0.0601 0.0203  0.0013  29  VAL B C     
3014 O O     . VAL B 29  ? 0.5212 0.4606 0.4644 -0.0654 0.0193  0.0031  29  VAL B O     
3015 C CB    . VAL B 29  ? 0.5093 0.4368 0.4543 -0.0550 0.0217  0.0025  29  VAL B CB    
3016 C CG1   . VAL B 29  ? 0.4846 0.4262 0.4345 -0.0571 0.0216  0.0046  29  VAL B CG1   
3017 C CG2   . VAL B 29  ? 0.4532 0.3716 0.3939 -0.0557 0.0216  0.0035  29  VAL B CG2   
3018 N N     . LYS B 30  ? 0.8211 0.7556 0.7681 -0.0552 0.0213  -0.0004 30  LYS B N     
3019 C CA    . LYS B 30  ? 0.8978 0.8422 0.8481 -0.0560 0.0212  -0.0004 30  LYS B CA    
3020 C C     . LYS B 30  ? 0.8877 0.8282 0.8324 -0.0618 0.0196  -0.0008 30  LYS B C     
3021 O O     . LYS B 30  ? 0.8744 0.8242 0.8203 -0.0656 0.0189  0.0005  30  LYS B O     
3022 C CB    . LYS B 30  ? 0.8923 0.8384 0.8471 -0.0496 0.0225  -0.0022 30  LYS B CB    
3023 C CG    . LYS B 30  ? 0.8746 0.8339 0.8354 -0.0483 0.0231  -0.0014 30  LYS B CG    
3024 C CD    . LYS B 30  ? 0.8400 0.7987 0.8039 -0.0425 0.0243  -0.0033 30  LYS B CD    
3025 C CE    . LYS B 30  ? 0.7978 0.7689 0.7679 -0.0402 0.0252  -0.0023 30  LYS B CE    
3026 N NZ    . LYS B 30  ? 0.7106 0.6807 0.6835 -0.0349 0.0263  -0.0040 30  LYS B NZ    
3027 N N     . TYR B 31  ? 0.8058 0.7330 0.7439 -0.0627 0.0192  -0.0025 31  TYR B N     
3028 C CA    . TYR B 31  ? 0.7630 0.6860 0.6949 -0.0688 0.0178  -0.0030 31  TYR B CA    
3029 C C     . TYR B 31  ? 0.7805 0.7062 0.7096 -0.0761 0.0164  -0.0007 31  TYR B C     
3030 O O     . TYR B 31  ? 0.8214 0.7541 0.7499 -0.0812 0.0152  0.0002  31  TYR B O     
3031 C CB    . TYR B 31  ? 0.7043 0.6111 0.6289 -0.0680 0.0178  -0.0054 31  TYR B CB    
3032 C CG    . TYR B 31  ? 0.6638 0.5626 0.5800 -0.0751 0.0162  -0.0058 31  TYR B CG    
3033 C CD1   . TYR B 31  ? 0.6409 0.5437 0.5556 -0.0791 0.0153  -0.0064 31  TYR B CD1   
3034 C CD2   . TYR B 31  ? 0.6921 0.5791 0.6015 -0.0781 0.0158  -0.0054 31  TYR B CD2   
3035 C CE1   . TYR B 31  ? 0.5968 0.4921 0.5033 -0.0862 0.0138  -0.0069 31  TYR B CE1   
3036 C CE2   . TYR B 31  ? 0.6085 0.4871 0.5095 -0.0850 0.0144  -0.0058 31  TYR B CE2   
3037 C CZ    . TYR B 31  ? 0.6169 0.4998 0.5165 -0.0892 0.0134  -0.0066 31  TYR B CZ    
3038 O OH    . TYR B 31  ? 0.7881 0.6624 0.6788 -0.0965 0.0120  -0.0072 31  TYR B OH    
3039 N N     . LEU B 32  ? 0.6866 0.6075 0.6140 -0.0766 0.0164  0.0005  32  LEU B N     
3040 C CA    . LEU B 32  ? 0.6513 0.5737 0.5755 -0.0838 0.0150  0.0029  32  LEU B CA    
3041 C C     . LEU B 32  ? 0.7492 0.6887 0.6795 -0.0858 0.0147  0.0054  32  LEU B C     
3042 O O     . LEU B 32  ? 0.7931 0.7372 0.7209 -0.0927 0.0133  0.0070  32  LEU B O     
3043 C CB    . LEU B 32  ? 0.5874 0.5008 0.5086 -0.0835 0.0152  0.0038  32  LEU B CB    
3044 C CG    . LEU B 32  ? 0.5743 0.4699 0.4877 -0.0827 0.0153  0.0018  32  LEU B CG    
3045 C CD1   . LEU B 32  ? 0.5728 0.4614 0.4853 -0.0798 0.0161  0.0028  32  LEU B CD1   
3046 C CD2   . LEU B 32  ? 0.5294 0.4173 0.4343 -0.0908 0.0137  0.0017  32  LEU B CD2   
3047 N N     . GLU B 33  ? 0.9133 0.8624 0.8513 -0.0798 0.0161  0.0057  33  GLU B N     
3048 C CA    . GLU B 33  ? 0.9564 0.9218 0.9004 -0.0805 0.0162  0.0081  33  GLU B CA    
3049 C C     . GLU B 33  ? 0.9411 0.9166 0.8873 -0.0820 0.0159  0.0084  33  GLU B C     
3050 O O     . GLU B 33  ? 0.9751 0.9646 0.9259 -0.0828 0.0159  0.0107  33  GLU B O     
3051 C CB    . GLU B 33  ? 0.9963 0.9677 0.9473 -0.0734 0.0181  0.0083  33  GLU B CB    
3052 C CG    . GLU B 33  ? 1.0781 1.0546 1.0306 -0.0746 0.0181  0.0107  33  GLU B CG    
3053 C CD    . GLU B 33  ? 1.1127 1.1022 1.0727 -0.0697 0.0196  0.0117  33  GLU B CD    
3054 O OE1   . GLU B 33  ? 1.0637 1.0531 1.0274 -0.0634 0.0210  0.0099  33  GLU B OE1   
3055 O OE2   . GLU B 33  ? 1.0860 1.0858 1.0480 -0.0723 0.0193  0.0143  33  GLU B OE2   
3056 N N     . LYS B 34  ? 0.6923 0.6613 0.6354 -0.0822 0.0155  0.0061  34  LYS B N     
3057 C CA    . LYS B 34  ? 0.5889 0.5669 0.5335 -0.0839 0.0151  0.0063  34  LYS B CA    
3058 C C     . LYS B 34  ? 0.6104 0.5861 0.5484 -0.0927 0.0131  0.0070  34  LYS B C     
3059 O O     . LYS B 34  ? 0.5456 0.5333 0.4849 -0.0972 0.0122  0.0093  34  LYS B O     
3060 C CB    . LYS B 34  ? 0.5417 0.5132 0.4861 -0.0794 0.0158  0.0034  34  LYS B CB    
3061 C CG    . LYS B 34  ? 0.5473 0.5283 0.4939 -0.0801 0.0156  0.0035  34  LYS B CG    
3062 C CD    . LYS B 34  ? 0.5114 0.5019 0.4660 -0.0728 0.0174  0.0038  34  LYS B CD    
3063 C CE    . LYS B 34  ? 0.5340 0.5353 0.4911 -0.0735 0.0172  0.0046  34  LYS B CE    
3064 N NZ    . LYS B 34  ? 0.5488 0.5641 0.5137 -0.0689 0.0187  0.0066  34  LYS B NZ    
3065 N N     . SER B 35  ? 0.7600 0.7200 0.6905 -0.0950 0.0124  0.0051  35  SER B N     
3066 C CA    . SER B 35  ? 0.7705 0.7253 0.6932 -0.1038 0.0105  0.0053  35  SER B CA    
3067 C C     . SER B 35  ? 0.8443 0.8062 0.7667 -0.1098 0.0094  0.0086  35  SER B C     
3068 O O     . SER B 35  ? 0.8472 0.8204 0.7701 -0.1154 0.0082  0.0106  35  SER B O     
3069 C CB    . SER B 35  ? 0.7210 0.6562 0.6357 -0.1039 0.0104  0.0027  35  SER B CB    
3070 O OG    . SER B 35  ? 0.7106 0.6397 0.6260 -0.0975 0.0116  -0.0002 35  SER B OG    
3071 N N     . LEU B 36  ? 1.0717 1.0276 0.9933 -0.1087 0.0098  0.0094  36  LEU B N     
3072 C CA    . LEU B 36  ? 1.0642 1.0269 0.9859 -0.1140 0.0089  0.0127  36  LEU B CA    
3073 C C     . LEU B 36  ? 1.0809 1.0561 1.0116 -0.1077 0.0104  0.0142  36  LEU B C     
3074 O O     . LEU B 36  ? 1.1434 1.1132 1.0758 -0.1024 0.0116  0.0136  36  LEU B O     
3075 C CB    . LEU B 36  ? 1.0029 0.9511 0.9182 -0.1164 0.0084  0.0127  36  LEU B CB    
3076 C CG    . LEU B 36  ? 0.9803 0.9117 0.8850 -0.1225 0.0072  0.0113  36  LEU B CG    
3077 C CD1   . LEU B 36  ? 0.9058 0.8348 0.8073 -0.1243 0.0066  0.0089  36  LEU B CD1   
3078 C CD2   . LEU B 36  ? 0.9702 0.8850 0.8714 -0.1176 0.0083  0.0096  36  LEU B CD2   
3079 N N     . GLY B 37  ? 1.0286 1.0205 0.9648 -0.1079 0.0104  0.0161  37  GLY B N     
3080 C CA    . GLY B 37  ? 1.0548 1.0578 0.9992 -0.1012 0.0121  0.0173  37  GLY B CA    
3081 C C     . GLY B 37  ? 1.0674 1.0873 1.0155 -0.1044 0.0117  0.0210  37  GLY B C     
3082 O O     . GLY B 37  ? 1.0276 1.0545 0.9737 -0.1108 0.0103  0.0225  37  GLY B O     
3083 N N     . LYS B 38  ? 1.5036 1.5306 1.4569 -0.1001 0.0130  0.0224  38  LYS B N     
3084 C CA    . LYS B 38  ? 1.5038 1.5477 1.4610 -0.1023 0.0128  0.0262  38  LYS B CA    
3085 C C     . LYS B 38  ? 1.4480 1.4909 1.4003 -0.1105 0.0110  0.0286  38  LYS B C     
3086 O O     . LYS B 38  ? 1.4594 1.5145 1.4146 -0.1119 0.0110  0.0317  38  LYS B O     
3087 C CB    . LYS B 38  ? 1.5014 1.5607 1.4624 -0.1024 0.0129  0.0277  38  LYS B CB    
3088 C CG    . LYS B 38  ? 1.4786 1.5563 1.4439 -0.1037 0.0131  0.0317  38  LYS B CG    
3089 C CD    . LYS B 38  ? 1.4165 1.5085 1.3854 -0.1029 0.0133  0.0331  38  LYS B CD    
3090 C CE    . LYS B 38  ? 1.3787 1.4899 1.3518 -0.1038 0.0136  0.0374  38  LYS B CE    
3091 N NZ    . LYS B 38  ? 1.3493 1.4750 1.3260 -0.1027 0.0140  0.0391  38  LYS B NZ    
3092 N N     . LYS B 39  ? 0.8699 0.8986 0.8147 -0.1160 0.0095  0.0273  39  LYS B N     
3093 C CA    . LYS B 39  ? 0.9060 0.9318 0.8457 -0.1237 0.0079  0.0295  39  LYS B CA    
3094 C C     . LYS B 39  ? 0.9567 0.9816 0.8993 -0.1193 0.0091  0.0303  39  LYS B C     
3095 O O     . LYS B 39  ? 0.9794 0.9928 0.9218 -0.1136 0.0102  0.0278  39  LYS B O     
3096 C CB    . LYS B 39  ? 0.8925 0.8998 0.8232 -0.1286 0.0066  0.0274  39  LYS B CB    
3097 C CG    . LYS B 39  ? 0.8775 0.8835 0.8015 -0.1393 0.0043  0.0297  39  LYS B CG    
3098 C CD    . LYS B 39  ? 0.8895 0.8882 0.8067 -0.1453 0.0028  0.0280  39  LYS B CD    
3099 C CE    . LYS B 39  ? 0.9224 0.9076 0.8299 -0.1541 0.0010  0.0285  39  LYS B CE    
3100 N NZ    . LYS B 39  ? 0.9567 0.9507 0.8647 -0.1594 0.0001  0.0326  39  LYS B NZ    
3101 N N     . LYS B 40  ? 0.9294 0.9669 0.8746 -0.1218 0.0088  0.0338  40  LYS B N     
3102 C CA    . LYS B 40  ? 0.9761 1.0142 0.9244 -0.1174 0.0100  0.0345  40  LYS B CA    
3103 C C     . LYS B 40  ? 0.9481 0.9719 0.8898 -0.1217 0.0089  0.0347  40  LYS B C     
3104 O O     . LYS B 40  ? 0.8885 0.9105 0.8317 -0.1188 0.0097  0.0353  40  LYS B O     
3105 C CB    . LYS B 40  ? 0.9999 1.0573 0.9536 -0.1176 0.0103  0.0381  40  LYS B CB    
3106 C CG    . LYS B 40  ? 0.9826 1.0551 0.9404 -0.1170 0.0105  0.0391  40  LYS B CG    
3107 C CD    . LYS B 40  ? 0.9836 1.0602 0.9480 -0.1070 0.0130  0.0371  40  LYS B CD    
3108 C CE    . LYS B 40  ? 1.0233 1.1171 0.9924 -0.1058 0.0135  0.0389  40  LYS B CE    
3109 N NZ    . LYS B 40  ? 1.0423 1.1529 1.0142 -0.1081 0.0134  0.0431  40  LYS B NZ    
3110 N N     . GLU B 41  ? 1.1489 1.1624 1.0832 -0.1286 0.0072  0.0343  41  GLU B N     
3111 C CA    . GLU B 41  ? 1.1509 1.1487 1.0783 -0.1323 0.0064  0.0343  41  GLU B CA    
3112 C C     . GLU B 41  ? 1.2162 1.2006 1.1437 -0.1245 0.0080  0.0309  41  GLU B C     
3113 O O     . GLU B 41  ? 1.2316 1.2074 1.1575 -0.1225 0.0085  0.0310  41  GLU B O     
3114 C CB    . GLU B 41  ? 1.1597 1.1484 1.0786 -0.1410 0.0044  0.0340  41  GLU B CB    
3115 C CG    . GLU B 41  ? 1.2333 1.2032 1.1438 -0.1448 0.0036  0.0337  41  GLU B CG    
3116 C CD    . GLU B 41  ? 1.3108 1.2673 1.2125 -0.1507 0.0023  0.0317  41  GLU B CD    
3117 O OE1   . GLU B 41  ? 1.3482 1.3086 1.2510 -0.1502 0.0023  0.0299  41  GLU B OE1   
3118 O OE2   . GLU B 41  ? 1.3171 1.2589 1.2106 -0.1557 0.0014  0.0320  41  GLU B OE2   
3119 N N     . PHE B 42  ? 0.9790 0.9622 0.9084 -0.1199 0.0088  0.0280  42  PHE B N     
3120 C CA    . PHE B 42  ? 0.9165 0.8877 0.8459 -0.1126 0.0103  0.0248  42  PHE B CA    
3121 C C     . PHE B 42  ? 0.9193 0.8990 0.8568 -0.1042 0.0122  0.0244  42  PHE B C     
3122 O O     . PHE B 42  ? 0.9575 0.9294 0.8960 -0.0978 0.0135  0.0219  42  PHE B O     
3123 C CB    . PHE B 42  ? 0.8877 0.8533 0.8149 -0.1121 0.0101  0.0218  42  PHE B CB    
3124 C CG    . PHE B 42  ? 0.8686 0.8245 0.7871 -0.1203 0.0083  0.0216  42  PHE B CG    
3125 C CD1   . PHE B 42  ? 0.8488 0.7886 0.7597 -0.1232 0.0077  0.0215  42  PHE B CD1   
3126 C CD2   . PHE B 42  ? 0.8563 0.8186 0.7738 -0.1250 0.0072  0.0216  42  PHE B CD2   
3127 C CE1   . PHE B 42  ? 0.8271 0.7568 0.7293 -0.1308 0.0061  0.0211  42  PHE B CE1   
3128 C CE2   . PHE B 42  ? 0.8594 0.8124 0.7684 -0.1329 0.0055  0.0212  42  PHE B CE2   
3129 C CZ    . PHE B 42  ? 0.8562 0.7924 0.7573 -0.1359 0.0049  0.0208  42  PHE B CZ    
3130 N N     . SER B 43  ? 0.8224 0.8179 0.7653 -0.1041 0.0125  0.0269  43  SER B N     
3131 C CA    . SER B 43  ? 0.7479 0.7517 0.6981 -0.0965 0.0144  0.0266  43  SER B CA    
3132 C C     . SER B 43  ? 0.7364 0.7305 0.6856 -0.0930 0.0152  0.0259  43  SER B C     
3133 O O     . SER B 43  ? 0.7590 0.7509 0.7114 -0.0860 0.0168  0.0238  43  SER B O     
3134 C CB    . SER B 43  ? 0.7213 0.7427 0.6760 -0.0980 0.0145  0.0298  43  SER B CB    
3135 O OG    . SER B 43  ? 0.6479 0.6700 0.6016 -0.1006 0.0141  0.0322  43  SER B OG    
3136 N N     . GLY B 44  ? 0.8094 0.7976 0.7538 -0.0981 0.0141  0.0278  44  GLY B N     
3137 C CA    . GLY B 44  ? 0.7727 0.7519 0.7158 -0.0952 0.0148  0.0276  44  GLY B CA    
3138 C C     . GLY B 44  ? 0.7168 0.6818 0.6575 -0.0903 0.0156  0.0244  44  GLY B C     
3139 O O     . GLY B 44  ? 0.7800 0.7439 0.7240 -0.0838 0.0171  0.0231  44  GLY B O     
3140 N N     . PHE B 45  ? 0.5373 0.4915 0.4722 -0.0935 0.0146  0.0230  45  PHE B N     
3141 C CA    . PHE B 45  ? 0.5287 0.4684 0.4603 -0.0893 0.0153  0.0202  45  PHE B CA    
3142 C C     . PHE B 45  ? 0.5345 0.4781 0.4721 -0.0813 0.0170  0.0178  45  PHE B C     
3143 O O     . PHE B 45  ? 0.4451 0.3821 0.3831 -0.0759 0.0182  0.0165  45  PHE B O     
3144 C CB    . PHE B 45  ? 0.5510 0.4805 0.4757 -0.0940 0.0141  0.0189  45  PHE B CB    
3145 C CG    . PHE B 45  ? 0.6034 0.5196 0.5251 -0.0892 0.0150  0.0158  45  PHE B CG    
3146 C CD1   . PHE B 45  ? 0.5886 0.4905 0.5049 -0.0879 0.0153  0.0157  45  PHE B CD1   
3147 C CD2   . PHE B 45  ? 0.6189 0.5377 0.5434 -0.0856 0.0156  0.0133  45  PHE B CD2   
3148 C CE1   . PHE B 45  ? 0.5713 0.4620 0.4850 -0.0831 0.0162  0.0130  45  PHE B CE1   
3149 C CE2   . PHE B 45  ? 0.5248 0.4324 0.4468 -0.0811 0.0164  0.0106  45  PHE B CE2   
3150 C CZ    . PHE B 45  ? 0.6086 0.5024 0.5252 -0.0798 0.0167  0.0104  45  PHE B CZ    
3151 N N     . PHE B 46  ? 0.8511 0.8055 0.7934 -0.0802 0.0173  0.0172  46  PHE B N     
3152 C CA    . PHE B 46  ? 0.8643 0.8218 0.8119 -0.0730 0.0189  0.0149  46  PHE B CA    
3153 C C     . PHE B 46  ? 0.9131 0.8788 0.8662 -0.0687 0.0202  0.0158  46  PHE B C     
3154 O O     . PHE B 46  ? 0.9954 0.9583 0.9509 -0.0628 0.0215  0.0141  46  PHE B O     
3155 C CB    . PHE B 46  ? 0.8995 0.8657 0.8502 -0.0730 0.0189  0.0142  46  PHE B CB    
3156 C CG    . PHE B 46  ? 0.9850 0.9451 0.9304 -0.0780 0.0175  0.0135  46  PHE B CG    
3157 C CD1   . PHE B 46  ? 1.0423 0.9905 0.9841 -0.0758 0.0177  0.0108  46  PHE B CD1   
3158 C CD2   . PHE B 46  ? 1.0159 0.9827 0.9596 -0.0848 0.0161  0.0155  46  PHE B CD2   
3159 C CE1   . PHE B 46  ? 1.0566 0.9990 0.9931 -0.0805 0.0165  0.0099  46  PHE B CE1   
3160 C CE2   . PHE B 46  ? 1.0607 1.0219 0.9990 -0.0899 0.0147  0.0148  46  PHE B CE2   
3161 C CZ    . PHE B 46  ? 1.0706 1.0193 1.0052 -0.0876 0.0150  0.0118  46  PHE B CZ    
3162 N N     . GLU B 47  ? 0.9731 0.9493 0.9284 -0.0716 0.0198  0.0184  47  GLU B N     
3163 C CA    . GLU B 47  ? 0.9951 0.9785 0.9550 -0.0676 0.0211  0.0191  47  GLU B CA    
3164 C C     . GLU B 47  ? 1.0634 1.0367 1.0212 -0.0650 0.0216  0.0186  47  GLU B C     
3165 O O     . GLU B 47  ? 1.0843 1.0598 1.0457 -0.0596 0.0230  0.0176  47  GLU B O     
3166 C CB    . GLU B 47  ? 0.9859 0.9806 0.9470 -0.0721 0.0204  0.0224  47  GLU B CB    
3167 C CG    . GLU B 47  ? 1.0770 1.0755 1.0402 -0.0701 0.0212  0.0237  47  GLU B CG    
3168 C CD    . GLU B 47  ? 1.1507 1.1594 1.1203 -0.0640 0.0230  0.0227  47  GLU B CD    
3169 O OE1   . GLU B 47  ? 1.1674 1.1780 1.1395 -0.0605 0.0239  0.0207  47  GLU B OE1   
3170 O OE2   . GLU B 47  ? 1.1698 1.1843 1.1415 -0.0628 0.0236  0.0239  47  GLU B OE2   
3171 N N     . ASP B 48  ? 0.9651 0.9273 0.9167 -0.0688 0.0205  0.0194  48  ASP B N     
3172 C CA    . ASP B 48  ? 0.9273 0.8803 0.8766 -0.0664 0.0209  0.0195  48  ASP B CA    
3173 C C     . ASP B 48  ? 0.8742 0.8172 0.8223 -0.0613 0.0218  0.0166  48  ASP B C     
3174 O O     . ASP B 48  ? 0.8819 0.8217 0.8309 -0.0569 0.0228  0.0162  48  ASP B O     
3175 C CB    . ASP B 48  ? 0.9493 0.8940 0.8921 -0.0722 0.0196  0.0218  48  ASP B CB    
3176 C CG    . ASP B 48  ? 1.0572 1.0121 1.0014 -0.0767 0.0188  0.0250  48  ASP B CG    
3177 O OD1   . ASP B 48  ? 1.0735 1.0400 1.0235 -0.0737 0.0198  0.0255  48  ASP B OD1   
3178 O OD2   . ASP B 48  ? 1.0780 1.0296 1.0174 -0.0833 0.0174  0.0271  48  ASP B OD2   
3179 N N     . ILE B 49  ? 0.6969 0.6353 0.6430 -0.0620 0.0214  0.0148  49  ILE B N     
3180 C CA    . ILE B 49  ? 0.5743 0.5047 0.5198 -0.0569 0.0222  0.0121  49  ILE B CA    
3181 C C     . ILE B 49  ? 0.6705 0.6093 0.6228 -0.0510 0.0237  0.0107  49  ILE B C     
3182 O O     . ILE B 49  ? 0.6799 0.6142 0.6328 -0.0460 0.0247  0.0093  49  ILE B O     
3183 C CB    . ILE B 49  ? 0.5921 0.5165 0.5338 -0.0593 0.0215  0.0106  49  ILE B CB    
3184 C CG1   . ILE B 49  ? 0.7102 0.6238 0.6440 -0.0651 0.0201  0.0118  49  ILE B CG1   
3185 C CG2   . ILE B 49  ? 0.5666 0.4846 0.5084 -0.0538 0.0224  0.0078  49  ILE B CG2   
3186 C CD1   . ILE B 49  ? 0.7918 0.6924 0.7208 -0.0628 0.0206  0.0119  49  ILE B CD1   
3187 N N     . GLU B 50  ? 0.7074 0.6583 0.6645 -0.0513 0.0239  0.0110  50  GLU B N     
3188 C CA    . GLU B 50  ? 0.6416 0.5996 0.6045 -0.0459 0.0254  0.0095  50  GLU B CA    
3189 C C     . GLU B 50  ? 0.6341 0.5931 0.5989 -0.0425 0.0264  0.0098  50  GLU B C     
3190 O O     . GLU B 50  ? 0.5648 0.5237 0.5321 -0.0377 0.0275  0.0080  50  GLU B O     
3191 C CB    . GLU B 50  ? 0.6656 0.6359 0.6326 -0.0470 0.0255  0.0101  50  GLU B CB    
3192 C CG    . GLU B 50  ? 0.6794 0.6499 0.6457 -0.0486 0.0249  0.0093  50  GLU B CG    
3193 C CD    . GLU B 50  ? 0.6962 0.6791 0.6677 -0.0472 0.0257  0.0094  50  GLU B CD    
3194 O OE1   . GLU B 50  ? 0.8072 0.7967 0.7828 -0.0436 0.0270  0.0094  50  GLU B OE1   
3195 O OE2   . GLU B 50  ? 0.5712 0.5572 0.5425 -0.0495 0.0251  0.0096  50  GLU B OE2   
3196 N N     . LYS B 51  ? 0.6553 0.6159 0.6189 -0.0453 0.0259  0.0121  51  LYS B N     
3197 C CA    . LYS B 51  ? 0.6157 0.5767 0.5804 -0.0426 0.0267  0.0127  51  LYS B CA    
3198 C C     . LYS B 51  ? 0.6117 0.5611 0.5726 -0.0406 0.0267  0.0122  51  LYS B C     
3199 O O     . LYS B 51  ? 0.6342 0.5838 0.5967 -0.0368 0.0277  0.0117  51  LYS B O     
3200 C CB    . LYS B 51  ? 0.5563 0.5229 0.5207 -0.0464 0.0261  0.0155  51  LYS B CB    
3201 C CG    . LYS B 51  ? 0.4720 0.4510 0.4399 -0.0484 0.0260  0.0165  51  LYS B CG    
3202 C CD    . LYS B 51  ? 0.5018 0.4853 0.4687 -0.0527 0.0253  0.0196  51  LYS B CD    
3203 C CE    . LYS B 51  ? 0.5953 0.5915 0.5651 -0.0551 0.0251  0.0210  51  LYS B CE    
3204 N NZ    . LYS B 51  ? 0.5802 0.5867 0.5555 -0.0505 0.0267  0.0199  51  LYS B NZ    
3205 N N     . LEU B 52  ? 0.6568 0.5963 0.6125 -0.0432 0.0258  0.0123  52  LEU B N     
3206 C CA    . LEU B 52  ? 0.6629 0.5907 0.6144 -0.0409 0.0260  0.0121  52  LEU B CA    
3207 C C     . LEU B 52  ? 0.7152 0.6409 0.6684 -0.0358 0.0270  0.0094  52  LEU B C     
3208 O O     . LEU B 52  ? 0.7561 0.6775 0.7088 -0.0319 0.0277  0.0091  52  LEU B O     
3209 C CB    . LEU B 52  ? 0.5908 0.5078 0.5354 -0.0452 0.0248  0.0129  52  LEU B CB    
3210 C CG    . LEU B 52  ? 0.6282 0.5410 0.5686 -0.0491 0.0241  0.0158  52  LEU B CG    
3211 C CD1   . LEU B 52  ? 0.6284 0.5292 0.5614 -0.0533 0.0230  0.0160  52  LEU B CD1   
3212 C CD2   . LEU B 52  ? 0.5505 0.4602 0.4907 -0.0452 0.0250  0.0168  52  LEU B CD2   
3213 N N     . TYR B 53  ? 0.5601 0.4892 0.5155 -0.0357 0.0269  0.0077  53  TYR B N     
3214 C CA    . TYR B 53  ? 0.5208 0.4491 0.4783 -0.0311 0.0278  0.0053  53  TYR B CA    
3215 C C     . TYR B 53  ? 0.5178 0.4535 0.4803 -0.0271 0.0290  0.0048  53  TYR B C     
3216 O O     . TYR B 53  ? 0.6617 0.5947 0.6248 -0.0231 0.0298  0.0036  53  TYR B O     
3217 C CB    . TYR B 53  ? 0.5095 0.4404 0.4682 -0.0321 0.0275  0.0038  53  TYR B CB    
3218 C CG    . TYR B 53  ? 0.4654 0.3974 0.4271 -0.0276 0.0285  0.0015  53  TYR B CG    
3219 C CD1   . TYR B 53  ? 0.5466 0.4701 0.5055 -0.0253 0.0286  0.0001  53  TYR B CD1   
3220 C CD2   . TYR B 53  ? 0.3393 0.2807 0.3065 -0.0256 0.0293  0.0008  53  TYR B CD2   
3221 C CE1   . TYR B 53  ? 0.4941 0.4191 0.4558 -0.0214 0.0294  -0.0018 53  TYR B CE1   
3222 C CE2   . TYR B 53  ? 0.4152 0.3573 0.3850 -0.0217 0.0302  -0.0012 53  TYR B CE2   
3223 C CZ    . TYR B 53  ? 0.4958 0.4300 0.4629 -0.0198 0.0302  -0.0024 53  TYR B CZ    
3224 O OH    . TYR B 53  ? 0.5098 0.4452 0.4796 -0.0162 0.0310  -0.0042 53  TYR B OH    
3225 N N     . PHE B 54  ? 0.4470 0.3920 0.4129 -0.0284 0.0292  0.0056  54  PHE B N     
3226 C CA    . PHE B 54  ? 0.3915 0.3433 0.3616 -0.0250 0.0304  0.0050  54  PHE B CA    
3227 C C     . PHE B 54  ? 0.4153 0.3638 0.3841 -0.0233 0.0307  0.0059  54  PHE B C     
3228 O O     . PHE B 54  ? 0.5072 0.4559 0.4776 -0.0196 0.0315  0.0047  54  PHE B O     
3229 C CB    . PHE B 54  ? 0.3391 0.3014 0.3127 -0.0266 0.0306  0.0058  54  PHE B CB    
3230 C CG    . PHE B 54  ? 0.3900 0.3586 0.3674 -0.0232 0.0319  0.0049  54  PHE B CG    
3231 C CD1   . PHE B 54  ? 0.4538 0.4260 0.4344 -0.0203 0.0329  0.0027  54  PHE B CD1   
3232 C CD2   . PHE B 54  ? 0.3903 0.3609 0.3676 -0.0230 0.0322  0.0061  54  PHE B CD2   
3233 C CE1   . PHE B 54  ? 0.4547 0.4317 0.4380 -0.0174 0.0342  0.0017  54  PHE B CE1   
3234 C CE2   . PHE B 54  ? 0.4186 0.3948 0.3989 -0.0202 0.0333  0.0050  54  PHE B CE2   
3235 C CZ    . PHE B 54  ? 0.4837 0.4628 0.4669 -0.0175 0.0343  0.0027  54  PHE B CZ    
3236 N N     . LYS B 55  ? 0.5420 0.4878 0.5077 -0.0262 0.0299  0.0082  55  LYS B N     
3237 C CA    . LYS B 55  ? 0.6265 0.5691 0.5907 -0.0245 0.0302  0.0094  55  LYS B CA    
3238 C C     . LYS B 55  ? 0.7041 0.6383 0.6659 -0.0209 0.0306  0.0084  55  LYS B C     
3239 O O     . LYS B 55  ? 0.7485 0.6816 0.7100 -0.0183 0.0311  0.0091  55  LYS B O     
3240 C CB    . LYS B 55  ? 0.6586 0.5978 0.6190 -0.0283 0.0293  0.0123  55  LYS B CB    
3241 C CG    . LYS B 55  ? 0.6961 0.6446 0.6588 -0.0317 0.0290  0.0138  55  LYS B CG    
3242 C CD    . LYS B 55  ? 0.6663 0.6231 0.6327 -0.0293 0.0299  0.0140  55  LYS B CD    
3243 C CE    . LYS B 55  ? 0.7327 0.6988 0.7011 -0.0325 0.0296  0.0156  55  LYS B CE    
3244 N NZ    . LYS B 55  ? 0.8413 0.8160 0.8132 -0.0303 0.0306  0.0155  55  LYS B NZ    
3245 N N     . GLN B 56  ? 0.5390 0.4682 0.4995 -0.0206 0.0304  0.0068  56  GLN B N     
3246 C CA    . GLN B 56  ? 0.4979 0.4183 0.4553 -0.0176 0.0306  0.0060  56  GLN B CA    
3247 C C     . GLN B 56  ? 0.5369 0.4472 0.4881 -0.0190 0.0301  0.0079  56  GLN B C     
3248 O O     . GLN B 56  ? 0.6415 0.5453 0.5901 -0.0157 0.0306  0.0081  56  GLN B O     
3249 C CB    . GLN B 56  ? 0.4194 0.3428 0.3794 -0.0128 0.0317  0.0053  56  GLN B CB    
3250 C CG    . GLN B 56  ? 0.4561 0.3854 0.4206 -0.0105 0.0324  0.0029  56  GLN B CG    
3251 C CD    . GLN B 56  ? 0.4521 0.3852 0.4190 -0.0067 0.0333  0.0025  56  GLN B CD    
3252 O OE1   . GLN B 56  ? 0.4487 0.3895 0.4195 -0.0062 0.0339  0.0017  56  GLN B OE1   
3253 N NE2   . GLN B 56  ? 0.4191 0.3465 0.3832 -0.0040 0.0336  0.0032  56  GLN B NE2   
3254 N N     . ASN B 57  ? 0.5629 0.4716 0.5116 -0.0237 0.0292  0.0093  57  ASN B N     
3255 C CA    . ASN B 57  ? 0.6811 0.5789 0.6233 -0.0255 0.0286  0.0110  57  ASN B CA    
3256 C C     . ASN B 57  ? 0.7017 0.5919 0.6400 -0.0276 0.0280  0.0096  57  ASN B C     
3257 O O     . ASN B 57  ? 0.6887 0.5782 0.6249 -0.0327 0.0269  0.0101  57  ASN B O     
3258 C CB    . ASN B 57  ? 0.7187 0.6185 0.6598 -0.0299 0.0279  0.0138  57  ASN B CB    
3259 C CG    . ASN B 57  ? 0.7980 0.6859 0.7322 -0.0311 0.0276  0.0159  57  ASN B CG    
3260 O OD1   . ASN B 57  ? 0.8287 0.7088 0.7599 -0.0271 0.0284  0.0159  57  ASN B OD1   
3261 N ND2   . ASN B 57  ? 0.8554 0.7417 0.7867 -0.0366 0.0266  0.0179  57  ASN B ND2   
3262 N N     . TYR B 58  ? 0.7071 0.5925 0.6444 -0.0238 0.0286  0.0077  58  TYR B N     
3263 C CA    . TYR B 58  ? 0.6647 0.5431 0.5983 -0.0252 0.0281  0.0060  58  TYR B CA    
3264 C C     . TYR B 58  ? 0.6763 0.5416 0.6018 -0.0276 0.0276  0.0069  58  TYR B C     
3265 O O     . TYR B 58  ? 0.6754 0.5369 0.5975 -0.0321 0.0266  0.0064  58  TYR B O     
3266 C CB    . TYR B 58  ? 0.6772 0.5552 0.6125 -0.0200 0.0290  0.0038  58  TYR B CB    
3267 C CG    . TYR B 58  ? 0.7142 0.6041 0.6570 -0.0179 0.0295  0.0025  58  TYR B CG    
3268 C CD1   . TYR B 58  ? 0.6849 0.5847 0.6322 -0.0206 0.0292  0.0030  58  TYR B CD1   
3269 C CD2   . TYR B 58  ? 0.7599 0.6508 0.7048 -0.0132 0.0304  0.0009  58  TYR B CD2   
3270 C CE1   . TYR B 58  ? 0.6831 0.5925 0.6364 -0.0186 0.0298  0.0018  58  TYR B CE1   
3271 C CE2   . TYR B 58  ? 0.7366 0.6372 0.6877 -0.0116 0.0308  -0.0003 58  TYR B CE2   
3272 C CZ    . TYR B 58  ? 0.6616 0.5710 0.6167 -0.0142 0.0306  0.0001  58  TYR B CZ    
3273 O OH    . TYR B 58  ? 0.6199 0.5378 0.5805 -0.0124 0.0312  -0.0011 58  TYR B OH    
3274 N N     . LYS B 59  ? 0.5647 0.4231 0.4868 -0.0247 0.0283  0.0085  59  LYS B N     
3275 C CA    . LYS B 59  ? 0.5023 0.3470 0.4161 -0.0265 0.0281  0.0095  59  LYS B CA    
3276 C C     . LYS B 59  ? 0.5149 0.3585 0.4259 -0.0338 0.0267  0.0109  59  LYS B C     
3277 O O     . LYS B 59  ? 0.6258 0.4606 0.5309 -0.0374 0.0260  0.0102  59  LYS B O     
3278 C CB    . LYS B 59  ? 0.5142 0.3539 0.4257 -0.0223 0.0291  0.0117  59  LYS B CB    
3279 C CG    . LYS B 59  ? 0.6359 0.4594 0.5380 -0.0226 0.0293  0.0126  59  LYS B CG    
3280 C CD    . LYS B 59  ? 0.6544 0.4692 0.5525 -0.0187 0.0300  0.0103  59  LYS B CD    
3281 C CE    . LYS B 59  ? 0.6365 0.4344 0.5247 -0.0185 0.0305  0.0112  59  LYS B CE    
3282 N NZ    . LYS B 59  ? 0.5811 0.3708 0.4654 -0.0131 0.0316  0.0093  59  LYS B NZ    
3283 N N     . GLU B 60  ? 0.6387 0.4914 0.5538 -0.0359 0.0263  0.0129  60  GLU B N     
3284 C CA    . GLU B 60  ? 0.7269 0.5805 0.6401 -0.0430 0.0250  0.0146  60  GLU B CA    
3285 C C     . GLU B 60  ? 0.7441 0.6015 0.6580 -0.0473 0.0240  0.0128  60  GLU B C     
3286 O O     . GLU B 60  ? 0.7497 0.6005 0.6580 -0.0529 0.0229  0.0131  60  GLU B O     
3287 C CB    . GLU B 60  ? 0.7240 0.5891 0.6425 -0.0438 0.0250  0.0169  60  GLU B CB    
3288 C CG    . GLU B 60  ? 0.8493 0.7148 0.7652 -0.0509 0.0236  0.0193  60  GLU B CG    
3289 C CD    . GLU B 60  ? 0.9544 0.8288 0.8741 -0.0514 0.0237  0.0220  60  GLU B CD    
3290 O OE1   . GLU B 60  ? 1.0235 0.8951 0.9427 -0.0475 0.0246  0.0234  60  GLU B OE1   
3291 O OE2   . GLU B 60  ? 0.9242 0.8087 0.8471 -0.0556 0.0229  0.0229  60  GLU B OE2   
3292 N N     . ALA B 61  ? 0.6063 0.4741 0.5269 -0.0448 0.0243  0.0109  61  ALA B N     
3293 C CA    . ALA B 61  ? 0.5779 0.4512 0.5001 -0.0485 0.0234  0.0096  61  ALA B CA    
3294 C C     . ALA B 61  ? 0.6901 0.5520 0.6058 -0.0497 0.0231  0.0077  61  ALA B C     
3295 O O     . ALA B 61  ? 0.7746 0.6346 0.6868 -0.0557 0.0218  0.0078  61  ALA B O     
3296 C CB    . ALA B 61  ? 0.6126 0.4981 0.5427 -0.0447 0.0242  0.0080  61  ALA B CB    
3297 N N     . ILE B 62  ? 0.6013 0.4556 0.5151 -0.0443 0.0241  0.0061  62  ILE B N     
3298 C CA    . ILE B 62  ? 0.5359 0.3784 0.4430 -0.0448 0.0240  0.0043  62  ILE B CA    
3299 C C     . ILE B 62  ? 0.5490 0.3803 0.4477 -0.0508 0.0229  0.0055  62  ILE B C     
3300 O O     . ILE B 62  ? 0.5618 0.3894 0.4563 -0.0558 0.0219  0.0045  62  ILE B O     
3301 C CB    . ILE B 62  ? 0.4834 0.3187 0.3890 -0.0377 0.0254  0.0031  62  ILE B CB    
3302 C CG1   . ILE B 62  ? 0.5010 0.3474 0.4147 -0.0326 0.0262  0.0018  62  ILE B CG1   
3303 C CG2   . ILE B 62  ? 0.4682 0.2903 0.3660 -0.0381 0.0254  0.0012  62  ILE B CG2   
3304 C CD1   . ILE B 62  ? 0.5231 0.3651 0.4365 -0.0254 0.0277  0.0011  62  ILE B CD1   
3305 N N     . GLU B 63  ? 0.6009 0.4270 0.4968 -0.0507 0.0232  0.0079  63  GLU B N     
3306 C CA    . GLU B 63  ? 0.6969 0.5120 0.5845 -0.0567 0.0223  0.0095  63  GLU B CA    
3307 C C     . GLU B 63  ? 0.7023 0.5249 0.5909 -0.0647 0.0206  0.0102  63  GLU B C     
3308 O O     . GLU B 63  ? 0.6251 0.4401 0.5071 -0.0704 0.0195  0.0096  63  GLU B O     
3309 C CB    . GLU B 63  ? 0.7322 0.5435 0.6184 -0.0552 0.0229  0.0124  63  GLU B CB    
3310 C CG    . GLU B 63  ? 0.7987 0.6031 0.6836 -0.0473 0.0246  0.0121  63  GLU B CG    
3311 C CD    . GLU B 63  ? 0.8418 0.6439 0.7258 -0.0459 0.0251  0.0153  63  GLU B CD    
3312 O OE1   . GLU B 63  ? 0.8758 0.6783 0.7581 -0.0518 0.0241  0.0176  63  GLU B OE1   
3313 O OE2   . GLU B 63  ? 0.7714 0.5721 0.6564 -0.0391 0.0266  0.0158  63  GLU B OE2   
3314 N N     . LYS B 64  ? 0.6021 0.4397 0.4984 -0.0655 0.0203  0.0117  64  LYS B N     
3315 C CA    . LYS B 64  ? 0.6230 0.4696 0.5209 -0.0725 0.0188  0.0126  64  LYS B CA    
3316 C C     . LYS B 64  ? 0.7423 0.5901 0.6396 -0.0745 0.0182  0.0101  64  LYS B C     
3317 O O     . LYS B 64  ? 0.7350 0.5802 0.6275 -0.0815 0.0168  0.0103  64  LYS B O     
3318 C CB    . LYS B 64  ? 0.5859 0.4493 0.4929 -0.0712 0.0190  0.0141  64  LYS B CB    
3319 C CG    . LYS B 64  ? 0.6828 0.5468 0.5898 -0.0717 0.0191  0.0171  64  LYS B CG    
3320 C CD    . LYS B 64  ? 0.7158 0.5954 0.6287 -0.0752 0.0184  0.0191  64  LYS B CD    
3321 C CE    . LYS B 64  ? 0.6162 0.4966 0.5287 -0.0766 0.0183  0.0224  64  LYS B CE    
3322 N NZ    . LYS B 64  ? 0.5781 0.4572 0.4931 -0.0695 0.0199  0.0223  64  LYS B NZ    
3323 N N     . ILE B 65  ? 0.8498 0.7015 0.7516 -0.0687 0.0192  0.0077  65  ILE B N     
3324 C CA    . ILE B 65  ? 0.8313 0.6862 0.7338 -0.0700 0.0187  0.0054  65  ILE B CA    
3325 C C     . ILE B 65  ? 0.8485 0.6889 0.7413 -0.0740 0.0180  0.0041  65  ILE B C     
3326 O O     . ILE B 65  ? 0.7840 0.6265 0.6747 -0.0798 0.0167  0.0036  65  ILE B O     
3327 C CB    . ILE B 65  ? 0.7372 0.5968 0.6455 -0.0626 0.0200  0.0032  65  ILE B CB    
3328 C CG1   . ILE B 65  ? 0.7151 0.5873 0.6320 -0.0586 0.0209  0.0043  65  ILE B CG1   
3329 C CG2   . ILE B 65  ? 0.7040 0.5686 0.6137 -0.0640 0.0195  0.0013  65  ILE B CG2   
3330 C CD1   . ILE B 65  ? 0.7403 0.6258 0.6618 -0.0629 0.0201  0.0062  65  ILE B CD1   
3331 N N     . LEU B 66  ? 0.6864 0.5122 0.5731 -0.0707 0.0188  0.0033  66  LEU B N     
3332 C CA    . LEU B 66  ? 0.6633 0.4740 0.5399 -0.0743 0.0183  0.0019  66  LEU B CA    
3333 C C     . LEU B 66  ? 0.7762 0.5824 0.6468 -0.0829 0.0168  0.0040  66  LEU B C     
3334 O O     . LEU B 66  ? 0.7658 0.5674 0.6305 -0.0893 0.0156  0.0031  66  LEU B O     
3335 C CB    . LEU B 66  ? 0.6301 0.4263 0.5014 -0.0681 0.0198  0.0010  66  LEU B CB    
3336 C CG    . LEU B 66  ? 0.5523 0.3532 0.4296 -0.0594 0.0214  -0.0006 66  LEU B CG    
3337 C CD1   . LEU B 66  ? 0.5636 0.3520 0.4361 -0.0537 0.0228  -0.0002 66  LEU B CD1   
3338 C CD2   . LEU B 66  ? 0.4746 0.2766 0.3521 -0.0585 0.0213  -0.0037 66  LEU B CD2   
3339 N N     . ASP B 67  ? 1.1462 0.9550 1.0183 -0.0840 0.0167  0.0070  67  ASP B N     
3340 C CA    . ASP B 67  ? 1.1831 0.9896 1.0503 -0.0928 0.0152  0.0094  67  ASP B CA    
3341 C C     . ASP B 67  ? 1.1435 0.9634 1.0141 -0.0994 0.0135  0.0098  67  ASP B C     
3342 O O     . ASP B 67  ? 1.2149 1.0314 1.0797 -0.1076 0.0120  0.0109  67  ASP B O     
3343 C CB    . ASP B 67  ? 1.2370 1.0469 1.1066 -0.0924 0.0154  0.0128  67  ASP B CB    
3344 C CG    . ASP B 67  ? 1.2695 1.0621 1.1299 -0.0936 0.0156  0.0141  67  ASP B CG    
3345 O OD1   . ASP B 67  ? 1.2994 1.0770 1.1505 -0.0963 0.0154  0.0126  67  ASP B OD1   
3346 O OD2   . ASP B 67  ? 1.2659 1.0595 1.1280 -0.0918 0.0161  0.0168  67  ASP B OD2   
3347 N N     . PHE B 68  ? 1.0062 0.8416 0.8860 -0.0962 0.0139  0.0093  68  PHE B N     
3348 C CA    . PHE B 68  ? 0.9699 0.8189 0.8532 -0.1017 0.0125  0.0098  68  PHE B CA    
3349 C C     . PHE B 68  ? 0.9927 0.8342 0.8695 -0.1058 0.0117  0.0074  68  PHE B C     
3350 O O     . PHE B 68  ? 0.9888 0.8331 0.8625 -0.1137 0.0101  0.0083  68  PHE B O     
3351 C CB    . PHE B 68  ? 0.9160 0.7805 0.8098 -0.0958 0.0135  0.0092  68  PHE B CB    
3352 C CG    . PHE B 68  ? 0.8563 0.7377 0.7555 -0.1000 0.0125  0.0107  68  PHE B CG    
3353 C CD1   . PHE B 68  ? 0.7679 0.6593 0.6706 -0.1029 0.0120  0.0138  68  PHE B CD1   
3354 C CD2   . PHE B 68  ? 0.8856 0.7738 0.7871 -0.1004 0.0122  0.0090  68  PHE B CD2   
3355 C CE1   . PHE B 68  ? 0.7320 0.6397 0.6399 -0.1061 0.0113  0.0154  68  PHE B CE1   
3356 C CE2   . PHE B 68  ? 0.8577 0.7621 0.7645 -0.1036 0.0115  0.0107  68  PHE B CE2   
3357 C CZ    . PHE B 68  ? 0.8040 0.7183 0.7140 -0.1064 0.0110  0.0139  68  PHE B CZ    
3358 N N     . CYS B 69  ? 0.9726 0.8047 0.8471 -0.1004 0.0128  0.0045  69  CYS B N     
3359 C CA    . CYS B 69  ? 0.9260 0.7508 0.7943 -0.1036 0.0121  0.0019  69  CYS B CA    
3360 C C     . CYS B 69  ? 1.0596 0.8665 0.9162 -0.1087 0.0115  0.0019  69  CYS B C     
3361 O O     . CYS B 69  ? 1.1699 0.9685 1.0193 -0.1131 0.0108  -0.0001 69  CYS B O     
3362 C CB    . CYS B 69  ? 0.8531 0.6751 0.7233 -0.0958 0.0136  -0.0011 69  CYS B CB    
3363 S SG    . CYS B 69  ? 0.8280 0.6687 0.7116 -0.0882 0.0147  -0.0011 69  CYS B SG    
3364 N N     . LYS B 70  ? 1.2064 1.0063 1.0607 -0.1082 0.0119  0.0040  70  LYS B N     
3365 C CA    . LYS B 70  ? 1.2035 0.9862 1.0462 -0.1140 0.0113  0.0044  70  LYS B CA    
3366 C C     . LYS B 70  ? 1.2340 1.0226 1.0748 -0.1245 0.0092  0.0069  70  LYS B C     
3367 O O     . LYS B 70  ? 1.3588 1.1380 1.1906 -0.1320 0.0079  0.0061  70  LYS B O     
3368 C CB    . LYS B 70  ? 1.1892 0.9607 1.0293 -0.1090 0.0126  0.0058  70  LYS B CB    
3369 C CG    . LYS B 70  ? 1.1975 0.9463 1.0255 -0.1087 0.0133  0.0042  70  LYS B CG    
3370 C CD    . LYS B 70  ? 1.1828 0.9223 1.0095 -0.1017 0.0151  0.0056  70  LYS B CD    
3371 C CE    . LYS B 70  ? 1.1875 0.9367 1.0238 -0.0916 0.0167  0.0050  70  LYS B CE    
3372 N NZ    . LYS B 70  ? 1.1645 0.9093 0.9999 -0.0860 0.0178  0.0014  70  LYS B NZ    
3373 N N     . LYS B 71  ? 0.9346 0.7388 0.7835 -0.1253 0.0088  0.0099  71  LYS B N     
3374 C CA    . LYS B 71  ? 0.9255 0.7376 0.7734 -0.1350 0.0068  0.0126  71  LYS B CA    
3375 C C     . LYS B 71  ? 0.8732 0.6987 0.7244 -0.1394 0.0055  0.0118  71  LYS B C     
3376 O O     . LYS B 71  ? 0.8239 0.6537 0.6720 -0.1486 0.0037  0.0135  71  LYS B O     
3377 C CB    . LYS B 71  ? 0.9154 0.7404 0.7708 -0.1342 0.0068  0.0163  71  LYS B CB    
3378 C CG    . LYS B 71  ? 0.9135 0.7301 0.7689 -0.1279 0.0084  0.0174  71  LYS B CG    
3379 C CD    . LYS B 71  ? 0.8650 0.6980 0.7302 -0.1250 0.0087  0.0201  71  LYS B CD    
3380 C CE    . LYS B 71  ? 0.8382 0.6652 0.7051 -0.1169 0.0105  0.0205  71  LYS B CE    
3381 N NZ    . LYS B 71  ? 0.8441 0.6517 0.7008 -0.1187 0.0106  0.0213  71  LYS B NZ    
3382 N N     . ASN B 72  ? 0.9259 0.7584 0.7832 -0.1329 0.0065  0.0095  72  ASN B N     
3383 C CA    . ASN B 72  ? 0.9391 0.7856 0.8005 -0.1359 0.0056  0.0089  72  ASN B CA    
3384 C C     . ASN B 72  ? 0.9893 0.8282 0.8468 -0.1344 0.0059  0.0051  72  ASN B C     
3385 O O     . ASN B 72  ? 1.0104 0.8613 0.8735 -0.1330 0.0058  0.0042  72  ASN B O     
3386 C CB    . ASN B 72  ? 0.8776 0.7435 0.7514 -0.1301 0.0065  0.0101  72  ASN B CB    
3387 C CG    . ASN B 72  ? 0.8685 0.7440 0.7467 -0.1316 0.0062  0.0139  72  ASN B CG    
3388 O OD1   . ASN B 72  ? 0.9110 0.7853 0.7845 -0.1395 0.0048  0.0162  72  ASN B OD1   
3389 N ND2   . ASN B 72  ? 0.8657 0.7508 0.7527 -0.1243 0.0076  0.0144  72  ASN B ND2   
3390 N N     . GLU B 73  ? 1.0751 0.8943 0.9230 -0.1343 0.0062  0.0029  73  GLU B N     
3391 C CA    . GLU B 73  ? 1.0998 0.9120 0.9442 -0.1319 0.0067  -0.0008 73  GLU B CA    
3392 C C     . GLU B 73  ? 1.1621 0.9838 1.0061 -0.1388 0.0051  -0.0015 73  GLU B C     
3393 O O     . GLU B 73  ? 1.2004 1.0286 1.0484 -0.1351 0.0055  -0.0035 73  GLU B O     
3394 C CB    . GLU B 73  ? 1.1366 0.9252 0.9687 -0.1324 0.0071  -0.0030 73  GLU B CB    
3395 C CG    . GLU B 73  ? 1.2573 1.0387 1.0861 -0.1285 0.0079  -0.0071 73  GLU B CG    
3396 C CD    . GLU B 73  ? 1.3293 1.0923 1.1444 -0.1347 0.0072  -0.0096 73  GLU B CD    
3397 O OE1   . GLU B 73  ? 1.3989 1.1433 1.2057 -0.1327 0.0082  -0.0103 73  GLU B OE1   
3398 O OE2   . GLU B 73  ? 1.2682 1.0353 1.0807 -0.1414 0.0058  -0.0107 73  GLU B OE2   
3399 N N     . SER B 74  ? 1.0107 0.8348 0.8506 -0.1486 0.0032  0.0006  74  SER B N     
3400 C CA    . SER B 74  ? 0.9173 0.7503 0.7559 -0.1563 0.0015  0.0004  74  SER B CA    
3401 C C     . SER B 74  ? 0.8654 0.7200 0.7151 -0.1532 0.0016  0.0011  74  SER B C     
3402 O O     . SER B 74  ? 0.7792 0.6401 0.6282 -0.1571 0.0006  0.0001  74  SER B O     
3403 C CB    . SER B 74  ? 0.8147 0.6476 0.6475 -0.1674 -0.0006 0.0031  74  SER B CB    
3404 O OG    . SER B 74  ? 0.8641 0.7000 0.7005 -0.1664 -0.0003 0.0063  74  SER B OG    
3405 N N     . LEU B 75  ? 0.9693 0.8348 0.8289 -0.1463 0.0028  0.0028  75  LEU B N     
3406 C CA    . LEU B 75  ? 1.0131 0.8986 0.8830 -0.1432 0.0030  0.0038  75  LEU B CA    
3407 C C     . LEU B 75  ? 1.0304 0.9159 0.9055 -0.1334 0.0049  0.0012  75  LEU B C     
3408 O O     . LEU B 75  ? 1.0388 0.9396 0.9227 -0.1297 0.0054  0.0019  75  LEU B O     
3409 C CB    . LEU B 75  ? 1.0370 0.9356 0.9146 -0.1419 0.0033  0.0074  75  LEU B CB    
3410 C CG    . LEU B 75  ? 1.0232 0.9247 0.8974 -0.1510 0.0016  0.0107  75  LEU B CG    
3411 C CD1   . LEU B 75  ? 0.9828 0.8849 0.8605 -0.1477 0.0024  0.0131  75  LEU B CD1   
3412 C CD2   . LEU B 75  ? 0.9986 0.9200 0.8773 -0.1564 0.0003  0.0131  75  LEU B CD2   
3413 N N     . LEU B 76  ? 0.9223 0.7908 0.7920 -0.1292 0.0059  -0.0016 76  LEU B N     
3414 C CA    . LEU B 76  ? 0.8571 0.7253 0.7319 -0.1197 0.0076  -0.0038 76  LEU B CA    
3415 C C     . LEU B 76  ? 0.8677 0.7228 0.7352 -0.1191 0.0078  -0.0074 76  LEU B C     
3416 O O     . LEU B 76  ? 0.9467 0.7899 0.8045 -0.1254 0.0068  -0.0084 76  LEU B O     
3417 C CB    . LEU B 76  ? 0.8032 0.6661 0.6806 -0.1129 0.0092  -0.0031 76  LEU B CB    
3418 C CG    . LEU B 76  ? 0.7358 0.6108 0.6197 -0.1137 0.0090  0.0004  76  LEU B CG    
3419 C CD1   . LEU B 76  ? 0.7712 0.6375 0.6544 -0.1097 0.0100  0.0013  76  LEU B CD1   
3420 C CD2   . LEU B 76  ? 0.7085 0.6018 0.6033 -0.1091 0.0097  0.0012  76  LEU B CD2   
3421 N N     . SER B 77  ? 0.8747 0.7326 0.7469 -0.1118 0.0091  -0.0094 77  SER B N     
3422 C CA    . SER B 77  ? 0.9598 0.8066 0.8258 -0.1104 0.0094  -0.0129 77  SER B CA    
3423 C C     . SER B 77  ? 1.0114 0.8393 0.8706 -0.1061 0.0106  -0.0148 77  SER B C     
3424 O O     . SER B 77  ? 1.0601 0.8870 0.9237 -0.0989 0.0121  -0.0143 77  SER B O     
3425 C CB    . SER B 77  ? 1.0005 0.8579 0.8743 -0.1041 0.0103  -0.0140 77  SER B CB    
3426 O OG    . SER B 77  ? 1.0222 0.8723 0.8902 -0.1047 0.0102  -0.0171 77  SER B OG    
3427 N N     . GLU B 78  ? 1.0387 0.8516 0.8870 -0.1103 0.0101  -0.0169 78  GLU B N     
3428 C CA    . GLU B 78  ? 1.0228 0.8166 0.8631 -0.1068 0.0112  -0.0186 78  GLU B CA    
3429 C C     . GLU B 78  ? 1.0816 0.8713 0.9246 -0.0966 0.0132  -0.0205 78  GLU B C     
3430 O O     . GLU B 78  ? 1.1983 0.9799 1.0404 -0.0915 0.0145  -0.0199 78  GLU B O     
3431 C CB    . GLU B 78  ? 1.0456 0.8269 0.8744 -0.1132 0.0103  -0.0212 78  GLU B CB    
3432 C CG    . GLU B 78  ? 0.9948 0.7859 0.8255 -0.1155 0.0095  -0.0229 78  GLU B CG    
3433 C CD    . GLU B 78  ? 1.1139 0.8911 0.9326 -0.1205 0.0089  -0.0261 78  GLU B CD    
3434 O OE1   . GLU B 78  ? 1.1472 0.9152 0.9571 -0.1287 0.0077  -0.0258 78  GLU B OE1   
3435 O OE2   . GLU B 78  ? 1.1718 0.9475 0.9898 -0.1165 0.0096  -0.0288 78  GLU B OE2   
3436 N N     . GLN B 79  ? 1.2315 1.0272 1.0777 -0.0934 0.0136  -0.0224 79  GLN B N     
3437 C CA    . GLN B 79  ? 1.2574 1.0503 1.1065 -0.0839 0.0154  -0.0239 79  GLN B CA    
3438 C C     . GLN B 79  ? 1.2905 1.0932 1.1496 -0.0778 0.0164  -0.0215 79  GLN B C     
3439 O O     . GLN B 79  ? 1.3071 1.1033 1.1663 -0.0710 0.0179  -0.0218 79  GLN B O     
3440 C CB    . GLN B 79  ? 1.2474 1.0455 1.0981 -0.0818 0.0156  -0.0263 79  GLN B CB    
3441 C CG    . GLN B 79  ? 1.2642 1.0820 1.1265 -0.0802 0.0154  -0.0249 79  GLN B CG    
3442 C CD    . GLN B 79  ? 1.3642 1.1932 1.2281 -0.0885 0.0135  -0.0234 79  GLN B CD    
3443 O OE1   . GLN B 79  ? 1.4168 1.2392 1.2729 -0.0962 0.0122  -0.0235 79  GLN B OE1   
3444 N NE2   . GLN B 79  ? 1.4065 1.2528 1.2805 -0.0870 0.0135  -0.0218 79  GLN B NE2   
3445 N N     . VAL B 80  ? 1.0283 0.8469 0.8958 -0.0800 0.0157  -0.0192 80  VAL B N     
3446 C CA    . VAL B 80  ? 0.9474 0.7752 0.8239 -0.0749 0.0166  -0.0170 80  VAL B CA    
3447 C C     . VAL B 80  ? 0.9081 0.7277 0.7817 -0.0748 0.0169  -0.0153 80  VAL B C     
3448 O O     . VAL B 80  ? 0.8189 0.6367 0.6954 -0.0683 0.0183  -0.0149 80  VAL B O     
3449 C CB    . VAL B 80  ? 0.9397 0.7854 0.8244 -0.0781 0.0157  -0.0149 80  VAL B CB    
3450 C CG1   . VAL B 80  ? 0.8586 0.7140 0.7526 -0.0725 0.0168  -0.0130 80  VAL B CG1   
3451 C CG2   . VAL B 80  ? 0.9079 0.7622 0.7953 -0.0785 0.0153  -0.0163 80  VAL B CG2   
3452 N N     . VAL B 81  ? 0.8184 0.6325 0.6857 -0.0822 0.0156  -0.0142 81  VAL B N     
3453 C CA    . VAL B 81  ? 0.8617 0.6675 0.7257 -0.0826 0.0159  -0.0124 81  VAL B CA    
3454 C C     . VAL B 81  ? 0.9056 0.6948 0.7629 -0.0772 0.0173  -0.0139 81  VAL B C     
3455 O O     . VAL B 81  ? 0.9707 0.7564 0.8290 -0.0731 0.0183  -0.0125 81  VAL B O     
3456 C CB    . VAL B 81  ? 0.8544 0.6574 0.7126 -0.0922 0.0142  -0.0107 81  VAL B CB    
3457 C CG1   . VAL B 81  ? 0.7969 0.6176 0.6618 -0.0973 0.0128  -0.0090 81  VAL B CG1   
3458 C CG2   . VAL B 81  ? 0.9073 0.6941 0.7533 -0.0974 0.0135  -0.0128 81  VAL B CG2   
3459 N N     . GLN B 82  ? 0.9840 0.7632 0.8344 -0.0772 0.0175  -0.0168 82  GLN B N     
3460 C CA    . GLN B 82  ? 1.0268 0.7897 0.8699 -0.0720 0.0189  -0.0182 82  GLN B CA    
3461 C C     . GLN B 82  ? 0.9975 0.7652 0.8471 -0.0626 0.0206  -0.0190 82  GLN B C     
3462 O O     . GLN B 82  ? 1.0043 0.7637 0.8518 -0.0565 0.0220  -0.0188 82  GLN B O     
3463 C CB    . GLN B 82  ? 1.0307 0.7797 0.8627 -0.0759 0.0185  -0.0211 82  GLN B CB    
3464 C CG    . GLN B 82  ? 1.0573 0.7856 0.8779 -0.0750 0.0195  -0.0216 82  GLN B CG    
3465 C CD    . GLN B 82  ? 1.1464 0.8668 0.9653 -0.0655 0.0216  -0.0233 82  GLN B CD    
3466 O OE1   . GLN B 82  ? 1.1917 0.9160 1.0126 -0.0622 0.0220  -0.0256 82  GLN B OE1   
3467 N NE2   . GLN B 82  ? 1.1123 0.8217 0.9272 -0.0611 0.0229  -0.0220 82  GLN B NE2   
3468 N N     . ARG B 83  ? 0.7225 0.5039 0.5801 -0.0608 0.0204  -0.0197 83  ARG B N     
3469 C CA    . ARG B 83  ? 0.6402 0.4271 0.5044 -0.0522 0.0219  -0.0202 83  ARG B CA    
3470 C C     . ARG B 83  ? 0.7234 0.5173 0.5947 -0.0485 0.0226  -0.0176 83  ARG B C     
3471 O O     . ARG B 83  ? 0.7207 0.5118 0.5932 -0.0417 0.0240  -0.0174 83  ARG B O     
3472 C CB    . ARG B 83  ? 0.6056 0.4053 0.4764 -0.0517 0.0216  -0.0213 83  ARG B CB    
3473 C CG    . ARG B 83  ? 0.5870 0.3928 0.4647 -0.0434 0.0230  -0.0218 83  ARG B CG    
3474 C CD    . ARG B 83  ? 0.6705 0.4648 0.5417 -0.0388 0.0241  -0.0242 83  ARG B CD    
3475 N NE    . ARG B 83  ? 0.7060 0.5039 0.5825 -0.0306 0.0256  -0.0240 83  ARG B NE    
3476 C CZ    . ARG B 83  ? 0.6634 0.4725 0.5473 -0.0274 0.0259  -0.0245 83  ARG B CZ    
3477 N NH1   . ARG B 83  ? 0.5270 0.3452 0.4143 -0.0313 0.0248  -0.0250 83  ARG B NH1   
3478 N NH2   . ARG B 83  ? 0.6941 0.5057 0.5821 -0.0204 0.0272  -0.0243 83  ARG B NH2   
3479 N N     . LEU B 84  ? 0.7755 0.5789 0.6514 -0.0531 0.0216  -0.0154 84  LEU B N     
3480 C CA    . LEU B 84  ? 0.7207 0.5308 0.6029 -0.0503 0.0221  -0.0130 84  LEU B CA    
3481 C C     . LEU B 84  ? 0.7702 0.5672 0.6460 -0.0486 0.0229  -0.0120 84  LEU B C     
3482 O O     . LEU B 84  ? 0.8851 0.6830 0.7642 -0.0428 0.0240  -0.0110 84  LEU B O     
3483 C CB    . LEU B 84  ? 0.6546 0.4754 0.5409 -0.0564 0.0208  -0.0108 84  LEU B CB    
3484 C CG    . LEU B 84  ? 0.6651 0.5017 0.5591 -0.0582 0.0201  -0.0107 84  LEU B CG    
3485 C CD1   . LEU B 84  ? 0.6357 0.4800 0.5312 -0.0650 0.0188  -0.0084 84  LEU B CD1   
3486 C CD2   . LEU B 84  ? 0.5377 0.3846 0.4408 -0.0514 0.0214  -0.0107 84  LEU B CD2   
3487 N N     . ALA B 85  ? 0.6675 0.4520 0.5339 -0.0537 0.0222  -0.0122 85  ALA B N     
3488 C CA    . ALA B 85  ? 0.7346 0.5053 0.5941 -0.0521 0.0230  -0.0111 85  ALA B CA    
3489 C C     . ALA B 85  ? 0.7895 0.5518 0.6464 -0.0440 0.0248  -0.0125 85  ALA B C     
3490 O O     . ALA B 85  ? 0.7961 0.5526 0.6515 -0.0397 0.0259  -0.0110 85  ALA B O     
3491 C CB    . ALA B 85  ? 0.7139 0.4717 0.5630 -0.0595 0.0219  -0.0113 85  ALA B CB    
3492 N N     . GLU B 86  ? 0.8848 0.6472 0.7413 -0.0419 0.0250  -0.0151 86  GLU B N     
3493 C CA    . GLU B 86  ? 0.8934 0.6483 0.7471 -0.0343 0.0267  -0.0165 86  GLU B CA    
3494 C C     . GLU B 86  ? 0.8394 0.6055 0.7024 -0.0272 0.0278  -0.0156 86  GLU B C     
3495 O O     . GLU B 86  ? 0.8881 0.6491 0.7497 -0.0208 0.0293  -0.0150 86  GLU B O     
3496 C CB    . GLU B 86  ? 0.9487 0.7008 0.7989 -0.0350 0.0265  -0.0197 86  GLU B CB    
3497 C CG    . GLU B 86  ? 1.0354 0.7847 0.8851 -0.0269 0.0281  -0.0214 86  GLU B CG    
3498 C CD    . GLU B 86  ? 1.1332 0.8821 0.9806 -0.0282 0.0277  -0.0245 86  GLU B CD    
3499 O OE1   . GLU B 86  ? 1.1619 0.9166 1.0105 -0.0350 0.0262  -0.0250 86  GLU B OE1   
3500 O OE2   . GLU B 86  ? 1.1703 0.9137 1.0145 -0.0225 0.0290  -0.0262 86  GLU B OE2   
3501 N N     . VAL B 87  ? 0.8300 0.6116 0.7024 -0.0282 0.0271  -0.0153 87  VAL B N     
3502 C CA    . VAL B 87  ? 0.8246 0.6168 0.7055 -0.0219 0.0281  -0.0147 87  VAL B CA    
3503 C C     . VAL B 87  ? 0.8805 0.6747 0.7641 -0.0204 0.0285  -0.0120 87  VAL B C     
3504 O O     . VAL B 87  ? 0.9115 0.7072 0.7976 -0.0142 0.0298  -0.0112 87  VAL B O     
3505 C CB    . VAL B 87  ? 0.8052 0.6122 0.6947 -0.0232 0.0274  -0.0154 87  VAL B CB    
3506 C CG1   . VAL B 87  ? 0.7753 0.5922 0.6729 -0.0170 0.0284  -0.0149 87  VAL B CG1   
3507 C CG2   . VAL B 87  ? 0.8353 0.6402 0.7218 -0.0244 0.0270  -0.0180 87  VAL B CG2   
3508 N N     . ALA B 88  ? 0.6684 0.4629 0.5511 -0.0262 0.0275  -0.0104 88  ALA B N     
3509 C CA    . ALA B 88  ? 0.6633 0.4602 0.5485 -0.0254 0.0278  -0.0076 88  ALA B CA    
3510 C C     . ALA B 88  ? 0.7276 0.5161 0.6093 -0.0194 0.0293  -0.0063 88  ALA B C     
3511 O O     . ALA B 88  ? 0.7506 0.5467 0.6380 -0.0156 0.0299  -0.0048 88  ALA B O     
3512 C CB    . ALA B 88  ? 0.5089 0.3048 0.3916 -0.0331 0.0264  -0.0061 88  ALA B CB    
3513 N N     . PRO B 89  ? 0.6799 0.4527 0.5518 -0.0186 0.0299  -0.0067 89  PRO B N     
3514 C CA    . PRO B 89  ? 0.6842 0.4504 0.5534 -0.0125 0.0314  -0.0050 89  PRO B CA    
3515 C C     . PRO B 89  ? 0.7247 0.4989 0.6000 -0.0049 0.0327  -0.0052 89  PRO B C     
3516 O O     . PRO B 89  ? 0.7206 0.4969 0.5979 -0.0007 0.0336  -0.0030 89  PRO B O     
3517 C CB    . PRO B 89  ? 0.6273 0.3755 0.4851 -0.0125 0.0319  -0.0061 89  PRO B CB    
3518 C CG    . PRO B 89  ? 0.6330 0.3777 0.4869 -0.0211 0.0303  -0.0070 89  PRO B CG    
3519 C CD    . PRO B 89  ? 0.6144 0.3746 0.4771 -0.0236 0.0291  -0.0083 89  PRO B CD    
3520 N N     . ARG B 90  ? 0.8878 0.6666 0.7658 -0.0032 0.0327  -0.0076 90  ARG B N     
3521 C CA    . ARG B 90  ? 0.8936 0.6803 0.7771 0.0036  0.0338  -0.0078 90  ARG B CA    
3522 C C     . ARG B 90  ? 0.7882 0.5915 0.6824 0.0039  0.0335  -0.0072 90  ARG B C     
3523 O O     . ARG B 90  ? 0.7570 0.5668 0.6556 0.0090  0.0343  -0.0074 90  ARG B O     
3524 C CB    . ARG B 90  ? 0.9191 0.7025 0.7999 0.0053  0.0341  -0.0106 90  ARG B CB    
3525 C CG    . ARG B 90  ? 0.9511 0.7189 0.8219 0.0086  0.0352  -0.0113 90  ARG B CG    
3526 C CD    . ARG B 90  ? 0.9853 0.7508 0.8537 0.0097  0.0353  -0.0144 90  ARG B CD    
3527 N NE    . ARG B 90  ? 0.9791 0.7447 0.8465 0.0026  0.0338  -0.0163 90  ARG B NE    
3528 C CZ    . ARG B 90  ? 0.9604 0.7380 0.8349 0.0002  0.0328  -0.0174 90  ARG B CZ    
3529 N NH1   . ARG B 90  ? 0.9615 0.7515 0.8446 0.0042  0.0332  -0.0169 90  ARG B NH1   
3530 N NH2   . ARG B 90  ? 0.9350 0.7124 0.8079 -0.0062 0.0314  -0.0188 90  ARG B NH2   
3531 N N     . LEU B 91  ? 0.5261 0.3362 0.4243 -0.0015 0.0323  -0.0066 91  LEU B N     
3532 C CA    . LEU B 91  ? 0.4680 0.2929 0.3756 -0.0014 0.0320  -0.0064 91  LEU B CA    
3533 C C     . LEU B 91  ? 0.4741 0.3046 0.3857 0.0031  0.0330  -0.0045 91  LEU B C     
3534 O O     . LEU B 91  ? 0.5112 0.3361 0.4194 0.0042  0.0335  -0.0025 91  LEU B O     
3535 C CB    . LEU B 91  ? 0.4024 0.2333 0.3129 -0.0080 0.0307  -0.0060 91  LEU B CB    
3536 C CG    . LEU B 91  ? 0.4080 0.2383 0.3169 -0.0132 0.0295  -0.0077 91  LEU B CG    
3537 C CD1   . LEU B 91  ? 0.3733 0.2080 0.2836 -0.0194 0.0284  -0.0063 91  LEU B CD1   
3538 C CD2   . LEU B 91  ? 0.4664 0.3058 0.3812 -0.0115 0.0296  -0.0095 91  LEU B CD2   
3539 N N     . LYS B 92  ? 0.6168 0.4583 0.5356 0.0056  0.0333  -0.0050 92  LYS B N     
3540 C CA    . LYS B 92  ? 0.6095 0.4571 0.5322 0.0097  0.0342  -0.0035 92  LYS B CA    
3541 C C     . LYS B 92  ? 0.7060 0.5666 0.6368 0.0082  0.0338  -0.0039 92  LYS B C     
3542 O O     . LYS B 92  ? 0.7215 0.5857 0.6546 0.0050  0.0331  -0.0054 92  LYS B O     
3543 C CB    . LYS B 92  ? 0.5547 0.4007 0.4763 0.0159  0.0353  -0.0039 92  LYS B CB    
3544 C CG    . LYS B 92  ? 0.6143 0.4472 0.5275 0.0187  0.0361  -0.0035 92  LYS B CG    
3545 C CD    . LYS B 92  ? 0.7057 0.5357 0.6166 0.0217  0.0369  -0.0007 92  LYS B CD    
3546 C CE    . LYS B 92  ? 0.7546 0.5702 0.6564 0.0243  0.0378  -0.0002 92  LYS B CE    
3547 N NZ    . LYS B 92  ? 0.7080 0.5132 0.6038 0.0190  0.0370  -0.0003 92  LYS B NZ    
3548 N N     . SER B 93  ? 0.6104 0.4781 0.5453 0.0102  0.0343  -0.0025 93  SER B N     
3549 C CA    . SER B 93  ? 0.4861 0.3656 0.4283 0.0094  0.0342  -0.0032 93  SER B CA    
3550 C C     . SER B 93  ? 0.5445 0.4292 0.4896 0.0142  0.0351  -0.0029 93  SER B C     
3551 O O     . SER B 93  ? 0.6142 0.4962 0.5569 0.0173  0.0358  -0.0013 93  SER B O     
3552 C CB    . SER B 93  ? 0.4976 0.3820 0.4422 0.0058  0.0337  -0.0019 93  SER B CB    
3553 O OG    . SER B 93  ? 0.5296 0.4139 0.4741 0.0010  0.0327  -0.0026 93  SER B OG    
3554 N N     . ASN B 94  ? 0.6216 0.5137 0.5716 0.0147  0.0352  -0.0044 94  ASN B N     
3555 C CA    . ASN B 94  ? 0.7181 0.6159 0.6710 0.0186  0.0360  -0.0042 94  ASN B CA    
3556 C C     . ASN B 94  ? 0.7430 0.6506 0.7018 0.0171  0.0359  -0.0047 94  ASN B C     
3557 O O     . ASN B 94  ? 0.6815 0.5923 0.6431 0.0149  0.0356  -0.0062 94  ASN B O     
3558 C CB    . ASN B 94  ? 0.8280 0.7241 0.7803 0.0212  0.0362  -0.0057 94  ASN B CB    
3559 C CG    . ASN B 94  ? 0.8964 0.7989 0.8516 0.0249  0.0369  -0.0054 94  ASN B CG    
3560 O OD1   . ASN B 94  ? 0.9119 0.8183 0.8681 0.0264  0.0373  -0.0039 94  ASN B OD1   
3561 N ND2   . ASN B 94  ? 0.8697 0.7737 0.8261 0.0262  0.0370  -0.0069 94  ASN B ND2   
3562 N N     . PRO B 95  ? 0.6725 0.5850 0.6330 0.0186  0.0364  -0.0034 95  PRO B N     
3563 C CA    . PRO B 95  ? 0.6524 0.5738 0.6180 0.0171  0.0365  -0.0039 95  PRO B CA    
3564 C C     . PRO B 95  ? 0.6606 0.5867 0.6297 0.0177  0.0367  -0.0058 95  PRO B C     
3565 O O     . PRO B 95  ? 0.6804 0.6111 0.6528 0.0155  0.0366  -0.0069 95  PRO B O     
3566 C CB    . PRO B 95  ? 0.6144 0.5393 0.5801 0.0189  0.0369  -0.0020 95  PRO B CB    
3567 C CG    . PRO B 95  ? 0.6054 0.5239 0.5666 0.0221  0.0372  -0.0004 95  PRO B CG    
3568 C CD    . PRO B 95  ? 0.6743 0.5839 0.6317 0.0208  0.0368  -0.0011 95  PRO B CD    
3569 N N     . LYS B 96  ? 0.5794 0.5044 0.5477 0.0207  0.0370  -0.0060 96  LYS B N     
3570 C CA    . LYS B 96  ? 0.5511 0.4803 0.5225 0.0213  0.0371  -0.0075 96  LYS B CA    
3571 C C     . LYS B 96  ? 0.5249 0.4525 0.4971 0.0190  0.0367  -0.0091 96  LYS B C     
3572 O O     . LYS B 96  ? 0.4685 0.4005 0.4441 0.0181  0.0369  -0.0103 96  LYS B O     
3573 C CB    . LYS B 96  ? 0.5532 0.4809 0.5228 0.0251  0.0375  -0.0071 96  LYS B CB    
3574 C CG    . LYS B 96  ? 0.5529 0.4856 0.5231 0.0276  0.0380  -0.0056 96  LYS B CG    
3575 C CD    . LYS B 96  ? 0.5021 0.4334 0.4702 0.0316  0.0384  -0.0050 96  LYS B CD    
3576 C CE    . LYS B 96  ? 0.4890 0.4277 0.4587 0.0339  0.0389  -0.0036 96  LYS B CE    
3577 N NZ    . LYS B 96  ? 0.4556 0.3936 0.4233 0.0381  0.0394  -0.0029 96  LYS B NZ    
3578 N N     . ASP B 97  ? 0.9121 0.8332 0.8810 0.0180  0.0363  -0.0091 97  ASP B N     
3579 C CA    . ASP B 97  ? 1.0146 0.9345 0.9840 0.0156  0.0358  -0.0104 97  ASP B CA    
3580 C C     . ASP B 97  ? 1.0149 0.9323 0.9828 0.0122  0.0352  -0.0099 97  ASP B C     
3581 O O     . ASP B 97  ? 1.1244 1.0350 1.0880 0.0116  0.0348  -0.0096 97  ASP B O     
3582 C CB    . ASP B 97  ? 1.1138 1.0276 1.0797 0.0172  0.0357  -0.0110 97  ASP B CB    
3583 C CG    . ASP B 97  ? 1.0970 1.0137 1.0648 0.0199  0.0361  -0.0118 97  ASP B CG    
3584 O OD1   . ASP B 97  ? 1.1470 1.0694 1.1178 0.0213  0.0365  -0.0115 97  ASP B OD1   
3585 O OD2   . ASP B 97  ? 1.0626 0.9757 1.0284 0.0206  0.0359  -0.0127 97  ASP B OD2   
3586 N N     . ASN B 98  ? 0.6060 0.5285 0.5769 0.0098  0.0352  -0.0099 98  ASN B N     
3587 C CA    . ASN B 98  ? 0.5178 0.4387 0.4873 0.0063  0.0345  -0.0093 98  ASN B CA    
3588 C C     . ASN B 98  ? 0.5244 0.4509 0.4976 0.0045  0.0345  -0.0102 98  ASN B C     
3589 O O     . ASN B 98  ? 0.4652 0.3965 0.4408 0.0030  0.0347  -0.0098 98  ASN B O     
3590 C CB    . ASN B 98  ? 0.5694 0.4912 0.5384 0.0053  0.0345  -0.0077 98  ASN B CB    
3591 C CG    . ASN B 98  ? 0.5675 0.4821 0.5317 0.0063  0.0344  -0.0063 98  ASN B CG    
3592 O OD1   . ASN B 98  ? 0.6019 0.5094 0.5620 0.0061  0.0340  -0.0065 98  ASN B OD1   
3593 N ND2   . ASN B 98  ? 0.5029 0.4190 0.4671 0.0073  0.0347  -0.0049 98  ASN B ND2   
3594 N N     . GLU B 99  ? 0.4111 0.3369 0.3846 0.0045  0.0344  -0.0113 99  GLU B N     
3595 C CA    . GLU B 99  ? 0.5014 0.4330 0.4787 0.0036  0.0346  -0.0121 99  GLU B CA    
3596 C C     . GLU B 99  ? 0.5315 0.4659 0.5095 0.0003  0.0342  -0.0115 99  GLU B C     
3597 O O     . GLU B 99  ? 0.5197 0.4600 0.5011 0.0001  0.0347  -0.0117 99  GLU B O     
3598 C CB    . GLU B 99  ? 0.5548 0.4855 0.5326 0.0053  0.0347  -0.0132 99  GLU B CB    
3599 C CG    . GLU B 99  ? 0.6215 0.5514 0.5994 0.0086  0.0352  -0.0136 99  GLU B CG    
3600 C CD    . GLU B 99  ? 0.7406 0.6644 0.7147 0.0101  0.0349  -0.0138 99  GLU B CD    
3601 O OE1   . GLU B 99  ? 0.6334 0.5515 0.6034 0.0094  0.0344  -0.0132 99  GLU B OE1   
3602 O OE2   . GLU B 99  ? 0.8445 0.7690 0.8196 0.0120  0.0351  -0.0146 99  GLU B OE2   
3603 N N     . SER B 100 ? 0.5371 0.4674 0.5116 -0.0022 0.0333  -0.0109 100 SER B N     
3604 C CA    . SER B 100 ? 0.5380 0.4717 0.5130 -0.0056 0.0328  -0.0100 100 SER B CA    
3605 C C     . SER B 100 ? 0.5514 0.4893 0.5281 -0.0061 0.0332  -0.0090 100 SER B C     
3606 O O     . SER B 100 ? 0.4675 0.4118 0.4470 -0.0071 0.0335  -0.0087 100 SER B O     
3607 C CB    . SER B 100 ? 0.5335 0.4607 0.5035 -0.0085 0.0318  -0.0094 100 SER B CB    
3608 O OG    . SER B 100 ? 0.5896 0.5095 0.5559 -0.0068 0.0318  -0.0093 100 SER B OG    
3609 N N     . ARG B 101 ? 0.4346 0.3692 0.4094 -0.0053 0.0332  -0.0084 101 ARG B N     
3610 C CA    . ARG B 101 ? 0.3784 0.3170 0.3547 -0.0057 0.0336  -0.0074 101 ARG B CA    
3611 C C     . ARG B 101 ? 0.4022 0.3467 0.3826 -0.0032 0.0347  -0.0084 101 ARG B C     
3612 O O     . ARG B 101 ? 0.4495 0.3992 0.4318 -0.0039 0.0351  -0.0080 101 ARG B O     
3613 C CB    . ARG B 101 ? 0.3503 0.2840 0.3232 -0.0058 0.0333  -0.0061 101 ARG B CB    
3614 C CG    . ARG B 101 ? 0.4568 0.3954 0.4314 -0.0062 0.0336  -0.0050 101 ARG B CG    
3615 C CD    . ARG B 101 ? 0.5711 0.5054 0.5421 -0.0076 0.0331  -0.0031 101 ARG B CD    
3616 N NE    . ARG B 101 ? 0.6538 0.5941 0.6266 -0.0089 0.0333  -0.0020 101 ARG B NE    
3617 C CZ    . ARG B 101 ? 0.5905 0.5344 0.5638 -0.0121 0.0328  -0.0009 101 ARG B CZ    
3618 N NH1   . ARG B 101 ? 0.4996 0.4418 0.4714 -0.0148 0.0320  -0.0008 101 ARG B NH1   
3619 N NH2   . ARG B 101 ? 0.5099 0.4595 0.4848 -0.0128 0.0331  0.0000  101 ARG B NH2   
3620 N N     . ARG B 102 ? 0.3585 0.3019 0.3398 -0.0006 0.0352  -0.0096 102 ARG B N     
3621 C CA    . ARG B 102 ? 0.2697 0.2180 0.2545 0.0012  0.0362  -0.0107 102 ARG B CA    
3622 C C     . ARG B 102 ? 0.2849 0.2382 0.2723 0.0004  0.0367  -0.0111 102 ARG B C     
3623 O O     . ARG B 102 ? 0.3621 0.3198 0.3515 0.0007  0.0374  -0.0113 102 ARG B O     
3624 C CB    . ARG B 102 ? 0.2808 0.2270 0.2658 0.0039  0.0365  -0.0118 102 ARG B CB    
3625 C CG    . ARG B 102 ? 0.2646 0.2080 0.2477 0.0055  0.0364  -0.0113 102 ARG B CG    
3626 C CD    . ARG B 102 ? 0.3117 0.2538 0.2951 0.0080  0.0367  -0.0122 102 ARG B CD    
3627 N NE    . ARG B 102 ? 0.4179 0.3577 0.3992 0.0099  0.0366  -0.0114 102 ARG B NE    
3628 C CZ    . ARG B 102 ? 0.3993 0.3423 0.3815 0.0109  0.0371  -0.0111 102 ARG B CZ    
3629 N NH1   . ARG B 102 ? 0.3033 0.2512 0.2881 0.0100  0.0376  -0.0117 102 ARG B NH1   
3630 N NH2   . ARG B 102 ? 0.4002 0.3414 0.3804 0.0128  0.0371  -0.0100 102 ARG B NH2   
3631 N N     . LEU B 103 ? 0.3468 0.2995 0.3340 -0.0005 0.0362  -0.0111 103 LEU B N     
3632 C CA    . LEU B 103 ? 0.3743 0.3323 0.3639 -0.0011 0.0367  -0.0111 103 LEU B CA    
3633 C C     . LEU B 103 ? 0.3643 0.3262 0.3540 -0.0034 0.0365  -0.0097 103 LEU B C     
3634 O O     . LEU B 103 ? 0.4501 0.4173 0.4421 -0.0029 0.0374  -0.0098 103 LEU B O     
3635 C CB    . LEU B 103 ? 0.3391 0.2961 0.3284 -0.0018 0.0361  -0.0111 103 LEU B CB    
3636 C CG    . LEU B 103 ? 0.4487 0.4115 0.4401 -0.0027 0.0364  -0.0105 103 LEU B CG    
3637 C CD1   . LEU B 103 ? 0.5568 0.5215 0.5508 -0.0001 0.0374  -0.0115 103 LEU B CD1   
3638 C CD2   . LEU B 103 ? 0.4521 0.4142 0.4414 -0.0058 0.0352  -0.0096 103 LEU B CD2   
3639 N N     . TYR B 104 ? 0.4709 0.4299 0.4577 -0.0059 0.0354  -0.0085 104 TYR B N     
3640 C CA    . TYR B 104 ? 0.4017 0.3645 0.3883 -0.0086 0.0351  -0.0070 104 TYR B CA    
3641 C C     . TYR B 104 ? 0.4515 0.4184 0.4397 -0.0076 0.0359  -0.0069 104 TYR B C     
3642 O O     . TYR B 104 ? 0.4047 0.3777 0.3946 -0.0084 0.0364  -0.0062 104 TYR B O     
3643 C CB    . TYR B 104 ? 0.3877 0.3448 0.3703 -0.0112 0.0338  -0.0058 104 TYR B CB    
3644 C CG    . TYR B 104 ? 0.4269 0.3868 0.4086 -0.0144 0.0332  -0.0039 104 TYR B CG    
3645 C CD1   . TYR B 104 ? 0.4944 0.4582 0.4760 -0.0175 0.0326  -0.0028 104 TYR B CD1   
3646 C CD2   . TYR B 104 ? 0.4738 0.4330 0.4545 -0.0144 0.0333  -0.0031 104 TYR B CD2   
3647 C CE1   . TYR B 104 ? 0.5215 0.4884 0.5022 -0.0207 0.0320  -0.0009 104 TYR B CE1   
3648 C CE2   . TYR B 104 ? 0.5031 0.4652 0.4831 -0.0175 0.0327  -0.0012 104 TYR B CE2   
3649 C CZ    . TYR B 104 ? 0.5239 0.4897 0.5038 -0.0207 0.0321  -0.0001 104 TYR B CZ    
3650 O OH    . TYR B 104 ? 0.4653 0.4345 0.4444 -0.0239 0.0315  0.0019  104 TYR B OH    
3651 N N     . GLU B 105 ? 0.5656 0.5297 0.5534 -0.0058 0.0363  -0.0076 105 GLU B N     
3652 C CA    . GLU B 105 ? 0.5946 0.5624 0.5836 -0.0051 0.0370  -0.0076 105 GLU B CA    
3653 C C     . GLU B 105 ? 0.5743 0.5460 0.5660 -0.0030 0.0384  -0.0091 105 GLU B C     
3654 O O     . GLU B 105 ? 0.6488 0.6252 0.6416 -0.0028 0.0392  -0.0091 105 GLU B O     
3655 C CB    . GLU B 105 ? 0.5981 0.5622 0.5855 -0.0040 0.0369  -0.0076 105 GLU B CB    
3656 C CG    . GLU B 105 ? 0.5487 0.5080 0.5328 -0.0057 0.0358  -0.0059 105 GLU B CG    
3657 C CD    . GLU B 105 ? 0.5930 0.5499 0.5759 -0.0040 0.0359  -0.0057 105 GLU B CD    
3658 O OE1   . GLU B 105 ? 0.6252 0.5850 0.6099 -0.0021 0.0367  -0.0068 105 GLU B OE1   
3659 O OE2   . GLU B 105 ? 0.5375 0.4898 0.5175 -0.0047 0.0352  -0.0042 105 GLU B OE2   
3660 N N     . THR B 106 ? 0.3311 0.3006 0.3235 -0.0012 0.0387  -0.0104 106 THR B N     
3661 C CA    . THR B 106 ? 0.2531 0.2257 0.2478 0.0008  0.0401  -0.0117 106 THR B CA    
3662 C C     . THR B 106 ? 0.2627 0.2405 0.2588 0.0003  0.0406  -0.0110 106 THR B C     
3663 O O     . THR B 106 ? 0.2712 0.2526 0.2687 0.0017  0.0419  -0.0117 106 THR B O     
3664 C CB    . THR B 106 ? 0.2520 0.2214 0.2472 0.0025  0.0403  -0.0129 106 THR B CB    
3665 O OG1   . THR B 106 ? 0.2720 0.2370 0.2657 0.0030  0.0397  -0.0132 106 THR B OG1   
3666 C CG2   . THR B 106 ? 0.2501 0.2215 0.2471 0.0045  0.0418  -0.0143 106 THR B CG2   
3667 N N     . LEU B 107 ? 0.2536 0.2320 0.2492 -0.0016 0.0396  -0.0097 107 LEU B N     
3668 C CA    . LEU B 107 ? 0.2531 0.2377 0.2501 -0.0023 0.0400  -0.0085 107 LEU B CA    
3669 C C     . LEU B 107 ? 0.3086 0.2974 0.3052 -0.0039 0.0400  -0.0074 107 LEU B C     
3670 O O     . LEU B 107 ? 0.3109 0.3055 0.3090 -0.0029 0.0411  -0.0071 107 LEU B O     
3671 C CB    . LEU B 107 ? 0.2545 0.2389 0.2507 -0.0045 0.0388  -0.0073 107 LEU B CB    
3672 C CG    . LEU B 107 ? 0.2571 0.2391 0.2542 -0.0027 0.0390  -0.0084 107 LEU B CG    
3673 C CD1   . LEU B 107 ? 0.2552 0.2361 0.2509 -0.0051 0.0377  -0.0075 107 LEU B CD1   
3674 C CD2   . LEU B 107 ? 0.2531 0.2394 0.2528 0.0002  0.0407  -0.0089 107 LEU B CD2   
3675 N N     . TYR B 108 ? 0.4566 0.4425 0.4512 -0.0059 0.0389  -0.0066 108 TYR B N     
3676 C CA    . TYR B 108 ? 0.4738 0.4636 0.4680 -0.0076 0.0387  -0.0052 108 TYR B CA    
3677 C C     . TYR B 108 ? 0.4848 0.4781 0.4803 -0.0055 0.0402  -0.0063 108 TYR B C     
3678 O O     . TYR B 108 ? 0.5993 0.5982 0.5953 -0.0061 0.0406  -0.0053 108 TYR B O     
3679 C CB    . TYR B 108 ? 0.4389 0.4239 0.4304 -0.0099 0.0373  -0.0041 108 TYR B CB    
3680 C CG    . TYR B 108 ? 0.5218 0.5090 0.5129 -0.0104 0.0375  -0.0034 108 TYR B CG    
3681 C CD1   . TYR B 108 ? 0.5505 0.5432 0.5416 -0.0127 0.0372  -0.0016 108 TYR B CD1   
3682 C CD2   . TYR B 108 ? 0.5283 0.5125 0.5189 -0.0087 0.0379  -0.0044 108 TYR B CD2   
3683 C CE1   . TYR B 108 ? 0.5299 0.5250 0.5208 -0.0131 0.0374  -0.0009 108 TYR B CE1   
3684 C CE2   . TYR B 108 ? 0.5211 0.5079 0.5114 -0.0091 0.0380  -0.0037 108 TYR B CE2   
3685 C CZ    . TYR B 108 ? 0.4903 0.4823 0.4807 -0.0113 0.0378  -0.0020 108 TYR B CZ    
3686 O OH    . TYR B 108 ? 0.4915 0.4862 0.4815 -0.0117 0.0379  -0.0012 108 TYR B OH    
3687 N N     . ALA B 109 ? 0.3903 0.3805 0.3861 -0.0031 0.0410  -0.0082 109 ALA B N     
3688 C CA    . ALA B 109 ? 0.3381 0.3309 0.3344 -0.0014 0.0423  -0.0095 109 ALA B CA    
3689 C C     . ALA B 109 ? 0.4341 0.4304 0.4320 0.0009  0.0440  -0.0105 109 ALA B C     
3690 O O     . ALA B 109 ? 0.4586 0.4571 0.4566 0.0023  0.0454  -0.0116 109 ALA B O     
3691 C CB    . ALA B 109 ? 0.3247 0.3129 0.3202 -0.0004 0.0424  -0.0110 109 ALA B CB    
3692 N N     . ASP B 110 ? 0.5399 0.5366 0.5388 0.0014  0.0441  -0.0101 110 ASP B N     
3693 C CA    . ASP B 110 ? 0.5427 0.5441 0.5431 0.0035  0.0456  -0.0101 110 ASP B CA    
3694 C C     . ASP B 110 ? 0.5506 0.5593 0.5514 0.0023  0.0456  -0.0081 110 ASP B C     
3695 O O     . ASP B 110 ? 0.5483 0.5618 0.5497 0.0043  0.0471  -0.0083 110 ASP B O     
3696 C CB    . ASP B 110 ? 0.5884 0.5887 0.5897 0.0043  0.0454  -0.0098 110 ASP B CB    
3697 C CG    . ASP B 110 ? 0.6553 0.6512 0.6570 0.0071  0.0466  -0.0118 110 ASP B CG    
3698 O OD1   . ASP B 110 ? 0.6024 0.5940 0.6032 0.0075  0.0468  -0.0135 110 ASP B OD1   
3699 O OD2   . ASP B 110 ? 0.7263 0.7234 0.7292 0.0087  0.0473  -0.0115 110 ASP B OD2   
3700 N N     . HIS B 111 ? 0.5861 0.5958 0.5864 -0.0010 0.0438  -0.0061 111 HIS B N     
3701 C CA    . HIS B 111 ? 0.5919 0.6087 0.5924 -0.0030 0.0435  -0.0039 111 HIS B CA    
3702 C C     . HIS B 111 ? 0.5158 0.5345 0.5156 -0.0033 0.0438  -0.0040 111 HIS B C     
3703 O O     . HIS B 111 ? 0.6050 0.6307 0.6054 -0.0028 0.0447  -0.0031 111 HIS B O     
3704 C CB    . HIS B 111 ? 0.6090 0.6247 0.6084 -0.0070 0.0414  -0.0019 111 HIS B CB    
3705 C CG    . HIS B 111 ? 0.6345 0.6578 0.6341 -0.0097 0.0408  0.0008  111 HIS B CG    
3706 N ND1   . HIS B 111 ? 0.6515 0.6738 0.6494 -0.0141 0.0388  0.0027  111 HIS B ND1   
3707 C CD2   . HIS B 111 ? 0.6516 0.6838 0.6526 -0.0088 0.0419  0.0019  111 HIS B CD2   
3708 C CE1   . HIS B 111 ? 0.6902 0.7208 0.6886 -0.0161 0.0387  0.0050  111 HIS B CE1   
3709 N NE2   . HIS B 111 ? 0.7273 0.7645 0.7278 -0.0127 0.0405  0.0046  111 HIS B NE2   
3710 N N     . LEU B 112 ? 0.4052 0.4183 0.4036 -0.0039 0.0432  -0.0050 112 LEU B N     
3711 C CA    . LEU B 112 ? 0.4385 0.4534 0.4363 -0.0040 0.0436  -0.0052 112 LEU B CA    
3712 C C     . LEU B 112 ? 0.4356 0.4525 0.4339 -0.0007 0.0457  -0.0074 112 LEU B C     
3713 O O     . LEU B 112 ? 0.4995 0.5205 0.4974 -0.0006 0.0463  -0.0074 112 LEU B O     
3714 C CB    . LEU B 112 ? 0.3570 0.3656 0.3532 -0.0051 0.0425  -0.0057 112 LEU B CB    
3715 C CG    . LEU B 112 ? 0.3459 0.3564 0.3412 -0.0060 0.0424  -0.0053 112 LEU B CG    
3716 C CD1   . LEU B 112 ? 0.2783 0.2942 0.2734 -0.0086 0.0417  -0.0026 112 LEU B CD1   
3717 C CD2   . LEU B 112 ? 0.4168 0.4210 0.4106 -0.0066 0.0414  -0.0054 112 LEU B CD2   
3718 N N     . GLU B 113 ? 0.3768 0.3907 0.3756 0.0019  0.0468  -0.0091 113 GLU B N     
3719 C CA    . GLU B 113 ? 0.4130 0.4281 0.4116 0.0049  0.0489  -0.0112 113 GLU B CA    
3720 C C     . GLU B 113 ? 0.3773 0.3994 0.3769 0.0066  0.0502  -0.0101 113 GLU B C     
3721 O O     . GLU B 113 ? 0.4158 0.4412 0.4148 0.0083  0.0518  -0.0109 113 GLU B O     
3722 C CB    . GLU B 113 ? 0.4921 0.5008 0.4905 0.0070  0.0497  -0.0134 113 GLU B CB    
3723 C CG    . GLU B 113 ? 0.5587 0.5654 0.5557 0.0088  0.0513  -0.0160 113 GLU B CG    
3724 C CD    . GLU B 113 ? 0.6590 0.6587 0.6554 0.0095  0.0514  -0.0180 113 GLU B CD    
3725 O OE1   . GLU B 113 ? 0.7004 0.6979 0.6970 0.0117  0.0526  -0.0187 113 GLU B OE1   
3726 O OE2   . GLU B 113 ? 0.6610 0.6576 0.6566 0.0078  0.0503  -0.0185 113 GLU B OE2   
3727 N N     . SER B 114 ? 0.4049 0.4297 0.4058 0.0061  0.0496  -0.0082 114 SER B N     
3728 C CA    . SER B 114 ? 0.4081 0.4412 0.4101 0.0073  0.0506  -0.0064 114 SER B CA    
3729 C C     . SER B 114 ? 0.5039 0.5436 0.5056 0.0053  0.0502  -0.0047 114 SER B C     
3730 O O     . SER B 114 ? 0.5708 0.6167 0.5726 0.0074  0.0518  -0.0045 114 SER B O     
3731 C CB    . SER B 114 ? 0.3481 0.3834 0.3515 0.0064  0.0497  -0.0044 114 SER B CB    
3732 O OG    . SER B 114 ? 0.4677 0.4975 0.4714 0.0085  0.0503  -0.0058 114 SER B OG    
3733 N N     . VAL B 115 ? 0.4991 0.5375 0.5003 0.0014  0.0481  -0.0035 115 VAL B N     
3734 C CA    . VAL B 115 ? 0.5242 0.5690 0.5252 -0.0009 0.0475  -0.0015 115 VAL B CA    
3735 C C     . VAL B 115 ? 0.5922 0.6379 0.5922 0.0007  0.0488  -0.0031 115 VAL B C     
3736 O O     . VAL B 115 ? 0.5989 0.6520 0.5990 0.0010  0.0495  -0.0021 115 VAL B O     
3737 C CB    . VAL B 115 ? 0.4893 0.5314 0.4895 -0.0055 0.0450  0.0004  115 VAL B CB    
3738 C CG1   . VAL B 115 ? 0.4454 0.4937 0.4452 -0.0081 0.0444  0.0026  115 VAL B CG1   
3739 C CG2   . VAL B 115 ? 0.4506 0.4923 0.4513 -0.0073 0.0439  0.0019  115 VAL B CG2   
3740 N N     . ILE B 116 ? 0.7119 0.7504 0.7108 0.0016  0.0490  -0.0057 116 ILE B N     
3741 C CA    . ILE B 116 ? 0.6639 0.7032 0.6615 0.0030  0.0504  -0.0076 116 ILE B CA    
3742 C C     . ILE B 116 ? 0.6135 0.6558 0.6110 0.0070  0.0529  -0.0090 116 ILE B C     
3743 O O     . ILE B 116 ? 0.5973 0.6432 0.5938 0.0082  0.0542  -0.0099 116 ILE B O     
3744 C CB    . ILE B 116 ? 0.5691 0.6007 0.5654 0.0030  0.0502  -0.0100 116 ILE B CB    
3745 C CG1   . ILE B 116 ? 0.6210 0.6478 0.6174 0.0001  0.0480  -0.0088 116 ILE B CG1   
3746 C CG2   . ILE B 116 ? 0.4970 0.5309 0.4919 0.0031  0.0509  -0.0113 116 ILE B CG2   
3747 C CD1   . ILE B 116 ? 0.6854 0.7151 0.6815 -0.0031 0.0464  -0.0063 116 ILE B CD1   
3748 N N     . LYS B 117 ? 0.5689 0.6095 0.5672 0.0091  0.0536  -0.0093 117 LYS B N     
3749 C CA    . LYS B 117 ? 0.5423 0.5844 0.5401 0.0134  0.0562  -0.0107 117 LYS B CA    
3750 C C     . LYS B 117 ? 0.5774 0.6296 0.5761 0.0145  0.0570  -0.0083 117 LYS B C     
3751 O O     . LYS B 117 ? 0.5635 0.6191 0.5610 0.0174  0.0590  -0.0093 117 LYS B O     
3752 C CB    . LYS B 117 ? 0.4823 0.5191 0.4806 0.0155  0.0568  -0.0115 117 LYS B CB    
3753 C CG    . LYS B 117 ? 0.4212 0.4523 0.4175 0.0191  0.0591  -0.0146 117 LYS B CG    
3754 C CD    . LYS B 117 ? 0.4618 0.4910 0.4590 0.0221  0.0602  -0.0144 117 LYS B CD    
3755 C CE    . LYS B 117 ? 0.6076 0.6322 0.6023 0.0262  0.0630  -0.0171 117 LYS B CE    
3756 N NZ    . LYS B 117 ? 0.6026 0.6255 0.5981 0.0295  0.0642  -0.0166 117 LYS B NZ    
3757 N N     . GLN B 118 ? 0.6043 0.6617 0.6049 0.0121  0.0554  -0.0051 118 GLN B N     
3758 C CA    . GLN B 118 ? 0.6027 0.6709 0.6043 0.0123  0.0558  -0.0024 118 GLN B CA    
3759 C C     . GLN B 118 ? 0.6173 0.6900 0.6180 0.0111  0.0558  -0.0022 118 GLN B C     
3760 O O     . GLN B 118 ? 0.6100 0.6902 0.6104 0.0134  0.0575  -0.0017 118 GLN B O     
3761 C CB    . GLN B 118 ? 0.5660 0.6385 0.5694 0.0088  0.0538  0.0010  118 GLN B CB    
3762 C CG    . GLN B 118 ? 0.6363 0.7072 0.6409 0.0103  0.0539  0.0013  118 GLN B CG    
3763 C CD    . GLN B 118 ? 0.6833 0.7516 0.6886 0.0058  0.0513  0.0029  118 GLN B CD    
3764 O OE1   . GLN B 118 ? 0.7213 0.7944 0.7269 0.0016  0.0495  0.0055  118 GLN B OE1   
3765 N NE2   . GLN B 118 ? 0.6149 0.6753 0.6202 0.0065  0.0510  0.0014  118 GLN B NE2   
3766 N N     . GLU B 119 ? 0.7253 0.7936 0.7252 0.0076  0.0541  -0.0026 119 GLU B N     
3767 C CA    . GLU B 119 ? 0.7503 0.8236 0.7495 0.0056  0.0536  -0.0017 119 GLU B CA    
3768 C C     . GLU B 119 ? 0.7018 0.7739 0.6991 0.0081  0.0555  -0.0046 119 GLU B C     
3769 O O     . GLU B 119 ? 0.6353 0.7145 0.6321 0.0087  0.0563  -0.0040 119 GLU B O     
3770 C CB    . GLU B 119 ? 0.8326 0.9020 0.8318 0.0009  0.0510  -0.0004 119 GLU B CB    
3771 C CG    . GLU B 119 ? 0.9350 1.0085 0.9334 -0.0013 0.0504  0.0006  119 GLU B CG    
3772 C CD    . GLU B 119 ? 1.0092 1.0786 1.0073 -0.0056 0.0480  0.0023  119 GLU B CD    
3773 O OE1   . GLU B 119 ? 1.0156 1.0794 1.0140 -0.0070 0.0467  0.0027  119 GLU B OE1   
3774 O OE2   . GLU B 119 ? 1.0198 1.0915 1.0172 -0.0074 0.0474  0.0032  119 GLU B OE2   
3775 N N     . SER B 120 ? 0.6603 0.7237 0.6562 0.0094  0.0561  -0.0078 120 SER B N     
3776 C CA    . SER B 120 ? 0.6404 0.7018 0.6339 0.0105  0.0573  -0.0106 120 SER B CA    
3777 C C     . SER B 120 ? 0.7174 0.7786 0.7093 0.0152  0.0602  -0.0130 120 SER B C     
3778 O O     . SER B 120 ? 0.7504 0.8083 0.7427 0.0177  0.0612  -0.0136 120 SER B O     
3779 C CB    . SER B 120 ? 0.5779 0.6305 0.5705 0.0089  0.0563  -0.0127 120 SER B CB    
3780 O OG    . SER B 120 ? 0.5519 0.6032 0.5421 0.0095  0.0575  -0.0154 120 SER B OG    
3781 N N     . ASP B 121 ? 0.8062 0.8707 0.7961 0.0165  0.0617  -0.0144 121 ASP B N     
3782 C CA    . ASP B 121 ? 0.8622 0.9243 0.8493 0.0208  0.0646  -0.0175 121 ASP B CA    
3783 C C     . ASP B 121 ? 0.8626 0.9158 0.8468 0.0204  0.0651  -0.0213 121 ASP B C     
3784 O O     . ASP B 121 ? 0.8868 0.9369 0.8677 0.0234  0.0674  -0.0243 121 ASP B O     
3785 C CB    . ASP B 121 ? 0.9128 0.9839 0.8989 0.0228  0.0662  -0.0169 121 ASP B CB    
3786 C CG    . ASP B 121 ? 0.9973 1.0708 0.9820 0.0201  0.0655  -0.0176 121 ASP B CG    
3787 O OD1   . ASP B 121 ? 1.0669 1.1455 1.0538 0.0164  0.0633  -0.0148 121 ASP B OD1   
3788 O OD2   . ASP B 121 ? 0.9311 1.0011 0.9124 0.0216  0.0671  -0.0211 121 ASP B OD2   
3789 N N     . LEU B 122 ? 0.6968 0.7459 0.6817 0.0167  0.0629  -0.0212 122 LEU B N     
3790 C CA    . LEU B 122 ? 0.6740 0.7156 0.6564 0.0158  0.0630  -0.0245 122 LEU B CA    
3791 C C     . LEU B 122 ? 0.7130 0.7570 0.6926 0.0152  0.0638  -0.0264 122 LEU B C     
3792 O O     . LEU B 122 ? 0.7238 0.7621 0.7005 0.0149  0.0646  -0.0296 122 LEU B O     
3793 C CB    . LEU B 122 ? 0.6336 0.6671 0.6144 0.0186  0.0647  -0.0270 122 LEU B CB    
3794 C CG    . LEU B 122 ? 0.6597 0.6909 0.6434 0.0188  0.0636  -0.0250 122 LEU B CG    
3795 C CD1   . LEU B 122 ? 0.6589 0.6882 0.6420 0.0231  0.0659  -0.0256 122 LEU B CD1   
3796 C CD2   . LEU B 122 ? 0.6770 0.7008 0.6606 0.0164  0.0622  -0.0262 122 LEU B CD2   
3797 N N     . SER B 123 ? 0.5782 0.6309 0.5585 0.0147  0.0637  -0.0245 123 SER B N     
3798 C CA    . SER B 123 ? 0.5285 0.5842 0.5060 0.0144  0.0646  -0.0264 123 SER B CA    
3799 C C     . SER B 123 ? 0.4504 0.5060 0.4282 0.0102  0.0625  -0.0260 123 SER B C     
3800 O O     . SER B 123 ? 0.4210 0.4760 0.3960 0.0094  0.0631  -0.0285 123 SER B O     
3801 C CB    . SER B 123 ? 0.4968 0.5625 0.4748 0.0157  0.0654  -0.0244 123 SER B CB    
3802 O OG    . SER B 123 ? 0.5254 0.5972 0.5069 0.0127  0.0630  -0.0204 123 SER B OG    
3803 N N     . VAL B 124 ? 0.4306 0.4867 0.4116 0.0077  0.0601  -0.0229 124 VAL B N     
3804 C CA    . VAL B 124 ? 0.4132 0.4683 0.3944 0.0043  0.0582  -0.0224 124 VAL B CA    
3805 C C     . VAL B 124 ? 0.4430 0.4898 0.4224 0.0039  0.0583  -0.0254 124 VAL B C     
3806 O O     . VAL B 124 ? 0.3822 0.4288 0.3603 0.0019  0.0577  -0.0263 124 VAL B O     
3807 C CB    . VAL B 124 ? 0.3583 0.4148 0.3427 0.0021  0.0558  -0.0184 124 VAL B CB    
3808 C CG1   . VAL B 124 ? 0.3820 0.4319 0.3679 0.0029  0.0554  -0.0182 124 VAL B CG1   
3809 C CG2   . VAL B 124 ? 0.2809 0.3377 0.2654 -0.0008 0.0541  -0.0173 124 VAL B CG2   
3810 N N     . PHE B 125 ? 0.4884 0.5287 0.4678 0.0058  0.0591  -0.0267 125 PHE B N     
3811 C CA    . PHE B 125 ? 0.4542 0.4868 0.4319 0.0053  0.0592  -0.0293 125 PHE B CA    
3812 C C     . PHE B 125 ? 0.5784 0.6092 0.5518 0.0059  0.0611  -0.0331 125 PHE B C     
3813 O O     . PHE B 125 ? 0.6828 0.7094 0.6543 0.0042  0.0609  -0.0353 125 PHE B O     
3814 C CB    . PHE B 125 ? 0.4363 0.4627 0.4151 0.0071  0.0594  -0.0295 125 PHE B CB    
3815 C CG    . PHE B 125 ? 0.5242 0.5518 0.5066 0.0063  0.0575  -0.0260 125 PHE B CG    
3816 C CD1   . PHE B 125 ? 0.4775 0.5029 0.4612 0.0039  0.0555  -0.0247 125 PHE B CD1   
3817 C CD2   . PHE B 125 ? 0.5270 0.5585 0.5113 0.0079  0.0578  -0.0239 125 PHE B CD2   
3818 C CE1   . PHE B 125 ? 0.4906 0.5165 0.4770 0.0031  0.0539  -0.0217 125 PHE B CE1   
3819 C CE2   . PHE B 125 ? 0.4930 0.5256 0.4801 0.0067  0.0561  -0.0208 125 PHE B CE2   
3820 C CZ    . PHE B 125 ? 0.5514 0.5807 0.5394 0.0043  0.0541  -0.0199 125 PHE B CZ    
3821 N N     . ASN B 126 ? 0.6430 0.6772 0.6148 0.0082  0.0630  -0.0340 126 ASN B N     
3822 C CA    . ASN B 126 ? 0.6196 0.6527 0.5868 0.0087  0.0650  -0.0377 126 ASN B CA    
3823 C C     . ASN B 126 ? 0.4818 0.5211 0.4483 0.0058  0.0640  -0.0374 126 ASN B C     
3824 O O     . ASN B 126 ? 0.4027 0.4398 0.3657 0.0042  0.0645  -0.0404 126 ASN B O     
3825 C CB    . ASN B 126 ? 0.5456 0.5800 0.5110 0.0127  0.0675  -0.0386 126 ASN B CB    
3826 C CG    . ASN B 126 ? 0.5243 0.5504 0.4881 0.0157  0.0692  -0.0406 126 ASN B CG    
3827 O OD1   . ASN B 126 ? 0.4819 0.5019 0.4410 0.0165  0.0711  -0.0443 126 ASN B OD1   
3828 N ND2   . ASN B 126 ? 0.5632 0.5886 0.5304 0.0170  0.0686  -0.0381 126 ASN B ND2   
3829 N N     . GLU B 127 ? 0.4317 0.4787 0.4014 0.0049  0.0626  -0.0338 127 GLU B N     
3830 C CA    . GLU B 127 ? 0.4878 0.5414 0.4574 0.0022  0.0615  -0.0328 127 GLU B CA    
3831 C C     . GLU B 127 ? 0.5418 0.5932 0.5121 -0.0010 0.0596  -0.0322 127 GLU B C     
3832 O O     . GLU B 127 ? 0.5634 0.6180 0.5321 -0.0032 0.0592  -0.0329 127 GLU B O     
3833 C CB    . GLU B 127 ? 0.4738 0.5359 0.4466 0.0021  0.0605  -0.0287 127 GLU B CB    
3834 C CG    . GLU B 127 ? 0.4163 0.4834 0.3887 0.0051  0.0624  -0.0286 127 GLU B CG    
3835 C CD    . GLU B 127 ? 0.5343 0.6094 0.5102 0.0045  0.0611  -0.0241 127 GLU B CD    
3836 O OE1   . GLU B 127 ? 0.5832 0.6597 0.5613 0.0016  0.0589  -0.0212 127 GLU B OE1   
3837 O OE2   . GLU B 127 ? 0.5816 0.6615 0.5578 0.0069  0.0624  -0.0233 127 GLU B OE2   
3838 N N     . LEU B 128 ? 0.4803 0.5265 0.4529 -0.0011 0.0584  -0.0310 128 LEU B N     
3839 C CA    . LEU B 128 ? 0.3784 0.4224 0.3518 -0.0036 0.0566  -0.0303 128 LEU B CA    
3840 C C     . LEU B 128 ? 0.3303 0.3686 0.3004 -0.0044 0.0574  -0.0340 128 LEU B C     
3841 O O     . LEU B 128 ? 0.3052 0.3429 0.2755 -0.0067 0.0561  -0.0336 128 LEU B O     
3842 C CB    . LEU B 128 ? 0.3449 0.3858 0.3217 -0.0033 0.0551  -0.0274 128 LEU B CB    
3843 C CG    . LEU B 128 ? 0.3555 0.3950 0.3340 -0.0052 0.0530  -0.0253 128 LEU B CG    
3844 C CD1   . LEU B 128 ? 0.3677 0.4137 0.3467 -0.0071 0.0519  -0.0228 128 LEU B CD1   
3845 C CD2   . LEU B 128 ? 0.3352 0.3713 0.3165 -0.0044 0.0519  -0.0229 128 LEU B CD2   
3846 N N     . ARG B 129 ? 0.3235 0.3578 0.2903 -0.0028 0.0595  -0.0375 129 ARG B N     
3847 C CA    . ARG B 129 ? 0.2892 0.3180 0.2523 -0.0042 0.0603  -0.0412 129 ARG B CA    
3848 C C     . ARG B 129 ? 0.3800 0.4135 0.3410 -0.0074 0.0597  -0.0420 129 ARG B C     
3849 O O     . ARG B 129 ? 0.4216 0.4531 0.3815 -0.0099 0.0589  -0.0428 129 ARG B O     
3850 C CB    . ARG B 129 ? 0.3144 0.3380 0.2735 -0.0017 0.0629  -0.0447 129 ARG B CB    
3851 C CG    . ARG B 129 ? 0.4538 0.4710 0.4142 0.0011  0.0636  -0.0445 129 ARG B CG    
3852 C CD    . ARG B 129 ? 0.5035 0.5134 0.4591 0.0031  0.0662  -0.0484 129 ARG B CD    
3853 N NE    . ARG B 129 ? 0.5924 0.6050 0.5470 0.0066  0.0682  -0.0487 129 ARG B NE    
3854 C CZ    . ARG B 129 ? 0.6106 0.6235 0.5606 0.0072  0.0701  -0.0516 129 ARG B CZ    
3855 N NH1   . ARG B 129 ? 0.6393 0.6497 0.5851 0.0040  0.0702  -0.0546 129 ARG B NH1   
3856 N NH2   . ARG B 129 ? 0.5349 0.5508 0.4841 0.0109  0.0720  -0.0515 129 ARG B NH2   
3857 N N     . ASP B 130 ? 0.5490 0.5895 0.5093 -0.0075 0.0601  -0.0415 130 ASP B N     
3858 C CA    . ASP B 130 ? 0.5955 0.6412 0.5535 -0.0103 0.0599  -0.0425 130 ASP B CA    
3859 C C     . ASP B 130 ? 0.6607 0.7124 0.6219 -0.0125 0.0575  -0.0387 130 ASP B C     
3860 O O     . ASP B 130 ? 0.7250 0.7811 0.6847 -0.0152 0.0570  -0.0392 130 ASP B O     
3861 C CB    . ASP B 130 ? 0.7048 0.7555 0.6605 -0.0091 0.0614  -0.0437 130 ASP B CB    
3862 C CG    . ASP B 130 ? 0.8233 0.8682 0.7765 -0.0057 0.0638  -0.0464 130 ASP B CG    
3863 O OD1   . ASP B 130 ? 0.8742 0.9124 0.8227 -0.0059 0.0654  -0.0505 130 ASP B OD1   
3864 O OD2   . ASP B 130 ? 0.7923 0.8390 0.7482 -0.0027 0.0642  -0.0443 130 ASP B OD2   
3865 N N     . SER B 131 ? 0.5525 0.6044 0.5181 -0.0114 0.0562  -0.0350 131 SER B N     
3866 C CA    . SER B 131 ? 0.5036 0.5584 0.4718 -0.0131 0.0541  -0.0317 131 SER B CA    
3867 C C     . SER B 131 ? 0.5107 0.5600 0.4784 -0.0142 0.0535  -0.0328 131 SER B C     
3868 O O     . SER B 131 ? 0.4396 0.4921 0.4073 -0.0163 0.0524  -0.0318 131 SER B O     
3869 C CB    . SER B 131 ? 0.5496 0.6054 0.5218 -0.0117 0.0529  -0.0276 131 SER B CB    
3870 O OG    . SER B 131 ? 0.6545 0.7170 0.6273 -0.0114 0.0531  -0.0259 131 SER B OG    
3871 N N     . TYR B 132 ? 0.6001 0.6418 0.5676 -0.0127 0.0542  -0.0345 132 TYR B N     
3872 C CA    . TYR B 132 ? 0.6154 0.6520 0.5822 -0.0138 0.0538  -0.0357 132 TYR B CA    
3873 C C     . TYR B 132 ? 0.6009 0.6385 0.5636 -0.0167 0.0543  -0.0388 132 TYR B C     
3874 O O     . TYR B 132 ? 0.6424 0.6827 0.6052 -0.0190 0.0531  -0.0379 132 TYR B O     
3875 C CB    . TYR B 132 ? 0.5993 0.6276 0.5661 -0.0117 0.0547  -0.0373 132 TYR B CB    
3876 C CG    . TYR B 132 ? 0.5919 0.6147 0.5575 -0.0130 0.0545  -0.0390 132 TYR B CG    
3877 C CD1   . TYR B 132 ? 0.5506 0.5734 0.5188 -0.0135 0.0529  -0.0366 132 TYR B CD1   
3878 C CD2   . TYR B 132 ? 0.5890 0.6065 0.5504 -0.0137 0.0561  -0.0430 132 TYR B CD2   
3879 C CE1   . TYR B 132 ? 0.6214 0.6399 0.5885 -0.0148 0.0527  -0.0379 132 TYR B CE1   
3880 C CE2   . TYR B 132 ? 0.6002 0.6128 0.5603 -0.0153 0.0559  -0.0443 132 TYR B CE2   
3881 C CZ    . TYR B 132 ? 0.6339 0.6475 0.5970 -0.0159 0.0541  -0.0417 132 TYR B CZ    
3882 O OH    . TYR B 132 ? 0.6714 0.6809 0.6334 -0.0176 0.0538  -0.0428 132 TYR B OH    
3883 N N     . ASN B 133 ? 0.5018 0.5373 0.4606 -0.0166 0.0562  -0.0424 133 ASN B N     
3884 C CA    . ASN B 133 ? 0.4739 0.5090 0.4279 -0.0197 0.0569  -0.0459 133 ASN B CA    
3885 C C     . ASN B 133 ? 0.4405 0.4849 0.3944 -0.0225 0.0558  -0.0446 133 ASN B C     
3886 O O     . ASN B 133 ? 0.4389 0.4844 0.3903 -0.0258 0.0554  -0.0460 133 ASN B O     
3887 C CB    . ASN B 133 ? 0.4858 0.5167 0.4354 -0.0185 0.0592  -0.0499 133 ASN B CB    
3888 C CG    . ASN B 133 ? 0.5985 0.6201 0.5477 -0.0158 0.0605  -0.0513 133 ASN B CG    
3889 O OD1   . ASN B 133 ? 0.5978 0.6123 0.5432 -0.0169 0.0615  -0.0545 133 ASN B OD1   
3890 N ND2   . ASN B 133 ? 0.7008 0.7226 0.6539 -0.0124 0.0605  -0.0489 133 ASN B ND2   
3891 N N     . ALA B 134 ? 0.2910 0.3423 0.2474 -0.0214 0.0553  -0.0418 134 ALA B N     
3892 C CA    . ALA B 134 ? 0.2890 0.3497 0.2462 -0.0235 0.0540  -0.0394 134 ALA B CA    
3893 C C     . ALA B 134 ? 0.2921 0.3545 0.2517 -0.0249 0.0522  -0.0366 134 ALA B C     
3894 O O     . ALA B 134 ? 0.2934 0.3610 0.2514 -0.0277 0.0516  -0.0367 134 ALA B O     
3895 C CB    . ALA B 134 ? 0.2856 0.3519 0.2458 -0.0216 0.0537  -0.0361 134 ALA B CB    
3896 N N     . VAL B 135 ? 0.3343 0.3933 0.2976 -0.0227 0.0513  -0.0338 135 VAL B N     
3897 C CA    . VAL B 135 ? 0.2777 0.3394 0.2435 -0.0232 0.0496  -0.0305 135 VAL B CA    
3898 C C     . VAL B 135 ? 0.2915 0.3485 0.2563 -0.0244 0.0493  -0.0320 135 VAL B C     
3899 O O     . VAL B 135 ? 0.2768 0.3376 0.2427 -0.0254 0.0481  -0.0297 135 VAL B O     
3900 C CB    . VAL B 135 ? 0.2731 0.3340 0.2430 -0.0205 0.0486  -0.0263 135 VAL B CB    
3901 C CG1   . VAL B 135 ? 0.2723 0.3385 0.2431 -0.0198 0.0486  -0.0243 135 VAL B CG1   
3902 C CG2   . VAL B 135 ? 0.2723 0.3244 0.2434 -0.0182 0.0490  -0.0271 135 VAL B CG2   
3903 N N     . LYS B 136 ? 0.3678 0.4172 0.3304 -0.0244 0.0505  -0.0356 136 LYS B N     
3904 C CA    . LYS B 136 ? 0.4316 0.4757 0.3937 -0.0252 0.0502  -0.0366 136 LYS B CA    
3905 C C     . LYS B 136 ? 0.5214 0.5703 0.4814 -0.0289 0.0495  -0.0371 136 LYS B C     
3906 O O     . LYS B 136 ? 0.5437 0.5978 0.5009 -0.0315 0.0498  -0.0385 136 LYS B O     
3907 C CB    . LYS B 136 ? 0.4316 0.4668 0.3911 -0.0247 0.0518  -0.0406 136 LYS B CB    
3908 C CG    . LYS B 136 ? 0.4184 0.4533 0.3728 -0.0268 0.0534  -0.0446 136 LYS B CG    
3909 C CD    . LYS B 136 ? 0.4544 0.4803 0.4064 -0.0248 0.0553  -0.0478 136 LYS B CD    
3910 C CE    . LYS B 136 ? 0.3960 0.4146 0.3437 -0.0271 0.0561  -0.0514 136 LYS B CE    
3911 N NZ    . LYS B 136 ? 0.3732 0.3966 0.3182 -0.0318 0.0553  -0.0523 136 LYS B NZ    
3912 N N     . PRO B 137 ? 0.5858 0.6328 0.5468 -0.0294 0.0487  -0.0362 137 PRO B N     
3913 C CA    . PRO B 137 ? 0.5804 0.6321 0.5391 -0.0334 0.0481  -0.0370 137 PRO B CA    
3914 C C     . PRO B 137 ? 0.5817 0.6277 0.5352 -0.0362 0.0495  -0.0419 137 PRO B C     
3915 O O     . PRO B 137 ? 0.5390 0.5769 0.4914 -0.0344 0.0508  -0.0442 137 PRO B O     
3916 C CB    . PRO B 137 ? 0.5388 0.5890 0.4999 -0.0326 0.0471  -0.0348 137 PRO B CB    
3917 C CG    . PRO B 137 ? 0.5506 0.5984 0.5159 -0.0282 0.0467  -0.0318 137 PRO B CG    
3918 C CD    . PRO B 137 ? 0.5748 0.6176 0.5394 -0.0266 0.0480  -0.0339 137 PRO B CD    
3919 N N     . GLU B 138 ? 0.7392 0.7893 0.6893 -0.0407 0.0493  -0.0435 138 GLU B N     
3920 C CA    . GLU B 138 ? 0.7002 0.7442 0.6445 -0.0438 0.0506  -0.0484 138 GLU B CA    
3921 C C     . GLU B 138 ? 0.7216 0.7558 0.6651 -0.0436 0.0510  -0.0499 138 GLU B C     
3922 O O     . GLU B 138 ? 0.7543 0.7800 0.6938 -0.0441 0.0525  -0.0537 138 GLU B O     
3923 C CB    . GLU B 138 ? 0.7451 0.7962 0.6858 -0.0492 0.0500  -0.0494 138 GLU B CB    
3924 C CG    . GLU B 138 ? 0.8693 0.9301 0.8133 -0.0503 0.0481  -0.0453 138 GLU B CG    
3925 C CD    . GLU B 138 ? 0.9259 0.9840 0.8691 -0.0527 0.0475  -0.0456 138 GLU B CD    
3926 O OE1   . GLU B 138 ? 0.9044 0.9559 0.8427 -0.0561 0.0483  -0.0496 138 GLU B OE1   
3927 O OE2   . GLU B 138 ? 0.9618 1.0241 0.9090 -0.0513 0.0462  -0.0418 138 GLU B OE2   
3928 N N     . TYR B 139 ? 0.6373 0.6725 0.5846 -0.0425 0.0497  -0.0470 139 TYR B N     
3929 C CA    . TYR B 139 ? 0.5595 0.5861 0.5067 -0.0421 0.0500  -0.0480 139 TYR B CA    
3930 C C     . TYR B 139 ? 0.5813 0.6000 0.5305 -0.0373 0.0511  -0.0481 139 TYR B C     
3931 O O     . TYR B 139 ? 0.7011 0.7115 0.6495 -0.0366 0.0517  -0.0495 139 TYR B O     
3932 C CB    . TYR B 139 ? 0.4975 0.5286 0.4479 -0.0425 0.0484  -0.0447 139 TYR B CB    
3933 C CG    . TYR B 139 ? 0.5194 0.5558 0.4753 -0.0385 0.0472  -0.0401 139 TYR B CG    
3934 C CD1   . TYR B 139 ? 0.6075 0.6383 0.5667 -0.0342 0.0474  -0.0388 139 TYR B CD1   
3935 C CD2   . TYR B 139 ? 0.5318 0.5788 0.4892 -0.0393 0.0460  -0.0371 139 TYR B CD2   
3936 C CE1   . TYR B 139 ? 0.6294 0.6640 0.5929 -0.0309 0.0464  -0.0348 139 TYR B CE1   
3937 C CE2   . TYR B 139 ? 0.5661 0.6169 0.5279 -0.0356 0.0451  -0.0329 139 TYR B CE2   
3938 C CZ    . TYR B 139 ? 0.6241 0.6683 0.5889 -0.0315 0.0453  -0.0319 139 TYR B CZ    
3939 O OH    . TYR B 139 ? 0.6976 0.7446 0.6661 -0.0280 0.0445  -0.0280 139 TYR B OH    
3940 N N     . ALA B 140 ? 0.4583 0.4797 0.4100 -0.0341 0.0512  -0.0466 140 ALA B N     
3941 C CA    . ALA B 140 ? 0.4547 0.4697 0.4084 -0.0298 0.0521  -0.0465 140 ALA B CA    
3942 C C     . ALA B 140 ? 0.4907 0.4995 0.4402 -0.0296 0.0542  -0.0505 140 ALA B C     
3943 O O     . ALA B 140 ? 0.4804 0.4917 0.4261 -0.0319 0.0549  -0.0526 140 ALA B O     
3944 C CB    . ALA B 140 ? 0.4628 0.4834 0.4209 -0.0267 0.0514  -0.0430 140 ALA B CB    
3945 N N     . VAL B 141 ? 0.5165 0.5170 0.4661 -0.0269 0.0553  -0.0515 141 VAL B N     
3946 C CA    . VAL B 141 ? 0.5756 0.5694 0.5206 -0.0263 0.0575  -0.0552 141 VAL B CA    
3947 C C     . VAL B 141 ? 0.6465 0.6425 0.5921 -0.0232 0.0586  -0.0551 141 VAL B C     
3948 O O     . VAL B 141 ? 0.6780 0.6753 0.6279 -0.0197 0.0583  -0.0525 141 VAL B O     
3949 C CB    . VAL B 141 ? 0.5723 0.5557 0.5158 -0.0251 0.0586  -0.0568 141 VAL B CB    
3950 C CG1   . VAL B 141 ? 0.4397 0.4220 0.3887 -0.0213 0.0580  -0.0538 141 VAL B CG1   
3951 C CG2   . VAL B 141 ? 0.6416 0.6173 0.5799 -0.0241 0.0611  -0.0606 141 VAL B CG2   
3952 N N     . THR B 142 ? 0.6477 0.6449 0.5889 -0.0247 0.0597  -0.0578 142 THR B N     
3953 C CA    . THR B 142 ? 0.6779 0.6773 0.6188 -0.0219 0.0610  -0.0582 142 THR B CA    
3954 C C     . THR B 142 ? 0.6458 0.6385 0.5876 -0.0173 0.0625  -0.0583 142 THR B C     
3955 O O     . THR B 142 ? 0.6120 0.5957 0.5506 -0.0169 0.0639  -0.0608 142 THR B O     
3956 C CB    . THR B 142 ? 0.7154 0.7143 0.6499 -0.0243 0.0625  -0.0622 142 THR B CB    
3957 O OG1   . THR B 142 ? 0.7458 0.7531 0.6800 -0.0282 0.0611  -0.0615 142 THR B OG1   
3958 C CG2   . THR B 142 ? 0.6840 0.6836 0.6175 -0.0207 0.0643  -0.0630 142 THR B CG2   
3959 N N     . HIS B 143 ? 0.5275 0.5247 0.4737 -0.0140 0.0623  -0.0555 143 HIS B N     
3960 C CA    . HIS B 143 ? 0.5500 0.5426 0.4975 -0.0095 0.0637  -0.0551 143 HIS B CA    
3961 C C     . HIS B 143 ? 0.6186 0.6112 0.5625 -0.0073 0.0659  -0.0574 143 HIS B C     
3962 O O     . HIS B 143 ? 0.6036 0.6037 0.5486 -0.0070 0.0657  -0.0562 143 HIS B O     
3963 C CB    . HIS B 143 ? 0.5723 0.5697 0.5260 -0.0074 0.0621  -0.0508 143 HIS B CB    
3964 C CG    . HIS B 143 ? 0.4835 0.4770 0.4390 -0.0033 0.0632  -0.0501 143 HIS B CG    
3965 N ND1   . HIS B 143 ? 0.4742 0.4667 0.4277 -0.0002 0.0654  -0.0514 143 HIS B ND1   
3966 C CD2   . HIS B 143 ? 0.4984 0.4891 0.4574 -0.0018 0.0625  -0.0480 143 HIS B CD2   
3967 C CE1   . HIS B 143 ? 0.4917 0.4815 0.4476 0.0031  0.0659  -0.0500 143 HIS B CE1   
3968 N NE2   . HIS B 143 ? 0.5230 0.5117 0.4823 0.0020  0.0641  -0.0480 143 HIS B NE2   
3969 N N     . GLU B 144 ? 0.9422 0.9259 0.8814 -0.0058 0.0682  -0.0607 144 GLU B N     
3970 C CA    . GLU B 144 ? 0.9505 0.9327 0.8854 -0.0033 0.0708  -0.0633 144 GLU B CA    
3971 C C     . GLU B 144 ? 0.8319 0.8118 0.7682 0.0022  0.0725  -0.0623 144 GLU B C     
3972 O O     . GLU B 144 ? 0.8323 0.8124 0.7654 0.0049  0.0747  -0.0639 144 GLU B O     
3973 C CB    . GLU B 144 ? 1.0684 1.0416 0.9957 -0.0054 0.0725  -0.0680 144 GLU B CB    
3974 C CG    . GLU B 144 ? 1.0854 1.0475 1.0111 -0.0042 0.0735  -0.0691 144 GLU B CG    
3975 C CD    . GLU B 144 ? 1.0375 0.9973 0.9640 -0.0086 0.0715  -0.0687 144 GLU B CD    
3976 O OE1   . GLU B 144 ? 0.9628 0.9271 0.8954 -0.0086 0.0694  -0.0651 144 GLU B OE1   
3977 O OE2   . GLU B 144 ? 1.0439 0.9973 0.9648 -0.0120 0.0721  -0.0719 144 GLU B OE2   
3978 N N     . THR B 145 ? 0.6544 0.6326 0.5951 0.0041  0.0717  -0.0597 145 THR B N     
3979 C CA    . THR B 145 ? 0.6472 0.6226 0.5886 0.0092  0.0736  -0.0589 145 THR B CA    
3980 C C     . THR B 145 ? 0.6134 0.5986 0.5591 0.0118  0.0732  -0.0558 145 THR B C     
3981 O O     . THR B 145 ? 0.6154 0.6085 0.5648 0.0095  0.0711  -0.0533 145 THR B O     
3982 C CB    . THR B 145 ? 0.6486 0.6185 0.5928 0.0101  0.0729  -0.0574 145 THR B CB    
3983 O OG1   . THR B 145 ? 0.6533 0.6156 0.5942 0.0069  0.0727  -0.0598 145 THR B OG1   
3984 C CG2   . THR B 145 ? 0.5476 0.5131 0.4911 0.0154  0.0754  -0.0574 145 THR B CG2   
3985 N N     . GLU B 146 ? 0.6353 0.6197 0.5802 0.0165  0.0754  -0.0557 146 GLU B N     
3986 C CA    . GLU B 146 ? 0.6049 0.5984 0.5545 0.0190  0.0750  -0.0521 146 GLU B CA    
3987 C C     . GLU B 146 ? 0.6569 0.6503 0.6118 0.0196  0.0735  -0.0488 146 GLU B C     
3988 O O     . GLU B 146 ? 0.5962 0.5821 0.5504 0.0209  0.0742  -0.0495 146 GLU B O     
3989 C CB    . GLU B 146 ? 0.5855 0.5797 0.5325 0.0240  0.0780  -0.0529 146 GLU B CB    
3990 C CG    . GLU B 146 ? 0.6940 0.6989 0.6457 0.0260  0.0774  -0.0490 146 GLU B CG    
3991 C CD    . GLU B 146 ? 0.8010 0.8077 0.7510 0.0317  0.0803  -0.0490 146 GLU B CD    
3992 O OE1   . GLU B 146 ? 0.8870 0.8872 0.8356 0.0352  0.0821  -0.0496 146 GLU B OE1   
3993 O OE2   . GLU B 146 ? 0.7880 0.8030 0.7379 0.0327  0.0808  -0.0483 146 GLU B OE2   
3994 N N     . ILE B 147 ? 0.6190 0.6209 0.5789 0.0187  0.0715  -0.0452 147 ILE B N     
3995 C CA    . ILE B 147 ? 0.5357 0.5384 0.5005 0.0187  0.0698  -0.0420 147 ILE B CA    
3996 C C     . ILE B 147 ? 0.5776 0.5853 0.5444 0.0227  0.0709  -0.0398 147 ILE B C     
3997 O O     . ILE B 147 ? 0.5248 0.5411 0.4932 0.0227  0.0705  -0.0378 147 ILE B O     
3998 C CB    . ILE B 147 ? 0.4888 0.4965 0.4572 0.0148  0.0668  -0.0396 147 ILE B CB    
3999 C CG1   . ILE B 147 ? 0.4544 0.4578 0.4204 0.0113  0.0659  -0.0418 147 ILE B CG1   
4000 C CG2   . ILE B 147 ? 0.5474 0.5558 0.5203 0.0150  0.0651  -0.0363 147 ILE B CG2   
4001 C CD1   . ILE B 147 ? 0.4262 0.4343 0.3949 0.0077  0.0633  -0.0396 147 ILE B CD1   
4002 N N     . LYS B 148 ? 0.7165 0.7192 0.6828 0.0261  0.0725  -0.0401 148 LYS B N     
4003 C CA    . LYS B 148 ? 0.7544 0.7620 0.7225 0.0302  0.0738  -0.0378 148 LYS B CA    
4004 C C     . LYS B 148 ? 0.7123 0.7215 0.6851 0.0300  0.0721  -0.0345 148 LYS B C     
4005 O O     . LYS B 148 ? 0.6740 0.6893 0.6491 0.0326  0.0726  -0.0319 148 LYS B O     
4006 C CB    . LYS B 148 ? 0.8404 0.8418 0.8042 0.0350  0.0772  -0.0402 148 LYS B CB    
4007 C CG    . LYS B 148 ? 0.8525 0.8518 0.8108 0.0357  0.0792  -0.0437 148 LYS B CG    
4008 C CD    . LYS B 148 ? 0.8531 0.8571 0.8096 0.0410  0.0820  -0.0433 148 LYS B CD    
4009 C CE    . LYS B 148 ? 0.7933 0.8104 0.7541 0.0408  0.0808  -0.0396 148 LYS B CE    
4010 N NZ    . LYS B 148 ? 0.7669 0.7895 0.7258 0.0460  0.0836  -0.0393 148 LYS B NZ    
4011 N N     . THR B 149 ? 0.7395 0.7434 0.7136 0.0273  0.0704  -0.0346 149 THR B N     
4012 C CA    . THR B 149 ? 0.7300 0.7353 0.7083 0.0269  0.0687  -0.0317 149 THR B CA    
4013 C C     . THR B 149 ? 0.6816 0.6874 0.6623 0.0224  0.0657  -0.0305 149 THR B C     
4014 O O     . THR B 149 ? 0.7108 0.7144 0.6899 0.0198  0.0650  -0.0322 149 THR B O     
4015 C CB    . THR B 149 ? 0.7958 0.7933 0.7735 0.0286  0.0695  -0.0327 149 THR B CB    
4016 O OG1   . THR B 149 ? 0.7977 0.7897 0.7752 0.0251  0.0678  -0.0339 149 THR B OG1   
4017 C CG2   . THR B 149 ? 0.8419 0.8343 0.8153 0.0326  0.0728  -0.0352 149 THR B CG2   
4018 N N     . LEU B 150 ? 0.5167 0.5257 0.5011 0.0217  0.0640  -0.0276 150 LEU B N     
4019 C CA    . LEU B 150 ? 0.5275 0.5367 0.5138 0.0178  0.0613  -0.0262 150 LEU B CA    
4020 C C     . LEU B 150 ? 0.6161 0.6175 0.6015 0.0164  0.0607  -0.0281 150 LEU B C     
4021 O O     . LEU B 150 ? 0.6589 0.6600 0.6448 0.0134  0.0588  -0.0277 150 LEU B O     
4022 C CB    . LEU B 150 ? 0.5764 0.5897 0.5662 0.0173  0.0598  -0.0229 150 LEU B CB    
4023 C CG    . LEU B 150 ? 0.6330 0.6486 0.6244 0.0134  0.0572  -0.0209 150 LEU B CG    
4024 C CD1   . LEU B 150 ? 0.7143 0.7356 0.7048 0.0122  0.0572  -0.0206 150 LEU B CD1   
4025 C CD2   . LEU B 150 ? 0.6307 0.6492 0.6247 0.0125  0.0557  -0.0179 150 LEU B CD2   
4026 N N     . ASP B 151 ? 0.7075 0.7029 0.6913 0.0185  0.0622  -0.0299 151 ASP B N     
4027 C CA    . ASP B 151 ? 0.7505 0.7391 0.7333 0.0170  0.0617  -0.0316 151 ASP B CA    
4028 C C     . ASP B 151 ? 0.8218 0.8078 0.8012 0.0154  0.0622  -0.0344 151 ASP B C     
4029 O O     . ASP B 151 ? 0.8760 0.8584 0.8548 0.0131  0.0612  -0.0353 151 ASP B O     
4030 C CB    . ASP B 151 ? 0.8828 0.8657 0.8655 0.0194  0.0628  -0.0321 151 ASP B CB    
4031 C CG    . ASP B 151 ? 1.0117 0.9973 0.9980 0.0202  0.0618  -0.0292 151 ASP B CG    
4032 O OD1   . ASP B 151 ? 1.0384 1.0293 1.0259 0.0223  0.0625  -0.0276 151 ASP B OD1   
4033 O OD2   . ASP B 151 ? 1.0767 1.0597 1.0646 0.0189  0.0603  -0.0286 151 ASP B OD2   
4034 N N     . GLU B 152 ? 0.7759 0.7639 0.7527 0.0164  0.0638  -0.0358 152 GLU B N     
4035 C CA    . GLU B 152 ? 0.7818 0.7683 0.7553 0.0142  0.0640  -0.0383 152 GLU B CA    
4036 C C     . GLU B 152 ? 0.7560 0.7489 0.7311 0.0111  0.0620  -0.0368 152 GLU B C     
4037 O O     . GLU B 152 ? 0.7571 0.7490 0.7312 0.0083  0.0610  -0.0377 152 GLU B O     
4038 C CB    . GLU B 152 ? 0.8209 0.8066 0.7904 0.0164  0.0667  -0.0408 152 GLU B CB    
4039 C CG    . GLU B 152 ? 0.9106 0.8908 0.8785 0.0202  0.0689  -0.0417 152 GLU B CG    
4040 C CD    . GLU B 152 ? 1.0087 0.9880 0.9722 0.0228  0.0717  -0.0441 152 GLU B CD    
4041 O OE1   . GLU B 152 ? 1.0668 1.0399 1.0257 0.0216  0.0727  -0.0474 152 GLU B OE1   
4042 O OE2   . GLU B 152 ? 1.0603 1.0452 1.0248 0.0258  0.0727  -0.0426 152 GLU B OE2   
4043 N N     . ALA B 153 ? 0.4797 0.4795 0.4573 0.0117  0.0614  -0.0342 153 ALA B N     
4044 C CA    . ALA B 153 ? 0.4298 0.4348 0.4094 0.0089  0.0593  -0.0321 153 ALA B CA    
4045 C C     . ALA B 153 ? 0.4645 0.4663 0.4458 0.0069  0.0573  -0.0310 153 ALA B C     
4046 O O     . ALA B 153 ? 0.3378 0.3413 0.3193 0.0045  0.0558  -0.0303 153 ALA B O     
4047 C CB    . ALA B 153 ? 0.2718 0.2838 0.2539 0.0095  0.0588  -0.0291 153 ALA B CB    
4048 N N     . LYS B 154 ? 0.6068 0.6042 0.5894 0.0082  0.0573  -0.0307 154 LYS B N     
4049 C CA    . LYS B 154 ? 0.5875 0.5817 0.5716 0.0069  0.0556  -0.0297 154 LYS B CA    
4050 C C     . LYS B 154 ? 0.5888 0.5785 0.5708 0.0055  0.0557  -0.0321 154 LYS B C     
4051 O O     . LYS B 154 ? 0.6834 0.6729 0.6660 0.0036  0.0542  -0.0313 154 LYS B O     
4052 C CB    . LYS B 154 ? 0.5910 0.5827 0.5771 0.0087  0.0556  -0.0287 154 LYS B CB    
4053 C CG    . LYS B 154 ? 0.5066 0.4978 0.4951 0.0076  0.0536  -0.0264 154 LYS B CG    
4054 C CD    . LYS B 154 ? 0.5371 0.5291 0.5276 0.0093  0.0537  -0.0248 154 LYS B CD    
4055 C CE    . LYS B 154 ? 0.6404 0.6382 0.6310 0.0103  0.0547  -0.0240 154 LYS B CE    
4056 N NZ    . LYS B 154 ? 0.6944 0.6943 0.6867 0.0123  0.0552  -0.0225 154 LYS B NZ    
4057 N N     . GLN B 155 ? 0.5668 0.5524 0.5459 0.0065  0.0576  -0.0348 155 GLN B N     
4058 C CA    . GLN B 155 ? 0.5817 0.5636 0.5581 0.0045  0.0577  -0.0372 155 GLN B CA    
4059 C C     . GLN B 155 ? 0.6012 0.5878 0.5764 0.0019  0.0570  -0.0374 155 GLN B C     
4060 O O     . GLN B 155 ? 0.5931 0.5802 0.5683 -0.0005 0.0557  -0.0372 155 GLN B O     
4061 C CB    . GLN B 155 ? 0.6059 0.5822 0.5787 0.0059  0.0600  -0.0402 155 GLN B CB    
4062 C CG    . GLN B 155 ? 0.7037 0.6750 0.6774 0.0084  0.0609  -0.0399 155 GLN B CG    
4063 C CD    . GLN B 155 ? 0.7966 0.7618 0.7692 0.0070  0.0606  -0.0410 155 GLN B CD    
4064 O OE1   . GLN B 155 ? 0.8144 0.7781 0.7844 0.0042  0.0604  -0.0428 155 GLN B OE1   
4065 N NE2   . GLN B 155 ? 0.7993 0.7614 0.7738 0.0087  0.0605  -0.0399 155 GLN B NE2   
4066 N N     . PHE B 156 ? 0.5893 0.5801 0.5637 0.0026  0.0579  -0.0376 156 PHE B N     
4067 C CA    . PHE B 156 ? 0.5283 0.5242 0.5015 0.0003  0.0573  -0.0377 156 PHE B CA    
4068 C C     . PHE B 156 ? 0.4949 0.4952 0.4711 -0.0012 0.0550  -0.0346 156 PHE B C     
4069 O O     . PHE B 156 ? 0.5396 0.5409 0.5152 -0.0035 0.0540  -0.0346 156 PHE B O     
4070 C CB    . PHE B 156 ? 0.4427 0.4429 0.4150 0.0018  0.0586  -0.0379 156 PHE B CB    
4071 C CG    . PHE B 156 ? 0.4088 0.4148 0.3802 -0.0003 0.0581  -0.0378 156 PHE B CG    
4072 C CD1   . PHE B 156 ? 0.4456 0.4507 0.4138 -0.0028 0.0582  -0.0402 156 PHE B CD1   
4073 C CD2   . PHE B 156 ? 0.3781 0.3908 0.3516 -0.0001 0.0574  -0.0353 156 PHE B CD2   
4074 C CE1   . PHE B 156 ? 0.3985 0.4096 0.3658 -0.0049 0.0577  -0.0401 156 PHE B CE1   
4075 C CE2   . PHE B 156 ? 0.4985 0.5169 0.4711 -0.0021 0.0569  -0.0351 156 PHE B CE2   
4076 C CZ    . PHE B 156 ? 0.4883 0.5061 0.4578 -0.0044 0.0571  -0.0375 156 PHE B CZ    
4077 N N     . ILE B 157 ? 0.4955 0.4982 0.4747 0.0000  0.0543  -0.0319 157 ILE B N     
4078 C CA    . ILE B 157 ? 0.5101 0.5162 0.4915 -0.0013 0.0523  -0.0288 157 ILE B CA    
4079 C C     . ILE B 157 ? 0.5471 0.5506 0.5288 -0.0025 0.0511  -0.0286 157 ILE B C     
4080 O O     . ILE B 157 ? 0.5719 0.5786 0.5537 -0.0041 0.0500  -0.0273 157 ILE B O     
4081 C CB    . ILE B 157 ? 0.5800 0.5866 0.5641 0.0001  0.0517  -0.0262 157 ILE B CB    
4082 C CG1   . ILE B 157 ? 0.6475 0.6578 0.6332 -0.0012 0.0499  -0.0230 157 ILE B CG1   
4083 C CG2   . ILE B 157 ? 0.5185 0.5197 0.5039 0.0011  0.0513  -0.0261 157 ILE B CG2   
4084 C CD1   . ILE B 157 ? 0.6954 0.7048 0.6833 -0.0006 0.0491  -0.0207 157 ILE B CD1   
4085 N N     . LEU B 158 ? 0.3932 0.3912 0.3748 -0.0017 0.0514  -0.0297 158 LEU B N     
4086 C CA    . LEU B 158 ? 0.4444 0.4402 0.4268 -0.0025 0.0502  -0.0290 158 LEU B CA    
4087 C C     . LEU B 158 ? 0.4780 0.4748 0.4582 -0.0047 0.0502  -0.0306 158 LEU B C     
4088 O O     . LEU B 158 ? 0.5161 0.5137 0.4970 -0.0055 0.0490  -0.0293 158 LEU B O     
4089 C CB    . LEU B 158 ? 0.4183 0.4084 0.4015 -0.0010 0.0505  -0.0295 158 LEU B CB    
4090 C CG    . LEU B 158 ? 0.4319 0.4211 0.4177 0.0008  0.0500  -0.0275 158 LEU B CG    
4091 C CD1   . LEU B 158 ? 0.4038 0.3882 0.3905 0.0019  0.0501  -0.0278 158 LEU B CD1   
4092 C CD2   . LEU B 158 ? 0.5292 0.5212 0.5166 0.0002  0.0483  -0.0245 158 LEU B CD2   
4093 N N     . SER B 159 ? 0.3935 0.3904 0.3709 -0.0055 0.0516  -0.0332 159 SER B N     
4094 C CA    . SER B 159 ? 0.3955 0.3934 0.3703 -0.0082 0.0516  -0.0350 159 SER B CA    
4095 C C     . SER B 159 ? 0.4546 0.4595 0.4298 -0.0098 0.0504  -0.0331 159 SER B C     
4096 O O     . SER B 159 ? 0.4324 0.4393 0.4059 -0.0122 0.0500  -0.0338 159 SER B O     
4097 C CB    . SER B 159 ? 0.3777 0.3732 0.3487 -0.0088 0.0534  -0.0385 159 SER B CB    
4098 O OG    . SER B 159 ? 0.4519 0.4497 0.4228 -0.0072 0.0544  -0.0386 159 SER B OG    
4099 N N     . PHE B 160 ? 0.3785 0.3871 0.3557 -0.0088 0.0497  -0.0306 160 PHE B N     
4100 C CA    . PHE B 160 ? 0.2985 0.3134 0.2763 -0.0100 0.0486  -0.0283 160 PHE B CA    
4101 C C     . PHE B 160 ? 0.3989 0.4143 0.3774 -0.0106 0.0474  -0.0268 160 PHE B C     
4102 O O     . PHE B 160 ? 0.3341 0.3549 0.3122 -0.0119 0.0467  -0.0255 160 PHE B O     
4103 C CB    . PHE B 160 ? 0.2640 0.2812 0.2440 -0.0086 0.0480  -0.0254 160 PHE B CB    
4104 C CG    . PHE B 160 ? 0.3240 0.3422 0.3036 -0.0079 0.0491  -0.0263 160 PHE B CG    
4105 C CD1   . PHE B 160 ? 0.3839 0.4012 0.3608 -0.0082 0.0507  -0.0296 160 PHE B CD1   
4106 C CD2   . PHE B 160 ? 0.3185 0.3386 0.2999 -0.0069 0.0486  -0.0237 160 PHE B CD2   
4107 C CE1   . PHE B 160 ? 0.3450 0.3637 0.3214 -0.0071 0.0519  -0.0304 160 PHE B CE1   
4108 C CE2   . PHE B 160 ? 0.3425 0.3645 0.3237 -0.0062 0.0496  -0.0243 160 PHE B CE2   
4109 C CZ    . PHE B 160 ? 0.4018 0.4234 0.3806 -0.0060 0.0513  -0.0276 160 PHE B CZ    
4110 N N     . VAL B 161 ? 0.4124 0.4226 0.3919 -0.0095 0.0472  -0.0269 161 VAL B N     
4111 C CA    . VAL B 161 ? 0.4014 0.4119 0.3815 -0.0098 0.0462  -0.0256 161 VAL B CA    
4112 C C     . VAL B 161 ? 0.4800 0.4940 0.4578 -0.0126 0.0463  -0.0271 161 VAL B C     
4113 O O     . VAL B 161 ? 0.5351 0.5531 0.5133 -0.0133 0.0453  -0.0254 161 VAL B O     
4114 C CB    . VAL B 161 ? 0.3705 0.3747 0.3517 -0.0083 0.0462  -0.0261 161 VAL B CB    
4115 C CG1   . VAL B 161 ? 0.3393 0.3392 0.3184 -0.0094 0.0474  -0.0294 161 VAL B CG1   
4116 C CG2   . VAL B 161 ? 0.3080 0.3127 0.2903 -0.0078 0.0450  -0.0240 161 VAL B CG2   
4117 N N     . MET B 162 ? 0.5904 0.6036 0.5656 -0.0143 0.0474  -0.0302 162 MET B N     
4118 C CA    . MET B 162 ? 0.5802 0.5969 0.5527 -0.0176 0.0475  -0.0318 162 MET B CA    
4119 C C     . MET B 162 ? 0.5644 0.5896 0.5372 -0.0187 0.0466  -0.0296 162 MET B C     
4120 O O     . MET B 162 ? 0.6234 0.6533 0.5950 -0.0211 0.0461  -0.0295 162 MET B O     
4121 C CB    . MET B 162 ? 0.5995 0.6129 0.5683 -0.0192 0.0490  -0.0357 162 MET B CB    
4122 C CG    . MET B 162 ? 0.5781 0.5836 0.5456 -0.0193 0.0498  -0.0381 162 MET B CG    
4123 S SD    . MET B 162 ? 0.6937 0.7002 0.6610 -0.0218 0.0487  -0.0375 162 MET B SD    
4124 C CE    . MET B 162 ? 0.7426 0.7413 0.7122 -0.0189 0.0488  -0.0370 162 MET B CE    
4125 N N     . LEU B 163 ? 0.3938 0.4216 0.3682 -0.0170 0.0464  -0.0275 163 LEU B N     
4126 C CA    . LEU B 163 ? 0.5174 0.5532 0.4920 -0.0177 0.0457  -0.0252 163 LEU B CA    
4127 C C     . LEU B 163 ? 0.4762 0.5147 0.4530 -0.0165 0.0444  -0.0215 163 LEU B C     
4128 O O     . LEU B 163 ? 0.4286 0.4736 0.4058 -0.0166 0.0438  -0.0190 163 LEU B O     
4129 C CB    . LEU B 163 ? 0.2766 0.3140 0.2520 -0.0165 0.0460  -0.0242 163 LEU B CB    
4130 C CG    . LEU B 163 ? 0.3494 0.3879 0.3226 -0.0177 0.0472  -0.0269 163 LEU B CG    
4131 C CD1   . LEU B 163 ? 0.4168 0.4494 0.3874 -0.0185 0.0485  -0.0310 163 LEU B CD1   
4132 C CD2   . LEU B 163 ? 0.3412 0.3791 0.3162 -0.0155 0.0473  -0.0253 163 LEU B CD2   
4133 N N     . ASN B 164 ? 0.5000 0.5335 0.4779 -0.0151 0.0441  -0.0213 164 ASN B N     
4134 C CA    . ASN B 164 ? 0.4952 0.5303 0.4748 -0.0132 0.0431  -0.0179 164 ASN B CA    
4135 C C     . ASN B 164 ? 0.5639 0.6059 0.5428 -0.0148 0.0425  -0.0168 164 ASN B C     
4136 O O     . ASN B 164 ? 0.5517 0.5957 0.5287 -0.0179 0.0428  -0.0192 164 ASN B O     
4137 C CB    . ASN B 164 ? 0.4058 0.4337 0.3867 -0.0111 0.0430  -0.0180 164 ASN B CB    
4138 C CG    . ASN B 164 ? 0.5253 0.5487 0.5078 -0.0086 0.0429  -0.0166 164 ASN B CG    
4139 O OD1   . ASN B 164 ? 0.4650 0.4873 0.4473 -0.0088 0.0435  -0.0176 164 ASN B OD1   
4140 N ND2   . ASN B 164 ? 0.5049 0.5256 0.4886 -0.0063 0.0423  -0.0144 164 ASN B ND2   
4141 N N     . ASP B 165 ? 0.7001 0.7458 0.6803 -0.0128 0.0418  -0.0131 165 ASP B N     
4142 C CA    . ASP B 165 ? 0.6978 0.7513 0.6777 -0.0137 0.0412  -0.0112 165 ASP B CA    
4143 C C     . ASP B 165 ? 0.6286 0.6908 0.6070 -0.0165 0.0412  -0.0111 165 ASP B C     
4144 O O     . ASP B 165 ? 0.5948 0.6645 0.5730 -0.0173 0.0407  -0.0093 165 ASP B O     
4145 C CB    . ASP B 165 ? 0.6649 0.7169 0.6448 -0.0140 0.0410  -0.0119 165 ASP B CB    
4146 C CG    . ASP B 165 ? 0.6573 0.7026 0.6388 -0.0104 0.0408  -0.0106 165 ASP B CG    
4147 O OD1   . ASP B 165 ? 0.7275 0.7731 0.7101 -0.0073 0.0404  -0.0074 165 ASP B OD1   
4148 O OD2   . ASP B 165 ? 0.6020 0.6415 0.5836 -0.0107 0.0410  -0.0127 165 ASP B OD2   
4149 N N     . ASN B 166 ? 0.6767 0.7382 0.6543 -0.0177 0.0418  -0.0130 166 ASN B N     
4150 C CA    . ASN B 166 ? 0.6116 0.6811 0.5875 -0.0205 0.0419  -0.0133 166 ASN B CA    
4151 C C     . ASN B 166 ? 0.6151 0.6863 0.5916 -0.0194 0.0420  -0.0119 166 ASN B C     
4152 O O     . ASN B 166 ? 0.6514 0.7284 0.6289 -0.0181 0.0415  -0.0082 166 ASN B O     
4153 C CB    . ASN B 166 ? 0.5694 0.6369 0.5425 -0.0243 0.0426  -0.0181 166 ASN B CB    
4154 C CG    . ASN B 166 ? 0.5962 0.6717 0.5669 -0.0278 0.0428  -0.0190 166 ASN B CG    
4155 O OD1   . ASN B 166 ? 0.6652 0.7497 0.6363 -0.0282 0.0421  -0.0161 166 ASN B OD1   
4156 N ND2   . ASN B 166 ? 0.5888 0.6611 0.5568 -0.0301 0.0437  -0.0230 166 ASN B ND2   
4157 N N     . VAL B 167 ? 0.4551 0.5216 0.4309 -0.0198 0.0428  -0.0146 167 VAL B N     
4158 C CA    . VAL B 167 ? 0.4459 0.5148 0.4221 -0.0192 0.0430  -0.0134 167 VAL B CA    
4159 C C     . VAL B 167 ? 0.5200 0.5858 0.4985 -0.0159 0.0425  -0.0098 167 VAL B C     
4160 O O     . VAL B 167 ? 0.5412 0.6108 0.5202 -0.0154 0.0424  -0.0075 167 VAL B O     
4161 C CB    . VAL B 167 ? 0.4504 0.5156 0.4250 -0.0204 0.0441  -0.0172 167 VAL B CB    
4162 C CG1   . VAL B 167 ? 0.4476 0.5201 0.4208 -0.0223 0.0444  -0.0175 167 VAL B CG1   
4163 C CG2   . VAL B 167 ? 0.4558 0.5165 0.4283 -0.0223 0.0448  -0.0214 167 VAL B CG2   
4164 N N     . GLU B 168 ? 0.7187 0.7777 0.6984 -0.0138 0.0423  -0.0094 168 GLU B N     
4165 C CA    . GLU B 168 ? 0.6991 0.7540 0.6803 -0.0110 0.0419  -0.0064 168 GLU B CA    
4166 C C     . GLU B 168 ? 0.6573 0.7155 0.6392 -0.0090 0.0411  -0.0022 168 GLU B C     
4167 O O     . GLU B 168 ? 0.6526 0.7072 0.6351 -0.0068 0.0408  0.0006  168 GLU B O     
4168 C CB    . GLU B 168 ? 0.7435 0.7896 0.7255 -0.0095 0.0419  -0.0078 168 GLU B CB    
4169 C CG    . GLU B 168 ? 0.8505 0.8955 0.8322 -0.0098 0.0419  -0.0091 168 GLU B CG    
4170 C CD    . GLU B 168 ? 0.8698 0.9102 0.8526 -0.0069 0.0413  -0.0069 168 GLU B CD    
4171 O OE1   . GLU B 168 ? 0.9409 0.9781 0.9244 -0.0050 0.0410  -0.0047 168 GLU B OE1   
4172 O OE2   . GLU B 168 ? 0.8136 0.8536 0.7965 -0.0068 0.0412  -0.0075 168 GLU B OE2   
4173 N N     . LEU B 169 ? 0.3006 0.3655 0.2819 -0.0099 0.0409  -0.0015 169 LEU B N     
4174 C CA    . LEU B 169 ? 0.3244 0.3927 0.3061 -0.0076 0.0404  0.0026  169 LEU B CA    
4175 C C     . LEU B 169 ? 0.3510 0.4235 0.3329 -0.0063 0.0402  0.0065  169 LEU B C     
4176 O O     . LEU B 169 ? 0.3837 0.4537 0.3659 -0.0032 0.0400  0.0099  169 LEU B O     
4177 C CB    . LEU B 169 ? 0.3320 0.4076 0.3132 -0.0090 0.0403  0.0023  169 LEU B CB    
4178 C CG    . LEU B 169 ? 0.4196 0.4928 0.4011 -0.0080 0.0401  0.0021  169 LEU B CG    
4179 C CD1   . LEU B 169 ? 0.4916 0.5562 0.4731 -0.0088 0.0404  -0.0018 169 LEU B CD1   
4180 C CD2   . LEU B 169 ? 0.3552 0.4380 0.3360 -0.0104 0.0399  0.0021  169 LEU B CD2   
4181 N N     . PRO B 170 ? 0.4272 0.5059 0.4086 -0.0086 0.0404  0.0061  170 PRO B N     
4182 C CA    . PRO B 170 ? 0.5000 0.5824 0.4816 -0.0074 0.0402  0.0100  170 PRO B CA    
4183 C C     . PRO B 170 ? 0.4947 0.5687 0.4766 -0.0054 0.0401  0.0116  170 PRO B C     
4184 O O     . PRO B 170 ? 0.5962 0.6702 0.5781 -0.0031 0.0399  0.0156  170 PRO B O     
4185 C CB    . PRO B 170 ? 0.4414 0.5307 0.4223 -0.0107 0.0405  0.0082  170 PRO B CB    
4186 C CG    . PRO B 170 ? 0.4680 0.5546 0.4481 -0.0132 0.0410  0.0030  170 PRO B CG    
4187 C CD    . PRO B 170 ? 0.4135 0.4971 0.3938 -0.0123 0.0408  0.0024  170 PRO B CD    
4188 N N     . LEU B 171 ? 0.4402 0.5074 0.4225 -0.0061 0.0403  0.0086  171 LEU B N     
4189 C CA    . LEU B 171 ? 0.4644 0.5233 0.4469 -0.0046 0.0401  0.0098  171 LEU B CA    
4190 C C     . LEU B 171 ? 0.5187 0.5708 0.5010 -0.0018 0.0398  0.0114  171 LEU B C     
4191 O O     . LEU B 171 ? 0.5615 0.6092 0.5432 0.0002  0.0396  0.0145  171 LEU B O     
4192 C CB    . LEU B 171 ? 0.4704 0.5249 0.4533 -0.0062 0.0405  0.0061  171 LEU B CB    
4193 C CG    . LEU B 171 ? 0.4288 0.4871 0.4116 -0.0082 0.0408  0.0055  171 LEU B CG    
4194 C CD1   . LEU B 171 ? 0.2829 0.3356 0.2661 -0.0088 0.0411  0.0027  171 LEU B CD1   
4195 C CD2   . LEU B 171 ? 0.4754 0.5356 0.4581 -0.0075 0.0403  0.0099  171 LEU B CD2   
4196 N N     . LYS B 172 ? 0.4928 0.5434 0.4753 -0.0016 0.0399  0.0090  172 LYS B N     
4197 C CA    . LYS B 172 ? 0.3601 0.4046 0.3425 0.0011  0.0397  0.0099  172 LYS B CA    
4198 C C     . LYS B 172 ? 0.4419 0.4885 0.4235 0.0041  0.0396  0.0144  172 LYS B C     
4199 O O     . LYS B 172 ? 0.3954 0.4351 0.3762 0.0069  0.0395  0.0163  172 LYS B O     
4200 C CB    . LYS B 172 ? 0.3250 0.3706 0.3079 0.0003  0.0399  0.0069  172 LYS B CB    
4201 C CG    . LYS B 172 ? 0.3995 0.4379 0.3824 0.0025  0.0398  0.0066  172 LYS B CG    
4202 C CD    . LYS B 172 ? 0.4027 0.4417 0.3861 0.0009  0.0400  0.0031  172 LYS B CD    
4203 C CE    . LYS B 172 ? 0.4548 0.5002 0.4381 0.0016  0.0398  0.0044  172 LYS B CE    
4204 N NZ    . LYS B 172 ? 0.4707 0.5175 0.4541 -0.0008 0.0400  0.0011  172 LYS B NZ    
4205 N N     . ALA B 173 ? 0.5570 0.6129 0.5386 0.0036  0.0397  0.0162  173 ALA B N     
4206 C CA    . ALA B 173 ? 0.5371 0.5959 0.5180 0.0067  0.0397  0.0207  173 ALA B CA    
4207 C C     . ALA B 173 ? 0.4996 0.5536 0.4794 0.0084  0.0396  0.0241  173 ALA B C     
4208 O O     . ALA B 173 ? 0.5287 0.5802 0.5073 0.0120  0.0398  0.0277  173 ALA B O     
4209 C CB    . ALA B 173 ? 0.4843 0.5554 0.4655 0.0054  0.0397  0.0217  173 ALA B CB    
4210 N N     . GLN B 174 ? 0.4927 0.5453 0.4726 0.0060  0.0395  0.0233  174 GLN B N     
4211 C CA    . GLN B 174 ? 0.5189 0.5670 0.4976 0.0071  0.0394  0.0267  174 GLN B CA    
4212 C C     . GLN B 174 ? 0.5094 0.5456 0.4867 0.0092  0.0393  0.0272  174 GLN B C     
4213 O O     . GLN B 174 ? 0.5029 0.5340 0.4783 0.0104  0.0392  0.0303  174 GLN B O     
4214 C CB    . GLN B 174 ? 0.3687 0.4190 0.3480 0.0039  0.0392  0.0259  174 GLN B CB    
4215 C CG    . GLN B 174 ? 0.4091 0.4707 0.3889 0.0025  0.0393  0.0271  174 GLN B CG    
4216 C CD    . GLN B 174 ? 0.4718 0.5377 0.4526 -0.0012 0.0394  0.0240  174 GLN B CD    
4217 O OE1   . GLN B 174 ? 0.5233 0.5859 0.5041 -0.0025 0.0392  0.0240  174 GLN B OE1   
4218 N NE2   . GLN B 174 ? 0.5017 0.5753 0.4832 -0.0030 0.0396  0.0213  174 GLN B NE2   
4219 N N     . SER B 175 ? 0.4970 0.5284 0.4746 0.0095  0.0392  0.0242  175 SER B N     
4220 C CA    . SER B 175 ? 0.4189 0.4390 0.3952 0.0104  0.0391  0.0237  175 SER B CA    
4221 C C     . SER B 175 ? 0.4547 0.4691 0.4287 0.0146  0.0393  0.0266  175 SER B C     
4222 O O     . SER B 175 ? 0.4331 0.4512 0.4074 0.0170  0.0396  0.0270  175 SER B O     
4223 C CB    . SER B 175 ? 0.3749 0.3924 0.3525 0.0090  0.0390  0.0194  175 SER B CB    
4224 O OG    . SER B 175 ? 0.4494 0.4568 0.4257 0.0100  0.0388  0.0192  175 SER B OG    
4225 N N     . GLU B 176 ? 0.6917 0.6972 0.6633 0.0155  0.0392  0.0286  176 GLU B N     
4226 C CA    . GLU B 176 ? 0.7952 0.7921 0.7638 0.0193  0.0395  0.0304  176 GLU B CA    
4227 C C     . GLU B 176 ? 0.7712 0.7613 0.7398 0.0194  0.0393  0.0271  176 GLU B C     
4228 O O     . GLU B 176 ? 0.7576 0.7438 0.7247 0.0229  0.0397  0.0277  176 GLU B O     
4229 C CB    . GLU B 176 ? 0.8853 0.8740 0.8505 0.0198  0.0394  0.0336  176 GLU B CB    
4230 C CG    . GLU B 176 ? 0.9453 0.9365 0.9087 0.0231  0.0400  0.0383  176 GLU B CG    
4231 C CD    . GLU B 176 ? 1.0112 1.0121 0.9764 0.0208  0.0399  0.0399  176 GLU B CD    
4232 O OE1   . GLU B 176 ? 1.0243 1.0236 0.9896 0.0173  0.0394  0.0396  176 GLU B OE1   
4233 O OE2   . GLU B 176 ? 1.0303 1.0410 0.9969 0.0223  0.0403  0.0414  176 GLU B OE2   
4234 N N     . ARG B 177 ? 0.7162 0.7047 0.6863 0.0160  0.0389  0.0239  177 ARG B N     
4235 C CA    . ARG B 177 ? 0.6746 0.6565 0.6446 0.0161  0.0387  0.0211  177 ARG B CA    
4236 C C     . ARG B 177 ? 0.6533 0.6401 0.6256 0.0168  0.0389  0.0186  177 ARG B C     
4237 O O     . ARG B 177 ? 0.6751 0.6579 0.6465 0.0192  0.0391  0.0182  177 ARG B O     
4238 C CB    . ARG B 177 ? 0.6693 0.6481 0.6401 0.0123  0.0381  0.0189  177 ARG B CB    
4239 C CG    . ARG B 177 ? 0.7262 0.6994 0.6973 0.0119  0.0379  0.0158  177 ARG B CG    
4240 C CD    . ARG B 177 ? 0.8248 0.7876 0.7928 0.0115  0.0375  0.0165  177 ARG B CD    
4241 N NE    . ARG B 177 ? 0.9132 0.8754 0.8809 0.0081  0.0370  0.0171  177 ARG B NE    
4242 C CZ    . ARG B 177 ? 0.8813 0.8358 0.8467 0.0063  0.0365  0.0173  177 ARG B CZ    
4243 N NH1   . ARG B 177 ? 0.8109 0.7571 0.7740 0.0076  0.0364  0.0166  177 ARG B NH1   
4244 N NH2   . ARG B 177 ? 0.8333 0.7886 0.7986 0.0030  0.0360  0.0182  177 ARG B NH2   
4245 N N     . TYR B 178 ? 0.5732 0.5686 0.5482 0.0145  0.0389  0.0169  178 TYR B N     
4246 C CA    . TYR B 178 ? 0.5616 0.5613 0.5386 0.0144  0.0391  0.0143  178 TYR B CA    
4247 C C     . TYR B 178 ? 0.6180 0.6193 0.5943 0.0180  0.0394  0.0159  178 TYR B C     
4248 O O     . TYR B 178 ? 0.5560 0.5559 0.5329 0.0185  0.0394  0.0139  178 TYR B O     
4249 C CB    . TYR B 178 ? 0.5072 0.5164 0.4864 0.0115  0.0392  0.0127  178 TYR B CB    
4250 C CG    . TYR B 178 ? 0.4645 0.4747 0.4453 0.0100  0.0392  0.0090  178 TYR B CG    
4251 C CD1   . TYR B 178 ? 0.4898 0.4948 0.4713 0.0084  0.0391  0.0063  178 TYR B CD1   
4252 C CD2   . TYR B 178 ? 0.4187 0.4350 0.4003 0.0102  0.0394  0.0084  178 TYR B CD2   
4253 C CE1   . TYR B 178 ? 0.5258 0.5311 0.5085 0.0073  0.0393  0.0031  178 TYR B CE1   
4254 C CE2   . TYR B 178 ? 0.4311 0.4476 0.4138 0.0087  0.0395  0.0051  178 TYR B CE2   
4255 C CZ    . TYR B 178 ? 0.4834 0.4940 0.4666 0.0074  0.0395  0.0025  178 TYR B CZ    
4256 O OH    . TYR B 178 ? 0.5965 0.6069 0.5807 0.0061  0.0397  -0.0005 178 TYR B OH    
4257 N N     . PRO B 179 ? 0.4802 0.4846 0.4552 0.0206  0.0397  0.0194  179 PRO B N     
4258 C CA    . PRO B 179 ? 0.4362 0.4429 0.4105 0.0243  0.0401  0.0210  179 PRO B CA    
4259 C C     . PRO B 179 ? 0.4650 0.4619 0.4372 0.0274  0.0402  0.0210  179 PRO B C     
4260 O O     . PRO B 179 ? 0.4621 0.4607 0.4341 0.0302  0.0406  0.0214  179 PRO B O     
4261 C CB    . PRO B 179 ? 0.3434 0.3552 0.3166 0.0266  0.0405  0.0253  179 PRO B CB    
4262 C CG    . PRO B 179 ? 0.3148 0.3307 0.2891 0.0229  0.0401  0.0250  179 PRO B CG    
4263 C CD    . PRO B 179 ? 0.3695 0.3773 0.3438 0.0202  0.0397  0.0223  179 PRO B CD    
4264 N N     . LYS B 180 ? 0.6041 0.5912 0.5745 0.0267  0.0400  0.0205  180 LYS B N     
4265 C CA    . LYS B 180 ? 0.5844 0.5615 0.5526 0.0286  0.0401  0.0197  180 LYS B CA    
4266 C C     . LYS B 180 ? 0.5215 0.4973 0.4918 0.0262  0.0397  0.0158  180 LYS B C     
4267 O O     . LYS B 180 ? 0.5646 0.5319 0.5332 0.0267  0.0395  0.0147  180 LYS B O     
4268 C CB    . LYS B 180 ? 0.6119 0.5790 0.5767 0.0284  0.0399  0.0211  180 LYS B CB    
4269 C CG    . LYS B 180 ? 0.6662 0.6332 0.6284 0.0310  0.0404  0.0252  180 LYS B CG    
4270 C CD    . LYS B 180 ? 0.6705 0.6254 0.6284 0.0314  0.0404  0.0266  180 LYS B CD    
4271 C CE    . LYS B 180 ? 0.6127 0.5649 0.5669 0.0357  0.0413  0.0309  180 LYS B CE    
4272 N NZ    . LYS B 180 ? 0.5445 0.5011 0.4987 0.0406  0.0421  0.0321  180 LYS B NZ    
4273 N N     . LYS B 181 ? 0.4444 0.4281 0.4178 0.0238  0.0395  0.0138  181 LYS B N     
4274 C CA    . LYS B 181 ? 0.3928 0.3760 0.3683 0.0220  0.0393  0.0103  181 LYS B CA    
4275 C C     . LYS B 181 ? 0.4081 0.3905 0.3830 0.0250  0.0395  0.0103  181 LYS B C     
4276 O O     . LYS B 181 ? 0.5446 0.5315 0.5190 0.0277  0.0399  0.0125  181 LYS B O     
4277 C CB    . LYS B 181 ? 0.2714 0.2630 0.2496 0.0189  0.0393  0.0084  181 LYS B CB    
4278 C CG    . LYS B 181 ? 0.2986 0.2885 0.2786 0.0157  0.0391  0.0050  181 LYS B CG    
4279 C CD    . LYS B 181 ? 0.3157 0.3131 0.2977 0.0135  0.0393  0.0030  181 LYS B CD    
4280 C CE    . LYS B 181 ? 0.3115 0.3065 0.2948 0.0123  0.0393  -0.0001 181 LYS B CE    
4281 N NZ    . LYS B 181 ? 0.2694 0.2690 0.2541 0.0091  0.0395  -0.0025 181 LYS B NZ    
4282 N N     . ASP B 182 ? 0.6317 0.6094 0.6071 0.0245  0.0394  0.0079  182 ASP B N     
4283 C CA    . ASP B 182 ? 0.5749 0.5517 0.5498 0.0273  0.0396  0.0078  182 ASP B CA    
4284 C C     . ASP B 182 ? 0.4909 0.4689 0.4682 0.0252  0.0394  0.0047  182 ASP B C     
4285 O O     . ASP B 182 ? 0.6035 0.5756 0.5804 0.0256  0.0392  0.0033  182 ASP B O     
4286 C CB    . ASP B 182 ? 0.6738 0.6414 0.6452 0.0305  0.0397  0.0090  182 ASP B CB    
4287 C CG    . ASP B 182 ? 0.7954 0.7544 0.7655 0.0284  0.0393  0.0078  182 ASP B CG    
4288 O OD1   . ASP B 182 ? 0.7961 0.7547 0.7660 0.0261  0.0391  0.0083  182 ASP B OD1   
4289 O OD2   . ASP B 182 ? 0.8377 0.7904 0.8066 0.0289  0.0392  0.0064  182 ASP B OD2   
4290 N N     . ARG B 183 ? 0.4964 0.4820 0.4761 0.0230  0.0394  0.0037  183 ARG B N     
4291 C CA    . ARG B 183 ? 0.4738 0.4605 0.4555 0.0211  0.0393  0.0010  183 ARG B CA    
4292 C C     . ARG B 183 ? 0.4047 0.3974 0.3868 0.0228  0.0394  0.0020  183 ARG B C     
4293 O O     . ARG B 183 ? 0.5123 0.5123 0.4946 0.0226  0.0395  0.0034  183 ARG B O     
4294 C CB    . ARG B 183 ? 0.4823 0.4728 0.4658 0.0172  0.0393  -0.0010 183 ARG B CB    
4295 C CG    . ARG B 183 ? 0.4967 0.4891 0.4819 0.0153  0.0393  -0.0035 183 ARG B CG    
4296 C CD    . ARG B 183 ? 0.4173 0.4118 0.4034 0.0117  0.0395  -0.0056 183 ARG B CD    
4297 N NE    . ARG B 183 ? 0.5076 0.5031 0.4948 0.0098  0.0397  -0.0080 183 ARG B NE    
4298 C CZ    . ARG B 183 ? 0.4896 0.4838 0.4774 0.0074  0.0401  -0.0105 183 ARG B CZ    
4299 N NH1   . ARG B 183 ? 0.4794 0.4719 0.4671 0.0065  0.0402  -0.0109 183 ARG B NH1   
4300 N NH2   . ARG B 183 ? 0.4336 0.4280 0.4219 0.0059  0.0403  -0.0124 183 ARG B NH2   
4301 N N     . SER B 184 ? 0.3365 0.3267 0.3186 0.0244  0.0394  0.0013  184 SER B N     
4302 C CA    . SER B 184 ? 0.3855 0.3818 0.3680 0.0260  0.0395  0.0024  184 SER B CA    
4303 C C     . SER B 184 ? 0.3534 0.3573 0.3378 0.0224  0.0394  0.0012  184 SER B C     
4304 O O     . SER B 184 ? 0.3404 0.3428 0.3260 0.0190  0.0393  -0.0014 184 SER B O     
4305 C CB    . SER B 184 ? 0.3979 0.3898 0.3802 0.0279  0.0395  0.0016  184 SER B CB    
4306 O OG    . SER B 184 ? 0.4239 0.4226 0.4068 0.0291  0.0396  0.0026  184 SER B OG    
4307 N N     . ARG B 185 ? 0.4512 0.4635 0.4357 0.0232  0.0394  0.0033  185 ARG B N     
4308 C CA    . ARG B 185 ? 0.5300 0.5501 0.5158 0.0194  0.0392  0.0023  185 ARG B CA    
4309 C C     . ARG B 185 ? 0.5150 0.5356 0.5018 0.0181  0.0391  0.0008  185 ARG B C     
4310 O O     . ARG B 185 ? 0.5380 0.5634 0.5255 0.0144  0.0389  -0.0005 185 ARG B O     
4311 C CB    . ARG B 185 ? 0.5454 0.5751 0.5308 0.0203  0.0392  0.0053  185 ARG B CB    
4312 C CG    . ARG B 185 ? 0.6099 0.6406 0.5945 0.0205  0.0394  0.0068  185 ARG B CG    
4313 C CD    . ARG B 185 ? 0.6641 0.7029 0.6481 0.0236  0.0396  0.0107  185 ARG B CD    
4314 N NE    . ARG B 185 ? 0.6180 0.6624 0.6019 0.0216  0.0395  0.0116  185 ARG B NE    
4315 C CZ    . ARG B 185 ? 0.5099 0.5652 0.4943 0.0196  0.0393  0.0128  185 ARG B CZ    
4316 N NH1   . ARG B 185 ? 0.5312 0.5932 0.5162 0.0193  0.0392  0.0133  185 ARG B NH1   
4317 N NH2   . ARG B 185 ? 0.4904 0.5504 0.4747 0.0178  0.0393  0.0135  185 ARG B NH2   
4318 N N     . GLU B 186 ? 0.6063 0.6218 0.5929 0.0209  0.0391  0.0008  186 GLU B N     
4319 C CA    . GLU B 186 ? 0.5337 0.5489 0.5214 0.0198  0.0390  -0.0007 186 GLU B CA    
4320 C C     . GLU B 186 ? 0.5683 0.5807 0.5569 0.0153  0.0389  -0.0039 186 GLU B C     
4321 O O     . GLU B 186 ? 0.6192 0.6254 0.6076 0.0147  0.0391  -0.0054 186 GLU B O     
4322 C CB    . GLU B 186 ? 0.4935 0.5015 0.4807 0.0232  0.0391  -0.0008 186 GLU B CB    
4323 C CG    . GLU B 186 ? 0.6484 0.6587 0.6344 0.0277  0.0392  0.0017  186 GLU B CG    
4324 C CD    . GLU B 186 ? 0.8306 0.8342 0.8163 0.0300  0.0393  0.0009  186 GLU B CD    
4325 O OE1   . GLU B 186 ? 0.9151 0.9204 0.9021 0.0287  0.0391  -0.0002 186 GLU B OE1   
4326 O OE2   . GLU B 186 ? 0.7898 0.7864 0.7736 0.0328  0.0395  0.0011  186 GLU B OE2   
4327 N N     . GLU B 187 ? 0.6191 0.6356 0.6083 0.0124  0.0388  -0.0048 187 GLU B N     
4328 C CA    . GLU B 187 ? 0.7436 0.7558 0.7333 0.0089  0.0390  -0.0078 187 GLU B CA    
4329 C C     . GLU B 187 ? 0.7943 0.8012 0.7847 0.0106  0.0390  -0.0085 187 GLU B C     
4330 O O     . GLU B 187 ? 0.7408 0.7509 0.7315 0.0113  0.0388  -0.0075 187 GLU B O     
4331 C CB    . GLU B 187 ? 0.7661 0.7841 0.7555 0.0047  0.0389  -0.0086 187 GLU B CB    
4332 C CG    . GLU B 187 ? 0.8261 0.8389 0.8153 0.0011  0.0393  -0.0118 187 GLU B CG    
4333 C CD    . GLU B 187 ? 0.9148 0.9208 0.9041 0.0022  0.0397  -0.0131 187 GLU B CD    
4334 O OE1   . GLU B 187 ? 1.0064 1.0141 0.9951 0.0022  0.0397  -0.0126 187 GLU B OE1   
4335 O OE2   . GLU B 187 ? 0.8530 0.8525 0.8428 0.0030  0.0400  -0.0144 187 GLU B OE2   
4336 N N     . LEU B 188 ? 0.7286 0.7279 0.7193 0.0113  0.0392  -0.0100 188 LEU B N     
4337 C CA    . LEU B 188 ? 0.5828 0.5770 0.5741 0.0125  0.0393  -0.0108 188 LEU B CA    
4338 C C     . LEU B 188 ? 0.6237 0.6144 0.6157 0.0096  0.0396  -0.0132 188 LEU B C     
4339 O O     . LEU B 188 ? 0.6552 0.6425 0.6479 0.0104  0.0397  -0.0138 188 LEU B O     
4340 C CB    . LEU B 188 ? 0.6057 0.5941 0.5965 0.0154  0.0393  -0.0104 188 LEU B CB    
4341 C CG    . LEU B 188 ? 0.7004 0.6910 0.6900 0.0187  0.0391  -0.0079 188 LEU B CG    
4342 C CD1   . LEU B 188 ? 0.7421 0.7258 0.7305 0.0214  0.0391  -0.0077 188 LEU B CD1   
4343 C CD2   . LEU B 188 ? 0.6733 0.6693 0.6630 0.0202  0.0389  -0.0064 188 LEU B CD2   
4344 N N     . GLY B 189 ? 0.5666 0.5580 0.5581 0.0065  0.0400  -0.0146 189 GLY B N     
4345 C CA    . GLY B 189 ? 0.4774 0.4648 0.4690 0.0041  0.0405  -0.0170 189 GLY B CA    
4346 C C     . GLY B 189 ? 0.4461 0.4272 0.4382 0.0053  0.0410  -0.0181 189 GLY B C     
4347 O O     . GLY B 189 ? 0.3775 0.3574 0.3697 0.0067  0.0409  -0.0176 189 GLY B O     
4348 N N     . ASN B 190 ? 0.5715 0.5490 0.5640 0.0043  0.0415  -0.0196 190 ASN B N     
4349 C CA    . ASN B 190 ? 0.5817 0.5541 0.5748 0.0052  0.0421  -0.0206 190 ASN B CA    
4350 C C     . ASN B 190 ? 0.5774 0.5471 0.5716 0.0068  0.0420  -0.0203 190 ASN B C     
4351 O O     . ASN B 190 ? 0.5657 0.5362 0.5601 0.0062  0.0420  -0.0202 190 ASN B O     
4352 C CB    . ASN B 190 ? 0.6245 0.5947 0.6166 0.0029  0.0431  -0.0227 190 ASN B CB    
4353 C CG    . ASN B 190 ? 0.6695 0.6431 0.6600 0.0005  0.0431  -0.0232 190 ASN B CG    
4354 O OD1   . ASN B 190 ? 0.6844 0.6595 0.6747 0.0008  0.0430  -0.0229 190 ASN B OD1   
4355 N ND2   . ASN B 190 ? 0.7375 0.7123 0.7268 -0.0021 0.0433  -0.0240 190 ASN B ND2   
4356 N N     . THR B 191 ? 0.5608 0.5277 0.5557 0.0087  0.0419  -0.0201 191 THR B N     
4357 C CA    . THR B 191 ? 0.5563 0.5208 0.5523 0.0102  0.0419  -0.0199 191 THR B CA    
4358 C C     . THR B 191 ? 0.5492 0.5101 0.5458 0.0100  0.0427  -0.0210 191 THR B C     
4359 O O     . THR B 191 ? 0.4916 0.4521 0.4878 0.0095  0.0431  -0.0216 191 THR B O     
4360 C CB    . THR B 191 ? 0.6181 0.5824 0.6140 0.0126  0.0411  -0.0185 191 THR B CB    
4361 O OG1   . THR B 191 ? 0.6562 0.6191 0.6530 0.0138  0.0409  -0.0183 191 THR B OG1   
4362 C CG2   . THR B 191 ? 0.6990 0.6612 0.6945 0.0131  0.0410  -0.0184 191 THR B CG2   
4363 N N     . PRO B 192 ? 0.6324 0.5913 0.6299 0.0106  0.0431  -0.0212 192 PRO B N     
4364 C CA    . PRO B 192 ? 0.5903 0.5465 0.5884 0.0109  0.0440  -0.0219 192 PRO B CA    
4365 C C     . PRO B 192 ? 0.5520 0.5078 0.5507 0.0123  0.0436  -0.0213 192 PRO B C     
4366 O O     . PRO B 192 ? 0.5243 0.4804 0.5230 0.0132  0.0427  -0.0204 192 PRO B O     
4367 C CB    . PRO B 192 ? 0.5150 0.4696 0.5138 0.0113  0.0444  -0.0219 192 PRO B CB    
4368 C CG    . PRO B 192 ? 0.4351 0.3914 0.4332 0.0100  0.0441  -0.0218 192 PRO B CG    
4369 C CD    . PRO B 192 ? 0.5095 0.4689 0.5073 0.0104  0.0430  -0.0209 192 PRO B CD    
4370 N N     . SER B 193 ? 0.3783 0.3332 0.3771 0.0122  0.0443  -0.0218 193 SER B N     
4371 C CA    . SER B 193 ? 0.3709 0.3260 0.3702 0.0129  0.0440  -0.0211 193 SER B CA    
4372 C C     . SER B 193 ? 0.3368 0.2916 0.3369 0.0133  0.0450  -0.0214 193 SER B C     
4373 O O     . SER B 193 ? 0.4184 0.3727 0.4181 0.0131  0.0462  -0.0223 193 SER B O     
4374 C CB    . SER B 193 ? 0.4136 0.3699 0.4119 0.0121  0.0434  -0.0208 193 SER B CB    
4375 O OG    . SER B 193 ? 0.4769 0.4334 0.4754 0.0122  0.0431  -0.0202 193 SER B OG    
4376 N N     . ALA B 194 ? 0.3513 0.3065 0.3522 0.0141  0.0447  -0.0206 194 ALA B N     
4377 C CA    . ALA B 194 ? 0.3854 0.3416 0.3872 0.0147  0.0457  -0.0204 194 ALA B CA    
4378 C C     . ALA B 194 ? 0.3691 0.3273 0.3708 0.0140  0.0450  -0.0196 194 ALA B C     
4379 O O     . ALA B 194 ? 0.3700 0.3301 0.3725 0.0144  0.0455  -0.0191 194 ALA B O     
4380 C CB    . ALA B 194 ? 0.4040 0.3601 0.4071 0.0159  0.0458  -0.0197 194 ALA B CB    
4381 N N     . ASN B 195 ? 0.4144 0.3723 0.4150 0.0130  0.0439  -0.0194 195 ASN B N     
4382 C CA    . ASN B 195 ? 0.4606 0.4197 0.4606 0.0119  0.0432  -0.0186 195 ASN B CA    
4383 C C     . ASN B 195 ? 0.4213 0.3819 0.4207 0.0111  0.0436  -0.0189 195 ASN B C     
4384 O O     . ASN B 195 ? 0.4161 0.3762 0.4149 0.0110  0.0439  -0.0197 195 ASN B O     
4385 C CB    . ASN B 195 ? 0.4655 0.4228 0.4642 0.0114  0.0417  -0.0179 195 ASN B CB    
4386 C CG    . ASN B 195 ? 0.4485 0.4051 0.4476 0.0118  0.0412  -0.0175 195 ASN B CG    
4387 O OD1   . ASN B 195 ? 0.4282 0.3866 0.4286 0.0120  0.0417  -0.0172 195 ASN B OD1   
4388 N ND2   . ASN B 195 ? 0.4048 0.3589 0.4025 0.0120  0.0403  -0.0173 195 ASN B ND2   
4389 N N     . PRO B 196 ? 0.4503 0.4132 0.4498 0.0105  0.0436  -0.0182 196 PRO B N     
4390 C CA    . PRO B 196 ? 0.4320 0.3969 0.4310 0.0097  0.0440  -0.0183 196 PRO B CA    
4391 C C     . PRO B 196 ? 0.3813 0.3461 0.3789 0.0083  0.0429  -0.0176 196 PRO B C     
4392 O O     . PRO B 196 ? 0.4249 0.3880 0.4217 0.0077  0.0418  -0.0167 196 PRO B O     
4393 C CB    . PRO B 196 ? 0.3898 0.3580 0.3897 0.0098  0.0446  -0.0176 196 PRO B CB    
4394 C CG    . PRO B 196 ? 0.4097 0.3777 0.4100 0.0094  0.0436  -0.0165 196 PRO B CG    
4395 C CD    . PRO B 196 ? 0.4067 0.3714 0.4071 0.0104  0.0435  -0.0172 196 PRO B CD    
4396 N N     . GLY B 197 ? 0.4158 0.3822 0.4129 0.0078  0.0434  -0.0180 197 GLY B N     
4397 C CA    . GLY B 197 ? 0.4347 0.4015 0.4306 0.0065  0.0425  -0.0171 197 GLY B CA    
4398 C C     . GLY B 197 ? 0.4386 0.4029 0.4332 0.0065  0.0415  -0.0166 197 GLY B C     
4399 O O     . GLY B 197 ? 0.3877 0.3513 0.3822 0.0073  0.0417  -0.0174 197 GLY B O     
4400 N N     . ILE B 198 ? 0.4559 0.4189 0.4492 0.0056  0.0405  -0.0151 198 ILE B N     
4401 C CA    . ILE B 198 ? 0.4457 0.4058 0.4375 0.0062  0.0397  -0.0145 198 ILE B CA    
4402 C C     . ILE B 198 ? 0.4089 0.3653 0.4001 0.0070  0.0391  -0.0144 198 ILE B C     
4403 O O     . ILE B 198 ? 0.4002 0.3534 0.3895 0.0075  0.0384  -0.0137 198 ILE B O     
4404 C CB    . ILE B 198 ? 0.4388 0.3986 0.4287 0.0052  0.0391  -0.0130 198 ILE B CB    
4405 C CG1   . ILE B 198 ? 0.3452 0.3038 0.3344 0.0035  0.0384  -0.0119 198 ILE B CG1   
4406 C CG2   . ILE B 198 ? 0.4290 0.3930 0.4196 0.0046  0.0397  -0.0131 198 ILE B CG2   
4407 C CD1   . ILE B 198 ? 0.3658 0.3209 0.3522 0.0028  0.0375  -0.0103 198 ILE B CD1   
4408 N N     . MET B 199 ? 0.3653 0.3221 0.3578 0.0071  0.0394  -0.0151 199 MET B N     
4409 C CA    . MET B 199 ? 0.3824 0.3362 0.3745 0.0078  0.0390  -0.0152 199 MET B CA    
4410 C C     . MET B 199 ? 0.3487 0.3017 0.3411 0.0096  0.0392  -0.0159 199 MET B C     
4411 O O     . MET B 199 ? 0.4020 0.3572 0.3955 0.0100  0.0399  -0.0166 199 MET B O     
4412 C CB    . MET B 199 ? 0.3545 0.3100 0.3484 0.0077  0.0394  -0.0156 199 MET B CB    
4413 C CG    . MET B 199 ? 0.4035 0.3608 0.3973 0.0059  0.0390  -0.0147 199 MET B CG    
4414 S SD    . MET B 199 ? 0.3591 0.3191 0.3550 0.0062  0.0395  -0.0147 199 MET B SD    
4415 C CE    . MET B 199 ? 0.3517 0.3075 0.3459 0.0061  0.0384  -0.0147 199 MET B CE    
4416 N N     . LYS B 200 ? 0.2896 0.2397 0.2808 0.0105  0.0386  -0.0157 200 LYS B N     
4417 C CA    . LYS B 200 ? 0.3344 0.2847 0.3259 0.0122  0.0389  -0.0161 200 LYS B CA    
4418 C C     . LYS B 200 ? 0.4274 0.3788 0.4210 0.0127  0.0394  -0.0170 200 LYS B C     
4419 O O     . LYS B 200 ? 0.4127 0.3636 0.4069 0.0123  0.0393  -0.0170 200 LYS B O     
4420 C CB    . LYS B 200 ? 0.3188 0.2659 0.3081 0.0136  0.0382  -0.0154 200 LYS B CB    
4421 C CG    . LYS B 200 ? 0.3498 0.2954 0.3367 0.0136  0.0379  -0.0143 200 LYS B CG    
4422 C CD    . LYS B 200 ? 0.3378 0.2780 0.3215 0.0141  0.0372  -0.0137 200 LYS B CD    
4423 C CE    . LYS B 200 ? 0.3513 0.2897 0.3336 0.0167  0.0372  -0.0136 200 LYS B CE    
4424 N NZ    . LYS B 200 ? 0.3354 0.2679 0.3143 0.0171  0.0366  -0.0134 200 LYS B NZ    
4425 N N     . PRO B 201 ? 0.4534 0.4062 0.4480 0.0134  0.0399  -0.0175 201 PRO B N     
4426 C CA    . PRO B 201 ? 0.4574 0.4108 0.4537 0.0138  0.0405  -0.0183 201 PRO B CA    
4427 C C     . PRO B 201 ? 0.4970 0.4489 0.4934 0.0147  0.0401  -0.0180 201 PRO B C     
4428 O O     . PRO B 201 ? 0.5600 0.5123 0.5577 0.0146  0.0404  -0.0182 201 PRO B O     
4429 C CB    . PRO B 201 ? 0.4339 0.3887 0.4303 0.0141  0.0408  -0.0186 201 PRO B CB    
4430 C CG    . PRO B 201 ? 0.3574 0.3134 0.3526 0.0136  0.0406  -0.0182 201 PRO B CG    
4431 C CD    . PRO B 201 ? 0.3504 0.3046 0.3443 0.0137  0.0399  -0.0173 201 PRO B CD    
4432 N N     . ASN B 202 ? 0.4994 0.4495 0.4941 0.0157  0.0393  -0.0175 202 ASN B N     
4433 C CA    . ASN B 202 ? 0.4591 0.4077 0.4535 0.0165  0.0389  -0.0175 202 ASN B CA    
4434 C C     . ASN B 202 ? 0.4149 0.3612 0.4077 0.0156  0.0383  -0.0172 202 ASN B C     
4435 O O     . ASN B 202 ? 0.4334 0.3781 0.4252 0.0161  0.0378  -0.0173 202 ASN B O     
4436 C CB    . ASN B 202 ? 0.4129 0.3609 0.4059 0.0183  0.0386  -0.0172 202 ASN B CB    
4437 C CG    . ASN B 202 ? 0.4529 0.4041 0.4475 0.0188  0.0391  -0.0172 202 ASN B CG    
4438 O OD1   . ASN B 202 ? 0.4072 0.3600 0.4037 0.0179  0.0397  -0.0177 202 ASN B OD1   
4439 N ND2   . ASN B 202 ? 0.5071 0.4590 0.5005 0.0201  0.0389  -0.0166 202 ASN B ND2   
4440 N N     . SER B 203 ? 0.4564 0.4028 0.4488 0.0141  0.0382  -0.0170 203 SER B N     
4441 C CA    . SER B 203 ? 0.4258 0.3703 0.4165 0.0127  0.0375  -0.0166 203 SER B CA    
4442 C C     . SER B 203 ? 0.4471 0.3941 0.4397 0.0116  0.0378  -0.0166 203 SER B C     
4443 O O     . SER B 203 ? 0.4442 0.3944 0.4393 0.0118  0.0386  -0.0168 203 SER B O     
4444 C CB    . SER B 203 ? 0.4331 0.3765 0.4222 0.0113  0.0372  -0.0160 203 SER B CB    
4445 O OG    . SER B 203 ? 0.4076 0.3474 0.3939 0.0124  0.0368  -0.0157 203 SER B OG    
4446 N N     . PRO B 204 ? 0.5381 0.4838 0.5293 0.0106  0.0371  -0.0164 204 PRO B N     
4447 C CA    . PRO B 204 ? 0.5419 0.4911 0.5350 0.0096  0.0372  -0.0161 204 PRO B CA    
4448 C C     . PRO B 204 ? 0.5560 0.5086 0.5504 0.0082  0.0376  -0.0155 204 PRO B C     
4449 O O     . PRO B 204 ? 0.5671 0.5186 0.5602 0.0072  0.0374  -0.0153 204 PRO B O     
4450 C CB    . PRO B 204 ? 0.4830 0.4297 0.4733 0.0081  0.0361  -0.0160 204 PRO B CB    
4451 C CG    . PRO B 204 ? 0.4661 0.4072 0.4529 0.0085  0.0356  -0.0164 204 PRO B CG    
4452 C CD    . PRO B 204 ? 0.4341 0.3754 0.4221 0.0109  0.0362  -0.0166 204 PRO B CD    
4453 N N     . ASN B 205 ? 0.5456 0.5024 0.5424 0.0083  0.0382  -0.0151 205 ASN B N     
4454 C CA    . ASN B 205 ? 0.5627 0.5234 0.5607 0.0075  0.0388  -0.0144 205 ASN B CA    
4455 C C     . ASN B 205 ? 0.5767 0.5423 0.5767 0.0074  0.0392  -0.0135 205 ASN B C     
4456 O O     . ASN B 205 ? 0.5127 0.4788 0.5136 0.0085  0.0393  -0.0135 205 ASN B O     
4457 C CB    . ASN B 205 ? 0.5487 0.5099 0.5482 0.0092  0.0400  -0.0151 205 ASN B CB    
4458 C CG    . ASN B 205 ? 0.5378 0.5021 0.5379 0.0084  0.0405  -0.0146 205 ASN B CG    
4459 O OD1   . ASN B 205 ? 0.6933 0.6592 0.6925 0.0064  0.0398  -0.0137 205 ASN B OD1   
4460 N ND2   . ASN B 205 ? 0.4506 0.4158 0.4518 0.0099  0.0418  -0.0152 205 ASN B ND2   
4461 N N     . PHE B 206 ? 0.4499 0.4195 0.4505 0.0063  0.0394  -0.0126 206 PHE B N     
4462 C CA    . PHE B 206 ? 0.4411 0.4166 0.4437 0.0067  0.0401  -0.0114 206 PHE B CA    
4463 C C     . PHE B 206 ? 0.4803 0.4570 0.4854 0.0099  0.0418  -0.0117 206 PHE B C     
4464 O O     . PHE B 206 ? 0.4563 0.4303 0.4614 0.0112  0.0426  -0.0128 206 PHE B O     
4465 C CB    . PHE B 206 ? 0.3645 0.3447 0.3671 0.0047  0.0399  -0.0101 206 PHE B CB    
4466 C CG    . PHE B 206 ? 0.3710 0.3495 0.3709 0.0011  0.0382  -0.0096 206 PHE B CG    
4467 C CD1   . PHE B 206 ? 0.3789 0.3553 0.3769 -0.0007 0.0370  -0.0097 206 PHE B CD1   
4468 C CD2   . PHE B 206 ? 0.4091 0.3876 0.4077 -0.0007 0.0379  -0.0092 206 PHE B CD2   
4469 C CE1   . PHE B 206 ? 0.4190 0.3927 0.4137 -0.0042 0.0355  -0.0094 206 PHE B CE1   
4470 C CE2   . PHE B 206 ? 0.4500 0.4262 0.4457 -0.0042 0.0363  -0.0087 206 PHE B CE2   
4471 C CZ    . PHE B 206 ? 0.3390 0.3123 0.3325 -0.0060 0.0352  -0.0089 206 PHE B CZ    
4472 N N     . THR B 207 ? 0.5874 0.5681 0.5943 0.0112  0.0425  -0.0107 207 THR B N     
4473 C CA    . THR B 207 ? 0.6479 0.6289 0.6565 0.0144  0.0443  -0.0108 207 THR B CA    
4474 C C     . THR B 207 ? 0.6628 0.6469 0.6722 0.0157  0.0458  -0.0104 207 THR B C     
4475 O O     . THR B 207 ? 0.6779 0.6601 0.6877 0.0181  0.0473  -0.0112 207 THR B O     
4476 C CB    . THR B 207 ? 0.6078 0.5919 0.6180 0.0156  0.0446  -0.0097 207 THR B CB    
4477 O OG1   . THR B 207 ? 0.5402 0.5219 0.5494 0.0141  0.0431  -0.0101 207 THR B OG1   
4478 C CG2   . THR B 207 ? 0.6390 0.6214 0.6505 0.0189  0.0464  -0.0099 207 THR B CG2   
4479 N N     . ASP B 208 ? 0.6605 0.6495 0.6699 0.0141  0.0454  -0.0092 208 ASP B N     
4480 C CA    . ASP B 208 ? 0.6570 0.6489 0.6668 0.0153  0.0467  -0.0089 208 ASP B CA    
4481 C C     . ASP B 208 ? 0.5844 0.5716 0.5927 0.0147  0.0467  -0.0107 208 ASP B C     
4482 O O     . ASP B 208 ? 0.7193 0.7071 0.7276 0.0163  0.0481  -0.0111 208 ASP B O     
4483 C CB    . ASP B 208 ? 0.7150 0.7140 0.7251 0.0134  0.0462  -0.0070 208 ASP B CB    
4484 C CG    . ASP B 208 ? 0.8097 0.8082 0.8182 0.0093  0.0439  -0.0066 208 ASP B CG    
4485 O OD1   . ASP B 208 ? 0.8757 0.8680 0.8827 0.0081  0.0428  -0.0080 208 ASP B OD1   
4486 O OD2   . ASP B 208 ? 0.8395 0.8438 0.8481 0.0071  0.0432  -0.0049 208 ASP B OD2   
4487 N N     . ASN B 209 ? 0.3015 0.2841 0.3084 0.0128  0.0452  -0.0116 209 ASN B N     
4488 C CA    . ASN B 209 ? 0.3976 0.3768 0.4030 0.0117  0.0448  -0.0128 209 ASN B CA    
4489 C C     . ASN B 209 ? 0.4256 0.3996 0.4305 0.0131  0.0453  -0.0145 209 ASN B C     
4490 O O     . ASN B 209 ? 0.4719 0.4434 0.4755 0.0122  0.0449  -0.0154 209 ASN B O     
4491 C CB    . ASN B 209 ? 0.4378 0.4153 0.4414 0.0087  0.0429  -0.0124 209 ASN B CB    
4492 C CG    . ASN B 209 ? 0.4606 0.4391 0.4631 0.0070  0.0425  -0.0121 209 ASN B CG    
4493 O OD1   . ASN B 209 ? 0.4804 0.4636 0.4836 0.0071  0.0432  -0.0114 209 ASN B OD1   
4494 N ND2   . ASN B 209 ? 0.4123 0.3866 0.4129 0.0056  0.0414  -0.0126 209 ASN B ND2   
4495 N N     . LEU B 210 ? 0.4718 0.4446 0.4776 0.0151  0.0462  -0.0148 210 LEU B N     
4496 C CA    . LEU B 210 ? 0.4065 0.3749 0.4118 0.0160  0.0468  -0.0163 210 LEU B CA    
4497 C C     . LEU B 210 ? 0.3649 0.3329 0.3697 0.0170  0.0483  -0.0173 210 LEU B C     
4498 O O     . LEU B 210 ? 0.3982 0.3694 0.4034 0.0178  0.0493  -0.0168 210 LEU B O     
4499 C CB    . LEU B 210 ? 0.2784 0.2454 0.2847 0.0174  0.0471  -0.0162 210 LEU B CB    
4500 C CG    . LEU B 210 ? 0.3696 0.3367 0.3760 0.0165  0.0456  -0.0155 210 LEU B CG    
4501 C CD1   . LEU B 210 ? 0.4492 0.4151 0.4567 0.0181  0.0461  -0.0154 210 LEU B CD1   
4502 C CD2   . LEU B 210 ? 0.4161 0.3802 0.4209 0.0148  0.0442  -0.0162 210 LEU B CD2   
4503 N N     . VAL B 211 ? 0.2836 0.2479 0.2873 0.0169  0.0486  -0.0188 211 VAL B N     
4504 C CA    . VAL B 211 ? 0.2768 0.2400 0.2795 0.0174  0.0500  -0.0200 211 VAL B CA    
4505 C C     . VAL B 211 ? 0.2880 0.2470 0.2901 0.0181  0.0508  -0.0211 211 VAL B C     
4506 O O     . VAL B 211 ? 0.3116 0.2692 0.3142 0.0179  0.0499  -0.0208 211 VAL B O     
4507 C CB    . VAL B 211 ? 0.2496 0.2131 0.2509 0.0156  0.0493  -0.0208 211 VAL B CB    
4508 C CG1   . VAL B 211 ? 0.2745 0.2420 0.2761 0.0148  0.0488  -0.0197 211 VAL B CG1   
4509 C CG2   . VAL B 211 ? 0.2486 0.2100 0.2493 0.0141  0.0479  -0.0211 211 VAL B CG2   
4510 N N     . PRO B 212 ? 0.3839 0.3409 0.3847 0.0190  0.0524  -0.0223 212 PRO B N     
4511 C CA    . PRO B 212 ? 0.4397 0.3921 0.4394 0.0190  0.0531  -0.0234 212 PRO B CA    
4512 C C     . PRO B 212 ? 0.4910 0.4422 0.4902 0.0168  0.0516  -0.0240 212 PRO B C     
4513 O O     . PRO B 212 ? 0.5222 0.4744 0.5204 0.0153  0.0510  -0.0246 212 PRO B O     
4514 C CB    . PRO B 212 ? 0.3539 0.3040 0.3514 0.0198  0.0550  -0.0249 212 PRO B CB    
4515 C CG    . PRO B 212 ? 0.3569 0.3104 0.3553 0.0218  0.0559  -0.0238 212 PRO B CG    
4516 C CD    . PRO B 212 ? 0.3547 0.3130 0.3548 0.0204  0.0540  -0.0226 212 PRO B CD    
4517 N N     . VAL B 213 ? 0.4626 0.4121 0.4623 0.0168  0.0512  -0.0237 213 VAL B N     
4518 C CA    . VAL B 213 ? 0.5666 0.5159 0.5659 0.0150  0.0498  -0.0239 213 VAL B CA    
4519 C C     . VAL B 213 ? 0.5935 0.5415 0.5907 0.0132  0.0501  -0.0254 213 VAL B C     
4520 O O     . VAL B 213 ? 0.5725 0.5174 0.5682 0.0129  0.0513  -0.0265 213 VAL B O     
4521 C CB    . VAL B 213 ? 0.5691 0.5170 0.5693 0.0155  0.0495  -0.0232 213 VAL B CB    
4522 C CG1   . VAL B 213 ? 0.4889 0.4374 0.4887 0.0140  0.0482  -0.0232 213 VAL B CG1   
4523 C CG2   . VAL B 213 ? 0.5821 0.5320 0.5843 0.0170  0.0490  -0.0218 213 VAL B CG2   
4524 N N     . ARG B 214 ? 0.5707 0.5210 0.5676 0.0118  0.0488  -0.0253 214 ARG B N     
4525 C CA    . ARG B 214 ? 0.5761 0.5265 0.5712 0.0098  0.0489  -0.0264 214 ARG B CA    
4526 C C     . ARG B 214 ? 0.5390 0.4919 0.5342 0.0087  0.0474  -0.0257 214 ARG B C     
4527 O O     . ARG B 214 ? 0.4917 0.4460 0.4882 0.0097  0.0463  -0.0244 214 ARG B O     
4528 C CB    . ARG B 214 ? 0.5506 0.5020 0.5446 0.0096  0.0495  -0.0272 214 ARG B CB    
4529 C CG    . ARG B 214 ? 0.5062 0.4613 0.5011 0.0094  0.0484  -0.0261 214 ARG B CG    
4530 C CD    . ARG B 214 ? 0.4654 0.4213 0.4616 0.0110  0.0485  -0.0252 214 ARG B CD    
4531 N NE    . ARG B 214 ? 0.5388 0.4977 0.5353 0.0105  0.0475  -0.0242 214 ARG B NE    
4532 C CZ    . ARG B 214 ? 0.5444 0.5040 0.5418 0.0107  0.0463  -0.0228 214 ARG B CZ    
4533 N NH1   . ARG B 214 ? 0.5921 0.5503 0.5905 0.0115  0.0459  -0.0223 214 ARG B NH1   
4534 N NH2   . ARG B 214 ? 0.5291 0.4906 0.5263 0.0100  0.0455  -0.0219 214 ARG B NH2   
4535 N N     . ASP B 215 ? 0.6566 0.6104 0.6502 0.0068  0.0473  -0.0265 215 ASP B N     
4536 C CA    . ASP B 215 ? 0.6116 0.5686 0.6053 0.0060  0.0460  -0.0255 215 ASP B CA    
4537 C C     . ASP B 215 ? 0.5158 0.4757 0.5095 0.0061  0.0454  -0.0249 215 ASP B C     
4538 O O     . ASP B 215 ? 0.5716 0.5318 0.5644 0.0054  0.0460  -0.0257 215 ASP B O     
4539 C CB    . ASP B 215 ? 0.6638 0.6216 0.6560 0.0037  0.0461  -0.0263 215 ASP B CB    
4540 C CG    . ASP B 215 ? 0.6663 0.6232 0.6590 0.0036  0.0458  -0.0257 215 ASP B CG    
4541 O OD1   . ASP B 215 ? 0.6224 0.5788 0.6168 0.0056  0.0454  -0.0246 215 ASP B OD1   
4542 O OD2   . ASP B 215 ? 0.7193 0.6759 0.7105 0.0014  0.0460  -0.0264 215 ASP B OD2   
4543 N N     . VAL B 216 ? 0.4484 0.4098 0.4429 0.0071  0.0443  -0.0234 216 VAL B N     
4544 C CA    . VAL B 216 ? 0.5282 0.4915 0.5224 0.0073  0.0436  -0.0225 216 VAL B CA    
4545 C C     . VAL B 216 ? 0.5607 0.5271 0.5543 0.0073  0.0427  -0.0213 216 VAL B C     
4546 O O     . VAL B 216 ? 0.6175 0.5842 0.6114 0.0080  0.0422  -0.0205 216 VAL B O     
4547 C CB    . VAL B 216 ? 0.5518 0.5137 0.5468 0.0088  0.0432  -0.0215 216 VAL B CB    
4548 C CG1   . VAL B 216 ? 0.4421 0.4024 0.4377 0.0090  0.0442  -0.0224 216 VAL B CG1   
4549 C CG2   . VAL B 216 ? 0.5051 0.4659 0.5006 0.0102  0.0424  -0.0204 216 VAL B CG2   
4550 N N     . PRO B 217 ? 0.4429 0.4121 0.4357 0.0065  0.0425  -0.0208 217 PRO B N     
4551 C CA    . PRO B 217 ? 0.4139 0.3866 0.4061 0.0068  0.0418  -0.0194 217 PRO B CA    
4552 C C     . PRO B 217 ? 0.4570 0.4289 0.4493 0.0091  0.0410  -0.0176 217 PRO B C     
4553 O O     . PRO B 217 ? 0.5682 0.5374 0.5605 0.0100  0.0408  -0.0172 217 PRO B O     
4554 C CB    . PRO B 217 ? 0.4264 0.4022 0.4178 0.0055  0.0419  -0.0194 217 PRO B CB    
4555 C CG    . PRO B 217 ? 0.3819 0.3560 0.3731 0.0041  0.0428  -0.0213 217 PRO B CG    
4556 C CD    . PRO B 217 ? 0.4018 0.3717 0.3941 0.0054  0.0431  -0.0216 217 PRO B CD    
4557 N N     . LYS B 218 ? 0.4439 0.4182 0.4360 0.0101  0.0406  -0.0164 218 LYS B N     
4558 C CA    . LYS B 218 ? 0.4176 0.3909 0.4091 0.0127  0.0400  -0.0147 218 LYS B CA    
4559 C C     . LYS B 218 ? 0.4202 0.3971 0.4105 0.0133  0.0397  -0.0130 218 LYS B C     
4560 O O     . LYS B 218 ? 0.4225 0.4046 0.4128 0.0126  0.0397  -0.0124 218 LYS B O     
4561 C CB    . LYS B 218 ? 0.4528 0.4267 0.4446 0.0141  0.0398  -0.0142 218 LYS B CB    
4562 C CG    . LYS B 218 ? 0.4402 0.4096 0.4328 0.0149  0.0398  -0.0150 218 LYS B CG    
4563 C CD    . LYS B 218 ? 0.3918 0.3605 0.3836 0.0177  0.0394  -0.0138 218 LYS B CD    
4564 C CE    . LYS B 218 ? 0.3288 0.3018 0.3211 0.0179  0.0393  -0.0132 218 LYS B CE    
4565 N NZ    . LYS B 218 ? 0.3723 0.3450 0.3661 0.0162  0.0396  -0.0145 218 LYS B NZ    
4566 N N     . ILE B 219 ? 0.2797 0.2540 0.2690 0.0145  0.0395  -0.0119 219 ILE B N     
4567 C CA    . ILE B 219 ? 0.3201 0.2973 0.3082 0.0155  0.0394  -0.0100 219 ILE B CA    
4568 C C     . ILE B 219 ? 0.3109 0.2845 0.2974 0.0187  0.0391  -0.0083 219 ILE B C     
4569 O O     . ILE B 219 ? 0.2933 0.2612 0.2792 0.0193  0.0389  -0.0088 219 ILE B O     
4570 C CB    . ILE B 219 ? 0.3513 0.3284 0.3392 0.0139  0.0394  -0.0101 219 ILE B CB    
4571 C CG1   . ILE B 219 ? 0.3590 0.3394 0.3480 0.0109  0.0399  -0.0119 219 ILE B CG1   
4572 C CG2   . ILE B 219 ? 0.3722 0.3523 0.3587 0.0150  0.0393  -0.0078 219 ILE B CG2   
4573 C CD1   . ILE B 219 ? 0.3275 0.3046 0.3172 0.0095  0.0402  -0.0138 219 ILE B CD1   
4574 N N     . ALA B 220 ? 0.3022 0.2794 0.2877 0.0209  0.0391  -0.0064 220 ALA B N     
4575 C CA    . ALA B 220 ? 0.3921 0.3659 0.3754 0.0246  0.0391  -0.0046 220 ALA B CA    
4576 C C     . ALA B 220 ? 0.4091 0.3817 0.3905 0.0256  0.0391  -0.0026 220 ALA B C     
4577 O O     . ALA B 220 ? 0.3906 0.3681 0.3726 0.0244  0.0392  -0.0019 220 ALA B O     
4578 C CB    . ALA B 220 ? 0.4972 0.4760 0.4805 0.0270  0.0392  -0.0032 220 ALA B CB    
4579 N N     . ILE B 221 ? 0.4479 0.4135 0.4266 0.0279  0.0391  -0.0018 221 ILE B N     
4580 C CA    . ILE B 221 ? 0.4233 0.3866 0.3995 0.0293  0.0392  0.0003  221 ILE B CA    
4581 C C     . ILE B 221 ? 0.5211 0.4883 0.4960 0.0331  0.0397  0.0029  221 ILE B C     
4582 O O     . ILE B 221 ? 0.5510 0.5181 0.5253 0.0358  0.0399  0.0031  221 ILE B O     
4583 C CB    . ILE B 221 ? 0.3184 0.2720 0.2916 0.0300  0.0391  0.0003  221 ILE B CB    
4584 C CG1   . ILE B 221 ? 0.4127 0.3633 0.3872 0.0263  0.0386  -0.0018 221 ILE B CG1   
4585 C CG2   . ILE B 221 ? 0.3505 0.3012 0.3207 0.0317  0.0393  0.0027  221 ILE B CG2   
4586 C CD1   . ILE B 221 ? 0.3937 0.3351 0.3650 0.0263  0.0383  -0.0019 221 ILE B CD1   
4587 N N     . ASN B 222 ? 0.6764 0.6474 0.6509 0.0335  0.0399  0.0050  222 ASN B N     
4588 C CA    . ASN B 222 ? 0.6225 0.5972 0.5954 0.0376  0.0404  0.0080  222 ASN B CA    
4589 C C     . ASN B 222 ? 0.6439 0.6096 0.6127 0.0406  0.0408  0.0096  222 ASN B C     
4590 O O     . ASN B 222 ? 0.7389 0.7016 0.7066 0.0393  0.0407  0.0103  222 ASN B O     
4591 C CB    . ASN B 222 ? 0.6017 0.5857 0.5761 0.0364  0.0404  0.0096  222 ASN B CB    
4592 C CG    . ASN B 222 ? 0.5956 0.5852 0.5687 0.0407  0.0411  0.0130  222 ASN B CG    
4593 O OD1   . ASN B 222 ? 0.6360 0.6233 0.6073 0.0448  0.0415  0.0141  222 ASN B OD1   
4594 N ND2   . ASN B 222 ? 0.6078 0.6051 0.5819 0.0400  0.0411  0.0148  222 ASN B ND2   
4595 N N     . GLU B 223 ? 0.5885 0.5494 0.5547 0.0444  0.0412  0.0100  223 GLU B N     
4596 C CA    . GLU B 223 ? 0.5948 0.5455 0.5562 0.0471  0.0416  0.0112  223 GLU B CA    
4597 C C     . GLU B 223 ? 0.6063 0.5586 0.5652 0.0516  0.0425  0.0149  223 GLU B C     
4598 O O     . GLU B 223 ? 0.5409 0.4850 0.4957 0.0532  0.0429  0.0163  223 GLU B O     
4599 C CB    . GLU B 223 ? 0.6035 0.5471 0.5626 0.0492  0.0418  0.0097  223 GLU B CB    
4600 C CG    . GLU B 223 ? 0.6687 0.6145 0.6312 0.0459  0.0411  0.0067  223 GLU B CG    
4601 C CD    . GLU B 223 ? 0.7549 0.6955 0.7154 0.0483  0.0413  0.0055  223 GLU B CD    
4602 O OE1   . GLU B 223 ? 0.6908 0.6282 0.6476 0.0531  0.0421  0.0071  223 GLU B OE1   
4603 O OE2   . GLU B 223 ? 0.7756 0.7153 0.7381 0.0455  0.0407  0.0030  223 GLU B OE2   
4604 N N     . LYS B 224 ? 0.6966 0.6595 0.6576 0.0533  0.0428  0.0166  224 LYS B N     
4605 C CA    . LYS B 224 ? 0.6914 0.6579 0.6505 0.0579  0.0437  0.0204  224 LYS B CA    
4606 C C     . LYS B 224 ? 0.8321 0.7999 0.7911 0.0563  0.0437  0.0222  224 LYS B C     
4607 O O     . LYS B 224 ? 0.9435 0.9131 0.9004 0.0602  0.0445  0.0257  224 LYS B O     
4608 C CB    . LYS B 224 ? 0.6111 0.5901 0.5729 0.0594  0.0439  0.0216  224 LYS B CB    
4609 C CG    . LYS B 224 ? 0.5614 0.5401 0.5226 0.0625  0.0443  0.0210  224 LYS B CG    
4610 C CD    . LYS B 224 ? 0.5825 0.5750 0.5469 0.0630  0.0443  0.0223  224 LYS B CD    
4611 C CE    . LYS B 224 ? 0.5714 0.5711 0.5403 0.0566  0.0432  0.0202  224 LYS B CE    
4612 N NZ    . LYS B 224 ? 0.5907 0.6028 0.5625 0.0558  0.0430  0.0208  224 LYS B NZ    
4613 N N     . VAL B 225 ? 0.7086 0.6759 0.6698 0.0509  0.0428  0.0202  225 VAL B N     
4614 C CA    . VAL B 225 ? 0.5741 0.5428 0.5353 0.0491  0.0427  0.0217  225 VAL B CA    
4615 C C     . VAL B 225 ? 0.5593 0.5165 0.5157 0.0511  0.0431  0.0233  225 VAL B C     
4616 O O     . VAL B 225 ? 0.6245 0.5716 0.5788 0.0500  0.0428  0.0214  225 VAL B O     
4617 C CB    . VAL B 225 ? 0.5193 0.4905 0.4841 0.0430  0.0417  0.0188  225 VAL B CB    
4618 C CG1   . VAL B 225 ? 0.5361 0.5109 0.5013 0.0410  0.0416  0.0206  225 VAL B CG1   
4619 C CG2   . VAL B 225 ? 0.4223 0.4026 0.3910 0.0409  0.0413  0.0168  225 VAL B CG2   
4620 N N     . ALA B 226 ? 0.5531 0.5119 0.5076 0.0539  0.0438  0.0270  226 ALA B N     
4621 C CA    . ALA B 226 ? 0.5793 0.5271 0.5290 0.0553  0.0442  0.0288  226 ALA B CA    
4622 C C     . ALA B 226 ? 0.6029 0.5483 0.5537 0.0498  0.0432  0.0276  226 ALA B C     
4623 O O     . ALA B 226 ? 0.6754 0.6299 0.6300 0.0465  0.0427  0.0274  226 ALA B O     
4624 C CB    . ALA B 226 ? 0.5818 0.5326 0.5294 0.0601  0.0453  0.0334  226 ALA B CB    
4625 N N     . GLY B 227 ? 0.5209 0.4541 0.4680 0.0486  0.0430  0.0268  227 GLY B N     
4626 C CA    . GLY B 227 ? 0.5552 0.4857 0.5030 0.0433  0.0421  0.0257  227 GLY B CA    
4627 C C     . GLY B 227 ? 0.5345 0.4711 0.4872 0.0385  0.0411  0.0221  227 GLY B C     
4628 O O     . GLY B 227 ? 0.5394 0.4780 0.4939 0.0343  0.0405  0.0215  227 GLY B O     
4629 N N     . GLY B 228 ? 0.4330 0.3724 0.3878 0.0392  0.0411  0.0199  228 GLY B N     
4630 C CA    . GLY B 228 ? 0.3436 0.2889 0.3029 0.0353  0.0404  0.0167  228 GLY B CA    
4631 C C     . GLY B 228 ? 0.3852 0.3250 0.3445 0.0309  0.0396  0.0145  228 GLY B C     
4632 O O     . GLY B 228 ? 0.4156 0.3454 0.3711 0.0309  0.0395  0.0147  228 GLY B O     
4633 N N     . TYR B 229 ? 0.4135 0.3595 0.3766 0.0271  0.0391  0.0127  229 TYR B N     
4634 C CA    . TYR B 229 ? 0.4811 0.4235 0.4446 0.0230  0.0384  0.0111  229 TYR B CA    
4635 C C     . TYR B 229 ? 0.5627 0.4978 0.5249 0.0222  0.0381  0.0090  229 TYR B C     
4636 O O     . TYR B 229 ? 0.5953 0.5243 0.5556 0.0198  0.0376  0.0089  229 TYR B O     
4637 C CB    . TYR B 229 ? 0.4957 0.4467 0.4634 0.0197  0.0382  0.0096  229 TYR B CB    
4638 C CG    . TYR B 229 ? 0.4733 0.4223 0.4417 0.0157  0.0376  0.0082  229 TYR B CG    
4639 C CD1   . TYR B 229 ? 0.4203 0.3682 0.3875 0.0137  0.0373  0.0099  229 TYR B CD1   
4640 C CD2   . TYR B 229 ? 0.4506 0.3993 0.4209 0.0141  0.0374  0.0054  229 TYR B CD2   
4641 C CE1   . TYR B 229 ? 0.5846 0.5315 0.5524 0.0101  0.0368  0.0089  229 TYR B CE1   
4642 C CE2   . TYR B 229 ? 0.5188 0.4664 0.4898 0.0108  0.0369  0.0044  229 TYR B CE2   
4643 C CZ    . TYR B 229 ? 0.6491 0.5961 0.6188 0.0087  0.0366  0.0061  229 TYR B CZ    
4644 O OH    . TYR B 229 ? 0.6868 0.6337 0.6573 0.0054  0.0362  0.0053  229 TYR B OH    
4645 N N     . SER B 230 ? 0.6727 0.6089 0.6361 0.0239  0.0383  0.0074  230 SER B N     
4646 C CA    . SER B 230 ? 0.6432 0.5727 0.6053 0.0234  0.0380  0.0054  230 SER B CA    
4647 C C     . SER B 230 ? 0.6074 0.5266 0.5640 0.0256  0.0382  0.0067  230 SER B C     
4648 O O     . SER B 230 ? 0.5443 0.4566 0.4988 0.0242  0.0378  0.0053  230 SER B O     
4649 C CB    . SER B 230 ? 0.6180 0.5513 0.5825 0.0249  0.0382  0.0036  230 SER B CB    
4650 O OG    . SER B 230 ? 0.7211 0.6504 0.6827 0.0290  0.0387  0.0044  230 SER B OG    
4651 N N     . LYS B 231 ? 0.5938 0.5119 0.5478 0.0291  0.0388  0.0094  231 LYS B N     
4652 C CA    . LYS B 231 ? 0.5656 0.4732 0.5137 0.0316  0.0392  0.0109  231 LYS B CA    
4653 C C     . LYS B 231 ? 0.5591 0.4610 0.5044 0.0287  0.0388  0.0124  231 LYS B C     
4654 O O     . LYS B 231 ? 0.6356 0.5267 0.5758 0.0285  0.0387  0.0125  231 LYS B O     
4655 C CB    . LYS B 231 ? 0.5362 0.4456 0.4827 0.0370  0.0403  0.0134  231 LYS B CB    
4656 C CG    . LYS B 231 ? 0.4395 0.3568 0.3893 0.0396  0.0406  0.0126  231 LYS B CG    
4657 C CD    . LYS B 231 ? 0.4894 0.4069 0.4365 0.0455  0.0418  0.0154  231 LYS B CD    
4658 C CE    . LYS B 231 ? 0.4809 0.4091 0.4318 0.0474  0.0420  0.0153  231 LYS B CE    
4659 N NZ    . LYS B 231 ? 0.5975 0.5328 0.5537 0.0425  0.0411  0.0128  231 LYS B NZ    
4660 N N     . THR B 232 ? 0.4486 0.3572 0.3967 0.0265  0.0386  0.0135  232 THR B N     
4661 C CA    . THR B 232 ? 0.4813 0.3856 0.4271 0.0234  0.0381  0.0151  232 THR B CA    
4662 C C     . THR B 232 ? 0.4988 0.4012 0.4454 0.0183  0.0371  0.0130  232 THR B C     
4663 O O     . THR B 232 ? 0.5348 0.4286 0.4772 0.0161  0.0367  0.0135  232 THR B O     
4664 C CB    . THR B 232 ? 0.4431 0.3562 0.3917 0.0229  0.0382  0.0171  232 THR B CB    
4665 O OG1   . THR B 232 ? 0.4892 0.4131 0.4436 0.0213  0.0380  0.0152  232 THR B OG1   
4666 C CG2   . THR B 232 ? 0.3742 0.2880 0.3209 0.0279  0.0392  0.0201  232 THR B CG2   
4667 N N     . LYS B 233 ? 0.4053 0.3157 0.3569 0.0163  0.0368  0.0107  233 LYS B N     
4668 C CA    . LYS B 233 ? 0.3637 0.2742 0.3167 0.0119  0.0359  0.0088  233 LYS B CA    
4669 C C     . LYS B 233 ? 0.3796 0.2906 0.3345 0.0124  0.0359  0.0060  233 LYS B C     
4670 O O     . LYS B 233 ? 0.4062 0.3249 0.3656 0.0118  0.0359  0.0044  233 LYS B O     
4671 C CB    . LYS B 233 ? 0.4041 0.3240 0.3616 0.0091  0.0357  0.0088  233 LYS B CB    
4672 C CG    . LYS B 233 ? 0.4714 0.3911 0.4294 0.0044  0.0349  0.0080  233 LYS B CG    
4673 C CD    . LYS B 233 ? 0.5344 0.4620 0.4953 0.0021  0.0348  0.0090  233 LYS B CD    
4674 C CE    . LYS B 233 ? 0.4583 0.3856 0.4189 -0.0024 0.0340  0.0090  233 LYS B CE    
4675 N NZ    . LYS B 233 ? 0.4250 0.3587 0.3873 -0.0046 0.0339  0.0105  233 LYS B NZ    
4676 N N     . PRO B 234 ? 0.5976 0.5002 0.5486 0.0136  0.0359  0.0054  234 PRO B N     
4677 C CA    . PRO B 234 ? 0.5498 0.4521 0.5019 0.0143  0.0358  0.0029  234 PRO B CA    
4678 C C     . PRO B 234 ? 0.6675 0.5720 0.6220 0.0102  0.0351  0.0011  234 PRO B C     
4679 O O     . PRO B 234 ? 0.7699 0.6773 0.7269 0.0107  0.0351  -0.0008 234 PRO B O     
4680 C CB    . PRO B 234 ? 0.5671 0.4589 0.5134 0.0166  0.0361  0.0032  234 PRO B CB    
4681 C CG    . PRO B 234 ? 0.6750 0.5597 0.6167 0.0147  0.0358  0.0052  234 PRO B CG    
4682 C CD    . PRO B 234 ? 0.6924 0.5842 0.6371 0.0142  0.0359  0.0071  234 PRO B CD    
4683 N N     . THR B 235 ? 0.4177 0.3211 0.3712 0.0064  0.0345  0.0019  235 THR B N     
4684 C CA    . THR B 235 ? 0.4219 0.3284 0.3777 0.0025  0.0338  0.0006  235 THR B CA    
4685 C C     . THR B 235 ? 0.4276 0.3442 0.3893 0.0026  0.0341  -0.0006 235 THR B C     
4686 O O     . THR B 235 ? 0.4065 0.3262 0.3706 0.0011  0.0339  -0.0021 235 THR B O     
4687 C CB    . THR B 235 ? 0.4627 0.3673 0.4164 -0.0015 0.0331  0.0022  235 THR B CB    
4688 O OG1   . THR B 235 ? 0.4251 0.3336 0.3799 -0.0010 0.0334  0.0041  235 THR B OG1   
4689 C CG2   . THR B 235 ? 0.3218 0.2151 0.2690 -0.0024 0.0327  0.0030  235 THR B CG2   
4690 N N     . THR B 236 ? 0.6102 0.5320 0.5739 0.0043  0.0347  0.0002  236 THR B N     
4691 C CA    . THR B 236 ? 0.6012 0.5320 0.5699 0.0043  0.0351  -0.0010 236 THR B CA    
4692 C C     . THR B 236 ? 0.6120 0.5444 0.5827 0.0068  0.0356  -0.0028 236 THR B C     
4693 O O     . THR B 236 ? 0.6227 0.5531 0.5921 0.0098  0.0359  -0.0024 236 THR B O     
4694 C CB    . THR B 236 ? 0.6118 0.5478 0.5817 0.0049  0.0355  0.0004  236 THR B CB    
4695 O OG1   . THR B 236 ? 0.6149 0.5494 0.5829 0.0027  0.0351  0.0024  236 THR B OG1   
4696 C CG2   . THR B 236 ? 0.6066 0.5509 0.5808 0.0044  0.0360  -0.0011 236 THR B CG2   
4697 N N     . PRO B 237 ? 0.5336 0.4695 0.5073 0.0057  0.0357  -0.0046 237 PRO B N     
4698 C CA    . PRO B 237 ? 0.5352 0.4731 0.5110 0.0079  0.0361  -0.0063 237 PRO B CA    
4699 C C     . PRO B 237 ? 0.5754 0.5188 0.5532 0.0096  0.0368  -0.0063 237 PRO B C     
4700 O O     . PRO B 237 ? 0.5808 0.5292 0.5603 0.0084  0.0370  -0.0062 237 PRO B O     
4701 C CB    . PRO B 237 ? 0.4541 0.3948 0.4325 0.0061  0.0362  -0.0078 237 PRO B CB    
4702 C CG    . PRO B 237 ? 0.4966 0.4390 0.4751 0.0032  0.0358  -0.0069 237 PRO B CG    
4703 C CD    . PRO B 237 ? 0.4733 0.4104 0.4479 0.0026  0.0353  -0.0051 237 PRO B CD    
4704 N N     . PHE B 238 ? 0.4952 0.4380 0.4726 0.0122  0.0370  -0.0064 238 PHE B N     
4705 C CA    . PHE B 238 ? 0.4089 0.3574 0.3881 0.0135  0.0375  -0.0064 238 PHE B CA    
4706 C C     . PHE B 238 ? 0.3680 0.3210 0.3503 0.0127  0.0379  -0.0083 238 PHE B C     
4707 O O     . PHE B 238 ? 0.4401 0.3919 0.4232 0.0133  0.0380  -0.0095 238 PHE B O     
4708 C CB    . PHE B 238 ? 0.3988 0.3458 0.3762 0.0168  0.0377  -0.0053 238 PHE B CB    
4709 C CG    . PHE B 238 ? 0.4479 0.4015 0.4268 0.0179  0.0381  -0.0048 238 PHE B CG    
4710 C CD1   . PHE B 238 ? 0.4492 0.4070 0.4303 0.0179  0.0384  -0.0061 238 PHE B CD1   
4711 C CD2   . PHE B 238 ? 0.4950 0.4504 0.4726 0.0188  0.0382  -0.0027 238 PHE B CD2   
4712 C CE1   . PHE B 238 ? 0.4313 0.3953 0.4135 0.0184  0.0387  -0.0056 238 PHE B CE1   
4713 C CE2   . PHE B 238 ? 0.4790 0.4411 0.4578 0.0195  0.0385  -0.0020 238 PHE B CE2   
4714 C CZ    . PHE B 238 ? 0.4389 0.4055 0.4200 0.0192  0.0387  -0.0035 238 PHE B CZ    
4715 N N     . VAL B 239 ? 0.2792 0.2373 0.2632 0.0113  0.0383  -0.0086 239 VAL B N     
4716 C CA    . VAL B 239 ? 0.3252 0.2870 0.3116 0.0106  0.0388  -0.0105 239 VAL B CA    
4717 C C     . VAL B 239 ? 0.3345 0.3013 0.3212 0.0110  0.0391  -0.0102 239 VAL B C     
4718 O O     . VAL B 239 ? 0.3357 0.3041 0.3231 0.0116  0.0393  -0.0109 239 VAL B O     
4719 C CB    . VAL B 239 ? 0.2871 0.2504 0.2749 0.0085  0.0392  -0.0117 239 VAL B CB    
4720 C CG1   . VAL B 239 ? 0.2540 0.2168 0.2434 0.0085  0.0396  -0.0135 239 VAL B CG1   
4721 C CG2   . VAL B 239 ? 0.3997 0.3600 0.3864 0.0076  0.0386  -0.0106 239 VAL B CG2   
4722 N N     . ALA B 240 ? 0.3755 0.3449 0.3616 0.0104  0.0391  -0.0090 240 ALA B N     
4723 C CA    . ALA B 240 ? 0.3229 0.2978 0.3091 0.0106  0.0393  -0.0084 240 ALA B CA    
4724 C C     . ALA B 240 ? 0.3763 0.3527 0.3611 0.0111  0.0391  -0.0060 240 ALA B C     
4725 O O     . ALA B 240 ? 0.4471 0.4291 0.4321 0.0104  0.0393  -0.0056 240 ALA B O     
4726 C CB    . ALA B 240 ? 0.2549 0.2340 0.2425 0.0083  0.0399  -0.0104 240 ALA B CB    
4727 N N     . SER B 241 ? 0.3440 0.3154 0.3269 0.0124  0.0387  -0.0044 241 SER B N     
4728 C CA    . SER B 241 ? 0.3231 0.2946 0.3042 0.0131  0.0386  -0.0018 241 SER B CA    
4729 C C     . SER B 241 ? 0.4007 0.3759 0.3825 0.0107  0.0386  -0.0016 241 SER B C     
4730 O O     . SER B 241 ? 0.5111 0.4866 0.4941 0.0087  0.0387  -0.0033 241 SER B O     
4731 C CB    . SER B 241 ? 0.3279 0.3022 0.3081 0.0157  0.0387  0.0002  241 SER B CB    
4732 O OG    . SER B 241 ? 0.3660 0.3369 0.3436 0.0173  0.0386  0.0029  241 SER B OG    
4733 N N     . LEU B 242 ? 0.4708 0.4494 0.4518 0.0112  0.0386  0.0005  242 LEU B N     
4734 C CA    . LEU B 242 ? 0.4091 0.3911 0.3905 0.0090  0.0387  0.0010  242 LEU B CA    
4735 C C     . LEU B 242 ? 0.4079 0.3963 0.3913 0.0070  0.0391  -0.0013 242 LEU B C     
4736 O O     . LEU B 242 ? 0.2613 0.2537 0.2452 0.0075  0.0393  -0.0019 242 LEU B O     
4737 C CB    . LEU B 242 ? 0.4138 0.3979 0.3936 0.0102  0.0386  0.0041  242 LEU B CB    
4738 C CG    . LEU B 242 ? 0.4832 0.4606 0.4604 0.0111  0.0383  0.0066  242 LEU B CG    
4739 C CD1   . LEU B 242 ? 0.4905 0.4656 0.4679 0.0082  0.0379  0.0060  242 LEU B CD1   
4740 C CD2   . LEU B 242 ? 0.5038 0.4741 0.4792 0.0136  0.0382  0.0068  242 LEU B CD2   
4741 N N     . SER B 243 ? 0.3069 0.2963 0.2911 0.0049  0.0393  -0.0026 243 SER B N     
4742 C CA    . SER B 243 ? 0.3073 0.3019 0.2928 0.0031  0.0398  -0.0049 243 SER B CA    
4743 C C     . SER B 243 ? 0.3016 0.3028 0.2868 0.0021  0.0400  -0.0040 243 SER B C     
4744 O O     . SER B 243 ? 0.2607 0.2629 0.2454 0.0017  0.0398  -0.0022 243 SER B O     
4745 C CB    . SER B 243 ? 0.2887 0.2818 0.2750 0.0017  0.0402  -0.0070 243 SER B CB    
4746 O OG    . SER B 243 ? 0.2814 0.2779 0.2684 0.0006  0.0410  -0.0096 243 SER B OG    
4747 N N     . GLY B 244 ? 0.6173 0.6231 0.6027 0.0016  0.0403  -0.0052 244 GLY B N     
4748 C CA    . GLY B 244 ? 0.5871 0.6001 0.5722 0.0003  0.0405  -0.0046 244 GLY B CA    
4749 C C     . GLY B 244 ? 0.5931 0.6087 0.5783 -0.0020 0.0411  -0.0075 244 GLY B C     
4750 O O     . GLY B 244 ? 0.6978 0.7193 0.6825 -0.0034 0.0413  -0.0075 244 GLY B O     
4751 N N     . THR B 245 ? 0.4752 0.4866 0.4609 -0.0024 0.0416  -0.0099 245 THR B N     
4752 C CA    . THR B 245 ? 0.4188 0.4319 0.4043 -0.0041 0.0424  -0.0126 245 THR B CA    
4753 C C     . THR B 245 ? 0.3672 0.3813 0.3529 -0.0043 0.0424  -0.0114 245 THR B C     
4754 O O     . THR B 245 ? 0.5523 0.5691 0.5376 -0.0054 0.0431  -0.0130 245 THR B O     
4755 C CB    . THR B 245 ? 0.3846 0.3932 0.3703 -0.0040 0.0431  -0.0155 245 THR B CB    
4756 O OG1   . THR B 245 ? 0.5023 0.5060 0.4890 -0.0027 0.0429  -0.0149 245 THR B OG1   
4757 C CG2   . THR B 245 ? 0.4104 0.4179 0.3958 -0.0040 0.0430  -0.0164 245 THR B CG2   
4758 N N     . THR B 246 ? 0.3215 0.3333 0.3075 -0.0032 0.0417  -0.0087 246 THR B N     
4759 C CA    . THR B 246 ? 0.3579 0.3711 0.3440 -0.0039 0.0415  -0.0071 246 THR B CA    
4760 C C     . THR B 246 ? 0.3534 0.3734 0.3388 -0.0049 0.0416  -0.0061 246 THR B C     
4761 O O     . THR B 246 ? 0.3752 0.3985 0.3606 -0.0060 0.0419  -0.0060 246 THR B O     
4762 C CB    . THR B 246 ? 0.4231 0.4319 0.4089 -0.0029 0.0406  -0.0041 246 THR B CB    
4763 O OG1   . THR B 246 ? 0.4664 0.4693 0.4524 -0.0016 0.0404  -0.0047 246 THR B OG1   
4764 C CG2   . THR B 246 ? 0.4276 0.4363 0.4136 -0.0040 0.0405  -0.0032 246 THR B CG2   
4765 N N     . TYR B 247 ? 0.2927 0.3154 0.2777 -0.0045 0.0413  -0.0050 247 TYR B N     
4766 C CA    . TYR B 247 ? 0.4156 0.4455 0.4000 -0.0056 0.0414  -0.0040 247 TYR B CA    
4767 C C     . TYR B 247 ? 0.4801 0.5142 0.4639 -0.0075 0.0422  -0.0073 247 TYR B C     
4768 O O     . TYR B 247 ? 0.4743 0.5140 0.4577 -0.0087 0.0424  -0.0069 247 TYR B O     
4769 C CB    . TYR B 247 ? 0.3702 0.4028 0.3542 -0.0045 0.0409  -0.0018 247 TYR B CB    
4770 C CG    . TYR B 247 ? 0.4631 0.4915 0.4469 -0.0022 0.0402  0.0016  247 TYR B CG    
4771 C CD1   . TYR B 247 ? 0.4542 0.4826 0.4376 -0.0020 0.0399  0.0046  247 TYR B CD1   
4772 C CD2   . TYR B 247 ? 0.5067 0.5309 0.4905 -0.0003 0.0400  0.0018  247 TYR B CD2   
4773 C CE1   . TYR B 247 ? 0.3622 0.3856 0.3448 0.0001  0.0394  0.0076  247 TYR B CE1   
4774 C CE2   . TYR B 247 ? 0.4437 0.4633 0.4267 0.0020  0.0396  0.0047  247 TYR B CE2   
4775 C CZ    . TYR B 247 ? 0.3683 0.3872 0.3506 0.0022  0.0393  0.0075  247 TYR B CZ    
4776 O OH    . TYR B 247 ? 0.4184 0.4316 0.3992 0.0045  0.0390  0.0103  247 TYR B OH    
4777 N N     . SER B 248 ? 0.4845 0.5159 0.4681 -0.0078 0.0428  -0.0104 248 SER B N     
4778 C CA    . SER B 248 ? 0.4210 0.4547 0.4034 -0.0096 0.0438  -0.0137 248 SER B CA    
4779 C C     . SER B 248 ? 0.4738 0.5069 0.4563 -0.0096 0.0445  -0.0148 248 SER B C     
4780 O O     . SER B 248 ? 0.5125 0.5501 0.4939 -0.0108 0.0451  -0.0159 248 SER B O     
4781 C CB    . SER B 248 ? 0.3674 0.3976 0.3492 -0.0100 0.0442  -0.0166 248 SER B CB    
4782 O OG    . SER B 248 ? 0.3730 0.4061 0.3542 -0.0107 0.0437  -0.0160 248 SER B OG    
4783 N N     . LEU B 249 ? 0.4449 0.4731 0.4286 -0.0082 0.0444  -0.0142 249 LEU B N     
4784 C CA    . LEU B 249 ? 0.3854 0.4140 0.3694 -0.0081 0.0450  -0.0146 249 LEU B CA    
4785 C C     . LEU B 249 ? 0.3754 0.4096 0.3595 -0.0089 0.0445  -0.0119 249 LEU B C     
4786 O O     . LEU B 249 ? 0.2763 0.3139 0.2602 -0.0094 0.0451  -0.0124 249 LEU B O     
4787 C CB    . LEU B 249 ? 0.3075 0.3306 0.2929 -0.0068 0.0448  -0.0139 249 LEU B CB    
4788 C CG    . LEU B 249 ? 0.2588 0.2828 0.2450 -0.0067 0.0447  -0.0125 249 LEU B CG    
4789 C CD1   . LEU B 249 ? 0.3938 0.4181 0.3798 -0.0062 0.0462  -0.0152 249 LEU B CD1   
4790 C CD2   . LEU B 249 ? 0.2581 0.2770 0.2454 -0.0060 0.0438  -0.0106 249 LEU B CD2   
4791 N N     . MET B 250 ? 0.4438 0.4786 0.4283 -0.0088 0.0434  -0.0089 250 MET B N     
4792 C CA    . MET B 250 ? 0.3494 0.3893 0.3338 -0.0094 0.0429  -0.0060 250 MET B CA    
4793 C C     . MET B 250 ? 0.4405 0.4876 0.4239 -0.0108 0.0435  -0.0071 250 MET B C     
4794 O O     . MET B 250 ? 0.3979 0.4498 0.3812 -0.0116 0.0436  -0.0059 250 MET B O     
4795 C CB    . MET B 250 ? 0.3600 0.3980 0.3446 -0.0085 0.0419  -0.0026 250 MET B CB    
4796 C CG    . MET B 250 ? 0.4734 0.5052 0.4585 -0.0077 0.0412  -0.0006 250 MET B CG    
4797 S SD    . MET B 250 ? 0.4578 0.4909 0.4433 -0.0089 0.0412  0.0002  250 MET B SD    
4798 C CE    . MET B 250 ? 0.3720 0.4108 0.3570 -0.0099 0.0407  0.0041  250 MET B CE    
4799 N N     . VAL B 251 ? 0.3530 0.4010 0.3354 -0.0113 0.0438  -0.0092 251 VAL B N     
4800 C CA    . VAL B 251 ? 0.4003 0.4548 0.3812 -0.0130 0.0444  -0.0108 251 VAL B CA    
4801 C C     . VAL B 251 ? 0.4319 0.4868 0.4118 -0.0135 0.0457  -0.0140 251 VAL B C     
4802 O O     . VAL B 251 ? 0.3673 0.4278 0.3465 -0.0144 0.0461  -0.0139 251 VAL B O     
4803 C CB    . VAL B 251 ? 0.3645 0.4203 0.3442 -0.0140 0.0444  -0.0124 251 VAL B CB    
4804 C CG1   . VAL B 251 ? 0.2887 0.3507 0.2663 -0.0163 0.0451  -0.0147 251 VAL B CG1   
4805 C CG2   . VAL B 251 ? 0.4451 0.5026 0.4257 -0.0132 0.0433  -0.0087 251 VAL B CG2   
4806 N N     . VAL B 252 ? 0.4011 0.4500 0.3810 -0.0126 0.0464  -0.0165 252 VAL B N     
4807 C CA    . VAL B 252 ? 0.3839 0.4324 0.3626 -0.0124 0.0478  -0.0194 252 VAL B CA    
4808 C C     . VAL B 252 ? 0.5122 0.5636 0.4921 -0.0118 0.0478  -0.0172 252 VAL B C     
4809 O O     . VAL B 252 ? 0.5260 0.5819 0.5048 -0.0122 0.0487  -0.0183 252 VAL B O     
4810 C CB    . VAL B 252 ? 0.2692 0.3102 0.2477 -0.0112 0.0485  -0.0219 252 VAL B CB    
4811 C CG1   . VAL B 252 ? 0.2832 0.3234 0.2604 -0.0103 0.0502  -0.0246 252 VAL B CG1   
4812 C CG2   . VAL B 252 ? 0.2712 0.3097 0.2482 -0.0123 0.0485  -0.0240 252 VAL B CG2   
4813 N N     . LEU B 253 ? 0.5270 0.5760 0.5089 -0.0110 0.0467  -0.0142 253 LEU B N     
4814 C CA    . LEU B 253 ? 0.4780 0.5297 0.4611 -0.0109 0.0465  -0.0119 253 LEU B CA    
4815 C C     . LEU B 253 ? 0.4811 0.5401 0.4639 -0.0122 0.0461  -0.0097 253 LEU B C     
4816 O O     . LEU B 253 ? 0.4466 0.5099 0.4296 -0.0124 0.0465  -0.0090 253 LEU B O     
4817 C CB    . LEU B 253 ? 0.4083 0.4549 0.3931 -0.0103 0.0454  -0.0093 253 LEU B CB    
4818 C CG    . LEU B 253 ? 0.3955 0.4377 0.3811 -0.0091 0.0459  -0.0104 253 LEU B CG    
4819 C CD1   . LEU B 253 ? 0.3663 0.4045 0.3531 -0.0092 0.0445  -0.0074 253 LEU B CD1   
4820 C CD2   . LEU B 253 ? 0.4705 0.5176 0.4561 -0.0090 0.0468  -0.0107 253 LEU B CD2   
4821 N N     . THR B 254 ? 0.5527 0.6135 0.5353 -0.0129 0.0453  -0.0081 254 THR B N     
4822 C CA    . THR B 254 ? 0.5556 0.6237 0.5380 -0.0141 0.0449  -0.0056 254 THR B CA    
4823 C C     . THR B 254 ? 0.5271 0.6011 0.5079 -0.0149 0.0461  -0.0083 254 THR B C     
4824 O O     . THR B 254 ? 0.5307 0.6105 0.5116 -0.0155 0.0462  -0.0068 254 THR B O     
4825 C CB    . THR B 254 ? 0.5259 0.5950 0.5082 -0.0143 0.0439  -0.0031 254 THR B CB    
4826 O OG1   . THR B 254 ? 0.6026 0.6663 0.5861 -0.0132 0.0429  0.0000  254 THR B OG1   
4827 C CG2   . THR B 254 ? 0.3702 0.4477 0.3522 -0.0154 0.0437  -0.0009 254 THR B CG2   
4828 N N     . ASP B 255 ? 0.7095 0.7818 0.6886 -0.0151 0.0471  -0.0123 255 ASP B N     
4829 C CA    . ASP B 255 ? 0.7531 0.8296 0.7300 -0.0158 0.0484  -0.0154 255 ASP B CA    
4830 C C     . ASP B 255 ? 0.7841 0.8607 0.7612 -0.0145 0.0494  -0.0160 255 ASP B C     
4831 O O     . ASP B 255 ? 0.8271 0.9096 0.8031 -0.0149 0.0502  -0.0166 255 ASP B O     
4832 C CB    . ASP B 255 ? 0.7384 0.8113 0.7128 -0.0163 0.0493  -0.0196 255 ASP B CB    
4833 C CG    . ASP B 255 ? 0.8245 0.9022 0.7958 -0.0177 0.0504  -0.0226 255 ASP B CG    
4834 O OD1   . ASP B 255 ? 0.8728 0.9577 0.8437 -0.0193 0.0499  -0.0212 255 ASP B OD1   
4835 O OD2   . ASP B 255 ? 0.8877 0.9618 0.8567 -0.0172 0.0519  -0.0264 255 ASP B OD2   
4836 N N     . TYR B 256 ? 0.5288 0.5997 0.5073 -0.0130 0.0494  -0.0159 256 TYR B N     
4837 C CA    . TYR B 256 ? 0.5393 0.6112 0.5183 -0.0117 0.0503  -0.0159 256 TYR B CA    
4838 C C     . TYR B 256 ? 0.5366 0.6149 0.5173 -0.0124 0.0495  -0.0120 256 TYR B C     
4839 O O     . TYR B 256 ? 0.4059 0.4893 0.3862 -0.0120 0.0504  -0.0123 256 TYR B O     
4840 C CB    . TYR B 256 ? 0.4773 0.5421 0.4577 -0.0101 0.0503  -0.0162 256 TYR B CB    
4841 C CG    . TYR B 256 ? 0.4318 0.4980 0.4127 -0.0085 0.0513  -0.0163 256 TYR B CG    
4842 C CD1   . TYR B 256 ? 0.4401 0.5061 0.4190 -0.0069 0.0533  -0.0197 256 TYR B CD1   
4843 C CD2   . TYR B 256 ? 0.4471 0.5147 0.4303 -0.0087 0.0503  -0.0128 256 TYR B CD2   
4844 C CE1   . TYR B 256 ? 0.4896 0.5576 0.4690 -0.0050 0.0543  -0.0195 256 TYR B CE1   
4845 C CE2   . TYR B 256 ? 0.4629 0.5330 0.4468 -0.0074 0.0511  -0.0125 256 TYR B CE2   
4846 C CZ    . TYR B 256 ? 0.5023 0.5729 0.4844 -0.0054 0.0532  -0.0158 256 TYR B CZ    
4847 O OH    . TYR B 256 ? 0.4817 0.5555 0.4645 -0.0037 0.0541  -0.0152 256 TYR B OH    
4848 N N     . ILE B 257 ? 0.5733 0.6511 0.5555 -0.0134 0.0478  -0.0083 257 ILE B N     
4849 C CA    . ILE B 257 ? 0.5341 0.6171 0.5175 -0.0144 0.0469  -0.0044 257 ILE B CA    
4850 C C     . ILE B 257 ? 0.5989 0.6904 0.5812 -0.0154 0.0474  -0.0043 257 ILE B C     
4851 O O     . ILE B 257 ? 0.6442 0.7416 0.6269 -0.0159 0.0475  -0.0026 257 ILE B O     
4852 C CB    . ILE B 257 ? 0.3867 0.4659 0.3713 -0.0151 0.0452  -0.0005 257 ILE B CB    
4853 C CG1   . ILE B 257 ? 0.4237 0.4947 0.4092 -0.0142 0.0449  -0.0008 257 ILE B CG1   
4854 C CG2   . ILE B 257 ? 0.2894 0.3735 0.2748 -0.0165 0.0443  0.0037  257 ILE B CG2   
4855 C CD1   . ILE B 257 ? 0.3977 0.4636 0.3837 -0.0146 0.0433  0.0024  257 ILE B CD1   
4856 N N     . GLU B 258 ? 0.6157 0.7082 0.5964 -0.0160 0.0476  -0.0060 258 GLU B N     
4857 C CA    . GLU B 258 ? 0.4757 0.5765 0.4550 -0.0171 0.0481  -0.0064 258 GLU B CA    
4858 C C     . GLU B 258 ? 0.4477 0.5516 0.4254 -0.0164 0.0498  -0.0098 258 GLU B C     
4859 O O     . GLU B 258 ? 0.4095 0.5206 0.3870 -0.0167 0.0501  -0.0086 258 GLU B O     
4860 C CB    . GLU B 258 ? 0.5200 0.6209 0.4978 -0.0180 0.0480  -0.0082 258 GLU B CB    
4861 C CG    . GLU B 258 ? 0.6299 0.7290 0.6090 -0.0184 0.0465  -0.0050 258 GLU B CG    
4862 C CD    . GLU B 258 ? 0.7212 0.8208 0.6987 -0.0192 0.0466  -0.0070 258 GLU B CD    
4863 O OE1   . GLU B 258 ? 0.6599 0.7607 0.6350 -0.0199 0.0477  -0.0111 258 GLU B OE1   
4864 O OE2   . GLU B 258 ? 0.7710 0.8697 0.7493 -0.0192 0.0455  -0.0046 258 GLU B OE2   
4865 N N     . LYS B 259 ? 0.2733 0.3714 0.2495 -0.0151 0.0510  -0.0138 259 LYS B N     
4866 C CA    . LYS B 259 ? 0.3241 0.4239 0.2981 -0.0139 0.0529  -0.0173 259 LYS B CA    
4867 C C     . LYS B 259 ? 0.3129 0.4147 0.2883 -0.0122 0.0535  -0.0159 259 LYS B C     
4868 O O     . LYS B 259 ? 0.3672 0.4726 0.3407 -0.0110 0.0551  -0.0179 259 LYS B O     
4869 C CB    . LYS B 259 ? 0.2760 0.3686 0.2474 -0.0131 0.0542  -0.0220 259 LYS B CB    
4870 C CG    . LYS B 259 ? 0.3690 0.4611 0.3385 -0.0153 0.0537  -0.0234 259 LYS B CG    
4871 C CD    . LYS B 259 ? 0.3908 0.4761 0.3571 -0.0151 0.0550  -0.0283 259 LYS B CD    
4872 C CE    . LYS B 259 ? 0.4973 0.5842 0.4616 -0.0178 0.0545  -0.0296 259 LYS B CE    
4873 N NZ    . LYS B 259 ? 0.4937 0.5748 0.4538 -0.0184 0.0558  -0.0346 259 LYS B NZ    
4874 N N     . HIS B 260 ? 0.5903 0.6898 0.5685 -0.0121 0.0523  -0.0126 260 HIS B N     
4875 C CA    . HIS B 260 ? 0.5956 0.6974 0.5754 -0.0110 0.0525  -0.0109 260 HIS B CA    
4876 C C     . HIS B 260 ? 0.5727 0.6791 0.5548 -0.0128 0.0508  -0.0058 260 HIS B C     
4877 O O     . HIS B 260 ? 0.5370 0.6431 0.5208 -0.0126 0.0504  -0.0037 260 HIS B O     
4878 C CB    . HIS B 260 ? 0.5354 0.6293 0.5159 -0.0092 0.0528  -0.0121 260 HIS B CB    
4879 C CG    . HIS B 260 ? 0.6159 0.7057 0.5939 -0.0070 0.0549  -0.0168 260 HIS B CG    
4880 N ND1   . HIS B 260 ? 0.6796 0.7643 0.6554 -0.0074 0.0553  -0.0201 260 HIS B ND1   
4881 C CD2   . HIS B 260 ? 0.6858 0.7755 0.6629 -0.0043 0.0567  -0.0186 260 HIS B CD2   
4882 C CE1   . HIS B 260 ? 0.7321 0.8132 0.7056 -0.0052 0.0572  -0.0238 260 HIS B CE1   
4883 N NE2   . HIS B 260 ? 0.7136 0.7975 0.6879 -0.0031 0.0582  -0.0230 260 HIS B NE2   
4884 N N     . LYS B 261 ? 0.3756 0.4863 0.3577 -0.0147 0.0499  -0.0036 261 LYS B N     
4885 C CA    . LYS B 261 ? 0.4500 0.5636 0.4340 -0.0166 0.0482  0.0015  261 LYS B CA    
4886 C C     . LYS B 261 ? 0.4471 0.5678 0.4320 -0.0169 0.0484  0.0039  261 LYS B C     
4887 O O     . LYS B 261 ? 0.4712 0.5923 0.4576 -0.0185 0.0470  0.0079  261 LYS B O     
4888 C CB    . LYS B 261 ? 0.4587 0.5753 0.4424 -0.0183 0.0472  0.0038  261 LYS B CB    
4889 C CG    . LYS B 261 ? 0.5537 0.6790 0.5359 -0.0187 0.0481  0.0025  261 LYS B CG    
4890 C CD    . LYS B 261 ? 0.6220 0.7492 0.6038 -0.0201 0.0471  0.0043  261 LYS B CD    
4891 C CE    . LYS B 261 ? 0.5347 0.6545 0.5160 -0.0196 0.0469  0.0023  261 LYS B CE    
4892 N NZ    . LYS B 261 ? 0.4460 0.5696 0.4263 -0.0206 0.0465  0.0026  261 LYS B NZ    
4893 N N     . THR B 262 ? 0.2731 0.3996 0.2569 -0.0155 0.0500  0.0015  262 THR B N     
4894 C CA    . THR B 262 ? 0.2678 0.4022 0.2524 -0.0155 0.0504  0.0036  262 THR B CA    
4895 C C     . THR B 262 ? 0.2685 0.4011 0.2542 -0.0140 0.0509  0.0035  262 THR B C     
4896 O O     . THR B 262 ? 0.2858 0.4247 0.2727 -0.0145 0.0508  0.0062  262 THR B O     
4897 C CB    . THR B 262 ? 0.3305 0.4728 0.3131 -0.0145 0.0520  0.0012  262 THR B CB    
4898 O OG1   . THR B 262 ? 0.3883 0.5258 0.3684 -0.0121 0.0538  -0.0040 262 THR B OG1   
4899 C CG2   . THR B 262 ? 0.2698 0.4165 0.2518 -0.0166 0.0512  0.0027  262 THR B CG2   
4900 N N     . ASP B 263 ? 0.5074 0.6315 0.4928 -0.0124 0.0514  0.0007  263 ASP B N     
4901 C CA    . ASP B 263 ? 0.6046 0.7267 0.5911 -0.0108 0.0519  0.0006  263 ASP B CA    
4902 C C     . ASP B 263 ? 0.5517 0.6736 0.5404 -0.0131 0.0500  0.0050  263 ASP B C     
4903 O O     . ASP B 263 ? 0.5726 0.6901 0.5618 -0.0154 0.0483  0.0071  263 ASP B O     
4904 C CB    . ASP B 263 ? 0.6543 0.7668 0.6399 -0.0088 0.0526  -0.0032 263 ASP B CB    
4905 C CG    . ASP B 263 ? 0.7284 0.8410 0.7115 -0.0058 0.0551  -0.0076 263 ASP B CG    
4906 O OD1   . ASP B 263 ? 0.8084 0.9286 0.7904 -0.0050 0.0562  -0.0080 263 ASP B OD1   
4907 O OD2   . ASP B 263 ? 0.7166 0.8214 0.6986 -0.0042 0.0558  -0.0108 263 ASP B OD2   
4908 N N     . LYS B 264 ? 0.5678 0.6946 0.5575 -0.0124 0.0505  0.0063  264 LYS B N     
4909 C CA    . LYS B 264 ? 0.6791 0.8066 0.6707 -0.0151 0.0487  0.0105  264 LYS B CA    
4910 C C     . LYS B 264 ? 0.6419 0.7615 0.6342 -0.0146 0.0483  0.0099  264 LYS B C     
4911 O O     . LYS B 264 ? 0.6829 0.8007 0.6762 -0.0172 0.0467  0.0129  264 LYS B O     
4912 C CB    . LYS B 264 ? 0.7427 0.8815 0.7351 -0.0155 0.0491  0.0132  264 LYS B CB    
4913 C CG    . LYS B 264 ? 0.8161 0.9573 0.8099 -0.0196 0.0470  0.0181  264 LYS B CG    
4914 C CD    . LYS B 264 ? 0.8189 0.9546 0.8122 -0.0228 0.0450  0.0202  264 LYS B CD    
4915 C CE    . LYS B 264 ? 0.8324 0.9670 0.8262 -0.0269 0.0429  0.0247  264 LYS B CE    
4916 N NZ    . LYS B 264 ? 0.8802 1.0085 0.8745 -0.0268 0.0425  0.0242  264 LYS B NZ    
4917 N N     . ASP B 265 ? 0.5035 0.6182 0.4950 -0.0114 0.0498  0.0059  265 ASP B N     
4918 C CA    . ASP B 265 ? 0.5519 0.6592 0.5441 -0.0106 0.0496  0.0050  265 ASP B CA    
4919 C C     . ASP B 265 ? 0.5747 0.6719 0.5661 -0.0109 0.0489  0.0032  265 ASP B C     
4920 O O     . ASP B 265 ? 0.5220 0.6125 0.5137 -0.0097 0.0490  0.0017  265 ASP B O     
4921 C CB    . ASP B 265 ? 0.6066 0.7155 0.5987 -0.0066 0.0518  0.0024  265 ASP B CB    
4922 C CG    . ASP B 265 ? 0.6700 0.7780 0.6598 -0.0036 0.0539  -0.0018 265 ASP B CG    
4923 O OD1   . ASP B 265 ? 0.7059 0.8182 0.6945 -0.0043 0.0542  -0.0021 265 ASP B OD1   
4924 O OD2   . ASP B 265 ? 0.6790 0.7820 0.6680 -0.0006 0.0554  -0.0048 265 ASP B OD2   
4925 N N     . ILE B 266 ? 0.4524 0.5493 0.4430 -0.0123 0.0482  0.0035  266 ILE B N     
4926 C CA    . ILE B 266 ? 0.4686 0.5573 0.4584 -0.0123 0.0477  0.0018  266 ILE B CA    
4927 C C     . ILE B 266 ? 0.4582 0.5389 0.4487 -0.0136 0.0461  0.0033  266 ILE B C     
4928 O O     . ILE B 266 ? 0.4183 0.4920 0.4085 -0.0124 0.0462  0.0011  266 ILE B O     
4929 C CB    . ILE B 266 ? 0.4469 0.5385 0.4356 -0.0134 0.0475  0.0019  266 ILE B CB    
4930 C CG1   . ILE B 266 ? 0.4359 0.5214 0.4234 -0.0123 0.0479  -0.0014 266 ILE B CG1   
4931 C CG2   . ILE B 266 ? 0.4572 0.5500 0.4465 -0.0163 0.0456  0.0062  266 ILE B CG2   
4932 C CD1   . ILE B 266 ? 0.4004 0.4870 0.3871 -0.0138 0.0471  -0.0003 266 ILE B CD1   
4933 N N     . GLU B 267 ? 0.4735 0.5551 0.4647 -0.0161 0.0446  0.0071  267 GLU B N     
4934 C CA    . GLU B 267 ? 0.5180 0.5917 0.5094 -0.0173 0.0432  0.0083  267 GLU B CA    
4935 C C     . GLU B 267 ? 0.5913 0.6617 0.5835 -0.0156 0.0438  0.0064  267 GLU B C     
4936 O O     . GLU B 267 ? 0.5549 0.6176 0.5469 -0.0152 0.0433  0.0054  267 GLU B O     
4937 C CB    . GLU B 267 ? 0.5041 0.5796 0.4955 -0.0207 0.0415  0.0126  267 GLU B CB    
4938 C CG    . GLU B 267 ? 0.4845 0.5514 0.4750 -0.0226 0.0399  0.0145  267 GLU B CG    
4939 C CD    . GLU B 267 ? 0.5638 0.6329 0.5541 -0.0262 0.0385  0.0185  267 GLU B CD    
4940 O OE1   . GLU B 267 ? 0.5740 0.6493 0.5653 -0.0268 0.0388  0.0190  267 GLU B OE1   
4941 O OE2   . GLU B 267 ? 0.5461 0.6110 0.5348 -0.0284 0.0372  0.0211  267 GLU B OE2   
4942 N N     . LYS B 268 ? 0.4436 0.5202 0.4366 -0.0145 0.0449  0.0061  268 LYS B N     
4943 C CA    . LYS B 268 ? 0.4087 0.4831 0.4025 -0.0125 0.0457  0.0044  268 LYS B CA    
4944 C C     . LYS B 268 ? 0.4864 0.5554 0.4795 -0.0095 0.0471  0.0004  268 LYS B C     
4945 O O     . LYS B 268 ? 0.5139 0.5766 0.5072 -0.0085 0.0470  -0.0008 268 LYS B O     
4946 C CB    . LYS B 268 ? 0.3949 0.4783 0.3895 -0.0113 0.0469  0.0050  268 LYS B CB    
4947 C CG    . LYS B 268 ? 0.4182 0.5008 0.4135 -0.0083 0.0483  0.0032  268 LYS B CG    
4948 C CD    . LYS B 268 ? 0.4732 0.5659 0.4692 -0.0069 0.0496  0.0042  268 LYS B CD    
4949 C CE    . LYS B 268 ? 0.5019 0.5941 0.4981 -0.0029 0.0516  0.0021  268 LYS B CE    
4950 N NZ    . LYS B 268 ? 0.5161 0.6187 0.5128 -0.0008 0.0531  0.0032  268 LYS B NZ    
4951 N N     . LYS B 269 ? 0.5628 0.6344 0.5547 -0.0082 0.0483  -0.0016 269 LYS B N     
4952 C CA    . LYS B 269 ? 0.5209 0.5875 0.5116 -0.0059 0.0496  -0.0055 269 LYS B CA    
4953 C C     . LYS B 269 ? 0.5237 0.5829 0.5140 -0.0068 0.0485  -0.0062 269 LYS B C     
4954 O O     . LYS B 269 ? 0.5428 0.5959 0.5327 -0.0054 0.0490  -0.0085 269 LYS B O     
4955 C CB    . LYS B 269 ? 0.4564 0.5282 0.4456 -0.0046 0.0513  -0.0076 269 LYS B CB    
4956 C CG    . LYS B 269 ? 0.4048 0.4823 0.3940 -0.0022 0.0530  -0.0080 269 LYS B CG    
4957 C CD    . LYS B 269 ? 0.3295 0.4104 0.3164 -0.0005 0.0549  -0.0107 269 LYS B CD    
4958 C CE    . LYS B 269 ? 0.4481 0.5350 0.4347 -0.0029 0.0540  -0.0091 269 LYS B CE    
4959 N NZ    . LYS B 269 ? 0.5754 0.6668 0.5596 -0.0013 0.0559  -0.0116 269 LYS B NZ    
4960 N N     . VAL B 270 ? 0.3920 0.4517 0.3821 -0.0091 0.0471  -0.0039 270 VAL B N     
4961 C CA    . VAL B 270 ? 0.3469 0.4002 0.3365 -0.0097 0.0460  -0.0040 270 VAL B CA    
4962 C C     . VAL B 270 ? 0.3553 0.4022 0.3458 -0.0099 0.0450  -0.0031 270 VAL B C     
4963 O O     . VAL B 270 ? 0.2630 0.3038 0.2532 -0.0092 0.0448  -0.0043 270 VAL B O     
4964 C CB    . VAL B 270 ? 0.3132 0.3691 0.3023 -0.0116 0.0450  -0.0016 270 VAL B CB    
4965 C CG1   . VAL B 270 ? 0.2610 0.3103 0.2498 -0.0121 0.0437  -0.0007 270 VAL B CG1   
4966 C CG2   . VAL B 270 ? 0.2829 0.3439 0.2709 -0.0112 0.0461  -0.0036 270 VAL B CG2   
4967 N N     . ASN B 271 ? 0.4839 0.5327 0.4752 -0.0110 0.0444  -0.0007 271 ASN B N     
4968 C CA    . ASN B 271 ? 0.4725 0.5158 0.4644 -0.0114 0.0435  0.0000  271 ASN B CA    
4969 C C     . ASN B 271 ? 0.4757 0.5162 0.4682 -0.0089 0.0447  -0.0028 271 ASN B C     
4970 O O     . ASN B 271 ? 0.4807 0.5149 0.4732 -0.0087 0.0441  -0.0032 271 ASN B O     
4971 C CB    . ASN B 271 ? 0.5033 0.5501 0.4957 -0.0138 0.0425  0.0032  271 ASN B CB    
4972 C CG    . ASN B 271 ? 0.4931 0.5357 0.4844 -0.0165 0.0407  0.0061  271 ASN B CG    
4973 O OD1   . ASN B 271 ? 0.4686 0.5038 0.4593 -0.0164 0.0400  0.0058  271 ASN B OD1   
4974 N ND2   . ASN B 271 ? 0.4283 0.4757 0.4192 -0.0189 0.0400  0.0090  271 ASN B ND2   
4975 N N     . GLN B 272 ? 0.3283 0.3732 0.3210 -0.0070 0.0464  -0.0046 272 GLN B N     
4976 C CA    . GLN B 272 ? 0.2581 0.2999 0.2509 -0.0044 0.0477  -0.0072 272 GLN B CA    
4977 C C     . GLN B 272 ? 0.3708 0.4062 0.3626 -0.0035 0.0480  -0.0099 272 GLN B C     
4978 O O     . GLN B 272 ? 0.3697 0.3998 0.3619 -0.0024 0.0481  -0.0111 272 GLN B O     
4979 C CB    . GLN B 272 ? 0.2589 0.3065 0.2516 -0.0023 0.0496  -0.0085 272 GLN B CB    
4980 C CG    . GLN B 272 ? 0.2811 0.3348 0.2751 -0.0022 0.0498  -0.0063 272 GLN B CG    
4981 C CD    . GLN B 272 ? 0.3797 0.4391 0.3731 0.0006  0.0520  -0.0077 272 GLN B CD    
4982 O OE1   . GLN B 272 ? 0.3648 0.4229 0.3565 0.0022  0.0534  -0.0104 272 GLN B OE1   
4983 N NE2   . GLN B 272 ? 0.4412 0.5071 0.4358 0.0012  0.0524  -0.0057 272 GLN B NE2   
4984 N N     . ILE B 273 ? 0.3150 0.3516 0.3056 -0.0040 0.0481  -0.0106 273 ILE B N     
4985 C CA    . ILE B 273 ? 0.3076 0.3392 0.2972 -0.0036 0.0482  -0.0128 273 ILE B CA    
4986 C C     . ILE B 273 ? 0.3731 0.3993 0.3632 -0.0046 0.0466  -0.0114 273 ILE B C     
4987 O O     . ILE B 273 ? 0.3116 0.3326 0.3016 -0.0037 0.0466  -0.0129 273 ILE B O     
4988 C CB    . ILE B 273 ? 0.2600 0.2952 0.2482 -0.0043 0.0486  -0.0139 273 ILE B CB    
4989 C CG1   . ILE B 273 ? 0.2918 0.3328 0.2792 -0.0034 0.0502  -0.0149 273 ILE B CG1   
4990 C CG2   . ILE B 273 ? 0.3219 0.3526 0.3087 -0.0039 0.0490  -0.0166 273 ILE B CG2   
4991 C CD1   . ILE B 273 ? 0.4509 0.4891 0.4368 -0.0012 0.0521  -0.0186 273 ILE B CD1   
4992 N N     . ILE B 274 ? 0.3911 0.4185 0.3815 -0.0064 0.0451  -0.0084 274 ILE B N     
4993 C CA    . ILE B 274 ? 0.4287 0.4506 0.4190 -0.0070 0.0437  -0.0069 274 ILE B CA    
4994 C C     . ILE B 274 ? 0.4742 0.4915 0.4653 -0.0064 0.0435  -0.0071 274 ILE B C     
4995 O O     . ILE B 274 ? 0.5109 0.5228 0.5018 -0.0058 0.0431  -0.0077 274 ILE B O     
4996 C CB    . ILE B 274 ? 0.3966 0.4200 0.3864 -0.0090 0.0424  -0.0036 274 ILE B CB    
4997 C CG1   . ILE B 274 ? 0.3482 0.3759 0.3373 -0.0094 0.0426  -0.0034 274 ILE B CG1   
4998 C CG2   . ILE B 274 ? 0.3317 0.3485 0.3209 -0.0094 0.0411  -0.0020 274 ILE B CG2   
4999 C CD1   . ILE B 274 ? 0.2594 0.2843 0.2478 -0.0084 0.0428  -0.0049 274 ILE B CD1   
5000 N N     . ASN B 275 ? 0.4989 0.5189 0.4907 -0.0066 0.0437  -0.0064 275 ASN B N     
5001 C CA    . ASN B 275 ? 0.4405 0.4572 0.4332 -0.0063 0.0434  -0.0064 275 ASN B CA    
5002 C C     . ASN B 275 ? 0.4309 0.4447 0.4240 -0.0038 0.0446  -0.0092 275 ASN B C     
5003 O O     . ASN B 275 ? 0.4088 0.4178 0.4022 -0.0034 0.0442  -0.0095 275 ASN B O     
5004 C CB    . ASN B 275 ? 0.3810 0.4024 0.3744 -0.0075 0.0432  -0.0043 275 ASN B CB    
5005 C CG    . ASN B 275 ? 0.3315 0.3540 0.3241 -0.0104 0.0417  -0.0012 275 ASN B CG    
5006 O OD1   . ASN B 275 ? 0.4540 0.4731 0.4455 -0.0112 0.0409  -0.0005 275 ASN B OD1   
5007 N ND2   . ASN B 275 ? 0.3141 0.3415 0.3073 -0.0120 0.0414  0.0007  275 ASN B ND2   
5008 N N     . LEU B 276 ? 0.3765 0.3928 0.3694 -0.0023 0.0462  -0.0114 276 LEU B N     
5009 C CA    . LEU B 276 ? 0.3217 0.3343 0.3144 -0.0002 0.0475  -0.0141 276 LEU B CA    
5010 C C     . LEU B 276 ? 0.3576 0.3651 0.3496 -0.0004 0.0469  -0.0151 276 LEU B C     
5011 O O     . LEU B 276 ? 0.3823 0.3856 0.3745 0.0008  0.0472  -0.0165 276 LEU B O     
5012 C CB    . LEU B 276 ? 0.3910 0.4065 0.3828 0.0014  0.0494  -0.0163 276 LEU B CB    
5013 C CG    . LEU B 276 ? 0.3712 0.3823 0.3625 0.0037  0.0509  -0.0189 276 LEU B CG    
5014 C CD1   . LEU B 276 ? 0.4035 0.4140 0.3965 0.0049  0.0509  -0.0179 276 LEU B CD1   
5015 C CD2   . LEU B 276 ? 0.3644 0.3773 0.3539 0.0053  0.0529  -0.0213 276 LEU B CD2   
5016 N N     . TRP B 277 ? 0.3645 0.3729 0.3558 -0.0017 0.0461  -0.0144 277 TRP B N     
5017 C CA    . TRP B 277 ? 0.3965 0.4010 0.3871 -0.0018 0.0455  -0.0149 277 TRP B CA    
5018 C C     . TRP B 277 ? 0.3569 0.3568 0.3481 -0.0017 0.0443  -0.0136 277 TRP B C     
5019 O O     . TRP B 277 ? 0.3583 0.3543 0.3495 -0.0009 0.0443  -0.0147 277 TRP B O     
5020 C CB    . TRP B 277 ? 0.3827 0.3902 0.3725 -0.0031 0.0448  -0.0135 277 TRP B CB    
5021 C CG    . TRP B 277 ? 0.3988 0.4043 0.3880 -0.0032 0.0443  -0.0138 277 TRP B CG    
5022 C CD1   . TRP B 277 ? 0.4316 0.4340 0.4206 -0.0031 0.0431  -0.0119 277 TRP B CD1   
5023 C CD2   . TRP B 277 ? 0.4314 0.4380 0.4195 -0.0032 0.0450  -0.0159 277 TRP B CD2   
5024 N NE1   . TRP B 277 ? 0.3852 0.3876 0.3736 -0.0029 0.0430  -0.0125 277 TRP B NE1   
5025 C CE2   . TRP B 277 ? 0.3715 0.3766 0.3593 -0.0033 0.0441  -0.0149 277 TRP B CE2   
5026 C CE3   . TRP B 277 ? 0.4465 0.4552 0.4336 -0.0034 0.0463  -0.0185 277 TRP B CE3   
5027 C CZ2   . TRP B 277 ? 0.3841 0.3906 0.3710 -0.0037 0.0444  -0.0163 277 TRP B CZ2   
5028 C CZ3   . TRP B 277 ? 0.4851 0.4942 0.4709 -0.0040 0.0466  -0.0201 277 TRP B CZ3   
5029 C CH2   . TRP B 277 ? 0.4456 0.4541 0.4315 -0.0044 0.0456  -0.0189 277 TRP B CH2   
5030 N N     . ILE B 278 ? 0.4146 0.4150 0.4061 -0.0028 0.0433  -0.0112 278 ILE B N     
5031 C CA    . ILE B 278 ? 0.4591 0.4546 0.4505 -0.0030 0.0422  -0.0099 278 ILE B CA    
5032 C C     . ILE B 278 ? 0.4727 0.4659 0.4651 -0.0018 0.0427  -0.0112 278 ILE B C     
5033 O O     . ILE B 278 ? 0.4275 0.4161 0.4198 -0.0011 0.0423  -0.0116 278 ILE B O     
5034 C CB    . ILE B 278 ? 0.4515 0.4479 0.4425 -0.0050 0.0411  -0.0071 278 ILE B CB    
5035 C CG1   . ILE B 278 ? 0.3909 0.3889 0.3807 -0.0059 0.0406  -0.0056 278 ILE B CG1   
5036 C CG2   . ILE B 278 ? 0.2647 0.2557 0.2551 -0.0055 0.0400  -0.0061 278 ILE B CG2   
5037 C CD1   . ILE B 278 ? 0.4520 0.4515 0.4411 -0.0081 0.0396  -0.0028 278 ILE B CD1   
5038 N N     . SER B 279 ? 0.4403 0.4369 0.4336 -0.0014 0.0437  -0.0119 279 SER B N     
5039 C CA    . SER B 279 ? 0.3286 0.3238 0.3229 0.0000  0.0443  -0.0128 279 SER B CA    
5040 C C     . SER B 279 ? 0.3787 0.3704 0.3728 0.0016  0.0451  -0.0151 279 SER B C     
5041 O O     . SER B 279 ? 0.4098 0.3980 0.4045 0.0024  0.0449  -0.0155 279 SER B O     
5042 C CB    . SER B 279 ? 0.3392 0.3395 0.3342 0.0008  0.0456  -0.0131 279 SER B CB    
5043 O OG    . SER B 279 ? 0.4472 0.4521 0.4425 -0.0008 0.0450  -0.0109 279 SER B OG    
5044 N N     . SER B 280 ? 0.3974 0.3904 0.3907 0.0018  0.0459  -0.0166 280 SER B N     
5045 C CA    . SER B 280 ? 0.4079 0.3979 0.4006 0.0028  0.0467  -0.0189 280 SER B CA    
5046 C C     . SER B 280 ? 0.5025 0.4889 0.4949 0.0025  0.0457  -0.0188 280 SER B C     
5047 O O     . SER B 280 ? 0.5549 0.5380 0.5474 0.0034  0.0460  -0.0200 280 SER B O     
5048 C CB    . SER B 280 ? 0.3703 0.3628 0.3617 0.0027  0.0479  -0.0206 280 SER B CB    
5049 O OG    . SER B 280 ? 0.3811 0.3767 0.3726 0.0036  0.0492  -0.0209 280 SER B OG    
5050 N N     . TYR B 281 ? 0.4373 0.4244 0.4293 0.0014  0.0445  -0.0172 281 TYR B N     
5051 C CA    . TYR B 281 ? 0.4076 0.3916 0.3992 0.0016  0.0437  -0.0167 281 TYR B CA    
5052 C C     . TYR B 281 ? 0.4478 0.4279 0.4400 0.0023  0.0430  -0.0161 281 TYR B C     
5053 O O     . TYR B 281 ? 0.4147 0.3920 0.4069 0.0031  0.0428  -0.0166 281 TYR B O     
5054 C CB    . TYR B 281 ? 0.3193 0.3053 0.3100 0.0007  0.0429  -0.0151 281 TYR B CB    
5055 C CG    . TYR B 281 ? 0.4540 0.4431 0.4439 0.0002  0.0434  -0.0163 281 TYR B CG    
5056 C CD1   . TYR B 281 ? 0.4917 0.4838 0.4813 -0.0003 0.0446  -0.0179 281 TYR B CD1   
5057 C CD2   . TYR B 281 ? 0.5664 0.5557 0.5557 0.0003  0.0429  -0.0159 281 TYR B CD2   
5058 C CE1   . TYR B 281 ? 0.5397 0.5345 0.5282 -0.0011 0.0451  -0.0193 281 TYR B CE1   
5059 C CE2   . TYR B 281 ? 0.5408 0.5337 0.5293 -0.0006 0.0434  -0.0170 281 TYR B CE2   
5060 C CZ    . TYR B 281 ? 0.5411 0.5364 0.5291 -0.0015 0.0444  -0.0188 281 TYR B CZ    
5061 O OH    . TYR B 281 ? 0.5870 0.5855 0.5737 -0.0027 0.0449  -0.0201 281 TYR B OH    
5062 N N     . ILE B 282 ? 0.3265 0.3066 0.3191 0.0018  0.0426  -0.0148 282 ILE B N     
5063 C CA    . ILE B 282 ? 0.3099 0.2867 0.3029 0.0022  0.0420  -0.0143 282 ILE B CA    
5064 C C     . ILE B 282 ? 0.3860 0.3619 0.3802 0.0035  0.0429  -0.0159 282 ILE B C     
5065 O O     . ILE B 282 ? 0.4042 0.3769 0.3985 0.0043  0.0426  -0.0162 282 ILE B O     
5066 C CB    . ILE B 282 ? 0.3567 0.3339 0.3494 0.0008  0.0412  -0.0125 282 ILE B CB    
5067 C CG1   . ILE B 282 ? 0.3614 0.3385 0.3526 -0.0005 0.0403  -0.0106 282 ILE B CG1   
5068 C CG2   . ILE B 282 ? 0.3008 0.2745 0.2936 0.0010  0.0405  -0.0122 282 ILE B CG2   
5069 C CD1   . ILE B 282 ? 0.2574 0.2351 0.2480 -0.0025 0.0394  -0.0087 282 ILE B CD1   
5070 N N     . LYS B 283 ? 0.5285 0.5071 0.5232 0.0040  0.0441  -0.0169 283 LYS B N     
5071 C CA    . LYS B 283 ? 0.5500 0.5275 0.5456 0.0055  0.0452  -0.0182 283 LYS B CA    
5072 C C     . LYS B 283 ? 0.5735 0.5481 0.5687 0.0062  0.0457  -0.0199 283 LYS B C     
5073 O O     . LYS B 283 ? 0.6284 0.6006 0.6242 0.0073  0.0460  -0.0205 283 LYS B O     
5074 C CB    . LYS B 283 ? 0.5548 0.5357 0.5507 0.0062  0.0466  -0.0188 283 LYS B CB    
5075 C CG    . LYS B 283 ? 0.5813 0.5654 0.5782 0.0058  0.0463  -0.0170 283 LYS B CG    
5076 C CD    . LYS B 283 ? 0.5242 0.5116 0.5217 0.0075  0.0480  -0.0174 283 LYS B CD    
5077 C CE    . LYS B 283 ? 0.5905 0.5748 0.5883 0.0097  0.0492  -0.0188 283 LYS B CE    
5078 N NZ    . LYS B 283 ? 0.6349 0.6223 0.6333 0.0118  0.0509  -0.0188 283 LYS B NZ    
5079 N N     . GLU B 284 ? 0.5501 0.5254 0.5442 0.0055  0.0457  -0.0205 284 GLU B N     
5080 C CA    . GLU B 284 ? 0.4907 0.4640 0.4842 0.0056  0.0460  -0.0220 284 GLU B CA    
5081 C C     . GLU B 284 ? 0.4210 0.3924 0.4144 0.0055  0.0448  -0.0211 284 GLU B C     
5082 O O     . GLU B 284 ? 0.4785 0.4488 0.4716 0.0055  0.0450  -0.0220 284 GLU B O     
5083 C CB    . GLU B 284 ? 0.5614 0.5369 0.5534 0.0045  0.0467  -0.0232 284 GLU B CB    
5084 C CG    . GLU B 284 ? 0.5652 0.5422 0.5568 0.0050  0.0481  -0.0244 284 GLU B CG    
5085 C CD    . GLU B 284 ? 0.6656 0.6393 0.6569 0.0063  0.0495  -0.0260 284 GLU B CD    
5086 O OE1   . GLU B 284 ? 0.6208 0.5917 0.6111 0.0059  0.0498  -0.0273 284 GLU B OE1   
5087 O OE2   . GLU B 284 ? 0.7500 0.7241 0.7419 0.0077  0.0504  -0.0259 284 GLU B OE2   
5088 N N     . GLY B 285 ? 0.2520 0.2232 0.2456 0.0054  0.0437  -0.0193 285 GLY B N     
5089 C CA    . GLY B 285 ? 0.2505 0.2196 0.2437 0.0059  0.0427  -0.0184 285 GLY B CA    
5090 C C     . GLY B 285 ? 0.2933 0.2641 0.2855 0.0055  0.0422  -0.0178 285 GLY B C     
5091 O O     . GLY B 285 ? 0.3234 0.2931 0.3152 0.0062  0.0416  -0.0170 285 GLY B O     
5092 N N     . TYR B 286 ? 0.2515 0.2256 0.2432 0.0045  0.0426  -0.0180 286 TYR B N     
5093 C CA    . TYR B 286 ? 0.2520 0.2287 0.2428 0.0040  0.0422  -0.0172 286 TYR B CA    
5094 C C     . TYR B 286 ? 0.3292 0.3051 0.3193 0.0044  0.0413  -0.0149 286 TYR B C     
5095 O O     . TYR B 286 ? 0.4450 0.4214 0.4344 0.0051  0.0408  -0.0138 286 TYR B O     
5096 C CB    . TYR B 286 ? 0.3419 0.3224 0.3323 0.0027  0.0429  -0.0180 286 TYR B CB    
5097 C CG    . TYR B 286 ? 0.3842 0.3650 0.3744 0.0021  0.0441  -0.0205 286 TYR B CG    
5098 C CD1   . TYR B 286 ? 0.3716 0.3502 0.3618 0.0023  0.0444  -0.0218 286 TYR B CD1   
5099 C CD2   . TYR B 286 ? 0.4478 0.4308 0.4375 0.0014  0.0450  -0.0215 286 TYR B CD2   
5100 C CE1   . TYR B 286 ? 0.3901 0.3679 0.3795 0.0017  0.0456  -0.0241 286 TYR B CE1   
5101 C CE2   . TYR B 286 ? 0.5042 0.4866 0.4931 0.0010  0.0463  -0.0239 286 TYR B CE2   
5102 C CZ    . TYR B 286 ? 0.4681 0.4474 0.4566 0.0011  0.0466  -0.0252 286 TYR B CZ    
5103 O OH    . TYR B 286 ? 0.4889 0.4665 0.4761 0.0007  0.0479  -0.0276 286 TYR B OH    
5104 N N     . HIS B 287 ? 0.3090 0.2839 0.2991 0.0040  0.0410  -0.0140 287 HIS B N     
5105 C CA    . HIS B 287 ? 0.3023 0.2757 0.2912 0.0041  0.0401  -0.0117 287 HIS B CA    
5106 C C     . HIS B 287 ? 0.3063 0.2768 0.2949 0.0035  0.0396  -0.0108 287 HIS B C     
5107 O O     . HIS B 287 ? 0.2898 0.2610 0.2794 0.0028  0.0400  -0.0117 287 HIS B O     
5108 C CB    . HIS B 287 ? 0.2673 0.2446 0.2556 0.0032  0.0401  -0.0105 287 HIS B CB    
5109 C CG    . HIS B 287 ? 0.3204 0.3006 0.3082 0.0037  0.0402  -0.0103 287 HIS B CG    
5110 N ND1   . HIS B 287 ? 0.3107 0.2896 0.2974 0.0052  0.0397  -0.0086 287 HIS B ND1   
5111 C CD2   . HIS B 287 ? 0.2609 0.2456 0.2490 0.0029  0.0408  -0.0116 287 HIS B CD2   
5112 C CE1   . HIS B 287 ? 0.2570 0.2403 0.2437 0.0053  0.0399  -0.0086 287 HIS B CE1   
5113 N NE2   . HIS B 287 ? 0.2579 0.2447 0.2454 0.0037  0.0405  -0.0105 287 HIS B NE2   
5114 N N     . SER B 288 ? 0.6086 0.5757 0.5954 0.0037  0.0388  -0.0090 288 SER B N     
5115 C CA    . SER B 288 ? 0.6802 0.6444 0.6660 0.0024  0.0381  -0.0079 288 SER B CA    
5116 C C     . SER B 288 ? 0.6900 0.6575 0.6755 0.0007  0.0381  -0.0066 288 SER B C     
5117 O O     . SER B 288 ? 0.6914 0.6624 0.6771 0.0009  0.0384  -0.0063 288 SER B O     
5118 C CB    . SER B 288 ? 0.6633 0.6216 0.6465 0.0034  0.0374  -0.0066 288 SER B CB    
5119 O OG    . SER B 288 ? 0.6640 0.6218 0.6454 0.0034  0.0372  -0.0047 288 SER B OG    
5120 N N     . TYR B 289 ? 0.4636 0.4304 0.4486 -0.0012 0.0376  -0.0056 289 TYR B N     
5121 C CA    . TYR B 289 ? 0.3734 0.3438 0.3583 -0.0031 0.0375  -0.0042 289 TYR B CA    
5122 C C     . TYR B 289 ? 0.3597 0.3287 0.3425 -0.0030 0.0370  -0.0022 289 TYR B C     
5123 O O     . TYR B 289 ? 0.4061 0.3797 0.3894 -0.0035 0.0373  -0.0015 289 TYR B O     
5124 C CB    . TYR B 289 ? 0.3881 0.3572 0.3723 -0.0053 0.0368  -0.0032 289 TYR B CB    
5125 C CG    . TYR B 289 ? 0.3365 0.3076 0.3197 -0.0078 0.0363  -0.0011 289 TYR B CG    
5126 C CD1   . TYR B 289 ? 0.3486 0.3149 0.3288 -0.0089 0.0354  0.0011  289 TYR B CD1   
5127 C CD2   . TYR B 289 ? 0.3163 0.2940 0.3013 -0.0091 0.0367  -0.0010 289 TYR B CD2   
5128 C CE1   . TYR B 289 ? 0.3440 0.3119 0.3232 -0.0114 0.0349  0.0032  289 TYR B CE1   
5129 C CE2   . TYR B 289 ? 0.3565 0.3367 0.3407 -0.0115 0.0361  0.0011  289 TYR B CE2   
5130 C CZ    . TYR B 289 ? 0.4035 0.3787 0.3848 -0.0129 0.0352  0.0033  289 TYR B CZ    
5131 O OH    . TYR B 289 ? 0.4655 0.4429 0.4457 -0.0156 0.0346  0.0056  289 TYR B OH    
5132 N N     . SER B 290 ? 0.4887 0.4515 0.4691 -0.0021 0.0365  -0.0012 290 SER B N     
5133 C CA    . SER B 290 ? 0.5027 0.4635 0.4808 -0.0017 0.0362  0.0011  290 SER B CA    
5134 C C     . SER B 290 ? 0.4461 0.4093 0.4248 0.0008  0.0367  0.0010  290 SER B C     
5135 O O     . SER B 290 ? 0.4409 0.4033 0.4179 0.0017  0.0367  0.0029  290 SER B O     
5136 C CB    . SER B 290 ? 0.5646 0.5169 0.5392 -0.0019 0.0354  0.0024  290 SER B CB    
5137 O OG    . SER B 290 ? 0.5639 0.5150 0.5375 -0.0051 0.0348  0.0034  290 SER B OG    
5138 N N     . GLU B 291 ? 0.4051 0.3715 0.3860 0.0017  0.0373  -0.0013 291 GLU B N     
5139 C CA    . GLU B 291 ? 0.4035 0.3735 0.3852 0.0034  0.0378  -0.0016 291 GLU B CA    
5140 C C     . GLU B 291 ? 0.3651 0.3421 0.3483 0.0020  0.0383  -0.0020 291 GLU B C     
5141 O O     . GLU B 291 ? 0.3804 0.3615 0.3638 0.0027  0.0386  -0.0018 291 GLU B O     
5142 C CB    . GLU B 291 ? 0.3755 0.3448 0.3583 0.0048  0.0381  -0.0036 291 GLU B CB    
5143 C CG    . GLU B 291 ? 0.3781 0.3415 0.3591 0.0069  0.0378  -0.0030 291 GLU B CG    
5144 C CD    . GLU B 291 ? 0.3946 0.3577 0.3770 0.0080  0.0381  -0.0051 291 GLU B CD    
5145 O OE1   . GLU B 291 ? 0.4729 0.4398 0.4574 0.0071  0.0385  -0.0069 291 GLU B OE1   
5146 O OE2   . GLU B 291 ? 0.3404 0.2993 0.3215 0.0098  0.0379  -0.0049 291 GLU B OE2   
5147 N N     . VAL B 292 ? 0.2647 0.2433 0.2486 0.0001  0.0383  -0.0024 292 VAL B N     
5148 C CA    . VAL B 292 ? 0.4124 0.3975 0.3974 -0.0012 0.0388  -0.0027 292 VAL B CA    
5149 C C     . VAL B 292 ? 0.4750 0.4611 0.4589 -0.0026 0.0383  0.0000  292 VAL B C     
5150 O O     . VAL B 292 ? 0.3363 0.3265 0.3199 -0.0027 0.0384  0.0012  292 VAL B O     
5151 C CB    . VAL B 292 ? 0.4312 0.4185 0.4179 -0.0020 0.0394  -0.0050 292 VAL B CB    
5152 C CG1   . VAL B 292 ? 0.3360 0.3300 0.3233 -0.0029 0.0401  -0.0056 292 VAL B CG1   
5153 C CG2   . VAL B 292 ? 0.4676 0.4527 0.4551 -0.0006 0.0399  -0.0074 292 VAL B CG2   
5154 N N     . VAL B 293 ? 0.4252 0.4082 0.4085 -0.0040 0.0377  0.0008  293 VAL B N     
5155 C CA    . VAL B 293 ? 0.3327 0.3162 0.3147 -0.0059 0.0371  0.0034  293 VAL B CA    
5156 C C     . VAL B 293 ? 0.3410 0.3220 0.3209 -0.0049 0.0368  0.0060  293 VAL B C     
5157 O O     . VAL B 293 ? 0.3327 0.3171 0.3121 -0.0056 0.0367  0.0079  293 VAL B O     
5158 C CB    . VAL B 293 ? 0.3178 0.2973 0.2989 -0.0078 0.0365  0.0040  293 VAL B CB    
5159 C CG1   . VAL B 293 ? 0.3413 0.3204 0.3206 -0.0100 0.0357  0.0070  293 VAL B CG1   
5160 C CG2   . VAL B 293 ? 0.2691 0.2527 0.2526 -0.0085 0.0370  0.0020  293 VAL B CG2   
5161 N N     . ASP B 294 ? 0.4842 0.4590 0.4625 -0.0029 0.0366  0.0061  294 ASP B N     
5162 C CA    . ASP B 294 ? 0.4337 0.4055 0.4096 -0.0012 0.0365  0.0086  294 ASP B CA    
5163 C C     . ASP B 294 ? 0.4286 0.4072 0.4056 0.0001  0.0370  0.0091  294 ASP B C     
5164 O O     . ASP B 294 ? 0.4642 0.4422 0.4395 0.0014  0.0370  0.0117  294 ASP B O     
5165 C CB    . ASP B 294 ? 0.4463 0.4104 0.4202 0.0010  0.0364  0.0084  294 ASP B CB    
5166 C CG    . ASP B 294 ? 0.5725 0.5282 0.5435 -0.0004 0.0357  0.0093  294 ASP B CG    
5167 O OD1   . ASP B 294 ? 0.6546 0.6110 0.6257 -0.0034 0.0352  0.0095  294 ASP B OD1   
5168 O OD2   . ASP B 294 ? 0.6441 0.5925 0.6124 0.0015  0.0356  0.0098  294 ASP B OD2   
5169 N N     . VAL B 295 ? 0.3359 0.3208 0.3155 -0.0002 0.0376  0.0066  295 VAL B N     
5170 C CA    . VAL B 295 ? 0.3296 0.3220 0.3101 0.0000  0.0380  0.0070  295 VAL B CA    
5171 C C     . VAL B 295 ? 0.3675 0.3647 0.3483 -0.0022 0.0379  0.0082  295 VAL B C     
5172 O O     . VAL B 295 ? 0.4179 0.4178 0.3978 -0.0020 0.0378  0.0107  295 VAL B O     
5173 C CB    . VAL B 295 ? 0.3437 0.3402 0.3262 0.0001  0.0386  0.0037  295 VAL B CB    
5174 C CG1   . VAL B 295 ? 0.3411 0.3458 0.3242 -0.0004 0.0391  0.0036  295 VAL B CG1   
5175 C CG2   . VAL B 295 ? 0.4126 0.4055 0.3948 0.0023  0.0386  0.0029  295 VAL B CG2   
5176 N N     . LEU B 296 ? 0.4237 0.4217 0.4055 -0.0041 0.0380  0.0068  296 LEU B N     
5177 C CA    . LEU B 296 ? 0.4479 0.4515 0.4303 -0.0062 0.0380  0.0076  296 LEU B CA    
5178 C C     . LEU B 296 ? 0.4414 0.4432 0.4220 -0.0071 0.0373  0.0113  296 LEU B C     
5179 O O     . LEU B 296 ? 0.5769 0.5843 0.5575 -0.0080 0.0374  0.0129  296 LEU B O     
5180 C CB    . LEU B 296 ? 0.4494 0.4536 0.4331 -0.0076 0.0382  0.0057  296 LEU B CB    
5181 C CG    . LEU B 296 ? 0.4398 0.4476 0.4250 -0.0070 0.0392  0.0022  296 LEU B CG    
5182 C CD1   . LEU B 296 ? 0.3608 0.3675 0.3470 -0.0077 0.0394  0.0007  296 LEU B CD1   
5183 C CD2   . LEU B 296 ? 0.4432 0.4588 0.4288 -0.0077 0.0398  0.0021  296 LEU B CD2   
5184 N N     . THR B 297 ? 0.2779 0.2718 0.2565 -0.0071 0.0367  0.0126  297 THR B N     
5185 C CA    . THR B 297 ? 0.2900 0.2805 0.2664 -0.0086 0.0360  0.0160  297 THR B CA    
5186 C C     . THR B 297 ? 0.3519 0.3408 0.3262 -0.0067 0.0360  0.0189  297 THR B C     
5187 O O     . THR B 297 ? 0.4527 0.4385 0.4248 -0.0078 0.0355  0.0220  297 THR B O     
5188 C CB    . THR B 297 ? 0.3880 0.3698 0.3624 -0.0096 0.0353  0.0161  297 THR B CB    
5189 O OG1   . THR B 297 ? 0.3659 0.3409 0.3389 -0.0069 0.0354  0.0155  297 THR B OG1   
5190 C CG2   . THR B 297 ? 0.3493 0.3335 0.3258 -0.0113 0.0353  0.0136  297 THR B CG2   
5191 N N     . GLU B 298 ? 0.3480 0.3387 0.3228 -0.0040 0.0365  0.0183  298 GLU B N     
5192 C CA    . GLU B 298 ? 0.3339 0.3250 0.3071 -0.0020 0.0367  0.0214  298 GLU B CA    
5193 C C     . GLU B 298 ? 0.3428 0.3406 0.3165 -0.0040 0.0366  0.0235  298 GLU B C     
5194 O O     . GLU B 298 ? 0.3579 0.3634 0.3340 -0.0056 0.0368  0.0217  298 GLU B O     
5195 C CB    . GLU B 298 ? 0.3297 0.3249 0.3041 0.0008  0.0372  0.0205  298 GLU B CB    
5196 C CG    . GLU B 298 ? 0.3883 0.3830 0.3606 0.0034  0.0374  0.0242  298 GLU B CG    
5197 C CD    . GLU B 298 ? 0.4750 0.4723 0.4478 0.0066  0.0379  0.0238  298 GLU B CD    
5198 O OE1   . GLU B 298 ? 0.4601 0.4583 0.4345 0.0066  0.0381  0.0206  298 GLU B OE1   
5199 O OE2   . GLU B 298 ? 0.5618 0.5604 0.5332 0.0091  0.0382  0.0269  298 GLU B OE2   
5200 N N     . PRO B 299 ? 0.3721 0.3671 0.3435 -0.0037 0.0363  0.0274  299 PRO B N     
5201 C CA    . PRO B 299 ? 0.4605 0.4614 0.4321 -0.0059 0.0362  0.0297  299 PRO B CA    
5202 C C     . PRO B 299 ? 0.4798 0.4924 0.4541 -0.0061 0.0366  0.0288  299 PRO B C     
5203 O O     . PRO B 299 ? 0.4273 0.4458 0.4031 -0.0087 0.0366  0.0282  299 PRO B O     
5204 C CB    . PRO B 299 ? 0.4146 0.4098 0.3828 -0.0044 0.0361  0.0341  299 PRO B CB    
5205 C CG    . PRO B 299 ? 0.3948 0.3784 0.3603 -0.0027 0.0360  0.0337  299 PRO B CG    
5206 C CD    . PRO B 299 ? 0.3428 0.3286 0.3107 -0.0012 0.0363  0.0297  299 PRO B CD    
5207 N N     . PHE B 300 ? 0.3588 0.3753 0.3337 -0.0036 0.0372  0.0286  300 PHE B N     
5208 C CA    . PHE B 300 ? 0.2840 0.3116 0.2609 -0.0042 0.0376  0.0280  300 PHE B CA    
5209 C C     . PHE B 300 ? 0.3212 0.3534 0.3002 -0.0064 0.0378  0.0239  300 PHE B C     
5210 O O     . PHE B 300 ? 0.4006 0.4409 0.3807 -0.0080 0.0380  0.0236  300 PHE B O     
5211 C CB    . PHE B 300 ? 0.2831 0.3140 0.2600 -0.0014 0.0380  0.0282  300 PHE B CB    
5212 C CG    . PHE B 300 ? 0.3253 0.3561 0.3036 -0.0008 0.0383  0.0242  300 PHE B CG    
5213 C CD1   . PHE B 300 ? 0.3259 0.3484 0.3033 0.0011  0.0382  0.0235  300 PHE B CD1   
5214 C CD2   . PHE B 300 ? 0.3007 0.3396 0.2808 -0.0023 0.0387  0.0212  300 PHE B CD2   
5215 C CE1   . PHE B 300 ? 0.2997 0.3223 0.2783 0.0015  0.0385  0.0199  300 PHE B CE1   
5216 C CE2   . PHE B 300 ? 0.2718 0.3101 0.2527 -0.0020 0.0390  0.0176  300 PHE B CE2   
5217 C CZ    . PHE B 300 ? 0.2726 0.3029 0.2530 -0.0001 0.0388  0.0171  300 PHE B CZ    
5218 N N     . LEU B 301 ? 0.5306 0.5578 0.5101 -0.0061 0.0379  0.0207  301 LEU B N     
5219 C CA    . LEU B 301 ? 0.4729 0.5028 0.4542 -0.0078 0.0382  0.0170  301 LEU B CA    
5220 C C     . LEU B 301 ? 0.5300 0.5590 0.5113 -0.0101 0.0379  0.0177  301 LEU B C     
5221 O O     . LEU B 301 ? 0.5756 0.6096 0.5582 -0.0114 0.0383  0.0156  301 LEU B O     
5222 C CB    . LEU B 301 ? 0.4947 0.5191 0.4763 -0.0067 0.0384  0.0139  301 LEU B CB    
5223 C CG    . LEU B 301 ? 0.6040 0.6295 0.5859 -0.0049 0.0388  0.0124  301 LEU B CG    
5224 C CD1   . LEU B 301 ? 0.6185 0.6363 0.6002 -0.0035 0.0386  0.0109  301 LEU B CD1   
5225 C CD2   . LEU B 301 ? 0.5941 0.6269 0.5773 -0.0060 0.0395  0.0093  301 LEU B CD2   
5226 N N     . GLN B 302 ? 0.6726 0.6954 0.6523 -0.0105 0.0372  0.0205  302 GLN B N     
5227 C CA    . GLN B 302 ? 0.6893 0.7121 0.6689 -0.0132 0.0367  0.0215  302 GLN B CA    
5228 C C     . GLN B 302 ? 0.6263 0.6574 0.6064 -0.0147 0.0368  0.0233  302 GLN B C     
5229 O O     . GLN B 302 ? 0.6479 0.6831 0.6289 -0.0167 0.0368  0.0231  302 GLN B O     
5230 C CB    . GLN B 302 ? 0.7125 0.7261 0.6896 -0.0138 0.0358  0.0242  302 GLN B CB    
5231 C CG    . GLN B 302 ? 0.8263 0.8326 0.8031 -0.0136 0.0356  0.0221  302 GLN B CG    
5232 C CD    . GLN B 302 ? 0.8687 0.8797 0.8478 -0.0150 0.0359  0.0192  302 GLN B CD    
5233 O OE1   . GLN B 302 ? 0.8929 0.9040 0.8734 -0.0136 0.0365  0.0160  302 GLN B OE1   
5234 N NE2   . GLN B 302 ? 0.8337 0.8487 0.8131 -0.0177 0.0356  0.0205  302 GLN B NE2   
5235 N N     . SER B 303 ? 0.3907 0.4252 0.3704 -0.0135 0.0370  0.0251  303 SER B N     
5236 C CA    . SER B 303 ? 0.4766 0.5193 0.4567 -0.0147 0.0370  0.0270  303 SER B CA    
5237 C C     . SER B 303 ? 0.5878 0.6386 0.5698 -0.0157 0.0377  0.0237  303 SER B C     
5238 O O     . SER B 303 ? 0.6035 0.6602 0.5860 -0.0175 0.0377  0.0247  303 SER B O     
5239 C CB    . SER B 303 ? 0.5124 0.5580 0.4920 -0.0129 0.0372  0.0289  303 SER B CB    
5240 O OG    . SER B 303 ? 0.5494 0.5874 0.5267 -0.0115 0.0368  0.0323  303 SER B OG    
5241 N N     . ILE B 304 ? 0.5992 0.6505 0.5821 -0.0145 0.0384  0.0199  304 ILE B N     
5242 C CA    . ILE B 304 ? 0.5290 0.5874 0.5130 -0.0151 0.0393  0.0166  304 ILE B CA    
5243 C C     . ILE B 304 ? 0.5389 0.5979 0.5236 -0.0166 0.0393  0.0161  304 ILE B C     
5244 O O     . ILE B 304 ? 0.6006 0.6669 0.5858 -0.0176 0.0398  0.0157  304 ILE B O     
5245 C CB    . ILE B 304 ? 0.4980 0.5549 0.4824 -0.0137 0.0400  0.0125  304 ILE B CB    
5246 C CG1   . ILE B 304 ? 0.4961 0.5559 0.4799 -0.0128 0.0401  0.0130  304 ILE B CG1   
5247 C CG2   . ILE B 304 ? 0.4103 0.4719 0.3952 -0.0143 0.0410  0.0088  304 ILE B CG2   
5248 C CD1   . ILE B 304 ? 0.4265 0.4797 0.4097 -0.0110 0.0396  0.0143  304 ILE B CD1   
5249 N N     . PHE B 305 ? 0.5214 0.5733 0.5060 -0.0166 0.0389  0.0159  305 PHE B N     
5250 C CA    . PHE B 305 ? 0.5103 0.5630 0.4956 -0.0180 0.0389  0.0158  305 PHE B CA    
5251 C C     . PHE B 305 ? 0.4917 0.5472 0.4765 -0.0203 0.0381  0.0198  305 PHE B C     
5252 O O     . PHE B 305 ? 0.4646 0.5270 0.4501 -0.0216 0.0384  0.0200  305 PHE B O     
5253 C CB    . PHE B 305 ? 0.4491 0.4934 0.4342 -0.0176 0.0385  0.0148  305 PHE B CB    
5254 C CG    . PHE B 305 ? 0.3754 0.4166 0.3610 -0.0154 0.0392  0.0112  305 PHE B CG    
5255 C CD1   . PHE B 305 ? 0.3179 0.3622 0.3046 -0.0147 0.0403  0.0077  305 PHE B CD1   
5256 C CD2   . PHE B 305 ? 0.4087 0.4436 0.3935 -0.0140 0.0388  0.0113  305 PHE B CD2   
5257 C CE1   . PHE B 305 ? 0.3444 0.3854 0.3312 -0.0130 0.0409  0.0045  305 PHE B CE1   
5258 C CE2   . PHE B 305 ? 0.3657 0.3982 0.3510 -0.0123 0.0394  0.0082  305 PHE B CE2   
5259 C CZ    . PHE B 305 ? 0.3535 0.3888 0.3398 -0.0120 0.0404  0.0048  305 PHE B CZ    
5260 N N     . ASP B 306 ? 0.7076 0.7581 0.6908 -0.0208 0.0371  0.0232  306 ASP B N     
5261 C CA    . ASP B 306 ? 0.7652 0.8169 0.7475 -0.0233 0.0363  0.0272  306 ASP B CA    
5262 C C     . ASP B 306 ? 0.7313 0.7930 0.7143 -0.0241 0.0366  0.0287  306 ASP B C     
5263 O O     . ASP B 306 ? 0.8194 0.8859 0.8027 -0.0263 0.0363  0.0304  306 ASP B O     
5264 C CB    . ASP B 306 ? 0.8061 0.8494 0.7860 -0.0231 0.0354  0.0306  306 ASP B CB    
5265 C CG    . ASP B 306 ? 0.8672 0.9001 0.8459 -0.0228 0.0350  0.0297  306 ASP B CG    
5266 O OD1   . ASP B 306 ? 0.8879 0.9199 0.8678 -0.0221 0.0354  0.0264  306 ASP B OD1   
5267 O OD2   . ASP B 306 ? 0.8299 0.8550 0.8059 -0.0230 0.0343  0.0325  306 ASP B OD2   
5268 N N     . LYS B 307 ? 0.6692 0.7347 0.6523 -0.0225 0.0372  0.0280  307 LYS B N     
5269 C CA    . LYS B 307 ? 0.6830 0.7582 0.6666 -0.0233 0.0375  0.0295  307 LYS B CA    
5270 C C     . LYS B 307 ? 0.7435 0.8263 0.7284 -0.0237 0.0383  0.0266  307 LYS B C     
5271 O O     . LYS B 307 ? 0.8150 0.9064 0.8003 -0.0247 0.0386  0.0276  307 LYS B O     
5272 C CB    . LYS B 307 ? 0.6906 0.7685 0.6739 -0.0217 0.0378  0.0299  307 LYS B CB    
5273 C CG    . LYS B 307 ? 0.6771 0.7477 0.6588 -0.0206 0.0371  0.0331  307 LYS B CG    
5274 C CD    . LYS B 307 ? 0.7188 0.7935 0.7003 -0.0188 0.0374  0.0338  307 LYS B CD    
5275 C CE    . LYS B 307 ? 0.7718 0.8556 0.7534 -0.0200 0.0374  0.0369  307 LYS B CE    
5276 N NZ    . LYS B 307 ? 0.7474 0.8370 0.7290 -0.0184 0.0378  0.0374  307 LYS B NZ    
5277 N N     . ALA B 308 ? 0.6889 0.7689 0.6746 -0.0227 0.0390  0.0228  308 ALA B N     
5278 C CA    . ALA B 308 ? 0.6648 0.7511 0.6514 -0.0226 0.0400  0.0201  308 ALA B CA    
5279 C C     . ALA B 308 ? 0.6971 0.7822 0.6842 -0.0240 0.0396  0.0211  308 ALA B C     
5280 O O     . ALA B 308 ? 0.6412 0.7312 0.6292 -0.0236 0.0405  0.0191  308 ALA B O     
5281 C CB    . ALA B 308 ? 0.5938 0.6784 0.5805 -0.0205 0.0411  0.0153  308 ALA B CB    
5282 N N     . ASN B 309 ? 0.6644 0.7435 0.6508 -0.0256 0.0383  0.0243  309 ASN B N     
5283 C CA    . ASN B 309 ? 0.6483 0.7258 0.6350 -0.0274 0.0377  0.0254  309 ASN B CA    
5284 C C     . ASN B 309 ? 0.5294 0.6033 0.5169 -0.0261 0.0382  0.0221  309 ASN B C     
5285 O O     . ASN B 309 ? 0.5119 0.5898 0.5003 -0.0267 0.0385  0.0219  309 ASN B O     
5286 C CB    . ASN B 309 ? 0.7216 0.8084 0.7089 -0.0297 0.0376  0.0279  309 ASN B CB    
5287 C CG    . ASN B 309 ? 0.7515 0.8387 0.7376 -0.0322 0.0364  0.0326  309 ASN B CG    
5288 O OD1   . ASN B 309 ? 0.7776 0.8627 0.7629 -0.0350 0.0353  0.0357  309 ASN B OD1   
5289 N ND2   . ASN B 309 ? 0.7530 0.8430 0.7387 -0.0312 0.0367  0.0332  309 ASN B ND2   
5290 N N     . ILE B 310 ? 0.5034 0.5702 0.4906 -0.0240 0.0384  0.0198  310 ILE B N     
5291 C CA    . ILE B 310 ? 0.5037 0.5659 0.4915 -0.0227 0.0388  0.0170  310 ILE B CA    
5292 C C     . ILE B 310 ? 0.5010 0.5534 0.4876 -0.0236 0.0376  0.0184  310 ILE B C     
5293 O O     . ILE B 310 ? 0.5419 0.5884 0.5274 -0.0226 0.0373  0.0185  310 ILE B O     
5294 C CB    . ILE B 310 ? 0.5019 0.5635 0.4901 -0.0199 0.0401  0.0128  310 ILE B CB    
5295 C CG1   . ILE B 310 ? 0.4628 0.5332 0.4514 -0.0191 0.0414  0.0112  310 ILE B CG1   
5296 C CG2   . ILE B 310 ? 0.4643 0.5210 0.4531 -0.0185 0.0406  0.0102  310 ILE B CG2   
5297 C CD1   . ILE B 310 ? 0.5131 0.5826 0.5014 -0.0168 0.0427  0.0071  310 ILE B CD1   
5298 N N     . LYS B 311 ? 0.4058 0.4571 0.3924 -0.0255 0.0370  0.0196  311 LYS B N     
5299 C CA    . LYS B 311 ? 0.4730 0.5149 0.4581 -0.0267 0.0359  0.0206  311 LYS B CA    
5300 C C     . LYS B 311 ? 0.5260 0.5647 0.5122 -0.0248 0.0364  0.0173  311 LYS B C     
5301 O O     . LYS B 311 ? 0.4829 0.5262 0.4705 -0.0250 0.0369  0.0165  311 LYS B O     
5302 C CB    . LYS B 311 ? 0.4197 0.4620 0.4037 -0.0306 0.0346  0.0241  311 LYS B CB    
5303 C CG    . LYS B 311 ? 0.4657 0.4979 0.4476 -0.0320 0.0335  0.0248  311 LYS B CG    
5304 C CD    . LYS B 311 ? 0.4931 0.5250 0.4732 -0.0365 0.0322  0.0283  311 LYS B CD    
5305 C CE    . LYS B 311 ? 0.4276 0.4480 0.4046 -0.0380 0.0311  0.0289  311 LYS B CE    
5306 N NZ    . LYS B 311 ? 0.4324 0.4444 0.4078 -0.0351 0.0314  0.0281  311 LYS B NZ    
5307 N N     . LEU B 312 ? 0.4012 0.4327 0.3867 -0.0228 0.0365  0.0156  312 LEU B N     
5308 C CA    . LEU B 312 ? 0.3949 0.4234 0.3814 -0.0207 0.0372  0.0124  312 LEU B CA    
5309 C C     . LEU B 312 ? 0.4610 0.4833 0.4466 -0.0222 0.0362  0.0132  312 LEU B C     
5310 O O     . LEU B 312 ? 0.4996 0.5157 0.4830 -0.0239 0.0350  0.0153  312 LEU B O     
5311 C CB    . LEU B 312 ? 0.3482 0.3726 0.3346 -0.0180 0.0377  0.0104  312 LEU B CB    
5312 C CG    . LEU B 312 ? 0.2918 0.3222 0.2793 -0.0161 0.0390  0.0080  312 LEU B CG    
5313 C CD1   . LEU B 312 ? 0.2651 0.2911 0.2523 -0.0139 0.0394  0.0057  312 LEU B CD1   
5314 C CD2   . LEU B 312 ? 0.2640 0.2999 0.2529 -0.0157 0.0401  0.0061  312 LEU B CD2   
5315 N N     . ASN B 313 ? 0.5431 0.5671 0.5302 -0.0217 0.0367  0.0114  313 ASN B N     
5316 C CA    . ASN B 313 ? 0.4924 0.5113 0.4787 -0.0231 0.0358  0.0119  313 ASN B CA    
5317 C C     . ASN B 313 ? 0.4707 0.4818 0.4567 -0.0208 0.0359  0.0096  313 ASN B C     
5318 O O     . ASN B 313 ? 0.5036 0.5090 0.4883 -0.0220 0.0351  0.0099  313 ASN B O     
5319 C CB    . ASN B 313 ? 0.4329 0.4584 0.4210 -0.0240 0.0361  0.0118  313 ASN B CB    
5320 C CG    . ASN B 313 ? 0.4623 0.4921 0.4527 -0.0205 0.0379  0.0088  313 ASN B CG    
5321 O OD1   . ASN B 313 ? 0.5513 0.5771 0.5419 -0.0178 0.0386  0.0063  313 ASN B OD1   
5322 N ND2   . ASN B 313 ? 0.4130 0.4509 0.4048 -0.0206 0.0386  0.0091  313 ASN B ND2   
5323 N N     . TYR B 314 ? 0.4009 0.4118 0.3877 -0.0179 0.0369  0.0074  314 TYR B N     
5324 C CA    . TYR B 314 ? 0.4440 0.4481 0.4304 -0.0157 0.0370  0.0054  314 TYR B CA    
5325 C C     . TYR B 314 ? 0.4096 0.4116 0.3968 -0.0154 0.0371  0.0041  314 TYR B C     
5326 O O     . TYR B 314 ? 0.4537 0.4489 0.4396 -0.0154 0.0364  0.0040  314 TYR B O     
5327 C CB    . TYR B 314 ? 0.5198 0.5165 0.5036 -0.0161 0.0360  0.0071  314 TYR B CB    
5328 C CG    . TYR B 314 ? 0.4868 0.4853 0.4697 -0.0163 0.0359  0.0090  314 TYR B CG    
5329 C CD1   . TYR B 314 ? 0.4680 0.4688 0.4516 -0.0141 0.0367  0.0079  314 TYR B CD1   
5330 C CD2   . TYR B 314 ? 0.4999 0.4977 0.4809 -0.0190 0.0350  0.0122  314 TYR B CD2   
5331 C CE1   . TYR B 314 ? 0.4861 0.4891 0.4688 -0.0143 0.0366  0.0098  314 TYR B CE1   
5332 C CE2   . TYR B 314 ? 0.4662 0.4656 0.4463 -0.0191 0.0349  0.0142  314 TYR B CE2   
5333 C CZ    . TYR B 314 ? 0.5580 0.5603 0.5390 -0.0166 0.0357  0.0130  314 TYR B CZ    
5334 O OH    . TYR B 314 ? 0.6686 0.6735 0.6489 -0.0167 0.0357  0.0152  314 TYR B OH    
5335 N N     . GLY B 315 ? 0.4648 0.4727 0.4538 -0.0152 0.0378  0.0033  315 GLY B N     
5336 C CA    . GLY B 315 ? 0.5255 0.5325 0.5155 -0.0148 0.0380  0.0023  315 GLY B CA    
5337 C C     . GLY B 315 ? 0.6192 0.6248 0.6082 -0.0177 0.0367  0.0042  315 GLY B C     
5338 O O     . GLY B 315 ? 0.6748 0.6789 0.6643 -0.0174 0.0367  0.0034  315 GLY B O     
5339 N N     . VAL B 316 ? 0.4082 0.4142 0.3956 -0.0208 0.0357  0.0068  316 VAL B N     
5340 C CA    . VAL B 316 ? 0.3980 0.4017 0.3838 -0.0241 0.0344  0.0085  316 VAL B CA    
5341 C C     . VAL B 316 ? 0.4343 0.4465 0.4220 -0.0252 0.0347  0.0092  316 VAL B C     
5342 O O     . VAL B 316 ? 0.4257 0.4451 0.4142 -0.0263 0.0349  0.0107  316 VAL B O     
5343 C CB    . VAL B 316 ? 0.3378 0.3367 0.3203 -0.0273 0.0330  0.0111  316 VAL B CB    
5344 C CG1   . VAL B 316 ? 0.2970 0.2941 0.2776 -0.0314 0.0317  0.0128  316 VAL B CG1   
5345 C CG2   . VAL B 316 ? 0.2997 0.2897 0.2803 -0.0254 0.0329  0.0103  316 VAL B CG2   
5346 N N     . LEU B 317 ? 0.3999 0.4119 0.3885 -0.0248 0.0347  0.0083  317 LEU B N     
5347 C CA    . LEU B 317 ? 0.3434 0.3641 0.3340 -0.0253 0.0352  0.0091  317 LEU B CA    
5348 C C     . LEU B 317 ? 0.3812 0.4034 0.3702 -0.0300 0.0336  0.0117  317 LEU B C     
5349 O O     . LEU B 317 ? 0.3379 0.3530 0.3239 -0.0330 0.0322  0.0126  317 LEU B O     
5350 C CB    . LEU B 317 ? 0.3474 0.3679 0.3399 -0.0218 0.0363  0.0067  317 LEU B CB    
5351 C CG    . LEU B 317 ? 0.3346 0.3539 0.3286 -0.0173 0.0380  0.0040  317 LEU B CG    
5352 C CD1   . LEU B 317 ? 0.2595 0.2768 0.2546 -0.0149 0.0387  0.0022  317 LEU B CD1   
5353 C CD2   . LEU B 317 ? 0.3618 0.3892 0.3573 -0.0156 0.0394  0.0039  317 LEU B CD2   
5354 N N     . ASP B 318 ? 0.6500 0.6818 0.6409 -0.0308 0.0339  0.0130  318 ASP B N     
5355 C CA    . ASP B 318 ? 0.7189 0.7537 0.7084 -0.0357 0.0325  0.0157  318 ASP B CA    
5356 C C     . ASP B 318 ? 0.7496 0.7788 0.7376 -0.0374 0.0315  0.0151  318 ASP B C     
5357 O O     . ASP B 318 ? 0.7741 0.7986 0.7590 -0.0419 0.0298  0.0165  318 ASP B O     
5358 C CB    . ASP B 318 ? 0.8201 0.8679 0.8124 -0.0354 0.0333  0.0171  318 ASP B CB    
5359 C CG    . ASP B 318 ? 0.9586 1.0135 0.9519 -0.0350 0.0339  0.0184  318 ASP B CG    
5360 O OD1   . ASP B 318 ? 0.9906 1.0406 0.9820 -0.0364 0.0333  0.0188  318 ASP B OD1   
5361 O OD2   . ASP B 318 ? 0.9926 1.0578 0.9882 -0.0332 0.0351  0.0191  318 ASP B OD2   
5362 N N     . ASP B 319 ? 0.6331 0.6621 0.6231 -0.0338 0.0325  0.0131  319 ASP B N     
5363 C CA    . ASP B 319 ? 0.6548 0.6798 0.6438 -0.0349 0.0318  0.0125  319 ASP B CA    
5364 C C     . ASP B 319 ? 0.6829 0.7000 0.6723 -0.0307 0.0326  0.0095  319 ASP B C     
5365 O O     . ASP B 319 ? 0.7133 0.7324 0.7051 -0.0264 0.0342  0.0079  319 ASP B O     
5366 C CB    . ASP B 319 ? 0.6780 0.7136 0.6697 -0.0345 0.0324  0.0135  319 ASP B CB    
5367 C CG    . ASP B 319 ? 0.7890 0.8224 0.7805 -0.0349 0.0319  0.0128  319 ASP B CG    
5368 O OD1   . ASP B 319 ? 0.8631 0.8946 0.8564 -0.0306 0.0331  0.0107  319 ASP B OD1   
5369 O OD2   . ASP B 319 ? 0.8362 0.8703 0.8256 -0.0398 0.0303  0.0145  319 ASP B OD2   
5370 N N     . THR B 320 ? 0.5133 0.5213 0.4999 -0.0321 0.0315  0.0087  320 THR B N     
5371 C CA    . THR B 320 ? 0.4640 0.4652 0.4509 -0.0284 0.0322  0.0061  320 THR B CA    
5372 C C     . THR B 320 ? 0.4907 0.4912 0.4773 -0.0294 0.0317  0.0057  320 THR B C     
5373 O O     . THR B 320 ? 0.5368 0.5306 0.5227 -0.0275 0.0318  0.0039  320 THR B O     
5374 C CB    . THR B 320 ? 0.5031 0.4939 0.4869 -0.0285 0.0316  0.0054  320 THR B CB    
5375 O OG1   . THR B 320 ? 0.5065 0.4931 0.4863 -0.0333 0.0300  0.0072  320 THR B OG1   
5376 C CG2   . THR B 320 ? 0.4605 0.4522 0.4453 -0.0261 0.0325  0.0051  320 THR B CG2   
5377 N N     . HIS B 321 ? 0.4938 0.5015 0.4809 -0.0324 0.0311  0.0076  321 HIS B N     
5378 C CA    . HIS B 321 ? 0.5643 0.5721 0.5507 -0.0341 0.0304  0.0076  321 HIS B CA    
5379 C C     . HIS B 321 ? 0.4739 0.4820 0.4628 -0.0300 0.0315  0.0058  321 HIS B C     
5380 O O     . HIS B 321 ? 0.3912 0.3931 0.3784 -0.0303 0.0309  0.0046  321 HIS B O     
5381 C CB    . HIS B 321 ? 0.5764 0.5939 0.5631 -0.0383 0.0296  0.0103  321 HIS B CB    
5382 C CG    . HIS B 321 ? 0.6803 0.6978 0.6653 -0.0416 0.0284  0.0107  321 HIS B CG    
5383 N ND1   . HIS B 321 ? 0.7024 0.7113 0.6827 -0.0461 0.0267  0.0106  321 HIS B ND1   
5384 C CD2   . HIS B 321 ? 0.7391 0.7645 0.7264 -0.0413 0.0287  0.0114  321 HIS B CD2   
5385 C CE1   . HIS B 321 ? 0.7462 0.7574 0.7257 -0.0486 0.0260  0.0109  321 HIS B CE1   
5386 N NE2   . HIS B 321 ? 0.7860 0.8078 0.7700 -0.0457 0.0271  0.0115  321 HIS B NE2   
5387 N N     . ALA B 322 ? 0.3308 0.3463 0.3235 -0.0263 0.0331  0.0057  322 ALA B N     
5388 C CA    . ALA B 322 ? 0.3235 0.3392 0.3185 -0.0222 0.0343  0.0042  322 ALA B CA    
5389 C C     . ALA B 322 ? 0.4276 0.4329 0.4213 -0.0200 0.0344  0.0017  322 ALA B C     
5390 O O     . ALA B 322 ? 0.5062 0.5087 0.5001 -0.0188 0.0344  0.0006  322 ALA B O     
5391 C CB    . ALA B 322 ? 0.2583 0.2815 0.2568 -0.0179 0.0363  0.0042  322 ALA B CB    
5392 N N     . GLU B 323 ? 0.4214 0.4216 0.4140 -0.0192 0.0345  0.0008  323 GLU B N     
5393 C CA    . GLU B 323 ? 0.3361 0.3274 0.3277 -0.0170 0.0346  -0.0013 323 GLU B CA    
5394 C C     . GLU B 323 ? 0.3538 0.3373 0.3414 -0.0201 0.0330  -0.0012 323 GLU B C     
5395 O O     . GLU B 323 ? 0.5280 0.5056 0.5147 -0.0186 0.0329  -0.0027 323 GLU B O     
5396 C CB    . GLU B 323 ? 0.3079 0.2973 0.2999 -0.0146 0.0355  -0.0022 323 GLU B CB    
5397 C CG    . GLU B 323 ? 0.4186 0.4086 0.4090 -0.0171 0.0348  -0.0007 323 GLU B CG    
5398 C CD    . GLU B 323 ? 0.4664 0.4656 0.4592 -0.0167 0.0358  0.0003  323 GLU B CD    
5399 O OE1   . GLU B 323 ? 0.4877 0.4939 0.4815 -0.0182 0.0357  0.0019  323 GLU B OE1   
5400 O OE2   . GLU B 323 ? 0.3843 0.3838 0.3777 -0.0147 0.0367  -0.0004 323 GLU B OE2   
5401 N N     . PHE B 324 ? 0.3044 0.2879 0.2895 -0.0244 0.0317  0.0005  324 PHE B N     
5402 C CA    . PHE B 324 ? 0.3422 0.3177 0.3228 -0.0276 0.0302  0.0006  324 PHE B CA    
5403 C C     . PHE B 324 ? 0.4178 0.3936 0.3981 -0.0284 0.0298  0.0000  324 PHE B C     
5404 O O     . PHE B 324 ? 0.5289 0.4973 0.5071 -0.0275 0.0295  -0.0015 324 PHE B O     
5405 C CB    . PHE B 324 ? 0.3186 0.2946 0.2964 -0.0326 0.0290  0.0027  324 PHE B CB    
5406 C CG    . PHE B 324 ? 0.4204 0.3857 0.3925 -0.0356 0.0277  0.0028  324 PHE B CG    
5407 C CD1   . PHE B 324 ? 0.3625 0.3201 0.3325 -0.0340 0.0278  0.0024  324 PHE B CD1   
5408 C CD2   . PHE B 324 ? 0.4921 0.4554 0.4608 -0.0402 0.0263  0.0033  324 PHE B CD2   
5409 C CE1   . PHE B 324 ? 0.3733 0.3205 0.3376 -0.0364 0.0268  0.0025  324 PHE B CE1   
5410 C CE2   . PHE B 324 ? 0.4919 0.4443 0.4546 -0.0431 0.0252  0.0032  324 PHE B CE2   
5411 C CZ    . PHE B 324 ? 0.4375 0.3816 0.3979 -0.0410 0.0256  0.0029  324 PHE B CZ    
5412 N N     . ARG B 325 ? 0.5338 0.5189 0.5166 -0.0296 0.0299  0.0013  325 ARG B N     
5413 C CA    . ARG B 325 ? 0.5989 0.5857 0.5817 -0.0305 0.0295  0.0010  325 ARG B CA    
5414 C C     . ARG B 325 ? 0.5746 0.5596 0.5597 -0.0256 0.0306  -0.0009 325 ARG B C     
5415 O O     . ARG B 325 ? 0.5727 0.5545 0.5565 -0.0259 0.0301  -0.0018 325 ARG B O     
5416 C CB    . ARG B 325 ? 0.6102 0.6086 0.5954 -0.0325 0.0294  0.0032  325 ARG B CB    
5417 C CG    . ARG B 325 ? 0.6719 0.6715 0.6535 -0.0390 0.0277  0.0051  325 ARG B CG    
5418 C CD    . ARG B 325 ? 0.7356 0.7297 0.7135 -0.0421 0.0263  0.0042  325 ARG B CD    
5419 N NE    . ARG B 325 ? 0.8014 0.8016 0.7820 -0.0405 0.0268  0.0041  325 ARG B NE    
5420 C CZ    . ARG B 325 ? 0.8491 0.8460 0.8313 -0.0360 0.0278  0.0022  325 ARG B CZ    
5421 N NH1   . ARG B 325 ? 0.8323 0.8203 0.8138 -0.0329 0.0283  0.0003  325 ARG B NH1   
5422 N NH2   . ARG B 325 ? 0.8642 0.8672 0.8489 -0.0347 0.0282  0.0024  325 ARG B NH2   
5423 N N     . LYS B 326 ? 0.4535 0.4397 0.4417 -0.0213 0.0321  -0.0017 326 LYS B N     
5424 C CA    . LYS B 326 ? 0.4938 0.4783 0.4840 -0.0171 0.0332  -0.0034 326 LYS B CA    
5425 C C     . LYS B 326 ? 0.5078 0.4825 0.4953 -0.0161 0.0328  -0.0051 326 LYS B C     
5426 O O     . LYS B 326 ? 0.4637 0.4358 0.4514 -0.0144 0.0329  -0.0063 326 LYS B O     
5427 C CB    . LYS B 326 ? 0.4808 0.4704 0.4748 -0.0131 0.0350  -0.0037 326 LYS B CB    
5428 C CG    . LYS B 326 ? 0.4500 0.4494 0.4468 -0.0128 0.0357  -0.0021 326 LYS B CG    
5429 C CD    . LYS B 326 ? 0.4784 0.4808 0.4783 -0.0082 0.0377  -0.0028 326 LYS B CD    
5430 C CE    . LYS B 326 ? 0.5473 0.5440 0.5477 -0.0050 0.0384  -0.0047 326 LYS B CE    
5431 N NZ    . LYS B 326 ? 0.6217 0.6213 0.6249 -0.0008 0.0404  -0.0052 326 LYS B NZ    
5432 N N     . ALA B 327 ? 0.5014 0.4710 0.4865 -0.0170 0.0323  -0.0051 327 ALA B N     
5433 C CA    . ALA B 327 ? 0.5036 0.4639 0.4856 -0.0161 0.0319  -0.0064 327 ALA B CA    
5434 C C     . ALA B 327 ? 0.5500 0.5053 0.5282 -0.0190 0.0307  -0.0065 327 ALA B C     
5435 O O     . ALA B 327 ? 0.4836 0.4325 0.4598 -0.0175 0.0305  -0.0078 327 ALA B O     
5436 C CB    . ALA B 327 ? 0.4837 0.4405 0.4640 -0.0165 0.0318  -0.0059 327 ALA B CB    
5437 N N     . GLN B 328 ? 0.6870 0.6452 0.6637 -0.0233 0.0297  -0.0051 328 GLN B N     
5438 C CA    . GLN B 328 ? 0.6525 0.6066 0.6253 -0.0267 0.0284  -0.0053 328 GLN B CA    
5439 C C     . GLN B 328 ? 0.6969 0.6531 0.6712 -0.0252 0.0286  -0.0064 328 GLN B C     
5440 O O     . GLN B 328 ? 0.6699 0.6196 0.6408 -0.0257 0.0281  -0.0075 328 GLN B O     
5441 C CB    . GLN B 328 ? 0.7057 0.6649 0.6774 -0.0319 0.0274  -0.0034 328 GLN B CB    
5442 C CG    . GLN B 328 ? 0.8402 0.7943 0.8081 -0.0349 0.0266  -0.0023 328 GLN B CG    
5443 C CD    . GLN B 328 ? 0.8748 0.8339 0.8413 -0.0406 0.0255  -0.0003 328 GLN B CD    
5444 O OE1   . GLN B 328 ? 0.9468 0.9148 0.9158 -0.0419 0.0254  0.0006  328 GLN B OE1   
5445 N NE2   . GLN B 328 ? 0.7792 0.7330 0.7416 -0.0441 0.0246  0.0007  328 GLN B NE2   
5446 N N     . ASP B 329 ? 0.6267 0.5915 0.6059 -0.0230 0.0296  -0.0059 329 ASP B N     
5447 C CA    . ASP B 329 ? 0.5458 0.5132 0.5269 -0.0211 0.0300  -0.0066 329 ASP B CA    
5448 C C     . ASP B 329 ? 0.5248 0.4860 0.5060 -0.0170 0.0307  -0.0085 329 ASP B C     
5449 O O     . ASP B 329 ? 0.6053 0.5645 0.5858 -0.0163 0.0305  -0.0095 329 ASP B O     
5450 C CB    . ASP B 329 ? 0.5309 0.5087 0.5170 -0.0193 0.0311  -0.0054 329 ASP B CB    
5451 C CG    . ASP B 329 ? 0.6459 0.6316 0.6322 -0.0232 0.0304  -0.0034 329 ASP B CG    
5452 O OD1   . ASP B 329 ? 0.6198 0.6049 0.6036 -0.0264 0.0292  -0.0033 329 ASP B OD1   
5453 O OD2   . ASP B 329 ? 0.6984 0.6912 0.6872 -0.0230 0.0310  -0.0019 329 ASP B OD2   
5454 N N     . TYR B 330 ? 0.3501 0.3089 0.3323 -0.0144 0.0315  -0.0090 330 TYR B N     
5455 C CA    . TYR B 330 ? 0.3501 0.3040 0.3325 -0.0106 0.0321  -0.0105 330 TYR B CA    
5456 C C     . TYR B 330 ? 0.3516 0.2968 0.3294 -0.0112 0.0313  -0.0114 330 TYR B C     
5457 O O     . TYR B 330 ? 0.3613 0.3032 0.3385 -0.0091 0.0315  -0.0126 330 TYR B O     
5458 C CB    . TYR B 330 ? 0.4218 0.3764 0.4062 -0.0085 0.0330  -0.0105 330 TYR B CB    
5459 C CG    . TYR B 330 ? 0.4296 0.3805 0.4146 -0.0048 0.0338  -0.0117 330 TYR B CG    
5460 C CD1   . TYR B 330 ? 0.3859 0.3394 0.3739 -0.0020 0.0347  -0.0125 330 TYR B CD1   
5461 C CD2   . TYR B 330 ? 0.4177 0.3633 0.4004 -0.0042 0.0337  -0.0119 330 TYR B CD2   
5462 C CE1   . TYR B 330 ? 0.3496 0.3004 0.3382 0.0010  0.0353  -0.0134 330 TYR B CE1   
5463 C CE2   . TYR B 330 ? 0.3993 0.3429 0.3828 -0.0010 0.0343  -0.0128 330 TYR B CE2   
5464 C CZ    . TYR B 330 ? 0.4098 0.3561 0.3962 0.0014  0.0351  -0.0136 330 TYR B CZ    
5465 O OH    . TYR B 330 ? 0.4113 0.3559 0.3983 0.0042  0.0357  -0.0144 330 TYR B OH    
5466 N N     . VAL B 331 ? 0.3835 0.3245 0.3575 -0.0142 0.0305  -0.0108 331 VAL B N     
5467 C CA    . VAL B 331 ? 0.4554 0.3871 0.4243 -0.0146 0.0298  -0.0116 331 VAL B CA    
5468 C C     . VAL B 331 ? 0.5095 0.4395 0.4758 -0.0166 0.0290  -0.0122 331 VAL B C     
5469 O O     . VAL B 331 ? 0.4995 0.4239 0.4633 -0.0149 0.0291  -0.0136 331 VAL B O     
5470 C CB    . VAL B 331 ? 0.4248 0.3521 0.3901 -0.0172 0.0292  -0.0105 331 VAL B CB    
5471 C CG1   . VAL B 331 ? 0.5497 0.4663 0.5087 -0.0179 0.0286  -0.0113 331 VAL B CG1   
5472 C CG2   . VAL B 331 ? 0.3353 0.2638 0.3029 -0.0146 0.0301  -0.0100 331 VAL B CG2   
5473 N N     . PHE B 332 ? 0.5110 0.4467 0.4779 -0.0202 0.0284  -0.0113 332 PHE B N     
5474 C CA    . PHE B 332 ? 0.5142 0.4496 0.4788 -0.0227 0.0276  -0.0118 332 PHE B CA    
5475 C C     . PHE B 332 ? 0.4405 0.3775 0.4075 -0.0191 0.0283  -0.0130 332 PHE B C     
5476 O O     . PHE B 332 ? 0.5217 0.4531 0.4853 -0.0189 0.0279  -0.0143 332 PHE B O     
5477 C CB    . PHE B 332 ? 0.5605 0.5045 0.5268 -0.0268 0.0270  -0.0101 332 PHE B CB    
5478 C CG    . PHE B 332 ? 0.5839 0.5295 0.5480 -0.0301 0.0260  -0.0103 332 PHE B CG    
5479 C CD1   . PHE B 332 ? 0.6611 0.6008 0.6191 -0.0351 0.0247  -0.0105 332 PHE B CD1   
5480 C CD2   . PHE B 332 ? 0.6122 0.5653 0.5802 -0.0285 0.0264  -0.0102 332 PHE B CD2   
5481 C CE1   . PHE B 332 ? 0.7448 0.6862 0.7005 -0.0387 0.0237  -0.0107 332 PHE B CE1   
5482 C CE2   . PHE B 332 ? 0.7065 0.6619 0.6726 -0.0317 0.0255  -0.0102 332 PHE B CE2   
5483 C CZ    . PHE B 332 ? 0.7547 0.7044 0.7146 -0.0370 0.0241  -0.0105 332 PHE B CZ    
5484 N N     . GLY B 333 ? 0.5235 0.4679 0.4962 -0.0162 0.0293  -0.0125 333 GLY B N     
5485 C CA    . GLY B 333 ? 0.5364 0.4829 0.5117 -0.0130 0.0299  -0.0133 333 GLY B CA    
5486 C C     . GLY B 333 ? 0.5859 0.5261 0.5602 -0.0093 0.0305  -0.0147 333 GLY B C     
5487 O O     . GLY B 333 ? 0.6839 0.6254 0.6598 -0.0069 0.0309  -0.0154 333 GLY B O     
5488 N N     . LEU B 334 ? 0.5038 0.4379 0.4757 -0.0086 0.0305  -0.0150 334 LEU B N     
5489 C CA    . LEU B 334 ? 0.5618 0.4911 0.5329 -0.0049 0.0311  -0.0160 334 LEU B CA    
5490 C C     . LEU B 334 ? 0.6545 0.5754 0.6197 -0.0056 0.0304  -0.0170 334 LEU B C     
5491 O O     . LEU B 334 ? 0.7171 0.6344 0.6810 -0.0027 0.0307  -0.0180 334 LEU B O     
5492 C CB    . LEU B 334 ? 0.6383 0.5666 0.6104 -0.0032 0.0316  -0.0156 334 LEU B CB    
5493 C CG    . LEU B 334 ? 0.6422 0.5773 0.6198 -0.0012 0.0327  -0.0151 334 LEU B CG    
5494 C CD1   . LEU B 334 ? 0.7037 0.6367 0.6814 0.0009  0.0332  -0.0150 334 LEU B CD1   
5495 C CD2   . LEU B 334 ? 0.5966 0.5353 0.5773 0.0011  0.0332  -0.0157 334 LEU B CD2   
5496 N N     . THR B 335 ? 0.6097 0.5270 0.5709 -0.0095 0.0295  -0.0167 335 THR B N     
5497 C CA    . THR B 335 ? 0.5546 0.4626 0.5092 -0.0105 0.0289  -0.0177 335 THR B CA    
5498 C C     . THR B 335 ? 0.5968 0.5053 0.5496 -0.0124 0.0283  -0.0187 335 THR B C     
5499 O O     . THR B 335 ? 0.6246 0.5262 0.5727 -0.0116 0.0282  -0.0200 335 THR B O     
5500 C CB    . THR B 335 ? 0.4885 0.3916 0.4389 -0.0143 0.0282  -0.0168 335 THR B CB    
5501 O OG1   . THR B 335 ? 0.5828 0.4935 0.5361 -0.0180 0.0277  -0.0155 335 THR B OG1   
5502 C CG2   . THR B 335 ? 0.5032 0.4032 0.4537 -0.0117 0.0289  -0.0161 335 THR B CG2   
5503 N N     . ILE B 336 ? 0.5032 0.4202 0.4596 -0.0146 0.0280  -0.0179 336 ILE B N     
5504 C CA    . ILE B 336 ? 0.5904 0.5093 0.5457 -0.0162 0.0274  -0.0187 336 ILE B CA    
5505 C C     . ILE B 336 ? 0.6353 0.5565 0.5938 -0.0115 0.0283  -0.0194 336 ILE B C     
5506 O O     . ILE B 336 ? 0.6952 0.6145 0.6514 -0.0113 0.0281  -0.0206 336 ILE B O     
5507 C CB    . ILE B 336 ? 0.6066 0.5345 0.5647 -0.0199 0.0268  -0.0173 336 ILE B CB    
5508 C CG1   . ILE B 336 ? 0.6498 0.5762 0.6049 -0.0247 0.0259  -0.0163 336 ILE B CG1   
5509 C CG2   . ILE B 336 ? 0.5999 0.5291 0.5557 -0.0224 0.0261  -0.0181 336 ILE B CG2   
5510 C CD1   . ILE B 336 ? 0.7264 0.6501 0.6760 -0.0301 0.0246  -0.0168 336 ILE B CD1   
5511 N N     . GLN B 337 ? 0.6767 0.6018 0.6403 -0.0079 0.0293  -0.0188 337 GLN B N     
5512 C CA    . GLN B 337 ? 0.6223 0.5494 0.5890 -0.0036 0.0302  -0.0193 337 GLN B CA    
5513 C C     . GLN B 337 ? 0.6360 0.5552 0.5987 -0.0009 0.0304  -0.0205 337 GLN B C     
5514 O O     . GLN B 337 ? 0.6650 0.5846 0.6283 0.0018  0.0308  -0.0212 337 GLN B O     
5515 C CB    . GLN B 337 ? 0.5285 0.4615 0.5011 -0.0012 0.0312  -0.0182 337 GLN B CB    
5516 C CG    . GLN B 337 ? 0.5513 0.4850 0.5266 0.0031  0.0321  -0.0186 337 GLN B CG    
5517 C CD    . GLN B 337 ? 0.6684 0.6096 0.6489 0.0043  0.0328  -0.0179 337 GLN B CD    
5518 O OE1   . GLN B 337 ? 0.6559 0.6015 0.6374 0.0024  0.0324  -0.0174 337 GLN B OE1   
5519 N NE2   . GLN B 337 ? 0.6573 0.6002 0.6411 0.0073  0.0337  -0.0178 337 GLN B NE2   
5520 N N     . SER B 338 ? 0.6157 0.5276 0.5740 -0.0016 0.0302  -0.0207 338 SER B N     
5521 C CA    . SER B 338 ? 0.5268 0.4308 0.4807 0.0013  0.0305  -0.0216 338 SER B CA    
5522 C C     . SER B 338 ? 0.5433 0.4417 0.4915 -0.0003 0.0299  -0.0231 338 SER B C     
5523 O O     . SER B 338 ? 0.5325 0.4267 0.4779 0.0028  0.0303  -0.0241 338 SER B O     
5524 C CB    . SER B 338 ? 0.4496 0.3481 0.4009 0.0012  0.0306  -0.0210 338 SER B CB    
5525 O OG    . SER B 338 ? 0.4627 0.3564 0.4121 0.0055  0.0314  -0.0213 338 SER B OG    
5526 N N     . ALA B 339 ? 0.5407 0.4393 0.4869 -0.0051 0.0290  -0.0231 339 ALA B N     
5527 C CA    . ALA B 339 ? 0.4710 0.3646 0.4114 -0.0073 0.0283  -0.0246 339 ALA B CA    
5528 C C     . ALA B 339 ? 0.5058 0.4068 0.4499 -0.0064 0.0283  -0.0249 339 ALA B C     
5529 O O     . ALA B 339 ? 0.5306 0.4284 0.4712 -0.0056 0.0283  -0.0263 339 ALA B O     
5530 C CB    . ALA B 339 ? 0.4109 0.3031 0.3480 -0.0133 0.0271  -0.0243 339 ALA B CB    
5531 N N     . MET B 340 ? 0.6228 0.5337 0.5737 -0.0065 0.0285  -0.0235 340 MET B N     
5532 C CA    . MET B 340 ? 0.5910 0.5092 0.5460 -0.0050 0.0287  -0.0234 340 MET B CA    
5533 C C     . MET B 340 ? 0.6017 0.5180 0.5572 0.0001  0.0296  -0.0241 340 MET B C     
5534 O O     . MET B 340 ? 0.5944 0.5108 0.5486 0.0012  0.0296  -0.0251 340 MET B O     
5535 C CB    . MET B 340 ? 0.5041 0.4322 0.4661 -0.0051 0.0291  -0.0216 340 MET B CB    
5536 C CG    . MET B 340 ? 0.5570 0.4928 0.5228 -0.0044 0.0292  -0.0212 340 MET B CG    
5537 S SD    . MET B 340 ? 0.5460 0.4845 0.5165 0.0013  0.0305  -0.0210 340 MET B SD    
5538 C CE    . MET B 340 ? 0.5583 0.5027 0.5350 0.0020  0.0313  -0.0192 340 MET B CE    
5539 N N     . HIS B 341 ? 0.4448 0.3598 0.4022 0.0032  0.0304  -0.0236 341 HIS B N     
5540 C CA    . HIS B 341 ? 0.4259 0.3395 0.3836 0.0079  0.0312  -0.0241 341 HIS B CA    
5541 C C     . HIS B 341 ? 0.3857 0.2906 0.3363 0.0089  0.0311  -0.0257 341 HIS B C     
5542 O O     . HIS B 341 ? 0.3649 0.2701 0.3151 0.0119  0.0315  -0.0264 341 HIS B O     
5543 C CB    . HIS B 341 ? 0.2897 0.2039 0.2503 0.0104  0.0319  -0.0231 341 HIS B CB    
5544 C CG    . HIS B 341 ? 0.2813 0.2038 0.2487 0.0104  0.0323  -0.0219 341 HIS B CG    
5545 N ND1   . HIS B 341 ? 0.3021 0.2264 0.2726 0.0117  0.0329  -0.0210 341 HIS B ND1   
5546 C CD2   . HIS B 341 ? 0.2969 0.2262 0.2682 0.0093  0.0323  -0.0213 341 HIS B CD2   
5547 C CE1   . HIS B 341 ? 0.4181 0.3492 0.3938 0.0114  0.0333  -0.0202 341 HIS B CE1   
5548 N NE2   . HIS B 341 ? 0.3813 0.3156 0.3577 0.0102  0.0329  -0.0202 341 HIS B NE2   
5549 N N     . HIS B 342 ? 0.4850 0.3820 0.4299 0.0065  0.0306  -0.0263 342 HIS B N     
5550 C CA    . HIS B 342 ? 0.5298 0.4174 0.4673 0.0079  0.0308  -0.0279 342 HIS B CA    
5551 C C     . HIS B 342 ? 0.5029 0.3907 0.4377 0.0065  0.0303  -0.0294 342 HIS B C     
5552 O O     . HIS B 342 ? 0.4598 0.3450 0.3920 0.0099  0.0308  -0.0305 342 HIS B O     
5553 C CB    . HIS B 342 ? 0.5751 0.4533 0.5064 0.0054  0.0304  -0.0281 342 HIS B CB    
5554 C CG    . HIS B 342 ? 0.6481 0.5154 0.5708 0.0061  0.0306  -0.0299 342 HIS B CG    
5555 N ND1   . HIS B 342 ? 0.6601 0.5202 0.5760 0.0015  0.0297  -0.0311 342 HIS B ND1   
5556 C CD2   . HIS B 342 ? 0.6472 0.5094 0.5663 0.0111  0.0315  -0.0308 342 HIS B CD2   
5557 C CE1   . HIS B 342 ? 0.6293 0.4795 0.5377 0.0035  0.0302  -0.0328 342 HIS B CE1   
5558 N NE2   . HIS B 342 ? 0.6636 0.5150 0.5739 0.0096  0.0314  -0.0325 342 HIS B NE2   
5559 N N     . GLU B 343 ? 0.3808 0.2719 0.3159 0.0016  0.0293  -0.0294 343 GLU B N     
5560 C CA    . GLU B 343 ? 0.5557 0.4480 0.4884 0.0000  0.0288  -0.0307 343 GLU B CA    
5561 C C     . GLU B 343 ? 0.6794 0.5795 0.6174 0.0038  0.0294  -0.0303 343 GLU B C     
5562 O O     . GLU B 343 ? 0.7124 0.6110 0.6474 0.0052  0.0295  -0.0317 343 GLU B O     
5563 C CB    . GLU B 343 ? 0.5640 0.4609 0.4973 -0.0059 0.0276  -0.0302 343 GLU B CB    
5564 C CG    . GLU B 343 ? 0.6043 0.5044 0.5361 -0.0075 0.0271  -0.0313 343 GLU B CG    
5565 C CD    . GLU B 343 ? 0.6468 0.5535 0.5798 -0.0131 0.0260  -0.0305 343 GLU B CD    
5566 O OE1   . GLU B 343 ? 0.7370 0.6464 0.6726 -0.0155 0.0257  -0.0290 343 GLU B OE1   
5567 O OE2   . GLU B 343 ? 0.5904 0.5003 0.5219 -0.0151 0.0254  -0.0313 343 GLU B OE2   
5568 N N     . LEU B 344 ? 0.5339 0.4422 0.4794 0.0052  0.0298  -0.0285 344 LEU B N     
5569 C CA    . LEU B 344 ? 0.4463 0.3623 0.3972 0.0083  0.0303  -0.0279 344 LEU B CA    
5570 C C     . LEU B 344 ? 0.4320 0.3442 0.3807 0.0131  0.0311  -0.0287 344 LEU B C     
5571 O O     . LEU B 344 ? 0.3899 0.3040 0.3378 0.0145  0.0312  -0.0294 344 LEU B O     
5572 C CB    . LEU B 344 ? 0.3961 0.3193 0.3544 0.0091  0.0308  -0.0259 344 LEU B CB    
5573 C CG    . LEU B 344 ? 0.4206 0.3507 0.3845 0.0125  0.0315  -0.0249 344 LEU B CG    
5574 C CD1   . LEU B 344 ? 0.4163 0.3516 0.3809 0.0117  0.0312  -0.0251 344 LEU B CD1   
5575 C CD2   . LEU B 344 ? 0.3851 0.3207 0.3551 0.0127  0.0320  -0.0232 344 LEU B CD2   
5576 N N     . GLN B 345 ? 0.5640 0.4721 0.5120 0.0158  0.0317  -0.0284 345 GLN B N     
5577 C CA    . GLN B 345 ? 0.6161 0.5213 0.5620 0.0205  0.0325  -0.0289 345 GLN B CA    
5578 C C     . GLN B 345 ? 0.6234 0.5208 0.5614 0.0208  0.0325  -0.0310 345 GLN B C     
5579 O O     . GLN B 345 ? 0.6343 0.5319 0.5709 0.0243  0.0330  -0.0316 345 GLN B O     
5580 C CB    . GLN B 345 ? 0.6568 0.5592 0.6031 0.0230  0.0332  -0.0280 345 GLN B CB    
5581 C CG    . GLN B 345 ? 0.6597 0.5700 0.6135 0.0235  0.0335  -0.0261 345 GLN B CG    
5582 C CD    . GLN B 345 ? 0.7268 0.6348 0.6810 0.0244  0.0338  -0.0252 345 GLN B CD    
5583 O OE1   . GLN B 345 ? 0.7214 0.6235 0.6721 0.0223  0.0335  -0.0255 345 GLN B OE1   
5584 N NE2   . GLN B 345 ? 0.7765 0.6892 0.7348 0.0271  0.0345  -0.0241 345 GLN B NE2   
5585 N N     . GLU B 346 ? 0.7095 0.5999 0.6420 0.0171  0.0318  -0.0321 346 GLU B N     
5586 C CA    . GLU B 346 ? 0.7590 0.6413 0.6834 0.0167  0.0317  -0.0343 346 GLU B CA    
5587 C C     . GLU B 346 ? 0.7884 0.6760 0.7133 0.0145  0.0311  -0.0352 346 GLU B C     
5588 O O     . GLU B 346 ? 0.8513 0.7335 0.7698 0.0149  0.0311  -0.0371 346 GLU B O     
5589 C CB    . GLU B 346 ? 0.7954 0.6676 0.7130 0.0131  0.0312  -0.0352 346 GLU B CB    
5590 C CG    . GLU B 346 ? 0.8588 0.7224 0.7725 0.0167  0.0322  -0.0350 346 GLU B CG    
5591 C CD    . GLU B 346 ? 0.9341 0.7845 0.8382 0.0143  0.0320  -0.0365 346 GLU B CD    
5592 O OE1   . GLU B 346 ? 0.9422 0.7906 0.8431 0.0088  0.0309  -0.0376 346 GLU B OE1   
5593 O OE2   . GLU B 346 ? 0.9357 0.7778 0.8353 0.0179  0.0330  -0.0366 346 GLU B OE2   
5594 N N     . ARG B 347 ? 0.7257 0.6236 0.6577 0.0130  0.0307  -0.0337 347 ARG B N     
5595 C CA    . ARG B 347 ? 0.6588 0.5629 0.5919 0.0117  0.0302  -0.0341 347 ARG B CA    
5596 C C     . ARG B 347 ? 0.6200 0.5297 0.5570 0.0167  0.0311  -0.0335 347 ARG B C     
5597 O O     . ARG B 347 ? 0.7311 0.6426 0.6665 0.0176  0.0311  -0.0344 347 ARG B O     
5598 C CB    . ARG B 347 ? 0.6730 0.5860 0.6119 0.0077  0.0295  -0.0325 347 ARG B CB    
5599 C CG    . ARG B 347 ? 0.7243 0.6439 0.6640 0.0060  0.0289  -0.0328 347 ARG B CG    
5600 C CD    . ARG B 347 ? 0.7604 0.6903 0.7068 0.0033  0.0285  -0.0306 347 ARG B CD    
5601 N NE    . ARG B 347 ? 0.8744 0.8044 0.8177 -0.0024 0.0274  -0.0310 347 ARG B NE    
5602 C CZ    . ARG B 347 ? 0.8933 0.8324 0.8412 -0.0053 0.0269  -0.0292 347 ARG B CZ    
5603 N NH1   . ARG B 347 ? 0.8710 0.8188 0.8265 -0.0028 0.0276  -0.0270 347 ARG B NH1   
5604 N NH2   . ARG B 347 ? 0.8780 0.8175 0.8227 -0.0107 0.0258  -0.0295 347 ARG B NH2   
5605 N N     . PHE B 348 ? 0.6146 0.5270 0.5565 0.0198  0.0317  -0.0319 348 PHE B N     
5606 C CA    . PHE B 348 ? 0.7054 0.6235 0.6511 0.0241  0.0325  -0.0311 348 PHE B CA    
5607 C C     . PHE B 348 ? 0.7141 0.6261 0.6544 0.0285  0.0333  -0.0323 348 PHE B C     
5608 O O     . PHE B 348 ? 0.7272 0.6437 0.6691 0.0319  0.0338  -0.0319 348 PHE B O     
5609 C CB    . PHE B 348 ? 0.7591 0.6827 0.7118 0.0254  0.0329  -0.0289 348 PHE B CB    
5610 C CG    . PHE B 348 ? 0.8104 0.7432 0.7693 0.0270  0.0332  -0.0275 348 PHE B CG    
5611 C CD1   . PHE B 348 ? 0.7491 0.6885 0.7124 0.0243  0.0328  -0.0264 348 PHE B CD1   
5612 C CD2   . PHE B 348 ? 0.8724 0.8073 0.8322 0.0311  0.0339  -0.0270 348 PHE B CD2   
5613 C CE1   . PHE B 348 ? 0.7817 0.7288 0.7503 0.0258  0.0331  -0.0250 348 PHE B CE1   
5614 C CE2   . PHE B 348 ? 0.8311 0.7742 0.7963 0.0323  0.0341  -0.0255 348 PHE B CE2   
5615 C CZ    . PHE B 348 ? 0.8576 0.8064 0.8271 0.0296  0.0337  -0.0245 348 PHE B CZ    
5616 N N     . LYS B 349 ? 0.8178 0.7199 0.7516 0.0286  0.0334  -0.0335 349 LYS B N     
5617 C CA    . LYS B 349 ? 0.8346 0.7298 0.7621 0.0328  0.0343  -0.0348 349 LYS B CA    
5618 C C     . LYS B 349 ? 0.9028 0.7963 0.8252 0.0327  0.0342  -0.0368 349 LYS B C     
5619 O O     . LYS B 349 ? 0.9400 0.8297 0.8578 0.0369  0.0350  -0.0379 349 LYS B O     
5620 C CB    . LYS B 349 ? 0.8314 0.7154 0.7525 0.0325  0.0345  -0.0356 349 LYS B CB    
5621 C CG    . LYS B 349 ? 0.8364 0.7211 0.7612 0.0338  0.0349  -0.0337 349 LYS B CG    
5622 C CD    . LYS B 349 ? 0.8880 0.7611 0.8054 0.0351  0.0354  -0.0344 349 LYS B CD    
5623 C CE    . LYS B 349 ? 0.9123 0.7800 0.8237 0.0404  0.0366  -0.0355 349 LYS B CE    
5624 N NZ    . LYS B 349 ? 0.9576 0.8131 0.8612 0.0419  0.0373  -0.0361 349 LYS B NZ    
5625 N N     . ASN B 350 ? 0.9882 0.8843 0.9110 0.0279  0.0331  -0.0375 350 ASN B N     
5626 C CA    . ASN B 350 ? 1.0176 0.9118 0.9351 0.0267  0.0328  -0.0396 350 ASN B CA    
5627 C C     . ASN B 350 ? 1.0186 0.9237 0.9414 0.0274  0.0327  -0.0388 350 ASN B C     
5628 O O     . ASN B 350 ? 1.0217 0.9268 0.9407 0.0262  0.0324  -0.0405 350 ASN B O     
5629 C CB    . ASN B 350 ? 1.0089 0.8980 0.9220 0.0205  0.0317  -0.0410 350 ASN B CB    
5630 C CG    . ASN B 350 ? 0.9159 0.7926 0.8221 0.0198  0.0319  -0.0420 350 ASN B CG    
5631 O OD1   . ASN B 350 ? 0.9248 0.7953 0.8278 0.0245  0.0331  -0.0423 350 ASN B OD1   
5632 N ND2   . ASN B 350 ? 0.8381 0.7113 0.7419 0.0140  0.0309  -0.0425 350 ASN B ND2   
5633 N N     . LYS B 351 ? 0.9365 0.8507 0.8675 0.0292  0.0329  -0.0364 351 LYS B N     
5634 C CA    . LYS B 351 ? 0.8994 0.8238 0.8356 0.0302  0.0329  -0.0353 351 LYS B CA    
5635 C C     . LYS B 351 ? 1.0171 0.9425 0.9519 0.0355  0.0338  -0.0355 351 LYS B C     
5636 O O     . LYS B 351 ? 1.0582 0.9918 0.9968 0.0367  0.0338  -0.0345 351 LYS B O     
5637 C CB    . LYS B 351 ? 0.7804 0.7136 0.7256 0.0295  0.0328  -0.0325 351 LYS B CB    
5638 C CG    . LYS B 351 ? 0.7901 0.7242 0.7374 0.0246  0.0319  -0.0320 351 LYS B CG    
5639 C CD    . LYS B 351 ? 0.7870 0.7232 0.7320 0.0209  0.0311  -0.0329 351 LYS B CD    
5640 C CE    . LYS B 351 ? 0.8986 0.8282 0.8386 0.0162  0.0303  -0.0343 351 LYS B CE    
5641 N NZ    . LYS B 351 ? 0.9534 0.8858 0.8910 0.0122  0.0294  -0.0352 351 LYS B NZ    
5642 N N     . GLU B 352 ? 1.1195 1.0370 1.0489 0.0389  0.0346  -0.0365 352 GLU B N     
5643 C CA    . GLU B 352 ? 1.1322 1.0505 1.0593 0.0444  0.0356  -0.0368 352 GLU B CA    
5644 C C     . GLU B 352 ? 1.1241 1.0378 1.0437 0.0445  0.0357  -0.0395 352 GLU B C     
5645 O O     . GLU B 352 ? 1.1421 1.0455 1.0541 0.0428  0.0356  -0.0418 352 GLU B O     
5646 C CB    . GLU B 352 ? 1.0943 1.0068 1.0189 0.0486  0.0366  -0.0364 352 GLU B CB    
5647 C CG    . GLU B 352 ? 1.0754 0.9751 0.9920 0.0476  0.0368  -0.0384 352 GLU B CG    
5648 C CD    . GLU B 352 ? 1.0432 0.9397 0.9611 0.0492  0.0373  -0.0370 352 GLU B CD    
5649 O OE1   . GLU B 352 ? 0.9921 0.8961 0.9161 0.0517  0.0376  -0.0347 352 GLU B OE1   
5650 O OE2   . GLU B 352 ? 1.0393 0.9258 0.9518 0.0476  0.0372  -0.0381 352 GLU B OE2   
5651 N N     . MET C 1   ? 0.7804 0.7805 0.6697 -0.1375 0.0400  -0.0585 1   MET C N     
5652 C CA    . MET C 1   ? 0.8841 0.8833 0.7723 -0.1348 0.0411  -0.0610 1   MET C CA    
5653 C C     . MET C 1   ? 0.9028 0.9197 0.7975 -0.1315 0.0398  -0.0576 1   MET C C     
5654 O O     . MET C 1   ? 0.9744 1.0061 0.8726 -0.1335 0.0379  -0.0536 1   MET C O     
5655 C CB    . MET C 1   ? 0.8578 0.8423 0.7471 -0.1269 0.0434  -0.0633 1   MET C CB    
5656 C CG    . MET C 1   ? 0.8302 0.8149 0.7275 -0.1189 0.0433  -0.0598 1   MET C CG    
5657 S SD    . MET C 1   ? 0.8361 0.8099 0.7365 -0.1089 0.0455  -0.0614 1   MET C SD    
5658 C CE    . MET C 1   ? 0.8903 0.8441 0.7806 -0.1122 0.0480  -0.0673 1   MET C CE    
5659 N N     . GLN C 2   ? 0.9429 0.9581 0.8390 -0.1262 0.0409  -0.0590 2   GLN C N     
5660 C CA    . GLN C 2   ? 0.9656 0.9956 0.8662 -0.1237 0.0400  -0.0565 2   GLN C CA    
5661 C C     . GLN C 2   ? 0.9915 1.0161 0.8958 -0.1152 0.0415  -0.0572 2   GLN C C     
5662 O O     . GLN C 2   ? 1.0003 1.0100 0.9015 -0.1129 0.0433  -0.0606 2   GLN C O     
5663 C CB    . GLN C 2   ? 1.0253 1.0618 0.9198 -0.1314 0.0395  -0.0586 2   GLN C CB    
5664 C CG    . GLN C 2   ? 1.0245 1.0790 0.9234 -0.1302 0.0382  -0.0553 2   GLN C CG    
5665 C CD    . GLN C 2   ? 1.0386 1.1087 0.9414 -0.1324 0.0362  -0.0503 2   GLN C CD    
5666 O OE1   . GLN C 2   ? 1.0711 1.1465 0.9811 -0.1261 0.0356  -0.0461 2   GLN C OE1   
5667 N NE2   . GLN C 2   ? 0.9909 1.0688 0.8888 -0.1414 0.0350  -0.0506 2   GLN C NE2   
5668 N N     . ILE C 3   ? 0.8519 0.8887 0.7625 -0.1103 0.0407  -0.0536 3   ILE C N     
5669 C CA    . ILE C 3   ? 0.7900 0.8245 0.7040 -0.1031 0.0418  -0.0539 3   ILE C CA    
5670 C C     . ILE C 3   ? 0.7317 0.7823 0.6497 -0.1018 0.0406  -0.0505 3   ILE C C     
5671 O O     . ILE C 3   ? 0.7604 0.8238 0.6799 -0.1048 0.0390  -0.0473 3   ILE C O     
5672 C CB    . ILE C 3   ? 0.7793 0.8064 0.6988 -0.0952 0.0424  -0.0523 3   ILE C CB    
5673 C CG1   . ILE C 3   ? 0.7661 0.8045 0.6926 -0.0918 0.0409  -0.0470 3   ILE C CG1   
5674 C CG2   . ILE C 3   ? 0.7919 0.8041 0.7080 -0.0962 0.0436  -0.0549 3   ILE C CG2   
5675 C CD1   . ILE C 3   ? 0.7493 0.7814 0.6811 -0.0842 0.0414  -0.0454 3   ILE C CD1   
5676 N N     . PHE C 4   ? 0.7035 0.7537 0.6233 -0.0971 0.0414  -0.0510 4   PHE C N     
5677 C CA    . PHE C 4   ? 0.6499 0.7142 0.5737 -0.0949 0.0405  -0.0476 4   PHE C CA    
5678 C C     . PHE C 4   ? 0.5970 0.6591 0.5269 -0.0862 0.0410  -0.0455 4   PHE C C     
5679 O O     . PHE C 4   ? 0.6442 0.6959 0.5732 -0.0831 0.0425  -0.0482 4   PHE C O     
5680 C CB    . PHE C 4   ? 0.5856 0.6533 0.5046 -0.0990 0.0408  -0.0503 4   PHE C CB    
5681 C CG    . PHE C 4   ? 0.6602 0.7251 0.5716 -0.1076 0.0409  -0.0540 4   PHE C CG    
5682 C CD1   . PHE C 4   ? 0.7500 0.7994 0.6552 -0.1095 0.0425  -0.0591 4   PHE C CD1   
5683 C CD2   . PHE C 4   ? 0.7357 0.8133 0.6455 -0.1140 0.0393  -0.0522 4   PHE C CD2   
5684 C CE1   . PHE C 4   ? 0.8669 0.9124 0.7641 -0.1178 0.0426  -0.0627 4   PHE C CE1   
5685 C CE2   . PHE C 4   ? 0.7995 0.8743 0.7017 -0.1227 0.0392  -0.0558 4   PHE C CE2   
5686 C CZ    . PHE C 4   ? 0.8502 0.9083 0.7459 -0.1247 0.0409  -0.0611 4   PHE C CZ    
5687 N N     . VAL C 5   ? 0.4595 0.5319 0.3953 -0.0825 0.0399  -0.0407 5   VAL C N     
5688 C CA    . VAL C 5   ? 0.4610 0.5322 0.4023 -0.0747 0.0402  -0.0383 5   VAL C CA    
5689 C C     . VAL C 5   ? 0.5244 0.6060 0.4675 -0.0732 0.0398  -0.0361 5   VAL C C     
5690 O O     . VAL C 5   ? 0.5829 0.6772 0.5276 -0.0743 0.0386  -0.0327 5   VAL C O     
5691 C CB    . VAL C 5   ? 0.5461 0.6201 0.4923 -0.0712 0.0393  -0.0343 5   VAL C CB    
5692 C CG1   . VAL C 5   ? 0.5817 0.6548 0.5332 -0.0635 0.0395  -0.0317 5   VAL C CG1   
5693 C CG2   . VAL C 5   ? 0.5704 0.6341 0.5149 -0.0727 0.0397  -0.0363 5   VAL C CG2   
5694 N N     . LYS C 6   ? 0.6126 0.6892 0.5556 -0.0704 0.0409  -0.0379 6   LYS C N     
5695 C CA    . LYS C 6   ? 0.6515 0.7372 0.5960 -0.0690 0.0407  -0.0359 6   LYS C CA    
5696 C C     . LYS C 6   ? 0.6965 0.7841 0.6468 -0.0619 0.0405  -0.0320 6   LYS C C     
5697 O O     . LYS C 6   ? 0.7807 0.8591 0.7331 -0.0576 0.0411  -0.0323 6   LYS C O     
5698 C CB    . LYS C 6   ? 0.7266 0.8075 0.6670 -0.0707 0.0419  -0.0400 6   LYS C CB    
5699 C CG    . LYS C 6   ? 0.8524 0.9378 0.7869 -0.0781 0.0417  -0.0427 6   LYS C CG    
5700 C CD    . LYS C 6   ? 0.9204 1.0126 0.8539 -0.0786 0.0419  -0.0431 6   LYS C CD    
5701 C CE    . LYS C 6   ? 0.8636 0.9573 0.7901 -0.0861 0.0421  -0.0470 6   LYS C CE    
5702 N NZ    . LYS C 6   ? 0.7822 0.8841 0.7076 -0.0869 0.0422  -0.0470 6   LYS C NZ    
5703 N N     . THR C 7   ? 0.5716 0.6713 0.5242 -0.0609 0.0396  -0.0282 7   THR C N     
5704 C CA    . THR C 7   ? 0.6041 0.7061 0.5616 -0.0545 0.0394  -0.0241 7   THR C CA    
5705 C C     . THR C 7   ? 0.6326 0.7342 0.5905 -0.0524 0.0400  -0.0244 7   THR C C     
5706 O O     . THR C 7   ? 0.6452 0.7456 0.5996 -0.0556 0.0407  -0.0277 7   THR C O     
5707 C CB    . THR C 7   ? 0.5356 0.6513 0.4955 -0.0540 0.0382  -0.0191 7   THR C CB    
5708 O OG1   . THR C 7   ? 0.5064 0.6327 0.4637 -0.0588 0.0378  -0.0192 7   THR C OG1   
5709 C CG2   . THR C 7   ? 0.4842 0.6007 0.4447 -0.0548 0.0376  -0.0180 7   THR C CG2   
5710 N N     . LEU C 8   ? 0.5616 0.6643 0.5234 -0.0469 0.0399  -0.0208 8   LEU C N     
5711 C CA    . LEU C 8   ? 0.5335 0.6362 0.4961 -0.0447 0.0404  -0.0205 8   LEU C CA    
5712 C C     . LEU C 8   ? 0.6056 0.7214 0.5676 -0.0468 0.0398  -0.0183 8   LEU C C     
5713 O O     . LEU C 8   ? 0.6761 0.7950 0.6389 -0.0451 0.0400  -0.0170 8   LEU C O     
5714 C CB    . LEU C 8   ? 0.4704 0.5692 0.4371 -0.0384 0.0404  -0.0173 8   LEU C CB    
5715 C CG    . LEU C 8   ? 0.3711 0.4574 0.3390 -0.0353 0.0410  -0.0190 8   LEU C CG    
5716 C CD1   . LEU C 8   ? 0.2686 0.3539 0.2398 -0.0302 0.0409  -0.0156 8   LEU C CD1   
5717 C CD2   . LEU C 8   ? 0.3480 0.4270 0.3130 -0.0375 0.0421  -0.0238 8   LEU C CD2   
5718 N N     . THR C 9   ? 0.9981 1.1223 0.9588 -0.0506 0.0391  -0.0175 9   THR C N     
5719 C CA    . THR C 9   ? 1.0094 1.1471 0.9692 -0.0531 0.0385  -0.0154 9   THR C CA    
5720 C C     . THR C 9   ? 0.9627 1.1009 0.9175 -0.0598 0.0387  -0.0199 9   THR C C     
5721 O O     . THR C 9   ? 0.9577 1.1052 0.9108 -0.0626 0.0385  -0.0197 9   THR C O     
5722 C CB    . THR C 9   ? 1.0256 1.1743 0.9872 -0.0530 0.0374  -0.0110 9   THR C CB    
5723 O OG1   . THR C 9   ? 1.0517 1.1983 1.0113 -0.0569 0.0371  -0.0131 9   THR C OG1   
5724 C CG2   . THR C 9   ? 1.0320 1.1795 0.9981 -0.0461 0.0373  -0.0066 9   THR C CG2   
5725 N N     . GLY C 10  ? 0.5721 0.7001 0.5243 -0.0622 0.0392  -0.0241 10  GLY C N     
5726 C CA    . GLY C 10  ? 0.5202 0.6467 0.4668 -0.0687 0.0396  -0.0288 10  GLY C CA    
5727 C C     . GLY C 10  ? 0.6329 0.7665 0.5774 -0.0741 0.0386  -0.0284 10  GLY C C     
5728 O O     . GLY C 10  ? 0.7701 0.9030 0.7093 -0.0803 0.0387  -0.0321 10  GLY C O     
5729 N N     . LYS C 11  ? 0.5507 0.6909 0.4988 -0.0718 0.0376  -0.0240 11  LYS C N     
5730 C CA    . LYS C 11  ? 0.5749 0.7226 0.5215 -0.0767 0.0366  -0.0231 11  LYS C CA    
5731 C C     . LYS C 11  ? 0.6307 0.7661 0.5746 -0.0792 0.0370  -0.0270 11  LYS C C     
5732 O O     . LYS C 11  ? 0.6492 0.7726 0.5947 -0.0750 0.0378  -0.0282 11  LYS C O     
5733 C CB    . LYS C 11  ? 0.5855 0.7424 0.5369 -0.0725 0.0357  -0.0173 11  LYS C CB    
5734 C CG    . LYS C 11  ? 0.6295 0.7983 0.5840 -0.0690 0.0354  -0.0127 11  LYS C CG    
5735 C CD    . LYS C 11  ? 0.5729 0.7541 0.5242 -0.0748 0.0349  -0.0129 11  LYS C CD    
5736 C CE    . LYS C 11  ? 0.4920 0.6884 0.4467 -0.0716 0.0343  -0.0069 11  LYS C CE    
5737 N NZ    . LYS C 11  ? 0.4460 0.6382 0.4047 -0.0639 0.0349  -0.0042 11  LYS C NZ    
5738 N N     . THR C 12  ? 0.7615 0.8998 0.7013 -0.0861 0.0364  -0.0287 12  THR C N     
5739 C CA    . THR C 12  ? 0.7382 0.8636 0.6746 -0.0891 0.0369  -0.0327 12  THR C CA    
5740 C C     . THR C 12  ? 0.7440 0.8738 0.6817 -0.0909 0.0358  -0.0302 12  THR C C     
5741 O O     . THR C 12  ? 0.7957 0.9357 0.7309 -0.0968 0.0348  -0.0294 12  THR C O     
5742 C CB    . THR C 12  ? 0.6476 0.7685 0.5768 -0.0962 0.0375  -0.0380 12  THR C CB    
5743 O OG1   . THR C 12  ? 0.5916 0.7100 0.5198 -0.0943 0.0385  -0.0400 12  THR C OG1   
5744 C CG2   . THR C 12  ? 0.6075 0.7130 0.5331 -0.0983 0.0383  -0.0422 12  THR C CG2   
5745 N N     . ILE C 13  ? 0.5539 0.6759 0.4949 -0.0859 0.0361  -0.0292 13  ILE C N     
5746 C CA    . ILE C 13  ? 0.4524 0.5760 0.3943 -0.0873 0.0353  -0.0275 13  ILE C CA    
5747 C C     . ILE C 13  ? 0.4528 0.5651 0.3892 -0.0933 0.0357  -0.0322 13  ILE C C     
5748 O O     . ILE C 13  ? 0.6131 0.7113 0.5474 -0.0920 0.0371  -0.0361 13  ILE C O     
5749 C CB    . ILE C 13  ? 0.4831 0.6024 0.4307 -0.0795 0.0355  -0.0246 13  ILE C CB    
5750 C CG1   . ILE C 13  ? 0.4439 0.5692 0.3959 -0.0729 0.0355  -0.0211 13  ILE C CG1   
5751 C CG2   . ILE C 13  ? 0.5158 0.6412 0.4653 -0.0799 0.0344  -0.0214 13  ILE C CG2   
5752 C CD1   . ILE C 13  ? 0.3768 0.4957 0.3337 -0.0652 0.0359  -0.0189 13  ILE C CD1   
5753 N N     . THR C 14  ? 0.3921 0.5104 0.3257 -0.0997 0.0347  -0.0319 14  THR C N     
5754 C CA    . THR C 14  ? 0.4770 0.5844 0.4050 -0.1057 0.0351  -0.0360 14  THR C CA    
5755 C C     . THR C 14  ? 0.5020 0.6083 0.4325 -0.1049 0.0345  -0.0338 14  THR C C     
5756 O O     . THR C 14  ? 0.6241 0.7432 0.5561 -0.1072 0.0331  -0.0302 14  THR C O     
5757 C CB    . THR C 14  ? 0.6133 0.7270 0.5350 -0.1151 0.0344  -0.0381 14  THR C CB    
5758 O OG1   . THR C 14  ? 0.7113 0.8301 0.6319 -0.1152 0.0347  -0.0390 14  THR C OG1   
5759 C CG2   . THR C 14  ? 0.6133 0.7121 0.5279 -0.1210 0.0353  -0.0434 14  THR C CG2   
5760 N N     . LEU C 15  ? 0.6767 0.7685 0.6073 -0.1019 0.0355  -0.0359 15  LEU C N     
5761 C CA    . LEU C 15  ? 0.7419 0.8315 0.6748 -0.1009 0.0351  -0.0340 15  LEU C CA    
5762 C C     . LEU C 15  ? 0.8522 0.9296 0.7793 -0.1067 0.0356  -0.0379 15  LEU C C     
5763 O O     . LEU C 15  ? 0.9343 0.9974 0.8588 -0.1054 0.0371  -0.0417 15  LEU C O     
5764 C CB    . LEU C 15  ? 0.7206 0.8025 0.6587 -0.0921 0.0359  -0.0329 15  LEU C CB    
5765 C CG    . LEU C 15  ? 0.6402 0.7303 0.5850 -0.0845 0.0355  -0.0284 15  LEU C CG    
5766 C CD1   . LEU C 15  ? 0.6422 0.7352 0.5876 -0.0820 0.0359  -0.0287 15  LEU C CD1   
5767 C CD2   . LEU C 15  ? 0.6347 0.7132 0.5826 -0.0785 0.0363  -0.0287 15  LEU C CD2   
5768 N N     . GLU C 16  ? 0.7650 0.8480 0.6899 -0.1130 0.0344  -0.0369 16  GLU C N     
5769 C CA    . GLU C 16  ? 0.7657 0.8367 0.6851 -0.1186 0.0349  -0.0401 16  GLU C CA    
5770 C C     . GLU C 16  ? 0.7218 0.7838 0.6448 -0.1133 0.0354  -0.0391 16  GLU C C     
5771 O O     . GLU C 16  ? 0.6357 0.7060 0.5643 -0.1094 0.0345  -0.0349 16  GLU C O     
5772 C CB    . GLU C 16  ? 0.8567 0.9372 0.7725 -0.1276 0.0333  -0.0390 16  GLU C CB    
5773 C CG    . GLU C 16  ? 0.9009 0.9870 0.8107 -0.1353 0.0329  -0.0413 16  GLU C CG    
5774 C CD    . GLU C 16  ? 0.9081 1.0153 0.8211 -0.1367 0.0312  -0.0367 16  GLU C CD    
5775 O OE1   . GLU C 16  ? 0.8874 1.0047 0.8022 -0.1390 0.0298  -0.0331 16  GLU C OE1   
5776 O OE2   . GLU C 16  ? 0.9043 1.0185 0.8182 -0.1350 0.0313  -0.0365 16  GLU C OE2   
5777 N N     . VAL C 17  ? 0.6373 0.6823 0.5568 -0.1129 0.0369  -0.0430 17  VAL C N     
5778 C CA    . VAL C 17  ? 0.5860 0.6210 0.5087 -0.1074 0.0377  -0.0426 17  VAL C CA    
5779 C C     . VAL C 17  ? 0.5929 0.6136 0.5093 -0.1124 0.0386  -0.0460 17  VAL C C     
5780 O O     . VAL C 17  ? 0.5917 0.6080 0.5011 -0.1192 0.0389  -0.0494 17  VAL C O     
5781 C CB    . VAL C 17  ? 0.6030 0.6315 0.5294 -0.0990 0.0391  -0.0433 17  VAL C CB    
5782 C CG1   . VAL C 17  ? 0.6557 0.6973 0.5868 -0.0950 0.0383  -0.0404 17  VAL C CG1   
5783 C CG2   . VAL C 17  ? 0.6212 0.6362 0.5418 -0.1003 0.0408  -0.0483 17  VAL C CG2   
5784 N N     . GLU C 18  ? 0.8240 0.8370 0.7428 -0.1088 0.0391  -0.0452 18  GLU C N     
5785 C CA    . GLU C 18  ? 0.8723 0.8699 0.7857 -0.1119 0.0402  -0.0482 18  GLU C CA    
5786 C C     . GLU C 18  ? 0.8717 0.8571 0.7875 -0.1040 0.0420  -0.0495 18  GLU C C     
5787 O O     . GLU C 18  ? 0.8970 0.8864 0.8196 -0.0972 0.0418  -0.0466 18  GLU C O     
5788 C CB    . GLU C 18  ? 0.8896 0.8895 0.8034 -0.1155 0.0391  -0.0458 18  GLU C CB    
5789 C CG    . GLU C 18  ? 0.8837 0.8974 0.7956 -0.1234 0.0372  -0.0438 18  GLU C CG    
5790 C CD    . GLU C 18  ? 0.9831 0.9891 0.8859 -0.1331 0.0373  -0.0473 18  GLU C CD    
5791 O OE1   . GLU C 18  ? 0.9433 0.9337 0.8406 -0.1335 0.0392  -0.0516 18  GLU C OE1   
5792 O OE2   . GLU C 18  ? 1.0457 1.0611 0.9463 -0.1405 0.0357  -0.0456 18  GLU C OE2   
5793 N N     . PRO C 19  ? 0.7685 0.7389 0.6786 -0.1048 0.0439  -0.0536 19  PRO C N     
5794 C CA    . PRO C 19  ? 0.7007 0.6621 0.6128 -0.0973 0.0457  -0.0551 19  PRO C CA    
5795 C C     . PRO C 19  ? 0.6615 0.6213 0.5801 -0.0903 0.0458  -0.0523 19  PRO C C     
5796 O O     . PRO C 19  ? 0.6568 0.6129 0.5785 -0.0836 0.0469  -0.0526 19  PRO C O     
5797 C CB    . PRO C 19  ? 0.7187 0.6639 0.6226 -0.1002 0.0478  -0.0597 19  PRO C CB    
5798 C CG    . PRO C 19  ? 0.7668 0.7101 0.6653 -0.1085 0.0470  -0.0601 19  PRO C CG    
5799 C CD    . PRO C 19  ? 0.7752 0.7357 0.6765 -0.1126 0.0446  -0.0570 19  PRO C CD    
5800 N N     . SER C 20  ? 0.7020 0.6646 0.6225 -0.0918 0.0447  -0.0497 20  SER C N     
5801 C CA    . SER C 20  ? 0.7902 0.7531 0.7171 -0.0853 0.0446  -0.0469 20  SER C CA    
5802 C C     . SER C 20  ? 0.7785 0.7560 0.7124 -0.0814 0.0430  -0.0430 20  SER C C     
5803 O O     . SER C 20  ? 0.8339 0.8123 0.7731 -0.0759 0.0429  -0.0406 20  SER C O     
5804 C CB    . SER C 20  ? 0.8146 0.7732 0.7403 -0.0883 0.0443  -0.0458 20  SER C CB    
5805 O OG    . SER C 20  ? 0.8060 0.7579 0.7354 -0.0820 0.0452  -0.0448 20  SER C OG    
5806 N N     . ASP C 21  ? 0.9007 0.8894 0.8346 -0.0841 0.0420  -0.0423 21  ASP C N     
5807 C CA    . ASP C 21  ? 0.8833 0.8847 0.8234 -0.0796 0.0408  -0.0388 21  ASP C CA    
5808 C C     . ASP C 21  ? 0.9354 0.9323 0.8792 -0.0719 0.0418  -0.0391 21  ASP C C     
5809 O O     . ASP C 21  ? 1.0032 0.9936 0.9445 -0.0712 0.0431  -0.0419 21  ASP C O     
5810 C CB    . ASP C 21  ? 0.8697 0.8828 0.8083 -0.0836 0.0398  -0.0383 21  ASP C CB    
5811 C CG    . ASP C 21  ? 0.9264 0.9486 0.8630 -0.0906 0.0383  -0.0366 21  ASP C CG    
5812 O OD1   . ASP C 21  ? 0.9066 0.9226 0.8402 -0.0946 0.0383  -0.0374 21  ASP C OD1   
5813 O OD2   . ASP C 21  ? 0.9465 0.9825 0.8844 -0.0922 0.0370  -0.0343 21  ASP C OD2   
5814 N N     . THR C 22  ? 0.8535 0.8539 0.8030 -0.0662 0.0413  -0.0361 22  THR C N     
5815 C CA    . THR C 22  ? 0.8013 0.7983 0.7546 -0.0592 0.0421  -0.0358 22  THR C CA    
5816 C C     . THR C 22  ? 0.7688 0.7740 0.7239 -0.0573 0.0417  -0.0350 22  THR C C     
5817 O O     . THR C 22  ? 0.8075 0.8231 0.7621 -0.0604 0.0406  -0.0336 22  THR C O     
5818 C CB    . THR C 22  ? 0.7953 0.7937 0.7537 -0.0542 0.0416  -0.0329 22  THR C CB    
5819 O OG1   . THR C 22  ? 0.7157 0.7268 0.6768 -0.0543 0.0400  -0.0294 22  THR C OG1   
5820 C CG2   . THR C 22  ? 0.8006 0.7907 0.7575 -0.0558 0.0421  -0.0336 22  THR C CG2   
5821 N N     . ILE C 23  ? 0.6609 0.6619 0.6180 -0.0522 0.0425  -0.0356 23  ILE C N     
5822 C CA    . ILE C 23  ? 0.6385 0.6471 0.5976 -0.0499 0.0421  -0.0343 23  ILE C CA    
5823 C C     . ILE C 23  ? 0.6365 0.6558 0.5998 -0.0475 0.0407  -0.0302 23  ILE C C     
5824 O O     . ILE C 23  ? 0.6993 0.7285 0.6631 -0.0484 0.0399  -0.0285 23  ILE C O     
5825 C CB    . ILE C 23  ? 0.6282 0.6299 0.5886 -0.0450 0.0433  -0.0356 23  ILE C CB    
5826 C CG1   . ILE C 23  ? 0.6209 0.6122 0.5768 -0.0472 0.0449  -0.0396 23  ILE C CG1   
5827 C CG2   . ILE C 23  ? 0.5834 0.5921 0.5454 -0.0431 0.0430  -0.0344 23  ILE C CG2   
5828 C CD1   . ILE C 23  ? 0.5912 0.5845 0.5420 -0.0532 0.0449  -0.0418 23  ILE C CD1   
5829 N N     . GLU C 24  ? 0.5640 0.5816 0.5303 -0.0443 0.0405  -0.0284 24  GLU C N     
5830 C CA    . GLU C 24  ? 0.4974 0.5248 0.4669 -0.0424 0.0393  -0.0246 24  GLU C CA    
5831 C C     . GLU C 24  ? 0.4837 0.5211 0.4513 -0.0478 0.0383  -0.0234 24  GLU C C     
5832 O O     . GLU C 24  ? 0.4619 0.5102 0.4315 -0.0465 0.0374  -0.0202 24  GLU C O     
5833 C CB    . GLU C 24  ? 0.5784 0.6014 0.5500 -0.0399 0.0393  -0.0237 24  GLU C CB    
5834 C CG    . GLU C 24  ? 0.6697 0.6952 0.6456 -0.0336 0.0389  -0.0208 24  GLU C CG    
5835 C CD    . GLU C 24  ? 0.7566 0.7781 0.7341 -0.0319 0.0389  -0.0201 24  GLU C CD    
5836 O OE1   . GLU C 24  ? 0.7714 0.7917 0.7470 -0.0360 0.0388  -0.0208 24  GLU C OE1   
5837 O OE2   . GLU C 24  ? 0.7682 0.7877 0.7485 -0.0267 0.0390  -0.0189 24  GLU C OE2   
5838 N N     . ASN C 25  ? 0.6904 0.7242 0.6539 -0.0538 0.0384  -0.0257 25  ASN C N     
5839 C CA    . ASN C 25  ? 0.7077 0.7511 0.6690 -0.0598 0.0374  -0.0247 25  ASN C CA    
5840 C C     . ASN C 25  ? 0.6702 0.7213 0.6299 -0.0621 0.0371  -0.0248 25  ASN C C     
5841 O O     . ASN C 25  ? 0.6387 0.7024 0.5990 -0.0638 0.0360  -0.0220 25  ASN C O     
5842 C CB    . ASN C 25  ? 0.7211 0.7571 0.6777 -0.0661 0.0377  -0.0274 25  ASN C CB    
5843 C CG    . ASN C 25  ? 0.8568 0.8938 0.8147 -0.0667 0.0370  -0.0255 25  ASN C CG    
5844 O OD1   . ASN C 25  ? 0.9520 0.9785 0.9086 -0.0671 0.0378  -0.0271 25  ASN C OD1   
5845 N ND2   . ASN C 25  ? 0.9154 0.9652 0.8757 -0.0667 0.0358  -0.0217 25  ASN C ND2   
5846 N N     . VAL C 26  ? 0.5275 0.5718 0.4851 -0.0621 0.0381  -0.0278 26  VAL C N     
5847 C CA    . VAL C 26  ? 0.4865 0.5378 0.4423 -0.0648 0.0379  -0.0282 26  VAL C CA    
5848 C C     . VAL C 26  ? 0.5777 0.6383 0.5374 -0.0599 0.0374  -0.0249 26  VAL C C     
5849 O O     . VAL C 26  ? 0.6866 0.7581 0.6460 -0.0621 0.0366  -0.0233 26  VAL C O     
5850 C CB    . VAL C 26  ? 0.4704 0.5117 0.4217 -0.0671 0.0391  -0.0327 26  VAL C CB    
5851 C CG1   . VAL C 26  ? 0.4958 0.5291 0.4420 -0.0730 0.0395  -0.0358 26  VAL C CG1   
5852 C CG2   . VAL C 26  ? 0.5376 0.5696 0.4911 -0.0610 0.0403  -0.0339 26  VAL C CG2   
5853 N N     . LYS C 27  ? 0.3725 0.4293 0.3362 -0.0533 0.0377  -0.0236 27  LYS C N     
5854 C CA    . LYS C 27  ? 0.2871 0.3516 0.2543 -0.0484 0.0373  -0.0202 27  LYS C CA    
5855 C C     . LYS C 27  ? 0.3373 0.4141 0.3062 -0.0485 0.0362  -0.0163 27  LYS C C     
5856 O O     . LYS C 27  ? 0.4469 0.5334 0.4172 -0.0467 0.0357  -0.0134 27  LYS C O     
5857 C CB    . LYS C 27  ? 0.2747 0.3310 0.2448 -0.0420 0.0380  -0.0201 27  LYS C CB    
5858 C CG    . LYS C 27  ? 0.2767 0.3231 0.2454 -0.0416 0.0391  -0.0235 27  LYS C CG    
5859 C CD    . LYS C 27  ? 0.2728 0.3121 0.2446 -0.0356 0.0396  -0.0230 27  LYS C CD    
5860 C CE    . LYS C 27  ? 0.2905 0.3218 0.2612 -0.0347 0.0407  -0.0258 27  LYS C CE    
5861 N NZ    . LYS C 27  ? 0.3125 0.3375 0.2861 -0.0293 0.0411  -0.0252 27  LYS C NZ    
5862 N N     . ALA C 28  ? 0.4555 0.5320 0.4245 -0.0500 0.0358  -0.0157 28  ALA C N     
5863 C CA    . ALA C 28  ? 0.4281 0.5169 0.3984 -0.0504 0.0347  -0.0119 28  ALA C CA    
5864 C C     . ALA C 28  ? 0.3826 0.4827 0.3505 -0.0564 0.0339  -0.0112 28  ALA C C     
5865 O O     . ALA C 28  ? 0.4830 0.5958 0.4524 -0.0554 0.0332  -0.0074 28  ALA C O     
5866 C CB    . ALA C 28  ? 0.3429 0.4282 0.3136 -0.0511 0.0345  -0.0117 28  ALA C CB    
5867 N N     . LYS C 29  ? 0.5045 0.6001 0.4681 -0.0629 0.0341  -0.0147 29  LYS C N     
5868 C CA    . LYS C 29  ? 0.5655 0.6712 0.5261 -0.0694 0.0333  -0.0146 29  LYS C CA    
5869 C C     . LYS C 29  ? 0.5516 0.6640 0.5132 -0.0670 0.0334  -0.0134 29  LYS C C     
5870 O O     . LYS C 29  ? 0.5774 0.7033 0.5390 -0.0689 0.0326  -0.0107 29  LYS C O     
5871 C CB    . LYS C 29  ? 0.5279 0.6247 0.4830 -0.0764 0.0337  -0.0193 29  LYS C CB    
5872 C CG    . LYS C 29  ? 0.5836 0.6713 0.5369 -0.0792 0.0339  -0.0211 29  LYS C CG    
5873 C CD    . LYS C 29  ? 0.6250 0.7035 0.5721 -0.0861 0.0345  -0.0258 29  LYS C CD    
5874 C CE    . LYS C 29  ? 0.6562 0.7246 0.6012 -0.0887 0.0348  -0.0274 29  LYS C CE    
5875 N NZ    . LYS C 29  ? 0.6837 0.7617 0.6301 -0.0911 0.0334  -0.0240 29  LYS C NZ    
5876 N N     . ILE C 30  ? 0.3559 0.4592 0.3183 -0.0628 0.0344  -0.0152 30  ILE C N     
5877 C CA    . ILE C 30  ? 0.3987 0.5074 0.3620 -0.0605 0.0345  -0.0141 30  ILE C CA    
5878 C C     . ILE C 30  ? 0.3757 0.4958 0.3430 -0.0553 0.0340  -0.0088 30  ILE C C     
5879 O O     . ILE C 30  ? 0.4159 0.5479 0.3832 -0.0562 0.0335  -0.0064 30  ILE C O     
5880 C CB    . ILE C 30  ? 0.3944 0.4909 0.3581 -0.0566 0.0357  -0.0168 30  ILE C CB    
5881 C CG1   . ILE C 30  ? 0.2918 0.3793 0.2510 -0.0616 0.0365  -0.0218 30  ILE C CG1   
5882 C CG2   . ILE C 30  ? 0.3772 0.4796 0.3430 -0.0525 0.0358  -0.0145 30  ILE C CG2   
5883 C CD1   . ILE C 30  ? 0.2966 0.3718 0.2563 -0.0576 0.0377  -0.0243 30  ILE C CD1   
5884 N N     . GLN C 31  ? 0.3709 0.4878 0.3412 -0.0500 0.0341  -0.0070 31  GLN C N     
5885 C CA    . GLN C 31  ? 0.4367 0.5636 0.4104 -0.0447 0.0337  -0.0020 31  GLN C CA    
5886 C C     . GLN C 31  ? 0.4096 0.5515 0.3829 -0.0481 0.0327  0.0011  31  GLN C C     
5887 O O     . GLN C 31  ? 0.4092 0.5627 0.3838 -0.0458 0.0324  0.0048  31  GLN C O     
5888 C CB    . GLN C 31  ? 0.4363 0.5560 0.4126 -0.0389 0.0340  -0.0011 31  GLN C CB    
5889 C CG    . GLN C 31  ? 0.4297 0.5581 0.4089 -0.0329 0.0339  0.0038  31  GLN C CG    
5890 C CD    . GLN C 31  ? 0.5271 0.6495 0.5081 -0.0288 0.0340  0.0044  31  GLN C CD    
5891 O OE1   . GLN C 31  ? 0.4886 0.6064 0.4688 -0.0320 0.0339  0.0024  31  GLN C OE1   
5892 N NE2   . GLN C 31  ? 0.6439 0.7663 0.6271 -0.0217 0.0344  0.0072  31  GLN C NE2   
5893 N N     . ASP C 32  ? 0.4416 0.5836 0.4128 -0.0539 0.0322  -0.0004 32  ASP C N     
5894 C CA    . ASP C 32  ? 0.5005 0.6574 0.4711 -0.0578 0.0312  0.0025  32  ASP C CA    
5895 C C     . ASP C 32  ? 0.4310 0.5984 0.3996 -0.0621 0.0307  0.0030  32  ASP C C     
5896 O O     . ASP C 32  ? 0.5790 0.7612 0.5490 -0.0613 0.0301  0.0072  32  ASP C O     
5897 C CB    . ASP C 32  ? 0.7058 0.8601 0.6741 -0.0640 0.0306  0.0007  32  ASP C CB    
5898 C CG    . ASP C 32  ? 0.8360 0.9850 0.8068 -0.0596 0.0308  0.0018  32  ASP C CG    
5899 O OD1   . ASP C 32  ? 0.8321 0.9832 0.8065 -0.0521 0.0311  0.0048  32  ASP C OD1   
5900 O OD2   . ASP C 32  ? 0.8841 1.0267 0.8532 -0.0638 0.0306  -0.0004 32  ASP C OD2   
5901 N N     . LYS C 33  ? 0.4495 0.6103 0.4149 -0.0667 0.0310  -0.0011 33  LYS C N     
5902 C CA    . LYS C 33  ? 0.5496 0.7201 0.5131 -0.0703 0.0307  -0.0008 33  LYS C CA    
5903 C C     . LYS C 33  ? 0.6311 0.8062 0.5974 -0.0639 0.0311  0.0020  33  LYS C C     
5904 O O     . LYS C 33  ? 0.6656 0.8550 0.6323 -0.0644 0.0306  0.0053  33  LYS C O     
5905 C CB    . LYS C 33  ? 0.5905 0.7513 0.5493 -0.0763 0.0311  -0.0063 33  LYS C CB    
5906 C CG    . LYS C 33  ? 0.6320 0.8035 0.5879 -0.0821 0.0306  -0.0065 33  LYS C CG    
5907 C CD    . LYS C 33  ? 0.6777 0.8381 0.6292 -0.0862 0.0313  -0.0121 33  LYS C CD    
5908 C CE    . LYS C 33  ? 0.6245 0.7741 0.5715 -0.0924 0.0314  -0.0164 33  LYS C CE    
5909 N NZ    . LYS C 33  ? 0.5859 0.7429 0.5277 -0.1018 0.0306  -0.0178 33  LYS C NZ    
5910 N N     . GLU C 34  ? 0.6582 0.8215 0.6263 -0.0580 0.0321  0.0008  34  GLU C N     
5911 C CA    . GLU C 34  ? 0.5906 0.7561 0.5608 -0.0524 0.0326  0.0030  34  GLU C CA    
5912 C C     . GLU C 34  ? 0.5669 0.7316 0.5410 -0.0436 0.0330  0.0067  34  GLU C C     
5913 O O     . GLU C 34  ? 0.5718 0.7389 0.5473 -0.0392 0.0334  0.0090  34  GLU C O     
5914 C CB    . GLU C 34  ? 0.6024 0.7556 0.5709 -0.0531 0.0334  -0.0015 34  GLU C CB    
5915 C CG    . GLU C 34  ? 0.6091 0.7618 0.5731 -0.0611 0.0333  -0.0055 34  GLU C CG    
5916 C CD    . GLU C 34  ? 0.6163 0.7802 0.5795 -0.0628 0.0330  -0.0041 34  GLU C CD    
5917 O OE1   . GLU C 34  ? 0.5492 0.7187 0.5155 -0.0571 0.0332  -0.0003 34  GLU C OE1   
5918 O OE2   . GLU C 34  ? 0.6768 0.8436 0.6361 -0.0697 0.0327  -0.0067 34  GLU C OE2   
5919 N N     . GLY C 35  ? 0.4221 0.5828 0.3976 -0.0412 0.0330  0.0074  35  GLY C N     
5920 C CA    . GLY C 35  ? 0.4682 0.6277 0.4467 -0.0330 0.0335  0.0107  35  GLY C CA    
5921 C C     . GLY C 35  ? 0.5406 0.6855 0.5202 -0.0283 0.0343  0.0088  35  GLY C C     
5922 O O     . GLY C 35  ? 0.5717 0.7139 0.5533 -0.0218 0.0347  0.0112  35  GLY C O     
5923 N N     . ILE C 36  ? 0.4429 0.5782 0.4208 -0.0313 0.0346  0.0045  36  ILE C N     
5924 C CA    . ILE C 36  ? 0.3786 0.5014 0.3575 -0.0271 0.0354  0.0029  36  ILE C CA    
5925 C C     . ILE C 36  ? 0.4574 0.5707 0.4374 -0.0246 0.0356  0.0019  36  ILE C C     
5926 O O     . ILE C 36  ? 0.5270 0.6371 0.5059 -0.0285 0.0354  -0.0005 36  ILE C O     
5927 C CB    . ILE C 36  ? 0.3649 0.4808 0.3416 -0.0312 0.0358  -0.0015 36  ILE C CB    
5928 C CG1   . ILE C 36  ? 0.2645 0.3904 0.2400 -0.0339 0.0356  -0.0005 36  ILE C CG1   
5929 C CG2   . ILE C 36  ? 0.3137 0.4169 0.2914 -0.0272 0.0366  -0.0032 36  ILE C CG2   
5930 C CD1   . ILE C 36  ? 0.3094 0.4321 0.2815 -0.0403 0.0357  -0.0050 36  ILE C CD1   
5931 N N     . PRO C 37  ? 0.4723 0.5805 0.4542 -0.0183 0.0360  0.0036  37  PRO C N     
5932 C CA    . PRO C 37  ? 0.4820 0.5812 0.4650 -0.0158 0.0362  0.0026  37  PRO C CA    
5933 C C     . PRO C 37  ? 0.5507 0.6384 0.5325 -0.0189 0.0366  -0.0021 37  PRO C C     
5934 O O     . PRO C 37  ? 0.5962 0.6788 0.5773 -0.0195 0.0370  -0.0041 37  PRO C O     
5935 C CB    . PRO C 37  ? 0.4585 0.5537 0.4429 -0.0089 0.0367  0.0049  37  PRO C CB    
5936 C CG    . PRO C 37  ? 0.4861 0.5920 0.4706 -0.0071 0.0366  0.0086  37  PRO C CG    
5937 C CD    . PRO C 37  ? 0.5212 0.6327 0.5042 -0.0131 0.0363  0.0070  37  PRO C CD    
5938 N N     . PRO C 38  ? 0.6060 0.6896 0.5877 -0.0207 0.0365  -0.0037 38  PRO C N     
5939 C CA    . PRO C 38  ? 0.6410 0.7139 0.6212 -0.0237 0.0370  -0.0080 38  PRO C CA    
5940 C C     . PRO C 38  ? 0.7061 0.7685 0.6875 -0.0197 0.0377  -0.0093 38  PRO C C     
5941 O O     . PRO C 38  ? 0.7221 0.7771 0.7022 -0.0217 0.0382  -0.0125 38  PRO C O     
5942 C CB    . PRO C 38  ? 0.5362 0.6079 0.5164 -0.0255 0.0367  -0.0084 38  PRO C CB    
5943 C CG    . PRO C 38  ? 0.4977 0.5769 0.4799 -0.0216 0.0362  -0.0044 38  PRO C CG    
5944 C CD    . PRO C 38  ? 0.5875 0.6769 0.5699 -0.0205 0.0360  -0.0016 38  PRO C CD    
5945 N N     . ASP C 39  ? 0.8800 0.9419 0.8632 -0.0142 0.0377  -0.0067 39  ASP C N     
5946 C CA    . ASP C 39  ? 0.8214 0.8738 0.8056 -0.0105 0.0382  -0.0076 39  ASP C CA    
5947 C C     . ASP C 39  ? 0.6995 0.7514 0.6833 -0.0100 0.0385  -0.0076 39  ASP C C     
5948 O O     . ASP C 39  ? 0.6384 0.6829 0.6227 -0.0078 0.0389  -0.0085 39  ASP C O     
5949 C CB    . ASP C 39  ? 0.8544 0.9056 0.8402 -0.0052 0.0381  -0.0050 39  ASP C CB    
5950 C CG    . ASP C 39  ? 0.9834 1.0321 0.9697 -0.0055 0.0380  -0.0056 39  ASP C CG    
5951 O OD1   . ASP C 39  ? 0.9475 0.9929 0.9330 -0.0094 0.0381  -0.0084 39  ASP C OD1   
5952 O OD2   . ASP C 39  ? 1.0575 1.1073 1.0448 -0.0016 0.0378  -0.0034 39  ASP C OD2   
5953 N N     . GLN C 40  ? 0.5816 0.6420 0.5646 -0.0120 0.0383  -0.0065 40  GLN C N     
5954 C CA    . GLN C 40  ? 0.5937 0.6543 0.5763 -0.0121 0.0385  -0.0068 40  GLN C CA    
5955 C C     . GLN C 40  ? 0.5060 0.5651 0.4865 -0.0172 0.0389  -0.0104 40  GLN C C     
5956 O O     . GLN C 40  ? 0.5161 0.5742 0.4959 -0.0179 0.0392  -0.0115 40  GLN C O     
5957 C CB    . GLN C 40  ? 0.5055 0.5760 0.4883 -0.0105 0.0382  -0.0030 40  GLN C CB    
5958 C CG    . GLN C 40  ? 0.5198 0.6019 0.5017 -0.0138 0.0377  -0.0017 40  GLN C CG    
5959 C CD    . GLN C 40  ? 0.5657 0.6570 0.5480 -0.0117 0.0376  0.0020  40  GLN C CD    
5960 O OE1   . GLN C 40  ? 0.6227 0.7106 0.6056 -0.0080 0.0379  0.0034  40  GLN C OE1   
5961 N NE2   . GLN C 40  ? 0.6365 0.7393 0.6182 -0.0144 0.0371  0.0036  40  GLN C NE2   
5962 N N     . GLN C 41  ? 0.3953 0.4534 0.3746 -0.0207 0.0388  -0.0124 41  GLN C N     
5963 C CA    . GLN C 41  ? 0.4088 0.4649 0.3854 -0.0257 0.0392  -0.0160 41  GLN C CA    
5964 C C     . GLN C 41  ? 0.4174 0.4626 0.3931 -0.0259 0.0401  -0.0195 41  GLN C C     
5965 O O     . GLN C 41  ? 0.2711 0.3090 0.2477 -0.0240 0.0404  -0.0203 41  GLN C O     
5966 C CB    . GLN C 41  ? 0.4819 0.5424 0.4568 -0.0302 0.0387  -0.0166 41  GLN C CB    
5967 C CG    . GLN C 41  ? 0.5445 0.6176 0.5200 -0.0307 0.0378  -0.0130 41  GLN C CG    
5968 C CD    . GLN C 41  ? 0.5301 0.6080 0.5032 -0.0366 0.0373  -0.0140 41  GLN C CD    
5969 O OE1   . GLN C 41  ? 0.4527 0.5263 0.4228 -0.0412 0.0377  -0.0175 41  GLN C OE1   
5970 N NE2   . GLN C 41  ? 0.5373 0.6241 0.5115 -0.0363 0.0366  -0.0108 41  GLN C NE2   
5971 N N     . ARG C 42  ? 0.7701 0.8148 0.7440 -0.0279 0.0407  -0.0215 42  ARG C N     
5972 C CA    . ARG C 42  ? 0.8423 0.8776 0.8149 -0.0281 0.0417  -0.0249 42  ARG C CA    
5973 C C     . ARG C 42  ? 0.8502 0.8865 0.8189 -0.0332 0.0421  -0.0279 42  ARG C C     
5974 O O     . ARG C 42  ? 0.8737 0.9168 0.8414 -0.0350 0.0419  -0.0275 42  ARG C O     
5975 C CB    . ARG C 42  ? 0.8670 0.9001 0.8411 -0.0247 0.0421  -0.0244 42  ARG C CB    
5976 C CG    . ARG C 42  ? 0.9077 0.9371 0.8849 -0.0199 0.0419  -0.0222 42  ARG C CG    
5977 C CD    . ARG C 42  ? 0.9874 1.0158 0.9657 -0.0174 0.0421  -0.0215 42  ARG C CD    
5978 N NE    . ARG C 42  ? 1.0201 1.0457 0.9964 -0.0193 0.0431  -0.0244 42  ARG C NE    
5979 C CZ    . ARG C 42  ? 0.9332 0.9630 0.9088 -0.0199 0.0432  -0.0242 42  ARG C CZ    
5980 N NH1   . ARG C 42  ? 0.9268 0.9634 0.9037 -0.0187 0.0424  -0.0210 42  ARG C NH1   
5981 N NH2   . ARG C 42  ? 0.8554 0.8826 0.8291 -0.0214 0.0442  -0.0271 42  ARG C NH2   
5982 N N     . LEU C 43  ? 0.4948 0.5243 0.4611 -0.0357 0.0427  -0.0308 43  LEU C N     
5983 C CA    . LEU C 43  ? 0.4375 0.4659 0.3993 -0.0408 0.0433  -0.0341 43  LEU C CA    
5984 C C     . LEU C 43  ? 0.4715 0.4902 0.4315 -0.0398 0.0448  -0.0373 43  LEU C C     
5985 O O     . LEU C 43  ? 0.4478 0.4588 0.4090 -0.0371 0.0454  -0.0379 43  LEU C O     
5986 C CB    . LEU C 43  ? 0.4138 0.4417 0.3735 -0.0448 0.0429  -0.0347 43  LEU C CB    
5987 C CG    . LEU C 43  ? 0.4069 0.4463 0.3674 -0.0471 0.0415  -0.0318 43  LEU C CG    
5988 C CD1   . LEU C 43  ? 0.4277 0.4655 0.3870 -0.0502 0.0411  -0.0321 43  LEU C CD1   
5989 C CD2   . LEU C 43  ? 0.3842 0.4312 0.3418 -0.0514 0.0413  -0.0325 43  LEU C CD2   
5990 N N     . ILE C 44  ? 0.5053 0.5251 0.4625 -0.0417 0.0454  -0.0394 44  ILE C N     
5991 C CA    . ILE C 44  ? 0.5046 0.5161 0.4595 -0.0407 0.0471  -0.0425 44  ILE C CA    
5992 C C     . ILE C 44  ? 0.4485 0.4559 0.3974 -0.0457 0.0480  -0.0465 44  ILE C C     
5993 O O     . ILE C 44  ? 0.4006 0.4143 0.3470 -0.0503 0.0473  -0.0468 44  ILE C O     
5994 C CB    . ILE C 44  ? 0.4884 0.5041 0.4447 -0.0384 0.0473  -0.0418 44  ILE C CB    
5995 C CG1   . ILE C 44  ? 0.4938 0.5107 0.4553 -0.0333 0.0466  -0.0384 44  ILE C CG1   
5996 C CG2   . ILE C 44  ? 0.4853 0.4944 0.4382 -0.0383 0.0490  -0.0454 44  ILE C CG2   
5997 C CD1   . ILE C 44  ? 0.4643 0.4910 0.4285 -0.0330 0.0451  -0.0346 44  ILE C CD1   
5998 N N     . PHE C 45  ? 0.4922 0.4888 0.4386 -0.0449 0.0495  -0.0494 45  PHE C N     
5999 C CA    . PHE C 45  ? 0.4649 0.4549 0.4049 -0.0489 0.0508  -0.0536 45  PHE C CA    
6000 C C     . PHE C 45  ? 0.5526 0.5334 0.4911 -0.0454 0.0528  -0.0560 45  PHE C C     
6001 O O     . PHE C 45  ? 0.5629 0.5384 0.5042 -0.0412 0.0533  -0.0551 45  PHE C O     
6002 C CB    . PHE C 45  ? 0.4120 0.3969 0.3495 -0.0523 0.0506  -0.0544 45  PHE C CB    
6003 C CG    . PHE C 45  ? 0.4990 0.4768 0.4292 -0.0572 0.0518  -0.0586 45  PHE C CG    
6004 C CD1   . PHE C 45  ? 0.4272 0.4108 0.3535 -0.0629 0.0512  -0.0598 45  PHE C CD1   
6005 C CD2   . PHE C 45  ? 0.6036 0.5685 0.5304 -0.0560 0.0537  -0.0613 45  PHE C CD2   
6006 C CE1   . PHE C 45  ? 0.5392 0.5154 0.4579 -0.0678 0.0523  -0.0639 45  PHE C CE1   
6007 C CE2   . PHE C 45  ? 0.5832 0.5402 0.5024 -0.0604 0.0550  -0.0653 45  PHE C CE2   
6008 C CZ    . PHE C 45  ? 0.5482 0.5105 0.4632 -0.0665 0.0543  -0.0667 45  PHE C CZ    
6009 N N     . ALA C 46  ? 0.7459 0.7250 0.6797 -0.0470 0.0541  -0.0591 46  ALA C N     
6010 C CA    . ALA C 46  ? 0.7974 0.7688 0.7295 -0.0433 0.0561  -0.0613 46  ALA C CA    
6011 C C     . ALA C 46  ? 0.7352 0.7097 0.6735 -0.0375 0.0559  -0.0583 46  ALA C C     
6012 O O     . ALA C 46  ? 0.7216 0.6895 0.6605 -0.0335 0.0573  -0.0588 46  ALA C O     
6013 C CB    . ALA C 46  ? 0.8383 0.7973 0.7667 -0.0432 0.0577  -0.0638 46  ALA C CB    
6014 N N     . GLY C 47  ? 0.4477 0.4322 0.3903 -0.0371 0.0542  -0.0551 47  GLY C N     
6015 C CA    . GLY C 47  ? 0.4651 0.4527 0.4125 -0.0323 0.0541  -0.0526 47  GLY C CA    
6016 C C     . GLY C 47  ? 0.5215 0.5069 0.4736 -0.0289 0.0534  -0.0499 47  GLY C C     
6017 O O     . GLY C 47  ? 0.6083 0.5947 0.5640 -0.0251 0.0534  -0.0481 47  GLY C O     
6018 N N     . LYS C 48  ? 0.5594 0.5420 0.5115 -0.0305 0.0528  -0.0497 48  LYS C N     
6019 C CA    . LYS C 48  ? 0.6171 0.5972 0.5732 -0.0275 0.0523  -0.0475 48  LYS C CA    
6020 C C     . LYS C 48  ? 0.5809 0.5668 0.5392 -0.0292 0.0504  -0.0449 48  LYS C C     
6021 O O     . LYS C 48  ? 0.5399 0.5268 0.4955 -0.0333 0.0500  -0.0459 48  LYS C O     
6022 C CB    . LYS C 48  ? 0.6330 0.6028 0.5867 -0.0270 0.0537  -0.0496 48  LYS C CB    
6023 C CG    . LYS C 48  ? 0.5881 0.5547 0.5382 -0.0314 0.0536  -0.0512 48  LYS C CG    
6024 C CD    . LYS C 48  ? 0.6335 0.5889 0.5800 -0.0310 0.0554  -0.0537 48  LYS C CD    
6025 C CE    . LYS C 48  ? 0.6460 0.5977 0.5963 -0.0275 0.0552  -0.0518 48  LYS C CE    
6026 N NZ    . LYS C 48  ? 0.5701 0.5112 0.5171 -0.0275 0.0568  -0.0537 48  LYS C NZ    
6027 N N     . GLN C 49  ? 0.7983 0.7873 0.7614 -0.0260 0.0494  -0.0417 49  GLN C N     
6028 C CA    . GLN C 49  ? 0.8701 0.8641 0.8353 -0.0267 0.0478  -0.0391 49  GLN C CA    
6029 C C     . GLN C 49  ? 0.8475 0.8361 0.8116 -0.0281 0.0480  -0.0400 49  GLN C C     
6030 O O     . GLN C 49  ? 0.9262 0.9079 0.8911 -0.0257 0.0487  -0.0405 49  GLN C O     
6031 C CB    . GLN C 49  ? 0.8812 0.8776 0.8510 -0.0226 0.0469  -0.0358 49  GLN C CB    
6032 C CG    . GLN C 49  ? 0.9286 0.9308 0.9006 -0.0225 0.0454  -0.0328 49  GLN C CG    
6033 C CD    . GLN C 49  ? 0.9897 0.9936 0.9654 -0.0184 0.0447  -0.0298 49  GLN C CD    
6034 O OE1   . GLN C 49  ? 1.0332 1.0346 1.0099 -0.0161 0.0452  -0.0298 49  GLN C OE1   
6035 N NE2   . GLN C 49  ? 0.9700 0.9780 0.9475 -0.0176 0.0436  -0.0271 49  GLN C NE2   
6036 N N     . LEU C 50  ? 0.5915 0.5836 0.5537 -0.0321 0.0472  -0.0401 50  LEU C N     
6037 C CA    . LEU C 50  ? 0.5146 0.5022 0.4753 -0.0342 0.0473  -0.0409 50  LEU C CA    
6038 C C     . LEU C 50  ? 0.5119 0.5010 0.4768 -0.0314 0.0463  -0.0379 50  LEU C C     
6039 O O     . LEU C 50  ? 0.4761 0.4730 0.4437 -0.0304 0.0450  -0.0350 50  LEU C O     
6040 C CB    . LEU C 50  ? 0.5155 0.5074 0.4727 -0.0400 0.0467  -0.0417 50  LEU C CB    
6041 C CG    . LEU C 50  ? 0.4770 0.4689 0.4292 -0.0439 0.0475  -0.0447 50  LEU C CG    
6042 C CD1   . LEU C 50  ? 0.3526 0.3470 0.3007 -0.0504 0.0469  -0.0458 50  LEU C CD1   
6043 C CD2   . LEU C 50  ? 0.4952 0.4769 0.4446 -0.0424 0.0494  -0.0479 50  LEU C CD2   
6044 N N     . GLU C 51  ? 0.6430 0.6246 0.6083 -0.0297 0.0469  -0.0384 51  GLU C N     
6045 C CA    . GLU C 51  ? 0.6588 0.6411 0.6277 -0.0272 0.0461  -0.0359 51  GLU C CA    
6046 C C     . GLU C 51  ? 0.6953 0.6809 0.6632 -0.0307 0.0452  -0.0352 51  GLU C C     
6047 O O     . GLU C 51  ? 0.7759 0.7575 0.7402 -0.0345 0.0457  -0.0372 51  GLU C O     
6048 C CB    . GLU C 51  ? 0.6840 0.6578 0.6538 -0.0242 0.0471  -0.0366 51  GLU C CB    
6049 C CG    . GLU C 51  ? 0.8326 0.8043 0.8042 -0.0203 0.0478  -0.0367 51  GLU C CG    
6050 C CD    . GLU C 51  ? 0.9469 0.9128 0.9205 -0.0169 0.0483  -0.0363 51  GLU C CD    
6051 O OE1   . GLU C 51  ? 0.9420 0.9072 0.9167 -0.0169 0.0478  -0.0353 51  GLU C OE1   
6052 O OE2   . GLU C 51  ? 0.9697 0.9323 0.9438 -0.0143 0.0493  -0.0370 51  GLU C OE2   
6053 N N     . ASP C 52  ? 0.7993 0.7920 0.7702 -0.0294 0.0439  -0.0322 52  ASP C N     
6054 C CA    . ASP C 52  ? 0.9251 0.9234 0.8951 -0.0330 0.0430  -0.0311 52  ASP C CA    
6055 C C     . ASP C 52  ? 0.9373 0.9301 0.9067 -0.0341 0.0432  -0.0315 52  ASP C C     
6056 O O     . ASP C 52  ? 0.9232 0.9196 0.8911 -0.0381 0.0425  -0.0311 52  ASP C O     
6057 C CB    . ASP C 52  ? 0.9543 0.9623 0.9275 -0.0307 0.0417  -0.0275 52  ASP C CB    
6058 C CG    . ASP C 52  ? 1.0291 1.0348 1.0060 -0.0250 0.0416  -0.0258 52  ASP C CG    
6059 O OD1   . ASP C 52  ? 1.0316 1.0294 1.0087 -0.0230 0.0425  -0.0273 52  ASP C OD1   
6060 O OD2   . ASP C 52  ? 1.0454 1.0573 1.0246 -0.0226 0.0407  -0.0229 52  ASP C OD2   
6061 N N     . GLY C 53  ? 0.9127 0.8974 0.8832 -0.0310 0.0440  -0.0322 53  GLY C N     
6062 C CA    . GLY C 53  ? 0.8718 0.8508 0.8417 -0.0319 0.0444  -0.0326 53  GLY C CA    
6063 C C     . GLY C 53  ? 0.8694 0.8401 0.8345 -0.0356 0.0456  -0.0357 53  GLY C C     
6064 O O     . GLY C 53  ? 0.8779 0.8436 0.8419 -0.0369 0.0459  -0.0360 53  GLY C O     
6065 N N     . ARG C 54  ? 0.8176 0.7864 0.7797 -0.0373 0.0464  -0.0381 54  ARG C N     
6066 C CA    . ARG C 54  ? 0.8072 0.7679 0.7639 -0.0411 0.0477  -0.0412 54  ARG C CA    
6067 C C     . ARG C 54  ? 0.7836 0.7495 0.7367 -0.0473 0.0469  -0.0418 54  ARG C C     
6068 O O     . ARG C 54  ? 0.7434 0.7197 0.6985 -0.0484 0.0454  -0.0396 54  ARG C O     
6069 C CB    . ARG C 54  ? 0.8592 0.8135 0.8141 -0.0388 0.0493  -0.0437 54  ARG C CB    
6070 C CG    . ARG C 54  ? 0.9390 0.8867 0.8964 -0.0333 0.0504  -0.0434 54  ARG C CG    
6071 C CD    . ARG C 54  ? 0.9979 0.9506 0.9597 -0.0287 0.0500  -0.0419 54  ARG C CD    
6072 N NE    . ARG C 54  ? 0.9752 0.9222 0.9388 -0.0240 0.0512  -0.0419 54  ARG C NE    
6073 C CZ    . ARG C 54  ? 0.9112 0.8567 0.8779 -0.0211 0.0510  -0.0402 54  ARG C CZ    
6074 N NH1   . ARG C 54  ? 0.8990 0.8481 0.8675 -0.0222 0.0497  -0.0383 54  ARG C NH1   
6075 N NH2   . ARG C 54  ? 0.8744 0.8155 0.8426 -0.0171 0.0520  -0.0402 54  ARG C NH2   
6076 N N     . THR C 55  ? 0.8911 0.8495 0.8384 -0.0515 0.0479  -0.0448 55  THR C N     
6077 C CA    . THR C 55  ? 0.9557 0.9180 0.8988 -0.0582 0.0472  -0.0458 55  THR C CA    
6078 C C     . THR C 55  ? 0.9663 0.9260 0.9047 -0.0606 0.0482  -0.0490 55  THR C C     
6079 O O     . THR C 55  ? 0.9239 0.8776 0.8618 -0.0570 0.0497  -0.0507 55  THR C O     
6080 C CB    . THR C 55  ? 1.0233 0.9783 0.9623 -0.0626 0.0476  -0.0468 55  THR C CB    
6081 O OG1   . THR C 55  ? 1.0626 1.0041 0.9980 -0.0613 0.0497  -0.0497 55  THR C OG1   
6082 C CG2   . THR C 55  ? 1.0343 0.9921 0.9776 -0.0609 0.0466  -0.0436 55  THR C CG2   
6083 N N     . LEU C 56  ? 0.8805 0.8449 0.8151 -0.0669 0.0475  -0.0498 56  LEU C N     
6084 C CA    . LEU C 56  ? 0.8023 0.7649 0.7319 -0.0697 0.0483  -0.0530 56  LEU C CA    
6085 C C     . LEU C 56  ? 0.8450 0.7931 0.7684 -0.0712 0.0503  -0.0568 56  LEU C C     
6086 O O     . LEU C 56  ? 0.8895 0.8328 0.8091 -0.0711 0.0517  -0.0597 56  LEU C O     
6087 C CB    . LEU C 56  ? 0.6935 0.6657 0.6205 -0.0765 0.0469  -0.0527 56  LEU C CB    
6088 C CG    . LEU C 56  ? 0.6107 0.5978 0.5430 -0.0760 0.0448  -0.0485 56  LEU C CG    
6089 C CD1   . LEU C 56  ? 0.6320 0.6244 0.5610 -0.0835 0.0436  -0.0482 56  LEU C CD1   
6090 C CD2   . LEU C 56  ? 0.6218 0.6182 0.5562 -0.0741 0.0444  -0.0477 56  LEU C CD2   
6091 N N     . SER C 57  ? 1.0749 1.0157 0.9970 -0.0722 0.0506  -0.0567 57  SER C N     
6092 C CA    . SER C 57  ? 1.0916 1.0172 1.0077 -0.0728 0.0528  -0.0600 57  SER C CA    
6093 C C     . SER C 57  ? 1.0220 0.9411 0.9406 -0.0653 0.0545  -0.0604 57  SER C C     
6094 O O     . SER C 57  ? 1.0521 0.9608 0.9659 -0.0644 0.0566  -0.0634 57  SER C O     
6095 C CB    . SER C 57  ? 1.1016 1.0216 1.0159 -0.0759 0.0526  -0.0593 57  SER C CB    
6096 O OG    . SER C 57  ? 1.0829 1.0083 0.9939 -0.0836 0.0511  -0.0592 57  SER C OG    
6097 N N     . ASP C 58  ? 0.8996 0.8251 0.8255 -0.0600 0.0536  -0.0572 58  ASP C N     
6098 C CA    . ASP C 58  ? 0.9162 0.8373 0.8451 -0.0530 0.0550  -0.0571 58  ASP C CA    
6099 C C     . ASP C 58  ? 0.8341 0.7577 0.7628 -0.0508 0.0557  -0.0585 58  ASP C C     
6100 O O     . ASP C 58  ? 0.8344 0.7521 0.7631 -0.0462 0.0574  -0.0595 58  ASP C O     
6101 C CB    . ASP C 58  ? 0.9664 0.8937 0.9028 -0.0486 0.0538  -0.0533 58  ASP C CB    
6102 C CG    . ASP C 58  ? 0.9790 0.9002 0.9157 -0.0482 0.0540  -0.0522 58  ASP C CG    
6103 O OD1   . ASP C 58  ? 0.9912 0.9013 0.9246 -0.0471 0.0559  -0.0540 58  ASP C OD1   
6104 O OD2   . ASP C 58  ? 0.9914 0.9193 0.9319 -0.0488 0.0523  -0.0494 58  ASP C OD2   
6105 N N     . TYR C 59  ? 0.6517 0.5848 0.5805 -0.0538 0.0544  -0.0583 59  TYR C N     
6106 C CA    . TYR C 59  ? 0.7149 0.6509 0.6431 -0.0523 0.0550  -0.0596 59  TYR C CA    
6107 C C     . TYR C 59  ? 0.6792 0.6096 0.5996 -0.0568 0.0563  -0.0637 59  TYR C C     
6108 O O     . TYR C 59  ? 0.6679 0.6017 0.5872 -0.0565 0.0567  -0.0650 59  TYR C O     
6109 C CB    . TYR C 59  ? 0.7212 0.6711 0.6542 -0.0523 0.0530  -0.0568 59  TYR C CB    
6110 C CG    . TYR C 59  ? 0.6665 0.6208 0.6068 -0.0469 0.0521  -0.0533 59  TYR C CG    
6111 C CD1   . TYR C 59  ? 0.6455 0.5976 0.5885 -0.0413 0.0531  -0.0530 59  TYR C CD1   
6112 C CD2   . TYR C 59  ? 0.6362 0.5966 0.5801 -0.0473 0.0504  -0.0502 59  TYR C CD2   
6113 C CE1   . TYR C 59  ? 0.5908 0.5463 0.5399 -0.0367 0.0523  -0.0499 59  TYR C CE1   
6114 C CE2   . TYR C 59  ? 0.6064 0.5699 0.5563 -0.0423 0.0497  -0.0472 59  TYR C CE2   
6115 C CZ    . TYR C 59  ? 0.5720 0.5328 0.5244 -0.0372 0.0506  -0.0472 59  TYR C CZ    
6116 O OH    . TYR C 59  ? 0.5529 0.5162 0.5106 -0.0327 0.0500  -0.0444 59  TYR C OH    
6117 N N     . ASN C 60  ? 0.6823 0.6044 0.5970 -0.0612 0.0569  -0.0657 60  ASN C N     
6118 C CA    . ASN C 60  ? 0.7292 0.6460 0.6357 -0.0666 0.0579  -0.0696 60  ASN C CA    
6119 C C     . ASN C 60  ? 0.7816 0.7105 0.6880 -0.0714 0.0561  -0.0693 60  ASN C C     
6120 O O     . ASN C 60  ? 0.7355 0.6632 0.6361 -0.0750 0.0568  -0.0724 60  ASN C O     
6121 C CB    . ASN C 60  ? 0.7573 0.6653 0.6601 -0.0629 0.0605  -0.0728 60  ASN C CB    
6122 C CG    . ASN C 60  ? 0.7903 0.6855 0.6835 -0.0670 0.0623  -0.0770 60  ASN C CG    
6123 O OD1   . ASN C 60  ? 0.8215 0.7130 0.7112 -0.0723 0.0617  -0.0774 60  ASN C OD1   
6124 N ND2   . ASN C 60  ? 0.7464 0.6347 0.6351 -0.0646 0.0646  -0.0802 60  ASN C ND2   
6125 N N     . ILE C 61  ? 0.9234 0.8642 0.8360 -0.0712 0.0539  -0.0654 61  ILE C N     
6126 C CA    . ILE C 61  ? 0.9276 0.8809 0.8405 -0.0757 0.0522  -0.0644 61  ILE C CA    
6127 C C     . ILE C 61  ? 0.9674 0.9187 0.8739 -0.0838 0.0517  -0.0661 61  ILE C C     
6128 O O     . ILE C 61  ? 0.9654 0.9133 0.8718 -0.0857 0.0512  -0.0651 61  ILE C O     
6129 C CB    . ILE C 61  ? 0.8226 0.7884 0.7436 -0.0726 0.0502  -0.0596 61  ILE C CB    
6130 C CG1   . ILE C 61  ? 0.7348 0.7028 0.6608 -0.0657 0.0507  -0.0584 61  ILE C CG1   
6131 C CG2   . ILE C 61  ? 0.8527 0.8317 0.7737 -0.0777 0.0483  -0.0580 61  ILE C CG2   
6132 C CD1   . ILE C 61  ? 0.7403 0.7203 0.6732 -0.0628 0.0489  -0.0541 61  ILE C CD1   
6133 N N     . GLN C 62  ? 0.9560 0.9091 0.8569 -0.0890 0.0518  -0.0688 62  GLN C N     
6134 C CA    . GLN C 62  ? 0.9611 0.9099 0.8543 -0.0972 0.0517  -0.0713 62  GLN C CA    
6135 C C     . GLN C 62  ? 0.9592 0.9211 0.8510 -0.1035 0.0500  -0.0708 62  GLN C C     
6136 O O     . GLN C 62  ? 0.9206 0.8957 0.8181 -0.1011 0.0487  -0.0680 62  GLN C O     
6137 C CB    . GLN C 62  ? 0.9790 0.9121 0.8639 -0.0980 0.0543  -0.0764 62  GLN C CB    
6138 C CG    . GLN C 62  ? 1.0569 0.9762 0.9366 -0.1007 0.0552  -0.0780 62  GLN C CG    
6139 C CD    . GLN C 62  ? 1.0681 0.9839 0.9539 -0.0947 0.0554  -0.0750 62  GLN C CD    
6140 O OE1   . GLN C 62  ? 1.1136 1.0376 1.0048 -0.0951 0.0535  -0.0714 62  GLN C OE1   
6141 N NE2   . GLN C 62  ? 1.0498 0.9541 0.9349 -0.0888 0.0576  -0.0766 62  GLN C NE2   
6142 N N     . LYS C 63  ? 0.9682 0.9268 0.8523 -0.1117 0.0498  -0.0734 63  LYS C N     
6143 C CA    . LYS C 63  ? 0.9645 0.9362 0.8469 -0.1185 0.0481  -0.0729 63  LYS C CA    
6144 C C     . LYS C 63  ? 0.9984 0.9755 0.8801 -0.1173 0.0485  -0.0743 63  LYS C C     
6145 O O     . LYS C 63  ? 1.0634 1.0306 0.9419 -0.1144 0.0505  -0.0777 63  LYS C O     
6146 C CB    . LYS C 63  ? 1.0119 0.9769 0.8851 -0.1280 0.0481  -0.0759 63  LYS C CB    
6147 C CG    . LYS C 63  ? 1.0884 1.0677 0.9596 -0.1361 0.0460  -0.0750 63  LYS C CG    
6148 C CD    . LYS C 63  ? 1.0896 1.0824 0.9672 -0.1369 0.0437  -0.0697 63  LYS C CD    
6149 C CE    . LYS C 63  ? 1.0747 1.0804 0.9491 -0.1462 0.0417  -0.0688 63  LYS C CE    
6150 N NZ    . LYS C 63  ? 1.0441 1.0397 0.9090 -0.1554 0.0419  -0.0722 63  LYS C NZ    
6151 N N     . GLU C 64  ? 0.9686 0.9623 0.8538 -0.1192 0.0467  -0.0715 64  GLU C N     
6152 C CA    . GLU C 64  ? 0.9207 0.9220 0.8061 -0.1181 0.0468  -0.0721 64  GLU C CA    
6153 C C     . GLU C 64  ? 0.8661 0.8661 0.7572 -0.1090 0.0478  -0.0711 64  GLU C C     
6154 O O     . GLU C 64  ? 0.9445 0.9480 0.8351 -0.1077 0.0484  -0.0722 64  GLU C O     
6155 C CB    . GLU C 64  ? 0.9108 0.9067 0.7866 -0.1246 0.0478  -0.0773 64  GLU C CB    
6156 C CG    . GLU C 64  ? 0.9366 0.9294 0.8049 -0.1342 0.0472  -0.0793 64  GLU C CG    
6157 C CD    . GLU C 64  ? 0.9669 0.9766 0.8350 -0.1411 0.0449  -0.0772 64  GLU C CD    
6158 O OE1   . GLU C 64  ? 0.9598 0.9842 0.8342 -0.1380 0.0438  -0.0737 64  GLU C OE1   
6159 O OE2   . GLU C 64  ? 0.9767 0.9851 0.8382 -0.1498 0.0443  -0.0789 64  GLU C OE2   
6160 N N     . SER C 65  ? 0.6004 0.5962 0.4971 -0.1029 0.0480  -0.0688 65  SER C N     
6161 C CA    . SER C 65  ? 0.5418 0.5361 0.4439 -0.0945 0.0489  -0.0677 65  SER C CA    
6162 C C     . SER C 65  ? 0.6230 0.6327 0.5326 -0.0914 0.0473  -0.0629 65  SER C C     
6163 O O     . SER C 65  ? 0.6427 0.6621 0.5554 -0.0933 0.0455  -0.0595 65  SER C O     
6164 C CB    . SER C 65  ? 0.6062 0.5898 0.5110 -0.0894 0.0499  -0.0671 65  SER C CB    
6165 O OG    . SER C 65  ? 0.6774 0.6457 0.5755 -0.0911 0.0517  -0.0713 65  SER C OG    
6166 N N     . THR C 66  ? 0.7431 0.7549 0.6555 -0.0864 0.0479  -0.0625 66  THR C N     
6167 C CA    . THR C 66  ? 0.7641 0.7890 0.6833 -0.0829 0.0465  -0.0581 66  THR C CA    
6168 C C     . THR C 66  ? 0.7239 0.7451 0.6494 -0.0752 0.0468  -0.0557 66  THR C C     
6169 O O     . THR C 66  ? 0.7041 0.7153 0.6289 -0.0715 0.0484  -0.0578 66  THR C O     
6170 C CB    . THR C 66  ? 0.8212 0.8530 0.7393 -0.0832 0.0467  -0.0588 66  THR C CB    
6171 O OG1   . THR C 66  ? 0.8238 0.8598 0.7359 -0.0908 0.0463  -0.0610 66  THR C OG1   
6172 C CG2   . THR C 66  ? 0.8247 0.8693 0.7498 -0.0792 0.0454  -0.0538 66  THR C CG2   
6173 N N     . LEU C 67  ? 0.6183 0.6478 0.5496 -0.0728 0.0453  -0.0512 67  LEU C N     
6174 C CA    . LEU C 67  ? 0.5945 0.6226 0.5320 -0.0658 0.0453  -0.0484 67  LEU C CA    
6175 C C     . LEU C 67  ? 0.5811 0.6205 0.5228 -0.0629 0.0444  -0.0449 67  LEU C C     
6176 O O     . LEU C 67  ? 0.6003 0.6501 0.5411 -0.0663 0.0435  -0.0438 67  LEU C O     
6177 C CB    . LEU C 67  ? 0.5661 0.5934 0.5065 -0.0648 0.0445  -0.0460 67  LEU C CB    
6178 C CG    . LEU C 67  ? 0.6636 0.6792 0.6005 -0.0669 0.0454  -0.0488 67  LEU C CG    
6179 C CD1   . LEU C 67  ? 0.6732 0.6879 0.6032 -0.0746 0.0454  -0.0519 67  LEU C CD1   
6180 C CD2   . LEU C 67  ? 0.6370 0.6523 0.5777 -0.0649 0.0446  -0.0461 67  LEU C CD2   
6181 N N     . HIS C 68  ? 0.3800 0.4171 0.3260 -0.0568 0.0447  -0.0432 68  HIS C N     
6182 C CA    . HIS C 68  ? 0.4007 0.4470 0.3507 -0.0537 0.0440  -0.0398 68  HIS C CA    
6183 C C     . HIS C 68  ? 0.3929 0.4417 0.3482 -0.0494 0.0430  -0.0356 68  HIS C C     
6184 O O     . HIS C 68  ? 0.3603 0.4013 0.3173 -0.0465 0.0434  -0.0358 68  HIS C O     
6185 C CB    . HIS C 68  ? 0.4515 0.4943 0.4018 -0.0506 0.0451  -0.0410 68  HIS C CB    
6186 C CG    . HIS C 68  ? 0.4190 0.4639 0.3646 -0.0544 0.0457  -0.0439 68  HIS C CG    
6187 N ND1   . HIS C 68  ? 0.4187 0.4551 0.3589 -0.0574 0.0470  -0.0485 68  HIS C ND1   
6188 C CD2   . HIS C 68  ? 0.4161 0.4708 0.3613 -0.0560 0.0452  -0.0429 68  HIS C CD2   
6189 C CE1   . HIS C 68  ? 0.4122 0.4528 0.3488 -0.0606 0.0474  -0.0504 68  HIS C CE1   
6190 N NE2   . HIS C 68  ? 0.3945 0.4466 0.3342 -0.0599 0.0462  -0.0470 68  HIS C NE2   
6191 N N     . LEU C 69  ? 0.4310 0.4909 0.3885 -0.0490 0.0419  -0.0320 69  LEU C N     
6192 C CA    . LEU C 69  ? 0.4471 0.5104 0.4091 -0.0448 0.0411  -0.0279 69  LEU C CA    
6193 C C     . LEU C 69  ? 0.4394 0.5062 0.4045 -0.0403 0.0410  -0.0251 69  LEU C C     
6194 O O     . LEU C 69  ? 0.4779 0.5517 0.4421 -0.0416 0.0408  -0.0245 69  LEU C O     
6195 C CB    . LEU C 69  ? 0.4169 0.4902 0.3789 -0.0475 0.0399  -0.0254 69  LEU C CB    
6196 C CG    . LEU C 69  ? 0.3929 0.4703 0.3589 -0.0434 0.0391  -0.0212 69  LEU C CG    
6197 C CD1   . LEU C 69  ? 0.3484 0.4159 0.3158 -0.0408 0.0394  -0.0220 69  LEU C CD1   
6198 C CD2   . LEU C 69  ? 0.4404 0.5293 0.4059 -0.0467 0.0381  -0.0189 69  LEU C CD2   
6199 N N     . VAL C 70  ? 0.4133 0.4747 0.3814 -0.0354 0.0411  -0.0236 70  VAL C N     
6200 C CA    . VAL C 70  ? 0.4422 0.5054 0.4132 -0.0309 0.0410  -0.0207 70  VAL C CA    
6201 C C     . VAL C 70  ? 0.5250 0.5885 0.4991 -0.0269 0.0403  -0.0172 70  VAL C C     
6202 O O     . VAL C 70  ? 0.4528 0.5088 0.4278 -0.0252 0.0405  -0.0180 70  VAL C O     
6203 C CB    . VAL C 70  ? 0.4171 0.4717 0.3882 -0.0289 0.0419  -0.0227 70  VAL C CB    
6204 C CG1   . VAL C 70  ? 0.3386 0.3958 0.3122 -0.0252 0.0417  -0.0197 70  VAL C CG1   
6205 C CG2   . VAL C 70  ? 0.3827 0.4356 0.3503 -0.0327 0.0428  -0.0267 70  VAL C CG2   
6206 N N     . LEU C 71  ? 0.6298 0.7019 0.6052 -0.0253 0.0397  -0.0134 71  LEU C N     
6207 C CA    . LEU C 71  ? 0.5395 0.6125 0.5173 -0.0212 0.0392  -0.0100 71  LEU C CA    
6208 C C     . LEU C 71  ? 0.4949 0.5618 0.4747 -0.0162 0.0394  -0.0084 71  LEU C C     
6209 O O     . LEU C 71  ? 0.4160 0.4842 0.3961 -0.0149 0.0395  -0.0072 71  LEU C O     
6210 C CB    . LEU C 71  ? 0.5689 0.6541 0.5469 -0.0213 0.0385  -0.0064 71  LEU C CB    
6211 C CG    . LEU C 71  ? 0.5799 0.6712 0.5566 -0.0256 0.0380  -0.0070 71  LEU C CG    
6212 C CD1   . LEU C 71  ? 0.5908 0.6746 0.5679 -0.0253 0.0381  -0.0086 71  LEU C CD1   
6213 C CD2   . LEU C 71  ? 0.5296 0.6229 0.5032 -0.0316 0.0382  -0.0104 71  LEU C CD2   
6214 N N     . ARG C 72  ? 0.5223 0.5825 0.5032 -0.0137 0.0394  -0.0085 72  ARG C N     
6215 C CA    . ARG C 72  ? 0.5654 0.6190 0.5477 -0.0094 0.0396  -0.0072 72  ARG C CA    
6216 C C     . ARG C 72  ? 0.5853 0.6439 0.5685 -0.0058 0.0392  -0.0029 72  ARG C C     
6217 O O     . ARG C 72  ? 0.5859 0.6517 0.5692 -0.0054 0.0389  -0.0006 72  ARG C O     
6218 C CB    . ARG C 72  ? 0.4557 0.5007 0.4388 -0.0080 0.0397  -0.0087 72  ARG C CB    
6219 C CG    . ARG C 72  ? 0.4314 0.4703 0.4136 -0.0108 0.0403  -0.0127 72  ARG C CG    
6220 C CD    . ARG C 72  ? 0.5000 0.5332 0.4827 -0.0102 0.0403  -0.0138 72  ARG C CD    
6221 N NE    . ARG C 72  ? 0.5463 0.5755 0.5307 -0.0059 0.0401  -0.0118 72  ARG C NE    
6222 C CZ    . ARG C 72  ? 0.6936 0.7156 0.6787 -0.0046 0.0403  -0.0130 72  ARG C CZ    
6223 N NH1   . ARG C 72  ? 0.7724 0.7905 0.7569 -0.0069 0.0407  -0.0159 72  ARG C NH1   
6224 N NH2   . ARG C 72  ? 0.6970 0.7156 0.6832 -0.0009 0.0401  -0.0112 72  ARG C NH2   
6225 N N     . LEU C 73  ? 0.5614 0.6160 0.5450 -0.0031 0.0394  -0.0017 73  LEU C N     
6226 C CA    . LEU C 73  ? 0.6326 0.6904 0.6165 0.0005  0.0393  0.0024  73  LEU C CA    
6227 C C     . LEU C 73  ? 0.6342 0.6832 0.6184 0.0046  0.0394  0.0037  73  LEU C C     
6228 O O     . LEU C 73  ? 0.6025 0.6464 0.5866 0.0048  0.0395  0.0033  73  LEU C O     
6229 C CB    . LEU C 73  ? 0.6488 0.7116 0.6322 -0.0008 0.0393  0.0033  73  LEU C CB    
6230 C CG    . LEU C 73  ? 0.5988 0.6709 0.5814 -0.0050 0.0392  0.0023  73  LEU C CG    
6231 C CD1   . LEU C 73  ? 0.6465 0.7209 0.6286 -0.0062 0.0394  0.0025  73  LEU C CD1   
6232 C CD2   . LEU C 73  ? 0.5806 0.6627 0.5633 -0.0043 0.0389  0.0055  73  LEU C CD2   
6233 N N     . ARG C 74  ? 0.6795 0.7266 0.6639 0.0077  0.0393  0.0051  74  ARG C N     
6234 C CA    . ARG C 74  ? 0.6890 0.7279 0.6730 0.0115  0.0394  0.0065  74  ARG C CA    
6235 C C     . ARG C 74  ? 0.7859 0.8274 0.7692 0.0159  0.0395  0.0107  74  ARG C C     
6236 O O     . ARG C 74  ? 0.8191 0.8600 0.8022 0.0187  0.0396  0.0117  74  ARG C O     
6237 C CB    . ARG C 74  ? 0.7567 0.7879 0.7412 0.0120  0.0394  0.0043  74  ARG C CB    
6238 C CG    . ARG C 74  ? 0.8483 0.8697 0.8322 0.0138  0.0395  0.0040  74  ARG C CG    
6239 C CD    . ARG C 74  ? 0.8682 0.8883 0.8522 0.0112  0.0395  0.0028  74  ARG C CD    
6240 N NE    . ARG C 74  ? 0.8604 0.8784 0.8452 0.0080  0.0396  -0.0009 74  ARG C NE    
6241 C CZ    . ARG C 74  ? 0.7943 0.8136 0.7793 0.0053  0.0398  -0.0025 74  ARG C CZ    
6242 N NH1   . ARG C 74  ? 0.7295 0.7528 0.7140 0.0050  0.0398  -0.0007 74  ARG C NH1   
6243 N NH2   . ARG C 74  ? 0.7376 0.7545 0.7231 0.0030  0.0401  -0.0057 74  ARG C NH2   
6244 N N     . GLY C 75  ? 0.9540 0.9982 0.9365 0.0169  0.0397  0.0132  75  GLY C N     
6245 C CA    . GLY C 75  ? 1.0068 1.0525 0.9882 0.0215  0.0400  0.0174  75  GLY C CA    
6246 C C     . GLY C 75  ? 1.0614 1.0967 1.0412 0.0241  0.0402  0.0184  75  GLY C C     
6247 O O     . GLY C 75  ? 1.1547 1.1886 1.1328 0.0283  0.0406  0.0219  75  GLY C O     
6248 N N     . GLY C 76  ? 0.7855 0.8137 0.7656 0.0216  0.0399  0.0155  76  GLY C N     
6249 C CA    . GLY C 76  ? 0.6559 0.6745 0.6344 0.0228  0.0400  0.0161  76  GLY C CA    
6250 C C     . GLY C 76  ? 0.5573 0.5730 0.5368 0.0188  0.0397  0.0132  76  GLY C C     
6251 O O     . GLY C 76  ? 0.4749 0.4939 0.4560 0.0156  0.0396  0.0103  76  GLY C O     
6252 P PG    . ANP D .   ? 0.5775 0.5688 0.6011 0.0315  0.0450  -0.0003 401 ANP A PG    
6253 O O1G   . ANP D .   ? 0.4908 0.4792 0.5142 0.0316  0.0449  -0.0007 401 ANP A O1G   
6254 O O2G   . ANP D .   ? 0.5439 0.5400 0.5669 0.0304  0.0437  -0.0004 401 ANP A O2G   
6255 O O3G   . ANP D .   ? 0.5702 0.5579 0.5922 0.0302  0.0448  -0.0022 401 ANP A O3G   
6256 P PB    . ANP D .   ? 0.3494 0.3440 0.3775 0.0363  0.0484  0.0053  401 ANP A PB    
6257 O O1B   . ANP D .   ? 0.4761 0.4778 0.5060 0.0375  0.0488  0.0077  401 ANP A O1B   
6258 O O2B   . ANP D .   ? 0.3563 0.3458 0.3844 0.0379  0.0503  0.0059  401 ANP A O2B   
6259 N N3B   . ANP D .   ? 0.4479 0.4413 0.4739 0.0339  0.0470  0.0024  401 ANP A N3B   
6260 P PA    . ANP D .   ? 0.4562 0.4555 0.4844 0.0350  0.0461  0.0053  401 ANP A PA    
6261 O O1A   . ANP D .   ? 0.3450 0.3419 0.3710 0.0333  0.0446  0.0028  401 ANP A O1A   
6262 O O2A   . ANP D .   ? 0.3635 0.3694 0.3923 0.0350  0.0456  0.0063  401 ANP A O2A   
6263 O O3A   . ANP D .   ? 0.5151 0.5090 0.5430 0.0357  0.0476  0.0051  401 ANP A O3A   
6264 O "O5'" . ANP D .   ? 0.4340 0.4340 0.4638 0.0364  0.0468  0.0076  401 ANP A "O5'" 
6265 C "C5'" . ANP D .   ? 0.5227 0.5166 0.5518 0.0363  0.0476  0.0072  401 ANP A "C5'" 
6266 C "C4'" . ANP D .   ? 0.4975 0.4911 0.5275 0.0369  0.0481  0.0091  401 ANP A "C4'" 
6267 O "O4'" . ANP D .   ? 0.5011 0.4974 0.5308 0.0360  0.0467  0.0085  401 ANP A "O4'" 
6268 C "C3'" . ANP D .   ? 0.3461 0.3438 0.3781 0.0389  0.0491  0.0122  401 ANP A "C3'" 
6269 O "O3'" . ANP D .   ? 0.4058 0.3990 0.4380 0.0403  0.0510  0.0135  401 ANP A "O3'" 
6270 C "C2'" . ANP D .   ? 0.3783 0.3792 0.4112 0.0388  0.0485  0.0136  401 ANP A "C2'" 
6271 O "O2'" . ANP D .   ? 0.3605 0.3589 0.3943 0.0402  0.0502  0.0164  401 ANP A "O2'" 
6272 C "C1'" . ANP D .   ? 0.3999 0.3990 0.4314 0.0371  0.0473  0.0115  401 ANP A "C1'" 
6273 N N9    . ANP D .   ? 0.4106 0.4151 0.4422 0.0367  0.0459  0.0112  401 ANP A N9    
6274 C C8    . ANP D .   ? 0.3466 0.3566 0.3783 0.0369  0.0451  0.0111  401 ANP A C8    
6275 N N7    . ANP D .   ? 0.3700 0.3833 0.4012 0.0365  0.0439  0.0107  401 ANP A N7    
6276 C C5    . ANP D .   ? 0.4222 0.4328 0.4532 0.0361  0.0440  0.0108  401 ANP A C5    
6277 C C6    . ANP D .   ? 0.4147 0.4275 0.4453 0.0357  0.0432  0.0107  401 ANP A C6    
6278 N N6    . ANP D .   ? 0.5450 0.5631 0.5750 0.0360  0.0420  0.0102  401 ANP A N6    
6279 N N1    . ANP D .   ? 0.4635 0.4734 0.4938 0.0350  0.0434  0.0110  401 ANP A N1    
6280 C C2    . ANP D .   ? 0.4099 0.4140 0.4402 0.0344  0.0444  0.0113  401 ANP A C2    
6281 N N3    . ANP D .   ? 0.3473 0.3486 0.3779 0.0350  0.0454  0.0112  401 ANP A N3    
6282 C C4    . ANP D .   ? 0.4211 0.4261 0.4522 0.0359  0.0452  0.0111  401 ANP A C4    
6296 N N1    . AR6 E .   ? 1.2048 1.1910 1.1816 -0.0132 0.0472  -0.0330 401 AR6 B N1    
6297 C C2    . AR6 E .   ? 1.2129 1.1982 1.1902 -0.0114 0.0478  -0.0332 401 AR6 B C2    
6298 N N3    . AR6 E .   ? 1.2407 1.2291 1.2204 -0.0094 0.0470  -0.0308 401 AR6 B N3    
6299 C C4    . AR6 E .   ? 1.2380 1.2296 1.2195 -0.0087 0.0457  -0.0282 401 AR6 B C4    
6300 C C5    . AR6 E .   ? 1.2481 1.2409 1.2292 -0.0099 0.0452  -0.0280 401 AR6 B C5    
6301 C C6    . AR6 E .   ? 1.2286 1.2189 1.2074 -0.0124 0.0458  -0.0304 401 AR6 B C6    
6302 N N6    . AR6 E .   ? 1.2211 1.2126 1.1991 -0.0145 0.0454  -0.0304 401 AR6 B N6    
6303 N N7    . AR6 E .   ? 1.2347 1.2309 1.2176 -0.0084 0.0440  -0.0251 401 AR6 B N7    
6304 C C8    . AR6 E .   ? 1.2027 1.1991 1.1868 -0.0064 0.0438  -0.0237 401 AR6 B C8    
6305 N N9    . AR6 E .   ? 1.2000 1.1940 1.1834 -0.0067 0.0448  -0.0255 401 AR6 B N9    
6306 P PA    . AR6 E .   ? 1.3313 1.3236 1.3191 0.0017  0.0416  -0.0148 401 AR6 B PA    
6307 P PB    . AR6 E .   ? 0.7338 0.7357 0.7204 0.0012  0.0410  -0.0110 401 AR6 B PB    
6308 C "C1'" . AR6 E .   ? 1.1834 1.1767 1.1673 -0.0056 0.0452  -0.0253 401 AR6 B "C1'" 
6309 O O1A   . AR6 E .   ? 1.3661 1.3593 1.3539 0.0014  0.0417  -0.0158 401 AR6 B O1A   
6310 O O1B   . AR6 E .   ? 0.6378 0.6412 0.6239 0.0027  0.0404  -0.0077 401 AR6 B O1B   
6311 C C1D   . AR6 E .   ? 0.9443 0.9541 0.9295 -0.0042 0.0416  -0.0165 401 AR6 B C1D   
6312 O O1D   . AR6 E .   ? 0.9462 0.9614 0.9316 -0.0029 0.0409  -0.0135 401 AR6 B O1D   
6313 C "C2'" . AR6 E .   ? 1.0905 1.0791 1.0754 -0.0040 0.0456  -0.0258 401 AR6 B "C2'" 
6314 O "O2'" . AR6 E .   ? 0.9699 0.9556 0.9533 -0.0046 0.0470  -0.0285 401 AR6 B "O2'" 
6315 O O2A   . AR6 E .   ? 1.4103 1.3971 1.3989 0.0031  0.0414  -0.0146 401 AR6 B O2A   
6316 O O2B   . AR6 E .   ? 0.7550 0.7559 0.7418 0.0001  0.0415  -0.0121 401 AR6 B O2B   
6317 C C2D   . AR6 E .   ? 0.9394 0.9521 0.9230 -0.0074 0.0422  -0.0187 401 AR6 B C2D   
6318 O O2D   . AR6 E .   ? 0.8950 0.9145 0.8776 -0.0095 0.0418  -0.0181 401 AR6 B O2D   
6319 C "C3'" . AR6 E .   ? 1.1944 1.1841 1.1805 -0.0026 0.0453  -0.0239 401 AR6 B "C3'" 
6320 O "O3'" . AR6 E .   ? 1.2120 1.2029 1.1972 -0.0032 0.0462  -0.0252 401 AR6 B "O3'" 
6321 O O3A   . AR6 E .   ? 1.0422 1.0380 1.0294 0.0027  0.0409  -0.0118 401 AR6 B O3A   
6322 C C3D   . AR6 E .   ? 0.9073 0.9204 0.8912 -0.0064 0.0422  -0.0176 401 AR6 B C3D   
6323 O O3D   . AR6 E .   ? 0.8950 0.9158 0.8783 -0.0075 0.0418  -0.0160 401 AR6 B O3D   
6324 C "C4'" . AR6 E .   ? 1.2608 1.2544 1.2471 -0.0027 0.0443  -0.0217 401 AR6 B "C4'" 
6325 O "O4'" . AR6 E .   ? 1.2580 1.2542 1.2433 -0.0041 0.0441  -0.0221 401 AR6 B "O4'" 
6326 C C4D   . AR6 E .   ? 0.9078 0.9179 0.8931 -0.0035 0.0417  -0.0155 401 AR6 B C4D   
6327 O O4D   . AR6 E .   ? 0.9077 0.9132 0.8936 -0.0026 0.0417  -0.0163 401 AR6 B O4D   
6328 C "C5'" . AR6 E .   ? 1.2725 1.2637 1.2601 -0.0007 0.0433  -0.0193 401 AR6 B "C5'" 
6329 O "O5'" . AR6 E .   ? 1.3119 1.3062 1.2993 -0.0003 0.0425  -0.0169 401 AR6 B "O5'" 
6330 C C5D   . AR6 E .   ? 0.8452 0.8515 0.8310 -0.0025 0.0420  -0.0155 401 AR6 B C5D   
6331 O O5D   . AR6 E .   ? 0.7864 0.7939 0.7724 -0.0008 0.0413  -0.0125 401 AR6 B O5D   
6353 O O     . HOH F .   ? 0.4295 0.4305 0.4521 0.0147  0.0417  0.0146  501 HOH A O     
6354 O O     . HOH F .   ? 0.4309 0.4065 0.4218 0.0332  0.0386  -0.0095 502 HOH A O     
6355 O O     . HOH F .   ? 0.5685 0.5848 0.5787 0.0029  0.0373  0.0053  503 HOH A O     
6356 O O     . HOH F .   ? 0.7566 0.7354 0.7422 0.0358  0.0391  -0.0055 504 HOH A O     
6357 O O     . HOH F .   ? 0.2427 0.3106 0.2624 0.0094  0.0458  0.0123  505 HOH A O     
6358 O O     . HOH F .   ? 0.2334 0.2307 0.2573 0.0307  0.0455  0.0005  506 HOH A O     
6359 O O     . HOH F .   ? 0.2861 0.2708 0.2764 0.0437  0.0385  -0.0078 507 HOH A O     
6360 O O     . HOH F .   ? 0.4742 0.4449 0.5107 0.0583  0.0699  0.0709  508 HOH A O     
6361 O O     . HOH F .   ? 0.4018 0.5327 0.4116 -0.0316 0.0283  0.0230  509 HOH A O     
6362 O O     . HOH F .   ? 0.5054 0.6068 0.5443 0.0524  0.0615  0.0328  510 HOH A O     
6363 O O     . HOH F .   ? 0.2512 0.2390 0.2802 0.0339  0.0477  0.0105  511 HOH A O     
6364 O O     . HOH F .   ? 0.2291 0.2405 0.2475 0.0354  0.0385  0.0012  512 HOH A O     
6365 O O     . HOH F .   ? 0.4302 0.4559 0.4611 0.0352  0.0434  0.0101  513 HOH A O     
6366 O O     . HOH F .   ? 0.2619 0.2935 0.2630 0.0369  0.0373  0.0026  514 HOH A O     
6367 O O     . HOH F .   ? 0.4344 0.4214 0.4438 -0.0061 0.0410  0.0089  515 HOH A O     
6368 O O     . HOH F .   ? 0.2665 0.2257 0.2504 -0.0063 0.0315  -0.0138 516 HOH A O     
6369 O O     . HOH F .   ? 0.2527 0.2265 0.2523 0.0286  0.0363  -0.0146 517 HOH A O     
6370 O O     . HOH F .   ? 0.3273 0.2420 0.3190 -0.0042 0.0527  -0.0060 518 HOH A O     
6371 O O     . HOH F .   ? 0.4461 0.3873 0.4243 0.0357  0.0366  -0.0188 519 HOH A O     
6372 O O     . HOH F .   ? 0.5942 0.7223 0.6160 -0.0076 0.0409  0.0278  520 HOH A O     
6373 O O     . HOH F .   ? 0.3993 0.4430 0.4233 0.0181  0.0370  0.0195  521 HOH A O     
6374 O O     . HOH F .   ? 0.3958 0.3187 0.4055 0.0437  0.0660  0.0043  522 HOH A O     
6375 O O     . HOH F .   ? 0.4790 0.4282 0.4999 0.0506  0.0647  0.0132  523 HOH A O     
6376 O O     . HOH F .   ? 0.4519 0.5410 0.4930 0.0359  0.0448  0.0275  524 HOH A O     
6377 O O     . HOH F .   ? 0.4354 0.6412 0.4629 -0.0115 0.0303  0.0381  525 HOH A O     
6378 O O     . HOH F .   ? 0.2741 0.2926 0.3210 0.0808  0.0726  0.0602  526 HOH A O     
6379 O O     . HOH F .   ? 0.4814 0.5005 0.4944 0.0361  0.0367  -0.0030 527 HOH A O     
6380 O O     . HOH F .   ? 0.4576 0.4996 0.4555 0.0461  0.0379  0.0056  528 HOH A O     
6381 O O     . HOH F .   ? 0.4288 0.3560 0.3988 0.0324  0.0359  -0.0207 529 HOH A O     
6382 O O     . HOH F .   ? 0.5009 0.5130 0.5124 0.0388  0.0371  -0.0036 530 HOH A O     
6383 O O     . HOH F .   ? 0.3942 0.4177 0.4087 0.0058  0.0371  0.0104  531 HOH A O     
6384 O O     . HOH F .   ? 0.5665 0.4921 0.5722 -0.0038 0.0563  0.0478  532 HOH A O     
6385 O O     . HOH F .   ? 0.2495 0.2694 0.2873 0.0429  0.0493  0.0200  533 HOH A O     
6386 O O     . HOH F .   ? 0.4166 0.4362 0.4574 0.0470  0.0523  0.0268  534 HOH A O     
6387 O O     . HOH F .   ? 0.5508 0.5670 0.5749 0.0510  0.0632  0.0086  535 HOH A O     
6388 O O     . HOH F .   ? 0.3301 0.3364 0.3353 0.0406  0.0374  -0.0043 536 HOH A O     
6389 O O     . HOH F .   ? 0.7596 0.6736 0.7683 0.0355  0.0645  0.0129  537 HOH A O     
6390 O O     . HOH F .   ? 0.4142 0.5383 0.4529 0.0244  0.0342  0.0471  538 HOH A O     
6391 O O     . HOH F .   ? 0.2577 0.2974 0.2822 0.0241  0.0375  0.0166  539 HOH A O     
6392 O O     . HOH F .   ? 0.6405 0.6402 0.6071 -0.0544 0.0210  -0.0014 540 HOH A O     
6393 O O     . HOH F .   ? 0.5305 0.4541 0.5409 0.0615  0.0746  0.0140  541 HOH A O     
6394 O O     . HOH F .   ? 0.3378 0.3283 0.3314 0.0307  0.0385  -0.0071 542 HOH A O     
6395 O O     . HOH F .   ? 0.5086 0.4517 0.5281 0.0644  0.0729  0.0227  543 HOH A O     
6396 O O     . HOH F .   ? 0.4920 0.4479 0.4987 0.0206  0.0487  -0.0180 544 HOH A O     
6397 O O     . HOH F .   ? 0.3597 0.4477 0.3534 -0.0195 0.0253  0.0016  545 HOH A O     
6398 O O     . HOH F .   ? 0.3330 0.3571 0.3072 -0.0441 0.0220  -0.0040 546 HOH A O     
6399 O O     . HOH F .   ? 0.4568 0.4479 0.4377 0.0586  0.0401  -0.0036 547 HOH A O     
6400 O O     . HOH F .   ? 0.4298 0.4421 0.4506 0.0573  0.0678  0.0078  548 HOH A O     
6401 O O     . HOH F .   ? 0.5104 0.5630 0.5618 0.1411  0.1000  0.1065  549 HOH A O     
6402 O O     . HOH F .   ? 0.3851 0.4739 0.4443 0.1414  0.0978  0.1102  550 HOH A O     
6403 O O     . HOH G .   ? 0.5894 0.5701 0.5949 0.0088  0.0405  -0.0101 501 HOH B O     
6404 O O     . HOH G .   ? 0.3562 0.3313 0.3515 0.0147  0.0398  -0.0150 502 HOH B O     
6405 O O     . HOH G .   ? 0.5253 0.5028 0.4982 0.0274  0.0703  -0.0377 503 HOH B O     
6406 O O     . HOH G .   ? 0.6167 0.6481 0.5949 0.0131  0.0396  0.0221  504 HOH B O     
6407 O O     . HOH G .   ? 0.5800 0.5535 0.5518 -0.0011 0.0362  0.0164  505 HOH B O     
6408 O O     . HOH G .   ? 0.5047 0.4624 0.4736 -0.0069 0.0346  0.0139  506 HOH B O     
6409 O O     . HOH G .   ? 0.4237 0.4538 0.4161 -0.0209 0.0377  0.0080  507 HOH B O     
6410 O O     . HOH G .   ? 0.4656 0.3028 0.3763 -0.0093 0.0292  -0.0188 508 HOH B O     
6411 O O     . HOH G .   ? 0.7745 0.8528 0.7635 0.0089  0.0589  -0.0118 509 HOH B O     
6412 O O     . HOH G .   ? 0.4049 0.3135 0.3514 0.0301  0.0341  -0.0287 510 HOH B O     
6413 O O     . HOH G .   ? 0.5359 0.4855 0.5127 -0.0024 0.0353  -0.0016 511 HOH B O     
6414 O O     . HOH G .   ? 0.2556 0.2583 0.2606 -0.0002 0.0396  -0.0042 512 HOH B O     
6415 O O     . HOH G .   ? 0.3407 0.3381 0.3282 -0.0013 0.0412  -0.0091 513 HOH B O     
6416 O O     . HOH G .   ? 0.4823 0.4889 0.4612 0.0025  0.0383  0.0141  514 HOH B O     
6417 O O     . HOH G .   ? 0.3491 0.3292 0.3478 0.0059  0.0445  -0.0150 515 HOH B O     
6418 O O     . HOH G .   ? 0.4455 0.4633 0.4241 -0.0139 0.0442  -0.0243 516 HOH B O     
6419 O O     . HOH G .   ? 0.3807 0.3385 0.3668 0.0008  0.0325  -0.0158 517 HOH B O     
6420 O O     . HOH G .   ? 0.4037 0.4777 0.3815 -0.0171 0.0454  -0.0115 518 HOH B O     
6421 O O     . HOH G .   ? 0.2588 0.2022 0.2456 0.0091  0.0371  -0.0145 519 HOH B O     
6422 O O     . HOH G .   ? 0.7836 0.5662 0.6475 -0.0721 0.0200  0.0110  520 HOH B O     
6423 O O     . HOH G .   ? 0.4030 0.3362 0.3708 0.0141  0.0367  0.0009  521 HOH B O     
6424 O O     . HOH G .   ? 0.3750 0.2564 0.2800 -0.0670 0.0170  -0.0184 522 HOH B O     
6425 O O     . HOH G .   ? 0.7584 0.7946 0.7400 -0.0263 0.0350  0.0254  523 HOH B O     
6426 O O     . HOH G .   ? 0.5712 0.3190 0.4273 -0.0069 0.0326  -0.0134 524 HOH B O     
6427 O O     . HOH G .   ? 0.3506 0.4166 0.3208 -0.0082 0.0564  -0.0290 525 HOH B O     
6428 O O     . HOH G .   ? 0.7695 0.5754 0.6035 -0.1331 0.0061  -0.0125 526 HOH B O     
6429 O O     . HOH G .   ? 0.2686 0.3272 0.2633 0.0267  0.0647  -0.0118 527 HOH B O     
6430 O O     . HOH G .   ? 0.3608 0.3070 0.3274 -0.0152 0.0324  0.0104  528 HOH B O     
6431 O O     . HOH G .   ? 0.5304 0.4815 0.5058 0.0135  0.0375  -0.0006 529 HOH B O     
6432 O O     . HOH G .   ? 0.7000 0.7226 0.6466 -0.1140 0.0112  0.0383  530 HOH B O     
6433 O O     . HOH G .   ? 0.8074 0.6347 0.6957 0.0036  0.0306  -0.0380 531 HOH B O     
6434 O O     . HOH G .   ? 0.5419 0.5620 0.5236 -0.0213 0.0355  0.0186  532 HOH B O     
6435 O O     . HOH G .   ? 0.2714 0.2197 0.2621 0.0175  0.0385  -0.0162 533 HOH B O     
6436 O O     . HOH G .   ? 0.5711 0.5449 0.5394 0.0069  0.0372  0.0220  534 HOH B O     
6437 O O     . HOH G .   ? 0.3078 0.3057 0.3135 0.0067  0.0441  -0.0077 535 HOH B O     
6438 O O     . HOH G .   ? 0.3047 0.2575 0.2754 -0.0092 0.0340  0.0084  536 HOH B O     
6439 O O     . HOH G .   ? 0.3227 0.2794 0.3247 0.0145  0.0421  -0.0176 537 HOH B O     
6440 O O     . HOH G .   ? 0.5341 0.4484 0.4508 0.0230  0.0314  -0.0424 538 HOH B O     
6441 O O     . HOH G .   ? 0.3865 0.3518 0.3755 -0.0034 0.0446  -0.0258 539 HOH B O     
6442 O O     . HOH G .   ? 0.4902 0.3733 0.4314 0.0280  0.0377  0.0006  540 HOH B O     
6443 O O     . HOH G .   ? 0.2868 0.2969 0.2647 -0.0267 0.0334  0.0228  541 HOH B O     
6444 O O     . HOH G .   ? 0.2536 0.2620 0.2406 0.0111  0.0394  -0.0050 542 HOH B O     
6445 O O     . HOH G .   ? 0.2909 0.2027 0.2549 0.0004  0.0325  -0.0123 543 HOH B O     
6446 O O     . HOH G .   ? 0.7628 0.7538 0.7002 -0.1082 0.0108  0.0205  544 HOH B O     
6447 O O     . HOH G .   ? 0.4706 0.3475 0.4031 -0.0093 0.0283  -0.0226 545 HOH B O     
6448 O O     . HOH G .   ? 0.5245 0.4276 0.4805 -0.0026 0.0323  -0.0051 546 HOH B O     
6449 O O     . HOH G .   ? 0.2794 0.2329 0.2523 0.0198  0.0382  0.0029  547 HOH B O     
6450 O O     . HOH G .   ? 0.3056 0.3010 0.2950 0.0101  0.0396  -0.0106 548 HOH B O     
6451 O O     . HOH G .   ? 0.5273 0.5160 0.5176 0.0052  0.0406  -0.0159 549 HOH B O     
6452 O O     . HOH G .   ? 0.5968 0.5764 0.5912 0.0089  0.0403  -0.0164 550 HOH B O     
6453 O O     . HOH G .   ? 0.5078 0.3118 0.3297 -0.1564 0.0019  -0.0072 551 HOH B O     
6454 O O     . HOH G .   ? 0.5582 0.4440 0.4555 -0.0845 0.0136  -0.0157 552 HOH B O     
6455 O O     . HOH G .   ? 0.3813 0.3364 0.3861 0.0206  0.0506  -0.0195 553 HOH B O     
6456 O O     . HOH G .   ? 0.6573 0.5827 0.5907 0.0566  0.0380  -0.0322 554 HOH B O     
6457 O O     . HOH G .   ? 0.4364 0.4811 0.4325 -0.0075 0.0453  -0.0010 555 HOH B O     
6458 O O     . HOH G .   ? 0.5362 0.4297 0.4751 -0.0177 0.0306  0.0179  556 HOH B O     
6459 O O     . HOH G .   ? 0.3719 0.3581 0.3090 -0.1101 0.0117  0.0347  557 HOH B O     
6460 O O     . HOH G .   ? 0.5817 0.6802 0.5739 -0.0225 0.0425  0.0163  558 HOH B O     
6461 O O     . HOH G .   ? 0.5782 0.6555 0.5404 -0.0328 0.0466  -0.0291 559 HOH B O     
6462 O O     . HOH G .   ? 0.3955 0.4369 0.3688 0.0187  0.0402  0.0393  560 HOH B O     
6463 O O     . HOH G .   ? 0.4897 0.5174 0.4608 0.0250  0.0408  0.0378  561 HOH B O     
6464 O O     . HOH G .   ? 0.4915 0.4581 0.4671 0.0384  0.0399  0.0005  562 HOH B O     
6465 O O     . HOH G .   ? 0.5379 0.5621 0.5146 -0.0595 0.0230  0.0139  563 HOH B O     
6466 O O     . HOH G .   ? 0.5405 0.6383 0.5370 0.0181  0.0618  -0.0030 564 HOH B O     
6467 O O     . HOH G .   ? 0.5739 0.5557 0.5584 -0.0058 0.0451  -0.0274 565 HOH B O     
6468 O O     . HOH G .   ? 0.5369 0.5194 0.5417 0.0147  0.0486  -0.0145 566 HOH B O     
6469 O O     . HOH G .   ? 0.6060 0.5946 0.5618 -0.0652 0.0183  -0.0017 567 HOH B O     
6470 O O     . HOH G .   ? 0.2742 0.3401 0.2678 0.0361  0.0695  -0.0110 568 HOH B O     
6471 O O     . HOH G .   ? 0.5107 0.6017 0.5076 0.0356  0.0691  -0.0043 569 HOH B O     
6472 O O     . HOH H .   ? 0.3480 0.3781 0.3223 0.0377  0.0417  0.0280  101 HOH C O     
6473 O O     . HOH H .   ? 0.7823 0.8178 0.7618 -0.0221 0.0394  -0.0178 102 HOH C O     
6474 O O     . HOH H .   ? 0.5983 0.5277 0.5567 -0.0214 0.0550  -0.0457 103 HOH C O     
6475 O O     . HOH H .   ? 0.4074 0.4223 0.3644 -0.0672 0.0381  -0.0266 104 HOH C O     
6476 O O     . HOH H .   ? 0.5347 0.5408 0.4207 -0.1502 0.0373  -0.0547 105 HOH C O     
6477 O O     . HOH H .   ? 0.3880 0.4856 0.3569 -0.0376 0.0392  -0.0149 106 HOH C O     
6478 O O     . HOH H .   ? 0.2627 0.3415 0.2395 -0.0214 0.0399  -0.0094 107 HOH C O     
# 
