data_9DJX
# 
_entry.id   9DJX 
# 
_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   9DJX         pdb_00009djx 10.2210/pdb9djx/pdb 
WWPDB D_1000288240 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-11 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DJX 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9DJT 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              james.partridge@novartis.com 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Partridge 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5652-4351 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Partridge, J.R.' 1 0000-0002-5652-4351 
'Ma, X.'          2 ?                   
'Ornelas, E.'     3 ?                   
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                20682 
_citation.page_last                 20694 
_citation.title                     
;Discovery and Optimization of First-in-Class Molecular Glue Degraders of the WIZ Transcription Factor for Fetal Hemoglobin Induction to Treat Sickle Cell Disease.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02251 
_citation.pdbx_database_id_PubMed   39541509 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kerrigan, J.R.'  1  ? 
primary 'Thomsen, N.M.'   2  ? 
primary 'Cernijenko, A.'  3  ? 
primary 'Kochanek, S.E.'  4  ? 
primary 'Dewhurst, J.'    5  ? 
primary 
;O'Brien, G.
;
6  ? 
primary 'Ware, N.F.'      7  ? 
primary 'Sanchez, C.C.'   8  ? 
primary 'Manning, J.R.'   9  ? 
primary 'Ma, X.'          10 ? 
primary 'Ornelas, E.'     11 ? 
primary 'Savage, N.A.'    12 ? 
primary 'Partridge, J.R.' 13 ? 
primary 'Patterson, A.W.' 14 ? 
primary 'Lam, P.'         15 ? 
primary 'Dales, N.A.'     16 ? 
primary 'Bonazzi, S.'     17 ? 
primary 'Borikar, S.'     18 ? 
primary 'Hinman, A.E.'    19 ? 
primary 'Ting, P.Y.'      20 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protein cereblon' 42971.574 2  ? ? ? ? 
2 polymer     man 'DNA damage-binding protein 1' 93347.078 2  ? ? ? ? 
3 polymer     man 'Protein Wiz' 3299.722  2  ? ? ? ? 
4 non-polymer syn 'ZINC ION' 65.409    4  ? ? ? ? 
5 non-polymer syn 'SULFATE ION' 96.063    3  ? ? ? ? 
6 non-polymer syn 
'(3S)-3-(5-{[(3R,6S)-1-ethyl-6-methylpiperidin-3-yl]oxy}-1-oxo-1,3-dihydro-2H-isoindol-2-yl)piperidine-2,6-dione' 385.457   2  ? ? 
? ? 
7 water       nat water 18.015    22 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
2 
;DDB p127 subunit,DNA damage-binding protein a,DDBa,Damage-specific DNA-binding protein 1,HBV X-associated protein 1,XAP-1,UV-damaged DNA-binding factor,UV-damaged DNA-binding protein 1,UV-DDB 1,XPE-binding factor,XPE-BF,Xeroderma pigmentosum group E-complementing protein,XPCe
;
3 'Widely-interspaced zinc finger-containing protein,Zinc finger protein 803' 
# 
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 
;RTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQD
FGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQK
RKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLR
CELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVA
QCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
;
;RTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQD
FGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQK
RKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLR
CELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVA
QCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
;
A,D ? 
2 'polypeptide(L)' no no 
;MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGGNGNS
GEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGE
EVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEK
EVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEE
IARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPT
QGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPK
MQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
;
;MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGGNGNS
GEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGE
EVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEK
EVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEE
IARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPT
QGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPK
MQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
;
B,E ? 
3 'polypeptide(L)' no no SQSLTTCEVCGACFETRKGLSSHARSHLRQ SQSLTTCEVCGACFETRKGLSSHARSHLRQ C,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'ZINC ION'                                                                                                        ZN    
5 'SULFATE ION'                                                                                                     SO4   
6 '(3S)-3-(5-{[(3R,6S)-1-ethyl-6-methylpiperidin-3-yl]oxy}-1-oxo-1,3-dihydro-2H-isoindol-2-yl)piperidine-2,6-dione' A1A5I 
7 water                                                                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   THR n 
1 3   LEU n 
1 4   HIS n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   SER n 
1 9   CYS n 
1 10  GLN n 
1 11  VAL n 
1 12  ILE n 
1 13  PRO n 
1 14  VAL n 
1 15  LEU n 
1 16  PRO n 
1 17  GLN n 
1 18  VAL n 
1 19  MET n 
1 20  MET n 
1 21  ILE n 
1 22  LEU n 
1 23  ILE n 
1 24  PRO n 
1 25  GLY n 
1 26  GLN n 
1 27  THR n 
1 28  LEU n 
1 29  PRO n 
1 30  LEU n 
1 31  GLN n 
1 32  LEU n 
1 33  PHE n 
1 34  HIS n 
1 35  PRO n 
1 36  GLN n 
1 37  GLU n 
1 38  VAL n 
1 39  SER n 
1 40  MET n 
1 41  VAL n 
1 42  ARG n 
1 43  ASN n 
1 44  LEU n 
1 45  ILE n 
1 46  GLN n 
1 47  LYS n 
1 48  ASP n 
1 49  ARG n 
1 50  THR n 
1 51  PHE n 
1 52  ALA n 
1 53  VAL n 
1 54  LEU n 
1 55  ALA n 
1 56  TYR n 
1 57  SER n 
1 58  ASN n 
1 59  VAL n 
1 60  GLN n 
1 61  GLU n 
1 62  ARG n 
1 63  GLU n 
1 64  ALA n 
1 65  GLN n 
1 66  PHE n 
1 67  GLY n 
1 68  THR n 
1 69  THR n 
1 70  ALA n 
1 71  GLU n 
1 72  ILE n 
1 73  TYR n 
1 74  ALA n 
1 75  TYR n 
1 76  ARG n 
1 77  GLU n 
1 78  GLU n 
1 79  GLN n 
1 80  ASP n 
1 81  PHE n 
1 82  GLY n 
1 83  ILE n 
1 84  GLU n 
1 85  ILE n 
1 86  VAL n 
1 87  LYS n 
1 88  VAL n 
1 89  LYS n 
1 90  ALA n 
1 91  ILE n 
1 92  GLY n 
1 93  ARG n 
1 94  GLN n 
1 95  ARG n 
1 96  PHE n 
1 97  LYS n 
1 98  VAL n 
1 99  LEU n 
1 100 GLU n 
1 101 LEU n 
1 102 ARG n 
1 103 THR n 
1 104 GLN n 
1 105 SER n 
1 106 ASP n 
1 107 GLY n 
1 108 ILE n 
1 109 GLN n 
1 110 GLN n 
1 111 ALA n 
1 112 LYS n 
1 113 VAL n 
1 114 GLN n 
1 115 ILE n 
1 116 LEU n 
1 117 PRO n 
1 118 GLU n 
1 119 CYS n 
1 120 VAL n 
1 121 LEU n 
1 122 PRO n 
1 123 SER n 
1 124 THR n 
1 125 MET n 
1 126 SER n 
1 127 ALA n 
1 128 VAL n 
1 129 GLN n 
1 130 LEU n 
1 131 GLU n 
1 132 SER n 
1 133 LEU n 
1 134 ASN n 
1 135 LYS n 
1 136 CYS n 
1 137 GLN n 
1 138 ILE n 
1 139 PHE n 
1 140 PRO n 
1 141 SER n 
1 142 LYS n 
1 143 PRO n 
1 144 VAL n 
1 145 SER n 
1 146 ARG n 
1 147 GLU n 
1 148 ASP n 
1 149 GLN n 
1 150 CYS n 
1 151 SER n 
1 152 TYR n 
1 153 LYS n 
1 154 TRP n 
1 155 TRP n 
1 156 GLN n 
1 157 LYS n 
1 158 TYR n 
1 159 GLN n 
1 160 LYS n 
1 161 ARG n 
1 162 LYS n 
1 163 PHE n 
1 164 HIS n 
1 165 CYS n 
1 166 ALA n 
1 167 ASN n 
1 168 LEU n 
1 169 THR n 
1 170 SER n 
1 171 TRP n 
1 172 PRO n 
1 173 ARG n 
1 174 TRP n 
1 175 LEU n 
1 176 TYR n 
1 177 SER n 
1 178 LEU n 
1 179 TYR n 
1 180 ASP n 
1 181 ALA n 
1 182 GLU n 
1 183 THR n 
1 184 LEU n 
1 185 MET n 
1 186 ASP n 
1 187 ARG n 
1 188 ILE n 
1 189 LYS n 
1 190 LYS n 
1 191 GLN n 
1 192 LEU n 
1 193 ARG n 
1 194 GLU n 
1 195 TRP n 
1 196 ASP n 
1 197 GLU n 
1 198 ASN n 
1 199 LEU n 
1 200 LYS n 
1 201 ASP n 
1 202 ASP n 
1 203 SER n 
1 204 LEU n 
1 205 PRO n 
1 206 SER n 
1 207 ASN n 
1 208 PRO n 
1 209 ILE n 
1 210 ASP n 
1 211 PHE n 
1 212 SER n 
1 213 TYR n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ALA n 
1 218 CYS n 
1 219 LEU n 
1 220 PRO n 
1 221 ILE n 
1 222 ASP n 
1 223 ASP n 
1 224 VAL n 
1 225 LEU n 
1 226 ARG n 
1 227 ILE n 
1 228 GLN n 
1 229 LEU n 
1 230 LEU n 
1 231 LYS n 
1 232 ILE n 
1 233 GLY n 
1 234 SER n 
1 235 ALA n 
1 236 ILE n 
1 237 GLN n 
1 238 ARG n 
1 239 LEU n 
1 240 ARG n 
1 241 CYS n 
1 242 GLU n 
1 243 LEU n 
1 244 ASP n 
1 245 ILE n 
1 246 MET n 
1 247 ASN n 
1 248 LYS n 
1 249 CYS n 
1 250 THR n 
1 251 SER n 
1 252 LEU n 
1 253 CYS n 
1 254 CYS n 
1 255 LYS n 
1 256 GLN n 
1 257 CYS n 
1 258 GLN n 
1 259 GLU n 
1 260 THR n 
1 261 GLU n 
1 262 ILE n 
1 263 THR n 
1 264 THR n 
1 265 LYS n 
1 266 ASN n 
1 267 GLU n 
1 268 ILE n 
1 269 PHE n 
1 270 SER n 
1 271 LEU n 
1 272 SER n 
1 273 LEU n 
1 274 CYS n 
1 275 GLY n 
1 276 PRO n 
1 277 MET n 
1 278 ALA n 
1 279 ALA n 
1 280 TYR n 
1 281 VAL n 
1 282 ASN n 
1 283 PRO n 
1 284 HIS n 
1 285 GLY n 
1 286 TYR n 
1 287 VAL n 
1 288 HIS n 
1 289 GLU n 
1 290 THR n 
1 291 LEU n 
1 292 THR n 
1 293 VAL n 
1 294 TYR n 
1 295 LYS n 
1 296 ALA n 
1 297 CYS n 
1 298 ASN n 
1 299 LEU n 
1 300 ASN n 
1 301 LEU n 
1 302 ILE n 
1 303 GLY n 
1 304 ARG n 
1 305 PRO n 
1 306 SER n 
1 307 THR n 
1 308 GLU n 
1 309 HIS n 
1 310 SER n 
1 311 TRP n 
1 312 PHE n 
1 313 PRO n 
1 314 GLY n 
1 315 TYR n 
1 316 ALA n 
1 317 TRP n 
1 318 THR n 
1 319 VAL n 
1 320 ALA n 
1 321 GLN n 
1 322 CYS n 
1 323 LYS n 
1 324 ILE n 
1 325 CYS n 
1 326 ALA n 
1 327 SER n 
1 328 HIS n 
1 329 ILE n 
1 330 GLY n 
1 331 TRP n 
1 332 LYS n 
1 333 PHE n 
1 334 THR n 
1 335 ALA n 
1 336 THR n 
1 337 LYS n 
1 338 LYS n 
1 339 ASP n 
1 340 MET n 
1 341 SER n 
1 342 PRO n 
1 343 GLN n 
1 344 LYS n 
1 345 PHE n 
1 346 TRP n 
1 347 GLY n 
1 348 LEU n 
1 349 THR n 
1 350 ARG n 
1 351 SER n 
1 352 ALA n 
1 353 LEU n 
1 354 LEU n 
1 355 PRO n 
1 356 THR n 
1 357 ILE n 
1 358 PRO n 
1 359 ASP n 
1 360 THR n 
1 361 GLU n 
1 362 ASP n 
1 363 GLU n 
1 364 ILE n 
1 365 SER n 
1 366 PRO n 
1 367 ASP n 
1 368 LYS n 
1 369 VAL n 
1 370 ILE n 
1 371 LEU n 
1 372 CYS n 
1 373 LEU n 
2 1   MET n 
2 2   SER n 
2 3   TYR n 
2 4   ASN n 
2 5   TYR n 
2 6   VAL n 
2 7   VAL n 
2 8   THR n 
2 9   ALA n 
2 10  GLN n 
2 11  LYS n 
2 12  PRO n 
2 13  THR n 
2 14  ALA n 
2 15  VAL n 
2 16  ASN n 
2 17  GLY n 
2 18  CYS n 
2 19  VAL n 
2 20  THR n 
2 21  GLY n 
2 22  HIS n 
2 23  PHE n 
2 24  THR n 
2 25  SER n 
2 26  ALA n 
2 27  GLU n 
2 28  ASP n 
2 29  LEU n 
2 30  ASN n 
2 31  LEU n 
2 32  LEU n 
2 33  ILE n 
2 34  ALA n 
2 35  LYS n 
2 36  ASN n 
2 37  THR n 
2 38  ARG n 
2 39  LEU n 
2 40  GLU n 
2 41  ILE n 
2 42  TYR n 
2 43  VAL n 
2 44  VAL n 
2 45  THR n 
2 46  ALA n 
2 47  GLU n 
2 48  GLY n 
2 49  LEU n 
2 50  ARG n 
2 51  PRO n 
2 52  VAL n 
2 53  LYS n 
2 54  GLU n 
2 55  VAL n 
2 56  GLY n 
2 57  MET n 
2 58  TYR n 
2 59  GLY n 
2 60  LYS n 
2 61  ILE n 
2 62  ALA n 
2 63  VAL n 
2 64  MET n 
2 65  GLU n 
2 66  LEU n 
2 67  PHE n 
2 68  ARG n 
2 69  PRO n 
2 70  LYS n 
2 71  GLY n 
2 72  GLU n 
2 73  SER n 
2 74  LYS n 
2 75  ASP n 
2 76  LEU n 
2 77  LEU n 
2 78  PHE n 
2 79  ILE n 
2 80  LEU n 
2 81  THR n 
2 82  ALA n 
2 83  LYS n 
2 84  TYR n 
2 85  ASN n 
2 86  ALA n 
2 87  CYS n 
2 88  ILE n 
2 89  LEU n 
2 90  GLU n 
2 91  TYR n 
2 92  LYS n 
2 93  GLN n 
2 94  SER n 
2 95  GLY n 
2 96  GLU n 
2 97  SER n 
2 98  ILE n 
2 99  ASP n 
2 100 ILE n 
2 101 ILE n 
2 102 THR n 
2 103 ARG n 
2 104 ALA n 
2 105 HIS n 
2 106 GLY n 
2 107 ASN n 
2 108 VAL n 
2 109 GLN n 
2 110 ASP n 
2 111 ARG n 
2 112 ILE n 
2 113 GLY n 
2 114 ARG n 
2 115 PRO n 
2 116 SER n 
2 117 GLU n 
2 118 THR n 
2 119 GLY n 
2 120 ILE n 
2 121 ILE n 
2 122 GLY n 
2 123 ILE n 
2 124 ILE n 
2 125 ASP n 
2 126 PRO n 
2 127 GLU n 
2 128 CYS n 
2 129 ARG n 
2 130 MET n 
2 131 ILE n 
2 132 GLY n 
2 133 LEU n 
2 134 ARG n 
2 135 LEU n 
2 136 TYR n 
2 137 ASP n 
2 138 GLY n 
2 139 LEU n 
2 140 PHE n 
2 141 LYS n 
2 142 VAL n 
2 143 ILE n 
2 144 PRO n 
2 145 LEU n 
2 146 ASP n 
2 147 ARG n 
2 148 ASP n 
2 149 ASN n 
2 150 LYS n 
2 151 GLU n 
2 152 LEU n 
2 153 LYS n 
2 154 ALA n 
2 155 PHE n 
2 156 ASN n 
2 157 ILE n 
2 158 ARG n 
2 159 LEU n 
2 160 GLU n 
2 161 GLU n 
2 162 LEU n 
2 163 HIS n 
2 164 VAL n 
2 165 ILE n 
2 166 ASP n 
2 167 VAL n 
2 168 LYS n 
2 169 PHE n 
2 170 LEU n 
2 171 TYR n 
2 172 GLY n 
2 173 CYS n 
2 174 GLN n 
2 175 ALA n 
2 176 PRO n 
2 177 THR n 
2 178 ILE n 
2 179 CYS n 
2 180 PHE n 
2 181 VAL n 
2 182 TYR n 
2 183 GLN n 
2 184 ASP n 
2 185 PRO n 
2 186 GLN n 
2 187 GLY n 
2 188 ARG n 
2 189 HIS n 
2 190 VAL n 
2 191 LYS n 
2 192 THR n 
2 193 TYR n 
2 194 GLU n 
2 195 VAL n 
2 196 SER n 
2 197 LEU n 
2 198 ARG n 
2 199 GLU n 
2 200 LYS n 
2 201 GLU n 
2 202 PHE n 
2 203 ASN n 
2 204 LYS n 
2 205 GLY n 
2 206 PRO n 
2 207 TRP n 
2 208 LYS n 
2 209 GLN n 
2 210 GLU n 
2 211 ASN n 
2 212 VAL n 
2 213 GLU n 
2 214 ALA n 
2 215 GLU n 
2 216 ALA n 
2 217 SER n 
2 218 MET n 
2 219 VAL n 
2 220 ILE n 
2 221 ALA n 
2 222 VAL n 
2 223 PRO n 
2 224 GLU n 
2 225 PRO n 
2 226 PHE n 
2 227 GLY n 
2 228 GLY n 
2 229 ALA n 
2 230 ILE n 
2 231 ILE n 
2 232 ILE n 
2 233 GLY n 
2 234 GLN n 
2 235 GLU n 
2 236 SER n 
2 237 ILE n 
2 238 THR n 
2 239 TYR n 
2 240 HIS n 
2 241 ASN n 
2 242 GLY n 
2 243 ASP n 
2 244 LYS n 
2 245 TYR n 
2 246 LEU n 
2 247 ALA n 
2 248 ILE n 
2 249 ALA n 
2 250 PRO n 
2 251 PRO n 
2 252 ILE n 
2 253 ILE n 
2 254 LYS n 
2 255 GLN n 
2 256 SER n 
2 257 THR n 
2 258 ILE n 
2 259 VAL n 
2 260 CYS n 
2 261 HIS n 
2 262 ASN n 
2 263 ARG n 
2 264 VAL n 
2 265 ASP n 
2 266 PRO n 
2 267 ASN n 
2 268 GLY n 
2 269 SER n 
2 270 ARG n 
2 271 TYR n 
2 272 LEU n 
2 273 LEU n 
2 274 GLY n 
2 275 ASP n 
2 276 MET n 
2 277 GLU n 
2 278 GLY n 
2 279 ARG n 
2 280 LEU n 
2 281 PHE n 
2 282 MET n 
2 283 LEU n 
2 284 LEU n 
2 285 LEU n 
2 286 GLU n 
2 287 LYS n 
2 288 GLU n 
2 289 GLU n 
2 290 GLN n 
2 291 MET n 
2 292 ASP n 
2 293 GLY n 
2 294 THR n 
2 295 VAL n 
2 296 THR n 
2 297 LEU n 
2 298 LYS n 
2 299 ASP n 
2 300 LEU n 
2 301 ARG n 
2 302 VAL n 
2 303 GLU n 
2 304 LEU n 
2 305 LEU n 
2 306 GLY n 
2 307 GLU n 
2 308 THR n 
2 309 SER n 
2 310 ILE n 
2 311 ALA n 
2 312 GLU n 
2 313 CYS n 
2 314 LEU n 
2 315 THR n 
2 316 TYR n 
2 317 LEU n 
2 318 ASP n 
2 319 ASN n 
2 320 GLY n 
2 321 VAL n 
2 322 VAL n 
2 323 PHE n 
2 324 VAL n 
2 325 GLY n 
2 326 SER n 
2 327 ARG n 
2 328 LEU n 
2 329 GLY n 
2 330 ASP n 
2 331 SER n 
2 332 GLN n 
2 333 LEU n 
2 334 VAL n 
2 335 LYS n 
2 336 LEU n 
2 337 ASN n 
2 338 VAL n 
2 339 ASP n 
2 340 SER n 
2 341 ASN n 
2 342 GLU n 
2 343 GLN n 
2 344 GLY n 
2 345 SER n 
2 346 TYR n 
2 347 VAL n 
2 348 VAL n 
2 349 ALA n 
2 350 MET n 
2 351 GLU n 
2 352 THR n 
2 353 PHE n 
2 354 THR n 
2 355 ASN n 
2 356 LEU n 
2 357 GLY n 
2 358 PRO n 
2 359 ILE n 
2 360 VAL n 
2 361 ASP n 
2 362 MET n 
2 363 CYS n 
2 364 VAL n 
2 365 VAL n 
2 366 ASP n 
2 367 LEU n 
2 368 GLU n 
2 369 ARG n 
2 370 GLN n 
2 371 GLY n 
2 372 GLN n 
2 373 GLY n 
2 374 GLN n 
2 375 LEU n 
2 376 VAL n 
2 377 THR n 
2 378 CYS n 
2 379 SER n 
2 380 GLY n 
2 381 ALA n 
2 382 PHE n 
2 383 LYS n 
2 384 GLU n 
2 385 GLY n 
2 386 SER n 
2 387 LEU n 
2 388 ARG n 
2 389 ILE n 
2 390 ILE n 
2 391 ARG n 
2 392 ASN n 
2 393 GLY n 
2 394 ILE n 
2 395 GLY n 
2 396 GLY n 
2 397 ASN n 
2 398 GLY n 
2 399 ASN n 
2 400 SER n 
2 401 GLY n 
2 402 GLU n 
2 403 ILE n 
2 404 GLN n 
2 405 LYS n 
2 406 LEU n 
2 407 HIS n 
2 408 ILE n 
2 409 ARG n 
2 410 THR n 
2 411 VAL n 
2 412 PRO n 
2 413 LEU n 
2 414 TYR n 
2 415 GLU n 
2 416 SER n 
2 417 PRO n 
2 418 ARG n 
2 419 LYS n 
2 420 ILE n 
2 421 CYS n 
2 422 TYR n 
2 423 GLN n 
2 424 GLU n 
2 425 VAL n 
2 426 SER n 
2 427 GLN n 
2 428 CYS n 
2 429 PHE n 
2 430 GLY n 
2 431 VAL n 
2 432 LEU n 
2 433 SER n 
2 434 SER n 
2 435 ARG n 
2 436 ILE n 
2 437 GLU n 
2 438 VAL n 
2 439 GLN n 
2 440 ASP n 
2 441 THR n 
2 442 SER n 
2 443 GLY n 
2 444 GLY n 
2 445 THR n 
2 446 THR n 
2 447 ALA n 
2 448 LEU n 
2 449 ARG n 
2 450 PRO n 
2 451 SER n 
2 452 ALA n 
2 453 SER n 
2 454 THR n 
2 455 GLN n 
2 456 ALA n 
2 457 LEU n 
2 458 SER n 
2 459 SER n 
2 460 SER n 
2 461 VAL n 
2 462 SER n 
2 463 SER n 
2 464 SER n 
2 465 LYS n 
2 466 LEU n 
2 467 PHE n 
2 468 SER n 
2 469 SER n 
2 470 SER n 
2 471 THR n 
2 472 ALA n 
2 473 PRO n 
2 474 HIS n 
2 475 GLU n 
2 476 THR n 
2 477 SER n 
2 478 PHE n 
2 479 GLY n 
2 480 GLU n 
2 481 GLU n 
2 482 VAL n 
2 483 GLU n 
2 484 VAL n 
2 485 HIS n 
2 486 ASN n 
2 487 LEU n 
2 488 LEU n 
2 489 ILE n 
2 490 ILE n 
2 491 ASP n 
2 492 GLN n 
2 493 HIS n 
2 494 THR n 
2 495 PHE n 
2 496 GLU n 
2 497 VAL n 
2 498 LEU n 
2 499 HIS n 
2 500 ALA n 
2 501 HIS n 
2 502 GLN n 
2 503 PHE n 
2 504 LEU n 
2 505 GLN n 
2 506 ASN n 
2 507 GLU n 
2 508 TYR n 
2 509 ALA n 
2 510 LEU n 
2 511 SER n 
2 512 LEU n 
2 513 VAL n 
2 514 SER n 
2 515 CYS n 
2 516 LYS n 
2 517 LEU n 
2 518 GLY n 
2 519 LYS n 
2 520 ASP n 
2 521 PRO n 
2 522 ASN n 
2 523 THR n 
2 524 TYR n 
2 525 PHE n 
2 526 ILE n 
2 527 VAL n 
2 528 GLY n 
2 529 THR n 
2 530 ALA n 
2 531 MET n 
2 532 VAL n 
2 533 TYR n 
2 534 PRO n 
2 535 GLU n 
2 536 GLU n 
2 537 ALA n 
2 538 GLU n 
2 539 PRO n 
2 540 LYS n 
2 541 GLN n 
2 542 GLY n 
2 543 ARG n 
2 544 ILE n 
2 545 VAL n 
2 546 VAL n 
2 547 PHE n 
2 548 GLN n 
2 549 TYR n 
2 550 SER n 
2 551 ASP n 
2 552 GLY n 
2 553 LYS n 
2 554 LEU n 
2 555 GLN n 
2 556 THR n 
2 557 VAL n 
2 558 ALA n 
2 559 GLU n 
2 560 LYS n 
2 561 GLU n 
2 562 VAL n 
2 563 LYS n 
2 564 GLY n 
2 565 ALA n 
2 566 VAL n 
2 567 TYR n 
2 568 SER n 
2 569 MET n 
2 570 VAL n 
2 571 GLU n 
2 572 PHE n 
2 573 ASN n 
2 574 GLY n 
2 575 LYS n 
2 576 LEU n 
2 577 LEU n 
2 578 ALA n 
2 579 SER n 
2 580 ILE n 
2 581 ASN n 
2 582 SER n 
2 583 THR n 
2 584 VAL n 
2 585 ARG n 
2 586 LEU n 
2 587 TYR n 
2 588 GLU n 
2 589 TRP n 
2 590 THR n 
2 591 THR n 
2 592 GLU n 
2 593 LYS n 
2 594 GLU n 
2 595 LEU n 
2 596 ARG n 
2 597 THR n 
2 598 GLU n 
2 599 CYS n 
2 600 ASN n 
2 601 HIS n 
2 602 TYR n 
2 603 ASN n 
2 604 ASN n 
2 605 ILE n 
2 606 MET n 
2 607 ALA n 
2 608 LEU n 
2 609 TYR n 
2 610 LEU n 
2 611 LYS n 
2 612 THR n 
2 613 LYS n 
2 614 GLY n 
2 615 ASP n 
2 616 PHE n 
2 617 ILE n 
2 618 LEU n 
2 619 VAL n 
2 620 GLY n 
2 621 ASP n 
2 622 LEU n 
2 623 MET n 
2 624 ARG n 
2 625 SER n 
2 626 VAL n 
2 627 LEU n 
2 628 LEU n 
2 629 LEU n 
2 630 ALA n 
2 631 TYR n 
2 632 LYS n 
2 633 PRO n 
2 634 MET n 
2 635 GLU n 
2 636 GLY n 
2 637 ASN n 
2 638 PHE n 
2 639 GLU n 
2 640 GLU n 
2 641 ILE n 
2 642 ALA n 
2 643 ARG n 
2 644 ASP n 
2 645 PHE n 
2 646 ASN n 
2 647 PRO n 
2 648 ASN n 
2 649 TRP n 
2 650 MET n 
2 651 SER n 
2 652 ALA n 
2 653 VAL n 
2 654 GLU n 
2 655 ILE n 
2 656 LEU n 
2 657 ASP n 
2 658 ASP n 
2 659 ASP n 
2 660 ASN n 
2 661 PHE n 
2 662 LEU n 
2 663 GLY n 
2 664 ALA n 
2 665 GLU n 
2 666 ASN n 
2 667 ALA n 
2 668 PHE n 
2 669 ASN n 
2 670 LEU n 
2 671 PHE n 
2 672 VAL n 
2 673 CYS n 
2 674 GLN n 
2 675 LYS n 
2 676 ASP n 
2 677 SER n 
2 678 ALA n 
2 679 ALA n 
2 680 THR n 
2 681 THR n 
2 682 ASP n 
2 683 GLU n 
2 684 GLU n 
2 685 ARG n 
2 686 GLN n 
2 687 HIS n 
2 688 LEU n 
2 689 GLN n 
2 690 GLU n 
2 691 VAL n 
2 692 GLY n 
2 693 LEU n 
2 694 PHE n 
2 695 HIS n 
2 696 LEU n 
2 697 GLY n 
2 698 GLU n 
2 699 PHE n 
2 700 VAL n 
2 701 ASN n 
2 702 VAL n 
2 703 PHE n 
2 704 CYS n 
2 705 HIS n 
2 706 GLY n 
2 707 SER n 
2 708 LEU n 
2 709 VAL n 
2 710 MET n 
2 711 GLN n 
2 712 ASN n 
2 713 LEU n 
2 714 GLY n 
2 715 GLU n 
2 716 THR n 
2 717 SER n 
2 718 THR n 
2 719 PRO n 
2 720 THR n 
2 721 GLN n 
2 722 GLY n 
2 723 SER n 
2 724 VAL n 
2 725 LEU n 
2 726 PHE n 
2 727 GLY n 
2 728 THR n 
2 729 VAL n 
2 730 ASN n 
2 731 GLY n 
2 732 MET n 
2 733 ILE n 
2 734 GLY n 
2 735 LEU n 
2 736 VAL n 
2 737 THR n 
2 738 SER n 
2 739 LEU n 
2 740 SER n 
2 741 GLU n 
2 742 SER n 
2 743 TRP n 
2 744 TYR n 
2 745 ASN n 
2 746 LEU n 
2 747 LEU n 
2 748 LEU n 
2 749 ASP n 
2 750 MET n 
2 751 GLN n 
2 752 ASN n 
2 753 ARG n 
2 754 LEU n 
2 755 ASN n 
2 756 LYS n 
2 757 VAL n 
2 758 ILE n 
2 759 LYS n 
2 760 SER n 
2 761 VAL n 
2 762 GLY n 
2 763 LYS n 
2 764 ILE n 
2 765 GLU n 
2 766 HIS n 
2 767 SER n 
2 768 PHE n 
2 769 TRP n 
2 770 ARG n 
2 771 SER n 
2 772 PHE n 
2 773 HIS n 
2 774 THR n 
2 775 GLU n 
2 776 ARG n 
2 777 LYS n 
2 778 THR n 
2 779 GLU n 
2 780 PRO n 
2 781 ALA n 
2 782 THR n 
2 783 GLY n 
2 784 PHE n 
2 785 ILE n 
2 786 ASP n 
2 787 GLY n 
2 788 ASP n 
2 789 LEU n 
2 790 ILE n 
2 791 GLU n 
2 792 SER n 
2 793 PHE n 
2 794 LEU n 
2 795 ASP n 
2 796 ILE n 
2 797 SER n 
2 798 ARG n 
2 799 PRO n 
2 800 LYS n 
2 801 MET n 
2 802 GLN n 
2 803 GLU n 
2 804 VAL n 
2 805 VAL n 
2 806 ALA n 
2 807 ASN n 
2 808 LEU n 
2 809 GLN n 
2 810 TYR n 
2 811 ASP n 
2 812 ASP n 
2 813 GLY n 
2 814 SER n 
2 815 GLY n 
2 816 MET n 
2 817 LYS n 
2 818 ARG n 
2 819 GLU n 
2 820 ALA n 
2 821 THR n 
2 822 ALA n 
2 823 ASP n 
2 824 ASP n 
2 825 LEU n 
2 826 ILE n 
2 827 LYS n 
2 828 VAL n 
2 829 VAL n 
2 830 GLU n 
2 831 GLU n 
2 832 LEU n 
2 833 THR n 
2 834 ARG n 
2 835 ILE n 
2 836 HIS n 
3 1   SER n 
3 2   GLN n 
3 3   SER n 
3 4   LEU n 
3 5   THR n 
3 6   THR n 
3 7   CYS n 
3 8   GLU n 
3 9   VAL n 
3 10  CYS n 
3 11  GLY n 
3 12  ALA n 
3 13  CYS n 
3 14  PHE n 
3 15  GLU n 
3 16  THR n 
3 17  ARG n 
3 18  LYS n 
3 19  GLY n 
3 20  LEU n 
3 21  SER n 
3 22  SER n 
3 23  HIS n 
3 24  ALA n 
3 25  ARG n 
3 26  SER n 
3 27  HIS n 
3 28  LEU n 
3 29  ARG n 
3 30  GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   373 human ? CRBN          ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   395 human ? 'DDB1, XAP1'  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 396 836 human ? 'DDB1, XAP1'  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? baculovirus ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1   30  human ? 'WIZ, ZNF803' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ?               
'Escherichia coli'      562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?           ? ? ? ? ? ? 
# 
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 
A1A5I non-polymer         . 
'(3S)-3-(5-{[(3R,6S)-1-ethyl-6-methylpiperidin-3-yl]oxy}-1-oxo-1,3-dihydro-2H-isoindol-2-yl)piperidine-2,6-dione' ? 
'C21 H27 N3 O4'  385.457 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
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 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'        96.063  
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 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'           65.409  
# 
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   ARG 1   70   ?    ?   ?   A . n 
A 1 2   THR 2   71   ?    ?   ?   A . n 
A 1 3   LEU 3   72   ?    ?   ?   A . n 
A 1 4   HIS 4   73   73   HIS HIS A . n 
A 1 5   ASP 5   74   74   ASP ASP A . n 
A 1 6   ASP 6   75   75   ASP ASP A . n 
A 1 7   ASP 7   76   76   ASP ASP A . n 
A 1 8   SER 8   77   77   SER SER A . n 
A 1 9   CYS 9   78   78   CYS CYS A . n 
A 1 10  GLN 10  79   79   GLN GLN A . n 
A 1 11  VAL 11  80   80   VAL VAL A . n 
A 1 12  ILE 12  81   81   ILE ILE A . n 
A 1 13  PRO 13  82   82   PRO PRO A . n 
A 1 14  VAL 14  83   83   VAL VAL A . n 
A 1 15  LEU 15  84   84   LEU LEU A . n 
A 1 16  PRO 16  85   85   PRO PRO A . n 
A 1 17  GLN 17  86   86   GLN GLN A . n 
A 1 18  VAL 18  87   87   VAL VAL A . n 
A 1 19  MET 19  88   88   MET MET A . n 
A 1 20  MET 20  89   89   MET MET A . n 
A 1 21  ILE 21  90   90   ILE ILE A . n 
A 1 22  LEU 22  91   91   LEU LEU A . n 
A 1 23  ILE 23  92   92   ILE ILE A . n 
A 1 24  PRO 24  93   93   PRO PRO A . n 
A 1 25  GLY 25  94   94   GLY GLY A . n 
A 1 26  GLN 26  95   95   GLN GLN A . n 
A 1 27  THR 27  96   96   THR THR A . n 
A 1 28  LEU 28  97   97   LEU LEU A . n 
A 1 29  PRO 29  98   98   PRO PRO A . n 
A 1 30  LEU 30  99   99   LEU LEU A . n 
A 1 31  GLN 31  100  100  GLN GLN A . n 
A 1 32  LEU 32  101  101  LEU LEU A . n 
A 1 33  PHE 33  102  102  PHE PHE A . n 
A 1 34  HIS 34  103  103  HIS HIS A . n 
A 1 35  PRO 35  104  104  PRO PRO A . n 
A 1 36  GLN 36  105  105  GLN GLN A . n 
A 1 37  GLU 37  106  106  GLU GLU A . n 
A 1 38  VAL 38  107  107  VAL VAL A . n 
A 1 39  SER 39  108  108  SER SER A . n 
A 1 40  MET 40  109  109  MET MET A . n 
A 1 41  VAL 41  110  110  VAL VAL A . n 
A 1 42  ARG 42  111  111  ARG ARG A . n 
A 1 43  ASN 43  112  112  ASN ASN A . n 
A 1 44  LEU 44  113  113  LEU LEU A . n 
A 1 45  ILE 45  114  114  ILE ILE A . n 
A 1 46  GLN 46  115  115  GLN GLN A . n 
A 1 47  LYS 47  116  116  LYS LYS A . n 
A 1 48  ASP 48  117  117  ASP ASP A . n 
A 1 49  ARG 49  118  118  ARG ARG A . n 
A 1 50  THR 50  119  119  THR THR A . n 
A 1 51  PHE 51  120  120  PHE PHE A . n 
A 1 52  ALA 52  121  121  ALA ALA A . n 
A 1 53  VAL 53  122  122  VAL VAL A . n 
A 1 54  LEU 54  123  123  LEU LEU A . n 
A 1 55  ALA 55  124  124  ALA ALA A . n 
A 1 56  TYR 56  125  125  TYR TYR A . n 
A 1 57  SER 57  126  ?    ?   ?   A . n 
A 1 58  ASN 58  127  ?    ?   ?   A . n 
A 1 59  VAL 59  128  ?    ?   ?   A . n 
A 1 60  GLN 60  129  ?    ?   ?   A . n 
A 1 61  GLU 61  130  ?    ?   ?   A . n 
A 1 62  ARG 62  131  ?    ?   ?   A . n 
A 1 63  GLU 63  132  ?    ?   ?   A . n 
A 1 64  ALA 64  133  133  ALA ALA A . n 
A 1 65  GLN 65  134  134  GLN GLN A . n 
A 1 66  PHE 66  135  135  PHE PHE A . n 
A 1 67  GLY 67  136  136  GLY GLY A . n 
A 1 68  THR 68  137  137  THR THR A . n 
A 1 69  THR 69  138  138  THR THR A . n 
A 1 70  ALA 70  139  139  ALA ALA A . n 
A 1 71  GLU 71  140  140  GLU GLU A . n 
A 1 72  ILE 72  141  141  ILE ILE A . n 
A 1 73  TYR 73  142  142  TYR TYR A . n 
A 1 74  ALA 74  143  143  ALA ALA A . n 
A 1 75  TYR 75  144  144  TYR TYR A . n 
A 1 76  ARG 76  145  145  ARG ARG A . n 
A 1 77  GLU 77  146  146  GLU GLU A . n 
A 1 78  GLU 78  147  147  GLU GLU A . n 
A 1 79  GLN 79  148  148  GLN GLN A . n 
A 1 80  ASP 80  149  149  ASP ASP A . n 
A 1 81  PHE 81  150  150  PHE PHE A . n 
A 1 82  GLY 82  151  151  GLY GLY A . n 
A 1 83  ILE 83  152  152  ILE ILE A . n 
A 1 84  GLU 84  153  153  GLU GLU A . n 
A 1 85  ILE 85  154  154  ILE ILE A . n 
A 1 86  VAL 86  155  155  VAL VAL A . n 
A 1 87  LYS 87  156  156  LYS LYS A . n 
A 1 88  VAL 88  157  157  VAL VAL A . n 
A 1 89  LYS 89  158  158  LYS LYS A . n 
A 1 90  ALA 90  159  159  ALA ALA A . n 
A 1 91  ILE 91  160  160  ILE ILE A . n 
A 1 92  GLY 92  161  161  GLY GLY A . n 
A 1 93  ARG 93  162  162  ARG ARG A . n 
A 1 94  GLN 94  163  163  GLN GLN A . n 
A 1 95  ARG 95  164  164  ARG ARG A . n 
A 1 96  PHE 96  165  165  PHE PHE A . n 
A 1 97  LYS 97  166  166  LYS LYS A . n 
A 1 98  VAL 98  167  167  VAL VAL A . n 
A 1 99  LEU 99  168  168  LEU LEU A . n 
A 1 100 GLU 100 169  169  GLU GLU A . n 
A 1 101 LEU 101 170  170  LEU LEU A . n 
A 1 102 ARG 102 171  171  ARG ARG A . n 
A 1 103 THR 103 172  172  THR THR A . n 
A 1 104 GLN 104 173  173  GLN GLN A . n 
A 1 105 SER 105 174  174  SER SER A . n 
A 1 106 ASP 106 175  175  ASP ASP A . n 
A 1 107 GLY 107 176  176  GLY GLY A . n 
A 1 108 ILE 108 177  177  ILE ILE A . n 
A 1 109 GLN 109 178  178  GLN GLN A . n 
A 1 110 GLN 110 179  179  GLN GLN A . n 
A 1 111 ALA 111 180  180  ALA ALA A . n 
A 1 112 LYS 112 181  181  LYS LYS A . n 
A 1 113 VAL 113 182  182  VAL VAL A . n 
A 1 114 GLN 114 183  183  GLN GLN A . n 
A 1 115 ILE 115 184  184  ILE ILE A . n 
A 1 116 LEU 116 185  185  LEU LEU A . n 
A 1 117 PRO 117 186  186  PRO PRO A . n 
A 1 118 GLU 118 187  187  GLU GLU A . n 
A 1 119 CYS 119 188  188  CYS CYS A . n 
A 1 120 VAL 120 189  189  VAL VAL A . n 
A 1 121 LEU 121 190  190  LEU LEU A . n 
A 1 122 PRO 122 191  191  PRO PRO A . n 
A 1 123 SER 123 192  192  SER SER A . n 
A 1 124 THR 124 193  193  THR THR A . n 
A 1 125 MET 125 194  194  MET MET A . n 
A 1 126 SER 126 195  195  SER SER A . n 
A 1 127 ALA 127 196  196  ALA ALA A . n 
A 1 128 VAL 128 197  197  VAL VAL A . n 
A 1 129 GLN 129 198  198  GLN GLN A . n 
A 1 130 LEU 130 199  199  LEU LEU A . n 
A 1 131 GLU 131 200  200  GLU GLU A . n 
A 1 132 SER 132 201  201  SER SER A . n 
A 1 133 LEU 133 202  202  LEU LEU A . n 
A 1 134 ASN 134 203  203  ASN ASN A . n 
A 1 135 LYS 135 204  204  LYS LYS A . n 
A 1 136 CYS 136 205  205  CYS CYS A . n 
A 1 137 GLN 137 206  206  GLN GLN A . n 
A 1 138 ILE 138 207  207  ILE ILE A . n 
A 1 139 PHE 139 208  208  PHE PHE A . n 
A 1 140 PRO 140 209  209  PRO PRO A . n 
A 1 141 SER 141 210  210  SER SER A . n 
A 1 142 LYS 142 211  ?    ?   ?   A . n 
A 1 143 PRO 143 212  ?    ?   ?   A . n 
A 1 144 VAL 144 213  ?    ?   ?   A . n 
A 1 145 SER 145 214  ?    ?   ?   A . n 
A 1 146 ARG 146 215  ?    ?   ?   A . n 
A 1 147 GLU 147 216  ?    ?   ?   A . n 
A 1 148 ASP 148 217  ?    ?   ?   A . n 
A 1 149 GLN 149 218  ?    ?   ?   A . n 
A 1 150 CYS 150 219  ?    ?   ?   A . n 
A 1 151 SER 151 220  220  SER SER A . n 
A 1 152 TYR 152 221  221  TYR TYR A . n 
A 1 153 LYS 153 222  222  LYS LYS A . n 
A 1 154 TRP 154 223  223  TRP TRP A . n 
A 1 155 TRP 155 224  224  TRP TRP A . n 
A 1 156 GLN 156 225  225  GLN GLN A . n 
A 1 157 LYS 157 226  226  LYS LYS A . n 
A 1 158 TYR 158 227  227  TYR TYR A . n 
A 1 159 GLN 159 228  228  GLN GLN A . n 
A 1 160 LYS 160 229  229  LYS LYS A . n 
A 1 161 ARG 161 230  230  ARG ARG A . n 
A 1 162 LYS 162 231  231  LYS LYS A . n 
A 1 163 PHE 163 232  232  PHE PHE A . n 
A 1 164 HIS 164 233  233  HIS HIS A . n 
A 1 165 CYS 165 234  234  CYS CYS A . n 
A 1 166 ALA 166 235  235  ALA ALA A . n 
A 1 167 ASN 167 236  236  ASN ASN A . n 
A 1 168 LEU 168 237  237  LEU LEU A . n 
A 1 169 THR 169 238  238  THR THR A . n 
A 1 170 SER 170 239  239  SER SER A . n 
A 1 171 TRP 171 240  240  TRP TRP A . n 
A 1 172 PRO 172 241  241  PRO PRO A . n 
A 1 173 ARG 173 242  242  ARG ARG A . n 
A 1 174 TRP 174 243  243  TRP TRP A . n 
A 1 175 LEU 175 244  244  LEU LEU A . n 
A 1 176 TYR 176 245  245  TYR TYR A . n 
A 1 177 SER 177 246  246  SER SER A . n 
A 1 178 LEU 178 247  247  LEU LEU A . n 
A 1 179 TYR 179 248  248  TYR TYR A . n 
A 1 180 ASP 180 249  249  ASP ASP A . n 
A 1 181 ALA 181 250  250  ALA ALA A . n 
A 1 182 GLU 182 251  251  GLU GLU A . n 
A 1 183 THR 183 252  252  THR THR A . n 
A 1 184 LEU 184 253  253  LEU LEU A . n 
A 1 185 MET 185 254  254  MET MET A . n 
A 1 186 ASP 186 255  255  ASP ASP A . n 
A 1 187 ARG 187 256  256  ARG ARG A . n 
A 1 188 ILE 188 257  257  ILE ILE A . n 
A 1 189 LYS 189 258  258  LYS LYS A . n 
A 1 190 LYS 190 259  259  LYS LYS A . n 
A 1 191 GLN 191 260  260  GLN GLN A . n 
A 1 192 LEU 192 261  261  LEU LEU A . n 
A 1 193 ARG 193 262  262  ARG ARG A . n 
A 1 194 GLU 194 263  263  GLU GLU A . n 
A 1 195 TRP 195 264  264  TRP TRP A . n 
A 1 196 ASP 196 265  265  ASP ASP A . n 
A 1 197 GLU 197 266  266  GLU GLU A . n 
A 1 198 ASN 198 267  267  ASN ASN A . n 
A 1 199 LEU 199 268  268  LEU LEU A . n 
A 1 200 LYS 200 269  269  LYS LYS A . n 
A 1 201 ASP 201 270  270  ASP ASP A . n 
A 1 202 ASP 202 271  271  ASP ASP A . n 
A 1 203 SER 203 272  272  SER SER A . n 
A 1 204 LEU 204 273  273  LEU LEU A . n 
A 1 205 PRO 205 274  274  PRO PRO A . n 
A 1 206 SER 206 275  275  SER SER A . n 
A 1 207 ASN 207 276  276  ASN ASN A . n 
A 1 208 PRO 208 277  277  PRO PRO A . n 
A 1 209 ILE 209 278  278  ILE ILE A . n 
A 1 210 ASP 210 279  279  ASP ASP A . n 
A 1 211 PHE 211 280  280  PHE PHE A . n 
A 1 212 SER 212 281  281  SER SER A . n 
A 1 213 TYR 213 282  282  TYR TYR A . n 
A 1 214 ARG 214 283  283  ARG ARG A . n 
A 1 215 VAL 215 284  284  VAL VAL A . n 
A 1 216 ALA 216 285  285  ALA ALA A . n 
A 1 217 ALA 217 286  286  ALA ALA A . n 
A 1 218 CYS 218 287  287  CYS CYS A . n 
A 1 219 LEU 219 288  288  LEU LEU A . n 
A 1 220 PRO 220 289  289  PRO PRO A . n 
A 1 221 ILE 221 290  290  ILE ILE A . n 
A 1 222 ASP 222 291  291  ASP ASP A . n 
A 1 223 ASP 223 292  292  ASP ASP A . n 
A 1 224 VAL 224 293  293  VAL VAL A . n 
A 1 225 LEU 225 294  294  LEU LEU A . n 
A 1 226 ARG 226 295  295  ARG ARG A . n 
A 1 227 ILE 227 296  296  ILE ILE A . n 
A 1 228 GLN 228 297  297  GLN GLN A . n 
A 1 229 LEU 229 298  298  LEU LEU A . n 
A 1 230 LEU 230 299  299  LEU LEU A . n 
A 1 231 LYS 231 300  300  LYS LYS A . n 
A 1 232 ILE 232 301  301  ILE ILE A . n 
A 1 233 GLY 233 302  302  GLY GLY A . n 
A 1 234 SER 234 303  303  SER SER A . n 
A 1 235 ALA 235 304  304  ALA ALA A . n 
A 1 236 ILE 236 305  305  ILE ILE A . n 
A 1 237 GLN 237 306  306  GLN GLN A . n 
A 1 238 ARG 238 307  307  ARG ARG A . n 
A 1 239 LEU 239 308  308  LEU LEU A . n 
A 1 240 ARG 240 309  309  ARG ARG A . n 
A 1 241 CYS 241 310  310  CYS CYS A . n 
A 1 242 GLU 242 311  311  GLU GLU A . n 
A 1 243 LEU 243 312  312  LEU LEU A . n 
A 1 244 ASP 244 313  313  ASP ASP A . n 
A 1 245 ILE 245 314  314  ILE ILE A . n 
A 1 246 MET 246 315  315  MET MET A . n 
A 1 247 ASN 247 316  316  ASN ASN A . n 
A 1 248 LYS 248 317  317  LYS LYS A . n 
A 1 249 CYS 249 318  318  CYS CYS A . n 
A 1 250 THR 250 319  319  THR THR A . n 
A 1 251 SER 251 320  320  SER SER A . n 
A 1 252 LEU 252 321  321  LEU LEU A . n 
A 1 253 CYS 253 322  322  CYS CYS A . n 
A 1 254 CYS 254 323  323  CYS CYS A . n 
A 1 255 LYS 255 324  324  LYS LYS A . n 
A 1 256 GLN 256 325  325  GLN GLN A . n 
A 1 257 CYS 257 326  326  CYS CYS A . n 
A 1 258 GLN 258 327  327  GLN GLN A . n 
A 1 259 GLU 259 328  328  GLU GLU A . n 
A 1 260 THR 260 329  329  THR THR A . n 
A 1 261 GLU 261 330  330  GLU GLU A . n 
A 1 262 ILE 262 331  331  ILE ILE A . n 
A 1 263 THR 263 332  332  THR THR A . n 
A 1 264 THR 264 333  333  THR THR A . n 
A 1 265 LYS 265 334  334  LYS LYS A . n 
A 1 266 ASN 266 335  335  ASN ASN A . n 
A 1 267 GLU 267 336  336  GLU GLU A . n 
A 1 268 ILE 268 337  337  ILE ILE A . n 
A 1 269 PHE 269 338  338  PHE PHE A . n 
A 1 270 SER 270 339  339  SER SER A . n 
A 1 271 LEU 271 340  340  LEU LEU A . n 
A 1 272 SER 272 341  341  SER SER A . n 
A 1 273 LEU 273 342  342  LEU LEU A . n 
A 1 274 CYS 274 343  343  CYS CYS A . n 
A 1 275 GLY 275 344  344  GLY GLY A . n 
A 1 276 PRO 276 345  345  PRO PRO A . n 
A 1 277 MET 277 346  346  MET MET A . n 
A 1 278 ALA 278 347  347  ALA ALA A . n 
A 1 279 ALA 279 348  348  ALA ALA A . n 
A 1 280 TYR 280 349  349  TYR TYR A . n 
A 1 281 VAL 281 350  350  VAL VAL A . n 
A 1 282 ASN 282 351  351  ASN ASN A . n 
A 1 283 PRO 283 352  352  PRO PRO A . n 
A 1 284 HIS 284 353  353  HIS HIS A . n 
A 1 285 GLY 285 354  354  GLY GLY A . n 
A 1 286 TYR 286 355  355  TYR TYR A . n 
A 1 287 VAL 287 356  356  VAL VAL A . n 
A 1 288 HIS 288 357  357  HIS HIS A . n 
A 1 289 GLU 289 358  358  GLU GLU A . n 
A 1 290 THR 290 359  359  THR THR A . n 
A 1 291 LEU 291 360  360  LEU LEU A . n 
A 1 292 THR 292 361  361  THR THR A . n 
A 1 293 VAL 293 362  362  VAL VAL A . n 
A 1 294 TYR 294 363  363  TYR TYR A . n 
A 1 295 LYS 295 364  364  LYS LYS A . n 
A 1 296 ALA 296 365  365  ALA ALA A . n 
A 1 297 CYS 297 366  366  CYS CYS A . n 
A 1 298 ASN 298 367  367  ASN ASN A . n 
A 1 299 LEU 299 368  368  LEU LEU A . n 
A 1 300 ASN 300 369  369  ASN ASN A . n 
A 1 301 LEU 301 370  370  LEU LEU A . n 
A 1 302 ILE 302 371  371  ILE ILE A . n 
A 1 303 GLY 303 372  372  GLY GLY A . n 
A 1 304 ARG 304 373  373  ARG ARG A . n 
A 1 305 PRO 305 374  374  PRO PRO A . n 
A 1 306 SER 306 375  375  SER SER A . n 
A 1 307 THR 307 376  376  THR THR A . n 
A 1 308 GLU 308 377  377  GLU GLU A . n 
A 1 309 HIS 309 378  378  HIS HIS A . n 
A 1 310 SER 310 379  379  SER SER A . n 
A 1 311 TRP 311 380  380  TRP TRP A . n 
A 1 312 PHE 312 381  381  PHE PHE A . n 
A 1 313 PRO 313 382  382  PRO PRO A . n 
A 1 314 GLY 314 383  383  GLY GLY A . n 
A 1 315 TYR 315 384  384  TYR TYR A . n 
A 1 316 ALA 316 385  385  ALA ALA A . n 
A 1 317 TRP 317 386  386  TRP TRP A . n 
A 1 318 THR 318 387  387  THR THR A . n 
A 1 319 VAL 319 388  388  VAL VAL A . n 
A 1 320 ALA 320 389  389  ALA ALA A . n 
A 1 321 GLN 321 390  390  GLN GLN A . n 
A 1 322 CYS 322 391  391  CYS CYS A . n 
A 1 323 LYS 323 392  392  LYS LYS A . n 
A 1 324 ILE 324 393  393  ILE ILE A . n 
A 1 325 CYS 325 394  394  CYS CYS A . n 
A 1 326 ALA 326 395  395  ALA ALA A . n 
A 1 327 SER 327 396  396  SER SER A . n 
A 1 328 HIS 328 397  397  HIS HIS A . n 
A 1 329 ILE 329 398  398  ILE ILE A . n 
A 1 330 GLY 330 399  399  GLY GLY A . n 
A 1 331 TRP 331 400  400  TRP TRP A . n 
A 1 332 LYS 332 401  401  LYS LYS A . n 
A 1 333 PHE 333 402  402  PHE PHE A . n 
A 1 334 THR 334 403  403  THR THR A . n 
A 1 335 ALA 335 404  404  ALA ALA A . n 
A 1 336 THR 336 405  405  THR THR A . n 
A 1 337 LYS 337 406  406  LYS LYS A . n 
A 1 338 LYS 338 407  407  LYS LYS A . n 
A 1 339 ASP 339 408  408  ASP ASP A . n 
A 1 340 MET 340 409  409  MET MET A . n 
A 1 341 SER 341 410  410  SER SER A . n 
A 1 342 PRO 342 411  411  PRO PRO A . n 
A 1 343 GLN 343 412  412  GLN GLN A . n 
A 1 344 LYS 344 413  413  LYS LYS A . n 
A 1 345 PHE 345 414  414  PHE PHE A . n 
A 1 346 TRP 346 415  415  TRP TRP A . n 
A 1 347 GLY 347 416  416  GLY GLY A . n 
A 1 348 LEU 348 417  417  LEU LEU A . n 
A 1 349 THR 349 418  418  THR THR A . n 
A 1 350 ARG 350 419  419  ARG ARG A . n 
A 1 351 SER 351 420  420  SER SER A . n 
A 1 352 ALA 352 421  421  ALA ALA A . n 
A 1 353 LEU 353 422  422  LEU LEU A . n 
A 1 354 LEU 354 423  423  LEU LEU A . n 
A 1 355 PRO 355 424  424  PRO PRO A . n 
A 1 356 THR 356 425  425  THR THR A . n 
A 1 357 ILE 357 426  426  ILE ILE A . n 
A 1 358 PRO 358 427  427  PRO PRO A . n 
A 1 359 ASP 359 428  ?    ?   ?   A . n 
A 1 360 THR 360 429  ?    ?   ?   A . n 
A 1 361 GLU 361 430  ?    ?   ?   A . n 
A 1 362 ASP 362 431  ?    ?   ?   A . n 
A 1 363 GLU 363 432  ?    ?   ?   A . n 
A 1 364 ILE 364 433  ?    ?   ?   A . n 
A 1 365 SER 365 434  ?    ?   ?   A . n 
A 1 366 PRO 366 435  ?    ?   ?   A . n 
A 1 367 ASP 367 436  ?    ?   ?   A . n 
A 1 368 LYS 368 437  ?    ?   ?   A . n 
A 1 369 VAL 369 438  438  VAL VAL A . n 
A 1 370 ILE 370 439  439  ILE ILE A . n 
A 1 371 LEU 371 440  440  LEU LEU A . n 
A 1 372 CYS 372 441  441  CYS CYS A . n 
A 1 373 LEU 373 442  442  LEU LEU A . n 
B 2 1   MET 1   1    ?    ?   ?   B . n 
B 2 2   SER 2   2    2    SER SER B . n 
B 2 3   TYR 3   3    3    TYR TYR B . n 
B 2 4   ASN 4   4    4    ASN ASN B . n 
B 2 5   TYR 5   5    5    TYR TYR B . n 
B 2 6   VAL 6   6    6    VAL VAL B . n 
B 2 7   VAL 7   7    7    VAL VAL B . n 
B 2 8   THR 8   8    8    THR THR B . n 
B 2 9   ALA 9   9    9    ALA ALA B . n 
B 2 10  GLN 10  10   10   GLN GLN B . n 
B 2 11  LYS 11  11   11   LYS LYS B . n 
B 2 12  PRO 12  12   12   PRO PRO B . n 
B 2 13  THR 13  13   13   THR THR B . n 
B 2 14  ALA 14  14   14   ALA ALA B . n 
B 2 15  VAL 15  15   15   VAL VAL B . n 
B 2 16  ASN 16  16   16   ASN ASN B . n 
B 2 17  GLY 17  17   17   GLY GLY B . n 
B 2 18  CYS 18  18   18   CYS CYS B . n 
B 2 19  VAL 19  19   19   VAL VAL B . n 
B 2 20  THR 20  20   20   THR THR B . n 
B 2 21  GLY 21  21   21   GLY GLY B . n 
B 2 22  HIS 22  22   22   HIS HIS B . n 
B 2 23  PHE 23  23   23   PHE PHE B . n 
B 2 24  THR 24  24   24   THR THR B . n 
B 2 25  SER 25  25   25   SER SER B . n 
B 2 26  ALA 26  26   26   ALA ALA B . n 
B 2 27  GLU 27  27   27   GLU GLU B . n 
B 2 28  ASP 28  28   28   ASP ASP B . n 
B 2 29  LEU 29  29   29   LEU LEU B . n 
B 2 30  ASN 30  30   30   ASN ASN B . n 
B 2 31  LEU 31  31   31   LEU LEU B . n 
B 2 32  LEU 32  32   32   LEU LEU B . n 
B 2 33  ILE 33  33   33   ILE ILE B . n 
B 2 34  ALA 34  34   34   ALA ALA B . n 
B 2 35  LYS 35  35   35   LYS LYS B . n 
B 2 36  ASN 36  36   36   ASN ASN B . n 
B 2 37  THR 37  37   37   THR THR B . n 
B 2 38  ARG 38  38   38   ARG ARG B . n 
B 2 39  LEU 39  39   39   LEU LEU B . n 
B 2 40  GLU 40  40   40   GLU GLU B . n 
B 2 41  ILE 41  41   41   ILE ILE B . n 
B 2 42  TYR 42  42   42   TYR TYR B . n 
B 2 43  VAL 43  43   43   VAL VAL B . n 
B 2 44  VAL 44  44   44   VAL VAL B . n 
B 2 45  THR 45  45   45   THR THR B . n 
B 2 46  ALA 46  46   46   ALA ALA B . n 
B 2 47  GLU 47  47   47   GLU GLU B . n 
B 2 48  GLY 48  48   48   GLY GLY B . n 
B 2 49  LEU 49  49   49   LEU LEU B . n 
B 2 50  ARG 50  50   50   ARG ARG B . n 
B 2 51  PRO 51  51   51   PRO PRO B . n 
B 2 52  VAL 52  52   52   VAL VAL B . n 
B 2 53  LYS 53  53   53   LYS LYS B . n 
B 2 54  GLU 54  54   54   GLU GLU B . n 
B 2 55  VAL 55  55   55   VAL VAL B . n 
B 2 56  GLY 56  56   56   GLY GLY B . n 
B 2 57  MET 57  57   57   MET MET B . n 
B 2 58  TYR 58  58   58   TYR TYR B . n 
B 2 59  GLY 59  59   59   GLY GLY B . n 
B 2 60  LYS 60  60   60   LYS LYS B . n 
B 2 61  ILE 61  61   61   ILE ILE B . n 
B 2 62  ALA 62  62   62   ALA ALA B . n 
B 2 63  VAL 63  63   63   VAL VAL B . n 
B 2 64  MET 64  64   64   MET MET B . n 
B 2 65  GLU 65  65   65   GLU GLU B . n 
B 2 66  LEU 66  66   66   LEU LEU B . n 
B 2 67  PHE 67  67   67   PHE PHE B . n 
B 2 68  ARG 68  68   68   ARG ARG B . n 
B 2 69  PRO 69  69   69   PRO PRO B . n 
B 2 70  LYS 70  70   70   LYS LYS B . n 
B 2 71  GLY 71  71   71   GLY GLY B . n 
B 2 72  GLU 72  72   72   GLU GLU B . n 
B 2 73  SER 73  73   73   SER SER B . n 
B 2 74  LYS 74  74   74   LYS LYS B . n 
B 2 75  ASP 75  75   75   ASP ASP B . n 
B 2 76  LEU 76  76   76   LEU LEU B . n 
B 2 77  LEU 77  77   77   LEU LEU B . n 
B 2 78  PHE 78  78   78   PHE PHE B . n 
B 2 79  ILE 79  79   79   ILE ILE B . n 
B 2 80  LEU 80  80   80   LEU LEU B . n 
B 2 81  THR 81  81   81   THR THR B . n 
B 2 82  ALA 82  82   82   ALA ALA B . n 
B 2 83  LYS 83  83   83   LYS LYS B . n 
B 2 84  TYR 84  84   84   TYR TYR B . n 
B 2 85  ASN 85  85   85   ASN ASN B . n 
B 2 86  ALA 86  86   86   ALA ALA B . n 
B 2 87  CYS 87  87   87   CYS CYS B . n 
B 2 88  ILE 88  88   88   ILE ILE B . n 
B 2 89  LEU 89  89   89   LEU LEU B . n 
B 2 90  GLU 90  90   90   GLU GLU B . n 
B 2 91  TYR 91  91   91   TYR TYR B . n 
B 2 92  LYS 92  92   92   LYS LYS B . n 
B 2 93  GLN 93  93   93   GLN GLN B . n 
B 2 94  SER 94  94   94   SER SER B . n 
B 2 95  GLY 95  95   95   GLY GLY B . n 
B 2 96  GLU 96  96   96   GLU GLU B . n 
B 2 97  SER 97  97   97   SER SER B . n 
B 2 98  ILE 98  98   98   ILE ILE B . n 
B 2 99  ASP 99  99   99   ASP ASP B . n 
B 2 100 ILE 100 100  100  ILE ILE B . n 
B 2 101 ILE 101 101  101  ILE ILE B . n 
B 2 102 THR 102 102  102  THR THR B . n 
B 2 103 ARG 103 103  103  ARG ARG B . n 
B 2 104 ALA 104 104  104  ALA ALA B . n 
B 2 105 HIS 105 105  105  HIS HIS B . n 
B 2 106 GLY 106 106  106  GLY GLY B . n 
B 2 107 ASN 107 107  107  ASN ASN B . n 
B 2 108 VAL 108 108  108  VAL VAL B . n 
B 2 109 GLN 109 109  109  GLN GLN B . n 
B 2 110 ASP 110 110  110  ASP ASP B . n 
B 2 111 ARG 111 111  111  ARG ARG B . n 
B 2 112 ILE 112 112  112  ILE ILE B . n 
B 2 113 GLY 113 113  113  GLY GLY B . n 
B 2 114 ARG 114 114  114  ARG ARG B . n 
B 2 115 PRO 115 115  115  PRO PRO B . n 
B 2 116 SER 116 116  116  SER SER B . n 
B 2 117 GLU 117 117  117  GLU GLU B . n 
B 2 118 THR 118 118  118  THR THR B . n 
B 2 119 GLY 119 119  119  GLY GLY B . n 
B 2 120 ILE 120 120  120  ILE ILE B . n 
B 2 121 ILE 121 121  121  ILE ILE B . n 
B 2 122 GLY 122 122  122  GLY GLY B . n 
B 2 123 ILE 123 123  123  ILE ILE B . n 
B 2 124 ILE 124 124  124  ILE ILE B . n 
B 2 125 ASP 125 125  125  ASP ASP B . n 
B 2 126 PRO 126 126  126  PRO PRO B . n 
B 2 127 GLU 127 127  127  GLU GLU B . n 
B 2 128 CYS 128 128  128  CYS CYS B . n 
B 2 129 ARG 129 129  129  ARG ARG B . n 
B 2 130 MET 130 130  130  MET MET B . n 
B 2 131 ILE 131 131  131  ILE ILE B . n 
B 2 132 GLY 132 132  132  GLY GLY B . n 
B 2 133 LEU 133 133  133  LEU LEU B . n 
B 2 134 ARG 134 134  134  ARG ARG B . n 
B 2 135 LEU 135 135  135  LEU LEU B . n 
B 2 136 TYR 136 136  136  TYR TYR B . n 
B 2 137 ASP 137 137  137  ASP ASP B . n 
B 2 138 GLY 138 138  138  GLY GLY B . n 
B 2 139 LEU 139 139  139  LEU LEU B . n 
B 2 140 PHE 140 140  140  PHE PHE B . n 
B 2 141 LYS 141 141  141  LYS LYS B . n 
B 2 142 VAL 142 142  142  VAL VAL B . n 
B 2 143 ILE 143 143  143  ILE ILE B . n 
B 2 144 PRO 144 144  144  PRO PRO B . n 
B 2 145 LEU 145 145  145  LEU LEU B . n 
B 2 146 ASP 146 146  146  ASP ASP B . n 
B 2 147 ARG 147 147  147  ARG ARG B . n 
B 2 148 ASP 148 148  148  ASP ASP B . n 
B 2 149 ASN 149 149  149  ASN ASN B . n 
B 2 150 LYS 150 150  150  LYS LYS B . n 
B 2 151 GLU 151 151  151  GLU GLU B . n 
B 2 152 LEU 152 152  152  LEU LEU B . n 
B 2 153 LYS 153 153  153  LYS LYS B . n 
B 2 154 ALA 154 154  154  ALA ALA B . n 
B 2 155 PHE 155 155  155  PHE PHE B . n 
B 2 156 ASN 156 156  156  ASN ASN B . n 
B 2 157 ILE 157 157  157  ILE ILE B . n 
B 2 158 ARG 158 158  158  ARG ARG B . n 
B 2 159 LEU 159 159  159  LEU LEU B . n 
B 2 160 GLU 160 160  160  GLU GLU B . n 
B 2 161 GLU 161 161  161  GLU GLU B . n 
B 2 162 LEU 162 162  162  LEU LEU B . n 
B 2 163 HIS 163 163  163  HIS HIS B . n 
B 2 164 VAL 164 164  164  VAL VAL B . n 
B 2 165 ILE 165 165  165  ILE ILE B . n 
B 2 166 ASP 166 166  166  ASP ASP B . n 
B 2 167 VAL 167 167  167  VAL VAL B . n 
B 2 168 LYS 168 168  168  LYS LYS B . n 
B 2 169 PHE 169 169  169  PHE PHE B . n 
B 2 170 LEU 170 170  170  LEU LEU B . n 
B 2 171 TYR 171 171  171  TYR TYR B . n 
B 2 172 GLY 172 172  172  GLY GLY B . n 
B 2 173 CYS 173 173  173  CYS CYS B . n 
B 2 174 GLN 174 174  174  GLN GLN B . n 
B 2 175 ALA 175 175  175  ALA ALA B . n 
B 2 176 PRO 176 176  176  PRO PRO B . n 
B 2 177 THR 177 177  177  THR THR B . n 
B 2 178 ILE 178 178  178  ILE ILE B . n 
B 2 179 CYS 179 179  179  CYS CYS B . n 
B 2 180 PHE 180 180  180  PHE PHE B . n 
B 2 181 VAL 181 181  181  VAL VAL B . n 
B 2 182 TYR 182 182  182  TYR TYR B . n 
B 2 183 GLN 183 183  183  GLN GLN B . n 
B 2 184 ASP 184 184  184  ASP ASP B . n 
B 2 185 PRO 185 185  185  PRO PRO B . n 
B 2 186 GLN 186 186  186  GLN GLN B . n 
B 2 187 GLY 187 187  187  GLY GLY B . n 
B 2 188 ARG 188 188  188  ARG ARG B . n 
B 2 189 HIS 189 189  189  HIS HIS B . n 
B 2 190 VAL 190 190  190  VAL VAL B . n 
B 2 191 LYS 191 191  191  LYS LYS B . n 
B 2 192 THR 192 192  192  THR THR B . n 
B 2 193 TYR 193 193  193  TYR TYR B . n 
B 2 194 GLU 194 194  194  GLU GLU B . n 
B 2 195 VAL 195 195  195  VAL VAL B . n 
B 2 196 SER 196 196  196  SER SER B . n 
B 2 197 LEU 197 197  197  LEU LEU B . n 
B 2 198 ARG 198 198  198  ARG ARG B . n 
B 2 199 GLU 199 199  199  GLU GLU B . n 
B 2 200 LYS 200 200  200  LYS LYS B . n 
B 2 201 GLU 201 201  201  GLU GLU B . n 
B 2 202 PHE 202 202  202  PHE PHE B . n 
B 2 203 ASN 203 203  203  ASN ASN B . n 
B 2 204 LYS 204 204  204  LYS LYS B . n 
B 2 205 GLY 205 205  205  GLY GLY B . n 
B 2 206 PRO 206 206  206  PRO PRO B . n 
B 2 207 TRP 207 207  207  TRP TRP B . n 
B 2 208 LYS 208 208  208  LYS LYS B . n 
B 2 209 GLN 209 209  209  GLN GLN B . n 
B 2 210 GLU 210 210  210  GLU GLU B . n 
B 2 211 ASN 211 211  211  ASN ASN B . n 
B 2 212 VAL 212 212  212  VAL VAL B . n 
B 2 213 GLU 213 213  213  GLU GLU B . n 
B 2 214 ALA 214 214  214  ALA ALA B . n 
B 2 215 GLU 215 215  215  GLU GLU B . n 
B 2 216 ALA 216 216  216  ALA ALA B . n 
B 2 217 SER 217 217  217  SER SER B . n 
B 2 218 MET 218 218  218  MET MET B . n 
B 2 219 VAL 219 219  219  VAL VAL B . n 
B 2 220 ILE 220 220  220  ILE ILE B . n 
B 2 221 ALA 221 221  221  ALA ALA B . n 
B 2 222 VAL 222 222  222  VAL VAL B . n 
B 2 223 PRO 223 223  223  PRO PRO B . n 
B 2 224 GLU 224 224  224  GLU GLU B . n 
B 2 225 PRO 225 225  225  PRO PRO B . n 
B 2 226 PHE 226 226  226  PHE PHE 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 ALA 229 229  229  ALA ALA B . n 
B 2 230 ILE 230 230  230  ILE ILE B . n 
B 2 231 ILE 231 231  231  ILE ILE B . n 
B 2 232 ILE 232 232  232  ILE ILE B . n 
B 2 233 GLY 233 233  233  GLY GLY B . n 
B 2 234 GLN 234 234  234  GLN GLN B . n 
B 2 235 GLU 235 235  235  GLU GLU B . n 
B 2 236 SER 236 236  236  SER SER B . n 
B 2 237 ILE 237 237  237  ILE ILE B . n 
B 2 238 THR 238 238  238  THR THR B . n 
B 2 239 TYR 239 239  239  TYR TYR B . n 
B 2 240 HIS 240 240  240  HIS HIS B . n 
B 2 241 ASN 241 241  241  ASN ASN B . n 
B 2 242 GLY 242 242  242  GLY GLY B . n 
B 2 243 ASP 243 243  243  ASP ASP B . n 
B 2 244 LYS 244 244  244  LYS LYS B . n 
B 2 245 TYR 245 245  245  TYR TYR B . n 
B 2 246 LEU 246 246  246  LEU LEU B . n 
B 2 247 ALA 247 247  247  ALA ALA B . n 
B 2 248 ILE 248 248  248  ILE ILE B . n 
B 2 249 ALA 249 249  249  ALA ALA B . n 
B 2 250 PRO 250 250  250  PRO PRO B . n 
B 2 251 PRO 251 251  251  PRO PRO B . n 
B 2 252 ILE 252 252  252  ILE ILE B . n 
B 2 253 ILE 253 253  253  ILE ILE B . n 
B 2 254 LYS 254 254  254  LYS LYS B . n 
B 2 255 GLN 255 255  255  GLN GLN B . n 
B 2 256 SER 256 256  256  SER SER B . n 
B 2 257 THR 257 257  257  THR THR B . n 
B 2 258 ILE 258 258  258  ILE ILE B . n 
B 2 259 VAL 259 259  259  VAL VAL B . n 
B 2 260 CYS 260 260  260  CYS CYS B . n 
B 2 261 HIS 261 261  261  HIS HIS B . n 
B 2 262 ASN 262 262  262  ASN ASN B . n 
B 2 263 ARG 263 263  263  ARG ARG B . n 
B 2 264 VAL 264 264  264  VAL VAL B . n 
B 2 265 ASP 265 265  265  ASP ASP B . n 
B 2 266 PRO 266 266  266  PRO PRO B . n 
B 2 267 ASN 267 267  267  ASN ASN B . n 
B 2 268 GLY 268 268  268  GLY GLY B . n 
B 2 269 SER 269 269  269  SER SER B . n 
B 2 270 ARG 270 270  270  ARG ARG B . n 
B 2 271 TYR 271 271  271  TYR TYR B . n 
B 2 272 LEU 272 272  272  LEU LEU B . n 
B 2 273 LEU 273 273  273  LEU LEU B . n 
B 2 274 GLY 274 274  274  GLY GLY B . n 
B 2 275 ASP 275 275  275  ASP ASP B . n 
B 2 276 MET 276 276  276  MET MET B . n 
B 2 277 GLU 277 277  277  GLU GLU B . n 
B 2 278 GLY 278 278  278  GLY GLY B . n 
B 2 279 ARG 279 279  279  ARG ARG B . n 
B 2 280 LEU 280 280  280  LEU LEU B . n 
B 2 281 PHE 281 281  281  PHE PHE B . n 
B 2 282 MET 282 282  282  MET MET B . n 
B 2 283 LEU 283 283  283  LEU LEU B . n 
B 2 284 LEU 284 284  284  LEU LEU B . n 
B 2 285 LEU 285 285  285  LEU LEU B . n 
B 2 286 GLU 286 286  286  GLU GLU B . n 
B 2 287 LYS 287 287  287  LYS LYS B . n 
B 2 288 GLU 288 288  288  GLU GLU B . n 
B 2 289 GLU 289 289  289  GLU GLU B . n 
B 2 290 GLN 290 290  290  GLN GLN B . n 
B 2 291 MET 291 291  291  MET MET B . n 
B 2 292 ASP 292 292  292  ASP ASP B . n 
B 2 293 GLY 293 293  293  GLY GLY B . n 
B 2 294 THR 294 294  294  THR THR B . n 
B 2 295 VAL 295 295  295  VAL VAL B . n 
B 2 296 THR 296 296  296  THR THR B . n 
B 2 297 LEU 297 297  297  LEU LEU B . n 
B 2 298 LYS 298 298  298  LYS LYS B . n 
B 2 299 ASP 299 299  299  ASP ASP B . n 
B 2 300 LEU 300 300  300  LEU LEU B . n 
B 2 301 ARG 301 301  301  ARG ARG B . n 
B 2 302 VAL 302 302  302  VAL VAL B . n 
B 2 303 GLU 303 303  303  GLU GLU B . n 
B 2 304 LEU 304 304  304  LEU LEU B . n 
B 2 305 LEU 305 305  305  LEU LEU B . n 
B 2 306 GLY 306 306  306  GLY GLY B . n 
B 2 307 GLU 307 307  307  GLU GLU B . n 
B 2 308 THR 308 308  308  THR THR B . n 
B 2 309 SER 309 309  309  SER SER B . n 
B 2 310 ILE 310 310  310  ILE ILE B . n 
B 2 311 ALA 311 311  311  ALA ALA B . n 
B 2 312 GLU 312 312  312  GLU GLU B . n 
B 2 313 CYS 313 313  313  CYS CYS B . n 
B 2 314 LEU 314 314  314  LEU LEU B . n 
B 2 315 THR 315 315  315  THR THR B . n 
B 2 316 TYR 316 316  316  TYR TYR 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 ASN 319 319  319  ASN ASN B . n 
B 2 320 GLY 320 320  320  GLY GLY B . n 
B 2 321 VAL 321 321  321  VAL VAL B . n 
B 2 322 VAL 322 322  322  VAL VAL B . n 
B 2 323 PHE 323 323  323  PHE PHE B . n 
B 2 324 VAL 324 324  324  VAL VAL B . n 
B 2 325 GLY 325 325  325  GLY GLY B . n 
B 2 326 SER 326 326  326  SER SER B . n 
B 2 327 ARG 327 327  327  ARG ARG B . n 
B 2 328 LEU 328 328  328  LEU LEU B . n 
B 2 329 GLY 329 329  329  GLY GLY B . n 
B 2 330 ASP 330 330  330  ASP ASP B . n 
B 2 331 SER 331 331  331  SER SER B . n 
B 2 332 GLN 332 332  332  GLN GLN B . n 
B 2 333 LEU 333 333  333  LEU LEU B . n 
B 2 334 VAL 334 334  334  VAL VAL B . n 
B 2 335 LYS 335 335  335  LYS LYS B . n 
B 2 336 LEU 336 336  336  LEU LEU B . n 
B 2 337 ASN 337 337  337  ASN ASN B . n 
B 2 338 VAL 338 338  338  VAL VAL B . n 
B 2 339 ASP 339 339  339  ASP ASP B . n 
B 2 340 SER 340 340  340  SER SER B . n 
B 2 341 ASN 341 341  341  ASN ASN B . n 
B 2 342 GLU 342 342  342  GLU GLU B . n 
B 2 343 GLN 343 343  343  GLN GLN B . n 
B 2 344 GLY 344 344  344  GLY GLY B . n 
B 2 345 SER 345 345  345  SER SER B . n 
B 2 346 TYR 346 346  346  TYR TYR B . n 
B 2 347 VAL 347 347  347  VAL VAL B . n 
B 2 348 VAL 348 348  348  VAL VAL B . n 
B 2 349 ALA 349 349  349  ALA ALA B . n 
B 2 350 MET 350 350  350  MET MET B . n 
B 2 351 GLU 351 351  351  GLU GLU B . n 
B 2 352 THR 352 352  352  THR THR B . n 
B 2 353 PHE 353 353  353  PHE PHE B . n 
B 2 354 THR 354 354  354  THR THR B . n 
B 2 355 ASN 355 355  355  ASN ASN B . n 
B 2 356 LEU 356 356  356  LEU LEU B . n 
B 2 357 GLY 357 357  357  GLY GLY B . n 
B 2 358 PRO 358 358  358  PRO PRO B . n 
B 2 359 ILE 359 359  359  ILE ILE B . n 
B 2 360 VAL 360 360  360  VAL VAL B . n 
B 2 361 ASP 361 361  361  ASP ASP B . n 
B 2 362 MET 362 362  362  MET MET B . n 
B 2 363 CYS 363 363  363  CYS CYS B . n 
B 2 364 VAL 364 364  364  VAL VAL B . n 
B 2 365 VAL 365 365  365  VAL VAL B . n 
B 2 366 ASP 366 366  366  ASP ASP B . n 
B 2 367 LEU 367 367  367  LEU LEU B . n 
B 2 368 GLU 368 368  368  GLU GLU B . n 
B 2 369 ARG 369 369  369  ARG ARG B . n 
B 2 370 GLN 370 370  370  GLN GLN B . n 
B 2 371 GLY 371 371  371  GLY GLY B . n 
B 2 372 GLN 372 372  372  GLN GLN B . n 
B 2 373 GLY 373 373  373  GLY GLY B . n 
B 2 374 GLN 374 374  374  GLN GLN B . n 
B 2 375 LEU 375 375  375  LEU LEU B . n 
B 2 376 VAL 376 376  376  VAL VAL B . n 
B 2 377 THR 377 377  377  THR THR B . n 
B 2 378 CYS 378 378  378  CYS CYS B . n 
B 2 379 SER 379 379  379  SER SER B . n 
B 2 380 GLY 380 380  380  GLY GLY B . n 
B 2 381 ALA 381 381  381  ALA ALA B . n 
B 2 382 PHE 382 382  382  PHE PHE B . n 
B 2 383 LYS 383 383  383  LYS LYS B . n 
B 2 384 GLU 384 384  384  GLU GLU B . n 
B 2 385 GLY 385 385  385  GLY GLY B . n 
B 2 386 SER 386 386  386  SER SER B . n 
B 2 387 LEU 387 387  387  LEU LEU B . n 
B 2 388 ARG 388 388  388  ARG ARG B . n 
B 2 389 ILE 389 389  389  ILE ILE B . n 
B 2 390 ILE 390 390  390  ILE ILE B . n 
B 2 391 ARG 391 391  391  ARG ARG B . n 
B 2 392 ASN 392 392  392  ASN ASN B . n 
B 2 393 GLY 393 697  ?    ?   ?   B . n 
B 2 394 ILE 394 698  ?    ?   ?   B . n 
B 2 395 GLY 395 699  ?    ?   ?   B . n 
B 2 396 GLY 396 700  ?    ?   ?   B . n 
B 2 397 ASN 397 701  ?    ?   ?   B . n 
B 2 398 GLY 398 702  ?    ?   ?   B . n 
B 2 399 ASN 399 703  ?    ?   ?   B . n 
B 2 400 SER 400 704  ?    ?   ?   B . n 
B 2 401 GLY 401 705  ?    ?   ?   B . n 
B 2 402 GLU 402 706  ?    ?   ?   B . n 
B 2 403 ILE 403 707  ?    ?   ?   B . n 
B 2 404 GLN 404 708  ?    ?   ?   B . n 
B 2 405 LYS 405 709  ?    ?   ?   B . n 
B 2 406 LEU 406 710  710  LEU LEU B . n 
B 2 407 HIS 407 711  711  HIS HIS B . n 
B 2 408 ILE 408 712  712  ILE ILE B . n 
B 2 409 ARG 409 713  713  ARG ARG B . n 
B 2 410 THR 410 714  714  THR THR B . n 
B 2 411 VAL 411 715  715  VAL VAL B . n 
B 2 412 PRO 412 716  716  PRO PRO B . n 
B 2 413 LEU 413 717  717  LEU LEU B . n 
B 2 414 TYR 414 718  718  TYR TYR B . n 
B 2 415 GLU 415 719  719  GLU GLU B . n 
B 2 416 SER 416 720  720  SER SER B . n 
B 2 417 PRO 417 721  721  PRO PRO B . n 
B 2 418 ARG 418 722  722  ARG ARG B . n 
B 2 419 LYS 419 723  723  LYS LYS B . n 
B 2 420 ILE 420 724  724  ILE ILE B . n 
B 2 421 CYS 421 725  725  CYS CYS B . n 
B 2 422 TYR 422 726  726  TYR TYR B . n 
B 2 423 GLN 423 727  727  GLN GLN B . n 
B 2 424 GLU 424 728  728  GLU GLU B . n 
B 2 425 VAL 425 729  729  VAL VAL B . n 
B 2 426 SER 426 730  730  SER SER B . n 
B 2 427 GLN 427 731  731  GLN GLN B . n 
B 2 428 CYS 428 732  732  CYS CYS B . n 
B 2 429 PHE 429 733  733  PHE PHE B . n 
B 2 430 GLY 430 734  734  GLY GLY B . n 
B 2 431 VAL 431 735  735  VAL VAL B . n 
B 2 432 LEU 432 736  736  LEU LEU B . n 
B 2 433 SER 433 737  737  SER SER B . n 
B 2 434 SER 434 738  738  SER SER B . n 
B 2 435 ARG 435 739  739  ARG ARG B . n 
B 2 436 ILE 436 740  740  ILE ILE B . n 
B 2 437 GLU 437 741  741  GLU GLU B . n 
B 2 438 VAL 438 742  742  VAL VAL B . n 
B 2 439 GLN 439 743  743  GLN GLN B . n 
B 2 440 ASP 440 744  744  ASP ASP B . n 
B 2 441 THR 441 745  745  THR THR B . n 
B 2 442 SER 442 746  746  SER SER B . n 
B 2 443 GLY 443 747  747  GLY GLY B . n 
B 2 444 GLY 444 748  748  GLY GLY B . n 
B 2 445 THR 445 749  749  THR THR B . n 
B 2 446 THR 446 750  750  THR THR B . n 
B 2 447 ALA 447 751  751  ALA ALA B . n 
B 2 448 LEU 448 752  752  LEU LEU B . n 
B 2 449 ARG 449 753  753  ARG ARG B . n 
B 2 450 PRO 450 754  754  PRO PRO B . n 
B 2 451 SER 451 755  755  SER SER B . n 
B 2 452 ALA 452 756  756  ALA ALA B . n 
B 2 453 SER 453 757  757  SER SER B . n 
B 2 454 THR 454 758  758  THR THR B . n 
B 2 455 GLN 455 759  759  GLN GLN B . n 
B 2 456 ALA 456 760  760  ALA ALA B . n 
B 2 457 LEU 457 761  761  LEU LEU B . n 
B 2 458 SER 458 762  762  SER SER B . n 
B 2 459 SER 459 763  763  SER SER B . n 
B 2 460 SER 460 764  764  SER SER B . n 
B 2 461 VAL 461 765  765  VAL VAL B . n 
B 2 462 SER 462 766  766  SER SER B . n 
B 2 463 SER 463 767  767  SER SER B . n 
B 2 464 SER 464 768  768  SER SER B . n 
B 2 465 LYS 465 769  769  LYS LYS B . n 
B 2 466 LEU 466 770  770  LEU LEU B . n 
B 2 467 PHE 467 771  771  PHE PHE B . n 
B 2 468 SER 468 772  772  SER SER B . n 
B 2 469 SER 469 773  773  SER SER B . n 
B 2 470 SER 470 774  ?    ?   ?   B . n 
B 2 471 THR 471 775  ?    ?   ?   B . n 
B 2 472 ALA 472 776  ?    ?   ?   B . n 
B 2 473 PRO 473 777  ?    ?   ?   B . n 
B 2 474 HIS 474 778  ?    ?   ?   B . n 
B 2 475 GLU 475 779  ?    ?   ?   B . n 
B 2 476 THR 476 780  780  THR THR B . n 
B 2 477 SER 477 781  781  SER SER B . n 
B 2 478 PHE 478 782  782  PHE PHE B . n 
B 2 479 GLY 479 783  783  GLY GLY B . n 
B 2 480 GLU 480 784  784  GLU GLU B . n 
B 2 481 GLU 481 785  785  GLU GLU B . n 
B 2 482 VAL 482 786  786  VAL VAL B . n 
B 2 483 GLU 483 787  787  GLU GLU B . n 
B 2 484 VAL 484 788  788  VAL VAL B . n 
B 2 485 HIS 485 789  789  HIS HIS B . n 
B 2 486 ASN 486 790  790  ASN ASN B . n 
B 2 487 LEU 487 791  791  LEU LEU B . n 
B 2 488 LEU 488 792  792  LEU LEU B . n 
B 2 489 ILE 489 793  793  ILE ILE B . n 
B 2 490 ILE 490 794  794  ILE ILE B . n 
B 2 491 ASP 491 795  795  ASP ASP B . n 
B 2 492 GLN 492 796  796  GLN GLN B . n 
B 2 493 HIS 493 797  797  HIS HIS B . n 
B 2 494 THR 494 798  798  THR THR B . n 
B 2 495 PHE 495 799  799  PHE PHE B . n 
B 2 496 GLU 496 800  800  GLU GLU B . n 
B 2 497 VAL 497 801  801  VAL VAL B . n 
B 2 498 LEU 498 802  802  LEU LEU B . n 
B 2 499 HIS 499 803  803  HIS HIS B . n 
B 2 500 ALA 500 804  804  ALA ALA B . n 
B 2 501 HIS 501 805  805  HIS HIS B . n 
B 2 502 GLN 502 806  806  GLN GLN B . n 
B 2 503 PHE 503 807  807  PHE PHE B . n 
B 2 504 LEU 504 808  808  LEU LEU B . n 
B 2 505 GLN 505 809  809  GLN GLN B . n 
B 2 506 ASN 506 810  810  ASN ASN B . n 
B 2 507 GLU 507 811  811  GLU GLU B . n 
B 2 508 TYR 508 812  812  TYR TYR B . n 
B 2 509 ALA 509 813  813  ALA ALA B . n 
B 2 510 LEU 510 814  814  LEU LEU B . n 
B 2 511 SER 511 815  815  SER SER B . n 
B 2 512 LEU 512 816  816  LEU LEU B . n 
B 2 513 VAL 513 817  817  VAL VAL B . n 
B 2 514 SER 514 818  818  SER SER B . n 
B 2 515 CYS 515 819  819  CYS CYS B . n 
B 2 516 LYS 516 820  820  LYS LYS B . n 
B 2 517 LEU 517 821  821  LEU LEU B . n 
B 2 518 GLY 518 822  822  GLY GLY B . n 
B 2 519 LYS 519 823  823  LYS LYS B . n 
B 2 520 ASP 520 824  824  ASP ASP B . n 
B 2 521 PRO 521 825  825  PRO PRO B . n 
B 2 522 ASN 522 826  826  ASN ASN B . n 
B 2 523 THR 523 827  827  THR THR B . n 
B 2 524 TYR 524 828  828  TYR TYR B . n 
B 2 525 PHE 525 829  829  PHE PHE B . n 
B 2 526 ILE 526 830  830  ILE ILE B . n 
B 2 527 VAL 527 831  831  VAL VAL B . n 
B 2 528 GLY 528 832  832  GLY GLY B . n 
B 2 529 THR 529 833  833  THR THR B . n 
B 2 530 ALA 530 834  834  ALA ALA B . n 
B 2 531 MET 531 835  835  MET MET B . n 
B 2 532 VAL 532 836  836  VAL VAL B . n 
B 2 533 TYR 533 837  837  TYR TYR B . n 
B 2 534 PRO 534 838  838  PRO PRO B . n 
B 2 535 GLU 535 839  839  GLU GLU B . n 
B 2 536 GLU 536 840  840  GLU GLU B . n 
B 2 537 ALA 537 841  841  ALA ALA B . n 
B 2 538 GLU 538 842  842  GLU GLU B . n 
B 2 539 PRO 539 843  843  PRO PRO B . n 
B 2 540 LYS 540 844  844  LYS LYS B . n 
B 2 541 GLN 541 845  845  GLN GLN B . n 
B 2 542 GLY 542 846  846  GLY GLY B . n 
B 2 543 ARG 543 847  847  ARG ARG B . n 
B 2 544 ILE 544 848  848  ILE ILE B . n 
B 2 545 VAL 545 849  849  VAL VAL B . n 
B 2 546 VAL 546 850  850  VAL VAL B . n 
B 2 547 PHE 547 851  851  PHE PHE B . n 
B 2 548 GLN 548 852  852  GLN GLN B . n 
B 2 549 TYR 549 853  853  TYR TYR B . n 
B 2 550 SER 550 854  854  SER SER B . n 
B 2 551 ASP 551 855  855  ASP ASP B . n 
B 2 552 GLY 552 856  856  GLY GLY B . n 
B 2 553 LYS 553 857  857  LYS LYS B . n 
B 2 554 LEU 554 858  858  LEU LEU B . n 
B 2 555 GLN 555 859  859  GLN GLN B . n 
B 2 556 THR 556 860  860  THR THR B . n 
B 2 557 VAL 557 861  861  VAL VAL B . n 
B 2 558 ALA 558 862  862  ALA ALA B . n 
B 2 559 GLU 559 863  863  GLU GLU B . n 
B 2 560 LYS 560 864  864  LYS LYS B . n 
B 2 561 GLU 561 865  865  GLU GLU B . n 
B 2 562 VAL 562 866  866  VAL VAL B . n 
B 2 563 LYS 563 867  867  LYS LYS B . n 
B 2 564 GLY 564 868  868  GLY GLY B . n 
B 2 565 ALA 565 869  869  ALA ALA B . n 
B 2 566 VAL 566 870  870  VAL VAL B . n 
B 2 567 TYR 567 871  871  TYR TYR B . n 
B 2 568 SER 568 872  872  SER SER B . n 
B 2 569 MET 569 873  873  MET MET B . n 
B 2 570 VAL 570 874  874  VAL VAL B . n 
B 2 571 GLU 571 875  875  GLU GLU B . n 
B 2 572 PHE 572 876  876  PHE PHE B . n 
B 2 573 ASN 573 877  877  ASN ASN B . n 
B 2 574 GLY 574 878  878  GLY GLY B . n 
B 2 575 LYS 575 879  879  LYS LYS B . n 
B 2 576 LEU 576 880  880  LEU LEU B . n 
B 2 577 LEU 577 881  881  LEU LEU B . n 
B 2 578 ALA 578 882  882  ALA ALA B . n 
B 2 579 SER 579 883  883  SER SER B . n 
B 2 580 ILE 580 884  884  ILE ILE B . n 
B 2 581 ASN 581 885  885  ASN ASN B . n 
B 2 582 SER 582 886  886  SER SER B . n 
B 2 583 THR 583 887  887  THR THR B . n 
B 2 584 VAL 584 888  888  VAL VAL B . n 
B 2 585 ARG 585 889  889  ARG ARG B . n 
B 2 586 LEU 586 890  890  LEU LEU B . n 
B 2 587 TYR 587 891  891  TYR TYR B . n 
B 2 588 GLU 588 892  892  GLU GLU B . n 
B 2 589 TRP 589 893  893  TRP TRP B . n 
B 2 590 THR 590 894  894  THR THR B . n 
B 2 591 THR 591 895  895  THR THR B . n 
B 2 592 GLU 592 896  896  GLU GLU B . n 
B 2 593 LYS 593 897  897  LYS LYS B . n 
B 2 594 GLU 594 898  898  GLU GLU B . n 
B 2 595 LEU 595 899  899  LEU LEU B . n 
B 2 596 ARG 596 900  900  ARG ARG B . n 
B 2 597 THR 597 901  901  THR THR B . n 
B 2 598 GLU 598 902  902  GLU GLU B . n 
B 2 599 CYS 599 903  903  CYS CYS B . n 
B 2 600 ASN 600 904  904  ASN ASN B . n 
B 2 601 HIS 601 905  905  HIS HIS B . n 
B 2 602 TYR 602 906  906  TYR TYR B . n 
B 2 603 ASN 603 907  907  ASN ASN B . n 
B 2 604 ASN 604 908  908  ASN ASN B . n 
B 2 605 ILE 605 909  909  ILE ILE B . n 
B 2 606 MET 606 910  910  MET MET B . n 
B 2 607 ALA 607 911  911  ALA ALA B . n 
B 2 608 LEU 608 912  912  LEU LEU B . n 
B 2 609 TYR 609 913  913  TYR TYR B . n 
B 2 610 LEU 610 914  914  LEU LEU B . n 
B 2 611 LYS 611 915  915  LYS LYS B . n 
B 2 612 THR 612 916  916  THR THR B . n 
B 2 613 LYS 613 917  917  LYS LYS B . n 
B 2 614 GLY 614 918  918  GLY GLY B . n 
B 2 615 ASP 615 919  919  ASP ASP B . n 
B 2 616 PHE 616 920  920  PHE PHE B . n 
B 2 617 ILE 617 921  921  ILE ILE B . n 
B 2 618 LEU 618 922  922  LEU LEU B . n 
B 2 619 VAL 619 923  923  VAL VAL B . n 
B 2 620 GLY 620 924  924  GLY GLY B . n 
B 2 621 ASP 621 925  925  ASP ASP B . n 
B 2 622 LEU 622 926  926  LEU LEU B . n 
B 2 623 MET 623 927  927  MET MET B . n 
B 2 624 ARG 624 928  928  ARG ARG B . n 
B 2 625 SER 625 929  929  SER SER B . n 
B 2 626 VAL 626 930  930  VAL VAL B . n 
B 2 627 LEU 627 931  931  LEU LEU B . n 
B 2 628 LEU 628 932  932  LEU LEU B . n 
B 2 629 LEU 629 933  933  LEU LEU B . n 
B 2 630 ALA 630 934  934  ALA ALA B . n 
B 2 631 TYR 631 935  935  TYR TYR B . n 
B 2 632 LYS 632 936  936  LYS LYS B . n 
B 2 633 PRO 633 937  937  PRO PRO B . n 
B 2 634 MET 634 938  938  MET MET B . n 
B 2 635 GLU 635 939  939  GLU GLU B . n 
B 2 636 GLY 636 940  940  GLY GLY B . n 
B 2 637 ASN 637 941  941  ASN ASN B . n 
B 2 638 PHE 638 942  942  PHE PHE B . n 
B 2 639 GLU 639 943  943  GLU GLU B . n 
B 2 640 GLU 640 944  944  GLU GLU B . n 
B 2 641 ILE 641 945  945  ILE ILE B . n 
B 2 642 ALA 642 946  946  ALA ALA B . n 
B 2 643 ARG 643 947  947  ARG ARG B . n 
B 2 644 ASP 644 948  948  ASP ASP B . n 
B 2 645 PHE 645 949  949  PHE PHE B . n 
B 2 646 ASN 646 950  950  ASN ASN B . n 
B 2 647 PRO 647 951  951  PRO PRO B . n 
B 2 648 ASN 648 952  952  ASN ASN B . n 
B 2 649 TRP 649 953  953  TRP TRP B . n 
B 2 650 MET 650 954  954  MET MET B . n 
B 2 651 SER 651 955  955  SER SER B . n 
B 2 652 ALA 652 956  956  ALA ALA B . n 
B 2 653 VAL 653 957  957  VAL VAL B . n 
B 2 654 GLU 654 958  958  GLU GLU B . n 
B 2 655 ILE 655 959  959  ILE ILE B . n 
B 2 656 LEU 656 960  960  LEU LEU B . n 
B 2 657 ASP 657 961  961  ASP ASP B . n 
B 2 658 ASP 658 962  962  ASP ASP B . n 
B 2 659 ASP 659 963  963  ASP ASP B . n 
B 2 660 ASN 660 964  964  ASN ASN B . n 
B 2 661 PHE 661 965  965  PHE PHE B . n 
B 2 662 LEU 662 966  966  LEU LEU B . n 
B 2 663 GLY 663 967  967  GLY GLY B . n 
B 2 664 ALA 664 968  968  ALA ALA B . n 
B 2 665 GLU 665 969  969  GLU GLU B . n 
B 2 666 ASN 666 970  970  ASN ASN B . n 
B 2 667 ALA 667 971  971  ALA ALA B . n 
B 2 668 PHE 668 972  972  PHE PHE B . n 
B 2 669 ASN 669 973  973  ASN ASN B . n 
B 2 670 LEU 670 974  974  LEU LEU B . n 
B 2 671 PHE 671 975  975  PHE PHE B . n 
B 2 672 VAL 672 976  976  VAL VAL B . n 
B 2 673 CYS 673 977  977  CYS CYS B . n 
B 2 674 GLN 674 978  978  GLN GLN B . n 
B 2 675 LYS 675 979  979  LYS LYS B . n 
B 2 676 ASP 676 980  980  ASP ASP B . n 
B 2 677 SER 677 981  ?    ?   ?   B . n 
B 2 678 ALA 678 982  ?    ?   ?   B . n 
B 2 679 ALA 679 983  ?    ?   ?   B . n 
B 2 680 THR 680 984  ?    ?   ?   B . n 
B 2 681 THR 681 985  985  THR THR B . n 
B 2 682 ASP 682 986  986  ASP ASP B . n 
B 2 683 GLU 683 987  987  GLU GLU B . n 
B 2 684 GLU 684 988  988  GLU GLU B . n 
B 2 685 ARG 685 989  989  ARG ARG B . n 
B 2 686 GLN 686 990  990  GLN GLN B . n 
B 2 687 HIS 687 991  991  HIS HIS B . n 
B 2 688 LEU 688 992  992  LEU LEU B . n 
B 2 689 GLN 689 993  993  GLN GLN B . n 
B 2 690 GLU 690 994  994  GLU GLU B . n 
B 2 691 VAL 691 995  995  VAL VAL B . n 
B 2 692 GLY 692 996  996  GLY GLY B . n 
B 2 693 LEU 693 997  997  LEU LEU B . n 
B 2 694 PHE 694 998  998  PHE PHE B . n 
B 2 695 HIS 695 999  999  HIS HIS B . n 
B 2 696 LEU 696 1000 1000 LEU LEU B . n 
B 2 697 GLY 697 1001 1001 GLY GLY B . n 
B 2 698 GLU 698 1002 1002 GLU GLU B . n 
B 2 699 PHE 699 1003 1003 PHE PHE B . n 
B 2 700 VAL 700 1004 1004 VAL VAL B . n 
B 2 701 ASN 701 1005 1005 ASN ASN B . n 
B 2 702 VAL 702 1006 1006 VAL VAL B . n 
B 2 703 PHE 703 1007 1007 PHE PHE B . n 
B 2 704 CYS 704 1008 1008 CYS CYS B . n 
B 2 705 HIS 705 1009 1009 HIS HIS B . n 
B 2 706 GLY 706 1010 1010 GLY GLY B . n 
B 2 707 SER 707 1011 1011 SER SER B . n 
B 2 708 LEU 708 1012 1012 LEU LEU B . n 
B 2 709 VAL 709 1013 1013 VAL VAL B . n 
B 2 710 MET 710 1014 1014 MET MET B . n 
B 2 711 GLN 711 1015 ?    ?   ?   B . n 
B 2 712 ASN 712 1016 ?    ?   ?   B . n 
B 2 713 LEU 713 1017 ?    ?   ?   B . n 
B 2 714 GLY 714 1018 ?    ?   ?   B . n 
B 2 715 GLU 715 1019 ?    ?   ?   B . n 
B 2 716 THR 716 1020 ?    ?   ?   B . n 
B 2 717 SER 717 1021 ?    ?   ?   B . n 
B 2 718 THR 718 1022 ?    ?   ?   B . n 
B 2 719 PRO 719 1023 1023 PRO PRO B . n 
B 2 720 THR 720 1024 1024 THR THR B . n 
B 2 721 GLN 721 1025 1025 GLN GLN B . n 
B 2 722 GLY 722 1026 1026 GLY GLY B . n 
B 2 723 SER 723 1027 1027 SER SER B . n 
B 2 724 VAL 724 1028 1028 VAL VAL B . n 
B 2 725 LEU 725 1029 1029 LEU LEU B . n 
B 2 726 PHE 726 1030 1030 PHE PHE B . n 
B 2 727 GLY 727 1031 1031 GLY GLY B . n 
B 2 728 THR 728 1032 1032 THR THR B . n 
B 2 729 VAL 729 1033 1033 VAL VAL B . n 
B 2 730 ASN 730 1034 1034 ASN ASN B . n 
B 2 731 GLY 731 1035 1035 GLY GLY B . n 
B 2 732 MET 732 1036 1036 MET MET B . n 
B 2 733 ILE 733 1037 1037 ILE ILE B . n 
B 2 734 GLY 734 1038 1038 GLY GLY B . n 
B 2 735 LEU 735 1039 1039 LEU LEU B . n 
B 2 736 VAL 736 1040 1040 VAL VAL B . n 
B 2 737 THR 737 1041 1041 THR THR B . n 
B 2 738 SER 738 1042 1042 SER SER B . n 
B 2 739 LEU 739 1043 1043 LEU LEU B . n 
B 2 740 SER 740 1044 1044 SER SER B . n 
B 2 741 GLU 741 1045 1045 GLU GLU B . n 
B 2 742 SER 742 1046 1046 SER SER B . n 
B 2 743 TRP 743 1047 1047 TRP TRP B . n 
B 2 744 TYR 744 1048 1048 TYR TYR B . n 
B 2 745 ASN 745 1049 1049 ASN ASN B . n 
B 2 746 LEU 746 1050 1050 LEU LEU B . n 
B 2 747 LEU 747 1051 1051 LEU LEU B . n 
B 2 748 LEU 748 1052 1052 LEU LEU B . n 
B 2 749 ASP 749 1053 1053 ASP ASP B . n 
B 2 750 MET 750 1054 1054 MET MET B . n 
B 2 751 GLN 751 1055 1055 GLN GLN B . n 
B 2 752 ASN 752 1056 1056 ASN ASN B . n 
B 2 753 ARG 753 1057 1057 ARG ARG B . n 
B 2 754 LEU 754 1058 1058 LEU LEU B . n 
B 2 755 ASN 755 1059 1059 ASN ASN B . n 
B 2 756 LYS 756 1060 1060 LYS LYS B . n 
B 2 757 VAL 757 1061 1061 VAL VAL B . n 
B 2 758 ILE 758 1062 1062 ILE ILE B . n 
B 2 759 LYS 759 1063 1063 LYS LYS B . n 
B 2 760 SER 760 1064 1064 SER SER B . n 
B 2 761 VAL 761 1065 1065 VAL VAL B . n 
B 2 762 GLY 762 1066 1066 GLY GLY B . n 
B 2 763 LYS 763 1067 1067 LYS LYS B . n 
B 2 764 ILE 764 1068 1068 ILE ILE B . n 
B 2 765 GLU 765 1069 1069 GLU GLU B . n 
B 2 766 HIS 766 1070 1070 HIS HIS B . n 
B 2 767 SER 767 1071 1071 SER SER B . n 
B 2 768 PHE 768 1072 1072 PHE PHE B . n 
B 2 769 TRP 769 1073 1073 TRP TRP B . n 
B 2 770 ARG 770 1074 1074 ARG ARG B . n 
B 2 771 SER 771 1075 1075 SER SER B . n 
B 2 772 PHE 772 1076 1076 PHE PHE B . n 
B 2 773 HIS 773 1077 1077 HIS HIS B . n 
B 2 774 THR 774 1078 1078 THR THR B . n 
B 2 775 GLU 775 1079 1079 GLU GLU B . n 
B 2 776 ARG 776 1080 1080 ARG ARG B . n 
B 2 777 LYS 777 1081 1081 LYS LYS B . n 
B 2 778 THR 778 1082 1082 THR THR B . n 
B 2 779 GLU 779 1083 1083 GLU GLU B . n 
B 2 780 PRO 780 1084 1084 PRO PRO B . n 
B 2 781 ALA 781 1085 1085 ALA ALA B . n 
B 2 782 THR 782 1086 1086 THR THR B . n 
B 2 783 GLY 783 1087 1087 GLY GLY B . n 
B 2 784 PHE 784 1088 1088 PHE PHE B . n 
B 2 785 ILE 785 1089 1089 ILE ILE B . n 
B 2 786 ASP 786 1090 1090 ASP ASP B . n 
B 2 787 GLY 787 1091 1091 GLY GLY B . n 
B 2 788 ASP 788 1092 1092 ASP ASP B . n 
B 2 789 LEU 789 1093 1093 LEU LEU B . n 
B 2 790 ILE 790 1094 1094 ILE ILE B . n 
B 2 791 GLU 791 1095 1095 GLU GLU B . n 
B 2 792 SER 792 1096 1096 SER SER B . n 
B 2 793 PHE 793 1097 1097 PHE PHE B . n 
B 2 794 LEU 794 1098 1098 LEU LEU B . n 
B 2 795 ASP 795 1099 1099 ASP ASP B . n 
B 2 796 ILE 796 1100 1100 ILE ILE B . n 
B 2 797 SER 797 1101 1101 SER SER B . n 
B 2 798 ARG 798 1102 1102 ARG ARG B . n 
B 2 799 PRO 799 1103 1103 PRO PRO B . n 
B 2 800 LYS 800 1104 1104 LYS LYS B . n 
B 2 801 MET 801 1105 1105 MET MET B . n 
B 2 802 GLN 802 1106 1106 GLN GLN B . n 
B 2 803 GLU 803 1107 1107 GLU GLU B . n 
B 2 804 VAL 804 1108 1108 VAL VAL B . n 
B 2 805 VAL 805 1109 1109 VAL VAL B . n 
B 2 806 ALA 806 1110 1110 ALA ALA B . n 
B 2 807 ASN 807 1111 1111 ASN ASN B . n 
B 2 808 LEU 808 1112 1112 LEU LEU B . n 
B 2 809 GLN 809 1113 ?    ?   ?   B . n 
B 2 810 TYR 810 1114 ?    ?   ?   B . n 
B 2 811 ASP 811 1115 ?    ?   ?   B . n 
B 2 812 ASP 812 1116 ?    ?   ?   B . n 
B 2 813 GLY 813 1117 ?    ?   ?   B . n 
B 2 814 SER 814 1118 ?    ?   ?   B . n 
B 2 815 GLY 815 1119 ?    ?   ?   B . n 
B 2 816 MET 816 1120 ?    ?   ?   B . n 
B 2 817 LYS 817 1121 ?    ?   ?   B . n 
B 2 818 ARG 818 1122 ?    ?   ?   B . n 
B 2 819 GLU 819 1123 1123 GLU GLU B . n 
B 2 820 ALA 820 1124 1124 ALA ALA B . n 
B 2 821 THR 821 1125 1125 THR THR B . n 
B 2 822 ALA 822 1126 1126 ALA ALA B . n 
B 2 823 ASP 823 1127 1127 ASP ASP B . n 
B 2 824 ASP 824 1128 1128 ASP ASP B . n 
B 2 825 LEU 825 1129 1129 LEU LEU B . n 
B 2 826 ILE 826 1130 1130 ILE ILE B . n 
B 2 827 LYS 827 1131 1131 LYS LYS B . n 
B 2 828 VAL 828 1132 1132 VAL VAL B . n 
B 2 829 VAL 829 1133 1133 VAL VAL B . n 
B 2 830 GLU 830 1134 1134 GLU GLU B . n 
B 2 831 GLU 831 1135 1135 GLU GLU B . n 
B 2 832 LEU 832 1136 1136 LEU LEU B . n 
B 2 833 THR 833 1137 1137 THR THR B . n 
B 2 834 ARG 834 1138 1138 ARG ARG B . n 
B 2 835 ILE 835 1139 1139 ILE ILE B . n 
B 2 836 HIS 836 1140 1140 HIS HIS B . n 
C 3 1   SER 1   866  ?    ?   ?   C . n 
C 3 2   GLN 2   867  ?    ?   ?   C . n 
C 3 3   SER 3   868  868  SER SER C . n 
C 3 4   LEU 4   869  869  LEU LEU C . n 
C 3 5   THR 5   870  870  THR THR C . n 
C 3 6   THR 6   871  871  THR THR C . n 
C 3 7   CYS 7   872  872  CYS CYS C . n 
C 3 8   GLU 8   873  873  GLU GLU C . n 
C 3 9   VAL 9   874  874  VAL VAL C . n 
C 3 10  CYS 10  875  875  CYS CYS C . n 
C 3 11  GLY 11  876  876  GLY GLY C . n 
C 3 12  ALA 12  877  877  ALA ALA C . n 
C 3 13  CYS 13  878  878  CYS CYS C . n 
C 3 14  PHE 14  879  879  PHE PHE C . n 
C 3 15  GLU 15  880  880  GLU GLU C . n 
C 3 16  THR 16  881  881  THR THR C . n 
C 3 17  ARG 17  882  882  ARG ARG C . n 
C 3 18  LYS 18  883  883  LYS LYS C . n 
C 3 19  GLY 19  884  884  GLY GLY C . n 
C 3 20  LEU 20  885  885  LEU LEU C . n 
C 3 21  SER 21  886  886  SER SER C . n 
C 3 22  SER 22  887  887  SER SER C . n 
C 3 23  HIS 23  888  888  HIS HIS C . n 
C 3 24  ALA 24  889  889  ALA ALA C . n 
C 3 25  ARG 25  890  890  ARG ARG C . n 
C 3 26  SER 26  891  891  SER SER C . n 
C 3 27  HIS 27  892  892  HIS HIS C . n 
C 3 28  LEU 28  893  893  LEU LEU C . n 
C 3 29  ARG 29  894  ?    ?   ?   C . n 
C 3 30  GLN 30  895  ?    ?   ?   C . n 
D 1 1   ARG 1   70   ?    ?   ?   D . n 
D 1 2   THR 2   71   ?    ?   ?   D . n 
D 1 3   LEU 3   72   ?    ?   ?   D . n 
D 1 4   HIS 4   73   ?    ?   ?   D . n 
D 1 5   ASP 5   74   ?    ?   ?   D . n 
D 1 6   ASP 6   75   75   ASP ASP D . n 
D 1 7   ASP 7   76   76   ASP ASP D . n 
D 1 8   SER 8   77   77   SER SER D . n 
D 1 9   CYS 9   78   78   CYS CYS D . n 
D 1 10  GLN 10  79   79   GLN GLN D . n 
D 1 11  VAL 11  80   80   VAL VAL D . n 
D 1 12  ILE 12  81   81   ILE ILE D . n 
D 1 13  PRO 13  82   82   PRO PRO D . n 
D 1 14  VAL 14  83   83   VAL VAL D . n 
D 1 15  LEU 15  84   84   LEU LEU D . n 
D 1 16  PRO 16  85   85   PRO PRO D . n 
D 1 17  GLN 17  86   86   GLN GLN D . n 
D 1 18  VAL 18  87   87   VAL VAL D . n 
D 1 19  MET 19  88   88   MET MET D . n 
D 1 20  MET 20  89   89   MET MET D . n 
D 1 21  ILE 21  90   90   ILE ILE D . n 
D 1 22  LEU 22  91   91   LEU LEU D . n 
D 1 23  ILE 23  92   92   ILE ILE D . n 
D 1 24  PRO 24  93   93   PRO PRO D . n 
D 1 25  GLY 25  94   94   GLY GLY D . n 
D 1 26  GLN 26  95   95   GLN GLN D . n 
D 1 27  THR 27  96   96   THR THR D . n 
D 1 28  LEU 28  97   97   LEU LEU D . n 
D 1 29  PRO 29  98   98   PRO PRO D . n 
D 1 30  LEU 30  99   99   LEU LEU D . n 
D 1 31  GLN 31  100  100  GLN GLN D . n 
D 1 32  LEU 32  101  101  LEU LEU D . n 
D 1 33  PHE 33  102  102  PHE PHE D . n 
D 1 34  HIS 34  103  103  HIS HIS D . n 
D 1 35  PRO 35  104  104  PRO PRO D . n 
D 1 36  GLN 36  105  105  GLN GLN D . n 
D 1 37  GLU 37  106  106  GLU GLU D . n 
D 1 38  VAL 38  107  107  VAL VAL D . n 
D 1 39  SER 39  108  108  SER SER D . n 
D 1 40  MET 40  109  109  MET MET D . n 
D 1 41  VAL 41  110  110  VAL VAL D . n 
D 1 42  ARG 42  111  111  ARG ARG D . n 
D 1 43  ASN 43  112  112  ASN ASN D . n 
D 1 44  LEU 44  113  113  LEU LEU D . n 
D 1 45  ILE 45  114  114  ILE ILE D . n 
D 1 46  GLN 46  115  115  GLN GLN D . n 
D 1 47  LYS 47  116  116  LYS LYS D . n 
D 1 48  ASP 48  117  117  ASP ASP D . n 
D 1 49  ARG 49  118  118  ARG ARG D . n 
D 1 50  THR 50  119  119  THR THR D . n 
D 1 51  PHE 51  120  120  PHE PHE D . n 
D 1 52  ALA 52  121  121  ALA ALA D . n 
D 1 53  VAL 53  122  122  VAL VAL D . n 
D 1 54  LEU 54  123  123  LEU LEU D . n 
D 1 55  ALA 55  124  124  ALA ALA D . n 
D 1 56  TYR 56  125  125  TYR TYR D . n 
D 1 57  SER 57  126  ?    ?   ?   D . n 
D 1 58  ASN 58  127  ?    ?   ?   D . n 
D 1 59  VAL 59  128  ?    ?   ?   D . n 
D 1 60  GLN 60  129  ?    ?   ?   D . n 
D 1 61  GLU 61  130  ?    ?   ?   D . n 
D 1 62  ARG 62  131  ?    ?   ?   D . n 
D 1 63  GLU 63  132  ?    ?   ?   D . n 
D 1 64  ALA 64  133  133  ALA ALA D . n 
D 1 65  GLN 65  134  134  GLN GLN D . n 
D 1 66  PHE 66  135  135  PHE PHE D . n 
D 1 67  GLY 67  136  136  GLY GLY D . n 
D 1 68  THR 68  137  137  THR THR D . n 
D 1 69  THR 69  138  138  THR THR D . n 
D 1 70  ALA 70  139  139  ALA ALA D . n 
D 1 71  GLU 71  140  140  GLU GLU D . n 
D 1 72  ILE 72  141  141  ILE ILE D . n 
D 1 73  TYR 73  142  142  TYR TYR D . n 
D 1 74  ALA 74  143  143  ALA ALA D . n 
D 1 75  TYR 75  144  144  TYR TYR D . n 
D 1 76  ARG 76  145  145  ARG ARG D . n 
D 1 77  GLU 77  146  146  GLU GLU D . n 
D 1 78  GLU 78  147  147  GLU GLU D . n 
D 1 79  GLN 79  148  ?    ?   ?   D . n 
D 1 80  ASP 80  149  ?    ?   ?   D . n 
D 1 81  PHE 81  150  ?    ?   ?   D . n 
D 1 82  GLY 82  151  151  GLY GLY D . n 
D 1 83  ILE 83  152  152  ILE ILE D . n 
D 1 84  GLU 84  153  153  GLU GLU D . n 
D 1 85  ILE 85  154  154  ILE ILE D . n 
D 1 86  VAL 86  155  155  VAL VAL D . n 
D 1 87  LYS 87  156  156  LYS LYS D . n 
D 1 88  VAL 88  157  157  VAL VAL D . n 
D 1 89  LYS 89  158  158  LYS LYS D . n 
D 1 90  ALA 90  159  159  ALA ALA D . n 
D 1 91  ILE 91  160  160  ILE ILE D . n 
D 1 92  GLY 92  161  161  GLY GLY D . n 
D 1 93  ARG 93  162  162  ARG ARG D . n 
D 1 94  GLN 94  163  163  GLN GLN D . n 
D 1 95  ARG 95  164  164  ARG ARG D . n 
D 1 96  PHE 96  165  165  PHE PHE D . n 
D 1 97  LYS 97  166  166  LYS LYS D . n 
D 1 98  VAL 98  167  167  VAL VAL D . n 
D 1 99  LEU 99  168  168  LEU LEU D . n 
D 1 100 GLU 100 169  169  GLU GLU D . n 
D 1 101 LEU 101 170  170  LEU LEU D . n 
D 1 102 ARG 102 171  171  ARG ARG D . n 
D 1 103 THR 103 172  172  THR THR D . n 
D 1 104 GLN 104 173  ?    ?   ?   D . n 
D 1 105 SER 105 174  ?    ?   ?   D . n 
D 1 106 ASP 106 175  ?    ?   ?   D . n 
D 1 107 GLY 107 176  ?    ?   ?   D . n 
D 1 108 ILE 108 177  177  ILE ILE D . n 
D 1 109 GLN 109 178  178  GLN GLN D . n 
D 1 110 GLN 110 179  179  GLN GLN D . n 
D 1 111 ALA 111 180  180  ALA ALA D . n 
D 1 112 LYS 112 181  181  LYS LYS D . n 
D 1 113 VAL 113 182  182  VAL VAL D . n 
D 1 114 GLN 114 183  183  GLN GLN D . n 
D 1 115 ILE 115 184  184  ILE ILE D . n 
D 1 116 LEU 116 185  185  LEU LEU D . n 
D 1 117 PRO 117 186  186  PRO PRO D . n 
D 1 118 GLU 118 187  187  GLU GLU D . n 
D 1 119 CYS 119 188  188  CYS CYS D . n 
D 1 120 VAL 120 189  189  VAL VAL D . n 
D 1 121 LEU 121 190  190  LEU LEU D . n 
D 1 122 PRO 122 191  191  PRO PRO D . n 
D 1 123 SER 123 192  192  SER SER D . n 
D 1 124 THR 124 193  193  THR THR D . n 
D 1 125 MET 125 194  194  MET MET D . n 
D 1 126 SER 126 195  195  SER SER D . n 
D 1 127 ALA 127 196  196  ALA ALA D . n 
D 1 128 VAL 128 197  197  VAL VAL D . n 
D 1 129 GLN 129 198  198  GLN GLN D . n 
D 1 130 LEU 130 199  199  LEU LEU D . n 
D 1 131 GLU 131 200  200  GLU GLU D . n 
D 1 132 SER 132 201  201  SER SER D . n 
D 1 133 LEU 133 202  202  LEU LEU D . n 
D 1 134 ASN 134 203  203  ASN ASN D . n 
D 1 135 LYS 135 204  204  LYS LYS D . n 
D 1 136 CYS 136 205  205  CYS CYS D . n 
D 1 137 GLN 137 206  206  GLN GLN D . n 
D 1 138 ILE 138 207  207  ILE ILE D . n 
D 1 139 PHE 139 208  208  PHE PHE D . n 
D 1 140 PRO 140 209  209  PRO PRO D . n 
D 1 141 SER 141 210  210  SER SER D . n 
D 1 142 LYS 142 211  211  LYS LYS D . n 
D 1 143 PRO 143 212  212  PRO PRO D . n 
D 1 144 VAL 144 213  213  VAL VAL D . n 
D 1 145 SER 145 214  ?    ?   ?   D . n 
D 1 146 ARG 146 215  ?    ?   ?   D . n 
D 1 147 GLU 147 216  ?    ?   ?   D . n 
D 1 148 ASP 148 217  ?    ?   ?   D . n 
D 1 149 GLN 149 218  ?    ?   ?   D . n 
D 1 150 CYS 150 219  ?    ?   ?   D . n 
D 1 151 SER 151 220  220  SER SER D . n 
D 1 152 TYR 152 221  221  TYR TYR D . n 
D 1 153 LYS 153 222  222  LYS LYS D . n 
D 1 154 TRP 154 223  223  TRP TRP D . n 
D 1 155 TRP 155 224  224  TRP TRP D . n 
D 1 156 GLN 156 225  225  GLN GLN D . n 
D 1 157 LYS 157 226  226  LYS LYS D . n 
D 1 158 TYR 158 227  227  TYR TYR D . n 
D 1 159 GLN 159 228  228  GLN GLN D . n 
D 1 160 LYS 160 229  229  LYS LYS D . n 
D 1 161 ARG 161 230  230  ARG ARG D . n 
D 1 162 LYS 162 231  231  LYS LYS D . n 
D 1 163 PHE 163 232  232  PHE PHE D . n 
D 1 164 HIS 164 233  233  HIS HIS D . n 
D 1 165 CYS 165 234  234  CYS CYS D . n 
D 1 166 ALA 166 235  235  ALA ALA D . n 
D 1 167 ASN 167 236  236  ASN ASN D . n 
D 1 168 LEU 168 237  237  LEU LEU D . n 
D 1 169 THR 169 238  238  THR THR D . n 
D 1 170 SER 170 239  239  SER SER D . n 
D 1 171 TRP 171 240  240  TRP TRP D . n 
D 1 172 PRO 172 241  241  PRO PRO D . n 
D 1 173 ARG 173 242  242  ARG ARG D . n 
D 1 174 TRP 174 243  243  TRP TRP D . n 
D 1 175 LEU 175 244  244  LEU LEU D . n 
D 1 176 TYR 176 245  245  TYR TYR D . n 
D 1 177 SER 177 246  246  SER SER D . n 
D 1 178 LEU 178 247  247  LEU LEU D . n 
D 1 179 TYR 179 248  248  TYR TYR D . n 
D 1 180 ASP 180 249  249  ASP ASP D . n 
D 1 181 ALA 181 250  250  ALA ALA D . n 
D 1 182 GLU 182 251  251  GLU GLU D . n 
D 1 183 THR 183 252  252  THR THR D . n 
D 1 184 LEU 184 253  253  LEU LEU D . n 
D 1 185 MET 185 254  254  MET MET D . n 
D 1 186 ASP 186 255  255  ASP ASP D . n 
D 1 187 ARG 187 256  256  ARG ARG D . n 
D 1 188 ILE 188 257  257  ILE ILE D . n 
D 1 189 LYS 189 258  258  LYS LYS D . n 
D 1 190 LYS 190 259  259  LYS LYS D . n 
D 1 191 GLN 191 260  260  GLN GLN D . n 
D 1 192 LEU 192 261  261  LEU LEU D . n 
D 1 193 ARG 193 262  262  ARG ARG D . n 
D 1 194 GLU 194 263  263  GLU GLU D . n 
D 1 195 TRP 195 264  264  TRP TRP D . n 
D 1 196 ASP 196 265  265  ASP ASP D . n 
D 1 197 GLU 197 266  266  GLU GLU D . n 
D 1 198 ASN 198 267  267  ASN ASN D . n 
D 1 199 LEU 199 268  268  LEU LEU D . n 
D 1 200 LYS 200 269  269  LYS LYS D . n 
D 1 201 ASP 201 270  270  ASP ASP D . n 
D 1 202 ASP 202 271  271  ASP ASP D . n 
D 1 203 SER 203 272  272  SER SER D . n 
D 1 204 LEU 204 273  273  LEU LEU D . n 
D 1 205 PRO 205 274  274  PRO PRO D . n 
D 1 206 SER 206 275  275  SER SER D . n 
D 1 207 ASN 207 276  276  ASN ASN D . n 
D 1 208 PRO 208 277  277  PRO PRO D . n 
D 1 209 ILE 209 278  278  ILE ILE D . n 
D 1 210 ASP 210 279  279  ASP ASP D . n 
D 1 211 PHE 211 280  280  PHE PHE D . n 
D 1 212 SER 212 281  281  SER SER D . n 
D 1 213 TYR 213 282  282  TYR TYR D . n 
D 1 214 ARG 214 283  283  ARG ARG D . n 
D 1 215 VAL 215 284  284  VAL VAL D . n 
D 1 216 ALA 216 285  285  ALA ALA D . n 
D 1 217 ALA 217 286  286  ALA ALA D . n 
D 1 218 CYS 218 287  287  CYS CYS D . n 
D 1 219 LEU 219 288  288  LEU LEU D . n 
D 1 220 PRO 220 289  289  PRO PRO D . n 
D 1 221 ILE 221 290  290  ILE ILE D . n 
D 1 222 ASP 222 291  291  ASP ASP D . n 
D 1 223 ASP 223 292  292  ASP ASP D . n 
D 1 224 VAL 224 293  293  VAL VAL D . n 
D 1 225 LEU 225 294  294  LEU LEU D . n 
D 1 226 ARG 226 295  295  ARG ARG D . n 
D 1 227 ILE 227 296  296  ILE ILE D . n 
D 1 228 GLN 228 297  297  GLN GLN D . n 
D 1 229 LEU 229 298  298  LEU LEU D . n 
D 1 230 LEU 230 299  299  LEU LEU D . n 
D 1 231 LYS 231 300  300  LYS LYS D . n 
D 1 232 ILE 232 301  301  ILE ILE D . n 
D 1 233 GLY 233 302  302  GLY GLY D . n 
D 1 234 SER 234 303  303  SER SER D . n 
D 1 235 ALA 235 304  304  ALA ALA D . n 
D 1 236 ILE 236 305  305  ILE ILE D . n 
D 1 237 GLN 237 306  306  GLN GLN D . n 
D 1 238 ARG 238 307  307  ARG ARG D . n 
D 1 239 LEU 239 308  308  LEU LEU D . n 
D 1 240 ARG 240 309  309  ARG ARG D . n 
D 1 241 CYS 241 310  310  CYS CYS D . n 
D 1 242 GLU 242 311  311  GLU GLU D . n 
D 1 243 LEU 243 312  312  LEU LEU D . n 
D 1 244 ASP 244 313  313  ASP ASP D . n 
D 1 245 ILE 245 314  314  ILE ILE D . n 
D 1 246 MET 246 315  315  MET MET D . n 
D 1 247 ASN 247 316  316  ASN ASN D . n 
D 1 248 LYS 248 317  317  LYS LYS D . n 
D 1 249 CYS 249 318  318  CYS CYS D . n 
D 1 250 THR 250 319  319  THR THR D . n 
D 1 251 SER 251 320  320  SER SER D . n 
D 1 252 LEU 252 321  321  LEU LEU D . n 
D 1 253 CYS 253 322  322  CYS CYS D . n 
D 1 254 CYS 254 323  323  CYS CYS D . n 
D 1 255 LYS 255 324  324  LYS LYS D . n 
D 1 256 GLN 256 325  325  GLN GLN D . n 
D 1 257 CYS 257 326  326  CYS CYS D . n 
D 1 258 GLN 258 327  327  GLN GLN D . n 
D 1 259 GLU 259 328  328  GLU GLU D . n 
D 1 260 THR 260 329  329  THR THR D . n 
D 1 261 GLU 261 330  330  GLU GLU D . n 
D 1 262 ILE 262 331  331  ILE ILE D . n 
D 1 263 THR 263 332  332  THR THR D . n 
D 1 264 THR 264 333  333  THR THR D . n 
D 1 265 LYS 265 334  334  LYS LYS D . n 
D 1 266 ASN 266 335  335  ASN ASN D . n 
D 1 267 GLU 267 336  336  GLU GLU D . n 
D 1 268 ILE 268 337  337  ILE ILE D . n 
D 1 269 PHE 269 338  338  PHE PHE D . n 
D 1 270 SER 270 339  339  SER SER D . n 
D 1 271 LEU 271 340  340  LEU LEU D . n 
D 1 272 SER 272 341  341  SER SER D . n 
D 1 273 LEU 273 342  342  LEU LEU D . n 
D 1 274 CYS 274 343  343  CYS CYS D . n 
D 1 275 GLY 275 344  344  GLY GLY D . n 
D 1 276 PRO 276 345  345  PRO PRO D . n 
D 1 277 MET 277 346  346  MET MET D . n 
D 1 278 ALA 278 347  347  ALA ALA D . n 
D 1 279 ALA 279 348  348  ALA ALA D . n 
D 1 280 TYR 280 349  349  TYR TYR D . n 
D 1 281 VAL 281 350  350  VAL VAL D . n 
D 1 282 ASN 282 351  351  ASN ASN D . n 
D 1 283 PRO 283 352  352  PRO PRO D . n 
D 1 284 HIS 284 353  353  HIS HIS D . n 
D 1 285 GLY 285 354  354  GLY GLY D . n 
D 1 286 TYR 286 355  355  TYR TYR D . n 
D 1 287 VAL 287 356  356  VAL VAL D . n 
D 1 288 HIS 288 357  357  HIS HIS D . n 
D 1 289 GLU 289 358  358  GLU GLU D . n 
D 1 290 THR 290 359  359  THR THR D . n 
D 1 291 LEU 291 360  360  LEU LEU D . n 
D 1 292 THR 292 361  361  THR THR D . n 
D 1 293 VAL 293 362  362  VAL VAL D . n 
D 1 294 TYR 294 363  363  TYR TYR D . n 
D 1 295 LYS 295 364  364  LYS LYS D . n 
D 1 296 ALA 296 365  365  ALA ALA D . n 
D 1 297 CYS 297 366  366  CYS CYS D . n 
D 1 298 ASN 298 367  367  ASN ASN D . n 
D 1 299 LEU 299 368  368  LEU LEU D . n 
D 1 300 ASN 300 369  369  ASN ASN D . n 
D 1 301 LEU 301 370  370  LEU LEU D . n 
D 1 302 ILE 302 371  371  ILE ILE D . n 
D 1 303 GLY 303 372  372  GLY GLY D . n 
D 1 304 ARG 304 373  373  ARG ARG D . n 
D 1 305 PRO 305 374  374  PRO PRO D . n 
D 1 306 SER 306 375  375  SER SER D . n 
D 1 307 THR 307 376  376  THR THR D . n 
D 1 308 GLU 308 377  377  GLU GLU D . n 
D 1 309 HIS 309 378  378  HIS HIS D . n 
D 1 310 SER 310 379  379  SER SER D . n 
D 1 311 TRP 311 380  380  TRP TRP D . n 
D 1 312 PHE 312 381  381  PHE PHE D . n 
D 1 313 PRO 313 382  382  PRO PRO D . n 
D 1 314 GLY 314 383  383  GLY GLY D . n 
D 1 315 TYR 315 384  384  TYR TYR D . n 
D 1 316 ALA 316 385  385  ALA ALA D . n 
D 1 317 TRP 317 386  386  TRP TRP D . n 
D 1 318 THR 318 387  387  THR THR D . n 
D 1 319 VAL 319 388  388  VAL VAL D . n 
D 1 320 ALA 320 389  389  ALA ALA D . n 
D 1 321 GLN 321 390  390  GLN GLN D . n 
D 1 322 CYS 322 391  391  CYS CYS D . n 
D 1 323 LYS 323 392  392  LYS LYS D . n 
D 1 324 ILE 324 393  393  ILE ILE D . n 
D 1 325 CYS 325 394  394  CYS CYS D . n 
D 1 326 ALA 326 395  395  ALA ALA D . n 
D 1 327 SER 327 396  396  SER SER D . n 
D 1 328 HIS 328 397  397  HIS HIS D . n 
D 1 329 ILE 329 398  398  ILE ILE D . n 
D 1 330 GLY 330 399  399  GLY GLY D . n 
D 1 331 TRP 331 400  400  TRP TRP D . n 
D 1 332 LYS 332 401  401  LYS LYS D . n 
D 1 333 PHE 333 402  402  PHE PHE D . n 
D 1 334 THR 334 403  403  THR THR D . n 
D 1 335 ALA 335 404  404  ALA ALA D . n 
D 1 336 THR 336 405  405  THR THR D . n 
D 1 337 LYS 337 406  406  LYS LYS D . n 
D 1 338 LYS 338 407  407  LYS LYS D . n 
D 1 339 ASP 339 408  408  ASP ASP D . n 
D 1 340 MET 340 409  409  MET MET D . n 
D 1 341 SER 341 410  410  SER SER D . n 
D 1 342 PRO 342 411  411  PRO PRO D . n 
D 1 343 GLN 343 412  412  GLN GLN D . n 
D 1 344 LYS 344 413  413  LYS LYS D . n 
D 1 345 PHE 345 414  414  PHE PHE D . n 
D 1 346 TRP 346 415  415  TRP TRP D . n 
D 1 347 GLY 347 416  416  GLY GLY D . n 
D 1 348 LEU 348 417  417  LEU LEU D . n 
D 1 349 THR 349 418  418  THR THR D . n 
D 1 350 ARG 350 419  419  ARG ARG D . n 
D 1 351 SER 351 420  420  SER SER D . n 
D 1 352 ALA 352 421  421  ALA ALA D . n 
D 1 353 LEU 353 422  422  LEU LEU D . n 
D 1 354 LEU 354 423  423  LEU LEU D . n 
D 1 355 PRO 355 424  424  PRO PRO D . n 
D 1 356 THR 356 425  425  THR THR D . n 
D 1 357 ILE 357 426  426  ILE ILE D . n 
D 1 358 PRO 358 427  427  PRO PRO D . n 
D 1 359 ASP 359 428  ?    ?   ?   D . n 
D 1 360 THR 360 429  ?    ?   ?   D . n 
D 1 361 GLU 361 430  ?    ?   ?   D . n 
D 1 362 ASP 362 431  ?    ?   ?   D . n 
D 1 363 GLU 363 432  ?    ?   ?   D . n 
D 1 364 ILE 364 433  ?    ?   ?   D . n 
D 1 365 SER 365 434  ?    ?   ?   D . n 
D 1 366 PRO 366 435  ?    ?   ?   D . n 
D 1 367 ASP 367 436  ?    ?   ?   D . n 
D 1 368 LYS 368 437  ?    ?   ?   D . n 
D 1 369 VAL 369 438  438  VAL VAL D . n 
D 1 370 ILE 370 439  439  ILE ILE D . n 
D 1 371 LEU 371 440  440  LEU LEU D . n 
D 1 372 CYS 372 441  441  CYS CYS D . n 
D 1 373 LEU 373 442  442  LEU LEU D . n 
E 2 1   MET 1   1    ?    ?   ?   E . n 
E 2 2   SER 2   2    2    SER SER E . n 
E 2 3   TYR 3   3    3    TYR TYR E . n 
E 2 4   ASN 4   4    4    ASN ASN E . n 
E 2 5   TYR 5   5    5    TYR TYR E . n 
E 2 6   VAL 6   6    6    VAL VAL E . n 
E 2 7   VAL 7   7    7    VAL VAL E . n 
E 2 8   THR 8   8    8    THR THR E . n 
E 2 9   ALA 9   9    9    ALA ALA E . n 
E 2 10  GLN 10  10   10   GLN GLN E . n 
E 2 11  LYS 11  11   11   LYS LYS E . n 
E 2 12  PRO 12  12   12   PRO PRO E . n 
E 2 13  THR 13  13   13   THR THR E . n 
E 2 14  ALA 14  14   14   ALA ALA E . n 
E 2 15  VAL 15  15   15   VAL VAL E . n 
E 2 16  ASN 16  16   16   ASN ASN E . n 
E 2 17  GLY 17  17   17   GLY GLY E . n 
E 2 18  CYS 18  18   18   CYS CYS E . n 
E 2 19  VAL 19  19   19   VAL VAL E . n 
E 2 20  THR 20  20   20   THR THR E . n 
E 2 21  GLY 21  21   21   GLY GLY E . n 
E 2 22  HIS 22  22   22   HIS HIS E . n 
E 2 23  PHE 23  23   23   PHE PHE E . n 
E 2 24  THR 24  24   24   THR THR E . n 
E 2 25  SER 25  25   25   SER SER E . n 
E 2 26  ALA 26  26   26   ALA ALA E . n 
E 2 27  GLU 27  27   27   GLU GLU E . n 
E 2 28  ASP 28  28   28   ASP ASP E . n 
E 2 29  LEU 29  29   29   LEU LEU E . n 
E 2 30  ASN 30  30   30   ASN ASN E . n 
E 2 31  LEU 31  31   31   LEU LEU E . n 
E 2 32  LEU 32  32   32   LEU LEU E . n 
E 2 33  ILE 33  33   33   ILE ILE E . n 
E 2 34  ALA 34  34   34   ALA ALA E . n 
E 2 35  LYS 35  35   35   LYS LYS E . n 
E 2 36  ASN 36  36   36   ASN ASN E . n 
E 2 37  THR 37  37   37   THR THR E . n 
E 2 38  ARG 38  38   38   ARG ARG E . n 
E 2 39  LEU 39  39   39   LEU LEU E . n 
E 2 40  GLU 40  40   40   GLU GLU E . n 
E 2 41  ILE 41  41   41   ILE ILE E . n 
E 2 42  TYR 42  42   42   TYR TYR E . n 
E 2 43  VAL 43  43   43   VAL VAL E . n 
E 2 44  VAL 44  44   44   VAL VAL E . n 
E 2 45  THR 45  45   45   THR THR E . n 
E 2 46  ALA 46  46   46   ALA ALA E . n 
E 2 47  GLU 47  47   47   GLU GLU E . n 
E 2 48  GLY 48  48   48   GLY GLY E . n 
E 2 49  LEU 49  49   49   LEU LEU E . n 
E 2 50  ARG 50  50   50   ARG ARG E . n 
E 2 51  PRO 51  51   51   PRO PRO E . n 
E 2 52  VAL 52  52   52   VAL VAL E . n 
E 2 53  LYS 53  53   53   LYS LYS E . n 
E 2 54  GLU 54  54   54   GLU GLU E . n 
E 2 55  VAL 55  55   55   VAL VAL E . n 
E 2 56  GLY 56  56   56   GLY GLY E . n 
E 2 57  MET 57  57   57   MET MET E . n 
E 2 58  TYR 58  58   58   TYR TYR E . n 
E 2 59  GLY 59  59   59   GLY GLY E . n 
E 2 60  LYS 60  60   60   LYS LYS E . n 
E 2 61  ILE 61  61   61   ILE ILE E . n 
E 2 62  ALA 62  62   62   ALA ALA E . n 
E 2 63  VAL 63  63   63   VAL VAL E . n 
E 2 64  MET 64  64   64   MET MET E . n 
E 2 65  GLU 65  65   65   GLU GLU E . n 
E 2 66  LEU 66  66   66   LEU LEU E . n 
E 2 67  PHE 67  67   67   PHE PHE E . n 
E 2 68  ARG 68  68   68   ARG ARG E . n 
E 2 69  PRO 69  69   69   PRO PRO E . n 
E 2 70  LYS 70  70   70   LYS LYS E . n 
E 2 71  GLY 71  71   71   GLY GLY E . n 
E 2 72  GLU 72  72   72   GLU GLU E . n 
E 2 73  SER 73  73   73   SER SER E . n 
E 2 74  LYS 74  74   74   LYS LYS E . n 
E 2 75  ASP 75  75   75   ASP ASP E . n 
E 2 76  LEU 76  76   76   LEU LEU E . n 
E 2 77  LEU 77  77   77   LEU LEU E . n 
E 2 78  PHE 78  78   78   PHE PHE E . n 
E 2 79  ILE 79  79   79   ILE ILE E . n 
E 2 80  LEU 80  80   80   LEU LEU E . n 
E 2 81  THR 81  81   81   THR THR E . n 
E 2 82  ALA 82  82   82   ALA ALA E . n 
E 2 83  LYS 83  83   83   LYS LYS E . n 
E 2 84  TYR 84  84   84   TYR TYR E . n 
E 2 85  ASN 85  85   85   ASN ASN E . n 
E 2 86  ALA 86  86   86   ALA ALA E . n 
E 2 87  CYS 87  87   87   CYS CYS E . n 
E 2 88  ILE 88  88   88   ILE ILE E . n 
E 2 89  LEU 89  89   89   LEU LEU E . n 
E 2 90  GLU 90  90   90   GLU GLU E . n 
E 2 91  TYR 91  91   91   TYR TYR E . n 
E 2 92  LYS 92  92   92   LYS LYS E . n 
E 2 93  GLN 93  93   93   GLN GLN E . n 
E 2 94  SER 94  94   94   SER SER E . n 
E 2 95  GLY 95  95   95   GLY GLY E . n 
E 2 96  GLU 96  96   96   GLU GLU E . n 
E 2 97  SER 97  97   97   SER SER E . n 
E 2 98  ILE 98  98   98   ILE ILE E . n 
E 2 99  ASP 99  99   99   ASP ASP E . n 
E 2 100 ILE 100 100  100  ILE ILE E . n 
E 2 101 ILE 101 101  101  ILE ILE E . n 
E 2 102 THR 102 102  102  THR THR E . n 
E 2 103 ARG 103 103  103  ARG ARG E . n 
E 2 104 ALA 104 104  104  ALA ALA E . n 
E 2 105 HIS 105 105  105  HIS HIS E . n 
E 2 106 GLY 106 106  106  GLY GLY E . n 
E 2 107 ASN 107 107  107  ASN ASN E . n 
E 2 108 VAL 108 108  108  VAL VAL E . n 
E 2 109 GLN 109 109  109  GLN GLN E . n 
E 2 110 ASP 110 110  110  ASP ASP E . n 
E 2 111 ARG 111 111  111  ARG ARG E . n 
E 2 112 ILE 112 112  112  ILE ILE E . n 
E 2 113 GLY 113 113  113  GLY GLY E . n 
E 2 114 ARG 114 114  114  ARG ARG E . n 
E 2 115 PRO 115 115  115  PRO PRO E . n 
E 2 116 SER 116 116  116  SER SER E . n 
E 2 117 GLU 117 117  117  GLU GLU E . n 
E 2 118 THR 118 118  118  THR THR E . n 
E 2 119 GLY 119 119  119  GLY GLY E . n 
E 2 120 ILE 120 120  120  ILE ILE E . n 
E 2 121 ILE 121 121  121  ILE ILE E . n 
E 2 122 GLY 122 122  122  GLY GLY E . n 
E 2 123 ILE 123 123  123  ILE ILE E . n 
E 2 124 ILE 124 124  124  ILE ILE E . n 
E 2 125 ASP 125 125  125  ASP ASP E . n 
E 2 126 PRO 126 126  126  PRO PRO E . n 
E 2 127 GLU 127 127  127  GLU GLU E . n 
E 2 128 CYS 128 128  128  CYS CYS E . n 
E 2 129 ARG 129 129  129  ARG ARG E . n 
E 2 130 MET 130 130  130  MET MET E . n 
E 2 131 ILE 131 131  131  ILE ILE E . n 
E 2 132 GLY 132 132  132  GLY GLY E . n 
E 2 133 LEU 133 133  133  LEU LEU E . n 
E 2 134 ARG 134 134  134  ARG ARG E . n 
E 2 135 LEU 135 135  135  LEU LEU E . n 
E 2 136 TYR 136 136  136  TYR TYR E . n 
E 2 137 ASP 137 137  137  ASP ASP E . n 
E 2 138 GLY 138 138  138  GLY GLY E . n 
E 2 139 LEU 139 139  139  LEU LEU E . n 
E 2 140 PHE 140 140  140  PHE PHE E . n 
E 2 141 LYS 141 141  141  LYS LYS E . n 
E 2 142 VAL 142 142  142  VAL VAL E . n 
E 2 143 ILE 143 143  143  ILE ILE E . n 
E 2 144 PRO 144 144  144  PRO PRO E . n 
E 2 145 LEU 145 145  145  LEU LEU E . n 
E 2 146 ASP 146 146  146  ASP ASP E . n 
E 2 147 ARG 147 147  147  ARG ARG E . n 
E 2 148 ASP 148 148  148  ASP ASP E . n 
E 2 149 ASN 149 149  149  ASN ASN E . n 
E 2 150 LYS 150 150  150  LYS LYS E . n 
E 2 151 GLU 151 151  151  GLU GLU E . n 
E 2 152 LEU 152 152  152  LEU LEU E . n 
E 2 153 LYS 153 153  153  LYS LYS E . n 
E 2 154 ALA 154 154  154  ALA ALA E . n 
E 2 155 PHE 155 155  155  PHE PHE E . n 
E 2 156 ASN 156 156  156  ASN ASN E . n 
E 2 157 ILE 157 157  157  ILE ILE E . n 
E 2 158 ARG 158 158  158  ARG ARG E . n 
E 2 159 LEU 159 159  159  LEU LEU E . n 
E 2 160 GLU 160 160  160  GLU GLU E . n 
E 2 161 GLU 161 161  161  GLU GLU E . n 
E 2 162 LEU 162 162  162  LEU LEU E . n 
E 2 163 HIS 163 163  163  HIS HIS E . n 
E 2 164 VAL 164 164  164  VAL VAL E . n 
E 2 165 ILE 165 165  165  ILE ILE E . n 
E 2 166 ASP 166 166  166  ASP ASP E . n 
E 2 167 VAL 167 167  167  VAL VAL E . n 
E 2 168 LYS 168 168  168  LYS LYS E . n 
E 2 169 PHE 169 169  169  PHE PHE E . n 
E 2 170 LEU 170 170  170  LEU LEU E . n 
E 2 171 TYR 171 171  171  TYR TYR E . n 
E 2 172 GLY 172 172  172  GLY GLY E . n 
E 2 173 CYS 173 173  173  CYS CYS E . n 
E 2 174 GLN 174 174  174  GLN GLN E . n 
E 2 175 ALA 175 175  175  ALA ALA E . n 
E 2 176 PRO 176 176  176  PRO PRO E . n 
E 2 177 THR 177 177  177  THR THR E . n 
E 2 178 ILE 178 178  178  ILE ILE E . n 
E 2 179 CYS 179 179  179  CYS CYS E . n 
E 2 180 PHE 180 180  180  PHE PHE E . n 
E 2 181 VAL 181 181  181  VAL VAL E . n 
E 2 182 TYR 182 182  182  TYR TYR E . n 
E 2 183 GLN 183 183  183  GLN GLN E . n 
E 2 184 ASP 184 184  184  ASP ASP E . n 
E 2 185 PRO 185 185  185  PRO PRO E . n 
E 2 186 GLN 186 186  186  GLN GLN E . n 
E 2 187 GLY 187 187  187  GLY GLY E . n 
E 2 188 ARG 188 188  188  ARG ARG E . n 
E 2 189 HIS 189 189  189  HIS HIS E . n 
E 2 190 VAL 190 190  190  VAL VAL E . n 
E 2 191 LYS 191 191  191  LYS LYS E . n 
E 2 192 THR 192 192  192  THR THR E . n 
E 2 193 TYR 193 193  193  TYR TYR E . n 
E 2 194 GLU 194 194  194  GLU GLU E . n 
E 2 195 VAL 195 195  195  VAL VAL E . n 
E 2 196 SER 196 196  196  SER SER E . n 
E 2 197 LEU 197 197  197  LEU LEU E . n 
E 2 198 ARG 198 198  198  ARG ARG E . n 
E 2 199 GLU 199 199  199  GLU GLU E . n 
E 2 200 LYS 200 200  200  LYS LYS E . n 
E 2 201 GLU 201 201  201  GLU GLU E . n 
E 2 202 PHE 202 202  202  PHE PHE E . n 
E 2 203 ASN 203 203  203  ASN ASN E . n 
E 2 204 LYS 204 204  204  LYS LYS E . n 
E 2 205 GLY 205 205  205  GLY GLY E . n 
E 2 206 PRO 206 206  206  PRO PRO E . n 
E 2 207 TRP 207 207  207  TRP TRP E . n 
E 2 208 LYS 208 208  208  LYS LYS E . n 
E 2 209 GLN 209 209  209  GLN GLN E . n 
E 2 210 GLU 210 210  210  GLU GLU E . n 
E 2 211 ASN 211 211  211  ASN ASN E . n 
E 2 212 VAL 212 212  212  VAL VAL E . n 
E 2 213 GLU 213 213  213  GLU GLU E . n 
E 2 214 ALA 214 214  214  ALA ALA E . n 
E 2 215 GLU 215 215  215  GLU GLU E . n 
E 2 216 ALA 216 216  216  ALA ALA E . n 
E 2 217 SER 217 217  217  SER SER E . n 
E 2 218 MET 218 218  218  MET MET E . n 
E 2 219 VAL 219 219  219  VAL VAL E . n 
E 2 220 ILE 220 220  220  ILE ILE E . n 
E 2 221 ALA 221 221  221  ALA ALA E . n 
E 2 222 VAL 222 222  222  VAL VAL E . n 
E 2 223 PRO 223 223  223  PRO PRO E . n 
E 2 224 GLU 224 224  224  GLU GLU E . n 
E 2 225 PRO 225 225  225  PRO PRO E . n 
E 2 226 PHE 226 226  226  PHE PHE E . n 
E 2 227 GLY 227 227  227  GLY GLY E . n 
E 2 228 GLY 228 228  228  GLY GLY E . n 
E 2 229 ALA 229 229  229  ALA ALA E . n 
E 2 230 ILE 230 230  230  ILE ILE E . n 
E 2 231 ILE 231 231  231  ILE ILE E . n 
E 2 232 ILE 232 232  232  ILE ILE E . n 
E 2 233 GLY 233 233  233  GLY GLY E . n 
E 2 234 GLN 234 234  234  GLN GLN E . n 
E 2 235 GLU 235 235  235  GLU GLU E . n 
E 2 236 SER 236 236  236  SER SER E . n 
E 2 237 ILE 237 237  237  ILE ILE E . n 
E 2 238 THR 238 238  238  THR THR E . n 
E 2 239 TYR 239 239  239  TYR TYR E . n 
E 2 240 HIS 240 240  240  HIS HIS E . n 
E 2 241 ASN 241 241  241  ASN ASN E . n 
E 2 242 GLY 242 242  242  GLY GLY E . n 
E 2 243 ASP 243 243  243  ASP ASP E . n 
E 2 244 LYS 244 244  244  LYS LYS E . n 
E 2 245 TYR 245 245  245  TYR TYR E . n 
E 2 246 LEU 246 246  246  LEU LEU E . n 
E 2 247 ALA 247 247  247  ALA ALA E . n 
E 2 248 ILE 248 248  248  ILE ILE E . n 
E 2 249 ALA 249 249  249  ALA ALA E . n 
E 2 250 PRO 250 250  250  PRO PRO E . n 
E 2 251 PRO 251 251  251  PRO PRO E . n 
E 2 252 ILE 252 252  252  ILE ILE E . n 
E 2 253 ILE 253 253  253  ILE ILE E . n 
E 2 254 LYS 254 254  254  LYS LYS E . n 
E 2 255 GLN 255 255  255  GLN GLN E . n 
E 2 256 SER 256 256  256  SER SER E . n 
E 2 257 THR 257 257  257  THR THR E . n 
E 2 258 ILE 258 258  258  ILE ILE E . n 
E 2 259 VAL 259 259  259  VAL VAL E . n 
E 2 260 CYS 260 260  260  CYS CYS E . n 
E 2 261 HIS 261 261  261  HIS HIS E . n 
E 2 262 ASN 262 262  262  ASN ASN E . n 
E 2 263 ARG 263 263  263  ARG ARG E . n 
E 2 264 VAL 264 264  264  VAL VAL E . n 
E 2 265 ASP 265 265  265  ASP ASP E . n 
E 2 266 PRO 266 266  266  PRO PRO E . n 
E 2 267 ASN 267 267  267  ASN ASN E . n 
E 2 268 GLY 268 268  268  GLY GLY E . n 
E 2 269 SER 269 269  269  SER SER E . n 
E 2 270 ARG 270 270  270  ARG ARG E . n 
E 2 271 TYR 271 271  271  TYR TYR E . n 
E 2 272 LEU 272 272  272  LEU LEU E . n 
E 2 273 LEU 273 273  273  LEU LEU E . n 
E 2 274 GLY 274 274  274  GLY GLY E . n 
E 2 275 ASP 275 275  275  ASP ASP E . n 
E 2 276 MET 276 276  276  MET MET E . n 
E 2 277 GLU 277 277  277  GLU GLU E . n 
E 2 278 GLY 278 278  278  GLY GLY E . n 
E 2 279 ARG 279 279  279  ARG ARG E . n 
E 2 280 LEU 280 280  280  LEU LEU E . n 
E 2 281 PHE 281 281  281  PHE PHE E . n 
E 2 282 MET 282 282  282  MET MET E . n 
E 2 283 LEU 283 283  283  LEU LEU E . n 
E 2 284 LEU 284 284  284  LEU LEU E . n 
E 2 285 LEU 285 285  285  LEU LEU E . n 
E 2 286 GLU 286 286  286  GLU GLU E . n 
E 2 287 LYS 287 287  287  LYS LYS E . n 
E 2 288 GLU 288 288  288  GLU GLU E . n 
E 2 289 GLU 289 289  289  GLU GLU E . n 
E 2 290 GLN 290 290  290  GLN GLN E . n 
E 2 291 MET 291 291  291  MET MET E . n 
E 2 292 ASP 292 292  292  ASP ASP E . n 
E 2 293 GLY 293 293  293  GLY GLY E . n 
E 2 294 THR 294 294  294  THR THR E . n 
E 2 295 VAL 295 295  295  VAL VAL E . n 
E 2 296 THR 296 296  296  THR THR E . n 
E 2 297 LEU 297 297  297  LEU LEU E . n 
E 2 298 LYS 298 298  298  LYS LYS E . n 
E 2 299 ASP 299 299  299  ASP ASP E . n 
E 2 300 LEU 300 300  300  LEU LEU E . n 
E 2 301 ARG 301 301  301  ARG ARG E . n 
E 2 302 VAL 302 302  302  VAL VAL E . n 
E 2 303 GLU 303 303  303  GLU GLU E . n 
E 2 304 LEU 304 304  304  LEU LEU E . n 
E 2 305 LEU 305 305  305  LEU LEU E . n 
E 2 306 GLY 306 306  306  GLY GLY E . n 
E 2 307 GLU 307 307  307  GLU GLU E . n 
E 2 308 THR 308 308  308  THR THR E . n 
E 2 309 SER 309 309  309  SER SER E . n 
E 2 310 ILE 310 310  310  ILE ILE E . n 
E 2 311 ALA 311 311  311  ALA ALA E . n 
E 2 312 GLU 312 312  312  GLU GLU E . n 
E 2 313 CYS 313 313  313  CYS CYS E . n 
E 2 314 LEU 314 314  314  LEU LEU E . n 
E 2 315 THR 315 315  315  THR THR E . n 
E 2 316 TYR 316 316  316  TYR TYR E . n 
E 2 317 LEU 317 317  317  LEU LEU E . n 
E 2 318 ASP 318 318  318  ASP ASP E . n 
E 2 319 ASN 319 319  319  ASN ASN E . n 
E 2 320 GLY 320 320  320  GLY GLY E . n 
E 2 321 VAL 321 321  321  VAL VAL E . n 
E 2 322 VAL 322 322  322  VAL VAL E . n 
E 2 323 PHE 323 323  323  PHE PHE E . n 
E 2 324 VAL 324 324  324  VAL VAL E . n 
E 2 325 GLY 325 325  325  GLY GLY E . n 
E 2 326 SER 326 326  326  SER SER E . n 
E 2 327 ARG 327 327  327  ARG ARG E . n 
E 2 328 LEU 328 328  328  LEU LEU E . n 
E 2 329 GLY 329 329  329  GLY GLY E . n 
E 2 330 ASP 330 330  330  ASP ASP E . n 
E 2 331 SER 331 331  331  SER SER E . n 
E 2 332 GLN 332 332  332  GLN GLN E . n 
E 2 333 LEU 333 333  333  LEU LEU E . n 
E 2 334 VAL 334 334  334  VAL VAL E . n 
E 2 335 LYS 335 335  335  LYS LYS E . n 
E 2 336 LEU 336 336  336  LEU LEU E . n 
E 2 337 ASN 337 337  337  ASN ASN E . n 
E 2 338 VAL 338 338  338  VAL VAL E . n 
E 2 339 ASP 339 339  339  ASP ASP E . n 
E 2 340 SER 340 340  340  SER SER E . n 
E 2 341 ASN 341 341  341  ASN ASN E . n 
E 2 342 GLU 342 342  342  GLU GLU E . n 
E 2 343 GLN 343 343  343  GLN GLN E . n 
E 2 344 GLY 344 344  344  GLY GLY E . n 
E 2 345 SER 345 345  345  SER SER E . n 
E 2 346 TYR 346 346  346  TYR TYR E . n 
E 2 347 VAL 347 347  347  VAL VAL E . n 
E 2 348 VAL 348 348  348  VAL VAL E . n 
E 2 349 ALA 349 349  349  ALA ALA E . n 
E 2 350 MET 350 350  350  MET MET E . n 
E 2 351 GLU 351 351  351  GLU GLU E . n 
E 2 352 THR 352 352  352  THR THR E . n 
E 2 353 PHE 353 353  353  PHE PHE E . n 
E 2 354 THR 354 354  354  THR THR E . n 
E 2 355 ASN 355 355  355  ASN ASN E . n 
E 2 356 LEU 356 356  356  LEU LEU E . n 
E 2 357 GLY 357 357  357  GLY GLY E . n 
E 2 358 PRO 358 358  358  PRO PRO E . n 
E 2 359 ILE 359 359  359  ILE ILE E . n 
E 2 360 VAL 360 360  360  VAL VAL E . n 
E 2 361 ASP 361 361  361  ASP ASP E . n 
E 2 362 MET 362 362  362  MET MET E . n 
E 2 363 CYS 363 363  363  CYS CYS E . n 
E 2 364 VAL 364 364  364  VAL VAL E . n 
E 2 365 VAL 365 365  365  VAL VAL E . n 
E 2 366 ASP 366 366  366  ASP ASP E . n 
E 2 367 LEU 367 367  367  LEU LEU E . n 
E 2 368 GLU 368 368  368  GLU GLU E . n 
E 2 369 ARG 369 369  369  ARG ARG E . n 
E 2 370 GLN 370 370  370  GLN GLN E . n 
E 2 371 GLY 371 371  371  GLY GLY E . n 
E 2 372 GLN 372 372  372  GLN GLN E . n 
E 2 373 GLY 373 373  373  GLY GLY E . n 
E 2 374 GLN 374 374  374  GLN GLN E . n 
E 2 375 LEU 375 375  375  LEU LEU E . n 
E 2 376 VAL 376 376  376  VAL VAL E . n 
E 2 377 THR 377 377  377  THR THR E . n 
E 2 378 CYS 378 378  378  CYS CYS E . n 
E 2 379 SER 379 379  379  SER SER E . n 
E 2 380 GLY 380 380  380  GLY GLY E . n 
E 2 381 ALA 381 381  381  ALA ALA E . n 
E 2 382 PHE 382 382  382  PHE PHE E . n 
E 2 383 LYS 383 383  383  LYS LYS E . n 
E 2 384 GLU 384 384  384  GLU GLU E . n 
E 2 385 GLY 385 385  385  GLY GLY E . n 
E 2 386 SER 386 386  386  SER SER E . n 
E 2 387 LEU 387 387  387  LEU LEU E . n 
E 2 388 ARG 388 388  388  ARG ARG E . n 
E 2 389 ILE 389 389  389  ILE ILE E . n 
E 2 390 ILE 390 390  390  ILE ILE E . n 
E 2 391 ARG 391 391  391  ARG ARG E . n 
E 2 392 ASN 392 392  392  ASN ASN E . n 
E 2 393 GLY 393 697  ?    ?   ?   E . n 
E 2 394 ILE 394 698  ?    ?   ?   E . n 
E 2 395 GLY 395 699  ?    ?   ?   E . n 
E 2 396 GLY 396 700  ?    ?   ?   E . n 
E 2 397 ASN 397 701  ?    ?   ?   E . n 
E 2 398 GLY 398 702  ?    ?   ?   E . n 
E 2 399 ASN 399 703  ?    ?   ?   E . n 
E 2 400 SER 400 704  ?    ?   ?   E . n 
E 2 401 GLY 401 705  ?    ?   ?   E . n 
E 2 402 GLU 402 706  ?    ?   ?   E . n 
E 2 403 ILE 403 707  ?    ?   ?   E . n 
E 2 404 GLN 404 708  ?    ?   ?   E . n 
E 2 405 LYS 405 709  ?    ?   ?   E . n 
E 2 406 LEU 406 710  710  LEU LEU E . n 
E 2 407 HIS 407 711  711  HIS HIS E . n 
E 2 408 ILE 408 712  712  ILE ILE E . n 
E 2 409 ARG 409 713  713  ARG ARG E . n 
E 2 410 THR 410 714  714  THR THR E . n 
E 2 411 VAL 411 715  715  VAL VAL E . n 
E 2 412 PRO 412 716  716  PRO PRO E . n 
E 2 413 LEU 413 717  717  LEU LEU E . n 
E 2 414 TYR 414 718  718  TYR TYR E . n 
E 2 415 GLU 415 719  719  GLU GLU E . n 
E 2 416 SER 416 720  720  SER SER E . n 
E 2 417 PRO 417 721  721  PRO PRO E . n 
E 2 418 ARG 418 722  722  ARG ARG E . n 
E 2 419 LYS 419 723  723  LYS LYS E . n 
E 2 420 ILE 420 724  724  ILE ILE E . n 
E 2 421 CYS 421 725  725  CYS CYS E . n 
E 2 422 TYR 422 726  726  TYR TYR E . n 
E 2 423 GLN 423 727  727  GLN GLN E . n 
E 2 424 GLU 424 728  728  GLU GLU E . n 
E 2 425 VAL 425 729  729  VAL VAL E . n 
E 2 426 SER 426 730  730  SER SER E . n 
E 2 427 GLN 427 731  731  GLN GLN E . n 
E 2 428 CYS 428 732  732  CYS CYS E . n 
E 2 429 PHE 429 733  733  PHE PHE E . n 
E 2 430 GLY 430 734  734  GLY GLY E . n 
E 2 431 VAL 431 735  735  VAL VAL E . n 
E 2 432 LEU 432 736  736  LEU LEU E . n 
E 2 433 SER 433 737  737  SER SER E . n 
E 2 434 SER 434 738  738  SER SER E . n 
E 2 435 ARG 435 739  739  ARG ARG E . n 
E 2 436 ILE 436 740  740  ILE ILE E . n 
E 2 437 GLU 437 741  741  GLU GLU E . n 
E 2 438 VAL 438 742  742  VAL VAL E . n 
E 2 439 GLN 439 743  743  GLN GLN E . n 
E 2 440 ASP 440 744  ?    ?   ?   E . n 
E 2 441 THR 441 745  745  THR THR E . n 
E 2 442 SER 442 746  746  SER SER E . n 
E 2 443 GLY 443 747  747  GLY GLY E . n 
E 2 444 GLY 444 748  748  GLY GLY E . n 
E 2 445 THR 445 749  749  THR THR E . n 
E 2 446 THR 446 750  750  THR THR E . n 
E 2 447 ALA 447 751  751  ALA ALA E . n 
E 2 448 LEU 448 752  752  LEU LEU E . n 
E 2 449 ARG 449 753  753  ARG ARG E . n 
E 2 450 PRO 450 754  754  PRO PRO E . n 
E 2 451 SER 451 755  755  SER SER E . n 
E 2 452 ALA 452 756  756  ALA ALA E . n 
E 2 453 SER 453 757  757  SER SER E . n 
E 2 454 THR 454 758  758  THR THR E . n 
E 2 455 GLN 455 759  759  GLN GLN E . n 
E 2 456 ALA 456 760  760  ALA ALA E . n 
E 2 457 LEU 457 761  761  LEU LEU E . n 
E 2 458 SER 458 762  762  SER SER E . n 
E 2 459 SER 459 763  763  SER SER E . n 
E 2 460 SER 460 764  764  SER SER E . n 
E 2 461 VAL 461 765  765  VAL VAL E . n 
E 2 462 SER 462 766  766  SER SER E . n 
E 2 463 SER 463 767  767  SER SER E . n 
E 2 464 SER 464 768  768  SER SER E . n 
E 2 465 LYS 465 769  769  LYS LYS E . n 
E 2 466 LEU 466 770  770  LEU LEU E . n 
E 2 467 PHE 467 771  771  PHE PHE E . n 
E 2 468 SER 468 772  ?    ?   ?   E . n 
E 2 469 SER 469 773  ?    ?   ?   E . n 
E 2 470 SER 470 774  ?    ?   ?   E . n 
E 2 471 THR 471 775  ?    ?   ?   E . n 
E 2 472 ALA 472 776  ?    ?   ?   E . n 
E 2 473 PRO 473 777  ?    ?   ?   E . n 
E 2 474 HIS 474 778  ?    ?   ?   E . n 
E 2 475 GLU 475 779  ?    ?   ?   E . n 
E 2 476 THR 476 780  780  THR THR E . n 
E 2 477 SER 477 781  781  SER SER E . n 
E 2 478 PHE 478 782  782  PHE PHE E . n 
E 2 479 GLY 479 783  783  GLY GLY E . n 
E 2 480 GLU 480 784  784  GLU GLU E . n 
E 2 481 GLU 481 785  785  GLU GLU E . n 
E 2 482 VAL 482 786  786  VAL VAL E . n 
E 2 483 GLU 483 787  787  GLU GLU E . n 
E 2 484 VAL 484 788  788  VAL VAL E . n 
E 2 485 HIS 485 789  789  HIS HIS E . n 
E 2 486 ASN 486 790  790  ASN ASN E . n 
E 2 487 LEU 487 791  791  LEU LEU E . n 
E 2 488 LEU 488 792  792  LEU LEU E . n 
E 2 489 ILE 489 793  793  ILE ILE E . n 
E 2 490 ILE 490 794  794  ILE ILE E . n 
E 2 491 ASP 491 795  795  ASP ASP E . n 
E 2 492 GLN 492 796  796  GLN GLN E . n 
E 2 493 HIS 493 797  797  HIS HIS E . n 
E 2 494 THR 494 798  798  THR THR E . n 
E 2 495 PHE 495 799  799  PHE PHE E . n 
E 2 496 GLU 496 800  800  GLU GLU E . n 
E 2 497 VAL 497 801  801  VAL VAL E . n 
E 2 498 LEU 498 802  802  LEU LEU E . n 
E 2 499 HIS 499 803  803  HIS HIS E . n 
E 2 500 ALA 500 804  804  ALA ALA E . n 
E 2 501 HIS 501 805  805  HIS HIS E . n 
E 2 502 GLN 502 806  806  GLN GLN E . n 
E 2 503 PHE 503 807  807  PHE PHE E . n 
E 2 504 LEU 504 808  808  LEU LEU E . n 
E 2 505 GLN 505 809  809  GLN GLN E . n 
E 2 506 ASN 506 810  810  ASN ASN E . n 
E 2 507 GLU 507 811  811  GLU GLU E . n 
E 2 508 TYR 508 812  812  TYR TYR E . n 
E 2 509 ALA 509 813  813  ALA ALA E . n 
E 2 510 LEU 510 814  814  LEU LEU E . n 
E 2 511 SER 511 815  815  SER SER E . n 
E 2 512 LEU 512 816  816  LEU LEU E . n 
E 2 513 VAL 513 817  817  VAL VAL E . n 
E 2 514 SER 514 818  818  SER SER E . n 
E 2 515 CYS 515 819  819  CYS CYS E . n 
E 2 516 LYS 516 820  820  LYS LYS E . n 
E 2 517 LEU 517 821  821  LEU LEU E . n 
E 2 518 GLY 518 822  822  GLY GLY E . n 
E 2 519 LYS 519 823  823  LYS LYS E . n 
E 2 520 ASP 520 824  824  ASP ASP E . n 
E 2 521 PRO 521 825  825  PRO PRO E . n 
E 2 522 ASN 522 826  826  ASN ASN E . n 
E 2 523 THR 523 827  827  THR THR E . n 
E 2 524 TYR 524 828  828  TYR TYR E . n 
E 2 525 PHE 525 829  829  PHE PHE E . n 
E 2 526 ILE 526 830  830  ILE ILE E . n 
E 2 527 VAL 527 831  831  VAL VAL E . n 
E 2 528 GLY 528 832  832  GLY GLY E . n 
E 2 529 THR 529 833  833  THR THR E . n 
E 2 530 ALA 530 834  834  ALA ALA E . n 
E 2 531 MET 531 835  835  MET MET E . n 
E 2 532 VAL 532 836  836  VAL VAL E . n 
E 2 533 TYR 533 837  837  TYR TYR E . n 
E 2 534 PRO 534 838  838  PRO PRO E . n 
E 2 535 GLU 535 839  839  GLU GLU E . n 
E 2 536 GLU 536 840  840  GLU GLU E . n 
E 2 537 ALA 537 841  841  ALA ALA E . n 
E 2 538 GLU 538 842  842  GLU GLU E . n 
E 2 539 PRO 539 843  843  PRO PRO E . n 
E 2 540 LYS 540 844  844  LYS LYS E . n 
E 2 541 GLN 541 845  845  GLN GLN E . n 
E 2 542 GLY 542 846  846  GLY GLY E . n 
E 2 543 ARG 543 847  847  ARG ARG E . n 
E 2 544 ILE 544 848  848  ILE ILE E . n 
E 2 545 VAL 545 849  849  VAL VAL E . n 
E 2 546 VAL 546 850  850  VAL VAL E . n 
E 2 547 PHE 547 851  851  PHE PHE E . n 
E 2 548 GLN 548 852  852  GLN GLN E . n 
E 2 549 TYR 549 853  853  TYR TYR E . n 
E 2 550 SER 550 854  854  SER SER E . n 
E 2 551 ASP 551 855  855  ASP ASP E . n 
E 2 552 GLY 552 856  856  GLY GLY E . n 
E 2 553 LYS 553 857  857  LYS LYS E . n 
E 2 554 LEU 554 858  858  LEU LEU E . n 
E 2 555 GLN 555 859  859  GLN GLN E . n 
E 2 556 THR 556 860  860  THR THR E . n 
E 2 557 VAL 557 861  861  VAL VAL E . n 
E 2 558 ALA 558 862  862  ALA ALA E . n 
E 2 559 GLU 559 863  863  GLU GLU E . n 
E 2 560 LYS 560 864  864  LYS LYS E . n 
E 2 561 GLU 561 865  865  GLU GLU E . n 
E 2 562 VAL 562 866  866  VAL VAL E . n 
E 2 563 LYS 563 867  867  LYS LYS E . n 
E 2 564 GLY 564 868  868  GLY GLY E . n 
E 2 565 ALA 565 869  869  ALA ALA E . n 
E 2 566 VAL 566 870  870  VAL VAL E . n 
E 2 567 TYR 567 871  871  TYR TYR E . n 
E 2 568 SER 568 872  872  SER SER E . n 
E 2 569 MET 569 873  873  MET MET E . n 
E 2 570 VAL 570 874  874  VAL VAL E . n 
E 2 571 GLU 571 875  875  GLU GLU E . n 
E 2 572 PHE 572 876  876  PHE PHE E . n 
E 2 573 ASN 573 877  877  ASN ASN E . n 
E 2 574 GLY 574 878  878  GLY GLY E . n 
E 2 575 LYS 575 879  879  LYS LYS E . n 
E 2 576 LEU 576 880  880  LEU LEU E . n 
E 2 577 LEU 577 881  881  LEU LEU E . n 
E 2 578 ALA 578 882  882  ALA ALA E . n 
E 2 579 SER 579 883  883  SER SER E . n 
E 2 580 ILE 580 884  884  ILE ILE E . n 
E 2 581 ASN 581 885  885  ASN ASN E . n 
E 2 582 SER 582 886  886  SER SER E . n 
E 2 583 THR 583 887  887  THR THR E . n 
E 2 584 VAL 584 888  888  VAL VAL E . n 
E 2 585 ARG 585 889  889  ARG ARG E . n 
E 2 586 LEU 586 890  890  LEU LEU E . n 
E 2 587 TYR 587 891  891  TYR TYR E . n 
E 2 588 GLU 588 892  892  GLU GLU E . n 
E 2 589 TRP 589 893  893  TRP TRP E . n 
E 2 590 THR 590 894  894  THR THR E . n 
E 2 591 THR 591 895  895  THR THR E . n 
E 2 592 GLU 592 896  896  GLU GLU E . n 
E 2 593 LYS 593 897  897  LYS LYS E . n 
E 2 594 GLU 594 898  898  GLU GLU E . n 
E 2 595 LEU 595 899  899  LEU LEU E . n 
E 2 596 ARG 596 900  900  ARG ARG E . n 
E 2 597 THR 597 901  901  THR THR E . n 
E 2 598 GLU 598 902  902  GLU GLU E . n 
E 2 599 CYS 599 903  903  CYS CYS E . n 
E 2 600 ASN 600 904  904  ASN ASN E . n 
E 2 601 HIS 601 905  905  HIS HIS E . n 
E 2 602 TYR 602 906  906  TYR TYR E . n 
E 2 603 ASN 603 907  907  ASN ASN E . n 
E 2 604 ASN 604 908  908  ASN ASN E . n 
E 2 605 ILE 605 909  909  ILE ILE E . n 
E 2 606 MET 606 910  910  MET MET E . n 
E 2 607 ALA 607 911  911  ALA ALA E . n 
E 2 608 LEU 608 912  912  LEU LEU E . n 
E 2 609 TYR 609 913  913  TYR TYR E . n 
E 2 610 LEU 610 914  914  LEU LEU E . n 
E 2 611 LYS 611 915  915  LYS LYS E . n 
E 2 612 THR 612 916  916  THR THR E . n 
E 2 613 LYS 613 917  917  LYS LYS E . n 
E 2 614 GLY 614 918  918  GLY GLY E . n 
E 2 615 ASP 615 919  919  ASP ASP E . n 
E 2 616 PHE 616 920  920  PHE PHE E . n 
E 2 617 ILE 617 921  921  ILE ILE E . n 
E 2 618 LEU 618 922  922  LEU LEU E . n 
E 2 619 VAL 619 923  923  VAL VAL E . n 
E 2 620 GLY 620 924  924  GLY GLY E . n 
E 2 621 ASP 621 925  925  ASP ASP E . n 
E 2 622 LEU 622 926  926  LEU LEU E . n 
E 2 623 MET 623 927  927  MET MET E . n 
E 2 624 ARG 624 928  928  ARG ARG E . n 
E 2 625 SER 625 929  929  SER SER E . n 
E 2 626 VAL 626 930  930  VAL VAL E . n 
E 2 627 LEU 627 931  931  LEU LEU E . n 
E 2 628 LEU 628 932  932  LEU LEU E . n 
E 2 629 LEU 629 933  933  LEU LEU E . n 
E 2 630 ALA 630 934  934  ALA ALA E . n 
E 2 631 TYR 631 935  935  TYR TYR E . n 
E 2 632 LYS 632 936  936  LYS LYS E . n 
E 2 633 PRO 633 937  937  PRO PRO E . n 
E 2 634 MET 634 938  938  MET MET E . n 
E 2 635 GLU 635 939  939  GLU GLU E . n 
E 2 636 GLY 636 940  940  GLY GLY E . n 
E 2 637 ASN 637 941  941  ASN ASN E . n 
E 2 638 PHE 638 942  942  PHE PHE E . n 
E 2 639 GLU 639 943  943  GLU GLU E . n 
E 2 640 GLU 640 944  944  GLU GLU E . n 
E 2 641 ILE 641 945  945  ILE ILE E . n 
E 2 642 ALA 642 946  946  ALA ALA E . n 
E 2 643 ARG 643 947  947  ARG ARG E . n 
E 2 644 ASP 644 948  948  ASP ASP E . n 
E 2 645 PHE 645 949  949  PHE PHE E . n 
E 2 646 ASN 646 950  950  ASN ASN E . n 
E 2 647 PRO 647 951  951  PRO PRO E . n 
E 2 648 ASN 648 952  952  ASN ASN E . n 
E 2 649 TRP 649 953  953  TRP TRP E . n 
E 2 650 MET 650 954  954  MET MET E . n 
E 2 651 SER 651 955  955  SER SER E . n 
E 2 652 ALA 652 956  956  ALA ALA E . n 
E 2 653 VAL 653 957  957  VAL VAL E . n 
E 2 654 GLU 654 958  958  GLU GLU E . n 
E 2 655 ILE 655 959  959  ILE ILE E . n 
E 2 656 LEU 656 960  960  LEU LEU E . n 
E 2 657 ASP 657 961  961  ASP ASP E . n 
E 2 658 ASP 658 962  962  ASP ASP E . n 
E 2 659 ASP 659 963  963  ASP ASP E . n 
E 2 660 ASN 660 964  964  ASN ASN E . n 
E 2 661 PHE 661 965  965  PHE PHE E . n 
E 2 662 LEU 662 966  966  LEU LEU E . n 
E 2 663 GLY 663 967  967  GLY GLY E . n 
E 2 664 ALA 664 968  968  ALA ALA E . n 
E 2 665 GLU 665 969  969  GLU GLU E . n 
E 2 666 ASN 666 970  970  ASN ASN E . n 
E 2 667 ALA 667 971  971  ALA ALA E . n 
E 2 668 PHE 668 972  972  PHE PHE E . n 
E 2 669 ASN 669 973  973  ASN ASN E . n 
E 2 670 LEU 670 974  974  LEU LEU E . n 
E 2 671 PHE 671 975  975  PHE PHE E . n 
E 2 672 VAL 672 976  976  VAL VAL E . n 
E 2 673 CYS 673 977  977  CYS CYS E . n 
E 2 674 GLN 674 978  978  GLN GLN E . n 
E 2 675 LYS 675 979  979  LYS LYS E . n 
E 2 676 ASP 676 980  980  ASP ASP E . n 
E 2 677 SER 677 981  981  SER SER E . n 
E 2 678 ALA 678 982  982  ALA ALA E . n 
E 2 679 ALA 679 983  983  ALA ALA E . n 
E 2 680 THR 680 984  984  THR THR E . n 
E 2 681 THR 681 985  985  THR THR E . n 
E 2 682 ASP 682 986  986  ASP ASP E . n 
E 2 683 GLU 683 987  987  GLU GLU E . n 
E 2 684 GLU 684 988  988  GLU GLU E . n 
E 2 685 ARG 685 989  989  ARG ARG E . n 
E 2 686 GLN 686 990  990  GLN GLN E . n 
E 2 687 HIS 687 991  991  HIS HIS E . n 
E 2 688 LEU 688 992  992  LEU LEU E . n 
E 2 689 GLN 689 993  993  GLN GLN E . n 
E 2 690 GLU 690 994  994  GLU GLU E . n 
E 2 691 VAL 691 995  995  VAL VAL E . n 
E 2 692 GLY 692 996  996  GLY GLY E . n 
E 2 693 LEU 693 997  997  LEU LEU E . n 
E 2 694 PHE 694 998  998  PHE PHE E . n 
E 2 695 HIS 695 999  999  HIS HIS E . n 
E 2 696 LEU 696 1000 1000 LEU LEU E . n 
E 2 697 GLY 697 1001 1001 GLY GLY E . n 
E 2 698 GLU 698 1002 1002 GLU GLU E . n 
E 2 699 PHE 699 1003 1003 PHE PHE E . n 
E 2 700 VAL 700 1004 1004 VAL VAL E . n 
E 2 701 ASN 701 1005 1005 ASN ASN E . n 
E 2 702 VAL 702 1006 1006 VAL VAL E . n 
E 2 703 PHE 703 1007 1007 PHE PHE E . n 
E 2 704 CYS 704 1008 1008 CYS CYS E . n 
E 2 705 HIS 705 1009 1009 HIS HIS E . n 
E 2 706 GLY 706 1010 1010 GLY GLY E . n 
E 2 707 SER 707 1011 1011 SER SER E . n 
E 2 708 LEU 708 1012 1012 LEU LEU E . n 
E 2 709 VAL 709 1013 1013 VAL VAL E . n 
E 2 710 MET 710 1014 1014 MET MET E . n 
E 2 711 GLN 711 1015 ?    ?   ?   E . n 
E 2 712 ASN 712 1016 ?    ?   ?   E . n 
E 2 713 LEU 713 1017 ?    ?   ?   E . n 
E 2 714 GLY 714 1018 ?    ?   ?   E . n 
E 2 715 GLU 715 1019 ?    ?   ?   E . n 
E 2 716 THR 716 1020 ?    ?   ?   E . n 
E 2 717 SER 717 1021 ?    ?   ?   E . n 
E 2 718 THR 718 1022 ?    ?   ?   E . n 
E 2 719 PRO 719 1023 1023 PRO PRO E . n 
E 2 720 THR 720 1024 1024 THR THR E . n 
E 2 721 GLN 721 1025 1025 GLN GLN E . n 
E 2 722 GLY 722 1026 1026 GLY GLY E . n 
E 2 723 SER 723 1027 1027 SER SER E . n 
E 2 724 VAL 724 1028 1028 VAL VAL E . n 
E 2 725 LEU 725 1029 1029 LEU LEU E . n 
E 2 726 PHE 726 1030 1030 PHE PHE E . n 
E 2 727 GLY 727 1031 1031 GLY GLY E . n 
E 2 728 THR 728 1032 1032 THR THR E . n 
E 2 729 VAL 729 1033 1033 VAL VAL E . n 
E 2 730 ASN 730 1034 1034 ASN ASN E . n 
E 2 731 GLY 731 1035 1035 GLY GLY E . n 
E 2 732 MET 732 1036 1036 MET MET E . n 
E 2 733 ILE 733 1037 1037 ILE ILE E . n 
E 2 734 GLY 734 1038 1038 GLY GLY E . n 
E 2 735 LEU 735 1039 1039 LEU LEU E . n 
E 2 736 VAL 736 1040 1040 VAL VAL E . n 
E 2 737 THR 737 1041 1041 THR THR E . n 
E 2 738 SER 738 1042 1042 SER SER E . n 
E 2 739 LEU 739 1043 1043 LEU LEU E . n 
E 2 740 SER 740 1044 1044 SER SER E . n 
E 2 741 GLU 741 1045 1045 GLU GLU E . n 
E 2 742 SER 742 1046 1046 SER SER E . n 
E 2 743 TRP 743 1047 1047 TRP TRP E . n 
E 2 744 TYR 744 1048 1048 TYR TYR E . n 
E 2 745 ASN 745 1049 1049 ASN ASN E . n 
E 2 746 LEU 746 1050 1050 LEU LEU E . n 
E 2 747 LEU 747 1051 1051 LEU LEU E . n 
E 2 748 LEU 748 1052 1052 LEU LEU E . n 
E 2 749 ASP 749 1053 1053 ASP ASP E . n 
E 2 750 MET 750 1054 1054 MET MET E . n 
E 2 751 GLN 751 1055 1055 GLN GLN E . n 
E 2 752 ASN 752 1056 1056 ASN ASN E . n 
E 2 753 ARG 753 1057 1057 ARG ARG E . n 
E 2 754 LEU 754 1058 1058 LEU LEU E . n 
E 2 755 ASN 755 1059 1059 ASN ASN E . n 
E 2 756 LYS 756 1060 1060 LYS LYS E . n 
E 2 757 VAL 757 1061 1061 VAL VAL E . n 
E 2 758 ILE 758 1062 1062 ILE ILE E . n 
E 2 759 LYS 759 1063 1063 LYS LYS E . n 
E 2 760 SER 760 1064 1064 SER SER E . n 
E 2 761 VAL 761 1065 1065 VAL VAL E . n 
E 2 762 GLY 762 1066 1066 GLY GLY E . n 
E 2 763 LYS 763 1067 1067 LYS LYS E . n 
E 2 764 ILE 764 1068 1068 ILE ILE E . n 
E 2 765 GLU 765 1069 1069 GLU GLU E . n 
E 2 766 HIS 766 1070 1070 HIS HIS E . n 
E 2 767 SER 767 1071 1071 SER SER E . n 
E 2 768 PHE 768 1072 1072 PHE PHE E . n 
E 2 769 TRP 769 1073 1073 TRP TRP E . n 
E 2 770 ARG 770 1074 1074 ARG ARG E . n 
E 2 771 SER 771 1075 1075 SER SER E . n 
E 2 772 PHE 772 1076 1076 PHE PHE E . n 
E 2 773 HIS 773 1077 1077 HIS HIS E . n 
E 2 774 THR 774 1078 1078 THR THR E . n 
E 2 775 GLU 775 1079 1079 GLU GLU E . n 
E 2 776 ARG 776 1080 1080 ARG ARG E . n 
E 2 777 LYS 777 1081 1081 LYS LYS E . n 
E 2 778 THR 778 1082 1082 THR THR E . n 
E 2 779 GLU 779 1083 1083 GLU GLU E . n 
E 2 780 PRO 780 1084 1084 PRO PRO E . n 
E 2 781 ALA 781 1085 1085 ALA ALA E . n 
E 2 782 THR 782 1086 1086 THR THR E . n 
E 2 783 GLY 783 1087 1087 GLY GLY E . n 
E 2 784 PHE 784 1088 1088 PHE PHE E . n 
E 2 785 ILE 785 1089 1089 ILE ILE E . n 
E 2 786 ASP 786 1090 1090 ASP ASP E . n 
E 2 787 GLY 787 1091 1091 GLY GLY E . n 
E 2 788 ASP 788 1092 1092 ASP ASP E . n 
E 2 789 LEU 789 1093 1093 LEU LEU E . n 
E 2 790 ILE 790 1094 1094 ILE ILE E . n 
E 2 791 GLU 791 1095 1095 GLU GLU E . n 
E 2 792 SER 792 1096 1096 SER SER E . n 
E 2 793 PHE 793 1097 1097 PHE PHE E . n 
E 2 794 LEU 794 1098 1098 LEU LEU E . n 
E 2 795 ASP 795 1099 1099 ASP ASP E . n 
E 2 796 ILE 796 1100 1100 ILE ILE E . n 
E 2 797 SER 797 1101 1101 SER SER E . n 
E 2 798 ARG 798 1102 1102 ARG ARG E . n 
E 2 799 PRO 799 1103 1103 PRO PRO E . n 
E 2 800 LYS 800 1104 1104 LYS LYS E . n 
E 2 801 MET 801 1105 1105 MET MET E . n 
E 2 802 GLN 802 1106 1106 GLN GLN E . n 
E 2 803 GLU 803 1107 1107 GLU GLU E . n 
E 2 804 VAL 804 1108 1108 VAL VAL E . n 
E 2 805 VAL 805 1109 1109 VAL VAL E . n 
E 2 806 ALA 806 1110 1110 ALA ALA E . n 
E 2 807 ASN 807 1111 1111 ASN ASN E . n 
E 2 808 LEU 808 1112 1112 LEU LEU E . n 
E 2 809 GLN 809 1113 1113 GLN GLN E . n 
E 2 810 TYR 810 1114 ?    ?   ?   E . n 
E 2 811 ASP 811 1115 ?    ?   ?   E . n 
E 2 812 ASP 812 1116 ?    ?   ?   E . n 
E 2 813 GLY 813 1117 ?    ?   ?   E . n 
E 2 814 SER 814 1118 ?    ?   ?   E . n 
E 2 815 GLY 815 1119 ?    ?   ?   E . n 
E 2 816 MET 816 1120 ?    ?   ?   E . n 
E 2 817 LYS 817 1121 ?    ?   ?   E . n 
E 2 818 ARG 818 1122 ?    ?   ?   E . n 
E 2 819 GLU 819 1123 ?    ?   ?   E . n 
E 2 820 ALA 820 1124 1124 ALA ALA E . n 
E 2 821 THR 821 1125 1125 THR THR E . n 
E 2 822 ALA 822 1126 1126 ALA ALA E . n 
E 2 823 ASP 823 1127 1127 ASP ASP E . n 
E 2 824 ASP 824 1128 1128 ASP ASP E . n 
E 2 825 LEU 825 1129 1129 LEU LEU E . n 
E 2 826 ILE 826 1130 1130 ILE ILE E . n 
E 2 827 LYS 827 1131 1131 LYS LYS E . n 
E 2 828 VAL 828 1132 1132 VAL VAL E . n 
E 2 829 VAL 829 1133 1133 VAL VAL E . n 
E 2 830 GLU 830 1134 1134 GLU GLU E . n 
E 2 831 GLU 831 1135 1135 GLU GLU E . n 
E 2 832 LEU 832 1136 1136 LEU LEU E . n 
E 2 833 THR 833 1137 1137 THR THR E . n 
E 2 834 ARG 834 1138 1138 ARG ARG E . n 
E 2 835 ILE 835 1139 1139 ILE ILE E . n 
E 2 836 HIS 836 1140 1140 HIS HIS E . n 
F 3 1   SER 1   866  ?    ?   ?   F . n 
F 3 2   GLN 2   867  ?    ?   ?   F . n 
F 3 3   SER 3   868  868  SER SER F . n 
F 3 4   LEU 4   869  869  LEU LEU F . n 
F 3 5   THR 5   870  870  THR THR F . n 
F 3 6   THR 6   871  871  THR THR F . n 
F 3 7   CYS 7   872  872  CYS CYS F . n 
F 3 8   GLU 8   873  873  GLU GLU F . n 
F 3 9   VAL 9   874  874  VAL VAL F . n 
F 3 10  CYS 10  875  875  CYS CYS F . n 
F 3 11  GLY 11  876  876  GLY GLY F . n 
F 3 12  ALA 12  877  877  ALA ALA F . n 
F 3 13  CYS 13  878  878  CYS CYS F . n 
F 3 14  PHE 14  879  879  PHE PHE F . n 
F 3 15  GLU 15  880  880  GLU GLU F . n 
F 3 16  THR 16  881  881  THR THR F . n 
F 3 17  ARG 17  882  882  ARG ARG F . n 
F 3 18  LYS 18  883  883  LYS LYS F . n 
F 3 19  GLY 19  884  884  GLY GLY F . n 
F 3 20  LEU 20  885  885  LEU LEU F . n 
F 3 21  SER 21  886  886  SER SER F . n 
F 3 22  SER 22  887  887  SER SER F . n 
F 3 23  HIS 23  888  888  HIS HIS F . n 
F 3 24  ALA 24  889  889  ALA ALA F . n 
F 3 25  ARG 25  890  890  ARG ARG F . n 
F 3 26  SER 26  891  891  SER SER F . n 
F 3 27  HIS 27  892  892  HIS HIS F . n 
F 3 28  LEU 28  893  893  LEU LEU F . n 
F 3 29  ARG 29  894  894  ARG ARG F . n 
F 3 30  GLN 30  895  ?    ?   ?   F . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A5I 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A5I 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 4 ZN    1 501  501  ZN    ZN  A . 
H 5 SO4   1 502  502  SO4   SO4 A . 
I 6 A1A5I 1 503  1    A1A5I LI1 A . 
J 4 ZN    1 900  900  ZN    ZN  C . 
K 4 ZN    1 501  501  ZN    ZN  D . 
L 5 SO4   1 502  502  SO4   SO4 D . 
M 6 A1A5I 1 503  1    A1A5I LI1 D . 
N 5 SO4   1 1201 1201 SO4   SO4 E . 
O 4 ZN    1 900  900  ZN    ZN  F . 
P 7 HOH   1 601  4    HOH   HOH A . 
P 7 HOH   2 602  2    HOH   HOH A . 
P 7 HOH   3 603  16   HOH   HOH A . 
P 7 HOH   4 604  1    HOH   HOH A . 
Q 7 HOH   1 1201 6    HOH   HOH B . 
Q 7 HOH   2 1202 17   HOH   HOH B . 
Q 7 HOH   3 1203 5    HOH   HOH B . 
Q 7 HOH   4 1204 7    HOH   HOH B . 
Q 7 HOH   5 1205 3    HOH   HOH B . 
R 7 HOH   1 1001 21   HOH   HOH C . 
R 7 HOH   2 1002 18   HOH   HOH C . 
R 7 HOH   3 1003 22   HOH   HOH C . 
S 7 HOH   1 601  20   HOH   HOH D . 
S 7 HOH   2 602  8    HOH   HOH D . 
S 7 HOH   3 603  10   HOH   HOH D . 
S 7 HOH   4 604  9    HOH   HOH D . 
T 7 HOH   1 1301 12   HOH   HOH E . 
T 7 HOH   2 1302 11   HOH   HOH E . 
T 7 HOH   3 1303 13   HOH   HOH E . 
T 7 HOH   4 1304 19   HOH   HOH E . 
T 7 HOH   5 1305 15   HOH   HOH E . 
T 7 HOH   6 1306 14   HOH   HOH E . 
# 
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 HIS 73   ? CG  ? A HIS 4   CG  
2   1 Y 1 A HIS 73   ? ND1 ? A HIS 4   ND1 
3   1 Y 1 A HIS 73   ? CD2 ? A HIS 4   CD2 
4   1 Y 1 A HIS 73   ? CE1 ? A HIS 4   CE1 
5   1 Y 1 A HIS 73   ? NE2 ? A HIS 4   NE2 
6   1 Y 1 A GLN 86   ? CG  ? A GLN 17  CG  
7   1 Y 1 A GLN 86   ? CD  ? A GLN 17  CD  
8   1 Y 1 A GLN 86   ? OE1 ? A GLN 17  OE1 
9   1 Y 1 A GLN 86   ? NE2 ? A GLN 17  NE2 
10  1 Y 1 A GLN 105  ? CG  ? A GLN 36  CG  
11  1 Y 1 A GLN 105  ? CD  ? A GLN 36  CD  
12  1 Y 1 A GLN 105  ? OE1 ? A GLN 36  OE1 
13  1 Y 1 A GLN 105  ? NE2 ? A GLN 36  NE2 
14  1 Y 1 A ARG 111  ? CG  ? A ARG 42  CG  
15  1 Y 1 A ARG 111  ? CD  ? A ARG 42  CD  
16  1 Y 1 A ARG 111  ? NE  ? A ARG 42  NE  
17  1 Y 1 A ARG 111  ? CZ  ? A ARG 42  CZ  
18  1 Y 1 A ARG 111  ? NH1 ? A ARG 42  NH1 
19  1 Y 1 A ARG 111  ? NH2 ? A ARG 42  NH2 
20  1 Y 1 A LYS 116  ? CG  ? A LYS 47  CG  
21  1 Y 1 A LYS 116  ? CD  ? A LYS 47  CD  
22  1 Y 1 A LYS 116  ? CE  ? A LYS 47  CE  
23  1 Y 1 A LYS 116  ? NZ  ? A LYS 47  NZ  
24  1 Y 1 A ARG 118  ? CG  ? A ARG 49  CG  
25  1 Y 1 A ARG 118  ? CD  ? A ARG 49  CD  
26  1 Y 1 A ARG 118  ? NE  ? A ARG 49  NE  
27  1 Y 1 A ARG 118  ? CZ  ? A ARG 49  CZ  
28  1 Y 1 A ARG 118  ? NH1 ? A ARG 49  NH1 
29  1 Y 1 A ARG 118  ? NH2 ? A ARG 49  NH2 
30  1 Y 1 A GLU 147  ? CG  ? A GLU 78  CG  
31  1 Y 1 A GLU 147  ? CD  ? A GLU 78  CD  
32  1 Y 1 A GLU 147  ? OE1 ? A GLU 78  OE1 
33  1 Y 1 A GLU 147  ? OE2 ? A GLU 78  OE2 
34  1 Y 1 A GLN 148  ? CG  ? A GLN 79  CG  
35  1 Y 1 A GLN 148  ? CD  ? A GLN 79  CD  
36  1 Y 1 A GLN 148  ? OE1 ? A GLN 79  OE1 
37  1 Y 1 A GLN 148  ? NE2 ? A GLN 79  NE2 
38  1 Y 1 A ASP 149  ? CG  ? A ASP 80  CG  
39  1 Y 1 A ASP 149  ? OD1 ? A ASP 80  OD1 
40  1 Y 1 A ASP 149  ? OD2 ? A ASP 80  OD2 
41  1 Y 1 A GLU 153  ? CG  ? A GLU 84  CG  
42  1 Y 1 A GLU 153  ? CD  ? A GLU 84  CD  
43  1 Y 1 A GLU 153  ? OE1 ? A GLU 84  OE1 
44  1 Y 1 A GLU 153  ? OE2 ? A GLU 84  OE2 
45  1 Y 1 A LYS 156  ? CG  ? A LYS 87  CG  
46  1 Y 1 A LYS 156  ? CD  ? A LYS 87  CD  
47  1 Y 1 A LYS 156  ? CE  ? A LYS 87  CE  
48  1 Y 1 A LYS 156  ? NZ  ? A LYS 87  NZ  
49  1 Y 1 A ARG 164  ? CG  ? A ARG 95  CG  
50  1 Y 1 A ARG 164  ? CD  ? A ARG 95  CD  
51  1 Y 1 A ARG 164  ? NE  ? A ARG 95  NE  
52  1 Y 1 A ARG 164  ? CZ  ? A ARG 95  CZ  
53  1 Y 1 A ARG 164  ? NH1 ? A ARG 95  NH1 
54  1 Y 1 A ARG 164  ? NH2 ? A ARG 95  NH2 
55  1 Y 1 A LYS 166  ? CG  ? A LYS 97  CG  
56  1 Y 1 A LYS 166  ? CD  ? A LYS 97  CD  
57  1 Y 1 A LYS 166  ? CE  ? A LYS 97  CE  
58  1 Y 1 A LYS 166  ? NZ  ? A LYS 97  NZ  
59  1 Y 1 A ASP 175  ? CG  ? A ASP 106 CG  
60  1 Y 1 A ASP 175  ? OD1 ? A ASP 106 OD1 
61  1 Y 1 A ASP 175  ? OD2 ? A ASP 106 OD2 
62  1 Y 1 A LYS 258  ? CG  ? A LYS 189 CG  
63  1 Y 1 A LYS 258  ? CD  ? A LYS 189 CD  
64  1 Y 1 A LYS 258  ? CE  ? A LYS 189 CE  
65  1 Y 1 A LYS 258  ? NZ  ? A LYS 189 NZ  
66  1 Y 1 A ARG 262  ? CG  ? A ARG 193 CG  
67  1 Y 1 A ARG 262  ? CD  ? A ARG 193 CD  
68  1 Y 1 A ARG 262  ? NE  ? A ARG 193 NE  
69  1 Y 1 A ARG 262  ? CZ  ? A ARG 193 CZ  
70  1 Y 1 A ARG 262  ? NH1 ? A ARG 193 NH1 
71  1 Y 1 A ARG 262  ? NH2 ? A ARG 193 NH2 
72  1 Y 1 A LYS 269  ? CG  ? A LYS 200 CG  
73  1 Y 1 A LYS 269  ? CD  ? A LYS 200 CD  
74  1 Y 1 A LYS 269  ? CE  ? A LYS 200 CE  
75  1 Y 1 A LYS 269  ? NZ  ? A LYS 200 NZ  
76  1 Y 1 A ASP 270  ? CG  ? A ASP 201 CG  
77  1 Y 1 A ASP 270  ? OD1 ? A ASP 201 OD1 
78  1 Y 1 A ASP 270  ? OD2 ? A ASP 201 OD2 
79  1 Y 1 A ASP 271  ? CG  ? A ASP 202 CG  
80  1 Y 1 A ASP 271  ? OD1 ? A ASP 202 OD1 
81  1 Y 1 A ASP 271  ? OD2 ? A ASP 202 OD2 
82  1 Y 1 A LYS 317  ? CG  ? A LYS 248 CG  
83  1 Y 1 A LYS 317  ? CD  ? A LYS 248 CD  
84  1 Y 1 A LYS 317  ? CE  ? A LYS 248 CE  
85  1 Y 1 A LYS 317  ? NZ  ? A LYS 248 NZ  
86  1 Y 1 A GLU 328  ? CG  ? A GLU 259 CG  
87  1 Y 1 A GLU 328  ? CD  ? A GLU 259 CD  
88  1 Y 1 A GLU 328  ? OE1 ? A GLU 259 OE1 
89  1 Y 1 A GLU 328  ? OE2 ? A GLU 259 OE2 
90  1 Y 1 A LYS 334  ? CG  ? A LYS 265 CG  
91  1 Y 1 A LYS 334  ? CD  ? A LYS 265 CD  
92  1 Y 1 A LYS 334  ? CE  ? A LYS 265 CE  
93  1 Y 1 A LYS 334  ? NZ  ? A LYS 265 NZ  
94  1 Y 1 A LYS 364  ? CG  ? A LYS 295 CG  
95  1 Y 1 A LYS 364  ? CD  ? A LYS 295 CD  
96  1 Y 1 A LYS 364  ? CE  ? A LYS 295 CE  
97  1 Y 1 A LYS 364  ? NZ  ? A LYS 295 NZ  
98  1 Y 1 A ARG 373  ? CG  ? A ARG 304 CG  
99  1 Y 1 A ARG 373  ? CD  ? A ARG 304 CD  
100 1 Y 1 A ARG 373  ? NE  ? A ARG 304 NE  
101 1 Y 1 A ARG 373  ? CZ  ? A ARG 304 CZ  
102 1 Y 1 A ARG 373  ? NH1 ? A ARG 304 NH1 
103 1 Y 1 A ARG 373  ? NH2 ? A ARG 304 NH2 
104 1 Y 1 A LYS 401  ? CG  ? A LYS 332 CG  
105 1 Y 1 A LYS 401  ? CD  ? A LYS 332 CD  
106 1 Y 1 A LYS 401  ? CE  ? A LYS 332 CE  
107 1 Y 1 A LYS 401  ? NZ  ? A LYS 332 NZ  
108 1 Y 1 A LYS 406  ? CG  ? A LYS 337 CG  
109 1 Y 1 A LYS 406  ? CD  ? A LYS 337 CD  
110 1 Y 1 A LYS 406  ? CE  ? A LYS 337 CE  
111 1 Y 1 A LYS 406  ? NZ  ? A LYS 337 NZ  
112 1 Y 1 A LYS 407  ? CG  ? A LYS 338 CG  
113 1 Y 1 A LYS 407  ? CD  ? A LYS 338 CD  
114 1 Y 1 A LYS 407  ? CE  ? A LYS 338 CE  
115 1 Y 1 A LYS 407  ? NZ  ? A LYS 338 NZ  
116 1 Y 1 A ASP 408  ? CG  ? A ASP 339 CG  
117 1 Y 1 A ASP 408  ? OD1 ? A ASP 339 OD1 
118 1 Y 1 A ASP 408  ? OD2 ? A ASP 339 OD2 
119 1 Y 1 A LYS 413  ? CG  ? A LYS 344 CG  
120 1 Y 1 A LYS 413  ? CD  ? A LYS 344 CD  
121 1 Y 1 A LYS 413  ? CE  ? A LYS 344 CE  
122 1 Y 1 A LYS 413  ? NZ  ? A LYS 344 NZ  
123 1 Y 1 B LYS 11   ? CG  ? B LYS 11  CG  
124 1 Y 1 B LYS 11   ? CD  ? B LYS 11  CD  
125 1 Y 1 B LYS 11   ? CE  ? B LYS 11  CE  
126 1 Y 1 B LYS 11   ? NZ  ? B LYS 11  NZ  
127 1 Y 1 B GLU 47   ? CG  ? B GLU 47  CG  
128 1 Y 1 B GLU 47   ? CD  ? B GLU 47  CD  
129 1 Y 1 B GLU 47   ? OE1 ? B GLU 47  OE1 
130 1 Y 1 B GLU 47   ? OE2 ? B GLU 47  OE2 
131 1 Y 1 B LYS 70   ? CG  ? B LYS 70  CG  
132 1 Y 1 B LYS 70   ? CD  ? B LYS 70  CD  
133 1 Y 1 B LYS 70   ? CE  ? B LYS 70  CE  
134 1 Y 1 B LYS 70   ? NZ  ? B LYS 70  NZ  
135 1 Y 1 B LYS 92   ? CG  ? B LYS 92  CG  
136 1 Y 1 B LYS 92   ? CD  ? B LYS 92  CD  
137 1 Y 1 B LYS 92   ? CE  ? B LYS 92  CE  
138 1 Y 1 B LYS 92   ? NZ  ? B LYS 92  NZ  
139 1 Y 1 B GLU 96   ? CG  ? B GLU 96  CG  
140 1 Y 1 B GLU 96   ? CD  ? B GLU 96  CD  
141 1 Y 1 B GLU 96   ? OE1 ? B GLU 96  OE1 
142 1 Y 1 B GLU 96   ? OE2 ? B GLU 96  OE2 
143 1 Y 1 B ARG 111  ? CG  ? B ARG 111 CG  
144 1 Y 1 B ARG 111  ? CD  ? B ARG 111 CD  
145 1 Y 1 B ARG 111  ? NE  ? B ARG 111 NE  
146 1 Y 1 B ARG 111  ? CZ  ? B ARG 111 CZ  
147 1 Y 1 B ARG 111  ? NH1 ? B ARG 111 NH1 
148 1 Y 1 B ARG 111  ? NH2 ? B ARG 111 NH2 
149 1 Y 1 B ARG 147  ? CG  ? B ARG 147 CG  
150 1 Y 1 B ARG 147  ? CD  ? B ARG 147 CD  
151 1 Y 1 B ARG 147  ? NE  ? B ARG 147 NE  
152 1 Y 1 B ARG 147  ? CZ  ? B ARG 147 CZ  
153 1 Y 1 B ARG 147  ? NH1 ? B ARG 147 NH1 
154 1 Y 1 B ARG 147  ? NH2 ? B ARG 147 NH2 
155 1 Y 1 B LYS 150  ? CG  ? B LYS 150 CG  
156 1 Y 1 B LYS 150  ? CD  ? B LYS 150 CD  
157 1 Y 1 B LYS 150  ? CE  ? B LYS 150 CE  
158 1 Y 1 B LYS 150  ? NZ  ? B LYS 150 NZ  
159 1 Y 1 B LYS 153  ? CG  ? B LYS 153 CG  
160 1 Y 1 B LYS 153  ? CD  ? B LYS 153 CD  
161 1 Y 1 B LYS 153  ? CE  ? B LYS 153 CE  
162 1 Y 1 B LYS 153  ? NZ  ? B LYS 153 NZ  
163 1 Y 1 B GLU 160  ? CG  ? B GLU 160 CG  
164 1 Y 1 B GLU 160  ? CD  ? B GLU 160 CD  
165 1 Y 1 B GLU 160  ? OE1 ? B GLU 160 OE1 
166 1 Y 1 B GLU 160  ? OE2 ? B GLU 160 OE2 
167 1 Y 1 B ARG 198  ? CG  ? B ARG 198 CG  
168 1 Y 1 B ARG 198  ? CD  ? B ARG 198 CD  
169 1 Y 1 B ARG 198  ? NE  ? B ARG 198 NE  
170 1 Y 1 B ARG 198  ? CZ  ? B ARG 198 CZ  
171 1 Y 1 B ARG 198  ? NH1 ? B ARG 198 NH1 
172 1 Y 1 B ARG 198  ? NH2 ? B ARG 198 NH2 
173 1 Y 1 B LYS 200  ? CG  ? B LYS 200 CG  
174 1 Y 1 B LYS 200  ? CD  ? B LYS 200 CD  
175 1 Y 1 B LYS 200  ? CE  ? B LYS 200 CE  
176 1 Y 1 B LYS 200  ? NZ  ? B LYS 200 NZ  
177 1 Y 1 B GLU 201  ? CG  ? B GLU 201 CG  
178 1 Y 1 B GLU 201  ? CD  ? B GLU 201 CD  
179 1 Y 1 B GLU 201  ? OE1 ? B GLU 201 OE1 
180 1 Y 1 B GLU 201  ? OE2 ? B GLU 201 OE2 
181 1 Y 1 B LYS 204  ? CG  ? B LYS 204 CG  
182 1 Y 1 B LYS 204  ? CD  ? B LYS 204 CD  
183 1 Y 1 B LYS 204  ? CE  ? B LYS 204 CE  
184 1 Y 1 B LYS 204  ? NZ  ? B LYS 204 NZ  
185 1 Y 1 B GLN 209  ? CG  ? B GLN 209 CG  
186 1 Y 1 B GLN 209  ? CD  ? B GLN 209 CD  
187 1 Y 1 B GLN 209  ? OE1 ? B GLN 209 OE1 
188 1 Y 1 B GLN 209  ? NE2 ? B GLN 209 NE2 
189 1 Y 1 B GLU 210  ? CG  ? B GLU 210 CG  
190 1 Y 1 B GLU 210  ? CD  ? B GLU 210 CD  
191 1 Y 1 B GLU 210  ? OE1 ? B GLU 210 OE1 
192 1 Y 1 B GLU 210  ? OE2 ? B GLU 210 OE2 
193 1 Y 1 B GLU 215  ? CG  ? B GLU 215 CG  
194 1 Y 1 B GLU 215  ? CD  ? B GLU 215 CD  
195 1 Y 1 B GLU 215  ? OE1 ? B GLU 215 OE1 
196 1 Y 1 B GLU 215  ? OE2 ? B GLU 215 OE2 
197 1 Y 1 B PHE 226  ? CG  ? B PHE 226 CG  
198 1 Y 1 B PHE 226  ? CD1 ? B PHE 226 CD1 
199 1 Y 1 B PHE 226  ? CD2 ? B PHE 226 CD2 
200 1 Y 1 B PHE 226  ? CE1 ? B PHE 226 CE1 
201 1 Y 1 B PHE 226  ? CE2 ? B PHE 226 CE2 
202 1 Y 1 B PHE 226  ? CZ  ? B PHE 226 CZ  
203 1 Y 1 B GLN 234  ? CG  ? B GLN 234 CG  
204 1 Y 1 B GLN 234  ? CD  ? B GLN 234 CD  
205 1 Y 1 B GLN 234  ? OE1 ? B GLN 234 OE1 
206 1 Y 1 B GLN 234  ? NE2 ? B GLN 234 NE2 
207 1 Y 1 B GLU 235  ? CG  ? B GLU 235 CG  
208 1 Y 1 B GLU 235  ? CD  ? B GLU 235 CD  
209 1 Y 1 B GLU 235  ? OE1 ? B GLU 235 OE1 
210 1 Y 1 B GLU 235  ? OE2 ? B GLU 235 OE2 
211 1 Y 1 B ASP 243  ? CG  ? B ASP 243 CG  
212 1 Y 1 B ASP 243  ? OD1 ? B ASP 243 OD1 
213 1 Y 1 B ASP 243  ? OD2 ? B ASP 243 OD2 
214 1 Y 1 B LYS 244  ? CG  ? B LYS 244 CG  
215 1 Y 1 B LYS 244  ? CD  ? B LYS 244 CD  
216 1 Y 1 B LYS 244  ? CE  ? B LYS 244 CE  
217 1 Y 1 B LYS 244  ? NZ  ? B LYS 244 NZ  
218 1 Y 1 B LYS 254  ? CG  ? B LYS 254 CG  
219 1 Y 1 B LYS 254  ? CD  ? B LYS 254 CD  
220 1 Y 1 B LYS 254  ? CE  ? B LYS 254 CE  
221 1 Y 1 B LYS 254  ? NZ  ? B LYS 254 NZ  
222 1 Y 1 B GLN 255  ? CG  ? B GLN 255 CG  
223 1 Y 1 B GLN 255  ? CD  ? B GLN 255 CD  
224 1 Y 1 B GLN 255  ? OE1 ? B GLN 255 OE1 
225 1 Y 1 B GLN 255  ? NE2 ? B GLN 255 NE2 
226 1 Y 1 B GLU 286  ? CG  ? B GLU 286 CG  
227 1 Y 1 B GLU 286  ? CD  ? B GLU 286 CD  
228 1 Y 1 B GLU 286  ? OE1 ? B GLU 286 OE1 
229 1 Y 1 B GLU 286  ? OE2 ? B GLU 286 OE2 
230 1 Y 1 B LYS 287  ? CG  ? B LYS 287 CG  
231 1 Y 1 B LYS 287  ? CD  ? B LYS 287 CD  
232 1 Y 1 B LYS 287  ? CE  ? B LYS 287 CE  
233 1 Y 1 B LYS 287  ? NZ  ? B LYS 287 NZ  
234 1 Y 1 B GLU 288  ? CG  ? B GLU 288 CG  
235 1 Y 1 B GLU 288  ? CD  ? B GLU 288 CD  
236 1 Y 1 B GLU 288  ? OE1 ? B GLU 288 OE1 
237 1 Y 1 B GLU 288  ? OE2 ? B GLU 288 OE2 
238 1 Y 1 B GLU 289  ? CG  ? B GLU 289 CG  
239 1 Y 1 B GLU 289  ? CD  ? B GLU 289 CD  
240 1 Y 1 B GLU 289  ? OE1 ? B GLU 289 OE1 
241 1 Y 1 B GLU 289  ? OE2 ? B GLU 289 OE2 
242 1 Y 1 B THR 294  ? OG1 ? B THR 294 OG1 
243 1 Y 1 B THR 294  ? CG2 ? B THR 294 CG2 
244 1 Y 1 B LYS 298  ? CG  ? B LYS 298 CG  
245 1 Y 1 B LYS 298  ? CD  ? B LYS 298 CD  
246 1 Y 1 B LYS 298  ? CE  ? B LYS 298 CE  
247 1 Y 1 B LYS 298  ? NZ  ? B LYS 298 NZ  
248 1 Y 1 B LYS 335  ? CG  ? B LYS 335 CG  
249 1 Y 1 B LYS 335  ? CD  ? B LYS 335 CD  
250 1 Y 1 B LYS 335  ? CE  ? B LYS 335 CE  
251 1 Y 1 B LYS 335  ? NZ  ? B LYS 335 NZ  
252 1 Y 1 B ASP 339  ? CG  ? B ASP 339 CG  
253 1 Y 1 B ASP 339  ? OD1 ? B ASP 339 OD1 
254 1 Y 1 B ASP 339  ? OD2 ? B ASP 339 OD2 
255 1 Y 1 B GLN 731  ? CG  ? B GLN 427 CG  
256 1 Y 1 B GLN 731  ? CD  ? B GLN 427 CD  
257 1 Y 1 B GLN 731  ? OE1 ? B GLN 427 OE1 
258 1 Y 1 B GLN 731  ? NE2 ? B GLN 427 NE2 
259 1 Y 1 B LYS 769  ? CG  ? B LYS 465 CG  
260 1 Y 1 B LYS 769  ? CD  ? B LYS 465 CD  
261 1 Y 1 B LYS 769  ? CE  ? B LYS 465 CE  
262 1 Y 1 B LYS 769  ? NZ  ? B LYS 465 NZ  
263 1 Y 1 B LYS 820  ? CG  ? B LYS 516 CG  
264 1 Y 1 B LYS 820  ? CD  ? B LYS 516 CD  
265 1 Y 1 B LYS 820  ? CE  ? B LYS 516 CE  
266 1 Y 1 B LYS 820  ? NZ  ? B LYS 516 NZ  
267 1 Y 1 B GLU 840  ? CG  ? B GLU 536 CG  
268 1 Y 1 B GLU 840  ? CD  ? B GLU 536 CD  
269 1 Y 1 B GLU 840  ? OE1 ? B GLU 536 OE1 
270 1 Y 1 B GLU 840  ? OE2 ? B GLU 536 OE2 
271 1 Y 1 B LYS 844  ? CG  ? B LYS 540 CG  
272 1 Y 1 B LYS 844  ? CD  ? B LYS 540 CD  
273 1 Y 1 B LYS 844  ? CE  ? B LYS 540 CE  
274 1 Y 1 B LYS 844  ? NZ  ? B LYS 540 NZ  
275 1 Y 1 B ARG 847  ? CG  ? B ARG 543 CG  
276 1 Y 1 B ARG 847  ? CD  ? B ARG 543 CD  
277 1 Y 1 B ARG 847  ? NE  ? B ARG 543 NE  
278 1 Y 1 B ARG 847  ? CZ  ? B ARG 543 CZ  
279 1 Y 1 B ARG 847  ? NH1 ? B ARG 543 NH1 
280 1 Y 1 B ARG 847  ? NH2 ? B ARG 543 NH2 
281 1 Y 1 B ASP 855  ? CG  ? B ASP 551 CG  
282 1 Y 1 B ASP 855  ? OD1 ? B ASP 551 OD1 
283 1 Y 1 B ASP 855  ? OD2 ? B ASP 551 OD2 
284 1 Y 1 B LYS 857  ? CG  ? B LYS 553 CG  
285 1 Y 1 B LYS 857  ? CD  ? B LYS 553 CD  
286 1 Y 1 B LYS 857  ? CE  ? B LYS 553 CE  
287 1 Y 1 B LYS 857  ? NZ  ? B LYS 553 NZ  
288 1 Y 1 B GLN 859  ? CG  ? B GLN 555 CG  
289 1 Y 1 B GLN 859  ? CD  ? B GLN 555 CD  
290 1 Y 1 B GLN 859  ? OE1 ? B GLN 555 OE1 
291 1 Y 1 B GLN 859  ? NE2 ? B GLN 555 NE2 
292 1 Y 1 B GLU 863  ? CG  ? B GLU 559 CG  
293 1 Y 1 B GLU 863  ? CD  ? B GLU 559 CD  
294 1 Y 1 B GLU 863  ? OE1 ? B GLU 559 OE1 
295 1 Y 1 B GLU 863  ? OE2 ? B GLU 559 OE2 
296 1 Y 1 B LYS 864  ? CG  ? B LYS 560 CG  
297 1 Y 1 B LYS 864  ? CD  ? B LYS 560 CD  
298 1 Y 1 B LYS 864  ? CE  ? B LYS 560 CE  
299 1 Y 1 B LYS 864  ? NZ  ? B LYS 560 NZ  
300 1 Y 1 B LYS 867  ? CG  ? B LYS 563 CG  
301 1 Y 1 B LYS 867  ? CD  ? B LYS 563 CD  
302 1 Y 1 B LYS 867  ? CE  ? B LYS 563 CE  
303 1 Y 1 B LYS 867  ? NZ  ? B LYS 563 NZ  
304 1 Y 1 B LYS 879  ? CG  ? B LYS 575 CG  
305 1 Y 1 B LYS 879  ? CD  ? B LYS 575 CD  
306 1 Y 1 B LYS 879  ? CE  ? B LYS 575 CE  
307 1 Y 1 B LYS 879  ? NZ  ? B LYS 575 NZ  
308 1 Y 1 B LYS 897  ? CG  ? B LYS 593 CG  
309 1 Y 1 B LYS 897  ? CD  ? B LYS 593 CD  
310 1 Y 1 B LYS 897  ? CE  ? B LYS 593 CE  
311 1 Y 1 B LYS 897  ? NZ  ? B LYS 593 NZ  
312 1 Y 1 B LYS 936  ? CG  ? B LYS 632 CG  
313 1 Y 1 B LYS 936  ? CD  ? B LYS 632 CD  
314 1 Y 1 B LYS 936  ? CE  ? B LYS 632 CE  
315 1 Y 1 B LYS 936  ? NZ  ? B LYS 632 NZ  
316 1 Y 1 B MET 938  ? CG  ? B MET 634 CG  
317 1 Y 1 B MET 938  ? SD  ? B MET 634 SD  
318 1 Y 1 B MET 938  ? CE  ? B MET 634 CE  
319 1 Y 1 B GLU 939  ? CG  ? B GLU 635 CG  
320 1 Y 1 B GLU 939  ? CD  ? B GLU 635 CD  
321 1 Y 1 B GLU 939  ? OE1 ? B GLU 635 OE1 
322 1 Y 1 B GLU 939  ? OE2 ? B GLU 635 OE2 
323 1 Y 1 B GLU 943  ? CG  ? B GLU 639 CG  
324 1 Y 1 B GLU 943  ? CD  ? B GLU 639 CD  
325 1 Y 1 B GLU 943  ? OE1 ? B GLU 639 OE1 
326 1 Y 1 B GLU 943  ? OE2 ? B GLU 639 OE2 
327 1 Y 1 B ARG 947  ? CG  ? B ARG 643 CG  
328 1 Y 1 B ARG 947  ? CD  ? B ARG 643 CD  
329 1 Y 1 B ARG 947  ? NE  ? B ARG 643 NE  
330 1 Y 1 B ARG 947  ? CZ  ? B ARG 643 CZ  
331 1 Y 1 B ARG 947  ? NH1 ? B ARG 643 NH1 
332 1 Y 1 B ARG 947  ? NH2 ? B ARG 643 NH2 
333 1 Y 1 B ARG 1057 ? CG  ? B ARG 753 CG  
334 1 Y 1 B ARG 1057 ? CD  ? B ARG 753 CD  
335 1 Y 1 B ARG 1057 ? NE  ? B ARG 753 NE  
336 1 Y 1 B ARG 1057 ? CZ  ? B ARG 753 CZ  
337 1 Y 1 B ARG 1057 ? NH1 ? B ARG 753 NH1 
338 1 Y 1 B ARG 1057 ? NH2 ? B ARG 753 NH2 
339 1 Y 1 B LYS 1060 ? CG  ? B LYS 756 CG  
340 1 Y 1 B LYS 1060 ? CD  ? B LYS 756 CD  
341 1 Y 1 B LYS 1060 ? CE  ? B LYS 756 CE  
342 1 Y 1 B LYS 1060 ? NZ  ? B LYS 756 NZ  
343 1 Y 1 B LYS 1063 ? CG  ? B LYS 759 CG  
344 1 Y 1 B LYS 1063 ? CD  ? B LYS 759 CD  
345 1 Y 1 B LYS 1063 ? CE  ? B LYS 759 CE  
346 1 Y 1 B LYS 1063 ? NZ  ? B LYS 759 NZ  
347 1 Y 1 B LYS 1067 ? CG  ? B LYS 763 CG  
348 1 Y 1 B LYS 1067 ? CD  ? B LYS 763 CD  
349 1 Y 1 B LYS 1067 ? CE  ? B LYS 763 CE  
350 1 Y 1 B LYS 1067 ? NZ  ? B LYS 763 NZ  
351 1 Y 1 B ARG 1080 ? CG  ? B ARG 776 CG  
352 1 Y 1 B ARG 1080 ? CD  ? B ARG 776 CD  
353 1 Y 1 B ARG 1080 ? NE  ? B ARG 776 NE  
354 1 Y 1 B ARG 1080 ? CZ  ? B ARG 776 CZ  
355 1 Y 1 B ARG 1080 ? NH1 ? B ARG 776 NH1 
356 1 Y 1 B ARG 1080 ? NH2 ? B ARG 776 NH2 
357 1 Y 1 B LYS 1081 ? CG  ? B LYS 777 CG  
358 1 Y 1 B LYS 1081 ? CD  ? B LYS 777 CD  
359 1 Y 1 B LYS 1081 ? CE  ? B LYS 777 CE  
360 1 Y 1 B LYS 1081 ? NZ  ? B LYS 777 NZ  
361 1 Y 1 B GLU 1083 ? CG  ? B GLU 779 CG  
362 1 Y 1 B GLU 1083 ? CD  ? B GLU 779 CD  
363 1 Y 1 B GLU 1083 ? OE1 ? B GLU 779 OE1 
364 1 Y 1 B GLU 1083 ? OE2 ? B GLU 779 OE2 
365 1 Y 1 B GLU 1107 ? CG  ? B GLU 803 CG  
366 1 Y 1 B GLU 1107 ? CD  ? B GLU 803 CD  
367 1 Y 1 B GLU 1107 ? OE1 ? B GLU 803 OE1 
368 1 Y 1 B GLU 1107 ? OE2 ? B GLU 803 OE2 
369 1 Y 1 B ASN 1111 ? CG  ? B ASN 807 CG  
370 1 Y 1 B ASN 1111 ? OD1 ? B ASN 807 OD1 
371 1 Y 1 B ASN 1111 ? ND2 ? B ASN 807 ND2 
372 1 Y 1 B GLU 1123 ? CG  ? B GLU 819 CG  
373 1 Y 1 B GLU 1123 ? CD  ? B GLU 819 CD  
374 1 Y 1 B GLU 1123 ? OE1 ? B GLU 819 OE1 
375 1 Y 1 B GLU 1123 ? OE2 ? B GLU 819 OE2 
376 1 Y 1 B LYS 1131 ? CG  ? B LYS 827 CG  
377 1 Y 1 B LYS 1131 ? CD  ? B LYS 827 CD  
378 1 Y 1 B LYS 1131 ? CE  ? B LYS 827 CE  
379 1 Y 1 B LYS 1131 ? NZ  ? B LYS 827 NZ  
380 1 Y 1 B GLU 1134 ? CG  ? B GLU 830 CG  
381 1 Y 1 B GLU 1134 ? CD  ? B GLU 830 CD  
382 1 Y 1 B GLU 1134 ? OE1 ? B GLU 830 OE1 
383 1 Y 1 B GLU 1134 ? OE2 ? B GLU 830 OE2 
384 1 Y 1 B GLU 1135 ? CG  ? B GLU 831 CG  
385 1 Y 1 B GLU 1135 ? CD  ? B GLU 831 CD  
386 1 Y 1 B GLU 1135 ? OE1 ? B GLU 831 OE1 
387 1 Y 1 B GLU 1135 ? OE2 ? B GLU 831 OE2 
388 1 Y 1 B ARG 1138 ? CG  ? B ARG 834 CG  
389 1 Y 1 B ARG 1138 ? CD  ? B ARG 834 CD  
390 1 Y 1 B ARG 1138 ? NE  ? B ARG 834 NE  
391 1 Y 1 B ARG 1138 ? CZ  ? B ARG 834 CZ  
392 1 Y 1 B ARG 1138 ? NH1 ? B ARG 834 NH1 
393 1 Y 1 B ARG 1138 ? NH2 ? B ARG 834 NH2 
394 1 Y 1 C ARG 882  ? CG  ? C ARG 17  CG  
395 1 Y 1 C ARG 882  ? CD  ? C ARG 17  CD  
396 1 Y 1 C ARG 882  ? NE  ? C ARG 17  NE  
397 1 Y 1 C ARG 882  ? CZ  ? C ARG 17  CZ  
398 1 Y 1 C ARG 882  ? NH1 ? C ARG 17  NH1 
399 1 Y 1 C ARG 882  ? NH2 ? C ARG 17  NH2 
400 1 Y 1 C LYS 883  ? CG  ? C LYS 18  CG  
401 1 Y 1 C LYS 883  ? CD  ? C LYS 18  CD  
402 1 Y 1 C LYS 883  ? CE  ? C LYS 18  CE  
403 1 Y 1 C LYS 883  ? NZ  ? C LYS 18  NZ  
404 1 Y 1 C ARG 890  ? CG  ? C ARG 25  CG  
405 1 Y 1 C ARG 890  ? CD  ? C ARG 25  CD  
406 1 Y 1 C ARG 890  ? NE  ? C ARG 25  NE  
407 1 Y 1 C ARG 890  ? CZ  ? C ARG 25  CZ  
408 1 Y 1 C ARG 890  ? NH1 ? C ARG 25  NH1 
409 1 Y 1 C ARG 890  ? NH2 ? C ARG 25  NH2 
410 1 Y 1 D GLN 100  ? CG  ? D GLN 31  CG  
411 1 Y 1 D GLN 100  ? CD  ? D GLN 31  CD  
412 1 Y 1 D GLN 100  ? OE1 ? D GLN 31  OE1 
413 1 Y 1 D GLN 100  ? NE2 ? D GLN 31  NE2 
414 1 Y 1 D PHE 102  ? CG  ? D PHE 33  CG  
415 1 Y 1 D PHE 102  ? CD1 ? D PHE 33  CD1 
416 1 Y 1 D PHE 102  ? CD2 ? D PHE 33  CD2 
417 1 Y 1 D PHE 102  ? CE1 ? D PHE 33  CE1 
418 1 Y 1 D PHE 102  ? CE2 ? D PHE 33  CE2 
419 1 Y 1 D PHE 102  ? CZ  ? D PHE 33  CZ  
420 1 Y 1 D HIS 103  ? CG  ? D HIS 34  CG  
421 1 Y 1 D HIS 103  ? ND1 ? D HIS 34  ND1 
422 1 Y 1 D HIS 103  ? CD2 ? D HIS 34  CD2 
423 1 Y 1 D HIS 103  ? CE1 ? D HIS 34  CE1 
424 1 Y 1 D HIS 103  ? NE2 ? D HIS 34  NE2 
425 1 Y 1 D GLN 105  ? CG  ? D GLN 36  CG  
426 1 Y 1 D GLN 105  ? CD  ? D GLN 36  CD  
427 1 Y 1 D GLN 105  ? OE1 ? D GLN 36  OE1 
428 1 Y 1 D GLN 105  ? NE2 ? D GLN 36  NE2 
429 1 Y 1 D GLU 106  ? CG  ? D GLU 37  CG  
430 1 Y 1 D GLU 106  ? CD  ? D GLU 37  CD  
431 1 Y 1 D GLU 106  ? OE1 ? D GLU 37  OE1 
432 1 Y 1 D GLU 106  ? OE2 ? D GLU 37  OE2 
433 1 Y 1 D MET 109  ? CG  ? D MET 40  CG  
434 1 Y 1 D MET 109  ? SD  ? D MET 40  SD  
435 1 Y 1 D MET 109  ? CE  ? D MET 40  CE  
436 1 Y 1 D ARG 111  ? CG  ? D ARG 42  CG  
437 1 Y 1 D ARG 111  ? CD  ? D ARG 42  CD  
438 1 Y 1 D ARG 111  ? NE  ? D ARG 42  NE  
439 1 Y 1 D ARG 111  ? CZ  ? D ARG 42  CZ  
440 1 Y 1 D ARG 111  ? NH1 ? D ARG 42  NH1 
441 1 Y 1 D ARG 111  ? NH2 ? D ARG 42  NH2 
442 1 Y 1 D GLN 115  ? CG  ? D GLN 46  CG  
443 1 Y 1 D GLN 115  ? CD  ? D GLN 46  CD  
444 1 Y 1 D GLN 115  ? OE1 ? D GLN 46  OE1 
445 1 Y 1 D GLN 115  ? NE2 ? D GLN 46  NE2 
446 1 Y 1 D LYS 116  ? CG  ? D LYS 47  CG  
447 1 Y 1 D LYS 116  ? CD  ? D LYS 47  CD  
448 1 Y 1 D LYS 116  ? CE  ? D LYS 47  CE  
449 1 Y 1 D LYS 116  ? NZ  ? D LYS 47  NZ  
450 1 Y 1 D ARG 118  ? CG  ? D ARG 49  CG  
451 1 Y 1 D ARG 118  ? CD  ? D ARG 49  CD  
452 1 Y 1 D ARG 118  ? NE  ? D ARG 49  NE  
453 1 Y 1 D ARG 118  ? CZ  ? D ARG 49  CZ  
454 1 Y 1 D ARG 118  ? NH1 ? D ARG 49  NH1 
455 1 Y 1 D ARG 118  ? NH2 ? D ARG 49  NH2 
456 1 Y 1 D ARG 145  ? CG  ? D ARG 76  CG  
457 1 Y 1 D ARG 145  ? CD  ? D ARG 76  CD  
458 1 Y 1 D ARG 145  ? NE  ? D ARG 76  NE  
459 1 Y 1 D ARG 145  ? CZ  ? D ARG 76  CZ  
460 1 Y 1 D ARG 145  ? NH1 ? D ARG 76  NH1 
461 1 Y 1 D ARG 145  ? NH2 ? D ARG 76  NH2 
462 1 Y 1 D GLU 153  ? CG  ? D GLU 84  CG  
463 1 Y 1 D GLU 153  ? CD  ? D GLU 84  CD  
464 1 Y 1 D GLU 153  ? OE1 ? D GLU 84  OE1 
465 1 Y 1 D GLU 153  ? OE2 ? D GLU 84  OE2 
466 1 Y 1 D LYS 156  ? CG  ? D LYS 87  CG  
467 1 Y 1 D LYS 156  ? CD  ? D LYS 87  CD  
468 1 Y 1 D LYS 156  ? CE  ? D LYS 87  CE  
469 1 Y 1 D LYS 156  ? NZ  ? D LYS 87  NZ  
470 1 Y 1 D LYS 158  ? CG  ? D LYS 89  CG  
471 1 Y 1 D LYS 158  ? CD  ? D LYS 89  CD  
472 1 Y 1 D LYS 158  ? CE  ? D LYS 89  CE  
473 1 Y 1 D LYS 158  ? NZ  ? D LYS 89  NZ  
474 1 Y 1 D LYS 166  ? CG  ? D LYS 97  CG  
475 1 Y 1 D LYS 166  ? CD  ? D LYS 97  CD  
476 1 Y 1 D LYS 166  ? CE  ? D LYS 97  CE  
477 1 Y 1 D LYS 166  ? NZ  ? D LYS 97  NZ  
478 1 Y 1 D GLU 169  ? CG  ? D GLU 100 CG  
479 1 Y 1 D GLU 169  ? CD  ? D GLU 100 CD  
480 1 Y 1 D GLU 169  ? OE1 ? D GLU 100 OE1 
481 1 Y 1 D GLU 169  ? OE2 ? D GLU 100 OE2 
482 1 Y 1 D ARG 171  ? CG  ? D ARG 102 CG  
483 1 Y 1 D ARG 171  ? CD  ? D ARG 102 CD  
484 1 Y 1 D ARG 171  ? NE  ? D ARG 102 NE  
485 1 Y 1 D ARG 171  ? CZ  ? D ARG 102 CZ  
486 1 Y 1 D ARG 171  ? NH1 ? D ARG 102 NH1 
487 1 Y 1 D ARG 171  ? NH2 ? D ARG 102 NH2 
488 1 Y 1 D GLN 179  ? CG  ? D GLN 110 CG  
489 1 Y 1 D GLN 179  ? CD  ? D GLN 110 CD  
490 1 Y 1 D GLN 179  ? OE1 ? D GLN 110 OE1 
491 1 Y 1 D GLN 179  ? NE2 ? D GLN 110 NE2 
492 1 Y 1 D LYS 181  ? CG  ? D LYS 112 CG  
493 1 Y 1 D LYS 181  ? CD  ? D LYS 112 CD  
494 1 Y 1 D LYS 181  ? CE  ? D LYS 112 CE  
495 1 Y 1 D LYS 181  ? NZ  ? D LYS 112 NZ  
496 1 Y 1 D GLN 183  ? CG  ? D GLN 114 CG  
497 1 Y 1 D GLN 183  ? CD  ? D GLN 114 CD  
498 1 Y 1 D GLN 183  ? OE1 ? D GLN 114 OE1 
499 1 Y 1 D GLN 183  ? NE2 ? D GLN 114 NE2 
500 1 Y 1 D LYS 211  ? CG  ? D LYS 142 CG  
501 1 Y 1 D LYS 211  ? CD  ? D LYS 142 CD  
502 1 Y 1 D LYS 211  ? CE  ? D LYS 142 CE  
503 1 Y 1 D LYS 211  ? NZ  ? D LYS 142 NZ  
504 1 Y 1 D TYR 221  ? CG  ? D TYR 152 CG  
505 1 Y 1 D TYR 221  ? CD1 ? D TYR 152 CD1 
506 1 Y 1 D TYR 221  ? CD2 ? D TYR 152 CD2 
507 1 Y 1 D TYR 221  ? CE1 ? D TYR 152 CE1 
508 1 Y 1 D TYR 221  ? CE2 ? D TYR 152 CE2 
509 1 Y 1 D TYR 221  ? CZ  ? D TYR 152 CZ  
510 1 Y 1 D TYR 221  ? OH  ? D TYR 152 OH  
511 1 Y 1 D LYS 222  ? CG  ? D LYS 153 CG  
512 1 Y 1 D LYS 222  ? CD  ? D LYS 153 CD  
513 1 Y 1 D LYS 222  ? CE  ? D LYS 153 CE  
514 1 Y 1 D LYS 222  ? NZ  ? D LYS 153 NZ  
515 1 Y 1 D LYS 226  ? CG  ? D LYS 157 CG  
516 1 Y 1 D LYS 226  ? CD  ? D LYS 157 CD  
517 1 Y 1 D LYS 226  ? CE  ? D LYS 157 CE  
518 1 Y 1 D LYS 226  ? NZ  ? D LYS 157 NZ  
519 1 Y 1 D LYS 229  ? CG  ? D LYS 160 CG  
520 1 Y 1 D LYS 229  ? CD  ? D LYS 160 CD  
521 1 Y 1 D LYS 229  ? CE  ? D LYS 160 CE  
522 1 Y 1 D LYS 229  ? NZ  ? D LYS 160 NZ  
523 1 Y 1 D ARG 230  ? CG  ? D ARG 161 CG  
524 1 Y 1 D ARG 230  ? CD  ? D ARG 161 CD  
525 1 Y 1 D ARG 230  ? NE  ? D ARG 161 NE  
526 1 Y 1 D ARG 230  ? CZ  ? D ARG 161 CZ  
527 1 Y 1 D ARG 230  ? NH1 ? D ARG 161 NH1 
528 1 Y 1 D ARG 230  ? NH2 ? D ARG 161 NH2 
529 1 Y 1 D LYS 259  ? CG  ? D LYS 190 CG  
530 1 Y 1 D LYS 259  ? CD  ? D LYS 190 CD  
531 1 Y 1 D LYS 259  ? CE  ? D LYS 190 CE  
532 1 Y 1 D LYS 259  ? NZ  ? D LYS 190 NZ  
533 1 Y 1 D ARG 262  ? CG  ? D ARG 193 CG  
534 1 Y 1 D ARG 262  ? CD  ? D ARG 193 CD  
535 1 Y 1 D ARG 262  ? NE  ? D ARG 193 NE  
536 1 Y 1 D ARG 262  ? CZ  ? D ARG 193 CZ  
537 1 Y 1 D ARG 262  ? NH1 ? D ARG 193 NH1 
538 1 Y 1 D ARG 262  ? NH2 ? D ARG 193 NH2 
539 1 Y 1 D LYS 269  ? CG  ? D LYS 200 CG  
540 1 Y 1 D LYS 269  ? CD  ? D LYS 200 CD  
541 1 Y 1 D LYS 269  ? CE  ? D LYS 200 CE  
542 1 Y 1 D LYS 269  ? NZ  ? D LYS 200 NZ  
543 1 Y 1 D ASP 271  ? CG  ? D ASP 202 CG  
544 1 Y 1 D ASP 271  ? OD1 ? D ASP 202 OD1 
545 1 Y 1 D ASP 271  ? OD2 ? D ASP 202 OD2 
546 1 Y 1 D GLU 328  ? CG  ? D GLU 259 CG  
547 1 Y 1 D GLU 328  ? CD  ? D GLU 259 CD  
548 1 Y 1 D GLU 328  ? OE1 ? D GLU 259 OE1 
549 1 Y 1 D GLU 328  ? OE2 ? D GLU 259 OE2 
550 1 Y 1 D LYS 334  ? CG  ? D LYS 265 CG  
551 1 Y 1 D LYS 334  ? CD  ? D LYS 265 CD  
552 1 Y 1 D LYS 334  ? CE  ? D LYS 265 CE  
553 1 Y 1 D LYS 334  ? NZ  ? D LYS 265 NZ  
554 1 Y 1 D LYS 364  ? CG  ? D LYS 295 CG  
555 1 Y 1 D LYS 364  ? CD  ? D LYS 295 CD  
556 1 Y 1 D LYS 364  ? CE  ? D LYS 295 CE  
557 1 Y 1 D LYS 364  ? NZ  ? D LYS 295 NZ  
558 1 Y 1 D ARG 373  ? CG  ? D ARG 304 CG  
559 1 Y 1 D ARG 373  ? CD  ? D ARG 304 CD  
560 1 Y 1 D ARG 373  ? NE  ? D ARG 304 NE  
561 1 Y 1 D ARG 373  ? CZ  ? D ARG 304 CZ  
562 1 Y 1 D ARG 373  ? NH1 ? D ARG 304 NH1 
563 1 Y 1 D ARG 373  ? NH2 ? D ARG 304 NH2 
564 1 Y 1 D LYS 392  ? CG  ? D LYS 323 CG  
565 1 Y 1 D LYS 392  ? CD  ? D LYS 323 CD  
566 1 Y 1 D LYS 392  ? CE  ? D LYS 323 CE  
567 1 Y 1 D LYS 392  ? NZ  ? D LYS 323 NZ  
568 1 Y 1 D LYS 406  ? CG  ? D LYS 337 CG  
569 1 Y 1 D LYS 406  ? CD  ? D LYS 337 CD  
570 1 Y 1 D LYS 406  ? CE  ? D LYS 337 CE  
571 1 Y 1 D LYS 406  ? NZ  ? D LYS 337 NZ  
572 1 Y 1 D LYS 413  ? CG  ? D LYS 344 CG  
573 1 Y 1 D LYS 413  ? CD  ? D LYS 344 CD  
574 1 Y 1 D LYS 413  ? CE  ? D LYS 344 CE  
575 1 Y 1 D LYS 413  ? NZ  ? D LYS 344 NZ  
576 1 Y 1 E LYS 11   ? CG  ? E LYS 11  CG  
577 1 Y 1 E LYS 11   ? CD  ? E LYS 11  CD  
578 1 Y 1 E LYS 11   ? CE  ? E LYS 11  CE  
579 1 Y 1 E LYS 11   ? NZ  ? E LYS 11  NZ  
580 1 Y 1 E GLU 47   ? CG  ? E GLU 47  CG  
581 1 Y 1 E GLU 47   ? CD  ? E GLU 47  CD  
582 1 Y 1 E GLU 47   ? OE1 ? E GLU 47  OE1 
583 1 Y 1 E GLU 47   ? OE2 ? E GLU 47  OE2 
584 1 Y 1 E LYS 70   ? CG  ? E LYS 70  CG  
585 1 Y 1 E LYS 70   ? CD  ? E LYS 70  CD  
586 1 Y 1 E LYS 70   ? CE  ? E LYS 70  CE  
587 1 Y 1 E LYS 70   ? NZ  ? E LYS 70  NZ  
588 1 Y 1 E LYS 92   ? CG  ? E LYS 92  CG  
589 1 Y 1 E LYS 92   ? CD  ? E LYS 92  CD  
590 1 Y 1 E LYS 92   ? CE  ? E LYS 92  CE  
591 1 Y 1 E LYS 92   ? NZ  ? E LYS 92  NZ  
592 1 Y 1 E GLU 96   ? CG  ? E GLU 96  CG  
593 1 Y 1 E GLU 96   ? CD  ? E GLU 96  CD  
594 1 Y 1 E GLU 96   ? OE1 ? E GLU 96  OE1 
595 1 Y 1 E GLU 96   ? OE2 ? E GLU 96  OE2 
596 1 Y 1 E ARG 103  ? CG  ? E ARG 103 CG  
597 1 Y 1 E ARG 103  ? CD  ? E ARG 103 CD  
598 1 Y 1 E ARG 103  ? NE  ? E ARG 103 NE  
599 1 Y 1 E ARG 103  ? CZ  ? E ARG 103 CZ  
600 1 Y 1 E ARG 103  ? NH1 ? E ARG 103 NH1 
601 1 Y 1 E ARG 103  ? NH2 ? E ARG 103 NH2 
602 1 Y 1 E ARG 114  ? CG  ? E ARG 114 CG  
603 1 Y 1 E ARG 114  ? CD  ? E ARG 114 CD  
604 1 Y 1 E ARG 114  ? NE  ? E ARG 114 NE  
605 1 Y 1 E ARG 114  ? CZ  ? E ARG 114 CZ  
606 1 Y 1 E ARG 114  ? NH1 ? E ARG 114 NH1 
607 1 Y 1 E ARG 114  ? NH2 ? E ARG 114 NH2 
608 1 Y 1 E GLU 117  ? CG  ? E GLU 117 CG  
609 1 Y 1 E GLU 117  ? CD  ? E GLU 117 CD  
610 1 Y 1 E GLU 117  ? OE1 ? E GLU 117 OE1 
611 1 Y 1 E GLU 117  ? OE2 ? E GLU 117 OE2 
612 1 Y 1 E GLU 127  ? CG  ? E GLU 127 CG  
613 1 Y 1 E GLU 127  ? CD  ? E GLU 127 CD  
614 1 Y 1 E GLU 127  ? OE1 ? E GLU 127 OE1 
615 1 Y 1 E GLU 127  ? OE2 ? E GLU 127 OE2 
616 1 Y 1 E ARG 129  ? CG  ? E ARG 129 CG  
617 1 Y 1 E ARG 129  ? CD  ? E ARG 129 CD  
618 1 Y 1 E ARG 129  ? NE  ? E ARG 129 NE  
619 1 Y 1 E ARG 129  ? CZ  ? E ARG 129 CZ  
620 1 Y 1 E ARG 129  ? NH1 ? E ARG 129 NH1 
621 1 Y 1 E ARG 129  ? NH2 ? E ARG 129 NH2 
622 1 Y 1 E ARG 147  ? CG  ? E ARG 147 CG  
623 1 Y 1 E ARG 147  ? CD  ? E ARG 147 CD  
624 1 Y 1 E ARG 147  ? NE  ? E ARG 147 NE  
625 1 Y 1 E ARG 147  ? CZ  ? E ARG 147 CZ  
626 1 Y 1 E ARG 147  ? NH1 ? E ARG 147 NH1 
627 1 Y 1 E ARG 147  ? NH2 ? E ARG 147 NH2 
628 1 Y 1 E LYS 150  ? CG  ? E LYS 150 CG  
629 1 Y 1 E LYS 150  ? CD  ? E LYS 150 CD  
630 1 Y 1 E LYS 150  ? CE  ? E LYS 150 CE  
631 1 Y 1 E LYS 150  ? NZ  ? E LYS 150 NZ  
632 1 Y 1 E LYS 153  ? CG  ? E LYS 153 CG  
633 1 Y 1 E LYS 153  ? CD  ? E LYS 153 CD  
634 1 Y 1 E LYS 153  ? CE  ? E LYS 153 CE  
635 1 Y 1 E LYS 153  ? NZ  ? E LYS 153 NZ  
636 1 Y 1 E GLN 183  ? CG  ? E GLN 183 CG  
637 1 Y 1 E GLN 183  ? CD  ? E GLN 183 CD  
638 1 Y 1 E GLN 183  ? OE1 ? E GLN 183 OE1 
639 1 Y 1 E GLN 183  ? NE2 ? E GLN 183 NE2 
640 1 Y 1 E ARG 188  ? CG  ? E ARG 188 CG  
641 1 Y 1 E ARG 188  ? CD  ? E ARG 188 CD  
642 1 Y 1 E ARG 188  ? NE  ? E ARG 188 NE  
643 1 Y 1 E ARG 188  ? CZ  ? E ARG 188 CZ  
644 1 Y 1 E ARG 188  ? NH1 ? E ARG 188 NH1 
645 1 Y 1 E ARG 188  ? NH2 ? E ARG 188 NH2 
646 1 Y 1 E LYS 191  ? CG  ? E LYS 191 CG  
647 1 Y 1 E LYS 191  ? CD  ? E LYS 191 CD  
648 1 Y 1 E LYS 191  ? CE  ? E LYS 191 CE  
649 1 Y 1 E LYS 191  ? NZ  ? E LYS 191 NZ  
650 1 Y 1 E GLU 201  ? CG  ? E GLU 201 CG  
651 1 Y 1 E GLU 201  ? CD  ? E GLU 201 CD  
652 1 Y 1 E GLU 201  ? OE1 ? E GLU 201 OE1 
653 1 Y 1 E GLU 201  ? OE2 ? E GLU 201 OE2 
654 1 Y 1 E LYS 204  ? CG  ? E LYS 204 CG  
655 1 Y 1 E LYS 204  ? CD  ? E LYS 204 CD  
656 1 Y 1 E LYS 204  ? CE  ? E LYS 204 CE  
657 1 Y 1 E LYS 204  ? NZ  ? E LYS 204 NZ  
658 1 Y 1 E GLU 235  ? CG  ? E GLU 235 CG  
659 1 Y 1 E GLU 235  ? CD  ? E GLU 235 CD  
660 1 Y 1 E GLU 235  ? OE1 ? E GLU 235 OE1 
661 1 Y 1 E GLU 235  ? OE2 ? E GLU 235 OE2 
662 1 Y 1 E ASP 243  ? CG  ? E ASP 243 CG  
663 1 Y 1 E ASP 243  ? OD1 ? E ASP 243 OD1 
664 1 Y 1 E ASP 243  ? OD2 ? E ASP 243 OD2 
665 1 Y 1 E LYS 244  ? CG  ? E LYS 244 CG  
666 1 Y 1 E LYS 244  ? CD  ? E LYS 244 CD  
667 1 Y 1 E LYS 244  ? CE  ? E LYS 244 CE  
668 1 Y 1 E LYS 244  ? NZ  ? E LYS 244 NZ  
669 1 Y 1 E LYS 254  ? CG  ? E LYS 254 CG  
670 1 Y 1 E LYS 254  ? CD  ? E LYS 254 CD  
671 1 Y 1 E LYS 254  ? CE  ? E LYS 254 CE  
672 1 Y 1 E LYS 254  ? NZ  ? E LYS 254 NZ  
673 1 Y 1 E GLN 255  ? CG  ? E GLN 255 CG  
674 1 Y 1 E GLN 255  ? CD  ? E GLN 255 CD  
675 1 Y 1 E GLN 255  ? OE1 ? E GLN 255 OE1 
676 1 Y 1 E GLN 255  ? NE2 ? E GLN 255 NE2 
677 1 Y 1 E GLU 286  ? CG  ? E GLU 286 CG  
678 1 Y 1 E GLU 286  ? CD  ? E GLU 286 CD  
679 1 Y 1 E GLU 286  ? OE1 ? E GLU 286 OE1 
680 1 Y 1 E GLU 286  ? OE2 ? E GLU 286 OE2 
681 1 Y 1 E LYS 287  ? CG  ? E LYS 287 CG  
682 1 Y 1 E LYS 287  ? CD  ? E LYS 287 CD  
683 1 Y 1 E LYS 287  ? CE  ? E LYS 287 CE  
684 1 Y 1 E LYS 287  ? NZ  ? E LYS 287 NZ  
685 1 Y 1 E GLU 342  ? CG  ? E GLU 342 CG  
686 1 Y 1 E GLU 342  ? CD  ? E GLU 342 CD  
687 1 Y 1 E GLU 342  ? OE1 ? E GLU 342 OE1 
688 1 Y 1 E GLU 342  ? OE2 ? E GLU 342 OE2 
689 1 Y 1 E GLN 343  ? CG  ? E GLN 343 CG  
690 1 Y 1 E GLN 343  ? CD  ? E GLN 343 CD  
691 1 Y 1 E GLN 343  ? OE1 ? E GLN 343 OE1 
692 1 Y 1 E GLN 343  ? NE2 ? E GLN 343 NE2 
693 1 Y 1 E ARG 369  ? CG  ? E ARG 369 CG  
694 1 Y 1 E ARG 369  ? CD  ? E ARG 369 CD  
695 1 Y 1 E ARG 369  ? NE  ? E ARG 369 NE  
696 1 Y 1 E ARG 369  ? CZ  ? E ARG 369 CZ  
697 1 Y 1 E ARG 369  ? NH1 ? E ARG 369 NH1 
698 1 Y 1 E ARG 369  ? NH2 ? E ARG 369 NH2 
699 1 Y 1 E GLU 728  ? CG  ? E GLU 424 CG  
700 1 Y 1 E GLU 728  ? CD  ? E GLU 424 CD  
701 1 Y 1 E GLU 728  ? OE1 ? E GLU 424 OE1 
702 1 Y 1 E GLU 728  ? OE2 ? E GLU 424 OE2 
703 1 Y 1 E LYS 769  ? CG  ? E LYS 465 CG  
704 1 Y 1 E LYS 769  ? CD  ? E LYS 465 CD  
705 1 Y 1 E LYS 769  ? CE  ? E LYS 465 CE  
706 1 Y 1 E LYS 769  ? NZ  ? E LYS 465 NZ  
707 1 Y 1 E LEU 770  ? CG  ? E LEU 466 CG  
708 1 Y 1 E LEU 770  ? CD1 ? E LEU 466 CD1 
709 1 Y 1 E LEU 770  ? CD2 ? E LEU 466 CD2 
710 1 Y 1 E PHE 782  ? CG  ? E PHE 478 CG  
711 1 Y 1 E PHE 782  ? CD1 ? E PHE 478 CD1 
712 1 Y 1 E PHE 782  ? CD2 ? E PHE 478 CD2 
713 1 Y 1 E PHE 782  ? CE1 ? E PHE 478 CE1 
714 1 Y 1 E PHE 782  ? CE2 ? E PHE 478 CE2 
715 1 Y 1 E PHE 782  ? CZ  ? E PHE 478 CZ  
716 1 Y 1 E GLU 784  ? CG  ? E GLU 480 CG  
717 1 Y 1 E GLU 784  ? CD  ? E GLU 480 CD  
718 1 Y 1 E GLU 784  ? OE1 ? E GLU 480 OE1 
719 1 Y 1 E GLU 784  ? OE2 ? E GLU 480 OE2 
720 1 Y 1 E LYS 820  ? CG  ? E LYS 516 CG  
721 1 Y 1 E LYS 820  ? CD  ? E LYS 516 CD  
722 1 Y 1 E LYS 820  ? CE  ? E LYS 516 CE  
723 1 Y 1 E LYS 820  ? NZ  ? E LYS 516 NZ  
724 1 Y 1 E ASP 855  ? CG  ? E ASP 551 CG  
725 1 Y 1 E ASP 855  ? OD1 ? E ASP 551 OD1 
726 1 Y 1 E ASP 855  ? OD2 ? E ASP 551 OD2 
727 1 Y 1 E LYS 857  ? CG  ? E LYS 553 CG  
728 1 Y 1 E LYS 857  ? CD  ? E LYS 553 CD  
729 1 Y 1 E LYS 857  ? CE  ? E LYS 553 CE  
730 1 Y 1 E LYS 857  ? NZ  ? E LYS 553 NZ  
731 1 Y 1 E GLN 859  ? CG  ? E GLN 555 CG  
732 1 Y 1 E GLN 859  ? CD  ? E GLN 555 CD  
733 1 Y 1 E GLN 859  ? OE1 ? E GLN 555 OE1 
734 1 Y 1 E GLN 859  ? NE2 ? E GLN 555 NE2 
735 1 Y 1 E LYS 867  ? CG  ? E LYS 563 CG  
736 1 Y 1 E LYS 867  ? CD  ? E LYS 563 CD  
737 1 Y 1 E LYS 867  ? CE  ? E LYS 563 CE  
738 1 Y 1 E LYS 867  ? NZ  ? E LYS 563 NZ  
739 1 Y 1 E LYS 897  ? CG  ? E LYS 593 CG  
740 1 Y 1 E LYS 897  ? CD  ? E LYS 593 CD  
741 1 Y 1 E LYS 897  ? CE  ? E LYS 593 CE  
742 1 Y 1 E LYS 897  ? NZ  ? E LYS 593 NZ  
743 1 Y 1 E GLU 898  ? CG  ? E GLU 594 CG  
744 1 Y 1 E GLU 898  ? CD  ? E GLU 594 CD  
745 1 Y 1 E GLU 898  ? OE1 ? E GLU 594 OE1 
746 1 Y 1 E GLU 898  ? OE2 ? E GLU 594 OE2 
747 1 Y 1 E ARG 900  ? CG  ? E ARG 596 CG  
748 1 Y 1 E ARG 900  ? CD  ? E ARG 596 CD  
749 1 Y 1 E ARG 900  ? NE  ? E ARG 596 NE  
750 1 Y 1 E ARG 900  ? CZ  ? E ARG 596 CZ  
751 1 Y 1 E ARG 900  ? NH1 ? E ARG 596 NH1 
752 1 Y 1 E ARG 900  ? NH2 ? E ARG 596 NH2 
753 1 Y 1 E LYS 917  ? CG  ? E LYS 613 CG  
754 1 Y 1 E LYS 917  ? CD  ? E LYS 613 CD  
755 1 Y 1 E LYS 917  ? CE  ? E LYS 613 CE  
756 1 Y 1 E LYS 917  ? NZ  ? E LYS 613 NZ  
757 1 Y 1 E MET 938  ? CG  ? E MET 634 CG  
758 1 Y 1 E MET 938  ? SD  ? E MET 634 SD  
759 1 Y 1 E MET 938  ? CE  ? E MET 634 CE  
760 1 Y 1 E GLU 939  ? CG  ? E GLU 635 CG  
761 1 Y 1 E GLU 939  ? CD  ? E GLU 635 CD  
762 1 Y 1 E GLU 939  ? OE1 ? E GLU 635 OE1 
763 1 Y 1 E GLU 939  ? OE2 ? E GLU 635 OE2 
764 1 Y 1 E GLU 943  ? CG  ? E GLU 639 CG  
765 1 Y 1 E GLU 943  ? CD  ? E GLU 639 CD  
766 1 Y 1 E GLU 943  ? OE1 ? E GLU 639 OE1 
767 1 Y 1 E GLU 943  ? OE2 ? E GLU 639 OE2 
768 1 Y 1 E LYS 979  ? CG  ? E LYS 675 CG  
769 1 Y 1 E LYS 979  ? CD  ? E LYS 675 CD  
770 1 Y 1 E LYS 979  ? CE  ? E LYS 675 CE  
771 1 Y 1 E LYS 979  ? NZ  ? E LYS 675 NZ  
772 1 Y 1 E ASP 980  ? CG  ? E ASP 676 CG  
773 1 Y 1 E ASP 980  ? OD1 ? E ASP 676 OD1 
774 1 Y 1 E ASP 980  ? OD2 ? E ASP 676 OD2 
775 1 Y 1 E GLU 987  ? CG  ? E GLU 683 CG  
776 1 Y 1 E GLU 987  ? CD  ? E GLU 683 CD  
777 1 Y 1 E GLU 987  ? OE1 ? E GLU 683 OE1 
778 1 Y 1 E GLU 987  ? OE2 ? E GLU 683 OE2 
779 1 Y 1 E GLU 988  ? CG  ? E GLU 684 CG  
780 1 Y 1 E GLU 988  ? CD  ? E GLU 684 CD  
781 1 Y 1 E GLU 988  ? OE1 ? E GLU 684 OE1 
782 1 Y 1 E GLU 988  ? OE2 ? E GLU 684 OE2 
783 1 Y 1 E ARG 989  ? CG  ? E ARG 685 CG  
784 1 Y 1 E ARG 989  ? CD  ? E ARG 685 CD  
785 1 Y 1 E ARG 989  ? NE  ? E ARG 685 NE  
786 1 Y 1 E ARG 989  ? CZ  ? E ARG 685 CZ  
787 1 Y 1 E ARG 989  ? NH1 ? E ARG 685 NH1 
788 1 Y 1 E ARG 989  ? NH2 ? E ARG 685 NH2 
789 1 Y 1 E GLN 990  ? CG  ? E GLN 686 CG  
790 1 Y 1 E GLN 990  ? CD  ? E GLN 686 CD  
791 1 Y 1 E GLN 990  ? OE1 ? E GLN 686 OE1 
792 1 Y 1 E GLN 990  ? NE2 ? E GLN 686 NE2 
793 1 Y 1 E GLN 993  ? CG  ? E GLN 689 CG  
794 1 Y 1 E GLN 993  ? CD  ? E GLN 689 CD  
795 1 Y 1 E GLN 993  ? OE1 ? E GLN 689 OE1 
796 1 Y 1 E GLN 993  ? NE2 ? E GLN 689 NE2 
797 1 Y 1 E ASP 1053 ? CG  ? E ASP 749 CG  
798 1 Y 1 E ASP 1053 ? OD1 ? E ASP 749 OD1 
799 1 Y 1 E ASP 1053 ? OD2 ? E ASP 749 OD2 
800 1 Y 1 E ARG 1057 ? CG  ? E ARG 753 CG  
801 1 Y 1 E ARG 1057 ? CD  ? E ARG 753 CD  
802 1 Y 1 E ARG 1057 ? NE  ? E ARG 753 NE  
803 1 Y 1 E ARG 1057 ? CZ  ? E ARG 753 CZ  
804 1 Y 1 E ARG 1057 ? NH1 ? E ARG 753 NH1 
805 1 Y 1 E ARG 1057 ? NH2 ? E ARG 753 NH2 
806 1 Y 1 E LYS 1060 ? CG  ? E LYS 756 CG  
807 1 Y 1 E LYS 1060 ? CD  ? E LYS 756 CD  
808 1 Y 1 E LYS 1060 ? CE  ? E LYS 756 CE  
809 1 Y 1 E LYS 1060 ? NZ  ? E LYS 756 NZ  
810 1 Y 1 E LYS 1063 ? CG  ? E LYS 759 CG  
811 1 Y 1 E LYS 1063 ? CD  ? E LYS 759 CD  
812 1 Y 1 E LYS 1063 ? CE  ? E LYS 759 CE  
813 1 Y 1 E LYS 1063 ? NZ  ? E LYS 759 NZ  
814 1 Y 1 E ARG 1080 ? CG  ? E ARG 776 CG  
815 1 Y 1 E ARG 1080 ? CD  ? E ARG 776 CD  
816 1 Y 1 E ARG 1080 ? NE  ? E ARG 776 NE  
817 1 Y 1 E ARG 1080 ? CZ  ? E ARG 776 CZ  
818 1 Y 1 E ARG 1080 ? NH1 ? E ARG 776 NH1 
819 1 Y 1 E ARG 1080 ? NH2 ? E ARG 776 NH2 
820 1 Y 1 E ARG 1102 ? CG  ? E ARG 798 CG  
821 1 Y 1 E ARG 1102 ? CD  ? E ARG 798 CD  
822 1 Y 1 E ARG 1102 ? NE  ? E ARG 798 NE  
823 1 Y 1 E ARG 1102 ? CZ  ? E ARG 798 CZ  
824 1 Y 1 E ARG 1102 ? NH1 ? E ARG 798 NH1 
825 1 Y 1 E ARG 1102 ? NH2 ? E ARG 798 NH2 
826 1 Y 1 E LYS 1104 ? CG  ? E LYS 800 CG  
827 1 Y 1 E LYS 1104 ? CD  ? E LYS 800 CD  
828 1 Y 1 E LYS 1104 ? CE  ? E LYS 800 CE  
829 1 Y 1 E LYS 1104 ? NZ  ? E LYS 800 NZ  
830 1 Y 1 E GLN 1106 ? CG  ? E GLN 802 CG  
831 1 Y 1 E GLN 1106 ? CD  ? E GLN 802 CD  
832 1 Y 1 E GLN 1106 ? OE1 ? E GLN 802 OE1 
833 1 Y 1 E GLN 1106 ? NE2 ? E GLN 802 NE2 
834 1 Y 1 E GLU 1107 ? CG  ? E GLU 803 CG  
835 1 Y 1 E GLU 1107 ? CD  ? E GLU 803 CD  
836 1 Y 1 E GLU 1107 ? OE1 ? E GLU 803 OE1 
837 1 Y 1 E GLU 1107 ? OE2 ? E GLU 803 OE2 
838 1 Y 1 E LYS 1131 ? CG  ? E LYS 827 CG  
839 1 Y 1 E LYS 1131 ? CD  ? E LYS 827 CD  
840 1 Y 1 E LYS 1131 ? CE  ? E LYS 827 CE  
841 1 Y 1 E LYS 1131 ? NZ  ? E LYS 827 NZ  
842 1 Y 1 F ARG 882  ? CG  ? F ARG 17  CG  
843 1 Y 1 F ARG 882  ? CD  ? F ARG 17  CD  
844 1 Y 1 F ARG 882  ? NE  ? F ARG 17  NE  
845 1 Y 1 F ARG 882  ? CZ  ? F ARG 17  CZ  
846 1 Y 1 F ARG 882  ? NH1 ? F ARG 17  NH1 
847 1 Y 1 F ARG 882  ? NH2 ? F ARG 17  NH2 
848 1 Y 1 F LYS 883  ? CG  ? F LYS 18  CG  
849 1 Y 1 F LYS 883  ? CD  ? F LYS 18  CD  
850 1 Y 1 F LYS 883  ? CE  ? F LYS 18  CE  
851 1 Y 1 F LYS 883  ? NZ  ? F LYS 18  NZ  
852 1 Y 1 F ARG 890  ? CG  ? F ARG 25  CG  
853 1 Y 1 F ARG 890  ? CD  ? F ARG 25  CD  
854 1 Y 1 F ARG 890  ? NE  ? F ARG 25  NE  
855 1 Y 1 F ARG 890  ? CZ  ? F ARG 25  CZ  
856 1 Y 1 F ARG 890  ? NH1 ? F ARG 25  NH1 
857 1 Y 1 F ARG 890  ? NH2 ? F ARG 25  NH2 
# 
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  ? ? ? '(1.21_5207: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  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                     9DJX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     109.114 
_cell.length_a_esd                 ? 
_cell.length_b                     145.029 
_cell.length_b_esd                 ? 
_cell.length_c                     191.895 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DJX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DJX 
_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             2.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.76 
_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          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    '0.2 M Sodium Sulfate, 0.1M BIS-TRIS Propane pH 7.5, 20% PEG3350 (Qiagen PACT G8)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-01 
_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   1.0 
_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                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DJX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.35 
_reflns.d_resolution_low                               52.48 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     44026 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                23.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.289 
_reflns.pdbx_Rpim_I_all                                0.059 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1025053 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.283 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.35 
_reflns_shell.d_res_low                                     3.48 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           81974 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4613 
_reflns_shell.percent_possible_obs                          100.0 
_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                               17.8 
_reflns_shell.pdbx_chi_squared                              1.04 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               4.586 
_reflns_shell.pdbx_Rpim_I_all                               1.077 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.280 
_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                                  4.452 
_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                                 9DJX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.35 
_refine.ls_d_res_low                             46.88 
_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                     43910 
_refine.ls_number_reflns_R_free                  2207 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.67 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2057 
_refine.ls_R_factor_R_free                       0.2709 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2022 
_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                          1.97 
_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                 29.75 
_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                            0.52 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.35 
_refine_hist.d_res_low                        46.88 
_refine_hist.number_atoms_solvent             22 
_refine_hist.number_atoms_total               17640 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        17543 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         75 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 17990 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.048  ? 24513 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.457 ? 6321  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 2897  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 3154  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.35 3.42  . . 170 2576 100.00 . . . . 0.3320 . . . . . . . . . . . 0.3978 
'X-RAY DIFFRACTION' 3.42 3.50  . . 128 2609 100.00 . . . . 0.3168 . . . . . . . . . . . 0.3467 
'X-RAY DIFFRACTION' 3.50 3.59  . . 144 2585 100.00 . . . . 0.2878 . . . . . . . . . . . 0.3692 
'X-RAY DIFFRACTION' 3.59 3.69  . . 126 2376 90.00  . . . . 0.2770 . . . . . . . . . . . 0.3390 
'X-RAY DIFFRACTION' 3.69 3.80  . . 120 2604 100.00 . . . . 0.2449 . . . . . . . . . . . 0.3033 
'X-RAY DIFFRACTION' 3.80 3.92  . . 129 2346 90.00  . . . . 0.2545 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 3.92 4.06  . . 132 2620 100.00 . . . . 0.2234 . . . . . . . . . . . 0.3165 
'X-RAY DIFFRACTION' 4.06 4.22  . . 127 2643 100.00 . . . . 0.1947 . . . . . . . . . . . 0.3056 
'X-RAY DIFFRACTION' 4.22 4.41  . . 112 2646 100.00 . . . . 0.1617 . . . . . . . . . . . 0.2237 
'X-RAY DIFFRACTION' 4.41 4.64  . . 114 2633 100.00 . . . . 0.1647 . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 4.64 4.94  . . 141 2645 100.00 . . . . 0.1681 . . . . . . . . . . . 0.2342 
'X-RAY DIFFRACTION' 4.94 5.32  . . 145 2619 100.00 . . . . 0.1708 . . . . . . . . . . . 0.2754 
'X-RAY DIFFRACTION' 5.32 5.85  . . 156 2653 100.00 . . . . 0.1864 . . . . . . . . . . . 0.2450 
'X-RAY DIFFRACTION' 5.85 6.69  . . 144 2670 100.00 . . . . 0.1901 . . . . . . . . . . . 0.2786 
'X-RAY DIFFRACTION' 6.69 8.42  . . 176 2675 100.00 . . . . 0.2023 . . . . . . . . . . . 0.2446 
'X-RAY DIFFRACTION' 8.42 46.88 . . 143 2803 99.00  . . . . 0.1824 . . . . . . . . . . . 0.2388 
# 
_struct.entry_id                     9DJX 
_struct.title                        'Ternary complex structure of Cereblon-DDB1 bound to WIZ(ZF7) and the molecular glue WIZ-6' 
_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        9DJX 
_struct_keywords.text            'Cereblon, Ligase, Molecular Glue, degradation' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M N N 6 ? 
N N N 5 ? 
O N N 4 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 7 ? 
T N N 7 ? 
# 
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 CRBN_HUMAN Q96SW2 ? 1 
;RTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQD
FGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQK
RKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLR
CELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVA
QCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
;
70  
2 UNP DDB1_HUMAN Q16531 ? 2 
;MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL
TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE
ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH
NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG
VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIG
;
1   
3 UNP DDB1_HUMAN Q16531 ? 2 
;EIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEE
VEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKE
VKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEI
ARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQ
GSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKM
QEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
;
706 
4 UNP WIZ_HUMAN  O95785 ? 3 QSLTTCEVCGACFETRKGLSSHARSHLRQ 867 
# 
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 9DJX A 1   ? 373 ? Q96SW2 70  ? 442  ? 70  442  
2 2 9DJX B 1   ? 395 ? Q16531 1   ? 395  ? 1   699  
3 3 9DJX B 402 ? 836 ? Q16531 706 ? 1140 ? 706 1140 
4 4 9DJX C 2   ? 30  ? O95785 867 ? 895  ? 867 895  
5 1 9DJX D 1   ? 373 ? Q96SW2 70  ? 442  ? 70  442  
6 2 9DJX E 1   ? 395 ? Q16531 1   ? 395  ? 1   699  
7 3 9DJX E 402 ? 836 ? Q16531 706 ? 1140 ? 706 1140 
8 4 9DJX F 2   ? 30  ? O95785 867 ? 895  ? 867 895  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 9DJX GLY B 396 ? UNP Q16531 ? ? linker           700 1  
2 9DJX ASN B 397 ? UNP Q16531 ? ? linker           701 2  
2 9DJX GLY B 398 ? UNP Q16531 ? ? linker           702 3  
2 9DJX ASN B 399 ? UNP Q16531 ? ? linker           703 4  
2 9DJX SER B 400 ? UNP Q16531 ? ? linker           704 5  
2 9DJX GLY B 401 ? UNP Q16531 ? ? linker           705 6  
4 9DJX SER C 1   ? UNP O95785 ? ? 'expression tag' 866 7  
6 9DJX GLY E 396 ? UNP Q16531 ? ? linker           700 8  
6 9DJX ASN E 397 ? UNP Q16531 ? ? linker           701 9  
6 9DJX GLY E 398 ? UNP Q16531 ? ? linker           702 10 
6 9DJX ASN E 399 ? UNP Q16531 ? ? linker           703 11 
6 9DJX SER E 400 ? UNP Q16531 ? ? linker           704 12 
6 9DJX GLY E 401 ? UNP Q16531 ? ? linker           705 13 
8 9DJX SER F 1   ? UNP O95785 ? ? 'expression tag' 866 14 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA trimeric 3 
2 author_and_software_defined_assembly PISA trimeric 3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5800  ? 
1 MORE         -59   ? 
1 'SSA (A^2)'  47550 ? 
2 'ABSA (A^2)' 6170  ? 
2 MORE         -71   ? 
2 'SSA (A^2)'  47300 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,G,H,I,J,P,Q,R 
2 1 D,E,F,K,L,M,N,O,S,T 
# 
_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 HIS A 34  ? LYS A 47  ? HIS A 103  LYS A 116  1 ? 14 
HELX_P HELX_P2  AA2 LEU A 130 ? CYS A 136 ? LEU A 199  CYS A 205  1 ? 7  
HELX_P HELX_P3  AA3 TYR A 152 ? PHE A 163 ? TYR A 221  PHE A 232  1 ? 12 
HELX_P HELX_P4  AA4 HIS A 164 ? THR A 169 ? HIS A 233  THR A 238  5 ? 6  
HELX_P HELX_P5  AA5 PRO A 172 ? LEU A 178 ? PRO A 241  LEU A 247  1 ? 7  
HELX_P HELX_P6  AA6 ASP A 180 ? ASP A 196 ? ASP A 249  ASP A 265  1 ? 17 
HELX_P HELX_P7  AA7 ASN A 207 ? LEU A 219 ? ASN A 276  LEU A 288  1 ? 13 
HELX_P HELX_P8  AA8 ASP A 222 ? ILE A 232 ? ASP A 291  ILE A 301  1 ? 11 
HELX_P HELX_P9  AA9 SER A 234 ? CYS A 249 ? SER A 303  CYS A 318  1 ? 16 
HELX_P HELX_P10 AB1 ASN A 266 ? ILE A 268 ? ASN A 335  ILE A 337  5 ? 3  
HELX_P HELX_P11 AB2 PRO B 251 ? SER B 256 ? PRO B 251  SER B 256  5 ? 6  
HELX_P HELX_P12 AB3 ALA B 381 ? GLU B 384 ? ALA B 381  GLU B 384  5 ? 4  
HELX_P HELX_P13 AB4 SER B 740 ? ILE B 758 ? SER B 1044 ILE B 1062 1 ? 19 
HELX_P HELX_P14 AB5 GLU B 765 ? SER B 771 ? GLU B 1069 SER B 1075 1 ? 7  
HELX_P HELX_P15 AB6 GLY B 787 ? SER B 792 ? GLY B 1091 SER B 1096 1 ? 6  
HELX_P HELX_P16 AB7 PHE B 793 ? ILE B 796 ? PHE B 1097 ILE B 1100 5 ? 4  
HELX_P HELX_P17 AB8 SER B 797 ? ALA B 806 ? SER B 1101 ALA B 1110 1 ? 10 
HELX_P HELX_P18 AB9 THR B 821 ? ARG B 834 ? THR B 1125 ARG B 1138 1 ? 14 
HELX_P HELX_P19 AC1 THR C 16  ? HIS C 27  ? THR C 881  HIS C 892  1 ? 12 
HELX_P HELX_P20 AC2 HIS D 34  ? GLN D 46  ? HIS D 103  GLN D 115  1 ? 13 
HELX_P HELX_P21 AC3 LEU D 133 ? GLN D 137 ? LEU D 202  GLN D 206  5 ? 5  
HELX_P HELX_P22 AC4 LYS D 153 ? PHE D 163 ? LYS D 222  PHE D 232  1 ? 11 
HELX_P HELX_P23 AC5 HIS D 164 ? ASN D 167 ? HIS D 233  ASN D 236  5 ? 4  
HELX_P HELX_P24 AC6 PRO D 172 ? TYR D 179 ? PRO D 241  TYR D 248  1 ? 8  
HELX_P HELX_P25 AC7 ASP D 180 ? GLU D 194 ? ASP D 249  GLU D 263  1 ? 15 
HELX_P HELX_P26 AC8 ASN D 207 ? LEU D 219 ? ASN D 276  LEU D 288  1 ? 13 
HELX_P HELX_P27 AC9 ASP D 222 ? ILE D 232 ? ASP D 291  ILE D 301  1 ? 11 
HELX_P HELX_P28 AD1 SER D 234 ? CYS D 249 ? SER D 303  CYS D 318  1 ? 16 
HELX_P HELX_P29 AD2 ASN D 266 ? ILE D 268 ? ASN D 335  ILE D 337  5 ? 3  
HELX_P HELX_P30 AD3 ALA E 381 ? GLU E 384 ? ALA E 381  GLU E 384  5 ? 4  
HELX_P HELX_P31 AD4 THR E 681 ? GLN E 686 ? THR E 985  GLN E 990  1 ? 6  
HELX_P HELX_P32 AD5 SER E 740 ? ILE E 758 ? SER E 1044 ILE E 1062 1 ? 19 
HELX_P HELX_P33 AD6 GLU E 765 ? SER E 771 ? GLU E 1069 SER E 1075 1 ? 7  
HELX_P HELX_P34 AD7 GLY E 787 ? SER E 792 ? GLY E 1091 SER E 1096 1 ? 6  
HELX_P HELX_P35 AD8 PHE E 793 ? ILE E 796 ? PHE E 1097 ILE E 1100 5 ? 4  
HELX_P HELX_P36 AD9 SER E 797 ? VAL E 805 ? SER E 1101 VAL E 1109 1 ? 9  
HELX_P HELX_P37 AE1 THR E 821 ? THR E 833 ? THR E 1125 THR E 1137 1 ? 13 
HELX_P HELX_P38 AE2 THR F 16  ? HIS F 27  ? THR F 881  HIS F 892  1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? B CYS 18  SG  ? ? ? 1_555 B CYS 313 SG ? ? B CYS 18  B CYS 313 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
disulf2  disulf ? ? E CYS 18  SG  ? ? ? 1_555 E CYS 313 SG ? ? E CYS 18  E CYS 313 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc1  metalc ? ? A CYS 254 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 323 A ZN  501 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc2  metalc ? ? A CYS 257 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 326 A ZN  501 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc3  metalc ? ? A CYS 322 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 391 A ZN  501 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc4  metalc ? ? A CYS 325 SG  ? ? ? 1_555 G ZN  .   ZN ? ? A CYS 394 A ZN  501 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc5  metalc ? ? C CYS 7   SG  ? ? ? 1_555 J ZN  .   ZN ? ? C CYS 872 C ZN  900 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc6  metalc ? ? C CYS 10  SG  ? ? ? 1_555 J ZN  .   ZN ? ? C CYS 875 C ZN  900 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc7  metalc ? ? C HIS 23  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? C HIS 888 C ZN  900 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc8  metalc ? ? C HIS 27  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? C HIS 892 C ZN  900 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc9  metalc ? ? D CYS 254 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 323 D ZN  501 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc10 metalc ? ? D CYS 257 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 326 D ZN  501 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc11 metalc ? ? D CYS 322 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 391 D ZN  501 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc12 metalc ? ? D CYS 325 SG  ? ? ? 1_555 K ZN  .   ZN ? ? D CYS 394 D ZN  501 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc13 metalc ? ? F CYS 7   SG  ? ? ? 1_555 O ZN  .   ZN ? ? F CYS 872 F ZN  900 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc14 metalc ? ? F CYS 10  SG  ? ? ? 1_555 O ZN  .   ZN ? ? F CYS 875 F ZN  900 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc15 metalc ? ? F HIS 23  NE2 ? ? ? 1_555 O ZN  .   ZN ? ? F HIS 888 F ZN  900 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
metalc16 metalc ? ? F HIS 27  NE2 ? ? ? 1_555 O ZN  .   ZN ? ? F HIS 892 F ZN  900 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 254 ? A CYS 323 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 257 ? A CYS 326 ? 1_555 107.2 ? 
2  SG  ? A CYS 254 ? A CYS 323 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 322 ? A CYS 391 ? 1_555 108.7 ? 
3  SG  ? A CYS 257 ? A CYS 326 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 322 ? A CYS 391 ? 1_555 113.9 ? 
4  SG  ? A CYS 254 ? A CYS 323 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 325 ? A CYS 394 ? 1_555 97.4  ? 
5  SG  ? A CYS 257 ? A CYS 326 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 325 ? A CYS 394 ? 1_555 125.2 ? 
6  SG  ? A CYS 322 ? A CYS 391 ? 1_555 ZN ? G ZN . ? A ZN 501 ? 1_555 SG  ? A CYS 325 ? A CYS 394 ? 1_555 102.7 ? 
7  SG  ? C CYS 7   ? C CYS 872 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 SG  ? C CYS 10  ? C CYS 875 ? 1_555 114.9 ? 
8  SG  ? C CYS 7   ? C CYS 872 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 23  ? C HIS 888 ? 1_555 94.5  ? 
9  SG  ? C CYS 10  ? C CYS 875 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 23  ? C HIS 888 ? 1_555 89.6  ? 
10 SG  ? C CYS 7   ? C CYS 872 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 27  ? C HIS 892 ? 1_555 106.3 ? 
11 SG  ? C CYS 10  ? C CYS 875 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 27  ? C HIS 892 ? 1_555 136.3 ? 
12 NE2 ? C HIS 23  ? C HIS 888 ? 1_555 ZN ? J ZN . ? C ZN 900 ? 1_555 NE2 ? C HIS 27  ? C HIS 892 ? 1_555 101.3 ? 
13 SG  ? D CYS 254 ? D CYS 323 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 257 ? D CYS 326 ? 1_555 123.1 ? 
14 SG  ? D CYS 254 ? D CYS 323 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 322 ? D CYS 391 ? 1_555 106.8 ? 
15 SG  ? D CYS 257 ? D CYS 326 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 322 ? D CYS 391 ? 1_555 115.7 ? 
16 SG  ? D CYS 254 ? D CYS 323 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 325 ? D CYS 394 ? 1_555 90.0  ? 
17 SG  ? D CYS 257 ? D CYS 326 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 325 ? D CYS 394 ? 1_555 121.9 ? 
18 SG  ? D CYS 322 ? D CYS 391 ? 1_555 ZN ? K ZN . ? D ZN 501 ? 1_555 SG  ? D CYS 325 ? D CYS 394 ? 1_555 93.3  ? 
19 SG  ? F CYS 7   ? F CYS 872 ? 1_555 ZN ? O ZN . ? F ZN 900 ? 1_555 SG  ? F CYS 10  ? F CYS 875 ? 1_555 122.9 ? 
20 SG  ? F CYS 7   ? F CYS 872 ? 1_555 ZN ? O ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 23  ? F HIS 888 ? 1_555 116.7 ? 
21 SG  ? F CYS 10  ? F CYS 875 ? 1_555 ZN ? O ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 23  ? F HIS 888 ? 1_555 86.9  ? 
22 SG  ? F CYS 7   ? F CYS 872 ? 1_555 ZN ? O ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 27  ? F HIS 892 ? 1_555 123.0 ? 
23 SG  ? F CYS 10  ? F CYS 875 ? 1_555 ZN ? O ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 27  ? F HIS 892 ? 1_555 97.3  ? 
24 NE2 ? F HIS 23  ? F HIS 888 ? 1_555 ZN ? O ZN . ? F ZN 900 ? 1_555 NE2 ? F HIS 27  ? F HIS 892 ? 1_555 102.8 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS B 18 ? CYS B 313 ? CYS B 18 ? 1_555 CYS B 313 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS E 18 ? CYS E 313 ? CYS E 18 ? 1_555 CYS E 313 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 341 A . ? SER 410 A PRO 342 A ? PRO 411 A 1 9.04   
2 GLY 357 B . ? GLY 357 B PRO 358 B ? PRO 358 B 1 -6.65  
3 SER 341 D . ? SER 410 D PRO 342 D ? PRO 411 D 1 3.69   
4 GLY 357 E . ? GLY 357 E PRO 358 E ? PRO 358 E 1 -11.43 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 3 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 4 ? 
AC1 ? 4 ? 
AC2 ? 2 ? 
AC3 ? 4 ? 
AC4 ? 5 ? 
AC5 ? 3 ? 
AC6 ? 6 ? 
AC7 ? 5 ? 
AC8 ? 4 ? 
AC9 ? 4 ? 
AD1 ? 4 ? 
AD2 ? 4 ? 
AD3 ? 4 ? 
AD4 ? 4 ? 
AD5 ? 4 ? 
AD6 ? 4 ? 
AD7 ? 3 ? 
AD8 ? 4 ? 
AD9 ? 4 ? 
AE1 ? 4 ? 
AE2 ? 4 ? 
AE3 ? 4 ? 
AE4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC4 4 5 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC6 4 5 ? anti-parallel 
AC6 5 6 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC7 4 5 ? parallel      
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 2 3 ? anti-parallel 
AD8 1 2 ? anti-parallel 
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AE1 1 2 ? anti-parallel 
AE1 2 3 ? anti-parallel 
AE1 3 4 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE2 2 3 ? anti-parallel 
AE2 3 4 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE3 2 3 ? anti-parallel 
AE3 3 4 ? anti-parallel 
AE4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 27  ? LEU A 32  ? THR A 96   LEU A 101  
AA1 2 VAL A 86  ? THR A 103 ? VAL A 155  THR A 172  
AA1 3 GLN A 109 ? ILE A 115 ? GLN A 178  ILE A 184  
AA1 4 CYS A 9   ? VAL A 14  ? CYS A 78   VAL A 83   
AA1 5 THR A 50  ? ALA A 55  ? THR A 119  ALA A 124  
AA1 6 PHE A 66  ? GLU A 77  ? PHE A 135  GLU A 146  
AA1 7 VAL A 86  ? THR A 103 ? VAL A 155  THR A 172  
AA2 1 GLU A 261 ? THR A 264 ? GLU A 330  THR A 333  
AA2 2 SER A 251 ? CYS A 254 ? SER A 320  CYS A 323  
AA2 3 LEU A 353 ? THR A 356 ? LEU A 422  THR A 425  
AA3 1 MET A 277 ? VAL A 281 ? MET A 346  VAL A 350  
AA3 2 VAL A 287 ? VAL A 293 ? VAL A 356  VAL A 362  
AA3 3 LYS A 344 ? THR A 349 ? LYS A 413  THR A 418  
AA3 4 HIS A 328 ? ALA A 335 ? HIS A 397  ALA A 404  
AA3 5 TYR A 315 ? CYS A 322 ? TYR A 384  CYS A 391  
AA3 6 LEU A 299 ? SER A 306 ? LEU A 368  SER A 375  
AA4 1 VAL B 700 ? HIS B 705 ? VAL B 1004 HIS B 1009 
AA4 2 GLN B 721 ? THR B 728 ? GLN B 1025 THR B 1032 
AA4 3 ILE B 733 ? SER B 738 ? ILE B 1037 SER B 1042 
AA4 4 ASN B 4   ? GLN B 10  ? ASN B 4    GLN B 10   
AA4 5 PHE B 784 ? ASP B 786 ? PHE B 1088 ASP B 1090 
AA5 1 CYS B 18  ? GLY B 21  ? CYS B 18   GLY B 21   
AA5 2 ASN B 30  ? ALA B 34  ? ASN B 30   ALA B 34   
AA5 3 LEU B 39  ? VAL B 44  ? LEU B 39   VAL B 44   
AA5 4 LEU B 49  ? VAL B 55  ? LEU B 49   VAL B 55   
AA6 1 ILE B 61  ? PHE B 67  ? ILE B 61   PHE B 67   
AA6 2 LEU B 76  ? THR B 81  ? LEU B 76   THR B 81   
AA6 3 ASN B 85  ? SER B 94  ? ASN B 85   SER B 94   
AA6 4 SER B 97  ? ASN B 107 ? SER B 97   ASN B 107  
AA7 1 ARG B 114 ? PRO B 115 ? ARG B 114  PRO B 115  
AA7 2 TYR B 136 ? ASP B 137 ? TYR B 136  ASP B 137  
AA8 1 ILE B 121 ? ILE B 124 ? ILE B 121  ILE B 124  
AA8 2 MET B 130 ? ARG B 134 ? MET B 130  ARG B 134  
AA8 3 LEU B 139 ? PRO B 144 ? LEU B 139  PRO B 144  
AA8 4 PHE B 155 ? ARG B 158 ? PHE B 155  ARG B 158  
AA9 1 VAL B 164 ? PHE B 169 ? VAL B 164  PHE B 169  
AA9 2 THR B 177 ? GLN B 183 ? THR B 177  GLN B 183  
AA9 3 ARG B 188 ? SER B 196 ? ARG B 188  SER B 196  
AA9 4 GLU B 201 ? LYS B 204 ? GLU B 201  LYS B 204  
AB1 1 MET B 218 ? VAL B 222 ? MET B 218  VAL B 222  
AB1 2 GLY B 228 ? ILE B 232 ? GLY B 228  ILE B 232  
AB1 3 ILE B 237 ? ASN B 241 ? ILE B 237  ASN B 241  
AB1 4 LYS B 244 ? ILE B 248 ? LYS B 244  ILE B 248  
AB2 1 CYS B 260 ? ARG B 263 ? CYS B 260  ARG B 263  
AB2 2 ARG B 270 ? GLY B 274 ? ARG B 270  GLY B 274  
AB2 3 ARG B 279 ? GLU B 286 ? ARG B 279  GLU B 286  
AB2 4 ASP B 299 ? GLU B 307 ? ASP B 299  GLU B 307  
AB3 1 CYS B 313 ? ASP B 318 ? CYS B 313  ASP B 318  
AB3 2 VAL B 321 ? GLY B 325 ? VAL B 321  GLY B 325  
AB3 3 SER B 331 ? LEU B 336 ? SER B 331  LEU B 336  
AB3 4 VAL B 347 ? PHE B 353 ? VAL B 347  PHE B 353  
AB4 1 ILE B 359 ? VAL B 365 ? ILE B 359  VAL B 365  
AB4 2 GLN B 374 ? SER B 379 ? GLN B 374  SER B 379  
AB4 3 SER B 386 ? ARG B 391 ? SER B 386  ARG B 391  
AB4 4 HIS B 407 ? PRO B 412 ? HIS B 711  PRO B 716  
AB5 1 SER B 416 ? GLN B 423 ? SER B 720  GLN B 727  
AB5 2 CYS B 428 ? GLN B 439 ? CYS B 732  GLN B 743  
AB5 3 THR B 445 ? ALA B 447 ? THR B 749  ALA B 751  
AB6 1 SER B 416 ? GLN B 423 ? SER B 720  GLN B 727  
AB6 2 CYS B 428 ? GLN B 439 ? CYS B 732  GLN B 743  
AB6 3 GLU B 481 ? ASP B 491 ? GLU B 785  ASP B 795  
AB6 4 VAL B 497 ? GLN B 502 ? VAL B 801  GLN B 806  
AB7 1 GLU B 507 ? LYS B 516 ? GLU B 811  LYS B 820  
AB7 2 THR B 523 ? MET B 531 ? THR B 827  MET B 835  
AB7 3 ILE B 544 ? TYR B 549 ? ILE B 848  TYR B 853  
AB7 4 LEU B 554 ? LYS B 560 ? LEU B 858  LYS B 864  
AB8 1 VAL B 566 ? PHE B 572 ? VAL B 870  PHE B 876  
AB8 2 LYS B 575 ? ILE B 580 ? LYS B 879  ILE B 884  
AB8 3 THR B 583 ? TRP B 589 ? THR B 887  TRP B 893  
AB8 4 LEU B 595 ? TYR B 602 ? LEU B 899  TYR B 906  
AB9 1 TYR B 609 ? LYS B 613 ? TYR B 913  LYS B 917  
AB9 2 PHE B 616 ? GLY B 620 ? PHE B 920  GLY B 924  
AB9 3 SER B 625 ? LYS B 632 ? SER B 929  LYS B 936  
AB9 4 ASN B 637 ? PHE B 645 ? ASN B 941  PHE B 949  
AC1 1 MET B 650 ? ILE B 655 ? MET B 954  ILE B 959  
AC1 2 ASN B 660 ? GLU B 665 ? ASN B 964  GLU B 969  
AC1 3 ASN B 669 ? GLN B 674 ? ASN B 973  GLN B 978  
AC1 4 GLN B 689 ? HIS B 695 ? GLN B 993  HIS B 999  
AC2 1 PHE B 772 ? HIS B 773 ? PHE B 1076 HIS B 1077 
AC2 2 THR B 778 ? GLU B 779 ? THR B 1082 GLU B 1083 
AC3 1 CYS D 9   ? PRO D 13  ? CYS D 78   PRO D 82   
AC3 2 GLN D 110 ? ILE D 115 ? GLN D 179  ILE D 184  
AC3 3 VAL D 86  ? VAL D 98  ? VAL D 155  VAL D 167  
AC3 4 THR D 27  ? LEU D 32  ? THR D 96   LEU D 101  
AC4 1 CYS D 9   ? PRO D 13  ? CYS D 78   PRO D 82   
AC4 2 GLN D 110 ? ILE D 115 ? GLN D 179  ILE D 184  
AC4 3 VAL D 86  ? VAL D 98  ? VAL D 155  VAL D 167  
AC4 4 PHE D 66  ? GLU D 77  ? PHE D 135  GLU D 146  
AC4 5 THR D 50  ? ALA D 55  ? THR D 119  ALA D 124  
AC5 1 GLU D 261 ? THR D 264 ? GLU D 330  THR D 333  
AC5 2 SER D 251 ? CYS D 254 ? SER D 320  CYS D 323  
AC5 3 LEU D 353 ? THR D 356 ? LEU D 422  THR D 425  
AC6 1 MET D 277 ? VAL D 281 ? MET D 346  VAL D 350  
AC6 2 VAL D 287 ? VAL D 293 ? VAL D 356  VAL D 362  
AC6 3 LYS D 344 ? THR D 349 ? LYS D 413  THR D 418  
AC6 4 HIS D 328 ? ALA D 335 ? HIS D 397  ALA D 404  
AC6 5 TYR D 315 ? CYS D 322 ? TYR D 384  CYS D 391  
AC6 6 LEU D 299 ? SER D 306 ? LEU D 368  SER D 375  
AC7 1 VAL E 700 ? HIS E 705 ? VAL E 1004 HIS E 1009 
AC7 2 GLN E 721 ? THR E 728 ? GLN E 1025 THR E 1032 
AC7 3 ILE E 733 ? LEU E 739 ? ILE E 1037 LEU E 1043 
AC7 4 TYR E 3   ? GLN E 10  ? TYR E 3    GLN E 10   
AC7 5 PHE E 784 ? ASP E 786 ? PHE E 1088 ASP E 1090 
AC8 1 GLY E 17  ? GLY E 21  ? GLY E 17   GLY E 21   
AC8 2 ASN E 30  ? LYS E 35  ? ASN E 30   LYS E 35   
AC8 3 ARG E 38  ? VAL E 44  ? ARG E 38   VAL E 44   
AC8 4 LEU E 49  ? GLY E 56  ? LEU E 49   GLY E 56   
AC9 1 ILE E 61  ? PHE E 67  ? ILE E 61   PHE E 67   
AC9 2 LEU E 76  ? THR E 81  ? LEU E 76   THR E 81   
AC9 3 ASN E 85  ? GLN E 93  ? ASN E 85   GLN E 93   
AC9 4 ILE E 98  ? ASN E 107 ? ILE E 98   ASN E 107  
AD1 1 ILE E 121 ? ILE E 124 ? ILE E 121  ILE E 124  
AD1 2 MET E 130 ? ARG E 134 ? MET E 130  ARG E 134  
AD1 3 LEU E 139 ? PRO E 144 ? LEU E 139  PRO E 144  
AD1 4 PHE E 155 ? ARG E 158 ? PHE E 155  ARG E 158  
AD2 1 VAL E 164 ? PHE E 169 ? VAL E 164  PHE E 169  
AD2 2 THR E 177 ? ASP E 184 ? THR E 177  ASP E 184  
AD2 3 GLY E 187 ? SER E 196 ? GLY E 187  SER E 196  
AD2 4 GLU E 201 ? LYS E 204 ? GLU E 201  LYS E 204  
AD3 1 MET E 218 ? ALA E 221 ? MET E 218  ALA E 221  
AD3 2 ALA E 229 ? ILE E 232 ? ALA E 229  ILE E 232  
AD3 3 ILE E 237 ? ASN E 241 ? ILE E 237  ASN E 241  
AD3 4 LYS E 244 ? ILE E 248 ? LYS E 244  ILE E 248  
AD4 1 ILE E 258 ? ARG E 263 ? ILE E 258  ARG E 263  
AD4 2 ARG E 270 ? ASP E 275 ? ARG E 270  ASP E 275  
AD4 3 ARG E 279 ? GLU E 289 ? ARG E 279  GLU E 289  
AD4 4 VAL E 295 ? GLU E 307 ? VAL E 295  GLU E 307  
AD5 1 CYS E 313 ? ASP E 318 ? CYS E 313  ASP E 318  
AD5 2 VAL E 321 ? GLY E 325 ? VAL E 321  GLY E 325  
AD5 3 SER E 331 ? LEU E 336 ? SER E 331  LEU E 336  
AD5 4 VAL E 347 ? PHE E 353 ? VAL E 347  PHE E 353  
AD6 1 ILE E 359 ? VAL E 365 ? ILE E 359  VAL E 365  
AD6 2 GLN E 374 ? SER E 379 ? GLN E 374  SER E 379  
AD6 3 SER E 386 ? ARG E 391 ? SER E 386  ARG E 391  
AD6 4 HIS E 407 ? PRO E 412 ? HIS E 711  PRO E 716  
AD7 1 SER E 416 ? GLN E 423 ? SER E 720  GLN E 727  
AD7 2 CYS E 428 ? VAL E 438 ? CYS E 732  VAL E 742  
AD7 3 THR E 446 ? ALA E 447 ? THR E 750  ALA E 751  
AD8 1 SER E 416 ? GLN E 423 ? SER E 720  GLN E 727  
AD8 2 CYS E 428 ? VAL E 438 ? CYS E 732  VAL E 742  
AD8 3 GLU E 481 ? ASP E 491 ? GLU E 785  ASP E 795  
AD8 4 VAL E 497 ? GLN E 502 ? VAL E 801  GLN E 806  
AD9 1 GLU E 507 ? CYS E 515 ? GLU E 811  CYS E 819  
AD9 2 TYR E 524 ? MET E 531 ? TYR E 828  MET E 835  
AD9 3 GLY E 542 ? GLN E 548 ? GLY E 846  GLN E 852  
AD9 4 GLN E 555 ? VAL E 562 ? GLN E 859  VAL E 866  
AE1 1 VAL E 566 ? PHE E 572 ? VAL E 870  PHE E 876  
AE1 2 LYS E 575 ? ILE E 580 ? LYS E 879  ILE E 884  
AE1 3 THR E 583 ? TRP E 589 ? THR E 887  TRP E 893  
AE1 4 LEU E 595 ? TYR E 602 ? LEU E 899  TYR E 906  
AE2 1 TYR E 609 ? LYS E 613 ? TYR E 913  LYS E 917  
AE2 2 PHE E 616 ? ASP E 621 ? PHE E 920  ASP E 925  
AE2 3 SER E 625 ? LYS E 632 ? SER E 929  LYS E 936  
AE2 4 ASN E 637 ? PHE E 645 ? ASN E 941  PHE E 949  
AE3 1 MET E 650 ? ILE E 655 ? MET E 954  ILE E 959  
AE3 2 ASN E 660 ? GLU E 665 ? ASN E 964  GLU E 969  
AE3 3 ASN E 669 ? LYS E 675 ? ASN E 973  LYS E 979  
AE3 4 LEU E 688 ? HIS E 695 ? LEU E 992  HIS E 999  
AE4 1 PHE E 772 ? HIS E 773 ? PHE E 1076 HIS E 1077 
AE4 2 THR E 778 ? GLU E 779 ? THR E 1082 GLU E 1083 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 32  ? N LEU A 101  O VAL A 86  ? O VAL A 155  
AA1 2 3 N LEU A 99  ? N LEU A 168  O LYS A 112 ? O LYS A 181  
AA1 3 4 O VAL A 113 ? O VAL A 182  N GLN A 10  ? N GLN A 79   
AA1 4 5 N PRO A 13  ? N PRO A 82   O ALA A 52  ? O ALA A 121  
AA1 5 6 N PHE A 51  ? N PHE A 120  O ALA A 70  ? O ALA A 139  
AA1 6 7 N ARG A 76  ? N ARG A 145  O LYS A 87  ? O LYS A 156  
AA2 1 2 O ILE A 262 ? O ILE A 331  N LEU A 252 ? N LEU A 321  
AA2 2 3 N SER A 251 ? N SER A 320  O THR A 356 ? O THR A 425  
AA3 1 2 N ALA A 278 ? N ALA A 347  O THR A 290 ? O THR A 359  
AA3 2 3 N LEU A 291 ? N LEU A 360  O LEU A 348 ? O LEU A 417  
AA3 3 4 O GLY A 347 ? O GLY A 416  N TRP A 331 ? N TRP A 400  
AA3 4 5 O GLY A 330 ? O GLY A 399  N ALA A 320 ? N ALA A 389  
AA3 5 6 O GLN A 321 ? O GLN A 390  N ASN A 300 ? N ASN A 369  
AA4 1 2 N CYS B 704 ? N CYS B 1008 O LEU B 725 ? O LEU B 1029 
AA4 2 3 N GLN B 721 ? N GLN B 1025 O SER B 738 ? O SER B 1042 
AA4 3 4 O THR B 737 ? O THR B 1041 N TYR B 5   ? N TYR B 5    
AA4 4 5 N VAL B 6   ? N VAL B 6    O ILE B 785 ? O ILE B 1089 
AA5 1 2 N GLY B 21  ? N GLY B 21   O ASN B 30  ? O ASN B 30   
AA5 2 3 N ILE B 33  ? N ILE B 33   O GLU B 40  ? O GLU B 40   
AA5 3 4 N VAL B 43  ? N VAL B 43   O ARG B 50  ? O ARG B 50   
AA6 1 2 N GLU B 65  ? N GLU B 65   O PHE B 78  ? O PHE B 78   
AA6 2 3 N LEU B 77  ? N LEU B 77   O LEU B 89  ? O LEU B 89   
AA6 3 4 N ALA B 86  ? N ALA B 86   O GLY B 106 ? O GLY B 106  
AA7 1 2 N ARG B 114 ? N ARG B 114  O ASP B 137 ? O ASP B 137  
AA8 1 2 N ILE B 123 ? N ILE B 123  O GLY B 132 ? O GLY B 132  
AA8 2 3 N ILE B 131 ? N ILE B 131  O ILE B 143 ? O ILE B 143  
AA8 3 4 N PHE B 140 ? N PHE B 140  O ILE B 157 ? O ILE B 157  
AA9 1 2 N ILE B 165 ? N ILE B 165  O VAL B 181 ? O VAL B 181  
AA9 2 3 N PHE B 180 ? N PHE B 180  O LYS B 191 ? O LYS B 191  
AA9 3 4 N GLU B 194 ? N GLU B 194  O ASN B 203 ? O ASN B 203  
AB1 1 2 N ILE B 220 ? N ILE B 220  O ILE B 230 ? O ILE B 230  
AB1 2 3 N ILE B 231 ? N ILE B 231  O THR B 238 ? O THR B 238  
AB1 3 4 N TYR B 239 ? N TYR B 239  O LEU B 246 ? O LEU B 246  
AB2 1 2 N ASN B 262 ? N ASN B 262  O LEU B 272 ? O LEU B 272  
AB2 2 3 N LEU B 273 ? N LEU B 273  O PHE B 281 ? O PHE B 281  
AB2 3 4 N GLU B 286 ? N GLU B 286  O ASP B 299 ? O ASP B 299  
AB3 1 2 N LEU B 317 ? N LEU B 317  O VAL B 321 ? O VAL B 321  
AB3 2 3 N VAL B 324 ? N VAL B 324  O GLN B 332 ? O GLN B 332  
AB3 3 4 N SER B 331 ? N SER B 331  O PHE B 353 ? O PHE B 353  
AB4 1 2 N VAL B 365 ? N VAL B 365  O GLN B 374 ? O GLN B 374  
AB4 2 3 N LEU B 375 ? N LEU B 375  O ILE B 390 ? O ILE B 390  
AB4 3 4 N ARG B 391 ? N ARG B 391  O HIS B 407 ? O HIS B 711  
AB5 1 2 N ARG B 418 ? N ARG B 722  O LEU B 432 ? O LEU B 736  
AB5 2 3 N VAL B 438 ? N VAL B 742  O THR B 446 ? O THR B 750  
AB6 1 2 N ARG B 418 ? N ARG B 722  O LEU B 432 ? O LEU B 736  
AB6 2 3 N GLU B 437 ? N GLU B 741  O VAL B 482 ? O VAL B 786  
AB6 3 4 N LEU B 487 ? N LEU B 791  O HIS B 501 ? O HIS B 805  
AB7 1 2 N LEU B 510 ? N LEU B 814  O GLY B 528 ? O GLY B 832  
AB7 2 3 N VAL B 527 ? N VAL B 831  O VAL B 545 ? O VAL B 849  
AB7 3 4 N ILE B 544 ? N ILE B 848  O LYS B 560 ? O LYS B 864  
AB8 1 2 N VAL B 570 ? N VAL B 874  O LEU B 577 ? O LEU B 881  
AB8 2 3 N LEU B 576 ? N LEU B 880  O TYR B 587 ? O TYR B 891  
AB8 3 4 N VAL B 584 ? N VAL B 888  O HIS B 601 ? O HIS B 905  
AB9 1 2 N LYS B 611 ? N LYS B 915  O LEU B 618 ? O LEU B 922  
AB9 2 3 N ILE B 617 ? N ILE B 921  O LEU B 629 ? O LEU B 933  
AB9 3 4 N LEU B 628 ? N LEU B 932  O ILE B 641 ? O ILE B 945  
AC1 1 2 N GLU B 654 ? N GLU B 958  O LEU B 662 ? O LEU B 966  
AC1 2 3 N GLU B 665 ? N GLU B 969  O ASN B 669 ? O ASN B 973  
AC1 3 4 N VAL B 672 ? N VAL B 976  O VAL B 691 ? O VAL B 995  
AC2 1 2 N PHE B 772 ? N PHE B 1076 O GLU B 779 ? O GLU B 1083 
AC3 1 2 N GLN D 10  ? N GLN D 79   O VAL D 113 ? O VAL D 182  
AC3 2 3 O GLN D 114 ? O GLN D 183  N LYS D 97  ? N LYS D 166  
AC3 3 4 O ALA D 90  ? O ALA D 159  N LEU D 28  ? N LEU D 97   
AC4 1 2 N GLN D 10  ? N GLN D 79   O VAL D 113 ? O VAL D 182  
AC4 2 3 O GLN D 114 ? O GLN D 183  N LYS D 97  ? N LYS D 166  
AC4 3 4 O LYS D 87  ? O LYS D 156  N ARG D 76  ? N ARG D 145  
AC4 4 5 O THR D 68  ? O THR D 137  N VAL D 53  ? N VAL D 122  
AC5 1 2 O ILE D 262 ? O ILE D 331  N LEU D 252 ? N LEU D 321  
AC5 2 3 N CYS D 253 ? N CYS D 322  O LEU D 354 ? O LEU D 423  
AC6 1 2 N TYR D 280 ? N TYR D 349  O HIS D 288 ? O HIS D 357  
AC6 2 3 N VAL D 293 ? N VAL D 362  O TRP D 346 ? O TRP D 415  
AC6 3 4 O PHE D 345 ? O PHE D 414  N PHE D 333 ? N PHE D 402  
AC6 4 5 O LYS D 332 ? O LYS D 401  N THR D 318 ? N THR D 387  
AC6 5 6 O GLN D 321 ? O GLN D 390  N ASN D 300 ? N ASN D 369  
AC7 1 2 N CYS E 704 ? N CYS E 1008 O LEU E 725 ? O LEU E 1029 
AC7 2 3 N VAL E 724 ? N VAL E 1028 O VAL E 736 ? O VAL E 1040 
AC7 3 4 O LEU E 739 ? O LEU E 1043 N TYR E 3   ? N TYR E 3    
AC7 4 5 N VAL E 6   ? N VAL E 6    O ILE E 785 ? O ILE E 1089 
AC8 1 2 N GLY E 17  ? N GLY E 17   O ALA E 34  ? O ALA E 34   
AC8 2 3 N ILE E 33  ? N ILE E 33   O GLU E 40  ? O GLU E 40   
AC8 3 4 N ILE E 41  ? N ILE E 41   O LYS E 53  ? O LYS E 53   
AC9 1 2 N PHE E 67  ? N PHE E 67   O LEU E 76  ? O LEU E 76   
AC9 2 3 N THR E 81  ? N THR E 81   O ASN E 85  ? O ASN E 85   
AC9 3 4 N ALA E 86  ? N ALA E 86   O GLY E 106 ? O GLY E 106  
AD1 1 2 N ILE E 123 ? N ILE E 123  O GLY E 132 ? O GLY E 132  
AD1 2 3 N ILE E 131 ? N ILE E 131  O ILE E 143 ? O ILE E 143  
AD1 3 4 N VAL E 142 ? N VAL E 142  O PHE E 155 ? O PHE E 155  
AD2 1 2 N ILE E 165 ? N ILE E 165  O VAL E 181 ? O VAL E 181  
AD2 2 3 N ILE E 178 ? N ILE E 178  O TYR E 193 ? O TYR E 193  
AD2 3 4 N GLU E 194 ? N GLU E 194  O ASN E 203 ? O ASN E 203  
AD3 1 2 N ILE E 220 ? N ILE E 220  O ILE E 230 ? O ILE E 230  
AD3 2 3 N ILE E 231 ? N ILE E 231  O THR E 238 ? O THR E 238  
AD3 3 4 N TYR E 239 ? N TYR E 239  O LEU E 246 ? O LEU E 246  
AD4 1 2 N ASN E 262 ? N ASN E 262  O LEU E 272 ? O LEU E 272  
AD4 2 3 N LEU E 273 ? N LEU E 273  O PHE E 281 ? O PHE E 281  
AD4 3 4 N MET E 282 ? N MET E 282  O GLU E 303 ? O GLU E 303  
AD5 1 2 N THR E 315 ? N THR E 315  O PHE E 323 ? O PHE E 323  
AD5 2 3 N VAL E 324 ? N VAL E 324  O GLN E 332 ? O GLN E 332  
AD5 3 4 N SER E 331 ? N SER E 331  O PHE E 353 ? O PHE E 353  
AD6 1 2 N CYS E 363 ? N CYS E 363  O VAL E 376 ? O VAL E 376  
AD6 2 3 N SER E 379 ? N SER E 379  O SER E 386 ? O SER E 386  
AD6 3 4 N LEU E 387 ? N LEU E 387  O VAL E 411 ? O VAL E 715  
AD7 1 2 N ARG E 418 ? N ARG E 722  O LEU E 432 ? O LEU E 736  
AD7 2 3 N VAL E 438 ? N VAL E 742  O THR E 446 ? O THR E 750  
AD8 1 2 N ARG E 418 ? N ARG E 722  O LEU E 432 ? O LEU E 736  
AD8 2 3 N VAL E 431 ? N VAL E 735  O LEU E 488 ? O LEU E 792  
AD8 3 4 N ILE E 489 ? N ILE E 793  O LEU E 498 ? O LEU E 802  
AD9 1 2 N CYS E 515 ? N CYS E 819  O TYR E 524 ? O TYR E 828  
AD9 2 3 N VAL E 527 ? N VAL E 831  O VAL E 545 ? O VAL E 849  
AD9 3 4 N VAL E 546 ? N VAL E 850  O VAL E 557 ? O VAL E 861  
AE1 1 2 N PHE E 572 ? N PHE E 876  O LYS E 575 ? O LYS E 879  
AE1 2 3 N LEU E 576 ? N LEU E 880  O TYR E 587 ? O TYR E 891  
AE1 3 4 N LEU E 586 ? N LEU E 890  O GLU E 598 ? O GLU E 902  
AE2 1 2 N LYS E 611 ? N LYS E 915  O LEU E 618 ? O LEU E 922  
AE2 2 3 N ILE E 617 ? N ILE E 921  O LEU E 629 ? O LEU E 933  
AE2 3 4 N ALA E 630 ? N ALA E 934  O GLU E 639 ? O GLU E 943  
AE3 1 2 N ALA E 652 ? N ALA E 956  O ALA E 664 ? O ALA E 968  
AE3 2 3 N GLY E 663 ? N GLY E 967  O PHE E 671 ? O PHE E 975  
AE3 3 4 N LEU E 670 ? N LEU E 974  O PHE E 694 ? O PHE E 998  
AE4 1 2 N PHE E 772 ? N PHE E 1076 O GLU E 779 ? O GLU E 1083 
# 
_pdbx_entry_details.entry_id                   9DJX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             D 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              268 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             D 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              268 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             D 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              268 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                96.91 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            -13.49 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET A 88   ? ? -166.74 -22.48  
2  1 PHE A 102  ? ? -99.41  -61.73  
3  1 LYS A 116  ? ? -102.93 -154.64 
4  1 ARG A 162  ? ? -109.02 -67.34  
5  1 CYS A 205  ? ? -83.79  36.16   
6  1 CYS A 234  ? ? -68.63  4.10    
7  1 ASN A 267  ? ? -170.27 -165.81 
8  1 LEU A 268  ? ? -36.56  123.50  
9  1 ASP A 270  ? ? -172.25 -120.39 
10 1 GLN A 325  ? ? -85.18  -72.57  
11 1 GLU A 328  ? ? -155.30 49.72   
12 1 THR A 329  ? ? -156.17 89.79   
13 1 PHE A 338  ? ? -136.64 -159.08 
14 1 LEU A 342  ? ? -69.36  0.75    
15 1 MET A 346  ? ? -104.88 76.27   
16 1 PRO A 352  ? ? -67.34  6.88    
17 1 GLN B 10   ? ? -163.13 116.56  
18 1 ASN B 36   ? ? 59.27   -115.05 
19 1 THR B 37   ? ? -83.62  44.20   
20 1 ARG B 147  ? ? 74.50   166.53  
21 1 ASN B 149  ? ? -110.17 55.55   
22 1 ASN B 211  ? ? -171.73 130.84  
23 1 PRO B 223  ? ? -58.06  175.73  
24 1 ASN B 241  ? ? -162.04 92.87   
25 1 ASP B 275  ? ? -103.13 -158.65 
26 1 ASP B 318  ? ? 170.63  156.85  
27 1 GLU B 351  ? ? -171.23 135.01  
28 1 GLN B 372  ? ? -121.67 -72.30  
29 1 PHE B 382  ? ? 49.54   -137.33 
30 1 GLU B 719  ? ? -170.44 137.13  
31 1 GLN B 845  ? ? -174.54 143.80  
32 1 ALA B 862  ? ? 68.86   157.55  
33 1 LYS B 867  ? ? -111.78 66.38   
34 1 ASN B 885  ? ? 58.28   -123.74 
35 1 SER B 886  ? ? -91.01  30.77   
36 1 ALA B 911  ? ? -62.40  86.15   
37 1 MET B 927  ? ? -93.46  54.49   
38 1 ARG B 928  ? ? 37.81   60.40   
39 1 LEU B 931  ? ? -167.97 111.54  
40 1 ASN B 970  ? ? 48.19   -118.46 
41 1 ASP B 986  ? ? -166.29 -29.55  
42 1 GLN B 990  ? ? -88.88  49.63   
43 1 ARG B 1138 ? ? -79.81  46.36   
44 1 ASP D 76   ? ? -146.07 32.76   
45 1 PRO D 93   ? ? -39.54  121.31  
46 1 PHE D 102  ? ? -140.77 -55.17  
47 1 LYS D 116  ? ? -134.94 -109.22 
48 1 ILE D 152  ? ? -116.43 -163.92 
49 1 ARG D 162  ? ? -95.55  -73.96  
50 1 LEU D 170  ? ? -149.70 41.26   
51 1 PHE D 232  ? ? -102.72 40.69   
52 1 ASN D 267  ? ? -179.59 -170.88 
53 1 ASP D 270  ? ? -92.68  -127.66 
54 1 SER D 275  ? ? -107.03 -62.28  
55 1 GLU D 328  ? ? -140.75 -32.96  
56 1 ILE D 393  ? ? -127.17 -69.06  
57 1 ASN E 36   ? ? 66.48   -90.82  
58 1 VAL E 52   ? ? -132.00 -48.74  
59 1 TYR E 58   ? ? -85.60  47.55   
60 1 LYS E 83   ? ? -69.15  4.44    
61 1 SER E 94   ? ? -109.79 56.17   
62 1 GLU E 127  ? ? -85.62  44.21   
63 1 CYS E 128  ? ? 48.09   -115.38 
64 1 ARG E 129  ? ? 73.84   -59.71  
65 1 LYS E 200  ? ? 47.84   29.42   
66 1 ASN E 211  ? ? -161.22 117.02  
67 1 ASN E 241  ? ? -164.96 84.60   
68 1 LYS E 254  ? ? -81.57  42.51   
69 1 GLN E 255  ? ? -140.75 -16.13  
70 1 PRO E 266  ? ? -63.41  0.03    
71 1 THR E 308  ? ? -124.29 -160.60 
72 1 LEU E 317  ? ? -92.85  -72.80  
73 1 ASP E 318  ? ? 175.92  160.90  
74 1 ASN E 341  ? ? -93.08  -159.91 
75 1 PHE E 382  ? ? 50.89   -141.50 
76 1 GLN E 759  ? ? -96.67  57.64   
77 1 SER E 854  ? ? -39.50  85.31   
78 1 ASP E 855  ? ? 173.08  -65.10  
79 1 LYS E 867  ? ? -94.47  56.74   
80 1 ASN E 877  ? ? 60.46   63.88   
81 1 ASN E 885  ? ? 56.02   -129.03 
82 1 MET E 927  ? ? -95.69  59.33   
83 1 LEU E 931  ? ? -176.56 131.11  
84 1 ASN E 952  ? ? -177.17 145.71  
85 1 ALA E 956  ? ? -174.92 143.85  
86 1 ASN E 970  ? ? 45.31   -121.52 
87 1 PHE E 972  ? ? 38.63   60.02   
88 1 ALA E 983  ? ? -95.18  31.63   
89 1 GLN E 990  ? ? -88.91  32.77   
90 1 VAL E 995  ? ? -143.59 14.04   
91 1 SER E 1027 ? ? -165.36 95.09   
92 1 ASP E 1099 ? ? -105.85 49.80   
# 
_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         27.8091 
_pdbx_refine_tls.origin_y         10.6137 
_pdbx_refine_tls.origin_z         -20.8680 
_pdbx_refine_tls.T[1][1]          0.7947 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0325 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0532 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.9514 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0062 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.9293 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1178 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2182 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0099 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6948 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0389 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.2426 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0381 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0174 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0264 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0356 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0659 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0646 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0288 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0107 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0291 
_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_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 ARG 70   ? A ARG 1   
2   1 Y 1 A THR 71   ? A THR 2   
3   1 Y 1 A LEU 72   ? A LEU 3   
4   1 Y 1 A SER 126  ? A SER 57  
5   1 Y 1 A ASN 127  ? A ASN 58  
6   1 Y 1 A VAL 128  ? A VAL 59  
7   1 Y 1 A GLN 129  ? A GLN 60  
8   1 Y 1 A GLU 130  ? A GLU 61  
9   1 Y 1 A ARG 131  ? A ARG 62  
10  1 Y 1 A GLU 132  ? A GLU 63  
11  1 Y 1 A LYS 211  ? A LYS 142 
12  1 Y 1 A PRO 212  ? A PRO 143 
13  1 Y 1 A VAL 213  ? A VAL 144 
14  1 Y 1 A SER 214  ? A SER 145 
15  1 Y 1 A ARG 215  ? A ARG 146 
16  1 Y 1 A GLU 216  ? A GLU 147 
17  1 Y 1 A ASP 217  ? A ASP 148 
18  1 Y 1 A GLN 218  ? A GLN 149 
19  1 Y 1 A CYS 219  ? A CYS 150 
20  1 Y 1 A ASP 428  ? A ASP 359 
21  1 Y 1 A THR 429  ? A THR 360 
22  1 Y 1 A GLU 430  ? A GLU 361 
23  1 Y 1 A ASP 431  ? A ASP 362 
24  1 Y 1 A GLU 432  ? A GLU 363 
25  1 Y 1 A ILE 433  ? A ILE 364 
26  1 Y 1 A SER 434  ? A SER 365 
27  1 Y 1 A PRO 435  ? A PRO 366 
28  1 Y 1 A ASP 436  ? A ASP 367 
29  1 Y 1 A LYS 437  ? A LYS 368 
30  1 Y 1 B MET 1    ? B MET 1   
31  1 Y 1 B GLY 697  ? B GLY 393 
32  1 Y 1 B ILE 698  ? B ILE 394 
33  1 Y 1 B GLY 699  ? B GLY 395 
34  1 Y 1 B GLY 700  ? B GLY 396 
35  1 Y 1 B ASN 701  ? B ASN 397 
36  1 Y 1 B GLY 702  ? B GLY 398 
37  1 Y 1 B ASN 703  ? B ASN 399 
38  1 Y 1 B SER 704  ? B SER 400 
39  1 Y 1 B GLY 705  ? B GLY 401 
40  1 Y 1 B GLU 706  ? B GLU 402 
41  1 Y 1 B ILE 707  ? B ILE 403 
42  1 Y 1 B GLN 708  ? B GLN 404 
43  1 Y 1 B LYS 709  ? B LYS 405 
44  1 Y 1 B SER 774  ? B SER 470 
45  1 Y 1 B THR 775  ? B THR 471 
46  1 Y 1 B ALA 776  ? B ALA 472 
47  1 Y 1 B PRO 777  ? B PRO 473 
48  1 Y 1 B HIS 778  ? B HIS 474 
49  1 Y 1 B GLU 779  ? B GLU 475 
50  1 Y 1 B SER 981  ? B SER 677 
51  1 Y 1 B ALA 982  ? B ALA 678 
52  1 Y 1 B ALA 983  ? B ALA 679 
53  1 Y 1 B THR 984  ? B THR 680 
54  1 Y 1 B GLN 1015 ? B GLN 711 
55  1 Y 1 B ASN 1016 ? B ASN 712 
56  1 Y 1 B LEU 1017 ? B LEU 713 
57  1 Y 1 B GLY 1018 ? B GLY 714 
58  1 Y 1 B GLU 1019 ? B GLU 715 
59  1 Y 1 B THR 1020 ? B THR 716 
60  1 Y 1 B SER 1021 ? B SER 717 
61  1 Y 1 B THR 1022 ? B THR 718 
62  1 Y 1 B GLN 1113 ? B GLN 809 
63  1 Y 1 B TYR 1114 ? B TYR 810 
64  1 Y 1 B ASP 1115 ? B ASP 811 
65  1 Y 1 B ASP 1116 ? B ASP 812 
66  1 Y 1 B GLY 1117 ? B GLY 813 
67  1 Y 1 B SER 1118 ? B SER 814 
68  1 Y 1 B GLY 1119 ? B GLY 815 
69  1 Y 1 B MET 1120 ? B MET 816 
70  1 Y 1 B LYS 1121 ? B LYS 817 
71  1 Y 1 B ARG 1122 ? B ARG 818 
72  1 Y 1 C SER 866  ? C SER 1   
73  1 Y 1 C GLN 867  ? C GLN 2   
74  1 Y 1 C ARG 894  ? C ARG 29  
75  1 Y 1 C GLN 895  ? C GLN 30  
76  1 Y 1 D ARG 70   ? D ARG 1   
77  1 Y 1 D THR 71   ? D THR 2   
78  1 Y 1 D LEU 72   ? D LEU 3   
79  1 Y 1 D HIS 73   ? D HIS 4   
80  1 Y 1 D ASP 74   ? D ASP 5   
81  1 Y 1 D SER 126  ? D SER 57  
82  1 Y 1 D ASN 127  ? D ASN 58  
83  1 Y 1 D VAL 128  ? D VAL 59  
84  1 Y 1 D GLN 129  ? D GLN 60  
85  1 Y 1 D GLU 130  ? D GLU 61  
86  1 Y 1 D ARG 131  ? D ARG 62  
87  1 Y 1 D GLU 132  ? D GLU 63  
88  1 Y 1 D GLN 148  ? D GLN 79  
89  1 Y 1 D ASP 149  ? D ASP 80  
90  1 Y 1 D PHE 150  ? D PHE 81  
91  1 Y 1 D GLN 173  ? D GLN 104 
92  1 Y 1 D SER 174  ? D SER 105 
93  1 Y 1 D ASP 175  ? D ASP 106 
94  1 Y 1 D GLY 176  ? D GLY 107 
95  1 Y 1 D SER 214  ? D SER 145 
96  1 Y 1 D ARG 215  ? D ARG 146 
97  1 Y 1 D GLU 216  ? D GLU 147 
98  1 Y 1 D ASP 217  ? D ASP 148 
99  1 Y 1 D GLN 218  ? D GLN 149 
100 1 Y 1 D CYS 219  ? D CYS 150 
101 1 Y 1 D ASP 428  ? D ASP 359 
102 1 Y 1 D THR 429  ? D THR 360 
103 1 Y 1 D GLU 430  ? D GLU 361 
104 1 Y 1 D ASP 431  ? D ASP 362 
105 1 Y 1 D GLU 432  ? D GLU 363 
106 1 Y 1 D ILE 433  ? D ILE 364 
107 1 Y 1 D SER 434  ? D SER 365 
108 1 Y 1 D PRO 435  ? D PRO 366 
109 1 Y 1 D ASP 436  ? D ASP 367 
110 1 Y 1 D LYS 437  ? D LYS 368 
111 1 Y 1 E MET 1    ? E MET 1   
112 1 Y 1 E GLY 697  ? E GLY 393 
113 1 Y 1 E ILE 698  ? E ILE 394 
114 1 Y 1 E GLY 699  ? E GLY 395 
115 1 Y 1 E GLY 700  ? E GLY 396 
116 1 Y 1 E ASN 701  ? E ASN 397 
117 1 Y 1 E GLY 702  ? E GLY 398 
118 1 Y 1 E ASN 703  ? E ASN 399 
119 1 Y 1 E SER 704  ? E SER 400 
120 1 Y 1 E GLY 705  ? E GLY 401 
121 1 Y 1 E GLU 706  ? E GLU 402 
122 1 Y 1 E ILE 707  ? E ILE 403 
123 1 Y 1 E GLN 708  ? E GLN 404 
124 1 Y 1 E LYS 709  ? E LYS 405 
125 1 Y 1 E ASP 744  ? E ASP 440 
126 1 Y 1 E SER 772  ? E SER 468 
127 1 Y 1 E SER 773  ? E SER 469 
128 1 Y 1 E SER 774  ? E SER 470 
129 1 Y 1 E THR 775  ? E THR 471 
130 1 Y 1 E ALA 776  ? E ALA 472 
131 1 Y 1 E PRO 777  ? E PRO 473 
132 1 Y 1 E HIS 778  ? E HIS 474 
133 1 Y 1 E GLU 779  ? E GLU 475 
134 1 Y 1 E GLN 1015 ? E GLN 711 
135 1 Y 1 E ASN 1016 ? E ASN 712 
136 1 Y 1 E LEU 1017 ? E LEU 713 
137 1 Y 1 E GLY 1018 ? E GLY 714 
138 1 Y 1 E GLU 1019 ? E GLU 715 
139 1 Y 1 E THR 1020 ? E THR 716 
140 1 Y 1 E SER 1021 ? E SER 717 
141 1 Y 1 E THR 1022 ? E THR 718 
142 1 Y 1 E TYR 1114 ? E TYR 810 
143 1 Y 1 E ASP 1115 ? E ASP 811 
144 1 Y 1 E ASP 1116 ? E ASP 812 
145 1 Y 1 E GLY 1117 ? E GLY 813 
146 1 Y 1 E SER 1118 ? E SER 814 
147 1 Y 1 E GLY 1119 ? E GLY 815 
148 1 Y 1 E MET 1120 ? E MET 816 
149 1 Y 1 E LYS 1121 ? E LYS 817 
150 1 Y 1 E ARG 1122 ? E ARG 818 
151 1 Y 1 E GLU 1123 ? E GLU 819 
152 1 Y 1 F SER 866  ? F SER 1   
153 1 Y 1 F GLN 867  ? F GLN 2   
154 1 Y 1 F GLN 895  ? F GLN 30  
# 
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 
A1A5I C1   C  Y N 1   
A1A5I C2   C  Y N 2   
A1A5I C3   C  Y N 3   
A1A5I C12  C  N S 4   
A1A5I C13  C  N N 5   
A1A5I C14  C  N N 6   
A1A5I C15  C  N N 7   
A1A5I C17  C  N N 8   
A1A5I C20  C  N R 9   
A1A5I C21  C  N N 10  
A1A5I C22  C  N N 11  
A1A5I C23  C  N S 12  
A1A5I C25  C  N N 13  
A1A5I C26  C  N N 14  
A1A5I C27  C  N N 15  
A1A5I C28  C  N N 16  
A1A5I C4   C  Y N 17  
A1A5I C5   C  Y N 18  
A1A5I C6   C  Y N 19  
A1A5I C7   C  N N 20  
A1A5I C9   C  N N 21  
A1A5I N16  N  N N 22  
A1A5I N24  N  N N 23  
A1A5I N8   N  N N 24  
A1A5I O10  O  N N 25  
A1A5I O11  O  N N 26  
A1A5I O18  O  N N 27  
A1A5I O19  O  N N 28  
A1A5I H1   H  N N 29  
A1A5I H2   H  N N 30  
A1A5I H3   H  N N 31  
A1A5I H4   H  N N 32  
A1A5I H5   H  N N 33  
A1A5I H6   H  N N 34  
A1A5I H7   H  N N 35  
A1A5I H8   H  N N 36  
A1A5I H9   H  N N 37  
A1A5I H10  H  N N 38  
A1A5I H11  H  N N 39  
A1A5I H12  H  N N 40  
A1A5I H13  H  N N 41  
A1A5I H14  H  N N 42  
A1A5I H15  H  N N 43  
A1A5I H16  H  N N 44  
A1A5I H17  H  N N 45  
A1A5I H18  H  N N 46  
A1A5I H19  H  N N 47  
A1A5I H20  H  N N 48  
A1A5I H21  H  N N 49  
A1A5I H22  H  N N 50  
A1A5I H23  H  N N 51  
A1A5I H24  H  N N 52  
A1A5I H25  H  N N 53  
A1A5I H26  H  N N 54  
A1A5I H27  H  N N 55  
ALA   N    N  N N 56  
ALA   CA   C  N S 57  
ALA   C    C  N N 58  
ALA   O    O  N N 59  
ALA   CB   C  N N 60  
ALA   OXT  O  N N 61  
ALA   H    H  N N 62  
ALA   H2   H  N N 63  
ALA   HA   H  N N 64  
ALA   HB1  H  N N 65  
ALA   HB2  H  N N 66  
ALA   HB3  H  N N 67  
ALA   HXT  H  N N 68  
ARG   N    N  N N 69  
ARG   CA   C  N S 70  
ARG   C    C  N N 71  
ARG   O    O  N N 72  
ARG   CB   C  N N 73  
ARG   CG   C  N N 74  
ARG   CD   C  N N 75  
ARG   NE   N  N N 76  
ARG   CZ   C  N N 77  
ARG   NH1  N  N N 78  
ARG   NH2  N  N N 79  
ARG   OXT  O  N N 80  
ARG   H    H  N N 81  
ARG   H2   H  N N 82  
ARG   HA   H  N N 83  
ARG   HB2  H  N N 84  
ARG   HB3  H  N N 85  
ARG   HG2  H  N N 86  
ARG   HG3  H  N N 87  
ARG   HD2  H  N N 88  
ARG   HD3  H  N N 89  
ARG   HE   H  N N 90  
ARG   HH11 H  N N 91  
ARG   HH12 H  N N 92  
ARG   HH21 H  N N 93  
ARG   HH22 H  N N 94  
ARG   HXT  H  N N 95  
ASN   N    N  N N 96  
ASN   CA   C  N S 97  
ASN   C    C  N N 98  
ASN   O    O  N N 99  
ASN   CB   C  N N 100 
ASN   CG   C  N N 101 
ASN   OD1  O  N N 102 
ASN   ND2  N  N N 103 
ASN   OXT  O  N N 104 
ASN   H    H  N N 105 
ASN   H2   H  N N 106 
ASN   HA   H  N N 107 
ASN   HB2  H  N N 108 
ASN   HB3  H  N N 109 
ASN   HD21 H  N N 110 
ASN   HD22 H  N N 111 
ASN   HXT  H  N N 112 
ASP   N    N  N N 113 
ASP   CA   C  N S 114 
ASP   C    C  N N 115 
ASP   O    O  N N 116 
ASP   CB   C  N N 117 
ASP   CG   C  N N 118 
ASP   OD1  O  N N 119 
ASP   OD2  O  N N 120 
ASP   OXT  O  N N 121 
ASP   H    H  N N 122 
ASP   H2   H  N N 123 
ASP   HA   H  N N 124 
ASP   HB2  H  N N 125 
ASP   HB3  H  N N 126 
ASP   HD2  H  N N 127 
ASP   HXT  H  N N 128 
CYS   N    N  N N 129 
CYS   CA   C  N R 130 
CYS   C    C  N N 131 
CYS   O    O  N N 132 
CYS   CB   C  N N 133 
CYS   SG   S  N N 134 
CYS   OXT  O  N N 135 
CYS   H    H  N N 136 
CYS   H2   H  N N 137 
CYS   HA   H  N N 138 
CYS   HB2  H  N N 139 
CYS   HB3  H  N N 140 
CYS   HG   H  N N 141 
CYS   HXT  H  N N 142 
GLN   N    N  N N 143 
GLN   CA   C  N S 144 
GLN   C    C  N N 145 
GLN   O    O  N N 146 
GLN   CB   C  N N 147 
GLN   CG   C  N N 148 
GLN   CD   C  N N 149 
GLN   OE1  O  N N 150 
GLN   NE2  N  N N 151 
GLN   OXT  O  N N 152 
GLN   H    H  N N 153 
GLN   H2   H  N N 154 
GLN   HA   H  N N 155 
GLN   HB2  H  N N 156 
GLN   HB3  H  N N 157 
GLN   HG2  H  N N 158 
GLN   HG3  H  N N 159 
GLN   HE21 H  N N 160 
GLN   HE22 H  N N 161 
GLN   HXT  H  N N 162 
GLU   N    N  N N 163 
GLU   CA   C  N S 164 
GLU   C    C  N N 165 
GLU   O    O  N N 166 
GLU   CB   C  N N 167 
GLU   CG   C  N N 168 
GLU   CD   C  N N 169 
GLU   OE1  O  N N 170 
GLU   OE2  O  N N 171 
GLU   OXT  O  N N 172 
GLU   H    H  N N 173 
GLU   H2   H  N N 174 
GLU   HA   H  N N 175 
GLU   HB2  H  N N 176 
GLU   HB3  H  N N 177 
GLU   HG2  H  N N 178 
GLU   HG3  H  N N 179 
GLU   HE2  H  N N 180 
GLU   HXT  H  N N 181 
GLY   N    N  N N 182 
GLY   CA   C  N N 183 
GLY   C    C  N N 184 
GLY   O    O  N N 185 
GLY   OXT  O  N N 186 
GLY   H    H  N N 187 
GLY   H2   H  N N 188 
GLY   HA2  H  N N 189 
GLY   HA3  H  N N 190 
GLY   HXT  H  N N 191 
HIS   N    N  N N 192 
HIS   CA   C  N S 193 
HIS   C    C  N N 194 
HIS   O    O  N N 195 
HIS   CB   C  N N 196 
HIS   CG   C  Y N 197 
HIS   ND1  N  Y N 198 
HIS   CD2  C  Y N 199 
HIS   CE1  C  Y N 200 
HIS   NE2  N  Y N 201 
HIS   OXT  O  N N 202 
HIS   H    H  N N 203 
HIS   H2   H  N N 204 
HIS   HA   H  N N 205 
HIS   HB2  H  N N 206 
HIS   HB3  H  N N 207 
HIS   HD1  H  N N 208 
HIS   HD2  H  N N 209 
HIS   HE1  H  N N 210 
HIS   HE2  H  N N 211 
HIS   HXT  H  N N 212 
HOH   O    O  N N 213 
HOH   H1   H  N N 214 
HOH   H2   H  N N 215 
ILE   N    N  N N 216 
ILE   CA   C  N S 217 
ILE   C    C  N N 218 
ILE   O    O  N N 219 
ILE   CB   C  N S 220 
ILE   CG1  C  N N 221 
ILE   CG2  C  N N 222 
ILE   CD1  C  N N 223 
ILE   OXT  O  N N 224 
ILE   H    H  N N 225 
ILE   H2   H  N N 226 
ILE   HA   H  N N 227 
ILE   HB   H  N N 228 
ILE   HG12 H  N N 229 
ILE   HG13 H  N N 230 
ILE   HG21 H  N N 231 
ILE   HG22 H  N N 232 
ILE   HG23 H  N N 233 
ILE   HD11 H  N N 234 
ILE   HD12 H  N N 235 
ILE   HD13 H  N N 236 
ILE   HXT  H  N N 237 
LEU   N    N  N N 238 
LEU   CA   C  N S 239 
LEU   C    C  N N 240 
LEU   O    O  N N 241 
LEU   CB   C  N N 242 
LEU   CG   C  N N 243 
LEU   CD1  C  N N 244 
LEU   CD2  C  N N 245 
LEU   OXT  O  N N 246 
LEU   H    H  N N 247 
LEU   H2   H  N N 248 
LEU   HA   H  N N 249 
LEU   HB2  H  N N 250 
LEU   HB3  H  N N 251 
LEU   HG   H  N N 252 
LEU   HD11 H  N N 253 
LEU   HD12 H  N N 254 
LEU   HD13 H  N N 255 
LEU   HD21 H  N N 256 
LEU   HD22 H  N N 257 
LEU   HD23 H  N N 258 
LEU   HXT  H  N N 259 
LYS   N    N  N N 260 
LYS   CA   C  N S 261 
LYS   C    C  N N 262 
LYS   O    O  N N 263 
LYS   CB   C  N N 264 
LYS   CG   C  N N 265 
LYS   CD   C  N N 266 
LYS   CE   C  N N 267 
LYS   NZ   N  N N 268 
LYS   OXT  O  N N 269 
LYS   H    H  N N 270 
LYS   H2   H  N N 271 
LYS   HA   H  N N 272 
LYS   HB2  H  N N 273 
LYS   HB3  H  N N 274 
LYS   HG2  H  N N 275 
LYS   HG3  H  N N 276 
LYS   HD2  H  N N 277 
LYS   HD3  H  N N 278 
LYS   HE2  H  N N 279 
LYS   HE3  H  N N 280 
LYS   HZ1  H  N N 281 
LYS   HZ2  H  N N 282 
LYS   HZ3  H  N N 283 
LYS   HXT  H  N N 284 
MET   N    N  N N 285 
MET   CA   C  N S 286 
MET   C    C  N N 287 
MET   O    O  N N 288 
MET   CB   C  N N 289 
MET   CG   C  N N 290 
MET   SD   S  N N 291 
MET   CE   C  N N 292 
MET   OXT  O  N N 293 
MET   H    H  N N 294 
MET   H2   H  N N 295 
MET   HA   H  N N 296 
MET   HB2  H  N N 297 
MET   HB3  H  N N 298 
MET   HG2  H  N N 299 
MET   HG3  H  N N 300 
MET   HE1  H  N N 301 
MET   HE2  H  N N 302 
MET   HE3  H  N N 303 
MET   HXT  H  N N 304 
PHE   N    N  N N 305 
PHE   CA   C  N S 306 
PHE   C    C  N N 307 
PHE   O    O  N N 308 
PHE   CB   C  N N 309 
PHE   CG   C  Y N 310 
PHE   CD1  C  Y N 311 
PHE   CD2  C  Y N 312 
PHE   CE1  C  Y N 313 
PHE   CE2  C  Y N 314 
PHE   CZ   C  Y N 315 
PHE   OXT  O  N N 316 
PHE   H    H  N N 317 
PHE   H2   H  N N 318 
PHE   HA   H  N N 319 
PHE   HB2  H  N N 320 
PHE   HB3  H  N N 321 
PHE   HD1  H  N N 322 
PHE   HD2  H  N N 323 
PHE   HE1  H  N N 324 
PHE   HE2  H  N N 325 
PHE   HZ   H  N N 326 
PHE   HXT  H  N N 327 
PRO   N    N  N N 328 
PRO   CA   C  N S 329 
PRO   C    C  N N 330 
PRO   O    O  N N 331 
PRO   CB   C  N N 332 
PRO   CG   C  N N 333 
PRO   CD   C  N N 334 
PRO   OXT  O  N N 335 
PRO   H    H  N N 336 
PRO   HA   H  N N 337 
PRO   HB2  H  N N 338 
PRO   HB3  H  N N 339 
PRO   HG2  H  N N 340 
PRO   HG3  H  N N 341 
PRO   HD2  H  N N 342 
PRO   HD3  H  N N 343 
PRO   HXT  H  N N 344 
SER   N    N  N N 345 
SER   CA   C  N S 346 
SER   C    C  N N 347 
SER   O    O  N N 348 
SER   CB   C  N N 349 
SER   OG   O  N N 350 
SER   OXT  O  N N 351 
SER   H    H  N N 352 
SER   H2   H  N N 353 
SER   HA   H  N N 354 
SER   HB2  H  N N 355 
SER   HB3  H  N N 356 
SER   HG   H  N N 357 
SER   HXT  H  N N 358 
SO4   S    S  N N 359 
SO4   O1   O  N N 360 
SO4   O2   O  N N 361 
SO4   O3   O  N N 362 
SO4   O4   O  N N 363 
THR   N    N  N N 364 
THR   CA   C  N S 365 
THR   C    C  N N 366 
THR   O    O  N N 367 
THR   CB   C  N R 368 
THR   OG1  O  N N 369 
THR   CG2  C  N N 370 
THR   OXT  O  N N 371 
THR   H    H  N N 372 
THR   H2   H  N N 373 
THR   HA   H  N N 374 
THR   HB   H  N N 375 
THR   HG1  H  N N 376 
THR   HG21 H  N N 377 
THR   HG22 H  N N 378 
THR   HG23 H  N N 379 
THR   HXT  H  N N 380 
TRP   N    N  N N 381 
TRP   CA   C  N S 382 
TRP   C    C  N N 383 
TRP   O    O  N N 384 
TRP   CB   C  N N 385 
TRP   CG   C  Y N 386 
TRP   CD1  C  Y N 387 
TRP   CD2  C  Y N 388 
TRP   NE1  N  Y N 389 
TRP   CE2  C  Y N 390 
TRP   CE3  C  Y N 391 
TRP   CZ2  C  Y N 392 
TRP   CZ3  C  Y N 393 
TRP   CH2  C  Y N 394 
TRP   OXT  O  N N 395 
TRP   H    H  N N 396 
TRP   H2   H  N N 397 
TRP   HA   H  N N 398 
TRP   HB2  H  N N 399 
TRP   HB3  H  N N 400 
TRP   HD1  H  N N 401 
TRP   HE1  H  N N 402 
TRP   HE3  H  N N 403 
TRP   HZ2  H  N N 404 
TRP   HZ3  H  N N 405 
TRP   HH2  H  N N 406 
TRP   HXT  H  N N 407 
TYR   N    N  N N 408 
TYR   CA   C  N S 409 
TYR   C    C  N N 410 
TYR   O    O  N N 411 
TYR   CB   C  N N 412 
TYR   CG   C  Y N 413 
TYR   CD1  C  Y N 414 
TYR   CD2  C  Y N 415 
TYR   CE1  C  Y N 416 
TYR   CE2  C  Y N 417 
TYR   CZ   C  Y N 418 
TYR   OH   O  N N 419 
TYR   OXT  O  N N 420 
TYR   H    H  N N 421 
TYR   H2   H  N N 422 
TYR   HA   H  N N 423 
TYR   HB2  H  N N 424 
TYR   HB3  H  N N 425 
TYR   HD1  H  N N 426 
TYR   HD2  H  N N 427 
TYR   HE1  H  N N 428 
TYR   HE2  H  N N 429 
TYR   HH   H  N N 430 
TYR   HXT  H  N N 431 
VAL   N    N  N N 432 
VAL   CA   C  N S 433 
VAL   C    C  N N 434 
VAL   O    O  N N 435 
VAL   CB   C  N N 436 
VAL   CG1  C  N N 437 
VAL   CG2  C  N N 438 
VAL   OXT  O  N N 439 
VAL   H    H  N N 440 
VAL   H2   H  N N 441 
VAL   HA   H  N N 442 
VAL   HB   H  N N 443 
VAL   HG11 H  N N 444 
VAL   HG12 H  N N 445 
VAL   HG13 H  N N 446 
VAL   HG21 H  N N 447 
VAL   HG22 H  N N 448 
VAL   HG23 H  N N 449 
VAL   HXT  H  N N 450 
ZN    ZN   ZN N N 451 
# 
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 
A1A5I C26 C27  sing N N 1   
A1A5I C26 N24  sing N N 2   
A1A5I C28 C23  sing N N 3   
A1A5I N24 C23  sing N N 4   
A1A5I N24 C25  sing N N 5   
A1A5I C23 C22  sing N N 6   
A1A5I C25 C20  sing N N 7   
A1A5I C22 C21  sing N N 8   
A1A5I O10 C20  sing N N 9   
A1A5I O10 C2   sing N N 10  
A1A5I C20 C21  sing N N 11  
A1A5I C2  C1   doub Y N 12  
A1A5I C2  C3   sing Y N 13  
A1A5I C1  C6   sing Y N 14  
A1A5I C3  C4   doub Y N 15  
A1A5I C6  C5   doub Y N 16  
A1A5I C4  C5   sing Y N 17  
A1A5I C4  C7   sing N N 18  
A1A5I C5  C9   sing N N 19  
A1A5I C7  N8   sing N N 20  
A1A5I C9  N8   sing N N 21  
A1A5I C9  O11  doub N N 22  
A1A5I N8  C12  sing N N 23  
A1A5I C13 C12  sing N N 24  
A1A5I C13 C14  sing N N 25  
A1A5I C12 C17  sing N N 26  
A1A5I C14 C15  sing N N 27  
A1A5I C17 O18  doub N N 28  
A1A5I C17 N16  sing N N 29  
A1A5I C15 N16  sing N N 30  
A1A5I C15 O19  doub N N 31  
A1A5I C1  H1   sing N N 32  
A1A5I C3  H2   sing N N 33  
A1A5I C12 H3   sing N N 34  
A1A5I C13 H4   sing N N 35  
A1A5I C13 H5   sing N N 36  
A1A5I C14 H6   sing N N 37  
A1A5I C14 H7   sing N N 38  
A1A5I C20 H8   sing N N 39  
A1A5I C21 H9   sing N N 40  
A1A5I C21 H10  sing N N 41  
A1A5I C22 H11  sing N N 42  
A1A5I C22 H12  sing N N 43  
A1A5I C23 H13  sing N N 44  
A1A5I C25 H14  sing N N 45  
A1A5I C25 H15  sing N N 46  
A1A5I C26 H16  sing N N 47  
A1A5I C26 H17  sing N N 48  
A1A5I C27 H18  sing N N 49  
A1A5I C27 H19  sing N N 50  
A1A5I C27 H20  sing N N 51  
A1A5I C28 H21  sing N N 52  
A1A5I C28 H22  sing N N 53  
A1A5I C28 H23  sing N N 54  
A1A5I C6  H24  sing N N 55  
A1A5I C7  H25  sing N N 56  
A1A5I C7  H26  sing N N 57  
A1A5I N16 H27  sing N N 58  
ALA   N   CA   sing N N 59  
ALA   N   H    sing N N 60  
ALA   N   H2   sing N N 61  
ALA   CA  C    sing N N 62  
ALA   CA  CB   sing N N 63  
ALA   CA  HA   sing N N 64  
ALA   C   O    doub N N 65  
ALA   C   OXT  sing N N 66  
ALA   CB  HB1  sing N N 67  
ALA   CB  HB2  sing N N 68  
ALA   CB  HB3  sing N N 69  
ALA   OXT HXT  sing N N 70  
ARG   N   CA   sing N N 71  
ARG   N   H    sing N N 72  
ARG   N   H2   sing N N 73  
ARG   CA  C    sing N N 74  
ARG   CA  CB   sing N N 75  
ARG   CA  HA   sing N N 76  
ARG   C   O    doub N N 77  
ARG   C   OXT  sing N N 78  
ARG   CB  CG   sing N N 79  
ARG   CB  HB2  sing N N 80  
ARG   CB  HB3  sing N N 81  
ARG   CG  CD   sing N N 82  
ARG   CG  HG2  sing N N 83  
ARG   CG  HG3  sing N N 84  
ARG   CD  NE   sing N N 85  
ARG   CD  HD2  sing N N 86  
ARG   CD  HD3  sing N N 87  
ARG   NE  CZ   sing N N 88  
ARG   NE  HE   sing N N 89  
ARG   CZ  NH1  sing N N 90  
ARG   CZ  NH2  doub N N 91  
ARG   NH1 HH11 sing N N 92  
ARG   NH1 HH12 sing N N 93  
ARG   NH2 HH21 sing N N 94  
ARG   NH2 HH22 sing N N 95  
ARG   OXT HXT  sing N N 96  
ASN   N   CA   sing N N 97  
ASN   N   H    sing N N 98  
ASN   N   H2   sing N N 99  
ASN   CA  C    sing N N 100 
ASN   CA  CB   sing N N 101 
ASN   CA  HA   sing N N 102 
ASN   C   O    doub N N 103 
ASN   C   OXT  sing N N 104 
ASN   CB  CG   sing N N 105 
ASN   CB  HB2  sing N N 106 
ASN   CB  HB3  sing N N 107 
ASN   CG  OD1  doub N N 108 
ASN   CG  ND2  sing N N 109 
ASN   ND2 HD21 sing N N 110 
ASN   ND2 HD22 sing N N 111 
ASN   OXT HXT  sing N N 112 
ASP   N   CA   sing N N 113 
ASP   N   H    sing N N 114 
ASP   N   H2   sing N N 115 
ASP   CA  C    sing N N 116 
ASP   CA  CB   sing N N 117 
ASP   CA  HA   sing N N 118 
ASP   C   O    doub N N 119 
ASP   C   OXT  sing N N 120 
ASP   CB  CG   sing N N 121 
ASP   CB  HB2  sing N N 122 
ASP   CB  HB3  sing N N 123 
ASP   CG  OD1  doub N N 124 
ASP   CG  OD2  sing N N 125 
ASP   OD2 HD2  sing N N 126 
ASP   OXT HXT  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
HOH   O   H1   sing N N 208 
HOH   O   H2   sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
SO4   S   O1   doub N N 348 
SO4   S   O2   doub N N 349 
SO4   S   O3   sing N N 350 
SO4   S   O4   sing N N 351 
THR   N   CA   sing N N 352 
THR   N   H    sing N N 353 
THR   N   H2   sing N N 354 
THR   CA  C    sing N N 355 
THR   CA  CB   sing N N 356 
THR   CA  HA   sing N N 357 
THR   C   O    doub N N 358 
THR   C   OXT  sing N N 359 
THR   CB  OG1  sing N N 360 
THR   CB  CG2  sing N N 361 
THR   CB  HB   sing N N 362 
THR   OG1 HG1  sing N N 363 
THR   CG2 HG21 sing N N 364 
THR   CG2 HG22 sing N N 365 
THR   CG2 HG23 sing N N 366 
THR   OXT HXT  sing N N 367 
TRP   N   CA   sing N N 368 
TRP   N   H    sing N N 369 
TRP   N   H2   sing N N 370 
TRP   CA  C    sing N N 371 
TRP   CA  CB   sing N N 372 
TRP   CA  HA   sing N N 373 
TRP   C   O    doub N N 374 
TRP   C   OXT  sing N N 375 
TRP   CB  CG   sing N N 376 
TRP   CB  HB2  sing N N 377 
TRP   CB  HB3  sing N N 378 
TRP   CG  CD1  doub Y N 379 
TRP   CG  CD2  sing Y N 380 
TRP   CD1 NE1  sing Y N 381 
TRP   CD1 HD1  sing N N 382 
TRP   CD2 CE2  doub Y N 383 
TRP   CD2 CE3  sing Y N 384 
TRP   NE1 CE2  sing Y N 385 
TRP   NE1 HE1  sing N N 386 
TRP   CE2 CZ2  sing Y N 387 
TRP   CE3 CZ3  doub Y N 388 
TRP   CE3 HE3  sing N N 389 
TRP   CZ2 CH2  doub Y N 390 
TRP   CZ2 HZ2  sing N N 391 
TRP   CZ3 CH2  sing Y N 392 
TRP   CZ3 HZ3  sing N N 393 
TRP   CH2 HH2  sing N N 394 
TRP   OXT HXT  sing N N 395 
TYR   N   CA   sing N N 396 
TYR   N   H    sing N N 397 
TYR   N   H2   sing N N 398 
TYR   CA  C    sing N N 399 
TYR   CA  CB   sing N N 400 
TYR   CA  HA   sing N N 401 
TYR   C   O    doub N N 402 
TYR   C   OXT  sing N N 403 
TYR   CB  CG   sing N N 404 
TYR   CB  HB2  sing N N 405 
TYR   CB  HB3  sing N N 406 
TYR   CG  CD1  doub Y N 407 
TYR   CG  CD2  sing Y N 408 
TYR   CD1 CE1  sing Y N 409 
TYR   CD1 HD1  sing N N 410 
TYR   CD2 CE2  doub Y N 411 
TYR   CD2 HD2  sing N N 412 
TYR   CE1 CZ   doub Y N 413 
TYR   CE1 HE1  sing N N 414 
TYR   CE2 CZ   sing Y N 415 
TYR   CE2 HE2  sing N N 416 
TYR   CZ  OH   sing N N 417 
TYR   OH  HH   sing N N 418 
TYR   OXT HXT  sing N N 419 
VAL   N   CA   sing N N 420 
VAL   N   H    sing N N 421 
VAL   N   H2   sing N N 422 
VAL   CA  C    sing N N 423 
VAL   CA  CB   sing N N 424 
VAL   CA  HA   sing N N 425 
VAL   C   O    doub N N 426 
VAL   C   OXT  sing N N 427 
VAL   CB  CG1  sing N N 428 
VAL   CB  CG2  sing N N 429 
VAL   CB  HB   sing N N 430 
VAL   CG1 HG11 sing N N 431 
VAL   CG1 HG12 sing N N 432 
VAL   CG1 HG13 sing N N 433 
VAL   CG2 HG21 sing N N 434 
VAL   CG2 HG22 sing N N 435 
VAL   CG2 HG23 sing N N 436 
VAL   OXT HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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   8TZX 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DJX 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009165 
_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]   0.006895 
_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]   0.005211 
_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  
N  
O  
S  
ZN 
# 
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   . HIS   A 1 4   ? 45.890  33.146  -25.891 1.00 161.74 ? 73   HIS   A N   1 
ATOM   2     C  CA  . HIS   A 1 4   ? 45.934  31.763  -26.366 1.00 163.87 ? 73   HIS   A CA  1 
ATOM   3     C  C   . HIS   A 1 4   ? 45.281  31.622  -27.749 1.00 168.64 ? 73   HIS   A C   1 
ATOM   4     O  O   . HIS   A 1 4   ? 45.990  31.431  -28.750 1.00 164.68 ? 73   HIS   A O   1 
ATOM   5     C  CB  . HIS   A 1 4   ? 45.257  30.824  -25.359 1.00 153.24 ? 73   HIS   A CB  1 
ATOM   6     N  N   . ASP   A 1 5   ? 43.945  31.707  -27.811 1.00 181.67 ? 74   ASP   A N   1 
ATOM   7     C  CA  . ASP   A 1 5   ? 43.212  31.532  -29.066 1.00 178.82 ? 74   ASP   A CA  1 
ATOM   8     C  C   . ASP   A 1 5   ? 42.515  32.812  -29.523 1.00 174.14 ? 74   ASP   A C   1 
ATOM   9     O  O   . ASP   A 1 5   ? 42.741  33.253  -30.654 1.00 171.85 ? 74   ASP   A O   1 
ATOM   10    C  CB  . ASP   A 1 5   ? 42.194  30.378  -28.951 1.00 178.53 ? 74   ASP   A CB  1 
ATOM   11    C  CG  . ASP   A 1 5   ? 42.148  29.496  -30.212 1.00 175.10 ? 74   ASP   A CG  1 
ATOM   12    O  OD1 . ASP   A 1 5   ? 42.889  29.775  -31.186 1.00 171.50 ? 74   ASP   A OD1 1 
ATOM   13    O  OD2 . ASP   A 1 5   ? 41.372  28.510  -30.213 1.00 171.23 ? 74   ASP   A OD2 1 
ATOM   14    N  N   . ASP   A 1 6   ? 41.662  33.424  -28.690 1.00 157.96 ? 75   ASP   A N   1 
ATOM   15    C  CA  . ASP   A 1 6   ? 41.001  34.663  -29.094 1.00 153.37 ? 75   ASP   A CA  1 
ATOM   16    C  C   . ASP   A 1 6   ? 42.037  35.779  -29.272 1.00 151.89 ? 75   ASP   A C   1 
ATOM   17    O  O   . ASP   A 1 6   ? 43.063  35.817  -28.585 1.00 152.34 ? 75   ASP   A O   1 
ATOM   18    C  CB  . ASP   A 1 6   ? 39.921  35.068  -28.071 1.00 148.86 ? 75   ASP   A CB  1 
ATOM   19    C  CG  . ASP   A 1 6   ? 38.784  35.939  -28.686 1.00 145.52 ? 75   ASP   A CG  1 
ATOM   20    O  OD1 . ASP   A 1 6   ? 38.900  37.194  -28.724 1.00 143.30 ? 75   ASP   A OD1 1 
ATOM   21    O  OD2 . ASP   A 1 6   ? 37.762  35.359  -29.126 1.00 143.29 ? 75   ASP   A OD2 1 
ATOM   22    N  N   . ASP   A 1 7   ? 41.759  36.669  -30.237 1.00 143.41 ? 76   ASP   A N   1 
ATOM   23    C  CA  . ASP   A 1 7   ? 42.614  37.810  -30.638 1.00 137.92 ? 76   ASP   A CA  1 
ATOM   24    C  C   . ASP   A 1 7   ? 44.102  37.432  -30.691 1.00 134.29 ? 76   ASP   A C   1 
ATOM   25    O  O   . ASP   A 1 7   ? 44.984  38.162  -30.227 1.00 134.89 ? 76   ASP   A O   1 
ATOM   26    C  CB  . ASP   A 1 7   ? 42.386  39.031  -29.724 1.00 141.84 ? 76   ASP   A CB  1 
ATOM   27    C  CG  . ASP   A 1 7   ? 41.100  39.819  -30.056 1.00 141.60 ? 76   ASP   A CG  1 
ATOM   28    O  OD1 . ASP   A 1 7   ? 40.226  39.281  -30.765 1.00 137.85 ? 76   ASP   A OD1 1 
ATOM   29    O  OD2 . ASP   A 1 7   ? 40.966  40.980  -29.589 1.00 144.17 ? 76   ASP   A OD2 1 
ATOM   30    N  N   . SER   A 1 8   ? 44.386  36.282  -31.292 1.00 131.37 ? 77   SER   A N   1 
ATOM   31    C  CA  . SER   A 1 8   ? 45.751  35.792  -31.411 1.00 131.51 ? 77   SER   A CA  1 
ATOM   32    C  C   . SER   A 1 8   ? 46.066  35.531  -32.877 1.00 123.15 ? 77   SER   A C   1 
ATOM   33    O  O   . SER   A 1 8   ? 45.172  35.225  -33.672 1.00 118.86 ? 77   SER   A O   1 
ATOM   34    C  CB  . SER   A 1 8   ? 45.962  34.518  -30.580 1.00 142.16 ? 77   SER   A CB  1 
ATOM   35    O  OG  . SER   A 1 8   ? 45.503  33.368  -31.270 1.00 142.10 ? 77   SER   A OG  1 
ATOM   36    N  N   . CYS   A 1 9   ? 47.348  35.667  -33.234 1.00 121.10 ? 78   CYS   A N   1 
ATOM   37    C  CA  . CYS   A 1 9   ? 47.802  35.545  -34.619 1.00 117.71 ? 78   CYS   A CA  1 
ATOM   38    C  C   . CYS   A 1 9   ? 48.411  34.170  -34.836 1.00 117.36 ? 78   CYS   A C   1 
ATOM   39    O  O   . CYS   A 1 9   ? 49.559  33.926  -34.450 1.00 117.06 ? 78   CYS   A O   1 
ATOM   40    C  CB  . CYS   A 1 9   ? 48.824  36.621  -34.976 1.00 119.49 ? 78   CYS   A CB  1 
ATOM   41    S  SG  . CYS   A 1 9   ? 48.466  38.243  -34.275 1.00 136.87 ? 78   CYS   A SG  1 
ATOM   42    N  N   . GLN   A 1 10  ? 47.659  33.296  -35.501 1.00 113.70 ? 79   GLN   A N   1 
ATOM   43    C  CA  . GLN   A 1 10  ? 48.096  31.956  -35.848 1.00 111.13 ? 79   GLN   A CA  1 
ATOM   44    C  C   . GLN   A 1 10  ? 48.251  31.827  -37.359 1.00 104.45 ? 79   GLN   A C   1 
ATOM   45    O  O   . GLN   A 1 10  ? 47.717  32.624  -38.132 1.00 100.26 ? 79   GLN   A O   1 
ATOM   46    C  CB  . GLN   A 1 10  ? 47.088  30.918  -35.358 1.00 112.92 ? 79   GLN   A CB  1 
ATOM   47    C  CG  . GLN   A 1 10  ? 46.486  31.238  -34.015 1.00 119.55 ? 79   GLN   A CG  1 
ATOM   48    C  CD  . GLN   A 1 10  ? 47.455  30.958  -32.899 1.00 128.17 ? 79   GLN   A CD  1 
ATOM   49    O  OE1 . GLN   A 1 10  ? 48.350  30.110  -33.038 1.00 127.12 ? 79   GLN   A OE1 1 
ATOM   50    N  NE2 . GLN   A 1 10  ? 47.297  31.669  -31.782 1.00 133.42 ? 79   GLN   A NE2 1 
ATOM   51    N  N   . VAL   A 1 11  ? 48.971  30.799  -37.782 1.00 107.36 ? 80   VAL   A N   1 
ATOM   52    C  CA  . VAL   A 1 11  ? 48.983  30.398  -39.185 1.00 109.13 ? 80   VAL   A CA  1 
ATOM   53    C  C   . VAL   A 1 11  ? 48.281  29.051  -39.289 1.00 110.28 ? 80   VAL   A C   1 
ATOM   54    O  O   . VAL   A 1 11  ? 48.514  28.154  -38.468 1.00 109.29 ? 80   VAL   A O   1 
ATOM   55    C  CB  . VAL   A 1 11  ? 50.410  30.367  -39.776 1.00 105.25 ? 80   VAL   A CB  1 
ATOM   56    C  CG1 . VAL   A 1 11  ? 51.366  29.537  -38.924 1.00 107.10 ? 80   VAL   A CG1 1 
ATOM   57    C  CG2 . VAL   A 1 11  ? 50.389  29.887  -41.227 1.00 109.25 ? 80   VAL   A CG2 1 
ATOM   58    N  N   . ILE   A 1 12  ? 47.375  28.934  -40.256 1.00 110.37 ? 81   ILE   A N   1 
ATOM   59    C  CA  . ILE   A 1 12  ? 46.671  27.687  -40.533 1.00 110.57 ? 81   ILE   A CA  1 
ATOM   60    C  C   . ILE   A 1 12  ? 46.688  27.511  -42.042 1.00 117.72 ? 81   ILE   A C   1 
ATOM   61    O  O   . ILE   A 1 12  ? 46.666  28.511  -42.777 1.00 118.80 ? 81   ILE   A O   1 
ATOM   62    C  CB  . ILE   A 1 12  ? 45.235  27.703  -39.992 1.00 110.22 ? 81   ILE   A CB  1 
ATOM   63    C  CG1 . ILE   A 1 12  ? 44.538  28.987  -40.425 1.00 107.45 ? 81   ILE   A CG1 1 
ATOM   64    C  CG2 . ILE   A 1 12  ? 45.216  27.549  -38.469 1.00 109.99 ? 81   ILE   A CG2 1 
ATOM   65    C  CD1 . ILE   A 1 12  ? 43.237  29.218  -39.746 1.00 103.60 ? 81   ILE   A CD1 1 
ATOM   66    N  N   . PRO   A 1 13  ? 46.751  26.282  -42.546 1.00 122.13 ? 82   PRO   A N   1 
ATOM   67    C  CA  . PRO   A 1 13  ? 46.715  26.084  -43.994 1.00 123.14 ? 82   PRO   A CA  1 
ATOM   68    C  C   . PRO   A 1 13  ? 45.333  26.356  -44.535 1.00 121.68 ? 82   PRO   A C   1 
ATOM   69    O  O   . PRO   A 1 13  ? 44.327  26.379  -43.817 1.00 120.31 ? 82   PRO   A O   1 
ATOM   70    C  CB  . PRO   A 1 13  ? 47.092  24.613  -44.168 1.00 125.67 ? 82   PRO   A CB  1 
ATOM   71    C  CG  . PRO   A 1 13  ? 46.651  23.980  -42.885 1.00 124.71 ? 82   PRO   A CG  1 
ATOM   72    C  CD  . PRO   A 1 13  ? 46.864  25.011  -41.811 1.00 121.16 ? 82   PRO   A CD  1 
ATOM   73    N  N   . VAL   A 1 14  ? 45.292  26.573  -45.837 1.00 126.46 ? 83   VAL   A N   1 
ATOM   74    C  CA  . VAL   A 1 14  ? 44.067  26.937  -46.522 1.00 128.42 ? 83   VAL   A CA  1 
ATOM   75    C  C   . VAL   A 1 14  ? 43.730  25.834  -47.509 1.00 139.41 ? 83   VAL   A C   1 
ATOM   76    O  O   . VAL   A 1 14  ? 44.578  25.449  -48.321 1.00 146.45 ? 83   VAL   A O   1 
ATOM   77    C  CB  . VAL   A 1 14  ? 44.199  28.275  -47.258 1.00 125.37 ? 83   VAL   A CB  1 
ATOM   78    C  CG1 . VAL   A 1 14  ? 42.905  28.568  -47.975 1.00 126.13 ? 83   VAL   A CG1 1 
ATOM   79    C  CG2 . VAL   A 1 14  ? 44.552  29.381  -46.307 1.00 126.63 ? 83   VAL   A CG2 1 
ATOM   80    N  N   . LEU   A 1 15  ? 42.487  25.344  -47.461 1.00 132.52 ? 84   LEU   A N   1 
ATOM   81    C  CA  . LEU   A 1 15  ? 42.024  24.481  -48.540 1.00 139.53 ? 84   LEU   A CA  1 
ATOM   82    C  C   . LEU   A 1 15  ? 41.952  25.313  -49.822 1.00 149.46 ? 84   LEU   A C   1 
ATOM   83    O  O   . LEU   A 1 15  ? 41.143  26.247  -49.892 1.00 150.63 ? 84   LEU   A O   1 
ATOM   84    C  CB  . LEU   A 1 15  ? 40.667  23.873  -48.212 1.00 137.95 ? 84   LEU   A CB  1 
ATOM   85    C  CG  . LEU   A 1 15  ? 39.992  23.259  -49.434 1.00 146.67 ? 84   LEU   A CG  1 
ATOM   86    C  CD1 . LEU   A 1 15  ? 40.727  21.992  -49.878 1.00 145.63 ? 84   LEU   A CD1 1 
ATOM   87    C  CD2 . LEU   A 1 15  ? 38.533  22.992  -49.128 1.00 138.46 ? 84   LEU   A CD2 1 
ATOM   88    N  N   . PRO   A 1 16  ? 42.783  25.025  -50.837 1.00 158.51 ? 85   PRO   A N   1 
ATOM   89    C  CA  . PRO   A 1 16  ? 42.887  25.955  -51.980 1.00 160.92 ? 85   PRO   A CA  1 
ATOM   90    C  C   . PRO   A 1 16  ? 41.573  26.140  -52.703 1.00 162.55 ? 85   PRO   A C   1 
ATOM   91    O  O   . PRO   A 1 16  ? 41.137  27.278  -52.917 1.00 163.06 ? 85   PRO   A O   1 
ATOM   92    C  CB  . PRO   A 1 16  ? 43.955  25.306  -52.874 1.00 161.04 ? 85   PRO   A CB  1 
ATOM   93    C  CG  . PRO   A 1 16  ? 44.746  24.431  -51.933 1.00 157.78 ? 85   PRO   A CG  1 
ATOM   94    C  CD  . PRO   A 1 16  ? 43.710  23.888  -50.979 1.00 157.17 ? 85   PRO   A CD  1 
ATOM   95    N  N   . GLN   A 1 17  ? 40.910  25.041  -53.060 1.00 157.10 ? 86   GLN   A N   1 
ATOM   96    C  CA  . GLN   A 1 17  ? 39.617  25.109  -53.729 1.00 160.46 ? 86   GLN   A CA  1 
ATOM   97    C  C   . GLN   A 1 17  ? 38.541  25.275  -52.657 1.00 162.67 ? 86   GLN   A C   1 
ATOM   98    O  O   . GLN   A 1 17  ? 38.056  24.308  -52.070 1.00 158.99 ? 86   GLN   A O   1 
ATOM   99    C  CB  . GLN   A 1 17  ? 39.385  23.872  -54.584 1.00 159.61 ? 86   GLN   A CB  1 
ATOM   100   N  N   . VAL   A 1 18  ? 38.169  26.526  -52.400 1.00 166.14 ? 87   VAL   A N   1 
ATOM   101   C  CA  . VAL   A 1 18  ? 37.177  26.848  -51.386 1.00 166.53 ? 87   VAL   A CA  1 
ATOM   102   C  C   . VAL   A 1 18  ? 36.722  28.279  -51.616 1.00 166.48 ? 87   VAL   A C   1 
ATOM   103   O  O   . VAL   A 1 18  ? 37.410  29.049  -52.296 1.00 165.95 ? 87   VAL   A O   1 
ATOM   104   C  CB  . VAL   A 1 18  ? 37.743  26.677  -49.967 1.00 165.99 ? 87   VAL   A CB  1 
ATOM   105   C  CG1 . VAL   A 1 18  ? 38.540  27.923  -49.557 1.00 164.13 ? 87   VAL   A CG1 1 
ATOM   106   C  CG2 . VAL   A 1 18  ? 36.626  26.412  -48.983 1.00 164.69 ? 87   VAL   A CG2 1 
ATOM   107   N  N   . MET   A 1 19  ? 35.587  28.664  -51.039 1.00 154.88 ? 88   MET   A N   1 
ATOM   108   C  CA  . MET   A 1 19  ? 35.145  30.030  -51.220 1.00 152.22 ? 88   MET   A CA  1 
ATOM   109   C  C   . MET   A 1 19  ? 34.023  30.455  -50.273 1.00 149.93 ? 88   MET   A C   1 
ATOM   110   O  O   . MET   A 1 19  ? 33.829  31.650  -50.022 1.00 149.31 ? 88   MET   A O   1 
ATOM   111   C  CB  . MET   A 1 19  ? 34.618  30.249  -52.635 1.00 158.54 ? 88   MET   A CB  1 
ATOM   112   C  CG  . MET   A 1 19  ? 33.531  29.255  -53.042 1.00 163.76 ? 88   MET   A CG  1 
ATOM   113   S  SD  . MET   A 1 19  ? 32.157  29.996  -53.978 1.00 176.79 ? 88   MET   A SD  1 
ATOM   114   C  CE  . MET   A 1 19  ? 31.190  30.784  -52.670 1.00 156.70 ? 88   MET   A CE  1 
ATOM   115   N  N   . MET   A 1 20  ? 33.292  29.471  -49.759 1.00 143.63 ? 89   MET   A N   1 
ATOM   116   C  CA  . MET   A 1 20  ? 32.035  29.708  -49.066 1.00 132.35 ? 89   MET   A CA  1 
ATOM   117   C  C   . MET   A 1 20  ? 32.254  30.674  -47.899 1.00 123.48 ? 89   MET   A C   1 
ATOM   118   O  O   . MET   A 1 20  ? 33.367  30.827  -47.375 1.00 126.39 ? 89   MET   A O   1 
ATOM   119   C  CB  . MET   A 1 20  ? 31.463  28.395  -48.544 1.00 133.78 ? 89   MET   A CB  1 
ATOM   120   C  CG  . MET   A 1 20  ? 32.510  27.474  -47.925 1.00 128.70 ? 89   MET   A CG  1 
ATOM   121   S  SD  . MET   A 1 20  ? 31.766  26.116  -47.006 1.00 143.95 ? 89   MET   A SD  1 
ATOM   122   C  CE  . MET   A 1 20  ? 30.572  26.941  -45.933 1.00 118.55 ? 89   MET   A CE  1 
ATOM   123   N  N   . ILE   A 1 21  ? 31.175  31.329  -47.492 1.00 116.16 ? 90   ILE   A N   1 
ATOM   124   C  CA  . ILE   A 1 21  ? 31.116  32.023  -46.219 1.00 110.80 ? 90   ILE   A CA  1 
ATOM   125   C  C   . ILE   A 1 21  ? 30.703  30.969  -45.199 1.00 113.80 ? 90   ILE   A C   1 
ATOM   126   O  O   . ILE   A 1 21  ? 29.525  30.592  -45.101 1.00 113.19 ? 90   ILE   A O   1 
ATOM   127   C  CB  . ILE   A 1 21  ? 30.185  33.231  -46.254 1.00 97.96  ? 90   ILE   A CB  1 
ATOM   128   C  CG1 . ILE   A 1 21  ? 30.854  34.353  -47.018 1.00 102.48 ? 90   ILE   A CG1 1 
ATOM   129   C  CG2 . ILE   A 1 21  ? 29.911  33.759  -44.882 1.00 89.59  ? 90   ILE   A CG2 1 
ATOM   130   C  CD1 . ILE   A 1 21  ? 30.718  34.259  -48.500 1.00 110.55 ? 90   ILE   A CD1 1 
ATOM   131   N  N   . LEU   A 1 22  ? 31.684  30.428  -44.490 1.00 113.47 ? 91   LEU   A N   1 
ATOM   132   C  CA  . LEU   A 1 22  ? 31.462  29.384  -43.493 1.00 103.26 ? 91   LEU   A CA  1 
ATOM   133   C  C   . LEU   A 1 22  ? 31.067  30.066  -42.198 1.00 102.11 ? 91   LEU   A C   1 
ATOM   134   O  O   . LEU   A 1 22  ? 31.892  30.738  -41.569 1.00 102.85 ? 91   LEU   A O   1 
ATOM   135   C  CB  . LEU   A 1 22  ? 32.733  28.552  -43.329 1.00 99.31  ? 91   LEU   A CB  1 
ATOM   136   C  CG  . LEU   A 1 22  ? 32.661  27.555  -42.196 1.00 94.49  ? 91   LEU   A CG  1 
ATOM   137   C  CD1 . LEU   A 1 22  ? 31.573  26.578  -42.507 1.00 100.21 ? 91   LEU   A CD1 1 
ATOM   138   C  CD2 . LEU   A 1 22  ? 33.980  26.874  -42.051 1.00 92.97  ? 91   LEU   A CD2 1 
ATOM   139   N  N   . ILE   A 1 23  ? 29.798  29.946  -41.817 1.00 100.98 ? 92   ILE   A N   1 
ATOM   140   C  CA  . ILE   A 1 23  ? 29.380  30.458  -40.504 1.00 98.60  ? 92   ILE   A CA  1 
ATOM   141   C  C   . ILE   A 1 23  ? 29.808  29.458  -39.434 1.00 95.40  ? 92   ILE   A C   1 
ATOM   142   O  O   . ILE   A 1 23  ? 29.672  28.243  -39.662 1.00 97.63  ? 92   ILE   A O   1 
ATOM   143   C  CB  . ILE   A 1 23  ? 27.865  30.703  -40.466 1.00 92.70  ? 92   ILE   A CB  1 
ATOM   144   C  CG1 . ILE   A 1 23  ? 27.414  31.448  -41.712 1.00 90.60  ? 92   ILE   A CG1 1 
ATOM   145   C  CG2 . ILE   A 1 23  ? 27.472  31.491  -39.200 1.00 83.06  ? 92   ILE   A CG2 1 
ATOM   146   C  CD1 . ILE   A 1 23  ? 25.977  31.874  -41.650 1.00 91.00  ? 92   ILE   A CD1 1 
ATOM   147   N  N   . PRO   A 1 24  ? 30.371  29.923  -38.307 1.00 88.06  ? 93   PRO   A N   1 
ATOM   148   C  CA  . PRO   A 1 24  ? 30.766  28.999  -37.251 1.00 93.16  ? 93   PRO   A CA  1 
ATOM   149   C  C   . PRO   A 1 24  ? 29.614  28.047  -36.867 1.00 93.12  ? 93   PRO   A C   1 
ATOM   150   O  O   . PRO   A 1 24  ? 28.459  28.446  -36.759 1.00 91.16  ? 93   PRO   A O   1 
ATOM   151   C  CB  . PRO   A 1 24  ? 31.169  29.912  -36.103 1.00 88.43  ? 93   PRO   A CB  1 
ATOM   152   C  CG  . PRO   A 1 24  ? 30.819  31.316  -36.525 1.00 90.58  ? 93   PRO   A CG  1 
ATOM   153   C  CD  . PRO   A 1 24  ? 30.834  31.266  -38.028 1.00 90.29  ? 93   PRO   A CD  1 
ATOM   154   N  N   . GLY   A 1 25  ? 29.941  26.753  -36.682 1.00 90.66  ? 94   GLY   A N   1 
ATOM   155   C  CA  . GLY   A 1 25  ? 28.962  25.759  -36.385 1.00 93.90  ? 94   GLY   A CA  1 
ATOM   156   C  C   . GLY   A 1 25  ? 28.383  25.054  -37.600 1.00 99.75  ? 94   GLY   A C   1 
ATOM   157   O  O   . GLY   A 1 25  ? 27.923  23.907  -37.469 1.00 97.14  ? 94   GLY   A O   1 
ATOM   158   N  N   . GLN   A 1 26  ? 28.399  25.686  -38.773 1.00 108.29 ? 95   GLN   A N   1 
ATOM   159   C  CA  . GLN   A 1 26  ? 28.115  24.954  -40.004 1.00 110.11 ? 95   GLN   A CA  1 
ATOM   160   C  C   . GLN   A 1 26  ? 29.148  23.851  -40.225 1.00 109.37 ? 95   GLN   A C   1 
ATOM   161   O  O   . GLN   A 1 26  ? 30.261  23.894  -39.696 1.00 108.41 ? 95   GLN   A O   1 
ATOM   162   C  CB  . GLN   A 1 26  ? 28.139  25.870  -41.229 1.00 113.60 ? 95   GLN   A CB  1 
ATOM   163   C  CG  . GLN   A 1 26  ? 26.877  26.674  -41.495 1.00 117.66 ? 95   GLN   A CG  1 
ATOM   164   C  CD  . GLN   A 1 26  ? 27.030  27.580  -42.710 1.00 120.36 ? 95   GLN   A CD  1 
ATOM   165   O  OE1 . GLN   A 1 26  ? 28.155  27.844  -43.166 1.00 120.30 ? 95   GLN   A OE1 1 
ATOM   166   N  NE2 . GLN   A 1 26  ? 25.900  28.056  -43.247 1.00 118.46 ? 95   GLN   A NE2 1 
ATOM   167   N  N   . THR   A 1 27  ? 28.773  22.862  -41.044 1.00 102.99 ? 96   THR   A N   1 
ATOM   168   C  CA  . THR   A 1 27  ? 29.645  21.758  -41.435 1.00 100.35 ? 96   THR   A CA  1 
ATOM   169   C  C   . THR   A 1 27  ? 29.799  21.769  -42.950 1.00 102.06 ? 96   THR   A C   1 
ATOM   170   O  O   . THR   A 1 27  ? 28.885  22.161  -43.679 1.00 103.44 ? 96   THR   A O   1 
ATOM   171   C  CB  . THR   A 1 27  ? 29.092  20.381  -40.978 1.00 95.95  ? 96   THR   A CB  1 
ATOM   172   O  OG1 . THR   A 1 27  ? 27.672  20.352  -41.144 1.00 102.40 ? 96   THR   A OG1 1 
ATOM   173   C  CG2 . THR   A 1 27  ? 29.400  20.134  -39.546 1.00 93.09  ? 96   THR   A CG2 1 
ATOM   174   N  N   . LEU   A 1 28  ? 30.965  21.363  -43.430 1.00 100.40 ? 97   LEU   A N   1 
ATOM   175   C  CA  . LEU   A 1 28  ? 31.169  21.248  -44.858 1.00 101.18 ? 97   LEU   A CA  1 
ATOM   176   C  C   . LEU   A 1 28  ? 31.679  19.853  -45.202 1.00 106.09 ? 97   LEU   A C   1 
ATOM   177   O  O   . LEU   A 1 28  ? 32.628  19.370  -44.558 1.00 107.82 ? 97   LEU   A O   1 
ATOM   178   C  CB  . LEU   A 1 28  ? 32.136  22.329  -45.350 1.00 100.53 ? 97   LEU   A CB  1 
ATOM   179   C  CG  . LEU   A 1 28  ? 33.541  22.450  -44.758 1.00 98.85  ? 97   LEU   A CG  1 
ATOM   180   C  CD1 . LEU   A 1 28  ? 34.587  21.755  -45.636 1.00 100.45 ? 97   LEU   A CD1 1 
ATOM   181   C  CD2 . LEU   A 1 28  ? 33.903  23.913  -44.553 1.00 99.89  ? 97   LEU   A CD2 1 
ATOM   182   N  N   . PRO   A 1 29  ? 31.074  19.172  -46.176 1.00 108.19 ? 98   PRO   A N   1 
ATOM   183   C  CA  . PRO   A 1 29  ? 31.647  17.929  -46.691 1.00 109.18 ? 98   PRO   A CA  1 
ATOM   184   C  C   . PRO   A 1 29  ? 32.819  18.242  -47.604 1.00 109.72 ? 98   PRO   A C   1 
ATOM   185   O  O   . PRO   A 1 29  ? 32.918  19.327  -48.174 1.00 109.12 ? 98   PRO   A O   1 
ATOM   186   C  CB  . PRO   A 1 29  ? 30.488  17.322  -47.476 1.00 114.44 ? 98   PRO   A CB  1 
ATOM   187   C  CG  . PRO   A 1 29  ? 29.756  18.541  -48.011 1.00 116.35 ? 98   PRO   A CG  1 
ATOM   188   C  CD  . PRO   A 1 29  ? 29.844  19.555  -46.883 1.00 114.04 ? 98   PRO   A CD  1 
ATOM   189   N  N   . LEU   A 1 30  ? 33.716  17.273  -47.752 1.00 114.33 ? 99   LEU   A N   1 
ATOM   190   C  CA  . LEU   A 1 30  ? 34.929  17.555  -48.510 1.00 118.74 ? 99   LEU   A CA  1 
ATOM   191   C  C   . LEU   A 1 30  ? 35.453  16.289  -49.174 1.00 127.90 ? 99   LEU   A C   1 
ATOM   192   O  O   . LEU   A 1 30  ? 35.418  15.205  -48.585 1.00 129.18 ? 99   LEU   A O   1 
ATOM   193   C  CB  . LEU   A 1 30  ? 35.986  18.179  -47.600 1.00 116.11 ? 99   LEU   A CB  1 
ATOM   194   C  CG  . LEU   A 1 30  ? 36.922  19.226  -48.186 1.00 117.74 ? 99   LEU   A CG  1 
ATOM   195   C  CD1 . LEU   A 1 30  ? 36.168  20.044  -49.193 1.00 117.84 ? 99   LEU   A CD1 1 
ATOM   196   C  CD2 . LEU   A 1 30  ? 37.443  20.126  -47.093 1.00 113.23 ? 99   LEU   A CD2 1 
ATOM   197   N  N   . GLN   A 1 31  ? 35.929  16.434  -50.407 1.00 142.90 ? 100  GLN   A N   1 
ATOM   198   C  CA  . GLN   A 1 31  ? 36.426  15.313  -51.195 1.00 143.85 ? 100  GLN   A CA  1 
ATOM   199   C  C   . GLN   A 1 31  ? 37.721  15.753  -51.859 1.00 144.24 ? 100  GLN   A C   1 
ATOM   200   O  O   . GLN   A 1 31  ? 37.701  16.575  -52.781 1.00 144.90 ? 100  GLN   A O   1 
ATOM   201   C  CB  . GLN   A 1 31  ? 35.395  14.872  -52.231 1.00 146.46 ? 100  GLN   A CB  1 
ATOM   202   C  CG  . GLN   A 1 31  ? 35.799  13.619  -52.966 1.00 150.27 ? 100  GLN   A CG  1 
ATOM   203   C  CD  . GLN   A 1 31  ? 34.819  12.493  -52.760 1.00 160.15 ? 100  GLN   A CD  1 
ATOM   204   O  OE1 . GLN   A 1 31  ? 34.152  12.412  -51.717 1.00 159.29 ? 100  GLN   A OE1 1 
ATOM   205   N  NE2 . GLN   A 1 31  ? 34.714  11.612  -53.760 1.00 163.47 ? 100  GLN   A NE2 1 
ATOM   206   N  N   . LEU   A 1 32  ? 38.839  15.209  -51.389 1.00 140.05 ? 101  LEU   A N   1 
ATOM   207   C  CA  . LEU   A 1 32  ? 40.165  15.670  -51.772 1.00 143.67 ? 101  LEU   A CA  1 
ATOM   208   C  C   . LEU   A 1 32  ? 40.811  14.677  -52.722 1.00 149.19 ? 101  LEU   A C   1 
ATOM   209   O  O   . LEU   A 1 32  ? 41.126  13.544  -52.330 1.00 149.40 ? 101  LEU   A O   1 
ATOM   210   C  CB  . LEU   A 1 32  ? 41.031  15.876  -50.530 1.00 142.14 ? 101  LEU   A CB  1 
ATOM   211   C  CG  . LEU   A 1 32  ? 40.461  16.874  -49.512 1.00 139.83 ? 101  LEU   A CG  1 
ATOM   212   C  CD1 . LEU   A 1 32  ? 40.211  16.195  -48.187 1.00 134.51 ? 101  LEU   A CD1 1 
ATOM   213   C  CD2 . LEU   A 1 32  ? 41.375  18.079  -49.315 1.00 137.70 ? 101  LEU   A CD2 1 
ATOM   214   N  N   . PHE   A 1 33  ? 41.017  15.109  -53.973 1.00 158.42 ? 102  PHE   A N   1 
ATOM   215   C  CA  . PHE   A 1 33  ? 41.604  14.299  -55.028 1.00 159.47 ? 102  PHE   A CA  1 
ATOM   216   C  C   . PHE   A 1 33  ? 43.084  14.602  -55.229 1.00 159.51 ? 102  PHE   A C   1 
ATOM   217   O  O   . PHE   A 1 33  ? 43.929  13.716  -55.064 1.00 159.17 ? 102  PHE   A O   1 
ATOM   218   C  CB  . PHE   A 1 33  ? 40.847  14.536  -56.347 1.00 159.48 ? 102  PHE   A CB  1 
ATOM   219   C  CG  . PHE   A 1 33  ? 39.626  13.679  -56.512 1.00 165.34 ? 102  PHE   A CG  1 
ATOM   220   C  CD1 . PHE   A 1 33  ? 38.488  13.904  -55.753 1.00 165.27 ? 102  PHE   A CD1 1 
ATOM   221   C  CD2 . PHE   A 1 33  ? 39.609  12.637  -57.434 1.00 173.04 ? 102  PHE   A CD2 1 
ATOM   222   C  CE1 . PHE   A 1 33  ? 37.355  13.103  -55.905 1.00 166.45 ? 102  PHE   A CE1 1 
ATOM   223   C  CE2 . PHE   A 1 33  ? 38.476  11.830  -57.597 1.00 170.55 ? 102  PHE   A CE2 1 
ATOM   224   C  CZ  . PHE   A 1 33  ? 37.348  12.067  -56.829 1.00 170.22 ? 102  PHE   A CZ  1 
ATOM   225   N  N   . HIS   A 1 34  ? 43.401  15.846  -55.601 1.00 156.25 ? 103  HIS   A N   1 
ATOM   226   C  CA  . HIS   A 1 34  ? 44.752  16.214  -56.013 1.00 153.70 ? 103  HIS   A CA  1 
ATOM   227   C  C   . HIS   A 1 34  ? 45.739  15.939  -54.880 1.00 149.78 ? 103  HIS   A C   1 
ATOM   228   O  O   . HIS   A 1 34  ? 45.405  16.151  -53.708 1.00 151.24 ? 103  HIS   A O   1 
ATOM   229   C  CB  . HIS   A 1 34  ? 44.808  17.696  -56.410 1.00 153.54 ? 103  HIS   A CB  1 
ATOM   230   C  CG  . HIS   A 1 34  ? 43.635  18.155  -57.225 1.00 157.15 ? 103  HIS   A CG  1 
ATOM   231   N  ND1 . HIS   A 1 34  ? 42.581  18.857  -56.682 1.00 158.54 ? 103  HIS   A ND1 1 
ATOM   232   C  CD2 . HIS   A 1 34  ? 43.353  18.014  -58.541 1.00 157.97 ? 103  HIS   A CD2 1 
ATOM   233   C  CE1 . HIS   A 1 34  ? 41.698  19.127  -57.627 1.00 159.08 ? 103  HIS   A CE1 1 
ATOM   234   N  NE2 . HIS   A 1 34  ? 42.143  18.627  -58.765 1.00 160.38 ? 103  HIS   A NE2 1 
ATOM   235   N  N   . PRO   A 1 35  ? 46.954  15.469  -55.183 1.00 147.67 ? 104  PRO   A N   1 
ATOM   236   C  CA  . PRO   A 1 35  ? 47.871  15.065  -54.102 1.00 146.94 ? 104  PRO   A CA  1 
ATOM   237   C  C   . PRO   A 1 35  ? 48.333  16.214  -53.232 1.00 144.76 ? 104  PRO   A C   1 
ATOM   238   O  O   . PRO   A 1 35  ? 48.674  15.991  -52.061 1.00 146.62 ? 104  PRO   A O   1 
ATOM   239   C  CB  . PRO   A 1 35  ? 49.044  14.427  -54.860 1.00 150.11 ? 104  PRO   A CB  1 
ATOM   240   C  CG  . PRO   A 1 35  ? 48.971  14.990  -56.231 1.00 153.52 ? 104  PRO   A CG  1 
ATOM   241   C  CD  . PRO   A 1 35  ? 47.507  15.176  -56.512 1.00 154.14 ? 104  PRO   A CD  1 
ATOM   242   N  N   . GLN   A 1 36  ? 48.353  17.438  -53.761 1.00 148.82 ? 105  GLN   A N   1 
ATOM   243   C  CA  . GLN   A 1 36  ? 48.675  18.588  -52.925 1.00 149.35 ? 105  GLN   A CA  1 
ATOM   244   C  C   . GLN   A 1 36  ? 47.729  18.669  -51.721 1.00 150.45 ? 105  GLN   A C   1 
ATOM   245   O  O   . GLN   A 1 36  ? 48.169  18.696  -50.565 1.00 148.33 ? 105  GLN   A O   1 
ATOM   246   C  CB  . GLN   A 1 36  ? 48.633  19.868  -53.768 1.00 144.96 ? 105  GLN   A CB  1 
ATOM   247   N  N   . GLU   A 1 37  ? 46.415  18.659  -51.976 1.00 151.60 ? 106  GLU   A N   1 
ATOM   248   C  CA  . GLU   A 1 37  ? 45.456  18.757  -50.879 1.00 148.89 ? 106  GLU   A CA  1 
ATOM   249   C  C   . GLU   A 1 37  ? 45.356  17.459  -50.071 1.00 148.20 ? 106  GLU   A C   1 
ATOM   250   O  O   . GLU   A 1 37  ? 44.980  17.497  -48.893 1.00 147.47 ? 106  GLU   A O   1 
ATOM   251   C  CB  . GLU   A 1 37  ? 44.087  19.173  -51.431 1.00 147.29 ? 106  GLU   A CB  1 
ATOM   252   C  CG  . GLU   A 1 37  ? 43.638  18.391  -52.636 1.00 149.63 ? 106  GLU   A CG  1 
ATOM   253   C  CD  . GLU   A 1 37  ? 42.440  19.023  -53.316 1.00 153.90 ? 106  GLU   A CD  1 
ATOM   254   O  OE1 . GLU   A 1 37  ? 41.624  18.278  -53.908 1.00 157.23 ? 106  GLU   A OE1 1 
ATOM   255   O  OE2 . GLU   A 1 37  ? 42.296  20.264  -53.231 1.00 153.17 ? 106  GLU   A OE2 1 
ATOM   256   N  N   . VAL   A 1 38  ? 45.676  16.307  -50.668 1.00 143.35 ? 107  VAL   A N   1 
ATOM   257   C  CA  . VAL   A 1 38  ? 45.642  15.053  -49.909 1.00 141.16 ? 107  VAL   A CA  1 
ATOM   258   C  C   . VAL   A 1 38  ? 46.767  15.020  -48.882 1.00 138.30 ? 107  VAL   A C   1 
ATOM   259   O  O   . VAL   A 1 38  ? 46.588  14.510  -47.765 1.00 137.96 ? 107  VAL   A O   1 
ATOM   260   C  CB  . VAL   A 1 38  ? 45.698  13.834  -50.853 1.00 142.59 ? 107  VAL   A CB  1 
ATOM   261   C  CG1 . VAL   A 1 38  ? 46.180  12.568  -50.105 1.00 138.82 ? 107  VAL   A CG1 1 
ATOM   262   C  CG2 . VAL   A 1 38  ? 44.335  13.582  -51.497 1.00 143.16 ? 107  VAL   A CG2 1 
ATOM   263   N  N   . SER   A 1 39  ? 47.946  15.545  -49.234 1.00 140.41 ? 108  SER   A N   1 
ATOM   264   C  CA  . SER   A 1 39  ? 49.043  15.577  -48.271 1.00 139.20 ? 108  SER   A CA  1 
ATOM   265   C  C   . SER   A 1 39  ? 48.784  16.609  -47.185 1.00 140.06 ? 108  SER   A C   1 
ATOM   266   O  O   . SER   A 1 39  ? 49.202  16.426  -46.032 1.00 137.42 ? 108  SER   A O   1 
ATOM   267   C  CB  . SER   A 1 39  ? 50.367  15.876  -48.976 1.00 141.23 ? 108  SER   A CB  1 
ATOM   268   O  OG  . SER   A 1 39  ? 50.717  14.860  -49.903 1.00 139.92 ? 108  SER   A OG  1 
ATOM   269   N  N   . MET   A 1 40  ? 48.098  17.703  -47.536 1.00 144.30 ? 109  MET   A N   1 
ATOM   270   C  CA  . MET   A 1 40  ? 47.653  18.703  -46.570 1.00 144.09 ? 109  MET   A CA  1 
ATOM   271   C  C   . MET   A 1 40  ? 46.822  18.058  -45.452 1.00 142.70 ? 109  MET   A C   1 
ATOM   272   O  O   . MET   A 1 40  ? 47.269  18.012  -44.296 1.00 141.51 ? 109  MET   A O   1 
ATOM   273   C  CB  . MET   A 1 40  ? 46.856  19.817  -47.268 1.00 145.79 ? 109  MET   A CB  1 
ATOM   274   C  CG  . MET   A 1 40  ? 46.289  20.891  -46.311 1.00 144.15 ? 109  MET   A CG  1 
ATOM   275   S  SD  . MET   A 1 40  ? 44.771  21.653  -46.943 1.00 156.80 ? 109  MET   A SD  1 
ATOM   276   C  CE  . MET   A 1 40  ? 44.468  22.959  -45.763 1.00 137.58 ? 109  MET   A CE  1 
ATOM   277   N  N   . VAL   A 1 41  ? 45.618  17.555  -45.775 1.00 136.96 ? 110  VAL   A N   1 
ATOM   278   C  CA  . VAL   A 1 41  ? 44.746  16.974  -44.748 1.00 129.16 ? 110  VAL   A CA  1 
ATOM   279   C  C   . VAL   A 1 41  ? 45.460  15.884  -43.973 1.00 126.30 ? 110  VAL   A C   1 
ATOM   280   O  O   . VAL   A 1 41  ? 45.228  15.723  -42.774 1.00 125.54 ? 110  VAL   A O   1 
ATOM   281   C  CB  . VAL   A 1 41  ? 43.429  16.445  -45.359 1.00 122.79 ? 110  VAL   A CB  1 
ATOM   282   C  CG1 . VAL   A 1 41  ? 42.691  17.554  -46.013 1.00 124.71 ? 110  VAL   A CG1 1 
ATOM   283   C  CG2 . VAL   A 1 41  ? 43.713  15.354  -46.367 1.00 126.76 ? 110  VAL   A CG2 1 
ATOM   284   N  N   . ARG   A 1 42  ? 46.366  15.148  -44.627 1.00 127.98 ? 111  ARG   A N   1 
ATOM   285   C  CA  . ARG   A 1 42  ? 47.189  14.180  -43.913 1.00 128.69 ? 111  ARG   A CA  1 
ATOM   286   C  C   . ARG   A 1 42  ? 47.979  14.855  -42.797 1.00 132.30 ? 111  ARG   A C   1 
ATOM   287   O  O   . ARG   A 1 42  ? 47.923  14.428  -41.634 1.00 130.43 ? 111  ARG   A O   1 
ATOM   288   C  CB  . ARG   A 1 42  ? 48.119  13.478  -44.902 1.00 129.61 ? 111  ARG   A CB  1 
ATOM   289   N  N   . ASN   A 1 43  ? 48.695  15.936  -43.121 1.00 132.35 ? 112  ASN   A N   1 
ATOM   290   C  CA  . ASN   A 1 43  ? 49.379  16.693  -42.075 1.00 132.91 ? 112  ASN   A CA  1 
ATOM   291   C  C   . ASN   A 1 43  ? 48.388  17.268  -41.076 1.00 127.77 ? 112  ASN   A C   1 
ATOM   292   O  O   . ASN   A 1 43  ? 48.660  17.307  -39.872 1.00 127.33 ? 112  ASN   A O   1 
ATOM   293   C  CB  . ASN   A 1 43  ? 50.223  17.820  -42.667 1.00 136.02 ? 112  ASN   A CB  1 
ATOM   294   C  CG  . ASN   A 1 43  ? 51.483  17.319  -43.313 1.00 145.49 ? 112  ASN   A CG  1 
ATOM   295   O  OD1 . ASN   A 1 43  ? 51.987  16.244  -42.978 1.00 151.07 ? 112  ASN   A OD1 1 
ATOM   296   N  ND2 . ASN   A 1 43  ? 52.010  18.098  -44.251 1.00 147.63 ? 112  ASN   A ND2 1 
ATOM   297   N  N   . LEU   A 1 44  ? 47.232  17.721  -41.558 1.00 126.74 ? 113  LEU   A N   1 
ATOM   298   C  CA  . LEU   A 1 44  ? 46.277  18.388  -40.685 1.00 123.90 ? 113  LEU   A CA  1 
ATOM   299   C  C   . LEU   A 1 44  ? 45.803  17.459  -39.580 1.00 125.97 ? 113  LEU   A C   1 
ATOM   300   O  O   . LEU   A 1 44  ? 45.859  17.802  -38.393 1.00 126.27 ? 113  LEU   A O   1 
ATOM   301   C  CB  . LEU   A 1 44  ? 45.098  18.889  -41.508 1.00 123.41 ? 113  LEU   A CB  1 
ATOM   302   C  CG  . LEU   A 1 44  ? 45.144  20.344  -41.945 1.00 123.86 ? 113  LEU   A CG  1 
ATOM   303   C  CD1 . LEU   A 1 44  ? 44.010  20.589  -42.910 1.00 124.69 ? 113  LEU   A CD1 1 
ATOM   304   C  CD2 . LEU   A 1 44  ? 45.039  21.273  -40.738 1.00 124.66 ? 113  LEU   A CD2 1 
ATOM   305   N  N   . ILE   A 1 45  ? 45.344  16.268  -39.946 1.00 124.11 ? 114  ILE   A N   1 
ATOM   306   C  CA  . ILE   A 1 45  ? 44.720  15.402  -38.956 1.00 121.60 ? 114  ILE   A CA  1 
ATOM   307   C  C   . ILE   A 1 45  ? 45.764  14.815  -38.015 1.00 118.44 ? 114  ILE   A C   1 
ATOM   308   O  O   . ILE   A 1 45  ? 45.450  14.443  -36.874 1.00 114.07 ? 114  ILE   A O   1 
ATOM   309   C  CB  . ILE   A 1 45  ? 43.941  14.317  -39.690 1.00 115.37 ? 114  ILE   A CB  1 
ATOM   310   C  CG1 . ILE   A 1 45  ? 44.867  13.758  -40.752 1.00 117.34 ? 114  ILE   A CG1 1 
ATOM   311   C  CG2 . ILE   A 1 45  ? 42.650  14.846  -40.281 1.00 111.55 ? 114  ILE   A CG2 1 
ATOM   312   C  CD1 . ILE   A 1 45  ? 44.518  12.301  -41.147 1.00 119.96 ? 114  ILE   A CD1 1 
ATOM   313   N  N   . GLN   A 1 46  ? 47.006  14.694  -38.488 1.00 118.71 ? 115  GLN   A N   1 
ATOM   314   C  CA  . GLN   A 1 46  ? 48.119  14.424  -37.585 1.00 119.34 ? 115  GLN   A CA  1 
ATOM   315   C  C   . GLN   A 1 46  ? 48.336  15.554  -36.594 1.00 120.02 ? 115  GLN   A C   1 
ATOM   316   O  O   . GLN   A 1 46  ? 48.628  15.316  -35.417 1.00 116.48 ? 115  GLN   A O   1 
ATOM   317   C  CB  . GLN   A 1 46  ? 49.396  14.175  -38.384 1.00 118.71 ? 115  GLN   A CB  1 
ATOM   318   C  CG  . GLN   A 1 46  ? 49.340  12.928  -39.242 1.00 121.79 ? 115  GLN   A CG  1 
ATOM   319   C  CD  . GLN   A 1 46  ? 49.678  11.667  -38.463 1.00 127.62 ? 115  GLN   A CD  1 
ATOM   320   O  OE1 . GLN   A 1 46  ? 48.859  11.151  -37.680 1.00 124.32 ? 115  GLN   A OE1 1 
ATOM   321   N  NE2 . GLN   A 1 46  ? 50.901  11.166  -38.664 1.00 127.72 ? 115  GLN   A NE2 1 
ATOM   322   N  N   . LYS   A 1 47  ? 48.190  16.808  -37.053 1.00 123.91 ? 116  LYS   A N   1 
ATOM   323   C  CA  . LYS   A 1 47  ? 48.338  17.990  -36.216 1.00 123.42 ? 116  LYS   A CA  1 
ATOM   324   C  C   . LYS   A 1 47  ? 46.893  18.426  -35.955 1.00 128.67 ? 116  LYS   A C   1 
ATOM   325   O  O   . LYS   A 1 47  ? 45.981  17.595  -36.009 1.00 130.40 ? 116  LYS   A O   1 
ATOM   326   C  CB  . LYS   A 1 47  ? 48.983  19.123  -37.014 1.00 118.87 ? 116  LYS   A CB  1 
ATOM   327   N  N   . ASP   A 1 48  ? 46.668  19.710  -35.675 1.00 139.74 ? 117  ASP   A N   1 
ATOM   328   C  CA  . ASP   A 1 48  ? 45.362  20.215  -35.266 1.00 139.57 ? 117  ASP   A CA  1 
ATOM   329   C  C   . ASP   A 1 48  ? 44.107  19.837  -36.046 1.00 138.02 ? 117  ASP   A C   1 
ATOM   330   O  O   . ASP   A 1 48  ? 43.019  19.846  -35.466 1.00 136.43 ? 117  ASP   A O   1 
ATOM   331   C  CB  . ASP   A 1 48  ? 45.534  21.722  -35.038 1.00 142.02 ? 117  ASP   A CB  1 
ATOM   332   C  CG  . ASP   A 1 48  ? 45.657  22.508  -36.355 1.00 143.66 ? 117  ASP   A CG  1 
ATOM   333   O  OD1 . ASP   A 1 48  ? 46.234  21.965  -37.334 1.00 142.83 ? 117  ASP   A OD1 1 
ATOM   334   O  OD2 . ASP   A 1 48  ? 45.173  23.669  -36.419 1.00 141.07 ? 117  ASP   A OD2 1 
ATOM   335   N  N   . ARG   A 1 49  ? 44.237  19.528  -37.342 1.00 124.60 ? 118  ARG   A N   1 
ATOM   336   C  CA  . ARG   A 1 49  ? 43.147  19.248  -38.284 1.00 119.91 ? 118  ARG   A CA  1 
ATOM   337   C  C   . ARG   A 1 49  ? 42.206  20.443  -38.440 1.00 115.05 ? 118  ARG   A C   1 
ATOM   338   O  O   . ARG   A 1 49  ? 41.070  20.284  -38.897 1.00 110.68 ? 118  ARG   A O   1 
ATOM   339   C  CB  . ARG   A 1 49  ? 42.346  17.974  -37.968 1.00 121.70 ? 118  ARG   A CB  1 
ATOM   340   N  N   . THR   A 1 50  ? 42.680  21.643  -38.117 1.00 120.51 ? 119  THR   A N   1 
ATOM   341   C  CA  . THR   A 1 50  ? 41.937  22.877  -38.357 1.00 113.22 ? 119  THR   A CA  1 
ATOM   342   C  C   . THR   A 1 50  ? 42.596  23.589  -39.529 1.00 115.25 ? 119  THR   A C   1 
ATOM   343   O  O   . THR   A 1 50  ? 43.784  23.929  -39.468 1.00 115.99 ? 119  THR   A O   1 
ATOM   344   C  CB  . THR   A 1 50  ? 41.901  23.780  -37.130 1.00 110.20 ? 119  THR   A CB  1 
ATOM   345   O  OG1 . THR   A 1 50  ? 41.366  23.056  -36.018 1.00 114.12 ? 119  THR   A OG1 1 
ATOM   346   C  CG2 . THR   A 1 50  ? 40.992  24.960  -37.402 1.00 103.83 ? 119  THR   A CG2 1 
ATOM   347   N  N   . PHE   A 1 51  ? 41.831  23.796  -40.592 1.00 112.30 ? 120  PHE   A N   1 
ATOM   348   C  CA  . PHE   A 1 51  ? 42.276  24.558  -41.747 1.00 110.09 ? 120  PHE   A CA  1 
ATOM   349   C  C   . PHE   A 1 51  ? 41.451  25.845  -41.852 1.00 106.07 ? 120  PHE   A C   1 
ATOM   350   O  O   . PHE   A 1 51  ? 40.565  26.123  -41.025 1.00 102.05 ? 120  PHE   A O   1 
ATOM   351   C  CB  . PHE   A 1 51  ? 42.209  23.696  -43.019 1.00 108.93 ? 120  PHE   A CB  1 
ATOM   352   C  CG  . PHE   A 1 51  ? 40.816  23.370  -43.477 1.00 102.69 ? 120  PHE   A CG  1 
ATOM   353   C  CD1 . PHE   A 1 51  ? 40.062  22.416  -42.832 1.00 99.03  ? 120  PHE   A CD1 1 
ATOM   354   C  CD2 . PHE   A 1 51  ? 40.274  24.013  -44.578 1.00 107.16 ? 120  PHE   A CD2 1 
ATOM   355   C  CE1 . PHE   A 1 51  ? 38.794  22.125  -43.258 1.00 99.21  ? 120  PHE   A CE1 1 
ATOM   356   C  CE2 . PHE   A 1 51  ? 39.000  23.723  -45.010 1.00 106.09 ? 120  PHE   A CE2 1 
ATOM   357   C  CZ  . PHE   A 1 51  ? 38.261  22.780  -44.349 1.00 99.95  ? 120  PHE   A CZ  1 
ATOM   358   N  N   . ALA   A 1 52  ? 41.756  26.641  -42.879 1.00 106.63 ? 121  ALA   A N   1 
ATOM   359   C  CA  . ALA   A 1 52  ? 41.155  27.952  -43.079 1.00 105.79 ? 121  ALA   A CA  1 
ATOM   360   C  C   . ALA   A 1 52  ? 40.229  27.923  -44.283 1.00 109.90 ? 121  ALA   A C   1 
ATOM   361   O  O   . ALA   A 1 52  ? 40.607  27.432  -45.352 1.00 117.36 ? 121  ALA   A O   1 
ATOM   362   C  CB  . ALA   A 1 52  ? 42.218  29.026  -43.278 1.00 103.97 ? 121  ALA   A CB  1 
ATOM   363   N  N   . VAL   A 1 53  ? 39.024  28.454  -44.106 1.00 108.17 ? 122  VAL   A N   1 
ATOM   364   C  CA  . VAL   A 1 53  ? 38.071  28.613  -45.192 1.00 114.43 ? 122  VAL   A CA  1 
ATOM   365   C  C   . VAL   A 1 53  ? 38.019  30.096  -45.521 1.00 121.49 ? 122  VAL   A C   1 
ATOM   366   O  O   . VAL   A 1 53  ? 37.380  30.889  -44.818 1.00 121.02 ? 122  VAL   A O   1 
ATOM   367   C  CB  . VAL   A 1 53  ? 36.687  28.070  -44.846 1.00 109.02 ? 122  VAL   A CB  1 
ATOM   368   C  CG1 . VAL   A 1 53  ? 35.751  28.364  -45.997 1.00 119.89 ? 122  VAL   A CG1 1 
ATOM   369   C  CG2 . VAL   A 1 53  ? 36.771  26.595  -44.622 1.00 104.47 ? 122  VAL   A CG2 1 
ATOM   370   N  N   . LEU   A 1 54  ? 38.677  30.456  -46.620 1.00 125.31 ? 123  LEU   A N   1 
ATOM   371   C  CA  . LEU   A 1 54  ? 38.818  31.845  -47.021 1.00 131.62 ? 123  LEU   A CA  1 
ATOM   372   C  C   . LEU   A 1 54  ? 37.494  32.382  -47.549 1.00 143.92 ? 123  LEU   A C   1 
ATOM   373   O  O   . LEU   A 1 54  ? 36.968  31.882  -48.548 1.00 147.05 ? 123  LEU   A O   1 
ATOM   374   C  CB  . LEU   A 1 54  ? 39.904  31.968  -48.091 1.00 128.39 ? 123  LEU   A CB  1 
ATOM   375   C  CG  . LEU   A 1 54  ? 41.320  32.339  -47.655 1.00 119.82 ? 123  LEU   A CG  1 
ATOM   376   C  CD1 . LEU   A 1 54  ? 41.395  33.776  -47.189 1.00 123.14 ? 123  LEU   A CD1 1 
ATOM   377   C  CD2 . LEU   A 1 54  ? 41.724  31.425  -46.547 1.00 119.76 ? 123  LEU   A CD2 1 
ATOM   378   N  N   . ALA   A 1 55  ? 36.968  33.421  -46.901 1.00 180.77 ? 124  ALA   A N   1 
ATOM   379   C  CA  . ALA   A 1 55  ? 35.695  34.025  -47.291 1.00 181.40 ? 124  ALA   A CA  1 
ATOM   380   C  C   . ALA   A 1 55  ? 35.979  35.310  -48.070 1.00 182.66 ? 124  ALA   A C   1 
ATOM   381   O  O   . ALA   A 1 55  ? 36.064  36.402  -47.501 1.00 183.03 ? 124  ALA   A O   1 
ATOM   382   C  CB  . ALA   A 1 55  ? 34.823  34.281  -46.066 1.00 180.23 ? 124  ALA   A CB  1 
ATOM   383   N  N   . TYR   A 1 56  ? 36.120  35.176  -49.389 1.00 156.52 ? 125  TYR   A N   1 
ATOM   384   C  CA  . TYR   A 1 56  ? 36.462  36.302  -50.243 1.00 147.85 ? 125  TYR   A CA  1 
ATOM   385   C  C   . TYR   A 1 56  ? 35.281  37.254  -50.398 1.00 145.91 ? 125  TYR   A C   1 
ATOM   386   O  O   . TYR   A 1 56  ? 34.120  36.845  -50.320 1.00 140.40 ? 125  TYR   A O   1 
ATOM   387   C  CB  . TYR   A 1 56  ? 36.920  35.815  -51.607 1.00 143.75 ? 125  TYR   A CB  1 
ATOM   388   C  CG  . TYR   A 1 56  ? 37.683  34.507  -51.591 1.00 144.17 ? 125  TYR   A CG  1 
ATOM   389   C  CD1 . TYR   A 1 56  ? 39.050  34.473  -51.338 1.00 141.48 ? 125  TYR   A CD1 1 
ATOM   390   C  CD2 . TYR   A 1 56  ? 37.040  33.304  -51.868 1.00 144.79 ? 125  TYR   A CD2 1 
ATOM   391   C  CE1 . TYR   A 1 56  ? 39.757  33.268  -51.353 1.00 138.02 ? 125  TYR   A CE1 1 
ATOM   392   C  CE2 . TYR   A 1 56  ? 37.732  32.106  -51.884 1.00 142.55 ? 125  TYR   A CE2 1 
ATOM   393   C  CZ  . TYR   A 1 56  ? 39.086  32.086  -51.625 1.00 139.98 ? 125  TYR   A CZ  1 
ATOM   394   O  OH  . TYR   A 1 56  ? 39.753  30.876  -51.639 1.00 141.39 ? 125  TYR   A OH  1 
ATOM   395   N  N   . ALA   A 1 64  ? 39.115  38.059  -50.695 1.00 147.41 ? 133  ALA   A N   1 
ATOM   396   C  CA  . ALA   A 1 64  ? 39.084  39.060  -49.629 1.00 149.88 ? 133  ALA   A CA  1 
ATOM   397   C  C   . ALA   A 1 64  ? 39.923  38.643  -48.411 1.00 144.71 ? 133  ALA   A C   1 
ATOM   398   O  O   . ALA   A 1 64  ? 40.729  37.704  -48.486 1.00 141.31 ? 133  ALA   A O   1 
ATOM   399   C  CB  . ALA   A 1 64  ? 37.642  39.352  -49.197 1.00 150.00 ? 133  ALA   A CB  1 
ATOM   400   N  N   . GLN   A 1 65  ? 39.724  39.345  -47.295 1.00 132.95 ? 134  GLN   A N   1 
ATOM   401   C  CA  . GLN   A 1 65  ? 40.620  39.253  -46.149 1.00 126.33 ? 134  GLN   A CA  1 
ATOM   402   C  C   . GLN   A 1 65  ? 39.929  38.696  -44.903 1.00 124.95 ? 134  GLN   A C   1 
ATOM   403   O  O   . GLN   A 1 65  ? 40.258  39.090  -43.785 1.00 119.54 ? 134  GLN   A O   1 
ATOM   404   C  CB  . GLN   A 1 65  ? 41.238  40.622  -45.843 1.00 121.45 ? 134  GLN   A CB  1 
ATOM   405   C  CG  . GLN   A 1 65  ? 40.313  41.818  -46.052 1.00 126.78 ? 134  GLN   A CG  1 
ATOM   406   C  CD  . GLN   A 1 65  ? 40.647  42.583  -47.325 1.00 132.08 ? 134  GLN   A CD  1 
ATOM   407   O  OE1 . GLN   A 1 65  ? 41.257  42.035  -48.247 1.00 130.79 ? 134  GLN   A OE1 1 
ATOM   408   N  NE2 . GLN   A 1 65  ? 40.259  43.859  -47.376 1.00 132.41 ? 134  GLN   A NE2 1 
ATOM   409   N  N   . PHE   A 1 66  ? 38.953  37.793  -45.077 1.00 127.83 ? 135  PHE   A N   1 
ATOM   410   C  CA  . PHE   A 1 66  ? 38.232  37.223  -43.941 1.00 122.22 ? 135  PHE   A CA  1 
ATOM   411   C  C   . PHE   A 1 66  ? 37.892  35.762  -44.211 1.00 124.37 ? 135  PHE   A C   1 
ATOM   412   O  O   . PHE   A 1 66  ? 37.996  35.269  -45.339 1.00 126.00 ? 135  PHE   A O   1 
ATOM   413   C  CB  . PHE   A 1 66  ? 36.939  37.991  -43.633 1.00 121.82 ? 135  PHE   A CB  1 
ATOM   414   C  CG  . PHE   A 1 66  ? 37.150  39.387  -43.104 1.00 116.06 ? 135  PHE   A CG  1 
ATOM   415   C  CD1 . PHE   A 1 66  ? 37.466  40.441  -43.962 1.00 119.63 ? 135  PHE   A CD1 1 
ATOM   416   C  CD2 . PHE   A 1 66  ? 36.976  39.656  -41.755 1.00 113.45 ? 135  PHE   A CD2 1 
ATOM   417   C  CE1 . PHE   A 1 66  ? 37.642  41.717  -43.478 1.00 115.77 ? 135  PHE   A CE1 1 
ATOM   418   C  CE2 . PHE   A 1 66  ? 37.145  40.944  -41.259 1.00 113.32 ? 135  PHE   A CE2 1 
ATOM   419   C  CZ  . PHE   A 1 66  ? 37.476  41.975  -42.124 1.00 115.85 ? 135  PHE   A CZ  1 
ATOM   420   N  N   . GLY   A 1 67  ? 37.437  35.085  -43.161 1.00 123.06 ? 136  GLY   A N   1 
ATOM   421   C  CA  . GLY   A 1 67  ? 37.101  33.680  -43.256 1.00 119.42 ? 136  GLY   A CA  1 
ATOM   422   C  C   . GLY   A 1 67  ? 36.876  33.079  -41.880 1.00 106.25 ? 136  GLY   A C   1 
ATOM   423   O  O   . GLY   A 1 67  ? 36.832  33.783  -40.870 1.00 104.08 ? 136  GLY   A O   1 
ATOM   424   N  N   . THR   A 1 68  ? 36.743  31.759  -41.863 1.00 102.61 ? 137  THR   A N   1 
ATOM   425   C  CA  . THR   A 1 68  ? 36.490  31.041  -40.630 1.00 99.71  ? 137  THR   A CA  1 
ATOM   426   C  C   . THR   A 1 68  ? 37.337  29.785  -40.623 1.00 99.45  ? 137  THR   A C   1 
ATOM   427   O  O   . THR   A 1 68  ? 37.485  29.126  -41.653 1.00 102.44 ? 137  THR   A O   1 
ATOM   428   C  CB  . THR   A 1 68  ? 35.006  30.690  -40.480 1.00 98.07  ? 137  THR   A CB  1 
ATOM   429   O  OG1 . THR   A 1 68  ? 34.250  31.894  -40.299 1.00 100.37 ? 137  THR   A OG1 1 
ATOM   430   C  CG2 . THR   A 1 68  ? 34.790  29.790  -39.299 1.00 93.82  ? 137  THR   A CG2 1 
ATOM   431   N  N   . THR   A 1 69  ? 37.931  29.492  -39.471 1.00 98.10  ? 138  THR   A N   1 
ATOM   432   C  CA  . THR   A 1 69  ? 38.650  28.239  -39.304 1.00 95.21  ? 138  THR   A CA  1 
ATOM   433   C  C   . THR   A 1 69  ? 37.662  27.092  -39.224 1.00 96.05  ? 138  THR   A C   1 
ATOM   434   O  O   . THR   A 1 69  ? 36.601  27.205  -38.594 1.00 97.50  ? 138  THR   A O   1 
ATOM   435   C  CB  . THR   A 1 69  ? 39.493  28.273  -38.035 1.00 93.23  ? 138  THR   A CB  1 
ATOM   436   O  OG1 . THR   A 1 69  ? 38.633  28.276  -36.890 1.00 92.64  ? 138  THR   A OG1 1 
ATOM   437   C  CG2 . THR   A 1 69  ? 40.295  29.524  -38.006 1.00 93.48  ? 138  THR   A CG2 1 
ATOM   438   N  N   . ALA   A 1 70  ? 37.997  25.984  -39.868 1.00 95.22  ? 139  ALA   A N   1 
ATOM   439   C  CA  . ALA   A 1 70  ? 37.141  24.812  -39.860 1.00 91.96  ? 139  ALA   A CA  1 
ATOM   440   C  C   . ALA   A 1 70  ? 37.918  23.639  -39.287 1.00 99.81  ? 139  ALA   A C   1 
ATOM   441   O  O   . ALA   A 1 70  ? 39.073  23.412  -39.672 1.00 102.88 ? 139  ALA   A O   1 
ATOM   442   C  CB  . ALA   A 1 70  ? 36.615  24.495  -41.253 1.00 90.05  ? 139  ALA   A CB  1 
ATOM   443   N  N   . GLU   A 1 71  ? 37.296  22.925  -38.334 1.00 97.66  ? 140  GLU   A N   1 
ATOM   444   C  CA  . GLU   A 1 71  ? 37.933  21.831  -37.599 1.00 95.78  ? 140  GLU   A CA  1 
ATOM   445   C  C   . GLU   A 1 71  ? 37.452  20.515  -38.178 1.00 97.76  ? 140  GLU   A C   1 
ATOM   446   O  O   . GLU   A 1 71  ? 36.246  20.247  -38.190 1.00 100.26 ? 140  GLU   A O   1 
ATOM   447   C  CB  . GLU   A 1 71  ? 37.621  21.880  -36.099 1.00 92.79  ? 140  GLU   A CB  1 
ATOM   448   C  CG  . GLU   A 1 71  ? 38.385  20.830  -35.275 1.00 96.03  ? 140  GLU   A CG  1 
ATOM   449   C  CD  . GLU   A 1 71  ? 37.781  20.547  -33.893 1.00 101.50 ? 140  GLU   A CD  1 
ATOM   450   O  OE1 . GLU   A 1 71  ? 37.276  21.479  -33.223 1.00 96.38  ? 140  GLU   A OE1 1 
ATOM   451   O  OE2 . GLU   A 1 71  ? 37.819  19.367  -33.471 1.00 108.17 ? 140  GLU   A OE2 1 
ATOM   452   N  N   . ILE   A 1 72  ? 38.388  19.695  -38.648 1.00 103.19 ? 141  ILE   A N   1 
ATOM   453   C  CA  . ILE   A 1 72  ? 38.038  18.380  -39.170 1.00 105.47 ? 141  ILE   A CA  1 
ATOM   454   C  C   . ILE   A 1 72  ? 37.530  17.518  -38.020 1.00 103.87 ? 141  ILE   A C   1 
ATOM   455   O  O   . ILE   A 1 72  ? 38.174  17.411  -36.971 1.00 104.02 ? 141  ILE   A O   1 
ATOM   456   C  CB  . ILE   A 1 72  ? 39.242  17.745  -39.887 1.00 108.31 ? 141  ILE   A CB  1 
ATOM   457   C  CG1 . ILE   A 1 72  ? 39.729  18.643  -41.040 1.00 107.67 ? 141  ILE   A CG1 1 
ATOM   458   C  CG2 . ILE   A 1 72  ? 38.897  16.363  -40.435 1.00 108.22 ? 141  ILE   A CG2 1 
ATOM   459   C  CD1 . ILE   A 1 72  ? 41.001  18.157  -41.739 1.00 111.49 ? 141  ILE   A CD1 1 
ATOM   460   N  N   . TYR   A 1 73  ? 36.340  16.943  -38.186 1.00 98.85  ? 142  TYR   A N   1 
ATOM   461   C  CA  . TYR   A 1 73  ? 35.798  16.021  -37.203 1.00 101.83 ? 142  TYR   A CA  1 
ATOM   462   C  C   . TYR   A 1 73  ? 35.515  14.640  -37.771 1.00 103.07 ? 142  TYR   A C   1 
ATOM   463   O  O   . TYR   A 1 73  ? 35.164  13.743  -37.000 1.00 106.59 ? 142  TYR   A O   1 
ATOM   464   C  CB  . TYR   A 1 73  ? 34.516  16.590  -36.561 1.00 103.58 ? 142  TYR   A CB  1 
ATOM   465   C  CG  . TYR   A 1 73  ? 33.302  16.725  -37.476 1.00 101.19 ? 142  TYR   A CG  1 
ATOM   466   C  CD1 . TYR   A 1 73  ? 32.474  15.636  -37.749 1.00 99.15  ? 142  TYR   A CD1 1 
ATOM   467   C  CD2 . TYR   A 1 73  ? 32.969  17.949  -38.036 1.00 100.49 ? 142  TYR   A CD2 1 
ATOM   468   C  CE1 . TYR   A 1 73  ? 31.373  15.757  -38.567 1.00 100.37 ? 142  TYR   A CE1 1 
ATOM   469   C  CE2 . TYR   A 1 73  ? 31.873  18.076  -38.860 1.00 100.49 ? 142  TYR   A CE2 1 
ATOM   470   C  CZ  . TYR   A 1 73  ? 31.073  16.978  -39.119 1.00 101.18 ? 142  TYR   A CZ  1 
ATOM   471   O  OH  . TYR   A 1 73  ? 29.970  17.102  -39.940 1.00 109.88 ? 142  TYR   A OH  1 
ATOM   472   N  N   . ALA   A 1 74  ? 35.670  14.439  -39.081 1.00 103.42 ? 143  ALA   A N   1 
ATOM   473   C  CA  . ALA   A 1 74  ? 35.445  13.152  -39.733 1.00 104.26 ? 143  ALA   A CA  1 
ATOM   474   C  C   . ALA   A 1 74  ? 36.481  12.953  -40.831 1.00 109.32 ? 143  ALA   A C   1 
ATOM   475   O  O   . ALA   A 1 74  ? 36.601  13.800  -41.721 1.00 112.84 ? 143  ALA   A O   1 
ATOM   476   C  CB  . ALA   A 1 74  ? 34.037  13.079  -40.330 1.00 107.19 ? 143  ALA   A CB  1 
ATOM   477   N  N   . TYR   A 1 75  ? 37.216  11.835  -40.784 1.00 109.69 ? 144  TYR   A N   1 
ATOM   478   C  CA  . TYR   A 1 75  ? 38.340  11.616  -41.702 1.00 109.83 ? 144  TYR   A CA  1 
ATOM   479   C  C   . TYR   A 1 75  ? 38.337  10.187  -42.235 1.00 109.40 ? 144  TYR   A C   1 
ATOM   480   O  O   . TYR   A 1 75  ? 38.465  9.227   -41.465 1.00 105.97 ? 144  TYR   A O   1 
ATOM   481   C  CB  . TYR   A 1 75  ? 39.688  11.928  -41.021 1.00 110.10 ? 144  TYR   A CB  1 
ATOM   482   C  CG  . TYR   A 1 75  ? 40.903  11.790  -41.932 1.00 111.96 ? 144  TYR   A CG  1 
ATOM   483   C  CD1 . TYR   A 1 75  ? 41.363  12.856  -42.682 1.00 113.85 ? 144  TYR   A CD1 1 
ATOM   484   C  CD2 . TYR   A 1 75  ? 41.573  10.585  -42.059 1.00 110.97 ? 144  TYR   A CD2 1 
ATOM   485   C  CE1 . TYR   A 1 75  ? 42.455  12.720  -43.534 1.00 114.42 ? 144  TYR   A CE1 1 
ATOM   486   C  CE2 . TYR   A 1 75  ? 42.673  10.458  -42.895 1.00 115.98 ? 144  TYR   A CE2 1 
ATOM   487   C  CZ  . TYR   A 1 75  ? 43.110  11.526  -43.623 1.00 113.44 ? 144  TYR   A CZ  1 
ATOM   488   O  OH  . TYR   A 1 75  ? 44.194  11.391  -44.455 1.00 107.85 ? 144  TYR   A OH  1 
ATOM   489   N  N   . ARG   A 1 76  ? 38.301  10.065  -43.562 1.00 110.86 ? 145  ARG   A N   1 
ATOM   490   C  CA  . ARG   A 1 76  ? 38.089  8.795   -44.250 1.00 114.77 ? 145  ARG   A CA  1 
ATOM   491   C  C   . ARG   A 1 76  ? 38.871  8.818   -45.557 1.00 119.72 ? 145  ARG   A C   1 
ATOM   492   O  O   . ARG   A 1 76  ? 38.659  9.709   -46.388 1.00 122.92 ? 145  ARG   A O   1 
ATOM   493   C  CB  . ARG   A 1 76  ? 36.584  8.586   -44.512 1.00 114.93 ? 145  ARG   A CB  1 
ATOM   494   C  CG  . ARG   A 1 76  ? 36.135  7.188   -44.908 1.00 112.99 ? 145  ARG   A CG  1 
ATOM   495   C  CD  . ARG   A 1 76  ? 34.696  6.928   -44.451 1.00 115.22 ? 145  ARG   A CD  1 
ATOM   496   N  NE  . ARG   A 1 76  ? 33.663  7.420   -45.367 1.00 127.13 ? 145  ARG   A NE  1 
ATOM   497   C  CZ  . ARG   A 1 76  ? 32.723  8.318   -45.069 1.00 128.54 ? 145  ARG   A CZ  1 
ATOM   498   N  NH1 . ARG   A 1 76  ? 32.710  8.960   -43.907 1.00 123.47 ? 145  ARG   A NH1 1 
ATOM   499   N  NH2 . ARG   A 1 76  ? 31.754  8.564   -45.954 1.00 123.47 ? 145  ARG   A NH2 1 
ATOM   500   N  N   . GLU   A 1 77  ? 39.781  7.857   -45.737 1.00 123.48 ? 146  GLU   A N   1 
ATOM   501   C  CA  . GLU   A 1 77  ? 40.466  7.652   -47.013 1.00 125.97 ? 146  GLU   A CA  1 
ATOM   502   C  C   . GLU   A 1 77  ? 39.894  6.399   -47.671 1.00 134.48 ? 146  GLU   A C   1 
ATOM   503   O  O   . GLU   A 1 77  ? 40.182  5.282   -47.238 1.00 135.74 ? 146  GLU   A O   1 
ATOM   504   C  CB  . GLU   A 1 77  ? 41.973  7.501   -46.819 1.00 119.17 ? 146  GLU   A CB  1 
ATOM   505   C  CG  . GLU   A 1 77  ? 42.593  8.467   -45.829 1.00 118.93 ? 146  GLU   A CG  1 
ATOM   506   C  CD  . GLU   A 1 77  ? 44.119  8.411   -45.828 1.00 116.58 ? 146  GLU   A CD  1 
ATOM   507   O  OE1 . GLU   A 1 77  ? 44.746  8.993   -46.744 1.00 111.09 ? 146  GLU   A OE1 1 
ATOM   508   O  OE2 . GLU   A 1 77  ? 44.692  7.769   -44.918 1.00 119.48 ? 146  GLU   A OE2 1 
ATOM   509   N  N   . GLU   A 1 78  ? 39.104  6.577   -48.727 1.00 138.33 ? 147  GLU   A N   1 
ATOM   510   C  CA  . GLU   A 1 78  ? 38.511  5.454   -49.450 1.00 145.94 ? 147  GLU   A CA  1 
ATOM   511   C  C   . GLU   A 1 78  ? 39.060  5.469   -50.876 1.00 155.59 ? 147  GLU   A C   1 
ATOM   512   O  O   . GLU   A 1 78  ? 38.490  6.119   -51.755 1.00 160.42 ? 147  GLU   A O   1 
ATOM   513   C  CB  . GLU   A 1 78  ? 36.968  5.529   -49.420 1.00 141.78 ? 147  GLU   A CB  1 
ATOM   514   N  N   . GLN   A 1 79  ? 40.172  4.759   -51.097 1.00 160.91 ? 148  GLN   A N   1 
ATOM   515   C  CA  . GLN   A 1 79  ? 40.752  4.597   -52.427 1.00 166.56 ? 148  GLN   A CA  1 
ATOM   516   C  C   . GLN   A 1 79  ? 39.711  4.041   -53.387 1.00 176.03 ? 148  GLN   A C   1 
ATOM   517   O  O   . GLN   A 1 79  ? 39.279  2.892   -53.252 1.00 174.02 ? 148  GLN   A O   1 
ATOM   518   C  CB  . GLN   A 1 79  ? 41.974  3.680   -52.378 1.00 160.01 ? 148  GLN   A CB  1 
ATOM   519   N  N   . ASP   A 1 80  ? 39.277  4.873   -54.335 1.00 184.27 ? 149  ASP   A N   1 
ATOM   520   C  CA  . ASP   A 1 80  ? 38.250  4.499   -55.294 1.00 185.45 ? 149  ASP   A CA  1 
ATOM   521   C  C   . ASP   A 1 80  ? 38.586  5.147   -56.624 1.00 188.32 ? 149  ASP   A C   1 
ATOM   522   O  O   . ASP   A 1 80  ? 39.091  6.272   -56.664 1.00 184.71 ? 149  ASP   A O   1 
ATOM   523   C  CB  . ASP   A 1 80  ? 36.849  4.929   -54.839 1.00 184.88 ? 149  ASP   A CB  1 
ATOM   524   N  N   . PHE   A 1 81  ? 38.285  4.437   -57.709 1.00 196.35 ? 150  PHE   A N   1 
ATOM   525   C  CA  . PHE   A 1 81  ? 38.629  4.886   -59.056 1.00 197.32 ? 150  PHE   A CA  1 
ATOM   526   C  C   . PHE   A 1 81  ? 40.136  5.076   -59.210 1.00 196.91 ? 150  PHE   A C   1 
ATOM   527   O  O   . PHE   A 1 81  ? 40.593  5.995   -59.891 1.00 196.32 ? 150  PHE   A O   1 
ATOM   528   C  CB  . PHE   A 1 81  ? 37.893  6.177   -59.433 1.00 198.52 ? 150  PHE   A CB  1 
ATOM   529   C  CG  . PHE   A 1 81  ? 36.504  6.290   -58.857 1.00 200.00 ? 150  PHE   A CG  1 
ATOM   530   C  CD1 . PHE   A 1 81  ? 35.513  5.372   -59.184 1.00 198.86 ? 150  PHE   A CD1 1 
ATOM   531   C  CD2 . PHE   A 1 81  ? 36.185  7.336   -58.002 1.00 199.98 ? 150  PHE   A CD2 1 
ATOM   532   C  CE1 . PHE   A 1 81  ? 34.240  5.493   -58.656 1.00 197.83 ? 150  PHE   A CE1 1 
ATOM   533   C  CE2 . PHE   A 1 81  ? 34.916  7.459   -57.475 1.00 199.78 ? 150  PHE   A CE2 1 
ATOM   534   C  CZ  . PHE   A 1 81  ? 33.944  6.537   -57.802 1.00 199.18 ? 150  PHE   A CZ  1 
ATOM   535   N  N   . GLY   A 1 82  ? 40.911  4.217   -58.547 1.00 189.42 ? 151  GLY   A N   1 
ATOM   536   C  CA  . GLY   A 1 82  ? 42.345  4.158   -58.773 1.00 182.16 ? 151  GLY   A CA  1 
ATOM   537   C  C   . GLY   A 1 82  ? 43.114  5.393   -58.375 1.00 180.64 ? 151  GLY   A C   1 
ATOM   538   O  O   . GLY   A 1 82  ? 44.230  5.600   -58.852 1.00 172.43 ? 151  GLY   A O   1 
ATOM   539   N  N   . ILE   A 1 83  ? 42.544  6.230   -57.517 1.00 179.63 ? 152  ILE   A N   1 
ATOM   540   C  CA  . ILE   A 1 83  ? 43.216  7.413   -57.004 1.00 176.73 ? 152  ILE   A CA  1 
ATOM   541   C  C   . ILE   A 1 83  ? 42.966  7.478   -55.503 1.00 173.68 ? 152  ILE   A C   1 
ATOM   542   O  O   . ILE   A 1 83  ? 41.919  7.047   -55.008 1.00 172.41 ? 152  ILE   A O   1 
ATOM   543   C  CB  . ILE   A 1 83  ? 42.729  8.695   -57.720 1.00 175.50 ? 152  ILE   A CB  1 
ATOM   544   C  CG1 . ILE   A 1 83  ? 43.273  9.956   -57.039 1.00 173.78 ? 152  ILE   A CG1 1 
ATOM   545   C  CG2 . ILE   A 1 83  ? 41.203  8.718   -57.794 1.00 177.30 ? 152  ILE   A CG2 1 
ATOM   546   C  CD1 . ILE   A 1 83  ? 44.777  10.090  -57.117 1.00 174.41 ? 152  ILE   A CD1 1 
ATOM   547   N  N   . GLU   A 1 84  ? 43.951  7.992   -54.769 1.00 169.34 ? 153  GLU   A N   1 
ATOM   548   C  CA  . GLU   A 1 84  ? 43.857  8.086   -53.314 1.00 170.03 ? 153  GLU   A CA  1 
ATOM   549   C  C   . GLU   A 1 84  ? 42.955  9.266   -52.946 1.00 168.52 ? 153  GLU   A C   1 
ATOM   550   O  O   . GLU   A 1 84  ? 43.409  10.368  -52.630 1.00 167.54 ? 153  GLU   A O   1 
ATOM   551   C  CB  . GLU   A 1 84  ? 45.245  8.220   -52.698 1.00 169.84 ? 153  GLU   A CB  1 
ATOM   552   N  N   . ILE   A 1 85  ? 41.642  9.025   -52.985 1.00 164.21 ? 154  ILE   A N   1 
ATOM   553   C  CA  . ILE   A 1 85  ? 40.674  10.026  -52.535 1.00 151.36 ? 154  ILE   A CA  1 
ATOM   554   C  C   . ILE   A 1 85  ? 40.636  10.018  -51.013 1.00 146.72 ? 154  ILE   A C   1 
ATOM   555   O  O   . ILE   A 1 85  ? 40.463  8.963   -50.389 1.00 146.76 ? 154  ILE   A O   1 
ATOM   556   C  CB  . ILE   A 1 85  ? 39.275  9.751   -53.115 1.00 153.53 ? 154  ILE   A CB  1 
ATOM   557   C  CG1 . ILE   A 1 85  ? 39.314  9.572   -54.638 1.00 165.09 ? 154  ILE   A CG1 1 
ATOM   558   C  CG2 . ILE   A 1 85  ? 38.321  10.876  -52.727 1.00 149.51 ? 154  ILE   A CG2 1 
ATOM   559   C  CD1 . ILE   A 1 85  ? 38.002  9.040   -55.253 1.00 169.13 ? 154  ILE   A CD1 1 
ATOM   560   N  N   . VAL   A 1 86  ? 40.800  11.192  -50.404 1.00 146.02 ? 155  VAL   A N   1 
ATOM   561   C  CA  . VAL   A 1 86  ? 40.529  11.386  -48.984 1.00 134.82 ? 155  VAL   A CA  1 
ATOM   562   C  C   . VAL   A 1 86  ? 39.219  12.150  -48.863 1.00 131.29 ? 155  VAL   A C   1 
ATOM   563   O  O   . VAL   A 1 86  ? 39.022  13.164  -49.543 1.00 134.24 ? 155  VAL   A O   1 
ATOM   564   C  CB  . VAL   A 1 86  ? 41.678  12.133  -48.290 1.00 127.84 ? 155  VAL   A CB  1 
ATOM   565   C  CG1 . VAL   A 1 86  ? 41.362  12.309  -46.832 1.00 123.31 ? 155  VAL   A CG1 1 
ATOM   566   C  CG2 . VAL   A 1 86  ? 42.975  11.368  -48.464 1.00 131.43 ? 155  VAL   A CG2 1 
ATOM   567   N  N   . LYS   A 1 87  ? 38.303  11.651  -48.036 1.00 123.02 ? 156  LYS   A N   1 
ATOM   568   C  CA  . LYS   A 1 87  ? 36.993  12.270  -47.864 1.00 122.54 ? 156  LYS   A CA  1 
ATOM   569   C  C   . LYS   A 1 87  ? 36.864  12.739  -46.420 1.00 117.38 ? 156  LYS   A C   1 
ATOM   570   O  O   . LYS   A 1 87  ? 36.890  11.921  -45.498 1.00 116.87 ? 156  LYS   A O   1 
ATOM   571   C  CB  . LYS   A 1 87  ? 35.868  11.295  -48.233 1.00 119.75 ? 156  LYS   A CB  1 
ATOM   572   N  N   . VAL   A 1 88  ? 36.719  14.056  -46.223 1.00 116.20 ? 157  VAL   A N   1 
ATOM   573   C  CA  . VAL   A 1 88  ? 36.717  14.653  -44.891 1.00 113.95 ? 157  VAL   A CA  1 
ATOM   574   C  C   . VAL   A 1 88  ? 35.503  15.562  -44.700 1.00 109.78 ? 157  VAL   A C   1 
ATOM   575   O  O   . VAL   A 1 88  ? 34.843  15.979  -45.655 1.00 112.31 ? 157  VAL   A O   1 
ATOM   576   C  CB  . VAL   A 1 88  ? 38.026  15.441  -44.609 1.00 112.96 ? 157  VAL   A CB  1 
ATOM   577   C  CG1 . VAL   A 1 88  ? 39.253  14.630  -45.053 1.00 115.04 ? 157  VAL   A CG1 1 
ATOM   578   C  CG2 . VAL   A 1 88  ? 38.007  16.788  -45.275 1.00 110.55 ? 157  VAL   A CG2 1 
ATOM   579   N  N   . LYS   A 1 89  ? 35.205  15.853  -43.438 1.00 106.98 ? 158  LYS   A N   1 
ATOM   580   C  CA  . LYS   A 1 89  ? 34.101  16.718  -43.039 1.00 105.53 ? 158  LYS   A CA  1 
ATOM   581   C  C   . LYS   A 1 89  ? 34.608  17.628  -41.930 1.00 106.75 ? 158  LYS   A C   1 
ATOM   582   O  O   . LYS   A 1 89  ? 35.230  17.139  -40.982 1.00 108.08 ? 158  LYS   A O   1 
ATOM   583   C  CB  . LYS   A 1 89  ? 32.910  15.898  -42.537 1.00 106.33 ? 158  LYS   A CB  1 
ATOM   584   C  CG  . LYS   A 1 89  ? 31.946  15.440  -43.600 1.00 113.22 ? 158  LYS   A CG  1 
ATOM   585   C  CD  . LYS   A 1 89  ? 31.053  14.299  -43.079 1.00 120.15 ? 158  LYS   A CD  1 
ATOM   586   C  CE  . LYS   A 1 89  ? 31.823  12.966  -43.019 1.00 124.97 ? 158  LYS   A CE  1 
ATOM   587   N  NZ  . LYS   A 1 89  ? 30.999  11.746  -43.341 1.00 127.77 ? 158  LYS   A NZ  1 
ATOM   588   N  N   . ALA   A 1 90  ? 34.374  18.938  -42.037 1.00 103.32 ? 159  ALA   A N   1 
ATOM   589   C  CA  . ALA   A 1 90  ? 34.847  19.863  -41.016 1.00 96.35  ? 159  ALA   A CA  1 
ATOM   590   C  C   . ALA   A 1 90  ? 33.682  20.688  -40.485 1.00 98.57  ? 159  ALA   A C   1 
ATOM   591   O  O   . ALA   A 1 90  ? 32.613  20.756  -41.094 1.00 99.81  ? 159  ALA   A O   1 
ATOM   592   C  CB  . ALA   A 1 90  ? 35.959  20.780  -41.536 1.00 89.92  ? 159  ALA   A CB  1 
ATOM   593   N  N   . ILE   A 1 91  ? 33.901  21.310  -39.328 1.00 96.52  ? 160  ILE   A N   1 
ATOM   594   C  CA  . ILE   A 1 91  ? 32.943  22.241  -38.744 1.00 92.55  ? 160  ILE   A CA  1 
ATOM   595   C  C   . ILE   A 1 91  ? 33.636  23.574  -38.473 1.00 97.71  ? 160  ILE   A C   1 
ATOM   596   O  O   . ILE   A 1 91  ? 34.827  23.632  -38.143 1.00 97.63  ? 160  ILE   A O   1 
ATOM   597   C  CB  . ILE   A 1 91  ? 32.314  21.700  -37.452 1.00 86.78  ? 160  ILE   A CB  1 
ATOM   598   C  CG1 . ILE   A 1 91  ? 31.256  22.690  -36.957 1.00 87.05  ? 160  ILE   A CG1 1 
ATOM   599   C  CG2 . ILE   A 1 91  ? 33.396  21.443  -36.437 1.00 88.86  ? 160  ILE   A CG2 1 
ATOM   600   C  CD1 . ILE   A 1 91  ? 30.601  22.345  -35.676 1.00 87.86  ? 160  ILE   A CD1 1 
ATOM   601   N  N   . GLY   A 1 92  ? 32.865  24.654  -38.598 1.00 98.69  ? 161  GLY   A N   1 
ATOM   602   C  CA  . GLY   A 1 92  ? 33.417  25.990  -38.483 1.00 93.05  ? 161  GLY   A CA  1 
ATOM   603   C  C   . GLY   A 1 92  ? 33.499  26.412  -37.039 1.00 85.31  ? 161  GLY   A C   1 
ATOM   604   O  O   . GLY   A 1 92  ? 32.520  26.320  -36.294 1.00 85.01  ? 161  GLY   A O   1 
ATOM   605   N  N   . ARG   A 1 93  ? 34.670  26.886  -36.640 1.00 85.73  ? 162  ARG   A N   1 
ATOM   606   C  CA  . ARG   A 1 93  ? 34.935  27.200  -35.244 1.00 92.02  ? 162  ARG   A CA  1 
ATOM   607   C  C   . ARG   A 1 93  ? 35.027  28.705  -35.013 1.00 93.59  ? 162  ARG   A C   1 
ATOM   608   O  O   . ARG   A 1 93  ? 34.155  29.278  -34.348 1.00 94.39  ? 162  ARG   A O   1 
ATOM   609   C  CB  . ARG   A 1 93  ? 36.208  26.474  -34.806 1.00 94.17  ? 162  ARG   A CB  1 
ATOM   610   C  CG  . ARG   A 1 93  ? 36.142  24.959  -34.981 1.00 89.00  ? 162  ARG   A CG  1 
ATOM   611   C  CD  . ARG   A 1 93  ? 34.874  24.355  -34.386 1.00 86.55  ? 162  ARG   A CD  1 
ATOM   612   N  NE  . ARG   A 1 93  ? 35.147  23.045  -33.810 1.00 87.40  ? 162  ARG   A NE  1 
ATOM   613   C  CZ  . ARG   A 1 93  ? 34.267  22.313  -33.142 1.00 84.64  ? 162  ARG   A CZ  1 
ATOM   614   N  NH1 . ARG   A 1 93  ? 33.002  22.684  -33.039 1.00 81.63  ? 162  ARG   A NH1 1 
ATOM   615   N  NH2 . ARG   A 1 93  ? 34.671  21.189  -32.548 1.00 81.46  ? 162  ARG   A NH2 1 
ATOM   616   N  N   . GLN   A 1 94  ? 36.054  29.371  -35.551 1.00 92.67  ? 163  GLN   A N   1 
ATOM   617   C  CA  . GLN   A 1 94  ? 36.365  30.753  -35.208 1.00 95.98  ? 163  GLN   A CA  1 
ATOM   618   C  C   . GLN   A 1 94  ? 36.568  31.576  -36.463 1.00 97.93  ? 163  GLN   A C   1 
ATOM   619   O  O   . GLN   A 1 94  ? 37.302  31.159  -37.364 1.00 99.48  ? 163  GLN   A O   1 
ATOM   620   C  CB  . GLN   A 1 94  ? 37.625  30.829  -34.365 1.00 99.40  ? 163  GLN   A CB  1 
ATOM   621   C  CG  . GLN   A 1 94  ? 37.683  29.855  -33.222 1.00 100.49 ? 163  GLN   A CG  1 
ATOM   622   C  CD  . GLN   A 1 94  ? 39.065  29.798  -32.640 1.00 111.62 ? 163  GLN   A CD  1 
ATOM   623   O  OE1 . GLN   A 1 94  ? 39.386  30.532  -31.709 1.00 123.73 ? 163  GLN   A OE1 1 
ATOM   624   N  NE2 . GLN   A 1 94  ? 39.909  28.944  -33.206 1.00 109.84 ? 163  GLN   A NE2 1 
ATOM   625   N  N   . ARG   A 1 95  ? 35.934  32.748  -36.515 1.00 99.21  ? 164  ARG   A N   1 
ATOM   626   C  CA  . ARG   A 1 95  ? 36.160  33.664  -37.622 1.00 99.01  ? 164  ARG   A CA  1 
ATOM   627   C  C   . ARG   A 1 95  ? 37.534  34.301  -37.486 1.00 101.87 ? 164  ARG   A C   1 
ATOM   628   O  O   . ARG   A 1 95  ? 38.140  34.295  -36.412 1.00 102.56 ? 164  ARG   A O   1 
ATOM   629   C  CB  . ARG   A 1 95  ? 35.119  34.775  -37.652 1.00 97.03  ? 164  ARG   A CB  1 
ATOM   630   N  N   . PHE   A 1 96  ? 38.015  34.885  -38.583 1.00 107.75 ? 165  PHE   A N   1 
ATOM   631   C  CA  . PHE   A 1 96  ? 39.362  35.430  -38.591 1.00 107.54 ? 165  PHE   A CA  1 
ATOM   632   C  C   . PHE   A 1 96  ? 39.496  36.477  -39.693 1.00 107.95 ? 165  PHE   A C   1 
ATOM   633   O  O   . PHE   A 1 96  ? 38.761  36.463  -40.686 1.00 109.04 ? 165  PHE   A O   1 
ATOM   634   C  CB  . PHE   A 1 96  ? 40.412  34.307  -38.731 1.00 107.19 ? 165  PHE   A CB  1 
ATOM   635   C  CG  . PHE   A 1 96  ? 40.417  33.558  -40.065 1.00 106.83 ? 165  PHE   A CG  1 
ATOM   636   C  CD1 . PHE   A 1 96  ? 40.756  34.202  -41.247 1.00 107.95 ? 165  PHE   A CD1 1 
ATOM   637   C  CD2 . PHE   A 1 96  ? 40.166  32.191  -40.115 1.00 106.41 ? 165  PHE   A CD2 1 
ATOM   638   C  CE1 . PHE   A 1 96  ? 40.789  33.528  -42.447 1.00 110.99 ? 165  PHE   A CE1 1 
ATOM   639   C  CE2 . PHE   A 1 96  ? 40.206  31.499  -41.321 1.00 108.96 ? 165  PHE   A CE2 1 
ATOM   640   C  CZ  . PHE   A 1 96  ? 40.519  32.174  -42.490 1.00 112.63 ? 165  PHE   A CZ  1 
ATOM   641   N  N   . LYS   A 1 97  ? 40.458  37.384  -39.510 1.00 105.04 ? 166  LYS   A N   1 
ATOM   642   C  CA  . LYS   A 1 97  ? 40.860  38.344  -40.537 1.00 106.74 ? 166  LYS   A CA  1 
ATOM   643   C  C   . LYS   A 1 97  ? 42.276  38.026  -41.006 1.00 102.40 ? 166  LYS   A C   1 
ATOM   644   O  O   . LYS   A 1 97  ? 43.204  38.010  -40.195 1.00 101.14 ? 166  LYS   A O   1 
ATOM   645   C  CB  . LYS   A 1 97  ? 40.791  39.766  -39.982 1.00 105.92 ? 166  LYS   A CB  1 
ATOM   646   N  N   . VAL   A 1 98  ? 42.452  37.787  -42.314 1.00 103.73 ? 167  VAL   A N   1 
ATOM   647   C  CA  . VAL   A 1 98  ? 43.779  37.349  -42.769 1.00 103.67 ? 167  VAL   A CA  1 
ATOM   648   C  C   . VAL   A 1 98  ? 44.776  38.495  -42.594 1.00 102.59 ? 167  VAL   A C   1 
ATOM   649   O  O   . VAL   A 1 98  ? 44.413  39.668  -42.532 1.00 105.12 ? 167  VAL   A O   1 
ATOM   650   C  CB  . VAL   A 1 98  ? 43.767  36.853  -44.227 1.00 102.88 ? 167  VAL   A CB  1 
ATOM   651   C  CG1 . VAL   A 1 98  ? 42.612  35.923  -44.492 1.00 106.50 ? 167  VAL   A CG1 1 
ATOM   652   C  CG2 . VAL   A 1 98  ? 43.687  38.006  -45.202 1.00 110.93 ? 167  VAL   A CG2 1 
ATOM   653   N  N   . LEU   A 1 99  ? 46.057  38.142  -42.549 1.00 101.10 ? 168  LEU   A N   1 
ATOM   654   C  CA  . LEU   A 1 99  ? 47.133  39.112  -42.458 1.00 101.87 ? 168  LEU   A CA  1 
ATOM   655   C  C   . LEU   A 1 99  ? 48.125  38.990  -43.605 1.00 104.14 ? 168  LEU   A C   1 
ATOM   656   O  O   . LEU   A 1 99  ? 48.529  40.008  -44.187 1.00 109.76 ? 168  LEU   A O   1 
ATOM   657   C  CB  . LEU   A 1 99  ? 47.867  38.940  -41.120 1.00 98.73  ? 168  LEU   A CB  1 
ATOM   658   C  CG  . LEU   A 1 99  ? 47.003  38.985  -39.873 1.00 93.73  ? 168  LEU   A CG  1 
ATOM   659   C  CD1 . LEU   A 1 99  ? 47.860  38.679  -38.673 1.00 96.06  ? 168  LEU   A CD1 1 
ATOM   660   C  CD2 . LEU   A 1 99  ? 46.381  40.342  -39.763 1.00 94.18  ? 168  LEU   A CD2 1 
ATOM   661   N  N   . GLU   A 1 100 ? 48.568  37.775  -43.919 1.00 100.17 ? 169  GLU   A N   1 
ATOM   662   C  CA  . GLU   A 1 100 ? 49.538  37.492  -44.967 1.00 101.78 ? 169  GLU   A CA  1 
ATOM   663   C  C   . GLU   A 1 100 ? 49.210  36.141  -45.587 1.00 114.39 ? 169  GLU   A C   1 
ATOM   664   O  O   . GLU   A 1 100 ? 49.097  35.144  -44.870 1.00 119.27 ? 169  GLU   A O   1 
ATOM   665   C  CB  . GLU   A 1 100 ? 50.967  37.450  -44.421 1.00 107.06 ? 169  GLU   A CB  1 
ATOM   666   C  CG  . GLU   A 1 100 ? 51.323  38.575  -43.523 1.00 110.84 ? 169  GLU   A CG  1 
ATOM   667   C  CD  . GLU   A 1 100 ? 52.760  38.498  -43.011 1.00 121.13 ? 169  GLU   A CD  1 
ATOM   668   O  OE1 . GLU   A 1 100 ? 53.486  37.509  -43.301 1.00 118.85 ? 169  GLU   A OE1 1 
ATOM   669   O  OE2 . GLU   A 1 100 ? 53.175  39.464  -42.330 1.00 129.95 ? 169  GLU   A OE2 1 
ATOM   670   N  N   . LEU   A 1 101 ? 49.085  36.097  -46.911 1.00 121.34 ? 170  LEU   A N   1 
ATOM   671   C  CA  . LEU   A 1 101 ? 48.904  34.845  -47.646 1.00 124.04 ? 170  LEU   A CA  1 
ATOM   672   C  C   . LEU   A 1 101 ? 50.203  34.485  -48.358 1.00 130.74 ? 170  LEU   A C   1 
ATOM   673   O  O   . LEU   A 1 101 ? 50.658  35.208  -49.252 1.00 132.36 ? 170  LEU   A O   1 
ATOM   674   C  CB  . LEU   A 1 101 ? 47.766  34.954  -48.652 1.00 118.29 ? 170  LEU   A CB  1 
ATOM   675   C  CG  . LEU   A 1 101 ? 46.357  34.776  -48.143 1.00 115.62 ? 170  LEU   A CG  1 
ATOM   676   C  CD1 . LEU   A 1 101 ? 45.415  34.849  -49.318 1.00 105.02 ? 170  LEU   A CD1 1 
ATOM   677   C  CD2 . LEU   A 1 101 ? 46.327  33.410  -47.515 1.00 125.67 ? 170  LEU   A CD2 1 
ATOM   678   N  N   . ARG   A 1 102 ? 50.791  33.360  -47.970 1.00 137.77 ? 171  ARG   A N   1 
ATOM   679   C  CA  . ARG   A 1 102 ? 52.005  32.847  -48.584 1.00 139.52 ? 171  ARG   A CA  1 
ATOM   680   C  C   . ARG   A 1 102 ? 51.664  31.576  -49.342 1.00 146.28 ? 171  ARG   A C   1 
ATOM   681   O  O   . ARG   A 1 102 ? 51.223  30.596  -48.732 1.00 151.23 ? 171  ARG   A O   1 
ATOM   682   C  CB  . ARG   A 1 102 ? 53.075  32.570  -47.531 1.00 139.13 ? 171  ARG   A CB  1 
ATOM   683   C  CG  . ARG   A 1 102 ? 52.553  32.246  -46.143 1.00 139.98 ? 171  ARG   A CG  1 
ATOM   684   C  CD  . ARG   A 1 102 ? 53.709  32.451  -45.204 1.00 141.62 ? 171  ARG   A CD  1 
ATOM   685   N  NE  . ARG   A 1 102 ? 53.508  32.080  -43.808 1.00 148.67 ? 171  ARG   A NE  1 
ATOM   686   C  CZ  . ARG   A 1 102 ? 53.362  32.956  -42.821 1.00 140.90 ? 171  ARG   A CZ  1 
ATOM   687   N  NH1 . ARG   A 1 102 ? 53.298  34.256  -43.059 1.00 135.68 ? 171  ARG   A NH1 1 
ATOM   688   N  NH2 . ARG   A 1 102 ? 53.277  32.517  -41.567 1.00 137.11 ? 171  ARG   A NH2 1 
ATOM   689   N  N   . THR   A 1 103 ? 51.863  31.593  -50.663 1.00 149.95 ? 172  THR   A N   1 
ATOM   690   C  CA  . THR   A 1 103 ? 51.534  30.455  -51.518 1.00 153.13 ? 172  THR   A CA  1 
ATOM   691   C  C   . THR   A 1 103 ? 52.752  29.537  -51.619 1.00 158.22 ? 172  THR   A C   1 
ATOM   692   O  O   . THR   A 1 103 ? 53.804  29.951  -52.107 1.00 160.48 ? 172  THR   A O   1 
ATOM   693   C  CB  . THR   A 1 103 ? 51.075  30.927  -52.904 1.00 150.38 ? 172  THR   A CB  1 
ATOM   694   O  OG1 . THR   A 1 103 ? 49.969  31.837  -52.773 1.00 142.62 ? 172  THR   A OG1 1 
ATOM   695   C  CG2 . THR   A 1 103 ? 50.625  29.737  -53.753 1.00 151.65 ? 172  THR   A CG2 1 
ATOM   696   N  N   . GLN   A 1 104 ? 52.618  28.296  -51.136 1.00 173.12 ? 173  GLN   A N   1 
ATOM   697   C  CA  . GLN   A 1 104 ? 53.753  27.375  -51.112 1.00 174.59 ? 173  GLN   A CA  1 
ATOM   698   C  C   . GLN   A 1 104 ? 54.065  26.869  -52.516 1.00 180.61 ? 173  GLN   A C   1 
ATOM   699   O  O   . GLN   A 1 104 ? 53.354  27.154  -53.484 1.00 182.56 ? 173  GLN   A O   1 
ATOM   700   C  CB  . GLN   A 1 104 ? 53.474  26.179  -50.202 1.00 174.72 ? 173  GLN   A CB  1 
ATOM   701   C  CG  . GLN   A 1 104 ? 53.567  26.492  -48.727 1.00 174.65 ? 173  GLN   A CG  1 
ATOM   702   C  CD  . GLN   A 1 104 ? 53.258  25.286  -47.867 1.00 176.49 ? 173  GLN   A CD  1 
ATOM   703   O  OE1 . GLN   A 1 104 ? 52.514  24.390  -48.282 1.00 176.03 ? 173  GLN   A OE1 1 
ATOM   704   N  NE2 . GLN   A 1 104 ? 53.834  25.248  -46.663 1.00 174.03 ? 173  GLN   A NE2 1 
ATOM   705   N  N   . SER   A 1 105 ? 55.151  26.092  -52.622 1.00 171.60 ? 174  SER   A N   1 
ATOM   706   C  CA  . SER   A 1 105 ? 55.503  25.509  -53.912 1.00 165.96 ? 174  SER   A CA  1 
ATOM   707   C  C   . SER   A 1 105 ? 54.462  24.482  -54.353 1.00 164.55 ? 174  SER   A C   1 
ATOM   708   O  O   . SER   A 1 105 ? 54.143  24.383  -55.543 1.00 162.94 ? 174  SER   A O   1 
ATOM   709   C  CB  . SER   A 1 105 ? 56.904  24.895  -53.856 1.00 161.37 ? 174  SER   A CB  1 
ATOM   710   O  OG  . SER   A 1 105 ? 57.060  24.060  -52.724 1.00 167.68 ? 174  SER   A OG  1 
ATOM   711   N  N   . ASP   A 1 106 ? 53.885  23.742  -53.397 1.00 163.92 ? 175  ASP   A N   1 
ATOM   712   C  CA  . ASP   A 1 106 ? 52.854  22.752  -53.703 1.00 162.29 ? 175  ASP   A CA  1 
ATOM   713   C  C   . ASP   A 1 106 ? 51.566  23.382  -54.233 1.00 159.61 ? 175  ASP   A C   1 
ATOM   714   O  O   . ASP   A 1 106 ? 50.770  22.686  -54.880 1.00 153.26 ? 175  ASP   A O   1 
ATOM   715   C  CB  . ASP   A 1 106 ? 52.551  21.922  -52.449 1.00 157.17 ? 175  ASP   A CB  1 
ATOM   716   N  N   . GLY   A 1 107 ? 51.350  24.678  -53.974 1.00 158.02 ? 176  GLY   A N   1 
ATOM   717   C  CA  . GLY   A 1 107 ? 50.103  25.360  -54.233 1.00 155.57 ? 176  GLY   A CA  1 
ATOM   718   C  C   . GLY   A 1 107 ? 49.253  25.586  -52.991 1.00 157.39 ? 176  GLY   A C   1 
ATOM   719   O  O   . GLY   A 1 107 ? 48.450  26.527  -52.960 1.00 155.17 ? 176  GLY   A O   1 
ATOM   720   N  N   . ILE   A 1 108 ? 49.410  24.732  -51.971 1.00 160.79 ? 177  ILE   A N   1 
ATOM   721   C  CA  . ILE   A 1 108 ? 48.708  24.891  -50.700 1.00 154.23 ? 177  ILE   A CA  1 
ATOM   722   C  C   . ILE   A 1 108 ? 49.122  26.217  -50.072 1.00 152.49 ? 177  ILE   A C   1 
ATOM   723   O  O   . ILE   A 1 108 ? 50.303  26.434  -49.772 1.00 153.81 ? 177  ILE   A O   1 
ATOM   724   C  CB  . ILE   A 1 108 ? 49.017  23.715  -49.760 1.00 151.00 ? 177  ILE   A CB  1 
ATOM   725   C  CG1 . ILE   A 1 108 ? 49.170  22.407  -50.533 1.00 148.40 ? 177  ILE   A CG1 1 
ATOM   726   C  CG2 . ILE   A 1 108 ? 47.929  23.557  -48.722 1.00 148.25 ? 177  ILE   A CG2 1 
ATOM   727   C  CD1 . ILE   A 1 108 ? 49.854  21.309  -49.727 1.00 145.48 ? 177  ILE   A CD1 1 
ATOM   728   N  N   . GLN   A 1 109 ? 48.151  27.107  -49.857 1.00 147.30 ? 178  GLN   A N   1 
ATOM   729   C  CA  . GLN   A 1 109 ? 48.427  28.440  -49.335 1.00 145.61 ? 178  GLN   A CA  1 
ATOM   730   C  C   . GLN   A 1 109 ? 48.306  28.474  -47.815 1.00 147.24 ? 178  GLN   A C   1 
ATOM   731   O  O   . GLN   A 1 109 ? 47.337  27.951  -47.254 1.00 144.39 ? 178  GLN   A O   1 
ATOM   732   C  CB  . GLN   A 1 109 ? 47.481  29.463  -49.965 1.00 142.38 ? 178  GLN   A CB  1 
ATOM   733   C  CG  . GLN   A 1 109 ? 47.941  29.921  -51.339 1.00 144.35 ? 178  GLN   A CG  1 
ATOM   734   C  CD  . GLN   A 1 109 ? 46.969  30.860  -52.019 1.00 138.06 ? 178  GLN   A CD  1 
ATOM   735   O  OE1 . GLN   A 1 109 ? 45.828  31.032  -51.563 1.00 128.11 ? 178  GLN   A OE1 1 
ATOM   736   N  NE2 . GLN   A 1 109 ? 47.411  31.471  -53.129 1.00 133.46 ? 178  GLN   A NE2 1 
ATOM   737   N  N   . GLN   A 1 110 ? 49.295  29.091  -47.153 1.00 155.49 ? 179  GLN   A N   1 
ATOM   738   C  CA  . GLN   A 1 110 ? 49.314  29.295  -45.707 1.00 151.60 ? 179  GLN   A CA  1 
ATOM   739   C  C   . GLN   A 1 110 ? 48.952  30.739  -45.385 1.00 149.95 ? 179  GLN   A C   1 
ATOM   740   O  O   . GLN   A 1 110 ? 49.217  31.650  -46.173 1.00 152.55 ? 179  GLN   A O   1 
ATOM   741   C  CB  . GLN   A 1 110 ? 50.688  28.979  -45.116 1.00 152.30 ? 179  GLN   A CB  1 
ATOM   742   C  CG  . GLN   A 1 110 ? 51.383  27.792  -45.755 1.00 158.79 ? 179  GLN   A CG  1 
ATOM   743   C  CD  . GLN   A 1 110 ? 50.783  26.457  -45.334 1.00 160.00 ? 179  GLN   A CD  1 
ATOM   744   O  OE1 . GLN   A 1 110 ? 50.639  25.542  -46.152 1.00 160.54 ? 179  GLN   A OE1 1 
ATOM   745   N  NE2 . GLN   A 1 110 ? 50.425  26.340  -44.055 1.00 163.66 ? 179  GLN   A NE2 1 
ATOM   746   N  N   . ALA   A 1 111 ? 48.369  30.954  -44.205 1.00 130.77 ? 180  ALA   A N   1 
ATOM   747   C  CA  . ALA   A 1 111 ? 47.755  32.244  -43.902 1.00 119.21 ? 180  ALA   A CA  1 
ATOM   748   C  C   . ALA   A 1 111 ? 48.045  32.682  -42.475 1.00 110.40 ? 180  ALA   A C   1 
ATOM   749   O  O   . ALA   A 1 111 ? 47.604  32.038  -41.519 1.00 109.98 ? 180  ALA   A O   1 
ATOM   750   C  CB  . ALA   A 1 111 ? 46.245  32.184  -44.137 1.00 112.45 ? 180  ALA   A CB  1 
ATOM   751   N  N   . LYS   A 1 112 ? 48.768  33.788  -42.335 1.00 107.55 ? 181  LYS   A N   1 
ATOM   752   C  CA  . LYS   A 1 112 ? 48.810  34.489  -41.061 1.00 100.80 ? 181  LYS   A CA  1 
ATOM   753   C  C   . LYS   A 1 112 ? 47.445  35.096  -40.796 1.00 102.55 ? 181  LYS   A C   1 
ATOM   754   O  O   . LYS   A 1 112 ? 46.868  35.772  -41.651 1.00 104.11 ? 181  LYS   A O   1 
ATOM   755   C  CB  . LYS   A 1 112 ? 49.881  35.576  -41.072 1.00 103.72 ? 181  LYS   A CB  1 
ATOM   756   C  CG  . LYS   A 1 112 ? 50.260  36.122  -39.697 1.00 104.23 ? 181  LYS   A CG  1 
ATOM   757   C  CD  . LYS   A 1 112 ? 51.686  36.666  -39.706 1.00 107.19 ? 181  LYS   A CD  1 
ATOM   758   C  CE  . LYS   A 1 112 ? 52.309  36.636  -38.316 1.00 105.87 ? 181  LYS   A CE  1 
ATOM   759   N  NZ  . LYS   A 1 112 ? 51.640  37.565  -37.369 1.00 103.52 ? 181  LYS   A NZ  1 
ATOM   760   N  N   . VAL   A 1 113 ? 46.935  34.885  -39.594 1.00 104.91 ? 182  VAL   A N   1 
ATOM   761   C  CA  . VAL   A 1 113 ? 45.509  35.014  -39.337 1.00 99.49  ? 182  VAL   A CA  1 
ATOM   762   C  C   . VAL   A 1 113 ? 45.298  35.681  -37.980 1.00 99.26  ? 182  VAL   A C   1 
ATOM   763   O  O   . VAL   A 1 113 ? 45.917  35.283  -36.992 1.00 105.59 ? 182  VAL   A O   1 
ATOM   764   C  CB  . VAL   A 1 113 ? 44.848  33.624  -39.375 1.00 98.96  ? 182  VAL   A CB  1 
ATOM   765   C  CG1 . VAL   A 1 113 ? 43.562  33.646  -38.619 1.00 101.92 ? 182  VAL   A CG1 1 
ATOM   766   C  CG2 . VAL   A 1 113 ? 44.611  33.176  -40.793 1.00 100.18 ? 182  VAL   A CG2 1 
ATOM   767   N  N   . GLN   A 1 114 ? 44.433  36.686  -37.911 1.00 97.76  ? 183  GLN   A N   1 
ATOM   768   C  CA  . GLN   A 1 114 ? 44.083  37.291  -36.627 1.00 101.12 ? 183  GLN   A CA  1 
ATOM   769   C  C   . GLN   A 1 114 ? 42.699  36.811  -36.212 1.00 107.97 ? 183  GLN   A C   1 
ATOM   770   O  O   . GLN   A 1 114 ? 41.718  37.018  -36.941 1.00 106.99 ? 183  GLN   A O   1 
ATOM   771   C  CB  . GLN   A 1 114 ? 44.126  38.818  -36.685 1.00 104.24 ? 183  GLN   A CB  1 
ATOM   772   C  CG  . GLN   A 1 114 ? 43.593  39.527  -35.431 1.00 108.87 ? 183  GLN   A CG  1 
ATOM   773   C  CD  . GLN   A 1 114 ? 44.684  39.907  -34.440 1.00 111.86 ? 183  GLN   A CD  1 
ATOM   774   O  OE1 . GLN   A 1 114 ? 45.841  40.074  -34.813 1.00 110.04 ? 183  GLN   A OE1 1 
ATOM   775   N  NE2 . GLN   A 1 114 ? 44.316  40.031  -33.167 1.00 115.64 ? 183  GLN   A NE2 1 
ATOM   776   N  N   . ILE   A 1 115 ? 42.622  36.169  -35.045 1.00 115.64 ? 184  ILE   A N   1 
ATOM   777   C  CA  . ILE   A 1 115 ? 41.357  35.602  -34.583 1.00 118.41 ? 184  ILE   A CA  1 
ATOM   778   C  C   . ILE   A 1 115 ? 40.407  36.738  -34.221 1.00 115.77 ? 184  ILE   A C   1 
ATOM   779   O  O   . ILE   A 1 115 ? 40.692  37.542  -33.330 1.00 120.92 ? 184  ILE   A O   1 
ATOM   780   C  CB  . ILE   A 1 115 ? 41.575  34.651  -33.397 1.00 120.66 ? 184  ILE   A CB  1 
ATOM   781   C  CG1 . ILE   A 1 115 ? 42.424  33.468  -33.831 1.00 118.04 ? 184  ILE   A CG1 1 
ATOM   782   C  CG2 . ILE   A 1 115 ? 40.251  34.127  -32.895 1.00 122.02 ? 184  ILE   A CG2 1 
ATOM   783   C  CD1 . ILE   A 1 115 ? 41.863  32.751  -35.009 1.00 111.54 ? 184  ILE   A CD1 1 
ATOM   784   N  N   . LEU   A 1 116 ? 39.280  36.814  -34.916 1.00 112.03 ? 185  LEU   A N   1 
ATOM   785   C  CA  . LEU   A 1 116 ? 38.271  37.818  -34.636 1.00 110.01 ? 185  LEU   A CA  1 
ATOM   786   C  C   . LEU   A 1 116 ? 37.727  37.643  -33.220 1.00 121.50 ? 185  LEU   A C   1 
ATOM   787   O  O   . LEU   A 1 116 ? 37.995  36.624  -32.566 1.00 122.70 ? 185  LEU   A O   1 
ATOM   788   C  CB  . LEU   A 1 116 ? 37.168  37.724  -35.687 1.00 108.25 ? 185  LEU   A CB  1 
ATOM   789   C  CG  . LEU   A 1 116 ? 37.652  38.219  -37.047 1.00 108.43 ? 185  LEU   A CG  1 
ATOM   790   C  CD1 . LEU   A 1 116 ? 36.474  38.563  -37.944 1.00 100.52 ? 185  LEU   A CD1 1 
ATOM   791   C  CD2 . LEU   A 1 116 ? 38.611  39.407  -36.907 1.00 111.82 ? 185  LEU   A CD2 1 
ATOM   792   N  N   . PRO   A 1 117 ? 36.969  38.620  -32.693 1.00 126.92 ? 186  PRO   A N   1 
ATOM   793   C  CA  . PRO   A 1 117 ? 36.516  38.540  -31.293 1.00 129.20 ? 186  PRO   A CA  1 
ATOM   794   C  C   . PRO   A 1 117 ? 35.142  37.911  -31.105 1.00 123.81 ? 186  PRO   A C   1 
ATOM   795   O  O   . PRO   A 1 117 ? 34.258  38.006  -31.963 1.00 120.54 ? 186  PRO   A O   1 
ATOM   796   C  CB  . PRO   A 1 117 ? 36.479  40.014  -30.874 1.00 130.43 ? 186  PRO   A CB  1 
ATOM   797   C  CG  . PRO   A 1 117 ? 36.086  40.731  -32.125 1.00 125.45 ? 186  PRO   A CG  1 
ATOM   798   C  CD  . PRO   A 1 117 ? 36.774  39.972  -33.249 1.00 123.61 ? 186  PRO   A CD  1 
ATOM   799   N  N   . GLU   A 1 118 ? 34.973  37.264  -29.941 1.00 116.20 ? 187  GLU   A N   1 
ATOM   800   C  CA  . GLU   A 1 118 ? 33.670  36.798  -29.447 1.00 108.48 ? 187  GLU   A CA  1 
ATOM   801   C  C   . GLU   A 1 118 ? 33.525  37.374  -28.043 1.00 105.29 ? 187  GLU   A C   1 
ATOM   802   O  O   . GLU   A 1 118 ? 33.920  36.734  -27.067 1.00 106.33 ? 187  GLU   A O   1 
ATOM   803   C  CB  . GLU   A 1 118 ? 33.554  35.275  -29.455 1.00 103.72 ? 187  GLU   A CB  1 
ATOM   804   C  CG  . GLU   A 1 118 ? 33.544  34.653  -30.858 1.00 104.08 ? 187  GLU   A CG  1 
ATOM   805   C  CD  . GLU   A 1 118 ? 33.501  33.110  -30.843 1.00 101.90 ? 187  GLU   A CD  1 
ATOM   806   O  OE1 . GLU   A 1 118 ? 33.669  32.510  -29.752 1.00 95.88  ? 187  GLU   A OE1 1 
ATOM   807   O  OE2 . GLU   A 1 118 ? 33.298  32.489  -31.923 1.00 99.96  ? 187  GLU   A OE2 1 
ATOM   808   N  N   . CYS   A 1 119 ? 32.976  38.586  -27.957 1.00 100.95 ? 188  CYS   A N   1 
ATOM   809   C  CA  . CYS   A 1 119 ? 32.908  39.330  -26.703 1.00 97.64  ? 188  CYS   A CA  1 
ATOM   810   C  C   . CYS   A 1 119 ? 31.842  38.747  -25.795 1.00 97.64  ? 188  CYS   A C   1 
ATOM   811   O  O   . CYS   A 1 119 ? 30.645  38.911  -26.047 1.00 100.78 ? 188  CYS   A O   1 
ATOM   812   C  CB  . CYS   A 1 119 ? 32.598  40.793  -26.973 1.00 98.34  ? 188  CYS   A CB  1 
ATOM   813   S  SG  . CYS   A 1 119 ? 33.904  41.672  -27.786 1.00 108.20 ? 188  CYS   A SG  1 
ATOM   814   N  N   . VAL   A 1 120 ? 32.275  38.105  -24.722 1.00 90.07  ? 189  VAL   A N   1 
ATOM   815   C  CA  . VAL   A 1 120 ? 31.357  37.648  -23.693 1.00 85.97  ? 189  VAL   A CA  1 
ATOM   816   C  C   . VAL   A 1 120 ? 31.124  38.795  -22.740 1.00 88.32  ? 189  VAL   A C   1 
ATOM   817   O  O   . VAL   A 1 120 ? 32.081  39.405  -22.243 1.00 92.57  ? 189  VAL   A O   1 
ATOM   818   C  CB  . VAL   A 1 120 ? 31.928  36.440  -22.958 1.00 87.21  ? 189  VAL   A CB  1 
ATOM   819   C  CG1 . VAL   A 1 120 ? 30.846  35.764  -22.181 1.00 90.00  ? 189  VAL   A CG1 1 
ATOM   820   C  CG2 . VAL   A 1 120 ? 32.559  35.500  -23.950 1.00 96.21  ? 189  VAL   A CG2 1 
ATOM   821   N  N   . LEU   A 1 121 ? 29.855  39.109  -22.485 1.00 87.24  ? 190  LEU   A N   1 
ATOM   822   C  CA  . LEU   A 1 121 ? 29.540  40.267  -21.666 1.00 86.84  ? 190  LEU   A CA  1 
ATOM   823   C  C   . LEU   A 1 121 ? 28.610  39.896  -20.525 1.00 85.46  ? 190  LEU   A C   1 
ATOM   824   O  O   . LEU   A 1 121 ? 27.676  39.104  -20.709 1.00 84.89  ? 190  LEU   A O   1 
ATOM   825   C  CB  . LEU   A 1 121 ? 28.901  41.382  -22.499 1.00 86.07  ? 190  LEU   A CB  1 
ATOM   826   C  CG  . LEU   A 1 121 ? 29.908  42.441  -22.915 1.00 82.60  ? 190  LEU   A CG  1 
ATOM   827   C  CD1 . LEU   A 1 121 ? 30.784  41.934  -24.038 1.00 91.21  ? 190  LEU   A CD1 1 
ATOM   828   C  CD2 . LEU   A 1 121 ? 29.188  43.675  -23.314 1.00 80.74  ? 190  LEU   A CD2 1 
ATOM   829   N  N   . PRO   A 1 122 ? 28.831  40.479  -19.348 1.00 86.13  ? 191  PRO   A N   1 
ATOM   830   C  CA  . PRO   A 1 122 ? 27.990  40.187  -18.181 1.00 86.86  ? 191  PRO   A CA  1 
ATOM   831   C  C   . PRO   A 1 122 ? 26.607  40.798  -18.305 1.00 92.06  ? 191  PRO   A C   1 
ATOM   832   O  O   . PRO   A 1 122 ? 26.345  41.546  -19.234 1.00 94.95  ? 191  PRO   A O   1 
ATOM   833   C  CB  . PRO   A 1 122 ? 28.762  40.840  -17.037 1.00 96.10  ? 191  PRO   A CB  1 
ATOM   834   C  CG  . PRO   A 1 122 ? 29.451  41.977  -17.687 1.00 100.03 ? 191  PRO   A CG  1 
ATOM   835   C  CD  . PRO   A 1 122 ? 29.850  41.494  -19.051 1.00 91.59  ? 191  PRO   A CD  1 
ATOM   836   N  N   . SER   A 1 123 ? 25.729  40.500  -17.342 1.00 95.59  ? 192  SER   A N   1 
ATOM   837   C  CA  . SER   A 1 123 ? 24.420  41.131  -17.338 1.00 96.87  ? 192  SER   A CA  1 
ATOM   838   C  C   . SER   A 1 123 ? 24.570  42.645  -17.312 1.00 98.81  ? 192  SER   A C   1 
ATOM   839   O  O   . SER   A 1 123 ? 25.525  43.185  -16.743 1.00 99.93  ? 192  SER   A O   1 
ATOM   840   C  CB  . SER   A 1 123 ? 23.596  40.679  -16.139 1.00 99.42  ? 192  SER   A CB  1 
ATOM   841   O  OG  . SER   A 1 123 ? 22.455  41.512  -15.974 1.00 100.91 ? 192  SER   A OG  1 
ATOM   842   N  N   . THR   A 1 124 ? 23.610  43.327  -17.950 1.00 96.43  ? 193  THR   A N   1 
ATOM   843   C  CA  . THR   A 1 124 ? 23.614  44.788  -17.977 1.00 90.75  ? 193  THR   A CA  1 
ATOM   844   C  C   . THR   A 1 124 ? 23.546  45.358  -16.556 1.00 92.76  ? 193  THR   A C   1 
ATOM   845   O  O   . THR   A 1 124 ? 24.140  46.410  -16.275 1.00 86.65  ? 193  THR   A O   1 
ATOM   846   C  CB  . THR   A 1 124 ? 22.458  45.261  -18.872 1.00 84.37  ? 193  THR   A CB  1 
ATOM   847   O  OG1 . THR   A 1 124 ? 21.216  45.093  -18.190 1.00 91.28  ? 193  THR   A OG1 1 
ATOM   848   C  CG2 . THR   A 1 124 ? 22.376  44.388  -20.108 1.00 84.68  ? 193  THR   A CG2 1 
ATOM   849   N  N   . MET   A 1 125 ? 22.930  44.614  -15.632 1.00 94.43  ? 194  MET   A N   1 
ATOM   850   C  CA  . MET   A 1 125 ? 22.708  45.025  -14.249 1.00 94.48  ? 194  MET   A CA  1 
ATOM   851   C  C   . MET   A 1 125 ? 23.717  44.429  -13.283 1.00 99.40  ? 194  MET   A C   1 
ATOM   852   O  O   . MET   A 1 125 ? 23.512  44.480  -12.064 1.00 99.14  ? 194  MET   A O   1 
ATOM   853   C  CB  . MET   A 1 125 ? 21.291  44.641  -13.835 1.00 92.23  ? 194  MET   A CB  1 
ATOM   854   C  CG  . MET   A 1 125 ? 20.257  45.301  -14.698 1.00 85.84  ? 194  MET   A CG  1 
ATOM   855   S  SD  . MET   A 1 125 ? 20.135  46.986  -14.165 1.00 92.02  ? 194  MET   A SD  1 
ATOM   856   C  CE  . MET   A 1 125 ? 21.282  47.949  -15.146 1.00 86.13  ? 194  MET   A CE  1 
ATOM   857   N  N   . SER   A 1 126 ? 24.803  43.860  -13.805 1.00 103.93 ? 195  SER   A N   1 
ATOM   858   C  CA  . SER   A 1 126 ? 25.755  43.171  -12.949 1.00 105.84 ? 195  SER   A CA  1 
ATOM   859   C  C   . SER   A 1 126 ? 26.407  44.128  -11.967 1.00 107.88 ? 195  SER   A C   1 
ATOM   860   O  O   . SER   A 1 126 ? 26.703  43.751  -10.830 1.00 109.46 ? 195  SER   A O   1 
ATOM   861   C  CB  . SER   A 1 126 ? 26.816  42.457  -13.785 1.00 105.14 ? 195  SER   A CB  1 
ATOM   862   O  OG  . SER   A 1 126 ? 27.747  43.375  -14.334 1.00 105.95 ? 195  SER   A OG  1 
ATOM   863   N  N   . ALA   A 1 127 ? 26.632  45.385  -12.378 1.00 107.12 ? 196  ALA   A N   1 
ATOM   864   C  CA  . ALA   A 1 127 ? 27.301  46.361  -11.529 1.00 106.71 ? 196  ALA   A CA  1 
ATOM   865   C  C   . ALA   A 1 127 ? 26.332  47.190  -10.698 1.00 108.88 ? 196  ALA   A C   1 
ATOM   866   O  O   . ALA   A 1 127 ? 26.697  47.684  -9.626  1.00 111.46 ? 196  ALA   A O   1 
ATOM   867   C  CB  . ALA   A 1 127 ? 28.159  47.296  -12.382 1.00 104.38 ? 196  ALA   A CB  1 
ATOM   868   N  N   . VAL   A 1 128 ? 25.102  47.357  -11.163 1.00 109.88 ? 197  VAL   A N   1 
ATOM   869   C  CA  . VAL   A 1 128 ? 24.163  48.165  -10.407 1.00 110.45 ? 197  VAL   A CA  1 
ATOM   870   C  C   . VAL   A 1 128 ? 23.322  47.345  -9.435  1.00 111.67 ? 197  VAL   A C   1 
ATOM   871   O  O   . VAL   A 1 128 ? 22.716  47.917  -8.518  1.00 112.73 ? 197  VAL   A O   1 
ATOM   872   C  CB  . VAL   A 1 128 ? 23.277  48.945  -11.385 1.00 109.31 ? 197  VAL   A CB  1 
ATOM   873   C  CG1 . VAL   A 1 128 ? 22.632  50.105  -10.661 1.00 112.28 ? 197  VAL   A CG1 1 
ATOM   874   C  CG2 . VAL   A 1 128 ? 24.115  49.416  -12.563 1.00 107.43 ? 197  VAL   A CG2 1 
ATOM   875   N  N   . GLN   A 1 129 ? 23.287  46.024  -9.593  1.00 105.92 ? 198  GLN   A N   1 
ATOM   876   C  CA  . GLN   A 1 129 ? 22.471  45.173  -8.740  1.00 104.08 ? 198  GLN   A CA  1 
ATOM   877   C  C   . GLN   A 1 129 ? 22.770  45.436  -7.269  1.00 106.05 ? 198  GLN   A C   1 
ATOM   878   O  O   . GLN   A 1 129 ? 23.910  45.274  -6.816  1.00 109.42 ? 198  GLN   A O   1 
ATOM   879   C  CB  . GLN   A 1 129 ? 22.722  43.705  -9.086  1.00 104.59 ? 198  GLN   A CB  1 
ATOM   880   C  CG  . GLN   A 1 129 ? 21.677  42.761  -8.546  1.00 105.91 ? 198  GLN   A CG  1 
ATOM   881   C  CD  . GLN   A 1 129 ? 20.337  42.932  -9.230  1.00 109.32 ? 198  GLN   A CD  1 
ATOM   882   O  OE1 . GLN   A 1 129 ? 19.391  43.492  -8.661  1.00 109.37 ? 198  GLN   A OE1 1 
ATOM   883   N  NE2 . GLN   A 1 129 ? 20.241  42.430  -10.459 1.00 113.04 ? 198  GLN   A NE2 1 
ATOM   884   N  N   . LEU   A 1 130 ? 21.740  45.874  -6.535  1.00 105.10 ? 199  LEU   A N   1 
ATOM   885   C  CA  . LEU   A 1 130 ? 21.868  46.122  -5.104  1.00 101.88 ? 199  LEU   A CA  1 
ATOM   886   C  C   . LEU   A 1 130 ? 22.177  44.823  -4.368  1.00 103.26 ? 199  LEU   A C   1 
ATOM   887   O  O   . LEU   A 1 130 ? 21.633  43.768  -4.699  1.00 105.76 ? 199  LEU   A O   1 
ATOM   888   C  CB  . LEU   A 1 130 ? 20.576  46.742  -4.563  1.00 97.67  ? 199  LEU   A CB  1 
ATOM   889   C  CG  . LEU   A 1 130 ? 20.671  48.210  -4.150  1.00 93.96  ? 199  LEU   A CG  1 
ATOM   890   C  CD1 . LEU   A 1 130 ? 20.855  49.055  -5.372  1.00 92.72  ? 199  LEU   A CD1 1 
ATOM   891   C  CD2 . LEU   A 1 130 ? 19.448  48.649  -3.371  1.00 95.44  ? 199  LEU   A CD2 1 
ATOM   892   N  N   . GLU   A 1 131 ? 23.056  44.904  -3.360  1.00 101.95 ? 200  GLU   A N   1 
ATOM   893   C  CA  . GLU   A 1 131 ? 23.476  43.708  -2.619  1.00 103.67 ? 200  GLU   A CA  1 
ATOM   894   C  C   . GLU   A 1 131 ? 22.287  42.966  -2.013  1.00 101.00 ? 200  GLU   A C   1 
ATOM   895   O  O   . GLU   A 1 131 ? 22.217  41.732  -2.073  1.00 102.50 ? 200  GLU   A O   1 
ATOM   896   C  CB  . GLU   A 1 131 ? 24.476  44.097  -1.524  1.00 106.61 ? 200  GLU   A CB  1 
ATOM   897   C  CG  . GLU   A 1 131 ? 25.926  44.133  -1.988  1.00 108.35 ? 200  GLU   A CG  1 
ATOM   898   C  CD  . GLU   A 1 131 ? 26.115  45.027  -3.207  1.00 110.34 ? 200  GLU   A CD  1 
ATOM   899   O  OE1 . GLU   A 1 131 ? 25.591  46.174  -3.183  1.00 104.94 ? 200  GLU   A OE1 1 
ATOM   900   O  OE2 . GLU   A 1 131 ? 26.770  44.575  -4.186  1.00 111.10 ? 200  GLU   A OE2 1 
ATOM   901   N  N   . SER   A 1 132 ? 21.354  43.703  -1.409  1.00 102.66 ? 201  SER   A N   1 
ATOM   902   C  CA  . SER   A 1 132 ? 20.135  43.103  -0.874  1.00 101.84 ? 201  SER   A CA  1 
ATOM   903   C  C   . SER   A 1 132 ? 19.325  42.440  -1.974  1.00 103.07 ? 201  SER   A C   1 
ATOM   904   O  O   . SER   A 1 132 ? 18.728  41.376  -1.772  1.00 105.74 ? 201  SER   A O   1 
ATOM   905   C  CB  . SER   A 1 132 ? 19.302  44.179  -0.179  1.00 99.67  ? 201  SER   A CB  1 
ATOM   906   O  OG  . SER   A 1 132 ? 19.157  45.335  -0.996  1.00 93.53  ? 201  SER   A OG  1 
ATOM   907   N  N   . LEU   A 1 133 ? 19.296  43.056  -3.145  1.00 104.54 ? 202  LEU   A N   1 
ATOM   908   C  CA  . LEU   A 1 133 ? 18.564  42.552  -4.292  1.00 107.28 ? 202  LEU   A CA  1 
ATOM   909   C  C   . LEU   A 1 133 ? 19.272  41.386  -4.984  1.00 112.50 ? 202  LEU   A C   1 
ATOM   910   O  O   . LEU   A 1 133 ? 18.668  40.741  -5.852  1.00 115.32 ? 202  LEU   A O   1 
ATOM   911   C  CB  . LEU   A 1 133 ? 18.331  43.710  -5.274  1.00 104.83 ? 202  LEU   A CB  1 
ATOM   912   C  CG  . LEU   A 1 133 ? 17.044  44.504  -5.058  1.00 97.08  ? 202  LEU   A CG  1 
ATOM   913   C  CD1 . LEU   A 1 133 ? 15.930  43.596  -5.431  1.00 107.00 ? 202  LEU   A CD1 1 
ATOM   914   C  CD2 . LEU   A 1 133 ? 16.860  44.896  -3.634  1.00 95.39  ? 202  LEU   A CD2 1 
ATOM   915   N  N   . ASN   A 1 134 ? 20.540  41.118  -4.630  1.00 113.98 ? 203  ASN   A N   1 
ATOM   916   C  CA  . ASN   A 1 134 ? 21.276  39.998  -5.216  1.00 113.93 ? 203  ASN   A CA  1 
ATOM   917   C  C   . ASN   A 1 134 ? 20.602  38.669  -4.885  1.00 113.29 ? 203  ASN   A C   1 
ATOM   918   O  O   . ASN   A 1 134 ? 20.559  37.766  -5.727  1.00 113.75 ? 203  ASN   A O   1 
ATOM   919   C  CB  . ASN   A 1 134 ? 22.741  39.996  -4.728  1.00 112.42 ? 203  ASN   A CB  1 
ATOM   920   C  CG  . ASN   A 1 134 ? 23.723  40.743  -5.685  1.00 114.31 ? 203  ASN   A CG  1 
ATOM   921   O  OD1 . ASN   A 1 134 ? 24.593  41.515  -5.236  1.00 111.99 ? 203  ASN   A OD1 1 
ATOM   922   N  ND2 . ASN   A 1 134 ? 23.596  40.492  -6.995  1.00 114.23 ? 203  ASN   A ND2 1 
ATOM   923   N  N   . LYS   A 1 135 ? 20.057  38.539  -3.666  1.00 119.35 ? 204  LYS   A N   1 
ATOM   924   C  CA  . LYS   A 1 135 ? 19.445  37.279  -3.234  1.00 118.59 ? 204  LYS   A CA  1 
ATOM   925   C  C   . LYS   A 1 135 ? 18.137  37.004  -3.967  1.00 121.56 ? 204  LYS   A C   1 
ATOM   926   O  O   . LYS   A 1 135 ? 17.836  35.850  -4.297  1.00 121.67 ? 204  LYS   A O   1 
ATOM   927   C  CB  . LYS   A 1 135 ? 19.190  37.299  -1.725  1.00 117.95 ? 204  LYS   A CB  1 
ATOM   928   C  CG  . LYS   A 1 135 ? 20.420  37.546  -0.878  1.00 117.93 ? 204  LYS   A CG  1 
ATOM   929   C  CD  . LYS   A 1 135 ? 21.419  36.410  -1.031  1.00 117.91 ? 204  LYS   A CD  1 
ATOM   930   C  CE  . LYS   A 1 135 ? 22.758  36.789  -0.440  1.00 117.27 ? 204  LYS   A CE  1 
ATOM   931   N  NZ  . LYS   A 1 135 ? 23.270  38.055  -1.035  1.00 119.74 ? 204  LYS   A NZ  1 
ATOM   932   N  N   . CYS   A 1 136 ? 17.334  38.044  -4.205  1.00 127.23 ? 205  CYS   A N   1 
ATOM   933   C  CA  . CYS   A 1 136 ? 16.030  37.910  -4.859  1.00 127.32 ? 205  CYS   A CA  1 
ATOM   934   C  C   . CYS   A 1 136 ? 16.133  37.889  -6.374  1.00 130.18 ? 205  CYS   A C   1 
ATOM   935   O  O   . CYS   A 1 136 ? 15.268  38.440  -7.060  1.00 131.80 ? 205  CYS   A O   1 
ATOM   936   C  CB  . CYS   A 1 136 ? 15.119  39.048  -4.405  1.00 123.80 ? 205  CYS   A CB  1 
ATOM   937   S  SG  . CYS   A 1 136 ? 15.447  39.589  -2.717  1.00 130.46 ? 205  CYS   A SG  1 
ATOM   938   N  N   . GLN   A 1 137 ? 17.180  37.280  -6.925  1.00 123.98 ? 206  GLN   A N   1 
ATOM   939   C  CA  . GLN   A 1 137 ? 17.411  37.329  -8.360  1.00 121.33 ? 206  GLN   A CA  1 
ATOM   940   C  C   . GLN   A 1 137 ? 17.052  36.032  -9.060  1.00 118.79 ? 206  GLN   A C   1 
ATOM   941   O  O   . GLN   A 1 137 ? 16.228  36.051  -9.980  1.00 118.84 ? 206  GLN   A O   1 
ATOM   942   C  CB  . GLN   A 1 137 ? 18.872  37.710  -8.669  1.00 120.65 ? 206  GLN   A CB  1 
ATOM   943   C  CG  . GLN   A 1 137 ? 19.077  39.206  -8.769  1.00 118.34 ? 206  GLN   A CG  1 
ATOM   944   C  CD  . GLN   A 1 137 ? 17.839  39.895  -9.332  1.00 120.22 ? 206  GLN   A CD  1 
ATOM   945   O  OE1 . GLN   A 1 137 ? 17.190  40.719  -8.655  1.00 119.74 ? 206  GLN   A OE1 1 
ATOM   946   N  NE2 . GLN   A 1 137 ? 17.495  39.552  -10.582 1.00 114.56 ? 206  GLN   A NE2 1 
ATOM   947   N  N   . ILE   A 1 138 ? 17.647  34.910  -8.648  1.00 113.91 ? 207  ILE   A N   1 
ATOM   948   C  CA  . ILE   A 1 138 ? 17.410  33.621  -9.288  1.00 111.31 ? 207  ILE   A CA  1 
ATOM   949   C  C   . ILE   A 1 138 ? 15.912  33.567  -9.538  1.00 112.43 ? 207  ILE   A C   1 
ATOM   950   O  O   . ILE   A 1 138 ? 15.106  33.702  -8.612  1.00 112.94 ? 207  ILE   A O   1 
ATOM   951   C  CB  . ILE   A 1 138 ? 17.959  32.455  -8.452  1.00 110.53 ? 207  ILE   A CB  1 
ATOM   952   C  CG1 . ILE   A 1 138 ? 19.482  32.399  -8.544  1.00 113.90 ? 207  ILE   A CG1 1 
ATOM   953   C  CG2 . ILE   A 1 138 ? 17.401  31.133  -8.969  1.00 108.35 ? 207  ILE   A CG2 1 
ATOM   954   C  CD1 . ILE   A 1 138 ? 19.986  31.731  -9.820  1.00 109.61 ? 207  ILE   A CD1 1 
ATOM   955   N  N   . PHE   A 1 139 ? 15.538  33.379  -10.792 1.00 116.01 ? 208  PHE   A N   1 
ATOM   956   C  CA  . PHE   A 1 139 ? 14.131  33.402  -11.174 1.00 114.66 ? 208  PHE   A CA  1 
ATOM   957   C  C   . PHE   A 1 139 ? 13.571  32.012  -10.908 1.00 115.42 ? 208  PHE   A C   1 
ATOM   958   O  O   . PHE   A 1 139 ? 14.216  31.009  -11.245 1.00 117.11 ? 208  PHE   A O   1 
ATOM   959   C  CB  . PHE   A 1 139 ? 13.953  33.762  -12.641 1.00 115.48 ? 208  PHE   A CB  1 
ATOM   960   C  CG  . PHE   A 1 139 ? 14.018  35.226  -12.902 1.00 111.75 ? 208  PHE   A CG  1 
ATOM   961   C  CD1 . PHE   A 1 139 ? 15.243  35.871  -12.979 1.00 111.67 ? 208  PHE   A CD1 1 
ATOM   962   C  CD2 . PHE   A 1 139 ? 12.855  35.969  -13.046 1.00 110.67 ? 208  PHE   A CD2 1 
ATOM   963   C  CE1 . PHE   A 1 139 ? 15.310  37.242  -13.205 1.00 108.30 ? 208  PHE   A CE1 1 
ATOM   964   C  CE2 . PHE   A 1 139 ? 12.908  37.321  -13.274 1.00 108.05 ? 208  PHE   A CE2 1 
ATOM   965   C  CZ  . PHE   A 1 139 ? 14.140  37.965  -13.359 1.00 107.63 ? 208  PHE   A CZ  1 
ATOM   966   N  N   . PRO   A 1 140 ? 12.383  31.907  -10.318 1.00 114.03 ? 209  PRO   A N   1 
ATOM   967   C  CA  . PRO   A 1 140 ? 11.747  30.592  -10.207 1.00 118.59 ? 209  PRO   A CA  1 
ATOM   968   C  C   . PRO   A 1 140 ? 11.524  30.032  -11.607 1.00 126.50 ? 209  PRO   A C   1 
ATOM   969   O  O   . PRO   A 1 140 ? 11.190  30.765  -12.543 1.00 125.09 ? 209  PRO   A O   1 
ATOM   970   C  CB  . PRO   A 1 140 ? 10.435  30.881  -9.460  1.00 115.40 ? 209  PRO   A CB  1 
ATOM   971   C  CG  . PRO   A 1 140 ? 10.220  32.372  -9.579  1.00 113.77 ? 209  PRO   A CG  1 
ATOM   972   C  CD  . PRO   A 1 140 ? 11.564  32.993  -9.745  1.00 112.66 ? 209  PRO   A CD  1 
ATOM   973   N  N   . SER   A 1 141 ? 11.762  28.724  -11.753 1.00 133.01 ? 210  SER   A N   1 
ATOM   974   C  CA  . SER   A 1 141 ? 11.843  28.049  -13.058 1.00 134.03 ? 210  SER   A CA  1 
ATOM   975   C  C   . SER   A 1 141 ? 10.759  28.445  -14.087 1.00 133.47 ? 210  SER   A C   1 
ATOM   976   O  O   . SER   A 1 141 ? 9.660   28.886  -13.736 1.00 130.54 ? 210  SER   A O   1 
ATOM   977   C  CB  . SER   A 1 141 ? 11.813  26.532  -12.829 1.00 131.77 ? 210  SER   A CB  1 
ATOM   978   O  OG  . SER   A 1 141 ? 12.723  26.158  -11.805 1.00 128.21 ? 210  SER   A OG  1 
ATOM   979   N  N   . SER   A 1 151 ? 3.155   32.777  -19.848 1.00 152.04 ? 220  SER   A N   1 
ATOM   980   C  CA  . SER   A 1 151 ? 2.792   33.273  -21.169 1.00 164.15 ? 220  SER   A CA  1 
ATOM   981   C  C   . SER   A 1 151 ? 3.620   34.509  -21.538 1.00 168.59 ? 220  SER   A C   1 
ATOM   982   O  O   . SER   A 1 151 ? 4.797   34.404  -21.890 1.00 159.82 ? 220  SER   A O   1 
ATOM   983   C  CB  . SER   A 1 151 ? 1.297   33.588  -21.216 1.00 165.56 ? 220  SER   A CB  1 
ATOM   984   O  OG  . SER   A 1 151 ? 0.876   34.154  -19.987 1.00 161.13 ? 220  SER   A OG  1 
ATOM   985   N  N   . TYR   A 1 152 ? 2.990   35.685  -21.448 1.00 177.45 ? 221  TYR   A N   1 
ATOM   986   C  CA  . TYR   A 1 152 ? 3.617   36.959  -21.776 1.00 174.73 ? 221  TYR   A CA  1 
ATOM   987   C  C   . TYR   A 1 152 ? 3.760   37.874  -20.582 1.00 172.75 ? 221  TYR   A C   1 
ATOM   988   O  O   . TYR   A 1 152 ? 4.682   38.690  -20.550 1.00 170.83 ? 221  TYR   A O   1 
ATOM   989   C  CB  . TYR   A 1 152 ? 2.805   37.701  -22.844 1.00 176.84 ? 221  TYR   A CB  1 
ATOM   990   C  CG  . TYR   A 1 152 ? 2.172   36.783  -23.861 1.00 185.00 ? 221  TYR   A CG  1 
ATOM   991   C  CD1 . TYR   A 1 152 ? 2.924   35.812  -24.513 1.00 189.55 ? 221  TYR   A CD1 1 
ATOM   992   C  CD2 . TYR   A 1 152 ? 0.817   36.873  -24.158 1.00 185.86 ? 221  TYR   A CD2 1 
ATOM   993   C  CE1 . TYR   A 1 152 ? 2.352   34.965  -25.439 1.00 191.82 ? 221  TYR   A CE1 1 
ATOM   994   C  CE2 . TYR   A 1 152 ? 0.233   36.034  -25.086 1.00 190.77 ? 221  TYR   A CE2 1 
ATOM   995   C  CZ  . TYR   A 1 152 ? 1.006   35.079  -25.726 1.00 194.16 ? 221  TYR   A CZ  1 
ATOM   996   O  OH  . TYR   A 1 152 ? 0.437   34.232  -26.657 1.00 198.33 ? 221  TYR   A OH  1 
ATOM   997   N  N   . LYS   A 1 153 ? 2.848   37.771  -19.615 1.00 157.48 ? 222  LYS   A N   1 
ATOM   998   C  CA  . LYS   A 1 153 ? 3.008   38.497  -18.366 1.00 149.50 ? 222  LYS   A CA  1 
ATOM   999   C  C   . LYS   A 1 153 ? 4.308   38.126  -17.693 1.00 142.99 ? 222  LYS   A C   1 
ATOM   1000  O  O   . LYS   A 1 153 ? 4.860   38.925  -16.927 1.00 139.31 ? 222  LYS   A O   1 
ATOM   1001  C  CB  . LYS   A 1 153 ? 1.850   38.205  -17.430 1.00 149.20 ? 222  LYS   A CB  1 
ATOM   1002  C  CG  . LYS   A 1 153 ? 0.542   38.802  -17.881 1.00 149.98 ? 222  LYS   A CG  1 
ATOM   1003  C  CD  . LYS   A 1 153 ? -0.547  38.447  -16.887 1.00 158.78 ? 222  LYS   A CD  1 
ATOM   1004  C  CE  . LYS   A 1 153 ? -1.845  39.166  -17.227 1.00 158.10 ? 222  LYS   A CE  1 
ATOM   1005  N  NZ  . LYS   A 1 153 ? -2.922  38.845  -16.247 1.00 159.34 ? 222  LYS   A NZ  1 
ATOM   1006  N  N   . TRP   A 1 154 ? 4.804   36.916  -17.954 1.00 131.64 ? 223  TRP   A N   1 
ATOM   1007  C  CA  . TRP   A 1 154 ? 6.080   36.512  -17.383 1.00 117.53 ? 223  TRP   A CA  1 
ATOM   1008  C  C   . TRP   A 1 154 ? 7.200   37.436  -17.837 1.00 116.40 ? 223  TRP   A C   1 
ATOM   1009  O  O   . TRP   A 1 154 ? 8.116   37.730  -17.062 1.00 115.76 ? 223  TRP   A O   1 
ATOM   1010  C  CB  . TRP   A 1 154 ? 6.394   35.073  -17.757 1.00 114.17 ? 223  TRP   A CB  1 
ATOM   1011  C  CG  . TRP   A 1 154 ? 7.778   34.667  -17.380 1.00 103.76 ? 223  TRP   A CG  1 
ATOM   1012  C  CD1 . TRP   A 1 154 ? 8.916   34.826  -18.118 1.00 102.21 ? 223  TRP   A CD1 1 
ATOM   1013  C  CD2 . TRP   A 1 154 ? 8.172   34.033  -16.175 1.00 108.68 ? 223  TRP   A CD2 1 
ATOM   1014  N  NE1 . TRP   A 1 154 ? 10.000  34.331  -17.446 1.00 96.32  ? 223  TRP   A NE1 1 
ATOM   1015  C  CE2 . TRP   A 1 154 ? 9.572   33.832  -16.246 1.00 111.02 ? 223  TRP   A CE2 1 
ATOM   1016  C  CE3 . TRP   A 1 154 ? 7.482   33.614  -15.032 1.00 116.91 ? 223  TRP   A CE3 1 
ATOM   1017  C  CZ2 . TRP   A 1 154 ? 10.299  33.230  -15.211 1.00 121.36 ? 223  TRP   A CZ2 1 
ATOM   1018  C  CZ3 . TRP   A 1 154 ? 8.206   33.012  -13.994 1.00 125.82 ? 223  TRP   A CZ3 1 
ATOM   1019  C  CH2 . TRP   A 1 154 ? 9.602   32.828  -14.095 1.00 124.69 ? 223  TRP   A CH2 1 
ATOM   1020  N  N   . TRP   A 1 155 ? 7.156   37.901  -19.094 1.00 117.16 ? 224  TRP   A N   1 
ATOM   1021  C  CA  . TRP   A 1 155 ? 8.238   38.755  -19.578 1.00 107.83 ? 224  TRP   A CA  1 
ATOM   1022  C  C   . TRP   A 1 155 ? 8.090   40.189  -19.098 1.00 106.04 ? 224  TRP   A C   1 
ATOM   1023  O  O   . TRP   A 1 155 ? 9.105   40.869  -18.923 1.00 104.52 ? 224  TRP   A O   1 
ATOM   1024  C  CB  . TRP   A 1 155 ? 8.352   38.691  -21.108 1.00 103.96 ? 224  TRP   A CB  1 
ATOM   1025  C  CG  . TRP   A 1 155 ? 9.009   37.407  -21.557 1.00 93.94  ? 224  TRP   A CG  1 
ATOM   1026  C  CD1 . TRP   A 1 155 ? 8.386   36.252  -21.896 1.00 93.83  ? 224  TRP   A CD1 1 
ATOM   1027  C  CD2 . TRP   A 1 155 ? 10.420  37.145  -21.654 1.00 88.27  ? 224  TRP   A CD2 1 
ATOM   1028  N  NE1 . TRP   A 1 155 ? 9.312   35.293  -22.214 1.00 88.72  ? 224  TRP   A NE1 1 
ATOM   1029  C  CE2 . TRP   A 1 155 ? 10.568  35.817  -22.072 1.00 82.71  ? 224  TRP   A CE2 1 
ATOM   1030  C  CE3 . TRP   A 1 155 ? 11.569  37.912  -21.436 1.00 92.93  ? 224  TRP   A CE3 1 
ATOM   1031  C  CZ2 . TRP   A 1 155 ? 11.813  35.233  -22.274 1.00 84.96  ? 224  TRP   A CZ2 1 
ATOM   1032  C  CZ3 . TRP   A 1 155 ? 12.815  37.323  -21.637 1.00 88.42  ? 224  TRP   A CZ3 1 
ATOM   1033  C  CH2 . TRP   A 1 155 ? 12.923  36.005  -22.051 1.00 86.00  ? 224  TRP   A CH2 1 
ATOM   1034  N  N   . GLN   A 1 156 ? 6.861   40.672  -18.868 1.00 109.73 ? 225  GLN   A N   1 
ATOM   1035  C  CA  . GLN   A 1 156 ? 6.725   41.949  -18.171 1.00 109.10 ? 225  GLN   A CA  1 
ATOM   1036  C  C   . GLN   A 1 156 ? 7.285   41.850  -16.758 1.00 105.03 ? 225  GLN   A C   1 
ATOM   1037  O  O   . GLN   A 1 156 ? 7.969   42.770  -16.295 1.00 101.99 ? 225  GLN   A O   1 
ATOM   1038  C  CB  . GLN   A 1 156 ? 5.271   42.413  -18.142 1.00 115.65 ? 225  GLN   A CB  1 
ATOM   1039  C  CG  . GLN   A 1 156 ? 4.720   42.817  -19.504 1.00 122.82 ? 225  GLN   A CG  1 
ATOM   1040  C  CD  . GLN   A 1 156 ? 3.305   42.294  -19.723 1.00 137.26 ? 225  GLN   A CD  1 
ATOM   1041  O  OE1 . GLN   A 1 156 ? 2.469   42.317  -18.808 1.00 138.10 ? 225  GLN   A OE1 1 
ATOM   1042  N  NE2 . GLN   A 1 156 ? 3.032   41.803  -20.936 1.00 140.74 ? 225  GLN   A NE2 1 
ATOM   1043  N  N   . LYS   A 1 157 ? 7.024   40.727  -16.073 1.00 108.48 ? 226  LYS   A N   1 
ATOM   1044  C  CA  . LYS   A 1 157 ? 7.588   40.484  -14.746 1.00 98.30  ? 226  LYS   A CA  1 
ATOM   1045  C  C   . LYS   A 1 157 ? 9.087   40.279  -14.811 1.00 96.29  ? 226  LYS   A C   1 
ATOM   1046  O  O   . LYS   A 1 157 ? 9.810   40.774  -13.948 1.00 97.78  ? 226  LYS   A O   1 
ATOM   1047  C  CB  . LYS   A 1 157 ? 6.947   39.261  -14.106 1.00 103.41 ? 226  LYS   A CB  1 
ATOM   1048  C  CG  . LYS   A 1 157 ? 5.462   39.399  -13.832 1.00 111.35 ? 226  LYS   A CG  1 
ATOM   1049  C  CD  . LYS   A 1 157 ? 4.821   38.050  -13.492 1.00 113.94 ? 226  LYS   A CD  1 
ATOM   1050  C  CE  . LYS   A 1 157 ? 3.311   38.177  -13.309 1.00 109.67 ? 226  LYS   A CE  1 
ATOM   1051  N  NZ  . LYS   A 1 157 ? 2.873   37.820  -11.931 1.00 107.64 ? 226  LYS   A NZ  1 
ATOM   1052  N  N   . TYR   A 1 158 ? 9.565   39.518  -15.804 1.00 100.94 ? 227  TYR   A N   1 
ATOM   1053  C  CA  . TYR   A 1 158 ? 11.003  39.314  -15.977 1.00 95.29  ? 227  TYR   A CA  1 
ATOM   1054  C  C   . TYR   A 1 158 ? 11.719  40.648  -16.065 1.00 93.97  ? 227  TYR   A C   1 
ATOM   1055  O  O   . TYR   A 1 158 ? 12.798  40.826  -15.487 1.00 90.30  ? 227  TYR   A O   1 
ATOM   1056  C  CB  . TYR   A 1 158 ? 11.268  38.473  -17.230 1.00 94.30  ? 227  TYR   A CB  1 
ATOM   1057  C  CG  . TYR   A 1 158 ? 12.727  38.336  -17.660 1.00 94.22  ? 227  TYR   A CG  1 
ATOM   1058  C  CD1 . TYR   A 1 158 ? 13.284  39.221  -18.579 1.00 95.72  ? 227  TYR   A CD1 1 
ATOM   1059  C  CD2 . TYR   A 1 158 ? 13.533  37.304  -17.176 1.00 94.64  ? 227  TYR   A CD2 1 
ATOM   1060  C  CE1 . TYR   A 1 158 ? 14.598  39.097  -18.985 1.00 92.54  ? 227  TYR   A CE1 1 
ATOM   1061  C  CE2 . TYR   A 1 158 ? 14.850  37.172  -17.575 1.00 89.40  ? 227  TYR   A CE2 1 
ATOM   1062  C  CZ  . TYR   A 1 158 ? 15.377  38.074  -18.481 1.00 93.31  ? 227  TYR   A CZ  1 
ATOM   1063  O  OH  . TYR   A 1 158 ? 16.692  37.969  -18.893 1.00 100.64 ? 227  TYR   A OH  1 
ATOM   1064  N  N   . GLN   A 1 159 ? 11.095  41.608  -16.751 1.00 95.87  ? 228  GLN   A N   1 
ATOM   1065  C  CA  . GLN   A 1 159 ? 11.726  42.901  -16.998 1.00 92.73  ? 228  GLN   A CA  1 
ATOM   1066  C  C   . GLN   A 1 159 ? 11.680  43.788  -15.755 1.00 93.18  ? 228  GLN   A C   1 
ATOM   1067  O  O   . GLN   A 1 159 ? 12.673  44.467  -15.438 1.00 91.69  ? 228  GLN   A O   1 
ATOM   1068  C  CB  . GLN   A 1 159 ? 11.053  43.563  -18.207 1.00 91.09  ? 228  GLN   A CB  1 
ATOM   1069  C  CG  . GLN   A 1 159 ? 11.682  44.860  -18.703 1.00 88.17  ? 228  GLN   A CG  1 
ATOM   1070  C  CD  . GLN   A 1 159 ? 10.725  45.658  -19.571 1.00 84.09  ? 228  GLN   A CD  1 
ATOM   1071  O  OE1 . GLN   A 1 159 ? 9.783   46.278  -19.069 1.00 84.69  ? 228  GLN   A OE1 1 
ATOM   1072  N  NE2 . GLN   A 1 159 ? 10.947  45.631  -20.878 1.00 84.51  ? 228  GLN   A NE2 1 
ATOM   1073  N  N   . LYS   A 1 160 ? 10.543  43.793  -15.028 1.00 93.10  ? 229  LYS   A N   1 
ATOM   1074  C  CA  . LYS   A 1 160 ? 10.477  44.476  -13.735 1.00 90.77  ? 229  LYS   A CA  1 
ATOM   1075  C  C   . LYS   A 1 160 ? 11.587  44.003  -12.805 1.00 90.02  ? 229  LYS   A C   1 
ATOM   1076  O  O   . LYS   A 1 160 ? 12.266  44.824  -12.175 1.00 89.06  ? 229  LYS   A O   1 
ATOM   1077  C  CB  . LYS   A 1 160 ? 9.117   44.264  -13.066 1.00 89.44  ? 229  LYS   A CB  1 
ATOM   1078  C  CG  . LYS   A 1 160 ? 7.962   45.082  -13.620 1.00 96.06  ? 229  LYS   A CG  1 
ATOM   1079  C  CD  . LYS   A 1 160 ? 6.616   44.399  -13.278 1.00 106.45 ? 229  LYS   A CD  1 
ATOM   1080  C  CE  . LYS   A 1 160 ? 5.687   44.267  -14.517 1.00 107.82 ? 229  LYS   A CE  1 
ATOM   1081  N  NZ  . LYS   A 1 160 ? 4.555   43.288  -14.384 1.00 99.00  ? 229  LYS   A NZ  1 
ATOM   1082  N  N   . ARG   A 1 161 ? 11.809  42.685  -12.727 1.00 92.86  ? 230  ARG   A N   1 
ATOM   1083  C  CA  . ARG   A 1 161 ? 12.742  42.157  -11.738 1.00 93.80  ? 230  ARG   A CA  1 
ATOM   1084  C  C   . ARG   A 1 161 ? 14.202  42.318  -12.155 1.00 94.64  ? 230  ARG   A C   1 
ATOM   1085  O  O   . ARG   A 1 161 ? 14.996  42.907  -11.417 1.00 100.78 ? 230  ARG   A O   1 
ATOM   1086  C  CB  . ARG   A 1 161 ? 12.467  40.689  -11.437 1.00 96.04  ? 230  ARG   A CB  1 
ATOM   1087  C  CG  . ARG   A 1 161 ? 13.413  40.222  -10.332 1.00 110.55 ? 230  ARG   A CG  1 
ATOM   1088  C  CD  . ARG   A 1 161 ? 13.557  38.726  -10.227 1.00 114.09 ? 230  ARG   A CD  1 
ATOM   1089  N  NE  . ARG   A 1 161 ? 12.281  38.083  -9.957  1.00 117.14 ? 230  ARG   A NE  1 
ATOM   1090  C  CZ  . ARG   A 1 161 ? 12.150  36.809  -9.618  1.00 119.42 ? 230  ARG   A CZ  1 
ATOM   1091  N  NH1 . ARG   A 1 161 ? 13.210  36.035  -9.421  1.00 119.49 ? 230  ARG   A NH1 1 
ATOM   1092  N  NH2 . ARG   A 1 161 ? 10.928  36.296  -9.484  1.00 119.31 ? 230  ARG   A NH2 1 
ATOM   1093  N  N   . LYS   A 1 162 ? 14.594  41.767  -13.309 1.00 92.24  ? 231  LYS   A N   1 
ATOM   1094  C  CA  . LYS   A 1 162 ? 16.014  41.762  -13.661 1.00 89.49  ? 231  LYS   A CA  1 
ATOM   1095  C  C   . LYS   A 1 162 ? 16.582  43.181  -13.694 1.00 90.27  ? 231  LYS   A C   1 
ATOM   1096  O  O   . LYS   A 1 162 ? 17.708  43.421  -13.242 1.00 92.97  ? 231  LYS   A O   1 
ATOM   1097  C  CB  . LYS   A 1 162 ? 16.217  41.042  -15.000 1.00 90.90  ? 231  LYS   A CB  1 
ATOM   1098  C  CG  . LYS   A 1 162 ? 17.677  40.885  -15.441 1.00 90.96  ? 231  LYS   A CG  1 
ATOM   1099  C  CD  . LYS   A 1 162 ? 17.866  39.895  -16.605 1.00 88.46  ? 231  LYS   A CD  1 
ATOM   1100  C  CE  . LYS   A 1 162 ? 19.368  39.668  -16.892 1.00 96.03  ? 231  LYS   A CE  1 
ATOM   1101  N  NZ  . LYS   A 1 162 ? 19.715  38.344  -17.511 1.00 94.19  ? 231  LYS   A NZ  1 
ATOM   1102  N  N   . PHE   A 1 163 ? 15.792  44.144  -14.164 1.00 88.00  ? 232  PHE   A N   1 
ATOM   1103  C  CA  . PHE   A 1 163 ? 16.256  45.505  -14.394 1.00 86.16  ? 232  PHE   A CA  1 
ATOM   1104  C  C   . PHE   A 1 163 ? 15.680  46.493  -13.389 1.00 91.55  ? 232  PHE   A C   1 
ATOM   1105  O  O   . PHE   A 1 163 ? 15.542  47.688  -13.680 1.00 93.96  ? 232  PHE   A O   1 
ATOM   1106  C  CB  . PHE   A 1 163 ? 15.906  45.927  -15.811 1.00 85.70  ? 232  PHE   A CB  1 
ATOM   1107  C  CG  . PHE   A 1 163 ? 16.395  44.977  -16.853 1.00 85.01  ? 232  PHE   A CG  1 
ATOM   1108  C  CD1 . PHE   A 1 163 ? 17.758  44.839  -17.096 1.00 83.27  ? 232  PHE   A CD1 1 
ATOM   1109  C  CD2 . PHE   A 1 163 ? 15.497  44.223  -17.599 1.00 82.97  ? 232  PHE   A CD2 1 
ATOM   1110  C  CE1 . PHE   A 1 163 ? 18.222  43.965  -18.068 1.00 82.73  ? 232  PHE   A CE1 1 
ATOM   1111  C  CE2 . PHE   A 1 163 ? 15.946  43.354  -18.566 1.00 83.16  ? 232  PHE   A CE2 1 
ATOM   1112  C  CZ  . PHE   A 1 163 ? 17.317  43.223  -18.801 1.00 85.39  ? 232  PHE   A CZ  1 
ATOM   1113  N  N   . HIS   A 1 164 ? 15.321  45.997  -12.207 1.00 90.49  ? 233  HIS   A N   1 
ATOM   1114  C  CA  . HIS   A 1 164 ? 14.821  46.859  -11.142 1.00 88.76  ? 233  HIS   A CA  1 
ATOM   1115  C  C   . HIS   A 1 164 ? 15.842  47.931  -10.781 1.00 90.10  ? 233  HIS   A C   1 
ATOM   1116  O  O   . HIS   A 1 164 ? 15.498  49.114  -10.633 1.00 93.44  ? 233  HIS   A O   1 
ATOM   1117  C  CB  . HIS   A 1 164 ? 14.488  45.985  -9.947  1.00 89.04  ? 233  HIS   A CB  1 
ATOM   1118  C  CG  . HIS   A 1 164 ? 14.012  46.727  -8.753  1.00 87.28  ? 233  HIS   A CG  1 
ATOM   1119  N  ND1 . HIS   A 1 164 ? 14.744  46.783  -7.589  1.00 88.12  ? 233  HIS   A ND1 1 
ATOM   1120  C  CD2 . HIS   A 1 164 ? 12.861  47.396  -8.512  1.00 89.02  ? 233  HIS   A CD2 1 
ATOM   1121  C  CE1 . HIS   A 1 164 ? 14.076  47.476  -6.686  1.00 89.36  ? 233  HIS   A CE1 1 
ATOM   1122  N  NE2 . HIS   A 1 164 ? 12.930  47.857  -7.218  1.00 90.75  ? 233  HIS   A NE2 1 
ATOM   1123  N  N   . CYS   A 1 165 ? 17.114  47.544  -10.679 1.00 87.53  ? 234  CYS   A N   1 
ATOM   1124  C  CA  . CYS   A 1 165 ? 18.190  48.458  -10.337 1.00 86.62  ? 234  CYS   A CA  1 
ATOM   1125  C  C   . CYS   A 1 165 ? 18.458  49.464  -11.441 1.00 89.89  ? 234  CYS   A C   1 
ATOM   1126  O  O   . CYS   A 1 165 ? 19.423  50.219  -11.366 1.00 92.10  ? 234  CYS   A O   1 
ATOM   1127  C  CB  . CYS   A 1 165 ? 19.458  47.677  -10.014 1.00 92.00  ? 234  CYS   A CB  1 
ATOM   1128  S  SG  . CYS   A 1 165 ? 19.348  46.971  -8.383  1.00 105.98 ? 234  CYS   A SG  1 
ATOM   1129  N  N   . ALA   A 1 166 ? 17.664  49.459  -12.512 1.00 88.89  ? 235  ALA   A N   1 
ATOM   1130  C  CA  . ALA   A 1 166 ? 17.863  50.466  -13.531 1.00 88.39  ? 235  ALA   A CA  1 
ATOM   1131  C  C   . ALA   A 1 166 ? 17.437  51.840  -13.030 1.00 91.19  ? 235  ALA   A C   1 
ATOM   1132  O  O   . ALA   A 1 166 ? 17.836  52.872  -13.600 1.00 86.78  ? 235  ALA   A O   1 
ATOM   1133  C  CB  . ALA   A 1 166 ? 17.082  50.040  -14.765 1.00 87.46  ? 235  ALA   A CB  1 
ATOM   1134  N  N   . ASN   A 1 167 ? 16.634  51.887  -11.983 1.00 99.37  ? 236  ASN   A N   1 
ATOM   1135  C  CA  . ASN   A 1 167 ? 16.212  53.164  -11.442 1.00 100.53 ? 236  ASN   A CA  1 
ATOM   1136  C  C   . ASN   A 1 167 ? 17.380  53.937  -10.882 1.00 100.27 ? 236  ASN   A C   1 
ATOM   1137  O  O   . ASN   A 1 167 ? 17.307  55.166  -10.796 1.00 101.03 ? 236  ASN   A O   1 
ATOM   1138  C  CB  . ASN   A 1 167 ? 15.136  52.949  -10.386 1.00 103.03 ? 236  ASN   A CB  1 
ATOM   1139  C  CG  . ASN   A 1 167 ? 13.835  52.456  -11.001 1.00 106.85 ? 236  ASN   A CG  1 
ATOM   1140  O  OD1 . ASN   A 1 167 ? 12.946  53.261  -11.359 1.00 108.74 ? 236  ASN   A OD1 1 
ATOM   1141  N  ND2 . ASN   A 1 167 ? 13.736  51.128  -11.188 1.00 104.58 ? 236  ASN   A ND2 1 
ATOM   1142  N  N   . LEU   A 1 168 ? 18.462  53.243  -10.533 1.00 87.12  ? 237  LEU   A N   1 
ATOM   1143  C  CA  . LEU   A 1 168 ? 19.687  53.869  -10.046 1.00 90.02  ? 237  LEU   A CA  1 
ATOM   1144  C  C   . LEU   A 1 168 ? 20.562  54.417  -11.169 1.00 88.20  ? 237  LEU   A C   1 
ATOM   1145  O  O   . LEU   A 1 168 ? 21.558  55.105  -10.889 1.00 84.82  ? 237  LEU   A O   1 
ATOM   1146  C  CB  . LEU   A 1 168 ? 20.520  52.875  -9.223  1.00 84.24  ? 237  LEU   A CB  1 
ATOM   1147  C  CG  . LEU   A 1 168 ? 19.987  52.317  -7.912  1.00 78.06  ? 237  LEU   A CG  1 
ATOM   1148  C  CD1 . LEU   A 1 168 ? 19.241  51.056  -8.100  1.00 86.53  ? 237  LEU   A CD1 1 
ATOM   1149  C  CD2 . LEU   A 1 168 ? 21.149  52.027  -7.081  1.00 83.32  ? 237  LEU   A CD2 1 
ATOM   1150  N  N   . THR   A 1 169 ? 20.247  54.099  -12.416 1.00 88.11  ? 238  THR   A N   1 
ATOM   1151  C  CA  . THR   A 1 169 ? 21.012  54.574  -13.553 1.00 83.54  ? 238  THR   A CA  1 
ATOM   1152  C  C   . THR   A 1 169 ? 20.219  55.684  -14.234 1.00 82.28  ? 238  THR   A C   1 
ATOM   1153  O  O   . THR   A 1 169 ? 19.199  56.155  -13.720 1.00 83.61  ? 238  THR   A O   1 
ATOM   1154  C  CB  . THR   A 1 169 ? 21.334  53.436  -14.518 1.00 78.70  ? 238  THR   A CB  1 
ATOM   1155  O  OG1 . THR   A 1 169 ? 20.130  53.046  -15.189 1.00 83.23  ? 238  THR   A OG1 1 
ATOM   1156  C  CG2 . THR   A 1 169 ? 21.900  52.244  -13.786 1.00 79.34  ? 238  THR   A CG2 1 
ATOM   1157  N  N   . SER   A 1 170 ? 20.716  56.133  -15.383 1.00 78.37  ? 239  SER   A N   1 
ATOM   1158  C  CA  . SER   A 1 170 ? 20.129  57.240  -16.117 1.00 80.20  ? 239  SER   A CA  1 
ATOM   1159  C  C   . SER   A 1 170 ? 19.322  56.769  -17.315 1.00 78.68  ? 239  SER   A C   1 
ATOM   1160  O  O   . SER   A 1 170 ? 18.863  57.591  -18.110 1.00 79.50  ? 239  SER   A O   1 
ATOM   1161  C  CB  . SER   A 1 170 ? 21.225  58.215  -16.562 1.00 79.17  ? 239  SER   A CB  1 
ATOM   1162  O  OG  . SER   A 1 170 ? 22.403  57.490  -16.905 1.00 81.34  ? 239  SER   A OG  1 
ATOM   1163  N  N   . TRP   A 1 171 ? 19.125  55.467  -17.443 1.00 77.23  ? 240  TRP   A N   1 
ATOM   1164  C  CA  . TRP   A 1 171 ? 18.398  54.859  -18.536 1.00 75.62  ? 240  TRP   A CA  1 
ATOM   1165  C  C   . TRP   A 1 171 ? 17.248  54.039  -17.976 1.00 79.28  ? 240  TRP   A C   1 
ATOM   1166  O  O   . TRP   A 1 171 ? 17.306  53.603  -16.817 1.00 85.26  ? 240  TRP   A O   1 
ATOM   1167  C  CB  . TRP   A 1 171 ? 19.335  53.969  -19.370 1.00 76.68  ? 240  TRP   A CB  1 
ATOM   1168  C  CG  . TRP   A 1 171 ? 20.345  54.742  -20.200 1.00 79.90  ? 240  TRP   A CG  1 
ATOM   1169  C  CD1 . TRP   A 1 171 ? 21.702  54.549  -20.249 1.00 77.55  ? 240  TRP   A CD1 1 
ATOM   1170  C  CD2 . TRP   A 1 171 ? 20.066  55.817  -21.101 1.00 82.22  ? 240  TRP   A CD2 1 
ATOM   1171  N  NE1 . TRP   A 1 171 ? 22.276  55.433  -21.124 1.00 78.00  ? 240  TRP   A NE1 1 
ATOM   1172  C  CE2 . TRP   A 1 171 ? 21.294  56.224  -21.659 1.00 84.99  ? 240  TRP   A CE2 1 
ATOM   1173  C  CE3 . TRP   A 1 171 ? 18.896  56.476  -21.491 1.00 81.91  ? 240  TRP   A CE3 1 
ATOM   1174  C  CZ2 . TRP   A 1 171 ? 21.379  57.263  -22.583 1.00 92.12  ? 240  TRP   A CZ2 1 
ATOM   1175  C  CZ3 . TRP   A 1 171 ? 18.983  57.506  -22.397 1.00 84.69  ? 240  TRP   A CZ3 1 
ATOM   1176  C  CH2 . TRP   A 1 171 ? 20.213  57.892  -22.939 1.00 92.42  ? 240  TRP   A CH2 1 
ATOM   1177  N  N   . PRO   A 1 172 ? 16.177  53.825  -18.748 1.00 79.46  ? 241  PRO   A N   1 
ATOM   1178  C  CA  . PRO   A 1 172 ? 15.025  53.074  -18.248 1.00 80.25  ? 241  PRO   A CA  1 
ATOM   1179  C  C   . PRO   A 1 172 ? 15.199  51.580  -18.472 1.00 77.06  ? 241  PRO   A C   1 
ATOM   1180  O  O   . PRO   A 1 172 ? 16.107  51.133  -19.168 1.00 77.15  ? 241  PRO   A O   1 
ATOM   1181  C  CB  . PRO   A 1 172 ? 13.877  53.598  -19.113 1.00 80.41  ? 241  PRO   A CB  1 
ATOM   1182  C  CG  . PRO   A 1 172 ? 14.519  53.794  -20.411 1.00 80.64  ? 241  PRO   A CG  1 
ATOM   1183  C  CD  . PRO   A 1 172 ? 15.960  54.240  -20.137 1.00 83.38  ? 241  PRO   A CD  1 
ATOM   1184  N  N   . ARG   A 1 173 ? 14.280  50.815  -17.872 1.00 79.73  ? 242  ARG   A N   1 
ATOM   1185  C  CA  . ARG   A 1 173 ? 14.338  49.357  -17.966 1.00 81.47  ? 242  ARG   A CA  1 
ATOM   1186  C  C   . ARG   A 1 173 ? 14.188  48.871  -19.413 1.00 81.85  ? 242  ARG   A C   1 
ATOM   1187  O  O   . ARG   A 1 173 ? 14.931  47.979  -19.857 1.00 80.18  ? 242  ARG   A O   1 
ATOM   1188  C  CB  . ARG   A 1 173 ? 13.256  48.745  -17.080 1.00 81.76  ? 242  ARG   A CB  1 
ATOM   1189  C  CG  . ARG   A 1 173 ? 13.443  48.981  -15.598 1.00 84.95  ? 242  ARG   A CG  1 
ATOM   1190  C  CD  . ARG   A 1 173 ? 12.441  48.161  -14.813 1.00 84.85  ? 242  ARG   A CD  1 
ATOM   1191  N  NE  . ARG   A 1 173 ? 11.344  47.723  -15.675 1.00 93.79  ? 242  ARG   A NE  1 
ATOM   1192  C  CZ  . ARG   A 1 173 ? 10.055  47.978  -15.465 1.00 98.19  ? 242  ARG   A CZ  1 
ATOM   1193  N  NH1 . ARG   A 1 173 ? 9.654   48.699  -14.423 1.00 99.73  ? 242  ARG   A NH1 1 
ATOM   1194  N  NH2 . ARG   A 1 173 ? 9.143   47.477  -16.308 1.00 89.23  ? 242  ARG   A NH2 1 
ATOM   1195  N  N   . TRP   A 1 174 ? 13.234  49.432  -20.165 1.00 80.77  ? 243  TRP   A N   1 
ATOM   1196  C  CA  . TRP   A 1 174 ? 12.996  48.942  -21.517 1.00 76.87  ? 243  TRP   A CA  1 
ATOM   1197  C  C   . TRP   A 1 174 ? 14.192  49.159  -22.446 1.00 78.57  ? 243  TRP   A C   1 
ATOM   1198  O  O   . TRP   A 1 174 ? 14.305  48.451  -23.455 1.00 81.90  ? 243  TRP   A O   1 
ATOM   1199  C  CB  . TRP   A 1 174 ? 11.723  49.575  -22.102 1.00 78.28  ? 243  TRP   A CB  1 
ATOM   1200  C  CG  . TRP   A 1 174 ? 11.657  51.090  -22.074 1.00 82.10  ? 243  TRP   A CG  1 
ATOM   1201  C  CD1 . TRP   A 1 174 ? 11.014  51.862  -21.157 1.00 81.96  ? 243  TRP   A CD1 1 
ATOM   1202  C  CD2 . TRP   A 1 174 ? 12.236  52.003  -23.024 1.00 84.52  ? 243  TRP   A CD2 1 
ATOM   1203  N  NE1 . TRP   A 1 174 ? 11.169  53.195  -21.456 1.00 81.72  ? 243  TRP   A NE1 1 
ATOM   1204  C  CE2 . TRP   A 1 174 ? 11.915  53.306  -22.598 1.00 81.55  ? 243  TRP   A CE2 1 
ATOM   1205  C  CE3 . TRP   A 1 174 ? 13.004  51.841  -24.191 1.00 83.60  ? 243  TRP   A CE3 1 
ATOM   1206  C  CZ2 . TRP   A 1 174 ? 12.331  54.436  -23.291 1.00 83.68  ? 243  TRP   A CZ2 1 
ATOM   1207  C  CZ3 . TRP   A 1 174 ? 13.421  52.967  -24.877 1.00 81.06  ? 243  TRP   A CZ3 1 
ATOM   1208  C  CH2 . TRP   A 1 174 ? 13.084  54.246  -24.428 1.00 84.56  ? 243  TRP   A CH2 1 
ATOM   1209  N  N   . LEU   A 1 175 ? 15.086  50.106  -22.148 1.00 78.33  ? 244  LEU   A N   1 
ATOM   1210  C  CA  . LEU   A 1 175 ? 16.323  50.161  -22.915 1.00 76.14  ? 244  LEU   A CA  1 
ATOM   1211  C  C   . LEU   A 1 175 ? 17.219  48.994  -22.557 1.00 79.43  ? 244  LEU   A C   1 
ATOM   1212  O  O   . LEU   A 1 175 ? 17.751  48.334  -23.452 1.00 82.48  ? 244  LEU   A O   1 
ATOM   1213  C  CB  . LEU   A 1 175 ? 17.064  51.471  -22.689 1.00 76.03  ? 244  LEU   A CB  1 
ATOM   1214  C  CG  . LEU   A 1 175 ? 18.382  51.663  -23.448 1.00 77.83  ? 244  LEU   A CG  1 
ATOM   1215  C  CD1 . LEU   A 1 175 ? 18.221  51.368  -24.932 1.00 81.33  ? 244  LEU   A CD1 1 
ATOM   1216  C  CD2 . LEU   A 1 175 ? 18.899  53.079  -23.253 1.00 83.63  ? 244  LEU   A CD2 1 
ATOM   1217  N  N   . TYR   A 1 176 ? 17.372  48.701  -21.257 1.00 79.29  ? 245  TYR   A N   1 
ATOM   1218  C  CA  . TYR   A 1 176 ? 18.233  47.596  -20.831 1.00 80.71  ? 245  TYR   A CA  1 
ATOM   1219  C  C   . TYR   A 1 176 ? 17.776  46.267  -21.408 1.00 80.40  ? 245  TYR   A C   1 
ATOM   1220  O  O   . TYR   A 1 176 ? 18.596  45.351  -21.558 1.00 81.48  ? 245  TYR   A O   1 
ATOM   1221  C  CB  . TYR   A 1 176 ? 18.300  47.521  -19.295 1.00 78.84  ? 245  TYR   A CB  1 
ATOM   1222  C  CG  . TYR   A 1 176 ? 19.161  48.606  -18.719 1.00 76.51  ? 245  TYR   A CG  1 
ATOM   1223  C  CD1 . TYR   A 1 176 ? 20.524  48.654  -18.989 1.00 74.95  ? 245  TYR   A CD1 1 
ATOM   1224  C  CD2 . TYR   A 1 176 ? 18.610  49.608  -17.942 1.00 78.90  ? 245  TYR   A CD2 1 
ATOM   1225  C  CE1 . TYR   A 1 176 ? 21.317  49.674  -18.495 1.00 76.11  ? 245  TYR   A CE1 1 
ATOM   1226  C  CE2 . TYR   A 1 176 ? 19.390  50.631  -17.435 1.00 77.69  ? 245  TYR   A CE2 1 
ATOM   1227  C  CZ  . TYR   A 1 176 ? 20.744  50.658  -17.716 1.00 77.50  ? 245  TYR   A CZ  1 
ATOM   1228  O  OH  . TYR   A 1 176 ? 21.525  51.670  -17.216 1.00 78.53  ? 245  TYR   A OH  1 
ATOM   1229  N  N   . SER   A 1 177 ? 16.488  46.152  -21.744 1.00 77.62  ? 246  SER   A N   1 
ATOM   1230  C  CA  . SER   A 1 177 ? 15.989  44.932  -22.354 1.00 79.72  ? 246  SER   A CA  1 
ATOM   1231  C  C   . SER   A 1 177 ? 16.412  44.820  -23.819 1.00 81.30  ? 246  SER   A C   1 
ATOM   1232  O  O   . SER   A 1 177 ? 16.625  43.713  -24.326 1.00 77.70  ? 246  SER   A O   1 
ATOM   1233  C  CB  . SER   A 1 177 ? 14.464  44.880  -22.210 1.00 81.08  ? 246  SER   A CB  1 
ATOM   1234  O  OG  . SER   A 1 177 ? 13.951  43.565  -22.454 1.00 98.10  ? 246  SER   A OG  1 
ATOM   1235  N  N   . LEU   A 1 178 ? 16.565  45.942  -24.510 1.00 81.14  ? 247  LEU   A N   1 
ATOM   1236  C  CA  . LEU   A 1 178 ? 17.012  45.857  -25.887 1.00 76.80  ? 247  LEU   A CA  1 
ATOM   1237  C  C   . LEU   A 1 178 ? 18.472  45.459  -26.003 1.00 77.29  ? 247  LEU   A C   1 
ATOM   1238  O  O   . LEU   A 1 178 ? 18.975  45.429  -27.125 1.00 83.09  ? 247  LEU   A O   1 
ATOM   1239  C  CB  . LEU   A 1 178 ? 16.782  47.188  -26.603 1.00 75.84  ? 247  LEU   A CB  1 
ATOM   1240  C  CG  . LEU   A 1 178 ? 15.413  47.856  -26.523 1.00 76.64  ? 247  LEU   A CG  1 
ATOM   1241  C  CD1 . LEU   A 1 178 ? 15.533  49.234  -27.122 1.00 83.69  ? 247  LEU   A CD1 1 
ATOM   1242  C  CD2 . LEU   A 1 178 ? 14.344  47.057  -27.225 1.00 79.79  ? 247  LEU   A CD2 1 
ATOM   1243  N  N   . TYR   A 1 179 ? 19.176  45.184  -24.902 1.00 77.43  ? 248  TYR   A N   1 
ATOM   1244  C  CA  . TYR   A 1 179 ? 20.536  44.663  -24.973 1.00 76.55  ? 248  TYR   A CA  1 
ATOM   1245  C  C   . TYR   A 1 179 ? 20.682  43.416  -24.124 1.00 84.31  ? 248  TYR   A C   1 
ATOM   1246  O  O   . TYR   A 1 179 ? 21.810  42.989  -23.857 1.00 88.12  ? 248  TYR   A O   1 
ATOM   1247  C  CB  . TYR   A 1 179 ? 21.575  45.700  -24.525 1.00 76.15  ? 248  TYR   A CB  1 
ATOM   1248  C  CG  . TYR   A 1 179 ? 21.671  46.903  -25.433 1.00 77.32  ? 248  TYR   A CG  1 
ATOM   1249  C  CD1 . TYR   A 1 179 ? 20.833  47.984  -25.254 1.00 78.23  ? 248  TYR   A CD1 1 
ATOM   1250  C  CD2 . TYR   A 1 179 ? 22.599  46.958  -26.466 1.00 78.09  ? 248  TYR   A CD2 1 
ATOM   1251  C  CE1 . TYR   A 1 179 ? 20.905  49.085  -26.079 1.00 84.24  ? 248  TYR   A CE1 1 
ATOM   1252  C  CE2 . TYR   A 1 179 ? 22.683  48.063  -27.303 1.00 82.85  ? 248  TYR   A CE2 1 
ATOM   1253  C  CZ  . TYR   A 1 179 ? 21.830  49.126  -27.107 1.00 86.95  ? 248  TYR   A CZ  1 
ATOM   1254  O  OH  . TYR   A 1 179 ? 21.889  50.237  -27.938 1.00 94.56  ? 248  TYR   A OH  1 
ATOM   1255  N  N   . ASP   A 1 180 ? 19.584  42.840  -23.662 1.00 91.17  ? 249  ASP   A N   1 
ATOM   1256  C  CA  . ASP   A 1 180 ? 19.657  41.690  -22.778 1.00 90.20  ? 249  ASP   A CA  1 
ATOM   1257  C  C   . ASP   A 1 180 ? 19.563  40.431  -23.629 1.00 90.23  ? 249  ASP   A C   1 
ATOM   1258  O  O   . ASP   A 1 180 ? 18.532  40.179  -24.265 1.00 92.04  ? 249  ASP   A O   1 
ATOM   1259  C  CB  . ASP   A 1 180 ? 18.552  41.754  -21.734 1.00 89.40  ? 249  ASP   A CB  1 
ATOM   1260  C  CG  . ASP   A 1 180 ? 18.435  40.482  -20.959 1.00 93.80  ? 249  ASP   A CG  1 
ATOM   1261  O  OD1 . ASP   A 1 180 ? 19.444  40.072  -20.332 1.00 98.41  ? 249  ASP   A OD1 1 
ATOM   1262  O  OD2 . ASP   A 1 180 ? 17.334  39.891  -20.988 1.00 96.04  ? 249  ASP   A OD2 1 
ATOM   1263  N  N   . ALA   A 1 181 ? 20.653  39.657  -23.665 1.00 90.16  ? 250  ALA   A N   1 
ATOM   1264  C  CA  . ALA   A 1 181 ? 20.718  38.495  -24.539 1.00 87.53  ? 250  ALA   A CA  1 
ATOM   1265  C  C   . ALA   A 1 181 ? 19.482  37.626  -24.400 1.00 94.78  ? 250  ALA   A C   1 
ATOM   1266  O  O   . ALA   A 1 181 ? 18.889  37.206  -25.393 1.00 96.19  ? 250  ALA   A O   1 
ATOM   1267  C  CB  . ALA   A 1 181 ? 21.969  37.689  -24.243 1.00 92.64  ? 250  ALA   A CB  1 
ATOM   1268  N  N   . GLU   A 1 182 ? 19.047  37.377  -23.170 1.00 119.10 ? 251  GLU   A N   1 
ATOM   1269  C  CA  . GLU   A 1 182 ? 17.931  36.457  -22.987 1.00 120.25 ? 251  GLU   A CA  1 
ATOM   1270  C  C   . GLU   A 1 182 ? 16.648  37.008  -23.601 1.00 118.83 ? 251  GLU   A C   1 
ATOM   1271  O  O   . GLU   A 1 182 ? 15.859  36.248  -24.173 1.00 121.03 ? 251  GLU   A O   1 
ATOM   1272  C  CB  . GLU   A 1 182 ? 17.745  36.143  -21.505 1.00 122.48 ? 251  GLU   A CB  1 
ATOM   1273  C  CG  . GLU   A 1 182 ? 19.065  35.915  -20.752 1.00 128.68 ? 251  GLU   A CG  1 
ATOM   1274  C  CD  . GLU   A 1 182 ? 19.742  34.554  -21.064 1.00 142.74 ? 251  GLU   A CD  1 
ATOM   1275  O  OE1 . GLU   A 1 182 ? 19.016  33.531  -21.214 1.00 142.33 ? 251  GLU   A OE1 1 
ATOM   1276  O  OE2 . GLU   A 1 182 ? 21.004  34.510  -21.128 1.00 143.61 ? 251  GLU   A OE2 1 
ATOM   1277  N  N   . THR   A 1 183 ? 16.427  38.325  -23.515 1.00 97.13  ? 252  THR   A N   1 
ATOM   1278  C  CA  . THR   A 1 183 ? 15.224  38.902  -24.107 1.00 88.46  ? 252  THR   A CA  1 
ATOM   1279  C  C   . THR   A 1 183 ? 15.298  38.848  -25.615 1.00 88.76  ? 252  THR   A C   1 
ATOM   1280  O  O   . THR   A 1 183 ? 14.321  38.487  -26.288 1.00 88.81  ? 252  THR   A O   1 
ATOM   1281  C  CB  . THR   A 1 183 ? 15.035  40.352  -23.672 1.00 87.16  ? 252  THR   A CB  1 
ATOM   1282  O  OG1 . THR   A 1 183 ? 14.916  40.434  -22.249 1.00 90.63  ? 252  THR   A OG1 1 
ATOM   1283  C  CG2 . THR   A 1 183 ? 13.772  40.935  -24.323 1.00 87.52  ? 252  THR   A CG2 1 
ATOM   1284  N  N   . LEU   A 1 184 ? 16.451  39.239  -26.161 1.00 88.19  ? 253  LEU   A N   1 
ATOM   1285  C  CA  . LEU   A 1 184 ? 16.652  39.195  -27.602 1.00 84.57  ? 253  LEU   A CA  1 
ATOM   1286  C  C   . LEU   A 1 184 ? 16.391  37.798  -28.143 1.00 81.51  ? 253  LEU   A C   1 
ATOM   1287  O  O   . LEU   A 1 184 ? 15.542  37.618  -29.022 1.00 83.84  ? 253  LEU   A O   1 
ATOM   1288  C  CB  . LEU   A 1 184 ? 18.061  39.673  -27.956 1.00 78.85  ? 253  LEU   A CB  1 
ATOM   1289  C  CG  . LEU   A 1 184 ? 18.350  41.146  -27.657 1.00 75.66  ? 253  LEU   A CG  1 
ATOM   1290  C  CD1 . LEU   A 1 184 ? 19.774  41.448  -27.994 1.00 75.82  ? 253  LEU   A CD1 1 
ATOM   1291  C  CD2 . LEU   A 1 184 ? 17.418  42.086  -28.393 1.00 73.23  ? 253  LEU   A CD2 1 
ATOM   1292  N  N   . MET   A 1 185 ? 17.074  36.786  -27.600 1.00 81.23  ? 254  MET   A N   1 
ATOM   1293  C  CA  . MET   A 1 185 ? 16.912  35.431  -28.112 1.00 78.08  ? 254  MET   A CA  1 
ATOM   1294  C  C   . MET   A 1 185 ? 15.456  35.001  -28.139 1.00 79.95  ? 254  MET   A C   1 
ATOM   1295  O  O   . MET   A 1 185 ? 15.063  34.224  -29.015 1.00 79.97  ? 254  MET   A O   1 
ATOM   1296  C  CB  . MET   A 1 185 ? 17.728  34.449  -27.288 1.00 80.76  ? 254  MET   A CB  1 
ATOM   1297  C  CG  . MET   A 1 185 ? 19.213  34.561  -27.541 1.00 81.25  ? 254  MET   A CG  1 
ATOM   1298  S  SD  . MET   A 1 185 ? 20.292  33.641  -26.399 1.00 81.88  ? 254  MET   A SD  1 
ATOM   1299  C  CE  . MET   A 1 185 ? 19.396  32.081  -26.271 1.00 89.26  ? 254  MET   A CE  1 
ATOM   1300  N  N   . ASP   A 1 186 ? 14.629  35.499  -27.210 1.00 82.77  ? 255  ASP   A N   1 
ATOM   1301  C  CA  . ASP   A 1 186 ? 13.228  35.089  -27.253 1.00 80.73  ? 255  ASP   A CA  1 
ATOM   1302  C  C   . ASP   A 1 186 ? 12.476  35.825  -28.335 1.00 78.84  ? 255  ASP   A C   1 
ATOM   1303  O  O   . ASP   A 1 186 ? 11.625  35.235  -29.002 1.00 80.10  ? 255  ASP   A O   1 
ATOM   1304  C  CB  . ASP   A 1 186 ? 12.506  35.309  -25.931 1.00 83.14  ? 255  ASP   A CB  1 
ATOM   1305  C  CG  . ASP   A 1 186 ? 11.042  34.863  -26.003 1.00 82.18  ? 255  ASP   A CG  1 
ATOM   1306  O  OD1 . ASP   A 1 186 ? 10.804  33.634  -26.018 1.00 80.50  ? 255  ASP   A OD1 1 
ATOM   1307  O  OD2 . ASP   A 1 186 ? 10.139  35.732  -26.067 1.00 79.15  ? 255  ASP   A OD2 1 
ATOM   1308  N  N   . ARG   A 1 187 ? 12.749  37.118  -28.503 1.00 81.38  ? 256  ARG   A N   1 
ATOM   1309  C  CA  . ARG   A 1 187 ? 12.141  37.850  -29.605 1.00 83.39  ? 256  ARG   A CA  1 
ATOM   1310  C  C   . ARG   A 1 187 ? 12.460  37.192  -30.952 1.00 81.53  ? 256  ARG   A C   1 
ATOM   1311  O  O   . ARG   A 1 187 ? 11.576  37.025  -31.804 1.00 83.04  ? 256  ARG   A O   1 
ATOM   1312  C  CB  . ARG   A 1 187 ? 12.603  39.302  -29.567 1.00 82.89  ? 256  ARG   A CB  1 
ATOM   1313  C  CG  . ARG   A 1 187 ? 12.004  40.086  -28.448 1.00 80.97  ? 256  ARG   A CG  1 
ATOM   1314  C  CD  . ARG   A 1 187 ? 12.828  41.343  -28.219 1.00 87.38  ? 256  ARG   A CD  1 
ATOM   1315  N  NE  . ARG   A 1 187 ? 12.769  42.295  -29.324 1.00 84.38  ? 256  ARG   A NE  1 
ATOM   1316  C  CZ  . ARG   A 1 187 ? 13.571  43.340  -29.423 1.00 78.79  ? 256  ARG   A CZ  1 
ATOM   1317  N  NH1 . ARG   A 1 187 ? 14.514  43.561  -28.526 1.00 84.81  ? 256  ARG   A NH1 1 
ATOM   1318  N  NH2 . ARG   A 1 187 ? 13.444  44.162  -30.458 1.00 79.01  ? 256  ARG   A NH2 1 
ATOM   1319  N  N   . ILE   A 1 188 ? 13.724  36.798  -31.153 1.00 76.61  ? 257  ILE   A N   1 
ATOM   1320  C  CA  . ILE   A 1 188 ? 14.100  36.064  -32.359 1.00 74.37  ? 257  ILE   A CA  1 
ATOM   1321  C  C   . ILE   A 1 188 ? 13.322  34.758  -32.451 1.00 81.08  ? 257  ILE   A C   1 
ATOM   1322  O  O   . ILE   A 1 188 ? 12.695  34.458  -33.476 1.00 83.06  ? 257  ILE   A O   1 
ATOM   1323  C  CB  . ILE   A 1 188 ? 15.614  35.808  -32.368 1.00 73.21  ? 257  ILE   A CB  1 
ATOM   1324  C  CG1 . ILE   A 1 188 ? 16.376  37.127  -32.468 1.00 76.12  ? 257  ILE   A CG1 1 
ATOM   1325  C  CG2 . ILE   A 1 188 ? 15.980  34.811  -33.444 1.00 74.02  ? 257  ILE   A CG2 1 
ATOM   1326  C  CD1 . ILE   A 1 188 ? 17.874  36.964  -32.338 1.00 79.96  ? 257  ILE   A CD1 1 
ATOM   1327  N  N   . LYS   A 1 189 ? 13.356  33.957  -31.378 1.00 81.55  ? 258  LYS   A N   1 
ATOM   1328  C  CA  . LYS   A 1 189 ? 12.679  32.662  -31.376 1.00 78.40  ? 258  LYS   A CA  1 
ATOM   1329  C  C   . LYS   A 1 189 ? 11.165  32.781  -31.557 1.00 78.91  ? 258  LYS   A C   1 
ATOM   1330  O  O   . LYS   A 1 189 ? 10.537  31.810  -31.982 1.00 83.80  ? 258  LYS   A O   1 
ATOM   1331  C  CB  . LYS   A 1 189 ? 13.008  31.895  -30.076 1.00 75.16  ? 258  LYS   A CB  1 
ATOM   1332  N  N   . LYS   A 1 190 ? 10.544  33.923  -31.234 1.00 79.28  ? 259  LYS   A N   1 
ATOM   1333  C  CA  . LYS   A 1 190 ? 9.100   34.015  -31.451 1.00 82.05  ? 259  LYS   A CA  1 
ATOM   1334  C  C   . LYS   A 1 190 ? 8.792   34.190  -32.924 1.00 85.41  ? 259  LYS   A C   1 
ATOM   1335  O  O   . LYS   A 1 190 ? 7.876   33.553  -33.457 1.00 87.80  ? 259  LYS   A O   1 
ATOM   1336  C  CB  . LYS   A 1 190 ? 8.473   35.162  -30.651 1.00 81.43  ? 259  LYS   A CB  1 
ATOM   1337  C  CG  . LYS   A 1 190 ? 8.337   34.903  -29.148 1.00 80.47  ? 259  LYS   A CG  1 
ATOM   1338  C  CD  . LYS   A 1 190 ? 7.698   33.545  -28.833 1.00 83.35  ? 259  LYS   A CD  1 
ATOM   1339  C  CE  . LYS   A 1 190 ? 8.168   33.003  -27.481 1.00 86.91  ? 259  LYS   A CE  1 
ATOM   1340  N  NZ  . LYS   A 1 190 ? 7.595   31.675  -27.128 1.00 97.06  ? 259  LYS   A NZ  1 
ATOM   1341  N  N   . GLN   A 1 191 ? 9.555   35.054  -33.593 1.00 85.74  ? 260  GLN   A N   1 
ATOM   1342  C  CA  . GLN   A 1 191 ? 9.388   35.240  -35.027 1.00 86.32  ? 260  GLN   A CA  1 
ATOM   1343  C  C   . GLN   A 1 191 ? 9.703   33.960  -35.782 1.00 87.55  ? 260  GLN   A C   1 
ATOM   1344  O  O   . GLN   A 1 191 ? 8.990   33.589  -36.723 1.00 90.31  ? 260  GLN   A O   1 
ATOM   1345  C  CB  . GLN   A 1 191 ? 10.284  36.375  -35.499 1.00 86.81  ? 260  GLN   A CB  1 
ATOM   1346  C  CG  . GLN   A 1 191 ? 10.149  37.633  -34.677 1.00 87.59  ? 260  GLN   A CG  1 
ATOM   1347  C  CD  . GLN   A 1 191 ? 10.723  38.808  -35.409 1.00 91.54  ? 260  GLN   A CD  1 
ATOM   1348  O  OE1 . GLN   A 1 191 ? 10.818  38.799  -36.641 1.00 93.13  ? 260  GLN   A OE1 1 
ATOM   1349  N  NE2 . GLN   A 1 191 ? 11.124  39.829  -34.663 1.00 90.60  ? 260  GLN   A NE2 1 
ATOM   1350  N  N   . LEU   A 1 192 ? 10.778  33.275  -35.383 1.00 86.26  ? 261  LEU   A N   1 
ATOM   1351  C  CA  . LEU   A 1 192 ? 11.070  31.964  -35.939 1.00 83.86  ? 261  LEU   A CA  1 
ATOM   1352  C  C   . LEU   A 1 192 ? 9.878   31.023  -35.808 1.00 90.06  ? 261  LEU   A C   1 
ATOM   1353  O  O   . LEU   A 1 192 ? 9.677   30.160  -36.668 1.00 95.93  ? 261  LEU   A O   1 
ATOM   1354  C  CB  . LEU   A 1 192 ? 12.309  31.396  -35.251 1.00 76.60  ? 261  LEU   A CB  1 
ATOM   1355  C  CG  . LEU   A 1 192 ? 13.596  31.969  -35.829 1.00 76.65  ? 261  LEU   A CG  1 
ATOM   1356  C  CD1 . LEU   A 1 192 ? 14.812  31.422  -35.119 1.00 75.10  ? 261  LEU   A CD1 1 
ATOM   1357  C  CD2 . LEU   A 1 192 ? 13.652  31.635  -37.300 1.00 82.86  ? 261  LEU   A CD2 1 
ATOM   1358  N  N   . ARG   A 1 193 ? 9.054   31.201  -34.767 1.00 91.77  ? 262  ARG   A N   1 
ATOM   1359  C  CA  . ARG   A 1 193 ? 7.916   30.315  -34.548 1.00 94.99  ? 262  ARG   A CA  1 
ATOM   1360  C  C   . ARG   A 1 193 ? 6.805   30.563  -35.562 1.00 97.97  ? 262  ARG   A C   1 
ATOM   1361  O  O   . ARG   A 1 193 ? 6.057   29.639  -35.897 1.00 103.17 ? 262  ARG   A O   1 
ATOM   1362  C  CB  . ARG   A 1 193 ? 7.405   30.475  -33.114 1.00 97.10  ? 262  ARG   A CB  1 
ATOM   1363  N  N   . GLU   A 1 194 ? 6.694   31.783  -36.085 1.00 92.47  ? 263  GLU   A N   1 
ATOM   1364  C  CA  . GLU   A 1 194 ? 5.743   32.016  -37.163 1.00 91.59  ? 263  GLU   A CA  1 
ATOM   1365  C  C   . GLU   A 1 194 ? 6.115   31.274  -38.440 1.00 94.31  ? 263  GLU   A C   1 
ATOM   1366  O  O   . GLU   A 1 194 ? 5.247   31.061  -39.291 1.00 99.93  ? 263  GLU   A O   1 
ATOM   1367  C  CB  . GLU   A 1 194 ? 5.641   33.500  -37.478 1.00 91.39  ? 263  GLU   A CB  1 
ATOM   1368  C  CG  . GLU   A 1 194 ? 5.428   34.385  -36.291 1.00 93.88  ? 263  GLU   A CG  1 
ATOM   1369  C  CD  . GLU   A 1 194 ? 5.992   35.761  -36.543 1.00 98.70  ? 263  GLU   A CD  1 
ATOM   1370  O  OE1 . GLU   A 1 194 ? 6.620   35.946  -37.621 1.00 98.73  ? 263  GLU   A OE1 1 
ATOM   1371  O  OE2 . GLU   A 1 194 ? 5.820   36.648  -35.671 1.00 101.77 ? 263  GLU   A OE2 1 
ATOM   1372  N  N   . TRP   A 1 195 ? 7.384   30.910  -38.617 1.00 91.20  ? 264  TRP   A N   1 
ATOM   1373  C  CA  . TRP   A 1 195 ? 7.769   30.177  -39.819 1.00 91.00  ? 264  TRP   A CA  1 
ATOM   1374  C  C   . TRP   A 1 195 ? 7.602   28.681  -39.628 1.00 99.24  ? 264  TRP   A C   1 
ATOM   1375  O  O   . TRP   A 1 195 ? 7.028   27.996  -40.481 1.00 102.32 ? 264  TRP   A O   1 
ATOM   1376  C  CB  . TRP   A 1 195 ? 9.211   30.490  -40.208 1.00 88.16  ? 264  TRP   A CB  1 
ATOM   1377  C  CG  . TRP   A 1 195 ? 9.451   31.924  -40.504 1.00 85.88  ? 264  TRP   A CG  1 
ATOM   1378  C  CD1 . TRP   A 1 195 ? 8.509   32.902  -40.626 1.00 86.25  ? 264  TRP   A CD1 1 
ATOM   1379  C  CD2 . TRP   A 1 195 ? 10.716  32.555  -40.708 1.00 82.54  ? 264  TRP   A CD2 1 
ATOM   1380  N  NE1 . TRP   A 1 195 ? 9.110   34.106  -40.887 1.00 86.21  ? 264  TRP   A NE1 1 
ATOM   1381  C  CE2 . TRP   A 1 195 ? 10.468  33.918  -40.944 1.00 84.82  ? 264  TRP   A CE2 1 
ATOM   1382  C  CE3 . TRP   A 1 195 ? 12.033  32.103  -40.710 1.00 84.59  ? 264  TRP   A CE3 1 
ATOM   1383  C  CZ2 . TRP   A 1 195 ? 11.494  34.834  -41.184 1.00 87.01  ? 264  TRP   A CZ2 1 
ATOM   1384  C  CZ3 . TRP   A 1 195 ? 13.055  33.023  -40.954 1.00 83.00  ? 264  TRP   A CZ3 1 
ATOM   1385  C  CH2 . TRP   A 1 195 ? 12.779  34.367  -41.185 1.00 80.25  ? 264  TRP   A CH2 1 
ATOM   1386  N  N   . ASP   A 1 196 ? 8.135   28.169  -38.517 1.00 105.98 ? 265  ASP   A N   1 
ATOM   1387  C  CA  . ASP   A 1 196 ? 8.038   26.713  -38.227 1.00 111.81 ? 265  ASP   A CA  1 
ATOM   1388  C  C   . ASP   A 1 196 ? 7.322   26.515  -36.896 1.00 117.24 ? 265  ASP   A C   1 
ATOM   1389  O  O   . ASP   A 1 196 ? 7.998   26.562  -35.852 1.00 120.20 ? 265  ASP   A O   1 
ATOM   1390  C  CB  . ASP   A 1 196 ? 9.399   26.040  -38.178 1.00 112.29 ? 265  ASP   A CB  1 
ATOM   1391  C  CG  . ASP   A 1 196 ? 9.382   24.520  -38.251 1.00 116.26 ? 265  ASP   A CG  1 
ATOM   1392  O  OD1 . ASP   A 1 196 ? 8.283   23.950  -38.405 1.00 118.15 ? 265  ASP   A OD1 1 
ATOM   1393  O  OD2 . ASP   A 1 196 ? 10.470  23.918  -38.157 1.00 118.36 ? 265  ASP   A OD2 1 
ATOM   1394  N  N   . GLU   A 1 197 ? 6.008   26.309  -36.934 1.00 120.30 ? 266  GLU   A N   1 
ATOM   1395  C  CA  . GLU   A 1 197 ? 5.274   26.009  -35.682 1.00 127.87 ? 266  GLU   A CA  1 
ATOM   1396  C  C   . GLU   A 1 197 ? 5.869   24.643  -35.331 1.00 132.12 ? 266  GLU   A C   1 
ATOM   1397  O  O   . GLU   A 1 197 ? 5.438   23.641  -35.934 1.00 129.47 ? 266  GLU   A O   1 
ATOM   1398  C  CB  . GLU   A 1 197 ? 3.774   26.016  -35.964 1.00 129.04 ? 266  GLU   A CB  1 
ATOM   1399  C  CG  . GLU   A 1 197 ? 3.375   27.010  -37.051 1.00 126.67 ? 266  GLU   A CG  1 
ATOM   1400  C  CD  . GLU   A 1 197 ? 3.106   28.414  -36.540 1.00 128.45 ? 266  GLU   A CD  1 
ATOM   1401  O  OE1 . GLU   A 1 197 ? 2.842   28.565  -35.329 1.00 133.07 ? 266  GLU   A OE1 1 
ATOM   1402  O  OE2 . GLU   A 1 197 ? 3.161   29.358  -37.354 1.00 126.32 ? 266  GLU   A OE2 1 
ATOM   1403  N  N   . ASN   A 1 198 ? 6.821   24.611  -34.398 1.00 146.94 ? 267  ASN   A N   1 
ATOM   1404  C  CA  . ASN   A 1 198 ? 7.505   23.319  -34.117 1.00 151.20 ? 267  ASN   A CA  1 
ATOM   1405  C  C   . ASN   A 1 198 ? 8.379   23.483  -32.843 1.00 151.58 ? 267  ASN   A C   1 
ATOM   1406  O  O   . ASN   A 1 198 ? 8.204   24.483  -32.117 1.00 152.88 ? 267  ASN   A O   1 
ATOM   1407  C  CB  . ASN   A 1 198 ? 8.332   22.721  -35.225 1.00 150.02 ? 267  ASN   A CB  1 
ATOM   1408  C  CG  . ASN   A 1 198 ? 7.711   21.453  -35.756 1.00 154.68 ? 267  ASN   A CG  1 
ATOM   1409  O  OD1 . ASN   A 1 198 ? 6.834   21.507  -36.625 1.00 156.94 ? 267  ASN   A OD1 1 
ATOM   1410  N  ND2 . ASN   A 1 198 ? 8.149   20.309  -35.251 1.00 154.93 ? 267  ASN   A ND2 1 
ATOM   1411  N  N   . LEU   A 1 199 ? 9.280   22.525  -32.615 1.00 141.45 ? 268  LEU   A N   1 
ATOM   1412  C  CA  . LEU   A 1 199 ? 10.123  22.506  -31.421 1.00 138.24 ? 268  LEU   A CA  1 
ATOM   1413  C  C   . LEU   A 1 199 ? 10.492  23.970  -31.079 1.00 137.10 ? 268  LEU   A C   1 
ATOM   1414  O  O   . LEU   A 1 199 ? 11.053  24.655  -31.955 1.00 140.86 ? 268  LEU   A O   1 
ATOM   1415  C  CB  . LEU   A 1 199 ? 11.345  21.636  -31.673 1.00 134.92 ? 268  LEU   A CB  1 
ATOM   1416  C  CG  . LEU   A 1 199 ? 11.031  20.172  -31.999 1.00 142.78 ? 268  LEU   A CG  1 
ATOM   1417  C  CD1 . LEU   A 1 199 ? 12.278  19.402  -32.398 1.00 144.71 ? 268  LEU   A CD1 1 
ATOM   1418  C  CD2 . LEU   A 1 199 ? 10.325  19.492  -30.840 1.00 135.62 ? 268  LEU   A CD2 1 
ATOM   1419  N  N   . LYS   A 1 200 ? 10.179  24.407  -29.863 1.00 135.70 ? 269  LYS   A N   1 
ATOM   1420  C  CA  . LYS   A 1 200 ? 10.556  25.776  -29.436 1.00 134.65 ? 269  LYS   A CA  1 
ATOM   1421  C  C   . LYS   A 1 200 ? 11.328  25.430  -28.159 1.00 128.82 ? 269  LYS   A C   1 
ATOM   1422  O  O   . LYS   A 1 200 ? 10.824  25.714  -27.050 1.00 124.11 ? 269  LYS   A O   1 
ATOM   1423  C  CB  . LYS   A 1 200 ? 9.335   26.660  -29.159 1.00 137.41 ? 269  LYS   A CB  1 
ATOM   1424  N  N   . ASP   A 1 201 ? 12.503  24.829  -28.326 1.00 130.26 ? 270  ASP   A N   1 
ATOM   1425  C  CA  . ASP   A 1 201 ? 13.297  24.409  -27.147 1.00 132.14 ? 270  ASP   A CA  1 
ATOM   1426  C  C   . ASP   A 1 201 ? 14.655  23.938  -27.654 1.00 126.35 ? 270  ASP   A C   1 
ATOM   1427  O  O   . ASP   A 1 201 ? 15.352  24.733  -28.314 1.00 119.99 ? 270  ASP   A O   1 
ATOM   1428  C  CB  . ASP   A 1 201 ? 12.658  23.366  -26.248 1.00 129.28 ? 270  ASP   A CB  1 
ATOM   1429  N  N   . ASP   A 1 202 ? 14.994  22.679  -27.383 1.00 129.68 ? 271  ASP   A N   1 
ATOM   1430  C  CA  . ASP   A 1 202 ? 16.315  22.139  -27.794 1.00 130.31 ? 271  ASP   A CA  1 
ATOM   1431  C  C   . ASP   A 1 202 ? 16.619  22.465  -29.255 1.00 130.08 ? 271  ASP   A C   1 
ATOM   1432  O  O   . ASP   A 1 202 ? 17.811  22.466  -29.619 1.00 130.49 ? 271  ASP   A O   1 
ATOM   1433  C  CB  . ASP   A 1 202 ? 16.355  20.629  -27.637 1.00 133.85 ? 271  ASP   A CB  1 
ATOM   1434  N  N   . SER   A 1 203 ? 15.586  22.714  -30.059 1.00 123.45 ? 272  SER   A N   1 
ATOM   1435  C  CA  . SER   A 1 203 ? 15.772  23.089  -31.504 1.00 120.11 ? 272  SER   A CA  1 
ATOM   1436  C  C   . SER   A 1 203 ? 16.862  24.151  -31.649 1.00 114.89 ? 272  SER   A C   1 
ATOM   1437  O  O   . SER   A 1 203 ? 17.661  24.032  -32.597 1.00 110.08 ? 272  SER   A O   1 
ATOM   1438  C  CB  . SER   A 1 203 ? 14.505  23.713  -31.965 1.00 126.32 ? 272  SER   A CB  1 
ATOM   1439  O  OG  . SER   A 1 203 ? 13.829  24.360  -30.895 1.00 126.27 ? 272  SER   A OG  1 
ATOM   1440  N  N   . LEU   A 1 204 ? 16.870  25.158  -30.776 1.00 115.41 ? 273  LEU   A N   1 
ATOM   1441  C  CA  . LEU   A 1 204 ? 17.846  26.266  -30.911 1.00 104.88 ? 273  LEU   A CA  1 
ATOM   1442  C  C   . LEU   A 1 204 ? 18.709  26.206  -29.623 1.00 101.27 ? 273  LEU   A C   1 
ATOM   1443  O  O   . LEU   A 1 204 ? 18.237  25.663  -28.608 1.00 107.90 ? 273  LEU   A O   1 
ATOM   1444  C  CB  . LEU   A 1 204 ? 17.112  27.596  -31.011 1.00 99.38  ? 273  LEU   A CB  1 
ATOM   1445  C  CG  . LEU   A 1 204 ? 16.664  27.994  -32.419 1.00 92.98  ? 273  LEU   A CG  1 
ATOM   1446  C  CD1 . LEU   A 1 204 ? 15.440  28.882  -32.310 1.00 84.47  ? 273  LEU   A CD1 1 
ATOM   1447  C  CD2 . LEU   A 1 204 ? 17.786  28.717  -33.137 1.00 95.89  ? 273  LEU   A CD2 1 
ATOM   1448  N  N   . PRO   A 1 205 ? 19.943  26.745  -29.633 1.00 93.33  ? 274  PRO   A N   1 
ATOM   1449  C  CA  . PRO   A 1 205 ? 20.808  26.668  -28.469 1.00 94.09  ? 274  PRO   A CA  1 
ATOM   1450  C  C   . PRO   A 1 205 ? 20.392  27.577  -27.327 1.00 97.88  ? 274  PRO   A C   1 
ATOM   1451  O  O   . PRO   A 1 205 ? 19.430  28.349  -27.481 1.00 97.67  ? 274  PRO   A O   1 
ATOM   1452  C  CB  . PRO   A 1 205 ? 22.162  27.091  -29.049 1.00 94.84  ? 274  PRO   A CB  1 
ATOM   1453  C  CG  . PRO   A 1 205 ? 21.994  26.983  -30.545 1.00 97.60  ? 274  PRO   A CG  1 
ATOM   1454  C  CD  . PRO   A 1 205 ? 20.559  27.399  -30.766 1.00 95.34  ? 274  PRO   A CD  1 
ATOM   1455  N  N   . SER   A 1 206 ? 21.101  27.496  -26.200 1.00 92.12  ? 275  SER   A N   1 
ATOM   1456  C  CA  . SER   A 1 206 ? 20.823  28.340  -25.052 1.00 87.29  ? 275  SER   A CA  1 
ATOM   1457  C  C   . SER   A 1 206 ? 21.901  29.376  -24.796 1.00 87.17  ? 275  SER   A C   1 
ATOM   1458  O  O   . SER   A 1 206 ? 21.597  30.414  -24.203 1.00 89.73  ? 275  SER   A O   1 
ATOM   1459  C  CB  . SER   A 1 206 ? 20.616  27.478  -23.796 1.00 87.76  ? 275  SER   A CB  1 
ATOM   1460  O  OG  . SER   A 1 206 ? 21.622  26.482  -23.691 1.00 91.62  ? 275  SER   A OG  1 
ATOM   1461  N  N   . ASN   A 1 207 ? 23.137  29.145  -25.217 1.00 83.90  ? 276  ASN   A N   1 
ATOM   1462  C  CA  . ASN   A 1 207 ? 24.115  30.210  -25.055 1.00 87.34  ? 276  ASN   A CA  1 
ATOM   1463  C  C   . ASN   A 1 207 ? 23.904  31.263  -26.137 1.00 94.63  ? 276  ASN   A C   1 
ATOM   1464  O  O   . ASN   A 1 207 ? 23.784  30.911  -27.313 1.00 100.08 ? 276  ASN   A O   1 
ATOM   1465  C  CB  . ASN   A 1 207 ? 25.540  29.684  -25.140 1.00 92.29  ? 276  ASN   A CB  1 
ATOM   1466  C  CG  . ASN   A 1 207 ? 26.598  30.775  -24.880 1.00 94.68  ? 276  ASN   A CG  1 
ATOM   1467  O  OD1 . ASN   A 1 207 ? 26.434  31.946  -25.240 1.00 90.28  ? 276  ASN   A OD1 1 
ATOM   1468  N  ND2 . ASN   A 1 207 ? 27.704  30.373  -24.263 1.00 101.06 ? 276  ASN   A ND2 1 
ATOM   1469  N  N   . PRO   A 1 208 ? 23.862  32.550  -25.785 1.00 90.05  ? 277  PRO   A N   1 
ATOM   1470  C  CA  . PRO   A 1 208 ? 23.886  33.587  -26.815 1.00 86.79  ? 277  PRO   A CA  1 
ATOM   1471  C  C   . PRO   A 1 208 ? 24.946  33.386  -27.877 1.00 90.18  ? 277  PRO   A C   1 
ATOM   1472  O  O   . PRO   A 1 208 ? 24.617  33.526  -29.058 1.00 91.48  ? 277  PRO   A O   1 
ATOM   1473  C  CB  . PRO   A 1 208 ? 24.116  34.850  -25.991 1.00 85.97  ? 277  PRO   A CB  1 
ATOM   1474  C  CG  . PRO   A 1 208 ? 23.341  34.583  -24.781 1.00 87.40  ? 277  PRO   A CG  1 
ATOM   1475  C  CD  . PRO   A 1 208 ? 23.501  33.118  -24.481 1.00 93.81  ? 277  PRO   A CD  1 
ATOM   1476  N  N   . ILE   A 1 209 ? 26.190  33.048  -27.525 1.00 93.86  ? 278  ILE   A N   1 
ATOM   1477  C  CA  . ILE   A 1 209 ? 27.218  33.020  -28.572 1.00 98.34  ? 278  ILE   A CA  1 
ATOM   1478  C  C   . ILE   A 1 209 ? 26.855  32.001  -29.654 1.00 96.96  ? 278  ILE   A C   1 
ATOM   1479  O  O   . ILE   A 1 209 ? 27.100  32.241  -30.843 1.00 93.34  ? 278  ILE   A O   1 
ATOM   1480  C  CB  . ILE   A 1 209 ? 28.642  32.774  -27.994 1.00 99.59  ? 278  ILE   A CB  1 
ATOM   1481  C  CG1 . ILE   A 1 209 ? 28.727  31.456  -27.214 1.00 106.36 ? 278  ILE   A CG1 1 
ATOM   1482  C  CG2 . ILE   A 1 209 ? 29.162  33.987  -27.171 1.00 92.01  ? 278  ILE   A CG2 1 
ATOM   1483  C  CD1 . ILE   A 1 209 ? 30.121  31.144  -26.626 1.00 109.60 ? 278  ILE   A CD1 1 
ATOM   1484  N  N   . ASP   A 1 210 ? 26.215  30.888  -29.286 1.00 111.04 ? 279  ASP   A N   1 
ATOM   1485  C  CA  . ASP   A 1 210 ? 25.842  29.895  -30.294 1.00 111.31 ? 279  ASP   A CA  1 
ATOM   1486  C  C   . ASP   A 1 210 ? 24.535  30.241  -30.988 1.00 111.63 ? 279  ASP   A C   1 
ATOM   1487  O  O   . ASP   A 1 210 ? 24.404  30.051  -32.200 1.00 113.79 ? 279  ASP   A O   1 
ATOM   1488  C  CB  . ASP   A 1 210 ? 25.719  28.511  -29.670 1.00 116.86 ? 279  ASP   A CB  1 
ATOM   1489  C  CG  . ASP   A 1 210 ? 26.950  28.112  -28.871 1.00 120.20 ? 279  ASP   A CG  1 
ATOM   1490  O  OD1 . ASP   A 1 210 ? 28.085  28.489  -29.277 1.00 123.11 ? 279  ASP   A OD1 1 
ATOM   1491  O  OD2 . ASP   A 1 210 ? 26.781  27.418  -27.836 1.00 117.16 ? 279  ASP   A OD2 1 
ATOM   1492  N  N   . PHE   A 1 211 ? 23.566  30.739  -30.224 1.00 97.01  ? 280  PHE   A N   1 
ATOM   1493  C  CA  . PHE   A 1 211 ? 22.252  31.080  -30.757 1.00 91.09  ? 280  PHE   A CA  1 
ATOM   1494  C  C   . PHE   A 1 211 ? 22.350  32.100  -31.875 1.00 87.68  ? 280  PHE   A C   1 
ATOM   1495  O  O   . PHE   A 1 211 ? 21.578  32.045  -32.839 1.00 86.87  ? 280  PHE   A O   1 
ATOM   1496  C  CB  . PHE   A 1 211 ? 21.400  31.623  -29.625 1.00 87.41  ? 280  PHE   A CB  1 
ATOM   1497  C  CG  . PHE   A 1 211 ? 19.953  31.791  -29.958 1.00 85.12  ? 280  PHE   A CG  1 
ATOM   1498  C  CD1 . PHE   A 1 211 ? 19.487  32.923  -30.618 1.00 83.76  ? 280  PHE   A CD1 1 
ATOM   1499  C  CD2 . PHE   A 1 211 ? 19.037  30.850  -29.537 1.00 85.68  ? 280  PHE   A CD2 1 
ATOM   1500  C  CE1 . PHE   A 1 211 ? 18.139  33.078  -30.876 1.00 82.53  ? 280  PHE   A CE1 1 
ATOM   1501  C  CE2 . PHE   A 1 211 ? 17.699  31.005  -29.796 1.00 85.98  ? 280  PHE   A CE2 1 
ATOM   1502  C  CZ  . PHE   A 1 211 ? 17.248  32.114  -30.465 1.00 83.47  ? 280  PHE   A CZ  1 
ATOM   1503  N  N   . SER   A 1 212 ? 23.269  33.052  -31.748 1.00 87.14  ? 281  SER   A N   1 
ATOM   1504  C  CA  . SER   A 1 212 ? 23.500  34.006  -32.824 1.00 84.40  ? 281  SER   A CA  1 
ATOM   1505  C  C   . SER   A 1 212 ? 23.986  33.304  -34.084 1.00 85.08  ? 281  SER   A C   1 
ATOM   1506  O  O   . SER   A 1 212 ? 23.381  33.446  -35.149 1.00 86.05  ? 281  SER   A O   1 
ATOM   1507  C  CB  . SER   A 1 212 ? 24.499  35.068  -32.377 1.00 86.39  ? 281  SER   A CB  1 
ATOM   1508  O  OG  . SER   A 1 212 ? 25.819  34.561  -32.323 1.00 89.00  ? 281  SER   A OG  1 
ATOM   1509  N  N   . TYR   A 1 213 ? 25.066  32.521  -33.984 1.00 88.00  ? 282  TYR   A N   1 
ATOM   1510  C  CA  . TYR   A 1 213 ? 25.617  31.865  -35.173 1.00 86.64  ? 282  TYR   A CA  1 
ATOM   1511  C  C   . TYR   A 1 213 ? 24.640  30.878  -35.783 1.00 87.68  ? 282  TYR   A C   1 
ATOM   1512  O  O   . TYR   A 1 213 ? 24.687  30.624  -36.990 1.00 89.87  ? 282  TYR   A O   1 
ATOM   1513  C  CB  . TYR   A 1 213 ? 26.911  31.130  -34.851 1.00 84.93  ? 282  TYR   A CB  1 
ATOM   1514  C  CG  . TYR   A 1 213 ? 28.069  32.019  -34.519 1.00 85.45  ? 282  TYR   A CG  1 
ATOM   1515  C  CD1 . TYR   A 1 213 ? 28.275  33.229  -35.176 1.00 83.09  ? 282  TYR   A CD1 1 
ATOM   1516  C  CD2 . TYR   A 1 213 ? 28.965  31.647  -33.538 1.00 92.19  ? 282  TYR   A CD2 1 
ATOM   1517  C  CE1 . TYR   A 1 213 ? 29.350  34.035  -34.850 1.00 85.20  ? 282  TYR   A CE1 1 
ATOM   1518  C  CE2 . TYR   A 1 213 ? 30.040  32.446  -33.203 1.00 92.59  ? 282  TYR   A CE2 1 
ATOM   1519  C  CZ  . TYR   A 1 213 ? 30.230  33.627  -33.854 1.00 88.62  ? 282  TYR   A CZ  1 
ATOM   1520  O  OH  . TYR   A 1 213 ? 31.314  34.374  -33.468 1.00 92.30  ? 282  TYR   A OH  1 
ATOM   1521  N  N   . ARG   A 1 214 ? 23.767  30.294  -34.973 1.00 88.92  ? 283  ARG   A N   1 
ATOM   1522  C  CA  . ARG   A 1 214 ? 22.741  29.423  -35.523 1.00 89.64  ? 283  ARG   A CA  1 
ATOM   1523  C  C   . ARG   A 1 214 ? 21.703  30.220  -36.315 1.00 91.92  ? 283  ARG   A C   1 
ATOM   1524  O  O   . ARG   A 1 214 ? 21.363  29.854  -37.446 1.00 92.04  ? 283  ARG   A O   1 
ATOM   1525  C  CB  . ARG   A 1 214 ? 22.090  28.638  -34.395 1.00 94.07  ? 283  ARG   A CB  1 
ATOM   1526  C  CG  . ARG   A 1 214 ? 21.112  27.630  -34.870 1.00 96.82  ? 283  ARG   A CG  1 
ATOM   1527  C  CD  . ARG   A 1 214 ? 21.794  26.421  -35.437 1.00 98.42  ? 283  ARG   A CD  1 
ATOM   1528  N  NE  . ARG   A 1 214 ? 20.752  25.546  -35.953 1.00 108.08 ? 283  ARG   A NE  1 
ATOM   1529  C  CZ  . ARG   A 1 214 ? 19.909  24.864  -35.188 1.00 112.98 ? 283  ARG   A CZ  1 
ATOM   1530  N  NH1 . ARG   A 1 214 ? 20.024  24.863  -33.865 1.00 107.91 ? 283  ARG   A NH1 1 
ATOM   1531  N  NH2 . ARG   A 1 214 ? 18.924  24.172  -35.763 1.00 115.98 ? 283  ARG   A NH2 1 
ATOM   1532  N  N   . VAL   A 1 215 ? 21.196  31.323  -35.748 1.00 88.92  ? 284  VAL   A N   1 
ATOM   1533  C  CA  . VAL   A 1 215 ? 20.207  32.138  -36.457 1.00 83.76  ? 284  VAL   A CA  1 
ATOM   1534  C  C   . VAL   A 1 215 ? 20.743  32.609  -37.803 1.00 82.50  ? 284  VAL   A C   1 
ATOM   1535  O  O   . VAL   A 1 215 ? 20.019  32.619  -38.805 1.00 82.68  ? 284  VAL   A O   1 
ATOM   1536  C  CB  . VAL   A 1 215 ? 19.774  33.331  -35.592 1.00 80.33  ? 284  VAL   A CB  1 
ATOM   1537  C  CG1 . VAL   A 1 215 ? 18.892  34.260  -36.400 1.00 83.37  ? 284  VAL   A CG1 1 
ATOM   1538  C  CG2 . VAL   A 1 215 ? 19.048  32.849  -34.365 1.00 85.40  ? 284  VAL   A CG2 1 
ATOM   1539  N  N   . ALA   A 1 216 ? 22.011  33.017  -37.846 1.00 81.96  ? 285  ALA   A N   1 
ATOM   1540  C  CA  . ALA   A 1 216 ? 22.576  33.541  -39.083 1.00 81.08  ? 285  ALA   A CA  1 
ATOM   1541  C  C   . ALA   A 1 216 ? 22.665  32.473  -40.159 1.00 84.51  ? 285  ALA   A C   1 
ATOM   1542  O  O   . ALA   A 1 216 ? 22.655  32.795  -41.358 1.00 86.45  ? 285  ALA   A O   1 
ATOM   1543  C  CB  . ALA   A 1 216 ? 23.961  34.127  -38.825 1.00 77.03  ? 285  ALA   A CB  1 
ATOM   1544  N  N   . ALA   A 1 217 ? 22.761  31.209  -39.765 1.00 83.76  ? 286  ALA   A N   1 
ATOM   1545  C  CA  . ALA   A 1 217 ? 22.882  30.154  -40.752 1.00 84.81  ? 286  ALA   A CA  1 
ATOM   1546  C  C   . ALA   A 1 217 ? 21.534  29.583  -41.174 1.00 88.70  ? 286  ALA   A C   1 
ATOM   1547  O  O   . ALA   A 1 217 ? 21.489  28.808  -42.134 1.00 91.28  ? 286  ALA   A O   1 
ATOM   1548  C  CB  . ALA   A 1 217 ? 23.801  29.039  -40.233 1.00 90.17  ? 286  ALA   A CB  1 
ATOM   1549  N  N   . CYS   A 1 218 ? 20.436  29.962  -40.504 1.00 92.61  ? 287  CYS   A N   1 
ATOM   1550  C  CA  . CYS   A 1 218 ? 19.095  29.532  -40.896 1.00 92.86  ? 287  CYS   A CA  1 
ATOM   1551  C  C   . CYS   A 1 218 ? 18.175  30.708  -41.213 1.00 92.13  ? 287  CYS   A C   1 
ATOM   1552  O  O   . CYS   A 1 218 ? 16.953  30.520  -41.347 1.00 91.19  ? 287  CYS   A O   1 
ATOM   1553  C  CB  . CYS   A 1 218 ? 18.460  28.660  -39.812 1.00 96.66  ? 287  CYS   A CB  1 
ATOM   1554  S  SG  . CYS   A 1 218 ? 17.854  29.628  -38.423 1.00 108.75 ? 287  CYS   A SG  1 
ATOM   1555  N  N   . LEU   A 1 219 ? 18.724  31.916  -41.304 1.00 84.28  ? 288  LEU   A N   1 
ATOM   1556  C  CA  . LEU   A 1 219 ? 17.962  33.002  -41.896 1.00 83.71  ? 288  LEU   A CA  1 
ATOM   1557  C  C   . LEU   A 1 219 ? 18.067  32.927  -43.411 1.00 85.45  ? 288  LEU   A C   1 
ATOM   1558  O  O   . LEU   A 1 219 ? 19.127  32.553  -43.931 1.00 82.14  ? 288  LEU   A O   1 
ATOM   1559  C  CB  . LEU   A 1 219 ? 18.496  34.348  -41.431 1.00 81.00  ? 288  LEU   A CB  1 
ATOM   1560  C  CG  . LEU   A 1 219 ? 17.719  34.921  -40.273 1.00 76.97  ? 288  LEU   A CG  1 
ATOM   1561  C  CD1 . LEU   A 1 219 ? 18.503  36.039  -39.658 1.00 75.07  ? 288  LEU   A CD1 1 
ATOM   1562  C  CD2 . LEU   A 1 219 ? 16.347  35.380  -40.770 1.00 83.04  ? 288  LEU   A CD2 1 
ATOM   1563  N  N   . PRO   A 1 220 ? 16.982  33.262  -44.151 1.00 85.13  ? 289  PRO   A N   1 
ATOM   1564  C  CA  . PRO   A 1 220 ? 17.092  33.509  -45.599 1.00 85.32  ? 289  PRO   A CA  1 
ATOM   1565  C  C   . PRO   A 1 220 ? 17.779  34.853  -45.837 1.00 88.91  ? 289  PRO   A C   1 
ATOM   1566  O  O   . PRO   A 1 220 ? 17.114  35.881  -46.006 1.00 92.11  ? 289  PRO   A O   1 
ATOM   1567  C  CB  . PRO   A 1 220 ? 15.627  33.507  -46.064 1.00 80.53  ? 289  PRO   A CB  1 
ATOM   1568  C  CG  . PRO   A 1 220 ? 14.877  33.986  -44.893 1.00 82.87  ? 289  PRO   A CG  1 
ATOM   1569  C  CD  . PRO   A 1 220 ? 15.630  33.522  -43.647 1.00 82.71  ? 289  PRO   A CD  1 
ATOM   1570  N  N   . ILE   A 1 221 ? 19.106  34.879  -45.760 1.00 81.00  ? 290  ILE   A N   1 
ATOM   1571  C  CA  . ILE   A 1 221 ? 19.873  36.091  -45.972 1.00 81.77  ? 290  ILE   A CA  1 
ATOM   1572  C  C   . ILE   A 1 221 ? 20.871  35.747  -47.053 1.00 85.08  ? 290  ILE   A C   1 
ATOM   1573  O  O   . ILE   A 1 221 ? 21.089  34.578  -47.360 1.00 80.60  ? 290  ILE   A O   1 
ATOM   1574  C  CB  . ILE   A 1 221 ? 20.585  36.583  -44.690 1.00 86.68  ? 290  ILE   A CB  1 
ATOM   1575  C  CG1 . ILE   A 1 221 ? 21.387  35.445  -44.053 1.00 85.29  ? 290  ILE   A CG1 1 
ATOM   1576  C  CG2 . ILE   A 1 221 ? 19.578  37.111  -43.686 1.00 83.84  ? 290  ILE   A CG2 1 
ATOM   1577  C  CD1 . ILE   A 1 221 ? 22.218  35.871  -42.864 1.00 79.80  ? 290  ILE   A CD1 1 
ATOM   1578  N  N   . ASP   A 1 222 ? 21.458  36.779  -47.659 1.00 100.62 ? 291  ASP   A N   1 
ATOM   1579  C  CA  . ASP   A 1 222 ? 22.435  36.583  -48.721 1.00 100.39 ? 291  ASP   A CA  1 
ATOM   1580  C  C   . ASP   A 1 222 ? 23.821  36.561  -48.107 1.00 101.13 ? 291  ASP   A C   1 
ATOM   1581  O  O   . ASP   A 1 222 ? 23.984  36.741  -46.900 1.00 103.17 ? 291  ASP   A O   1 
ATOM   1582  C  CB  . ASP   A 1 222 ? 22.316  37.657  -49.805 1.00 100.67 ? 291  ASP   A CB  1 
ATOM   1583  C  CG  . ASP   A 1 222 ? 22.405  39.085  -49.262 1.00 103.53 ? 291  ASP   A CG  1 
ATOM   1584  O  OD1 . ASP   A 1 222 ? 22.373  39.287  -48.022 1.00 104.21 ? 291  ASP   A OD1 1 
ATOM   1585  O  OD2 . ASP   A 1 222 ? 22.509  40.023  -50.094 1.00 104.32 ? 291  ASP   A OD2 1 
ATOM   1586  N  N   . ASP   A 1 223 ? 24.836  36.308  -48.927 1.00 91.05  ? 292  ASP   A N   1 
ATOM   1587  C  CA  . ASP   A 1 223 ? 26.163  36.157  -48.350 1.00 91.43  ? 292  ASP   A CA  1 
ATOM   1588  C  C   . ASP   A 1 223 ? 26.688  37.463  -47.750 1.00 87.04  ? 292  ASP   A C   1 
ATOM   1589  O  O   . ASP   A 1 223 ? 27.516  37.416  -46.834 1.00 84.07  ? 292  ASP   A O   1 
ATOM   1590  C  CB  . ASP   A 1 223 ? 27.142  35.579  -49.387 1.00 89.79  ? 292  ASP   A CB  1 
ATOM   1591  C  CG  . ASP   A 1 223 ? 27.252  34.065  -49.296 1.00 89.03  ? 292  ASP   A CG  1 
ATOM   1592  O  OD1 . ASP   A 1 223 ? 26.552  33.462  -48.457 1.00 88.60  ? 292  ASP   A OD1 1 
ATOM   1593  O  OD2 . ASP   A 1 223 ? 28.039  33.486  -50.064 1.00 95.16  ? 292  ASP   A OD2 1 
ATOM   1594  N  N   . VAL   A 1 224 ? 26.206  38.623  -48.193 1.00 87.33  ? 293  VAL   A N   1 
ATOM   1595  C  CA  . VAL   A 1 224 ? 26.797  39.841  -47.645 1.00 85.08  ? 293  VAL   A CA  1 
ATOM   1596  C  C   . VAL   A 1 224 ? 26.250  40.127  -46.252 1.00 88.87  ? 293  VAL   A C   1 
ATOM   1597  O  O   . VAL   A 1 224 ? 26.963  40.672  -45.402 1.00 92.23  ? 293  VAL   A O   1 
ATOM   1598  C  CB  . VAL   A 1 224 ? 26.618  41.032  -48.603 1.00 81.25  ? 293  VAL   A CB  1 
ATOM   1599  C  CG1 . VAL   A 1 224 ? 25.165  41.224  -48.990 1.00 80.58  ? 293  VAL   A CG1 1 
ATOM   1600  C  CG2 . VAL   A 1 224 ? 27.224  42.294  -47.981 1.00 88.16  ? 293  VAL   A CG2 1 
ATOM   1601  N  N   . LEU   A 1 225 ? 25.009  39.734  -45.973 1.00 89.23  ? 294  LEU   A N   1 
ATOM   1602  C  CA  . LEU   A 1 225 ? 24.487  39.845  -44.614 1.00 85.06  ? 294  LEU   A CA  1 
ATOM   1603  C  C   . LEU   A 1 225 ? 25.178  38.873  -43.679 1.00 84.10  ? 294  LEU   A C   1 
ATOM   1604  O  O   . LEU   A 1 225 ? 25.547  39.239  -42.562 1.00 86.25  ? 294  LEU   A O   1 
ATOM   1605  C  CB  . LEU   A 1 225 ? 22.991  39.583  -44.588 1.00 86.81  ? 294  LEU   A CB  1 
ATOM   1606  C  CG  . LEU   A 1 225 ? 22.130  40.818  -44.571 1.00 80.16  ? 294  LEU   A CG  1 
ATOM   1607  C  CD1 . LEU   A 1 225 ? 22.558  41.679  -45.724 1.00 85.18  ? 294  LEU   A CD1 1 
ATOM   1608  C  CD2 . LEU   A 1 225 ? 20.714  40.351  -44.710 1.00 85.73  ? 294  LEU   A CD2 1 
ATOM   1609  N  N   . ARG   A 1 226 ? 25.300  37.610  -44.091 1.00 83.47  ? 295  ARG   A N   1 
ATOM   1610  C  CA  . ARG   A 1 226 ? 26.138  36.681  -43.348 1.00 81.64  ? 295  ARG   A CA  1 
ATOM   1611  C  C   . ARG   A 1 226 ? 27.452  37.352  -42.968 1.00 82.67  ? 295  ARG   A C   1 
ATOM   1612  O  O   . ARG   A 1 226 ? 27.850  37.352  -41.799 1.00 80.39  ? 295  ARG   A O   1 
ATOM   1613  C  CB  . ARG   A 1 226 ? 26.414  35.414  -44.167 1.00 83.56  ? 295  ARG   A CB  1 
ATOM   1614  C  CG  . ARG   A 1 226 ? 25.191  34.711  -44.675 1.00 82.44  ? 295  ARG   A CG  1 
ATOM   1615  C  CD  . ARG   A 1 226 ? 25.460  33.248  -44.973 1.00 81.45  ? 295  ARG   A CD  1 
ATOM   1616  N  NE  . ARG   A 1 226 ? 24.245  32.511  -44.657 1.00 85.18  ? 295  ARG   A NE  1 
ATOM   1617  C  CZ  . ARG   A 1 226 ? 23.920  31.324  -45.142 1.00 82.50  ? 295  ARG   A CZ  1 
ATOM   1618  N  NH1 . ARG   A 1 226 ? 24.737  30.664  -45.944 1.00 79.09  ? 295  ARG   A NH1 1 
ATOM   1619  N  NH2 . ARG   A 1 226 ? 22.738  30.793  -44.818 1.00 81.52  ? 295  ARG   A NH2 1 
ATOM   1620  N  N   . ILE   A 1 227 ? 28.113  37.981  -43.947 1.00 85.77  ? 296  ILE   A N   1 
ATOM   1621  C  CA  . ILE   A 1 227 ? 29.480  38.454  -43.739 1.00 84.78  ? 296  ILE   A CA  1 
ATOM   1622  C  C   . ILE   A 1 227 ? 29.519  39.577  -42.705 1.00 83.82  ? 296  ILE   A C   1 
ATOM   1623  O  O   . ILE   A 1 227 ? 30.463  39.667  -41.911 1.00 84.00  ? 296  ILE   A O   1 
ATOM   1624  C  CB  . ILE   A 1 227 ? 30.103  38.842  -45.104 1.00 81.36  ? 296  ILE   A CB  1 
ATOM   1625  C  CG1 . ILE   A 1 227 ? 30.383  37.585  -45.918 1.00 78.61  ? 296  ILE   A CG1 1 
ATOM   1626  C  CG2 . ILE   A 1 227 ? 31.389  39.604  -44.939 1.00 84.69  ? 296  ILE   A CG2 1 
ATOM   1627  C  CD1 . ILE   A 1 227 ? 31.210  37.814  -47.142 1.00 83.80  ? 296  ILE   A CD1 1 
ATOM   1628  N  N   . GLN   A 1 228 ? 28.473  40.400  -42.645 1.00 90.36  ? 297  GLN   A N   1 
ATOM   1629  C  CA  . GLN   A 1 228 ? 28.413  41.459  -41.645 1.00 90.74  ? 297  GLN   A CA  1 
ATOM   1630  C  C   . GLN   A 1 228 ? 28.093  40.909  -40.251 1.00 89.24  ? 297  GLN   A C   1 
ATOM   1631  O  O   . GLN   A 1 228 ? 28.688  41.343  -39.255 1.00 90.47  ? 297  GLN   A O   1 
ATOM   1632  C  CB  . GLN   A 1 228 ? 27.382  42.504  -42.085 1.00 97.12  ? 297  GLN   A CB  1 
ATOM   1633  C  CG  . GLN   A 1 228 ? 27.677  43.110  -43.469 1.00 102.24 ? 297  GLN   A CG  1 
ATOM   1634  C  CD  . GLN   A 1 228 ? 26.422  43.626  -44.198 1.00 111.47 ? 297  GLN   A CD  1 
ATOM   1635  O  OE1 . GLN   A 1 228 ? 25.292  43.404  -43.753 1.00 114.31 ? 297  GLN   A OE1 1 
ATOM   1636  N  NE2 . GLN   A 1 228 ? 26.624  44.308  -45.330 1.00 109.27 ? 297  GLN   A NE2 1 
ATOM   1637  N  N   . LEU   A 1 229 ? 27.147  39.973  -40.152 1.00 83.31  ? 298  LEU   A N   1 
ATOM   1638  C  CA  . LEU   A 1 229 ? 26.921  39.297  -38.882 1.00 77.57  ? 298  LEU   A CA  1 
ATOM   1639  C  C   . LEU   A 1 229 ? 28.192  38.611  -38.401 1.00 80.46  ? 298  LEU   A C   1 
ATOM   1640  O  O   . LEU   A 1 229 ? 28.459  38.563  -37.195 1.00 82.80  ? 298  LEU   A O   1 
ATOM   1641  C  CB  . LEU   A 1 229 ? 25.803  38.263  -39.008 1.00 79.53  ? 298  LEU   A CB  1 
ATOM   1642  C  CG  . LEU   A 1 229 ? 24.304  38.574  -39.010 1.00 78.77  ? 298  LEU   A CG  1 
ATOM   1643  C  CD1 . LEU   A 1 229 ? 23.828  39.105  -37.656 1.00 82.26  ? 298  LEU   A CD1 1 
ATOM   1644  C  CD2 . LEU   A 1 229 ? 23.959  39.506  -40.149 1.00 86.22  ? 298  LEU   A CD2 1 
ATOM   1645  N  N   . LEU   A 1 230 ? 28.979  38.050  -39.328 1.00 80.96  ? 299  LEU   A N   1 
ATOM   1646  C  CA  . LEU   A 1 230 ? 30.197  37.342  -38.934 1.00 80.87  ? 299  LEU   A CA  1 
ATOM   1647  C  C   . LEU   A 1 230 ? 31.252  38.299  -38.411 1.00 81.74  ? 299  LEU   A C   1 
ATOM   1648  O  O   . LEU   A 1 230 ? 31.994  37.940  -37.492 1.00 88.45  ? 299  LEU   A O   1 
ATOM   1649  C  CB  . LEU   A 1 230 ? 30.764  36.524  -40.103 1.00 80.39  ? 299  LEU   A CB  1 
ATOM   1650  C  CG  . LEU   A 1 230 ? 30.052  35.217  -40.482 1.00 81.12  ? 299  LEU   A CG  1 
ATOM   1651  C  CD1 . LEU   A 1 230 ? 30.898  34.420  -41.437 1.00 83.61  ? 299  LEU   A CD1 1 
ATOM   1652  C  CD2 . LEU   A 1 230 ? 29.697  34.380  -39.263 1.00 83.49  ? 299  LEU   A CD2 1 
ATOM   1653  N  N   . LYS   A 1 231 ? 31.321  39.518  -38.967 1.00 81.34  ? 300  LYS   A N   1 
ATOM   1654  C  CA  . LYS   A 1 231 ? 32.270  40.529  -38.512 1.00 80.50  ? 300  LYS   A CA  1 
ATOM   1655  C  C   . LYS   A 1 231 ? 31.844  41.196  -37.201 1.00 84.22  ? 300  LYS   A C   1 
ATOM   1656  O  O   . LYS   A 1 231 ? 32.686  41.788  -36.518 1.00 85.92  ? 300  LYS   A O   1 
ATOM   1657  C  CB  . LYS   A 1 231 ? 32.474  41.579  -39.611 1.00 80.18  ? 300  LYS   A CB  1 
ATOM   1658  C  CG  . LYS   A 1 231 ? 33.110  41.034  -40.882 1.00 79.10  ? 300  LYS   A CG  1 
ATOM   1659  C  CD  . LYS   A 1 231 ? 33.646  42.138  -41.753 1.00 87.65  ? 300  LYS   A CD  1 
ATOM   1660  C  CE  . LYS   A 1 231 ? 33.523  41.803  -43.217 1.00 90.81  ? 300  LYS   A CE  1 
ATOM   1661  N  NZ  . LYS   A 1 231 ? 32.944  42.925  -44.024 1.00 79.50  ? 300  LYS   A NZ  1 
ATOM   1662  N  N   . ILE   A 1 232 ? 30.574  41.078  -36.814 1.00 84.59  ? 301  ILE   A N   1 
ATOM   1663  C  CA  . ILE   A 1 232 ? 30.094  41.651  -35.561 1.00 81.59  ? 301  ILE   A CA  1 
ATOM   1664  C  C   . ILE   A 1 232 ? 30.733  40.932  -34.373 1.00 90.16  ? 301  ILE   A C   1 
ATOM   1665  O  O   . ILE   A 1 232 ? 30.670  39.699  -34.251 1.00 90.70  ? 301  ILE   A O   1 
ATOM   1666  C  CB  . ILE   A 1 232 ? 28.560  41.592  -35.526 1.00 79.20  ? 301  ILE   A CB  1 
ATOM   1667  C  CG1 . ILE   A 1 232 ? 27.996  42.752  -36.336 1.00 80.56  ? 301  ILE   A CG1 1 
ATOM   1668  C  CG2 . ILE   A 1 232 ? 28.023  41.599  -34.107 1.00 84.59  ? 301  ILE   A CG2 1 
ATOM   1669  C  CD1 . ILE   A 1 232 ? 26.508  42.701  -36.556 1.00 85.02  ? 301  ILE   A CD1 1 
ATOM   1670  N  N   . GLY   A 1 233 ? 31.350  41.711  -33.480 1.00 101.26 ? 302  GLY   A N   1 
ATOM   1671  C  CA  . GLY   A 1 233 ? 32.120  41.194  -32.361 1.00 102.12 ? 302  GLY   A CA  1 
ATOM   1672  C  C   . GLY   A 1 233 ? 31.311  40.490  -31.292 1.00 100.07 ? 302  GLY   A C   1 
ATOM   1673  O  O   . GLY   A 1 233 ? 31.500  39.297  -31.056 1.00 101.85 ? 302  GLY   A O   1 
ATOM   1674  N  N   . SER   A 1 234 ? 30.392  41.201  -30.654 1.00 102.32 ? 303  SER   A N   1 
ATOM   1675  C  CA  . SER   A 1 234 ? 29.682  40.675  -29.495 1.00 100.05 ? 303  SER   A CA  1 
ATOM   1676  C  C   . SER   A 1 234 ? 28.422  39.913  -29.894 1.00 97.65  ? 303  SER   A C   1 
ATOM   1677  O  O   . SER   A 1 234 ? 27.724  40.300  -30.834 1.00 97.69  ? 303  SER   A O   1 
ATOM   1678  C  CB  . SER   A 1 234 ? 29.297  41.817  -28.565 1.00 98.91  ? 303  SER   A CB  1 
ATOM   1679  O  OG  . SER   A 1 234 ? 28.357  42.648  -29.229 1.00 98.34  ? 303  SER   A OG  1 
ATOM   1680  N  N   . ALA   A 1 235 ? 28.105  38.856  -29.135 1.00 85.72  ? 304  ALA   A N   1 
ATOM   1681  C  CA  . ALA   A 1 235 ? 26.920  38.064  -29.445 1.00 80.58  ? 304  ALA   A CA  1 
ATOM   1682  C  C   . ALA   A 1 235 ? 25.633  38.874  -29.307 1.00 78.71  ? 304  ALA   A C   1 
ATOM   1683  O  O   . ALA   A 1 235 ? 24.646  38.578  -29.978 1.00 82.54  ? 304  ALA   A O   1 
ATOM   1684  C  CB  . ALA   A 1 235 ? 26.884  36.830  -28.553 1.00 86.15  ? 304  ALA   A CB  1 
ATOM   1685  N  N   . ILE   A 1 236 ? 25.609  39.892  -28.452 1.00 82.54  ? 305  ILE   A N   1 
ATOM   1686  C  CA  . ILE   A 1 236 ? 24.399  40.702  -28.297 1.00 78.36  ? 305  ILE   A CA  1 
ATOM   1687  C  C   . ILE   A 1 236 ? 24.210  41.610  -29.501 1.00 79.16  ? 305  ILE   A C   1 
ATOM   1688  O  O   . ILE   A 1 236 ? 23.111  41.722  -30.049 1.00 79.35  ? 305  ILE   A O   1 
ATOM   1689  C  CB  . ILE   A 1 236 ? 24.452  41.519  -26.996 1.00 76.30  ? 305  ILE   A CB  1 
ATOM   1690  C  CG1 . ILE   A 1 236 ? 24.025  40.678  -25.792 1.00 77.07  ? 305  ILE   A CG1 1 
ATOM   1691  C  CG2 . ILE   A 1 236 ? 23.599  42.747  -27.109 1.00 74.68  ? 305  ILE   A CG2 1 
ATOM   1692  C  CD1 . ILE   A 1 236 ? 24.615  41.169  -24.501 1.00 82.76  ? 305  ILE   A CD1 1 
ATOM   1693  N  N   . GLN   A 1 237 ? 25.272  42.297  -29.911 1.00 80.69  ? 306  GLN   A N   1 
ATOM   1694  C  CA  . GLN   A 1 237 ? 25.200  43.090  -31.132 1.00 84.43  ? 306  GLN   A CA  1 
ATOM   1695  C  C   . GLN   A 1 237 ? 24.768  42.245  -32.329 1.00 86.06  ? 306  GLN   A C   1 
ATOM   1696  O  O   . GLN   A 1 237 ? 24.053  42.731  -33.218 1.00 85.15  ? 306  GLN   A O   1 
ATOM   1697  C  CB  . GLN   A 1 237 ? 26.555  43.729  -31.408 1.00 84.81  ? 306  GLN   A CB  1 
ATOM   1698  C  CG  . GLN   A 1 237 ? 26.824  44.981  -30.643 1.00 84.37  ? 306  GLN   A CG  1 
ATOM   1699  C  CD  . GLN   A 1 237 ? 28.285  45.301  -30.641 1.00 86.63  ? 306  GLN   A CD  1 
ATOM   1700  O  OE1 . GLN   A 1 237 ? 29.114  44.459  -31.004 1.00 85.62  ? 306  GLN   A OE1 1 
ATOM   1701  N  NE2 . GLN   A 1 237 ? 28.622  46.518  -30.229 1.00 87.59  ? 306  GLN   A NE2 1 
ATOM   1702  N  N   . ARG   A 1 238 ? 25.209  40.975  -32.367 1.00 84.31  ? 307  ARG   A N   1 
ATOM   1703  C  CA  . ARG   A 1 238 ? 24.883  40.066  -33.467 1.00 78.92  ? 307  ARG   A CA  1 
ATOM   1704  C  C   . ARG   A 1 238 ? 23.413  39.671  -33.440 1.00 79.03  ? 307  ARG   A C   1 
ATOM   1705  O  O   . ARG   A 1 238 ? 22.763  39.610  -34.491 1.00 79.44  ? 307  ARG   A O   1 
ATOM   1706  C  CB  . ARG   A 1 238 ? 25.778  38.826  -33.391 1.00 80.61  ? 307  ARG   A CB  1 
ATOM   1707  C  CG  . ARG   A 1 238 ? 25.749  37.890  -34.604 1.00 80.46  ? 307  ARG   A CG  1 
ATOM   1708  C  CD  . ARG   A 1 238 ? 26.712  36.703  -34.483 1.00 76.26  ? 307  ARG   A CD  1 
ATOM   1709  N  NE  . ARG   A 1 238 ? 28.110  37.111  -34.376 1.00 81.87  ? 307  ARG   A NE  1 
ATOM   1710  C  CZ  . ARG   A 1 238 ? 28.838  37.054  -33.262 1.00 89.03  ? 307  ARG   A CZ  1 
ATOM   1711  N  NH1 . ARG   A 1 238 ? 28.344  36.567  -32.129 1.00 87.79  ? 307  ARG   A NH1 1 
ATOM   1712  N  NH2 . ARG   A 1 238 ? 30.095  37.497  -33.283 1.00 89.39  ? 307  ARG   A NH2 1 
ATOM   1713  N  N   . LEU   A 1 239 ? 22.869  39.409  -32.246 1.00 77.63  ? 308  LEU   A N   1 
ATOM   1714  C  CA  . LEU   A 1 239 ? 21.432  39.180  -32.105 1.00 78.53  ? 308  LEU   A CA  1 
ATOM   1715  C  C   . LEU   A 1 239 ? 20.628  40.424  -32.487 1.00 81.53  ? 308  LEU   A C   1 
ATOM   1716  O  O   . LEU   A 1 239 ? 19.628  40.340  -33.217 1.00 77.55  ? 308  LEU   A O   1 
ATOM   1717  C  CB  . LEU   A 1 239 ? 21.117  38.775  -30.666 1.00 73.95  ? 308  LEU   A CB  1 
ATOM   1718  C  CG  . LEU   A 1 239 ? 21.809  37.523  -30.182 1.00 74.38  ? 308  LEU   A CG  1 
ATOM   1719  C  CD1 . LEU   A 1 239 ? 21.714  37.475  -28.681 1.00 72.74  ? 308  LEU   A CD1 1 
ATOM   1720  C  CD2 . LEU   A 1 239 ? 21.190  36.298  -30.856 1.00 78.84  ? 308  LEU   A CD2 1 
ATOM   1721  N  N   . ARG   A 1 240 ? 21.042  41.588  -31.969 1.00 82.48  ? 309  ARG   A N   1 
ATOM   1722  C  CA  . ARG   A 1 240 ? 20.316  42.836  -32.197 1.00 80.51  ? 309  ARG   A CA  1 
ATOM   1723  C  C   . ARG   A 1 240 ? 20.202  43.157  -33.673 1.00 80.55  ? 309  ARG   A C   1 
ATOM   1724  O  O   . ARG   A 1 240 ? 19.231  43.793  -34.108 1.00 78.12  ? 309  ARG   A O   1 
ATOM   1725  C  CB  . ARG   A 1 240 ? 21.028  43.979  -31.488 1.00 80.65  ? 309  ARG   A CB  1 
ATOM   1726  C  CG  . ARG   A 1 240 ? 20.729  44.064  -30.047 1.00 76.08  ? 309  ARG   A CG  1 
ATOM   1727  C  CD  . ARG   A 1 240 ? 21.521  45.155  -29.430 1.00 78.09  ? 309  ARG   A CD  1 
ATOM   1728  N  NE  . ARG   A 1 240 ? 21.398  46.411  -30.150 1.00 75.42  ? 309  ARG   A NE  1 
ATOM   1729  C  CZ  . ARG   A 1 240 ? 20.337  47.202  -30.102 1.00 82.36  ? 309  ARG   A CZ  1 
ATOM   1730  N  NH1 . ARG   A 1 240 ? 19.223  46.842  -29.480 1.00 80.60  ? 309  ARG   A NH1 1 
ATOM   1731  N  NH2 . ARG   A 1 240 ? 20.395  48.386  -30.695 1.00 96.70  ? 309  ARG   A NH2 1 
ATOM   1732  N  N   . CYS   A 1 241 ? 21.216  42.758  -34.442 1.00 81.09  ? 310  CYS   A N   1 
ATOM   1733  C  CA  . CYS   A 1 241 ? 21.239  42.907  -35.883 1.00 82.41  ? 310  CYS   A CA  1 
ATOM   1734  C  C   . CYS   A 1 241 ? 20.378  41.844  -36.547 1.00 81.06  ? 310  CYS   A C   1 
ATOM   1735  O  O   . CYS   A 1 241 ? 19.573  42.156  -37.433 1.00 79.01  ? 310  CYS   A O   1 
ATOM   1736  C  CB  . CYS   A 1 241 ? 22.686  42.813  -36.372 1.00 87.19  ? 310  CYS   A CB  1 
ATOM   1737  S  SG  . CYS   A 1 241 ? 22.951  42.966  -38.166 1.00 85.72  ? 310  CYS   A SG  1 
ATOM   1738  N  N   . GLU   A 1 242 ? 20.552  40.581  -36.127 1.00 82.10  ? 311  GLU   A N   1 
ATOM   1739  C  CA  . GLU   A 1 242 ? 19.686  39.517  -36.628 1.00 83.64  ? 311  GLU   A CA  1 
ATOM   1740  C  C   . GLU   A 1 242 ? 18.228  39.865  -36.424 1.00 83.01  ? 311  GLU   A C   1 
ATOM   1741  O  O   . GLU   A 1 242 ? 17.366  39.468  -37.220 1.00 81.28  ? 311  GLU   A O   1 
ATOM   1742  C  CB  . GLU   A 1 242 ? 19.976  38.200  -35.913 1.00 82.41  ? 311  GLU   A CB  1 
ATOM   1743  C  CG  . GLU   A 1 242 ? 21.019  37.374  -36.545 1.00 81.04  ? 311  GLU   A CG  1 
ATOM   1744  C  CD  . GLU   A 1 242 ? 21.611  36.435  -35.553 1.00 83.44  ? 311  GLU   A CD  1 
ATOM   1745  O  OE1 . GLU   A 1 242 ? 20.912  36.115  -34.571 1.00 84.77  ? 311  GLU   A OE1 1 
ATOM   1746  O  OE2 . GLU   A 1 242 ? 22.780  36.042  -35.727 1.00 86.31  ? 311  GLU   A OE2 1 
ATOM   1747  N  N   . LEU   A 1 243 ? 17.932  40.572  -35.344 1.00 79.14  ? 312  LEU   A N   1 
ATOM   1748  C  CA  . LEU   A 1 243 ? 16.571  41.003  -35.147 1.00 75.54  ? 312  LEU   A CA  1 
ATOM   1749  C  C   . LEU   A 1 243 ? 16.225  42.102  -36.131 1.00 79.54  ? 312  LEU   A C   1 
ATOM   1750  O  O   . LEU   A 1 243 ? 15.086  42.173  -36.603 1.00 84.40  ? 312  LEU   A O   1 
ATOM   1751  C  CB  . LEU   A 1 243 ? 16.405  41.452  -33.699 1.00 80.02  ? 312  LEU   A CB  1 
ATOM   1752  C  CG  . LEU   A 1 243 ? 15.016  41.354  -33.086 1.00 80.71  ? 312  LEU   A CG  1 
ATOM   1753  C  CD1 . LEU   A 1 243 ? 14.382  40.020  -33.356 1.00 82.06  ? 312  LEU   A CD1 1 
ATOM   1754  C  CD2 . LEU   A 1 243 ? 15.195  41.561  -31.621 1.00 85.93  ? 312  LEU   A CD2 1 
ATOM   1755  N  N   . ASP   A 1 244 ? 17.205  42.939  -36.480 1.00 80.59  ? 313  ASP   A N   1 
ATOM   1756  C  CA  . ASP   A 1 244 ? 16.955  44.048  -37.394 1.00 80.46  ? 313  ASP   A CA  1 
ATOM   1757  C  C   . ASP   A 1 244 ? 16.647  43.529  -38.793 1.00 81.76  ? 313  ASP   A C   1 
ATOM   1758  O  O   . ASP   A 1 244 ? 15.669  43.957  -39.420 1.00 79.51  ? 313  ASP   A O   1 
ATOM   1759  C  CB  . ASP   A 1 244 ? 18.169  44.983  -37.410 1.00 83.90  ? 313  ASP   A CB  1 
ATOM   1760  C  CG  . ASP   A 1 244 ? 17.794  46.459  -37.278 1.00 89.26  ? 313  ASP   A CG  1 
ATOM   1761  O  OD1 . ASP   A 1 244 ? 16.587  46.781  -37.303 1.00 90.93  ? 313  ASP   A OD1 1 
ATOM   1762  O  OD2 . ASP   A 1 244 ? 18.716  47.299  -37.149 1.00 92.77  ? 313  ASP   A OD2 1 
ATOM   1763  N  N   . ILE   A 1 245 ? 17.463  42.584  -39.278 1.00 83.70  ? 314  ILE   A N   1 
ATOM   1764  C  CA  . ILE   A 1 245 ? 17.237  41.938  -40.573 1.00 78.94  ? 314  ILE   A CA  1 
ATOM   1765  C  C   . ILE   A 1 245 ? 15.845  41.317  -40.649 1.00 80.42  ? 314  ILE   A C   1 
ATOM   1766  O  O   . ILE   A 1 245 ? 15.172  41.397  -41.684 1.00 82.81  ? 314  ILE   A O   1 
ATOM   1767  C  CB  . ILE   A 1 245 ? 18.316  40.876  -40.815 1.00 76.10  ? 314  ILE   A CB  1 
ATOM   1768  C  CG1 . ILE   A 1 245 ? 19.680  41.521  -40.947 1.00 76.28  ? 314  ILE   A CG1 1 
ATOM   1769  C  CG2 . ILE   A 1 245 ? 17.952  40.001  -41.993 1.00 77.25  ? 314  ILE   A CG2 1 
ATOM   1770  C  CD1 . ILE   A 1 245 ? 20.735  40.519  -40.993 1.00 76.19  ? 314  ILE   A CD1 1 
ATOM   1771  N  N   . MET   A 1 246 ? 15.411  40.642  -39.579 1.00 81.07  ? 315  MET   A N   1 
ATOM   1772  C  CA  . MET   A 1 246 ? 14.096  40.011  -39.568 1.00 78.62  ? 315  MET   A CA  1 
ATOM   1773  C  C   . MET   A 1 246 ? 12.969  41.021  -39.510 1.00 80.67  ? 315  MET   A C   1 
ATOM   1774  O  O   . MET   A 1 246 ? 11.816  40.661  -39.790 1.00 85.02  ? 315  MET   A O   1 
ATOM   1775  C  CB  . MET   A 1 246 ? 13.960  39.076  -38.380 1.00 75.19  ? 315  MET   A CB  1 
ATOM   1776  C  CG  . MET   A 1 246 ? 15.045  38.080  -38.276 1.00 74.98  ? 315  MET   A CG  1 
ATOM   1777  S  SD  . MET   A 1 246 ? 14.618  37.119  -36.863 1.00 75.27  ? 315  MET   A SD  1 
ATOM   1778  C  CE  . MET   A 1 246 ? 13.299  36.136  -37.548 1.00 80.63  ? 315  MET   A CE  1 
ATOM   1779  N  N   . ASN   A 1 247 ? 13.269  42.259  -39.128 1.00 80.47  ? 316  ASN   A N   1 
ATOM   1780  C  CA  . ASN   A 1 247 ? 12.272  43.316  -39.066 1.00 82.00  ? 316  ASN   A CA  1 
ATOM   1781  C  C   . ASN   A 1 247 ? 12.341  44.265  -40.255 1.00 79.83  ? 316  ASN   A C   1 
ATOM   1782  O  O   . ASN   A 1 247 ? 11.303  44.766  -40.693 1.00 79.80  ? 316  ASN   A O   1 
ATOM   1783  C  CB  . ASN   A 1 247 ? 12.425  44.125  -37.771 1.00 84.58  ? 316  ASN   A CB  1 
ATOM   1784  C  CG  . ASN   A 1 247 ? 12.292  43.276  -36.505 1.00 86.08  ? 316  ASN   A CG  1 
ATOM   1785  O  OD1 . ASN   A 1 247 ? 11.527  42.308  -36.440 1.00 84.45  ? 316  ASN   A OD1 1 
ATOM   1786  N  ND2 . ASN   A 1 247 ? 13.037  43.664  -35.477 1.00 91.89  ? 316  ASN   A ND2 1 
ATOM   1787  N  N   . LYS   A 1 248 ? 13.533  44.523  -40.793 1.00 81.61  ? 317  LYS   A N   1 
ATOM   1788  C  CA  . LYS   A 1 248 ? 13.707  45.470  -41.886 1.00 82.58  ? 317  LYS   A CA  1 
ATOM   1789  C  C   . LYS   A 1 248 ? 13.673  44.809  -43.267 1.00 83.90  ? 317  LYS   A C   1 
ATOM   1790  O  O   . LYS   A 1 248 ? 12.928  45.260  -44.140 1.00 82.71  ? 317  LYS   A O   1 
ATOM   1791  C  CB  . LYS   A 1 248 ? 15.024  46.237  -41.696 1.00 83.58  ? 317  LYS   A CB  1 
ATOM   1792  N  N   . CYS   A 1 249 ? 14.449  43.736  -43.469 1.00 82.83  ? 318  CYS   A N   1 
ATOM   1793  C  CA  . CYS   A 1 249 ? 14.621  43.083  -44.770 1.00 77.86  ? 318  CYS   A CA  1 
ATOM   1794  C  C   . CYS   A 1 249 ? 13.627  41.940  -44.930 1.00 77.79  ? 318  CYS   A C   1 
ATOM   1795  O  O   . CYS   A 1 249 ? 13.957  40.749  -44.951 1.00 77.80  ? 318  CYS   A O   1 
ATOM   1796  C  CB  . CYS   A 1 249 ? 16.045  42.594  -44.918 1.00 77.81  ? 318  CYS   A CB  1 
ATOM   1797  S  SG  . CYS   A 1 249 ? 17.176  43.914  -44.648 1.00 79.46  ? 318  CYS   A SG  1 
ATOM   1798  N  N   . THR   A 1 250 ? 12.390  42.355  -45.100 1.00 77.99  ? 319  THR   A N   1 
ATOM   1799  C  CA  . THR   A 1 250 ? 11.232  41.496  -45.135 1.00 83.32  ? 319  THR   A CA  1 
ATOM   1800  C  C   . THR   A 1 250 ? 10.796  41.158  -46.544 1.00 86.22  ? 319  THR   A C   1 
ATOM   1801  O  O   . THR   A 1 250 ? 9.922   40.298  -46.725 1.00 84.71  ? 319  THR   A O   1 
ATOM   1802  C  CB  . THR   A 1 250 ? 10.100  42.196  -44.417 1.00 84.92  ? 319  THR   A CB  1 
ATOM   1803  O  OG1 . THR   A 1 250 ? 9.857   43.443  -45.082 1.00 80.21  ? 319  THR   A OG1 1 
ATOM   1804  C  CG2 . THR   A 1 250 ? 10.529  42.459  -42.982 1.00 88.06  ? 319  THR   A CG2 1 
ATOM   1805  N  N   . SER   A 1 251 ? 11.372  41.826  -47.536 1.00 89.36  ? 320  SER   A N   1 
ATOM   1806  C  CA  . SER   A 1 251 ? 11.170  41.487  -48.935 1.00 91.67  ? 320  SER   A CA  1 
ATOM   1807  C  C   . SER   A 1 251 ? 12.417  40.779  -49.465 1.00 91.78  ? 320  SER   A C   1 
ATOM   1808  O  O   . SER   A 1 251 ? 13.543  41.239  -49.237 1.00 90.53  ? 320  SER   A O   1 
ATOM   1809  C  CB  . SER   A 1 251 ? 10.855  42.744  -49.750 1.00 91.46  ? 320  SER   A CB  1 
ATOM   1810  O  OG  . SER   A 1 251 ? 10.434  42.433  -51.069 1.00 93.10  ? 320  SER   A OG  1 
ATOM   1811  N  N   . LEU   A 1 252 ? 12.208  39.639  -50.134 1.00 89.64  ? 321  LEU   A N   1 
ATOM   1812  C  CA  . LEU   A 1 252 ? 13.262  38.862  -50.779 1.00 85.45  ? 321  LEU   A CA  1 
ATOM   1813  C  C   . LEU   A 1 252 ? 13.204  39.086  -52.285 1.00 90.39  ? 321  LEU   A C   1 
ATOM   1814  O  O   . LEU   A 1 252 ? 12.126  38.952  -52.888 1.00 89.50  ? 321  LEU   A O   1 
ATOM   1815  C  CB  . LEU   A 1 252 ? 13.102  37.376  -50.472 1.00 82.14  ? 321  LEU   A CB  1 
ATOM   1816  C  CG  . LEU   A 1 252 ? 13.260  37.022  -49.013 1.00 81.77  ? 321  LEU   A CG  1 
ATOM   1817  C  CD1 . LEU   A 1 252 ? 13.143  35.526  -48.852 1.00 79.50  ? 321  LEU   A CD1 1 
ATOM   1818  C  CD2 . LEU   A 1 252 ? 14.589  37.568  -48.470 1.00 85.24  ? 321  LEU   A CD2 1 
ATOM   1819  N  N   . CYS   A 1 253 ? 14.355  39.419  -52.890 1.00 90.01  ? 322  CYS   A N   1 
ATOM   1820  C  CA  . CYS   A 1 253 ? 14.449  39.788  -54.306 1.00 90.85  ? 322  CYS   A CA  1 
ATOM   1821  C  C   . CYS   A 1 253 ? 15.427  38.900  -55.075 1.00 89.83  ? 322  CYS   A C   1 
ATOM   1822  O  O   . CYS   A 1 253 ? 16.138  38.073  -54.495 1.00 89.52  ? 322  CYS   A O   1 
ATOM   1823  C  CB  . CYS   A 1 253 ? 14.865  41.250  -54.449 1.00 85.13  ? 322  CYS   A CB  1 
ATOM   1824  S  SG  . CYS   A 1 253 ? 13.608  42.281  -53.780 1.00 89.77  ? 322  CYS   A SG  1 
ATOM   1825  N  N   . CYS   A 1 254 ? 15.460  39.101  -56.400 1.00 88.92  ? 323  CYS   A N   1 
ATOM   1826  C  CA  . CYS   A 1 254 ? 16.421  38.419  -57.261 1.00 92.04  ? 323  CYS   A CA  1 
ATOM   1827  C  C   . CYS   A 1 254 ? 17.829  38.965  -57.036 1.00 93.74  ? 323  CYS   A C   1 
ATOM   1828  O  O   . CYS   A 1 254 ? 18.062  40.161  -57.194 1.00 96.30  ? 323  CYS   A O   1 
ATOM   1829  C  CB  . CYS   A 1 254 ? 16.028  38.604  -58.728 1.00 93.95  ? 323  CYS   A CB  1 
ATOM   1830  S  SG  . CYS   A 1 254 ? 17.124  37.788  -59.920 1.00 104.97 ? 323  CYS   A SG  1 
ATOM   1831  N  N   . LYS   A 1 255 ? 18.778  38.090  -56.688 1.00 91.37  ? 324  LYS   A N   1 
ATOM   1832  C  CA  . LYS   A 1 255 ? 20.128  38.546  -56.368 1.00 89.75  ? 324  LYS   A CA  1 
ATOM   1833  C  C   . LYS   A 1 255 ? 20.812  39.205  -57.565 1.00 88.03  ? 324  LYS   A C   1 
ATOM   1834  O  O   . LYS   A 1 255 ? 21.618  40.116  -57.370 1.00 89.19  ? 324  LYS   A O   1 
ATOM   1835  C  CB  . LYS   A 1 255 ? 20.980  37.378  -55.843 1.00 92.17  ? 324  LYS   A CB  1 
ATOM   1836  C  CG  . LYS   A 1 255 ? 22.453  37.709  -55.489 1.00 91.52  ? 324  LYS   A CG  1 
ATOM   1837  C  CD  . LYS   A 1 255 ? 22.643  38.270  -54.067 1.00 88.88  ? 324  LYS   A CD  1 
ATOM   1838  C  CE  . LYS   A 1 255 ? 23.933  39.095  -53.921 1.00 85.12  ? 324  LYS   A CE  1 
ATOM   1839  N  NZ  . LYS   A 1 255 ? 23.964  40.329  -54.781 1.00 82.17  ? 324  LYS   A NZ  1 
ATOM   1840  N  N   . GLN   A 1 256 ? 20.494  38.781  -58.797 1.00 92.29  ? 325  GLN   A N   1 
ATOM   1841  C  CA  . GLN   A 1 256 ? 21.224  39.248  -59.987 1.00 96.20  ? 325  GLN   A CA  1 
ATOM   1842  C  C   . GLN   A 1 256 ? 20.679  40.570  -60.525 1.00 98.13  ? 325  GLN   A C   1 
ATOM   1843  O  O   . GLN   A 1 256 ? 21.319  41.619  -60.390 1.00 104.62 ? 325  GLN   A O   1 
ATOM   1844  C  CB  . GLN   A 1 256 ? 21.200  38.178  -61.083 1.00 94.36  ? 325  GLN   A CB  1 
ATOM   1845  C  CG  . GLN   A 1 256 ? 21.389  36.749  -60.576 1.00 97.18  ? 325  GLN   A CG  1 
ATOM   1846  C  CD  . GLN   A 1 256 ? 22.830  36.419  -60.182 1.00 99.30  ? 325  GLN   A CD  1 
ATOM   1847  O  OE1 . GLN   A 1 256 ? 23.573  37.283  -59.718 1.00 98.78  ? 325  GLN   A OE1 1 
ATOM   1848  N  NE2 . GLN   A 1 256 ? 23.230  35.157  -60.380 1.00 103.11 ? 325  GLN   A NE2 1 
ATOM   1849  N  N   . CYS   A 1 257 ? 19.494  40.530  -61.146 1.00 94.56  ? 326  CYS   A N   1 
ATOM   1850  C  CA  . CYS   A 1 257 ? 18.914  41.741  -61.705 1.00 97.75  ? 326  CYS   A CA  1 
ATOM   1851  C  C   . CYS   A 1 257 ? 18.530  42.741  -60.617 1.00 100.95 ? 326  CYS   A C   1 
ATOM   1852  O  O   . CYS   A 1 257 ? 18.363  43.930  -60.908 1.00 107.78 ? 326  CYS   A O   1 
ATOM   1853  C  CB  . CYS   A 1 257 ? 17.699  41.383  -62.553 1.00 95.10  ? 326  CYS   A CB  1 
ATOM   1854  S  SG  . CYS   A 1 257 ? 16.260  41.051  -61.532 1.00 95.48  ? 326  CYS   A SG  1 
ATOM   1855  N  N   . GLN   A 1 258 ? 18.405  42.260  -59.380 1.00 97.59  ? 327  GLN   A N   1 
ATOM   1856  C  CA  . GLN   A 1 258 ? 18.069  43.135  -58.226 1.00 97.25  ? 327  GLN   A CA  1 
ATOM   1857  C  C   . GLN   A 1 258 ? 16.861  44.014  -58.559 1.00 100.31 ? 327  GLN   A C   1 
ATOM   1858  O  O   . GLN   A 1 258 ? 16.862  45.185  -58.141 1.00 106.14 ? 327  GLN   A O   1 
ATOM   1859  C  CB  . GLN   A 1 258 ? 19.256  44.006  -57.824 1.00 100.08 ? 327  GLN   A CB  1 
ATOM   1860  C  CG  . GLN   A 1 258 ? 20.261  43.293  -56.928 1.00 100.49 ? 327  GLN   A CG  1 
ATOM   1861  C  CD  . GLN   A 1 258 ? 21.429  44.171  -56.543 1.00 112.94 ? 327  GLN   A CD  1 
ATOM   1862  O  OE1 . GLN   A 1 258 ? 21.298  45.392  -56.405 1.00 109.82 ? 327  GLN   A OE1 1 
ATOM   1863  N  NE2 . GLN   A 1 258 ? 22.588  43.554  -56.369 1.00 114.63 ? 327  GLN   A NE2 1 
ATOM   1864  N  N   . GLU   A 1 259 ? 15.868  43.463  -59.256 1.00 100.13 ? 328  GLU   A N   1 
ATOM   1865  C  CA  . GLU   A 1 259 ? 14.640  44.242  -59.550 1.00 100.68 ? 328  GLU   A CA  1 
ATOM   1866  C  C   . GLU   A 1 259 ? 13.468  43.284  -59.782 1.00 102.91 ? 328  GLU   A C   1 
ATOM   1867  O  O   . GLU   A 1 259 ? 12.770  43.445  -60.800 1.00 103.32 ? 328  GLU   A O   1 
ATOM   1868  C  CB  . GLU   A 1 259 ? 14.874  45.123  -60.774 1.00 108.47 ? 328  GLU   A CB  1 
ATOM   1869  N  N   . THR   A 1 260 ? 13.265  42.328  -58.876 1.00 113.63 ? 329  THR   A N   1 
ATOM   1870  C  CA  . THR   A 1 260 ? 12.163  41.355  -59.005 1.00 112.16 ? 329  THR   A CA  1 
ATOM   1871  C  C   . THR   A 1 260 ? 11.837  40.830  -57.627 1.00 106.16 ? 329  THR   A C   1 
ATOM   1872  O  O   . THR   A 1 260 ? 12.460  39.837  -57.210 1.00 104.12 ? 329  THR   A O   1 
ATOM   1873  C  CB  . THR   A 1 260 ? 12.593  40.232  -59.945 1.00 111.67 ? 329  THR   A CB  1 
ATOM   1874  O  OG1 . THR   A 1 260 ? 12.871  40.812  -61.215 1.00 110.53 ? 329  THR   A OG1 1 
ATOM   1875  C  CG2 . THR   A 1 260 ? 11.515  39.185  -60.149 1.00 109.34 ? 329  THR   A CG2 1 
ATOM   1876  N  N   . GLU   A 1 261 ? 10.921  41.491  -56.920 1.00 96.08  ? 330  GLU   A N   1 
ATOM   1877  C  CA  . GLU   A 1 261 ? 10.501  41.012  -55.581 1.00 92.79  ? 330  GLU   A CA  1 
ATOM   1878  C  C   . GLU   A 1 261 ? 9.891   39.622  -55.751 1.00 96.07  ? 330  GLU   A C   1 
ATOM   1879  O  O   . GLU   A 1 261 ? 8.901   39.503  -56.494 1.00 97.98  ? 330  GLU   A O   1 
ATOM   1880  C  CB  . GLU   A 1 261 ? 9.489   41.964  -54.951 1.00 93.58  ? 330  GLU   A CB  1 
ATOM   1881  C  CG  . GLU   A 1 261 ? 8.763   41.373  -53.747 1.00 94.51  ? 330  GLU   A CG  1 
ATOM   1882  C  CD  . GLU   A 1 261 ? 7.877   42.387  -53.052 1.00 95.11  ? 330  GLU   A CD  1 
ATOM   1883  O  OE1 . GLU   A 1 261 ? 8.401   43.446  -52.652 1.00 94.14  ? 330  GLU   A OE1 1 
ATOM   1884  O  OE2 . GLU   A 1 261 ? 6.666   42.122  -52.914 1.00 94.09  ? 330  GLU   A OE2 1 
ATOM   1885  N  N   . ILE   A 1 262 ? 10.460  38.615  -55.093 1.00 95.08  ? 331  ILE   A N   1 
ATOM   1886  C  CA  . ILE   A 1 262 ? 9.967   37.260  -55.307 1.00 93.67  ? 331  ILE   A CA  1 
ATOM   1887  C  C   . ILE   A 1 262 ? 8.928   36.909  -54.259 1.00 96.33  ? 331  ILE   A C   1 
ATOM   1888  O  O   . ILE   A 1 262 ? 7.815   36.473  -54.582 1.00 97.48  ? 331  ILE   A O   1 
ATOM   1889  C  CB  . ILE   A 1 262 ? 11.138  36.261  -55.276 1.00 93.10  ? 331  ILE   A CB  1 
ATOM   1890  C  CG1 . ILE   A 1 262 ? 12.262  36.700  -56.201 1.00 93.09  ? 331  ILE   A CG1 1 
ATOM   1891  C  CG2 . ILE   A 1 262 ? 10.661  34.874  -55.653 1.00 96.07  ? 331  ILE   A CG2 1 
ATOM   1892  C  CD1 . ILE   A 1 262 ? 11.998  36.365  -57.618 1.00 97.03  ? 331  ILE   A CD1 1 
ATOM   1893  N  N   . THR   A 1 263 ? 9.281   37.104  -52.988 1.00 93.61  ? 332  THR   A N   1 
ATOM   1894  C  CA  . THR   A 1 263 ? 8.438   36.685  -51.878 1.00 93.60  ? 332  THR   A CA  1 
ATOM   1895  C  C   . THR   A 1 263 ? 8.685   37.644  -50.710 1.00 91.07  ? 332  THR   A C   1 
ATOM   1896  O  O   . THR   A 1 263 ? 9.575   38.500  -50.758 1.00 85.34  ? 332  THR   A O   1 
ATOM   1897  C  CB  . THR   A 1 263 ? 8.699   35.202  -51.537 1.00 87.61  ? 332  THR   A CB  1 
ATOM   1898  O  OG1 . THR   A 1 263 ? 7.683   34.698  -50.665 1.00 87.70  ? 332  THR   A OG1 1 
ATOM   1899  C  CG2 . THR   A 1 263 ? 10.058  35.030  -50.880 1.00 89.02  ? 332  THR   A CG2 1 
ATOM   1900  N  N   . THR   A 1 264 ? 7.869   37.491  -49.659 1.00 91.77  ? 333  THR   A N   1 
ATOM   1901  C  CA  . THR   A 1 264 ? 7.826   38.409  -48.526 1.00 90.14  ? 333  THR   A CA  1 
ATOM   1902  C  C   . THR   A 1 264 ? 7.688   37.622  -47.218 1.00 91.26  ? 333  THR   A C   1 
ATOM   1903  O  O   . THR   A 1 264 ? 7.129   36.521  -47.198 1.00 90.93  ? 333  THR   A O   1 
ATOM   1904  C  CB  . THR   A 1 264 ? 6.671   39.405  -48.699 1.00 90.86  ? 333  THR   A CB  1 
ATOM   1905  O  OG1 . THR   A 1 264 ? 6.494   40.140  -47.483 1.00 100.29 ? 333  THR   A OG1 1 
ATOM   1906  C  CG2 . THR   A 1 264 ? 5.363   38.676  -49.062 1.00 91.85  ? 333  THR   A CG2 1 
ATOM   1907  N  N   . LYS   A 1 265 ? 8.177   38.209  -46.115 1.00 88.51  ? 334  LYS   A N   1 
ATOM   1908  C  CA  . LYS   A 1 265 ? 8.408   37.433  -44.893 1.00 88.14  ? 334  LYS   A CA  1 
ATOM   1909  C  C   . LYS   A 1 265 ? 7.172   36.682  -44.442 1.00 91.85  ? 334  LYS   A C   1 
ATOM   1910  O  O   . LYS   A 1 265 ? 7.292   35.599  -43.858 1.00 97.05  ? 334  LYS   A O   1 
ATOM   1911  C  CB  . LYS   A 1 265 ? 8.898   38.332  -43.752 1.00 86.38  ? 334  LYS   A CB  1 
ATOM   1912  N  N   . ASN   A 1 266 ? 5.985   37.218  -44.696 1.00 92.37  ? 335  ASN   A N   1 
ATOM   1913  C  CA  . ASN   A 1 266 ? 4.783   36.599  -44.162 1.00 93.65  ? 335  ASN   A CA  1 
ATOM   1914  C  C   . ASN   A 1 266 ? 4.317   35.419  -44.993 1.00 95.24  ? 335  ASN   A C   1 
ATOM   1915  O  O   . ASN   A 1 266 ? 3.317   34.794  -44.635 1.00 97.66  ? 335  ASN   A O   1 
ATOM   1916  C  CB  . ASN   A 1 266 ? 3.669   37.636  -44.042 1.00 95.70  ? 335  ASN   A CB  1 
ATOM   1917  C  CG  . ASN   A 1 266 ? 3.580   38.522  -45.260 1.00 100.04 ? 335  ASN   A CG  1 
ATOM   1918  O  OD1 . ASN   A 1 266 ? 3.239   38.068  -46.354 1.00 111.42 ? 335  ASN   A OD1 1 
ATOM   1919  N  ND2 . ASN   A 1 266 ? 3.894   39.800  -45.084 1.00 98.42  ? 335  ASN   A ND2 1 
ATOM   1920  N  N   . GLU   A 1 267 ? 5.005   35.095  -46.082 1.00 95.30  ? 336  GLU   A N   1 
ATOM   1921  C  CA  . GLU   A 1 267 ? 4.671   33.915  -46.874 1.00 95.68  ? 336  GLU   A CA  1 
ATOM   1922  C  C   . GLU   A 1 267 ? 5.586   32.743  -46.585 1.00 92.00  ? 336  GLU   A C   1 
ATOM   1923  O  O   . GLU   A 1 267 ? 5.428   31.690  -47.200 1.00 91.28  ? 336  GLU   A O   1 
ATOM   1924  C  CB  . GLU   A 1 267 ? 4.713   34.219  -48.381 1.00 97.37  ? 336  GLU   A CB  1 
ATOM   1925  C  CG  . GLU   A 1 267 ? 3.749   35.316  -48.863 1.00 99.72  ? 336  GLU   A CG  1 
ATOM   1926  C  CD  . GLU   A 1 267 ? 2.259   35.009  -48.591 1.00 103.81 ? 336  GLU   A CD  1 
ATOM   1927  O  OE1 . GLU   A 1 267 ? 1.872   33.814  -48.457 1.00 104.10 ? 336  GLU   A OE1 1 
ATOM   1928  O  OE2 . GLU   A 1 267 ? 1.465   35.979  -48.522 1.00 104.23 ? 336  GLU   A OE2 1 
ATOM   1929  N  N   . ILE   A 1 268 ? 6.561   32.913  -45.700 1.00 88.89  ? 337  ILE   A N   1 
ATOM   1930  C  CA  . ILE   A 1 268 ? 7.430   31.808  -45.333 1.00 86.68  ? 337  ILE   A CA  1 
ATOM   1931  C  C   . ILE   A 1 268 ? 6.662   30.877  -44.411 1.00 90.06  ? 337  ILE   A C   1 
ATOM   1932  O  O   . ILE   A 1 268 ? 5.975   31.319  -43.480 1.00 93.86  ? 337  ILE   A O   1 
ATOM   1933  C  CB  . ILE   A 1 268 ? 8.707   32.323  -44.652 1.00 85.69  ? 337  ILE   A CB  1 
ATOM   1934  C  CG1 . ILE   A 1 268 ? 9.529   33.196  -45.595 1.00 83.00  ? 337  ILE   A CG1 1 
ATOM   1935  C  CG2 . ILE   A 1 268 ? 9.538   31.174  -44.130 1.00 87.56  ? 337  ILE   A CG2 1 
ATOM   1936  C  CD1 . ILE   A 1 268 ? 10.808  33.710  -44.981 1.00 78.51  ? 337  ILE   A CD1 1 
ATOM   1937  N  N   . PHE   A 1 269 ? 6.759   29.583  -44.669 1.00 87.33  ? 338  PHE   A N   1 
ATOM   1938  C  CA  . PHE   A 1 269 ? 6.248   28.606  -43.725 1.00 90.09  ? 338  PHE   A CA  1 
ATOM   1939  C  C   . PHE   A 1 269 ? 7.295   27.503  -43.628 1.00 92.48  ? 338  PHE   A C   1 
ATOM   1940  O  O   . PHE   A 1 269 ? 8.473   27.718  -43.938 1.00 91.28  ? 338  PHE   A O   1 
ATOM   1941  C  CB  . PHE   A 1 269 ? 4.842   28.145  -44.133 1.00 89.62  ? 338  PHE   A CB  1 
ATOM   1942  C  CG  . PHE   A 1 269 ? 4.812   27.249  -45.327 1.00 90.81  ? 338  PHE   A CG  1 
ATOM   1943  C  CD1 . PHE   A 1 269 ? 5.221   27.701  -46.564 1.00 92.94  ? 338  PHE   A CD1 1 
ATOM   1944  C  CD2 . PHE   A 1 269 ? 4.363   25.949  -45.216 1.00 96.30  ? 338  PHE   A CD2 1 
ATOM   1945  C  CE1 . PHE   A 1 269 ? 5.197   26.866  -47.654 1.00 93.10  ? 338  PHE   A CE1 1 
ATOM   1946  C  CE2 . PHE   A 1 269 ? 4.329   25.108  -46.312 1.00 95.83  ? 338  PHE   A CE2 1 
ATOM   1947  C  CZ  . PHE   A 1 269 ? 4.745   25.565  -47.523 1.00 93.11  ? 338  PHE   A CZ  1 
ATOM   1948  N  N   . SER   A 1 270 ? 6.885   26.312  -43.173 1.00 94.63  ? 339  SER   A N   1 
ATOM   1949  C  CA  . SER   A 1 270 ? 7.822   25.194  -43.015 1.00 98.28  ? 339  SER   A CA  1 
ATOM   1950  C  C   . SER   A 1 270 ? 7.065   23.904  -43.325 1.00 102.84 ? 339  SER   A C   1 
ATOM   1951  O  O   . SER   A 1 270 ? 6.420   23.328  -42.451 1.00 108.74 ? 339  SER   A O   1 
ATOM   1952  C  CB  . SER   A 1 270 ? 8.427   25.156  -41.622 1.00 100.07 ? 339  SER   A CB  1 
ATOM   1953  O  OG  . SER   A 1 270 ? 9.282   26.261  -41.427 1.00 97.41  ? 339  SER   A OG  1 
ATOM   1954  N  N   . LEU   A 1 271 ? 7.169   23.462  -44.580 1.00 105.96 ? 340  LEU   A N   1 
ATOM   1955  C  CA  . LEU   A 1 271 ? 6.365   22.338  -45.041 1.00 108.01 ? 340  LEU   A CA  1 
ATOM   1956  C  C   . LEU   A 1 271 ? 6.595   21.110  -44.180 1.00 118.38 ? 340  LEU   A C   1 
ATOM   1957  O  O   . LEU   A 1 271 ? 5.643   20.417  -43.803 1.00 121.45 ? 340  LEU   A O   1 
ATOM   1958  C  CB  . LEU   A 1 271 ? 6.690   22.031  -46.491 1.00 99.80  ? 340  LEU   A CB  1 
ATOM   1959  C  CG  . LEU   A 1 271 ? 5.846   20.866  -46.948 1.00 101.34 ? 340  LEU   A CG  1 
ATOM   1960  C  CD1 . LEU   A 1 271 ? 4.363   21.275  -47.039 1.00 104.44 ? 340  LEU   A CD1 1 
ATOM   1961  C  CD2 . LEU   A 1 271 ? 6.398   20.369  -48.255 1.00 102.26 ? 340  LEU   A CD2 1 
ATOM   1962  N  N   . SER   A 1 272 ? 7.853   20.837  -43.846 1.00 133.56 ? 341  SER   A N   1 
ATOM   1963  C  CA  . SER   A 1 272 ? 8.218   19.727  -42.981 1.00 136.94 ? 341  SER   A CA  1 
ATOM   1964  C  C   . SER   A 1 272 ? 8.811   20.255  -41.687 1.00 133.76 ? 341  SER   A C   1 
ATOM   1965  O  O   . SER   A 1 272 ? 9.121   21.443  -41.546 1.00 132.70 ? 341  SER   A O   1 
ATOM   1966  C  CB  . SER   A 1 272 ? 9.203   18.777  -43.672 1.00 141.01 ? 341  SER   A CB  1 
ATOM   1967  O  OG  . SER   A 1 272 ? 8.526   17.922  -44.584 1.00 141.17 ? 341  SER   A OG  1 
ATOM   1968  N  N   . LEU   A 1 273 ? 8.977   19.337  -40.740 1.00 130.76 ? 342  LEU   A N   1 
ATOM   1969  C  CA  . LEU   A 1 273 ? 9.471   19.659  -39.411 1.00 131.71 ? 342  LEU   A CA  1 
ATOM   1970  C  C   . LEU   A 1 273 ? 10.936  20.068  -39.395 1.00 128.58 ? 342  LEU   A C   1 
ATOM   1971  O  O   . LEU   A 1 273 ? 11.459  20.356  -38.314 1.00 129.71 ? 342  LEU   A O   1 
ATOM   1972  C  CB  . LEU   A 1 273 ? 9.258   18.457  -38.489 1.00 136.15 ? 342  LEU   A CB  1 
ATOM   1973  C  CG  . LEU   A 1 273 ? 9.897   17.138  -38.941 1.00 137.10 ? 342  LEU   A CG  1 
ATOM   1974  C  CD1 . LEU   A 1 273 ? 11.208  16.890  -38.196 1.00 136.76 ? 342  LEU   A CD1 1 
ATOM   1975  C  CD2 . LEU   A 1 273 ? 8.932   15.954  -38.772 1.00 131.24 ? 342  LEU   A CD2 1 
ATOM   1976  N  N   . CYS   A 1 274 ? 11.609  20.111  -40.545 1.00 127.98 ? 343  CYS   A N   1 
ATOM   1977  C  CA  . CYS   A 1 274 ? 13.049  20.346  -40.580 1.00 126.24 ? 343  CYS   A CA  1 
ATOM   1978  C  C   . CYS   A 1 274 ? 13.426  21.824  -40.611 1.00 121.50 ? 343  CYS   A C   1 
ATOM   1979  O  O   . CYS   A 1 274 ? 14.621  22.138  -40.555 1.00 117.11 ? 343  CYS   A O   1 
ATOM   1980  C  CB  . CYS   A 1 274 ? 13.652  19.640  -41.795 1.00 130.96 ? 343  CYS   A CB  1 
ATOM   1981  S  SG  . CYS   A 1 274 ? 12.790  18.112  -42.233 1.00 138.39 ? 343  CYS   A SG  1 
ATOM   1982  N  N   . GLY   A 1 275 ? 12.448  22.725  -40.703 1.00 116.63 ? 344  GLY   A N   1 
ATOM   1983  C  CA  . GLY   A 1 275 ? 12.696  24.147  -40.798 1.00 109.03 ? 344  GLY   A CA  1 
ATOM   1984  C  C   . GLY   A 1 275 ? 11.852  24.821  -41.865 1.00 98.91  ? 344  GLY   A C   1 
ATOM   1985  O  O   . GLY   A 1 275 ? 10.924  24.221  -42.421 1.00 100.43 ? 344  GLY   A O   1 
ATOM   1986  N  N   . PRO   A 1 276 ? 12.140  26.099  -42.161 1.00 91.09  ? 345  PRO   A N   1 
ATOM   1987  C  CA  . PRO   A 1 276 ? 11.563  26.715  -43.356 1.00 86.29  ? 345  PRO   A CA  1 
ATOM   1988  C  C   . PRO   A 1 276 ? 12.576  26.636  -44.478 1.00 89.28  ? 345  PRO   A C   1 
ATOM   1989  O  O   . PRO   A 1 276 ? 12.294  26.109  -45.561 1.00 96.22  ? 345  PRO   A O   1 
ATOM   1990  C  CB  . PRO   A 1 276 ? 11.360  28.187  -42.973 1.00 83.87  ? 345  PRO   A CB  1 
ATOM   1991  C  CG  . PRO   A 1 276 ? 11.654  28.279  -41.522 1.00 92.23  ? 345  PRO   A CG  1 
ATOM   1992  C  CD  . PRO   A 1 276 ? 12.550  27.119  -41.195 1.00 96.19  ? 345  PRO   A CD  1 
ATOM   1993  N  N   . MET   A 1 277 ? 13.789  27.112  -44.200 1.00 86.96  ? 346  MET   A N   1 
ATOM   1994  C  CA  . MET   A 1 277 ? 14.884  27.094  -45.169 1.00 80.85  ? 346  MET   A CA  1 
ATOM   1995  C  C   . MET   A 1 277 ? 15.823  25.970  -44.725 1.00 80.21  ? 346  MET   A C   1 
ATOM   1996  O  O   . MET   A 1 277 ? 16.884  26.196  -44.151 1.00 84.63  ? 346  MET   A O   1 
ATOM   1997  C  CB  . MET   A 1 277 ? 15.593  28.440  -45.247 1.00 80.91  ? 346  MET   A CB  1 
ATOM   1998  C  CG  . MET   A 1 277 ? 16.512  28.562  -46.401 1.00 82.52  ? 346  MET   A CG  1 
ATOM   1999  S  SD  . MET   A 1 277 ? 17.726  29.844  -46.121 1.00 88.48  ? 346  MET   A SD  1 
ATOM   2000  C  CE  . MET   A 1 277 ? 18.753  29.135  -44.840 1.00 86.32  ? 346  MET   A CE  1 
ATOM   2001  N  N   . ALA   A 1 278 ? 15.413  24.735  -44.994 1.00 76.89  ? 347  ALA   A N   1 
ATOM   2002  C  CA  . ALA   A 1 278 ? 16.310  23.616  -44.770 1.00 80.81  ? 347  ALA   A CA  1 
ATOM   2003  C  C   . ALA   A 1 278 ? 17.281  23.502  -45.941 1.00 82.92  ? 347  ALA   A C   1 
ATOM   2004  O  O   . ALA   A 1 278 ? 17.154  24.211  -46.938 1.00 85.42  ? 347  ALA   A O   1 
ATOM   2005  C  CB  . ALA   A 1 278 ? 15.508  22.335  -44.595 1.00 90.14  ? 347  ALA   A CB  1 
ATOM   2006  N  N   . ALA   A 1 279 ? 18.267  22.610  -45.825 1.00 82.70  ? 348  ALA   A N   1 
ATOM   2007  C  CA  . ALA   A 1 279 ? 19.197  22.318  -46.918 1.00 83.29  ? 348  ALA   A CA  1 
ATOM   2008  C  C   . ALA   A 1 279 ? 18.925  20.926  -47.476 1.00 86.21  ? 348  ALA   A C   1 
ATOM   2009  O  O   . ALA   A 1 279 ? 18.907  19.953  -46.714 1.00 93.03  ? 348  ALA   A O   1 
ATOM   2010  C  CB  . ALA   A 1 279 ? 20.646  22.415  -46.445 1.00 84.53  ? 348  ALA   A CB  1 
ATOM   2011  N  N   . TYR   A 1 280 ? 18.710  20.834  -48.796 1.00 84.17  ? 349  TYR   A N   1 
ATOM   2012  C  CA  . TYR   A 1 280 ? 18.364  19.591  -49.481 1.00 85.20  ? 349  TYR   A CA  1 
ATOM   2013  C  C   . TYR   A 1 280 ? 19.437  19.286  -50.513 1.00 89.80  ? 349  TYR   A C   1 
ATOM   2014  O  O   . TYR   A 1 280 ? 20.215  20.164  -50.891 1.00 91.62  ? 349  TYR   A O   1 
ATOM   2015  C  CB  . TYR   A 1 280 ? 16.989  19.661  -50.173 1.00 87.09  ? 349  TYR   A CB  1 
ATOM   2016  C  CG  . TYR   A 1 280 ? 15.835  20.030  -49.258 1.00 87.37  ? 349  TYR   A CG  1 
ATOM   2017  C  CD1 . TYR   A 1 280 ? 15.746  21.304  -48.735 1.00 88.13  ? 349  TYR   A CD1 1 
ATOM   2018  C  CD2 . TYR   A 1 280 ? 14.835  19.114  -48.927 1.00 89.41  ? 349  TYR   A CD2 1 
ATOM   2019  C  CE1 . TYR   A 1 280 ? 14.720  21.674  -47.903 1.00 90.83  ? 349  TYR   A CE1 1 
ATOM   2020  C  CE2 . TYR   A 1 280 ? 13.793  19.473  -48.082 1.00 89.96  ? 349  TYR   A CE2 1 
ATOM   2021  C  CZ  . TYR   A 1 280 ? 13.748  20.768  -47.572 1.00 94.12  ? 349  TYR   A CZ  1 
ATOM   2022  O  OH  . TYR   A 1 280 ? 12.748  21.205  -46.719 1.00 104.12 ? 349  TYR   A OH  1 
ATOM   2023  N  N   . VAL   A 1 281 ? 19.491  18.034  -50.967 1.00 91.96  ? 350  VAL   A N   1 
ATOM   2024  C  CA  . VAL   A 1 281 ? 20.531  17.607  -51.895 1.00 94.55  ? 350  VAL   A CA  1 
ATOM   2025  C  C   . VAL   A 1 281 ? 19.895  17.023  -53.138 1.00 102.37 ? 350  VAL   A C   1 
ATOM   2026  O  O   . VAL   A 1 281 ? 19.044  16.129  -53.049 1.00 104.05 ? 350  VAL   A O   1 
ATOM   2027  C  CB  . VAL   A 1 281 ? 21.490  16.573  -51.289 1.00 96.55  ? 350  VAL   A CB  1 
ATOM   2028  C  CG1 . VAL   A 1 281 ? 22.677  16.425  -52.204 1.00 98.29  ? 350  VAL   A CG1 1 
ATOM   2029  C  CG2 . VAL   A 1 281 ? 21.918  16.951  -49.872 1.00 101.99 ? 350  VAL   A CG2 1 
ATOM   2030  N  N   . ASN   A 1 282 ? 20.346  17.501  -54.293 1.00 108.77 ? 351  ASN   A N   1 
ATOM   2031  C  CA  . ASN   A 1 282 ? 19.884  17.011  -55.583 1.00 109.07 ? 351  ASN   A CA  1 
ATOM   2032  C  C   . ASN   A 1 282 ? 20.666  15.754  -55.946 1.00 110.30 ? 351  ASN   A C   1 
ATOM   2033  O  O   . ASN   A 1 282 ? 21.681  15.428  -55.316 1.00 110.92 ? 351  ASN   A O   1 
ATOM   2034  C  CB  . ASN   A 1 282 ? 20.006  18.121  -56.636 1.00 106.33 ? 351  ASN   A CB  1 
ATOM   2035  C  CG  . ASN   A 1 282 ? 21.417  18.277  -57.207 1.00 109.26 ? 351  ASN   A CG  1 
ATOM   2036  O  OD1 . ASN   A 1 282 ? 22.421  17.913  -56.588 1.00 111.18 ? 351  ASN   A OD1 1 
ATOM   2037  N  ND2 . ASN   A 1 282 ? 21.491  18.853  -58.396 1.00 109.57 ? 351  ASN   A ND2 1 
ATOM   2038  N  N   . PRO   A 1 283 ? 20.218  15.009  -56.948 1.00 108.38 ? 352  PRO   A N   1 
ATOM   2039  C  CA  . PRO   A 1 283 ? 20.866  13.729  -57.222 1.00 106.77 ? 352  PRO   A CA  1 
ATOM   2040  C  C   . PRO   A 1 283 ? 22.288  13.859  -57.728 1.00 101.31 ? 352  PRO   A C   1 
ATOM   2041  O  O   . PRO   A 1 283 ? 22.891  12.856  -58.106 1.00 106.21 ? 352  PRO   A O   1 
ATOM   2042  C  CB  . PRO   A 1 283 ? 19.950  13.097  -58.272 1.00 106.28 ? 352  PRO   A CB  1 
ATOM   2043  C  CG  . PRO   A 1 283 ? 19.220  14.197  -58.847 1.00 104.29 ? 352  PRO   A CG  1 
ATOM   2044  C  CD  . PRO   A 1 283 ? 19.013  15.178  -57.767 1.00 106.81 ? 352  PRO   A CD  1 
ATOM   2045  N  N   . HIS   A 1 284 ? 22.850  15.063  -57.742 1.00 99.05  ? 353  HIS   A N   1 
ATOM   2046  C  CA  . HIS   A 1 284 ? 24.250  15.234  -58.107 1.00 100.22 ? 353  HIS   A CA  1 
ATOM   2047  C  C   . HIS   A 1 284 ? 25.060  15.905  -57.008 1.00 100.55 ? 353  HIS   A C   1 
ATOM   2048  O  O   . HIS   A 1 284 ? 26.157  16.416  -57.281 1.00 101.32 ? 353  HIS   A O   1 
ATOM   2049  C  CB  . HIS   A 1 284 ? 24.385  16.029  -59.411 1.00 103.55 ? 353  HIS   A CB  1 
ATOM   2050  C  CG  . HIS   A 1 284 ? 23.821  15.328  -60.610 1.00 103.95 ? 353  HIS   A CG  1 
ATOM   2051  N  ND1 . HIS   A 1 284 ? 24.454  14.265  -61.220 1.00 100.47 ? 353  HIS   A ND1 1 
ATOM   2052  C  CD2 . HIS   A 1 284 ? 22.689  15.551  -61.322 1.00 105.01 ? 353  HIS   A CD2 1 
ATOM   2053  C  CE1 . HIS   A 1 284 ? 23.727  13.858  -62.247 1.00 105.21 ? 353  HIS   A CE1 1 
ATOM   2054  N  NE2 . HIS   A 1 284 ? 22.652  14.621  -62.331 1.00 103.22 ? 353  HIS   A NE2 1 
ATOM   2055  N  N   . GLY   A 1 285 ? 24.558  15.919  -55.778 1.00 99.46  ? 354  GLY   A N   1 
ATOM   2056  C  CA  . GLY   A 1 285 ? 25.311  16.444  -54.658 1.00 102.97 ? 354  GLY   A CA  1 
ATOM   2057  C  C   . GLY   A 1 285 ? 25.243  17.943  -54.475 1.00 99.45  ? 354  GLY   A C   1 
ATOM   2058  O  O   . GLY   A 1 285 ? 25.816  18.467  -53.505 1.00 98.88  ? 354  GLY   A O   1 
ATOM   2059  N  N   . TYR   A 1 286 ? 24.576  18.657  -55.367 1.00 98.31  ? 355  TYR   A N   1 
ATOM   2060  C  CA  . TYR   A 1 286 ? 24.369  20.070  -55.135 1.00 96.72  ? 355  TYR   A CA  1 
ATOM   2061  C  C   . TYR   A 1 286 ? 23.440  20.247  -53.937 1.00 97.57  ? 355  TYR   A C   1 
ATOM   2062  O  O   . TYR   A 1 286 ? 22.446  19.524  -53.799 1.00 97.91  ? 355  TYR   A O   1 
ATOM   2063  C  CB  . TYR   A 1 286 ? 23.813  20.727  -56.399 1.00 98.43  ? 355  TYR   A CB  1 
ATOM   2064  C  CG  . TYR   A 1 286 ? 24.842  20.780  -57.514 1.00 99.05  ? 355  TYR   A CG  1 
ATOM   2065  C  CD1 . TYR   A 1 286 ? 25.915  21.667  -57.444 1.00 98.15  ? 355  TYR   A CD1 1 
ATOM   2066  C  CD2 . TYR   A 1 286 ? 24.760  19.934  -58.617 1.00 97.19  ? 355  TYR   A CD2 1 
ATOM   2067  C  CE1 . TYR   A 1 286 ? 26.869  21.725  -58.437 1.00 92.32  ? 355  TYR   A CE1 1 
ATOM   2068  C  CE2 . TYR   A 1 286 ? 25.713  19.989  -59.624 1.00 99.50  ? 355  TYR   A CE2 1 
ATOM   2069  C  CZ  . TYR   A 1 286 ? 26.765  20.892  -59.524 1.00 95.67  ? 355  TYR   A CZ  1 
ATOM   2070  O  OH  . TYR   A 1 286 ? 27.718  20.965  -60.514 1.00 96.91  ? 355  TYR   A OH  1 
ATOM   2071  N  N   . VAL   A 1 287 ? 23.803  21.170  -53.033 1.00 96.60  ? 356  VAL   A N   1 
ATOM   2072  C  CA  . VAL   A 1 287 ? 23.015  21.478  -51.847 1.00 89.79  ? 356  VAL   A CA  1 
ATOM   2073  C  C   . VAL   A 1 287 ? 22.240  22.758  -52.098 1.00 85.75  ? 356  VAL   A C   1 
ATOM   2074  O  O   . VAL   A 1 287 ? 22.751  23.689  -52.722 1.00 91.51  ? 356  VAL   A O   1 
ATOM   2075  C  CB  . VAL   A 1 287 ? 23.904  21.620  -50.599 1.00 88.85  ? 356  VAL   A CB  1 
ATOM   2076  C  CG1 . VAL   A 1 287 ? 23.055  21.534  -49.343 1.00 92.64  ? 356  VAL   A CG1 1 
ATOM   2077  C  CG2 . VAL   A 1 287 ? 24.986  20.567  -50.596 1.00 89.71  ? 356  VAL   A CG2 1 
ATOM   2078  N  N   . HIS   A 1 288 ? 21.005  22.811  -51.611 1.00 83.75  ? 357  HIS   A N   1 
ATOM   2079  C  CA  . HIS   A 1 288 ? 20.095  23.908  -51.933 1.00 84.97  ? 357  HIS   A CA  1 
ATOM   2080  C  C   . HIS   A 1 288 ? 19.340  24.308  -50.672 1.00 84.53  ? 357  HIS   A C   1 
ATOM   2081  O  O   . HIS   A 1 288 ? 18.281  23.741  -50.384 1.00 83.23  ? 357  HIS   A O   1 
ATOM   2082  C  CB  . HIS   A 1 288 ? 19.123  23.500  -53.038 1.00 88.06  ? 357  HIS   A CB  1 
ATOM   2083  C  CG  . HIS   A 1 288 ? 19.681  23.626  -54.421 1.00 89.69  ? 357  HIS   A CG  1 
ATOM   2084  N  ND1 . HIS   A 1 288 ? 19.934  24.845  -55.012 1.00 85.80  ? 357  HIS   A ND1 1 
ATOM   2085  C  CD2 . HIS   A 1 288 ? 20.022  22.686  -55.335 1.00 91.17  ? 357  HIS   A CD2 1 
ATOM   2086  C  CE1 . HIS   A 1 288 ? 20.420  24.649  -56.226 1.00 90.06  ? 357  HIS   A CE1 1 
ATOM   2087  N  NE2 . HIS   A 1 288 ? 20.480  23.348  -56.448 1.00 91.93  ? 357  HIS   A NE2 1 
ATOM   2088  N  N   . GLU   A 1 289 ? 19.867  25.286  -49.934 1.00 83.45  ? 358  GLU   A N   1 
ATOM   2089  C  CA  . GLU   A 1 289 ? 19.079  25.861  -48.853 1.00 79.91  ? 358  GLU   A CA  1 
ATOM   2090  C  C   . GLU   A 1 289 ? 17.853  26.342  -49.630 1.00 80.77  ? 358  GLU   A C   1 
ATOM   2091  O  O   . GLU   A 1 289 ? 17.971  27.162  -50.546 1.00 81.89  ? 358  GLU   A O   1 
ATOM   2092  C  CB  . GLU   A 1 289 ? 19.894  26.923  -48.091 1.00 81.32  ? 358  GLU   A CB  1 
ATOM   2093  C  CG  . GLU   A 1 289 ? 21.419  26.682  -48.061 1.00 81.37  ? 358  GLU   A CG  1 
ATOM   2094  C  CD  . GLU   A 1 289 ? 22.212  27.711  -47.208 1.00 82.24  ? 358  GLU   A CD  1 
ATOM   2095  O  OE1 . GLU   A 1 289 ? 21.931  27.879  -45.992 1.00 84.59  ? 358  GLU   A OE1 1 
ATOM   2096  O  OE2 . GLU   A 1 289 ? 23.149  28.341  -47.755 1.00 80.43  ? 358  GLU   A OE2 1 
ATOM   2097  N  N   . THR   A 1 290 ? 16.673  25.818  -49.307 1.00 77.93  ? 359  THR   A N   1 
ATOM   2098  C  CA  . THR   A 1 290 ? 15.461  26.107  -50.061 1.00 80.20  ? 359  THR   A CA  1 
ATOM   2099  C  C   . THR   A 1 290 ? 14.432  26.592  -49.037 1.00 79.48  ? 359  THR   A C   1 
ATOM   2100  O  O   . THR   A 1 290 ? 13.940  25.818  -48.210 1.00 79.82  ? 359  THR   A O   1 
ATOM   2101  C  CB  . THR   A 1 290 ? 14.917  24.946  -50.895 1.00 83.49  ? 359  THR   A CB  1 
ATOM   2102  O  OG1 . THR   A 1 290 ? 14.899  23.768  -50.101 1.00 90.11  ? 359  THR   A OG1 1 
ATOM   2103  C  CG2 . THR   A 1 290 ? 15.818  24.661  -52.035 1.00 85.18  ? 359  THR   A CG2 1 
ATOM   2104  N  N   . LEU   A 1 291 ? 14.107  27.871  -49.110 1.00 77.95  ? 360  LEU   A N   1 
ATOM   2105  C  CA  . LEU   A 1 291 ? 13.161  28.500  -48.201 1.00 77.71  ? 360  LEU   A CA  1 
ATOM   2106  C  C   . LEU   A 1 291 ? 11.744  28.239  -48.695 1.00 81.35  ? 360  LEU   A C   1 
ATOM   2107  O  O   . LEU   A 1 291 ? 11.316  28.806  -49.702 1.00 85.37  ? 360  LEU   A O   1 
ATOM   2108  C  CB  . LEU   A 1 291 ? 13.461  29.989  -48.140 1.00 78.11  ? 360  LEU   A CB  1 
ATOM   2109  C  CG  . LEU   A 1 291 ? 12.436  30.891  -47.480 1.00 80.02  ? 360  LEU   A CG  1 
ATOM   2110  C  CD1 . LEU   A 1 291 ? 12.420  30.527  -46.014 1.00 86.56  ? 360  LEU   A CD1 1 
ATOM   2111  C  CD2 . LEU   A 1 291 ? 12.777  32.356  -47.712 1.00 77.84  ? 360  LEU   A CD2 1 
ATOM   2112  N  N   . THR   A 1 292 ? 10.998  27.394  -48.004 1.00 84.04  ? 361  THR   A N   1 
ATOM   2113  C  CA  . THR   A 1 292 ? 9.633   27.107  -48.430 1.00 83.82  ? 361  THR   A CA  1 
ATOM   2114  C  C   . THR   A 1 292 ? 8.736   28.321  -48.188 1.00 82.46  ? 361  THR   A C   1 
ATOM   2115  O  O   . THR   A 1 292 ? 8.598   28.785  -47.055 1.00 86.69  ? 361  THR   A O   1 
ATOM   2116  C  CB  . THR   A 1 292 ? 9.104   25.881  -47.688 1.00 87.29  ? 361  THR   A CB  1 
ATOM   2117  O  OG1 . THR   A 1 292 ? 9.312   26.047  -46.281 1.00 87.11  ? 361  THR   A OG1 1 
ATOM   2118  C  CG2 . THR   A 1 292 ? 9.833   24.617  -48.146 1.00 88.99  ? 361  THR   A CG2 1 
ATOM   2119  N  N   . VAL   A 1 293 ? 8.130   28.848  -49.244 1.00 84.86  ? 362  VAL   A N   1 
ATOM   2120  C  CA  . VAL   A 1 293 ? 7.162   29.932  -49.113 1.00 88.63  ? 362  VAL   A CA  1 
ATOM   2121  C  C   . VAL   A 1 293 ? 5.822   29.489  -49.703 1.00 91.65  ? 362  VAL   A C   1 
ATOM   2122  O  O   . VAL   A 1 293 ? 5.735   28.526  -50.473 1.00 90.83  ? 362  VAL   A O   1 
ATOM   2123  C  CB  . VAL   A 1 293 ? 7.644   31.239  -49.778 1.00 86.92  ? 362  VAL   A CB  1 
ATOM   2124  C  CG1 . VAL   A 1 293 ? 9.039   31.572  -49.298 1.00 85.60  ? 362  VAL   A CG1 1 
ATOM   2125  C  CG2 . VAL   A 1 293 ? 7.604   31.113  -51.287 1.00 84.11  ? 362  VAL   A CG2 1 
ATOM   2126  N  N   . TYR   A 1 294 ? 4.759   30.212  -49.319 1.00 94.18  ? 363  TYR   A N   1 
ATOM   2127  C  CA  . TYR   A 1 294 ? 3.402   29.873  -49.759 1.00 93.79  ? 363  TYR   A CA  1 
ATOM   2128  C  C   . TYR   A 1 294 ? 3.107   30.415  -51.157 1.00 92.18  ? 363  TYR   A C   1 
ATOM   2129  O  O   . TYR   A 1 294 ? 2.515   29.716  -51.993 1.00 91.26  ? 363  TYR   A O   1 
ATOM   2130  C  CB  . TYR   A 1 294 ? 2.370   30.406  -48.748 1.00 91.94  ? 363  TYR   A CB  1 
ATOM   2131  C  CG  . TYR   A 1 294 ? 2.043   29.441  -47.615 1.00 93.29  ? 363  TYR   A CG  1 
ATOM   2132  C  CD1 . TYR   A 1 294 ? 1.673   28.120  -47.879 1.00 96.35  ? 363  TYR   A CD1 1 
ATOM   2133  C  CD2 . TYR   A 1 294 ? 2.132   29.837  -46.278 1.00 96.19  ? 363  TYR   A CD2 1 
ATOM   2134  C  CE1 . TYR   A 1 294 ? 1.386   27.213  -46.842 1.00 98.44  ? 363  TYR   A CE1 1 
ATOM   2135  C  CE2 . TYR   A 1 294 ? 1.837   28.937  -45.231 1.00 97.10  ? 363  TYR   A CE2 1 
ATOM   2136  C  CZ  . TYR   A 1 294 ? 1.468   27.629  -45.526 1.00 97.40  ? 363  TYR   A CZ  1 
ATOM   2137  O  OH  . TYR   A 1 294 ? 1.171   26.732  -44.526 1.00 93.06  ? 363  TYR   A OH  1 
ATOM   2138  N  N   . LYS   A 1 295 ? 3.519   31.653  -51.417 1.00 93.77  ? 364  LYS   A N   1 
ATOM   2139  C  CA  . LYS   A 1 295 ? 3.275   32.337  -52.673 1.00 86.31  ? 364  LYS   A CA  1 
ATOM   2140  C  C   . LYS   A 1 295 ? 4.577   32.984  -53.126 1.00 91.84  ? 364  LYS   A C   1 
ATOM   2141  O  O   . LYS   A 1 295 ? 5.300   33.558  -52.309 1.00 95.21  ? 364  LYS   A O   1 
ATOM   2142  C  CB  . LYS   A 1 295 ? 2.165   33.376  -52.490 1.00 81.86  ? 364  LYS   A CB  1 
ATOM   2143  N  N   . ALA   A 1 296 ? 4.901   32.857  -54.414 1.00 97.62  ? 365  ALA   A N   1 
ATOM   2144  C  CA  . ALA   A 1 296 ? 5.998   33.594  -55.032 1.00 97.25  ? 365  ALA   A CA  1 
ATOM   2145  C  C   . ALA   A 1 296 ? 5.470   34.394  -56.219 1.00 101.44 ? 365  ALA   A C   1 
ATOM   2146  O  O   . ALA   A 1 296 ? 4.443   34.055  -56.819 1.00 100.64 ? 365  ALA   A O   1 
ATOM   2147  C  CB  . ALA   A 1 296 ? 7.136   32.667  -55.490 1.00 92.32  ? 365  ALA   A CB  1 
ATOM   2148  N  N   . CYS   A 1 297 ? 6.181   35.470  -56.558 1.00 107.68 ? 366  CYS   A N   1 
ATOM   2149  C  CA  . CYS   A 1 297 ? 5.777   36.359  -57.641 1.00 109.41 ? 366  CYS   A CA  1 
ATOM   2150  C  C   . CYS   A 1 297 ? 6.927   36.604  -58.608 1.00 109.45 ? 366  CYS   A C   1 
ATOM   2151  O  O   . CYS   A 1 297 ? 8.103   36.568  -58.226 1.00 110.77 ? 366  CYS   A O   1 
ATOM   2152  C  CB  . CYS   A 1 297 ? 5.275   37.711  -57.109 1.00 110.60 ? 366  CYS   A CB  1 
ATOM   2153  S  SG  . CYS   A 1 297 ? 3.508   37.742  -56.786 1.00 121.36 ? 366  CYS   A SG  1 
ATOM   2154  N  N   . ASN   A 1 298 ? 6.562   36.879  -59.865 1.00 100.75 ? 367  ASN   A N   1 
ATOM   2155  C  CA  . ASN   A 1 298 ? 7.503   37.293  -60.906 1.00 96.52  ? 367  ASN   A CA  1 
ATOM   2156  C  C   . ASN   A 1 298 ? 8.502   36.183  -61.228 1.00 94.43  ? 367  ASN   A C   1 
ATOM   2157  O  O   . ASN   A 1 298 ? 9.690   36.434  -61.423 1.00 93.86  ? 367  ASN   A O   1 
ATOM   2158  C  CB  . ASN   A 1 298 ? 8.221   38.588  -60.512 1.00 96.40  ? 367  ASN   A CB  1 
ATOM   2159  C  CG  . ASN   A 1 298 ? 7.260   39.729  -60.198 1.00 101.89 ? 367  ASN   A CG  1 
ATOM   2160  O  OD1 . ASN   A 1 298 ? 6.417   40.108  -61.022 1.00 100.48 ? 367  ASN   A OD1 1 
ATOM   2161  N  ND2 . ASN   A 1 298 ? 7.397   40.295  -58.999 1.00 104.41 ? 367  ASN   A ND2 1 
ATOM   2162  N  N   . LEU   A 1 299 ? 8.008   34.946  -61.311 1.00 96.51  ? 368  LEU   A N   1 
ATOM   2163  C  CA  . LEU   A 1 299 ? 8.814   33.765  -61.617 1.00 92.77  ? 368  LEU   A CA  1 
ATOM   2164  C  C   . LEU   A 1 299 ? 8.239   33.052  -62.832 1.00 89.47  ? 368  LEU   A C   1 
ATOM   2165  O  O   . LEU   A 1 299 ? 7.034   32.800  -62.879 1.00 95.20  ? 368  LEU   A O   1 
ATOM   2166  C  CB  . LEU   A 1 299 ? 8.845   32.798  -60.430 1.00 88.32  ? 368  LEU   A CB  1 
ATOM   2167  C  CG  . LEU   A 1 299 ? 9.751   33.229  -59.286 1.00 86.09  ? 368  LEU   A CG  1 
ATOM   2168  C  CD1 . LEU   A 1 299 ? 9.799   32.151  -58.249 1.00 89.83  ? 368  LEU   A CD1 1 
ATOM   2169  C  CD2 . LEU   A 1 299 ? 11.136  33.536  -59.777 1.00 84.86  ? 368  LEU   A CD2 1 
ATOM   2170  N  N   . ASN   A 1 300 ? 9.090   32.698  -63.794 1.00 88.45  ? 369  ASN   A N   1 
ATOM   2171  C  CA  . ASN   A 1 300 ? 8.680   31.943  -64.978 1.00 90.06  ? 369  ASN   A CA  1 
ATOM   2172  C  C   . ASN   A 1 300 ? 9.045   30.463  -64.794 1.00 90.47  ? 369  ASN   A C   1 
ATOM   2173  O  O   . ASN   A 1 300 ? 10.174  30.140  -64.404 1.00 90.06  ? 369  ASN   A O   1 
ATOM   2174  C  CB  . ASN   A 1 300 ? 9.349   32.500  -66.245 1.00 94.59  ? 369  ASN   A CB  1 
ATOM   2175  C  CG  . ASN   A 1 300 ? 8.604   33.708  -66.866 1.00 96.18  ? 369  ASN   A CG  1 
ATOM   2176  O  OD1 . ASN   A 1 300 ? 7.375   33.706  -67.028 1.00 99.52  ? 369  ASN   A OD1 1 
ATOM   2177  N  ND2 . ASN   A 1 300 ? 9.371   34.726  -67.250 1.00 95.18  ? 369  ASN   A ND2 1 
ATOM   2178  N  N   . LEU   A 1 301 ? 8.101   29.563  -65.092 1.00 87.32  ? 370  LEU   A N   1 
ATOM   2179  C  CA  . LEU   A 1 301 ? 8.289   28.130  -64.862 1.00 87.05  ? 370  LEU   A CA  1 
ATOM   2180  C  C   . LEU   A 1 301 ? 8.862   27.420  -66.093 1.00 87.74  ? 370  LEU   A C   1 
ATOM   2181  O  O   . LEU   A 1 301 ? 8.210   27.365  -67.139 1.00 99.60  ? 370  LEU   A O   1 
ATOM   2182  C  CB  . LEU   A 1 301 ? 6.961   27.487  -64.469 1.00 92.01  ? 370  LEU   A CB  1 
ATOM   2183  C  CG  . LEU   A 1 301 ? 6.694   27.149  -63.005 1.00 89.15  ? 370  LEU   A CG  1 
ATOM   2184  C  CD1 . LEU   A 1 301 ? 7.010   28.364  -62.189 1.00 87.72  ? 370  LEU   A CD1 1 
ATOM   2185  C  CD2 . LEU   A 1 301 ? 5.244   26.762  -62.837 1.00 86.79  ? 370  LEU   A CD2 1 
ATOM   2186  N  N   . ILE   A 1 302 ? 10.031  26.799  -65.940 1.00 87.38  ? 371  ILE   A N   1 
ATOM   2187  C  CA  . ILE   A 1 302 ? 10.810  26.236  -67.050 1.00 88.45  ? 371  ILE   A CA  1 
ATOM   2188  C  C   . ILE   A 1 302 ? 10.632  24.715  -67.075 1.00 91.16  ? 371  ILE   A C   1 
ATOM   2189  O  O   . ILE   A 1 302 ? 11.131  24.005  -66.195 1.00 95.32  ? 371  ILE   A O   1 
ATOM   2190  C  CB  . ILE   A 1 302 ? 12.299  26.607  -66.923 1.00 87.69  ? 371  ILE   A CB  1 
ATOM   2191  C  CG1 . ILE   A 1 302 ? 12.529  28.114  -67.110 1.00 87.89  ? 371  ILE   A CG1 1 
ATOM   2192  C  CG2 . ILE   A 1 302 ? 13.163  25.787  -67.858 1.00 88.16  ? 371  ILE   A CG2 1 
ATOM   2193  C  CD1 . ILE   A 1 302 ? 11.688  28.758  -68.186 1.00 90.15  ? 371  ILE   A CD1 1 
ATOM   2194  N  N   . GLY   A 1 303 ? 9.949   24.192  -68.087 1.00 94.29  ? 372  GLY   A N   1 
ATOM   2195  C  CA  . GLY   A 1 303 ? 9.833   22.750  -68.249 1.00 96.27  ? 372  GLY   A CA  1 
ATOM   2196  C  C   . GLY   A 1 303 ? 8.461   22.221  -67.876 1.00 103.85 ? 372  GLY   A C   1 
ATOM   2197  O  O   . GLY   A 1 303 ? 7.482   22.958  -67.707 1.00 103.70 ? 372  GLY   A O   1 
ATOM   2198  N  N   . ARG   A 1 304 ? 8.393   20.892  -67.779 1.00 106.80 ? 373  ARG   A N   1 
ATOM   2199  C  CA  . ARG   A 1 304 ? 7.160   20.264  -67.341 1.00 107.61 ? 373  ARG   A CA  1 
ATOM   2200  C  C   . ARG   A 1 304 ? 7.378   19.643  -65.966 1.00 112.16 ? 373  ARG   A C   1 
ATOM   2201  O  O   . ARG   A 1 304 ? 8.472   19.138  -65.680 1.00 112.47 ? 373  ARG   A O   1 
ATOM   2202  C  CB  . ARG   A 1 304 ? 6.668   19.196  -68.332 1.00 99.26  ? 373  ARG   A CB  1 
ATOM   2203  N  N   . PRO   A 1 305 ? 6.382   19.729  -65.085 1.00 119.50 ? 374  PRO   A N   1 
ATOM   2204  C  CA  . PRO   A 1 305 ? 6.526   19.194  -63.724 1.00 115.71 ? 374  PRO   A CA  1 
ATOM   2205  C  C   . PRO   A 1 305 ? 7.030   17.759  -63.703 1.00 112.65 ? 374  PRO   A C   1 
ATOM   2206  O  O   . PRO   A 1 305 ? 6.718   16.957  -64.583 1.00 111.83 ? 374  PRO   A O   1 
ATOM   2207  C  CB  . PRO   A 1 305 ? 5.106   19.285  -63.167 1.00 117.83 ? 374  PRO   A CB  1 
ATOM   2208  C  CG  . PRO   A 1 305 ? 4.509   20.480  -63.880 1.00 118.51 ? 374  PRO   A CG  1 
ATOM   2209  C  CD  . PRO   A 1 305 ? 5.138   20.505  -65.253 1.00 119.84 ? 374  PRO   A CD  1 
ATOM   2210  N  N   . SER   A 1 306 ? 7.821   17.447  -62.676 1.00 106.15 ? 375  SER   A N   1 
ATOM   2211  C  CA  . SER   A 1 306 ? 8.375   16.115  -62.458 1.00 106.01 ? 375  SER   A CA  1 
ATOM   2212  C  C   . SER   A 1 306 ? 8.315   15.784  -60.967 1.00 107.88 ? 375  SER   A C   1 
ATOM   2213  O  O   . SER   A 1 306 ? 8.154   16.666  -60.119 1.00 106.48 ? 375  SER   A O   1 
ATOM   2214  C  CB  . SER   A 1 306 ? 9.824   16.019  -62.970 1.00 100.91 ? 375  SER   A CB  1 
ATOM   2215  O  OG  . SER   A 1 306 ? 10.415  14.763  -62.671 1.00 101.90 ? 375  SER   A OG  1 
ATOM   2216  N  N   . THR   A 1 307 ? 8.444   14.495  -60.643 1.00 111.00 ? 376  THR   A N   1 
ATOM   2217  C  CA  . THR   A 1 307 ? 8.519   14.072  -59.249 1.00 107.13 ? 376  THR   A CA  1 
ATOM   2218  C  C   . THR   A 1 307 ? 9.756   13.244  -58.942 1.00 111.64 ? 376  THR   A C   1 
ATOM   2219  O  O   . THR   A 1 307 ? 9.936   12.846  -57.786 1.00 113.91 ? 376  THR   A O   1 
ATOM   2220  C  CB  . THR   A 1 307 ? 7.281   13.262  -58.838 1.00 104.24 ? 376  THR   A CB  1 
ATOM   2221  O  OG1 . THR   A 1 307 ? 7.263   12.026  -59.558 1.00 105.01 ? 376  THR   A OG1 1 
ATOM   2222  C  CG2 . THR   A 1 307 ? 6.004   14.030  -59.107 1.00 103.19 ? 376  THR   A CG2 1 
ATOM   2223  N  N   . GLU   A 1 308 ? 10.603  12.964  -59.933 1.00 121.92 ? 377  GLU   A N   1 
ATOM   2224  C  CA  . GLU   A 1 308 ? 11.844  12.247  -59.667 1.00 124.53 ? 377  GLU   A CA  1 
ATOM   2225  C  C   . GLU   A 1 308 ? 12.677  13.018  -58.643 1.00 124.50 ? 377  GLU   A C   1 
ATOM   2226  O  O   . GLU   A 1 308 ? 12.756  14.251  -58.677 1.00 122.35 ? 377  GLU   A O   1 
ATOM   2227  C  CB  . GLU   A 1 308 ? 12.631  12.030  -60.967 1.00 125.36 ? 377  GLU   A CB  1 
ATOM   2228  C  CG  . GLU   A 1 308 ? 13.661  13.117  -61.293 1.00 127.36 ? 377  GLU   A CG  1 
ATOM   2229  C  CD  . GLU   A 1 308 ? 14.370  12.926  -62.633 1.00 129.97 ? 377  GLU   A CD  1 
ATOM   2230  O  OE1 . GLU   A 1 308 ? 14.785  11.783  -62.951 1.00 132.01 ? 377  GLU   A OE1 1 
ATOM   2231  O  OE2 . GLU   A 1 308 ? 14.518  13.939  -63.361 1.00 129.85 ? 377  GLU   A OE2 1 
ATOM   2232  N  N   . HIS   A 1 309 ? 13.243  12.286  -57.684 1.00 129.03 ? 378  HIS   A N   1 
ATOM   2233  C  CA  . HIS   A 1 309 ? 14.065  12.854  -56.614 1.00 130.65 ? 378  HIS   A CA  1 
ATOM   2234  C  C   . HIS   A 1 309 ? 13.374  14.011  -55.883 1.00 126.25 ? 378  HIS   A C   1 
ATOM   2235  O  O   . HIS   A 1 309 ? 14.047  14.872  -55.309 1.00 126.45 ? 378  HIS   A O   1 
ATOM   2236  C  CB  . HIS   A 1 309 ? 15.425  13.318  -57.151 1.00 132.63 ? 378  HIS   A CB  1 
ATOM   2237  C  CG  . HIS   A 1 309 ? 16.557  13.161  -56.175 1.00 138.30 ? 378  HIS   A CG  1 
ATOM   2238  N  ND1 . HIS   A 1 309 ? 17.055  14.205  -55.422 1.00 134.68 ? 378  HIS   A ND1 1 
ATOM   2239  C  CD2 . HIS   A 1 309 ? 17.297  12.075  -55.841 1.00 139.58 ? 378  HIS   A CD2 1 
ATOM   2240  C  CE1 . HIS   A 1 309 ? 18.053  13.769  -54.670 1.00 133.72 ? 378  HIS   A CE1 1 
ATOM   2241  N  NE2 . HIS   A 1 309 ? 18.220  12.480  -54.904 1.00 135.81 ? 378  HIS   A NE2 1 
ATOM   2242  N  N   . SER   A 1 310 ? 12.043  14.059  -55.896 1.00 112.93 ? 379  SER   A N   1 
ATOM   2243  C  CA  . SER   A 1 310 ? 11.342  15.173  -55.274 1.00 106.17 ? 379  SER   A CA  1 
ATOM   2244  C  C   . SER   A 1 310 ? 11.654  15.230  -53.788 1.00 104.88 ? 379  SER   A C   1 
ATOM   2245  O  O   . SER   A 1 310 ? 11.518  14.235  -53.073 1.00 105.83 ? 379  SER   A O   1 
ATOM   2246  C  CB  . SER   A 1 310 ? 9.838   15.048  -55.484 1.00 105.17 ? 379  SER   A CB  1 
ATOM   2247  O  OG  . SER   A 1 310 ? 9.189   16.214  -55.002 1.00 101.13 ? 379  SER   A OG  1 
ATOM   2248  N  N   . TRP   A 1 311 ? 12.076  16.409  -53.325 1.00 102.50 ? 380  TRP   A N   1 
ATOM   2249  C  CA  . TRP   A 1 311 ? 12.482  16.552  -51.933 1.00 95.10  ? 380  TRP   A CA  1 
ATOM   2250  C  C   . TRP   A 1 311 ? 11.288  16.505  -50.999 1.00 92.84  ? 380  TRP   A C   1 
ATOM   2251  O  O   . TRP   A 1 311 ? 11.421  16.065  -49.856 1.00 97.93  ? 380  TRP   A O   1 
ATOM   2252  C  CB  . TRP   A 1 311 ? 13.238  17.857  -51.745 1.00 93.09  ? 380  TRP   A CB  1 
ATOM   2253  C  CG  . TRP   A 1 311 ? 14.623  17.877  -52.338 1.00 95.19  ? 380  TRP   A CG  1 
ATOM   2254  C  CD1 . TRP   A 1 311 ? 15.522  16.852  -52.372 1.00 97.72  ? 380  TRP   A CD1 1 
ATOM   2255  C  CD2 . TRP   A 1 311 ? 15.263  18.989  -52.975 1.00 95.87  ? 380  TRP   A CD2 1 
ATOM   2256  N  NE1 . TRP   A 1 311 ? 16.682  17.256  -52.983 1.00 97.50  ? 380  TRP   A NE1 1 
ATOM   2257  C  CE2 . TRP   A 1 311 ? 16.549  18.567  -53.360 1.00 97.73  ? 380  TRP   A CE2 1 
ATOM   2258  C  CE3 . TRP   A 1 311 ? 14.874  20.307  -53.251 1.00 96.09  ? 380  TRP   A CE3 1 
ATOM   2259  C  CZ2 . TRP   A 1 311 ? 17.453  19.421  -54.010 1.00 99.69  ? 380  TRP   A CZ2 1 
ATOM   2260  C  CZ3 . TRP   A 1 311 ? 15.776  21.155  -53.898 1.00 93.99  ? 380  TRP   A CZ3 1 
ATOM   2261  C  CH2 . TRP   A 1 311 ? 17.046  20.708  -54.270 1.00 95.38  ? 380  TRP   A CH2 1 
ATOM   2262  N  N   . PHE   A 1 312 ? 10.127  16.964  -51.461 1.00 94.46  ? 381  PHE   A N   1 
ATOM   2263  C  CA  . PHE   A 1 312 ? 8.885   16.954  -50.694 1.00 96.63  ? 381  PHE   A CA  1 
ATOM   2264  C  C   . PHE   A 1 312 ? 7.954   15.944  -51.326 1.00 98.03  ? 381  PHE   A C   1 
ATOM   2265  O  O   . PHE   A 1 312 ? 7.121   16.312  -52.172 1.00 97.49  ? 381  PHE   A O   1 
ATOM   2266  C  CB  . PHE   A 1 312 ? 8.238   18.337  -50.669 1.00 94.72  ? 381  PHE   A CB  1 
ATOM   2267  C  CG  . PHE   A 1 312 ? 9.209   19.426  -50.403 1.00 92.17  ? 381  PHE   A CG  1 
ATOM   2268  C  CD1 . PHE   A 1 312 ? 9.859   19.497  -49.189 1.00 91.38  ? 381  PHE   A CD1 1 
ATOM   2269  C  CD2 . PHE   A 1 312 ? 9.515   20.352  -51.379 1.00 93.80  ? 381  PHE   A CD2 1 
ATOM   2270  C  CE1 . PHE   A 1 312 ? 10.773  20.487  -48.946 1.00 91.71  ? 381  PHE   A CE1 1 
ATOM   2271  C  CE2 . PHE   A 1 312 ? 10.430  21.339  -51.136 1.00 91.70  ? 381  PHE   A CE2 1 
ATOM   2272  C  CZ  . PHE   A 1 312 ? 11.061  21.408  -49.909 1.00 88.46  ? 381  PHE   A CZ  1 
ATOM   2273  N  N   . PRO   A 1 313 ? 8.065   14.662  -50.959 1.00 97.95  ? 382  PRO   A N   1 
ATOM   2274  C  CA  . PRO   A 1 313 ? 7.250   13.625  -51.596 1.00 97.63  ? 382  PRO   A CA  1 
ATOM   2275  C  C   . PRO   A 1 313 ? 5.775   13.997  -51.604 1.00 98.49  ? 382  PRO   A C   1 
ATOM   2276  O  O   . PRO   A 1 313 ? 5.257   14.607  -50.663 1.00 101.39 ? 382  PRO   A O   1 
ATOM   2277  C  CB  . PRO   A 1 313 ? 7.535   12.388  -50.734 1.00 92.49  ? 382  PRO   A CB  1 
ATOM   2278  C  CG  . PRO   A 1 313 ? 8.943   12.579  -50.309 1.00 93.34  ? 382  PRO   A CG  1 
ATOM   2279  C  CD  . PRO   A 1 313 ? 9.032   14.071  -50.015 1.00 98.70  ? 382  PRO   A CD  1 
ATOM   2280  N  N   . GLY   A 1 314 ? 5.107   13.676  -52.701 1.00 93.17  ? 383  GLY   A N   1 
ATOM   2281  C  CA  . GLY   A 1 314 ? 3.749   14.089  -52.892 1.00 98.15  ? 383  GLY   A CA  1 
ATOM   2282  C  C   . GLY   A 1 314 ? 3.594   15.395  -53.632 1.00 107.75 ? 383  GLY   A C   1 
ATOM   2283  O  O   . GLY   A 1 314 ? 2.480   15.727  -54.061 1.00 112.13 ? 383  GLY   A O   1 
ATOM   2284  N  N   . TYR   A 1 315 ? 4.672   16.151  -53.808 1.00 110.37 ? 384  TYR   A N   1 
ATOM   2285  C  CA  . TYR   A 1 315 ? 4.629   17.318  -54.668 1.00 108.05 ? 384  TYR   A CA  1 
ATOM   2286  C  C   . TYR   A 1 315 ? 5.530   17.096  -55.879 1.00 108.07 ? 384  TYR   A C   1 
ATOM   2287  O  O   . TYR   A 1 315 ? 6.442   16.262  -55.859 1.00 107.79 ? 384  TYR   A O   1 
ATOM   2288  C  CB  . TYR   A 1 315 ? 5.031   18.582  -53.906 1.00 105.03 ? 384  TYR   A CB  1 
ATOM   2289  C  CG  . TYR   A 1 315 ? 4.078   18.988  -52.809 1.00 105.74 ? 384  TYR   A CG  1 
ATOM   2290  C  CD1 . TYR   A 1 315 ? 4.223   18.483  -51.531 1.00 108.01 ? 384  TYR   A CD1 1 
ATOM   2291  C  CD2 . TYR   A 1 315 ? 3.053   19.892  -53.043 1.00 106.46 ? 384  TYR   A CD2 1 
ATOM   2292  C  CE1 . TYR   A 1 315 ? 3.365   18.863  -50.508 1.00 109.82 ? 384  TYR   A CE1 1 
ATOM   2293  C  CE2 . TYR   A 1 315 ? 2.194   20.278  -52.029 1.00 106.51 ? 384  TYR   A CE2 1 
ATOM   2294  C  CZ  . TYR   A 1 315 ? 2.354   19.759  -50.765 1.00 106.30 ? 384  TYR   A CZ  1 
ATOM   2295  O  OH  . TYR   A 1 315 ? 1.508   20.133  -49.750 1.00 114.09 ? 384  TYR   A OH  1 
ATOM   2296  N  N   . ALA   A 1 316 ? 5.240   17.842  -56.950 1.00 106.22 ? 385  ALA   A N   1 
ATOM   2297  C  CA  . ALA   A 1 316 ? 5.926   17.707  -58.229 1.00 104.23 ? 385  ALA   A CA  1 
ATOM   2298  C  C   . ALA   A 1 316 ? 6.588   19.024  -58.615 1.00 104.13 ? 385  ALA   A C   1 
ATOM   2299  O  O   . ALA   A 1 316 ? 5.903   20.042  -58.775 1.00 103.40 ? 385  ALA   A O   1 
ATOM   2300  C  CB  . ALA   A 1 316 ? 4.943   17.270  -59.307 1.00 105.35 ? 385  ALA   A CB  1 
ATOM   2301  N  N   . TRP   A 1 317 ? 7.906   18.988  -58.820 1.00 99.75  ? 386  TRP   A N   1 
ATOM   2302  C  CA  . TRP   A 1 317 ? 8.712   20.191  -58.995 1.00 94.82  ? 386  TRP   A CA  1 
ATOM   2303  C  C   . TRP   A 1 317 ? 8.825   20.649  -60.442 1.00 96.52  ? 386  TRP   A C   1 
ATOM   2304  O  O   . TRP   A 1 317 ? 8.973   19.841  -61.359 1.00 101.24 ? 386  TRP   A O   1 
ATOM   2305  C  CB  . TRP   A 1 317 ? 10.113  19.960  -58.456 1.00 93.79  ? 386  TRP   A CB  1 
ATOM   2306  C  CG  . TRP   A 1 317 ? 10.849  18.812  -59.070 1.00 97.26  ? 386  TRP   A CG  1 
ATOM   2307  C  CD1 . TRP   A 1 317 ? 10.908  17.536  -58.593 1.00 100.92 ? 386  TRP   A CD1 1 
ATOM   2308  C  CD2 . TRP   A 1 317 ? 11.677  18.839  -60.242 1.00 97.78  ? 386  TRP   A CD2 1 
ATOM   2309  N  NE1 . TRP   A 1 317 ? 11.713  16.764  -59.394 1.00 101.06 ? 386  TRP   A NE1 1 
ATOM   2310  C  CE2 . TRP   A 1 317 ? 12.193  17.540  -60.415 1.00 99.82  ? 386  TRP   A CE2 1 
ATOM   2311  C  CE3 . TRP   A 1 317 ? 12.043  19.836  -61.152 1.00 93.05  ? 386  TRP   A CE3 1 
ATOM   2312  C  CZ2 . TRP   A 1 317 ? 13.035  17.210  -61.466 1.00 101.41 ? 386  TRP   A CZ2 1 
ATOM   2313  C  CZ3 . TRP   A 1 317 ? 12.884  19.503  -62.189 1.00 93.84  ? 386  TRP   A CZ3 1 
ATOM   2314  C  CH2 . TRP   A 1 317 ? 13.372  18.204  -62.337 1.00 97.75  ? 386  TRP   A CH2 1 
ATOM   2315  N  N   . THR   A 1 318 ? 8.804   21.967  -60.627 1.00 93.46  ? 387  THR   A N   1 
ATOM   2316  C  CA  . THR   A 1 318 ? 8.942   22.623  -61.926 1.00 94.38  ? 387  THR   A CA  1 
ATOM   2317  C  C   . THR   A 1 318 ? 9.941   23.761  -61.761 1.00 90.17  ? 387  THR   A C   1 
ATOM   2318  O  O   . THR   A 1 318 ? 9.750   24.624  -60.898 1.00 88.76  ? 387  THR   A O   1 
ATOM   2319  C  CB  . THR   A 1 318 ? 7.592   23.169  -62.415 1.00 95.47  ? 387  THR   A CB  1 
ATOM   2320  O  OG1 . THR   A 1 318 ? 6.566   22.185  -62.220 1.00 101.01 ? 387  THR   A OG1 1 
ATOM   2321  C  CG2 . THR   A 1 318 ? 7.653   23.574  -63.880 1.00 92.51  ? 387  THR   A CG2 1 
ATOM   2322  N  N   . VAL   A 1 319 ? 11.002  23.769  -62.573 1.00 88.52  ? 388  VAL   A N   1 
ATOM   2323  C  CA  . VAL   A 1 319 ? 12.064  24.757  -62.389 1.00 85.71  ? 388  VAL   A CA  1 
ATOM   2324  C  C   . VAL   A 1 319 ? 11.489  26.161  -62.548 1.00 88.55  ? 388  VAL   A C   1 
ATOM   2325  O  O   . VAL   A 1 319 ? 10.556  26.380  -63.329 1.00 92.41  ? 388  VAL   A O   1 
ATOM   2326  C  CB  . VAL   A 1 319 ? 13.218  24.472  -63.363 1.00 85.21  ? 388  VAL   A CB  1 
ATOM   2327  C  CG1 . VAL   A 1 319 ? 14.303  25.488  -63.237 1.00 85.08  ? 388  VAL   A CG1 1 
ATOM   2328  C  CG2 . VAL   A 1 319 ? 13.791  23.122  -63.035 1.00 90.15  ? 388  VAL   A CG2 1 
ATOM   2329  N  N   . ALA   A 1 320 ? 12.007  27.110  -61.757 1.00 86.83  ? 389  ALA   A N   1 
ATOM   2330  C  CA  . ALA   A 1 320 ? 11.493  28.475  -61.701 1.00 84.67  ? 389  ALA   A CA  1 
ATOM   2331  C  C   . ALA   A 1 320 ? 12.648  29.466  -61.788 1.00 84.66  ? 389  ALA   A C   1 
ATOM   2332  O  O   . ALA   A 1 320 ? 13.618  29.380  -61.028 1.00 84.11  ? 389  ALA   A O   1 
ATOM   2333  C  CB  . ALA   A 1 320 ? 10.679  28.700  -60.421 1.00 84.05  ? 389  ALA   A CB  1 
ATOM   2334  N  N   . GLN   A 1 321 ? 12.542  30.407  -62.717 1.00 85.30  ? 390  GLN   A N   1 
ATOM   2335  C  CA  . GLN   A 1 321 ? 13.574  31.408  -62.936 1.00 86.41  ? 390  GLN   A CA  1 
ATOM   2336  C  C   . GLN   A 1 321 ? 12.944  32.797  -62.948 1.00 85.94  ? 390  GLN   A C   1 
ATOM   2337  O  O   . GLN   A 1 321 ? 11.722  32.956  -62.993 1.00 86.71  ? 390  GLN   A O   1 
ATOM   2338  C  CB  . GLN   A 1 321 ? 14.336  31.146  -64.246 1.00 87.56  ? 390  GLN   A CB  1 
ATOM   2339  C  CG  . GLN   A 1 321 ? 13.446  31.198  -65.481 1.00 90.47  ? 390  GLN   A CG  1 
ATOM   2340  C  CD  . GLN   A 1 321 ? 14.229  31.224  -66.783 1.00 93.92  ? 390  GLN   A CD  1 
ATOM   2341  O  OE1 . GLN   A 1 321 ? 15.273  30.569  -66.901 1.00 96.22  ? 390  GLN   A OE1 1 
ATOM   2342  N  NE2 . GLN   A 1 321 ? 13.733  31.991  -67.769 1.00 90.31  ? 390  GLN   A NE2 1 
ATOM   2343  N  N   . CYS   A 1 322 ? 13.810  33.803  -62.906 1.00 85.63  ? 391  CYS   A N   1 
ATOM   2344  C  CA  . CYS   A 1 322 ? 13.395  35.197  -62.880 1.00 86.75  ? 391  CYS   A CA  1 
ATOM   2345  C  C   . CYS   A 1 322 ? 12.678  35.577  -64.180 1.00 90.90  ? 391  CYS   A C   1 
ATOM   2346  O  O   . CYS   A 1 322 ? 13.048  35.128  -65.269 1.00 95.45  ? 391  CYS   A O   1 
ATOM   2347  C  CB  . CYS   A 1 322 ? 14.639  36.058  -62.659 1.00 87.64  ? 391  CYS   A CB  1 
ATOM   2348  S  SG  . CYS   A 1 322 ? 14.399  37.813  -62.541 1.00 85.86  ? 391  CYS   A SG  1 
ATOM   2349  N  N   . LYS   A 1 323 ? 11.628  36.383  -64.076 1.00 89.21  ? 392  LYS   A N   1 
ATOM   2350  C  CA  . LYS   A 1 323 ? 10.967  36.844  -65.286 1.00 87.72  ? 392  LYS   A CA  1 
ATOM   2351  C  C   . LYS   A 1 323 ? 11.763  37.928  -66.001 1.00 89.86  ? 392  LYS   A C   1 
ATOM   2352  O  O   . LYS   A 1 323 ? 11.378  38.316  -67.110 1.00 94.40  ? 392  LYS   A O   1 
ATOM   2353  C  CB  . LYS   A 1 323 ? 9.562   37.355  -64.954 1.00 88.50  ? 392  LYS   A CB  1 
ATOM   2354  C  CG  . LYS   A 1 323 ? 9.495   38.869  -64.774 1.00 96.20  ? 392  LYS   A CG  1 
ATOM   2355  C  CD  . LYS   A 1 323 ? 8.373   39.349  -63.855 1.00 97.30  ? 392  LYS   A CD  1 
ATOM   2356  C  CE  . LYS   A 1 323 ? 7.022   39.354  -64.546 1.00 97.68  ? 392  LYS   A CE  1 
ATOM   2357  N  NZ  . LYS   A 1 323 ? 5.980   40.052  -63.733 1.00 94.81  ? 392  LYS   A NZ  1 
ATOM   2358  N  N   . ILE   A 1 324 ? 12.867  38.407  -65.413 1.00 90.44  ? 393  ILE   A N   1 
ATOM   2359  C  CA  . ILE   A 1 324 ? 13.639  39.541  -65.946 1.00 93.39  ? 393  ILE   A CA  1 
ATOM   2360  C  C   . ILE   A 1 324 ? 15.010  39.096  -66.483 1.00 94.39  ? 393  ILE   A C   1 
ATOM   2361  O  O   . ILE   A 1 324 ? 15.363  39.400  -67.625 1.00 94.73  ? 393  ILE   A O   1 
ATOM   2362  C  CB  . ILE   A 1 324 ? 13.795  40.663  -64.890 1.00 91.90  ? 393  ILE   A CB  1 
ATOM   2363  C  CG1 . ILE   A 1 324 ? 12.433  41.203  -64.438 1.00 89.27  ? 393  ILE   A CG1 1 
ATOM   2364  C  CG2 . ILE   A 1 324 ? 14.713  41.782  -65.414 1.00 91.12  ? 393  ILE   A CG2 1 
ATOM   2365  C  CD1 . ILE   A 1 324 ? 11.920  42.350  -65.263 1.00 88.62  ? 393  ILE   A CD1 1 
ATOM   2366  N  N   . CYS   A 1 325 ? 15.811  38.402  -65.656 1.00 90.91  ? 394  CYS   A N   1 
ATOM   2367  C  CA  . CYS   A 1 325 ? 17.182  38.032  -66.009 1.00 88.17  ? 394  CYS   A CA  1 
ATOM   2368  C  C   . CYS   A 1 325 ? 17.356  36.539  -66.204 1.00 88.74  ? 394  CYS   A C   1 
ATOM   2369  O  O   . CYS   A 1 325 ? 18.486  36.085  -66.443 1.00 92.04  ? 394  CYS   A O   1 
ATOM   2370  C  CB  . CYS   A 1 325 ? 18.168  38.511  -64.940 1.00 89.25  ? 394  CYS   A CB  1 
ATOM   2371  S  SG  . CYS   A 1 325 ? 17.937  37.749  -63.337 1.00 92.26  ? 394  CYS   A SG  1 
ATOM   2372  N  N   . ALA   A 1 326 ? 16.268  35.776  -66.096 1.00 87.83  ? 395  ALA   A N   1 
ATOM   2373  C  CA  . ALA   A 1 326 ? 16.265  34.326  -66.314 1.00 89.12  ? 395  ALA   A CA  1 
ATOM   2374  C  C   . ALA   A 1 326 ? 17.290  33.614  -65.436 1.00 90.96  ? 395  ALA   A C   1 
ATOM   2375  O  O   . ALA   A 1 326 ? 17.940  32.650  -65.860 1.00 93.59  ? 395  ALA   A O   1 
ATOM   2376  C  CB  . ALA   A 1 326 ? 16.482  33.988  -67.788 1.00 88.64  ? 395  ALA   A CB  1 
ATOM   2377  N  N   . SER   A 1 327 ? 17.449  34.086  -64.204 1.00 87.61  ? 396  SER   A N   1 
ATOM   2378  C  CA  . SER   A 1 327 ? 18.388  33.462  -63.292 1.00 87.33  ? 396  SER   A CA  1 
ATOM   2379  C  C   . SER   A 1 327 ? 17.609  32.578  -62.334 1.00 86.34  ? 396  SER   A C   1 
ATOM   2380  O  O   . SER   A 1 327 ? 16.534  32.957  -61.875 1.00 87.41  ? 396  SER   A O   1 
ATOM   2381  C  CB  . SER   A 1 327 ? 19.212  34.509  -62.550 1.00 88.88  ? 396  SER   A CB  1 
ATOM   2382  O  OG  . SER   A 1 327 ? 20.272  34.962  -63.380 1.00 88.85  ? 396  SER   A OG  1 
ATOM   2383  N  N   . HIS   A 1 328 ? 18.138  31.382  -62.090 1.00 84.68  ? 397  HIS   A N   1 
ATOM   2384  C  CA  . HIS   A 1 328 ? 17.410  30.367  -61.355 1.00 84.16  ? 397  HIS   A CA  1 
ATOM   2385  C  C   . HIS   A 1 328 ? 17.087  30.889  -59.971 1.00 83.42  ? 397  HIS   A C   1 
ATOM   2386  O  O   . HIS   A 1 328 ? 17.926  31.530  -59.332 1.00 83.10  ? 397  HIS   A O   1 
ATOM   2387  C  CB  . HIS   A 1 328 ? 18.257  29.114  -61.276 1.00 83.96  ? 397  HIS   A CB  1 
ATOM   2388  C  CG  . HIS   A 1 328 ? 17.631  27.988  -60.520 1.00 83.44  ? 397  HIS   A CG  1 
ATOM   2389  N  ND1 . HIS   A 1 328 ? 18.234  27.392  -59.430 1.00 82.75  ? 397  HIS   A ND1 1 
ATOM   2390  C  CD2 . HIS   A 1 328 ? 16.462  27.336  -60.708 1.00 83.55  ? 397  HIS   A CD2 1 
ATOM   2391  C  CE1 . HIS   A 1 328 ? 17.456  26.423  -58.981 1.00 82.45  ? 397  HIS   A CE1 1 
ATOM   2392  N  NE2 . HIS   A 1 328 ? 16.373  26.372  -59.736 1.00 82.93  ? 397  HIS   A NE2 1 
ATOM   2393  N  N   . ILE   A 1 329 ? 15.854  30.631  -59.527 1.00 83.20  ? 398  ILE   A N   1 
ATOM   2394  C  CA  . ILE   A 1 329 ? 15.398  31.087  -58.219 1.00 82.54  ? 398  ILE   A CA  1 
ATOM   2395  C  C   . ILE   A 1 329 ? 14.973  29.892  -57.371 1.00 82.00  ? 398  ILE   A C   1 
ATOM   2396  O  O   . ILE   A 1 329 ? 15.184  29.890  -56.160 1.00 81.35  ? 398  ILE   A O   1 
ATOM   2397  C  CB  . ILE   A 1 329 ? 14.263  32.115  -58.377 1.00 82.80  ? 398  ILE   A CB  1 
ATOM   2398  C  CG1 . ILE   A 1 329 ? 14.786  33.357  -59.077 1.00 83.28  ? 398  ILE   A CG1 1 
ATOM   2399  C  CG2 . ILE   A 1 329 ? 13.631  32.516  -57.055 1.00 82.53  ? 398  ILE   A CG2 1 
ATOM   2400  C  CD1 . ILE   A 1 329 ? 15.774  34.157  -58.251 1.00 82.86  ? 398  ILE   A CD1 1 
ATOM   2401  N  N   . GLY   A 1 330 ? 14.428  28.855  -57.999 1.00 82.29  ? 399  GLY   A N   1 
ATOM   2402  C  CA  . GLY   A 1 330 ? 14.026  27.644  -57.312 1.00 81.87  ? 399  GLY   A CA  1 
ATOM   2403  C  C   . GLY   A 1 330 ? 13.115  26.749  -58.133 1.00 83.32  ? 399  GLY   A C   1 
ATOM   2404  O  O   . GLY   A 1 330 ? 13.326  26.550  -59.331 1.00 85.52  ? 399  GLY   A O   1 
ATOM   2405  N  N   . TRP   A 1 331 ? 12.108  26.178  -57.479 1.00 86.08  ? 400  TRP   A N   1 
ATOM   2406  C  CA  . TRP   A 1 331 ? 11.139  25.292  -58.109 1.00 86.41  ? 400  TRP   A CA  1 
ATOM   2407  C  C   . TRP   A 1 331 ? 9.731   25.670  -57.653 1.00 87.21  ? 400  TRP   A C   1 
ATOM   2408  O  O   . TRP   A 1 331 ? 9.542   26.299  -56.608 1.00 89.94  ? 400  TRP   A O   1 
ATOM   2409  C  CB  . TRP   A 1 331 ? 11.432  23.815  -57.757 1.00 89.45  ? 400  TRP   A CB  1 
ATOM   2410  C  CG  . TRP   A 1 331 ? 12.835  23.326  -58.098 1.00 89.80  ? 400  TRP   A CG  1 
ATOM   2411  C  CD1 . TRP   A 1 331 ? 13.200  22.516  -59.157 1.00 90.32  ? 400  TRP   A CD1 1 
ATOM   2412  C  CD2 . TRP   A 1 331 ? 14.040  23.614  -57.384 1.00 89.14  ? 400  TRP   A CD2 1 
ATOM   2413  N  NE1 . TRP   A 1 331 ? 14.557  22.295  -59.132 1.00 90.29  ? 400  TRP   A NE1 1 
ATOM   2414  C  CE2 . TRP   A 1 331 ? 15.097  22.960  -58.059 1.00 91.80  ? 400  TRP   A CE2 1 
ATOM   2415  C  CE3 . TRP   A 1 331 ? 14.332  24.361  -56.247 1.00 89.62  ? 400  TRP   A CE3 1 
ATOM   2416  C  CZ2 . TRP   A 1 331 ? 16.426  23.041  -57.625 1.00 93.50  ? 400  TRP   A CZ2 1 
ATOM   2417  C  CZ3 . TRP   A 1 331 ? 15.652  24.438  -55.822 1.00 91.79  ? 400  TRP   A CZ3 1 
ATOM   2418  C  CH2 . TRP   A 1 331 ? 16.679  23.779  -56.504 1.00 91.02  ? 400  TRP   A CH2 1 
ATOM   2419  N  N   . LYS   A 1 332 ? 8.719   25.298  -58.446 1.00 87.08  ? 401  LYS   A N   1 
ATOM   2420  C  CA  . LYS   A 1 332 ? 7.317   25.450  -58.039 1.00 89.40  ? 401  LYS   A CA  1 
ATOM   2421  C  C   . LYS   A 1 332 ? 6.767   24.051  -57.813 1.00 89.30  ? 401  LYS   A C   1 
ATOM   2422  O  O   . LYS   A 1 332 ? 6.536   23.322  -58.780 1.00 92.44  ? 401  LYS   A O   1 
ATOM   2423  C  CB  . LYS   A 1 332 ? 6.467   26.211  -59.067 1.00 83.89  ? 401  LYS   A CB  1 
ATOM   2424  N  N   . PHE   A 1 333 ? 6.570   23.668  -56.546 1.00 88.54  ? 402  PHE   A N   1 
ATOM   2425  C  CA  . PHE   A 1 333 ? 6.129   22.317  -56.200 1.00 89.46  ? 402  PHE   A CA  1 
ATOM   2426  C  C   . PHE   A 1 333 ? 4.604   22.201  -56.232 1.00 93.50  ? 402  PHE   A C   1 
ATOM   2427  O  O   . PHE   A 1 333 ? 3.896   23.018  -55.634 1.00 92.04  ? 402  PHE   A O   1 
ATOM   2428  C  CB  . PHE   A 1 333 ? 6.657   21.923  -54.826 1.00 90.44  ? 402  PHE   A CB  1 
ATOM   2429  C  CG  . PHE   A 1 333 ? 8.141   21.752  -54.771 1.00 89.48  ? 402  PHE   A CG  1 
ATOM   2430  C  CD1 . PHE   A 1 333 ? 8.969   22.836  -54.550 1.00 87.58  ? 402  PHE   A CD1 1 
ATOM   2431  C  CD2 . PHE   A 1 333 ? 8.713   20.502  -54.921 1.00 93.81  ? 402  PHE   A CD2 1 
ATOM   2432  C  CE1 . PHE   A 1 333 ? 10.342  22.677  -54.492 1.00 88.28  ? 402  PHE   A CE1 1 
ATOM   2433  C  CE2 . PHE   A 1 333 ? 10.094  20.336  -54.857 1.00 93.91  ? 402  PHE   A CE2 1 
ATOM   2434  C  CZ  . PHE   A 1 333 ? 10.908  21.428  -54.643 1.00 86.70  ? 402  PHE   A CZ  1 
ATOM   2435  N  N   . THR   A 1 334 ? 4.108   21.165  -56.914 1.00 97.62  ? 403  THR   A N   1 
ATOM   2436  C  CA  . THR   A 1 334 ? 2.695   20.967  -57.207 1.00 96.59  ? 403  THR   A CA  1 
ATOM   2437  C  C   . THR   A 1 334 ? 2.176   19.708  -56.532 1.00 102.89 ? 403  THR   A C   1 
ATOM   2438  O  O   . THR   A 1 334 ? 2.782   18.635  -56.645 1.00 103.69 ? 403  THR   A O   1 
ATOM   2439  C  CB  . THR   A 1 334 ? 2.450   20.794  -58.706 1.00 96.32  ? 403  THR   A CB  1 
ATOM   2440  O  OG1 . THR   A 1 334 ? 3.249   21.720  -59.452 1.00 91.60  ? 403  THR   A OG1 1 
ATOM   2441  C  CG2 . THR   A 1 334 ? 0.964   20.950  -59.034 1.00 102.34 ? 403  THR   A CG2 1 
ATOM   2442  N  N   . ALA   A 1 335 ? 1.005   19.816  -55.912 1.00 102.64 ? 404  ALA   A N   1 
ATOM   2443  C  CA  . ALA   A 1 335 ? 0.402   18.651  -55.285 1.00 104.53 ? 404  ALA   A CA  1 
ATOM   2444  C  C   . ALA   A 1 335 ? 0.075   17.609  -56.338 1.00 103.62 ? 404  ALA   A C   1 
ATOM   2445  O  O   . ALA   A 1 335 ? -0.654  17.893  -57.290 1.00 106.10 ? 404  ALA   A O   1 
ATOM   2446  C  CB  . ALA   A 1 335 ? -0.865  19.050  -54.545 1.00 111.51 ? 404  ALA   A CB  1 
ATOM   2447  N  N   . THR   A 1 336 ? 0.616   16.401  -56.183 1.00 105.03 ? 405  THR   A N   1 
ATOM   2448  C  CA  . THR   A 1 336 ? 0.164   15.335  -57.065 1.00 109.69 ? 405  THR   A CA  1 
ATOM   2449  C  C   . THR   A 1 336 ? -1.276  14.963  -56.726 1.00 113.91 ? 405  THR   A C   1 
ATOM   2450  O  O   . THR   A 1 336 ? -2.173  15.058  -57.575 1.00 108.37 ? 405  THR   A O   1 
ATOM   2451  C  CB  . THR   A 1 336 ? 1.083   14.108  -56.985 1.00 102.21 ? 405  THR   A CB  1 
ATOM   2452  O  OG1 . THR   A 1 336 ? 1.074   13.568  -55.668 1.00 102.61 ? 405  THR   A OG1 1 
ATOM   2453  C  CG2 . THR   A 1 336 ? 2.495   14.468  -57.375 1.00 103.38 ? 405  THR   A CG2 1 
ATOM   2454  N  N   . LYS   A 1 337 ? -1.527  14.633  -55.455 1.00 116.28 ? 406  LYS   A N   1 
ATOM   2455  C  CA  . LYS   A 1 337 ? -2.824  14.148  -55.012 1.00 117.09 ? 406  LYS   A CA  1 
ATOM   2456  C  C   . LYS   A 1 337 ? -3.775  15.313  -54.794 1.00 125.54 ? 406  LYS   A C   1 
ATOM   2457  O  O   . LYS   A 1 337 ? -3.459  16.470  -55.090 1.00 122.17 ? 406  LYS   A O   1 
ATOM   2458  C  CB  . LYS   A 1 337 ? -2.696  13.474  -53.651 1.00 112.93 ? 406  LYS   A CB  1 
ATOM   2459  N  N   . LYS   A 1 338 ? -4.949  15.010  -54.264 1.00 146.15 ? 407  LYS   A N   1 
ATOM   2460  C  CA  . LYS   A 1 338 ? -5.879  16.044  -53.861 1.00 147.65 ? 407  LYS   A CA  1 
ATOM   2461  C  C   . LYS   A 1 338 ? -6.043  16.267  -52.374 1.00 148.39 ? 407  LYS   A C   1 
ATOM   2462  O  O   . LYS   A 1 338 ? -6.499  17.339  -51.962 1.00 150.92 ? 407  LYS   A O   1 
ATOM   2463  C  CB  . LYS   A 1 338 ? -7.235  15.691  -54.483 1.00 147.20 ? 407  LYS   A CB  1 
ATOM   2464  N  N   . ASP   A 1 339 ? -5.636  15.282  -51.558 1.00 137.28 ? 408  ASP   A N   1 
ATOM   2465  C  CA  . ASP   A 1 339 ? -5.727  15.429  -50.113 1.00 139.76 ? 408  ASP   A CA  1 
ATOM   2466  C  C   . ASP   A 1 339 ? -4.767  16.506  -49.621 1.00 139.11 ? 408  ASP   A C   1 
ATOM   2467  O  O   . ASP   A 1 339 ? -5.123  17.293  -48.732 1.00 137.23 ? 408  ASP   A O   1 
ATOM   2468  C  CB  . ASP   A 1 339 ? -5.458  14.088  -49.425 1.00 136.17 ? 408  ASP   A CB  1 
ATOM   2469  N  N   . MET   A 1 340 ? -3.578  16.597  -50.228 1.00 136.56 ? 409  MET   A N   1 
ATOM   2470  C  CA  . MET   A 1 340 ? -2.502  17.434  -49.717 1.00 131.97 ? 409  MET   A CA  1 
ATOM   2471  C  C   . MET   A 1 340 ? -2.947  18.876  -49.543 1.00 132.48 ? 409  MET   A C   1 
ATOM   2472  O  O   . MET   A 1 340 ? -3.731  19.400  -50.339 1.00 131.67 ? 409  MET   A O   1 
ATOM   2473  C  CB  . MET   A 1 340 ? -1.310  17.396  -50.669 1.00 125.47 ? 409  MET   A CB  1 
ATOM   2474  C  CG  . MET   A 1 340 ? -1.257  16.161  -51.545 1.00 122.37 ? 409  MET   A CG  1 
ATOM   2475  S  SD  . MET   A 1 340 ? 0.417   15.970  -52.145 1.00 117.02 ? 409  MET   A SD  1 
ATOM   2476  C  CE  . MET   A 1 340 ? 1.370   15.516  -50.682 1.00 100.39 ? 409  MET   A CE  1 
ATOM   2477  N  N   . SER   A 1 341 ? -2.413  19.518  -48.517 1.00 131.76 ? 410  SER   A N   1 
ATOM   2478  C  CA  . SER   A 1 341 ? -2.663  20.929  -48.269 1.00 132.32 ? 410  SER   A CA  1 
ATOM   2479  C  C   . SER   A 1 341 ? -1.431  21.496  -47.592 1.00 131.82 ? 410  SER   A C   1 
ATOM   2480  O  O   . SER   A 1 341 ? -1.087  21.050  -46.488 1.00 131.46 ? 410  SER   A O   1 
ATOM   2481  C  CB  . SER   A 1 341 ? -3.888  21.136  -47.391 1.00 138.09 ? 410  SER   A CB  1 
ATOM   2482  O  OG  . SER   A 1 341 ? -4.018  22.515  -47.089 1.00 143.60 ? 410  SER   A OG  1 
ATOM   2483  N  N   . PRO   A 1 342 ? -0.738  22.470  -48.208 1.00 126.05 ? 411  PRO   A N   1 
ATOM   2484  C  CA  . PRO   A 1 342 ? -1.090  23.231  -49.410 1.00 121.44 ? 411  PRO   A CA  1 
ATOM   2485  C  C   . PRO   A 1 342 ? -0.920  22.432  -50.700 1.00 120.71 ? 411  PRO   A C   1 
ATOM   2486  O  O   . PRO   A 1 342 ? -0.385  21.322  -50.715 1.00 120.34 ? 411  PRO   A O   1 
ATOM   2487  C  CB  . PRO   A 1 342 ? -0.110  24.409  -49.340 1.00 113.33 ? 411  PRO   A CB  1 
ATOM   2488  C  CG  . PRO   A 1 342 ? 1.140   23.763  -48.836 1.00 109.50 ? 411  PRO   A CG  1 
ATOM   2489  C  CD  . PRO   A 1 342 ? 0.671   22.713  -47.839 1.00 123.40 ? 411  PRO   A CD  1 
ATOM   2490  N  N   . GLN   A 1 343 ? -1.380  22.985  -51.814 1.00 117.87 ? 412  GLN   A N   1 
ATOM   2491  C  CA  . GLN   A 1 343 ? -1.247  22.345  -53.115 1.00 112.01 ? 412  GLN   A CA  1 
ATOM   2492  C  C   . GLN   A 1 343 ? -0.199  23.002  -54.002 1.00 108.26 ? 412  GLN   A C   1 
ATOM   2493  O  O   . GLN   A 1 343 ? 0.574   22.307  -54.667 1.00 105.95 ? 412  GLN   A O   1 
ATOM   2494  C  CB  . GLN   A 1 343 ? -2.597  22.342  -53.841 1.00 116.07 ? 412  GLN   A CB  1 
ATOM   2495  C  CG  . GLN   A 1 343 ? -3.703  21.605  -53.105 1.00 119.80 ? 412  GLN   A CG  1 
ATOM   2496  C  CD  . GLN   A 1 343 ? -4.082  20.291  -53.768 1.00 120.76 ? 412  GLN   A CD  1 
ATOM   2497  O  OE1 . GLN   A 1 343 ? -4.664  20.279  -54.858 1.00 117.23 ? 412  GLN   A OE1 1 
ATOM   2498  N  NE2 . GLN   A 1 343 ? -3.753  19.174  -53.111 1.00 124.58 ? 412  GLN   A NE2 1 
ATOM   2499  N  N   . LYS   A 1 344 ? -0.154  24.319  -54.042 1.00 103.08 ? 413  LYS   A N   1 
ATOM   2500  C  CA  . LYS   A 1 344 ? 0.933   25.034  -54.686 1.00 96.30  ? 413  LYS   A CA  1 
ATOM   2501  C  C   . LYS   A 1 344 ? 1.719   25.738  -53.587 1.00 98.97  ? 413  LYS   A C   1 
ATOM   2502  O  O   . LYS   A 1 344 ? 1.176   26.599  -52.886 1.00 101.98 ? 413  LYS   A O   1 
ATOM   2503  C  CB  . LYS   A 1 344 ? 0.402   26.025  -55.719 1.00 90.10  ? 413  LYS   A CB  1 
ATOM   2504  N  N   . PHE   A 1 345 ? 2.978   25.345  -53.408 1.00 94.75  ? 414  PHE   A N   1 
ATOM   2505  C  CA  . PHE   A 1 345 ? 3.955   26.196  -52.739 1.00 93.27  ? 414  PHE   A CA  1 
ATOM   2506  C  C   . PHE   A 1 345 ? 5.161   26.350  -53.662 1.00 92.20  ? 414  PHE   A C   1 
ATOM   2507  O  O   . PHE   A 1 345 ? 5.157   25.870  -54.796 1.00 92.28  ? 414  PHE   A O   1 
ATOM   2508  C  CB  . PHE   A 1 345 ? 4.326   25.662  -51.346 1.00 92.78  ? 414  PHE   A CB  1 
ATOM   2509  C  CG  . PHE   A 1 345 ? 5.105   24.360  -51.334 1.00 93.67  ? 414  PHE   A CG  1 
ATOM   2510  C  CD1 . PHE   A 1 345 ? 4.449   23.137  -51.367 1.00 94.70  ? 414  PHE   A CD1 1 
ATOM   2511  C  CD2 . PHE   A 1 345 ? 6.496   24.366  -51.209 1.00 91.62  ? 414  PHE   A CD2 1 
ATOM   2512  C  CE1 . PHE   A 1 345 ? 5.174   21.949  -51.324 1.00 94.74  ? 414  PHE   A CE1 1 
ATOM   2513  C  CE2 . PHE   A 1 345 ? 7.218   23.182  -51.166 1.00 89.12  ? 414  PHE   A CE2 1 
ATOM   2514  C  CZ  . PHE   A 1 345 ? 6.560   21.977  -51.228 1.00 92.66  ? 414  PHE   A CZ  1 
ATOM   2515  N  N   . TRP   A 1 346 ? 6.189   27.045  -53.186 1.00 97.06  ? 415  TRP   A N   1 
ATOM   2516  C  CA  . TRP   A 1 346 ? 7.393   27.273  -53.978 1.00 95.42  ? 415  TRP   A CA  1 
ATOM   2517  C  C   . TRP   A 1 346 ? 8.640   27.097  -53.128 1.00 94.86  ? 415  TRP   A C   1 
ATOM   2518  O  O   . TRP   A 1 346 ? 8.679   27.553  -51.983 1.00 96.59  ? 415  TRP   A O   1 
ATOM   2519  C  CB  . TRP   A 1 346 ? 7.435   28.681  -54.556 1.00 98.40  ? 415  TRP   A CB  1 
ATOM   2520  C  CG  . TRP   A 1 346 ? 6.272   29.083  -55.341 1.00 99.30  ? 415  TRP   A CG  1 
ATOM   2521  C  CD1 . TRP   A 1 346 ? 5.012   29.334  -54.880 1.00 100.60 ? 415  TRP   A CD1 1 
ATOM   2522  C  CD2 . TRP   A 1 346 ? 6.257   29.352  -56.735 1.00 100.02 ? 415  TRP   A CD2 1 
ATOM   2523  N  NE1 . TRP   A 1 346 ? 4.204   29.728  -55.914 1.00 102.58 ? 415  TRP   A NE1 1 
ATOM   2524  C  CE2 . TRP   A 1 346 ? 4.945   29.742  -57.069 1.00 102.71 ? 415  TRP   A CE2 1 
ATOM   2525  C  CE3 . TRP   A 1 346 ? 7.224   29.288  -57.741 1.00 98.11  ? 415  TRP   A CE3 1 
ATOM   2526  C  CZ2 . TRP   A 1 346 ? 4.575   30.061  -58.374 1.00 105.13 ? 415  TRP   A CZ2 1 
ATOM   2527  C  CZ3 . TRP   A 1 346 ? 6.860   29.607  -59.029 1.00 99.87  ? 415  TRP   A CZ3 1 
ATOM   2528  C  CH2 . TRP   A 1 346 ? 5.544   29.987  -59.340 1.00 102.63 ? 415  TRP   A CH2 1 
ATOM   2529  N  N   . GLY   A 1 347 ? 9.675   26.487  -53.701 1.00 84.34  ? 416  GLY   A N   1 
ATOM   2530  C  CA  . GLY   A 1 347 ? 10.939  26.349  -52.994 1.00 87.05  ? 416  GLY   A CA  1 
ATOM   2531  C  C   . GLY   A 1 347 ? 12.033  27.218  -53.579 1.00 87.19  ? 416  GLY   A C   1 
ATOM   2532  O  O   . GLY   A 1 347 ? 12.375  27.049  -54.749 1.00 91.23  ? 416  GLY   A O   1 
ATOM   2533  N  N   . LEU   A 1 348 ? 12.591  28.151  -52.804 1.00 85.68  ? 417  LEU   A N   1 
ATOM   2534  C  CA  . LEU   A 1 348 ? 13.540  29.133  -53.320 1.00 80.42  ? 417  LEU   A CA  1 
ATOM   2535  C  C   . LEU   A 1 348 ? 14.903  28.936  -52.674 1.00 79.56  ? 417  LEU   A C   1 
ATOM   2536  O  O   . LEU   A 1 348 ? 15.022  28.989  -51.446 1.00 80.36  ? 417  LEU   A O   1 
ATOM   2537  C  CB  . LEU   A 1 348 ? 13.042  30.540  -53.048 1.00 80.03  ? 417  LEU   A CB  1 
ATOM   2538  C  CG  . LEU   A 1 348 ? 11.557  30.773  -53.296 1.00 82.06  ? 417  LEU   A CG  1 
ATOM   2539  C  CD1 . LEU   A 1 348 ? 11.241  32.212  -52.918 1.00 83.01  ? 417  LEU   A CD1 1 
ATOM   2540  C  CD2 . LEU   A 1 348 ? 11.189  30.465  -54.735 1.00 81.06  ? 417  LEU   A CD2 1 
ATOM   2541  N  N   . THR   A 1 349 ? 15.929  28.738  -53.498 1.00 80.99  ? 418  THR   A N   1 
ATOM   2542  C  CA  . THR   A 1 349 ? 17.267  28.456  -52.973 1.00 84.39  ? 418  THR   A CA  1 
ATOM   2543  C  C   . THR   A 1 349 ? 17.779  29.806  -52.463 1.00 84.02  ? 418  THR   A C   1 
ATOM   2544  O  O   . THR   A 1 349 ? 17.521  30.863  -53.050 1.00 85.80  ? 418  THR   A O   1 
ATOM   2545  C  CB  . THR   A 1 349 ? 18.074  27.663  -54.041 1.00 84.87  ? 418  THR   A CB  1 
ATOM   2546  O  OG1 . THR   A 1 349 ? 19.423  27.421  -53.584 1.00 84.85  ? 418  THR   A OG1 1 
ATOM   2547  C  CG2 . THR   A 1 349 ? 18.060  28.370  -55.401 1.00 87.42  ? 418  THR   A CG2 1 
ATOM   2548  N  N   . ARG   A 1 350 ? 18.506  29.762  -51.351 1.00 78.83  ? 419  ARG   A N   1 
ATOM   2549  C  CA  . ARG   A 1 350 ? 19.032  30.927  -50.640 1.00 78.64  ? 419  ARG   A CA  1 
ATOM   2550  C  C   . ARG   A 1 350 ? 20.006  31.673  -51.555 1.00 79.92  ? 419  ARG   A C   1 
ATOM   2551  O  O   . ARG   A 1 350 ? 20.136  32.905  -51.483 1.00 79.25  ? 419  ARG   A O   1 
ATOM   2552  C  CB  . ARG   A 1 350 ? 19.784  30.441  -49.418 1.00 78.05  ? 419  ARG   A CB  1 
ATOM   2553  C  CG  . ARG   A 1 350 ? 20.194  31.523  -48.546 1.00 77.80  ? 419  ARG   A CG  1 
ATOM   2554  C  CD  . ARG   A 1 350 ? 21.217  31.080  -47.578 1.00 78.61  ? 419  ARG   A CD  1 
ATOM   2555  N  NE  . ARG   A 1 350 ? 22.508  30.783  -48.184 1.00 79.79  ? 419  ARG   A NE  1 
ATOM   2556  C  CZ  . ARG   A 1 350 ? 23.345  31.682  -48.692 1.00 86.04  ? 419  ARG   A CZ  1 
ATOM   2557  N  NH1 . ARG   A 1 350 ? 22.996  32.953  -48.853 1.00 87.68  ? 419  ARG   A NH1 1 
ATOM   2558  N  NH2 . ARG   A 1 350 ? 24.563  31.296  -49.057 1.00 87.48  ? 419  ARG   A NH2 1 
ATOM   2559  N  N   . SER   A 1 351 ? 20.727  30.920  -52.379 1.00 80.68  ? 420  SER   A N   1 
ATOM   2560  C  CA  . SER   A 1 351 ? 21.775  31.507  -53.196 1.00 79.93  ? 420  SER   A CA  1 
ATOM   2561  C  C   . SER   A 1 351 ? 21.198  32.598  -54.059 1.00 83.40  ? 420  SER   A C   1 
ATOM   2562  O  O   . SER   A 1 351 ? 21.887  33.586  -54.349 1.00 87.18  ? 420  SER   A O   1 
ATOM   2563  C  CB  . SER   A 1 351 ? 22.439  30.426  -54.029 1.00 83.72  ? 420  SER   A CB  1 
ATOM   2564  O  OG  . SER   A 1 351 ? 22.646  29.246  -53.266 1.00 88.33  ? 420  SER   A OG  1 
ATOM   2565  N  N   . ALA   A 1 352 ? 19.957  32.425  -54.495 1.00 85.27  ? 421  ALA   A N   1 
ATOM   2566  C  CA  . ALA   A 1 352 ? 19.361  33.313  -55.473 1.00 86.01  ? 421  ALA   A CA  1 
ATOM   2567  C  C   . ALA   A 1 352 ? 18.725  34.555  -54.896 1.00 87.54  ? 421  ALA   A C   1 
ATOM   2568  O  O   . ALA   A 1 352 ? 18.535  35.520  -55.635 1.00 92.70  ? 421  ALA   A O   1 
ATOM   2569  C  CB  . ALA   A 1 352 ? 18.313  32.531  -56.273 1.00 84.91  ? 421  ALA   A CB  1 
ATOM   2570  N  N   . LEU   A 1 353 ? 18.425  34.566  -53.602 1.00 87.95  ? 422  LEU   A N   1 
ATOM   2571  C  CA  . LEU   A 1 353 ? 17.641  35.641  -53.015 1.00 86.31  ? 422  LEU   A CA  1 
ATOM   2572  C  C   . LEU   A 1 353 ? 18.533  36.778  -52.512 1.00 86.37  ? 422  LEU   A C   1 
ATOM   2573  O  O   . LEU   A 1 353 ? 19.758  36.655  -52.402 1.00 87.11  ? 422  LEU   A O   1 
ATOM   2574  C  CB  . LEU   A 1 353 ? 16.764  35.088  -51.888 1.00 80.68  ? 422  LEU   A CB  1 
ATOM   2575  C  CG  . LEU   A 1 353 ? 15.959  33.873  -52.360 1.00 79.82  ? 422  LEU   A CG  1 
ATOM   2576  C  CD1 . LEU   A 1 353 ? 15.496  32.984  -51.212 1.00 79.21  ? 422  LEU   A CD1 1 
ATOM   2577  C  CD2 . LEU   A 1 353 ? 14.795  34.289  -53.261 1.00 82.45  ? 422  LEU   A CD2 1 
ATOM   2578  N  N   . LEU   A 1 354 ? 17.891  37.907  -52.234 1.00 87.69  ? 423  LEU   A N   1 
ATOM   2579  C  CA  . LEU   A 1 354 ? 18.554  39.075  -51.667 1.00 89.06  ? 423  LEU   A CA  1 
ATOM   2580  C  C   . LEU   A 1 354 ? 17.576  39.925  -50.853 1.00 87.92  ? 423  LEU   A C   1 
ATOM   2581  O  O   . LEU   A 1 354 ? 16.649  40.525  -51.421 1.00 84.79  ? 423  LEU   A O   1 
ATOM   2582  C  CB  . LEU   A 1 354 ? 19.206  39.886  -52.784 1.00 86.03  ? 423  LEU   A CB  1 
ATOM   2583  C  CG  . LEU   A 1 354 ? 19.717  41.262  -52.418 1.00 80.86  ? 423  LEU   A CG  1 
ATOM   2584  C  CD1 . LEU   A 1 354 ? 21.064  41.488  -53.035 1.00 87.66  ? 423  LEU   A CD1 1 
ATOM   2585  C  CD2 . LEU   A 1 354 ? 18.730  42.232  -52.950 1.00 81.25  ? 423  LEU   A CD2 1 
ATOM   2586  N  N   . PRO   A 1 355 ? 17.770  39.996  -49.523 1.00 88.13  ? 424  PRO   A N   1 
ATOM   2587  C  CA  . PRO   A 1 355 ? 16.877  40.776  -48.650 1.00 86.15  ? 424  PRO   A CA  1 
ATOM   2588  C  C   . PRO   A 1 355 ? 16.898  42.272  -48.948 1.00 86.23  ? 424  PRO   A C   1 
ATOM   2589  O  O   . PRO   A 1 355 ? 17.934  42.859  -49.267 1.00 88.02  ? 424  PRO   A O   1 
ATOM   2590  C  CB  . PRO   A 1 355 ? 17.436  40.497  -47.246 1.00 85.36  ? 424  PRO   A CB  1 
ATOM   2591  C  CG  . PRO   A 1 355 ? 18.184  39.225  -47.359 1.00 87.32  ? 424  PRO   A CG  1 
ATOM   2592  C  CD  . PRO   A 1 355 ? 18.744  39.213  -48.745 1.00 91.69  ? 424  PRO   A CD  1 
ATOM   2593  N  N   . THR   A 1 356 ? 15.736  42.899  -48.793 1.00 79.43  ? 425  THR   A N   1 
ATOM   2594  C  CA  . THR   A 1 356 ? 15.578  44.296  -49.154 1.00 79.82  ? 425  THR   A CA  1 
ATOM   2595  C  C   . THR   A 1 356 ? 14.582  44.946  -48.209 1.00 81.99  ? 425  THR   A C   1 
ATOM   2596  O  O   . THR   A 1 356 ? 13.662  44.294  -47.714 1.00 85.46  ? 425  THR   A O   1 
ATOM   2597  C  CB  . THR   A 1 356 ? 15.086  44.445  -50.597 1.00 88.82  ? 425  THR   A CB  1 
ATOM   2598  O  OG1 . THR   A 1 356 ? 13.908  43.647  -50.790 1.00 88.93  ? 425  THR   A OG1 1 
ATOM   2599  C  CG2 . THR   A 1 356 ? 16.155  44.017  -51.599 1.00 89.77  ? 425  THR   A CG2 1 
ATOM   2600  N  N   . ILE   A 1 357 ? 14.771  46.240  -47.974 1.00 83.20  ? 426  ILE   A N   1 
ATOM   2601  C  CA  . ILE   A 1 357 ? 13.931  47.026  -47.067 1.00 85.48  ? 426  ILE   A CA  1 
ATOM   2602  C  C   . ILE   A 1 357 ? 12.882  47.801  -47.871 1.00 85.14  ? 426  ILE   A C   1 
ATOM   2603  O  O   . ILE   A 1 357 ? 13.199  48.877  -48.402 1.00 86.94  ? 426  ILE   A O   1 
ATOM   2604  C  CB  . ILE   A 1 357 ? 14.796  47.983  -46.217 1.00 85.60  ? 426  ILE   A CB  1 
ATOM   2605  C  CG1 . ILE   A 1 357 ? 15.939  47.230  -45.533 1.00 81.35  ? 426  ILE   A CG1 1 
ATOM   2606  C  CG2 . ILE   A 1 357 ? 13.970  48.695  -45.177 1.00 86.53  ? 426  ILE   A CG2 1 
ATOM   2607  C  CD1 . ILE   A 1 357 ? 17.108  48.112  -45.156 1.00 84.76  ? 426  ILE   A CD1 1 
ATOM   2608  N  N   . PRO   A 1 358 ? 11.620  47.322  -47.977 1.00 80.23  ? 427  PRO   A N   1 
ATOM   2609  C  CA  . PRO   A 1 358 ? 10.497  47.952  -48.710 1.00 82.92  ? 427  PRO   A CA  1 
ATOM   2610  C  C   . PRO   A 1 358 ? 10.213  49.460  -48.446 1.00 87.14  ? 427  PRO   A C   1 
ATOM   2611  O  O   . PRO   A 1 358 ? 9.490   50.163  -49.197 1.00 82.89  ? 427  PRO   A O   1 
ATOM   2612  C  CB  . PRO   A 1 358 ? 9.301   47.104  -48.263 1.00 80.24  ? 427  PRO   A CB  1 
ATOM   2613  C  CG  . PRO   A 1 358 ? 9.886   45.738  -48.091 1.00 80.04  ? 427  PRO   A CG  1 
ATOM   2614  C  CD  . PRO   A 1 358 ? 11.259  45.971  -47.505 1.00 79.57  ? 427  PRO   A CD  1 
ATOM   2615  N  N   . VAL   A 1 369 ? 17.797  53.835  -44.173 1.00 135.84 ? 438  VAL   A N   1 
ATOM   2616  C  CA  . VAL   A 1 369 ? 17.547  52.522  -43.567 1.00 134.36 ? 438  VAL   A CA  1 
ATOM   2617  C  C   . VAL   A 1 369 ? 18.832  51.677  -43.491 1.00 131.48 ? 438  VAL   A C   1 
ATOM   2618  O  O   . VAL   A 1 369 ? 19.319  51.151  -44.505 1.00 133.57 ? 438  VAL   A O   1 
ATOM   2619  C  CB  . VAL   A 1 369 ? 16.426  51.759  -44.327 1.00 134.05 ? 438  VAL   A CB  1 
ATOM   2620  C  CG1 . VAL   A 1 369 ? 15.058  52.261  -43.892 1.00 136.72 ? 438  VAL   A CG1 1 
ATOM   2621  C  CG2 . VAL   A 1 369 ? 16.586  51.907  -45.859 1.00 132.87 ? 438  VAL   A CG2 1 
ATOM   2622  N  N   . ILE   A 1 370 ? 19.374  51.553  -42.277 1.00 118.24 ? 439  ILE   A N   1 
ATOM   2623  C  CA  . ILE   A 1 370 ? 20.610  50.821  -42.014 1.00 108.79 ? 439  ILE   A CA  1 
ATOM   2624  C  C   . ILE   A 1 370 ? 20.340  49.744  -40.973 1.00 104.00 ? 439  ILE   A C   1 
ATOM   2625  O  O   . ILE   A 1 370 ? 19.570  49.953  -40.028 1.00 104.06 ? 439  ILE   A O   1 
ATOM   2626  C  CB  . ILE   A 1 370 ? 21.725  51.757  -41.507 1.00 106.30 ? 439  ILE   A CB  1 
ATOM   2627  C  CG1 . ILE   A 1 370 ? 21.752  53.040  -42.322 1.00 105.08 ? 439  ILE   A CG1 1 
ATOM   2628  C  CG2 . ILE   A 1 370 ? 23.069  51.045  -41.493 1.00 104.46 ? 439  ILE   A CG2 1 
ATOM   2629  C  CD1 . ILE   A 1 370 ? 22.562  54.115  -41.695 1.00 100.95 ? 439  ILE   A CD1 1 
ATOM   2630  N  N   . LEU   A 1 371 ? 20.994  48.600  -41.125 1.00 99.17  ? 440  LEU   A N   1 
ATOM   2631  C  CA  . LEU   A 1 371 ? 20.938  47.583  -40.089 1.00 96.62  ? 440  LEU   A CA  1 
ATOM   2632  C  C   . LEU   A 1 371 ? 21.810  48.021  -38.906 1.00 98.31  ? 440  LEU   A C   1 
ATOM   2633  O  O   . LEU   A 1 371 ? 22.931  48.509  -39.095 1.00 98.24  ? 440  LEU   A O   1 
ATOM   2634  C  CB  . LEU   A 1 371 ? 21.367  46.228  -40.653 1.00 94.13  ? 440  LEU   A CB  1 
ATOM   2635  C  CG  . LEU   A 1 371 ? 20.432  45.407  -41.586 1.00 88.59  ? 440  LEU   A CG  1 
ATOM   2636  C  CD1 . LEU   A 1 371 ? 19.127  44.992  -40.934 1.00 86.38  ? 440  LEU   A CD1 1 
ATOM   2637  C  CD2 . LEU   A 1 371 ? 20.129  46.120  -42.879 1.00 92.92  ? 440  LEU   A CD2 1 
ATOM   2638  N  N   . CYS   A 1 372 ? 21.264  47.915  -37.694 1.00 102.22 ? 441  CYS   A N   1 
ATOM   2639  C  CA  . CYS   A 1 372 ? 21.998  48.447  -36.519 1.00 100.10 ? 441  CYS   A CA  1 
ATOM   2640  C  C   . CYS   A 1 372 ? 22.521  47.328  -35.622 1.00 97.30  ? 441  CYS   A C   1 
ATOM   2641  O  O   . CYS   A 1 372 ? 22.234  46.155  -35.906 1.00 97.96  ? 441  CYS   A O   1 
ATOM   2642  C  CB  . CYS   A 1 372 ? 21.092  49.316  -35.659 1.00 100.12 ? 441  CYS   A CB  1 
ATOM   2643  S  SG  . CYS   A 1 372 ? 20.446  50.760  -36.538 1.00 113.38 ? 441  CYS   A SG  1 
ATOM   2644  N  N   . LEU   A 1 373 ? 23.256  47.703  -34.578 1.00 94.36  ? 442  LEU   A N   1 
ATOM   2645  C  CA  . LEU   A 1 373 ? 23.800  46.708  -33.624 1.00 98.15  ? 442  LEU   A CA  1 
ATOM   2646  C  C   . LEU   A 1 373 ? 23.802  47.337  -32.224 1.00 98.80  ? 442  LEU   A C   1 
ATOM   2647  O  O   . LEU   A 1 373 ? 24.778  47.200  -31.504 1.00 95.14  ? 442  LEU   A O   1 
ATOM   2648  C  CB  . LEU   A 1 373 ? 25.197  46.274  -34.063 1.00 95.66  ? 442  LEU   A CB  1 
ATOM   2649  C  CG  . LEU   A 1 373 ? 26.270  47.365  -34.112 1.00 95.50  ? 442  LEU   A CG  1 
ATOM   2650  C  CD1 . LEU   A 1 373 ? 26.812  47.641  -32.723 1.00 101.67 ? 442  LEU   A CD1 1 
ATOM   2651  C  CD2 . LEU   A 1 373 ? 27.392  46.955  -35.047 1.00 84.70  ? 442  LEU   A CD2 1 
ATOM   2652  O  OXT . LEU   A 1 373 ? 22.793  47.969  -31.890 1.00 97.32  ? 442  LEU   A OXT 1 
ATOM   2653  N  N   . SER   B 2 2   ? 46.491  61.350  -24.125 1.00 118.08 ? 2    SER   B N   1 
ATOM   2654  C  CA  . SER   B 2 2   ? 46.056  62.144  -22.980 1.00 118.54 ? 2    SER   B CA  1 
ATOM   2655  C  C   . SER   B 2 2   ? 46.579  61.595  -21.672 1.00 116.64 ? 2    SER   B C   1 
ATOM   2656  O  O   . SER   B 2 2   ? 46.962  60.443  -21.567 1.00 116.85 ? 2    SER   B O   1 
ATOM   2657  C  CB  . SER   B 2 2   ? 44.529  62.214  -22.903 1.00 117.18 ? 2    SER   B CB  1 
ATOM   2658  O  OG  . SER   B 2 2   ? 44.102  63.307  -22.097 1.00 114.37 ? 2    SER   B OG  1 
ATOM   2659  N  N   . TYR   B 2 3   ? 46.568  62.450  -20.665 1.00 121.21 ? 3    TYR   B N   1 
ATOM   2660  C  CA  . TYR   B 2 3   ? 46.979  62.095  -19.319 1.00 122.53 ? 3    TYR   B CA  1 
ATOM   2661  C  C   . TYR   B 2 3   ? 46.082  62.858  -18.365 1.00 124.23 ? 3    TYR   B C   1 
ATOM   2662  O  O   . TYR   B 2 3   ? 45.954  64.083  -18.479 1.00 122.36 ? 3    TYR   B O   1 
ATOM   2663  C  CB  . TYR   B 2 3   ? 48.444  62.452  -19.064 1.00 126.89 ? 3    TYR   B CB  1 
ATOM   2664  C  CG  . TYR   B 2 3   ? 49.376  62.076  -20.184 1.00 130.01 ? 3    TYR   B CG  1 
ATOM   2665  C  CD1 . TYR   B 2 3   ? 49.625  60.744  -20.481 1.00 129.69 ? 3    TYR   B CD1 1 
ATOM   2666  C  CD2 . TYR   B 2 3   ? 50.019  63.050  -20.940 1.00 132.11 ? 3    TYR   B CD2 1 
ATOM   2667  C  CE1 . TYR   B 2 3   ? 50.478  60.389  -21.515 1.00 132.50 ? 3    TYR   B CE1 1 
ATOM   2668  C  CE2 . TYR   B 2 3   ? 50.878  62.706  -21.971 1.00 131.36 ? 3    TYR   B CE2 1 
ATOM   2669  C  CZ  . TYR   B 2 3   ? 51.107  61.373  -22.251 1.00 131.75 ? 3    TYR   B CZ  1 
ATOM   2670  O  OH  . TYR   B 2 3   ? 51.960  61.013  -23.264 1.00 131.27 ? 3    TYR   B OH  1 
ATOM   2671  N  N   . ASN   B 2 4   ? 45.460  62.144  -17.432 1.00 111.71 ? 4    ASN   B N   1 
ATOM   2672  C  CA  . ASN   B 2 4   ? 44.434  62.750  -16.609 1.00 107.99 ? 4    ASN   B CA  1 
ATOM   2673  C  C   . ASN   B 2 4   ? 44.668  62.462  -15.134 1.00 102.83 ? 4    ASN   B C   1 
ATOM   2674  O  O   . ASN   B 2 4   ? 45.397  61.543  -14.749 1.00 101.52 ? 4    ASN   B O   1 
ATOM   2675  C  CB  . ASN   B 2 4   ? 43.051  62.290  -17.070 1.00 103.41 ? 4    ASN   B CB  1 
ATOM   2676  C  CG  . ASN   B 2 4   ? 42.738  62.772  -18.487 1.00 112.62 ? 4    ASN   B CG  1 
ATOM   2677  O  OD1 . ASN   B 2 4   ? 42.379  63.945  -18.704 1.00 109.94 ? 4    ASN   B OD1 1 
ATOM   2678  N  ND2 . ASN   B 2 4   ? 42.900  61.876  -19.462 1.00 112.88 ? 4    ASN   B ND2 1 
ATOM   2679  N  N   . TYR   B 2 5   ? 44.058  63.312  -14.318 1.00 101.96 ? 5    TYR   B N   1 
ATOM   2680  C  CA  . TYR   B 2 5   ? 44.150  63.278  -12.868 1.00 98.76  ? 5    TYR   B CA  1 
ATOM   2681  C  C   . TYR   B 2 5   ? 42.721  63.156  -12.357 1.00 99.45  ? 5    TYR   B C   1 
ATOM   2682  O  O   . TYR   B 2 5   ? 41.875  63.990  -12.694 1.00 99.62  ? 5    TYR   B O   1 
ATOM   2683  C  CB  . TYR   B 2 5   ? 44.849  64.552  -12.378 1.00 99.79  ? 5    TYR   B CB  1 
ATOM   2684  C  CG  . TYR   B 2 5   ? 45.114  64.758  -10.885 1.00 99.61  ? 5    TYR   B CG  1 
ATOM   2685  C  CD1 . TYR   B 2 5   ? 44.220  65.479  -10.094 1.00 97.27  ? 5    TYR   B CD1 1 
ATOM   2686  C  CD2 . TYR   B 2 5   ? 46.296  64.326  -10.289 1.00 100.81 ? 5    TYR   B CD2 1 
ATOM   2687  C  CE1 . TYR   B 2 5   ? 44.463  65.717  -8.735  1.00 97.85  ? 5    TYR   B CE1 1 
ATOM   2688  C  CE2 . TYR   B 2 5   ? 46.550  64.565  -8.918  1.00 103.24 ? 5    TYR   B CE2 1 
ATOM   2689  C  CZ  . TYR   B 2 5   ? 45.624  65.268  -8.149  1.00 100.29 ? 5    TYR   B CZ  1 
ATOM   2690  O  OH  . TYR   B 2 5   ? 45.840  65.527  -6.806  1.00 94.71  ? 5    TYR   B OH  1 
ATOM   2691  N  N   . VAL   B 2 6   ? 42.432  62.080  -11.622 1.00 97.79  ? 6    VAL   B N   1 
ATOM   2692  C  CA  . VAL   B 2 6   ? 41.113  61.838  -11.035 1.00 92.13  ? 6    VAL   B CA  1 
ATOM   2693  C  C   . VAL   B 2 6   ? 41.230  62.029  -9.533  1.00 92.96  ? 6    VAL   B C   1 
ATOM   2694  O  O   . VAL   B 2 6   ? 42.121  61.454  -8.899  1.00 94.95  ? 6    VAL   B O   1 
ATOM   2695  C  CB  . VAL   B 2 6   ? 40.581  60.430  -11.371 1.00 92.40  ? 6    VAL   B CB  1 
ATOM   2696  C  CG1 . VAL   B 2 6   ? 40.109  60.368  -12.799 1.00 93.84  ? 6    VAL   B CG1 1 
ATOM   2697  C  CG2 . VAL   B 2 6   ? 41.662  59.359  -11.154 1.00 92.41  ? 6    VAL   B CG2 1 
ATOM   2698  N  N   . VAL   B 2 7   ? 40.361  62.853  -8.959  1.00 94.59  ? 7    VAL   B N   1 
ATOM   2699  C  CA  . VAL   B 2 7   ? 40.375  63.046  -7.515  1.00 94.74  ? 7    VAL   B CA  1 
ATOM   2700  C  C   . VAL   B 2 7   ? 38.952  63.034  -6.994  1.00 90.81  ? 7    VAL   B C   1 
ATOM   2701  O  O   . VAL   B 2 7   ? 38.007  63.444  -7.673  1.00 90.24  ? 7    VAL   B O   1 
ATOM   2702  C  CB  . VAL   B 2 7   ? 41.088  64.339  -7.070  1.00 96.41  ? 7    VAL   B CB  1 
ATOM   2703  C  CG1 . VAL   B 2 7   ? 40.144  65.537  -7.171  1.00 103.36 ? 7    VAL   B CG1 1 
ATOM   2704  C  CG2 . VAL   B 2 7   ? 41.633  64.182  -5.648  1.00 97.40  ? 7    VAL   B CG2 1 
ATOM   2705  N  N   . THR   B 2 8   ? 38.809  62.534  -5.779  1.00 87.90  ? 8    THR   B N   1 
ATOM   2706  C  CA  . THR   B 2 8   ? 37.503  62.410  -5.174  1.00 88.06  ? 8    THR   B CA  1 
ATOM   2707  C  C   . THR   B 2 8   ? 37.130  63.738  -4.554  1.00 87.68  ? 8    THR   B C   1 
ATOM   2708  O  O   . THR   B 2 8   ? 37.912  64.317  -3.801  1.00 98.45  ? 8    THR   B O   1 
ATOM   2709  C  CB  . THR   B 2 8   ? 37.509  61.304  -4.131  1.00 89.04  ? 8    THR   B CB  1 
ATOM   2710  O  OG1 . THR   B 2 8   ? 37.886  60.076  -4.774  1.00 88.82  ? 8    THR   B OG1 1 
ATOM   2711  C  CG2 . THR   B 2 8   ? 36.126  61.167  -3.505  1.00 89.58  ? 8    THR   B CG2 1 
ATOM   2712  N  N   . ALA   B 2 9   ? 35.958  64.237  -4.913  1.00 85.01  ? 9    ALA   B N   1 
ATOM   2713  C  CA  . ALA   B 2 9   ? 35.445  65.488  -4.400  1.00 82.43  ? 9    ALA   B CA  1 
ATOM   2714  C  C   . ALA   B 2 9   ? 34.361  65.272  -3.365  1.00 81.35  ? 9    ALA   B C   1 
ATOM   2715  O  O   . ALA   B 2 9   ? 33.957  66.226  -2.701  1.00 85.17  ? 9    ALA   B O   1 
ATOM   2716  C  CB  . ALA   B 2 9   ? 34.906  66.337  -5.551  1.00 85.99  ? 9    ALA   B CB  1 
ATOM   2717  N  N   . GLN   B 2 10  ? 33.898  64.041  -3.212  1.00 82.65  ? 10   GLN   B N   1 
ATOM   2718  C  CA  . GLN   B 2 10  ? 32.955  63.678  -2.161  1.00 81.85  ? 10   GLN   B CA  1 
ATOM   2719  C  C   . GLN   B 2 10  ? 32.997  62.169  -2.045  1.00 84.77  ? 10   GLN   B C   1 
ATOM   2720  O  O   . GLN   B 2 10  ? 32.658  61.474  -3.009  1.00 86.82  ? 10   GLN   B O   1 
ATOM   2721  C  CB  . GLN   B 2 10  ? 31.544  64.155  -2.481  1.00 80.25  ? 10   GLN   B CB  1 
ATOM   2722  C  CG  . GLN   B 2 10  ? 30.501  63.500  -1.610  1.00 79.90  ? 10   GLN   B CG  1 
ATOM   2723  C  CD  . GLN   B 2 10  ? 30.903  63.487  -0.153  1.00 86.50  ? 10   GLN   B CD  1 
ATOM   2724  O  OE1 . GLN   B 2 10  ? 31.261  64.512  0.411   1.00 91.95  ? 10   GLN   B OE1 1 
ATOM   2725  N  NE2 . GLN   B 2 10  ? 30.869  62.318  0.457   1.00 89.24  ? 10   GLN   B NE2 1 
ATOM   2726  N  N   . LYS   B 2 11  ? 33.427  61.655  -0.887  1.00 88.10  ? 11   LYS   B N   1 
ATOM   2727  C  CA  . LYS   B 2 11  ? 33.456  60.217  -0.629  1.00 88.72  ? 11   LYS   B CA  1 
ATOM   2728  C  C   . LYS   B 2 11  ? 32.069  59.629  -0.891  1.00 88.39  ? 11   LYS   B C   1 
ATOM   2729  O  O   . LYS   B 2 11  ? 31.077  60.373  -0.912  1.00 89.58  ? 11   LYS   B O   1 
ATOM   2730  C  CB  . LYS   B 2 11  ? 33.913  59.945  0.808   1.00 89.09  ? 11   LYS   B CB  1 
ATOM   2731  N  N   . PRO   B 2 12  ? 31.941  58.321  -1.117  1.00 84.00  ? 12   PRO   B N   1 
ATOM   2732  C  CA  . PRO   B 2 12  ? 30.606  57.736  -1.259  1.00 83.76  ? 12   PRO   B CA  1 
ATOM   2733  C  C   . PRO   B 2 12  ? 29.771  58.008  -0.012  1.00 85.49  ? 12   PRO   B C   1 
ATOM   2734  O  O   . PRO   B 2 12  ? 30.291  58.028  1.108   1.00 90.08  ? 12   PRO   B O   1 
ATOM   2735  C  CB  . PRO   B 2 12  ? 30.890  56.243  -1.434  1.00 85.39  ? 12   PRO   B CB  1 
ATOM   2736  C  CG  . PRO   B 2 12  ? 32.329  56.150  -1.868  1.00 84.26  ? 12   PRO   B CG  1 
ATOM   2737  C  CD  . PRO   B 2 12  ? 33.013  57.316  -1.253  1.00 86.80  ? 12   PRO   B CD  1 
ATOM   2738  N  N   . THR   B 2 13  ? 28.466  58.226  -0.212  1.00 82.18  ? 13   THR   B N   1 
ATOM   2739  C  CA  . THR   B 2 13  ? 27.546  58.547  0.872   1.00 80.31  ? 13   THR   B CA  1 
ATOM   2740  C  C   . THR   B 2 13  ? 26.580  57.421  1.213   1.00 84.38  ? 13   THR   B C   1 
ATOM   2741  O  O   . THR   B 2 13  ? 25.843  57.534  2.204   1.00 86.51  ? 13   THR   B O   1 
ATOM   2742  C  CB  . THR   B 2 13  ? 26.733  59.785  0.513   1.00 80.06  ? 13   THR   B CB  1 
ATOM   2743  O  OG1 . THR   B 2 13  ? 25.710  59.403  -0.418  1.00 81.26  ? 13   THR   B OG1 1 
ATOM   2744  C  CG2 . THR   B 2 13  ? 27.638  60.824  -0.150  1.00 81.87  ? 13   THR   B CG2 1 
ATOM   2745  N  N   . ALA   B 2 14  ? 26.547  56.353  0.421   1.00 83.46  ? 14   ALA   B N   1 
ATOM   2746  C  CA  . ALA   B 2 14  ? 25.591  55.275  0.606   1.00 81.03  ? 14   ALA   B CA  1 
ATOM   2747  C  C   . ALA   B 2 14  ? 26.171  54.239  1.543   1.00 82.10  ? 14   ALA   B C   1 
ATOM   2748  O  O   . ALA   B 2 14  ? 27.375  53.986  1.530   1.00 84.32  ? 14   ALA   B O   1 
ATOM   2749  C  CB  . ALA   B 2 14  ? 25.238  54.627  -0.730  1.00 79.61  ? 14   ALA   B CB  1 
ATOM   2750  N  N   . VAL   B 2 15  ? 25.316  53.658  2.372   1.00 82.92  ? 15   VAL   B N   1 
ATOM   2751  C  CA  . VAL   B 2 15  ? 25.693  52.575  3.267   1.00 80.23  ? 15   VAL   B CA  1 
ATOM   2752  C  C   . VAL   B 2 15  ? 25.367  51.252  2.578   1.00 82.10  ? 15   VAL   B C   1 
ATOM   2753  O  O   . VAL   B 2 15  ? 24.281  51.091  2.001   1.00 82.88  ? 15   VAL   B O   1 
ATOM   2754  C  CB  . VAL   B 2 15  ? 24.960  52.705  4.611   1.00 81.52  ? 15   VAL   B CB  1 
ATOM   2755  C  CG1 . VAL   B 2 15  ? 25.464  51.681  5.602   1.00 83.81  ? 15   VAL   B CG1 1 
ATOM   2756  C  CG2 . VAL   B 2 15  ? 25.072  54.139  5.140   1.00 82.85  ? 15   VAL   B CG2 1 
ATOM   2757  N  N   . ASN   B 2 16  ? 26.314  50.319  2.587   1.00 83.58  ? 16   ASN   B N   1 
ATOM   2758  C  CA  . ASN   B 2 16  ? 26.078  49.010  1.991   1.00 82.63  ? 16   ASN   B CA  1 
ATOM   2759  C  C   . ASN   B 2 16  ? 26.430  47.905  2.974   1.00 86.48  ? 16   ASN   B C   1 
ATOM   2760  O  O   . ASN   B 2 16  ? 26.804  46.798  2.579   1.00 94.46  ? 16   ASN   B O   1 
ATOM   2761  C  CB  . ASN   B 2 16  ? 26.812  48.847  0.649   1.00 86.56  ? 16   ASN   B CB  1 
ATOM   2762  C  CG  . ASN   B 2 16  ? 28.334  48.673  0.782   1.00 87.92  ? 16   ASN   B CG  1 
ATOM   2763  O  OD1 . ASN   B 2 16  ? 29.036  49.555  1.274   1.00 89.16  ? 16   ASN   B OD1 1 
ATOM   2764  N  ND2 . ASN   B 2 16  ? 28.849  47.553  0.269   1.00 91.29  ? 16   ASN   B ND2 1 
ATOM   2765  N  N   . GLY   B 2 17  ? 26.292  48.190  4.266   1.00 87.75  ? 17   GLY   B N   1 
ATOM   2766  C  CA  . GLY   B 2 17  ? 26.403  47.154  5.272   1.00 90.74  ? 17   GLY   B CA  1 
ATOM   2767  C  C   . GLY   B 2 17  ? 26.696  47.697  6.651   1.00 89.74  ? 17   GLY   B C   1 
ATOM   2768  O  O   . GLY   B 2 17  ? 27.430  48.678  6.814   1.00 88.39  ? 17   GLY   B O   1 
ATOM   2769  N  N   . CYS   B 2 18  ? 26.149  47.038  7.662   1.00 91.67  ? 18   CYS   B N   1 
ATOM   2770  C  CA  . CYS   B 2 18  ? 26.262  47.550  9.015   1.00 91.02  ? 18   CYS   B CA  1 
ATOM   2771  C  C   . CYS   B 2 18  ? 26.294  46.401  10.015  1.00 90.31  ? 18   CYS   B C   1 
ATOM   2772  O  O   . CYS   B 2 18  ? 25.389  45.563  10.026  1.00 92.44  ? 18   CYS   B O   1 
ATOM   2773  C  CB  . CYS   B 2 18  ? 25.108  48.520  9.306   1.00 91.70  ? 18   CYS   B CB  1 
ATOM   2774  S  SG  . CYS   B 2 18  ? 23.425  47.982  8.861   1.00 106.01 ? 18   CYS   B SG  1 
ATOM   2775  N  N   . VAL   B 2 19  ? 27.327  46.389  10.862  1.00 89.76  ? 19   VAL   B N   1 
ATOM   2776  C  CA  . VAL   B 2 19  ? 27.549  45.346  11.859  1.00 91.71  ? 19   VAL   B CA  1 
ATOM   2777  C  C   . VAL   B 2 19  ? 27.715  45.985  13.244  1.00 93.96  ? 19   VAL   B C   1 
ATOM   2778  O  O   . VAL   B 2 19  ? 28.362  47.031  13.385  1.00 90.67  ? 19   VAL   B O   1 
ATOM   2779  C  CB  . VAL   B 2 19  ? 28.778  44.483  11.481  1.00 89.09  ? 19   VAL   B CB  1 
ATOM   2780  C  CG1 . VAL   B 2 19  ? 28.512  43.739  10.194  1.00 90.48  ? 19   VAL   B CG1 1 
ATOM   2781  C  CG2 . VAL   B 2 19  ? 30.022  45.334  11.328  1.00 88.57  ? 19   VAL   B CG2 1 
ATOM   2782  N  N   . THR   B 2 20  ? 27.091  45.380  14.260  1.00 95.77  ? 20   THR   B N   1 
ATOM   2783  C  CA  . THR   B 2 20  ? 27.257  45.781  15.652  1.00 93.80  ? 20   THR   B CA  1 
ATOM   2784  C  C   . THR   B 2 20  ? 28.045  44.705  16.381  1.00 101.68 ? 20   THR   B C   1 
ATOM   2785  O  O   . THR   B 2 20  ? 27.636  43.542  16.410  1.00 103.59 ? 20   THR   B O   1 
ATOM   2786  C  CB  . THR   B 2 20  ? 25.921  46.007  16.375  1.00 93.35  ? 20   THR   B CB  1 
ATOM   2787  O  OG1 . THR   B 2 20  ? 24.936  45.055  15.947  1.00 95.27  ? 20   THR   B OG1 1 
ATOM   2788  C  CG2 . THR   B 2 20  ? 25.427  47.397  16.150  1.00 94.24  ? 20   THR   B CG2 1 
ATOM   2789  N  N   . GLY   B 2 21  ? 29.148  45.101  16.983  1.00 112.24 ? 21   GLY   B N   1 
ATOM   2790  C  CA  . GLY   B 2 21  ? 29.938  44.194  17.790  1.00 114.16 ? 21   GLY   B CA  1 
ATOM   2791  C  C   . GLY   B 2 21  ? 30.876  44.918  18.708  1.00 111.97 ? 21   GLY   B C   1 
ATOM   2792  O  O   . GLY   B 2 21  ? 30.573  46.009  19.195  1.00 111.38 ? 21   GLY   B O   1 
ATOM   2793  N  N   . HIS   B 2 22  ? 32.040  44.320  18.912  1.00 103.11 ? 22   HIS   B N   1 
ATOM   2794  C  CA  . HIS   B 2 22  ? 32.990  44.765  19.903  1.00 101.16 ? 22   HIS   B CA  1 
ATOM   2795  C  C   . HIS   B 2 22  ? 34.389  44.807  19.290  1.00 99.53  ? 22   HIS   B C   1 
ATOM   2796  O  O   . HIS   B 2 22  ? 35.308  44.102  19.693  1.00 100.10 ? 22   HIS   B O   1 
ATOM   2797  C  CB  . HIS   B 2 22  ? 32.898  43.860  21.120  1.00 103.47 ? 22   HIS   B CB  1 
ATOM   2798  C  CG  . HIS   B 2 22  ? 31.496  43.656  21.599  1.00 101.61 ? 22   HIS   B CG  1 
ATOM   2799  N  ND1 . HIS   B 2 22  ? 30.734  44.682  22.112  1.00 103.45 ? 22   HIS   B ND1 1 
ATOM   2800  C  CD2 . HIS   B 2 22  ? 30.711  42.554  21.629  1.00 100.79 ? 22   HIS   B CD2 1 
ATOM   2801  C  CE1 . HIS   B 2 22  ? 29.549  44.216  22.458  1.00 103.40 ? 22   HIS   B CE1 1 
ATOM   2802  N  NE2 . HIS   B 2 22  ? 29.509  42.927  22.177  1.00 101.04 ? 22   HIS   B NE2 1 
ATOM   2803  N  N   . PHE   B 2 23  ? 34.537  45.678  18.299  1.00 99.66  ? 23   PHE   B N   1 
ATOM   2804  C  CA  . PHE   B 2 23  ? 35.782  45.770  17.550  1.00 98.38  ? 23   PHE   B CA  1 
ATOM   2805  C  C   . PHE   B 2 23  ? 36.869  46.438  18.377  1.00 101.22 ? 23   PHE   B C   1 
ATOM   2806  O  O   . PHE   B 2 23  ? 37.957  45.874  18.576  1.00 101.40 ? 23   PHE   B O   1 
ATOM   2807  C  CB  . PHE   B 2 23  ? 35.515  46.538  16.253  1.00 95.72  ? 23   PHE   B CB  1 
ATOM   2808  C  CG  . PHE   B 2 23  ? 36.646  46.534  15.282  1.00 93.12  ? 23   PHE   B CG  1 
ATOM   2809  C  CD1 . PHE   B 2 23  ? 37.219  45.349  14.857  1.00 96.48  ? 23   PHE   B CD1 1 
ATOM   2810  C  CD2 . PHE   B 2 23  ? 37.111  47.717  14.762  1.00 94.26  ? 23   PHE   B CD2 1 
ATOM   2811  C  CE1 . PHE   B 2 23  ? 38.258  45.353  13.939  1.00 95.46  ? 23   PHE   B CE1 1 
ATOM   2812  C  CE2 . PHE   B 2 23  ? 38.132  47.735  13.854  1.00 97.26  ? 23   PHE   B CE2 1 
ATOM   2813  C  CZ  . PHE   B 2 23  ? 38.715  46.548  13.436  1.00 98.69  ? 23   PHE   B CZ  1 
ATOM   2814  N  N   . THR   B 2 24  ? 36.569  47.635  18.899  1.00 106.84 ? 24   THR   B N   1 
ATOM   2815  C  CA  . THR   B 2 24  ? 37.543  48.554  19.484  1.00 109.78 ? 24   THR   B CA  1 
ATOM   2816  C  C   . THR   B 2 24  ? 38.023  48.076  20.856  1.00 112.62 ? 24   THR   B C   1 
ATOM   2817  O  O   . THR   B 2 24  ? 39.205  47.776  21.034  1.00 114.81 ? 24   THR   B O   1 
ATOM   2818  C  CB  . THR   B 2 24  ? 36.948  49.975  19.568  1.00 106.65 ? 24   THR   B CB  1 
ATOM   2819  O  OG1 . THR   B 2 24  ? 35.840  50.002  20.476  1.00 111.63 ? 24   THR   B OG1 1 
ATOM   2820  C  CG2 . THR   B 2 24  ? 36.472  50.463  18.202  1.00 98.19  ? 24   THR   B CG2 1 
ATOM   2821  N  N   . SER   B 2 25  ? 37.131  48.019  21.843  1.00 121.01 ? 25   SER   B N   1 
ATOM   2822  C  CA  . SER   B 2 25  ? 37.415  47.324  23.093  1.00 123.90 ? 25   SER   B CA  1 
ATOM   2823  C  C   . SER   B 2 25  ? 36.319  46.301  23.350  1.00 123.70 ? 25   SER   B C   1 
ATOM   2824  O  O   . SER   B 2 25  ? 35.212  46.404  22.818  1.00 126.02 ? 25   SER   B O   1 
ATOM   2825  C  CB  . SER   B 2 25  ? 37.515  48.281  24.293  1.00 125.64 ? 25   SER   B CB  1 
ATOM   2826  O  OG  . SER   B 2 25  ? 36.303  48.311  25.040  1.00 127.95 ? 25   SER   B OG  1 
ATOM   2827  N  N   . ALA   B 2 26  ? 36.618  45.311  24.191  1.00 121.15 ? 26   ALA   B N   1 
ATOM   2828  C  CA  . ALA   B 2 26  ? 35.596  44.301  24.427  1.00 117.35 ? 26   ALA   B CA  1 
ATOM   2829  C  C   . ALA   B 2 26  ? 34.415  44.848  25.211  1.00 122.35 ? 26   ALA   B C   1 
ATOM   2830  O  O   . ALA   B 2 26  ? 33.402  44.152  25.324  1.00 119.51 ? 26   ALA   B O   1 
ATOM   2831  C  CB  . ALA   B 2 26  ? 36.200  43.100  25.147  1.00 118.51 ? 26   ALA   B CB  1 
ATOM   2832  N  N   . GLU   B 2 27  ? 34.506  46.089  25.693  1.00 132.21 ? 27   GLU   B N   1 
ATOM   2833  C  CA  . GLU   B 2 27  ? 33.577  46.653  26.662  1.00 134.76 ? 27   GLU   B CA  1 
ATOM   2834  C  C   . GLU   B 2 27  ? 32.564  47.619  26.068  1.00 134.28 ? 27   GLU   B C   1 
ATOM   2835  O  O   . GLU   B 2 27  ? 31.632  48.018  26.770  1.00 135.41 ? 27   GLU   B O   1 
ATOM   2836  C  CB  . GLU   B 2 27  ? 34.362  47.369  27.766  1.00 136.39 ? 27   GLU   B CB  1 
ATOM   2837  C  CG  . GLU   B 2 27  ? 35.432  46.498  28.402  1.00 141.91 ? 27   GLU   B CG  1 
ATOM   2838  C  CD  . GLU   B 2 27  ? 36.245  47.255  29.438  1.00 153.38 ? 27   GLU   B CD  1 
ATOM   2839  O  OE1 . GLU   B 2 27  ? 36.186  48.510  29.445  1.00 153.96 ? 27   GLU   B OE1 1 
ATOM   2840  O  OE2 . GLU   B 2 27  ? 36.937  46.596  30.248  1.00 159.28 ? 27   GLU   B OE2 1 
ATOM   2841  N  N   . ASP   B 2 28  ? 32.718  48.018  24.813  1.00 124.14 ? 28   ASP   B N   1 
ATOM   2842  C  CA  . ASP   B 2 28  ? 31.797  48.961  24.196  1.00 122.80 ? 28   ASP   B CA  1 
ATOM   2843  C  C   . ASP   B 2 28  ? 31.212  48.358  22.923  1.00 111.69 ? 28   ASP   B C   1 
ATOM   2844  O  O   . ASP   B 2 28  ? 31.883  47.614  22.200  1.00 112.19 ? 28   ASP   B O   1 
ATOM   2845  C  CB  . ASP   B 2 28  ? 32.491  50.324  23.901  1.00 117.35 ? 28   ASP   B CB  1 
ATOM   2846  C  CG  . ASP   B 2 28  ? 33.900  50.167  23.312  1.00 114.33 ? 28   ASP   B CG  1 
ATOM   2847  O  OD1 . ASP   B 2 28  ? 34.376  49.024  23.159  1.00 118.59 ? 28   ASP   B OD1 1 
ATOM   2848  O  OD2 . ASP   B 2 28  ? 34.539  51.189  22.999  1.00 110.02 ? 28   ASP   B OD2 1 
ATOM   2849  N  N   . LEU   B 2 29  ? 29.952  48.671  22.665  1.00 108.20 ? 29   LEU   B N   1 
ATOM   2850  C  CA  . LEU   B 2 29  ? 29.289  48.226  21.451  1.00 103.42 ? 29   LEU   B CA  1 
ATOM   2851  C  C   . LEU   B 2 29  ? 29.662  49.158  20.301  1.00 104.08 ? 29   LEU   B C   1 
ATOM   2852  O  O   . LEU   B 2 29  ? 29.339  50.355  20.321  1.00 103.33 ? 29   LEU   B O   1 
ATOM   2853  C  CB  . LEU   B 2 29  ? 27.781  48.185  21.673  1.00 99.47  ? 29   LEU   B CB  1 
ATOM   2854  C  CG  . LEU   B 2 29  ? 26.869  47.960  20.477  1.00 97.53  ? 29   LEU   B CG  1 
ATOM   2855  C  CD1 . LEU   B 2 29  ? 27.193  46.650  19.745  1.00 100.80 ? 29   LEU   B CD1 1 
ATOM   2856  C  CD2 . LEU   B 2 29  ? 25.425  48.008  20.945  1.00 100.31 ? 29   LEU   B CD2 1 
ATOM   2857  N  N   . ASN   B 2 30  ? 30.348  48.617  19.305  1.00 101.88 ? 30   ASN   B N   1 
ATOM   2858  C  CA  . ASN   B 2 30  ? 30.619  49.376  18.099  1.00 99.45  ? 30   ASN   B CA  1 
ATOM   2859  C  C   . ASN   B 2 30  ? 29.518  49.153  17.072  1.00 97.88  ? 30   ASN   B C   1 
ATOM   2860  O  O   . ASN   B 2 30  ? 28.836  48.121  17.070  1.00 97.30  ? 30   ASN   B O   1 
ATOM   2861  C  CB  . ASN   B 2 30  ? 31.961  48.978  17.498  1.00 97.06  ? 30   ASN   B CB  1 
ATOM   2862  C  CG  . ASN   B 2 30  ? 33.069  49.027  18.498  1.00 97.62  ? 30   ASN   B CG  1 
ATOM   2863  O  OD1 . ASN   B 2 30  ? 33.729  48.022  18.738  1.00 100.03 ? 30   ASN   B OD1 1 
ATOM   2864  N  ND2 . ASN   B 2 30  ? 33.274  50.196  19.111  1.00 98.74  ? 30   ASN   B ND2 1 
ATOM   2865  N  N   . LEU   B 2 31  ? 29.332  50.153  16.217  1.00 92.89  ? 31   LEU   B N   1 
ATOM   2866  C  CA  . LEU   B 2 31  ? 28.619  50.007  14.956  1.00 88.30  ? 31   LEU   B CA  1 
ATOM   2867  C  C   . LEU   B 2 31  ? 29.623  50.309  13.858  1.00 90.66  ? 31   LEU   B C   1 
ATOM   2868  O  O   . LEU   B 2 31  ? 30.160  51.422  13.803  1.00 94.33  ? 31   LEU   B O   1 
ATOM   2869  C  CB  . LEU   B 2 31  ? 27.422  50.957  14.872  1.00 86.94  ? 31   LEU   B CB  1 
ATOM   2870  C  CG  . LEU   B 2 31  ? 26.830  51.197  13.477  1.00 84.43  ? 31   LEU   B CG  1 
ATOM   2871  C  CD1 . LEU   B 2 31  ? 26.295  49.928  12.836  1.00 87.06  ? 31   LEU   B CD1 1 
ATOM   2872  C  CD2 . LEU   B 2 31  ? 25.750  52.248  13.543  1.00 85.27  ? 31   LEU   B CD2 1 
ATOM   2873  N  N   . LEU   B 2 32  ? 29.914  49.318  13.024  1.00 87.62  ? 32   LEU   B N   1 
ATOM   2874  C  CA  . LEU   B 2 32  ? 30.759  49.538  11.861  1.00 85.83  ? 32   LEU   B CA  1 
ATOM   2875  C  C   . LEU   B 2 32  ? 29.869  49.646  10.638  1.00 86.70  ? 32   LEU   B C   1 
ATOM   2876  O  O   . LEU   B 2 32  ? 28.943  48.850  10.468  1.00 86.57  ? 32   LEU   B O   1 
ATOM   2877  C  CB  . LEU   B 2 32  ? 31.772  48.417  11.654  1.00 85.89  ? 32   LEU   B CB  1 
ATOM   2878  C  CG  . LEU   B 2 32  ? 32.968  48.300  12.590  1.00 88.50  ? 32   LEU   B CG  1 
ATOM   2879  C  CD1 . LEU   B 2 32  ? 32.532  47.885  13.975  1.00 89.06  ? 32   LEU   B CD1 1 
ATOM   2880  C  CD2 . LEU   B 2 32  ? 33.935  47.273  12.031  1.00 88.34  ? 32   LEU   B CD2 1 
ATOM   2881  N  N   . ILE   B 2 33  ? 30.160  50.631  9.787   1.00 88.38  ? 33   ILE   B N   1 
ATOM   2882  C  CA  . ILE   B 2 33  ? 29.376  50.916  8.591   1.00 86.61  ? 33   ILE   B CA  1 
ATOM   2883  C  C   . ILE   B 2 33  ? 30.297  50.856  7.375   1.00 85.88  ? 33   ILE   B C   1 
ATOM   2884  O  O   . ILE   B 2 33  ? 31.459  51.277  7.441   1.00 84.55  ? 33   ILE   B O   1 
ATOM   2885  C  CB  . ILE   B 2 33  ? 28.676  52.289  8.710   1.00 84.12  ? 33   ILE   B CB  1 
ATOM   2886  C  CG1 . ILE   B 2 33  ? 27.353  52.158  9.438   1.00 81.68  ? 33   ILE   B CG1 1 
ATOM   2887  C  CG2 . ILE   B 2 33  ? 28.403  52.910  7.378   1.00 86.79  ? 33   ILE   B CG2 1 
ATOM   2888  C  CD1 . ILE   B 2 33  ? 26.864  53.485  9.923   1.00 85.38  ? 33   ILE   B CD1 1 
ATOM   2889  N  N   . ALA   B 2 34  ? 29.778  50.309  6.270   1.00 83.89  ? 34   ALA   B N   1 
ATOM   2890  C  CA  . ALA   B 2 34  ? 30.502  50.170  5.012   1.00 83.80  ? 34   ALA   B CA  1 
ATOM   2891  C  C   . ALA   B 2 34  ? 29.840  51.004  3.915   1.00 83.86  ? 34   ALA   B C   1 
ATOM   2892  O  O   . ALA   B 2 34  ? 28.638  50.864  3.653   1.00 82.13  ? 34   ALA   B O   1 
ATOM   2893  C  CB  . ALA   B 2 34  ? 30.572  48.697  4.596   1.00 84.63  ? 34   ALA   B CB  1 
ATOM   2894  N  N   . LYS   B 2 35  ? 30.643  51.878  3.277   1.00 85.11  ? 35   LYS   B N   1 
ATOM   2895  C  CA  . LYS   B 2 35  ? 30.238  52.763  2.178   1.00 83.16  ? 35   LYS   B CA  1 
ATOM   2896  C  C   . LYS   B 2 35  ? 31.212  52.565  1.002   1.00 81.51  ? 35   LYS   B C   1 
ATOM   2897  O  O   . LYS   B 2 35  ? 32.091  53.400  0.765   1.00 82.07  ? 35   LYS   B O   1 
ATOM   2898  C  CB  . LYS   B 2 35  ? 30.204  54.230  2.649   1.00 83.57  ? 35   LYS   B CB  1 
ATOM   2899  C  CG  . LYS   B 2 35  ? 29.373  54.468  3.894   1.00 80.68  ? 35   LYS   B CG  1 
ATOM   2900  C  CD  . LYS   B 2 35  ? 29.129  55.928  4.142   1.00 82.68  ? 35   LYS   B CD  1 
ATOM   2901  C  CE  . LYS   B 2 35  ? 28.540  56.106  5.522   1.00 91.71  ? 35   LYS   B CE  1 
ATOM   2902  N  NZ  . LYS   B 2 35  ? 28.121  57.490  5.912   1.00 94.61  ? 35   LYS   B NZ  1 
ATOM   2903  N  N   . ASN   B 2 36  ? 31.043  51.453  0.275   1.00 81.70  ? 36   ASN   B N   1 
ATOM   2904  C  CA  . ASN   B 2 36  ? 31.872  51.061  -0.868  1.00 82.29  ? 36   ASN   B CA  1 
ATOM   2905  C  C   . ASN   B 2 36  ? 33.240  50.983  -0.198  1.00 84.11  ? 36   ASN   B C   1 
ATOM   2906  O  O   . ASN   B 2 36  ? 33.460  50.139  0.683   1.00 85.53  ? 36   ASN   B O   1 
ATOM   2907  C  CB  . ASN   B 2 36  ? 31.770  52.102  -1.994  1.00 83.51  ? 36   ASN   B CB  1 
ATOM   2908  C  CG  . ASN   B 2 36  ? 32.186  51.548  -3.358  1.00 84.20  ? 36   ASN   B CG  1 
ATOM   2909  O  OD1 . ASN   B 2 36  ? 31.945  50.392  -3.670  1.00 90.14  ? 36   ASN   B OD1 1 
ATOM   2910  N  ND2 . ASN   B 2 36  ? 32.795  52.390  -4.178  1.00 84.80  ? 36   ASN   B ND2 1 
ATOM   2911  N  N   . THR   B 2 37  ? 34.159  51.862  -0.608  1.00 83.60  ? 37   THR   B N   1 
ATOM   2912  C  CA  . THR   B 2 37  ? 35.520  51.919  -0.077  1.00 81.10  ? 37   THR   B CA  1 
ATOM   2913  C  C   . THR   B 2 37  ? 35.783  52.682  1.208   1.00 83.86  ? 37   THR   B C   1 
ATOM   2914  O  O   . THR   B 2 37  ? 36.747  53.450  1.284   1.00 89.90  ? 37   THR   B O   1 
ATOM   2915  C  CB  . THR   B 2 37  ? 36.336  52.585  -1.166  1.00 84.14  ? 37   THR   B CB  1 
ATOM   2916  O  OG1 . THR   B 2 37  ? 35.811  53.901  -1.358  1.00 89.23  ? 37   THR   B OG1 1 
ATOM   2917  C  CG2 . THR   B 2 37  ? 36.244  51.798  -2.444  1.00 88.29  ? 37   THR   B CG2 1 
ATOM   2918  N  N   . ARG   B 2 38  ? 34.917  52.494  2.200   1.00 87.49  ? 38   ARG   B N   1 
ATOM   2919  C  CA  . ARG   B 2 38  ? 34.905  53.330  3.403   1.00 89.81  ? 38   ARG   B CA  1 
ATOM   2920  C  C   . ARG   B 2 38  ? 34.314  52.552  4.578   1.00 86.34  ? 38   ARG   B C   1 
ATOM   2921  O  O   . ARG   B 2 38  ? 33.132  52.186  4.567   1.00 80.90  ? 38   ARG   B O   1 
ATOM   2922  C  CB  . ARG   B 2 38  ? 34.123  54.637  3.151   1.00 85.96  ? 38   ARG   B CB  1 
ATOM   2923  C  CG  . ARG   B 2 38  ? 34.957  55.747  2.502   1.00 89.43  ? 38   ARG   B CG  1 
ATOM   2924  C  CD  . ARG   B 2 38  ? 36.211  56.071  3.326   1.00 94.12  ? 38   ARG   B CD  1 
ATOM   2925  N  NE  . ARG   B 2 38  ? 37.366  56.443  2.511   1.00 96.63  ? 38   ARG   B NE  1 
ATOM   2926  C  CZ  . ARG   B 2 38  ? 38.509  56.922  2.992   1.00 100.68 ? 38   ARG   B CZ  1 
ATOM   2927  N  NH1 . ARG   B 2 38  ? 38.685  57.133  4.290   1.00 97.98  ? 38   ARG   B NH1 1 
ATOM   2928  N  NH2 . ARG   B 2 38  ? 39.502  57.201  2.150   1.00 108.14 ? 38   ARG   B NH2 1 
ATOM   2929  N  N   . LEU   B 2 39  ? 35.136  52.298  5.588   1.00 87.59  ? 39   LEU   B N   1 
ATOM   2930  C  CA  . LEU   B 2 39  ? 34.711  51.634  6.806   1.00 86.31  ? 39   LEU   B CA  1 
ATOM   2931  C  C   . LEU   B 2 39  ? 34.663  52.681  7.900   1.00 89.39  ? 39   LEU   B C   1 
ATOM   2932  O  O   . LEU   B 2 39  ? 35.657  53.367  8.135   1.00 91.81  ? 39   LEU   B O   1 
ATOM   2933  C  CB  . LEU   B 2 39  ? 35.680  50.512  7.153   1.00 90.18  ? 39   LEU   B CB  1 
ATOM   2934  C  CG  . LEU   B 2 39  ? 35.510  49.785  8.479   1.00 91.63  ? 39   LEU   B CG  1 
ATOM   2935  C  CD1 . LEU   B 2 39  ? 34.157  49.082  8.617   1.00 89.51  ? 39   LEU   B CD1 1 
ATOM   2936  C  CD2 . LEU   B 2 39  ? 36.646  48.808  8.640   1.00 87.34  ? 39   LEU   B CD2 1 
ATOM   2937  N  N   . GLU   B 2 40  ? 33.496  52.849  8.515   1.00 97.75  ? 40   GLU   B N   1 
ATOM   2938  C  CA  . GLU   B 2 40  ? 33.293  53.828  9.580   1.00 99.87  ? 40   GLU   B CA  1 
ATOM   2939  C  C   . GLU   B 2 40  ? 33.103  53.080  10.893  1.00 98.88  ? 40   GLU   B C   1 
ATOM   2940  O  O   . GLU   B 2 40  ? 32.326  52.115  10.960  1.00 97.77  ? 40   GLU   B O   1 
ATOM   2941  C  CB  . GLU   B 2 40  ? 32.088  54.731  9.293   1.00 98.69  ? 40   GLU   B CB  1 
ATOM   2942  C  CG  . GLU   B 2 40  ? 31.871  54.953  7.821   1.00 100.02 ? 40   GLU   B CG  1 
ATOM   2943  C  CD  . GLU   B 2 40  ? 31.234  56.285  7.505   1.00 103.89 ? 40   GLU   B CD  1 
ATOM   2944  O  OE1 . GLU   B 2 40  ? 30.216  56.629  8.144   1.00 105.47 ? 40   GLU   B OE1 1 
ATOM   2945  O  OE2 . GLU   B 2 40  ? 31.763  57.005  6.628   1.00 106.84 ? 40   GLU   B OE2 1 
ATOM   2946  N  N   . ILE   B 2 41  ? 33.828  53.503  11.925  1.00 96.59  ? 41   ILE   B N   1 
ATOM   2947  C  CA  . ILE   B 2 41  ? 33.838  52.807  13.200  1.00 95.28  ? 41   ILE   B CA  1 
ATOM   2948  C  C   . ILE   B 2 41  ? 33.335  53.763  14.261  1.00 91.19  ? 41   ILE   B C   1 
ATOM   2949  O  O   . ILE   B 2 41  ? 33.916  54.834  14.471  1.00 90.19  ? 41   ILE   B O   1 
ATOM   2950  C  CB  . ILE   B 2 41  ? 35.228  52.261  13.541  1.00 93.99  ? 41   ILE   B CB  1 
ATOM   2951  C  CG1 . ILE   B 2 41  ? 35.752  51.443  12.362  1.00 88.59  ? 41   ILE   B CG1 1 
ATOM   2952  C  CG2 . ILE   B 2 41  ? 35.138  51.389  14.763  1.00 95.88  ? 41   ILE   B CG2 1 
ATOM   2953  C  CD1 . ILE   B 2 41  ? 37.237  51.194  12.376  1.00 91.90  ? 41   ILE   B CD1 1 
ATOM   2954  N  N   . TYR   B 2 42  ? 32.239  53.383  14.905  1.00 88.15  ? 42   TYR   B N   1 
ATOM   2955  C  CA  . TYR   B 2 42  ? 31.542  54.198  15.883  1.00 93.08  ? 42   TYR   B CA  1 
ATOM   2956  C  C   . TYR   B 2 42  ? 31.499  53.460  17.210  1.00 97.36  ? 42   TYR   B C   1 
ATOM   2957  O  O   . TYR   B 2 42  ? 31.786  52.262  17.301  1.00 95.28  ? 42   TYR   B O   1 
ATOM   2958  C  CB  . TYR   B 2 42  ? 30.112  54.540  15.421  1.00 95.22  ? 42   TYR   B CB  1 
ATOM   2959  C  CG  . TYR   B 2 42  ? 30.082  55.565  14.314  1.00 95.79  ? 42   TYR   B CG  1 
ATOM   2960  C  CD1 . TYR   B 2 42  ? 30.191  55.174  12.982  1.00 97.27  ? 42   TYR   B CD1 1 
ATOM   2961  C  CD2 . TYR   B 2 42  ? 30.001  56.925  14.594  1.00 93.67  ? 42   TYR   B CD2 1 
ATOM   2962  C  CE1 . TYR   B 2 42  ? 30.204  56.108  11.963  1.00 96.60  ? 42   TYR   B CE1 1 
ATOM   2963  C  CE2 . TYR   B 2 42  ? 30.014  57.861  13.574  1.00 91.52  ? 42   TYR   B CE2 1 
ATOM   2964  C  CZ  . TYR   B 2 42  ? 30.117  57.449  12.270  1.00 92.58  ? 42   TYR   B CZ  1 
ATOM   2965  O  OH  . TYR   B 2 42  ? 30.135  58.386  11.274  1.00 96.04  ? 42   TYR   B OH  1 
ATOM   2966  N  N   . VAL   B 2 43  ? 31.143  54.214  18.247  1.00 101.17 ? 43   VAL   B N   1 
ATOM   2967  C  CA  . VAL   B 2 43  ? 30.809  53.672  19.554  1.00 101.90 ? 43   VAL   B CA  1 
ATOM   2968  C  C   . VAL   B 2 43  ? 29.386  54.097  19.880  1.00 101.16 ? 43   VAL   B C   1 
ATOM   2969  O  O   . VAL   B 2 43  ? 29.027  55.269  19.729  1.00 99.89  ? 43   VAL   B O   1 
ATOM   2970  C  CB  . VAL   B 2 43  ? 31.801  54.135  20.637  1.00 98.64  ? 43   VAL   B CB  1 
ATOM   2971  C  CG1 . VAL   B 2 43  ? 31.314  53.699  22.023  1.00 99.87  ? 43   VAL   B CG1 1 
ATOM   2972  C  CG2 . VAL   B 2 43  ? 33.165  53.564  20.333  1.00 98.25  ? 43   VAL   B CG2 1 
ATOM   2973  N  N   . VAL   B 2 44  ? 28.575  53.130  20.300  1.00 99.99  ? 44   VAL   B N   1 
ATOM   2974  C  CA  . VAL   B 2 44  ? 27.172  53.362  20.623  1.00 104.04 ? 44   VAL   B CA  1 
ATOM   2975  C  C   . VAL   B 2 44  ? 27.082  53.977  22.022  1.00 112.65 ? 44   VAL   B C   1 
ATOM   2976  O  O   . VAL   B 2 44  ? 27.147  53.250  23.029  1.00 116.33 ? 44   VAL   B O   1 
ATOM   2977  C  CB  . VAL   B 2 44  ? 26.361  52.080  20.513  1.00 101.59 ? 44   VAL   B CB  1 
ATOM   2978  C  CG1 . VAL   B 2 44  ? 24.903  52.371  20.714  1.00 108.28 ? 44   VAL   B CG1 1 
ATOM   2979  C  CG2 . VAL   B 2 44  ? 26.593  51.423  19.183  1.00 98.20  ? 44   VAL   B CG2 1 
ATOM   2980  N  N   . THR   B 2 45  ? 26.891  55.290  22.105  1.00 117.12 ? 45   THR   B N   1 
ATOM   2981  C  CA  . THR   B 2 45  ? 26.671  55.990  23.364  1.00 120.42 ? 45   THR   B CA  1 
ATOM   2982  C  C   . THR   B 2 45  ? 25.175  56.097  23.643  1.00 130.04 ? 45   THR   B C   1 
ATOM   2983  O  O   . THR   B 2 45  ? 24.352  56.109  22.727  1.00 131.79 ? 45   THR   B O   1 
ATOM   2984  C  CB  . THR   B 2 45  ? 27.303  57.384  23.348  1.00 120.90 ? 45   THR   B CB  1 
ATOM   2985  O  OG1 . THR   B 2 45  ? 26.409  58.330  22.737  1.00 125.62 ? 45   THR   B OG1 1 
ATOM   2986  C  CG2 . THR   B 2 45  ? 28.630  57.359  22.582  1.00 111.18 ? 45   THR   B CG2 1 
ATOM   2987  N  N   . ALA   B 2 46  ? 24.832  56.165  24.938  1.00 142.71 ? 46   ALA   B N   1 
ATOM   2988  C  CA  . ALA   B 2 46  ? 23.435  56.272  25.355  1.00 143.09 ? 46   ALA   B CA  1 
ATOM   2989  C  C   . ALA   B 2 46  ? 22.757  57.469  24.700  1.00 142.49 ? 46   ALA   B C   1 
ATOM   2990  O  O   . ALA   B 2 46  ? 21.550  57.447  24.441  1.00 146.65 ? 46   ALA   B O   1 
ATOM   2991  C  CB  . ALA   B 2 46  ? 23.341  56.374  26.879  1.00 141.14 ? 46   ALA   B CB  1 
ATOM   2992  N  N   . GLU   B 2 47  ? 23.532  58.521  24.429  1.00 135.53 ? 47   GLU   B N   1 
ATOM   2993  C  CA  . GLU   B 2 47  ? 23.015  59.650  23.667  1.00 138.25 ? 47   GLU   B CA  1 
ATOM   2994  C  C   . GLU   B 2 47  ? 22.850  59.284  22.200  1.00 138.69 ? 47   GLU   B C   1 
ATOM   2995  O  O   . GLU   B 2 47  ? 21.736  59.323  21.667  1.00 142.59 ? 47   GLU   B O   1 
ATOM   2996  C  CB  . GLU   B 2 47  ? 23.929  60.866  23.832  1.00 141.86 ? 47   GLU   B CB  1 
ATOM   2997  N  N   . GLY   B 2 48  ? 23.954  58.900  21.528  1.00 138.92 ? 48   GLY   B N   1 
ATOM   2998  C  CA  . GLY   B 2 48  ? 23.910  58.551  20.108  1.00 135.14 ? 48   GLY   B CA  1 
ATOM   2999  C  C   . GLY   B 2 48  ? 25.038  57.692  19.536  1.00 125.59 ? 48   GLY   B C   1 
ATOM   3000  O  O   . GLY   B 2 48  ? 25.061  56.480  19.760  1.00 127.29 ? 48   GLY   B O   1 
ATOM   3001  N  N   . LEU   B 2 49  ? 25.951  58.299  18.769  1.00 112.73 ? 49   LEU   B N   1 
ATOM   3002  C  CA  . LEU   B 2 49  ? 27.098  57.611  18.185  1.00 104.97 ? 49   LEU   B CA  1 
ATOM   3003  C  C   . LEU   B 2 49  ? 28.335  58.485  18.327  1.00 101.15 ? 49   LEU   B C   1 
ATOM   3004  O  O   . LEU   B 2 49  ? 28.272  59.697  18.090  1.00 101.48 ? 49   LEU   B O   1 
ATOM   3005  C  CB  . LEU   B 2 49  ? 26.873  57.285  16.694  1.00 104.81 ? 49   LEU   B CB  1 
ATOM   3006  C  CG  . LEU   B 2 49  ? 26.089  56.037  16.266  1.00 100.18 ? 49   LEU   B CG  1 
ATOM   3007  C  CD1 . LEU   B 2 49  ? 26.072  55.881  14.774  1.00 91.28  ? 49   LEU   B CD1 1 
ATOM   3008  C  CD2 . LEU   B 2 49  ? 26.693  54.810  16.866  1.00 104.05 ? 49   LEU   B CD2 1 
ATOM   3009  N  N   . ARG   B 2 50  ? 29.456  57.875  18.716  1.00 98.36  ? 50   ARG   B N   1 
ATOM   3010  C  CA  . ARG   B 2 50  ? 30.723  58.589  18.797  1.00 95.50  ? 50   ARG   B CA  1 
ATOM   3011  C  C   . ARG   B 2 50  ? 31.644  58.148  17.672  1.00 93.23  ? 50   ARG   B C   1 
ATOM   3012  O  O   . ARG   B 2 50  ? 32.003  56.965  17.597  1.00 94.95  ? 50   ARG   B O   1 
ATOM   3013  C  CB  . ARG   B 2 50  ? 31.397  58.367  20.151  1.00 99.40  ? 50   ARG   B CB  1 
ATOM   3014  C  CG  . ARG   B 2 50  ? 32.909  58.672  20.159  1.00 99.58  ? 50   ARG   B CG  1 
ATOM   3015  C  CD  . ARG   B 2 50  ? 33.496  58.962  21.564  1.00 101.73 ? 50   ARG   B CD  1 
ATOM   3016  N  NE  . ARG   B 2 50  ? 33.093  58.008  22.597  1.00 104.25 ? 50   ARG   B NE  1 
ATOM   3017  C  CZ  . ARG   B 2 50  ? 33.641  56.812  22.782  1.00 106.81 ? 50   ARG   B CZ  1 
ATOM   3018  N  NH1 . ARG   B 2 50  ? 34.626  56.374  22.009  1.00 106.47 ? 50   ARG   B NH1 1 
ATOM   3019  N  NH2 . ARG   B 2 50  ? 33.189  56.034  23.763  1.00 106.67 ? 50   ARG   B NH2 1 
ATOM   3020  N  N   . PRO   B 2 51  ? 32.029  59.055  16.779  1.00 89.70  ? 51   PRO   B N   1 
ATOM   3021  C  CA  . PRO   B 2 51  ? 32.951  58.694  15.694  1.00 91.94  ? 51   PRO   B CA  1 
ATOM   3022  C  C   . PRO   B 2 51  ? 34.324  58.323  16.224  1.00 94.90  ? 51   PRO   B C   1 
ATOM   3023  O  O   . PRO   B 2 51  ? 34.890  59.029  17.059  1.00 101.57 ? 51   PRO   B O   1 
ATOM   3024  C  CB  . PRO   B 2 51  ? 33.023  59.976  14.856  1.00 94.47  ? 51   PRO   B CB  1 
ATOM   3025  C  CG  . PRO   B 2 51  ? 31.778  60.721  15.177  1.00 93.74  ? 51   PRO   B CG  1 
ATOM   3026  C  CD  . PRO   B 2 51  ? 31.466  60.401  16.606  1.00 93.08  ? 51   PRO   B CD  1 
ATOM   3027  N  N   . VAL   B 2 52  ? 34.881  57.227  15.709  1.00 96.28  ? 52   VAL   B N   1 
ATOM   3028  C  CA  . VAL   B 2 52  ? 36.149  56.727  16.237  1.00 97.04  ? 52   VAL   B CA  1 
ATOM   3029  C  C   . VAL   B 2 52  ? 37.262  56.820  15.200  1.00 96.68  ? 52   VAL   B C   1 
ATOM   3030  O  O   . VAL   B 2 52  ? 38.278  57.490  15.431  1.00 92.18  ? 52   VAL   B O   1 
ATOM   3031  C  CB  . VAL   B 2 52  ? 36.015  55.280  16.752  1.00 96.81  ? 52   VAL   B CB  1 
ATOM   3032  C  CG1 . VAL   B 2 52  ? 37.332  54.818  17.338  1.00 97.72  ? 52   VAL   B CG1 1 
ATOM   3033  C  CG2 . VAL   B 2 52  ? 34.889  55.169  17.779  1.00 92.92  ? 52   VAL   B CG2 1 
ATOM   3034  N  N   . LYS   B 2 53  ? 37.090  56.111  14.076  1.00 98.42  ? 53   LYS   B N   1 
ATOM   3035  C  CA  . LYS   B 2 53  ? 38.043  56.074  12.969  1.00 97.63  ? 53   LYS   B CA  1 
ATOM   3036  C  C   . LYS   B 2 53  ? 37.315  55.590  11.721  1.00 96.92  ? 53   LYS   B C   1 
ATOM   3037  O  O   . LYS   B 2 53  ? 36.519  54.646  11.799  1.00 96.17  ? 53   LYS   B O   1 
ATOM   3038  C  CB  . LYS   B 2 53  ? 39.238  55.151  13.262  1.00 97.58  ? 53   LYS   B CB  1 
ATOM   3039  C  CG  . LYS   B 2 53  ? 40.526  55.580  12.565  1.00 99.59  ? 53   LYS   B CG  1 
ATOM   3040  C  CD  . LYS   B 2 53  ? 41.423  54.394  12.260  1.00 112.54 ? 53   LYS   B CD  1 
ATOM   3041  C  CE  . LYS   B 2 53  ? 42.874  54.819  12.097  1.00 122.87 ? 53   LYS   B CE  1 
ATOM   3042  N  NZ  . LYS   B 2 53  ? 43.064  55.814  11.011  1.00 118.94 ? 53   LYS   B NZ  1 
ATOM   3043  N  N   . GLU   B 2 54  ? 37.584  56.244  10.580  1.00 98.56  ? 54   GLU   B N   1 
ATOM   3044  C  CA  . GLU   B 2 54  ? 37.084  55.798  9.279   1.00 98.57  ? 54   GLU   B CA  1 
ATOM   3045  C  C   . GLU   B 2 54  ? 38.252  55.676  8.308   1.00 96.55  ? 54   GLU   B C   1 
ATOM   3046  O  O   . GLU   B 2 54  ? 39.087  56.578  8.202   1.00 94.70  ? 54   GLU   B O   1 
ATOM   3047  C  CB  . GLU   B 2 54  ? 35.977  56.721  8.718   1.00 98.30  ? 54   GLU   B CB  1 
ATOM   3048  C  CG  . GLU   B 2 54  ? 36.396  58.121  8.289   1.00 105.13 ? 54   GLU   B CG  1 
ATOM   3049  C  CD  . GLU   B 2 54  ? 36.672  58.199  6.810   1.00 102.69 ? 54   GLU   B CD  1 
ATOM   3050  O  OE1 . GLU   B 2 54  ? 36.332  57.227  6.113   1.00 97.83  ? 54   GLU   B OE1 1 
ATOM   3051  O  OE2 . GLU   B 2 54  ? 37.228  59.222  6.348   1.00 110.49 ? 54   GLU   B OE2 1 
ATOM   3052  N  N   . VAL   B 2 55  ? 38.315  54.541  7.612   1.00 99.47  ? 55   VAL   B N   1 
ATOM   3053  C  CA  . VAL   B 2 55  ? 39.494  54.146  6.856   1.00 99.67  ? 55   VAL   B CA  1 
ATOM   3054  C  C   . VAL   B 2 55  ? 39.083  53.750  5.443   1.00 99.34  ? 55   VAL   B C   1 
ATOM   3055  O  O   . VAL   B 2 55  ? 37.946  53.358  5.183   1.00 99.00  ? 55   VAL   B O   1 
ATOM   3056  C  CB  . VAL   B 2 55  ? 40.239  52.984  7.537   1.00 98.69  ? 55   VAL   B CB  1 
ATOM   3057  C  CG1 . VAL   B 2 55  ? 40.935  53.472  8.795   1.00 109.25 ? 55   VAL   B CG1 1 
ATOM   3058  C  CG2 . VAL   B 2 55  ? 39.262  51.868  7.876   1.00 98.30  ? 55   VAL   B CG2 1 
ATOM   3059  N  N   . GLY   B 2 56  ? 40.051  53.841  4.533   1.00 97.24  ? 56   GLY   B N   1 
ATOM   3060  C  CA  . GLY   B 2 56  ? 39.803  53.539  3.138   1.00 96.71  ? 56   GLY   B CA  1 
ATOM   3061  C  C   . GLY   B 2 56  ? 40.618  52.367  2.628   1.00 97.51  ? 56   GLY   B C   1 
ATOM   3062  O  O   . GLY   B 2 56  ? 41.861  52.390  2.653   1.00 97.23  ? 56   GLY   B O   1 
ATOM   3063  N  N   . MET   B 2 57  ? 39.914  51.339  2.153   1.00 93.45  ? 57   MET   B N   1 
ATOM   3064  C  CA  . MET   B 2 57  ? 40.543  50.173  1.559   1.00 90.07  ? 57   MET   B CA  1 
ATOM   3065  C  C   . MET   B 2 57  ? 40.719  50.369  0.056   1.00 89.34  ? 57   MET   B C   1 
ATOM   3066  O  O   . MET   B 2 57  ? 39.998  51.139  -0.587  1.00 85.73  ? 57   MET   B O   1 
ATOM   3067  C  CB  . MET   B 2 57  ? 39.718  48.920  1.835   1.00 86.15  ? 57   MET   B CB  1 
ATOM   3068  C  CG  . MET   B 2 57  ? 39.370  48.737  3.297   1.00 86.19  ? 57   MET   B CG  1 
ATOM   3069  S  SD  . MET   B 2 57  ? 38.765  47.090  3.664   1.00 89.13  ? 57   MET   B SD  1 
ATOM   3070  C  CE  . MET   B 2 57  ? 40.209  46.080  3.350   1.00 88.39  ? 57   MET   B CE  1 
ATOM   3071  N  N   . TYR   B 2 58  ? 41.707  49.660  -0.488  1.00 91.89  ? 58   TYR   B N   1 
ATOM   3072  C  CA  . TYR   B 2 58  ? 42.008  49.623  -1.919  1.00 91.26  ? 58   TYR   B CA  1 
ATOM   3073  C  C   . TYR   B 2 58  ? 41.168  48.555  -2.630  1.00 88.08  ? 58   TYR   B C   1 
ATOM   3074  O  O   . TYR   B 2 58  ? 41.669  47.710  -3.359  1.00 89.00  ? 58   TYR   B O   1 
ATOM   3075  C  CB  . TYR   B 2 58  ? 43.507  49.387  -2.112  1.00 92.43  ? 58   TYR   B CB  1 
ATOM   3076  C  CG  . TYR   B 2 58  ? 44.362  50.615  -1.844  1.00 94.35  ? 58   TYR   B CG  1 
ATOM   3077  C  CD1 . TYR   B 2 58  ? 44.831  50.905  -0.569  1.00 98.88  ? 58   TYR   B CD1 1 
ATOM   3078  C  CD2 . TYR   B 2 58  ? 44.695  51.493  -2.866  1.00 97.35  ? 58   TYR   B CD2 1 
ATOM   3079  C  CE1 . TYR   B 2 58  ? 45.623  52.057  -0.318  1.00 105.92 ? 58   TYR   B CE1 1 
ATOM   3080  C  CE2 . TYR   B 2 58  ? 45.481  52.641  -2.634  1.00 101.49 ? 58   TYR   B CE2 1 
ATOM   3081  C  CZ  . TYR   B 2 58  ? 45.942  52.923  -1.364  1.00 104.92 ? 58   TYR   B CZ  1 
ATOM   3082  O  OH  . TYR   B 2 58  ? 46.713  54.060  -1.150  1.00 100.25 ? 58   TYR   B OH  1 
ATOM   3083  N  N   . GLY   B 2 59  ? 39.864  48.579  -2.397  1.00 83.10  ? 59   GLY   B N   1 
ATOM   3084  C  CA  . GLY   B 2 59  ? 38.977  47.550  -2.900  1.00 82.15  ? 59   GLY   B CA  1 
ATOM   3085  C  C   . GLY   B 2 59  ? 37.562  47.968  -2.590  1.00 83.02  ? 59   GLY   B C   1 
ATOM   3086  O  O   . GLY   B 2 59  ? 37.323  49.010  -1.982  1.00 82.85  ? 59   GLY   B O   1 
ATOM   3087  N  N   . LYS   B 2 60  ? 36.611  47.151  -3.013  1.00 83.95  ? 60   LYS   B N   1 
ATOM   3088  C  CA  . LYS   B 2 60  ? 35.208  47.423  -2.715  1.00 82.17  ? 60   LYS   B CA  1 
ATOM   3089  C  C   . LYS   B 2 60  ? 34.753  46.439  -1.655  1.00 80.46  ? 60   LYS   B C   1 
ATOM   3090  O  O   . LYS   B 2 60  ? 34.641  45.240  -1.927  1.00 81.12  ? 60   LYS   B O   1 
ATOM   3091  C  CB  . LYS   B 2 60  ? 34.343  47.324  -3.971  1.00 82.61  ? 60   LYS   B CB  1 
ATOM   3092  C  CG  . LYS   B 2 60  ? 34.259  48.618  -4.750  1.00 81.76  ? 60   LYS   B CG  1 
ATOM   3093  C  CD  . LYS   B 2 60  ? 33.670  48.373  -6.126  1.00 82.04  ? 60   LYS   B CD  1 
ATOM   3094  C  CE  . LYS   B 2 60  ? 32.167  48.163  -6.085  1.00 84.58  ? 60   LYS   B CE  1 
ATOM   3095  N  NZ  . LYS   B 2 60  ? 31.367  49.444  -6.140  1.00 88.49  ? 60   LYS   B NZ  1 
ATOM   3096  N  N   . ILE   B 2 61  ? 34.487  46.945  -0.457  1.00 81.63  ? 61   ILE   B N   1 
ATOM   3097  C  CA  . ILE   B 2 61  ? 34.055  46.104  0.650   1.00 83.01  ? 61   ILE   B CA  1 
ATOM   3098  C  C   . ILE   B 2 61  ? 32.829  45.342  0.183   1.00 82.32  ? 61   ILE   B C   1 
ATOM   3099  O  O   . ILE   B 2 61  ? 31.805  45.938  -0.162  1.00 80.13  ? 61   ILE   B O   1 
ATOM   3100  C  CB  . ILE   B 2 61  ? 33.779  46.921  1.923   1.00 81.39  ? 61   ILE   B CB  1 
ATOM   3101  C  CG1 . ILE   B 2 61  ? 35.117  47.363  2.529   1.00 84.24  ? 61   ILE   B CG1 1 
ATOM   3102  C  CG2 . ILE   B 2 61  ? 32.978  46.100  2.927   1.00 78.65  ? 61   ILE   B CG2 1 
ATOM   3103  C  CD1 . ILE   B 2 61  ? 35.014  48.393  3.638   1.00 83.40  ? 61   ILE   B CD1 1 
ATOM   3104  N  N   . ALA   B 2 62  ? 32.977  44.023  0.098   1.00 83.97  ? 62   ALA   B N   1 
ATOM   3105  C  CA  . ALA   B 2 62  ? 31.953  43.109  -0.374  1.00 80.68  ? 62   ALA   B CA  1 
ATOM   3106  C  C   . ALA   B 2 62  ? 31.393  42.268  0.757   1.00 80.18  ? 62   ALA   B C   1 
ATOM   3107  O  O   . ALA   B 2 62  ? 30.179  42.125  0.880   1.00 77.94  ? 62   ALA   B O   1 
ATOM   3108  C  CB  . ALA   B 2 62  ? 32.533  42.195  -1.449  1.00 83.65  ? 62   ALA   B CB  1 
ATOM   3109  N  N   . VAL   B 2 63  ? 32.269  41.702  1.571   1.00 88.53  ? 63   VAL   B N   1 
ATOM   3110  C  CA  . VAL   B 2 63  ? 31.884  41.029  2.802   1.00 89.06  ? 63   VAL   B CA  1 
ATOM   3111  C  C   . VAL   B 2 63  ? 32.441  41.848  3.955   1.00 89.79  ? 63   VAL   B C   1 
ATOM   3112  O  O   . VAL   B 2 63  ? 33.576  42.342  3.895   1.00 89.90  ? 63   VAL   B O   1 
ATOM   3113  C  CB  . VAL   B 2 63  ? 32.393  39.571  2.850   1.00 90.23  ? 63   VAL   B CB  1 
ATOM   3114  C  CG1 . VAL   B 2 63  ? 31.902  38.883  4.120   1.00 92.28  ? 63   VAL   B CG1 1 
ATOM   3115  C  CG2 . VAL   B 2 63  ? 31.936  38.797  1.621   1.00 87.78  ? 63   VAL   B CG2 1 
ATOM   3116  N  N   . MET   B 2 64  ? 31.616  42.045  4.980   1.00 81.39  ? 64   MET   B N   1 
ATOM   3117  C  CA  . MET   B 2 64  ? 32.060  42.672  6.218   1.00 83.99  ? 64   MET   B CA  1 
ATOM   3118  C  C   . MET   B 2 64  ? 31.371  41.963  7.365   1.00 90.73  ? 64   MET   B C   1 
ATOM   3119  O  O   . MET   B 2 64  ? 30.140  42.016  7.480   1.00 90.21  ? 64   MET   B O   1 
ATOM   3120  C  CB  . MET   B 2 64  ? 31.740  44.164  6.261   1.00 86.97  ? 64   MET   B CB  1 
ATOM   3121  C  CG  . MET   B 2 64  ? 32.028  44.784  7.615   1.00 87.71  ? 64   MET   B CG  1 
ATOM   3122  S  SD  . MET   B 2 64  ? 31.522  46.512  7.770   1.00 80.91  ? 64   MET   B SD  1 
ATOM   3123  C  CE  . MET   B 2 64  ? 29.750  46.408  8.019   1.00 83.58  ? 64   MET   B CE  1 
ATOM   3124  N  N   . GLU   B 2 65  ? 32.172  41.314  8.210   1.00 91.13  ? 65   GLU   B N   1 
ATOM   3125  C  CA  . GLU   B 2 65  ? 31.658  40.531  9.318   1.00 88.96  ? 65   GLU   B CA  1 
ATOM   3126  C  C   . GLU   B 2 65  ? 32.663  40.578  10.457  1.00 90.27  ? 65   GLU   B C   1 
ATOM   3127  O  O   . GLU   B 2 65  ? 33.876  40.472  10.231  1.00 87.73  ? 65   GLU   B O   1 
ATOM   3128  C  CB  . GLU   B 2 65  ? 31.361  39.087  8.884   1.00 90.51  ? 65   GLU   B CB  1 
ATOM   3129  C  CG  . GLU   B 2 65  ? 29.958  38.919  8.271   1.00 93.96  ? 65   GLU   B CG  1 
ATOM   3130  C  CD  . GLU   B 2 65  ? 28.849  39.493  9.169   1.00 101.19 ? 65   GLU   B CD  1 
ATOM   3131  O  OE1 . GLU   B 2 65  ? 28.995  39.425  10.414  1.00 100.39 ? 65   GLU   B OE1 1 
ATOM   3132  O  OE2 . GLU   B 2 65  ? 27.831  40.014  8.645   1.00 100.78 ? 65   GLU   B OE2 1 
ATOM   3133  N  N   . LEU   B 2 66  ? 32.143  40.777  11.671  1.00 93.05  ? 66   LEU   B N   1 
ATOM   3134  C  CA  . LEU   B 2 66  ? 32.923  40.705  12.898  1.00 91.37  ? 66   LEU   B CA  1 
ATOM   3135  C  C   . LEU   B 2 66  ? 32.741  39.332  13.532  1.00 88.53  ? 66   LEU   B C   1 
ATOM   3136  O  O   . LEU   B 2 66  ? 31.669  38.731  13.461  1.00 83.17  ? 66   LEU   B O   1 
ATOM   3137  C  CB  . LEU   B 2 66  ? 32.508  41.799  13.888  1.00 88.66  ? 66   LEU   B CB  1 
ATOM   3138  C  CG  . LEU   B 2 66  ? 32.939  43.229  13.611  1.00 85.90  ? 66   LEU   B CG  1 
ATOM   3139  C  CD1 . LEU   B 2 66  ? 32.131  44.142  14.507  1.00 90.51  ? 66   LEU   B CD1 1 
ATOM   3140  C  CD2 . LEU   B 2 66  ? 34.395  43.388  13.906  1.00 87.47  ? 66   LEU   B CD2 1 
ATOM   3141  N  N   . PHE   B 2 67  ? 33.817  38.850  14.147  1.00 87.82  ? 67   PHE   B N   1 
ATOM   3142  C  CA  . PHE   B 2 67  ? 33.874  37.542  14.778  1.00 87.99  ? 67   PHE   B CA  1 
ATOM   3143  C  C   . PHE   B 2 67  ? 34.988  37.598  15.809  1.00 95.09  ? 67   PHE   B C   1 
ATOM   3144  O  O   . PHE   B 2 67  ? 35.768  38.559  15.843  1.00 91.64  ? 67   PHE   B O   1 
ATOM   3145  C  CB  . PHE   B 2 67  ? 34.119  36.423  13.755  1.00 90.29  ? 67   PHE   B CB  1 
ATOM   3146  C  CG  . PHE   B 2 67  ? 35.489  36.474  13.078  1.00 89.22  ? 67   PHE   B CG  1 
ATOM   3147  C  CD1 . PHE   B 2 67  ? 35.807  37.479  12.173  1.00 87.82  ? 67   PHE   B CD1 1 
ATOM   3148  C  CD2 . PHE   B 2 67  ? 36.441  35.486  13.318  1.00 86.48  ? 67   PHE   B CD2 1 
ATOM   3149  C  CE1 . PHE   B 2 67  ? 37.057  37.506  11.545  1.00 83.77  ? 67   PHE   B CE1 1 
ATOM   3150  C  CE2 . PHE   B 2 67  ? 37.689  35.513  12.684  1.00 79.36  ? 67   PHE   B CE2 1 
ATOM   3151  C  CZ  . PHE   B 2 67  ? 37.994  36.516  11.804  1.00 79.28  ? 67   PHE   B CZ  1 
ATOM   3152  N  N   . ARG   B 2 68  ? 35.034  36.570  16.665  1.00 100.77 ? 68   ARG   B N   1 
ATOM   3153  C  CA  . ARG   B 2 68  ? 35.986  36.501  17.777  1.00 98.56  ? 68   ARG   B CA  1 
ATOM   3154  C  C   . ARG   B 2 68  ? 36.371  35.059  18.027  1.00 98.32  ? 68   ARG   B C   1 
ATOM   3155  O  O   . ARG   B 2 68  ? 35.711  34.351  18.801  1.00 99.37  ? 68   ARG   B O   1 
ATOM   3156  C  CB  . ARG   B 2 68  ? 35.427  37.111  19.059  1.00 97.69  ? 68   ARG   B CB  1 
ATOM   3157  C  CG  . ARG   B 2 68  ? 36.381  37.041  20.218  1.00 100.45 ? 68   ARG   B CG  1 
ATOM   3158  C  CD  . ARG   B 2 68  ? 35.741  37.650  21.439  1.00 102.27 ? 68   ARG   B CD  1 
ATOM   3159  N  NE  . ARG   B 2 68  ? 35.390  39.040  21.195  1.00 100.48 ? 68   ARG   B NE  1 
ATOM   3160  C  CZ  . ARG   B 2 68  ? 35.311  39.956  22.145  1.00 102.30 ? 68   ARG   B CZ  1 
ATOM   3161  N  NH1 . ARG   B 2 68  ? 35.543  39.651  23.409  1.00 110.52 ? 68   ARG   B NH1 1 
ATOM   3162  N  NH2 . ARG   B 2 68  ? 35.006  41.209  21.819  1.00 101.67 ? 68   ARG   B NH2 1 
ATOM   3163  N  N   . PRO   B 2 69  ? 37.459  34.599  17.423  1.00 100.02 ? 69   PRO   B N   1 
ATOM   3164  C  CA  . PRO   B 2 69  ? 37.857  33.197  17.554  1.00 101.71 ? 69   PRO   B CA  1 
ATOM   3165  C  C   . PRO   B 2 69  ? 38.591  32.986  18.873  1.00 105.86 ? 69   PRO   B C   1 
ATOM   3166  O  O   . PRO   B 2 69  ? 38.984  33.936  19.555  1.00 107.03 ? 69   PRO   B O   1 
ATOM   3167  C  CB  . PRO   B 2 69  ? 38.782  33.007  16.359  1.00 98.42  ? 69   PRO   B CB  1 
ATOM   3168  C  CG  . PRO   B 2 69  ? 39.490  34.362  16.309  1.00 102.94 ? 69   PRO   B CG  1 
ATOM   3169  C  CD  . PRO   B 2 69  ? 38.489  35.405  16.759  1.00 99.13  ? 69   PRO   B CD  1 
ATOM   3170  N  N   . LYS   B 2 70  ? 38.771  31.709  19.220  1.00 106.71 ? 70   LYS   B N   1 
ATOM   3171  C  CA  . LYS   B 2 70  ? 39.317  31.348  20.526  1.00 106.94 ? 70   LYS   B CA  1 
ATOM   3172  C  C   . LYS   B 2 70  ? 40.693  31.976  20.733  1.00 108.57 ? 70   LYS   B C   1 
ATOM   3173  O  O   . LYS   B 2 70  ? 41.621  31.718  19.964  1.00 108.76 ? 70   LYS   B O   1 
ATOM   3174  C  CB  . LYS   B 2 70  ? 39.398  29.828  20.652  1.00 103.71 ? 70   LYS   B CB  1 
ATOM   3175  N  N   . GLY   B 2 71  ? 40.813  32.815  21.761  1.00 113.31 ? 71   GLY   B N   1 
ATOM   3176  C  CA  . GLY   B 2 71  ? 42.061  33.503  22.053  1.00 115.80 ? 71   GLY   B CA  1 
ATOM   3177  C  C   . GLY   B 2 71  ? 42.135  34.906  21.487  1.00 118.30 ? 71   GLY   B C   1 
ATOM   3178  O  O   . GLY   B 2 71  ? 42.988  35.187  20.640  1.00 120.39 ? 71   GLY   B O   1 
ATOM   3179  N  N   . GLU   B 2 72  ? 41.266  35.792  21.972  1.00 120.36 ? 72   GLU   B N   1 
ATOM   3180  C  CA  . GLU   B 2 72  ? 41.141  37.149  21.448  1.00 116.53 ? 72   GLU   B CA  1 
ATOM   3181  C  C   . GLU   B 2 72  ? 40.565  38.069  22.508  1.00 114.72 ? 72   GLU   B C   1 
ATOM   3182  O  O   . GLU   B 2 72  ? 39.521  37.762  23.091  1.00 115.07 ? 72   GLU   B O   1 
ATOM   3183  C  CB  . GLU   B 2 72  ? 40.233  37.183  20.219  1.00 114.50 ? 72   GLU   B CB  1 
ATOM   3184  C  CG  . GLU   B 2 72  ? 40.917  36.892  18.934  1.00 116.35 ? 72   GLU   B CG  1 
ATOM   3185  C  CD  . GLU   B 2 72  ? 42.205  37.680  18.792  1.00 120.20 ? 72   GLU   B CD  1 
ATOM   3186  O  OE1 . GLU   B 2 72  ? 43.159  37.124  18.208  1.00 119.95 ? 72   GLU   B OE1 1 
ATOM   3187  O  OE2 . GLU   B 2 72  ? 42.264  38.858  19.249  1.00 121.10 ? 72   GLU   B OE2 1 
ATOM   3188  N  N   . SER   B 2 73  ? 41.226  39.200  22.744  1.00 116.88 ? 73   SER   B N   1 
ATOM   3189  C  CA  . SER   B 2 73  ? 40.686  40.140  23.722  1.00 117.16 ? 73   SER   B CA  1 
ATOM   3190  C  C   . SER   B 2 73  ? 39.386  40.763  23.217  1.00 117.92 ? 73   SER   B C   1 
ATOM   3191  O  O   . SER   B 2 73  ? 38.410  40.872  23.972  1.00 116.11 ? 73   SER   B O   1 
ATOM   3192  C  CB  . SER   B 2 73  ? 41.721  41.219  24.069  1.00 114.38 ? 73   SER   B CB  1 
ATOM   3193  O  OG  . SER   B 2 73  ? 42.312  41.788  22.916  1.00 117.89 ? 73   SER   B OG  1 
ATOM   3194  N  N   . LYS   B 2 74  ? 39.350  41.133  21.933  1.00 118.14 ? 74   LYS   B N   1 
ATOM   3195  C  CA  . LYS   B 2 74  ? 38.232  41.815  21.279  1.00 107.75 ? 74   LYS   B CA  1 
ATOM   3196  C  C   . LYS   B 2 74  ? 37.791  41.036  20.030  1.00 104.67 ? 74   LYS   B C   1 
ATOM   3197  O  O   . LYS   B 2 74  ? 38.363  39.991  19.668  1.00 101.61 ? 74   LYS   B O   1 
ATOM   3198  C  CB  . LYS   B 2 74  ? 38.625  43.257  20.920  1.00 105.82 ? 74   LYS   B CB  1 
ATOM   3199  C  CG  . LYS   B 2 74  ? 38.790  44.159  22.116  1.00 110.30 ? 74   LYS   B CG  1 
ATOM   3200  C  CD  . LYS   B 2 74  ? 40.257  44.358  22.548  1.00 114.88 ? 74   LYS   B CD  1 
ATOM   3201  C  CE  . LYS   B 2 74  ? 40.337  45.004  23.960  1.00 113.58 ? 74   LYS   B CE  1 
ATOM   3202  N  NZ  . LYS   B 2 74  ? 41.679  45.016  24.607  1.00 99.09  ? 74   LYS   B NZ  1 
ATOM   3203  N  N   . ASP   B 2 75  ? 36.754  41.572  19.383  1.00 102.65 ? 75   ASP   B N   1 
ATOM   3204  C  CA  . ASP   B 2 75  ? 36.282  41.114  18.079  1.00 96.40  ? 75   ASP   B CA  1 
ATOM   3205  C  C   . ASP   B 2 75  ? 37.250  41.528  16.972  1.00 94.57  ? 75   ASP   B C   1 
ATOM   3206  O  O   . ASP   B 2 75  ? 37.883  42.593  17.022  1.00 93.44  ? 75   ASP   B O   1 
ATOM   3207  C  CB  . ASP   B 2 75  ? 34.898  41.709  17.741  1.00 94.33  ? 75   ASP   B CB  1 
ATOM   3208  C  CG  . ASP   B 2 75  ? 33.724  40.927  18.334  1.00 93.99  ? 75   ASP   B CG  1 
ATOM   3209  O  OD1 . ASP   B 2 75  ? 33.167  40.070  17.621  1.00 95.56  ? 75   ASP   B OD1 1 
ATOM   3210  O  OD2 . ASP   B 2 75  ? 33.321  41.205  19.482  1.00 97.50  ? 75   ASP   B OD2 1 
ATOM   3211  N  N   . LEU   B 2 76  ? 37.328  40.682  15.944  1.00 94.59  ? 76   LEU   B N   1 
ATOM   3212  C  CA  . LEU   B 2 76  ? 38.049  40.957  14.708  1.00 92.17  ? 76   LEU   B CA  1 
ATOM   3213  C  C   . LEU   B 2 76  ? 37.061  41.137  13.562  1.00 90.03  ? 76   LEU   B C   1 
ATOM   3214  O  O   . LEU   B 2 76  ? 35.935  40.634  13.600  1.00 91.40  ? 76   LEU   B O   1 
ATOM   3215  C  CB  . LEU   B 2 76  ? 39.013  39.818  14.373  1.00 88.35  ? 76   LEU   B CB  1 
ATOM   3216  C  CG  . LEU   B 2 76  ? 39.961  39.472  15.497  1.00 91.00  ? 76   LEU   B CG  1 
ATOM   3217  C  CD1 . LEU   B 2 76  ? 40.817  38.285  15.114  1.00 89.30  ? 76   LEU   B CD1 1 
ATOM   3218  C  CD2 . LEU   B 2 76  ? 40.793  40.700  15.783  1.00 93.58  ? 76   LEU   B CD2 1 
ATOM   3219  N  N   . LEU   B 2 77  ? 37.501  41.826  12.518  1.00 86.63  ? 77   LEU   B N   1 
ATOM   3220  C  CA  . LEU   B 2 77  ? 36.641  42.172  11.398  1.00 87.34  ? 77   LEU   B CA  1 
ATOM   3221  C  C   . LEU   B 2 77  ? 37.135  41.517  10.112  1.00 89.44  ? 77   LEU   B C   1 
ATOM   3222  O  O   . LEU   B 2 77  ? 38.303  41.680  9.744   1.00 88.74  ? 77   LEU   B O   1 
ATOM   3223  C  CB  . LEU   B 2 77  ? 36.611  43.677  11.237  1.00 89.37  ? 77   LEU   B CB  1 
ATOM   3224  C  CG  . LEU   B 2 77  ? 35.921  44.152  9.988   1.00 86.45  ? 77   LEU   B CG  1 
ATOM   3225  C  CD1 . LEU   B 2 77  ? 34.468  43.790  10.121  1.00 86.91  ? 77   LEU   B CD1 1 
ATOM   3226  C  CD2 . LEU   B 2 77  ? 36.131  45.633  9.937   1.00 85.56  ? 77   LEU   B CD2 1 
ATOM   3227  N  N   . PHE   B 2 78  ? 36.248  40.788  9.419   1.00 90.34  ? 78   PHE   B N   1 
ATOM   3228  C  CA  . PHE   B 2 78  ? 36.597  40.117  8.165   1.00 88.71  ? 78   PHE   B CA  1 
ATOM   3229  C  C   . PHE   B 2 78  ? 36.049  40.900  6.984   1.00 89.78  ? 78   PHE   B C   1 
ATOM   3230  O  O   . PHE   B 2 78  ? 34.844  41.167  6.912   1.00 89.94  ? 78   PHE   B O   1 
ATOM   3231  C  CB  . PHE   B 2 78  ? 36.069  38.681  8.103   1.00 88.66  ? 78   PHE   B CB  1 
ATOM   3232  C  CG  . PHE   B 2 78  ? 36.309  37.985  6.769   1.00 87.79  ? 78   PHE   B CG  1 
ATOM   3233  C  CD1 . PHE   B 2 78  ? 37.546  37.416  6.464   1.00 87.28  ? 78   PHE   B CD1 1 
ATOM   3234  C  CD2 . PHE   B 2 78  ? 35.285  37.878  5.829   1.00 87.64  ? 78   PHE   B CD2 1 
ATOM   3235  C  CE1 . PHE   B 2 78  ? 37.758  36.761  5.244   1.00 87.76  ? 78   PHE   B CE1 1 
ATOM   3236  C  CE2 . PHE   B 2 78  ? 35.495  37.231  4.613   1.00 87.42  ? 78   PHE   B CE2 1 
ATOM   3237  C  CZ  . PHE   B 2 78  ? 36.733  36.671  4.323   1.00 87.54  ? 78   PHE   B CZ  1 
ATOM   3238  N  N   . ILE   B 2 79  ? 36.936  41.242  6.055   1.00 87.41  ? 79   ILE   B N   1 
ATOM   3239  C  CA  . ILE   B 2 79  ? 36.607  42.072  4.907   1.00 85.00  ? 79   ILE   B CA  1 
ATOM   3240  C  C   . ILE   B 2 79  ? 36.999  41.303  3.659   1.00 84.89  ? 79   ILE   B C   1 
ATOM   3241  O  O   . ILE   B 2 79  ? 38.162  40.917  3.504   1.00 86.16  ? 79   ILE   B O   1 
ATOM   3242  C  CB  . ILE   B 2 79  ? 37.331  43.428  4.945   1.00 85.56  ? 79   ILE   B CB  1 
ATOM   3243  C  CG1 . ILE   B 2 79  ? 36.771  44.325  6.061   1.00 83.45  ? 79   ILE   B CG1 1 
ATOM   3244  C  CG2 . ILE   B 2 79  ? 37.283  44.078  3.571   1.00 86.79  ? 79   ILE   B CG2 1 
ATOM   3245  C  CD1 . ILE   B 2 79  ? 35.293  44.595  5.978   1.00 81.72  ? 79   ILE   B CD1 1 
ATOM   3246  N  N   . LEU   B 2 80  ? 36.038  41.069  2.782   1.00 82.07  ? 80   LEU   B N   1 
ATOM   3247  C  CA  . LEU   B 2 80  ? 36.308  40.537  1.461   1.00 80.88  ? 80   LEU   B CA  1 
ATOM   3248  C  C   . LEU   B 2 80  ? 35.892  41.614  0.476   1.00 83.89  ? 80   LEU   B C   1 
ATOM   3249  O  O   . LEU   B 2 80  ? 34.793  42.157  0.600   1.00 85.25  ? 80   LEU   B O   1 
ATOM   3250  C  CB  . LEU   B 2 80  ? 35.546  39.225  1.231   1.00 82.73  ? 80   LEU   B CB  1 
ATOM   3251  C  CG  . LEU   B 2 80  ? 35.622  38.512  -0.129  1.00 81.29  ? 80   LEU   B CG  1 
ATOM   3252  C  CD1 . LEU   B 2 80  ? 37.004  38.624  -0.713  1.00 84.61  ? 80   LEU   B CD1 1 
ATOM   3253  C  CD2 . LEU   B 2 80  ? 35.218  37.041  -0.053  1.00 75.73  ? 80   LEU   B CD2 1 
ATOM   3254  N  N   . THR   B 2 81  ? 36.782  41.957  -0.461  1.00 82.89  ? 81   THR   B N   1 
ATOM   3255  C  CA  . THR   B 2 81  ? 36.471  42.967  -1.465  1.00 81.42  ? 81   THR   B CA  1 
ATOM   3256  C  C   . THR   B 2 81  ? 35.928  42.329  -2.744  1.00 85.06  ? 81   THR   B C   1 
ATOM   3257  O  O   . THR   B 2 81  ? 35.780  41.110  -2.862  1.00 84.05  ? 81   THR   B O   1 
ATOM   3258  C  CB  . THR   B 2 81  ? 37.689  43.812  -1.816  1.00 81.76  ? 81   THR   B CB  1 
ATOM   3259  O  OG1 . THR   B 2 81  ? 38.444  43.156  -2.846  1.00 79.90  ? 81   THR   B OG1 1 
ATOM   3260  C  CG2 . THR   B 2 81  ? 38.546  44.046  -0.578  1.00 83.45  ? 81   THR   B CG2 1 
ATOM   3261  N  N   . ALA   B 2 82  ? 35.623  43.178  -3.725  1.00 90.37  ? 82   ALA   B N   1 
ATOM   3262  C  CA  . ALA   B 2 82  ? 35.029  42.673  -4.955  1.00 89.80  ? 82   ALA   B CA  1 
ATOM   3263  C  C   . ALA   B 2 82  ? 36.064  41.989  -5.837  1.00 91.08  ? 82   ALA   B C   1 
ATOM   3264  O  O   . ALA   B 2 82  ? 35.724  41.075  -6.594  1.00 91.80  ? 82   ALA   B O   1 
ATOM   3265  C  CB  . ALA   B 2 82  ? 34.342  43.811  -5.706  1.00 91.17  ? 82   ALA   B CB  1 
ATOM   3266  N  N   . LYS   B 2 83  ? 37.323  42.412  -5.763  1.00 85.86  ? 83   LYS   B N   1 
ATOM   3267  C  CA  . LYS   B 2 83  ? 38.394  41.745  -6.476  1.00 82.64  ? 83   LYS   B CA  1 
ATOM   3268  C  C   . LYS   B 2 83  ? 38.968  40.576  -5.677  1.00 85.02  ? 83   LYS   B C   1 
ATOM   3269  O  O   . LYS   B 2 83  ? 40.099  40.152  -5.940  1.00 83.03  ? 83   LYS   B O   1 
ATOM   3270  C  CB  . LYS   B 2 83  ? 39.479  42.760  -6.840  1.00 85.79  ? 83   LYS   B CB  1 
ATOM   3271  C  CG  . LYS   B 2 83  ? 39.008  43.884  -7.768  1.00 89.51  ? 83   LYS   B CG  1 
ATOM   3272  C  CD  . LYS   B 2 83  ? 40.065  44.167  -8.802  1.00 87.43  ? 83   LYS   B CD  1 
ATOM   3273  C  CE  . LYS   B 2 83  ? 40.085  45.623  -9.206  1.00 83.43  ? 83   LYS   B CE  1 
ATOM   3274  N  NZ  . LYS   B 2 83  ? 41.322  45.814  -9.980  1.00 84.09  ? 83   LYS   B NZ  1 
ATOM   3275  N  N   . TYR   B 2 84  ? 38.201  40.068  -4.705  1.00 85.37  ? 84   TYR   B N   1 
ATOM   3276  C  CA  . TYR   B 2 84  ? 38.452  38.842  -3.942  1.00 82.94  ? 84   TYR   B CA  1 
ATOM   3277  C  C   . TYR   B 2 84  ? 39.550  39.014  -2.912  1.00 84.33  ? 84   TYR   B C   1 
ATOM   3278  O  O   . TYR   B 2 84  ? 40.075  38.030  -2.389  1.00 89.64  ? 84   TYR   B O   1 
ATOM   3279  C  CB  . TYR   B 2 84  ? 38.723  37.632  -4.858  1.00 87.03  ? 84   TYR   B CB  1 
ATOM   3280  C  CG  . TYR   B 2 84  ? 37.486  37.291  -5.674  1.00 88.71  ? 84   TYR   B CG  1 
ATOM   3281  C  CD1 . TYR   B 2 84  ? 36.334  36.821  -5.044  1.00 90.84  ? 84   TYR   B CD1 1 
ATOM   3282  C  CD2 . TYR   B 2 84  ? 37.430  37.509  -7.053  1.00 88.96  ? 84   TYR   B CD2 1 
ATOM   3283  C  CE1 . TYR   B 2 84  ? 35.156  36.538  -5.768  1.00 88.93  ? 84   TYR   B CE1 1 
ATOM   3284  C  CE2 . TYR   B 2 84  ? 36.259  37.233  -7.787  1.00 91.38  ? 84   TYR   B CE2 1 
ATOM   3285  C  CZ  . TYR   B 2 84  ? 35.125  36.743  -7.131  1.00 89.98  ? 84   TYR   B CZ  1 
ATOM   3286  O  OH  . TYR   B 2 84  ? 33.952  36.456  -7.807  1.00 87.79  ? 84   TYR   B OH  1 
ATOM   3287  N  N   . ASN   B 2 85  ? 39.865  40.255  -2.562  1.00 83.18  ? 85   ASN   B N   1 
ATOM   3288  C  CA  . ASN   B 2 85  ? 40.831  40.526  -1.498  1.00 85.13  ? 85   ASN   B CA  1 
ATOM   3289  C  C   . ASN   B 2 85  ? 40.187  40.250  -0.144  1.00 84.31  ? 85   ASN   B C   1 
ATOM   3290  O  O   . ASN   B 2 85  ? 39.261  40.953  0.277   1.00 83.38  ? 85   ASN   B O   1 
ATOM   3291  C  CB  . ASN   B 2 85  ? 41.317  41.970  -1.588  1.00 83.88  ? 85   ASN   B CB  1 
ATOM   3292  C  CG  . ASN   B 2 85  ? 41.736  42.345  -2.983  1.00 82.23  ? 85   ASN   B CG  1 
ATOM   3293  O  OD1 . ASN   B 2 85  ? 41.018  43.071  -3.663  1.00 82.78  ? 85   ASN   B OD1 1 
ATOM   3294  N  ND2 . ASN   B 2 85  ? 42.890  41.842  -3.431  1.00 80.63  ? 85   ASN   B ND2 1 
ATOM   3295  N  N   . ALA   B 2 86  ? 40.651  39.219  0.540   1.00 87.65  ? 86   ALA   B N   1 
ATOM   3296  C  CA  . ALA   B 2 86  ? 40.173  38.934  1.881   1.00 87.73  ? 86   ALA   B CA  1 
ATOM   3297  C  C   . ALA   B 2 86  ? 41.203  39.405  2.889   1.00 88.40  ? 86   ALA   B C   1 
ATOM   3298  O  O   . ALA   B 2 86  ? 42.411  39.409  2.627   1.00 89.31  ? 86   ALA   B O   1 
ATOM   3299  C  CB  . ALA   B 2 86  ? 39.881  37.443  2.083   1.00 89.69  ? 86   ALA   B CB  1 
ATOM   3300  N  N   . CYS   B 2 87  ? 40.707  39.839  4.038   1.00 88.41  ? 87   CYS   B N   1 
ATOM   3301  C  CA  . CYS   B 2 87  ? 41.612  40.285  5.084   1.00 94.15  ? 87   CYS   B CA  1 
ATOM   3302  C  C   . CYS   B 2 87  ? 40.876  40.340  6.411   1.00 92.05  ? 87   CYS   B C   1 
ATOM   3303  O  O   . CYS   B 2 87  ? 39.690  40.685  6.465   1.00 88.09  ? 87   CYS   B O   1 
ATOM   3304  C  CB  . CYS   B 2 87  ? 42.232  41.656  4.778   1.00 93.73  ? 87   CYS   B CB  1 
ATOM   3305  S  SG  . CYS   B 2 87  ? 41.044  42.980  4.840   1.00 90.03  ? 87   CYS   B SG  1 
ATOM   3306  N  N   . ILE   B 2 88  ? 41.604  40.005  7.475   1.00 95.04  ? 88   ILE   B N   1 
ATOM   3307  C  CA  . ILE   B 2 88  ? 41.100  40.058  8.836   1.00 93.56  ? 88   ILE   B CA  1 
ATOM   3308  C  C   . ILE   B 2 88  ? 41.798  41.196  9.562   1.00 98.95  ? 88   ILE   B C   1 
ATOM   3309  O  O   . ILE   B 2 88  ? 43.033  41.273  9.577   1.00 100.01 ? 88   ILE   B O   1 
ATOM   3310  C  CB  . ILE   B 2 88  ? 41.308  38.731  9.575   1.00 88.94  ? 88   ILE   B CB  1 
ATOM   3311  C  CG1 . ILE   B 2 88  ? 40.809  37.553  8.730   1.00 88.63  ? 88   ILE   B CG1 1 
ATOM   3312  C  CG2 . ILE   B 2 88  ? 40.570  38.799  10.869  1.00 89.90  ? 88   ILE   B CG2 1 
ATOM   3313  C  CD1 . ILE   B 2 88  ? 40.819  36.179  9.433   1.00 79.29  ? 88   ILE   B CD1 1 
ATOM   3314  N  N   . LEU   B 2 89  ? 41.000  42.068  10.176  1.00 98.16  ? 89   LEU   B N   1 
ATOM   3315  C  CA  . LEU   B 2 89  ? 41.464  43.317  10.753  1.00 96.72  ? 89   LEU   B CA  1 
ATOM   3316  C  C   . LEU   B 2 89  ? 41.244  43.317  12.259  1.00 97.32  ? 89   LEU   B C   1 
ATOM   3317  O  O   . LEU   B 2 89  ? 40.266  42.753  12.764  1.00 94.44  ? 89   LEU   B O   1 
ATOM   3318  C  CB  . LEU   B 2 89  ? 40.727  44.491  10.119  1.00 96.85  ? 89   LEU   B CB  1 
ATOM   3319  C  CG  . LEU   B 2 89  ? 40.691  44.386  8.600   1.00 92.89  ? 89   LEU   B CG  1 
ATOM   3320  C  CD1 . LEU   B 2 89  ? 39.809  45.473  8.051   1.00 87.74  ? 89   LEU   B CD1 1 
ATOM   3321  C  CD2 . LEU   B 2 89  ? 42.105  44.455  8.021   1.00 95.65  ? 89   LEU   B CD2 1 
ATOM   3322  N  N   . GLU   B 2 90  ? 42.176  43.962  12.960  1.00 102.47 ? 90   GLU   B N   1 
ATOM   3323  C  CA  . GLU   B 2 90  ? 42.119  44.155  14.397  1.00 101.84 ? 90   GLU   B CA  1 
ATOM   3324  C  C   . GLU   B 2 90  ? 42.349  45.625  14.692  1.00 104.44 ? 90   GLU   B C   1 
ATOM   3325  O  O   . GLU   B 2 90  ? 43.171  46.273  14.039  1.00 109.36 ? 90   GLU   B O   1 
ATOM   3326  C  CB  . GLU   B 2 90  ? 43.176  43.315  15.135  1.00 103.94 ? 90   GLU   B CB  1 
ATOM   3327  C  CG  . GLU   B 2 90  ? 43.046  43.337  16.669  1.00 110.22 ? 90   GLU   B CG  1 
ATOM   3328  C  CD  . GLU   B 2 90  ? 44.334  42.967  17.415  1.00 109.20 ? 90   GLU   B CD  1 
ATOM   3329  O  OE1 . GLU   B 2 90  ? 45.150  42.232  16.830  1.00 104.76 ? 90   GLU   B OE1 1 
ATOM   3330  O  OE2 . GLU   B 2 90  ? 44.529  43.413  18.577  1.00 115.39 ? 90   GLU   B OE2 1 
ATOM   3331  N  N   . TYR   B 2 91  ? 41.640  46.137  15.699  1.00 105.03 ? 91   TYR   B N   1 
ATOM   3332  C  CA  . TYR   B 2 91  ? 41.740  47.538  16.107  1.00 111.40 ? 91   TYR   B CA  1 
ATOM   3333  C  C   . TYR   B 2 91  ? 42.833  47.693  17.165  1.00 118.78 ? 91   TYR   B C   1 
ATOM   3334  O  O   . TYR   B 2 91  ? 42.941  46.880  18.084  1.00 119.96 ? 91   TYR   B O   1 
ATOM   3335  C  CB  . TYR   B 2 91  ? 40.382  48.010  16.637  1.00 106.53 ? 91   TYR   B CB  1 
ATOM   3336  C  CG  . TYR   B 2 91  ? 40.290  49.457  17.068  1.00 108.03 ? 91   TYR   B CG  1 
ATOM   3337  C  CD1 . TYR   B 2 91  ? 40.798  49.861  18.290  1.00 118.43 ? 91   TYR   B CD1 1 
ATOM   3338  C  CD2 . TYR   B 2 91  ? 39.659  50.413  16.280  1.00 107.57 ? 91   TYR   B CD2 1 
ATOM   3339  C  CE1 . TYR   B 2 91  ? 40.716  51.191  18.721  1.00 124.43 ? 91   TYR   B CE1 1 
ATOM   3340  C  CE2 . TYR   B 2 91  ? 39.567  51.760  16.701  1.00 110.17 ? 91   TYR   B CE2 1 
ATOM   3341  C  CZ  . TYR   B 2 91  ? 40.102  52.138  17.928  1.00 119.65 ? 91   TYR   B CZ  1 
ATOM   3342  O  OH  . TYR   B 2 91  ? 40.035  53.445  18.383  1.00 119.33 ? 91   TYR   B OH  1 
ATOM   3343  N  N   . LYS   B 2 92  ? 43.647  48.744  17.032  1.00 137.93 ? 92   LYS   B N   1 
ATOM   3344  C  CA  . LYS   B 2 92  ? 44.796  48.921  17.923  1.00 144.91 ? 92   LYS   B CA  1 
ATOM   3345  C  C   . LYS   B 2 92  ? 45.173  50.402  18.005  1.00 149.94 ? 92   LYS   B C   1 
ATOM   3346  O  O   . LYS   B 2 92  ? 45.678  50.982  17.032  1.00 150.92 ? 92   LYS   B O   1 
ATOM   3347  C  CB  . LYS   B 2 92  ? 45.983  48.064  17.465  1.00 142.00 ? 92   LYS   B CB  1 
ATOM   3348  N  N   . GLN   B 2 93  ? 44.969  50.991  19.193  1.00 143.44 ? 93   GLN   B N   1 
ATOM   3349  C  CA  . GLN   B 2 93  ? 45.150  52.415  19.471  1.00 140.40 ? 93   GLN   B CA  1 
ATOM   3350  C  C   . GLN   B 2 93  ? 46.119  52.613  20.629  1.00 141.94 ? 93   GLN   B C   1 
ATOM   3351  O  O   . GLN   B 2 93  ? 45.908  52.069  21.715  1.00 145.50 ? 93   GLN   B O   1 
ATOM   3352  C  CB  . GLN   B 2 93  ? 43.816  53.075  19.824  1.00 139.84 ? 93   GLN   B CB  1 
ATOM   3353  C  CG  . GLN   B 2 93  ? 43.947  54.383  20.592  1.00 139.69 ? 93   GLN   B CG  1 
ATOM   3354  C  CD  . GLN   B 2 93  ? 42.598  54.986  20.898  1.00 147.95 ? 93   GLN   B CD  1 
ATOM   3355  O  OE1 . GLN   B 2 93  ? 41.559  54.330  20.721  1.00 148.63 ? 93   GLN   B OE1 1 
ATOM   3356  N  NE2 . GLN   B 2 93  ? 42.595  56.248  21.346  1.00 150.49 ? 93   GLN   B NE2 1 
ATOM   3357  N  N   . SER   B 2 94  ? 47.149  53.423  20.425  1.00 140.12 ? 94   SER   B N   1 
ATOM   3358  C  CA  . SER   B 2 94  ? 48.147  53.684  21.461  1.00 140.49 ? 94   SER   B CA  1 
ATOM   3359  C  C   . SER   B 2 94  ? 47.905  55.088  22.020  1.00 142.48 ? 94   SER   B C   1 
ATOM   3360  O  O   . SER   B 2 94  ? 48.468  56.072  21.533  1.00 145.33 ? 94   SER   B O   1 
ATOM   3361  C  CB  . SER   B 2 94  ? 49.552  53.539  20.907  1.00 139.49 ? 94   SER   B CB  1 
ATOM   3362  O  OG  . SER   B 2 94  ? 50.510  53.869  21.896  1.00 129.81 ? 94   SER   B OG  1 
ATOM   3363  N  N   . GLY   B 2 95  ? 47.063  55.173  23.045  1.00 142.58 ? 95   GLY   B N   1 
ATOM   3364  C  CA  . GLY   B 2 95  ? 46.677  56.461  23.573  1.00 141.70 ? 95   GLY   B CA  1 
ATOM   3365  C  C   . GLY   B 2 95  ? 45.975  57.349  22.568  1.00 144.86 ? 95   GLY   B C   1 
ATOM   3366  O  O   . GLY   B 2 95  ? 44.762  57.565  22.657  1.00 144.17 ? 95   GLY   B O   1 
ATOM   3367  N  N   . GLU   B 2 96  ? 46.727  57.852  21.582  1.00 142.54 ? 96   GLU   B N   1 
ATOM   3368  C  CA  . GLU   B 2 96  ? 46.183  58.756  20.576  1.00 142.90 ? 96   GLU   B CA  1 
ATOM   3369  C  C   . GLU   B 2 96  ? 46.474  58.260  19.165  1.00 138.58 ? 96   GLU   B C   1 
ATOM   3370  O  O   . GLU   B 2 96  ? 46.105  58.942  18.199  1.00 132.79 ? 96   GLU   B O   1 
ATOM   3371  C  CB  . GLU   B 2 96  ? 46.699  60.196  20.740  1.00 142.82 ? 96   GLU   B CB  1 
ATOM   3372  N  N   . SER   B 2 97  ? 47.106  57.095  19.012  1.00 139.80 ? 97   SER   B N   1 
ATOM   3373  C  CA  . SER   B 2 97  ? 47.564  56.588  17.718  1.00 138.76 ? 97   SER   B CA  1 
ATOM   3374  C  C   . SER   B 2 97  ? 46.706  55.387  17.337  1.00 139.21 ? 97   SER   B C   1 
ATOM   3375  O  O   . SER   B 2 97  ? 46.928  54.280  17.842  1.00 142.55 ? 97   SER   B O   1 
ATOM   3376  C  CB  . SER   B 2 97  ? 49.045  56.205  17.780  1.00 136.48 ? 97   SER   B CB  1 
ATOM   3377  O  OG  . SER   B 2 97  ? 49.796  57.178  18.485  1.00 135.62 ? 97   SER   B OG  1 
ATOM   3378  N  N   . ILE   B 2 98  ? 45.753  55.596  16.422  1.00 142.88 ? 98   ILE   B N   1 
ATOM   3379  C  CA  . ILE   B 2 98  ? 44.818  54.558  15.989  1.00 142.24 ? 98   ILE   B CA  1 
ATOM   3380  C  C   . ILE   B 2 98  ? 45.277  53.955  14.668  1.00 145.01 ? 98   ILE   B C   1 
ATOM   3381  O  O   . ILE   B 2 98  ? 45.582  54.682  13.716  1.00 141.45 ? 98   ILE   B O   1 
ATOM   3382  C  CB  . ILE   B 2 98  ? 43.392  55.106  15.845  1.00 133.07 ? 98   ILE   B CB  1 
ATOM   3383  C  CG1 . ILE   B 2 98  ? 42.937  55.799  17.119  1.00 136.57 ? 98   ILE   B CG1 1 
ATOM   3384  C  CG2 . ILE   B 2 98  ? 42.444  53.976  15.560  1.00 129.92 ? 98   ILE   B CG2 1 
ATOM   3385  C  CD1 . ILE   B 2 98  ? 41.435  56.090  17.109  1.00 127.18 ? 98   ILE   B CD1 1 
ATOM   3386  N  N   . ASP   B 2 99  ? 45.286  52.623  14.602  1.00 158.53 ? 99   ASP   B N   1 
ATOM   3387  C  CA  . ASP   B 2 99  ? 45.673  51.915  13.387  1.00 159.59 ? 99   ASP   B CA  1 
ATOM   3388  C  C   . ASP   B 2 99  ? 44.958  50.566  13.271  1.00 157.28 ? 99   ASP   B C   1 
ATOM   3389  O  O   . ASP   B 2 99  ? 44.903  49.808  14.244  1.00 156.53 ? 99   ASP   B O   1 
ATOM   3390  C  CB  . ASP   B 2 99  ? 47.194  51.730  13.350  1.00 163.39 ? 99   ASP   B CB  1 
ATOM   3391  C  CG  . ASP   B 2 99  ? 47.788  52.196  12.039  1.00 171.53 ? 99   ASP   B CG  1 
ATOM   3392  O  OD1 . ASP   B 2 99  ? 47.135  51.974  10.983  1.00 169.40 ? 99   ASP   B OD1 1 
ATOM   3393  O  OD2 . ASP   B 2 99  ? 48.891  52.794  12.065  1.00 171.82 ? 99   ASP   B OD2 1 
ATOM   3394  N  N   . ILE   B 2 100 ? 44.421  50.281  12.080  1.00 138.76 ? 100  ILE   B N   1 
ATOM   3395  C  CA  . ILE   B 2 100 ? 43.655  49.062  11.803  1.00 125.37 ? 100  ILE   B CA  1 
ATOM   3396  C  C   . ILE   B 2 100 ? 44.633  48.039  11.239  1.00 123.70 ? 100  ILE   B C   1 
ATOM   3397  O  O   . ILE   B 2 100 ? 44.960  48.055  10.053  1.00 121.60 ? 100  ILE   B O   1 
ATOM   3398  C  CB  . ILE   B 2 100 ? 42.499  49.311  10.838  1.00 118.44 ? 100  ILE   B CB  1 
ATOM   3399  C  CG1 . ILE   B 2 100 ? 41.468  50.257  11.447  1.00 117.73 ? 100  ILE   B CG1 1 
ATOM   3400  C  CG2 . ILE   B 2 100 ? 41.801  48.016  10.484  1.00 110.24 ? 100  ILE   B CG2 1 
ATOM   3401  C  CD1 . ILE   B 2 100 ? 40.678  49.622  12.575  1.00 112.11 ? 100  ILE   B CD1 1 
ATOM   3402  N  N   . ILE   B 2 101 ? 45.091  47.138  12.083  1.00 118.00 ? 101  ILE   B N   1 
ATOM   3403  C  CA  . ILE   B 2 101 ? 46.139  46.204  11.690  1.00 113.47 ? 101  ILE   B CA  1 
ATOM   3404  C  C   . ILE   B 2 101 ? 45.533  45.048  10.923  1.00 110.23 ? 101  ILE   B C   1 
ATOM   3405  O  O   . ILE   B 2 101 ? 44.417  44.595  11.199  1.00 110.40 ? 101  ILE   B O   1 
ATOM   3406  C  CB  . ILE   B 2 101 ? 46.917  45.697  12.913  1.00 111.73 ? 101  ILE   B CB  1 
ATOM   3407  C  CG1 . ILE   B 2 101 ? 46.030  44.753  13.714  1.00 112.66 ? 101  ILE   B CG1 1 
ATOM   3408  C  CG2 . ILE   B 2 101 ? 47.339  46.855  13.778  1.00 119.19 ? 101  ILE   B CG2 1 
ATOM   3409  C  CD1 . ILE   B 2 101 ? 46.729  44.071  14.844  1.00 120.60 ? 101  ILE   B CD1 1 
ATOM   3410  N  N   . THR   B 2 102 ? 46.291  44.552  9.952   1.00 120.47 ? 102  THR   B N   1 
ATOM   3411  C  CA  . THR   B 2 102 ? 45.854  43.452  9.095   1.00 117.32 ? 102  THR   B CA  1 
ATOM   3412  C  C   . THR   B 2 102 ? 46.440  42.159  9.644   1.00 116.30 ? 102  THR   B C   1 
ATOM   3413  O  O   . THR   B 2 102 ? 47.594  41.819  9.369   1.00 117.49 ? 102  THR   B O   1 
ATOM   3414  C  CB  . THR   B 2 102 ? 46.278  43.683  7.651   1.00 117.62 ? 102  THR   B CB  1 
ATOM   3415  O  OG1 . THR   B 2 102 ? 46.086  45.066  7.336   1.00 121.35 ? 102  THR   B OG1 1 
ATOM   3416  C  CG2 . THR   B 2 102 ? 45.425  42.836  6.724   1.00 114.25 ? 102  THR   B CG2 1 
ATOM   3417  N  N   . ARG   B 2 103 ? 45.636  41.444  10.425  1.00 108.97 ? 103  ARG   B N   1 
ATOM   3418  C  CA  . ARG   B 2 103 ? 46.070  40.170  10.979  1.00 105.57 ? 103  ARG   B CA  1 
ATOM   3419  C  C   . ARG   B 2 103 ? 46.175  39.071  9.927   1.00 104.29 ? 103  ARG   B C   1 
ATOM   3420  O  O   . ARG   B 2 103 ? 46.935  38.120  10.123  1.00 106.89 ? 103  ARG   B O   1 
ATOM   3421  C  CB  . ARG   B 2 103 ? 45.109  39.748  12.090  1.00 102.22 ? 103  ARG   B CB  1 
ATOM   3422  C  CG  . ARG   B 2 103 ? 45.011  40.761  13.228  1.00 103.33 ? 103  ARG   B CG  1 
ATOM   3423  C  CD  . ARG   B 2 103 ? 45.854  40.326  14.426  1.00 108.29 ? 103  ARG   B CD  1 
ATOM   3424  N  NE  . ARG   B 2 103 ? 45.464  39.013  14.934  1.00 106.96 ? 103  ARG   B NE  1 
ATOM   3425  C  CZ  . ARG   B 2 103 ? 44.630  38.813  15.950  1.00 107.24 ? 103  ARG   B CZ  1 
ATOM   3426  N  NH1 . ARG   B 2 103 ? 44.102  39.824  16.622  1.00 111.07 ? 103  ARG   B NH1 1 
ATOM   3427  N  NH2 . ARG   B 2 103 ? 44.316  37.566  16.299  1.00 104.18 ? 103  ARG   B NH2 1 
ATOM   3428  N  N   . ALA   B 2 104 ? 45.439  39.177  8.819   1.00 105.98 ? 104  ALA   B N   1 
ATOM   3429  C  CA  . ALA   B 2 104 ? 45.437  38.157  7.777   1.00 106.02 ? 104  ALA   B CA  1 
ATOM   3430  C  C   . ALA   B 2 104 ? 44.987  38.785  6.466   1.00 104.50 ? 104  ALA   B C   1 
ATOM   3431  O  O   . ALA   B 2 104 ? 44.078  39.612  6.459   1.00 105.69 ? 104  ALA   B O   1 
ATOM   3432  C  CB  . ALA   B 2 104 ? 44.509  36.982  8.124   1.00 105.82 ? 104  ALA   B CB  1 
ATOM   3433  N  N   . HIS   B 2 105 ? 45.602  38.364  5.368   1.00 107.97 ? 105  HIS   B N   1 
ATOM   3434  C  CA  . HIS   B 2 105 ? 45.272  38.885  4.053   1.00 108.04 ? 105  HIS   B CA  1 
ATOM   3435  C  C   . HIS   B 2 105 ? 45.497  37.775  3.037   1.00 112.50 ? 105  HIS   B C   1 
ATOM   3436  O  O   . HIS   B 2 105 ? 46.218  36.806  3.298   1.00 113.84 ? 105  HIS   B O   1 
ATOM   3437  C  CB  . HIS   B 2 105 ? 46.136  40.095  3.702   1.00 108.66 ? 105  HIS   B CB  1 
ATOM   3438  C  CG  . HIS   B 2 105 ? 47.565  39.734  3.489   1.00 114.60 ? 105  HIS   B CG  1 
ATOM   3439  N  ND1 . HIS   B 2 105 ? 48.169  39.754  2.252   1.00 116.74 ? 105  HIS   B ND1 1 
ATOM   3440  C  CD2 . HIS   B 2 105 ? 48.489  39.256  4.353   1.00 118.82 ? 105  HIS   B CD2 1 
ATOM   3441  C  CE1 . HIS   B 2 105 ? 49.418  39.338  2.369   1.00 120.21 ? 105  HIS   B CE1 1 
ATOM   3442  N  NE2 . HIS   B 2 105 ? 49.638  39.030  3.635   1.00 124.18 ? 105  HIS   B NE2 1 
ATOM   3443  N  N   . GLY   B 2 106 ? 44.886  37.929  1.863   1.00 103.82 ? 106  GLY   B N   1 
ATOM   3444  C  CA  . GLY   B 2 106 ? 45.010  36.938  0.811   1.00 99.18  ? 106  GLY   B CA  1 
ATOM   3445  C  C   . GLY   B 2 106 ? 43.890  37.100  -0.189  1.00 98.17  ? 106  GLY   B C   1 
ATOM   3446  O  O   . GLY   B 2 106 ? 42.845  37.668  0.136   1.00 98.98  ? 106  GLY   B O   1 
ATOM   3447  N  N   . ASN   B 2 107 ? 44.092  36.612  -1.409  1.00 96.51  ? 107  ASN   B N   1 
ATOM   3448  C  CA  . ASN   B 2 107 ? 43.143  36.799  -2.501  1.00 90.22  ? 107  ASN   B CA  1 
ATOM   3449  C  C   . ASN   B 2 107 ? 42.438  35.484  -2.796  1.00 91.29  ? 107  ASN   B C   1 
ATOM   3450  O  O   . ASN   B 2 107 ? 42.999  34.609  -3.461  1.00 93.43  ? 107  ASN   B O   1 
ATOM   3451  C  CB  . ASN   B 2 107 ? 43.854  37.313  -3.739  1.00 87.68  ? 107  ASN   B CB  1 
ATOM   3452  C  CG  . ASN   B 2 107 ? 42.907  37.918  -4.716  1.00 88.50  ? 107  ASN   B CG  1 
ATOM   3453  O  OD1 . ASN   B 2 107 ? 42.182  37.212  -5.400  1.00 91.20  ? 107  ASN   B OD1 1 
ATOM   3454  N  ND2 . ASN   B 2 107 ? 42.884  39.240  -4.775  1.00 89.10  ? 107  ASN   B ND2 1 
ATOM   3455  N  N   . VAL   B 2 108 ? 41.193  35.367  -2.354  1.00 90.74  ? 108  VAL   B N   1 
ATOM   3456  C  CA  . VAL   B 2 108 ? 40.475  34.104  -2.461  1.00 91.88  ? 108  VAL   B CA  1 
ATOM   3457  C  C   . VAL   B 2 108 ? 40.047  33.769  -3.889  1.00 98.51  ? 108  VAL   B C   1 
ATOM   3458  O  O   . VAL   B 2 108 ? 39.517  32.680  -4.137  1.00 102.33 ? 108  VAL   B O   1 
ATOM   3459  C  CB  . VAL   B 2 108 ? 39.324  34.049  -1.444  1.00 86.88  ? 108  VAL   B CB  1 
ATOM   3460  C  CG1 . VAL   B 2 108 ? 39.898  33.938  -0.069  1.00 88.94  ? 108  VAL   B CG1 1 
ATOM   3461  C  CG2 . VAL   B 2 108 ? 38.434  35.259  -1.575  1.00 86.34  ? 108  VAL   B CG2 1 
ATOM   3462  N  N   . GLN   B 2 109 ? 40.288  34.668  -4.842  1.00 107.92 ? 109  GLN   B N   1 
ATOM   3463  C  CA  . GLN   B 2 109 ? 40.043  34.333  -6.246  1.00 111.54 ? 109  GLN   B CA  1 
ATOM   3464  C  C   . GLN   B 2 109 ? 40.531  32.934  -6.646  1.00 115.12 ? 109  GLN   B C   1 
ATOM   3465  O  O   . GLN   B 2 109 ? 41.649  32.526  -6.316  1.00 117.34 ? 109  GLN   B O   1 
ATOM   3466  C  CB  . GLN   B 2 109 ? 40.653  35.401  -7.167  1.00 113.63 ? 109  GLN   B CB  1 
ATOM   3467  C  CG  . GLN   B 2 109 ? 40.761  35.058  -8.652  1.00 119.18 ? 109  GLN   B CG  1 
ATOM   3468  C  CD  . GLN   B 2 109 ? 39.466  35.294  -9.419  1.00 125.07 ? 109  GLN   B CD  1 
ATOM   3469  O  OE1 . GLN   B 2 109 ? 38.762  34.344  -9.779  1.00 126.42 ? 109  GLN   B OE1 1 
ATOM   3470  N  NE2 . GLN   B 2 109 ? 39.161  36.564  -9.701  1.00 122.71 ? 109  GLN   B NE2 1 
ATOM   3471  N  N   . ASP   B 2 110 ? 39.668  32.197  -7.357  1.00 104.93 ? 110  ASP   B N   1 
ATOM   3472  C  CA  . ASP   B 2 110 ? 39.977  30.918  -7.988  1.00 103.36 ? 110  ASP   B CA  1 
ATOM   3473  C  C   . ASP   B 2 110 ? 40.026  31.131  -9.501  1.00 106.89 ? 110  ASP   B C   1 
ATOM   3474  O  O   . ASP   B 2 110 ? 39.037  31.591  -10.084 1.00 108.25 ? 110  ASP   B O   1 
ATOM   3475  C  CB  . ASP   B 2 110 ? 38.919  29.859  -7.650  1.00 103.24 ? 110  ASP   B CB  1 
ATOM   3476  C  CG  . ASP   B 2 110 ? 38.859  29.518  -6.182  1.00 101.20 ? 110  ASP   B CG  1 
ATOM   3477  O  OD1 . ASP   B 2 110 ? 39.898  29.059  -5.656  1.00 102.80 ? 110  ASP   B OD1 1 
ATOM   3478  O  OD2 . ASP   B 2 110 ? 37.768  29.683  -5.573  1.00 100.45 ? 110  ASP   B OD2 1 
ATOM   3479  N  N   . ARG   B 2 111 ? 41.154  30.766  -10.133 1.00 109.91 ? 111  ARG   B N   1 
ATOM   3480  C  CA  . ARG   B 2 111 ? 41.353  30.963  -11.568 1.00 108.13 ? 111  ARG   B CA  1 
ATOM   3481  C  C   . ARG   B 2 111 ? 40.134  30.519  -12.362 1.00 106.61 ? 111  ARG   B C   1 
ATOM   3482  O  O   . ARG   B 2 111 ? 39.524  31.304  -13.097 1.00 108.75 ? 111  ARG   B O   1 
ATOM   3483  C  CB  . ARG   B 2 111 ? 42.603  30.214  -12.049 1.00 104.14 ? 111  ARG   B CB  1 
ATOM   3484  N  N   . ILE   B 2 112 ? 39.727  29.295  -12.172 1.00 104.70 ? 112  ILE   B N   1 
ATOM   3485  C  CA  . ILE   B 2 112 ? 38.514  28.792  -12.805 1.00 108.05 ? 112  ILE   B CA  1 
ATOM   3486  C  C   . ILE   B 2 112 ? 37.334  28.941  -11.857 1.00 106.87 ? 112  ILE   B C   1 
ATOM   3487  O  O   . ILE   B 2 112 ? 37.440  28.683  -10.653 1.00 107.98 ? 112  ILE   B O   1 
ATOM   3488  C  CB  . ILE   B 2 112 ? 38.692  27.330  -13.235 1.00 108.01 ? 112  ILE   B CB  1 
ATOM   3489  C  CG1 . ILE   B 2 112 ? 37.366  26.772  -13.770 1.00 106.89 ? 112  ILE   B CG1 1 
ATOM   3490  C  CG2 . ILE   B 2 112 ? 39.262  26.515  -12.073 1.00 108.06 ? 112  ILE   B CG2 1 
ATOM   3491  C  CD1 . ILE   B 2 112 ? 36.841  27.516  -15.009 1.00 108.77 ? 112  ILE   B CD1 1 
ATOM   3492  N  N   . GLY   B 2 113 ? 36.194  29.326  -12.398 1.00 108.83 ? 113  GLY   B N   1 
ATOM   3493  C  CA  . GLY   B 2 113 ? 34.991  29.391  -11.605 1.00 106.07 ? 113  GLY   B CA  1 
ATOM   3494  C  C   . GLY   B 2 113 ? 33.900  30.148  -12.325 1.00 115.41 ? 113  GLY   B C   1 
ATOM   3495  O  O   . GLY   B 2 113 ? 34.176  30.989  -13.189 1.00 118.23 ? 113  GLY   B O   1 
ATOM   3496  N  N   . ARG   B 2 114 ? 32.653  29.834  -11.999 1.00 125.83 ? 114  ARG   B N   1 
ATOM   3497  C  CA  . ARG   B 2 114 ? 31.526  30.599  -12.519 1.00 129.89 ? 114  ARG   B CA  1 
ATOM   3498  C  C   . ARG   B 2 114 ? 31.053  31.527  -11.413 1.00 125.09 ? 114  ARG   B C   1 
ATOM   3499  O  O   . ARG   B 2 114 ? 30.491  31.050  -10.418 1.00 124.54 ? 114  ARG   B O   1 
ATOM   3500  C  CB  . ARG   B 2 114 ? 30.402  29.674  -12.986 1.00 130.63 ? 114  ARG   B CB  1 
ATOM   3501  C  CG  . ARG   B 2 114 ? 29.511  30.195  -14.123 1.00 128.88 ? 114  ARG   B CG  1 
ATOM   3502  C  CD  . ARG   B 2 114 ? 30.261  30.864  -15.299 1.00 137.83 ? 114  ARG   B CD  1 
ATOM   3503  N  NE  . ARG   B 2 114 ? 31.437  30.145  -15.791 1.00 144.28 ? 114  ARG   B NE  1 
ATOM   3504  C  CZ  . ARG   B 2 114 ? 31.469  29.381  -16.879 1.00 142.16 ? 114  ARG   B CZ  1 
ATOM   3505  N  NH1 . ARG   B 2 114 ? 30.380  29.149  -17.594 1.00 142.20 ? 114  ARG   B NH1 1 
ATOM   3506  N  NH2 . ARG   B 2 114 ? 32.625  28.837  -17.260 1.00 138.13 ? 114  ARG   B NH2 1 
ATOM   3507  N  N   . PRO   B 2 115 ? 31.294  32.828  -11.504 1.00 107.09 ? 115  PRO   B N   1 
ATOM   3508  C  CA  . PRO   B 2 115 ? 30.761  33.753  -10.498 1.00 98.72  ? 115  PRO   B CA  1 
ATOM   3509  C  C   . PRO   B 2 115 ? 29.292  33.509  -10.235 1.00 102.43 ? 115  PRO   B C   1 
ATOM   3510  O  O   . PRO   B 2 115 ? 28.478  33.480  -11.162 1.00 104.42 ? 115  PRO   B O   1 
ATOM   3511  C  CB  . PRO   B 2 115 ? 30.978  35.121  -11.134 1.00 98.22  ? 115  PRO   B CB  1 
ATOM   3512  C  CG  . PRO   B 2 115 ? 32.105  34.925  -12.072 1.00 102.64 ? 115  PRO   B CG  1 
ATOM   3513  C  CD  . PRO   B 2 115 ? 31.989  33.526  -12.594 1.00 109.63 ? 115  PRO   B CD  1 
ATOM   3514  N  N   . SER   B 2 116 ? 28.947  33.315  -8.968  1.00 99.93  ? 116  SER   B N   1 
ATOM   3515  C  CA  . SER   B 2 116 ? 27.577  32.978  -8.624  1.00 94.99  ? 116  SER   B CA  1 
ATOM   3516  C  C   . SER   B 2 116 ? 26.655  34.156  -8.869  1.00 98.82  ? 116  SER   B C   1 
ATOM   3517  O  O   . SER   B 2 116 ? 27.042  35.324  -8.721  1.00 97.01  ? 116  SER   B O   1 
ATOM   3518  C  CB  . SER   B 2 116 ? 27.480  32.564  -7.165  1.00 93.43  ? 116  SER   B CB  1 
ATOM   3519  O  OG  . SER   B 2 116 ? 27.893  31.232  -6.992  1.00 95.03  ? 116  SER   B OG  1 
ATOM   3520  N  N   . GLU   B 2 117 ? 25.411  33.827  -9.220  1.00 98.07  ? 117  GLU   B N   1 
ATOM   3521  C  CA  . GLU   B 2 117 ? 24.404  34.845  -9.500  1.00 96.53  ? 117  GLU   B CA  1 
ATOM   3522  C  C   . GLU   B 2 117 ? 24.120  35.705  -8.267  1.00 95.41  ? 117  GLU   B C   1 
ATOM   3523  O  O   . GLU   B 2 117 ? 24.322  36.925  -8.286  1.00 96.87  ? 117  GLU   B O   1 
ATOM   3524  C  CB  . GLU   B 2 117 ? 23.140  34.164  -10.012 1.00 100.99 ? 117  GLU   B CB  1 
ATOM   3525  C  CG  . GLU   B 2 117 ? 23.404  33.067  -11.017 1.00 103.96 ? 117  GLU   B CG  1 
ATOM   3526  C  CD  . GLU   B 2 117 ? 22.360  33.035  -12.129 1.00 118.17 ? 117  GLU   B CD  1 
ATOM   3527  O  OE1 . GLU   B 2 117 ? 21.414  33.858  -12.099 1.00 113.57 ? 117  GLU   B OE1 1 
ATOM   3528  O  OE2 . GLU   B 2 117 ? 22.489  32.193  -13.046 1.00 126.45 ? 117  GLU   B OE2 1 
ATOM   3529  N  N   . THR   B 2 118 ? 23.662  35.072  -7.175  1.00 95.80  ? 118  THR   B N   1 
ATOM   3530  C  CA  . THR   B 2 118 ? 23.357  35.756  -5.917  1.00 96.48  ? 118  THR   B CA  1 
ATOM   3531  C  C   . THR   B 2 118 ? 24.593  36.358  -5.260  1.00 96.30  ? 118  THR   B C   1 
ATOM   3532  O  O   . THR   B 2 118 ? 24.466  37.022  -4.226  1.00 99.37  ? 118  THR   B O   1 
ATOM   3533  C  CB  . THR   B 2 118 ? 22.676  34.798  -4.942  1.00 94.63  ? 118  THR   B CB  1 
ATOM   3534  O  OG1 . THR   B 2 118 ? 23.608  33.783  -4.544  1.00 94.56  ? 118  THR   B OG1 1 
ATOM   3535  C  CG2 . THR   B 2 118 ? 21.471  34.141  -5.607  1.00 93.84  ? 118  THR   B CG2 1 
ATOM   3536  N  N   . GLY   B 2 119 ? 25.772  36.136  -5.815  1.00 92.35  ? 119  GLY   B N   1 
ATOM   3537  C  CA  . GLY   B 2 119 ? 26.920  36.957  -5.484  1.00 92.12  ? 119  GLY   B CA  1 
ATOM   3538  C  C   . GLY   B 2 119 ? 27.778  36.398  -4.363  1.00 88.18  ? 119  GLY   B C   1 
ATOM   3539  O  O   . GLY   B 2 119 ? 27.618  35.262  -3.913  1.00 86.15  ? 119  GLY   B O   1 
ATOM   3540  N  N   . ILE   B 2 120 ? 28.715  37.238  -3.910  1.00 85.60  ? 120  ILE   B N   1 
ATOM   3541  C  CA  . ILE   B 2 120 ? 29.689  36.808  -2.905  1.00 81.51  ? 120  ILE   B CA  1 
ATOM   3542  C  C   . ILE   B 2 120 ? 29.000  36.700  -1.552  1.00 82.57  ? 120  ILE   B C   1 
ATOM   3543  O  O   . ILE   B 2 120 ? 28.444  37.683  -1.057  1.00 86.45  ? 120  ILE   B O   1 
ATOM   3544  C  CB  . ILE   B 2 120 ? 30.867  37.785  -2.825  1.00 76.04  ? 120  ILE   B CB  1 
ATOM   3545  C  CG1 . ILE   B 2 120 ? 31.498  38.030  -4.194  1.00 77.94  ? 120  ILE   B CG1 1 
ATOM   3546  C  CG2 . ILE   B 2 120 ? 31.880  37.261  -1.871  1.00 78.72  ? 120  ILE   B CG2 1 
ATOM   3547  C  CD1 . ILE   B 2 120 ? 32.662  39.024  -4.170  1.00 74.54  ? 120  ILE   B CD1 1 
ATOM   3548  N  N   . ILE   B 2 121 ? 29.037  35.513  -0.937  1.00 82.22  ? 121  ILE   B N   1 
ATOM   3549  C  CA  . ILE   B 2 121 ? 28.466  35.300  0.395   1.00 79.62  ? 121  ILE   B CA  1 
ATOM   3550  C  C   . ILE   B 2 121 ? 29.593  34.962  1.366   1.00 80.01  ? 121  ILE   B C   1 
ATOM   3551  O  O   . ILE   B 2 121 ? 30.373  34.031  1.131   1.00 79.63  ? 121  ILE   B O   1 
ATOM   3552  C  CB  . ILE   B 2 121 ? 27.403  34.188  0.399   1.00 80.22  ? 121  ILE   B CB  1 
ATOM   3553  C  CG1 . ILE   B 2 121 ? 26.298  34.485  -0.608  1.00 80.62  ? 121  ILE   B CG1 1 
ATOM   3554  C  CG2 . ILE   B 2 121 ? 26.820  34.022  1.793   1.00 84.62  ? 121  ILE   B CG2 1 
ATOM   3555  C  CD1 . ILE   B 2 121 ? 25.109  33.562  -0.480  1.00 83.30  ? 121  ILE   B CD1 1 
ATOM   3556  N  N   . GLY   B 2 122 ? 29.687  35.723  2.449   1.00 81.61  ? 122  GLY   B N   1 
ATOM   3557  C  CA  . GLY   B 2 122 ? 30.671  35.439  3.471   1.00 79.45  ? 122  GLY   B CA  1 
ATOM   3558  C  C   . GLY   B 2 122 ? 29.974  35.074  4.757   1.00 79.82  ? 122  GLY   B C   1 
ATOM   3559  O  O   . GLY   B 2 122 ? 29.108  35.826  5.217   1.00 82.74  ? 122  GLY   B O   1 
ATOM   3560  N  N   . ILE   B 2 123 ? 30.307  33.910  5.321   1.00 80.60  ? 123  ILE   B N   1 
ATOM   3561  C  CA  . ILE   B 2 123 ? 29.730  33.448  6.581   1.00 85.05  ? 123  ILE   B CA  1 
ATOM   3562  C  C   . ILE   B 2 123 ? 30.849  32.924  7.474   1.00 87.75  ? 123  ILE   B C   1 
ATOM   3563  O  O   . ILE   B 2 123 ? 31.904  32.484  7.002   1.00 87.74  ? 123  ILE   B O   1 
ATOM   3564  C  CB  . ILE   B 2 123 ? 28.627  32.369  6.373   1.00 85.25  ? 123  ILE   B CB  1 
ATOM   3565  C  CG1 . ILE   B 2 123 ? 29.130  31.221  5.483   1.00 82.49  ? 123  ILE   B CG1 1 
ATOM   3566  C  CG2 . ILE   B 2 123 ? 27.351  33.003  5.800   1.00 83.77  ? 123  ILE   B CG2 1 
ATOM   3567  C  CD1 . ILE   B 2 123 ? 28.121  30.092  5.245   1.00 79.64  ? 123  ILE   B CD1 1 
ATOM   3568  N  N   . ILE   B 2 124 ? 30.631  33.007  8.780   1.00 89.68  ? 124  ILE   B N   1 
ATOM   3569  C  CA  . ILE   B 2 124 ? 31.616  32.550  9.742   1.00 95.61  ? 124  ILE   B CA  1 
ATOM   3570  C  C   . ILE   B 2 124 ? 30.928  31.635  10.738  1.00 108.48 ? 124  ILE   B C   1 
ATOM   3571  O  O   . ILE   B 2 124 ? 29.787  31.886  11.138  1.00 107.81 ? 124  ILE   B O   1 
ATOM   3572  C  CB  . ILE   B 2 124 ? 32.317  33.730  10.432  1.00 92.55  ? 124  ILE   B CB  1 
ATOM   3573  C  CG1 . ILE   B 2 124 ? 33.126  34.493  9.391   1.00 85.46  ? 124  ILE   B CG1 1 
ATOM   3574  C  CG2 . ILE   B 2 124 ? 33.254  33.232  11.499  1.00 101.46 ? 124  ILE   B CG2 1 
ATOM   3575  C  CD1 . ILE   B 2 124 ? 33.710  35.778  9.856   1.00 79.81  ? 124  ILE   B CD1 1 
ATOM   3576  N  N   . ASP   B 2 125 ? 31.619  30.557  11.108  1.00 130.81 ? 125  ASP   B N   1 
ATOM   3577  C  CA  . ASP   B 2 125 ? 31.069  29.547  12.004  1.00 132.03 ? 125  ASP   B CA  1 
ATOM   3578  C  C   . ASP   B 2 125 ? 30.549  30.208  13.285  1.00 132.50 ? 125  ASP   B C   1 
ATOM   3579  O  O   . ASP   B 2 125 ? 31.101  31.232  13.717  1.00 133.10 ? 125  ASP   B O   1 
ATOM   3580  C  CB  . ASP   B 2 125 ? 32.160  28.505  12.309  1.00 132.23 ? 125  ASP   B CB  1 
ATOM   3581  C  CG  . ASP   B 2 125 ? 31.636  27.278  13.031  1.00 136.86 ? 125  ASP   B CG  1 
ATOM   3582  O  OD1 . ASP   B 2 125 ? 31.160  26.334  12.353  1.00 138.82 ? 125  ASP   B OD1 1 
ATOM   3583  O  OD2 . ASP   B 2 125 ? 31.716  27.254  14.282  1.00 138.14 ? 125  ASP   B OD2 1 
ATOM   3584  N  N   . PRO   B 2 126 ? 29.463  29.697  13.892  1.00 121.18 ? 126  PRO   B N   1 
ATOM   3585  C  CA  . PRO   B 2 126 ? 29.001  30.317  15.145  1.00 118.71 ? 126  PRO   B CA  1 
ATOM   3586  C  C   . PRO   B 2 126 ? 30.066  30.268  16.218  1.00 121.28 ? 126  PRO   B C   1 
ATOM   3587  O  O   . PRO   B 2 126 ? 30.211  31.226  16.987  1.00 121.51 ? 126  PRO   B O   1 
ATOM   3588  C  CB  . PRO   B 2 126 ? 27.764  29.492  15.529  1.00 113.96 ? 126  PRO   B CB  1 
ATOM   3589  C  CG  . PRO   B 2 126 ? 27.365  28.770  14.334  1.00 112.23 ? 126  PRO   B CG  1 
ATOM   3590  C  CD  . PRO   B 2 126 ? 28.601  28.568  13.499  1.00 120.27 ? 126  PRO   B CD  1 
ATOM   3591  N  N   . GLU   B 2 127 ? 30.832  29.172  16.267  1.00 122.24 ? 127  GLU   B N   1 
ATOM   3592  C  CA  . GLU   B 2 127 ? 31.974  29.008  17.157  1.00 120.05 ? 127  GLU   B CA  1 
ATOM   3593  C  C   . GLU   B 2 127 ? 33.298  29.361  16.477  1.00 119.78 ? 127  GLU   B C   1 
ATOM   3594  O  O   . GLU   B 2 127 ? 34.344  28.806  16.835  1.00 116.36 ? 127  GLU   B O   1 
ATOM   3595  C  CB  . GLU   B 2 127 ? 32.007  27.579  17.686  1.00 118.89 ? 127  GLU   B CB  1 
ATOM   3596  C  CG  . GLU   B 2 127 ? 30.646  26.924  17.600  1.00 123.97 ? 127  GLU   B CG  1 
ATOM   3597  C  CD  . GLU   B 2 127 ? 30.606  25.553  18.233  1.00 135.59 ? 127  GLU   B CD  1 
ATOM   3598  O  OE1 . GLU   B 2 127 ? 31.690  24.972  18.470  1.00 137.23 ? 127  GLU   B OE1 1 
ATOM   3599  O  OE2 . GLU   B 2 127 ? 29.486  25.055  18.494  1.00 137.59 ? 127  GLU   B OE2 1 
ATOM   3600  N  N   . CYS   B 2 128 ? 33.250  30.261  15.487  1.00 120.48 ? 128  CYS   B N   1 
ATOM   3601  C  CA  . CYS   B 2 128 ? 34.414  30.822  14.786  1.00 112.47 ? 128  CYS   B CA  1 
ATOM   3602  C  C   . CYS   B 2 128 ? 35.467  29.775  14.453  1.00 109.49 ? 128  CYS   B C   1 
ATOM   3603  O  O   . CYS   B 2 128 ? 36.666  29.985  14.655  1.00 110.66 ? 128  CYS   B O   1 
ATOM   3604  C  CB  . CYS   B 2 128 ? 35.030  31.960  15.586  1.00 104.98 ? 128  CYS   B CB  1 
ATOM   3605  S  SG  . CYS   B 2 128 ? 33.857  33.286  15.913  1.00 106.98 ? 128  CYS   B SG  1 
ATOM   3606  N  N   . ARG   B 2 129 ? 35.022  28.644  13.909  1.00 109.40 ? 129  ARG   B N   1 
ATOM   3607  C  CA  . ARG   B 2 129 ? 35.951  27.578  13.569  1.00 107.88 ? 129  ARG   B CA  1 
ATOM   3608  C  C   . ARG   B 2 129 ? 36.392  27.574  12.103  1.00 109.46 ? 129  ARG   B C   1 
ATOM   3609  O  O   . ARG   B 2 129 ? 37.411  26.949  11.784  1.00 110.55 ? 129  ARG   B O   1 
ATOM   3610  C  CB  . ARG   B 2 129 ? 35.349  26.214  13.926  1.00 111.15 ? 129  ARG   B CB  1 
ATOM   3611  C  CG  . ARG   B 2 129 ? 36.373  25.318  14.614  1.00 112.54 ? 129  ARG   B CG  1 
ATOM   3612  C  CD  . ARG   B 2 129 ? 35.787  24.050  15.180  1.00 112.47 ? 129  ARG   B CD  1 
ATOM   3613  N  NE  . ARG   B 2 129 ? 35.860  23.014  14.161  1.00 122.18 ? 129  ARG   B NE  1 
ATOM   3614  C  CZ  . ARG   B 2 129 ? 35.425  21.767  14.304  1.00 124.58 ? 129  ARG   B CZ  1 
ATOM   3615  N  NH1 . ARG   B 2 129 ? 34.930  21.328  15.456  1.00 117.90 ? 129  ARG   B NH1 1 
ATOM   3616  N  NH2 . ARG   B 2 129 ? 35.464  20.947  13.254  1.00 121.66 ? 129  ARG   B NH2 1 
ATOM   3617  N  N   . MET   B 2 130 ? 35.653  28.234  11.205  1.00 108.93 ? 130  MET   B N   1 
ATOM   3618  C  CA  . MET   B 2 130 ? 36.110  28.461  9.839   1.00 97.55  ? 130  MET   B CA  1 
ATOM   3619  C  C   . MET   B 2 130 ? 35.341  29.636  9.260   1.00 96.35  ? 130  MET   B C   1 
ATOM   3620  O  O   . MET   B 2 130 ? 34.367  30.119  9.846   1.00 96.33  ? 130  MET   B O   1 
ATOM   3621  C  CB  . MET   B 2 130 ? 35.912  27.239  8.962   1.00 94.20  ? 130  MET   B CB  1 
ATOM   3622  C  CG  . MET   B 2 130 ? 34.494  27.151  8.438   1.00 96.65  ? 130  MET   B CG  1 
ATOM   3623  S  SD  . MET   B 2 130 ? 33.982  25.429  8.527   1.00 101.46 ? 130  MET   B SD  1 
ATOM   3624  C  CE  . MET   B 2 130 ? 34.174  25.184  10.287  1.00 108.27 ? 130  MET   B CE  1 
ATOM   3625  N  N   . ILE   B 2 131 ? 35.788  30.082  8.089   1.00 93.23  ? 131  ILE   B N   1 
ATOM   3626  C  CA  . ILE   B 2 131 ? 35.128  31.138  7.328   1.00 86.19  ? 131  ILE   B CA  1 
ATOM   3627  C  C   . ILE   B 2 131 ? 34.734  30.543  5.983   1.00 87.91  ? 131  ILE   B C   1 
ATOM   3628  O  O   . ILE   B 2 131 ? 35.603  30.217  5.164   1.00 93.25  ? 131  ILE   B O   1 
ATOM   3629  C  CB  . ILE   B 2 131 ? 36.042  32.350  7.125   1.00 82.86  ? 131  ILE   B CB  1 
ATOM   3630  C  CG1 . ILE   B 2 131 ? 36.284  33.079  8.432   1.00 83.82  ? 131  ILE   B CG1 1 
ATOM   3631  C  CG2 . ILE   B 2 131 ? 35.443  33.287  6.121   1.00 83.02  ? 131  ILE   B CG2 1 
ATOM   3632  C  CD1 . ILE   B 2 131 ? 36.825  34.464  8.217   1.00 82.36  ? 131  ILE   B CD1 1 
ATOM   3633  N  N   . GLY   B 2 132 ? 33.436  30.408  5.732   1.00 84.56  ? 132  GLY   B N   1 
ATOM   3634  C  CA  . GLY   B 2 132 ? 32.936  29.883  4.472   1.00 79.98  ? 132  GLY   B CA  1 
ATOM   3635  C  C   . GLY   B 2 132 ? 32.646  30.981  3.463   1.00 77.99  ? 132  GLY   B C   1 
ATOM   3636  O  O   . GLY   B 2 132 ? 31.990  31.969  3.773   1.00 80.94  ? 132  GLY   B O   1 
ATOM   3637  N  N   . LEU   B 2 133 ? 33.145  30.800  2.249   1.00 78.93  ? 133  LEU   B N   1 
ATOM   3638  C  CA  . LEU   B 2 133 ? 32.882  31.718  1.150   1.00 77.61  ? 133  LEU   B CA  1 
ATOM   3639  C  C   . LEU   B 2 133 ? 32.163  30.974  0.029   1.00 79.53  ? 133  LEU   B C   1 
ATOM   3640  O  O   . LEU   B 2 133 ? 32.560  29.864  -0.341  1.00 83.16  ? 133  LEU   B O   1 
ATOM   3641  C  CB  . LEU   B 2 133 ? 34.186  32.320  0.633   1.00 76.03  ? 133  LEU   B CB  1 
ATOM   3642  C  CG  . LEU   B 2 133 ? 34.996  33.042  1.690   1.00 75.00  ? 133  LEU   B CG  1 
ATOM   3643  C  CD1 . LEU   B 2 133 ? 36.310  33.451  1.082   1.00 75.28  ? 133  LEU   B CD1 1 
ATOM   3644  C  CD2 . LEU   B 2 133 ? 34.198  34.225  2.134   1.00 75.09  ? 133  LEU   B CD2 1 
ATOM   3645  N  N   . ARG   B 2 134 ? 31.101  31.566  -0.495  1.00 78.82  ? 134  ARG   B N   1 
ATOM   3646  C  CA  . ARG   B 2 134 ? 30.473  31.111  -1.732  1.00 81.99  ? 134  ARG   B CA  1 
ATOM   3647  C  C   . ARG   B 2 134 ? 30.762  32.198  -2.761  1.00 85.25  ? 134  ARG   B C   1 
ATOM   3648  O  O   . ARG   B 2 134 ? 29.986  33.142  -2.928  1.00 82.88  ? 134  ARG   B O   1 
ATOM   3649  C  CB  . ARG   B 2 134 ? 28.981  30.866  -1.574  1.00 78.09  ? 134  ARG   B CB  1 
ATOM   3650  C  CG  . ARG   B 2 134 ? 28.444  29.788  -2.504  1.00 84.79  ? 134  ARG   B CG  1 
ATOM   3651  C  CD  . ARG   B 2 134 ? 28.219  30.336  -3.878  1.00 88.61  ? 134  ARG   B CD  1 
ATOM   3652  N  NE  . ARG   B 2 134 ? 27.545  31.625  -3.788  1.00 88.44  ? 134  ARG   B NE  1 
ATOM   3653  C  CZ  . ARG   B 2 134 ? 26.270  31.832  -4.095  1.00 89.31  ? 134  ARG   B CZ  1 
ATOM   3654  N  NH1 . ARG   B 2 134 ? 25.491  30.846  -4.519  1.00 89.79  ? 134  ARG   B NH1 1 
ATOM   3655  N  NH2 . ARG   B 2 134 ? 25.771  33.063  -3.996  1.00 88.70  ? 134  ARG   B NH2 1 
ATOM   3656  N  N   . LEU   B 2 135 ? 31.899  32.064  -3.438  1.00 83.67  ? 135  LEU   B N   1 
ATOM   3657  C  CA  . LEU   B 2 135 ? 32.271  33.025  -4.460  1.00 84.49  ? 135  LEU   B CA  1 
ATOM   3658  C  C   . LEU   B 2 135 ? 31.731  32.614  -5.816  1.00 88.82  ? 135  LEU   B C   1 
ATOM   3659  O  O   . LEU   B 2 135 ? 31.297  33.468  -6.606  1.00 88.28  ? 135  LEU   B O   1 
ATOM   3660  C  CB  . LEU   B 2 135 ? 33.789  33.148  -4.531  1.00 84.70  ? 135  LEU   B CB  1 
ATOM   3661  C  CG  . LEU   B 2 135 ? 34.530  33.412  -3.234  1.00 82.27  ? 135  LEU   B CG  1 
ATOM   3662  C  CD1 . LEU   B 2 135 ? 36.002  33.458  -3.559  1.00 85.92  ? 135  LEU   B CD1 1 
ATOM   3663  C  CD2 . LEU   B 2 135 ? 34.080  34.717  -2.611  1.00 79.54  ? 135  LEU   B CD2 1 
ATOM   3664  N  N   . TYR   B 2 136 ? 31.757  31.308  -6.078  1.00 90.53  ? 136  TYR   B N   1 
ATOM   3665  C  CA  . TYR   B 2 136 ? 31.396  30.755  -7.366  1.00 93.03  ? 136  TYR   B CA  1 
ATOM   3666  C  C   . TYR   B 2 136 ? 30.421  29.608  -7.178  1.00 93.54  ? 136  TYR   B C   1 
ATOM   3667  O  O   . TYR   B 2 136 ? 30.241  29.079  -6.079  1.00 95.73  ? 136  TYR   B O   1 
ATOM   3668  C  CB  . TYR   B 2 136 ? 32.621  30.261  -8.131  1.00 96.60  ? 136  TYR   B CB  1 
ATOM   3669  C  CG  . TYR   B 2 136 ? 33.806  31.177  -8.084  1.00 95.93  ? 136  TYR   B CG  1 
ATOM   3670  C  CD1 . TYR   B 2 136 ? 33.909  32.246  -8.959  1.00 95.27  ? 136  TYR   B CD1 1 
ATOM   3671  C  CD2 . TYR   B 2 136 ? 34.840  30.953  -7.174  1.00 96.59  ? 136  TYR   B CD2 1 
ATOM   3672  C  CE1 . TYR   B 2 136 ? 34.999  33.080  -8.918  1.00 93.18  ? 136  TYR   B CE1 1 
ATOM   3673  C  CE2 . TYR   B 2 136 ? 35.928  31.778  -7.130  1.00 95.86  ? 136  TYR   B CE2 1 
ATOM   3674  C  CZ  . TYR   B 2 136 ? 36.000  32.838  -8.004  1.00 92.05  ? 136  TYR   B CZ  1 
ATOM   3675  O  OH  . TYR   B 2 136 ? 37.087  33.659  -7.957  1.00 99.12  ? 136  TYR   B OH  1 
ATOM   3676  N  N   . ASP   B 2 137 ? 29.779  29.237  -8.277  1.00 95.19  ? 137  ASP   B N   1 
ATOM   3677  C  CA  . ASP   B 2 137 ? 28.800  28.169  -8.263  1.00 93.81  ? 137  ASP   B CA  1 
ATOM   3678  C  C   . ASP   B 2 137 ? 29.512  26.841  -8.402  1.00 95.19  ? 137  ASP   B C   1 
ATOM   3679  O  O   . ASP   B 2 137 ? 30.391  26.690  -9.249  1.00 96.67  ? 137  ASP   B O   1 
ATOM   3680  C  CB  . ASP   B 2 137 ? 27.787  28.366  -9.384  1.00 98.25  ? 137  ASP   B CB  1 
ATOM   3681  C  CG  . ASP   B 2 137 ? 26.670  29.338  -8.986  1.00 107.05 ? 137  ASP   B CG  1 
ATOM   3682  O  OD1 . ASP   B 2 137 ? 26.139  29.176  -7.848  1.00 109.03 ? 137  ASP   B OD1 1 
ATOM   3683  O  OD2 . ASP   B 2 137 ? 26.328  30.260  -9.784  1.00 102.91 ? 137  ASP   B OD2 1 
ATOM   3684  N  N   . GLY   B 2 138 ? 29.169  25.898  -7.537  1.00 105.19 ? 138  GLY   B N   1 
ATOM   3685  C  CA  . GLY   B 2 138 ? 29.775  24.586  -7.535  1.00 107.04 ? 138  GLY   B CA  1 
ATOM   3686  C  C   . GLY   B 2 138 ? 30.851  24.373  -6.494  1.00 105.09 ? 138  GLY   B C   1 
ATOM   3687  O  O   . GLY   B 2 138 ? 31.456  23.289  -6.468  1.00 104.45 ? 138  GLY   B O   1 
ATOM   3688  N  N   . LEU   B 2 139 ? 31.087  25.356  -5.624  1.00 101.88 ? 139  LEU   B N   1 
ATOM   3689  C  CA  . LEU   B 2 139 ? 32.275  25.393  -4.778  1.00 100.78 ? 139  LEU   B CA  1 
ATOM   3690  C  C   . LEU   B 2 139 ? 32.035  26.241  -3.524  1.00 96.75  ? 139  LEU   B C   1 
ATOM   3691  O  O   . LEU   B 2 139 ? 31.203  27.158  -3.517  1.00 93.06  ? 139  LEU   B O   1 
ATOM   3692  C  CB  . LEU   B 2 139 ? 33.471  25.940  -5.567  1.00 102.31 ? 139  LEU   B CB  1 
ATOM   3693  C  CG  . LEU   B 2 139 ? 34.097  24.966  -6.552  1.00 102.39 ? 139  LEU   B CG  1 
ATOM   3694  C  CD1 . LEU   B 2 139 ? 35.060  25.700  -7.454  1.00 101.16 ? 139  LEU   B CD1 1 
ATOM   3695  C  CD2 . LEU   B 2 139 ? 34.771  23.840  -5.775  1.00 102.58 ? 139  LEU   B CD2 1 
ATOM   3696  N  N   . PHE   B 2 140 ? 32.820  25.941  -2.481  1.00 91.71  ? 140  PHE   B N   1 
ATOM   3697  C  CA  . PHE   B 2 140 ? 32.643  26.568  -1.167  1.00 88.59  ? 140  PHE   B CA  1 
ATOM   3698  C  C   . PHE   B 2 140 ? 34.016  26.653  -0.498  1.00 89.28  ? 140  PHE   B C   1 
ATOM   3699  O  O   . PHE   B 2 140 ? 34.473  25.668  0.085   1.00 94.39  ? 140  PHE   B O   1 
ATOM   3700  C  CB  . PHE   B 2 140 ? 31.656  25.759  -0.331  1.00 87.26  ? 140  PHE   B CB  1 
ATOM   3701  C  CG  . PHE   B 2 140 ? 31.273  26.395  0.986   1.00 82.95  ? 140  PHE   B CG  1 
ATOM   3702  C  CD1 . PHE   B 2 140 ? 30.536  27.562  1.019   1.00 81.08  ? 140  PHE   B CD1 1 
ATOM   3703  C  CD2 . PHE   B 2 140 ? 31.599  25.786  2.193   1.00 83.86  ? 140  PHE   B CD2 1 
ATOM   3704  C  CE1 . PHE   B 2 140 ? 30.153  28.132  2.225   1.00 80.07  ? 140  PHE   B CE1 1 
ATOM   3705  C  CE2 . PHE   B 2 140 ? 31.218  26.353  3.395   1.00 80.01  ? 140  PHE   B CE2 1 
ATOM   3706  C  CZ  . PHE   B 2 140 ? 30.491  27.530  3.407   1.00 78.03  ? 140  PHE   B CZ  1 
ATOM   3707  N  N   . LYS   B 2 141 ? 34.662  27.820  -0.587  1.00 88.71  ? 141  LYS   B N   1 
ATOM   3708  C  CA  . LYS   B 2 141 ? 35.981  28.010  0.015   1.00 87.76  ? 141  LYS   B CA  1 
ATOM   3709  C  C   . LYS   B 2 141 ? 35.878  27.985  1.540   1.00 87.05  ? 141  LYS   B C   1 
ATOM   3710  O  O   . LYS   B 2 141 ? 34.940  28.525  2.131   1.00 84.66  ? 141  LYS   B O   1 
ATOM   3711  C  CB  . LYS   B 2 141 ? 36.609  29.323  -0.471  1.00 83.32  ? 141  LYS   B CB  1 
ATOM   3712  C  CG  . LYS   B 2 141 ? 37.955  29.156  -1.168  1.00 85.31  ? 141  LYS   B CG  1 
ATOM   3713  C  CD  . LYS   B 2 141 ? 38.365  30.406  -1.935  1.00 85.12  ? 141  LYS   B CD  1 
ATOM   3714  C  CE  . LYS   B 2 141 ? 39.658  30.206  -2.716  1.00 87.60  ? 141  LYS   B CE  1 
ATOM   3715  N  NZ  . LYS   B 2 141 ? 40.887  30.199  -1.861  1.00 91.64  ? 141  LYS   B NZ  1 
ATOM   3716  N  N   . VAL   B 2 142 ? 36.832  27.331  2.180   1.00 87.08  ? 142  VAL   B N   1 
ATOM   3717  C  CA  . VAL   B 2 142 ? 36.810  27.181  3.622   1.00 88.79  ? 142  VAL   B CA  1 
ATOM   3718  C  C   . VAL   B 2 142 ? 38.153  27.669  4.125   1.00 92.45  ? 142  VAL   B C   1 
ATOM   3719  O  O   . VAL   B 2 142 ? 39.170  26.987  3.973   1.00 92.27  ? 142  VAL   B O   1 
ATOM   3720  C  CB  . VAL   B 2 142 ? 36.531  25.740  4.054   1.00 87.84  ? 142  VAL   B CB  1 
ATOM   3721  C  CG1 . VAL   B 2 142 ? 36.542  25.641  5.568   1.00 92.29  ? 142  VAL   B CG1 1 
ATOM   3722  C  CG2 . VAL   B 2 142 ? 35.206  25.308  3.522   1.00 89.73  ? 142  VAL   B CG2 1 
ATOM   3723  N  N   . ILE   B 2 143 ? 38.172  28.879  4.667   1.00 92.21  ? 143  ILE   B N   1 
ATOM   3724  C  CA  . ILE   B 2 143 ? 39.331  29.330  5.424   1.00 92.74  ? 143  ILE   B CA  1 
ATOM   3725  C  C   . ILE   B 2 143 ? 39.199  28.729  6.811   1.00 94.75  ? 143  ILE   B C   1 
ATOM   3726  O  O   . ILE   B 2 143 ? 38.288  29.107  7.560   1.00 95.37  ? 143  ILE   B O   1 
ATOM   3727  C  CB  . ILE   B 2 143 ? 39.425  30.854  5.523   1.00 91.80  ? 143  ILE   B CB  1 
ATOM   3728  C  CG1 . ILE   B 2 143 ? 39.135  31.518  4.195   1.00 90.78  ? 143  ILE   B CG1 1 
ATOM   3729  C  CG2 . ILE   B 2 143 ? 40.820  31.241  5.967   1.00 93.62  ? 143  ILE   B CG2 1 
ATOM   3730  C  CD1 . ILE   B 2 143 ? 39.518  32.964  4.234   1.00 92.87  ? 143  ILE   B CD1 1 
ATOM   3731  N  N   . PRO   B 2 144 ? 40.051  27.793  7.198   1.00 97.20  ? 144  PRO   B N   1 
ATOM   3732  C  CA  . PRO   B 2 144 ? 39.966  27.274  8.565   1.00 102.95 ? 144  PRO   B CA  1 
ATOM   3733  C  C   . PRO   B 2 144 ? 40.449  28.337  9.533   1.00 104.17 ? 144  PRO   B C   1 
ATOM   3734  O  O   . PRO   B 2 144 ? 41.505  28.943  9.329   1.00 100.85 ? 144  PRO   B O   1 
ATOM   3735  C  CB  . PRO   B 2 144 ? 40.888  26.053  8.552   1.00 108.69 ? 144  PRO   B CB  1 
ATOM   3736  C  CG  . PRO   B 2 144 ? 41.147  25.760  7.079   1.00 104.51 ? 144  PRO   B CG  1 
ATOM   3737  C  CD  . PRO   B 2 144 ? 41.055  27.086  6.394   1.00 99.91  ? 144  PRO   B CD  1 
ATOM   3738  N  N   . LEU   B 2 145 ? 39.662  28.563  10.581  1.00 106.56 ? 145  LEU   B N   1 
ATOM   3739  C  CA  . LEU   B 2 145 ? 39.910  29.629  11.536  1.00 104.57 ? 145  LEU   B CA  1 
ATOM   3740  C  C   . LEU   B 2 145 ? 40.691  29.143  12.753  1.00 115.88 ? 145  LEU   B C   1 
ATOM   3741  O  O   . LEU   B 2 145 ? 41.383  29.931  13.408  1.00 124.86 ? 145  LEU   B O   1 
ATOM   3742  C  CB  . LEU   B 2 145 ? 38.592  30.210  12.009  1.00 103.13 ? 145  LEU   B CB  1 
ATOM   3743  C  CG  . LEU   B 2 145 ? 38.052  31.288  11.088  1.00 100.69 ? 145  LEU   B CG  1 
ATOM   3744  C  CD1 . LEU   B 2 145 ? 36.905  31.985  11.775  1.00 101.01 ? 145  LEU   B CD1 1 
ATOM   3745  C  CD2 . LEU   B 2 145 ? 39.142  32.265  10.717  1.00 93.93  ? 145  LEU   B CD2 1 
ATOM   3746  N  N   . ASP   B 2 146 ? 40.560  27.871  13.102  1.00 123.39 ? 146  ASP   B N   1 
ATOM   3747  C  CA  . ASP   B 2 146 ? 41.440  27.273  14.107  1.00 124.31 ? 146  ASP   B CA  1 
ATOM   3748  C  C   . ASP   B 2 146 ? 42.921  27.485  13.794  1.00 126.02 ? 146  ASP   B C   1 
ATOM   3749  O  O   . ASP   B 2 146 ? 43.338  27.192  12.682  1.00 132.00 ? 146  ASP   B O   1 
ATOM   3750  C  CB  . ASP   B 2 146 ? 41.182  25.770  14.208  1.00 124.60 ? 146  ASP   B CB  1 
ATOM   3751  C  CG  . ASP   B 2 146 ? 40.818  25.112  12.851  1.00 128.26 ? 146  ASP   B CG  1 
ATOM   3752  O  OD1 . ASP   B 2 146 ? 40.107  24.052  12.784  1.00 128.73 ? 146  ASP   B OD1 1 
ATOM   3753  O  OD2 . ASP   B 2 146 ? 41.270  25.685  11.831  1.00 128.18 ? 146  ASP   B OD2 1 
ATOM   3754  N  N   . ARG   B 2 147 ? 43.637  28.172  14.685  1.00 122.46 ? 147  ARG   B N   1 
ATOM   3755  C  CA  . ARG   B 2 147 ? 45.069  28.456  14.558  1.00 126.56 ? 147  ARG   B CA  1 
ATOM   3756  C  C   . ARG   B 2 147 ? 45.332  29.539  13.516  1.00 124.26 ? 147  ARG   B C   1 
ATOM   3757  O  O   . ARG   B 2 147 ? 44.524  29.752  12.623  1.00 124.53 ? 147  ARG   B O   1 
ATOM   3758  C  CB  . ARG   B 2 147 ? 45.838  27.142  14.370  1.00 125.89 ? 147  ARG   B CB  1 
ATOM   3759  N  N   . ASP   B 2 148 ? 46.474  30.105  13.440  1.00 126.09 ? 148  ASP   B N   1 
ATOM   3760  C  CA  . ASP   B 2 148 ? 46.723  31.390  12.786  1.00 123.95 ? 148  ASP   B CA  1 
ATOM   3761  C  C   . ASP   B 2 148 ? 46.768  31.106  11.304  1.00 125.00 ? 148  ASP   B C   1 
ATOM   3762  O  O   . ASP   B 2 148 ? 47.670  30.404  10.849  1.00 128.58 ? 148  ASP   B O   1 
ATOM   3763  C  CB  . ASP   B 2 148 ? 48.034  32.038  13.177  1.00 129.06 ? 148  ASP   B CB  1 
ATOM   3764  C  CG  . ASP   B 2 148 ? 47.925  32.765  14.473  1.00 143.05 ? 148  ASP   B CG  1 
ATOM   3765  O  OD1 . ASP   B 2 148 ? 47.071  32.356  15.296  1.00 144.70 ? 148  ASP   B OD1 1 
ATOM   3766  O  OD2 . ASP   B 2 148 ? 48.664  33.761  14.655  1.00 153.11 ? 148  ASP   B OD2 1 
ATOM   3767  N  N   . ASN   B 2 149 ? 45.816  31.638  10.550  1.00 113.96 ? 149  ASN   B N   1 
ATOM   3768  C  CA  . ASN   B 2 149 ? 45.845  31.444  9.106   1.00 107.58 ? 149  ASN   B CA  1 
ATOM   3769  C  C   . ASN   B 2 149 ? 46.175  32.765  8.419   1.00 105.40 ? 149  ASN   B C   1 
ATOM   3770  O  O   . ASN   B 2 149 ? 45.425  33.216  7.548   1.00 106.06 ? 149  ASN   B O   1 
ATOM   3771  C  CB  . ASN   B 2 149 ? 44.507  30.878  8.630   1.00 103.11 ? 149  ASN   B CB  1 
ATOM   3772  C  CG  . ASN   B 2 149 ? 44.594  30.187  7.281   1.00 102.77 ? 149  ASN   B CG  1 
ATOM   3773  O  OD1 . ASN   B 2 149 ? 45.524  30.405  6.486   1.00 101.89 ? 149  ASN   B OD1 1 
ATOM   3774  N  ND2 . ASN   B 2 149 ? 43.584  29.361  7.002   1.00 100.67 ? 149  ASN   B ND2 1 
ATOM   3775  N  N   . LYS   B 2 150 ? 47.308  33.371  8.805   1.00 106.48 ? 150  LYS   B N   1 
ATOM   3776  C  CA  . LYS   B 2 150 ? 47.677  34.713  8.348   1.00 104.50 ? 150  LYS   B CA  1 
ATOM   3777  C  C   . LYS   B 2 150 ? 47.567  34.870  6.825   1.00 106.28 ? 150  LYS   B C   1 
ATOM   3778  O  O   . LYS   B 2 150 ? 47.177  35.933  6.328   1.00 106.44 ? 150  LYS   B O   1 
ATOM   3779  C  CB  . LYS   B 2 150 ? 49.092  35.055  8.842   1.00 96.70  ? 150  LYS   B CB  1 
ATOM   3780  N  N   . GLU   B 2 151 ? 47.893  33.823  6.061   1.00 103.67 ? 151  GLU   B N   1 
ATOM   3781  C  CA  . GLU   B 2 151 ? 47.850  33.886  4.606   1.00 101.92 ? 151  GLU   B CA  1 
ATOM   3782  C  C   . GLU   B 2 151 ? 46.475  33.540  4.050   1.00 101.43 ? 151  GLU   B C   1 
ATOM   3783  O  O   . GLU   B 2 151 ? 46.267  33.618  2.832   1.00 102.18 ? 151  GLU   B O   1 
ATOM   3784  C  CB  . GLU   B 2 151 ? 48.911  32.954  4.015   1.00 105.24 ? 151  GLU   B CB  1 
ATOM   3785  C  CG  . GLU   B 2 151 ? 50.303  33.116  4.642   1.00 109.65 ? 151  GLU   B CG  1 
ATOM   3786  C  CD  . GLU   B 2 151 ? 51.034  34.383  4.198   1.00 120.99 ? 151  GLU   B CD  1 
ATOM   3787  O  OE1 . GLU   B 2 151 ? 51.610  34.374  3.086   1.00 132.89 ? 151  GLU   B OE1 1 
ATOM   3788  O  OE2 . GLU   B 2 151 ? 51.043  35.385  4.959   1.00 122.44 ? 151  GLU   B OE2 1 
ATOM   3789  N  N   . LEU   B 2 152 ? 45.534  33.167  4.922   1.00 100.88 ? 152  LEU   B N   1 
ATOM   3790  C  CA  . LEU   B 2 152 ? 44.174  32.804  4.533   1.00 97.80  ? 152  LEU   B CA  1 
ATOM   3791  C  C   . LEU   B 2 152 ? 44.195  31.622  3.567   1.00 97.37  ? 152  LEU   B C   1 
ATOM   3792  O  O   . LEU   B 2 152 ? 43.640  31.666  2.462   1.00 97.23  ? 152  LEU   B O   1 
ATOM   3793  C  CB  . LEU   B 2 152 ? 43.428  34.004  3.947   1.00 97.53  ? 152  LEU   B CB  1 
ATOM   3794  C  CG  . LEU   B 2 152 ? 43.271  35.148  4.947   1.00 97.07  ? 152  LEU   B CG  1 
ATOM   3795  C  CD1 . LEU   B 2 152 ? 42.524  36.307  4.317   1.00 98.45  ? 152  LEU   B CD1 1 
ATOM   3796  C  CD2 . LEU   B 2 152 ? 42.546  34.634  6.166   1.00 92.37  ? 152  LEU   B CD2 1 
ATOM   3797  N  N   . LYS   B 2 153 ? 44.887  30.566  3.992   1.00 96.88  ? 153  LYS   B N   1 
ATOM   3798  C  CA  . LYS   B 2 153 ? 44.842  29.295  3.294   1.00 93.55  ? 153  LYS   B CA  1 
ATOM   3799  C  C   . LYS   B 2 153 ? 43.421  28.747  3.333   1.00 93.06  ? 153  LYS   B C   1 
ATOM   3800  O  O   . LYS   B 2 153 ? 42.753  28.796  4.366   1.00 96.51  ? 153  LYS   B O   1 
ATOM   3801  C  CB  . LYS   B 2 153 ? 45.824  28.323  3.949   1.00 91.45  ? 153  LYS   B CB  1 
ATOM   3802  N  N   . ALA   B 2 154 ? 42.936  28.253  2.192   1.00 94.58  ? 154  ALA   B N   1 
ATOM   3803  C  CA  . ALA   B 2 154 ? 41.580  27.721  2.117   1.00 92.84  ? 154  ALA   B CA  1 
ATOM   3804  C  C   . ALA   B 2 154 ? 41.523  26.512  1.186   1.00 92.97  ? 154  ALA   B C   1 
ATOM   3805  O  O   . ALA   B 2 154 ? 42.311  26.384  0.243   1.00 90.54  ? 154  ALA   B O   1 
ATOM   3806  C  CB  . ALA   B 2 154 ? 40.579  28.779  1.637   1.00 89.28  ? 154  ALA   B CB  1 
ATOM   3807  N  N   . PHE   B 2 155 ? 40.556  25.640  1.450   1.00 92.43  ? 155  PHE   B N   1 
ATOM   3808  C  CA  . PHE   B 2 155 ? 40.220  24.541  0.561   1.00 90.06  ? 155  PHE   B CA  1 
ATOM   3809  C  C   . PHE   B 2 155 ? 38.810  24.759  0.033   1.00 91.98  ? 155  PHE   B C   1 
ATOM   3810  O  O   . PHE   B 2 155 ? 37.950  25.286  0.750   1.00 94.77  ? 155  PHE   B O   1 
ATOM   3811  C  CB  . PHE   B 2 155 ? 40.339  23.178  1.269   1.00 89.14  ? 155  PHE   B CB  1 
ATOM   3812  C  CG  . PHE   B 2 155 ? 39.518  23.040  2.534   1.00 83.61  ? 155  PHE   B CG  1 
ATOM   3813  C  CD1 . PHE   B 2 155 ? 40.028  23.442  3.746   1.00 89.06  ? 155  PHE   B CD1 1 
ATOM   3814  C  CD2 . PHE   B 2 155 ? 38.265  22.453  2.507   1.00 87.16  ? 155  PHE   B CD2 1 
ATOM   3815  C  CE1 . PHE   B 2 155 ? 39.294  23.290  4.907   1.00 94.62  ? 155  PHE   B CE1 1 
ATOM   3816  C  CE2 . PHE   B 2 155 ? 37.533  22.298  3.651   1.00 89.93  ? 155  PHE   B CE2 1 
ATOM   3817  C  CZ  . PHE   B 2 155 ? 38.045  22.710  4.854   1.00 95.20  ? 155  PHE   B CZ  1 
ATOM   3818  N  N   . ASN   B 2 156 ? 38.582  24.360  -1.224  1.00 88.99  ? 156  ASN   B N   1 
ATOM   3819  C  CA  . ASN   B 2 156 ? 37.324  24.605  -1.933  1.00 89.19  ? 156  ASN   B CA  1 
ATOM   3820  C  C   . ASN   B 2 156 ? 36.520  23.307  -1.994  1.00 92.61  ? 156  ASN   B C   1 
ATOM   3821  O  O   . ASN   B 2 156 ? 36.752  22.471  -2.869  1.00 97.15  ? 156  ASN   B O   1 
ATOM   3822  C  CB  . ASN   B 2 156 ? 37.600  25.141  -3.336  1.00 90.11  ? 156  ASN   B CB  1 
ATOM   3823  C  CG  . ASN   B 2 156 ? 37.091  26.563  -3.544  1.00 93.33  ? 156  ASN   B CG  1 
ATOM   3824  O  OD1 . ASN   B 2 156 ? 36.166  27.009  -2.865  1.00 95.23  ? 156  ASN   B OD1 1 
ATOM   3825  N  ND2 . ASN   B 2 156 ? 37.685  27.273  -4.505  1.00 93.00  ? 156  ASN   B ND2 1 
ATOM   3826  N  N   . ILE   B 2 157 ? 35.537  23.154  -1.094  1.00 98.98  ? 157  ILE   B N   1 
ATOM   3827  C  CA  . ILE   B 2 157 ? 34.696  21.961  -1.081  1.00 100.39 ? 157  ILE   B CA  1 
ATOM   3828  C  C   . ILE   B 2 157 ? 33.718  22.004  -2.251  1.00 100.87 ? 157  ILE   B C   1 
ATOM   3829  O  O   . ILE   B 2 157 ? 33.138  23.057  -2.568  1.00 98.57  ? 157  ILE   B O   1 
ATOM   3830  C  CB  . ILE   B 2 157 ? 33.963  21.817  0.265   1.00 103.97 ? 157  ILE   B CB  1 
ATOM   3831  C  CG1 . ILE   B 2 157 ? 34.959  21.703  1.412   1.00 106.14 ? 157  ILE   B CG1 1 
ATOM   3832  C  CG2 . ILE   B 2 157 ? 33.127  20.560  0.288   1.00 107.03 ? 157  ILE   B CG2 1 
ATOM   3833  C  CD1 . ILE   B 2 157 ? 34.297  21.357  2.756   1.00 109.19 ? 157  ILE   B CD1 1 
ATOM   3834  N  N   . ARG   B 2 158 ? 33.567  20.849  -2.914  1.00 100.28 ? 158  ARG   B N   1 
ATOM   3835  C  CA  . ARG   B 2 158 ? 32.689  20.701  -4.065  1.00 98.06  ? 158  ARG   B CA  1 
ATOM   3836  C  C   . ARG   B 2 158 ? 31.262  20.491  -3.590  1.00 101.49 ? 158  ARG   B C   1 
ATOM   3837  O  O   . ARG   B 2 158 ? 31.001  19.692  -2.682  1.00 100.98 ? 158  ARG   B O   1 
ATOM   3838  C  CB  . ARG   B 2 158 ? 33.131  19.520  -4.933  1.00 103.81 ? 158  ARG   B CB  1 
ATOM   3839  C  CG  . ARG   B 2 158 ? 34.419  19.707  -5.741  1.00 107.46 ? 158  ARG   B CG  1 
ATOM   3840  C  CD  . ARG   B 2 158 ? 34.192  19.216  -7.160  1.00 110.08 ? 158  ARG   B CD  1 
ATOM   3841  N  NE  . ARG   B 2 158 ? 32.979  19.832  -7.698  1.00 120.63 ? 158  ARG   B NE  1 
ATOM   3842  C  CZ  . ARG   B 2 158 ? 32.958  20.845  -8.558  1.00 116.71 ? 158  ARG   B CZ  1 
ATOM   3843  N  NH1 . ARG   B 2 158 ? 34.078  21.345  -9.063  1.00 112.38 ? 158  ARG   B NH1 1 
ATOM   3844  N  NH2 . ARG   B 2 158 ? 31.787  21.367  -8.919  1.00 107.58 ? 158  ARG   B NH2 1 
ATOM   3845  N  N   . LEU   B 2 159 ? 30.341  21.217  -4.211  1.00 104.83 ? 159  LEU   B N   1 
ATOM   3846  C  CA  . LEU   B 2 159 ? 28.941  21.277  -3.819  1.00 105.30 ? 159  LEU   B CA  1 
ATOM   3847  C  C   . LEU   B 2 159 ? 28.121  20.821  -5.016  1.00 108.06 ? 159  LEU   B C   1 
ATOM   3848  O  O   . LEU   B 2 159 ? 28.241  21.399  -6.104  1.00 109.96 ? 159  LEU   B O   1 
ATOM   3849  C  CB  . LEU   B 2 159 ? 28.580  22.709  -3.399  1.00 102.97 ? 159  LEU   B CB  1 
ATOM   3850  C  CG  . LEU   B 2 159 ? 27.562  22.997  -2.307  1.00 103.63 ? 159  LEU   B CG  1 
ATOM   3851  C  CD1 . LEU   B 2 159 ? 27.641  24.459  -2.027  1.00 99.69  ? 159  LEU   B CD1 1 
ATOM   3852  C  CD2 . LEU   B 2 159 ? 26.163  22.639  -2.755  1.00 108.82 ? 159  LEU   B CD2 1 
ATOM   3853  N  N   . GLU   B 2 160 ? 27.302  19.779  -4.826  1.00 109.36 ? 160  GLU   B N   1 
ATOM   3854  C  CA  . GLU   B 2 160 ? 26.571  19.207  -5.959  1.00 106.74 ? 160  GLU   B CA  1 
ATOM   3855  C  C   . GLU   B 2 160 ? 25.554  20.204  -6.518  1.00 102.96 ? 160  GLU   B C   1 
ATOM   3856  O  O   . GLU   B 2 160 ? 25.405  20.335  -7.744  1.00 97.22  ? 160  GLU   B O   1 
ATOM   3857  C  CB  . GLU   B 2 160 ? 25.892  17.894  -5.542  1.00 98.59  ? 160  GLU   B CB  1 
ATOM   3858  N  N   . GLU   B 2 161 ? 24.870  20.931  -5.627  1.00 104.34 ? 161  GLU   B N   1 
ATOM   3859  C  CA  . GLU   B 2 161 ? 23.823  21.883  -5.989  1.00 102.54 ? 161  GLU   B CA  1 
ATOM   3860  C  C   . GLU   B 2 161 ? 24.463  23.163  -6.506  1.00 102.91 ? 161  GLU   B C   1 
ATOM   3861  O  O   . GLU   B 2 161 ? 25.274  23.778  -5.810  1.00 102.11 ? 161  GLU   B O   1 
ATOM   3862  C  CB  . GLU   B 2 161 ? 22.951  22.186  -4.769  1.00 97.44  ? 161  GLU   B CB  1 
ATOM   3863  C  CG  . GLU   B 2 161 ? 22.135  21.020  -4.224  1.00 102.11 ? 161  GLU   B CG  1 
ATOM   3864  C  CD  . GLU   B 2 161 ? 22.959  19.898  -3.568  1.00 104.51 ? 161  GLU   B CD  1 
ATOM   3865  O  OE1 . GLU   B 2 161 ? 23.997  20.208  -2.942  1.00 102.96 ? 161  GLU   B OE1 1 
ATOM   3866  O  OE2 . GLU   B 2 161 ? 22.561  18.705  -3.682  1.00 105.97 ? 161  GLU   B OE2 1 
ATOM   3867  N  N   . LEU   B 2 162 ? 24.119  23.565  -7.725  1.00 105.31 ? 162  LEU   B N   1 
ATOM   3868  C  CA  . LEU   B 2 162 ? 24.864  24.622  -8.388  1.00 106.99 ? 162  LEU   B CA  1 
ATOM   3869  C  C   . LEU   B 2 162 ? 24.105  25.933  -8.429  1.00 110.30 ? 162  LEU   B C   1 
ATOM   3870  O  O   . LEU   B 2 162 ? 24.452  26.818  -9.213  1.00 111.38 ? 162  LEU   B O   1 
ATOM   3871  C  CB  . LEU   B 2 162 ? 25.239  24.202  -9.803  1.00 106.75 ? 162  LEU   B CB  1 
ATOM   3872  C  CG  . LEU   B 2 162 ? 25.846  22.807  -9.892  1.00 103.25 ? 162  LEU   B CG  1 
ATOM   3873  C  CD1 . LEU   B 2 162 ? 26.188  22.516  -11.315 1.00 101.63 ? 162  LEU   B CD1 1 
ATOM   3874  C  CD2 . LEU   B 2 162 ? 27.080  22.713  -9.026  1.00 105.29 ? 162  LEU   B CD2 1 
ATOM   3875  N  N   . HIS   B 2 163 ? 23.052  26.074  -7.634  1.00 116.79 ? 163  HIS   B N   1 
ATOM   3876  C  CA  . HIS   B 2 163 ? 22.199  27.240  -7.718  1.00 117.66 ? 163  HIS   B CA  1 
ATOM   3877  C  C   . HIS   B 2 163 ? 21.801  27.682  -6.325  1.00 119.05 ? 163  HIS   B C   1 
ATOM   3878  O  O   . HIS   B 2 163 ? 20.628  27.734  -5.982  1.00 123.82 ? 163  HIS   B O   1 
ATOM   3879  C  CB  . HIS   B 2 163 ? 20.946  26.971  -8.539  1.00 118.83 ? 163  HIS   B CB  1 
ATOM   3880  C  CG  . HIS   B 2 163 ? 21.213  26.718  -9.983  1.00 127.69 ? 163  HIS   B CG  1 
ATOM   3881  N  ND1 . HIS   B 2 163 ? 21.944  27.581  -10.770 1.00 131.49 ? 163  HIS   B ND1 1 
ATOM   3882  C  CD2 . HIS   B 2 163 ? 20.844  25.695  -10.789 1.00 131.64 ? 163  HIS   B CD2 1 
ATOM   3883  C  CE1 . HIS   B 2 163 ? 22.013  27.102  -12.000 1.00 134.21 ? 163  HIS   B CE1 1 
ATOM   3884  N  NE2 . HIS   B 2 163 ? 21.355  25.957  -12.039 1.00 138.12 ? 163  HIS   B NE2 1 
ATOM   3885  N  N   . VAL   B 2 164 ? 22.785  28.028  -5.519  1.00 102.73 ? 164  VAL   B N   1 
ATOM   3886  C  CA  . VAL   B 2 164 ? 22.518  28.414  -4.144  1.00 98.99  ? 164  VAL   B CA  1 
ATOM   3887  C  C   . VAL   B 2 164 ? 22.010  29.856  -4.093  1.00 96.01  ? 164  VAL   B C   1 
ATOM   3888  O  O   . VAL   B 2 164 ? 22.599  30.760  -4.698  1.00 95.36  ? 164  VAL   B O   1 
ATOM   3889  C  CB  . VAL   B 2 164 ? 23.779  28.227  -3.298  1.00 95.12  ? 164  VAL   B CB  1 
ATOM   3890  C  CG1 . VAL   B 2 164 ? 23.436  28.451  -1.854  1.00 94.30  ? 164  VAL   B CG1 1 
ATOM   3891  C  CG2 . VAL   B 2 164 ? 24.361  26.840  -3.544  1.00 96.25  ? 164  VAL   B CG2 1 
ATOM   3892  N  N   . ILE   B 2 165 ? 20.906  30.071  -3.373  1.00 93.35  ? 165  ILE   B N   1 
ATOM   3893  C  CA  . ILE   B 2 165 ? 20.320  31.398  -3.183  1.00 89.76  ? 165  ILE   B CA  1 
ATOM   3894  C  C   . ILE   B 2 165 ? 20.990  32.135  -2.015  1.00 91.87  ? 165  ILE   B C   1 
ATOM   3895  O  O   . ILE   B 2 165 ? 21.549  33.220  -2.203  1.00 95.09  ? 165  ILE   B O   1 
ATOM   3896  C  CB  . ILE   B 2 165 ? 18.799  31.291  -2.962  1.00 90.38  ? 165  ILE   B CB  1 
ATOM   3897  C  CG1 . ILE   B 2 165 ? 18.162  30.250  -3.881  1.00 89.63  ? 165  ILE   B CG1 1 
ATOM   3898  C  CG2 . ILE   B 2 165 ? 18.135  32.654  -3.145  1.00 94.04  ? 165  ILE   B CG2 1 
ATOM   3899  C  CD1 . ILE   B 2 165 ? 18.053  30.709  -5.281  1.00 94.00  ? 165  ILE   B CD1 1 
ATOM   3900  N  N   . ASP   B 2 166 ? 20.919  31.565  -0.799  1.00 90.88  ? 166  ASP   B N   1 
ATOM   3901  C  CA  . ASP   B 2 166 ? 21.470  32.147  0.431   1.00 89.69  ? 166  ASP   B CA  1 
ATOM   3902  C  C   . ASP   B 2 166 ? 21.862  31.020  1.385   1.00 83.97  ? 166  ASP   B C   1 
ATOM   3903  O  O   . ASP   B 2 166 ? 21.137  30.039  1.513   1.00 86.18  ? 166  ASP   B O   1 
ATOM   3904  C  CB  . ASP   B 2 166 ? 20.453  33.094  1.111   1.00 89.66  ? 166  ASP   B CB  1 
ATOM   3905  C  CG  . ASP   B 2 166 ? 21.033  33.850  2.317   1.00 87.95  ? 166  ASP   B CG  1 
ATOM   3906  O  OD1 . ASP   B 2 166 ? 22.023  34.607  2.156   1.00 84.74  ? 166  ASP   B OD1 1 
ATOM   3907  O  OD2 . ASP   B 2 166 ? 20.472  33.708  3.428   1.00 86.13  ? 166  ASP   B OD2 1 
ATOM   3908  N  N   . VAL   B 2 167 ? 23.007  31.164  2.051   1.00 85.22  ? 167  VAL   B N   1 
ATOM   3909  C  CA  . VAL   B 2 167 ? 23.536  30.140  2.948   1.00 85.90  ? 167  VAL   B CA  1 
ATOM   3910  C  C   . VAL   B 2 167 ? 23.980  30.797  4.243   1.00 85.53  ? 167  VAL   B C   1 
ATOM   3911  O  O   . VAL   B 2 167 ? 24.482  31.930  4.236   1.00 84.36  ? 167  VAL   B O   1 
ATOM   3912  C  CB  . VAL   B 2 167 ? 24.717  29.366  2.324   1.00 81.78  ? 167  VAL   B CB  1 
ATOM   3913  C  CG1 . VAL   B 2 167 ? 25.730  30.336  1.804   1.00 80.10  ? 167  VAL   B CG1 1 
ATOM   3914  C  CG2 . VAL   B 2 167 ? 25.378  28.475  3.352   1.00 80.47  ? 167  VAL   B CG2 1 
ATOM   3915  N  N   . LYS   B 2 168 ? 23.806  30.081  5.348   1.00 85.16  ? 168  LYS   B N   1 
ATOM   3916  C  CA  . LYS   B 2 168 ? 24.199  30.559  6.665   1.00 85.57  ? 168  LYS   B CA  1 
ATOM   3917  C  C   . LYS   B 2 168 ? 24.658  29.365  7.494   1.00 90.25  ? 168  LYS   B C   1 
ATOM   3918  O  O   . LYS   B 2 168 ? 24.165  28.247  7.310   1.00 93.87  ? 168  LYS   B O   1 
ATOM   3919  C  CB  . LYS   B 2 168 ? 23.031  31.291  7.361   1.00 80.59  ? 168  LYS   B CB  1 
ATOM   3920  C  CG  . LYS   B 2 168 ? 22.516  32.534  6.639   1.00 78.51  ? 168  LYS   B CG  1 
ATOM   3921  C  CD  . LYS   B 2 168 ? 23.186  33.806  7.142   1.00 77.85  ? 168  LYS   B CD  1 
ATOM   3922  C  CE  . LYS   B 2 168 ? 23.177  34.961  6.132   1.00 83.84  ? 168  LYS   B CE  1 
ATOM   3923  N  NZ  . LYS   B 2 168 ? 21.881  35.716  6.005   1.00 88.65  ? 168  LYS   B NZ  1 
ATOM   3924  N  N   . PHE   B 2 169 ? 25.614  29.594  8.401   1.00 89.35  ? 169  PHE   B N   1 
ATOM   3925  C  CA  . PHE   B 2 169 ? 26.012  28.561  9.354   1.00 91.29  ? 169  PHE   B CA  1 
ATOM   3926  C  C   . PHE   B 2 169 ? 24.944  28.419  10.430  1.00 92.86  ? 169  PHE   B C   1 
ATOM   3927  O  O   . PHE   B 2 169 ? 24.433  29.415  10.942  1.00 94.49  ? 169  PHE   B O   1 
ATOM   3928  C  CB  . PHE   B 2 169 ? 27.346  28.907  10.010  1.00 96.46  ? 169  PHE   B CB  1 
ATOM   3929  C  CG  . PHE   B 2 169 ? 28.556  28.434  9.250   1.00 99.70  ? 169  PHE   B CG  1 
ATOM   3930  C  CD1 . PHE   B 2 169 ? 28.929  27.100  9.272   1.00 101.08 ? 169  PHE   B CD1 1 
ATOM   3931  C  CD2 . PHE   B 2 169 ? 29.347  29.333  8.546   1.00 98.08  ? 169  PHE   B CD2 1 
ATOM   3932  C  CE1 . PHE   B 2 169 ? 30.047  26.675  8.586   1.00 97.53  ? 169  PHE   B CE1 1 
ATOM   3933  C  CE2 . PHE   B 2 169 ? 30.469  28.909  7.865   1.00 89.81  ? 169  PHE   B CE2 1 
ATOM   3934  C  CZ  . PHE   B 2 169 ? 30.812  27.583  7.884   1.00 88.82  ? 169  PHE   B CZ  1 
ATOM   3935  N  N   . LEU   B 2 170 ? 24.617  27.179  10.781  1.00 91.39  ? 170  LEU   B N   1 
ATOM   3936  C  CA  . LEU   B 2 170 ? 23.538  26.927  11.727  1.00 93.21  ? 170  LEU   B CA  1 
ATOM   3937  C  C   . LEU   B 2 170 ? 24.044  27.002  13.169  1.00 101.55 ? 170  LEU   B C   1 
ATOM   3938  O  O   . LEU   B 2 170 ? 25.227  26.779  13.450  1.00 104.15 ? 170  LEU   B O   1 
ATOM   3939  C  CB  . LEU   B 2 170 ? 22.911  25.561  11.454  1.00 92.40  ? 170  LEU   B CB  1 
ATOM   3940  C  CG  . LEU   B 2 170 ? 21.824  25.504  10.390  1.00 91.39  ? 170  LEU   B CG  1 
ATOM   3941  C  CD1 . LEU   B 2 170 ? 21.028  24.208  10.488  1.00 95.53  ? 170  LEU   B CD1 1 
ATOM   3942  C  CD2 . LEU   B 2 170 ? 20.931  26.688  10.595  1.00 90.78  ? 170  LEU   B CD2 1 
ATOM   3943  N  N   . TYR   B 2 171 ? 23.139  27.331  14.087  1.00 100.74 ? 171  TYR   B N   1 
ATOM   3944  C  CA  . TYR   B 2 171 ? 23.500  27.391  15.494  1.00 100.15 ? 171  TYR   B CA  1 
ATOM   3945  C  C   . TYR   B 2 171 ? 23.185  26.067  16.171  1.00 106.18 ? 171  TYR   B C   1 
ATOM   3946  O  O   . TYR   B 2 171 ? 22.543  25.185  15.597  1.00 108.50 ? 171  TYR   B O   1 
ATOM   3947  C  CB  . TYR   B 2 171 ? 22.750  28.512  16.193  1.00 97.26  ? 171  TYR   B CB  1 
ATOM   3948  C  CG  . TYR   B 2 171 ? 23.327  29.888  16.000  1.00 97.41  ? 171  TYR   B CG  1 
ATOM   3949  C  CD1 . TYR   B 2 171 ? 24.598  30.198  16.455  1.00 98.90  ? 171  TYR   B CD1 1 
ATOM   3950  C  CD2 . TYR   B 2 171 ? 22.581  30.899  15.395  1.00 98.82  ? 171  TYR   B CD2 1 
ATOM   3951  C  CE1 . TYR   B 2 171 ? 25.129  31.481  16.299  1.00 100.04 ? 171  TYR   B CE1 1 
ATOM   3952  C  CE2 . TYR   B 2 171 ? 23.091  32.187  15.242  1.00 95.84  ? 171  TYR   B CE2 1 
ATOM   3953  C  CZ  . TYR   B 2 171 ? 24.372  32.472  15.690  1.00 98.29  ? 171  TYR   B CZ  1 
ATOM   3954  O  OH  . TYR   B 2 171 ? 24.893  33.742  15.535  1.00 97.02  ? 171  TYR   B OH  1 
ATOM   3955  N  N   . GLY   B 2 172 ? 23.637  25.933  17.419  1.00 111.85 ? 172  GLY   B N   1 
ATOM   3956  C  CA  . GLY   B 2 172 ? 23.376  24.722  18.183  1.00 116.54 ? 172  GLY   B CA  1 
ATOM   3957  C  C   . GLY   B 2 172 ? 23.941  23.485  17.511  1.00 120.06 ? 172  GLY   B C   1 
ATOM   3958  O  O   . GLY   B 2 172 ? 23.681  22.342  17.916  1.00 116.73 ? 172  GLY   B O   1 
ATOM   3959  N  N   . CYS   B 2 173 ? 24.724  23.720  16.460  1.00 125.78 ? 173  CYS   B N   1 
ATOM   3960  C  CA  . CYS   B 2 173 ? 25.343  22.648  15.699  1.00 126.36 ? 173  CYS   B CA  1 
ATOM   3961  C  C   . CYS   B 2 173 ? 26.189  21.772  16.614  1.00 128.27 ? 173  CYS   B C   1 
ATOM   3962  O  O   . CYS   B 2 173 ? 26.922  22.270  17.475  1.00 128.35 ? 173  CYS   B O   1 
ATOM   3963  C  CB  . CYS   B 2 173 ? 26.207  23.236  14.568  1.00 125.27 ? 173  CYS   B CB  1 
ATOM   3964  S  SG  . CYS   B 2 173 ? 27.419  24.574  15.061  1.00 129.61 ? 173  CYS   B SG  1 
ATOM   3965  N  N   . GLN   B 2 174 ? 26.086  20.457  16.445  1.00 125.47 ? 174  GLN   B N   1 
ATOM   3966  C  CA  . GLN   B 2 174 ? 27.075  19.592  17.075  1.00 125.92 ? 174  GLN   B CA  1 
ATOM   3967  C  C   . GLN   B 2 174 ? 28.421  19.719  16.368  1.00 120.34 ? 174  GLN   B C   1 
ATOM   3968  O  O   . GLN   B 2 174 ? 29.468  19.855  17.009  1.00 119.08 ? 174  GLN   B O   1 
ATOM   3969  C  CB  . GLN   B 2 174 ? 26.570  18.148  17.103  1.00 130.98 ? 174  GLN   B CB  1 
ATOM   3970  C  CG  . GLN   B 2 174 ? 25.143  17.990  17.706  1.00 142.31 ? 174  GLN   B CG  1 
ATOM   3971  C  CD  . GLN   B 2 174 ? 25.043  18.289  19.226  1.00 143.94 ? 174  GLN   B CD  1 
ATOM   3972  O  OE1 . GLN   B 2 174 ? 26.044  18.254  19.951  1.00 141.88 ? 174  GLN   B OE1 1 
ATOM   3973  N  NE2 . GLN   B 2 174 ? 23.819  18.570  19.702  1.00 140.88 ? 174  GLN   B NE2 1 
ATOM   3974  N  N   . ALA   B 2 175 ? 28.409  19.718  15.045  1.00 117.21 ? 175  ALA   B N   1 
ATOM   3975  C  CA  . ALA   B 2 175 ? 29.581  19.942  14.215  1.00 112.23 ? 175  ALA   B CA  1 
ATOM   3976  C  C   . ALA   B 2 175 ? 29.249  21.034  13.213  1.00 109.97 ? 175  ALA   B C   1 
ATOM   3977  O  O   . ALA   B 2 175 ? 28.073  21.294  12.946  1.00 112.26 ? 175  ALA   B O   1 
ATOM   3978  C  CB  . ALA   B 2 175 ? 29.985  18.652  13.492  1.00 109.13 ? 175  ALA   B CB  1 
ATOM   3979  N  N   . PRO   B 2 176 ? 30.268  21.689  12.627  1.00 106.51 ? 176  PRO   B N   1 
ATOM   3980  C  CA  . PRO   B 2 176 ? 30.025  22.850  11.750  1.00 105.82 ? 176  PRO   B CA  1 
ATOM   3981  C  C   . PRO   B 2 176 ? 29.018  22.545  10.640  1.00 105.84 ? 176  PRO   B C   1 
ATOM   3982  O  O   . PRO   B 2 176 ? 29.303  21.798  9.697   1.00 105.19 ? 176  PRO   B O   1 
ATOM   3983  C  CB  . PRO   B 2 176 ? 31.429  23.181  11.212  1.00 99.49  ? 176  PRO   B CB  1 
ATOM   3984  C  CG  . PRO   B 2 176 ? 32.309  22.082  11.661  1.00 102.96 ? 176  PRO   B CG  1 
ATOM   3985  C  CD  . PRO   B 2 176 ? 31.697  21.513  12.889  1.00 107.02 ? 176  PRO   B CD  1 
ATOM   3986  N  N   . THR   B 2 177 ? 27.840  23.162  10.727  1.00 102.60 ? 177  THR   B N   1 
ATOM   3987  C  CA  . THR   B 2 177 ? 26.725  22.863  9.843   1.00 97.59  ? 177  THR   B CA  1 
ATOM   3988  C  C   . THR   B 2 177 ? 26.305  24.133  9.121   1.00 99.10  ? 177  THR   B C   1 
ATOM   3989  O  O   . THR   B 2 177 ? 26.201  25.201  9.739   1.00 100.02 ? 177  THR   B O   1 
ATOM   3990  C  CB  . THR   B 2 177 ? 25.531  22.304  10.589  1.00 101.01 ? 177  THR   B CB  1 
ATOM   3991  O  OG1 . THR   B 2 177 ? 25.901  21.077  11.234  1.00 103.12 ? 177  THR   B OG1 1 
ATOM   3992  C  CG2 . THR   B 2 177 ? 24.366  22.086  9.627   1.00 100.81 ? 177  THR   B CG2 1 
ATOM   3993  N  N   . ILE   B 2 178 ? 26.043  24.009  7.818   1.00 101.34 ? 178  ILE   B N   1 
ATOM   3994  C  CA  . ILE   B 2 178 ? 25.552  25.105  6.990   1.00 92.33  ? 178  ILE   B CA  1 
ATOM   3995  C  C   . ILE   B 2 178 ? 24.178  24.740  6.461   1.00 93.20  ? 178  ILE   B C   1 
ATOM   3996  O  O   . ILE   B 2 178 ? 23.980  23.644  5.922   1.00 94.03  ? 178  ILE   B O   1 
ATOM   3997  C  CB  . ILE   B 2 178 ? 26.501  25.428  5.821   1.00 89.49  ? 178  ILE   B CB  1 
ATOM   3998  C  CG1 . ILE   B 2 178 ? 26.772  24.186  4.965   1.00 92.52  ? 178  ILE   B CG1 1 
ATOM   3999  C  CG2 . ILE   B 2 178 ? 27.782  25.983  6.338   1.00 90.35  ? 178  ILE   B CG2 1 
ATOM   4000  C  CD1 . ILE   B 2 178 ? 27.555  24.476  3.711   1.00 83.72  ? 178  ILE   B CD1 1 
ATOM   4001  N  N   . CYS   B 2 179 ? 23.238  25.659  6.609   1.00 92.96  ? 179  CYS   B N   1 
ATOM   4002  C  CA  . CYS   B 2 179 ? 21.935  25.535  5.984   1.00 91.96  ? 179  CYS   B CA  1 
ATOM   4003  C  C   . CYS   B 2 179 ? 21.884  26.426  4.749   1.00 88.07  ? 179  CYS   B C   1 
ATOM   4004  O  O   . CYS   B 2 179 ? 22.218  27.617  4.820   1.00 82.98  ? 179  CYS   B O   1 
ATOM   4005  C  CB  . CYS   B 2 179 ? 20.824  25.897  6.959   1.00 87.55  ? 179  CYS   B CB  1 
ATOM   4006  S  SG  . CYS   B 2 179 ? 19.258  25.781  6.146   1.00 86.41  ? 179  CYS   B SG  1 
ATOM   4007  N  N   . PHE   B 2 180 ? 21.477  25.840  3.616   1.00 92.11  ? 180  PHE   B N   1 
ATOM   4008  C  CA  . PHE   B 2 180 ? 21.438  26.548  2.337   1.00 93.91  ? 180  PHE   B CA  1 
ATOM   4009  C  C   . PHE   B 2 180 ? 20.136  26.242  1.590   1.00 91.55  ? 180  PHE   B C   1 
ATOM   4010  O  O   . PHE   B 2 180 ? 19.429  25.274  1.889   1.00 94.18  ? 180  PHE   B O   1 
ATOM   4011  C  CB  . PHE   B 2 180 ? 22.697  26.238  1.480   1.00 93.36  ? 180  PHE   B CB  1 
ATOM   4012  C  CG  . PHE   B 2 180 ? 22.783  24.824  0.943   1.00 94.50  ? 180  PHE   B CG  1 
ATOM   4013  C  CD1 . PHE   B 2 180 ? 22.855  23.734  1.796   1.00 97.38  ? 180  PHE   B CD1 1 
ATOM   4014  C  CD2 . PHE   B 2 180 ? 22.846  24.595  -0.431  1.00 93.95  ? 180  PHE   B CD2 1 
ATOM   4015  C  CE1 . PHE   B 2 180 ? 22.943  22.437  1.286   1.00 101.36 ? 180  PHE   B CE1 1 
ATOM   4016  C  CE2 . PHE   B 2 180 ? 22.941  23.317  -0.941  1.00 97.43  ? 180  PHE   B CE2 1 
ATOM   4017  C  CZ  . PHE   B 2 180 ? 22.985  22.234  -0.083  1.00 100.43 ? 180  PHE   B CZ  1 
ATOM   4018  N  N   . VAL   B 2 181 ? 19.807  27.125  0.639   1.00 90.17  ? 181  VAL   B N   1 
ATOM   4019  C  CA  . VAL   B 2 181 ? 18.581  27.063  -0.158  1.00 92.63  ? 181  VAL   B CA  1 
ATOM   4020  C  C   . VAL   B 2 181 ? 18.989  27.142  -1.618  1.00 96.70  ? 181  VAL   B C   1 
ATOM   4021  O  O   . VAL   B 2 181 ? 19.535  28.165  -2.049  1.00 98.81  ? 181  VAL   B O   1 
ATOM   4022  C  CB  . VAL   B 2 181 ? 17.593  28.198  0.175   1.00 87.47  ? 181  VAL   B CB  1 
ATOM   4023  C  CG1 . VAL   B 2 181 ? 16.546  28.360  -0.938  1.00 87.03  ? 181  VAL   B CG1 1 
ATOM   4024  C  CG2 . VAL   B 2 181 ? 16.914  27.941  1.508   1.00 87.58  ? 181  VAL   B CG2 1 
ATOM   4025  N  N   . TYR   B 2 182 ? 18.721  26.076  -2.373  1.00 98.07  ? 182  TYR   B N   1 
ATOM   4026  C  CA  . TYR   B 2 182 ? 19.071  25.982  -3.783  1.00 98.93  ? 182  TYR   B CA  1 
ATOM   4027  C  C   . TYR   B 2 182 ? 17.808  25.937  -4.634  1.00 100.25 ? 182  TYR   B C   1 
ATOM   4028  O  O   . TYR   B 2 182 ? 16.709  25.675  -4.137  1.00 101.73 ? 182  TYR   B O   1 
ATOM   4029  C  CB  . TYR   B 2 182 ? 19.962  24.758  -4.064  1.00 98.33  ? 182  TYR   B CB  1 
ATOM   4030  C  CG  . TYR   B 2 182 ? 19.442  23.412  -3.570  1.00 99.90  ? 182  TYR   B CG  1 
ATOM   4031  C  CD1 . TYR   B 2 182 ? 19.362  23.130  -2.212  1.00 99.53  ? 182  TYR   B CD1 1 
ATOM   4032  C  CD2 . TYR   B 2 182 ? 19.069  22.413  -4.459  1.00 100.89 ? 182  TYR   B CD2 1 
ATOM   4033  C  CE1 . TYR   B 2 182 ? 18.900  21.906  -1.756  1.00 101.79 ? 182  TYR   B CE1 1 
ATOM   4034  C  CE2 . TYR   B 2 182 ? 18.614  21.186  -4.011  1.00 100.21 ? 182  TYR   B CE2 1 
ATOM   4035  C  CZ  . TYR   B 2 182 ? 18.530  20.943  -2.661  1.00 101.95 ? 182  TYR   B CZ  1 
ATOM   4036  O  OH  . TYR   B 2 182 ? 18.070  19.737  -2.193  1.00 104.79 ? 182  TYR   B OH  1 
ATOM   4037  N  N   . GLN   B 2 183 ? 17.965  26.239  -5.920  1.00 106.37 ? 183  GLN   B N   1 
ATOM   4038  C  CA  . GLN   B 2 183 ? 16.918  25.993  -6.893  1.00 108.14 ? 183  GLN   B CA  1 
ATOM   4039  C  C   . GLN   B 2 183 ? 17.347  24.833  -7.778  1.00 113.86 ? 183  GLN   B C   1 
ATOM   4040  O  O   . GLN   B 2 183 ? 18.525  24.721  -8.148  1.00 109.35 ? 183  GLN   B O   1 
ATOM   4041  C  CB  . GLN   B 2 183 ? 16.596  27.224  -7.739  1.00 106.15 ? 183  GLN   B CB  1 
ATOM   4042  C  CG  . GLN   B 2 183 ? 15.447  26.966  -8.682  1.00 107.10 ? 183  GLN   B CG  1 
ATOM   4043  C  CD  . GLN   B 2 183 ? 14.947  28.212  -9.338  1.00 110.42 ? 183  GLN   B CD  1 
ATOM   4044  O  OE1 . GLN   B 2 183 ? 14.484  29.133  -8.667  1.00 110.25 ? 183  GLN   B OE1 1 
ATOM   4045  N  NE2 . GLN   B 2 183 ? 15.040  28.262  -10.662 1.00 112.52 ? 183  GLN   B NE2 1 
ATOM   4046  N  N   . ASP   B 2 184 ? 16.402  23.950  -8.043  1.00 113.42 ? 184  ASP   B N   1 
ATOM   4047  C  CA  . ASP   B 2 184 ? 16.495  22.808  -8.917  1.00 112.28 ? 184  ASP   B CA  1 
ATOM   4048  C  C   . ASP   B 2 184 ? 15.597  23.020  -10.098 1.00 119.19 ? 184  ASP   B C   1 
ATOM   4049  O  O   . ASP   B 2 184 ? 14.733  23.903  -10.081 1.00 121.78 ? 184  ASP   B O   1 
ATOM   4050  C  CB  . ASP   B 2 184 ? 16.043  21.552  -8.185  1.00 111.53 ? 184  ASP   B CB  1 
ATOM   4051  C  CG  . ASP   B 2 184 ? 17.170  20.608  -7.932  1.00 120.98 ? 184  ASP   B CG  1 
ATOM   4052  O  OD1 . ASP   B 2 184 ? 18.302  20.884  -8.417  1.00 125.21 ? 184  ASP   B OD1 1 
ATOM   4053  O  OD2 . ASP   B 2 184 ? 16.922  19.594  -7.237  1.00 123.37 ? 184  ASP   B OD2 1 
ATOM   4054  N  N   . PRO   B 2 185 ? 15.731  22.205  -11.144 1.00 122.45 ? 185  PRO   B N   1 
ATOM   4055  C  CA  . PRO   B 2 185 ? 14.609  22.084  -12.083 1.00 119.68 ? 185  PRO   B CA  1 
ATOM   4056  C  C   . PRO   B 2 185 ? 13.301  21.815  -11.359 1.00 124.12 ? 185  PRO   B C   1 
ATOM   4057  O  O   . PRO   B 2 185 ? 12.268  22.386  -11.734 1.00 126.85 ? 185  PRO   B O   1 
ATOM   4058  C  CB  . PRO   B 2 185 ? 15.023  20.917  -12.988 1.00 117.42 ? 185  PRO   B CB  1 
ATOM   4059  C  CG  . PRO   B 2 185 ? 16.126  20.223  -12.248 1.00 121.20 ? 185  PRO   B CG  1 
ATOM   4060  C  CD  . PRO   B 2 185 ? 16.837  21.304  -11.500 1.00 125.63 ? 185  PRO   B CD  1 
ATOM   4061  N  N   . GLN   B 2 186 ? 13.331  21.013  -10.288 1.00 121.22 ? 186  GLN   B N   1 
ATOM   4062  C  CA  . GLN   B 2 186 ? 12.122  20.678  -9.549  1.00 120.36 ? 186  GLN   B CA  1 
ATOM   4063  C  C   . GLN   B 2 186 ? 11.629  21.810  -8.649  1.00 122.95 ? 186  GLN   B C   1 
ATOM   4064  O  O   . GLN   B 2 186 ? 10.440  21.825  -8.305  1.00 122.93 ? 186  GLN   B O   1 
ATOM   4065  C  CB  . GLN   B 2 186 ? 12.358  19.421  -8.716  1.00 120.62 ? 186  GLN   B CB  1 
ATOM   4066  C  CG  . GLN   B 2 186 ? 12.813  18.234  -9.533  1.00 123.46 ? 186  GLN   B CG  1 
ATOM   4067  C  CD  . GLN   B 2 186 ? 14.268  17.876  -9.292  1.00 127.51 ? 186  GLN   B CD  1 
ATOM   4068  O  OE1 . GLN   B 2 186 ? 14.782  18.067  -8.191  1.00 132.51 ? 186  GLN   B OE1 1 
ATOM   4069  N  NE2 . GLN   B 2 186 ? 14.943  17.355  -10.323 1.00 126.03 ? 186  GLN   B NE2 1 
ATOM   4070  N  N   . GLY   B 2 187 ? 12.489  22.742  -8.245  1.00 125.78 ? 187  GLY   B N   1 
ATOM   4071  C  CA  . GLY   B 2 187 ? 12.035  23.886  -7.468  1.00 121.91 ? 187  GLY   B CA  1 
ATOM   4072  C  C   . GLY   B 2 187 ? 13.136  24.419  -6.568  1.00 118.89 ? 187  GLY   B C   1 
ATOM   4073  O  O   . GLY   B 2 187 ? 14.315  24.255  -6.851  1.00 120.45 ? 187  GLY   B O   1 
ATOM   4074  N  N   . ARG   B 2 188 ? 12.718  25.072  -5.482  1.00 106.33 ? 188  ARG   B N   1 
ATOM   4075  C  CA  . ARG   B 2 188 ? 13.618  25.570  -4.445  1.00 102.93 ? 188  ARG   B CA  1 
ATOM   4076  C  C   . ARG   B 2 188 ? 13.494  24.729  -3.181  1.00 106.95 ? 188  ARG   B C   1 
ATOM   4077  O  O   . ARG   B 2 188 ? 12.399  24.573  -2.624  1.00 110.04 ? 188  ARG   B O   1 
ATOM   4078  C  CB  . ARG   B 2 188 ? 13.320  27.026  -4.099  1.00 98.74  ? 188  ARG   B CB  1 
ATOM   4079  C  CG  . ARG   B 2 188 ? 13.547  28.007  -5.214  1.00 101.84 ? 188  ARG   B CG  1 
ATOM   4080  C  CD  . ARG   B 2 188 ? 14.602  29.009  -4.819  1.00 97.69  ? 188  ARG   B CD  1 
ATOM   4081  N  NE  . ARG   B 2 188 ? 14.674  30.124  -5.749  1.00 92.48  ? 188  ARG   B NE  1 
ATOM   4082  C  CZ  . ARG   B 2 188 ? 14.161  31.316  -5.500  1.00 92.52  ? 188  ARG   B CZ  1 
ATOM   4083  N  NH1 . ARG   B 2 188 ? 13.501  31.555  -4.384  1.00 91.55  ? 188  ARG   B NH1 1 
ATOM   4084  N  NH2 . ARG   B 2 188 ? 14.315  32.292  -6.388  1.00 99.68  ? 188  ARG   B NH2 1 
ATOM   4085  N  N   . HIS   B 2 189 ? 14.616  24.221  -2.702  1.00 103.50 ? 189  HIS   B N   1 
ATOM   4086  C  CA  . HIS   B 2 189 ? 14.621  23.328  -1.560  1.00 102.08 ? 189  HIS   B CA  1 
ATOM   4087  C  C   . HIS   B 2 189 ? 15.617  23.839  -0.534  1.00 99.26  ? 189  HIS   B C   1 
ATOM   4088  O  O   . HIS   B 2 189 ? 16.419  24.734  -0.812  1.00 98.68  ? 189  HIS   B O   1 
ATOM   4089  C  CB  . HIS   B 2 189 ? 14.977  21.902  -1.987  1.00 106.29 ? 189  HIS   B CB  1 
ATOM   4090  C  CG  . HIS   B 2 189 ? 14.548  21.560  -3.375  1.00 107.82 ? 189  HIS   B CG  1 
ATOM   4091  N  ND1 . HIS   B 2 189 ? 13.270  21.773  -3.836  1.00 112.96 ? 189  HIS   B ND1 1 
ATOM   4092  C  CD2 . HIS   B 2 189 ? 15.232  21.010  -4.404  1.00 111.01 ? 189  HIS   B CD2 1 
ATOM   4093  C  CE1 . HIS   B 2 189 ? 13.184  21.375  -5.092  1.00 115.80 ? 189  HIS   B CE1 1 
ATOM   4094  N  NE2 . HIS   B 2 189 ? 14.362  20.907  -5.462  1.00 114.50 ? 189  HIS   B NE2 1 
ATOM   4095  N  N   . VAL   B 2 190 ? 15.564  23.261  0.671   1.00 98.65  ? 190  VAL   B N   1 
ATOM   4096  C  CA  . VAL   B 2 190 ? 16.477  23.588  1.764   1.00 95.34  ? 190  VAL   B CA  1 
ATOM   4097  C  C   . VAL   B 2 190 ? 17.198  22.326  2.207   1.00 94.68  ? 190  VAL   B C   1 
ATOM   4098  O  O   . VAL   B 2 190 ? 16.570  21.278  2.379   1.00 99.16  ? 190  VAL   B O   1 
ATOM   4099  C  CB  . VAL   B 2 190 ? 15.740  24.217  2.958   1.00 93.19  ? 190  VAL   B CB  1 
ATOM   4100  C  CG1 . VAL   B 2 190 ? 16.746  24.768  3.951   1.00 94.64  ? 190  VAL   B CG1 1 
ATOM   4101  C  CG2 . VAL   B 2 190 ? 14.826  25.301  2.491   1.00 94.76  ? 190  VAL   B CG2 1 
ATOM   4102  N  N   . LYS   B 2 191 ? 18.504  22.436  2.434   1.00 92.59  ? 191  LYS   B N   1 
ATOM   4103  C  CA  . LYS   B 2 191 ? 19.307  21.301  2.858   1.00 94.51  ? 191  LYS   B CA  1 
ATOM   4104  C  C   . LYS   B 2 191 ? 20.383  21.757  3.830   1.00 95.31  ? 191  LYS   B C   1 
ATOM   4105  O  O   . LYS   B 2 191 ? 20.627  22.954  3.997   1.00 96.62  ? 191  LYS   B O   1 
ATOM   4106  C  CB  . LYS   B 2 191 ? 19.952  20.611  1.666   1.00 98.12  ? 191  LYS   B CB  1 
ATOM   4107  C  CG  . LYS   B 2 191 ? 20.268  19.166  1.948   1.00 102.19 ? 191  LYS   B CG  1 
ATOM   4108  C  CD  . LYS   B 2 191 ? 21.472  18.743  1.176   1.00 101.79 ? 191  LYS   B CD  1 
ATOM   4109  C  CE  . LYS   B 2 191 ? 21.301  19.064  -0.270  1.00 99.88  ? 191  LYS   B CE  1 
ATOM   4110  N  NZ  . LYS   B 2 191 ? 21.895  17.955  -1.024  1.00 104.58 ? 191  LYS   B NZ  1 
ATOM   4111  N  N   . THR   B 2 192 ? 21.034  20.794  4.479   1.00 98.51  ? 192  THR   B N   1 
ATOM   4112  C  CA  . THR   B 2 192 ? 22.168  21.079  5.350   1.00 99.63  ? 192  THR   B CA  1 
ATOM   4113  C  C   . THR   B 2 192 ? 23.299  20.088  5.117   1.00 99.66  ? 192  THR   B C   1 
ATOM   4114  O  O   . THR   B 2 192 ? 23.077  18.911  4.802   1.00 97.03  ? 192  THR   B O   1 
ATOM   4115  C  CB  . THR   B 2 192 ? 21.799  21.052  6.843   1.00 97.76  ? 192  THR   B CB  1 
ATOM   4116  O  OG1 . THR   B 2 192 ? 21.192  19.796  7.167   1.00 99.25  ? 192  THR   B OG1 1 
ATOM   4117  C  CG2 . THR   B 2 192 ? 20.870  22.202  7.206   1.00 96.35  ? 192  THR   B CG2 1 
ATOM   4118  N  N   . TYR   B 2 193 ? 24.515  20.592  5.280   1.00 100.81 ? 193  TYR   B N   1 
ATOM   4119  C  CA  . TYR   B 2 193 ? 25.737  19.810  5.212   1.00 101.39 ? 193  TYR   B CA  1 
ATOM   4120  C  C   . TYR   B 2 193 ? 26.576  20.104  6.446   1.00 102.93 ? 193  TYR   B C   1 
ATOM   4121  O  O   . TYR   B 2 193 ? 26.406  21.130  7.112   1.00 100.93 ? 193  TYR   B O   1 
ATOM   4122  C  CB  . TYR   B 2 193 ? 26.565  20.131  3.960   1.00 101.28 ? 193  TYR   B CB  1 
ATOM   4123  C  CG  . TYR   B 2 193 ? 25.984  19.621  2.674   1.00 103.84 ? 193  TYR   B CG  1 
ATOM   4124  C  CD1 . TYR   B 2 193 ? 25.383  18.373  2.609   1.00 105.90 ? 193  TYR   B CD1 1 
ATOM   4125  C  CD2 . TYR   B 2 193 ? 26.038  20.389  1.515   1.00 105.85 ? 193  TYR   B CD2 1 
ATOM   4126  C  CE1 . TYR   B 2 193 ? 24.860  17.893  1.412   1.00 108.24 ? 193  TYR   B CE1 1 
ATOM   4127  C  CE2 . TYR   B 2 193 ? 25.516  19.926  0.324   1.00 107.64 ? 193  TYR   B CE2 1 
ATOM   4128  C  CZ  . TYR   B 2 193 ? 24.930  18.681  0.276   1.00 108.59 ? 193  TYR   B CZ  1 
ATOM   4129  O  OH  . TYR   B 2 193 ? 24.418  18.239  -0.915  1.00 109.11 ? 193  TYR   B OH  1 
ATOM   4130  N  N   . GLU   B 2 194 ? 27.494  19.190  6.739   1.00 98.41  ? 194  GLU   B N   1 
ATOM   4131  C  CA  . GLU   B 2 194 ? 28.459  19.357  7.813   1.00 94.81  ? 194  GLU   B CA  1 
ATOM   4132  C  C   . GLU   B 2 194 ? 29.835  19.473  7.189   1.00 95.89  ? 194  GLU   B C   1 
ATOM   4133  O  O   . GLU   B 2 194 ? 30.170  18.704  6.285   1.00 101.83 ? 194  GLU   B O   1 
ATOM   4134  C  CB  . GLU   B 2 194 ? 28.408  18.179  8.791   1.00 98.83  ? 194  GLU   B CB  1 
ATOM   4135  C  CG  . GLU   B 2 194 ? 26.994  17.842  9.303   1.00 104.44 ? 194  GLU   B CG  1 
ATOM   4136  C  CD  . GLU   B 2 194 ? 26.921  17.557  10.814  1.00 107.33 ? 194  GLU   B CD  1 
ATOM   4137  O  OE1 . GLU   B 2 194 ? 27.633  16.646  11.303  1.00 106.48 ? 194  GLU   B OE1 1 
ATOM   4138  O  OE2 . GLU   B 2 194 ? 26.131  18.242  11.511  1.00 104.08 ? 194  GLU   B OE2 1 
ATOM   4139  N  N   . VAL   B 2 195 ? 30.624  20.433  7.654   1.00 94.16  ? 195  VAL   B N   1 
ATOM   4140  C  CA  . VAL   B 2 195 ? 31.901  20.733  7.027   1.00 97.53  ? 195  VAL   B CA  1 
ATOM   4141  C  C   . VAL   B 2 195 ? 32.976  19.999  7.814   1.00 102.27 ? 195  VAL   B C   1 
ATOM   4142  O  O   . VAL   B 2 195 ? 33.420  20.457  8.869   1.00 106.63 ? 195  VAL   B O   1 
ATOM   4143  C  CB  . VAL   B 2 195 ? 32.157  22.234  6.965   1.00 100.00 ? 195  VAL   B CB  1 
ATOM   4144  C  CG1 . VAL   B 2 195 ? 33.327  22.513  6.043   1.00 99.11  ? 195  VAL   B CG1 1 
ATOM   4145  C  CG2 . VAL   B 2 195 ? 30.892  22.931  6.485   1.00 97.44  ? 195  VAL   B CG2 1 
ATOM   4146  N  N   . SER   B 2 196 ? 33.387  18.848  7.302   1.00 105.70 ? 196  SER   B N   1 
ATOM   4147  C  CA  . SER   B 2 196 ? 34.435  18.072  7.947   1.00 108.94 ? 196  SER   B CA  1 
ATOM   4148  C  C   . SER   B 2 196 ? 35.762  18.700  7.571   1.00 111.43 ? 196  SER   B C   1 
ATOM   4149  O  O   . SER   B 2 196 ? 36.280  18.483  6.473   1.00 111.08 ? 196  SER   B O   1 
ATOM   4150  C  CB  . SER   B 2 196 ? 34.380  16.614  7.529   1.00 119.36 ? 196  SER   B CB  1 
ATOM   4151  O  OG  . SER   B 2 196 ? 35.499  15.940  8.071   1.00 129.05 ? 196  SER   B OG  1 
ATOM   4152  N  N   . LEU   B 2 197 ? 36.302  19.500  8.481   1.00 108.99 ? 197  LEU   B N   1 
ATOM   4153  C  CA  . LEU   B 2 197 ? 37.650  20.007  8.285   1.00 109.94 ? 197  LEU   B CA  1 
ATOM   4154  C  C   . LEU   B 2 197 ? 38.648  18.860  8.185   1.00 119.44 ? 197  LEU   B C   1 
ATOM   4155  O  O   . LEU   B 2 197 ? 39.571  18.889  7.359   1.00 119.84 ? 197  LEU   B O   1 
ATOM   4156  C  CB  . LEU   B 2 197 ? 38.024  20.921  9.441   1.00 109.18 ? 197  LEU   B CB  1 
ATOM   4157  C  CG  . LEU   B 2 197 ? 37.233  22.180  9.698   1.00 106.83 ? 197  LEU   B CG  1 
ATOM   4158  C  CD1 . LEU   B 2 197 ? 37.690  22.736  11.040  1.00 112.11 ? 197  LEU   B CD1 1 
ATOM   4159  C  CD2 . LEU   B 2 197 ? 37.512  23.167  8.582   1.00 104.09 ? 197  LEU   B CD2 1 
ATOM   4160  N  N   . ARG   B 2 198 ? 38.484  17.848  9.044   1.00 122.40 ? 198  ARG   B N   1 
ATOM   4161  C  CA  . ARG   B 2 198 ? 39.389  16.709  9.056   1.00 120.62 ? 198  ARG   B CA  1 
ATOM   4162  C  C   . ARG   B 2 198 ? 39.463  16.066  7.680   1.00 125.29 ? 198  ARG   B C   1 
ATOM   4163  O  O   . ARG   B 2 198 ? 40.548  15.866  7.132   1.00 128.03 ? 198  ARG   B O   1 
ATOM   4164  C  CB  . ARG   B 2 198 ? 38.938  15.700  10.108  1.00 118.27 ? 198  ARG   B CB  1 
ATOM   4165  N  N   . GLU   B 2 199 ? 38.309  15.769  7.089   1.00 137.74 ? 199  GLU   B N   1 
ATOM   4166  C  CA  . GLU   B 2 199 ? 38.268  15.167  5.767   1.00 142.10 ? 199  GLU   B CA  1 
ATOM   4167  C  C   . GLU   B 2 199 ? 38.165  16.198  4.642   1.00 140.42 ? 199  GLU   B C   1 
ATOM   4168  O  O   . GLU   B 2 199 ? 38.177  15.804  3.475   1.00 144.89 ? 199  GLU   B O   1 
ATOM   4169  C  CB  . GLU   B 2 199 ? 37.111  14.148  5.686   1.00 148.05 ? 199  GLU   B CB  1 
ATOM   4170  C  CG  . GLU   B 2 199 ? 35.785  14.664  5.074   1.00 148.38 ? 199  GLU   B CG  1 
ATOM   4171  C  CD  . GLU   B 2 199 ? 34.710  13.567  4.901   1.00 148.40 ? 199  GLU   B CD  1 
ATOM   4172  O  OE1 . GLU   B 2 199 ? 34.436  12.828  5.878   1.00 149.51 ? 199  GLU   B OE1 1 
ATOM   4173  O  OE2 . GLU   B 2 199 ? 34.146  13.445  3.783   1.00 141.78 ? 199  GLU   B OE2 1 
ATOM   4174  N  N   . LYS   B 2 200 ? 38.121  17.498  4.959   1.00 126.04 ? 200  LYS   B N   1 
ATOM   4175  C  CA  . LYS   B 2 200 ? 38.032  18.584  3.965   1.00 115.72 ? 200  LYS   B CA  1 
ATOM   4176  C  C   . LYS   B 2 200 ? 37.040  18.240  2.854   1.00 117.80 ? 200  LYS   B C   1 
ATOM   4177  O  O   . LYS   B 2 200 ? 37.334  18.308  1.660   1.00 112.10 ? 200  LYS   B O   1 
ATOM   4178  C  CB  . LYS   B 2 200 ? 39.405  18.933  3.388   1.00 105.77 ? 200  LYS   B CB  1 
ATOM   4179  N  N   . GLU   B 2 201 ? 35.838  17.869  3.280   1.00 113.24 ? 201  GLU   B N   1 
ATOM   4180  C  CA  . GLU   B 2 201 ? 34.724  17.612  2.382   1.00 110.79 ? 201  GLU   B CA  1 
ATOM   4181  C  C   . GLU   B 2 201 ? 33.447  17.809  3.185   1.00 106.58 ? 201  GLU   B C   1 
ATOM   4182  O  O   . GLU   B 2 201 ? 33.488  18.032  4.398   1.00 108.56 ? 201  GLU   B O   1 
ATOM   4183  C  CB  . GLU   B 2 201 ? 34.806  16.205  1.783   1.00 112.97 ? 201  GLU   B CB  1 
ATOM   4184  N  N   . PHE   B 2 202 ? 32.310  17.722  2.493   1.00 102.84 ? 202  PHE   B N   1 
ATOM   4185  C  CA  . PHE   B 2 202 ? 30.998  17.821  3.119   1.00 102.66 ? 202  PHE   B CA  1 
ATOM   4186  C  C   . PHE   B 2 202 ? 30.523  16.457  3.607   1.00 107.66 ? 202  PHE   B C   1 
ATOM   4187  O  O   . PHE   B 2 202 ? 30.844  15.423  3.012   1.00 115.62 ? 202  PHE   B O   1 
ATOM   4188  C  CB  . PHE   B 2 202 ? 29.962  18.365  2.140   1.00 99.70  ? 202  PHE   B CB  1 
ATOM   4189  C  CG  . PHE   B 2 202 ? 29.963  19.838  2.007   1.00 96.51  ? 202  PHE   B CG  1 
ATOM   4190  C  CD1 . PHE   B 2 202 ? 30.172  20.641  3.099   1.00 98.60  ? 202  PHE   B CD1 1 
ATOM   4191  C  CD2 . PHE   B 2 202 ? 29.745  20.420  0.778   1.00 95.36  ? 202  PHE   B CD2 1 
ATOM   4192  C  CE1 . PHE   B 2 202 ? 30.160  22.002  2.967   1.00 99.83  ? 202  PHE   B CE1 1 
ATOM   4193  C  CE2 . PHE   B 2 202 ? 29.732  21.770  0.632   1.00 93.16  ? 202  PHE   B CE2 1 
ATOM   4194  C  CZ  . PHE   B 2 202 ? 29.937  22.569  1.723   1.00 96.99  ? 202  PHE   B CZ  1 
ATOM   4195  N  N   . ASN   B 2 203 ? 29.724  16.464  4.676   1.00 104.58 ? 203  ASN   B N   1 
ATOM   4196  C  CA  . ASN   B 2 203 ? 29.062  15.267  5.182   1.00 102.21 ? 203  ASN   B CA  1 
ATOM   4197  C  C   . ASN   B 2 203 ? 27.583  15.575  5.380   1.00 98.82  ? 203  ASN   B C   1 
ATOM   4198  O  O   . ASN   B 2 203 ? 27.210  16.722  5.646   1.00 98.15  ? 203  ASN   B O   1 
ATOM   4199  C  CB  . ASN   B 2 203 ? 29.680  14.790  6.508   1.00 105.06 ? 203  ASN   B CB  1 
ATOM   4200  C  CG  . ASN   B 2 203 ? 31.086  14.207  6.341   1.00 114.29 ? 203  ASN   B CG  1 
ATOM   4201  O  OD1 . ASN   B 2 203 ? 31.410  13.596  5.315   1.00 119.63 ? 203  ASN   B OD1 1 
ATOM   4202  N  ND2 . ASN   B 2 203 ? 31.921  14.377  7.370   1.00 112.90 ? 203  ASN   B ND2 1 
ATOM   4203  N  N   . LYS   B 2 204 ? 26.742  14.550  5.253   1.00 97.26  ? 204  LYS   B N   1 
ATOM   4204  C  CA  . LYS   B 2 204 ? 25.298  14.765  5.300   1.00 96.67  ? 204  LYS   B CA  1 
ATOM   4205  C  C   . LYS   B 2 204 ? 24.919  15.433  6.610   1.00 96.17  ? 204  LYS   B C   1 
ATOM   4206  O  O   . LYS   B 2 204 ? 25.529  15.177  7.646   1.00 100.96 ? 204  LYS   B O   1 
ATOM   4207  C  CB  . LYS   B 2 204 ? 24.554  13.438  5.151   1.00 92.34  ? 204  LYS   B CB  1 
ATOM   4208  N  N   . GLY   B 2 205 ? 23.914  16.317  6.557   1.00 95.78  ? 205  GLY   B N   1 
ATOM   4209  C  CA  . GLY   B 2 205 ? 23.570  17.164  7.687   1.00 97.45  ? 205  GLY   B CA  1 
ATOM   4210  C  C   . GLY   B 2 205 ? 22.440  16.645  8.564   1.00 96.70  ? 205  GLY   B C   1 
ATOM   4211  O  O   . GLY   B 2 205 ? 21.981  15.507  8.411   1.00 101.39 ? 205  GLY   B O   1 
ATOM   4212  N  N   . PRO   B 2 206 ? 21.986  17.467  9.522   1.00 94.53  ? 206  PRO   B N   1 
ATOM   4213  C  CA  . PRO   B 2 206 ? 20.867  17.031  10.373  1.00 94.98  ? 206  PRO   B CA  1 
ATOM   4214  C  C   . PRO   B 2 206 ? 19.507  16.978  9.680   1.00 98.00  ? 206  PRO   B C   1 
ATOM   4215  O  O   . PRO   B 2 206 ? 18.735  16.061  9.991   1.00 99.67  ? 206  PRO   B O   1 
ATOM   4216  C  CB  . PRO   B 2 206 ? 20.884  18.044  11.532  1.00 96.57  ? 206  PRO   B CB  1 
ATOM   4217  C  CG  . PRO   B 2 206 ? 21.765  19.158  11.105  1.00 94.60  ? 206  PRO   B CG  1 
ATOM   4218  C  CD  . PRO   B 2 206 ? 22.750  18.558  10.147  1.00 95.80  ? 206  PRO   B CD  1 
ATOM   4219  N  N   . TRP   B 2 207 ? 19.176  17.894  8.755   1.00 95.73  ? 207  TRP   B N   1 
ATOM   4220  C  CA  . TRP   B 2 207 ? 17.816  17.936  8.205   1.00 97.20  ? 207  TRP   B CA  1 
ATOM   4221  C  C   . TRP   B 2 207 ? 17.794  18.559  6.802   1.00 102.36 ? 207  TRP   B C   1 
ATOM   4222  O  O   . TRP   B 2 207 ? 18.776  19.165  6.359   1.00 104.23 ? 207  TRP   B O   1 
ATOM   4223  C  CB  . TRP   B 2 207 ? 16.876  18.681  9.157   1.00 99.27  ? 207  TRP   B CB  1 
ATOM   4224  C  CG  . TRP   B 2 207 ? 17.345  20.061  9.591   1.00 101.18 ? 207  TRP   B CG  1 
ATOM   4225  C  CD1 . TRP   B 2 207 ? 18.018  20.400  10.751  1.00 98.50  ? 207  TRP   B CD1 1 
ATOM   4226  C  CD2 . TRP   B 2 207 ? 17.133  21.285  8.883   1.00 101.45 ? 207  TRP   B CD2 1 
ATOM   4227  N  NE1 . TRP   B 2 207 ? 18.243  21.763  10.784  1.00 96.12  ? 207  TRP   B NE1 1 
ATOM   4228  C  CE2 . TRP   B 2 207 ? 17.709  22.325  9.649   1.00 98.23  ? 207  TRP   B CE2 1 
ATOM   4229  C  CE3 . TRP   B 2 207 ? 16.512  21.602  7.670   1.00 98.55  ? 207  TRP   B CE3 1 
ATOM   4230  C  CZ2 . TRP   B 2 207 ? 17.680  23.653  9.227   1.00 97.54  ? 207  TRP   B CZ2 1 
ATOM   4231  C  CZ3 . TRP   B 2 207 ? 16.487  22.906  7.261   1.00 98.47  ? 207  TRP   B CZ3 1 
ATOM   4232  C  CH2 . TRP   B 2 207 ? 17.060  23.919  8.032   1.00 97.80  ? 207  TRP   B CH2 1 
ATOM   4233  N  N   . LYS   B 2 208 ? 16.658  18.397  6.095   1.00 103.17 ? 208  LYS   B N   1 
ATOM   4234  C  CA  . LYS   B 2 208 ? 16.506  18.855  4.711   1.00 97.31  ? 208  LYS   B CA  1 
ATOM   4235  C  C   . LYS   B 2 208 ? 15.028  18.933  4.352   1.00 95.65  ? 208  LYS   B C   1 
ATOM   4236  O  O   . LYS   B 2 208 ? 14.254  18.067  4.742   1.00 102.24 ? 208  LYS   B O   1 
ATOM   4237  C  CB  . LYS   B 2 208 ? 17.237  17.928  3.733   1.00 96.09  ? 208  LYS   B CB  1 
ATOM   4238  C  CG  . LYS   B 2 208 ? 17.040  16.460  4.023   1.00 100.23 ? 208  LYS   B CG  1 
ATOM   4239  C  CD  . LYS   B 2 208 ? 18.041  15.593  3.266   1.00 101.77 ? 208  LYS   B CD  1 
ATOM   4240  C  CE  . LYS   B 2 208 ? 17.829  15.661  1.752   1.00 106.71 ? 208  LYS   B CE  1 
ATOM   4241  N  NZ  . LYS   B 2 208 ? 18.689  14.708  0.979   1.00 105.01 ? 208  LYS   B NZ  1 
ATOM   4242  N  N   . GLN   B 2 209 ? 14.639  19.975  3.618   1.00 101.60 ? 209  GLN   B N   1 
ATOM   4243  C  CA  . GLN   B 2 209 ? 13.236  20.287  3.358   1.00 109.28 ? 209  GLN   B CA  1 
ATOM   4244  C  C   . GLN   B 2 209 ? 12.925  20.094  1.889   1.00 113.85 ? 209  GLN   B C   1 
ATOM   4245  O  O   . GLN   B 2 209 ? 13.475  20.799  1.042   1.00 113.31 ? 209  GLN   B O   1 
ATOM   4246  C  CB  . GLN   B 2 209 ? 12.906  21.731  3.731   1.00 113.05 ? 209  GLN   B CB  1 
ATOM   4247  N  N   . GLU   B 2 210 ? 11.997  19.188  1.599   1.00 142.75 ? 210  GLU   B N   1 
ATOM   4248  C  CA  . GLU   B 2 210 ? 11.901  18.670  0.242   1.00 142.08 ? 210  GLU   B CA  1 
ATOM   4249  C  C   . GLU   B 2 210 ? 11.594  19.754  -0.790  1.00 139.91 ? 210  GLU   B C   1 
ATOM   4250  O  O   . GLU   B 2 210 ? 12.029  19.635  -1.939  1.00 139.03 ? 210  GLU   B O   1 
ATOM   4251  C  CB  . GLU   B 2 210 ? 10.854  17.553  0.184   1.00 145.57 ? 210  GLU   B CB  1 
ATOM   4252  N  N   . ASN   B 2 211 ? 10.876  20.818  -0.421  1.00 120.89 ? 211  ASN   B N   1 
ATOM   4253  C  CA  . ASN   B 2 211 ? 10.409  21.758  -1.440  1.00 115.04 ? 211  ASN   B CA  1 
ATOM   4254  C  C   . ASN   B 2 211 ? 9.877   22.822  -0.488  1.00 113.49 ? 211  ASN   B C   1 
ATOM   4255  O  O   . ASN   B 2 211 ? 9.125   22.505  0.443   1.00 116.32 ? 211  ASN   B O   1 
ATOM   4256  C  CB  . ASN   B 2 211 ? 9.443   21.054  -2.400  1.00 117.47 ? 211  ASN   B CB  1 
ATOM   4257  C  CG  . ASN   B 2 211 ? 9.523   21.581  -3.825  1.00 116.17 ? 211  ASN   B CG  1 
ATOM   4258  O  OD1 . ASN   B 2 211 ? 9.828   22.752  -4.070  1.00 115.33 ? 211  ASN   B OD1 1 
ATOM   4259  N  ND2 . ASN   B 2 211 ? 9.227   20.709  -4.775  1.00 119.03 ? 211  ASN   B ND2 1 
ATOM   4260  N  N   . VAL   B 2 212 ? 10.247  24.082  -0.705  1.00 109.28 ? 212  VAL   B N   1 
ATOM   4261  C  CA  . VAL   B 2 212 ? 9.924   25.110  0.255   1.00 101.19 ? 212  VAL   B CA  1 
ATOM   4262  C  C   . VAL   B 2 212 ? 9.456   26.190  -0.752  1.00 95.59  ? 212  VAL   B C   1 
ATOM   4263  O  O   . VAL   B 2 212 ? 9.565   25.984  -1.962  1.00 95.21  ? 212  VAL   B O   1 
ATOM   4264  C  CB  . VAL   B 2 212 ? 10.961  25.673  1.222   1.00 100.25 ? 212  VAL   B CB  1 
ATOM   4265  C  CG1 . VAL   B 2 212 ? 11.951  26.536  0.465   1.00 103.36 ? 212  VAL   B CG1 1 
ATOM   4266  C  CG2 . VAL   B 2 212 ? 10.289  26.403  2.387   1.00 105.02 ? 212  VAL   B CG2 1 
ATOM   4267  N  N   . GLU   B 2 213 ? 8.927   27.316  -0.265  1.00 93.24  ? 213  GLU   B N   1 
ATOM   4268  C  CA  . GLU   B 2 213 ? 8.391   28.320  -1.141  1.00 92.07  ? 213  GLU   B CA  1 
ATOM   4269  C  C   . GLU   B 2 213 ? 9.374   28.681  -2.263  1.00 94.59  ? 213  GLU   B C   1 
ATOM   4270  O  O   . GLU   B 2 213 ? 10.592  28.609  -2.065  1.00 96.75  ? 213  GLU   B O   1 
ATOM   4271  C  CB  . GLU   B 2 213 ? 8.030   29.615  -0.375  1.00 91.29  ? 213  GLU   B CB  1 
ATOM   4272  C  CG  . GLU   B 2 213 ? 7.360   30.720  -1.224  1.00 92.20  ? 213  GLU   B CG  1 
ATOM   4273  C  CD  . GLU   B 2 213 ? 7.755   32.133  -0.814  1.00 95.26  ? 213  GLU   B CD  1 
ATOM   4274  O  OE1 . GLU   B 2 213 ? 8.779   32.624  -1.332  1.00 95.74  ? 213  GLU   B OE1 1 
ATOM   4275  O  OE2 . GLU   B 2 213 ? 7.043   32.756  0.017   1.00 96.89  ? 213  GLU   B OE2 1 
ATOM   4276  N  N   . ALA   B 2 214 ? 8.840   29.073  -3.438  1.00 94.01  ? 214  ALA   B N   1 
ATOM   4277  C  CA  . ALA   B 2 214 ? 9.656   29.202  -4.647  1.00 89.28  ? 214  ALA   B CA  1 
ATOM   4278  C  C   . ALA   B 2 214 ? 10.388  30.536  -4.771  1.00 89.70  ? 214  ALA   B C   1 
ATOM   4279  O  O   . ALA   B 2 214 ? 11.353  30.613  -5.536  1.00 95.97  ? 214  ALA   B O   1 
ATOM   4280  C  CB  . ALA   B 2 214 ? 8.806   28.985  -5.901  1.00 91.63  ? 214  ALA   B CB  1 
ATOM   4281  N  N   . GLU   B 2 215 ? 9.954   31.588  -4.075  1.00 88.21  ? 215  GLU   B N   1 
ATOM   4282  C  CA  . GLU   B 2 215 ? 10.723  32.828  -3.997  1.00 89.19  ? 215  GLU   B CA  1 
ATOM   4283  C  C   . GLU   B 2 215 ? 11.424  32.961  -2.642  1.00 93.52  ? 215  GLU   B C   1 
ATOM   4284  O  O   . GLU   B 2 215 ? 11.642  34.074  -2.149  1.00 95.29  ? 215  GLU   B O   1 
ATOM   4285  C  CB  . GLU   B 2 215 ? 9.840   34.047  -4.277  1.00 85.87  ? 215  GLU   B CB  1 
ATOM   4286  N  N   . ALA   B 2 216 ? 11.770  31.827  -2.024  1.00 91.83  ? 216  ALA   B N   1 
ATOM   4287  C  CA  . ALA   B 2 216 ? 12.533  31.817  -0.782  1.00 87.32  ? 216  ALA   B CA  1 
ATOM   4288  C  C   . ALA   B 2 216 ? 13.947  32.327  -1.036  1.00 87.87  ? 216  ALA   B C   1 
ATOM   4289  O  O   . ALA   B 2 216 ? 14.724  31.685  -1.752  1.00 89.11  ? 216  ALA   B O   1 
ATOM   4290  C  CB  . ALA   B 2 216 ? 12.570  30.404  -0.213  1.00 87.24  ? 216  ALA   B CB  1 
ATOM   4291  N  N   . SER   B 2 217 ? 14.281  33.477  -0.439  1.00 86.67  ? 217  SER   B N   1 
ATOM   4292  C  CA  . SER   B 2 217 ? 15.553  34.156  -0.652  1.00 85.16  ? 217  SER   B CA  1 
ATOM   4293  C  C   . SER   B 2 217 ? 16.431  34.300  0.590   1.00 89.12  ? 217  SER   B C   1 
ATOM   4294  O  O   . SER   B 2 217 ? 17.651  34.441  0.440   1.00 90.60  ? 217  SER   B O   1 
ATOM   4295  C  CB  . SER   B 2 217 ? 15.297  35.557  -1.207  1.00 95.61  ? 217  SER   B CB  1 
ATOM   4296  O  OG  . SER   B 2 217 ? 14.251  36.175  -0.471  1.00 89.60  ? 217  SER   B OG  1 
ATOM   4297  N  N   . MET   B 2 218 ? 15.867  34.256  1.800   1.00 87.01  ? 218  MET   B N   1 
ATOM   4298  C  CA  . MET   B 2 218 ? 16.587  34.572  3.029   1.00 85.79  ? 218  MET   B CA  1 
ATOM   4299  C  C   . MET   B 2 218 ? 16.672  33.350  3.948   1.00 88.28  ? 218  MET   B C   1 
ATOM   4300  O  O   . MET   B 2 218 ? 15.648  32.741  4.273   1.00 88.49  ? 218  MET   B O   1 
ATOM   4301  C  CB  . MET   B 2 218 ? 15.900  35.738  3.754   1.00 84.35  ? 218  MET   B CB  1 
ATOM   4302  C  CG  . MET   B 2 218 ? 16.776  36.358  4.825   1.00 87.77  ? 218  MET   B CG  1 
ATOM   4303  S  SD  . MET   B 2 218 ? 16.322  38.022  5.333   1.00 97.35  ? 218  MET   B SD  1 
ATOM   4304  C  CE  . MET   B 2 218 ? 15.552  38.640  3.846   1.00 94.25  ? 218  MET   B CE  1 
ATOM   4305  N  N   . VAL   B 2 219 ? 17.889  32.996  4.369   1.00 86.90  ? 219  VAL   B N   1 
ATOM   4306  C  CA  . VAL   B 2 219 ? 18.118  32.006  5.418   1.00 79.83  ? 219  VAL   B CA  1 
ATOM   4307  C  C   . VAL   B 2 219 ? 18.633  32.766  6.624   1.00 82.98  ? 219  VAL   B C   1 
ATOM   4308  O  O   . VAL   B 2 219 ? 19.643  33.469  6.527   1.00 84.19  ? 219  VAL   B O   1 
ATOM   4309  C  CB  . VAL   B 2 219 ? 19.121  30.929  4.982   1.00 83.04  ? 219  VAL   B CB  1 
ATOM   4310  C  CG1 . VAL   B 2 219 ? 19.180  29.810  5.988   1.00 81.70  ? 219  VAL   B CG1 1 
ATOM   4311  C  CG2 . VAL   B 2 219 ? 18.731  30.370  3.637   1.00 87.19  ? 219  VAL   B CG2 1 
ATOM   4312  N  N   . ILE   B 2 220 ? 17.933  32.652  7.749   1.00 84.67  ? 220  ILE   B N   1 
ATOM   4313  C  CA  . ILE   B 2 220 ? 18.332  33.285  9.005   1.00 82.25  ? 220  ILE   B CA  1 
ATOM   4314  C  C   . ILE   B 2 220 ? 18.518  32.184  10.032  1.00 90.33  ? 220  ILE   B C   1 
ATOM   4315  O  O   . ILE   B 2 220 ? 17.555  31.469  10.350  1.00 93.30  ? 220  ILE   B O   1 
ATOM   4316  C  CB  . ILE   B 2 220 ? 17.288  34.286  9.519   1.00 83.31  ? 220  ILE   B CB  1 
ATOM   4317  C  CG1 . ILE   B 2 220 ? 16.905  35.300  8.447   1.00 87.83  ? 220  ILE   B CG1 1 
ATOM   4318  C  CG2 . ILE   B 2 220 ? 17.817  34.972  10.740  1.00 86.30  ? 220  ILE   B CG2 1 
ATOM   4319  C  CD1 . ILE   B 2 220 ? 15.628  36.030  8.758   1.00 83.95  ? 220  ILE   B CD1 1 
ATOM   4320  N  N   . ALA   B 2 221 ? 19.737  32.057  10.577  1.00 94.36  ? 221  ALA   B N   1 
ATOM   4321  C  CA  . ALA   B 2 221 ? 20.031  30.990  11.536  1.00 88.24  ? 221  ALA   B CA  1 
ATOM   4322  C  C   . ALA   B 2 221 ? 19.538  31.405  12.911  1.00 89.49  ? 221  ALA   B C   1 
ATOM   4323  O  O   . ALA   B 2 221 ? 19.935  32.447  13.440  1.00 88.39  ? 221  ALA   B O   1 
ATOM   4324  C  CB  . ALA   B 2 221 ? 21.523  30.666  11.572  1.00 83.34  ? 221  ALA   B CB  1 
ATOM   4325  N  N   . VAL   B 2 222 ? 18.655  30.604  13.483  1.00 90.76  ? 222  VAL   B N   1 
ATOM   4326  C  CA  . VAL   B 2 222 ? 18.113  30.904  14.807  1.00 95.65  ? 222  VAL   B CA  1 
ATOM   4327  C  C   . VAL   B 2 222 ? 19.118  30.444  15.861  1.00 94.20  ? 222  VAL   B C   1 
ATOM   4328  O  O   . VAL   B 2 222 ? 19.599  29.307  15.784  1.00 96.79  ? 222  VAL   B O   1 
ATOM   4329  C  CB  . VAL   B 2 222 ? 16.759  30.219  14.996  1.00 96.60  ? 222  VAL   B CB  1 
ATOM   4330  C  CG1 . VAL   B 2 222 ? 16.204  30.545  16.372  1.00 100.26 ? 222  VAL   B CG1 1 
ATOM   4331  C  CG2 . VAL   B 2 222 ? 15.783  30.650  13.910  1.00 89.32  ? 222  VAL   B CG2 1 
ATOM   4332  N  N   . PRO   B 2 223 ? 19.483  31.304  16.836  1.00 92.24  ? 223  PRO   B N   1 
ATOM   4333  C  CA  . PRO   B 2 223 ? 20.481  30.939  17.852  1.00 99.41  ? 223  PRO   B CA  1 
ATOM   4334  C  C   . PRO   B 2 223 ? 20.118  29.708  18.657  1.00 106.85 ? 223  PRO   B C   1 
ATOM   4335  O  O   . PRO   B 2 223 ? 19.017  29.161  18.522  1.00 105.54 ? 223  PRO   B O   1 
ATOM   4336  C  CB  . PRO   B 2 223 ? 20.533  32.185  18.754  1.00 100.08 ? 223  PRO   B CB  1 
ATOM   4337  C  CG  . PRO   B 2 223 ? 20.172  33.270  17.864  1.00 100.67 ? 223  PRO   B CG  1 
ATOM   4338  C  CD  . PRO   B 2 223 ? 19.108  32.712  16.945  1.00 100.09 ? 223  PRO   B CD  1 
ATOM   4339  N  N   . GLU   B 2 224 ? 21.038  29.295  19.526  1.00 110.76 ? 224  GLU   B N   1 
ATOM   4340  C  CA  . GLU   B 2 224 ? 20.874  28.010  20.189  1.00 113.23 ? 224  GLU   B CA  1 
ATOM   4341  C  C   . GLU   B 2 224 ? 19.578  27.885  20.992  1.00 114.04 ? 224  GLU   B C   1 
ATOM   4342  O  O   . GLU   B 2 224 ? 18.999  26.782  20.971  1.00 116.14 ? 224  GLU   B O   1 
ATOM   4343  C  CB  . GLU   B 2 224 ? 22.100  27.715  21.059  1.00 118.06 ? 224  GLU   B CB  1 
ATOM   4344  C  CG  . GLU   B 2 224 ? 22.205  26.239  21.489  1.00 127.06 ? 224  GLU   B CG  1 
ATOM   4345  C  CD  . GLU   B 2 224 ? 23.331  26.008  22.480  1.00 135.94 ? 224  GLU   B CD  1 
ATOM   4346  O  OE1 . GLU   B 2 224 ? 24.449  26.508  22.218  1.00 136.86 ? 224  GLU   B OE1 1 
ATOM   4347  O  OE2 . GLU   B 2 224 ? 23.096  25.352  23.525  1.00 142.02 ? 224  GLU   B OE2 1 
ATOM   4348  N  N   . PRO   B 2 225 ? 19.047  28.950  21.697  1.00 112.17 ? 225  PRO   B N   1 
ATOM   4349  C  CA  . PRO   B 2 225 ? 17.837  28.764  22.529  1.00 108.81 ? 225  PRO   B CA  1 
ATOM   4350  C  C   . PRO   B 2 225 ? 16.742  27.940  21.866  1.00 109.84 ? 225  PRO   B C   1 
ATOM   4351  O  O   . PRO   B 2 225 ? 16.228  26.987  22.455  1.00 109.54 ? 225  PRO   B O   1 
ATOM   4352  C  CB  . PRO   B 2 225 ? 17.368  30.198  22.785  1.00 106.88 ? 225  PRO   B CB  1 
ATOM   4353  C  CG  . PRO   B 2 225 ? 18.624  30.987  22.815  1.00 113.56 ? 225  PRO   B CG  1 
ATOM   4354  C  CD  . PRO   B 2 225 ? 19.621  30.296  21.886  1.00 111.84 ? 225  PRO   B CD  1 
ATOM   4355  N  N   . PHE   B 2 226 ? 16.391  28.262  20.631  1.00 110.06 ? 226  PHE   B N   1 
ATOM   4356  C  CA  . PHE   B 2 226 ? 15.423  27.458  19.900  1.00 104.69 ? 226  PHE   B CA  1 
ATOM   4357  C  C   . PHE   B 2 226 ? 16.057  26.622  18.787  1.00 105.20 ? 226  PHE   B C   1 
ATOM   4358  O  O   . PHE   B 2 226 ? 15.635  25.483  18.574  1.00 107.69 ? 226  PHE   B O   1 
ATOM   4359  C  CB  . PHE   B 2 226 ? 14.302  28.367  19.354  1.00 98.61  ? 226  PHE   B CB  1 
ATOM   4360  N  N   . GLY   B 2 227 ? 17.088  27.131  18.094  1.00 104.32 ? 227  GLY   B N   1 
ATOM   4361  C  CA  . GLY   B 2 227 ? 17.844  26.368  17.099  1.00 99.70  ? 227  GLY   B CA  1 
ATOM   4362  C  C   . GLY   B 2 227 ? 17.125  26.145  15.782  1.00 96.68  ? 227  GLY   B C   1 
ATOM   4363  O  O   . GLY   B 2 227 ? 15.910  25.988  15.787  1.00 98.58  ? 227  GLY   B O   1 
ATOM   4364  N  N   . GLY   B 2 228 ? 17.841  26.138  14.654  1.00 95.66  ? 228  GLY   B N   1 
ATOM   4365  C  CA  . GLY   B 2 228 ? 17.225  25.938  13.350  1.00 94.44  ? 228  GLY   B CA  1 
ATOM   4366  C  C   . GLY   B 2 228 ? 17.526  27.075  12.384  1.00 92.39  ? 228  GLY   B C   1 
ATOM   4367  O  O   . GLY   B 2 228 ? 18.584  27.703  12.476  1.00 95.63  ? 228  GLY   B O   1 
ATOM   4368  N  N   . ALA   B 2 229 ? 16.594  27.329  11.458  1.00 95.13  ? 229  ALA   B N   1 
ATOM   4369  C  CA  . ALA   B 2 229 ? 16.737  28.365  10.429  1.00 89.66  ? 229  ALA   B CA  1 
ATOM   4370  C  C   . ALA   B 2 229 ? 15.375  28.888  9.988   1.00 87.43  ? 229  ALA   B C   1 
ATOM   4371  O  O   . ALA   B 2 229 ? 14.401  28.141  9.954   1.00 90.71  ? 229  ALA   B O   1 
ATOM   4372  C  CB  . ALA   B 2 229 ? 17.494  27.864  9.194   1.00 88.37  ? 229  ALA   B CB  1 
ATOM   4373  N  N   . ILE   B 2 230 ? 15.310  30.173  9.643   1.00 85.84  ? 230  ILE   B N   1 
ATOM   4374  C  CA  . ILE   B 2 230 ? 14.092  30.803  9.134   1.00 89.14  ? 230  ILE   B CA  1 
ATOM   4375  C  C   . ILE   B 2 230 ? 14.274  31.076  7.642   1.00 89.82  ? 230  ILE   B C   1 
ATOM   4376  O  O   . ILE   B 2 230 ? 15.306  31.621  7.224   1.00 88.60  ? 230  ILE   B O   1 
ATOM   4377  C  CB  . ILE   B 2 230 ? 13.756  32.092  9.901   1.00 83.34  ? 230  ILE   B CB  1 
ATOM   4378  C  CG1 . ILE   B 2 230 ? 13.381  31.739  11.325  1.00 83.81  ? 230  ILE   B CG1 1 
ATOM   4379  C  CG2 . ILE   B 2 230 ? 12.622  32.831  9.248   1.00 83.41  ? 230  ILE   B CG2 1 
ATOM   4380  C  CD1 . ILE   B 2 230 ? 13.327  32.902  12.257  1.00 89.06  ? 230  ILE   B CD1 1 
ATOM   4381  N  N   . ILE   B 2 231 ? 13.288  30.665  6.835   1.00 90.25  ? 231  ILE   B N   1 
ATOM   4382  C  CA  . ILE   B 2 231 ? 13.317  30.862  5.387   1.00 88.02  ? 231  ILE   B CA  1 
ATOM   4383  C  C   . ILE   B 2 231 ? 12.300  31.931  5.004   1.00 89.11  ? 231  ILE   B C   1 
ATOM   4384  O  O   . ILE   B 2 231 ? 11.120  31.652  4.777   1.00 91.44  ? 231  ILE   B O   1 
ATOM   4385  C  CB  . ILE   B 2 231 ? 13.043  29.550  4.616   1.00 87.03  ? 231  ILE   B CB  1 
ATOM   4386  C  CG1 . ILE   B 2 231 ? 13.800  28.379  5.219   1.00 89.18  ? 231  ILE   B CG1 1 
ATOM   4387  C  CG2 . ILE   B 2 231 ? 13.529  29.654  3.217   1.00 85.23  ? 231  ILE   B CG2 1 
ATOM   4388  C  CD1 . ILE   B 2 231 ? 15.291  28.479  5.044   1.00 88.77  ? 231  ILE   B CD1 1 
ATOM   4389  N  N   . ILE   B 2 232 ? 12.762  33.185  4.918   1.00 87.50  ? 232  ILE   B N   1 
ATOM   4390  C  CA  . ILE   B 2 232 ? 11.878  34.266  4.507   1.00 89.74  ? 232  ILE   B CA  1 
ATOM   4391  C  C   . ILE   B 2 232 ? 11.676  34.186  3.001   1.00 92.03  ? 232  ILE   B C   1 
ATOM   4392  O  O   . ILE   B 2 232 ? 12.620  33.947  2.234   1.00 93.45  ? 232  ILE   B O   1 
ATOM   4393  C  CB  . ILE   B 2 232 ? 12.448  35.628  4.936   1.00 89.06  ? 232  ILE   B CB  1 
ATOM   4394  C  CG1 . ILE   B 2 232 ? 12.781  35.600  6.426   1.00 92.25  ? 232  ILE   B CG1 1 
ATOM   4395  C  CG2 . ILE   B 2 232 ? 11.427  36.719  4.656   1.00 94.82  ? 232  ILE   B CG2 1 
ATOM   4396  C  CD1 . ILE   B 2 232 ? 11.534  35.696  7.381   1.00 96.15  ? 232  ILE   B CD1 1 
ATOM   4397  N  N   . GLY   B 2 233 ? 10.426  34.319  2.578   1.00 100.28 ? 233  GLY   B N   1 
ATOM   4398  C  CA  . GLY   B 2 233 ? 10.040  34.262  1.186   1.00 99.61  ? 233  GLY   B CA  1 
ATOM   4399  C  C   . GLY   B 2 233 ? 9.260   35.492  0.753   1.00 100.60 ? 233  GLY   B C   1 
ATOM   4400  O  O   . GLY   B 2 233 ? 9.286   36.547  1.407   1.00 100.57 ? 233  GLY   B O   1 
ATOM   4401  N  N   . GLN   B 2 234 ? 8.568   35.357  -0.385  1.00 93.14  ? 234  GLN   B N   1 
ATOM   4402  C  CA  . GLN   B 2 234 ? 7.718   36.417  -0.916  1.00 91.94  ? 234  GLN   B CA  1 
ATOM   4403  C  C   . GLN   B 2 234 ? 6.410   36.518  -0.131  1.00 97.36  ? 234  GLN   B C   1 
ATOM   4404  O  O   . GLN   B 2 234 ? 5.994   37.612  0.294   1.00 101.27 ? 234  GLN   B O   1 
ATOM   4405  C  CB  . GLN   B 2 234 ? 7.459   36.172  -2.396  1.00 87.01  ? 234  GLN   B CB  1 
ATOM   4406  N  N   . GLU   B 2 235 ? 5.767   35.371  0.101   1.00 92.86  ? 235  GLU   B N   1 
ATOM   4407  C  CA  . GLU   B 2 235 ? 4.466   35.308  0.741   1.00 91.79  ? 235  GLU   B CA  1 
ATOM   4408  C  C   . GLU   B 2 235 ? 4.503   34.691  2.130   1.00 97.00  ? 235  GLU   B C   1 
ATOM   4409  O  O   . GLU   B 2 235 ? 3.605   34.967  2.937   1.00 101.54 ? 235  GLU   B O   1 
ATOM   4410  C  CB  . GLU   B 2 235 ? 3.482   34.514  -0.136  1.00 88.07  ? 235  GLU   B CB  1 
ATOM   4411  N  N   . SER   B 2 236 ? 5.526   33.879  2.434   1.00 94.11  ? 236  SER   B N   1 
ATOM   4412  C  CA  . SER   B 2 236 ? 5.576   33.116  3.674   1.00 93.40  ? 236  SER   B CA  1 
ATOM   4413  C  C   . SER   B 2 236 ? 6.927   33.263  4.350   1.00 94.36  ? 236  SER   B C   1 
ATOM   4414  O  O   . SER   B 2 236 ? 7.903   33.717  3.752   1.00 95.20  ? 236  SER   B O   1 
ATOM   4415  C  CB  . SER   B 2 236 ? 5.316   31.627  3.453   1.00 93.84  ? 236  SER   B CB  1 
ATOM   4416  O  OG  . SER   B 2 236 ? 6.381   31.020  2.737   1.00 99.19  ? 236  SER   B OG  1 
ATOM   4417  N  N   . ILE   B 2 237 ? 6.965   32.841  5.611   1.00 95.77  ? 237  ILE   B N   1 
ATOM   4418  C  CA  . ILE   B 2 237 ? 8.147   32.868  6.467   1.00 93.40  ? 237  ILE   B CA  1 
ATOM   4419  C  C   . ILE   B 2 237 ? 8.137   31.544  7.222   1.00 94.83  ? 237  ILE   B C   1 
ATOM   4420  O  O   . ILE   B 2 237 ? 7.299   31.332  8.104   1.00 102.03 ? 237  ILE   B O   1 
ATOM   4421  C  CB  . ILE   B 2 237 ? 8.108   34.096  7.410   1.00 97.07  ? 237  ILE   B CB  1 
ATOM   4422  C  CG1 . ILE   B 2 237 ? 8.466   35.378  6.662   1.00 96.44  ? 237  ILE   B CG1 1 
ATOM   4423  C  CG2 . ILE   B 2 237 ? 9.018   33.952  8.600   1.00 95.47  ? 237  ILE   B CG2 1 
ATOM   4424  C  CD1 . ILE   B 2 237 ? 8.127   36.637  7.444   1.00 95.29  ? 237  ILE   B CD1 1 
ATOM   4425  N  N   . THR   B 2 238 ? 9.004   30.610  6.857   1.00 94.06  ? 238  THR   B N   1 
ATOM   4426  C  CA  . THR   B 2 238 ? 8.974   29.288  7.461   1.00 95.75  ? 238  THR   B CA  1 
ATOM   4427  C  C   . THR   B 2 238 ? 10.207  29.081  8.348   1.00 96.48  ? 238  THR   B C   1 
ATOM   4428  O  O   . THR   B 2 238 ? 11.288  29.608  8.073   1.00 92.53  ? 238  THR   B O   1 
ATOM   4429  C  CB  . THR   B 2 238 ? 8.855   28.177  6.379   1.00 104.62 ? 238  THR   B CB  1 
ATOM   4430  O  OG1 . THR   B 2 238 ? 10.045  28.077  5.586   1.00 106.51 ? 238  THR   B OG1 1 
ATOM   4431  C  CG2 . THR   B 2 238 ? 7.713   28.479  5.425   1.00 105.08 ? 238  THR   B CG2 1 
ATOM   4432  N  N   . TYR   B 2 239 ? 10.003  28.373  9.470   1.00 105.55 ? 239  TYR   B N   1 
ATOM   4433  C  CA  . TYR   B 2 239 ? 11.062  27.940  10.386  1.00 102.80 ? 239  TYR   B CA  1 
ATOM   4434  C  C   . TYR   B 2 239 ? 11.262  26.429  10.255  1.00 103.58 ? 239  TYR   B C   1 
ATOM   4435  O  O   . TYR   B 2 239 ? 10.291  25.675  10.141  1.00 102.73 ? 239  TYR   B O   1 
ATOM   4436  C  CB  . TYR   B 2 239 ? 10.735  28.315  11.848  1.00 98.73  ? 239  TYR   B CB  1 
ATOM   4437  C  CG  . TYR   B 2 239 ? 11.566  27.573  12.885  1.00 102.56 ? 239  TYR   B CG  1 
ATOM   4438  C  CD1 . TYR   B 2 239 ? 11.217  26.290  13.275  1.00 106.13 ? 239  TYR   B CD1 1 
ATOM   4439  C  CD2 . TYR   B 2 239 ? 12.686  28.152  13.478  1.00 99.59  ? 239  TYR   B CD2 1 
ATOM   4440  C  CE1 . TYR   B 2 239 ? 11.946  25.594  14.192  1.00 103.60 ? 239  TYR   B CE1 1 
ATOM   4441  C  CE2 . TYR   B 2 239 ? 13.431  27.458  14.413  1.00 96.52  ? 239  TYR   B CE2 1 
ATOM   4442  C  CZ  . TYR   B 2 239 ? 13.047  26.170  14.768  1.00 102.47 ? 239  TYR   B CZ  1 
ATOM   4443  O  OH  . TYR   B 2 239 ? 13.742  25.425  15.700  1.00 101.53 ? 239  TYR   B OH  1 
ATOM   4444  N  N   . HIS   B 2 240 ? 12.524  25.988  10.281  1.00 108.67 ? 240  HIS   B N   1 
ATOM   4445  C  CA  . HIS   B 2 240 ? 12.890  24.599  10.004  1.00 111.13 ? 240  HIS   B CA  1 
ATOM   4446  C  C   . HIS   B 2 240 ? 13.945  24.128  11.000  1.00 109.32 ? 240  HIS   B C   1 
ATOM   4447  O  O   . HIS   B 2 240 ? 14.963  24.800  11.189  1.00 108.64 ? 240  HIS   B O   1 
ATOM   4448  C  CB  . HIS   B 2 240 ? 13.434  24.438  8.571   1.00 110.27 ? 240  HIS   B CB  1 
ATOM   4449  C  CG  . HIS   B 2 240 ? 12.419  24.664  7.496   1.00 111.99 ? 240  HIS   B CG  1 
ATOM   4450  N  ND1 . HIS   B 2 240 ? 11.708  23.638  6.915   1.00 115.75 ? 240  HIS   B ND1 1 
ATOM   4451  C  CD2 . HIS   B 2 240 ? 12.007  25.799  6.884   1.00 112.00 ? 240  HIS   B CD2 1 
ATOM   4452  C  CE1 . HIS   B 2 240 ? 10.897  24.131  5.995   1.00 117.51 ? 240  HIS   B CE1 1 
ATOM   4453  N  NE2 . HIS   B 2 240 ? 11.058  25.442  5.957   1.00 115.30 ? 240  HIS   B NE2 1 
ATOM   4454  N  N   . ASN   B 2 241 ? 13.712  22.975  11.634  1.00 105.62 ? 241  ASN   B N   1 
ATOM   4455  C  CA  . ASN   B 2 241 ? 14.740  22.391  12.497  1.00 103.32 ? 241  ASN   B CA  1 
ATOM   4456  C  C   . ASN   B 2 241 ? 14.398  20.917  12.713  1.00 107.33 ? 241  ASN   B C   1 
ATOM   4457  O  O   . ASN   B 2 241 ? 13.673  20.577  13.645  1.00 111.68 ? 241  ASN   B O   1 
ATOM   4458  C  CB  . ASN   B 2 241 ? 14.857  23.109  13.819  1.00 103.49 ? 241  ASN   B CB  1 
ATOM   4459  C  CG  . ASN   B 2 241 ? 16.103  22.718  14.559  1.00 102.29 ? 241  ASN   B CG  1 
ATOM   4460  O  OD1 . ASN   B 2 241 ? 17.096  22.323  13.938  1.00 104.14 ? 241  ASN   B OD1 1 
ATOM   4461  N  ND2 . ASN   B 2 241 ? 16.065  22.797  15.887  1.00 102.07 ? 241  ASN   B ND2 1 
ATOM   4462  N  N   . GLY   B 2 242 ? 14.963  20.063  11.863  1.00 110.42 ? 242  GLY   B N   1 
ATOM   4463  C  CA  . GLY   B 2 242 ? 14.757  18.630  11.937  1.00 109.10 ? 242  GLY   B CA  1 
ATOM   4464  C  C   . GLY   B 2 242 ? 13.280  18.355  12.080  1.00 113.91 ? 242  GLY   B C   1 
ATOM   4465  O  O   . GLY   B 2 242 ? 12.478  18.686  11.204  1.00 111.99 ? 242  GLY   B O   1 
ATOM   4466  N  N   . ASP   B 2 243 ? 12.923  17.756  13.218  1.00 120.34 ? 243  ASP   B N   1 
ATOM   4467  C  CA  . ASP   B 2 243 ? 11.523  17.464  13.509  1.00 125.94 ? 243  ASP   B CA  1 
ATOM   4468  C  C   . ASP   B 2 243 ? 10.593  18.665  13.344  1.00 128.69 ? 243  ASP   B C   1 
ATOM   4469  O  O   . ASP   B 2 243 ? 9.556   18.575  12.670  1.00 129.46 ? 243  ASP   B O   1 
ATOM   4470  C  CB  . ASP   B 2 243 ? 11.392  16.867  14.912  1.00 127.41 ? 243  ASP   B CB  1 
ATOM   4471  N  N   . LYS   B 2 244 ? 10.961  19.807  13.945  1.00 123.17 ? 244  LYS   B N   1 
ATOM   4472  C  CA  . LYS   B 2 244 ? 10.067  20.959  14.034  1.00 117.54 ? 244  LYS   B CA  1 
ATOM   4473  C  C   . LYS   B 2 244 ? 9.952   21.689  12.702  1.00 113.82 ? 244  LYS   B C   1 
ATOM   4474  O  O   . LYS   B 2 244 ? 10.918  21.792  11.941  1.00 111.49 ? 244  LYS   B O   1 
ATOM   4475  C  CB  . LYS   B 2 244 ? 10.570  21.927  15.106  1.00 112.77 ? 244  LYS   B CB  1 
ATOM   4476  N  N   . TYR   B 2 245 ? 8.748   22.197  12.426  1.00 118.61 ? 245  TYR   B N   1 
ATOM   4477  C  CA  . TYR   B 2 245 ? 8.491   22.978  11.215  1.00 119.64 ? 245  TYR   B CA  1 
ATOM   4478  C  C   . TYR   B 2 245 ? 7.233   23.820  11.425  1.00 118.64 ? 245  TYR   B C   1 
ATOM   4479  O  O   . TYR   B 2 245 ? 6.128   23.271  11.484  1.00 121.94 ? 245  TYR   B O   1 
ATOM   4480  C  CB  . TYR   B 2 245 ? 8.344   22.067  9.998   1.00 120.85 ? 245  TYR   B CB  1 
ATOM   4481  C  CG  . TYR   B 2 245 ? 7.728   22.758  8.799   1.00 118.12 ? 245  TYR   B CG  1 
ATOM   4482  C  CD1 . TYR   B 2 245 ? 8.201   23.993  8.379   1.00 118.61 ? 245  TYR   B CD1 1 
ATOM   4483  C  CD2 . TYR   B 2 245 ? 6.681   22.181  8.086   1.00 115.69 ? 245  TYR   B CD2 1 
ATOM   4484  C  CE1 . TYR   B 2 245 ? 7.654   24.644  7.286   1.00 118.53 ? 245  TYR   B CE1 1 
ATOM   4485  C  CE2 . TYR   B 2 245 ? 6.127   22.821  6.984   1.00 120.64 ? 245  TYR   B CE2 1 
ATOM   4486  C  CZ  . TYR   B 2 245 ? 6.623   24.065  6.585   1.00 121.62 ? 245  TYR   B CZ  1 
ATOM   4487  O  OH  . TYR   B 2 245 ? 6.124   24.771  5.499   1.00 121.79 ? 245  TYR   B OH  1 
ATOM   4488  N  N   . LEU   B 2 246 ? 7.404   25.145  11.522  1.00 111.46 ? 246  LEU   B N   1 
ATOM   4489  C  CA  . LEU   B 2 246 ? 6.315   26.112  11.600  1.00 107.79 ? 246  LEU   B CA  1 
ATOM   4490  C  C   . LEU   B 2 246 ? 6.377   27.067  10.413  1.00 108.11 ? 246  LEU   B C   1 
ATOM   4491  O  O   . LEU   B 2 246 ? 7.464   27.454  9.982   1.00 110.95 ? 246  LEU   B O   1 
ATOM   4492  C  CB  . LEU   B 2 246 ? 6.385   26.917  12.891  1.00 105.44 ? 246  LEU   B CB  1 
ATOM   4493  C  CG  . LEU   B 2 246 ? 5.336   26.527  13.921  1.00 112.21 ? 246  LEU   B CG  1 
ATOM   4494  C  CD1 . LEU   B 2 246 ? 5.227   27.600  15.008  1.00 117.46 ? 246  LEU   B CD1 1 
ATOM   4495  C  CD2 . LEU   B 2 246 ? 3.985   26.252  13.250  1.00 110.73 ? 246  LEU   B CD2 1 
ATOM   4496  N  N   . ALA   B 2 247 ? 5.212   27.482  9.909   1.00 105.87 ? 247  ALA   B N   1 
ATOM   4497  C  CA  . ALA   B 2 247 ? 5.170   28.367  8.750   1.00 99.86  ? 247  ALA   B CA  1 
ATOM   4498  C  C   . ALA   B 2 247 ? 3.941   29.268  8.809   1.00 100.35 ? 247  ALA   B C   1 
ATOM   4499  O  O   . ALA   B 2 247 ? 2.817   28.777  8.945   1.00 104.14 ? 247  ALA   B O   1 
ATOM   4500  C  CB  . ALA   B 2 247 ? 5.161   27.550  7.463   1.00 101.16 ? 247  ALA   B CB  1 
ATOM   4501  N  N   . ILE   B 2 248 ? 4.161   30.577  8.695   1.00 101.49 ? 248  ILE   B N   1 
ATOM   4502  C  CA  . ILE   B 2 248 ? 3.103   31.582  8.649   1.00 100.78 ? 248  ILE   B CA  1 
ATOM   4503  C  C   . ILE   B 2 248 ? 3.179   32.308  7.315   1.00 107.32 ? 248  ILE   B C   1 
ATOM   4504  O  O   . ILE   B 2 248 ? 4.238   32.374  6.676   1.00 105.27 ? 248  ILE   B O   1 
ATOM   4505  C  CB  . ILE   B 2 248 ? 3.217   32.590  9.805   1.00 103.96 ? 248  ILE   B CB  1 
ATOM   4506  C  CG1 . ILE   B 2 248 ? 4.489   33.422  9.635   1.00 103.48 ? 248  ILE   B CG1 1 
ATOM   4507  C  CG2 . ILE   B 2 248 ? 3.200   31.859  11.151  1.00 106.41 ? 248  ILE   B CG2 1 
ATOM   4508  C  CD1 . ILE   B 2 248 ? 4.638   34.505  10.659  1.00 111.30 ? 248  ILE   B CD1 1 
ATOM   4509  N  N   . ALA   B 2 249 ? 2.032   32.857  6.894   1.00 109.75 ? 249  ALA   B N   1 
ATOM   4510  C  CA  . ALA   B 2 249 ? 1.918   33.674  5.684   1.00 106.53 ? 249  ALA   B CA  1 
ATOM   4511  C  C   . ALA   B 2 249 ? 1.307   35.010  6.099   1.00 112.21 ? 249  ALA   B C   1 
ATOM   4512  O  O   . ALA   B 2 249 ? 0.107   35.248  5.886   1.00 117.55 ? 249  ALA   B O   1 
ATOM   4513  C  CB  . ALA   B 2 249 ? 1.073   32.985  4.615   1.00 102.67 ? 249  ALA   B CB  1 
ATOM   4514  N  N   . PRO   B 2 250 ? 2.085   35.884  6.719   1.00 123.85 ? 250  PRO   B N   1 
ATOM   4515  C  CA  . PRO   B 2 250 ? 1.528   37.119  7.265   1.00 121.44 ? 250  PRO   B CA  1 
ATOM   4516  C  C   . PRO   B 2 250 ? 0.862   37.923  6.175   1.00 116.85 ? 250  PRO   B C   1 
ATOM   4517  O  O   . PRO   B 2 250 ? 1.415   38.094  5.079   1.00 119.93 ? 250  PRO   B O   1 
ATOM   4518  C  CB  . PRO   B 2 250 ? 2.748   37.862  7.820   1.00 124.14 ? 250  PRO   B CB  1 
ATOM   4519  C  CG  . PRO   B 2 250 ? 3.805   36.829  7.959   1.00 125.37 ? 250  PRO   B CG  1 
ATOM   4520  C  CD  . PRO   B 2 250 ? 3.548   35.826  6.869   1.00 125.09 ? 250  PRO   B CD  1 
ATOM   4521  N  N   . PRO   B 2 251 ? -0.332  38.431  6.443   1.00 114.37 ? 251  PRO   B N   1 
ATOM   4522  C  CA  . PRO   B 2 251 ? -0.964  39.311  5.461   1.00 112.99 ? 251  PRO   B CA  1 
ATOM   4523  C  C   . PRO   B 2 251 ? -0.121  40.526  5.156   1.00 114.68 ? 251  PRO   B C   1 
ATOM   4524  O  O   . PRO   B 2 251 ? 0.063   40.874  3.979   1.00 117.65 ? 251  PRO   B O   1 
ATOM   4525  C  CB  . PRO   B 2 251 ? -2.275  39.689  6.151   1.00 116.71 ? 251  PRO   B CB  1 
ATOM   4526  C  CG  . PRO   B 2 251 ? -1.925  39.637  7.623   1.00 114.73 ? 251  PRO   B CG  1 
ATOM   4527  C  CD  . PRO   B 2 251 ? -1.022  38.443  7.739   1.00 115.64 ? 251  PRO   B CD  1 
ATOM   4528  N  N   . ILE   B 2 252 ? 0.406   41.186  6.189   1.00 112.67 ? 252  ILE   B N   1 
ATOM   4529  C  CA  . ILE   B 2 252 ? 1.017   42.491  5.990   1.00 111.29 ? 252  ILE   B CA  1 
ATOM   4530  C  C   . ILE   B 2 252 ? 2.240   42.388  5.078   1.00 115.50 ? 252  ILE   B C   1 
ATOM   4531  O  O   . ILE   B 2 252 ? 2.504   43.293  4.269   1.00 117.19 ? 252  ILE   B O   1 
ATOM   4532  C  CB  . ILE   B 2 252 ? 1.341   43.124  7.356   1.00 104.81 ? 252  ILE   B CB  1 
ATOM   4533  C  CG1 . ILE   B 2 252 ? 2.055   44.455  7.168   1.00 108.36 ? 252  ILE   B CG1 1 
ATOM   4534  C  CG2 . ILE   B 2 252 ? 2.156   42.180  8.172   1.00 108.20 ? 252  ILE   B CG2 1 
ATOM   4535  C  CD1 . ILE   B 2 252 ? 1.284   45.453  6.323   1.00 115.07 ? 252  ILE   B CD1 1 
ATOM   4536  N  N   . ILE   B 2 253 ? 2.971   41.268  5.149   1.00 113.50 ? 253  ILE   B N   1 
ATOM   4537  C  CA  . ILE   B 2 253 ? 4.184   41.110  4.346   1.00 114.85 ? 253  ILE   B CA  1 
ATOM   4538  C  C   . ILE   B 2 253 ? 3.908   40.829  2.878   1.00 118.70 ? 253  ILE   B C   1 
ATOM   4539  O  O   . ILE   B 2 253 ? 4.837   40.863  2.061   1.00 118.45 ? 253  ILE   B O   1 
ATOM   4540  C  CB  . ILE   B 2 253 ? 5.101   39.972  4.843   1.00 111.86 ? 253  ILE   B CB  1 
ATOM   4541  C  CG1 . ILE   B 2 253 ? 4.611   38.610  4.348   1.00 111.93 ? 253  ILE   B CG1 1 
ATOM   4542  C  CG2 . ILE   B 2 253 ? 5.229   40.011  6.329   1.00 111.67 ? 253  ILE   B CG2 1 
ATOM   4543  C  CD1 . ILE   B 2 253 ? 5.714   37.586  4.336   1.00 107.44 ? 253  ILE   B CD1 1 
ATOM   4544  N  N   . LYS   B 2 254 ? 2.665   40.535  2.518   1.00 118.85 ? 254  LYS   B N   1 
ATOM   4545  C  CA  . LYS   B 2 254 ? 2.388   40.259  1.121   1.00 117.53 ? 254  LYS   B CA  1 
ATOM   4546  C  C   . LYS   B 2 254 ? 2.536   41.506  0.240   1.00 121.71 ? 254  LYS   B C   1 
ATOM   4547  O  O   . LYS   B 2 254 ? 2.607   41.360  -0.984  1.00 127.12 ? 254  LYS   B O   1 
ATOM   4548  C  CB  . LYS   B 2 254 ? 0.986   39.631  0.983   1.00 111.48 ? 254  LYS   B CB  1 
ATOM   4549  N  N   . GLN   B 2 255 ? 2.631   42.711  0.816   1.00 125.83 ? 255  GLN   B N   1 
ATOM   4550  C  CA  . GLN   B 2 255 ? 2.634   43.917  -0.019  1.00 126.18 ? 255  GLN   B CA  1 
ATOM   4551  C  C   . GLN   B 2 255 ? 4.022   44.254  -0.571  1.00 126.74 ? 255  GLN   B C   1 
ATOM   4552  O  O   . GLN   B 2 255 ? 4.119   44.930  -1.601  1.00 127.23 ? 255  GLN   B O   1 
ATOM   4553  C  CB  . GLN   B 2 255 ? 2.087   45.116  0.760   1.00 125.15 ? 255  GLN   B CB  1 
ATOM   4554  N  N   . SER   B 2 256 ? 5.096   43.833  0.099   1.00 124.77 ? 256  SER   B N   1 
ATOM   4555  C  CA  . SER   B 2 256 ? 6.449   44.045  -0.420  1.00 123.22 ? 256  SER   B CA  1 
ATOM   4556  C  C   . SER   B 2 256 ? 7.301   42.829  -0.095  1.00 120.82 ? 256  SER   B C   1 
ATOM   4557  O  O   . SER   B 2 256 ? 6.816   41.826  0.436   1.00 124.12 ? 256  SER   B O   1 
ATOM   4558  C  CB  . SER   B 2 256 ? 7.096   45.318  0.134   1.00 119.47 ? 256  SER   B CB  1 
ATOM   4559  O  OG  . SER   B 2 256 ? 8.400   45.492  -0.411  1.00 116.03 ? 256  SER   B OG  1 
ATOM   4560  N  N   . THR   B 2 257 ? 8.594   42.920  -0.394  1.00 109.48 ? 257  THR   B N   1 
ATOM   4561  C  CA  . THR   B 2 257 ? 9.507   41.797  -0.233  1.00 110.72 ? 257  THR   B CA  1 
ATOM   4562  C  C   . THR   B 2 257 ? 10.566  42.140  0.799   1.00 107.64 ? 257  THR   B C   1 
ATOM   4563  O  O   . THR   B 2 257 ? 11.160  43.222  0.740   1.00 102.58 ? 257  THR   B O   1 
ATOM   4564  C  CB  . THR   B 2 257 ? 10.187  41.417  -1.552  1.00 112.12 ? 257  THR   B CB  1 
ATOM   4565  O  OG1 . THR   B 2 257 ? 9.208   40.930  -2.491  1.00 109.31 ? 257  THR   B OG1 1 
ATOM   4566  C  CG2 . THR   B 2 257 ? 11.259  40.329  -1.295  1.00 113.52 ? 257  THR   B CG2 1 
ATOM   4567  N  N   . ILE   B 2 258 ? 10.795  41.224  1.744   1.00 111.00 ? 258  ILE   B N   1 
ATOM   4568  C  CA  . ILE   B 2 258 ? 11.805  41.416  2.780   1.00 108.63 ? 258  ILE   B CA  1 
ATOM   4569  C  C   . ILE   B 2 258 ? 13.186  41.155  2.184   1.00 108.54 ? 258  ILE   B C   1 
ATOM   4570  O  O   . ILE   B 2 258 ? 13.395  40.148  1.489   1.00 106.58 ? 258  ILE   B O   1 
ATOM   4571  C  CB  . ILE   B 2 258 ? 11.540  40.498  3.980   1.00 109.20 ? 258  ILE   B CB  1 
ATOM   4572  C  CG1 . ILE   B 2 258 ? 10.070  40.553  4.415   1.00 108.63 ? 258  ILE   B CG1 1 
ATOM   4573  C  CG2 . ILE   B 2 258 ? 12.446  40.895  5.114   1.00 106.32 ? 258  ILE   B CG2 1 
ATOM   4574  C  CD1 . ILE   B 2 258 ? 9.699   41.804  5.164   1.00 106.19 ? 258  ILE   B CD1 1 
ATOM   4575  N  N   . VAL   B 2 259 ? 14.128  42.055  2.478   1.00 103.72 ? 259  VAL   B N   1 
ATOM   4576  C  CA  . VAL   B 2 259 ? 15.429  42.110  1.827   1.00 98.28  ? 259  VAL   B CA  1 
ATOM   4577  C  C   . VAL   B 2 259 ? 16.539  42.179  2.874   1.00 101.29 ? 259  VAL   B C   1 
ATOM   4578  O  O   . VAL   B 2 259 ? 17.655  41.720  2.624   1.00 104.10 ? 259  VAL   B O   1 
ATOM   4579  C  CB  . VAL   B 2 259 ? 15.496  43.304  0.859   1.00 96.74  ? 259  VAL   B CB  1 
ATOM   4580  C  CG1 . VAL   B 2 259 ? 14.692  43.022  -0.376  1.00 96.97  ? 259  VAL   B CG1 1 
ATOM   4581  C  CG2 . VAL   B 2 259 ? 14.965  44.539  1.537   1.00 97.90  ? 259  VAL   B CG2 1 
ATOM   4582  N  N   . CYS   B 2 260 ? 16.262  42.754  4.043   1.00 98.48  ? 260  CYS   B N   1 
ATOM   4583  C  CA  . CYS   B 2 260 ? 17.252  42.816  5.114   1.00 98.51  ? 260  CYS   B CA  1 
ATOM   4584  C  C   . CYS   B 2 260 ? 16.657  42.347  6.438   1.00 99.91  ? 260  CYS   B C   1 
ATOM   4585  O  O   . CYS   B 2 260 ? 15.443  42.398  6.669   1.00 100.68 ? 260  CYS   B O   1 
ATOM   4586  C  CB  . CYS   B 2 260 ? 17.801  44.230  5.278   1.00 100.96 ? 260  CYS   B CB  1 
ATOM   4587  S  SG  . CYS   B 2 260 ? 16.450  45.418  5.390   1.00 110.02 ? 260  CYS   B SG  1 
ATOM   4588  N  N   . HIS   B 2 261 ? 17.551  41.927  7.325   1.00 96.16  ? 261  HIS   B N   1 
ATOM   4589  C  CA  . HIS   B 2 261 ? 17.156  41.304  8.572   1.00 90.92  ? 261  HIS   B CA  1 
ATOM   4590  C  C   . HIS   B 2 261 ? 18.285  41.494  9.570   1.00 92.87  ? 261  HIS   B C   1 
ATOM   4591  O  O   . HIS   B 2 261 ? 19.463  41.419  9.205   1.00 97.83  ? 261  HIS   B O   1 
ATOM   4592  C  CB  . HIS   B 2 261 ? 16.846  39.827  8.354   1.00 88.54  ? 261  HIS   B CB  1 
ATOM   4593  C  CG  . HIS   B 2 261 ? 18.008  38.912  8.614   1.00 93.19  ? 261  HIS   B CG  1 
ATOM   4594  N  ND1 . HIS   B 2 261 ? 18.998  38.670  7.683   1.00 95.42  ? 261  HIS   B ND1 1 
ATOM   4595  C  CD2 . HIS   B 2 261 ? 18.325  38.167  9.700   1.00 92.97  ? 261  HIS   B CD2 1 
ATOM   4596  C  CE1 . HIS   B 2 261 ? 19.875  37.818  8.184   1.00 91.97  ? 261  HIS   B CE1 1 
ATOM   4597  N  NE2 . HIS   B 2 261 ? 19.489  37.497  9.408   1.00 93.06  ? 261  HIS   B NE2 1 
ATOM   4598  N  N   . ASN   B 2 262 ? 17.933  41.781  10.816  1.00 93.20  ? 262  ASN   B N   1 
ATOM   4599  C  CA  . ASN   B 2 262 ? 18.927  41.921  11.868  1.00 96.37  ? 262  ASN   B CA  1 
ATOM   4600  C  C   . ASN   B 2 262 ? 18.377  41.312  13.137  1.00 97.90  ? 262  ASN   B C   1 
ATOM   4601  O  O   . ASN   B 2 262 ? 17.202  41.511  13.457  1.00 97.05  ? 262  ASN   B O   1 
ATOM   4602  C  CB  . ASN   B 2 262 ? 19.298  43.377  12.129  1.00 94.58  ? 262  ASN   B CB  1 
ATOM   4603  C  CG  . ASN   B 2 262 ? 20.303  43.507  13.249  1.00 97.51  ? 262  ASN   B CG  1 
ATOM   4604  O  OD1 . ASN   B 2 262 ? 19.939  43.783  14.394  1.00 100.15 ? 262  ASN   B OD1 1 
ATOM   4605  N  ND2 . ASN   B 2 262 ? 21.578  43.289  12.932  1.00 96.94  ? 262  ASN   B ND2 1 
ATOM   4606  N  N   . ARG   B 2 263 ? 19.215  40.583  13.870  1.00 97.82  ? 263  ARG   B N   1 
ATOM   4607  C  CA  . ARG   B 2 263 ? 18.738  39.982  15.105  1.00 99.09  ? 263  ARG   B CA  1 
ATOM   4608  C  C   . ARG   B 2 263 ? 18.760  41.035  16.204  1.00 105.42 ? 263  ARG   B C   1 
ATOM   4609  O  O   . ARG   B 2 263 ? 19.763  41.742  16.368  1.00 107.10 ? 263  ARG   B O   1 
ATOM   4610  C  CB  . ARG   B 2 263 ? 19.578  38.767  15.501  1.00 98.66  ? 263  ARG   B CB  1 
ATOM   4611  C  CG  . ARG   B 2 263 ? 18.762  37.773  16.345  1.00 100.77 ? 263  ARG   B CG  1 
ATOM   4612  C  CD  . ARG   B 2 263 ? 19.572  36.724  17.098  1.00 98.84  ? 263  ARG   B CD  1 
ATOM   4613  N  NE  . ARG   B 2 263 ? 20.716  36.205  16.362  1.00 96.07  ? 263  ARG   B NE  1 
ATOM   4614  C  CZ  . ARG   B 2 263 ? 21.976  36.484  16.672  1.00 98.89  ? 263  ARG   B CZ  1 
ATOM   4615  N  NH1 . ARG   B 2 263 ? 22.274  37.274  17.695  1.00 102.33 ? 263  ARG   B NH1 1 
ATOM   4616  N  NH2 . ARG   B 2 263 ? 22.962  35.954  15.946  1.00 91.30  ? 263  ARG   B NH2 1 
ATOM   4617  N  N   . VAL   B 2 264 ? 17.647  41.155  16.936  1.00 107.07 ? 264  VAL   B N   1 
ATOM   4618  C  CA  . VAL   B 2 264 ? 17.536  42.120  18.026  1.00 106.62 ? 264  VAL   B CA  1 
ATOM   4619  C  C   . VAL   B 2 264 ? 18.078  41.675  19.365  1.00 109.37 ? 264  VAL   B C   1 
ATOM   4620  O  O   . VAL   B 2 264 ? 18.961  42.328  19.935  1.00 109.39 ? 264  VAL   B O   1 
ATOM   4621  C  CB  . VAL   B 2 264 ? 16.073  42.489  18.311  1.00 110.05 ? 264  VAL   B CB  1 
ATOM   4622  C  CG1 . VAL   B 2 264 ? 16.009  43.536  19.395  1.00 117.39 ? 264  VAL   B CG1 1 
ATOM   4623  C  CG2 . VAL   B 2 264 ? 15.437  43.027  17.047  1.00 107.85 ? 264  VAL   B CG2 1 
ATOM   4624  N  N   . ASP   B 2 265 ? 17.568  40.575  19.883  1.00 118.48 ? 265  ASP   B N   1 
ATOM   4625  C  CA  . ASP   B 2 265 ? 18.083  40.088  21.144  1.00 122.19 ? 265  ASP   B CA  1 
ATOM   4626  C  C   . ASP   B 2 265 ? 19.132  39.060  20.723  1.00 119.92 ? 265  ASP   B C   1 
ATOM   4627  O  O   . ASP   B 2 265 ? 18.900  38.286  19.784  1.00 117.96 ? 265  ASP   B O   1 
ATOM   4628  C  CB  . ASP   B 2 265 ? 17.044  39.418  22.046  1.00 126.32 ? 265  ASP   B CB  1 
ATOM   4629  C  CG  . ASP   B 2 265 ? 17.608  39.000  23.421  1.00 128.08 ? 265  ASP   B CG  1 
ATOM   4630  O  OD1 . ASP   B 2 265 ? 18.819  39.250  23.687  1.00 125.00 ? 265  ASP   B OD1 1 
ATOM   4631  O  OD2 . ASP   B 2 265 ? 16.817  38.439  24.233  1.00 132.47 ? 265  ASP   B OD2 1 
ATOM   4632  N  N   . PRO   B 2 266 ? 20.283  39.015  21.401  1.00 115.10 ? 266  PRO   B N   1 
ATOM   4633  C  CA  . PRO   B 2 266 ? 21.225  37.906  21.163  1.00 111.24 ? 266  PRO   B CA  1 
ATOM   4634  C  C   . PRO   B 2 266 ? 20.558  36.558  21.290  1.00 109.81 ? 266  PRO   B C   1 
ATOM   4635  O  O   . PRO   B 2 266 ? 20.989  35.585  20.664  1.00 109.99 ? 266  PRO   B O   1 
ATOM   4636  C  CB  . PRO   B 2 266 ? 22.288  38.115  22.245  1.00 107.71 ? 266  PRO   B CB  1 
ATOM   4637  C  CG  . PRO   B 2 266 ? 22.193  39.568  22.604  1.00 106.91 ? 266  PRO   B CG  1 
ATOM   4638  C  CD  . PRO   B 2 266 ? 20.761  39.942  22.445  1.00 109.24 ? 266  PRO   B CD  1 
ATOM   4639  N  N   . ASN   B 2 267 ? 19.494  36.494  22.095  1.00 112.26 ? 267  ASN   B N   1 
ATOM   4640  C  CA  . ASN   B 2 267 ? 18.730  35.268  22.298  1.00 112.59 ? 267  ASN   B CA  1 
ATOM   4641  C  C   . ASN   B 2 267 ? 18.212  34.696  20.985  1.00 108.38 ? 267  ASN   B C   1 
ATOM   4642  O  O   . ASN   B 2 267 ? 18.285  33.483  20.743  1.00 102.84 ? 267  ASN   B O   1 
ATOM   4643  C  CB  . ASN   B 2 267 ? 17.579  35.574  23.259  1.00 113.56 ? 267  ASN   B CB  1 
ATOM   4644  C  CG  . ASN   B 2 267 ? 16.579  34.444  23.360  1.00 113.84 ? 267  ASN   B CG  1 
ATOM   4645  O  OD1 . ASN   B 2 267 ? 15.570  34.445  22.655  1.00 115.70 ? 267  ASN   B OD1 1 
ATOM   4646  N  ND2 . ASN   B 2 267 ? 16.841  33.481  24.253  1.00 111.47 ? 267  ASN   B ND2 1 
ATOM   4647  N  N   . GLY   B 2 268 ? 17.678  35.552  20.121  1.00 109.29 ? 268  GLY   B N   1 
ATOM   4648  C  CA  . GLY   B 2 268 ? 17.060  35.130  18.892  1.00 106.81 ? 268  GLY   B CA  1 
ATOM   4649  C  C   . GLY   B 2 268 ? 15.527  35.074  18.862  1.00 108.94 ? 268  GLY   B C   1 
ATOM   4650  O  O   . GLY   B 2 268 ? 14.975  34.398  17.986  1.00 110.51 ? 268  GLY   B O   1 
ATOM   4651  N  N   . SER   B 2 269 ? 14.835  35.775  19.765  1.00 110.41 ? 269  SER   B N   1 
ATOM   4652  C  CA  . SER   B 2 269 ? 13.378  35.768  19.807  1.00 110.13 ? 269  SER   B CA  1 
ATOM   4653  C  C   . SER   B 2 269 ? 12.753  36.882  18.990  1.00 111.12 ? 269  SER   B C   1 
ATOM   4654  O  O   . SER   B 2 269 ? 11.595  36.753  18.580  1.00 112.37 ? 269  SER   B O   1 
ATOM   4655  C  CB  . SER   B 2 269 ? 12.892  35.891  21.252  1.00 121.48 ? 269  SER   B CB  1 
ATOM   4656  O  OG  . SER   B 2 269 ? 13.717  36.771  22.001  1.00 123.81 ? 269  SER   B OG  1 
ATOM   4657  N  N   . ARG   B 2 270 ? 13.496  37.964  18.752  1.00 112.57 ? 270  ARG   B N   1 
ATOM   4658  C  CA  . ARG   B 2 270 ? 13.041  39.107  17.976  1.00 107.37 ? 270  ARG   B CA  1 
ATOM   4659  C  C   . ARG   B 2 270 ? 14.052  39.410  16.875  1.00 105.39 ? 270  ARG   B C   1 
ATOM   4660  O  O   . ARG   B 2 270 ? 15.232  39.655  17.155  1.00 104.74 ? 270  ARG   B O   1 
ATOM   4661  C  CB  . ARG   B 2 270 ? 12.847  40.321  18.883  1.00 109.77 ? 270  ARG   B CB  1 
ATOM   4662  C  CG  . ARG   B 2 270 ? 11.620  40.233  19.748  1.00 116.29 ? 270  ARG   B CG  1 
ATOM   4663  C  CD  . ARG   B 2 270 ? 11.625  41.410  20.672  1.00 128.30 ? 270  ARG   B CD  1 
ATOM   4664  N  NE  . ARG   B 2 270 ? 12.920  41.447  21.333  1.00 133.28 ? 270  ARG   B NE  1 
ATOM   4665  C  CZ  . ARG   B 2 270 ? 13.350  42.422  22.119  1.00 141.32 ? 270  ARG   B CZ  1 
ATOM   4666  N  NH1 . ARG   B 2 270 ? 12.645  43.524  22.297  1.00 153.58 ? 270  ARG   B NH1 1 
ATOM   4667  N  NH2 . ARG   B 2 270 ? 14.511  42.278  22.757  1.00 136.84 ? 270  ARG   B NH2 1 
ATOM   4668  N  N   . TYR   B 2 271 ? 13.577  39.383  15.626  1.00 101.96 ? 271  TYR   B N   1 
ATOM   4669  C  CA  . TYR   B 2 271 ? 14.315  39.751  14.426  1.00 96.95  ? 271  TYR   B CA  1 
ATOM   4670  C  C   . TYR   B 2 271 ? 13.642  40.956  13.766  1.00 98.16  ? 271  TYR   B C   1 
ATOM   4671  O  O   . TYR   B 2 271 ? 12.411  41.039  13.721  1.00 100.85 ? 271  TYR   B O   1 
ATOM   4672  C  CB  . TYR   B 2 271 ? 14.352  38.579  13.436  1.00 94.07  ? 271  TYR   B CB  1 
ATOM   4673  C  CG  . TYR   B 2 271 ? 15.311  37.460  13.773  1.00 93.73  ? 271  TYR   B CG  1 
ATOM   4674  C  CD1 . TYR   B 2 271 ? 14.879  36.315  14.430  1.00 93.81  ? 271  TYR   B CD1 1 
ATOM   4675  C  CD2 . TYR   B 2 271 ? 16.647  37.541  13.420  1.00 96.15  ? 271  TYR   B CD2 1 
ATOM   4676  C  CE1 . TYR   B 2 271 ? 15.763  35.276  14.729  1.00 96.62  ? 271  TYR   B CE1 1 
ATOM   4677  C  CE2 . TYR   B 2 271 ? 17.533  36.511  13.707  1.00 101.10 ? 271  TYR   B CE2 1 
ATOM   4678  C  CZ  . TYR   B 2 271 ? 17.089  35.382  14.369  1.00 100.90 ? 271  TYR   B CZ  1 
ATOM   4679  O  OH  . TYR   B 2 271 ? 17.963  34.357  14.654  1.00 98.28  ? 271  TYR   B OH  1 
ATOM   4680  N  N   . LEU   B 2 272 ? 14.438  41.894  13.254  1.00 97.55  ? 272  LEU   B N   1 
ATOM   4681  C  CA  . LEU   B 2 272 ? 13.912  43.005  12.472  1.00 94.18  ? 272  LEU   B CA  1 
ATOM   4682  C  C   . LEU   B 2 272 ? 13.889  42.626  11.002  1.00 92.23  ? 272  LEU   B C   1 
ATOM   4683  O  O   . LEU   B 2 272 ? 14.831  42.014  10.500  1.00 95.78  ? 272  LEU   B O   1 
ATOM   4684  C  CB  . LEU   B 2 272 ? 14.769  44.258  12.650  1.00 94.46  ? 272  LEU   B CB  1 
ATOM   4685  C  CG  . LEU   B 2 272 ? 14.708  45.002  13.975  1.00 90.88  ? 272  LEU   B CG  1 
ATOM   4686  C  CD1 . LEU   B 2 272 ? 15.832  46.037  14.053  1.00 86.98  ? 272  LEU   B CD1 1 
ATOM   4687  C  CD2 . LEU   B 2 272 ? 13.337  45.638  14.104  1.00 93.34  ? 272  LEU   B CD2 1 
ATOM   4688  N  N   . LEU   B 2 273 ? 12.824  43.002  10.309  1.00 93.34  ? 273  LEU   B N   1 
ATOM   4689  C  CA  . LEU   B 2 273 ? 12.708  42.760  8.883   1.00 94.46  ? 273  LEU   B CA  1 
ATOM   4690  C  C   . LEU   B 2 273 ? 12.389  44.071  8.193   1.00 95.42  ? 273  LEU   B C   1 
ATOM   4691  O  O   . LEU   B 2 273 ? 11.610  44.875  8.715   1.00 99.45  ? 273  LEU   B O   1 
ATOM   4692  C  CB  . LEU   B 2 273 ? 11.618  41.739  8.566   1.00 96.13  ? 273  LEU   B CB  1 
ATOM   4693  C  CG  . LEU   B 2 273 ? 11.856  40.294  9.034   1.00 96.64  ? 273  LEU   B CG  1 
ATOM   4694  C  CD1 . LEU   B 2 273 ? 10.718  39.357  8.627   1.00 94.19  ? 273  LEU   B CD1 1 
ATOM   4695  C  CD2 . LEU   B 2 273 ? 13.198  39.764  8.523   1.00 96.28  ? 273  LEU   B CD2 1 
ATOM   4696  N  N   . GLY   B 2 274 ? 12.989  44.288  7.048   1.00 94.06  ? 274  GLY   B N   1 
ATOM   4697  C  CA  . GLY   B 2 274 ? 12.716  45.478  6.258   1.00 96.80  ? 274  GLY   B CA  1 
ATOM   4698  C  C   . GLY   B 2 274 ? 12.474  45.078  4.825   1.00 99.41  ? 274  GLY   B C   1 
ATOM   4699  O  O   . GLY   B 2 274 ? 13.054  44.118  4.335   1.00 103.90 ? 274  GLY   B O   1 
ATOM   4700  N  N   . ASP   B 2 275 ? 11.582  45.817  4.166   1.00 96.30  ? 275  ASP   B N   1 
ATOM   4701  C  CA  . ASP   B 2 275 ? 11.197  45.505  2.799   1.00 100.67 ? 275  ASP   B CA  1 
ATOM   4702  C  C   . ASP   B 2 275 ? 11.882  46.462  1.831   1.00 97.82  ? 275  ASP   B C   1 
ATOM   4703  O  O   . ASP   B 2 275 ? 12.917  47.069  2.156   1.00 95.40  ? 275  ASP   B O   1 
ATOM   4704  C  CB  . ASP   B 2 275 ? 9.659   45.506  2.666   1.00 100.54 ? 275  ASP   B CB  1 
ATOM   4705  C  CG  . ASP   B 2 275 ? 9.036   46.904  2.725   1.00 99.75  ? 275  ASP   B CG  1 
ATOM   4706  O  OD1 . ASP   B 2 275 ? 9.754   47.931  2.844   1.00 100.06 ? 275  ASP   B OD1 1 
ATOM   4707  O  OD2 . ASP   B 2 275 ? 7.787   46.956  2.647   1.00 101.74 ? 275  ASP   B OD2 1 
ATOM   4708  N  N   . MET   B 2 276 ? 11.330  46.612  0.625   1.00 97.07  ? 276  MET   B N   1 
ATOM   4709  C  CA  . MET   B 2 276 ? 11.896  47.492  -0.376  1.00 95.02  ? 276  MET   B CA  1 
ATOM   4710  C  C   . MET   B 2 276 ? 11.133  48.794  -0.501  1.00 94.51  ? 276  MET   B C   1 
ATOM   4711  O  O   . MET   B 2 276 ? 11.581  49.695  -1.210  1.00 93.12  ? 276  MET   B O   1 
ATOM   4712  C  CB  . MET   B 2 276 ? 11.945  46.793  -1.723  1.00 95.03  ? 276  MET   B CB  1 
ATOM   4713  C  CG  . MET   B 2 276 ? 12.120  45.308  -1.603  1.00 101.10 ? 276  MET   B CG  1 
ATOM   4714  S  SD  . MET   B 2 276 ? 12.044  44.557  -3.222  1.00 102.31 ? 276  MET   B SD  1 
ATOM   4715  C  CE  . MET   B 2 276 ? 13.390  45.407  -4.024  1.00 91.10  ? 276  MET   B CE  1 
ATOM   4716  N  N   . GLU   B 2 277 ? 9.994   48.923  0.187   1.00 95.54  ? 277  GLU   B N   1 
ATOM   4717  C  CA  . GLU   B 2 277 ? 9.241   50.163  0.219   1.00 94.78  ? 277  GLU   B CA  1 
ATOM   4718  C  C   . GLU   B 2 277 ? 9.471   50.956  1.510   1.00 96.14  ? 277  GLU   B C   1 
ATOM   4719  O  O   . GLU   B 2 277 ? 8.776   51.942  1.738   1.00 101.53 ? 277  GLU   B O   1 
ATOM   4720  C  CB  . GLU   B 2 277 ? 7.742   49.883  0.024   1.00 101.52 ? 277  GLU   B CB  1 
ATOM   4721  C  CG  . GLU   B 2 277 ? 7.398   48.863  -1.112  1.00 106.01 ? 277  GLU   B CG  1 
ATOM   4722  C  CD  . GLU   B 2 277 ? 5.907   48.424  -1.174  1.00 117.47 ? 277  GLU   B CD  1 
ATOM   4723  O  OE1 . GLU   B 2 277 ? 5.100   48.843  -0.313  1.00 118.41 ? 277  GLU   B OE1 1 
ATOM   4724  O  OE2 . GLU   B 2 277 ? 5.542   47.648  -2.094  1.00 118.43 ? 277  GLU   B OE2 1 
ATOM   4725  N  N   . GLY   B 2 278 ? 10.435  50.555  2.344   1.00 93.24  ? 278  GLY   B N   1 
ATOM   4726  C  CA  . GLY   B 2 278 ? 10.787  51.297  3.540   1.00 96.08  ? 278  GLY   B CA  1 
ATOM   4727  C  C   . GLY   B 2 278 ? 10.103  50.849  4.822   1.00 102.85 ? 278  GLY   B C   1 
ATOM   4728  O  O   . GLY   B 2 278 ? 10.431  51.372  5.898   1.00 105.75 ? 278  GLY   B O   1 
ATOM   4729  N  N   . ARG   B 2 279 ? 9.171   49.905  4.751   1.00 98.46  ? 279  ARG   B N   1 
ATOM   4730  C  CA  . ARG   B 2 279 ? 8.499   49.452  5.960   1.00 99.03  ? 279  ARG   B CA  1 
ATOM   4731  C  C   . ARG   B 2 279 ? 9.419   48.578  6.803   1.00 99.33  ? 279  ARG   B C   1 
ATOM   4732  O  O   . ARG   B 2 279 ? 10.250  47.835  6.281   1.00 101.14 ? 279  ARG   B O   1 
ATOM   4733  C  CB  . ARG   B 2 279 ? 7.236   48.697  5.587   1.00 98.12  ? 279  ARG   B CB  1 
ATOM   4734  C  CG  . ARG   B 2 279 ? 6.305   49.548  4.755   1.00 105.72 ? 279  ARG   B CG  1 
ATOM   4735  C  CD  . ARG   B 2 279 ? 4.919   48.957  4.729   1.00 110.44 ? 279  ARG   B CD  1 
ATOM   4736  N  NE  . ARG   B 2 279 ? 4.850   47.854  3.784   1.00 110.98 ? 279  ARG   B NE  1 
ATOM   4737  C  CZ  . ARG   B 2 279 ? 4.397   47.986  2.547   1.00 116.23 ? 279  ARG   B CZ  1 
ATOM   4738  N  NH1 . ARG   B 2 279 ? 3.899   49.138  2.114   1.00 110.65 ? 279  ARG   B NH1 1 
ATOM   4739  N  NH2 . ARG   B 2 279 ? 4.459   46.948  1.722   1.00 120.35 ? 279  ARG   B NH2 1 
ATOM   4740  N  N   . LEU   B 2 280 ? 9.275   48.669  8.120   1.00 104.91 ? 280  LEU   B N   1 
ATOM   4741  C  CA  . LEU   B 2 280 ? 10.129  47.953  9.064   1.00 101.25 ? 280  LEU   B CA  1 
ATOM   4742  C  C   . LEU   B 2 280 ? 9.262   47.041  9.918   1.00 99.22  ? 280  LEU   B C   1 
ATOM   4743  O  O   . LEU   B 2 280 ? 8.395   47.516  10.658  1.00 99.20  ? 280  LEU   B O   1 
ATOM   4744  C  CB  . LEU   B 2 280 ? 10.918  48.937  9.929   1.00 98.16  ? 280  LEU   B CB  1 
ATOM   4745  C  CG  . LEU   B 2 280 ? 11.633  48.442  11.177  1.00 91.25  ? 280  LEU   B CG  1 
ATOM   4746  C  CD1 . LEU   B 2 280 ? 12.589  47.308  10.847  1.00 95.08  ? 280  LEU   B CD1 1 
ATOM   4747  C  CD2 . LEU   B 2 280 ? 12.357  49.600  11.831  1.00 82.75  ? 280  LEU   B CD2 1 
ATOM   4748  N  N   . PHE   B 2 281 ? 9.479   45.735  9.789   1.00 99.00  ? 281  PHE   B N   1 
ATOM   4749  C  CA  . PHE   B 2 281 ? 8.704   44.739  10.507  1.00 97.09  ? 281  PHE   B CA  1 
ATOM   4750  C  C   . PHE   B 2 281 ? 9.507   44.175  11.667  1.00 100.18 ? 281  PHE   B C   1 
ATOM   4751  O  O   . PHE   B 2 281 ? 10.722  44.368  11.792  1.00 100.50 ? 281  PHE   B O   1 
ATOM   4752  C  CB  . PHE   B 2 281 ? 8.278   43.578  9.603   1.00 95.92  ? 281  PHE   B CB  1 
ATOM   4753  C  CG  . PHE   B 2 281 ? 7.508   43.987  8.387   1.00 96.27  ? 281  PHE   B CG  1 
ATOM   4754  C  CD1 . PHE   B 2 281 ? 8.157   44.544  7.312   1.00 98.51  ? 281  PHE   B CD1 1 
ATOM   4755  C  CD2 . PHE   B 2 281 ? 6.137   43.789  8.304   1.00 97.54  ? 281  PHE   B CD2 1 
ATOM   4756  C  CE1 . PHE   B 2 281 ? 7.461   44.913  6.188   1.00 104.78 ? 281  PHE   B CE1 1 
ATOM   4757  C  CE2 . PHE   B 2 281 ? 5.436   44.149  7.184   1.00 100.87 ? 281  PHE   B CE2 1 
ATOM   4758  C  CZ  . PHE   B 2 281 ? 6.095   44.715  6.122   1.00 105.93 ? 281  PHE   B CZ  1 
ATOM   4759  N  N   . MET   B 2 282 ? 8.799   43.415  12.500  1.00 106.72 ? 282  MET   B N   1 
ATOM   4760  C  CA  . MET   B 2 282 ? 9.369   42.776  13.686  1.00 103.41 ? 282  MET   B CA  1 
ATOM   4761  C  C   . MET   B 2 282 ? 8.897   41.326  13.737  1.00 102.77 ? 282  MET   B C   1 
ATOM   4762  O  O   . MET   B 2 282 ? 7.709   41.057  13.951  1.00 106.61 ? 282  MET   B O   1 
ATOM   4763  C  CB  . MET   B 2 282 ? 8.961   43.525  14.951  1.00 100.50 ? 282  MET   B CB  1 
ATOM   4764  C  CG  . MET   B 2 282 ? 9.343   42.823  16.201  1.00 98.88  ? 282  MET   B CG  1 
ATOM   4765  S  SD  . MET   B 2 282 ? 11.082  42.902  16.468  1.00 102.47 ? 282  MET   B SD  1 
ATOM   4766  C  CE  . MET   B 2 282 ? 11.060  43.727  18.067  1.00 120.84 ? 282  MET   B CE  1 
ATOM   4767  N  N   . LEU   B 2 283 ? 9.821   40.394  13.539  1.00 105.89 ? 283  LEU   B N   1 
ATOM   4768  C  CA  . LEU   B 2 283 ? 9.534   38.968  13.668  1.00 105.72 ? 283  LEU   B CA  1 
ATOM   4769  C  C   . LEU   B 2 283 ? 9.770   38.557  15.126  1.00 107.28 ? 283  LEU   B C   1 
ATOM   4770  O  O   . LEU   B 2 283 ? 10.899  38.644  15.627  1.00 106.83 ? 283  LEU   B O   1 
ATOM   4771  C  CB  . LEU   B 2 283 ? 10.404  38.152  12.705  1.00 101.59 ? 283  LEU   B CB  1 
ATOM   4772  C  CG  . LEU   B 2 283 ? 10.154  36.644  12.542  1.00 102.60 ? 283  LEU   B CG  1 
ATOM   4773  C  CD1 . LEU   B 2 283 ? 8.662   36.325  12.392  1.00 105.33 ? 283  LEU   B CD1 1 
ATOM   4774  C  CD2 . LEU   B 2 283 ? 10.961  36.103  11.362  1.00 100.96 ? 283  LEU   B CD2 1 
ATOM   4775  N  N   . LEU   B 2 284 ? 8.709   38.143  15.816  1.00 108.73 ? 284  LEU   B N   1 
ATOM   4776  C  CA  . LEU   B 2 284 ? 8.820   37.638  17.177  1.00 109.15 ? 284  LEU   B CA  1 
ATOM   4777  C  C   . LEU   B 2 284 ? 8.620   36.128  17.166  1.00 110.38 ? 284  LEU   B C   1 
ATOM   4778  O  O   . LEU   B 2 284 ? 7.643   35.632  16.602  1.00 112.81 ? 284  LEU   B O   1 
ATOM   4779  C  CB  . LEU   B 2 284 ? 7.799   38.303  18.102  1.00 109.87 ? 284  LEU   B CB  1 
ATOM   4780  C  CG  . LEU   B 2 284 ? 7.959   39.807  18.228  1.00 109.22 ? 284  LEU   B CG  1 
ATOM   4781  C  CD1 . LEU   B 2 284 ? 6.974   40.450  17.305  1.00 111.35 ? 284  LEU   B CD1 1 
ATOM   4782  C  CD2 . LEU   B 2 284 ? 7.723   40.243  19.651  1.00 123.58 ? 284  LEU   B CD2 1 
ATOM   4783  N  N   . LEU   B 2 285 ? 9.552   35.400  17.773  1.00 109.69 ? 285  LEU   B N   1 
ATOM   4784  C  CA  . LEU   B 2 285 ? 9.400   33.961  17.946  1.00 112.89 ? 285  LEU   B CA  1 
ATOM   4785  C  C   . LEU   B 2 285 ? 8.844   33.713  19.341  1.00 118.85 ? 285  LEU   B C   1 
ATOM   4786  O  O   . LEU   B 2 285 ? 9.502   34.010  20.346  1.00 121.09 ? 285  LEU   B O   1 
ATOM   4787  C  CB  . LEU   B 2 285 ? 10.724  33.240  17.729  1.00 107.80 ? 285  LEU   B CB  1 
ATOM   4788  C  CG  . LEU   B 2 285 ? 11.225  33.344  16.292  1.00 106.03 ? 285  LEU   B CG  1 
ATOM   4789  C  CD1 . LEU   B 2 285 ? 12.275  34.427  16.221  1.00 109.40 ? 285  LEU   B CD1 1 
ATOM   4790  C  CD2 . LEU   B 2 285 ? 11.782  32.035  15.779  1.00 97.33  ? 285  LEU   B CD2 1 
ATOM   4791  N  N   . GLU   B 2 286 ? 7.612   33.211  19.399  1.00 120.40 ? 286  GLU   B N   1 
ATOM   4792  C  CA  . GLU   B 2 286 ? 6.985   32.921  20.676  1.00 120.98 ? 286  GLU   B CA  1 
ATOM   4793  C  C   . GLU   B 2 286 ? 7.559   31.623  21.235  1.00 127.46 ? 286  GLU   B C   1 
ATOM   4794  O  O   . GLU   B 2 286 ? 7.532   30.584  20.563  1.00 127.00 ? 286  GLU   B O   1 
ATOM   4795  C  CB  . GLU   B 2 286 ? 5.465   32.819  20.513  1.00 123.08 ? 286  GLU   B CB  1 
ATOM   4796  N  N   . LYS   B 2 287 ? 8.079   31.691  22.463  1.00 132.70 ? 287  LYS   B N   1 
ATOM   4797  C  CA  . LYS   B 2 287 ? 8.764   30.585  23.113  1.00 127.80 ? 287  LYS   B CA  1 
ATOM   4798  C  C   . LYS   B 2 287 ? 7.805   29.822  24.024  1.00 135.21 ? 287  LYS   B C   1 
ATOM   4799  O  O   . LYS   B 2 287 ? 6.699   30.284  24.325  1.00 133.68 ? 287  LYS   B O   1 
ATOM   4800  C  CB  . LYS   B 2 287 ? 9.964   31.116  23.904  1.00 120.94 ? 287  LYS   B CB  1 
ATOM   4801  N  N   . GLU   B 2 288 ? 8.240   28.623  24.444  1.00 142.11 ? 288  GLU   B N   1 
ATOM   4802  C  CA  . GLU   B 2 288 ? 7.500   27.745  25.356  1.00 146.24 ? 288  GLU   B CA  1 
ATOM   4803  C  C   . GLU   B 2 288 ? 8.419   27.374  26.516  1.00 155.07 ? 288  GLU   B C   1 
ATOM   4804  O  O   . GLU   B 2 288 ? 9.424   26.681  26.319  1.00 156.70 ? 288  GLU   B O   1 
ATOM   4805  C  CB  . GLU   B 2 288 ? 6.996   26.478  24.645  1.00 142.80 ? 288  GLU   B CB  1 
ATOM   4806  N  N   . GLU   B 2 289 ? 8.072   27.816  27.730  1.00 182.02 ? 289  GLU   B N   1 
ATOM   4807  C  CA  . GLU   B 2 289 ? 8.868   27.573  28.937  1.00 180.22 ? 289  GLU   B CA  1 
ATOM   4808  C  C   . GLU   B 2 289 ? 8.459   26.238  29.560  1.00 176.38 ? 289  GLU   B C   1 
ATOM   4809  O  O   . GLU   B 2 289 ? 7.568   26.170  30.412  1.00 173.83 ? 289  GLU   B O   1 
ATOM   4810  C  CB  . GLU   B 2 289 ? 8.702   28.712  29.933  1.00 175.05 ? 289  GLU   B CB  1 
ATOM   4811  N  N   . GLN   B 2 290 ? 9.124   25.162  29.135  1.00 156.56 ? 290  GLN   B N   1 
ATOM   4812  C  CA  . GLN   B 2 290 ? 8.749   23.821  29.563  1.00 154.88 ? 290  GLN   B CA  1 
ATOM   4813  C  C   . GLN   B 2 290 ? 9.536   23.416  30.804  1.00 156.20 ? 290  GLN   B C   1 
ATOM   4814  O  O   . GLN   B 2 290 ? 10.588  23.984  31.110  1.00 158.17 ? 290  GLN   B O   1 
ATOM   4815  C  CB  . GLN   B 2 290 ? 8.978   22.804  28.445  1.00 153.43 ? 290  GLN   B CB  1 
ATOM   4816  C  CG  . GLN   B 2 290 ? 8.077   22.964  27.238  1.00 152.75 ? 290  GLN   B CG  1 
ATOM   4817  C  CD  . GLN   B 2 290 ? 8.388   21.986  26.135  1.00 152.60 ? 290  GLN   B CD  1 
ATOM   4818  O  OE1 . GLN   B 2 290 ? 9.513   21.493  26.029  1.00 161.81 ? 290  GLN   B OE1 1 
ATOM   4819  N  NE2 . GLN   B 2 290 ? 7.390   21.683  25.312  1.00 140.74 ? 290  GLN   B NE2 1 
ATOM   4820  N  N   . MET   B 2 291 ? 9.027   22.377  31.495  1.00 152.62 ? 291  MET   B N   1 
ATOM   4821  C  CA  . MET   B 2 291 ? 9.563   21.943  32.786  1.00 145.57 ? 291  MET   B CA  1 
ATOM   4822  C  C   . MET   B 2 291 ? 10.863  21.172  32.662  1.00 145.67 ? 291  MET   B C   1 
ATOM   4823  O  O   . MET   B 2 291 ? 11.715  21.263  33.555  1.00 141.40 ? 291  MET   B O   1 
ATOM   4824  C  CB  . MET   B 2 291 ? 8.543   21.085  33.529  1.00 138.31 ? 291  MET   B CB  1 
ATOM   4825  C  CG  . MET   B 2 291 ? 7.449   21.862  34.157  1.00 142.35 ? 291  MET   B CG  1 
ATOM   4826  S  SD  . MET   B 2 291 ? 8.009   23.556  34.367  1.00 145.69 ? 291  MET   B SD  1 
ATOM   4827  C  CE  . MET   B 2 291 ? 8.962   23.325  35.850  1.00 126.53 ? 291  MET   B CE  1 
ATOM   4828  N  N   . ASP   B 2 292 ? 11.037  20.417  31.574  1.00 154.10 ? 292  ASP   B N   1 
ATOM   4829  C  CA  . ASP   B 2 292 ? 12.304  19.726  31.299  1.00 155.56 ? 292  ASP   B CA  1 
ATOM   4830  C  C   . ASP   B 2 292 ? 13.392  20.666  30.807  1.00 158.74 ? 292  ASP   B C   1 
ATOM   4831  O  O   . ASP   B 2 292 ? 14.482  20.197  30.456  1.00 155.01 ? 292  ASP   B O   1 
ATOM   4832  C  CB  . ASP   B 2 292 ? 12.082  18.615  30.263  1.00 152.70 ? 292  ASP   B CB  1 
ATOM   4833  C  CG  . ASP   B 2 292 ? 11.691  19.162  28.893  1.00 159.52 ? 292  ASP   B CG  1 
ATOM   4834  O  OD1 . ASP   B 2 292 ? 11.045  20.229  28.837  1.00 159.69 ? 292  ASP   B OD1 1 
ATOM   4835  O  OD2 . ASP   B 2 292 ? 12.028  18.528  27.865  1.00 166.15 ? 292  ASP   B OD2 1 
ATOM   4836  N  N   . GLY   B 2 293 ? 13.126  21.972  30.772  1.00 156.29 ? 293  GLY   B N   1 
ATOM   4837  C  CA  . GLY   B 2 293 ? 14.037  22.977  30.231  1.00 153.07 ? 293  GLY   B CA  1 
ATOM   4838  C  C   . GLY   B 2 293 ? 13.794  23.305  28.765  1.00 155.43 ? 293  GLY   B C   1 
ATOM   4839  O  O   . GLY   B 2 293 ? 13.603  24.473  28.421  1.00 154.08 ? 293  GLY   B O   1 
ATOM   4840  N  N   . THR   B 2 294 ? 13.761  22.263  27.920  1.00 159.05 ? 294  THR   B N   1 
ATOM   4841  C  CA  . THR   B 2 294 ? 13.641  22.396  26.465  1.00 158.89 ? 294  THR   B CA  1 
ATOM   4842  C  C   . THR   B 2 294 ? 12.527  23.356  26.074  1.00 160.57 ? 294  THR   B C   1 
ATOM   4843  O  O   . THR   B 2 294 ? 11.438  23.344  26.656  1.00 161.71 ? 294  THR   B O   1 
ATOM   4844  C  CB  . THR   B 2 294 ? 13.383  21.029  25.830  1.00 153.88 ? 294  THR   B CB  1 
ATOM   4845  N  N   . VAL   B 2 295 ? 12.814  24.185  25.070  1.00 151.67 ? 295  VAL   B N   1 
ATOM   4846  C  CA  . VAL   B 2 295 ? 11.929  25.259  24.638  1.00 151.10 ? 295  VAL   B CA  1 
ATOM   4847  C  C   . VAL   B 2 295 ? 11.418  24.926  23.250  1.00 152.40 ? 295  VAL   B C   1 
ATOM   4848  O  O   . VAL   B 2 295 ? 12.167  24.412  22.408  1.00 151.92 ? 295  VAL   B O   1 
ATOM   4849  C  CB  . VAL   B 2 295 ? 12.641  26.625  24.665  1.00 148.66 ? 295  VAL   B CB  1 
ATOM   4850  C  CG1 . VAL   B 2 295 ? 12.029  27.576  23.634  1.00 148.16 ? 295  VAL   B CG1 1 
ATOM   4851  C  CG2 . VAL   B 2 295 ? 12.576  27.232  26.073  1.00 148.98 ? 295  VAL   B CG2 1 
ATOM   4852  N  N   . THR   B 2 296 ? 10.136  25.205  23.023  1.00 156.04 ? 296  THR   B N   1 
ATOM   4853  C  CA  . THR   B 2 296 ? 9.461   24.903  21.771  1.00 155.81 ? 296  THR   B CA  1 
ATOM   4854  C  C   . THR   B 2 296 ? 8.928   26.191  21.168  1.00 153.74 ? 296  THR   B C   1 
ATOM   4855  O  O   . THR   B 2 296 ? 8.310   26.994  21.872  1.00 153.87 ? 296  THR   B O   1 
ATOM   4856  C  CB  . THR   B 2 296 ? 8.311   23.920  21.989  1.00 157.28 ? 296  THR   B CB  1 
ATOM   4857  O  OG1 . THR   B 2 296 ? 8.837   22.633  22.341  1.00 157.46 ? 296  THR   B OG1 1 
ATOM   4858  C  CG2 . THR   B 2 296 ? 7.481   23.793  20.718  1.00 158.02 ? 296  THR   B CG2 1 
ATOM   4859  N  N   . LEU   B 2 297 ? 9.170   26.382  19.869  1.00 142.17 ? 297  LEU   B N   1 
ATOM   4860  C  CA  . LEU   B 2 297 ? 8.593   27.501  19.111  1.00 132.24 ? 297  LEU   B CA  1 
ATOM   4861  C  C   . LEU   B 2 297 ? 7.104   27.278  19.301  1.00 131.15 ? 297  LEU   B C   1 
ATOM   4862  O  O   . LEU   B 2 297 ? 6.575   26.203  18.988  1.00 128.15 ? 297  LEU   B O   1 
ATOM   4863  C  CB  . LEU   B 2 297 ? 9.168   27.510  17.698  1.00 128.33 ? 297  LEU   B CB  1 
ATOM   4864  C  CG  . LEU   B 2 297 ? 8.642   28.520  16.670  1.00 125.07 ? 297  LEU   B CG  1 
ATOM   4865  C  CD1 . LEU   B 2 297 ? 8.841   29.970  17.129  1.00 130.51 ? 297  LEU   B CD1 1 
ATOM   4866  C  CD2 . LEU   B 2 297 ? 9.253   28.295  15.286  1.00 110.35 ? 297  LEU   B CD2 1 
ATOM   4867  N  N   . LYS   B 2 298 ? 6.418   28.279  19.848  1.00 133.38 ? 298  LYS   B N   1 
ATOM   4868  C  CA  . LYS   B 2 298 ? 4.968   28.170  20.003  1.00 133.09 ? 298  LYS   B CA  1 
ATOM   4869  C  C   . LYS   B 2 298 ? 4.417   28.700  18.705  1.00 136.84 ? 298  LYS   B C   1 
ATOM   4870  O  O   . LYS   B 2 298 ? 3.657   28.009  18.013  1.00 133.74 ? 298  LYS   B O   1 
ATOM   4871  C  CB  . LYS   B 2 298 ? 4.469   28.978  21.208  1.00 129.66 ? 298  LYS   B CB  1 
ATOM   4872  N  N   . ASP   B 2 299 ? 4.829   29.907  18.320  1.00 141.96 ? 299  ASP   B N   1 
ATOM   4873  C  CA  . ASP   B 2 299 ? 4.246   30.602  17.179  1.00 143.20 ? 299  ASP   B CA  1 
ATOM   4874  C  C   . ASP   B 2 299 ? 5.243   31.636  16.654  1.00 140.27 ? 299  ASP   B C   1 
ATOM   4875  O  O   . ASP   B 2 299 ? 6.168   32.051  17.358  1.00 139.22 ? 299  ASP   B O   1 
ATOM   4876  C  CB  . ASP   B 2 299 ? 2.898   31.237  17.581  1.00 144.74 ? 299  ASP   B CB  1 
ATOM   4877  C  CG  . ASP   B 2 299 ? 2.064   31.745  16.385  1.00 150.34 ? 299  ASP   B CG  1 
ATOM   4878  O  OD1 . ASP   B 2 299 ? 1.857   30.995  15.395  1.00 152.00 ? 299  ASP   B OD1 1 
ATOM   4879  O  OD2 . ASP   B 2 299 ? 1.569   32.896  16.463  1.00 148.16 ? 299  ASP   B OD2 1 
ATOM   4880  N  N   . LEU   B 2 300 ? 5.049   32.023  15.390  1.00 127.40 ? 300  LEU   B N   1 
ATOM   4881  C  CA  . LEU   B 2 300 ? 5.775   33.102  14.729  1.00 120.57 ? 300  LEU   B CA  1 
ATOM   4882  C  C   . LEU   B 2 300 ? 4.840   34.285  14.495  1.00 117.97 ? 300  LEU   B C   1 
ATOM   4883  O  O   . LEU   B 2 300 ? 3.806   34.145  13.825  1.00 118.09 ? 300  LEU   B O   1 
ATOM   4884  C  CB  . LEU   B 2 300 ? 6.333   32.640  13.376  1.00 114.92 ? 300  LEU   B CB  1 
ATOM   4885  C  CG  . LEU   B 2 300 ? 7.380   31.544  13.376  1.00 112.80 ? 300  LEU   B CG  1 
ATOM   4886  C  CD1 . LEU   B 2 300 ? 7.137   30.584  12.215  1.00 105.20 ? 300  LEU   B CD1 1 
ATOM   4887  C  CD2 . LEU   B 2 300 ? 8.756   32.187  13.281  1.00 112.69 ? 300  LEU   B CD2 1 
ATOM   4888  N  N   . ARG   B 2 301 ? 5.206   35.446  15.032  1.00 114.93 ? 301  ARG   B N   1 
ATOM   4889  C  CA  . ARG   B 2 301 ? 4.388   36.648  14.951  1.00 113.80 ? 301  ARG   B CA  1 
ATOM   4890  C  C   . ARG   B 2 301 ? 5.110   37.704  14.122  1.00 113.67 ? 301  ARG   B C   1 
ATOM   4891  O  O   . ARG   B 2 301 ? 6.329   37.889  14.243  1.00 108.98 ? 301  ARG   B O   1 
ATOM   4892  C  CB  . ARG   B 2 301 ? 4.057   37.199  16.353  1.00 111.88 ? 301  ARG   B CB  1 
ATOM   4893  C  CG  . ARG   B 2 301 ? 2.687   37.887  16.493  1.00 113.30 ? 301  ARG   B CG  1 
ATOM   4894  C  CD  . ARG   B 2 301 ? 1.497   36.930  16.346  1.00 115.20 ? 301  ARG   B CD  1 
ATOM   4895  N  NE  . ARG   B 2 301 ? 1.706   35.681  17.073  1.00 124.32 ? 301  ARG   B NE  1 
ATOM   4896  C  CZ  . ARG   B 2 301 ? 1.600   35.543  18.388  1.00 119.11 ? 301  ARG   B CZ  1 
ATOM   4897  N  NH1 . ARG   B 2 301 ? 1.242   36.552  19.160  1.00 125.16 ? 301  ARG   B NH1 1 
ATOM   4898  N  NH2 . ARG   B 2 301 ? 1.865   34.364  18.941  1.00 114.58 ? 301  ARG   B NH2 1 
ATOM   4899  N  N   . VAL   B 2 302 ? 4.349   38.381  13.264  1.00 116.87 ? 302  VAL   B N   1 
ATOM   4900  C  CA  . VAL   B 2 302 ? 4.866   39.436  12.404  1.00 114.20 ? 302  VAL   B CA  1 
ATOM   4901  C  C   . VAL   B 2 302 ? 4.079   40.709  12.669  1.00 110.72 ? 302  VAL   B C   1 
ATOM   4902  O  O   . VAL   B 2 302 ? 2.854   40.742  12.485  1.00 110.55 ? 302  VAL   B O   1 
ATOM   4903  C  CB  . VAL   B 2 302 ? 4.792   39.049  10.924  1.00 109.38 ? 302  VAL   B CB  1 
ATOM   4904  C  CG1 . VAL   B 2 302 ? 4.888   40.294  10.073  1.00 110.48 ? 302  VAL   B CG1 1 
ATOM   4905  C  CG2 . VAL   B 2 302 ? 5.917   38.093  10.608  1.00 108.72 ? 302  VAL   B CG2 1 
ATOM   4906  N  N   . GLU   B 2 303 ? 4.786   41.754  13.080  1.00 107.24 ? 303  GLU   B N   1 
ATOM   4907  C  CA  . GLU   B 2 303 ? 4.190   43.034  13.408  1.00 109.89 ? 303  GLU   B CA  1 
ATOM   4908  C  C   . GLU   B 2 303 ? 4.889   44.151  12.634  1.00 109.01 ? 303  GLU   B C   1 
ATOM   4909  O  O   . GLU   B 2 303 ? 6.106   44.106  12.413  1.00 104.00 ? 303  GLU   B O   1 
ATOM   4910  C  CB  . GLU   B 2 303 ? 4.247   43.281  14.926  1.00 110.31 ? 303  GLU   B CB  1 
ATOM   4911  C  CG  . GLU   B 2 303 ? 3.562   44.586  15.347  1.00 118.37 ? 303  GLU   B CG  1 
ATOM   4912  C  CD  . GLU   B 2 303 ? 2.114   44.707  14.835  1.00 121.11 ? 303  GLU   B CD  1 
ATOM   4913  O  OE1 . GLU   B 2 303 ? 1.208   44.247  15.569  1.00 125.03 ? 303  GLU   B OE1 1 
ATOM   4914  O  OE2 . GLU   B 2 303 ? 1.878   45.257  13.717  1.00 113.82 ? 303  GLU   B OE2 1 
ATOM   4915  N  N   . LEU   B 2 304 ? 4.101   45.144  12.206  1.00 110.75 ? 304  LEU   B N   1 
ATOM   4916  C  CA  . LEU   B 2 304 ? 4.602   46.275  11.430  1.00 106.18 ? 304  LEU   B CA  1 
ATOM   4917  C  C   . LEU   B 2 304 ? 4.893   47.460  12.345  1.00 107.54 ? 304  LEU   B C   1 
ATOM   4918  O  O   . LEU   B 2 304 ? 4.006   47.932  13.061  1.00 107.96 ? 304  LEU   B O   1 
ATOM   4919  C  CB  . LEU   B 2 304 ? 3.592   46.680  10.357  1.00 101.34 ? 304  LEU   B CB  1 
ATOM   4920  C  CG  . LEU   B 2 304 ? 4.138   47.749  9.418   1.00 100.17 ? 304  LEU   B CG  1 
ATOM   4921  C  CD1 . LEU   B 2 304 ? 5.490   47.296  8.889   1.00 102.45 ? 304  LEU   B CD1 1 
ATOM   4922  C  CD2 . LEU   B 2 304 ? 3.157   48.031  8.286   1.00 100.83 ? 304  LEU   B CD2 1 
ATOM   4923  N  N   . LEU   B 2 305 ? 6.124   47.960  12.294  1.00 104.67 ? 305  LEU   B N   1 
ATOM   4924  C  CA  . LEU   B 2 305 ? 6.567   48.961  13.252  1.00 105.19 ? 305  LEU   B CA  1 
ATOM   4925  C  C   . LEU   B 2 305 ? 6.512   50.385  12.715  1.00 112.69 ? 305  LEU   B C   1 
ATOM   4926  O  O   . LEU   B 2 305 ? 6.399   51.325  13.506  1.00 119.68 ? 305  LEU   B O   1 
ATOM   4927  C  CB  . LEU   B 2 305 ? 7.995   48.648  13.721  1.00 109.31 ? 305  LEU   B CB  1 
ATOM   4928  C  CG  . LEU   B 2 305 ? 8.384   47.209  14.155  1.00 110.34 ? 305  LEU   B CG  1 
ATOM   4929  C  CD1 . LEU   B 2 305 ? 9.854   47.102  14.618  1.00 99.76  ? 305  LEU   B CD1 1 
ATOM   4930  C  CD2 . LEU   B 2 305 ? 7.451   46.652  15.223  1.00 114.73 ? 305  LEU   B CD2 1 
ATOM   4931  N  N   . GLY   B 2 306 ? 6.580   50.570  11.409  1.00 110.68 ? 306  GLY   B N   1 
ATOM   4932  C  CA  . GLY   B 2 306 ? 6.550   51.893  10.821  1.00 113.01 ? 306  GLY   B CA  1 
ATOM   4933  C  C   . GLY   B 2 306 ? 7.312   51.906  9.509   1.00 109.42 ? 306  GLY   B C   1 
ATOM   4934  O  O   . GLY   B 2 306 ? 7.556   50.869  8.897   1.00 107.58 ? 306  GLY   B O   1 
ATOM   4935  N  N   . GLU   B 2 307 ? 7.684   53.105  9.082   1.00 122.62 ? 307  GLU   B N   1 
ATOM   4936  C  CA  . GLU   B 2 307 ? 8.365   53.284  7.812   1.00 121.83 ? 307  GLU   B CA  1 
ATOM   4937  C  C   . GLU   B 2 307 ? 9.671   54.021  8.034   1.00 121.57 ? 307  GLU   B C   1 
ATOM   4938  O  O   . GLU   B 2 307 ? 9.750   54.926  8.868   1.00 121.97 ? 307  GLU   B O   1 
ATOM   4939  C  CB  . GLU   B 2 307 ? 7.505   54.055  6.817   1.00 120.67 ? 307  GLU   B CB  1 
ATOM   4940  C  CG  . GLU   B 2 307 ? 7.648   53.569  5.405   1.00 121.03 ? 307  GLU   B CG  1 
ATOM   4941  C  CD  . GLU   B 2 307 ? 6.839   54.404  4.428   1.00 126.23 ? 307  GLU   B CD  1 
ATOM   4942  O  OE1 . GLU   B 2 307 ? 6.629   55.614  4.711   1.00 125.02 ? 307  GLU   B OE1 1 
ATOM   4943  O  OE2 . GLU   B 2 307 ? 6.408   53.844  3.382   1.00 128.61 ? 307  GLU   B OE2 1 
ATOM   4944  N  N   . THR   B 2 308 ? 10.694  53.634  7.283   1.00 101.66 ? 308  THR   B N   1 
ATOM   4945  C  CA  . THR   B 2 308 ? 12.001  54.269  7.389   1.00 99.01  ? 308  THR   B CA  1 
ATOM   4946  C  C   . THR   B 2 308 ? 12.516  54.572  5.982   1.00 96.10  ? 308  THR   B C   1 
ATOM   4947  O  O   . THR   B 2 308 ? 11.762  54.628  5.005   1.00 100.36 ? 308  THR   B O   1 
ATOM   4948  C  CB  . THR   B 2 308 ? 12.974  53.386  8.175   1.00 97.95  ? 308  THR   B CB  1 
ATOM   4949  O  OG1 . THR   B 2 308 ? 13.252  52.207  7.416   1.00 99.02  ? 308  THR   B OG1 1 
ATOM   4950  C  CG2 . THR   B 2 308 ? 12.412  52.999  9.537   1.00 100.99 ? 308  THR   B CG2 1 
ATOM   4951  N  N   . SER   B 2 309 ? 13.823  54.808  5.861   1.00 93.62  ? 309  SER   B N   1 
ATOM   4952  C  CA  . SER   B 2 309 ? 14.439  54.941  4.548   1.00 89.02  ? 309  SER   B CA  1 
ATOM   4953  C  C   . SER   B 2 309 ? 14.553  53.579  3.895   1.00 88.02  ? 309  SER   B C   1 
ATOM   4954  O  O   . SER   B 2 309 ? 14.715  52.566  4.574   1.00 91.46  ? 309  SER   B O   1 
ATOM   4955  C  CB  . SER   B 2 309 ? 15.825  55.566  4.643   1.00 88.01  ? 309  SER   B CB  1 
ATOM   4956  O  OG  . SER   B 2 309 ? 15.731  56.935  4.985   1.00 90.52  ? 309  SER   B OG  1 
ATOM   4957  N  N   . ILE   B 2 310 ? 14.446  53.553  2.570   1.00 86.67  ? 310  ILE   B N   1 
ATOM   4958  C  CA  . ILE   B 2 310 ? 14.560  52.284  1.859   1.00 88.72  ? 310  ILE   B CA  1 
ATOM   4959  C  C   . ILE   B 2 310 ? 15.891  51.853  2.479   1.00 93.29  ? 310  ILE   B C   1 
ATOM   4960  O  O   . ILE   B 2 310 ? 16.904  52.566  2.388   1.00 92.77  ? 310  ILE   B O   1 
ATOM   4961  C  CB  . ILE   B 2 310 ? 14.461  52.478  0.335   1.00 87.39  ? 310  ILE   B CB  1 
ATOM   4962  C  CG1 . ILE   B 2 310 ? 13.200  53.250  -0.012  1.00 88.18  ? 310  ILE   B CG1 1 
ATOM   4963  C  CG2 . ILE   B 2 310 ? 14.367  51.158  -0.386  1.00 89.65  ? 310  ILE   B CG2 1 
ATOM   4964  C  CD1 . ILE   B 2 310 ? 12.904  53.271  -1.506  1.00 88.92  ? 310  ILE   B CD1 1 
ATOM   4965  N  N   . ALA   B 2 311 ? 15.880  50.690  3.140   1.00 90.34  ? 311  ALA   B N   1 
ATOM   4966  C  CA  . ALA   B 2 311 ? 16.971  50.258  4.004   1.00 88.05  ? 311  ALA   B CA  1 
ATOM   4967  C  C   . ALA   B 2 311 ? 17.701  49.205  3.199   1.00 89.59  ? 311  ALA   B C   1 
ATOM   4968  O  O   . ALA   B 2 311 ? 17.122  48.175  2.850   1.00 97.72  ? 311  ALA   B O   1 
ATOM   4969  C  CB  . ALA   B 2 311 ? 16.550  49.662  5.339   1.00 95.44  ? 311  ALA   B CB  1 
ATOM   4970  N  N   . GLU   B 2 312 ? 18.975  49.443  2.910   1.00 89.76  ? 312  GLU   B N   1 
ATOM   4971  C  CA  . GLU   B 2 312 ? 19.824  48.352  2.452   1.00 93.57  ? 312  GLU   B CA  1 
ATOM   4972  C  C   . GLU   B 2 312 ? 20.043  47.357  3.594   1.00 99.34  ? 312  GLU   B C   1 
ATOM   4973  O  O   . GLU   B 2 312 ? 19.575  46.216  3.540   1.00 96.01  ? 312  GLU   B O   1 
ATOM   4974  C  CB  . GLU   B 2 312 ? 21.138  48.918  1.875   1.00 87.41  ? 312  GLU   B CB  1 
ATOM   4975  C  CG  . GLU   B 2 312 ? 22.044  47.980  1.012   1.00 91.86  ? 312  GLU   B CG  1 
ATOM   4976  C  CD  . GLU   B 2 312 ? 21.325  47.215  -0.106  1.00 99.31  ? 312  GLU   B CD  1 
ATOM   4977  O  OE1 . GLU   B 2 312 ? 20.238  47.638  -0.564  1.00 98.14  ? 312  GLU   B OE1 1 
ATOM   4978  O  OE2 . GLU   B 2 312 ? 21.864  46.168  -0.532  1.00 101.75 ? 312  GLU   B OE2 1 
ATOM   4979  N  N   . CYS   B 2 313 ? 20.698  47.795  4.675   1.00 110.28 ? 313  CYS   B N   1 
ATOM   4980  C  CA  . CYS   B 2 313 ? 20.941  46.957  5.840   1.00 112.77 ? 313  CYS   B CA  1 
ATOM   4981  C  C   . CYS   B 2 313 ? 20.196  47.511  7.057   1.00 113.27 ? 313  CYS   B C   1 
ATOM   4982  O  O   . CYS   B 2 313 ? 19.740  48.659  7.068   1.00 113.19 ? 313  CYS   B O   1 
ATOM   4983  C  CB  . CYS   B 2 313 ? 22.446  46.852  6.137   1.00 116.96 ? 313  CYS   B CB  1 
ATOM   4984  S  SG  . CYS   B 2 313 ? 23.185  48.380  6.837   1.00 123.31 ? 313  CYS   B SG  1 
ATOM   4985  N  N   . LEU   B 2 314 ? 20.075  46.679  8.090   1.00 105.09 ? 314  LEU   B N   1 
ATOM   4986  C  CA  . LEU   B 2 314 ? 19.454  47.067  9.348   1.00 96.36  ? 314  LEU   B CA  1 
ATOM   4987  C  C   . LEU   B 2 314 ? 20.287  46.549  10.502  1.00 99.31  ? 314  LEU   B C   1 
ATOM   4988  O  O   . LEU   B 2 314 ? 20.899  45.482  10.400  1.00 105.94 ? 314  LEU   B O   1 
ATOM   4989  C  CB  . LEU   B 2 314 ? 18.053  46.490  9.490   1.00 96.52  ? 314  LEU   B CB  1 
ATOM   4990  C  CG  . LEU   B 2 314 ? 16.986  47.345  8.844   1.00 99.29  ? 314  LEU   B CG  1 
ATOM   4991  C  CD1 . LEU   B 2 314 ? 15.640  46.675  9.016   1.00 100.47 ? 314  LEU   B CD1 1 
ATOM   4992  C  CD2 . LEU   B 2 314 ? 17.012  48.714  9.477   1.00 96.34  ? 314  LEU   B CD2 1 
ATOM   4993  N  N   . THR   B 2 315 ? 20.282  47.284  11.613  1.00 94.68  ? 315  THR   B N   1 
ATOM   4994  C  CA  . THR   B 2 315 ? 20.918  46.764  12.821  1.00 95.77  ? 315  THR   B CA  1 
ATOM   4995  C  C   . THR   B 2 315 ? 20.371  47.456  14.060  1.00 95.22  ? 315  THR   B C   1 
ATOM   4996  O  O   . THR   B 2 315 ? 20.344  48.688  14.139  1.00 96.21  ? 315  THR   B O   1 
ATOM   4997  C  CB  . THR   B 2 315 ? 22.450  46.900  12.769  1.00 96.13  ? 315  THR   B CB  1 
ATOM   4998  O  OG1 . THR   B 2 315 ? 23.008  46.451  14.013  1.00 98.13  ? 315  THR   B OG1 1 
ATOM   4999  C  CG2 . THR   B 2 315 ? 22.901  48.334  12.475  1.00 92.03  ? 315  THR   B CG2 1 
ATOM   5000  N  N   . TYR   B 2 316 ? 19.939  46.658  15.024  1.00 94.14  ? 316  TYR   B N   1 
ATOM   5001  C  CA  . TYR   B 2 316 ? 19.601  47.198  16.316  1.00 96.48  ? 316  TYR   B CA  1 
ATOM   5002  C  C   . TYR   B 2 316 ? 20.881  47.553  17.081  1.00 98.24  ? 316  TYR   B C   1 
ATOM   5003  O  O   . TYR   B 2 316 ? 21.755  46.700  17.280  1.00 103.08 ? 316  TYR   B O   1 
ATOM   5004  C  CB  . TYR   B 2 316 ? 18.789  46.178  17.137  1.00 99.81  ? 316  TYR   B CB  1 
ATOM   5005  C  CG  . TYR   B 2 316 ? 18.380  46.709  18.502  1.00 99.74  ? 316  TYR   B CG  1 
ATOM   5006  C  CD1 . TYR   B 2 316 ? 17.348  47.630  18.637  1.00 100.83 ? 316  TYR   B CD1 1 
ATOM   5007  C  CD2 . TYR   B 2 316 ? 19.052  46.320  19.651  1.00 104.96 ? 316  TYR   B CD2 1 
ATOM   5008  C  CE1 . TYR   B 2 316 ? 16.982  48.134  19.889  1.00 109.07 ? 316  TYR   B CE1 1 
ATOM   5009  C  CE2 . TYR   B 2 316 ? 18.695  46.820  20.912  1.00 111.66 ? 316  TYR   B CE2 1 
ATOM   5010  C  CZ  . TYR   B 2 316 ? 17.660  47.727  21.028  1.00 111.16 ? 316  TYR   B CZ  1 
ATOM   5011  O  OH  . TYR   B 2 316 ? 17.316  48.219  22.280  1.00 110.10 ? 316  TYR   B OH  1 
ATOM   5012  N  N   . LEU   B 2 317 ? 21.000  48.825  17.471  1.00 97.93  ? 317  LEU   B N   1 
ATOM   5013  C  CA  . LEU   B 2 317 ? 22.097  49.268  18.316  1.00 101.37 ? 317  LEU   B CA  1 
ATOM   5014  C  C   . LEU   B 2 317 ? 21.921  49.045  19.826  1.00 105.73 ? 317  LEU   B C   1 
ATOM   5015  O  O   . LEU   B 2 317 ? 22.617  48.216  20.422  1.00 106.73 ? 317  LEU   B O   1 
ATOM   5016  C  CB  . LEU   B 2 317 ? 22.359  50.759  18.167  1.00 98.06  ? 317  LEU   B CB  1 
ATOM   5017  C  CG  . LEU   B 2 317 ? 22.360  51.271  16.731  1.00 96.14  ? 317  LEU   B CG  1 
ATOM   5018  C  CD1 . LEU   B 2 317 ? 22.890  52.714  16.657  1.00 92.67  ? 317  LEU   B CD1 1 
ATOM   5019  C  CD2 . LEU   B 2 317 ? 23.168  50.338  15.863  1.00 94.22  ? 317  LEU   B CD2 1 
ATOM   5020  N  N   . ASP   B 2 318 ? 20.985  49.772  20.436  1.00 109.07 ? 318  ASP   B N   1 
ATOM   5021  C  CA  . ASP   B 2 318 ? 20.614  49.543  21.826  1.00 111.23 ? 318  ASP   B CA  1 
ATOM   5022  C  C   . ASP   B 2 318 ? 19.705  50.683  22.257  1.00 113.21 ? 318  ASP   B C   1 
ATOM   5023  O  O   . ASP   B 2 318 ? 19.728  51.770  21.669  1.00 114.29 ? 318  ASP   B O   1 
ATOM   5024  C  CB  . ASP   B 2 318 ? 21.772  49.347  22.803  1.00 113.40 ? 318  ASP   B CB  1 
ATOM   5025  C  CG  . ASP   B 2 318 ? 21.313  48.808  24.132  1.00 120.62 ? 318  ASP   B CG  1 
ATOM   5026  O  OD1 . ASP   B 2 318 ? 20.468  47.881  24.129  1.00 121.94 ? 318  ASP   B OD1 1 
ATOM   5027  O  OD2 . ASP   B 2 318 ? 21.795  49.305  25.180  1.00 126.45 ? 318  ASP   B OD2 1 
ATOM   5028  N  N   . ASN   B 2 319 ? 18.899  50.413  23.290  1.00 110.81 ? 319  ASN   B N   1 
ATOM   5029  C  CA  . ASN   B 2 319 ? 17.939  51.373  23.857  1.00 112.45 ? 319  ASN   B CA  1 
ATOM   5030  C  C   . ASN   B 2 319 ? 16.877  51.807  22.842  1.00 110.32 ? 319  ASN   B C   1 
ATOM   5031  O  O   . ASN   B 2 319 ? 16.379  52.941  22.884  1.00 103.53 ? 319  ASN   B O   1 
ATOM   5032  C  CB  . ASN   B 2 319 ? 18.655  52.603  24.436  1.00 114.17 ? 319  ASN   B CB  1 
ATOM   5033  C  CG  . ASN   B 2 319 ? 19.749  52.240  25.439  1.00 115.69 ? 319  ASN   B CG  1 
ATOM   5034  O  OD1 . ASN   B 2 319 ? 19.470  51.953  26.609  1.00 115.27 ? 319  ASN   B OD1 1 
ATOM   5035  N  ND2 . ASN   B 2 319 ? 21.008  52.286  24.989  1.00 117.71 ? 319  ASN   B ND2 1 
ATOM   5036  N  N   . GLY   B 2 320 ? 16.528  50.903  21.922  1.00 109.63 ? 320  GLY   B N   1 
ATOM   5037  C  CA  . GLY   B 2 320 ? 15.546  51.166  20.892  1.00 107.66 ? 320  GLY   B CA  1 
ATOM   5038  C  C   . GLY   B 2 320 ? 16.051  51.878  19.652  1.00 104.93 ? 320  GLY   B C   1 
ATOM   5039  O  O   . GLY   B 2 320 ? 15.239  52.193  18.771  1.00 104.85 ? 320  GLY   B O   1 
ATOM   5040  N  N   . VAL   B 2 321 ? 17.348  52.146  19.543  1.00 102.19 ? 321  VAL   B N   1 
ATOM   5041  C  CA  . VAL   B 2 321 ? 17.884  52.840  18.379  1.00 96.13  ? 321  VAL   B CA  1 
ATOM   5042  C  C   . VAL   B 2 321 ? 18.274  51.805  17.339  1.00 96.75  ? 321  VAL   B C   1 
ATOM   5043  O  O   . VAL   B 2 321 ? 19.113  50.940  17.596  1.00 98.38  ? 321  VAL   B O   1 
ATOM   5044  C  CB  . VAL   B 2 321 ? 19.081  53.722  18.752  1.00 97.12  ? 321  VAL   B CB  1 
ATOM   5045  C  CG1 . VAL   B 2 321 ? 19.556  54.470  17.538  1.00 96.73  ? 321  VAL   B CG1 1 
ATOM   5046  C  CG2 . VAL   B 2 321 ? 18.679  54.701  19.822  1.00 107.11 ? 321  VAL   B CG2 1 
ATOM   5047  N  N   . VAL   B 2 322 ? 17.650  51.886  16.165  1.00 96.45  ? 322  VAL   B N   1 
ATOM   5048  C  CA  . VAL   B 2 322 ? 17.993  51.051  15.019  1.00 93.35  ? 322  VAL   B CA  1 
ATOM   5049  C  C   . VAL   B 2 322 ? 18.656  51.933  13.982  1.00 89.33  ? 322  VAL   B C   1 
ATOM   5050  O  O   . VAL   B 2 322 ? 18.151  53.017  13.666  1.00 89.34  ? 322  VAL   B O   1 
ATOM   5051  C  CB  . VAL   B 2 322 ? 16.756  50.361  14.416  1.00 94.10  ? 322  VAL   B CB  1 
ATOM   5052  C  CG1 . VAL   B 2 322 ? 17.153  49.455  13.236  1.00 89.61  ? 322  VAL   B CG1 1 
ATOM   5053  C  CG2 . VAL   B 2 322 ? 16.004  49.590  15.485  1.00 96.81  ? 322  VAL   B CG2 1 
ATOM   5054  N  N   . PHE   B 2 323 ? 19.785  51.479  13.461  1.00 87.64  ? 323  PHE   B N   1 
ATOM   5055  C  CA  . PHE   B 2 323 ? 20.422  52.178  12.364  1.00 86.83  ? 323  PHE   B CA  1 
ATOM   5056  C  C   . PHE   B 2 323 ? 19.894  51.633  11.050  1.00 89.28  ? 323  PHE   B C   1 
ATOM   5057  O  O   . PHE   B 2 323 ? 19.935  50.423  10.795  1.00 94.72  ? 323  PHE   B O   1 
ATOM   5058  C  CB  . PHE   B 2 323 ? 21.940  52.060  12.397  1.00 83.13  ? 323  PHE   B CB  1 
ATOM   5059  C  CG  . PHE   B 2 323 ? 22.585  52.707  11.230  1.00 83.52  ? 323  PHE   B CG  1 
ATOM   5060  C  CD1 . PHE   B 2 323 ? 22.753  54.083  11.194  1.00 85.16  ? 323  PHE   B CD1 1 
ATOM   5061  C  CD2 . PHE   B 2 323 ? 22.968  51.955  10.140  1.00 85.26  ? 323  PHE   B CD2 1 
ATOM   5062  C  CE1 . PHE   B 2 323 ? 23.331  54.694  10.104  1.00 85.75  ? 323  PHE   B CE1 1 
ATOM   5063  C  CE2 . PHE   B 2 323 ? 23.542  52.554  9.040   1.00 87.06  ? 323  PHE   B CE2 1 
ATOM   5064  C  CZ  . PHE   B 2 323 ? 23.719  53.928  9.017   1.00 88.82  ? 323  PHE   B CZ  1 
ATOM   5065  N  N   . VAL   B 2 324 ? 19.433  52.534  10.212  1.00 86.92  ? 324  VAL   B N   1 
ATOM   5066  C  CA  . VAL   B 2 324 ? 18.947  52.195  8.897   1.00 83.69  ? 324  VAL   B CA  1 
ATOM   5067  C  C   . VAL   B 2 324 ? 19.986  52.676  7.903   1.00 85.90  ? 324  VAL   B C   1 
ATOM   5068  O  O   . VAL   B 2 324 ? 20.136  53.882  7.666   1.00 87.23  ? 324  VAL   B O   1 
ATOM   5069  C  CB  . VAL   B 2 324 ? 17.576  52.825  8.661   1.00 86.77  ? 324  VAL   B CB  1 
ATOM   5070  C  CG1 . VAL   B 2 324 ? 17.137  52.620  7.252   1.00 92.54  ? 324  VAL   B CG1 1 
ATOM   5071  C  CG2 . VAL   B 2 324 ? 16.606  52.213  9.616   1.00 89.75  ? 324  VAL   B CG2 1 
ATOM   5072  N  N   . GLY   B 2 325 ? 20.760  51.749  7.343   1.00 87.17  ? 325  GLY   B N   1 
ATOM   5073  C  CA  . GLY   B 2 325 ? 21.654  52.069  6.252   1.00 84.43  ? 325  GLY   B CA  1 
ATOM   5074  C  C   . GLY   B 2 325 ? 20.877  52.050  4.953   1.00 86.98  ? 325  GLY   B C   1 
ATOM   5075  O  O   . GLY   B 2 325 ? 20.089  51.137  4.703   1.00 92.17  ? 325  GLY   B O   1 
ATOM   5076  N  N   . SER   B 2 326 ? 21.092  53.068  4.125   1.00 82.49  ? 326  SER   B N   1 
ATOM   5077  C  CA  . SER   B 2 326 ? 20.254  53.257  2.957   1.00 79.12  ? 326  SER   B CA  1 
ATOM   5078  C  C   . SER   B 2 326 ? 21.116  53.567  1.748   1.00 79.35  ? 326  SER   B C   1 
ATOM   5079  O  O   . SER   B 2 326 ? 22.098  54.315  1.845   1.00 76.81  ? 326  SER   B O   1 
ATOM   5080  C  CB  . SER   B 2 326 ? 19.243  54.389  3.188   1.00 85.04  ? 326  SER   B CB  1 
ATOM   5081  O  OG  . SER   B 2 326 ? 18.197  54.352  2.230   1.00 88.07  ? 326  SER   B OG  1 
ATOM   5082  N  N   . ARG   B 2 327 ? 20.710  52.995  0.611   1.00 79.69  ? 327  ARG   B N   1 
ATOM   5083  C  CA  . ARG   B 2 327 ? 21.368  53.177  -0.675  1.00 77.47  ? 327  ARG   B CA  1 
ATOM   5084  C  C   . ARG   B 2 327 ? 20.595  54.078  -1.618  1.00 75.69  ? 327  ARG   B C   1 
ATOM   5085  O  O   . ARG   B 2 327 ? 21.198  54.686  -2.508  1.00 77.85  ? 327  ARG   B O   1 
ATOM   5086  C  CB  . ARG   B 2 327 ? 21.589  51.828  -1.373  1.00 81.87  ? 327  ARG   B CB  1 
ATOM   5087  C  CG  . ARG   B 2 327 ? 22.735  50.977  -0.829  1.00 83.48  ? 327  ARG   B CG  1 
ATOM   5088  C  CD  . ARG   B 2 327 ? 24.067  51.289  -1.510  1.00 85.17  ? 327  ARG   B CD  1 
ATOM   5089  N  NE  . ARG   B 2 327 ? 24.060  51.055  -2.953  1.00 87.99  ? 327  ARG   B NE  1 
ATOM   5090  C  CZ  . ARG   B 2 327 ? 23.979  49.858  -3.525  1.00 95.73  ? 327  ARG   B CZ  1 
ATOM   5091  N  NH1 . ARG   B 2 327 ? 23.834  48.752  -2.806  1.00 97.24  ? 327  ARG   B NH1 1 
ATOM   5092  N  NH2 . ARG   B 2 327 ? 24.043  49.768  -4.852  1.00 95.41  ? 327  ARG   B NH2 1 
ATOM   5093  N  N   . LEU   B 2 328 ? 19.275  54.127  -1.493  1.00 75.62  ? 328  LEU   B N   1 
ATOM   5094  C  CA  . LEU   B 2 328 ? 18.484  55.015  -2.329  1.00 75.61  ? 328  LEU   B CA  1 
ATOM   5095  C  C   . LEU   B 2 328 ? 18.301  56.366  -1.665  1.00 76.38  ? 328  LEU   B C   1 
ATOM   5096  O  O   . LEU   B 2 328 ? 18.381  57.395  -2.333  1.00 82.46  ? 328  LEU   B O   1 
ATOM   5097  C  CB  . LEU   B 2 328 ? 17.129  54.394  -2.627  1.00 75.36  ? 328  LEU   B CB  1 
ATOM   5098  C  CG  . LEU   B 2 328 ? 17.187  53.041  -3.316  1.00 74.98  ? 328  LEU   B CG  1 
ATOM   5099  C  CD1 . LEU   B 2 328 ? 15.770  52.555  -3.561  1.00 74.82  ? 328  LEU   B CD1 1 
ATOM   5100  C  CD2 . LEU   B 2 328 ? 18.007  53.110  -4.603  1.00 74.84  ? 328  LEU   B CD2 1 
ATOM   5101  N  N   . GLY   B 2 329 ? 18.103  56.388  -0.353  1.00 77.66  ? 329  GLY   B N   1 
ATOM   5102  C  CA  . GLY   B 2 329 ? 17.919  57.640  0.347   1.00 79.85  ? 329  GLY   B CA  1 
ATOM   5103  C  C   . GLY   B 2 329 ? 18.830  57.830  1.538   1.00 82.27  ? 329  GLY   B C   1 
ATOM   5104  O  O   . GLY   B 2 329 ? 19.821  57.107  1.702   1.00 81.73  ? 329  GLY   B O   1 
ATOM   5105  N  N   . ASP   B 2 330 ? 18.503  58.806  2.377   1.00 81.48  ? 330  ASP   B N   1 
ATOM   5106  C  CA  . ASP   B 2 330 ? 19.353  59.097  3.519   1.00 82.18  ? 330  ASP   B CA  1 
ATOM   5107  C  C   . ASP   B 2 330 ? 19.336  57.941  4.524   1.00 85.66  ? 330  ASP   B C   1 
ATOM   5108  O  O   . ASP   B 2 330 ? 18.305  57.302  4.751   1.00 85.41  ? 330  ASP   B O   1 
ATOM   5109  C  CB  . ASP   B 2 330 ? 18.893  60.400  4.174   1.00 82.59  ? 330  ASP   B CB  1 
ATOM   5110  C  CG  . ASP   B 2 330 ? 19.638  61.603  3.652   1.00 81.26  ? 330  ASP   B CG  1 
ATOM   5111  O  OD1 . ASP   B 2 330 ? 20.247  61.491  2.579   1.00 83.80  ? 330  ASP   B OD1 1 
ATOM   5112  O  OD2 . ASP   B 2 330 ? 19.657  62.647  4.333   1.00 81.59  ? 330  ASP   B OD2 1 
ATOM   5113  N  N   . SER   B 2 331 ? 20.494  57.655  5.113   1.00 84.20  ? 331  SER   B N   1 
ATOM   5114  C  CA  . SER   B 2 331 ? 20.526  56.740  6.240   1.00 80.40  ? 331  SER   B CA  1 
ATOM   5115  C  C   . SER   B 2 331 ? 20.032  57.437  7.506   1.00 84.91  ? 331  SER   B C   1 
ATOM   5116  O  O   . SER   B 2 331 ? 20.073  58.665  7.628   1.00 85.68  ? 331  SER   B O   1 
ATOM   5117  C  CB  . SER   B 2 331 ? 21.934  56.201  6.450   1.00 81.19  ? 331  SER   B CB  1 
ATOM   5118  O  OG  . SER   B 2 331 ? 22.241  55.221  5.479   1.00 86.15  ? 331  SER   B OG  1 
ATOM   5119  N  N   . GLN   B 2 332 ? 19.569  56.638  8.470   1.00 87.92  ? 332  GLN   B N   1 
ATOM   5120  C  CA  . GLN   B 2 332 ? 18.997  57.230  9.672   1.00 90.03  ? 332  GLN   B CA  1 
ATOM   5121  C  C   . GLN   B 2 332 ? 19.206  56.360  10.917  1.00 91.34  ? 332  GLN   B C   1 
ATOM   5122  O  O   . GLN   B 2 332 ? 19.577  55.184  10.838  1.00 87.19  ? 332  GLN   B O   1 
ATOM   5123  C  CB  . GLN   B 2 332 ? 17.508  57.535  9.464   1.00 86.79  ? 332  GLN   B CB  1 
ATOM   5124  C  CG  . GLN   B 2 332 ? 16.736  56.445  8.750   1.00 85.47  ? 332  GLN   B CG  1 
ATOM   5125  C  CD  . GLN   B 2 332 ? 15.285  56.821  8.549   1.00 88.58  ? 332  GLN   B CD  1 
ATOM   5126  O  OE1 . GLN   B 2 332 ? 14.443  55.966  8.332   1.00 90.22  ? 332  GLN   B OE1 1 
ATOM   5127  N  NE2 . GLN   B 2 332 ? 14.985  58.116  8.629   1.00 90.83  ? 332  GLN   B NE2 1 
ATOM   5128  N  N   . LEU   B 2 333 ? 19.034  57.011  12.081  1.00 95.41  ? 333  LEU   B N   1 
ATOM   5129  C  CA  . LEU   B 2 333 ? 18.811  56.388  13.387  1.00 93.00  ? 333  LEU   B CA  1 
ATOM   5130  C  C   . LEU   B 2 333 ? 17.349  56.575  13.746  1.00 93.64  ? 333  LEU   B C   1 
ATOM   5131  O  O   . LEU   B 2 333 ? 16.857  57.708  13.777  1.00 98.24  ? 333  LEU   B O   1 
ATOM   5132  C  CB  . LEU   B 2 333 ? 19.674  57.023  14.475  1.00 91.96  ? 333  LEU   B CB  1 
ATOM   5133  C  CG  . LEU   B 2 333 ? 21.105  56.528  14.529  1.00 94.31  ? 333  LEU   B CG  1 
ATOM   5134  C  CD1 . LEU   B 2 333 ? 21.788  56.996  15.789  1.00 95.75  ? 333  LEU   B CD1 1 
ATOM   5135  C  CD2 . LEU   B 2 333 ? 21.122  55.021  14.451  1.00 95.12  ? 333  LEU   B CD2 1 
ATOM   5136  N  N   . VAL   B 2 334 ? 16.653  55.482  14.004  1.00 91.12  ? 334  VAL   B N   1 
ATOM   5137  C  CA  . VAL   B 2 334 ? 15.252  55.539  14.389  1.00 94.38  ? 334  VAL   B CA  1 
ATOM   5138  C  C   . VAL   B 2 334 ? 15.164  55.081  15.830  1.00 97.13  ? 334  VAL   B C   1 
ATOM   5139  O  O   . VAL   B 2 334 ? 15.861  54.143  16.231  1.00 100.89 ? 334  VAL   B O   1 
ATOM   5140  C  CB  . VAL   B 2 334 ? 14.350  54.672  13.486  1.00 94.83  ? 334  VAL   B CB  1 
ATOM   5141  C  CG1 . VAL   B 2 334 ? 14.268  55.240  12.081  1.00 92.68  ? 334  VAL   B CG1 1 
ATOM   5142  C  CG2 . VAL   B 2 334 ? 14.852  53.263  13.449  1.00 93.74  ? 334  VAL   B CG2 1 
ATOM   5143  N  N   . LYS   B 2 335 ? 14.327  55.753  16.611  1.00 97.43  ? 335  LYS   B N   1 
ATOM   5144  C  CA  . LYS   B 2 335 ? 13.946  55.271  17.931  1.00 100.27 ? 335  LYS   B CA  1 
ATOM   5145  C  C   . LYS   B 2 335 ? 12.636  54.513  17.765  1.00 104.39 ? 335  LYS   B C   1 
ATOM   5146  O  O   . LYS   B 2 335 ? 11.628  55.081  17.342  1.00 104.70 ? 335  LYS   B O   1 
ATOM   5147  C  CB  . LYS   B 2 335 ? 13.803  56.406  18.935  1.00 101.17 ? 335  LYS   B CB  1 
ATOM   5148  N  N   . LEU   B 2 336 ? 12.672  53.218  18.042  1.00 108.20 ? 336  LEU   B N   1 
ATOM   5149  C  CA  . LEU   B 2 336 ? 11.449  52.444  18.159  1.00 112.58 ? 336  LEU   B CA  1 
ATOM   5150  C  C   . LEU   B 2 336 ? 10.826  52.745  19.517  1.00 119.48 ? 336  LEU   B C   1 
ATOM   5151  O  O   . LEU   B 2 336 ? 11.465  52.549  20.555  1.00 120.21 ? 336  LEU   B O   1 
ATOM   5152  C  CB  . LEU   B 2 336 ? 11.742  50.960  18.002  1.00 112.38 ? 336  LEU   B CB  1 
ATOM   5153  C  CG  . LEU   B 2 336 ? 12.455  50.528  16.720  1.00 102.58 ? 336  LEU   B CG  1 
ATOM   5154  C  CD1 . LEU   B 2 336 ? 12.192  49.072  16.403  1.00 99.42  ? 336  LEU   B CD1 1 
ATOM   5155  C  CD2 . LEU   B 2 336 ? 12.025  51.400  15.560  1.00 108.57 ? 336  LEU   B CD2 1 
ATOM   5156  N  N   . ASN   B 2 337 ? 9.597   53.270  19.517  1.00 124.87 ? 337  ASN   B N   1 
ATOM   5157  C  CA  . ASN   B 2 337 ? 8.910   53.602  20.763  1.00 125.81 ? 337  ASN   B CA  1 
ATOM   5158  C  C   . ASN   B 2 337 ? 8.127   52.392  21.273  1.00 132.66 ? 337  ASN   B C   1 
ATOM   5159  O  O   . ASN   B 2 337 ? 8.080   51.331  20.642  1.00 131.69 ? 337  ASN   B O   1 
ATOM   5160  C  CB  . ASN   B 2 337 ? 7.967   54.799  20.570  1.00 124.19 ? 337  ASN   B CB  1 
ATOM   5161  C  CG  . ASN   B 2 337 ? 8.688   56.140  20.603  1.00 115.64 ? 337  ASN   B CG  1 
ATOM   5162  O  OD1 . ASN   B 2 337 ? 8.916   56.706  21.672  1.00 118.12 ? 337  ASN   B OD1 1 
ATOM   5163  N  ND2 . ASN   B 2 337 ? 9.021   56.664  19.431  1.00 109.72 ? 337  ASN   B ND2 1 
ATOM   5164  N  N   . VAL   B 2 338 ? 7.514   52.560  22.439  1.00 139.06 ? 338  VAL   B N   1 
ATOM   5165  C  CA  . VAL   B 2 338 ? 6.753   51.482  23.061  1.00 143.96 ? 338  VAL   B CA  1 
ATOM   5166  C  C   . VAL   B 2 338 ? 5.305   51.493  22.587  1.00 151.52 ? 338  VAL   B C   1 
ATOM   5167  O  O   . VAL   B 2 338 ? 4.758   50.453  22.200  1.00 151.42 ? 338  VAL   B O   1 
ATOM   5168  C  CB  . VAL   B 2 338 ? 6.848   51.574  24.603  1.00 139.66 ? 338  VAL   B CB  1 
ATOM   5169  C  CG1 . VAL   B 2 338 ? 8.277   51.642  25.022  1.00 138.71 ? 338  VAL   B CG1 1 
ATOM   5170  C  CG2 . VAL   B 2 338 ? 6.115   52.793  25.147  1.00 147.54 ? 338  VAL   B CG2 1 
ATOM   5171  N  N   . ASP   B 2 339 ? 4.695   52.675  22.542  1.00 164.98 ? 339  ASP   B N   1 
ATOM   5172  C  CA  . ASP   B 2 339 ? 3.281   52.825  22.253  1.00 166.40 ? 339  ASP   B CA  1 
ATOM   5173  C  C   . ASP   B 2 339 ? 3.114   53.201  20.791  1.00 169.40 ? 339  ASP   B C   1 
ATOM   5174  O  O   . ASP   B 2 339 ? 3.873   54.018  20.264  1.00 167.44 ? 339  ASP   B O   1 
ATOM   5175  C  CB  . ASP   B 2 339 ? 2.635   53.887  23.152  1.00 167.91 ? 339  ASP   B CB  1 
ATOM   5176  N  N   . SER   B 2 340 ? 2.138   52.568  20.133  1.00 159.21 ? 340  SER   B N   1 
ATOM   5177  C  CA  . SER   B 2 340 ? 1.752   52.972  18.789  1.00 157.96 ? 340  SER   B CA  1 
ATOM   5178  C  C   . SER   B 2 340 ? 1.529   54.478  18.763  1.00 161.25 ? 340  SER   B C   1 
ATOM   5179  O  O   . SER   B 2 340 ? 0.786   55.024  19.585  1.00 164.73 ? 340  SER   B O   1 
ATOM   5180  C  CB  . SER   B 2 340 ? 0.479   52.243  18.340  1.00 156.94 ? 340  SER   B CB  1 
ATOM   5181  O  OG  . SER   B 2 340 ? 0.510   50.860  18.646  1.00 151.66 ? 340  SER   B OG  1 
ATOM   5182  N  N   . ASN   B 2 341 ? 2.214   55.154  17.848  1.00 158.40 ? 341  ASN   B N   1 
ATOM   5183  C  CA  . ASN   B 2 341 ? 2.091   56.599  17.743  1.00 162.39 ? 341  ASN   B CA  1 
ATOM   5184  C  C   . ASN   B 2 341 ? 0.712   56.913  17.151  1.00 164.25 ? 341  ASN   B C   1 
ATOM   5185  O  O   . ASN   B 2 341 ? -0.127  56.029  16.960  1.00 162.83 ? 341  ASN   B O   1 
ATOM   5186  C  CB  . ASN   B 2 341 ? 3.271   57.186  16.955  1.00 163.96 ? 341  ASN   B CB  1 
ATOM   5187  C  CG  . ASN   B 2 341 ? 3.059   57.229  15.423  1.00 160.13 ? 341  ASN   B CG  1 
ATOM   5188  O  OD1 . ASN   B 2 341 ? 2.271   56.485  14.850  1.00 160.90 ? 341  ASN   B OD1 1 
ATOM   5189  N  ND2 . ASN   B 2 341 ? 3.814   58.104  14.761  1.00 153.93 ? 341  ASN   B ND2 1 
ATOM   5190  N  N   . GLU   B 2 342 ? 0.461   58.205  16.879  1.00 169.92 ? 342  GLU   B N   1 
ATOM   5191  C  CA  . GLU   B 2 342 ? -0.833  58.639  16.349  1.00 170.80 ? 342  GLU   B CA  1 
ATOM   5192  C  C   . GLU   B 2 342 ? -1.279  57.887  15.088  1.00 170.98 ? 342  GLU   B C   1 
ATOM   5193  O  O   . GLU   B 2 342 ? -2.488  57.747  14.847  1.00 170.63 ? 342  GLU   B O   1 
ATOM   5194  C  CB  . GLU   B 2 342 ? -0.785  60.159  16.081  1.00 170.76 ? 342  GLU   B CB  1 
ATOM   5195  C  CG  . GLU   B 2 342 ? 0.523   60.670  15.461  1.00 171.43 ? 342  GLU   B CG  1 
ATOM   5196  C  CD  . GLU   B 2 342 ? 1.525   61.194  16.497  1.00 168.46 ? 342  GLU   B CD  1 
ATOM   5197  O  OE1 . GLU   B 2 342 ? 1.789   60.488  17.503  1.00 164.99 ? 342  GLU   B OE1 1 
ATOM   5198  O  OE2 . GLU   B 2 342 ? 2.060   62.307  16.292  1.00 166.51 ? 342  GLU   B OE2 1 
ATOM   5199  N  N   . GLN   B 2 343 ? -0.334  57.425  14.259  1.00 165.90 ? 343  GLN   B N   1 
ATOM   5200  C  CA  . GLN   B 2 343 ? -0.651  56.630  13.078  1.00 163.31 ? 343  GLN   B CA  1 
ATOM   5201  C  C   . GLN   B 2 343 ? -0.312  55.145  13.220  1.00 159.79 ? 343  GLN   B C   1 
ATOM   5202  O  O   . GLN   B 2 343 ? -0.668  54.354  12.334  1.00 157.47 ? 343  GLN   B O   1 
ATOM   5203  C  CB  . GLN   B 2 343 ? 0.083   57.199  11.846  1.00 159.46 ? 343  GLN   B CB  1 
ATOM   5204  C  CG  . GLN   B 2 343 ? -0.295  58.632  11.487  1.00 162.85 ? 343  GLN   B CG  1 
ATOM   5205  C  CD  . GLN   B 2 343 ? -1.587  58.726  10.664  1.00 165.93 ? 343  GLN   B CD  1 
ATOM   5206  O  OE1 . GLN   B 2 343 ? -2.303  57.736  10.495  1.00 164.40 ? 343  GLN   B OE1 1 
ATOM   5207  N  NE2 . GLN   B 2 343 ? -1.880  59.920  10.141  1.00 164.79 ? 343  GLN   B NE2 1 
ATOM   5208  N  N   . GLY   B 2 344 ? 0.366   54.734  14.303  1.00 158.11 ? 344  GLY   B N   1 
ATOM   5209  C  CA  . GLY   B 2 344 ? 0.810   53.365  14.510  1.00 155.28 ? 344  GLY   B CA  1 
ATOM   5210  C  C   . GLY   B 2 344 ? 2.321   53.191  14.439  1.00 148.91 ? 344  GLY   B C   1 
ATOM   5211  O  O   . GLY   B 2 344 ? 2.877   52.347  15.156  1.00 145.27 ? 344  GLY   B O   1 
ATOM   5212  N  N   . SER   B 2 345 ? 2.991   53.983  13.599  1.00 148.52 ? 345  SER   B N   1 
ATOM   5213  C  CA  . SER   B 2 345 ? 4.443   53.990  13.489  1.00 141.25 ? 345  SER   B CA  1 
ATOM   5214  C  C   . SER   B 2 345 ? 4.873   54.023  14.941  1.00 140.65 ? 345  SER   B C   1 
ATOM   5215  O  O   . SER   B 2 345 ? 4.592   55.012  15.630  1.00 140.60 ? 345  SER   B O   1 
ATOM   5216  C  CB  . SER   B 2 345 ? 4.884   55.076  12.504  1.00 136.84 ? 345  SER   B CB  1 
ATOM   5217  O  OG  . SER   B 2 345 ? 6.225   54.913  12.063  1.00 130.19 ? 345  SER   B OG  1 
ATOM   5218  N  N   . TYR   B 2 346 ? 5.550   52.976  15.431  1.00 130.87 ? 346  TYR   B N   1 
ATOM   5219  C  CA  . TYR   B 2 346 ? 6.255   53.123  16.718  1.00 126.26 ? 346  TYR   B CA  1 
ATOM   5220  C  C   . TYR   B 2 346 ? 7.622   53.632  16.283  1.00 119.48 ? 346  TYR   B C   1 
ATOM   5221  O  O   . TYR   B 2 346 ? 8.412   54.043  17.135  1.00 117.12 ? 346  TYR   B O   1 
ATOM   5222  C  CB  . TYR   B 2 346 ? 6.476   51.728  17.357  1.00 129.77 ? 346  TYR   B CB  1 
ATOM   5223  C  CG  . TYR   B 2 346 ? 5.288   50.791  17.526  1.00 139.71 ? 346  TYR   B CG  1 
ATOM   5224  C  CD1 . TYR   B 2 346 ? 4.825   50.029  16.457  1.00 137.73 ? 346  TYR   B CD1 1 
ATOM   5225  C  CD2 . TYR   B 2 346 ? 4.684   50.605  18.770  1.00 147.13 ? 346  TYR   B CD2 1 
ATOM   5226  C  CE1 . TYR   B 2 346 ? 3.765   49.141  16.602  1.00 137.97 ? 346  TYR   B CE1 1 
ATOM   5227  C  CE2 . TYR   B 2 346 ? 3.619   49.715  18.927  1.00 151.02 ? 346  TYR   B CE2 1 
ATOM   5228  C  CZ  . TYR   B 2 346 ? 3.164   48.983  17.836  1.00 144.97 ? 346  TYR   B CZ  1 
ATOM   5229  O  OH  . TYR   B 2 346 ? 2.110   48.100  17.979  1.00 140.69 ? 346  TYR   B OH  1 
ATOM   5230  N  N   . VAL   B 2 347 ? 7.946   53.580  14.995  1.00 120.07 ? 347  VAL   B N   1 
ATOM   5231  C  CA  . VAL   B 2 347 ? 9.170   54.213  14.525  1.00 116.63 ? 347  VAL   B CA  1 
ATOM   5232  C  C   . VAL   B 2 347 ? 9.027   55.731  14.609  1.00 115.04 ? 347  VAL   B C   1 
ATOM   5233  O  O   . VAL   B 2 347 ? 7.984   56.306  14.258  1.00 116.11 ? 347  VAL   B O   1 
ATOM   5234  C  CB  . VAL   B 2 347 ? 9.498   53.757  13.093  1.00 114.65 ? 347  VAL   B CB  1 
ATOM   5235  C  CG1 . VAL   B 2 347 ? 10.902  54.192  12.704  1.00 108.13 ? 347  VAL   B CG1 1 
ATOM   5236  C  CG2 . VAL   B 2 347 ? 9.372   52.264  12.966  1.00 110.36 ? 347  VAL   B CG2 1 
ATOM   5237  N  N   . VAL   B 2 348 ? 10.082  56.392  15.074  1.00 107.72 ? 348  VAL   B N   1 
ATOM   5238  C  CA  . VAL   B 2 348 ? 10.144  57.847  15.173  1.00 101.82 ? 348  VAL   B CA  1 
ATOM   5239  C  C   . VAL   B 2 348 ? 11.535  58.245  14.716  1.00 99.75  ? 348  VAL   B C   1 
ATOM   5240  O  O   . VAL   B 2 348 ? 12.529  57.803  15.303  1.00 100.97 ? 348  VAL   B O   1 
ATOM   5241  C  CB  . VAL   B 2 348 ? 9.877   58.350  16.601  1.00 104.08 ? 348  VAL   B CB  1 
ATOM   5242  C  CG1 . VAL   B 2 348 ? 10.473  59.720  16.802  1.00 102.21 ? 348  VAL   B CG1 1 
ATOM   5243  C  CG2 . VAL   B 2 348 ? 8.378   58.364  16.877  1.00 111.09 ? 348  VAL   B CG2 1 
ATOM   5244  N  N   . ALA   B 2 349 ? 11.616  59.017  13.636  1.00 99.09  ? 349  ALA   B N   1 
ATOM   5245  C  CA  . ALA   B 2 349 ? 12.921  59.371  13.100  1.00 96.58  ? 349  ALA   B CA  1 
ATOM   5246  C  C   . ALA   B 2 349 ? 13.693  60.170  14.134  1.00 96.87  ? 349  ALA   B C   1 
ATOM   5247  O  O   . ALA   B 2 349 ? 13.117  60.941  14.903  1.00 102.52 ? 349  ALA   B O   1 
ATOM   5248  C  CB  . ALA   B 2 349 ? 12.777  60.161  11.799  1.00 103.27 ? 349  ALA   B CB  1 
ATOM   5249  N  N   . MET   B 2 350 ? 14.998  59.955  14.181  1.00 97.08  ? 350  MET   B N   1 
ATOM   5250  C  CA  . MET   B 2 350 ? 15.775  60.463  15.300  1.00 96.19  ? 350  MET   B CA  1 
ATOM   5251  C  C   . MET   B 2 350 ? 17.117  61.039  14.894  1.00 97.47  ? 350  MET   B C   1 
ATOM   5252  O  O   . MET   B 2 350 ? 17.689  61.818  15.659  1.00 101.42 ? 350  MET   B O   1 
ATOM   5253  C  CB  . MET   B 2 350 ? 15.978  59.347  16.323  1.00 97.36  ? 350  MET   B CB  1 
ATOM   5254  C  CG  . MET   B 2 350 ? 16.494  59.751  17.671  1.00 99.08  ? 350  MET   B CG  1 
ATOM   5255  S  SD  . MET   B 2 350 ? 16.936  58.276  18.634  1.00 112.76 ? 350  MET   B SD  1 
ATOM   5256  C  CE  . MET   B 2 350 ? 18.628  57.912  18.150  1.00 98.41  ? 350  MET   B CE  1 
ATOM   5257  N  N   . GLU   B 2 351 ? 17.640  60.704  13.725  1.00 110.95 ? 351  GLU   B N   1 
ATOM   5258  C  CA  . GLU   B 2 351 ? 18.817  61.348  13.173  1.00 112.37 ? 351  GLU   B CA  1 
ATOM   5259  C  C   . GLU   B 2 351 ? 18.970  60.849  11.747  1.00 110.73 ? 351  GLU   B C   1 
ATOM   5260  O  O   . GLU   B 2 351 ? 18.808  59.657  11.494  1.00 111.03 ? 351  GLU   B O   1 
ATOM   5261  C  CB  . GLU   B 2 351 ? 20.073  61.041  13.997  1.00 113.57 ? 351  GLU   B CB  1 
ATOM   5262  C  CG  . GLU   B 2 351 ? 21.058  62.197  14.025  1.00 121.32 ? 351  GLU   B CG  1 
ATOM   5263  C  CD  . GLU   B 2 351 ? 22.401  61.817  14.623  1.00 126.83 ? 351  GLU   B CD  1 
ATOM   5264  O  OE1 . GLU   B 2 351 ? 22.515  60.758  15.294  1.00 122.07 ? 351  GLU   B OE1 1 
ATOM   5265  O  OE2 . GLU   B 2 351 ? 23.354  62.591  14.412  1.00 133.73 ? 351  GLU   B OE2 1 
ATOM   5266  N  N   . THR   B 2 352 ? 19.240  61.754  10.819  1.00 96.78  ? 352  THR   B N   1 
ATOM   5267  C  CA  . THR   B 2 352 ? 19.395  61.381  9.423   1.00 92.00  ? 352  THR   B CA  1 
ATOM   5268  C  C   . THR   B 2 352 ? 20.798  61.714  8.977   1.00 92.32  ? 352  THR   B C   1 
ATOM   5269  O  O   . THR   B 2 352 ? 21.336  62.766  9.344   1.00 95.68  ? 352  THR   B O   1 
ATOM   5270  C  CB  . THR   B 2 352 ? 18.445  62.135  8.544   1.00 88.03  ? 352  THR   B CB  1 
ATOM   5271  O  OG1 . THR   B 2 352 ? 18.431  63.484  9.014   1.00 92.17  ? 352  THR   B OG1 1 
ATOM   5272  C  CG2 . THR   B 2 352 ? 17.039  61.522  8.565   1.00 87.60  ? 352  THR   B CG2 1 
ATOM   5273  N  N   . PHE   B 2 353 ? 21.366  60.845  8.148   1.00 88.60  ? 353  PHE   B N   1 
ATOM   5274  C  CA  . PHE   B 2 353 ? 22.680  61.071  7.564   1.00 89.56  ? 353  PHE   B CA  1 
ATOM   5275  C  C   . PHE   B 2 353 ? 22.543  61.247  6.063   1.00 86.28  ? 353  PHE   B C   1 
ATOM   5276  O  O   . PHE   B 2 353 ? 21.702  60.603  5.434   1.00 86.70  ? 353  PHE   B O   1 
ATOM   5277  C  CB  . PHE   B 2 353 ? 23.610  59.909  7.881   1.00 86.35  ? 353  PHE   B CB  1 
ATOM   5278  C  CG  . PHE   B 2 353 ? 23.529  59.481  9.290   1.00 83.98  ? 353  PHE   B CG  1 
ATOM   5279  C  CD1 . PHE   B 2 353 ? 24.127  60.224  10.276  1.00 84.23  ? 353  PHE   B CD1 1 
ATOM   5280  C  CD2 . PHE   B 2 353 ? 22.824  58.352  9.637   1.00 89.42  ? 353  PHE   B CD2 1 
ATOM   5281  C  CE1 . PHE   B 2 353 ? 24.049  59.838  11.582  1.00 89.64  ? 353  PHE   B CE1 1 
ATOM   5282  C  CE2 . PHE   B 2 353 ? 22.736  57.952  10.951  1.00 90.69  ? 353  PHE   B CE2 1 
ATOM   5283  C  CZ  . PHE   B 2 353 ? 23.350  58.699  11.928  1.00 92.70  ? 353  PHE   B CZ  1 
ATOM   5284  N  N   . THR   B 2 354 ? 23.375  62.104  5.489   1.00 85.00  ? 354  THR   B N   1 
ATOM   5285  C  CA  . THR   B 2 354 ? 23.207  62.449  4.084   1.00 83.13  ? 354  THR   B CA  1 
ATOM   5286  C  C   . THR   B 2 354 ? 23.578  61.291  3.165   1.00 82.22  ? 354  THR   B C   1 
ATOM   5287  O  O   . THR   B 2 354 ? 24.575  60.595  3.378   1.00 82.14  ? 354  THR   B O   1 
ATOM   5288  C  CB  . THR   B 2 354 ? 24.049  63.669  3.746   1.00 80.65  ? 354  THR   B CB  1 
ATOM   5289  O  OG1 . THR   B 2 354 ? 23.789  64.684  4.723   1.00 90.61  ? 354  THR   B OG1 1 
ATOM   5290  C  CG2 . THR   B 2 354 ? 23.676  64.187  2.373   1.00 79.36  ? 354  THR   B CG2 1 
ATOM   5291  N  N   . ASN   B 2 355 ? 22.762  61.090  2.133   1.00 80.69  ? 355  ASN   B N   1 
ATOM   5292  C  CA  . ASN   B 2 355 ? 23.084  60.167  1.051   1.00 81.68  ? 355  ASN   B CA  1 
ATOM   5293  C  C   . ASN   B 2 355 ? 22.709  60.876  -0.252  1.00 82.15  ? 355  ASN   B C   1 
ATOM   5294  O  O   . ASN   B 2 355 ? 21.523  61.041  -0.555  1.00 84.30  ? 355  ASN   B O   1 
ATOM   5295  C  CB  . ASN   B 2 355 ? 22.354  58.841  1.240   1.00 80.69  ? 355  ASN   B CB  1 
ATOM   5296  C  CG  . ASN   B 2 355 ? 22.551  57.871  0.076   1.00 82.87  ? 355  ASN   B CG  1 
ATOM   5297  O  OD1 . ASN   B 2 355 ? 23.411  58.051  -0.798  1.00 80.15  ? 355  ASN   B OD1 1 
ATOM   5298  N  ND2 . ASN   B 2 355 ? 21.747  56.811  0.078   1.00 82.64  ? 355  ASN   B ND2 1 
ATOM   5299  N  N   . LEU   B 2 356 ? 23.730  61.334  -0.991  1.00 82.00  ? 356  LEU   B N   1 
ATOM   5300  C  CA  . LEU   B 2 356 ? 23.571  61.929  -2.315  1.00 78.04  ? 356  LEU   B CA  1 
ATOM   5301  C  C   . LEU   B 2 356 ? 23.317  60.900  -3.403  1.00 84.15  ? 356  LEU   B C   1 
ATOM   5302  O  O   . LEU   B 2 356 ? 23.064  61.297  -4.548  1.00 82.53  ? 356  LEU   B O   1 
ATOM   5303  C  CB  . LEU   B 2 356 ? 24.814  62.710  -2.708  1.00 78.20  ? 356  LEU   B CB  1 
ATOM   5304  C  CG  . LEU   B 2 356 ? 25.354  63.676  -1.679  1.00 78.74  ? 356  LEU   B CG  1 
ATOM   5305  C  CD1 . LEU   B 2 356 ? 26.533  64.350  -2.264  1.00 79.08  ? 356  LEU   B CD1 1 
ATOM   5306  C  CD2 . LEU   B 2 356 ? 24.312  64.687  -1.319  1.00 82.61  ? 356  LEU   B CD2 1 
ATOM   5307  N  N   . GLY   B 2 357 ? 23.405  59.602  -3.081  1.00 86.21  ? 357  GLY   B N   1 
ATOM   5308  C  CA  . GLY   B 2 357 ? 23.209  58.538  -4.044  1.00 84.09  ? 357  GLY   B CA  1 
ATOM   5309  C  C   . GLY   B 2 357 ? 21.796  57.981  -4.096  1.00 79.96  ? 357  GLY   B C   1 
ATOM   5310  O  O   . GLY   B 2 357 ? 21.042  58.040  -3.118  1.00 77.20  ? 357  GLY   B O   1 
ATOM   5311  N  N   . PRO   B 2 358 ? 21.405  57.451  -5.268  1.00 87.97  ? 358  PRO   B N   1 
ATOM   5312  C  CA  . PRO   B 2 358 ? 22.146  57.474  -6.539  1.00 89.30  ? 358  PRO   B CA  1 
ATOM   5313  C  C   . PRO   B 2 358 ? 22.097  58.839  -7.214  1.00 89.66  ? 358  PRO   B C   1 
ATOM   5314  O  O   . PRO   B 2 358 ? 21.160  59.608  -7.021  1.00 90.74  ? 358  PRO   B O   1 
ATOM   5315  C  CB  . PRO   B 2 358 ? 21.426  56.406  -7.374  1.00 89.50  ? 358  PRO   B CB  1 
ATOM   5316  C  CG  . PRO   B 2 358 ? 20.009  56.465  -6.880  1.00 90.66  ? 358  PRO   B CG  1 
ATOM   5317  C  CD  . PRO   B 2 358 ? 20.167  56.658  -5.386  1.00 88.90  ? 358  PRO   B CD  1 
ATOM   5318  N  N   . ILE   B 2 359 ? 23.104  59.173  -8.006  1.00 82.59  ? 359  ILE   B N   1 
ATOM   5319  C  CA  . ILE   B 2 359 ? 23.145  60.446  -8.706  1.00 80.18  ? 359  ILE   B CA  1 
ATOM   5320  C  C   . ILE   B 2 359 ? 22.856  60.156  -10.170 1.00 82.71  ? 359  ILE   B C   1 
ATOM   5321  O  O   . ILE   B 2 359 ? 23.750  59.741  -10.921 1.00 80.35  ? 359  ILE   B O   1 
ATOM   5322  C  CB  . ILE   B 2 359 ? 24.486  61.167  -8.535  1.00 77.03  ? 359  ILE   B CB  1 
ATOM   5323  C  CG1 . ILE   B 2 359 ? 24.681  61.570  -7.075  1.00 79.09  ? 359  ILE   B CG1 1 
ATOM   5324  C  CG2 . ILE   B 2 359 ? 24.491  62.381  -9.395  1.00 78.40  ? 359  ILE   B CG2 1 
ATOM   5325  C  CD1 . ILE   B 2 359 ? 25.790  62.557  -6.836  1.00 77.81  ? 359  ILE   B CD1 1 
ATOM   5326  N  N   . VAL   B 2 360 ? 21.609  60.396  -10.578 1.00 81.16  ? 360  VAL   B N   1 
ATOM   5327  C  CA  . VAL   B 2 360 ? 21.168  60.071  -11.929 1.00 77.22  ? 360  VAL   B CA  1 
ATOM   5328  C  C   . VAL   B 2 360 ? 21.394  61.216  -12.927 1.00 81.32  ? 360  VAL   B C   1 
ATOM   5329  O  O   . VAL   B 2 360 ? 21.613  60.946  -14.115 1.00 83.41  ? 360  VAL   B O   1 
ATOM   5330  C  CB  . VAL   B 2 360 ? 19.692  59.636  -11.897 1.00 75.78  ? 360  VAL   B CB  1 
ATOM   5331  C  CG1 . VAL   B 2 360 ? 19.568  58.274  -11.285 1.00 78.94  ? 360  VAL   B CG1 1 
ATOM   5332  C  CG2 . VAL   B 2 360 ? 18.865  60.608  -11.106 1.00 75.97  ? 360  VAL   B CG2 1 
ATOM   5333  N  N   . ASP   B 2 361 ? 21.317  62.482  -12.490 1.00 78.69  ? 361  ASP   B N   1 
ATOM   5334  C  CA  . ASP   B 2 361 ? 21.696  63.624  -13.324 1.00 77.56  ? 361  ASP   B CA  1 
ATOM   5335  C  C   . ASP   B 2 361 ? 22.183  64.739  -12.413 1.00 82.62  ? 361  ASP   B C   1 
ATOM   5336  O  O   . ASP   B 2 361 ? 21.887  64.752  -11.214 1.00 83.00  ? 361  ASP   B O   1 
ATOM   5337  C  CB  . ASP   B 2 361 ? 20.539  64.137  -14.205 1.00 79.37  ? 361  ASP   B CB  1 
ATOM   5338  C  CG  . ASP   B 2 361 ? 21.019  65.055  -15.361 1.00 81.87  ? 361  ASP   B CG  1 
ATOM   5339  O  OD1 . ASP   B 2 361 ? 22.254  65.160  -15.541 1.00 85.09  ? 361  ASP   B OD1 1 
ATOM   5340  O  OD2 . ASP   B 2 361 ? 20.176  65.668  -16.091 1.00 77.40  ? 361  ASP   B OD2 1 
ATOM   5341  N  N   . MET   B 2 362 ? 22.949  65.671  -12.986 1.00 86.90  ? 362  MET   B N   1 
ATOM   5342  C  CA  . MET   B 2 362 ? 23.418  66.836  -12.242 1.00 86.94  ? 362  MET   B CA  1 
ATOM   5343  C  C   . MET   B 2 362 ? 23.631  68.004  -13.207 1.00 85.77  ? 362  MET   B C   1 
ATOM   5344  O  O   . MET   B 2 362 ? 23.538  67.856  -14.427 1.00 86.63  ? 362  MET   B O   1 
ATOM   5345  C  CB  . MET   B 2 362 ? 24.692  66.510  -11.429 1.00 89.10  ? 362  MET   B CB  1 
ATOM   5346  C  CG  . MET   B 2 362 ? 25.980  66.329  -12.258 1.00 91.82  ? 362  MET   B CG  1 
ATOM   5347  S  SD  . MET   B 2 362 ? 27.507  65.843  -11.386 1.00 87.88  ? 362  MET   B SD  1 
ATOM   5348  C  CE  . MET   B 2 362 ? 26.819  64.969  -10.009 1.00 86.49  ? 362  MET   B CE  1 
ATOM   5349  N  N   . CYS   B 2 363 ? 23.884  69.183  -12.635 1.00 87.40  ? 363  CYS   B N   1 
ATOM   5350  C  CA  . CYS   B 2 363 ? 24.163  70.408  -13.376 1.00 88.51  ? 363  CYS   B CA  1 
ATOM   5351  C  C   . CYS   B 2 363 ? 24.919  71.348  -12.447 1.00 89.44  ? 363  CYS   B C   1 
ATOM   5352  O  O   . CYS   B 2 363 ? 24.792  71.231  -11.226 1.00 91.71  ? 363  CYS   B O   1 
ATOM   5353  C  CB  . CYS   B 2 363 ? 22.868  71.049  -13.863 1.00 91.99  ? 363  CYS   B CB  1 
ATOM   5354  S  SG  . CYS   B 2 363 ? 21.836  71.732  -12.522 1.00 98.89  ? 363  CYS   B SG  1 
ATOM   5355  N  N   . VAL   B 2 364 ? 25.732  72.250  -13.019 1.00 83.59  ? 364  VAL   B N   1 
ATOM   5356  C  CA  . VAL   B 2 364 ? 26.571  73.177  -12.246 1.00 91.46  ? 364  VAL   B CA  1 
ATOM   5357  C  C   . VAL   B 2 364 ? 26.048  74.587  -12.452 1.00 96.09  ? 364  VAL   B C   1 
ATOM   5358  O  O   . VAL   B 2 364 ? 25.871  75.016  -13.593 1.00 101.99 ? 364  VAL   B O   1 
ATOM   5359  C  CB  . VAL   B 2 364 ? 28.058  73.125  -12.652 1.00 94.35  ? 364  VAL   B CB  1 
ATOM   5360  C  CG1 . VAL   B 2 364 ? 28.887  74.044  -11.744 1.00 97.86  ? 364  VAL   B CG1 1 
ATOM   5361  C  CG2 . VAL   B 2 364 ? 28.613  71.702  -12.632 1.00 97.56  ? 364  VAL   B CG2 1 
ATOM   5362  N  N   . VAL   B 2 365 ? 25.812  75.314  -11.364 1.00 99.11  ? 365  VAL   B N   1 
ATOM   5363  C  CA  . VAL   B 2 365 ? 25.105  76.591  -11.461 1.00 103.35 ? 365  VAL   B CA  1 
ATOM   5364  C  C   . VAL   B 2 365 ? 25.682  77.546  -10.427 1.00 114.41 ? 365  VAL   B C   1 
ATOM   5365  O  O   . VAL   B 2 365 ? 25.835  77.190  -9.258  1.00 117.34 ? 365  VAL   B O   1 
ATOM   5366  C  CB  . VAL   B 2 365 ? 23.579  76.428  -11.254 1.00 102.11 ? 365  VAL   B CB  1 
ATOM   5367  C  CG1 . VAL   B 2 365 ? 22.891  77.746  -11.392 1.00 107.08 ? 365  VAL   B CG1 1 
ATOM   5368  C  CG2 . VAL   B 2 365 ? 22.958  75.421  -12.242 1.00 100.07 ? 365  VAL   B CG2 1 
ATOM   5369  N  N   . ASP   B 2 366 ? 25.999  78.771  -10.851 1.00 134.44 ? 366  ASP   B N   1 
ATOM   5370  C  CA  . ASP   B 2 366 ? 26.473  79.811  -9.936  1.00 136.39 ? 366  ASP   B CA  1 
ATOM   5371  C  C   . ASP   B 2 366 ? 25.295  80.700  -9.541  1.00 137.45 ? 366  ASP   B C   1 
ATOM   5372  O  O   . ASP   B 2 366 ? 25.075  81.775  -10.095 1.00 139.47 ? 366  ASP   B O   1 
ATOM   5373  C  CB  . ASP   B 2 366 ? 27.596  80.614  -10.578 1.00 140.21 ? 366  ASP   B CB  1 
ATOM   5374  C  CG  . ASP   B 2 366 ? 28.169  81.654  -9.639  1.00 146.23 ? 366  ASP   B CG  1 
ATOM   5375  O  OD1 . ASP   B 2 366 ? 28.264  81.362  -8.422  1.00 146.32 ? 366  ASP   B OD1 1 
ATOM   5376  O  OD2 . ASP   B 2 366 ? 28.532  82.754  -10.116 1.00 149.08 ? 366  ASP   B OD2 1 
ATOM   5377  N  N   . LEU   B 2 367 ? 24.537  80.237  -8.542  1.00 124.94 ? 367  LEU   B N   1 
ATOM   5378  C  CA  . LEU   B 2 367 ? 23.286  80.902  -8.177  1.00 123.61 ? 367  LEU   B CA  1 
ATOM   5379  C  C   . LEU   B 2 367 ? 23.521  82.197  -7.407  1.00 126.18 ? 367  LEU   B C   1 
ATOM   5380  O  O   . LEU   B 2 367 ? 22.790  83.178  -7.597  1.00 128.30 ? 367  LEU   B O   1 
ATOM   5381  C  CB  . LEU   B 2 367 ? 22.415  79.963  -7.348  1.00 123.81 ? 367  LEU   B CB  1 
ATOM   5382  C  CG  . LEU   B 2 367 ? 21.743  78.795  -8.054  1.00 117.59 ? 367  LEU   B CG  1 
ATOM   5383  C  CD1 . LEU   B 2 367 ? 21.042  77.945  -7.025  1.00 117.06 ? 367  LEU   B CD1 1 
ATOM   5384  C  CD2 . LEU   B 2 367 ? 20.755  79.305  -9.076  1.00 114.73 ? 367  LEU   B CD2 1 
ATOM   5385  N  N   . GLU   B 2 368 ? 24.494  82.210  -6.499  1.00 123.30 ? 368  GLU   B N   1 
ATOM   5386  C  CA  . GLU   B 2 368 ? 24.767  83.412  -5.726  1.00 121.21 ? 368  GLU   B CA  1 
ATOM   5387  C  C   . GLU   B 2 368 ? 25.604  84.403  -6.512  1.00 127.10 ? 368  GLU   B C   1 
ATOM   5388  O  O   . GLU   B 2 368 ? 26.077  85.392  -5.937  1.00 126.16 ? 368  GLU   B O   1 
ATOM   5389  C  CB  . GLU   B 2 368 ? 25.447  83.047  -4.405  1.00 124.65 ? 368  GLU   B CB  1 
ATOM   5390  C  CG  . GLU   B 2 368 ? 24.665  82.030  -3.550  1.00 127.31 ? 368  GLU   B CG  1 
ATOM   5391  C  CD  . GLU   B 2 368 ? 25.441  81.530  -2.311  1.00 130.50 ? 368  GLU   B CD  1 
ATOM   5392  O  OE1 . GLU   B 2 368 ? 25.828  82.364  -1.460  1.00 133.43 ? 368  GLU   B OE1 1 
ATOM   5393  O  OE2 . GLU   B 2 368 ? 25.665  80.301  -2.186  1.00 123.88 ? 368  GLU   B OE2 1 
ATOM   5394  N  N   . ARG   B 2 369 ? 25.765  84.147  -7.814  1.00 129.36 ? 369  ARG   B N   1 
ATOM   5395  C  CA  . ARG   B 2 369 ? 26.468  85.036  -8.729  1.00 127.61 ? 369  ARG   B CA  1 
ATOM   5396  C  C   . ARG   B 2 369 ? 27.784  85.502  -8.131  1.00 131.76 ? 369  ARG   B C   1 
ATOM   5397  O  O   . ARG   B 2 369 ? 28.147  86.679  -8.177  1.00 132.01 ? 369  ARG   B O   1 
ATOM   5398  C  CB  . ARG   B 2 369 ? 25.578  86.198  -9.142  1.00 120.33 ? 369  ARG   B CB  1 
ATOM   5399  C  CG  . ARG   B 2 369 ? 24.680  85.849  -10.302 1.00 127.12 ? 369  ARG   B CG  1 
ATOM   5400  C  CD  . ARG   B 2 369 ? 25.461  85.670  -11.642 1.00 138.79 ? 369  ARG   B CD  1 
ATOM   5401  N  NE  . ARG   B 2 369 ? 26.441  84.582  -11.629 1.00 140.09 ? 369  ARG   B NE  1 
ATOM   5402  C  CZ  . ARG   B 2 369 ? 27.346  84.367  -12.575 1.00 139.24 ? 369  ARG   B CZ  1 
ATOM   5403  N  NH1 . ARG   B 2 369 ? 27.379  85.101  -13.676 1.00 141.90 ? 369  ARG   B NH1 1 
ATOM   5404  N  NH2 . ARG   B 2 369 ? 28.247  83.398  -12.406 1.00 134.79 ? 369  ARG   B NH2 1 
ATOM   5405  N  N   . GLN   B 2 370 ? 28.504  84.546  -7.554  1.00 131.86 ? 370  GLN   B N   1 
ATOM   5406  C  CA  . GLN   B 2 370 ? 29.750  84.795  -6.855  1.00 132.29 ? 370  GLN   B CA  1 
ATOM   5407  C  C   . GLN   B 2 370 ? 30.936  84.153  -7.559  1.00 132.93 ? 370  GLN   B C   1 
ATOM   5408  O  O   . GLN   B 2 370 ? 31.974  83.946  -6.927  1.00 134.69 ? 370  GLN   B O   1 
ATOM   5409  C  CB  . GLN   B 2 370 ? 29.660  84.281  -5.415  1.00 135.16 ? 370  GLN   B CB  1 
ATOM   5410  C  CG  . GLN   B 2 370 ? 29.353  82.760  -5.288  1.00 137.00 ? 370  GLN   B CG  1 
ATOM   5411  C  CD  . GLN   B 2 370 ? 29.504  82.208  -3.853  1.00 141.48 ? 370  GLN   B CD  1 
ATOM   5412  O  OE1 . GLN   B 2 370 ? 29.509  82.958  -2.873  1.00 142.49 ? 370  GLN   B OE1 1 
ATOM   5413  N  NE2 . GLN   B 2 370 ? 29.628  80.886  -3.737  1.00 138.42 ? 370  GLN   B NE2 1 
ATOM   5414  N  N   . GLY   B 2 371 ? 30.807  83.834  -8.844  1.00 132.60 ? 371  GLY   B N   1 
ATOM   5415  C  CA  . GLY   B 2 371 ? 31.932  83.242  -9.562  1.00 133.02 ? 371  GLY   B CA  1 
ATOM   5416  C  C   . GLY   B 2 371 ? 32.498  82.019  -8.884  1.00 132.39 ? 371  GLY   B C   1 
ATOM   5417  O  O   . GLY   B 2 371 ? 33.725  81.840  -8.819  1.00 132.41 ? 371  GLY   B O   1 
ATOM   5418  N  N   . GLN   B 2 372 ? 31.625  81.172  -8.349  1.00 127.98 ? 372  GLN   B N   1 
ATOM   5419  C  CA  . GLN   B 2 372 ? 32.047  79.947  -7.666  1.00 126.72 ? 372  GLN   B CA  1 
ATOM   5420  C  C   . GLN   B 2 372 ? 31.423  78.731  -8.338  1.00 123.60 ? 372  GLN   B C   1 
ATOM   5421  O  O   . GLN   B 2 372 ? 32.132  77.984  -9.015  1.00 123.86 ? 372  GLN   B O   1 
ATOM   5422  C  CB  . GLN   B 2 372 ? 31.664  80.024  -6.190  1.00 127.92 ? 372  GLN   B CB  1 
ATOM   5423  C  CG  . GLN   B 2 372 ? 32.236  78.925  -5.306  1.00 125.64 ? 372  GLN   B CG  1 
ATOM   5424  C  CD  . GLN   B 2 372 ? 33.741  79.040  -5.094  1.00 128.92 ? 372  GLN   B CD  1 
ATOM   5425  O  OE1 . GLN   B 2 372 ? 34.435  79.782  -5.796  1.00 131.70 ? 372  GLN   B OE1 1 
ATOM   5426  N  NE2 . GLN   B 2 372 ? 34.253  78.299  -4.117  1.00 131.00 ? 372  GLN   B NE2 1 
ATOM   5427  N  N   . GLY   B 2 373 ? 30.127  78.507  -8.178  1.00 121.81 ? 373  GLY   B N   1 
ATOM   5428  C  CA  . GLY   B 2 373 ? 29.507  77.360  -8.801  1.00 115.14 ? 373  GLY   B CA  1 
ATOM   5429  C  C   . GLY   B 2 373 ? 29.082  76.308  -7.797  1.00 110.94 ? 373  GLY   B C   1 
ATOM   5430  O  O   . GLY   B 2 373 ? 29.927  75.693  -7.140  1.00 110.40 ? 373  GLY   B O   1 
ATOM   5431  N  N   . GLN   B 2 374 ? 27.773  76.142  -7.611  1.00 105.95 ? 374  GLN   B N   1 
ATOM   5432  C  CA  . GLN   B 2 374 ? 27.210  75.070  -6.808  1.00 97.80  ? 374  GLN   B CA  1 
ATOM   5433  C  C   . GLN   B 2 374 ? 26.886  73.900  -7.741  1.00 101.22 ? 374  GLN   B C   1 
ATOM   5434  O  O   . GLN   B 2 374 ? 27.238  73.913  -8.932  1.00 100.22 ? 374  GLN   B O   1 
ATOM   5435  C  CB  . GLN   B 2 374 ? 25.990  75.574  -6.032  1.00 95.47  ? 374  GLN   B CB  1 
ATOM   5436  C  CG  . GLN   B 2 374 ? 26.156  77.008  -5.549  1.00 109.73 ? 374  GLN   B CG  1 
ATOM   5437  C  CD  . GLN   B 2 374 ? 25.075  77.465  -4.573  1.00 114.77 ? 374  GLN   B CD  1 
ATOM   5438  O  OE1 . GLN   B 2 374 ? 25.127  77.163  -3.367  1.00 112.20 ? 374  GLN   B OE1 1 
ATOM   5439  N  NE2 . GLN   B 2 374 ? 24.098  78.220  -5.087  1.00 113.53 ? 374  GLN   B NE2 1 
ATOM   5440  N  N   . LEU   B 2 375 ? 26.211  72.876  -7.211  1.00 97.93  ? 375  LEU   B N   1 
ATOM   5441  C  CA  . LEU   B 2 375 ? 25.914  71.667  -7.976  1.00 92.15  ? 375  LEU   B CA  1 
ATOM   5442  C  C   . LEU   B 2 375 ? 24.569  71.142  -7.505  1.00 90.24  ? 375  LEU   B C   1 
ATOM   5443  O  O   . LEU   B 2 375 ? 24.426  70.843  -6.318  1.00 91.23  ? 375  LEU   B O   1 
ATOM   5444  C  CB  . LEU   B 2 375 ? 27.017  70.618  -7.767  1.00 93.41  ? 375  LEU   B CB  1 
ATOM   5445  C  CG  . LEU   B 2 375 ? 27.018  69.305  -8.568  1.00 95.84  ? 375  LEU   B CG  1 
ATOM   5446  C  CD1 . LEU   B 2 375 ? 27.187  69.559  -10.059 1.00 96.40  ? 375  LEU   B CD1 1 
ATOM   5447  C  CD2 . LEU   B 2 375 ? 28.090  68.323  -8.068  1.00 91.56  ? 375  LEU   B CD2 1 
ATOM   5448  N  N   . VAL   B 2 376 ? 23.577  71.055  -8.401  1.00 85.62  ? 376  VAL   B N   1 
ATOM   5449  C  CA  . VAL   B 2 376 ? 22.309  70.405  -8.068  1.00 85.66  ? 376  VAL   B CA  1 
ATOM   5450  C  C   . VAL   B 2 376 ? 22.304  69.022  -8.687  1.00 87.92  ? 376  VAL   B C   1 
ATOM   5451  O  O   . VAL   B 2 376 ? 22.717  68.854  -9.841  1.00 89.74  ? 376  VAL   B O   1 
ATOM   5452  C  CB  . VAL   B 2 376 ? 21.076  71.190  -8.546  1.00 82.98  ? 376  VAL   B CB  1 
ATOM   5453  C  CG1 . VAL   B 2 376 ? 19.797  70.581  -7.927  1.00 79.07  ? 376  VAL   B CG1 1 
ATOM   5454  C  CG2 . VAL   B 2 376 ? 21.222  72.659  -8.222  1.00 84.58  ? 376  VAL   B CG2 1 
ATOM   5455  N  N   . THR   B 2 377 ? 21.826  68.027  -7.927  1.00 88.61  ? 377  THR   B N   1 
ATOM   5456  C  CA  . THR   B 2 377 ? 21.809  66.633  -8.367  1.00 86.30  ? 377  THR   B CA  1 
ATOM   5457  C  C   . THR   B 2 377 ? 20.394  66.075  -8.253  1.00 83.66  ? 377  THR   B C   1 
ATOM   5458  O  O   . THR   B 2 377 ? 19.733  66.246  -7.219  1.00 82.12  ? 377  THR   B O   1 
ATOM   5459  C  CB  . THR   B 2 377 ? 22.799  65.740  -7.552  1.00 83.10  ? 377  THR   B CB  1 
ATOM   5460  O  OG1 . THR   B 2 377 ? 22.483  65.767  -6.153  1.00 78.95  ? 377  THR   B OG1 1 
ATOM   5461  C  CG2 . THR   B 2 377 ? 24.251  66.172  -7.742  1.00 81.94  ? 377  THR   B CG2 1 
ATOM   5462  N  N   . CYS   B 2 378 ? 19.923  65.426  -9.323  1.00 84.50  ? 378  CYS   B N   1 
ATOM   5463  C  CA  . CYS   B 2 378 ? 18.850  64.450  -9.163  1.00 83.90  ? 378  CYS   B CA  1 
ATOM   5464  C  C   . CYS   B 2 378 ? 19.412  63.296  -8.359  1.00 83.09  ? 378  CYS   B C   1 
ATOM   5465  O  O   . CYS   B 2 378 ? 20.281  62.560  -8.841  1.00 82.75  ? 378  CYS   B O   1 
ATOM   5466  C  CB  . CYS   B 2 378 ? 18.323  63.933  -10.492 1.00 79.42  ? 378  CYS   B CB  1 
ATOM   5467  S  SG  . CYS   B 2 378 ? 17.893  65.229  -11.607 1.00 84.13  ? 378  CYS   B SG  1 
ATOM   5468  N  N   . SER   B 2 379 ? 18.937  63.142  -7.139  1.00 81.94  ? 379  SER   B N   1 
ATOM   5469  C  CA  . SER   B 2 379 ? 19.455  62.140  -6.241  1.00 79.30  ? 379  SER   B CA  1 
ATOM   5470  C  C   . SER   B 2 379 ? 18.306  61.288  -5.740  1.00 79.71  ? 379  SER   B C   1 
ATOM   5471  O  O   . SER   B 2 379 ? 17.164  61.749  -5.639  1.00 81.21  ? 379  SER   B O   1 
ATOM   5472  C  CB  . SER   B 2 379 ? 20.188  62.791  -5.087  1.00 80.50  ? 379  SER   B CB  1 
ATOM   5473  O  OG  . SER   B 2 379 ? 21.334  63.472  -5.567  1.00 83.30  ? 379  SER   B OG  1 
ATOM   5474  N  N   . GLY   B 2 380 ? 18.617  60.028  -5.477  1.00 79.25  ? 380  GLY   B N   1 
ATOM   5475  C  CA  . GLY   B 2 380 ? 17.671  59.140  -4.843  1.00 77.95  ? 380  GLY   B CA  1 
ATOM   5476  C  C   . GLY   B 2 380 ? 16.704  58.479  -5.802  1.00 80.02  ? 380  GLY   B C   1 
ATOM   5477  O  O   . GLY   B 2 380 ? 16.770  58.610  -7.026  1.00 86.93  ? 380  GLY   B O   1 
ATOM   5478  N  N   . ALA   B 2 381 ? 15.778  57.734  -5.205  1.00 75.64  ? 381  ALA   B N   1 
ATOM   5479  C  CA  . ALA   B 2 381 ? 14.734  57.056  -5.954  1.00 75.38  ? 381  ALA   B CA  1 
ATOM   5480  C  C   . ALA   B 2 381 ? 13.522  56.915  -5.063  1.00 75.46  ? 381  ALA   B C   1 
ATOM   5481  O  O   . ALA   B 2 381 ? 13.626  56.921  -3.837  1.00 76.11  ? 381  ALA   B O   1 
ATOM   5482  C  CB  . ALA   B 2 381 ? 15.200  55.690  -6.441  1.00 75.04  ? 381  ALA   B CB  1 
ATOM   5483  N  N   . PHE   B 2 382 ? 12.356  56.810  -5.701  1.00 78.93  ? 382  PHE   B N   1 
ATOM   5484  C  CA  . PHE   B 2 382 ? 11.065  56.612  -5.046  1.00 77.79  ? 382  PHE   B CA  1 
ATOM   5485  C  C   . PHE   B 2 382 ? 10.884  57.621  -3.915  1.00 75.99  ? 382  PHE   B C   1 
ATOM   5486  O  O   . PHE   B 2 382 ? 11.217  58.801  -4.095  1.00 76.02  ? 382  PHE   B O   1 
ATOM   5487  C  CB  . PHE   B 2 382 ? 10.963  55.147  -4.600  1.00 76.99  ? 382  PHE   B CB  1 
ATOM   5488  C  CG  . PHE   B 2 382 ? 11.467  54.174  -5.658  1.00 79.53  ? 382  PHE   B CG  1 
ATOM   5489  C  CD1 . PHE   B 2 382 ? 11.011  54.247  -6.965  1.00 78.23  ? 382  PHE   B CD1 1 
ATOM   5490  C  CD2 . PHE   B 2 382 ? 12.428  53.217  -5.355  1.00 83.07  ? 382  PHE   B CD2 1 
ATOM   5491  C  CE1 . PHE   B 2 382 ? 11.474  53.363  -7.942  1.00 80.94  ? 382  PHE   B CE1 1 
ATOM   5492  C  CE2 . PHE   B 2 382 ? 12.908  52.328  -6.340  1.00 80.69  ? 382  PHE   B CE2 1 
ATOM   5493  C  CZ  . PHE   B 2 382 ? 12.429  52.405  -7.633  1.00 77.67  ? 382  PHE   B CZ  1 
ATOM   5494  N  N   . LYS   B 2 383 ? 10.368  57.180  -2.763  1.00 75.94  ? 383  LYS   B N   1 
ATOM   5495  C  CA  . LYS   B 2 383 ? 10.136  58.093  -1.642  1.00 76.32  ? 383  LYS   B CA  1 
ATOM   5496  C  C   . LYS   B 2 383 ? 11.359  58.968  -1.356  1.00 80.12  ? 383  LYS   B C   1 
ATOM   5497  O  O   . LYS   B 2 383 ? 11.219  60.122  -0.936  1.00 81.64  ? 383  LYS   B O   1 
ATOM   5498  C  CB  . LYS   B 2 383 ? 9.730   57.276  -0.414  1.00 79.74  ? 383  LYS   B CB  1 
ATOM   5499  C  CG  . LYS   B 2 383 ? 10.894  56.706  0.397   1.00 85.17  ? 383  LYS   B CG  1 
ATOM   5500  C  CD  . LYS   B 2 383 ? 10.451  55.681  1.449   1.00 88.17  ? 383  LYS   B CD  1 
ATOM   5501  C  CE  . LYS   B 2 383 ? 9.407   56.223  2.386   1.00 93.88  ? 383  LYS   B CE  1 
ATOM   5502  N  NZ  . LYS   B 2 383 ? 9.484   55.555  3.699   1.00 97.69  ? 383  LYS   B NZ  1 
ATOM   5503  N  N   . GLU   B 2 384 ? 12.560  58.477  -1.652  1.00 77.86  ? 384  GLU   B N   1 
ATOM   5504  C  CA  . GLU   B 2 384 ? 13.780  59.187  -1.305  1.00 77.28  ? 384  GLU   B CA  1 
ATOM   5505  C  C   . GLU   B 2 384 ? 14.265  60.146  -2.395  1.00 77.32  ? 384  GLU   B C   1 
ATOM   5506  O  O   . GLU   B 2 384 ? 15.379  60.666  -2.279  1.00 78.97  ? 384  GLU   B O   1 
ATOM   5507  C  CB  . GLU   B 2 384 ? 14.897  58.196  -0.970  1.00 78.34  ? 384  GLU   B CB  1 
ATOM   5508  C  CG  . GLU   B 2 384 ? 14.462  56.948  -0.228  1.00 79.11  ? 384  GLU   B CG  1 
ATOM   5509  C  CD  . GLU   B 2 384 ? 14.212  57.174  1.241   1.00 84.80  ? 384  GLU   B CD  1 
ATOM   5510  O  OE1 . GLU   B 2 384 ? 14.543  58.269  1.754   1.00 90.39  ? 384  GLU   B OE1 1 
ATOM   5511  O  OE2 . GLU   B 2 384 ? 13.677  56.250  1.889   1.00 86.38  ? 384  GLU   B OE2 1 
ATOM   5512  N  N   . GLY   B 2 385 ? 13.470  60.361  -3.446  1.00 81.83  ? 385  GLY   B N   1 
ATOM   5513  C  CA  . GLY   B 2 385 ? 13.855  61.328  -4.466  1.00 83.79  ? 385  GLY   B CA  1 
ATOM   5514  C  C   . GLY   B 2 385 ? 14.134  62.684  -3.849  1.00 86.60  ? 385  GLY   B C   1 
ATOM   5515  O  O   . GLY   B 2 385 ? 13.525  63.062  -2.849  1.00 87.60  ? 385  GLY   B O   1 
ATOM   5516  N  N   . SER   B 2 386 ? 15.073  63.420  -4.450  1.00 81.26  ? 386  SER   B N   1 
ATOM   5517  C  CA  . SER   B 2 386 ? 15.547  64.647  -3.816  1.00 80.94  ? 386  SER   B CA  1 
ATOM   5518  C  C   . SER   B 2 386 ? 16.387  65.432  -4.803  1.00 81.53  ? 386  SER   B C   1 
ATOM   5519  O  O   . SER   B 2 386 ? 16.899  64.896  -5.790  1.00 84.33  ? 386  SER   B O   1 
ATOM   5520  C  CB  . SER   B 2 386 ? 16.376  64.368  -2.541  1.00 82.60  ? 386  SER   B CB  1 
ATOM   5521  O  OG  . SER   B 2 386 ? 17.480  63.494  -2.778  1.00 82.37  ? 386  SER   B OG  1 
ATOM   5522  N  N   . LEU   B 2 387 ? 16.515  66.715  -4.517  1.00 80.23  ? 387  LEU   B N   1 
ATOM   5523  C  CA  . LEU   B 2 387 ? 17.508  67.562  -5.147  1.00 81.33  ? 387  LEU   B CA  1 
ATOM   5524  C  C   . LEU   B 2 387 ? 18.485  67.988  -4.069  1.00 82.63  ? 387  LEU   B C   1 
ATOM   5525  O  O   . LEU   B 2 387 ? 18.088  68.647  -3.102  1.00 83.55  ? 387  LEU   B O   1 
ATOM   5526  C  CB  . LEU   B 2 387 ? 16.848  68.773  -5.799  1.00 78.41  ? 387  LEU   B CB  1 
ATOM   5527  C  CG  . LEU   B 2 387 ? 16.040  68.364  -7.017  1.00 79.46  ? 387  LEU   B CG  1 
ATOM   5528  C  CD1 . LEU   B 2 387 ? 15.483  69.573  -7.679  1.00 78.35  ? 387  LEU   B CD1 1 
ATOM   5529  C  CD2 . LEU   B 2 387 ? 16.914  67.598  -7.981  1.00 84.91  ? 387  LEU   B CD2 1 
ATOM   5530  N  N   . ARG   B 2 388 ? 19.745  67.596  -4.214  1.00 84.09  ? 388  ARG   B N   1 
ATOM   5531  C  CA  . ARG   B 2 388 ? 20.799  68.090  -3.337  1.00 85.17  ? 388  ARG   B CA  1 
ATOM   5532  C  C   . ARG   B 2 388 ? 21.553  69.218  -4.038  1.00 87.65  ? 388  ARG   B C   1 
ATOM   5533  O  O   . ARG   B 2 388 ? 21.890  69.106  -5.221  1.00 86.73  ? 388  ARG   B O   1 
ATOM   5534  C  CB  . ARG   B 2 388 ? 21.762  66.965  -2.953  1.00 81.01  ? 388  ARG   B CB  1 
ATOM   5535  C  CG  . ARG   B 2 388 ? 21.053  65.707  -2.586  1.00 81.81  ? 388  ARG   B CG  1 
ATOM   5536  C  CD  . ARG   B 2 388 ? 20.275  65.848  -1.298  1.00 82.31  ? 388  ARG   B CD  1 
ATOM   5537  N  NE  . ARG   B 2 388 ? 19.536  64.629  -0.979  1.00 86.28  ? 388  ARG   B NE  1 
ATOM   5538  C  CZ  . ARG   B 2 388 ? 19.779  63.821  0.048   1.00 79.07  ? 388  ARG   B CZ  1 
ATOM   5539  N  NH1 . ARG   B 2 388 ? 20.731  64.075  0.925   1.00 79.30  ? 388  ARG   B NH1 1 
ATOM   5540  N  NH2 . ARG   B 2 388 ? 19.032  62.735  0.199   1.00 82.42  ? 388  ARG   B NH2 1 
ATOM   5541  N  N   . ILE   B 2 389 ? 21.808  70.310  -3.305  1.00 90.10  ? 389  ILE   B N   1 
ATOM   5542  C  CA  . ILE   B 2 389 ? 22.558  71.455  -3.820  1.00 85.90  ? 389  ILE   B CA  1 
ATOM   5543  C  C   . ILE   B 2 389 ? 23.867  71.550  -3.057  1.00 86.38  ? 389  ILE   B C   1 
ATOM   5544  O  O   . ILE   B 2 389 ? 23.871  71.786  -1.841  1.00 88.39  ? 389  ILE   B O   1 
ATOM   5545  C  CB  . ILE   B 2 389 ? 21.773  72.769  -3.706  1.00 82.75  ? 389  ILE   B CB  1 
ATOM   5546  C  CG1 . ILE   B 2 389 ? 20.436  72.677  -4.430  1.00 80.19  ? 389  ILE   B CG1 1 
ATOM   5547  C  CG2 . ILE   B 2 389 ? 22.609  73.924  -4.228  1.00 89.01  ? 389  ILE   B CG2 1 
ATOM   5548  C  CD1 . ILE   B 2 389 ? 19.305  72.284  -3.529  1.00 80.03  ? 389  ILE   B CD1 1 
ATOM   5549  N  N   . ILE   B 2 390 ? 24.973  71.409  -3.783  1.00 87.07  ? 390  ILE   B N   1 
ATOM   5550  C  CA  . ILE   B 2 390 ? 26.296  71.213  -3.203  1.00 93.14  ? 390  ILE   B CA  1 
ATOM   5551  C  C   . ILE   B 2 390 ? 27.173  72.431  -3.512  1.00 98.60  ? 390  ILE   B C   1 
ATOM   5552  O  O   . ILE   B 2 390 ? 27.510  72.680  -4.680  1.00 98.26  ? 390  ILE   B O   1 
ATOM   5553  C  CB  . ILE   B 2 390 ? 26.926  69.912  -3.724  1.00 88.37  ? 390  ILE   B CB  1 
ATOM   5554  C  CG1 . ILE   B 2 390 ? 25.950  68.769  -3.480  1.00 87.54  ? 390  ILE   B CG1 1 
ATOM   5555  C  CG2 . ILE   B 2 390 ? 28.247  69.622  -3.039  1.00 87.49  ? 390  ILE   B CG2 1 
ATOM   5556  C  CD1 . ILE   B 2 390 ? 26.255  67.534  -4.245  1.00 89.44  ? 390  ILE   B CD1 1 
ATOM   5557  N  N   . ARG   B 2 391 ? 27.550  73.176  -2.463  1.00 98.47  ? 391  ARG   B N   1 
ATOM   5558  C  CA  . ARG   B 2 391 ? 28.447  74.323  -2.552  1.00 99.88  ? 391  ARG   B CA  1 
ATOM   5559  C  C   . ARG   B 2 391 ? 29.636  74.112  -1.619  1.00 103.21 ? 391  ARG   B C   1 
ATOM   5560  O  O   . ARG   B 2 391 ? 29.565  73.334  -0.668  1.00 104.78 ? 391  ARG   B O   1 
ATOM   5561  C  CB  . ARG   B 2 391 ? 27.730  75.627  -2.180  1.00 104.69 ? 391  ARG   B CB  1 
ATOM   5562  C  CG  . ARG   B 2 391 ? 27.213  75.645  -0.741  1.00 109.72 ? 391  ARG   B CG  1 
ATOM   5563  C  CD  . ARG   B 2 391 ? 26.519  76.946  -0.429  1.00 115.44 ? 391  ARG   B CD  1 
ATOM   5564  N  NE  . ARG   B 2 391 ? 27.455  78.066  -0.475  1.00 122.97 ? 391  ARG   B NE  1 
ATOM   5565  C  CZ  . ARG   B 2 391 ? 28.227  78.449  0.534   1.00 124.87 ? 391  ARG   B CZ  1 
ATOM   5566  N  NH1 . ARG   B 2 391 ? 28.193  77.826  1.702   1.00 131.18 ? 391  ARG   B NH1 1 
ATOM   5567  N  NH2 . ARG   B 2 391 ? 29.037  79.494  0.375   1.00 128.85 ? 391  ARG   B NH2 1 
ATOM   5568  N  N   . ASN   B 2 392 ? 30.736  74.816  -1.886  1.00 107.89 ? 392  ASN   B N   1 
ATOM   5569  C  CA  . ASN   B 2 392 ? 31.944  74.650  -1.073  1.00 107.19 ? 392  ASN   B CA  1 
ATOM   5570  C  C   . ASN   B 2 392 ? 31.850  75.443  0.235   1.00 110.41 ? 392  ASN   B C   1 
ATOM   5571  O  O   . ASN   B 2 392 ? 32.040  76.654  0.265   1.00 111.82 ? 392  ASN   B O   1 
ATOM   5572  C  CB  . ASN   B 2 392 ? 33.199  75.059  -1.864  1.00 107.55 ? 392  ASN   B CB  1 
ATOM   5573  C  CG  . ASN   B 2 392 ? 33.879  73.872  -2.562  1.00 109.48 ? 392  ASN   B CG  1 
ATOM   5574  O  OD1 . ASN   B 2 392 ? 34.477  73.013  -1.914  1.00 111.59 ? 392  ASN   B OD1 1 
ATOM   5575  N  ND2 . ASN   B 2 392 ? 33.822  73.852  -3.889  1.00 109.29 ? 392  ASN   B ND2 1 
ATOM   5576  N  N   . LEU   B 2 406 ? 32.293  71.469  1.852   1.00 113.13 ? 710  LEU   B N   1 
ATOM   5577  C  CA  . LEU   B 2 406 ? 31.076  71.123  1.118   1.00 108.89 ? 710  LEU   B CA  1 
ATOM   5578  C  C   . LEU   B 2 406 ? 29.851  71.161  2.038   1.00 109.58 ? 710  LEU   B C   1 
ATOM   5579  O  O   . LEU   B 2 406 ? 29.824  70.475  3.065   1.00 109.14 ? 710  LEU   B O   1 
ATOM   5580  C  CB  . LEU   B 2 406 ? 31.211  69.735  0.465   1.00 103.20 ? 710  LEU   B CB  1 
ATOM   5581  C  CG  . LEU   B 2 406 ? 32.186  69.543  -0.709  1.00 96.68  ? 710  LEU   B CG  1 
ATOM   5582  C  CD1 . LEU   B 2 406 ? 31.908  68.266  -1.435  1.00 85.90  ? 710  LEU   B CD1 1 
ATOM   5583  C  CD2 . LEU   B 2 406 ? 32.119  70.690  -1.685  1.00 102.16 ? 710  LEU   B CD2 1 
ATOM   5584  N  N   . HIS   B 2 407 ? 28.856  71.972  1.664   1.00 112.06 ? 711  HIS   B N   1 
ATOM   5585  C  CA  . HIS   B 2 407 ? 27.587  72.108  2.376   1.00 112.16 ? 711  HIS   B CA  1 
ATOM   5586  C  C   . HIS   B 2 407 ? 26.481  71.609  1.453   1.00 110.63 ? 711  HIS   B C   1 
ATOM   5587  O  O   . HIS   B 2 407 ? 26.512  71.871  0.248   1.00 108.81 ? 711  HIS   B O   1 
ATOM   5588  C  CB  . HIS   B 2 407 ? 27.341  73.576  2.815   1.00 114.86 ? 711  HIS   B CB  1 
ATOM   5589  C  CG  . HIS   B 2 407 ? 28.529  74.218  3.480   1.00 120.97 ? 711  HIS   B CG  1 
ATOM   5590  N  ND1 . HIS   B 2 407 ? 28.516  74.640  4.793   1.00 126.73 ? 711  HIS   B ND1 1 
ATOM   5591  C  CD2 . HIS   B 2 407 ? 29.775  74.491  3.015   1.00 123.06 ? 711  HIS   B CD2 1 
ATOM   5592  C  CE1 . HIS   B 2 407 ? 29.698  75.148  5.105   1.00 127.40 ? 711  HIS   B CE1 1 
ATOM   5593  N  NE2 . HIS   B 2 407 ? 30.481  75.067  4.043   1.00 123.09 ? 711  HIS   B NE2 1 
ATOM   5594  N  N   . ILE   B 2 408 ? 25.519  70.867  2.011   1.00 112.18 ? 712  ILE   B N   1 
ATOM   5595  C  CA  . ILE   B 2 408 ? 24.490  70.173  1.229   1.00 107.02 ? 712  ILE   B CA  1 
ATOM   5596  C  C   . ILE   B 2 408 ? 23.117  70.610  1.719   1.00 105.25 ? 712  ILE   B C   1 
ATOM   5597  O  O   . ILE   B 2 408 ? 22.788  70.416  2.900   1.00 106.40 ? 712  ILE   B O   1 
ATOM   5598  C  CB  . ILE   B 2 408 ? 24.612  68.639  1.323   1.00 107.12 ? 712  ILE   B CB  1 
ATOM   5599  C  CG1 . ILE   B 2 408 ? 25.870  68.137  0.620   1.00 108.54 ? 712  ILE   B CG1 1 
ATOM   5600  C  CG2 . ILE   B 2 408 ? 23.388  67.949  0.755   1.00 104.54 ? 712  ILE   B CG2 1 
ATOM   5601  C  CD1 . ILE   B 2 408 ? 27.081  68.109  1.518   1.00 113.04 ? 712  ILE   B CD1 1 
ATOM   5602  N  N   . ARG   B 2 409 ? 22.313  71.179  0.814   1.00 95.94  ? 713  ARG   B N   1 
ATOM   5603  C  CA  . ARG   B 2 409 ? 20.926  71.525  1.102   1.00 91.05  ? 713  ARG   B CA  1 
ATOM   5604  C  C   . ARG   B 2 409 ? 20.047  70.477  0.445   1.00 86.00  ? 713  ARG   B C   1 
ATOM   5605  O  O   . ARG   B 2 409 ? 20.106  70.309  -0.775  1.00 85.32  ? 713  ARG   B O   1 
ATOM   5606  C  CB  . ARG   B 2 409 ? 20.581  72.922  0.589   1.00 90.24  ? 713  ARG   B CB  1 
ATOM   5607  C  CG  . ARG   B 2 409 ? 19.206  73.428  1.009   1.00 92.61  ? 713  ARG   B CG  1 
ATOM   5608  C  CD  . ARG   B 2 409 ? 18.507  74.143  -0.145  1.00 96.63  ? 713  ARG   B CD  1 
ATOM   5609  N  NE  . ARG   B 2 409 ? 17.515  75.132  0.274   1.00 104.34 ? 713  ARG   B NE  1 
ATOM   5610  C  CZ  . ARG   B 2 409 ? 16.307  74.844  0.745   1.00 105.38 ? 713  ARG   B CZ  1 
ATOM   5611  N  NH1 . ARG   B 2 409 ? 15.932  73.594  0.976   1.00 98.51  ? 713  ARG   B NH1 1 
ATOM   5612  N  NH2 . ARG   B 2 409 ? 15.456  75.836  0.998   1.00 111.72 ? 713  ARG   B NH2 1 
ATOM   5613  N  N   . THR   B 2 410 ? 19.256  69.757  1.252   1.00 89.12  ? 714  THR   B N   1 
ATOM   5614  C  CA  . THR   B 2 410 ? 18.400  68.683  0.745   1.00 86.17  ? 714  THR   B CA  1 
ATOM   5615  C  C   . THR   B 2 410 ? 17.000  69.213  0.484   1.00 84.33  ? 714  THR   B C   1 
ATOM   5616  O  O   . THR   B 2 410 ? 16.341  69.741  1.388   1.00 82.03  ? 714  THR   B O   1 
ATOM   5617  C  CB  . THR   B 2 410 ? 18.280  67.492  1.699   1.00 84.08  ? 714  THR   B CB  1 
ATOM   5618  O  OG1 . THR   B 2 410 ? 19.512  66.771  1.759   1.00 86.78  ? 714  THR   B OG1 1 
ATOM   5619  C  CG2 . THR   B 2 410 ? 17.199  66.546  1.199   1.00 80.09  ? 714  THR   B CG2 1 
ATOM   5620  N  N   . VAL   B 2 411 ? 16.553  69.051  -0.753  1.00 82.27  ? 715  VAL   B N   1 
ATOM   5621  C  CA  . VAL   B 2 411 ? 15.156  69.256  -1.095  1.00 79.59  ? 715  VAL   B CA  1 
ATOM   5622  C  C   . VAL   B 2 411 ? 14.527  67.890  -1.329  1.00 83.39  ? 715  VAL   B C   1 
ATOM   5623  O  O   . VAL   B 2 411 ? 14.799  67.263  -2.367  1.00 86.73  ? 715  VAL   B O   1 
ATOM   5624  C  CB  . VAL   B 2 411 ? 15.004  70.122  -2.344  1.00 79.13  ? 715  VAL   B CB  1 
ATOM   5625  C  CG1 . VAL   B 2 411 ? 13.574  70.401  -2.526  1.00 79.11  ? 715  VAL   B CG1 1 
ATOM   5626  C  CG2 . VAL   B 2 411 ? 15.810  71.377  -2.236  1.00 83.10  ? 715  VAL   B CG2 1 
ATOM   5627  N  N   . PRO   B 2 412 ? 13.699  67.374  -0.421  1.00 78.64  ? 716  PRO   B N   1 
ATOM   5628  C  CA  . PRO   B 2 412 ? 13.011  66.119  -0.717  1.00 79.35  ? 716  PRO   B CA  1 
ATOM   5629  C  C   . PRO   B 2 412 ? 12.075  66.307  -1.900  1.00 82.51  ? 716  PRO   B C   1 
ATOM   5630  O  O   . PRO   B 2 412 ? 11.635  67.424  -2.202  1.00 84.69  ? 716  PRO   B O   1 
ATOM   5631  C  CB  . PRO   B 2 412 ? 12.231  65.837  0.569   1.00 78.78  ? 716  PRO   B CB  1 
ATOM   5632  C  CG  . PRO   B 2 412 ? 11.851  67.190  1.035   1.00 80.13  ? 716  PRO   B CG  1 
ATOM   5633  C  CD  . PRO   B 2 412 ? 13.078  68.051  0.727   1.00 83.68  ? 716  PRO   B CD  1 
ATOM   5634  N  N   . LEU   B 2 413 ? 11.778  65.203  -2.581  1.00 79.85  ? 717  LEU   B N   1 
ATOM   5635  C  CA  . LEU   B 2 413 ? 10.773  65.221  -3.627  1.00 77.55  ? 717  LEU   B CA  1 
ATOM   5636  C  C   . LEU   B 2 413 ? 9.743   64.088  -3.529  1.00 77.32  ? 717  LEU   B C   1 
ATOM   5637  O  O   . LEU   B 2 413 ? 8.671   64.220  -4.123  1.00 77.32  ? 717  LEU   B O   1 
ATOM   5638  C  CB  . LEU   B 2 413 ? 11.445  65.197  -5.012  1.00 77.35  ? 717  LEU   B CB  1 
ATOM   5639  C  CG  . LEU   B 2 413 ? 12.293  66.404  -5.423  1.00 77.60  ? 717  LEU   B CG  1 
ATOM   5640  C  CD1 . LEU   B 2 413 ? 13.312  66.040  -6.484  1.00 77.40  ? 717  LEU   B CD1 1 
ATOM   5641  C  CD2 . LEU   B 2 413 ? 11.394  67.511  -5.921  1.00 77.82  ? 717  LEU   B CD2 1 
ATOM   5642  N  N   . TYR   B 2 414 ? 10.022  63.012  -2.776  1.00 79.23  ? 718  TYR   B N   1 
ATOM   5643  C  CA  . TYR   B 2 414 ? 9.089   61.894  -2.569  1.00 80.17  ? 718  TYR   B CA  1 
ATOM   5644  C  C   . TYR   B 2 414 ? 8.666   61.266  -3.892  1.00 80.87  ? 718  TYR   B C   1 
ATOM   5645  O  O   . TYR   B 2 414 ? 7.585   60.658  -3.987  1.00 82.50  ? 718  TYR   B O   1 
ATOM   5646  C  CB  . TYR   B 2 414 ? 7.860   62.330  -1.755  1.00 81.93  ? 718  TYR   B CB  1 
ATOM   5647  C  CG  . TYR   B 2 414 ? 8.253   63.153  -0.546  1.00 81.29  ? 718  TYR   B CG  1 
ATOM   5648  C  CD1 . TYR   B 2 414 ? 8.568   62.548  0.659   1.00 84.44  ? 718  TYR   B CD1 1 
ATOM   5649  C  CD2 . TYR   B 2 414 ? 8.334   64.539  -0.623  1.00 84.50  ? 718  TYR   B CD2 1 
ATOM   5650  C  CE1 . TYR   B 2 414 ? 8.953   63.304  1.767   1.00 89.56  ? 718  TYR   B CE1 1 
ATOM   5651  C  CE2 . TYR   B 2 414 ? 8.715   65.305  0.473   1.00 90.16  ? 718  TYR   B CE2 1 
ATOM   5652  C  CZ  . TYR   B 2 414 ? 9.027   64.683  1.674   1.00 90.37  ? 718  TYR   B CZ  1 
ATOM   5653  O  OH  . TYR   B 2 414 ? 9.406   65.437  2.775   1.00 86.38  ? 718  TYR   B OH  1 
ATOM   5654  N  N   . GLU   B 2 415 ? 9.566   61.369  -4.876  1.00 76.53  ? 719  GLU   B N   1 
ATOM   5655  C  CA  . GLU   B 2 415 ? 9.336   61.201  -6.303  1.00 76.33  ? 719  GLU   B CA  1 
ATOM   5656  C  C   . GLU   B 2 415 ? 10.689  61.178  -6.979  1.00 76.20  ? 719  GLU   B C   1 
ATOM   5657  O  O   . GLU   B 2 415 ? 11.547  61.985  -6.639  1.00 79.79  ? 719  GLU   B O   1 
ATOM   5658  C  CB  . GLU   B 2 415 ? 8.506   62.370  -6.847  1.00 76.58  ? 719  GLU   B CB  1 
ATOM   5659  C  CG  . GLU   B 2 415 ? 7.788   62.138  -8.148  1.00 79.61  ? 719  GLU   B CG  1 
ATOM   5660  C  CD  . GLU   B 2 415 ? 6.819   63.264  -8.469  1.00 85.82  ? 719  GLU   B CD  1 
ATOM   5661  O  OE1 . GLU   B 2 415 ? 6.716   64.185  -7.640  1.00 92.25  ? 719  GLU   B OE1 1 
ATOM   5662  O  OE2 . GLU   B 2 415 ? 6.176   63.232  -9.546  1.00 87.27  ? 719  GLU   B OE2 1 
ATOM   5663  N  N   . SER   B 2 416 ? 10.883  60.276  -7.927  1.00 78.70  ? 720  SER   B N   1 
ATOM   5664  C  CA  . SER   B 2 416 ? 12.223  60.072  -8.504  1.00 79.78  ? 720  SER   B CA  1 
ATOM   5665  C  C   . SER   B 2 416 ? 12.567  61.201  -9.473  1.00 75.95  ? 720  SER   B C   1 
ATOM   5666  O  O   . SER   B 2 416 ? 11.900  61.339  -10.501 1.00 75.92  ? 720  SER   B O   1 
ATOM   5667  C  CB  . SER   B 2 416 ? 12.289  58.735  -9.226  1.00 78.92  ? 720  SER   B CB  1 
ATOM   5668  O  OG  . SER   B 2 416 ? 11.779  57.681  -8.428  1.00 75.28  ? 720  SER   B OG  1 
ATOM   5669  N  N   . PRO   B 2 417 ? 13.593  62.010  -9.206  1.00 82.07  ? 721  PRO   B N   1 
ATOM   5670  C  CA  . PRO   B 2 417 ? 14.068  62.930  -10.242 1.00 79.83  ? 721  PRO   B CA  1 
ATOM   5671  C  C   . PRO   B 2 417 ? 14.966  62.174  -11.203 1.00 81.47  ? 721  PRO   B C   1 
ATOM   5672  O  O   . PRO   B 2 417 ? 15.788  61.342  -10.793 1.00 82.17  ? 721  PRO   B O   1 
ATOM   5673  C  CB  . PRO   B 2 417 ? 14.852  63.991  -9.462  1.00 80.10  ? 721  PRO   B CB  1 
ATOM   5674  C  CG  . PRO   B 2 417 ? 15.426  63.247  -8.322  1.00 81.48  ? 721  PRO   B CG  1 
ATOM   5675  C  CD  . PRO   B 2 417 ? 14.447  62.077  -8.003  1.00 82.97  ? 721  PRO   B CD  1 
ATOM   5676  N  N   . ARG   B 2 418 ? 14.807  62.477  -12.491 1.00 79.03  ? 722  ARG   B N   1 
ATOM   5677  C  CA  . ARG   B 2 418 ? 15.541  61.782  -13.538 1.00 75.97  ? 722  ARG   B CA  1 
ATOM   5678  C  C   . ARG   B 2 418 ? 16.545  62.657  -14.285 1.00 76.23  ? 722  ARG   B C   1 
ATOM   5679  O  O   . ARG   B 2 418 ? 17.696  62.236  -14.442 1.00 76.20  ? 722  ARG   B O   1 
ATOM   5680  C  CB  . ARG   B 2 418 ? 14.541  61.153  -14.506 1.00 75.77  ? 722  ARG   B CB  1 
ATOM   5681  C  CG  . ARG   B 2 418 ? 13.708  60.067  -13.861 1.00 77.03  ? 722  ARG   B CG  1 
ATOM   5682  C  CD  . ARG   B 2 418 ? 14.579  58.953  -13.291 1.00 81.05  ? 722  ARG   B CD  1 
ATOM   5683  N  NE  . ARG   B 2 418 ? 15.023  57.961  -14.275 1.00 83.67  ? 722  ARG   B NE  1 
ATOM   5684  C  CZ  . ARG   B 2 418 ? 16.063  57.147  -14.101 1.00 84.73  ? 722  ARG   B CZ  1 
ATOM   5685  N  NH1 . ARG   B 2 418 ? 16.825  57.213  -13.012 1.00 83.42  ? 722  ARG   B NH1 1 
ATOM   5686  N  NH2 . ARG   B 2 418 ? 16.346  56.244  -15.041 1.00 86.72  ? 722  ARG   B NH2 1 
ATOM   5687  N  N   . LYS   B 2 419 ? 16.160  63.858  -14.743 1.00 76.51  ? 723  LYS   B N   1 
ATOM   5688  C  CA  . LYS   B 2 419 ? 17.050  64.735  -15.499 1.00 76.81  ? 723  LYS   B CA  1 
ATOM   5689  C  C   . LYS   B 2 419 ? 16.852  66.172  -15.027 1.00 78.77  ? 723  LYS   B C   1 
ATOM   5690  O  O   . LYS   B 2 419 ? 15.732  66.579  -14.713 1.00 81.01  ? 723  LYS   B O   1 
ATOM   5691  C  CB  . LYS   B 2 419 ? 16.800  64.610  -17.011 1.00 76.79  ? 723  LYS   B CB  1 
ATOM   5692  C  CG  . LYS   B 2 419 ? 17.120  63.221  -17.606 1.00 76.47  ? 723  LYS   B CG  1 
ATOM   5693  C  CD  . LYS   B 2 419 ? 18.605  62.883  -17.478 1.00 77.88  ? 723  LYS   B CD  1 
ATOM   5694  C  CE  . LYS   B 2 419 ? 18.898  61.379  -17.534 1.00 79.45  ? 723  LYS   B CE  1 
ATOM   5695  N  NZ  . LYS   B 2 419 ? 19.004  60.839  -18.919 1.00 83.08  ? 723  LYS   B NZ  1 
ATOM   5696  N  N   . ILE   B 2 420 ? 17.947  66.939  -14.940 1.00 80.35  ? 724  ILE   B N   1 
ATOM   5697  C  CA  . ILE   B 2 420 ? 17.891  68.309  -14.427 1.00 81.97  ? 724  ILE   B CA  1 
ATOM   5698  C  C   . ILE   B 2 420 ? 18.648  69.267  -15.344 1.00 84.46  ? 724  ILE   B C   1 
ATOM   5699  O  O   . ILE   B 2 420 ? 19.746  68.954  -15.819 1.00 86.57  ? 724  ILE   B O   1 
ATOM   5700  C  CB  . ILE   B 2 420 ? 18.447  68.414  -12.991 1.00 81.07  ? 724  ILE   B CB  1 
ATOM   5701  C  CG1 . ILE   B 2 420 ? 18.331  69.865  -12.495 1.00 83.46  ? 724  ILE   B CG1 1 
ATOM   5702  C  CG2 . ILE   B 2 420 ? 19.887  67.917  -12.937 1.00 78.02  ? 724  ILE   B CG2 1 
ATOM   5703  C  CD1 . ILE   B 2 420 ? 18.327  70.028  -10.995 1.00 80.53  ? 724  ILE   B CD1 1 
ATOM   5704  N  N   . CYS   B 2 421 ? 18.070  70.453  -15.565 1.00 84.57  ? 725  CYS   B N   1 
ATOM   5705  C  CA  . CYS   B 2 421 ? 18.713  71.534  -16.306 1.00 85.37  ? 725  CYS   B CA  1 
ATOM   5706  C  C   . CYS   B 2 421 ? 18.344  72.873  -15.670 1.00 87.94  ? 725  CYS   B C   1 
ATOM   5707  O  O   . CYS   B 2 421 ? 17.397  72.966  -14.882 1.00 85.43  ? 725  CYS   B O   1 
ATOM   5708  C  CB  . CYS   B 2 421 ? 18.295  71.511  -17.768 1.00 84.69  ? 725  CYS   B CB  1 
ATOM   5709  S  SG  . CYS   B 2 421 ? 16.660  72.162  -17.970 1.00 89.32  ? 725  CYS   B SG  1 
ATOM   5710  N  N   . TYR   B 2 422 ? 19.089  73.927  -16.021 1.00 88.03  ? 726  TYR   B N   1 
ATOM   5711  C  CA  . TYR   B 2 422 ? 18.946  75.229  -15.370 1.00 91.33  ? 726  TYR   B CA  1 
ATOM   5712  C  C   . TYR   B 2 422 ? 18.637  76.326  -16.385 1.00 95.53  ? 726  TYR   B C   1 
ATOM   5713  O  O   . TYR   B 2 422 ? 19.477  76.663  -17.227 1.00 97.66  ? 726  TYR   B O   1 
ATOM   5714  C  CB  . TYR   B 2 422 ? 20.202  75.576  -14.572 1.00 90.32  ? 726  TYR   B CB  1 
ATOM   5715  C  CG  . TYR   B 2 422 ? 20.184  76.972  -13.973 1.00 94.42  ? 726  TYR   B CG  1 
ATOM   5716  C  CD1 . TYR   B 2 422 ? 19.324  77.302  -12.929 1.00 97.01  ? 726  TYR   B CD1 1 
ATOM   5717  C  CD2 . TYR   B 2 422 ? 21.035  77.956  -14.446 1.00 97.20  ? 726  TYR   B CD2 1 
ATOM   5718  C  CE1 . TYR   B 2 422 ? 19.317  78.576  -12.380 1.00 95.98  ? 726  TYR   B CE1 1 
ATOM   5719  C  CE2 . TYR   B 2 422 ? 21.033  79.227  -13.903 1.00 98.45  ? 726  TYR   B CE2 1 
ATOM   5720  C  CZ  . TYR   B 2 422 ? 20.174  79.532  -12.877 1.00 96.50  ? 726  TYR   B CZ  1 
ATOM   5721  O  OH  . TYR   B 2 422 ? 20.185  80.803  -12.353 1.00 101.06 ? 726  TYR   B OH  1 
ATOM   5722  N  N   . GLN   B 2 423 ? 17.449  76.904  -16.274 1.00 96.79  ? 727  GLN   B N   1 
ATOM   5723  C  CA  . GLN   B 2 423 ? 17.019  78.014  -17.118 1.00 99.06  ? 727  GLN   B CA  1 
ATOM   5724  C  C   . GLN   B 2 423 ? 17.302  79.292  -16.351 1.00 102.51 ? 727  GLN   B C   1 
ATOM   5725  O  O   . GLN   B 2 423 ? 16.529  79.686  -15.466 1.00 101.30 ? 727  GLN   B O   1 
ATOM   5726  C  CB  . GLN   B 2 423 ? 15.546  77.896  -17.459 1.00 101.83 ? 727  GLN   B CB  1 
ATOM   5727  C  CG  . GLN   B 2 423 ? 15.031  78.947  -18.373 1.00 96.60  ? 727  GLN   B CG  1 
ATOM   5728  C  CD  . GLN   B 2 423 ? 13.916  78.396  -19.195 1.00 100.40 ? 727  GLN   B CD  1 
ATOM   5729  O  OE1 . GLN   B 2 423 ? 12.746  78.597  -18.887 1.00 102.53 ? 727  GLN   B OE1 1 
ATOM   5730  N  NE2 . GLN   B 2 423 ? 14.265  77.665  -20.242 1.00 103.15 ? 727  GLN   B NE2 1 
ATOM   5731  N  N   . GLU   B 2 424 ? 18.413  79.934  -16.700 1.00 102.71 ? 728  GLU   B N   1 
ATOM   5732  C  CA  . GLU   B 2 424 ? 18.851  81.094  -15.946 1.00 101.05 ? 728  GLU   B CA  1 
ATOM   5733  C  C   . GLU   B 2 424 ? 17.893  82.259  -16.137 1.00 102.05 ? 728  GLU   B C   1 
ATOM   5734  O  O   . GLU   B 2 424 ? 17.549  82.961  -15.182 1.00 103.08 ? 728  GLU   B O   1 
ATOM   5735  C  CB  . GLU   B 2 424 ? 20.261  81.475  -16.374 1.00 104.77 ? 728  GLU   B CB  1 
ATOM   5736  C  CG  . GLU   B 2 424 ? 20.964  82.353  -15.380 1.00 111.43 ? 728  GLU   B CG  1 
ATOM   5737  C  CD  . GLU   B 2 424 ? 22.242  82.906  -15.945 1.00 119.21 ? 728  GLU   B CD  1 
ATOM   5738  O  OE1 . GLU   B 2 424 ? 22.771  82.305  -16.908 1.00 120.87 ? 728  GLU   B OE1 1 
ATOM   5739  O  OE2 . GLU   B 2 424 ? 22.711  83.945  -15.439 1.00 131.16 ? 728  GLU   B OE2 1 
ATOM   5740  N  N   . VAL   B 2 425 ? 17.442  82.463  -17.369 1.00 101.15 ? 729  VAL   B N   1 
ATOM   5741  C  CA  . VAL   B 2 425 ? 16.527  83.558  -17.656 1.00 102.54 ? 729  VAL   B CA  1 
ATOM   5742  C  C   . VAL   B 2 425 ? 15.341  83.535  -16.697 1.00 102.87 ? 729  VAL   B C   1 
ATOM   5743  O  O   . VAL   B 2 425 ? 14.955  84.563  -16.134 1.00 100.20 ? 729  VAL   B O   1 
ATOM   5744  C  CB  . VAL   B 2 425 ? 16.083  83.488  -19.129 1.00 108.62 ? 729  VAL   B CB  1 
ATOM   5745  C  CG1 . VAL   B 2 425 ? 14.915  84.416  -19.399 1.00 113.89 ? 729  VAL   B CG1 1 
ATOM   5746  C  CG2 . VAL   B 2 425 ? 17.262  83.814  -20.037 1.00 106.83 ? 729  VAL   B CG2 1 
ATOM   5747  N  N   . SER   B 2 426 ? 14.779  82.346  -16.465 1.00 109.84 ? 730  SER   B N   1 
ATOM   5748  C  CA  . SER   B 2 426 ? 13.571  82.195  -15.655 1.00 109.52 ? 730  SER   B CA  1 
ATOM   5749  C  C   . SER   B 2 426 ? 13.849  82.131  -14.162 1.00 107.45 ? 730  SER   B C   1 
ATOM   5750  O  O   . SER   B 2 426 ? 12.896  82.145  -13.371 1.00 106.65 ? 730  SER   B O   1 
ATOM   5751  C  CB  . SER   B 2 426 ? 12.815  80.935  -16.078 1.00 109.52 ? 730  SER   B CB  1 
ATOM   5752  O  OG  . SER   B 2 426 ? 12.589  80.941  -17.472 1.00 111.82 ? 730  SER   B OG  1 
ATOM   5753  N  N   . GLN   B 2 427 ? 15.117  82.068  -13.768 1.00 103.50 ? 731  GLN   B N   1 
ATOM   5754  C  CA  . GLN   B 2 427 ? 15.512  81.878  -12.379 1.00 101.66 ? 731  GLN   B CA  1 
ATOM   5755  C  C   . GLN   B 2 427 ? 14.780  80.678  -11.780 1.00 101.21 ? 731  GLN   B C   1 
ATOM   5756  O  O   . GLN   B 2 427 ? 14.076  80.778  -10.778 1.00 100.79 ? 731  GLN   B O   1 
ATOM   5757  C  CB  . GLN   B 2 427 ? 15.278  83.152  -11.554 1.00 101.05 ? 731  GLN   B CB  1 
ATOM   5758  N  N   . CYS   B 2 428 ? 14.965  79.526  -12.423 1.00 105.22 ? 732  CYS   B N   1 
ATOM   5759  C  CA  . CYS   B 2 428 ? 14.359  78.280  -11.954 1.00 102.50 ? 732  CYS   B CA  1 
ATOM   5760  C  C   . CYS   B 2 428 ? 15.052  77.082  -12.606 1.00 101.20 ? 732  CYS   B C   1 
ATOM   5761  O  O   . CYS   B 2 428 ? 15.831  77.220  -13.554 1.00 101.92 ? 732  CYS   B O   1 
ATOM   5762  C  CB  . CYS   B 2 428 ? 12.856  78.251  -12.254 1.00 102.26 ? 732  CYS   B CB  1 
ATOM   5763  S  SG  . CYS   B 2 428 ? 12.570  78.062  -14.017 1.00 112.29 ? 732  CYS   B SG  1 
ATOM   5764  N  N   . PHE   B 2 429 ? 14.717  75.890  -12.108 1.00 96.68  ? 733  PHE   B N   1 
ATOM   5765  C  CA  . PHE   B 2 429 ? 15.258  74.642  -12.628 1.00 93.86  ? 733  PHE   B CA  1 
ATOM   5766  C  C   . PHE   B 2 429 ? 14.201  73.817  -13.349 1.00 92.23  ? 733  PHE   B C   1 
ATOM   5767  O  O   . PHE   B 2 429 ? 13.061  73.702  -12.884 1.00 89.54  ? 733  PHE   B O   1 
ATOM   5768  C  CB  . PHE   B 2 429 ? 15.841  73.795  -11.513 1.00 88.83  ? 733  PHE   B CB  1 
ATOM   5769  C  CG  . PHE   B 2 429 ? 17.128  74.307  -10.998 1.00 90.19  ? 733  PHE   B CG  1 
ATOM   5770  C  CD1 . PHE   B 2 429 ? 18.309  74.019  -11.660 1.00 95.48  ? 733  PHE   B CD1 1 
ATOM   5771  C  CD2 . PHE   B 2 429 ? 17.173  75.070  -9.848  1.00 90.04  ? 733  PHE   B CD2 1 
ATOM   5772  C  CE1 . PHE   B 2 429 ? 19.523  74.483  -11.176 1.00 92.30  ? 733  PHE   B CE1 1 
ATOM   5773  C  CE2 . PHE   B 2 429 ? 18.374  75.533  -9.359  1.00 90.85  ? 733  PHE   B CE2 1 
ATOM   5774  C  CZ  . PHE   B 2 429 ? 19.547  75.245  -10.023 1.00 91.11  ? 733  PHE   B CZ  1 
ATOM   5775  N  N   . GLY   B 2 430 ? 14.598  73.232  -14.477 1.00 89.01  ? 734  GLY   B N   1 
ATOM   5776  C  CA  . GLY   B 2 430 ? 13.810  72.197  -15.110 1.00 89.76  ? 734  GLY   B CA  1 
ATOM   5777  C  C   . GLY   B 2 430 ? 14.261  70.804  -14.683 1.00 90.26  ? 734  GLY   B C   1 
ATOM   5778  O  O   . GLY   B 2 430 ? 15.430  70.436  -14.864 1.00 89.37  ? 734  GLY   B O   1 
ATOM   5779  N  N   . VAL   B 2 431 ? 13.367  70.016  -14.089 1.00 85.88  ? 735  VAL   B N   1 
ATOM   5780  C  CA  . VAL   B 2 431 ? 13.688  68.650  -13.706 1.00 79.59  ? 735  VAL   B CA  1 
ATOM   5781  C  C   . VAL   B 2 431 ? 12.583  67.737  -14.205 1.00 80.79  ? 735  VAL   B C   1 
ATOM   5782  O  O   . VAL   B 2 431 ? 11.400  68.093  -14.174 1.00 79.35  ? 735  VAL   B O   1 
ATOM   5783  C  CB  . VAL   B 2 431 ? 13.876  68.489  -12.186 1.00 80.29  ? 735  VAL   B CB  1 
ATOM   5784  C  CG1 . VAL   B 2 431 ? 14.332  67.076  -11.864 1.00 81.40  ? 735  VAL   B CG1 1 
ATOM   5785  C  CG2 . VAL   B 2 431 ? 14.882  69.469  -11.680 1.00 84.23  ? 735  VAL   B CG2 1 
ATOM   5786  N  N   . LEU   B 2 432 ? 12.982  66.564  -14.683 1.00 78.36  ? 736  LEU   B N   1 
ATOM   5787  C  CA  . LEU   B 2 432 ? 12.069  65.539  -15.157 1.00 76.82  ? 736  LEU   B CA  1 
ATOM   5788  C  C   . LEU   B 2 432 ? 11.914  64.499  -14.052 1.00 76.56  ? 736  LEU   B C   1 
ATOM   5789  O  O   . LEU   B 2 432 ? 12.908  63.921  -13.596 1.00 76.42  ? 736  LEU   B O   1 
ATOM   5790  C  CB  . LEU   B 2 432 ? 12.596  64.908  -16.449 1.00 76.68  ? 736  LEU   B CB  1 
ATOM   5791  C  CG  . LEU   B 2 432 ? 12.636  65.630  -17.808 1.00 76.91  ? 736  LEU   B CG  1 
ATOM   5792  C  CD1 . LEU   B 2 432 ? 13.347  64.765  -18.840 1.00 76.75  ? 736  LEU   B CD1 1 
ATOM   5793  C  CD2 . LEU   B 2 432 ? 11.253  66.045  -18.325 1.00 80.01  ? 736  LEU   B CD2 1 
ATOM   5794  N  N   . SER   B 2 433 ? 10.670  64.286  -13.605 1.00 78.25  ? 737  SER   B N   1 
ATOM   5795  C  CA  . SER   B 2 433 ? 10.382  63.468  -12.433 1.00 76.36  ? 737  SER   B CA  1 
ATOM   5796  C  C   . SER   B 2 433 ? 9.315   62.420  -12.723 1.00 76.15  ? 737  SER   B C   1 
ATOM   5797  O  O   . SER   B 2 433 ? 8.430   62.622  -13.557 1.00 78.20  ? 737  SER   B O   1 
ATOM   5798  C  CB  . SER   B 2 433 ? 9.907   64.332  -11.272 1.00 76.63  ? 737  SER   B CB  1 
ATOM   5799  O  OG  . SER   B 2 433 ? 8.497   64.468  -11.308 1.00 78.16  ? 737  SER   B OG  1 
ATOM   5800  N  N   . SER   B 2 434 ? 9.356   61.338  -11.938 1.00 75.94  ? 738  SER   B N   1 
ATOM   5801  C  CA  . SER   B 2 434 ? 8.576   60.125  -12.170 1.00 75.71  ? 738  SER   B CA  1 
ATOM   5802  C  C   . SER   B 2 434 ? 7.857   59.718  -10.884 1.00 76.68  ? 738  SER   B C   1 
ATOM   5803  O  O   . SER   B 2 434 ? 8.507   59.512  -9.851  1.00 82.26  ? 738  SER   B O   1 
ATOM   5804  C  CB  . SER   B 2 434 ? 9.510   59.009  -12.665 1.00 75.40  ? 738  SER   B CB  1 
ATOM   5805  O  OG  . SER   B 2 434 ? 8.935   57.717  -12.622 1.00 78.82  ? 738  SER   B OG  1 
ATOM   5806  N  N   . ARG   B 2 435 ? 6.525   59.575  -10.953 1.00 75.91  ? 739  ARG   B N   1 
ATOM   5807  C  CA  . ARG   B 2 435 ? 5.684   59.181  -9.822  1.00 75.91  ? 739  ARG   B CA  1 
ATOM   5808  C  C   . ARG   B 2 435 ? 5.142   57.769  -10.019 1.00 76.24  ? 739  ARG   B C   1 
ATOM   5809  O  O   . ARG   B 2 435 ? 4.653   57.447  -11.107 1.00 76.68  ? 739  ARG   B O   1 
ATOM   5810  C  CB  . ARG   B 2 435 ? 4.509   60.152  -9.672  1.00 77.16  ? 739  ARG   B CB  1 
ATOM   5811  C  CG  . ARG   B 2 435 ? 3.728   59.976  -8.390  1.00 84.83  ? 739  ARG   B CG  1 
ATOM   5812  C  CD  . ARG   B 2 435 ? 2.645   61.024  -8.257  1.00 89.22  ? 739  ARG   B CD  1 
ATOM   5813  N  NE  . ARG   B 2 435 ? 1.603   60.894  -9.273  1.00 89.00  ? 739  ARG   B NE  1 
ATOM   5814  C  CZ  . ARG   B 2 435 ? 1.336   61.797  -10.212 1.00 89.90  ? 739  ARG   B CZ  1 
ATOM   5815  N  NH1 . ARG   B 2 435 ? 2.023   62.917  -10.310 1.00 92.17  ? 739  ARG   B NH1 1 
ATOM   5816  N  NH2 . ARG   B 2 435 ? 0.344   61.576  -11.069 1.00 92.56  ? 739  ARG   B NH2 1 
ATOM   5817  N  N   . ILE   B 2 436 ? 5.195   56.935  -8.984  1.00 82.49  ? 740  ILE   B N   1 
ATOM   5818  C  CA  . ILE   B 2 436 ? 4.670   55.567  -9.069  1.00 77.22  ? 740  ILE   B CA  1 
ATOM   5819  C  C   . ILE   B 2 436 ? 3.222   55.555  -8.592  1.00 75.83  ? 740  ILE   B C   1 
ATOM   5820  O  O   . ILE   B 2 436 ? 2.924   55.970  -7.466  1.00 80.04  ? 740  ILE   B O   1 
ATOM   5821  C  CB  . ILE   B 2 436 ? 5.505   54.571  -8.252  1.00 75.23  ? 740  ILE   B CB  1 
ATOM   5822  C  CG1 . ILE   B 2 436 ? 7.036   54.826  -8.376  1.00 79.87  ? 740  ILE   B CG1 1 
ATOM   5823  C  CG2 . ILE   B 2 436 ? 5.058   53.150  -8.563  1.00 75.03  ? 740  ILE   B CG2 1 
ATOM   5824  C  CD1 . ILE   B 2 436 ? 7.645   55.023  -9.818  1.00 80.83  ? 740  ILE   B CD1 1 
ATOM   5825  N  N   . GLU   B 2 437 ? 2.327   55.074  -9.435  1.00 77.49  ? 741  GLU   B N   1 
ATOM   5826  C  CA  . GLU   B 2 437 ? 0.916   55.006  -9.087  1.00 85.33  ? 741  GLU   B CA  1 
ATOM   5827  C  C   . GLU   B 2 437 ? 0.412   53.590  -9.346  1.00 87.44  ? 741  GLU   B C   1 
ATOM   5828  O  O   . GLU   B 2 437 ? 0.961   52.873  -10.185 1.00 84.54  ? 741  GLU   B O   1 
ATOM   5829  C  CB  . GLU   B 2 437 ? 0.113   56.065  -9.864  1.00 88.34  ? 741  GLU   B CB  1 
ATOM   5830  C  CG  . GLU   B 2 437 ? 0.589   57.497  -9.575  1.00 86.53  ? 741  GLU   B CG  1 
ATOM   5831  C  CD  . GLU   B 2 437 ? -0.469  58.546  -9.913  1.00 97.05  ? 741  GLU   B CD  1 
ATOM   5832  O  OE1 . GLU   B 2 437 ? -1.008  58.488  -11.039 1.00 98.15  ? 741  GLU   B OE1 1 
ATOM   5833  O  OE2 . GLU   B 2 437 ? -0.797  59.410  -9.055  1.00 100.99 ? 741  GLU   B OE2 1 
ATOM   5834  N  N   . VAL   B 2 438 ? -0.606  53.170  -8.588  1.00 94.57  ? 742  VAL   B N   1 
ATOM   5835  C  CA  . VAL   B 2 438 ? -1.132  51.807  -8.642  1.00 92.71  ? 742  VAL   B CA  1 
ATOM   5836  C  C   . VAL   B 2 438 ? -2.506  51.840  -9.294  1.00 101.77 ? 742  VAL   B C   1 
ATOM   5837  O  O   . VAL   B 2 438 ? -3.322  52.710  -8.975  1.00 110.88 ? 742  VAL   B O   1 
ATOM   5838  C  CB  . VAL   B 2 438 ? -1.200  51.188  -7.238  1.00 90.89  ? 742  VAL   B CB  1 
ATOM   5839  C  CG1 . VAL   B 2 438 ? -2.213  51.907  -6.382  1.00 98.03  ? 742  VAL   B CG1 1 
ATOM   5840  C  CG2 . VAL   B 2 438 ? -1.536  49.739  -7.317  1.00 102.80 ? 742  VAL   B CG2 1 
ATOM   5841  N  N   . GLN   B 2 439 ? -2.759  50.921  -10.226 1.00 104.04 ? 743  GLN   B N   1 
ATOM   5842  C  CA  . GLN   B 2 439 ? -4.060  50.901  -10.885 1.00 111.16 ? 743  GLN   B CA  1 
ATOM   5843  C  C   . GLN   B 2 439 ? -5.109  50.446  -9.880  1.00 117.61 ? 743  GLN   B C   1 
ATOM   5844  O  O   . GLN   B 2 439 ? -4.974  49.372  -9.290  1.00 114.60 ? 743  GLN   B O   1 
ATOM   5845  C  CB  . GLN   B 2 439 ? -4.048  49.997  -12.114 1.00 112.59 ? 743  GLN   B CB  1 
ATOM   5846  C  CG  . GLN   B 2 439 ? -5.459  49.549  -12.558 1.00 126.69 ? 743  GLN   B CG  1 
ATOM   5847  C  CD  . GLN   B 2 439 ? -6.062  50.365  -13.708 1.00 129.25 ? 743  GLN   B CD  1 
ATOM   5848  O  OE1 . GLN   B 2 439 ? -5.425  51.287  -14.240 1.00 125.42 ? 743  GLN   B OE1 1 
ATOM   5849  N  NE2 . GLN   B 2 439 ? -7.296  50.008  -14.105 1.00 121.80 ? 743  GLN   B NE2 1 
ATOM   5850  N  N   . ASP   B 2 440 ? -6.137  51.274  -9.660  1.00 125.37 ? 744  ASP   B N   1 
ATOM   5851  C  CA  . ASP   B 2 440 ? -7.139  51.017  -8.625  1.00 128.87 ? 744  ASP   B CA  1 
ATOM   5852  C  C   . ASP   B 2 440 ? -8.548  50.947  -9.232  1.00 133.90 ? 744  ASP   B C   1 
ATOM   5853  O  O   . ASP   B 2 440 ? -8.732  50.997  -10.457 1.00 131.51 ? 744  ASP   B O   1 
ATOM   5854  C  CB  . ASP   B 2 440 ? -7.065  52.059  -7.494  1.00 128.71 ? 744  ASP   B CB  1 
ATOM   5855  C  CG  . ASP   B 2 440 ? -7.735  53.396  -7.846  1.00 136.06 ? 744  ASP   B CG  1 
ATOM   5856  O  OD1 . ASP   B 2 440 ? -7.199  54.134  -8.706  1.00 134.34 ? 744  ASP   B OD1 1 
ATOM   5857  O  OD2 . ASP   B 2 440 ? -8.787  53.722  -7.237  1.00 141.21 ? 744  ASP   B OD2 1 
ATOM   5858  N  N   . THR   B 2 441 ? -9.548  50.869  -8.338  1.00 135.86 ? 745  THR   B N   1 
ATOM   5859  C  CA  . THR   B 2 441 ? -10.886 50.382  -8.688  1.00 133.30 ? 745  THR   B CA  1 
ATOM   5860  C  C   . THR   B 2 441 ? -11.642 51.320  -9.629  1.00 133.37 ? 745  THR   B C   1 
ATOM   5861  O  O   . THR   B 2 441 ? -12.505 50.873  -10.396 1.00 128.52 ? 745  THR   B O   1 
ATOM   5862  C  CB  . THR   B 2 441 ? -11.680 50.170  -7.405  1.00 124.99 ? 745  THR   B CB  1 
ATOM   5863  O  OG1 . THR   B 2 441 ? -12.201 51.432  -6.977  1.00 125.74 ? 745  THR   B OG1 1 
ATOM   5864  C  CG2 . THR   B 2 441 ? -10.754 49.618  -6.320  1.00 121.80 ? 745  THR   B CG2 1 
ATOM   5865  N  N   . SER   B 2 442 ? -11.363 52.619  -9.561  1.00 146.99 ? 746  SER   B N   1 
ATOM   5866  C  CA  . SER   B 2 442 ? -12.044 53.565  -10.437 1.00 149.07 ? 746  SER   B CA  1 
ATOM   5867  C  C   . SER   B 2 442 ? -11.737 53.314  -11.914 1.00 151.55 ? 746  SER   B C   1 
ATOM   5868  O  O   . SER   B 2 442 ? -12.457 53.816  -12.791 1.00 151.30 ? 746  SER   B O   1 
ATOM   5869  C  CB  . SER   B 2 442 ? -11.674 55.004  -10.034 1.00 147.68 ? 746  SER   B CB  1 
ATOM   5870  O  OG  . SER   B 2 442 ? -10.270 55.192  -9.933  1.00 149.01 ? 746  SER   B OG  1 
ATOM   5871  N  N   . GLY   B 2 443 ? -10.712 52.520  -12.211 1.00 149.92 ? 747  GLY   B N   1 
ATOM   5872  C  CA  . GLY   B 2 443 ? -10.192 52.396  -13.550 1.00 148.48 ? 747  GLY   B CA  1 
ATOM   5873  C  C   . GLY   B 2 443 ? -9.003  53.295  -13.829 1.00 147.99 ? 747  GLY   B C   1 
ATOM   5874  O  O   . GLY   B 2 443 ? -8.257  53.038  -14.782 1.00 145.48 ? 747  GLY   B O   1 
ATOM   5875  N  N   . GLY   B 2 444 ? -8.806  54.328  -13.019 1.00 149.53 ? 748  GLY   B N   1 
ATOM   5876  C  CA  . GLY   B 2 444 ? -7.632  55.179  -13.097 1.00 145.75 ? 748  GLY   B CA  1 
ATOM   5877  C  C   . GLY   B 2 444 ? -6.503  54.628  -12.258 1.00 140.67 ? 748  GLY   B C   1 
ATOM   5878  O  O   . GLY   B 2 444 ? -6.428  53.423  -11.993 1.00 139.34 ? 748  GLY   B O   1 
ATOM   5879  N  N   . THR   B 2 445 ? -5.605  55.513  -11.825 1.00 124.41 ? 749  THR   B N   1 
ATOM   5880  C  CA  . THR   B 2 445 ? -4.563  55.138  -10.876 1.00 113.01 ? 749  THR   B CA  1 
ATOM   5881  C  C   . THR   B 2 445 ? -4.480  56.192  -9.788  1.00 112.20 ? 749  THR   B C   1 
ATOM   5882  O  O   . THR   B 2 445 ? -4.398  57.393  -10.074 1.00 113.45 ? 749  THR   B O   1 
ATOM   5883  C  CB  . THR   B 2 445 ? -3.203  54.954  -11.544 1.00 99.96  ? 749  THR   B CB  1 
ATOM   5884  O  OG1 . THR   B 2 445 ? -2.866  56.142  -12.256 1.00 105.90 ? 749  THR   B OG1 1 
ATOM   5885  C  CG2 . THR   B 2 445 ? -3.247  53.804  -12.508 1.00 104.07 ? 749  THR   B CG2 1 
ATOM   5886  N  N   . THR   B 2 446 ? -4.541  55.737  -8.549  1.00 111.15 ? 750  THR   B N   1 
ATOM   5887  C  CA  . THR   B 2 446 ? -4.210  56.562  -7.411  1.00 107.71 ? 750  THR   B CA  1 
ATOM   5888  C  C   . THR   B 2 446 ? -2.700  56.524  -7.216  1.00 99.88  ? 750  THR   B C   1 
ATOM   5889  O  O   . THR   B 2 446 ? -2.035  55.564  -7.612  1.00 96.10  ? 750  THR   B O   1 
ATOM   5890  C  CB  . THR   B 2 446 ? -4.964  56.043  -6.179  1.00 114.28 ? 750  THR   B CB  1 
ATOM   5891  O  OG1 . THR   B 2 446 ? -4.706  56.882  -5.050  1.00 118.50 ? 750  THR   B OG1 1 
ATOM   5892  C  CG2 . THR   B 2 446 ? -4.575  54.595  -5.846  1.00 110.27 ? 750  THR   B CG2 1 
ATOM   5893  N  N   . ALA   B 2 447 ? -2.145  57.597  -6.648  1.00 103.36 ? 751  ALA   B N   1 
ATOM   5894  C  CA  . ALA   B 2 447 ? -0.743  57.539  -6.234  1.00 102.93 ? 751  ALA   B CA  1 
ATOM   5895  C  C   . ALA   B 2 447 ? -0.705  56.859  -4.868  1.00 104.30 ? 751  ALA   B C   1 
ATOM   5896  O  O   . ALA   B 2 447 ? -1.723  56.340  -4.400  1.00 108.58 ? 751  ALA   B O   1 
ATOM   5897  C  CB  . ALA   B 2 447 ? -0.134  58.939  -6.105  1.00 100.92 ? 751  ALA   B CB  1 
ATOM   5898  N  N   . LEU   B 2 448 ? 0.442   56.830  -4.217  1.00 92.74  ? 752  LEU   B N   1 
ATOM   5899  C  CA  . LEU   B 2 448 ? 0.459   56.248  -2.889  1.00 94.94  ? 752  LEU   B CA  1 
ATOM   5900  C  C   . LEU   B 2 448 ? 1.122   57.086  -1.815  1.00 95.29  ? 752  LEU   B C   1 
ATOM   5901  O  O   . LEU   B 2 448 ? 1.188   56.651  -0.660  1.00 96.80  ? 752  LEU   B O   1 
ATOM   5902  C  CB  . LEU   B 2 448 ? 1.154   54.893  -3.030  1.00 98.18  ? 752  LEU   B CB  1 
ATOM   5903  C  CG  . LEU   B 2 448 ? 2.539   54.895  -3.637  1.00 96.21  ? 752  LEU   B CG  1 
ATOM   5904  C  CD1 . LEU   B 2 448 ? 3.485   54.916  -2.464  1.00 98.64  ? 752  LEU   B CD1 1 
ATOM   5905  C  CD2 . LEU   B 2 448 ? 2.737   53.662  -4.489  1.00 83.41  ? 752  LEU   B CD2 1 
ATOM   5906  N  N   . ARG   B 2 449 ? 1.589   58.271  -2.171  1.00 94.48  ? 753  ARG   B N   1 
ATOM   5907  C  CA  . ARG   B 2 449 ? 2.101   59.284  -1.263  1.00 90.66  ? 753  ARG   B CA  1 
ATOM   5908  C  C   . ARG   B 2 449 ? 2.026   60.598  -2.010  1.00 91.07  ? 753  ARG   B C   1 
ATOM   5909  O  O   . ARG   B 2 449 ? 2.079   60.602  -3.245  1.00 95.50  ? 753  ARG   B O   1 
ATOM   5910  C  CB  . ARG   B 2 449 ? 3.552   58.972  -0.842  1.00 90.60  ? 753  ARG   B CB  1 
ATOM   5911  C  CG  . ARG   B 2 449 ? 4.626   59.698  -1.624  1.00 88.78  ? 753  ARG   B CG  1 
ATOM   5912  C  CD  . ARG   B 2 449 ? 5.990   59.085  -1.378  1.00 90.30  ? 753  ARG   B CD  1 
ATOM   5913  N  NE  . ARG   B 2 449 ? 6.195   57.792  -2.032  1.00 94.95  ? 753  ARG   B NE  1 
ATOM   5914  C  CZ  . ARG   B 2 449 ? 6.173   56.615  -1.413  1.00 93.58  ? 753  ARG   B CZ  1 
ATOM   5915  N  NH1 . ARG   B 2 449 ? 5.848   56.515  -0.132  1.00 90.05  ? 753  ARG   B NH1 1 
ATOM   5916  N  NH2 . ARG   B 2 449 ? 6.510   55.514  -2.093  1.00 92.84  ? 753  ARG   B NH2 1 
ATOM   5917  N  N   . PRO   B 2 450 ? 1.869   61.717  -1.316  1.00 91.04  ? 754  PRO   B N   1 
ATOM   5918  C  CA  . PRO   B 2 450 ? 1.872   63.007  -2.016  1.00 91.80  ? 754  PRO   B CA  1 
ATOM   5919  C  C   . PRO   B 2 450 ? 3.295   63.335  -2.431  1.00 90.72  ? 754  PRO   B C   1 
ATOM   5920  O  O   . PRO   B 2 450 ? 4.214   63.296  -1.621  1.00 94.32  ? 754  PRO   B O   1 
ATOM   5921  C  CB  . PRO   B 2 450 ? 1.334   63.984  -0.970  1.00 95.95  ? 754  PRO   B CB  1 
ATOM   5922  C  CG  . PRO   B 2 450 ? 0.662   63.083  0.071   1.00 99.95  ? 754  PRO   B CG  1 
ATOM   5923  C  CD  . PRO   B 2 450 ? 1.538   61.869  0.102   1.00 96.01  ? 754  PRO   B CD  1 
ATOM   5924  N  N   . SER   B 2 451 ? 3.482   63.567  -3.706  1.00 91.90  ? 755  SER   B N   1 
ATOM   5925  C  CA  . SER   B 2 451 ? 4.790   63.759  -4.293  1.00 86.38  ? 755  SER   B CA  1 
ATOM   5926  C  C   . SER   B 2 451 ? 4.928   65.221  -4.684  1.00 89.12  ? 755  SER   B C   1 
ATOM   5927  O  O   . SER   B 2 451 ? 4.031   66.027  -4.449  1.00 95.29  ? 755  SER   B O   1 
ATOM   5928  C  CB  . SER   B 2 451 ? 4.948   62.830  -5.497  1.00 88.48  ? 755  SER   B CB  1 
ATOM   5929  O  OG  . SER   B 2 451 ? 4.684   61.470  -5.150  1.00 94.63  ? 755  SER   B OG  1 
ATOM   5930  N  N   . ALA   B 2 452 ? 6.057   65.558  -5.305  1.00 88.57  ? 756  ALA   B N   1 
ATOM   5931  C  CA  . ALA   B 2 452 ? 6.257   66.917  -5.806  1.00 89.90  ? 756  ALA   B CA  1 
ATOM   5932  C  C   . ALA   B 2 452 ? 5.245   67.272  -6.884  1.00 94.89  ? 756  ALA   B C   1 
ATOM   5933  O  O   . ALA   B 2 452 ? 4.675   68.364  -6.871  1.00 102.05 ? 756  ALA   B O   1 
ATOM   5934  C  CB  . ALA   B 2 452 ? 7.670   67.081  -6.351  1.00 80.88  ? 756  ALA   B CB  1 
ATOM   5935  N  N   . SER   B 2 453 ? 5.036   66.377  -7.847  1.00 95.16  ? 757  SER   B N   1 
ATOM   5936  C  CA  . SER   B 2 453 ? 4.033   66.599  -8.884  1.00 97.81  ? 757  SER   B CA  1 
ATOM   5937  C  C   . SER   B 2 453 ? 2.646   66.811  -8.296  1.00 102.29 ? 757  SER   B C   1 
ATOM   5938  O  O   . SER   B 2 453 ? 1.909   67.711  -8.717  1.00 104.87 ? 757  SER   B O   1 
ATOM   5939  C  CB  . SER   B 2 453 ? 3.980   65.402  -9.810  1.00 97.39  ? 757  SER   B CB  1 
ATOM   5940  O  OG  . SER   B 2 453 ? 3.421   64.303  -9.113  1.00 99.32  ? 757  SER   B OG  1 
ATOM   5941  N  N   . THR   B 2 454 ? 2.246   65.951  -7.355  1.00 101.65 ? 758  THR   B N   1 
ATOM   5942  C  CA  . THR   B 2 454 ? 0.905   66.081  -6.796  1.00 104.25 ? 758  THR   B CA  1 
ATOM   5943  C  C   . THR   B 2 454 ? 0.777   67.369  -5.991  1.00 104.52 ? 758  THR   B C   1 
ATOM   5944  O  O   . THR   B 2 454 ? -0.278  68.014  -5.996  1.00 106.11 ? 758  THR   B O   1 
ATOM   5945  C  CB  . THR   B 2 454 ? 0.564   64.862  -5.940  1.00 102.62 ? 758  THR   B CB  1 
ATOM   5946  O  OG1 . THR   B 2 454 ? 1.156   65.005  -4.647  1.00 100.70 ? 758  THR   B OG1 1 
ATOM   5947  C  CG2 . THR   B 2 454 ? 1.101   63.601  -6.588  1.00 100.30 ? 758  THR   B CG2 1 
ATOM   5948  N  N   . GLN   B 2 455 ? 1.853   67.778  -5.325  1.00 100.59 ? 759  GLN   B N   1 
ATOM   5949  C  CA  . GLN   B 2 455 ? 1.863   68.981  -4.497  1.00 100.86 ? 759  GLN   B CA  1 
ATOM   5950  C  C   . GLN   B 2 455 ? 2.502   70.172  -5.219  1.00 102.36 ? 759  GLN   B C   1 
ATOM   5951  O  O   . GLN   B 2 455 ? 3.227   70.941  -4.593  1.00 106.48 ? 759  GLN   B O   1 
ATOM   5952  C  CB  . GLN   B 2 455 ? 2.579   68.713  -3.165  1.00 102.72 ? 759  GLN   B CB  1 
ATOM   5953  C  CG  . GLN   B 2 455 ? 2.108   67.497  -2.336  1.00 103.46 ? 759  GLN   B CG  1 
ATOM   5954  C  CD  . GLN   B 2 455 ? 0.609   67.504  -2.003  1.00 107.01 ? 759  GLN   B CD  1 
ATOM   5955  O  OE1 . GLN   B 2 455 ? 0.195   67.979  -0.941  1.00 105.97 ? 759  GLN   B OE1 1 
ATOM   5956  N  NE2 . GLN   B 2 455 ? -0.203  66.933  -2.899  1.00 109.00 ? 759  GLN   B NE2 1 
ATOM   5957  N  N   . ALA   B 2 456 ? 2.279   70.380  -6.516  1.00 99.60  ? 760  ALA   B N   1 
ATOM   5958  C  CA  . ALA   B 2 456 ? 2.789   71.598  -7.135  1.00 96.08  ? 760  ALA   B CA  1 
ATOM   5959  C  C   . ALA   B 2 456 ? 1.730   72.683  -7.046  1.00 98.26  ? 760  ALA   B C   1 
ATOM   5960  O  O   . ALA   B 2 456 ? 0.601   72.440  -6.628  1.00 104.83 ? 760  ALA   B O   1 
ATOM   5961  C  CB  . ALA   B 2 456 ? 3.194   71.371  -8.587  1.00 95.44  ? 760  ALA   B CB  1 
ATOM   5962  N  N   . LEU   B 2 457 ? 2.097   73.901  -7.438  1.00 96.28  ? 761  LEU   B N   1 
ATOM   5963  C  CA  . LEU   B 2 457 ? 1.150   75.005  -7.320  1.00 91.93  ? 761  LEU   B CA  1 
ATOM   5964  C  C   . LEU   B 2 457 ? 0.375   75.229  -8.607  1.00 93.19  ? 761  LEU   B C   1 
ATOM   5965  O  O   . LEU   B 2 457 ? -0.812  75.559  -8.561  1.00 97.88  ? 761  LEU   B O   1 
ATOM   5966  C  CB  . LEU   B 2 457 ? 1.868   76.289  -6.915  1.00 94.81  ? 761  LEU   B CB  1 
ATOM   5967  C  CG  . LEU   B 2 457 ? 3.088   76.130  -5.998  1.00 100.69 ? 761  LEU   B CG  1 
ATOM   5968  C  CD1 . LEU   B 2 457 ? 3.820   77.458  -5.860  1.00 103.70 ? 761  LEU   B CD1 1 
ATOM   5969  C  CD2 . LEU   B 2 457 ? 2.761   75.524  -4.613  1.00 94.50  ? 761  LEU   B CD2 1 
ATOM   5970  N  N   . SER   B 2 458 ? 1.022   75.072  -9.756  1.00 93.19  ? 762  SER   B N   1 
ATOM   5971  C  CA  . SER   B 2 458 ? 0.344   75.058  -11.042 1.00 93.42  ? 762  SER   B CA  1 
ATOM   5972  C  C   . SER   B 2 458 ? 0.638   73.730  -11.714 1.00 91.24  ? 762  SER   B C   1 
ATOM   5973  O  O   . SER   B 2 458 ? 1.614   73.057  -11.386 1.00 94.22  ? 762  SER   B O   1 
ATOM   5974  C  CB  . SER   B 2 458 ? 0.771   76.237  -11.938 1.00 97.07  ? 762  SER   B CB  1 
ATOM   5975  O  OG  . SER   B 2 458 ? 2.152   76.535  -11.820 1.00 100.10 ? 762  SER   B OG  1 
ATOM   5976  N  N   . SER   B 2 459 ? -0.225  73.334  -12.633 1.00 89.63  ? 763  SER   B N   1 
ATOM   5977  C  CA  . SER   B 2 459 ? -0.203  71.958  -13.104 1.00 90.98  ? 763  SER   B CA  1 
ATOM   5978  C  C   . SER   B 2 459 ? -0.825  71.889  -14.485 1.00 93.19  ? 763  SER   B C   1 
ATOM   5979  O  O   . SER   B 2 459 ? -2.039  72.066  -14.616 1.00 98.62  ? 763  SER   B O   1 
ATOM   5980  C  CB  . SER   B 2 459 ? -0.976  71.062  -12.138 1.00 97.24  ? 763  SER   B CB  1 
ATOM   5981  O  OG  . SER   B 2 459 ? -2.371  71.135  -12.391 1.00 99.99  ? 763  SER   B OG  1 
ATOM   5982  N  N   . SER   B 2 460 ? -0.022  71.607  -15.503 1.00 92.27  ? 764  SER   B N   1 
ATOM   5983  C  CA  . SER   B 2 460 ? -0.557  71.343  -16.831 1.00 94.01  ? 764  SER   B CA  1 
ATOM   5984  C  C   . SER   B 2 460 ? -0.553  69.847  -17.124 1.00 94.68  ? 764  SER   B C   1 
ATOM   5985  O  O   . SER   B 2 460 ? 0.253   69.089  -16.575 1.00 90.54  ? 764  SER   B O   1 
ATOM   5986  C  CB  . SER   B 2 460 ? 0.226   72.088  -17.920 1.00 95.47  ? 764  SER   B CB  1 
ATOM   5987  O  OG  . SER   B 2 460 ? 1.622   71.963  -17.741 1.00 96.44  ? 764  SER   B OG  1 
ATOM   5988  N  N   . VAL   B 2 461 ? -1.496  69.426  -17.974 1.00 98.93  ? 765  VAL   B N   1 
ATOM   5989  C  CA  . VAL   B 2 461 ? -1.505  68.092  -18.572 1.00 98.85  ? 765  VAL   B CA  1 
ATOM   5990  C  C   . VAL   B 2 461 ? -1.389  68.264  -20.085 1.00 101.23 ? 765  VAL   B C   1 
ATOM   5991  O  O   . VAL   B 2 461 ? -1.824  69.280  -20.642 1.00 102.01 ? 765  VAL   B O   1 
ATOM   5992  C  CB  . VAL   B 2 461 ? -2.766  67.274  -18.192 1.00 98.97  ? 765  VAL   B CB  1 
ATOM   5993  C  CG1 . VAL   B 2 461 ? -2.626  65.817  -18.624 1.00 97.91  ? 765  VAL   B CG1 1 
ATOM   5994  C  CG2 . VAL   B 2 461 ? -3.016  67.341  -16.699 1.00 95.86  ? 765  VAL   B CG2 1 
ATOM   5995  N  N   . SER   B 2 462 ? -0.774  67.276  -20.746 1.00 103.46 ? 766  SER   B N   1 
ATOM   5996  C  CA  . SER   B 2 462 ? -0.589  67.299  -22.191 1.00 103.30 ? 766  SER   B CA  1 
ATOM   5997  C  C   . SER   B 2 462 ? -1.916  67.014  -22.887 1.00 107.75 ? 766  SER   B C   1 
ATOM   5998  O  O   . SER   B 2 462 ? -2.824  66.398  -22.321 1.00 105.09 ? 766  SER   B O   1 
ATOM   5999  C  CB  . SER   B 2 462 ? 0.472   66.278  -22.607 1.00 95.48  ? 766  SER   B CB  1 
ATOM   6000  O  OG  . SER   B 2 462 ? 0.947   66.502  -23.919 1.00 97.16  ? 766  SER   B OG  1 
ATOM   6001  N  N   . SER   B 2 463 ? -2.037  67.489  -24.125 1.00 109.39 ? 767  SER   B N   1 
ATOM   6002  C  CA  . SER   B 2 463 ? -3.218  67.153  -24.924 1.00 116.17 ? 767  SER   B CA  1 
ATOM   6003  C  C   . SER   B 2 463 ? -2.794  67.141  -26.391 1.00 124.07 ? 767  SER   B C   1 
ATOM   6004  O  O   . SER   B 2 463 ? -2.863  68.164  -27.075 1.00 133.20 ? 767  SER   B O   1 
ATOM   6005  C  CB  . SER   B 2 463 ? -4.357  68.127  -24.682 1.00 119.52 ? 767  SER   B CB  1 
ATOM   6006  O  OG  . SER   B 2 463 ? -5.446  67.809  -25.536 1.00 128.87 ? 767  SER   B OG  1 
ATOM   6007  N  N   . SER   B 2 464 ? -2.349  65.983  -26.863 1.00 130.98 ? 768  SER   B N   1 
ATOM   6008  C  CA  . SER   B 2 464 ? -1.869  65.899  -28.235 1.00 140.27 ? 768  SER   B CA  1 
ATOM   6009  C  C   . SER   B 2 464 ? -2.781  65.103  -29.151 1.00 150.78 ? 768  SER   B C   1 
ATOM   6010  O  O   . SER   B 2 464 ? -2.930  65.471  -30.320 1.00 156.95 ? 768  SER   B O   1 
ATOM   6011  C  CB  . SER   B 2 464 ? -0.450  65.309  -28.284 1.00 137.61 ? 768  SER   B CB  1 
ATOM   6012  O  OG  . SER   B 2 464 ? 0.514   66.265  -27.834 1.00 133.33 ? 768  SER   B OG  1 
ATOM   6013  N  N   . LYS   B 2 465 ? -3.391  64.019  -28.660 1.00 151.55 ? 769  LYS   B N   1 
ATOM   6014  C  CA  . LYS   B 2 465 ? -4.192  63.108  -29.484 1.00 154.90 ? 769  LYS   B CA  1 
ATOM   6015  C  C   . LYS   B 2 465 ? -3.342  62.473  -30.585 1.00 158.87 ? 769  LYS   B C   1 
ATOM   6016  O  O   . LYS   B 2 465 ? -3.851  61.686  -31.392 1.00 158.51 ? 769  LYS   B O   1 
ATOM   6017  C  CB  . LYS   B 2 465 ? -5.411  63.826  -30.089 1.00 149.52 ? 769  LYS   B CB  1 
ATOM   6018  N  N   . LEU   B 2 466 ? -2.042  62.802  -30.603 1.00 168.07 ? 770  LEU   B N   1 
ATOM   6019  C  CA  . LEU   B 2 466 ? -1.132  62.321  -31.641 1.00 163.74 ? 770  LEU   B CA  1 
ATOM   6020  C  C   . LEU   B 2 466 ? -1.157  60.805  -31.731 1.00 162.12 ? 770  LEU   B C   1 
ATOM   6021  O  O   . LEU   B 2 466 ? -1.188  60.233  -32.829 1.00 163.64 ? 770  LEU   B O   1 
ATOM   6022  C  CB  . LEU   B 2 466 ? 0.286   62.813  -31.347 1.00 157.40 ? 770  LEU   B CB  1 
ATOM   6023  C  CG  . LEU   B 2 466 ? 0.790   64.129  -31.956 1.00 158.22 ? 770  LEU   B CG  1 
ATOM   6024  C  CD1 . LEU   B 2 466 ? -0.263  65.217  -31.919 1.00 160.93 ? 770  LEU   B CD1 1 
ATOM   6025  C  CD2 . LEU   B 2 466 ? 2.032   64.613  -31.229 1.00 154.73 ? 770  LEU   B CD2 1 
ATOM   6026  N  N   . PHE   B 2 467 ? -1.162  60.140  -30.585 1.00 152.79 ? 771  PHE   B N   1 
ATOM   6027  C  CA  . PHE   B 2 467 ? -1.166  58.688  -30.513 1.00 154.04 ? 771  PHE   B CA  1 
ATOM   6028  C  C   . PHE   B 2 467 ? -2.409  58.272  -29.740 1.00 162.14 ? 771  PHE   B C   1 
ATOM   6029  O  O   . PHE   B 2 467 ? -2.635  58.757  -28.628 1.00 163.77 ? 771  PHE   B O   1 
ATOM   6030  C  CB  . PHE   B 2 467 ? 0.120   58.187  -29.854 1.00 139.87 ? 771  PHE   B CB  1 
ATOM   6031  C  CG  . PHE   B 2 467 ? 1.331   59.028  -30.180 1.00 134.03 ? 771  PHE   B CG  1 
ATOM   6032  C  CD1 . PHE   B 2 467 ? 2.076   58.795  -31.333 1.00 129.84 ? 771  PHE   B CD1 1 
ATOM   6033  C  CD2 . PHE   B 2 467 ? 1.714   60.065  -29.342 1.00 131.53 ? 771  PHE   B CD2 1 
ATOM   6034  C  CE1 . PHE   B 2 467 ? 3.191   59.571  -31.632 1.00 120.32 ? 771  PHE   B CE1 1 
ATOM   6035  C  CE2 . PHE   B 2 467 ? 2.823   60.843  -29.634 1.00 124.02 ? 771  PHE   B CE2 1 
ATOM   6036  C  CZ  . PHE   B 2 467 ? 3.563   60.593  -30.779 1.00 119.00 ? 771  PHE   B CZ  1 
ATOM   6037  N  N   . SER   B 2 468 ? -3.223  57.393  -30.339 1.00 175.33 ? 772  SER   B N   1 
ATOM   6038  C  CA  . SER   B 2 468 ? -4.536  57.086  -29.772 1.00 175.10 ? 772  SER   B CA  1 
ATOM   6039  C  C   . SER   B 2 468 ? -4.414  56.410  -28.411 1.00 175.79 ? 772  SER   B C   1 
ATOM   6040  O  O   . SER   B 2 468 ? -5.074  56.809  -27.442 1.00 176.87 ? 772  SER   B O   1 
ATOM   6041  C  CB  . SER   B 2 468 ? -5.338  56.202  -30.724 1.00 174.98 ? 772  SER   B CB  1 
ATOM   6042  O  OG  . SER   B 2 468 ? -6.625  55.933  -30.188 1.00 174.64 ? 772  SER   B OG  1 
ATOM   6043  N  N   . SER   B 2 469 ? -3.588  55.369  -28.326 1.00 163.22 ? 773  SER   B N   1 
ATOM   6044  C  CA  . SER   B 2 469 ? -3.418  54.615  -27.086 1.00 157.46 ? 773  SER   B CA  1 
ATOM   6045  C  C   . SER   B 2 469 ? -2.071  54.909  -26.416 1.00 143.27 ? 773  SER   B C   1 
ATOM   6046  O  O   . SER   B 2 469 ? -1.893  55.935  -25.749 1.00 136.93 ? 773  SER   B O   1 
ATOM   6047  C  CB  . SER   B 2 469 ? -3.554  53.114  -27.359 1.00 154.60 ? 773  SER   B CB  1 
ATOM   6048  O  OG  . SER   B 2 469 ? -4.823  52.805  -27.909 1.00 153.77 ? 773  SER   B OG  1 
ATOM   6049  N  N   . THR   B 2 476 ? -3.509  46.387  -15.976 1.00 121.42 ? 780  THR   B N   1 
ATOM   6050  C  CA  . THR   B 2 476 ? -4.710  45.530  -15.934 1.00 125.28 ? 780  THR   B CA  1 
ATOM   6051  C  C   . THR   B 2 476 ? -4.981  45.135  -14.501 1.00 128.19 ? 780  THR   B C   1 
ATOM   6052  O  O   . THR   B 2 476 ? -6.079  45.451  -14.001 1.00 130.90 ? 780  THR   B O   1 
ATOM   6053  C  CB  . THR   B 2 476 ? -4.502  44.315  -16.833 1.00 131.22 ? 780  THR   B CB  1 
ATOM   6054  O  OG1 . THR   B 2 476 ? -4.622  44.821  -18.158 1.00 130.37 ? 780  THR   B OG1 1 
ATOM   6055  C  CG2 . THR   B 2 476 ? -5.540  43.231  -16.608 1.00 133.25 ? 780  THR   B CG2 1 
ATOM   6056  N  N   . SER   B 2 477 ? -4.022  44.480  -13.847 1.00 120.60 ? 781  SER   B N   1 
ATOM   6057  C  CA  . SER   B 2 477 ? -4.252  44.001  -12.460 1.00 120.79 ? 781  SER   B CA  1 
ATOM   6058  C  C   . SER   B 2 477 ? -4.548  45.193  -11.547 1.00 116.95 ? 781  SER   B C   1 
ATOM   6059  O  O   . SER   B 2 477 ? -4.064  46.302  -11.841 1.00 114.79 ? 781  SER   B O   1 
ATOM   6060  C  CB  . SER   B 2 477 ? -3.087  43.211  -11.945 1.00 123.27 ? 781  SER   B CB  1 
ATOM   6061  O  OG  . SER   B 2 477 ? -3.313  42.805  -10.603 1.00 121.53 ? 781  SER   B OG  1 
ATOM   6062  N  N   . PHE   B 2 478 ? -5.270  44.959  -10.452 1.00 116.49 ? 782  PHE   B N   1 
ATOM   6063  C  CA  . PHE   B 2 478 ? -5.677  46.093  -9.581  1.00 117.01 ? 782  PHE   B CA  1 
ATOM   6064  C  C   . PHE   B 2 478 ? -4.573  46.388  -8.572  1.00 116.61 ? 782  PHE   B C   1 
ATOM   6065  O  O   . PHE   B 2 478 ? -4.856  47.011  -7.530  1.00 114.21 ? 782  PHE   B O   1 
ATOM   6066  C  CB  . PHE   B 2 478 ? -7.043  45.798  -8.954  1.00 109.41 ? 782  PHE   B CB  1 
ATOM   6067  C  CG  . PHE   B 2 478 ? -8.179  46.468  -9.711  1.00 106.73 ? 782  PHE   B CG  1 
ATOM   6068  C  CD1 . PHE   B 2 478 ? -7.935  47.142  -10.901 1.00 120.01 ? 782  PHE   B CD1 1 
ATOM   6069  C  CD2 . PHE   B 2 478 ? -9.481  46.426  -9.233  1.00 109.02 ? 782  PHE   B CD2 1 
ATOM   6070  C  CE1 . PHE   B 2 478 ? -8.965  47.753  -11.594 1.00 125.35 ? 782  PHE   B CE1 1 
ATOM   6071  C  CE2 . PHE   B 2 478 ? -10.508 47.038  -9.932  1.00 116.76 ? 782  PHE   B CE2 1 
ATOM   6072  C  CZ  . PHE   B 2 478 ? -10.249 47.699  -11.108 1.00 124.37 ? 782  PHE   B CZ  1 
ATOM   6073  N  N   . GLY   B 2 479 ? -3.346  45.967  -8.870  1.00 111.14 ? 783  GLY   B N   1 
ATOM   6074  C  CA  . GLY   B 2 479 ? -2.205  46.294  -7.995  1.00 109.76 ? 783  GLY   B CA  1 
ATOM   6075  C  C   . GLY   B 2 479 ? -1.018  46.644  -8.858  1.00 110.53 ? 783  GLY   B C   1 
ATOM   6076  O  O   . GLY   B 2 479 ? 0.044   46.988  -8.304  1.00 108.49 ? 783  GLY   B O   1 
ATOM   6077  N  N   . GLU   B 2 480 ? -1.198  46.575  -10.174 1.00 110.08 ? 784  GLU   B N   1 
ATOM   6078  C  CA  . GLU   B 2 480 ? -0.101  46.823  -11.097 1.00 106.53 ? 784  GLU   B CA  1 
ATOM   6079  C  C   . GLU   B 2 480 ? 0.350   48.270  -10.996 1.00 103.53 ? 784  GLU   B C   1 
ATOM   6080  O  O   . GLU   B 2 480 ? -0.469  49.187  -10.930 1.00 105.71 ? 784  GLU   B O   1 
ATOM   6081  C  CB  . GLU   B 2 480 ? -0.514  46.512  -12.533 1.00 110.71 ? 784  GLU   B CB  1 
ATOM   6082  C  CG  . GLU   B 2 480 ? -0.287  45.082  -13.005 1.00 115.01 ? 784  GLU   B CG  1 
ATOM   6083  C  CD  . GLU   B 2 480 ? -0.399  44.969  -14.522 1.00 125.22 ? 784  GLU   B CD  1 
ATOM   6084  O  OE1 . GLU   B 2 480 ? 0.076   45.901  -15.221 1.00 125.25 ? 784  GLU   B OE1 1 
ATOM   6085  O  OE2 . GLU   B 2 480 ? -0.976  43.964  -15.013 1.00 129.86 ? 784  GLU   B OE2 1 
ATOM   6086  N  N   . GLU   B 2 481 ? 1.664   48.466  -10.986 1.00 89.40  ? 785  GLU   B N   1 
ATOM   6087  C  CA  . GLU   B 2 481 ? 2.227   49.798  -10.860 1.00 82.76  ? 785  GLU   B CA  1 
ATOM   6088  C  C   . GLU   B 2 481 ? 2.289   50.478  -12.219 1.00 80.88  ? 785  GLU   B C   1 
ATOM   6089  O  O   . GLU   B 2 481 ? 2.601   49.850  -13.233 1.00 82.51  ? 785  GLU   B O   1 
ATOM   6090  C  CB  . GLU   B 2 481 ? 3.625   49.722  -10.240 1.00 82.50  ? 785  GLU   B CB  1 
ATOM   6091  C  CG  . GLU   B 2 481 ? 3.640   49.165  -8.813  1.00 91.28  ? 785  GLU   B CG  1 
ATOM   6092  C  CD  . GLU   B 2 481 ? 5.053   48.977  -8.230  1.00 93.19  ? 785  GLU   B CD  1 
ATOM   6093  O  OE1 . GLU   B 2 481 ? 6.045   49.057  -8.997  1.00 91.33  ? 785  GLU   B OE1 1 
ATOM   6094  O  OE2 . GLU   B 2 481 ? 5.170   48.747  -6.998  1.00 90.95  ? 785  GLU   B OE2 1 
ATOM   6095  N  N   . VAL   B 2 482 ? 1.960   51.769  -12.240 1.00 78.71  ? 786  VAL   B N   1 
ATOM   6096  C  CA  . VAL   B 2 482 ? 2.196   52.608  -13.404 1.00 75.15  ? 786  VAL   B CA  1 
ATOM   6097  C  C   . VAL   B 2 482 ? 3.075   53.794  -13.017 1.00 75.87  ? 786  VAL   B C   1 
ATOM   6098  O  O   . VAL   B 2 482 ? 3.112   54.229  -11.863 1.00 81.02  ? 786  VAL   B O   1 
ATOM   6099  C  CB  . VAL   B 2 482 ? 0.892   53.103  -14.046 1.00 75.47  ? 786  VAL   B CB  1 
ATOM   6100  C  CG1 . VAL   B 2 482 ? 0.298   54.263  -13.261 1.00 81.13  ? 786  VAL   B CG1 1 
ATOM   6101  C  CG2 . VAL   B 2 482 ? 1.160   53.497  -15.482 1.00 78.99  ? 786  VAL   B CG2 1 
ATOM   6102  N  N   . GLU   B 2 483 ? 3.796   54.307  -14.009 1.00 75.12  ? 787  GLU   B N   1 
ATOM   6103  C  CA  . GLU   B 2 483 ? 4.669   55.463  -13.876 1.00 75.18  ? 787  GLU   B CA  1 
ATOM   6104  C  C   . GLU   B 2 483 ? 3.954   56.681  -14.431 1.00 75.49  ? 787  GLU   B C   1 
ATOM   6105  O  O   . GLU   B 2 483 ? 3.217   56.579  -15.415 1.00 77.14  ? 787  GLU   B O   1 
ATOM   6106  C  CB  . GLU   B 2 483 ? 5.963   55.230  -14.655 1.00 74.96  ? 787  GLU   B CB  1 
ATOM   6107  C  CG  . GLU   B 2 483 ? 7.230   55.687  -13.983 1.00 77.67  ? 787  GLU   B CG  1 
ATOM   6108  C  CD  . GLU   B 2 483 ? 8.434   54.869  -14.426 1.00 80.94  ? 787  GLU   B CD  1 
ATOM   6109  O  OE1 . GLU   B 2 483 ? 8.537   53.694  -14.000 1.00 82.41  ? 787  GLU   B OE1 1 
ATOM   6110  O  OE2 . GLU   B 2 483 ? 9.261   55.388  -15.214 1.00 80.15  ? 787  GLU   B OE2 1 
ATOM   6111  N  N   . VAL   B 2 484 ? 4.179   57.839  -13.818 1.00 75.68  ? 788  VAL   B N   1 
ATOM   6112  C  CA  . VAL   B 2 484 ? 3.602   59.100  -14.274 1.00 75.99  ? 788  VAL   B CA  1 
ATOM   6113  C  C   . VAL   B 2 484 ? 4.735   60.116  -14.382 1.00 76.85  ? 788  VAL   B C   1 
ATOM   6114  O  O   . VAL   B 2 484 ? 5.219   60.644  -13.368 1.00 76.22  ? 788  VAL   B O   1 
ATOM   6115  C  CB  . VAL   B 2 484 ? 2.480   59.592  -13.354 1.00 76.27  ? 788  VAL   B CB  1 
ATOM   6116  C  CG1 . VAL   B 2 484 ? 1.878   60.879  -13.888 1.00 83.75  ? 788  VAL   B CG1 1 
ATOM   6117  C  CG2 . VAL   B 2 484 ? 1.420   58.528  -13.238 1.00 76.46  ? 788  VAL   B CG2 1 
ATOM   6118  N  N   . HIS   B 2 485 ? 5.154   60.374  -15.615 1.00 79.26  ? 789  HIS   B N   1 
ATOM   6119  C  CA  . HIS   B 2 485 ? 6.221   61.313  -15.931 1.00 80.20  ? 789  HIS   B CA  1 
ATOM   6120  C  C   . HIS   B 2 485 ? 5.691   62.733  -16.078 1.00 83.21  ? 789  HIS   B C   1 
ATOM   6121  O  O   . HIS   B 2 485 ? 4.689   62.969  -16.764 1.00 84.06  ? 789  HIS   B O   1 
ATOM   6122  C  CB  . HIS   B 2 485 ? 6.910   60.922  -17.235 1.00 82.48  ? 789  HIS   B CB  1 
ATOM   6123  C  CG  . HIS   B 2 485 ? 7.797   59.733  -17.111 1.00 79.54  ? 789  HIS   B CG  1 
ATOM   6124  N  ND1 . HIS   B 2 485 ? 9.147   59.788  -17.378 1.00 79.91  ? 789  HIS   B ND1 1 
ATOM   6125  C  CD2 . HIS   B 2 485 ? 7.530   58.459  -16.742 1.00 79.06  ? 789  HIS   B CD2 1 
ATOM   6126  C  CE1 . HIS   B 2 485 ? 9.676   58.596  -17.177 1.00 84.36  ? 789  HIS   B CE1 1 
ATOM   6127  N  NE2 . HIS   B 2 485 ? 8.717   57.772  -16.792 1.00 83.74  ? 789  HIS   B NE2 1 
ATOM   6128  N  N   . ASN   B 2 486 ? 6.404   63.685  -15.471 1.00 85.55  ? 790  ASN   B N   1 
ATOM   6129  C  CA  . ASN   B 2 486 ? 6.010   65.083  -15.557 1.00 86.57  ? 790  ASN   B CA  1 
ATOM   6130  C  C   . ASN   B 2 486 ? 7.249   65.965  -15.432 1.00 80.91  ? 790  ASN   B C   1 
ATOM   6131  O  O   . ASN   B 2 486 ? 8.292   65.555  -14.916 1.00 78.40  ? 790  ASN   B O   1 
ATOM   6132  C  CB  . ASN   B 2 486 ? 4.930   65.400  -14.508 1.00 82.97  ? 790  ASN   B CB  1 
ATOM   6133  C  CG  . ASN   B 2 486 ? 5.217   64.759  -13.209 1.00 88.78  ? 790  ASN   B CG  1 
ATOM   6134  O  OD1 . ASN   B 2 486 ? 5.102   63.541  -13.051 1.00 88.42  ? 790  ASN   B OD1 1 
ATOM   6135  N  ND2 . ASN   B 2 486 ? 5.641   65.559  -12.260 1.00 95.05  ? 790  ASN   B ND2 1 
ATOM   6136  N  N   . LEU   B 2 487 ? 7.147   67.161  -15.996 1.00 84.28  ? 791  LEU   B N   1 
ATOM   6137  C  CA  . LEU   B 2 487 ? 8.195   68.156  -15.916 1.00 83.50  ? 791  LEU   B CA  1 
ATOM   6138  C  C   . LEU   B 2 487 ? 7.910   69.027  -14.712 1.00 87.47  ? 791  LEU   B C   1 
ATOM   6139  O  O   . LEU   B 2 487 ? 6.757   69.398  -14.467 1.00 85.97  ? 791  LEU   B O   1 
ATOM   6140  C  CB  . LEU   B 2 487 ? 8.252   69.012  -17.176 1.00 85.11  ? 791  LEU   B CB  1 
ATOM   6141  C  CG  . LEU   B 2 487 ? 9.133   70.252  -17.091 1.00 81.77  ? 791  LEU   B CG  1 
ATOM   6142  C  CD1 . LEU   B 2 487 ? 10.566  69.893  -16.799 1.00 80.50  ? 791  LEU   B CD1 1 
ATOM   6143  C  CD2 . LEU   B 2 487 ? 9.055   70.934  -18.402 1.00 88.93  ? 791  LEU   B CD2 1 
ATOM   6144  N  N   . LEU   B 2 488 ? 8.951   69.324  -13.953 1.00 91.40  ? 792  LEU   B N   1 
ATOM   6145  C  CA  . LEU   B 2 488 ? 8.855   70.195  -12.796 1.00 90.21  ? 792  LEU   B CA  1 
ATOM   6146  C  C   . LEU   B 2 488 ? 9.614   71.473  -13.089 1.00 88.18  ? 792  LEU   B C   1 
ATOM   6147  O  O   . LEU   B 2 488 ? 10.747  71.429  -13.579 1.00 86.21  ? 792  LEU   B O   1 
ATOM   6148  C  CB  . LEU   B 2 488 ? 9.426   69.518  -11.554 1.00 88.28  ? 792  LEU   B CB  1 
ATOM   6149  C  CG  . LEU   B 2 488 ? 8.667   68.260  -11.173 1.00 79.99  ? 792  LEU   B CG  1 
ATOM   6150  C  CD1 . LEU   B 2 488 ? 9.238   67.728  -9.900  1.00 78.05  ? 792  LEU   B CD1 1 
ATOM   6151  C  CD2 . LEU   B 2 488 ? 7.194   68.586  -11.033 1.00 83.48  ? 792  LEU   B CD2 1 
ATOM   6152  N  N   . ILE   B 2 489 ? 8.988   72.600  -12.794 1.00 93.18  ? 793  ILE   B N   1 
ATOM   6153  C  CA  . ILE   B 2 489 ? 9.640   73.895  -12.847 1.00 94.77  ? 793  ILE   B CA  1 
ATOM   6154  C  C   . ILE   B 2 489 ? 9.844   74.320  -11.403 1.00 96.07  ? 793  ILE   B C   1 
ATOM   6155  O  O   . ILE   B 2 489 ? 8.875   74.632  -10.698 1.00 95.71  ? 793  ILE   B O   1 
ATOM   6156  C  CB  . ILE   B 2 489 ? 8.819   74.922  -13.628 1.00 93.45  ? 793  ILE   B CB  1 
ATOM   6157  C  CG1 . ILE   B 2 489 ? 8.168   74.274  -14.845 1.00 90.24  ? 793  ILE   B CG1 1 
ATOM   6158  C  CG2 . ILE   B 2 489 ? 9.725   76.004  -14.092 1.00 98.96  ? 793  ILE   B CG2 1 
ATOM   6159  C  CD1 . ILE   B 2 489 ? 9.134   73.956  -15.924 1.00 90.17  ? 793  ILE   B CD1 1 
ATOM   6160  N  N   . ILE   B 2 490 ? 11.093  74.297  -10.948 1.00 95.96  ? 794  ILE   B N   1 
ATOM   6161  C  CA  . ILE   B 2 490 ? 11.421  74.470  -9.537  1.00 96.52  ? 794  ILE   B CA  1 
ATOM   6162  C  C   . ILE   B 2 490 ? 12.163  75.780  -9.355  1.00 96.84  ? 794  ILE   B C   1 
ATOM   6163  O  O   . ILE   B 2 490 ? 13.142  76.046  -10.066 1.00 96.67  ? 794  ILE   B O   1 
ATOM   6164  C  CB  . ILE   B 2 490 ? 12.270  73.309  -9.001  1.00 96.57  ? 794  ILE   B CB  1 
ATOM   6165  C  CG1 . ILE   B 2 490 ? 11.711  71.983  -9.488  1.00 97.13  ? 794  ILE   B CG1 1 
ATOM   6166  C  CG2 . ILE   B 2 490 ? 12.282  73.348  -7.494  1.00 96.72  ? 794  ILE   B CG2 1 
ATOM   6167  C  CD1 . ILE   B 2 490 ? 12.590  70.826  -9.150  1.00 93.96  ? 794  ILE   B CD1 1 
ATOM   6168  N  N   . ASP   B 2 491 ? 11.726  76.571  -8.375  1.00 95.66  ? 795  ASP   B N   1 
ATOM   6169  C  CA  . ASP   B 2 491 ? 12.311  77.885  -8.169  1.00 96.85  ? 795  ASP   B CA  1 
ATOM   6170  C  C   . ASP   B 2 491 ? 13.716  77.770  -7.600  1.00 96.58  ? 795  ASP   B C   1 
ATOM   6171  O  O   . ASP   B 2 491 ? 13.985  76.927  -6.741  1.00 98.90  ? 795  ASP   B O   1 
ATOM   6172  C  CB  . ASP   B 2 491 ? 11.446  78.701  -7.232  1.00 98.75  ? 795  ASP   B CB  1 
ATOM   6173  C  CG  . ASP   B 2 491 ? 12.122  79.975  -6.818  1.00 106.23 ? 795  ASP   B CG  1 
ATOM   6174  O  OD1 . ASP   B 2 491 ? 12.590  80.705  -7.723  1.00 107.67 ? 795  ASP   B OD1 1 
ATOM   6175  O  OD2 . ASP   B 2 491 ? 12.205  80.246  -5.595  1.00 109.04 ? 795  ASP   B OD2 1 
ATOM   6176  N  N   . GLN   B 2 492 ? 14.621  78.629  -8.075  1.00 96.90  ? 796  GLN   B N   1 
ATOM   6177  C  CA  . GLN   B 2 492 ? 16.015  78.488  -7.672  1.00 97.47  ? 796  GLN   B CA  1 
ATOM   6178  C  C   . GLN   B 2 492 ? 16.304  79.038  -6.277  1.00 98.12  ? 796  GLN   B C   1 
ATOM   6179  O  O   . GLN   B 2 492 ? 17.426  78.878  -5.790  1.00 94.95  ? 796  GLN   B O   1 
ATOM   6180  C  CB  . GLN   B 2 492 ? 16.939  79.137  -8.710  1.00 96.61  ? 796  GLN   B CB  1 
ATOM   6181  C  CG  . GLN   B 2 492 ? 16.718  80.598  -8.967  1.00 99.64  ? 796  GLN   B CG  1 
ATOM   6182  C  CD  . GLN   B 2 492 ? 17.896  81.225  -9.690  1.00 102.05 ? 796  GLN   B CD  1 
ATOM   6183  O  OE1 . GLN   B 2 492 ? 18.063  81.053  -10.894 1.00 101.48 ? 796  GLN   B OE1 1 
ATOM   6184  N  NE2 . GLN   B 2 492 ? 18.752  81.911  -8.939  1.00 104.39 ? 796  GLN   B NE2 1 
ATOM   6185  N  N   . HIS   B 2 493 ? 15.322  79.631  -5.599  1.00 98.94  ? 797  HIS   B N   1 
ATOM   6186  C  CA  . HIS   B 2 493 ? 15.531  80.204  -4.274  1.00 96.78  ? 797  HIS   B CA  1 
ATOM   6187  C  C   . HIS   B 2 493 ? 14.729  79.486  -3.204  1.00 98.58  ? 797  HIS   B C   1 
ATOM   6188  O  O   . HIS   B 2 493 ? 15.292  79.089  -2.181  1.00 105.09 ? 797  HIS   B O   1 
ATOM   6189  C  CB  . HIS   B 2 493 ? 15.150  81.682  -4.255  1.00 97.28  ? 797  HIS   B CB  1 
ATOM   6190  C  CG  . HIS   B 2 493 ? 15.734  82.469  -5.375  1.00 95.65  ? 797  HIS   B CG  1 
ATOM   6191  N  ND1 . HIS   B 2 493 ? 14.998  82.839  -6.479  1.00 96.91  ? 797  HIS   B ND1 1 
ATOM   6192  C  CD2 . HIS   B 2 493 ? 16.980  82.962  -5.562  1.00 95.06  ? 797  HIS   B CD2 1 
ATOM   6193  C  CE1 . HIS   B 2 493 ? 15.768  83.528  -7.302  1.00 102.62 ? 797  HIS   B CE1 1 
ATOM   6194  N  NE2 . HIS   B 2 493 ? 16.976  83.617  -6.768  1.00 99.82  ? 797  HIS   B NE2 1 
ATOM   6195  N  N   . THR   B 2 494 ? 13.414  79.389  -3.367  1.00 97.27  ? 798  THR   B N   1 
ATOM   6196  C  CA  . THR   B 2 494 ? 12.613  78.664  -2.397  1.00 99.83  ? 798  THR   B CA  1 
ATOM   6197  C  C   . THR   B 2 494 ? 12.647  77.161  -2.634  1.00 96.58  ? 798  THR   B C   1 
ATOM   6198  O  O   . THR   B 2 494 ? 12.409  76.394  -1.704  1.00 96.79  ? 798  THR   B O   1 
ATOM   6199  C  CB  . THR   B 2 494 ? 11.166  79.151  -2.448  1.00 102.83 ? 798  THR   B CB  1 
ATOM   6200  O  OG1 . THR   B 2 494 ? 10.538  78.635  -3.618  1.00 105.84 ? 798  THR   B OG1 1 
ATOM   6201  C  CG2 . THR   B 2 494 ? 11.130  80.644  -2.506  1.00 107.30 ? 798  THR   B CG2 1 
ATOM   6202  N  N   . PHE   B 2 495 ? 12.952  76.730  -3.854  1.00 98.15  ? 799  PHE   B N   1 
ATOM   6203  C  CA  . PHE   B 2 495 ? 12.881  75.319  -4.250  1.00 95.34  ? 799  PHE   B CA  1 
ATOM   6204  C  C   . PHE   B 2 495 ? 11.458  74.771  -4.157  1.00 94.76  ? 799  PHE   B C   1 
ATOM   6205  O  O   . PHE   B 2 495 ? 11.240  73.589  -3.880  1.00 88.55  ? 799  PHE   B O   1 
ATOM   6206  C  CB  . PHE   B 2 495 ? 13.876  74.467  -3.461  1.00 89.72  ? 799  PHE   B CB  1 
ATOM   6207  C  CG  . PHE   B 2 495 ? 15.240  74.532  -4.028  1.00 90.55  ? 799  PHE   B CG  1 
ATOM   6208  C  CD1 . PHE   B 2 495 ? 15.493  73.972  -5.267  1.00 90.37  ? 799  PHE   B CD1 1 
ATOM   6209  C  CD2 . PHE   B 2 495 ? 16.248  75.216  -3.385  1.00 96.76  ? 799  PHE   B CD2 1 
ATOM   6210  C  CE1 . PHE   B 2 495 ? 16.742  74.042  -5.852  1.00 88.72  ? 799  PHE   B CE1 1 
ATOM   6211  C  CE2 . PHE   B 2 495 ? 17.508  75.300  -3.958  1.00 101.48 ? 799  PHE   B CE2 1 
ATOM   6212  C  CZ  . PHE   B 2 495 ? 17.750  74.709  -5.210  1.00 97.88  ? 799  PHE   B CZ  1 
ATOM   6213  N  N   . GLU   B 2 496 ? 10.481  75.637  -4.419  1.00 95.98  ? 800  GLU   B N   1 
ATOM   6214  C  CA  . GLU   B 2 496 ? 9.105   75.186  -4.542  1.00 97.12  ? 800  GLU   B CA  1 
ATOM   6215  C  C   . GLU   B 2 496 ? 8.862   74.551  -5.899  1.00 100.12 ? 800  GLU   B C   1 
ATOM   6216  O  O   . GLU   B 2 496 ? 9.436   74.955  -6.922  1.00 99.10  ? 800  GLU   B O   1 
ATOM   6217  C  CB  . GLU   B 2 496 ? 8.119   76.337  -4.365  1.00 100.51 ? 800  GLU   B CB  1 
ATOM   6218  C  CG  . GLU   B 2 496 ? 7.783   76.693  -2.935  1.00 106.56 ? 800  GLU   B CG  1 
ATOM   6219  C  CD  . GLU   B 2 496 ? 6.656   77.726  -2.862  1.00 119.63 ? 800  GLU   B CD  1 
ATOM   6220  O  OE1 . GLU   B 2 496 ? 6.706   78.737  -3.612  1.00 118.76 ? 800  GLU   B OE1 1 
ATOM   6221  O  OE2 . GLU   B 2 496 ? 5.712   77.515  -2.064  1.00 123.55 ? 800  GLU   B OE2 1 
ATOM   6222  N  N   . VAL   B 2 497 ? 7.974   73.559  -5.895  1.00 104.72 ? 801  VAL   B N   1 
ATOM   6223  C  CA  . VAL   B 2 497 ? 7.474   72.945  -7.116  1.00 105.68 ? 801  VAL   B CA  1 
ATOM   6224  C  C   . VAL   B 2 497 ? 6.426   73.879  -7.700  1.00 107.67 ? 801  VAL   B C   1 
ATOM   6225  O  O   . VAL   B 2 497 ? 5.232   73.774  -7.374  1.00 106.76 ? 801  VAL   B O   1 
ATOM   6226  C  CB  . VAL   B 2 497 ? 6.894   71.549  -6.835  1.00 106.19 ? 801  VAL   B CB  1 
ATOM   6227  C  CG1 . VAL   B 2 497 ? 6.702   70.795  -8.132  1.00 105.80 ? 801  VAL   B CG1 1 
ATOM   6228  C  CG2 . VAL   B 2 497 ? 7.806   70.798  -5.894  1.00 104.95 ? 801  VAL   B CG2 1 
ATOM   6229  N  N   . LEU   B 2 498 ? 6.863   74.800  -8.567  1.00 102.35 ? 802  LEU   B N   1 
ATOM   6230  C  CA  . LEU   B 2 498 ? 5.996   75.805  -9.166  1.00 97.61  ? 802  LEU   B CA  1 
ATOM   6231  C  C   . LEU   B 2 498 ? 5.022   75.187  -10.162 1.00 93.38  ? 802  LEU   B C   1 
ATOM   6232  O  O   . LEU   B 2 498 ? 3.811   75.178  -9.930  1.00 94.02  ? 802  LEU   B O   1 
ATOM   6233  C  CB  . LEU   B 2 498 ? 6.828   76.891  -9.853  1.00 101.48 ? 802  LEU   B CB  1 
ATOM   6234  C  CG  . LEU   B 2 498 ? 7.989   77.476  -9.043  1.00 99.43  ? 802  LEU   B CG  1 
ATOM   6235  C  CD1 . LEU   B 2 498 ? 8.756   78.472  -9.903  1.00 100.08 ? 802  LEU   B CD1 1 
ATOM   6236  C  CD2 . LEU   B 2 498 ? 7.501   78.112  -7.745  1.00 94.48  ? 802  LEU   B CD2 1 
ATOM   6237  N  N   . HIS   B 2 499 ? 5.531   74.679  -11.279 1.00 93.23  ? 803  HIS   B N   1 
ATOM   6238  C  CA  . HIS   B 2 499 ? 4.680   74.006  -12.250 1.00 94.43  ? 803  HIS   B CA  1 
ATOM   6239  C  C   . HIS   B 2 499 ? 4.984   72.514  -12.322 1.00 92.90  ? 803  HIS   B C   1 
ATOM   6240  O  O   . HIS   B 2 499 ? 6.086   72.053  -12.008 1.00 91.62  ? 803  HIS   B O   1 
ATOM   6241  C  CB  . HIS   B 2 499 ? 4.815   74.621  -13.650 1.00 97.27  ? 803  HIS   B CB  1 
ATOM   6242  C  CG  . HIS   B 2 499 ? 3.580   74.469  -14.493 1.00 99.63  ? 803  HIS   B CG  1 
ATOM   6243  N  ND1 . HIS   B 2 499 ? 2.629   75.459  -14.606 1.00 103.91 ? 803  HIS   B ND1 1 
ATOM   6244  C  CD2 . HIS   B 2 499 ? 3.133   73.436  -15.248 1.00 99.62  ? 803  HIS   B CD2 1 
ATOM   6245  C  CE1 . HIS   B 2 499 ? 1.656   75.047  -15.398 1.00 102.94 ? 803  HIS   B CE1 1 
ATOM   6246  N  NE2 . HIS   B 2 499 ? 1.938   73.822  -15.802 1.00 98.40  ? 803  HIS   B NE2 1 
ATOM   6247  N  N   . ALA   B 2 500 ? 3.967   71.760  -12.755 1.00 92.22  ? 804  ALA   B N   1 
ATOM   6248  C  CA  . ALA   B 2 500 ? 4.063   70.310  -12.954 1.00 90.22  ? 804  ALA   B CA  1 
ATOM   6249  C  C   . ALA   B 2 500 ? 3.245   69.957  -14.197 1.00 90.47  ? 804  ALA   B C   1 
ATOM   6250  O  O   . ALA   B 2 500 ? 2.068   69.606  -14.102 1.00 93.58  ? 804  ALA   B O   1 
ATOM   6251  C  CB  . ALA   B 2 500 ? 3.576   69.537  -11.737 1.00 92.56  ? 804  ALA   B CB  1 
ATOM   6252  N  N   . HIS   B 2 501 ? 3.884   70.047  -15.357 1.00 89.56  ? 805  HIS   B N   1 
ATOM   6253  C  CA  . HIS   B 2 501 ? 3.300   69.484  -16.565 1.00 90.32  ? 805  HIS   B CA  1 
ATOM   6254  C  C   . HIS   B 2 501 ? 3.356   67.970  -16.474 1.00 90.33  ? 805  HIS   B C   1 
ATOM   6255  O  O   . HIS   B 2 501 ? 4.443   67.409  -16.349 1.00 86.56  ? 805  HIS   B O   1 
ATOM   6256  C  CB  . HIS   B 2 501 ? 4.057   69.955  -17.798 1.00 90.72  ? 805  HIS   B CB  1 
ATOM   6257  C  CG  . HIS   B 2 501 ? 3.503   69.420  -19.077 1.00 89.23  ? 805  HIS   B CG  1 
ATOM   6258  N  ND1 . HIS   B 2 501 ? 2.190   69.610  -19.454 1.00 90.48  ? 805  HIS   B ND1 1 
ATOM   6259  C  CD2 . HIS   B 2 501 ? 4.079   68.694  -20.063 1.00 88.94  ? 805  HIS   B CD2 1 
ATOM   6260  C  CE1 . HIS   B 2 501 ? 1.982   69.029  -20.621 1.00 92.78  ? 805  HIS   B CE1 1 
ATOM   6261  N  NE2 . HIS   B 2 501 ? 3.113   68.468  -21.014 1.00 91.64  ? 805  HIS   B NE2 1 
ATOM   6262  N  N   . GLN   B 2 502 ? 2.201   67.312  -16.519 1.00 91.68  ? 806  GLN   B N   1 
ATOM   6263  C  CA  . GLN   B 2 502 ? 2.146   65.862  -16.619 1.00 89.23  ? 806  GLN   B CA  1 
ATOM   6264  C  C   . GLN   B 2 502 ? 2.064   65.456  -18.088 1.00 85.27  ? 806  GLN   B C   1 
ATOM   6265  O  O   . GLN   B 2 502 ? 1.215   65.953  -18.825 1.00 87.52  ? 806  GLN   B O   1 
ATOM   6266  C  CB  . GLN   B 2 502 ? 0.954   65.303  -15.849 1.00 91.98  ? 806  GLN   B CB  1 
ATOM   6267  C  CG  . GLN   B 2 502 ? 0.766   63.813  -16.090 1.00 93.58  ? 806  GLN   B CG  1 
ATOM   6268  C  CD  . GLN   B 2 502 ? -0.666  63.329  -15.922 1.00 93.38  ? 806  GLN   B CD  1 
ATOM   6269  O  OE1 . GLN   B 2 502 ? -1.345  63.026  -16.906 1.00 89.34  ? 806  GLN   B OE1 1 
ATOM   6270  N  NE2 . GLN   B 2 502 ? -1.118  63.217  -14.669 1.00 94.44  ? 806  GLN   B NE2 1 
ATOM   6271  N  N   . PHE   B 2 503 ? 2.942   64.554  -18.504 1.00 82.97  ? 807  PHE   B N   1 
ATOM   6272  C  CA  . PHE   B 2 503 ? 3.015   64.168  -19.904 1.00 85.19  ? 807  PHE   B CA  1 
ATOM   6273  C  C   . PHE   B 2 503 ? 1.888   63.204  -20.267 1.00 90.43  ? 807  PHE   B C   1 
ATOM   6274  O  O   . PHE   B 2 503 ? 1.008   62.890  -19.457 1.00 92.05  ? 807  PHE   B O   1 
ATOM   6275  C  CB  . PHE   B 2 503 ? 4.370   63.540  -20.207 1.00 83.27  ? 807  PHE   B CB  1 
ATOM   6276  C  CG  . PHE   B 2 503 ? 5.438   64.529  -20.454 1.00 83.20  ? 807  PHE   B CG  1 
ATOM   6277  C  CD1 . PHE   B 2 503 ? 6.171   65.031  -19.407 1.00 85.33  ? 807  PHE   B CD1 1 
ATOM   6278  C  CD2 . PHE   B 2 503 ? 5.701   64.979  -21.735 1.00 87.09  ? 807  PHE   B CD2 1 
ATOM   6279  C  CE1 . PHE   B 2 503 ? 7.174   65.972  -19.630 1.00 87.74  ? 807  PHE   B CE1 1 
ATOM   6280  C  CE2 . PHE   B 2 503 ? 6.700   65.911  -21.973 1.00 87.80  ? 807  PHE   B CE2 1 
ATOM   6281  C  CZ  . PHE   B 2 503 ? 7.438   66.414  -20.915 1.00 86.18  ? 807  PHE   B CZ  1 
ATOM   6282  N  N   . LEU   B 2 504 ? 1.957   62.686  -21.495 1.00 91.94  ? 808  LEU   B N   1 
ATOM   6283  C  CA  . LEU   B 2 504 ? 0.926   61.803  -22.025 1.00 89.72  ? 808  LEU   B CA  1 
ATOM   6284  C  C   . LEU   B 2 504 ? 0.934   60.459  -21.321 1.00 90.55  ? 808  LEU   B C   1 
ATOM   6285  O  O   . LEU   B 2 504 ? 1.907   60.071  -20.675 1.00 96.74  ? 808  LEU   B O   1 
ATOM   6286  C  CB  . LEU   B 2 504 ? 1.132   61.564  -23.515 1.00 90.54  ? 808  LEU   B CB  1 
ATOM   6287  C  CG  . LEU   B 2 504 ? 1.075   62.814  -24.382 1.00 94.81  ? 808  LEU   B CG  1 
ATOM   6288  C  CD1 . LEU   B 2 504 ? 1.612   62.487  -25.755 1.00 101.13 ? 808  LEU   B CD1 1 
ATOM   6289  C  CD2 . LEU   B 2 504 ? -0.351  63.341  -24.451 1.00 100.71 ? 808  LEU   B CD2 1 
ATOM   6290  N  N   . GLN   B 2 505 ? -0.173  59.737  -21.462 1.00 89.13  ? 809  GLN   B N   1 
ATOM   6291  C  CA  . GLN   B 2 505 ? -0.207  58.373  -20.964 1.00 90.32  ? 809  GLN   B CA  1 
ATOM   6292  C  C   . GLN   B 2 505 ? 0.609   57.465  -21.873 1.00 93.09  ? 809  GLN   B C   1 
ATOM   6293  O  O   . GLN   B 2 505 ? 0.694   57.671  -23.088 1.00 97.90  ? 809  GLN   B O   1 
ATOM   6294  C  CB  . GLN   B 2 505 ? -1.640  57.864  -20.862 1.00 93.37  ? 809  GLN   B CB  1 
ATOM   6295  C  CG  . GLN   B 2 505 ? -1.756  56.563  -20.075 1.00 101.17 ? 809  GLN   B CG  1 
ATOM   6296  C  CD  . GLN   B 2 505 ? -3.193  56.162  -19.805 1.00 107.68 ? 809  GLN   B CD  1 
ATOM   6297  O  OE1 . GLN   B 2 505 ? -4.062  56.279  -20.678 1.00 105.78 ? 809  GLN   B OE1 1 
ATOM   6298  N  NE2 . GLN   B 2 505 ? -3.455  55.690  -18.585 1.00 111.09 ? 809  GLN   B NE2 1 
ATOM   6299  N  N   . ASN   B 2 506 ? 1.230   56.459  -21.264 1.00 92.58  ? 810  ASN   B N   1 
ATOM   6300  C  CA  . ASN   B 2 506 ? 2.195   55.617  -21.954 1.00 92.66  ? 810  ASN   B CA  1 
ATOM   6301  C  C   . ASN   B 2 506 ? 3.309   56.451  -22.577 1.00 91.74  ? 810  ASN   B C   1 
ATOM   6302  O  O   . ASN   B 2 506 ? 3.896   56.064  -23.586 1.00 93.86  ? 810  ASN   B O   1 
ATOM   6303  C  CB  . ASN   B 2 506 ? 1.523   54.744  -23.016 1.00 96.66  ? 810  ASN   B CB  1 
ATOM   6304  C  CG  . ASN   B 2 506 ? 0.549   53.774  -22.422 1.00 96.85  ? 810  ASN   B CG  1 
ATOM   6305  O  OD1 . ASN   B 2 506 ? -0.158  54.097  -21.471 1.00 99.70  ? 810  ASN   B OD1 1 
ATOM   6306  N  ND2 . ASN   B 2 506 ? 0.519   52.564  -22.958 1.00 98.63  ? 810  ASN   B ND2 1 
ATOM   6307  N  N   . GLU   B 2 507 ? 3.610   57.602  -21.986 1.00 91.27  ? 811  GLU   B N   1 
ATOM   6308  C  CA  . GLU   B 2 507 ? 4.683   58.464  -22.456 1.00 89.41  ? 811  GLU   B CA  1 
ATOM   6309  C  C   . GLU   B 2 507 ? 5.805   58.522  -21.423 1.00 90.10  ? 811  GLU   B C   1 
ATOM   6310  O  O   . GLU   B 2 507 ? 5.567   58.834  -20.250 1.00 87.41  ? 811  GLU   B O   1 
ATOM   6311  C  CB  . GLU   B 2 507 ? 4.166   59.862  -22.766 1.00 89.35  ? 811  GLU   B CB  1 
ATOM   6312  C  CG  . GLU   B 2 507 ? 5.285   60.857  -22.940 1.00 93.03  ? 811  GLU   B CG  1 
ATOM   6313  C  CD  . GLU   B 2 507 ? 4.929   62.013  -23.843 1.00 90.88  ? 811  GLU   B CD  1 
ATOM   6314  O  OE1 . GLU   B 2 507 ? 4.057   62.831  -23.478 1.00 92.20  ? 811  GLU   B OE1 1 
ATOM   6315  O  OE2 . GLU   B 2 507 ? 5.542   62.107  -24.918 1.00 86.64  ? 811  GLU   B OE2 1 
ATOM   6316  N  N   . TYR   B 2 508 ? 7.022   58.206  -21.872 1.00 93.37  ? 812  TYR   B N   1 
ATOM   6317  C  CA  . TYR   B 2 508 ? 8.230   58.213  -21.058 1.00 91.07  ? 812  TYR   B CA  1 
ATOM   6318  C  C   . TYR   B 2 508 ? 9.105   59.368  -21.534 1.00 89.59  ? 812  TYR   B C   1 
ATOM   6319  O  O   . TYR   B 2 508 ? 9.428   59.453  -22.720 1.00 91.70  ? 812  TYR   B O   1 
ATOM   6320  C  CB  . TYR   B 2 508 ? 8.964   56.871  -21.186 1.00 92.62  ? 812  TYR   B CB  1 
ATOM   6321  C  CG  . TYR   B 2 508 ? 9.925   56.555  -20.052 1.00 93.72  ? 812  TYR   B CG  1 
ATOM   6322  C  CD1 . TYR   B 2 508 ? 11.156  57.186  -19.976 1.00 93.90  ? 812  TYR   B CD1 1 
ATOM   6323  C  CD2 . TYR   B 2 508 ? 9.615   55.609  -19.067 1.00 93.02  ? 812  TYR   B CD2 1 
ATOM   6324  C  CE1 . TYR   B 2 508 ? 12.059  56.916  -18.940 1.00 94.47  ? 812  TYR   B CE1 1 
ATOM   6325  C  CE2 . TYR   B 2 508 ? 10.520  55.332  -18.022 1.00 93.28  ? 812  TYR   B CE2 1 
ATOM   6326  C  CZ  . TYR   B 2 508 ? 11.744  56.003  -17.971 1.00 92.90  ? 812  TYR   B CZ  1 
ATOM   6327  O  OH  . TYR   B 2 508 ? 12.685  55.796  -16.982 1.00 91.23  ? 812  TYR   B OH  1 
ATOM   6328  N  N   . ALA   B 2 509 ? 9.463   60.269  -20.627 1.00 83.59  ? 813  ALA   B N   1 
ATOM   6329  C  CA  . ALA   B 2 509 ? 10.335  61.383  -20.987 1.00 83.03  ? 813  ALA   B CA  1 
ATOM   6330  C  C   . ALA   B 2 509 ? 11.781  60.924  -20.939 1.00 81.97  ? 813  ALA   B C   1 
ATOM   6331  O  O   . ALA   B 2 509 ? 12.158  60.142  -20.075 1.00 88.88  ? 813  ALA   B O   1 
ATOM   6332  C  CB  . ALA   B 2 509 ? 10.142  62.572  -20.046 1.00 80.32  ? 813  ALA   B CB  1 
ATOM   6333  N  N   . LEU   B 2 510 ? 12.594  61.397  -21.867 1.00 80.38  ? 814  LEU   B N   1 
ATOM   6334  C  CA  . LEU   B 2 510 ? 13.981  60.962  -21.877 1.00 78.81  ? 814  LEU   B CA  1 
ATOM   6335  C  C   . LEU   B 2 510 ? 14.955  62.108  -21.701 1.00 79.45  ? 814  LEU   B C   1 
ATOM   6336  O  O   . LEU   B 2 510 ? 15.857  62.031  -20.862 1.00 83.57  ? 814  LEU   B O   1 
ATOM   6337  C  CB  . LEU   B 2 510 ? 14.292  60.221  -23.177 1.00 82.87  ? 814  LEU   B CB  1 
ATOM   6338  C  CG  . LEU   B 2 510 ? 13.526  58.918  -23.382 1.00 83.89  ? 814  LEU   B CG  1 
ATOM   6339  C  CD1 . LEU   B 2 510 ? 13.976  58.244  -24.672 1.00 85.92  ? 814  LEU   B CD1 1 
ATOM   6340  C  CD2 . LEU   B 2 510 ? 13.723  58.003  -22.188 1.00 83.17  ? 814  LEU   B CD2 1 
ATOM   6341  N  N   . SER   B 2 511 ? 14.798  63.166  -22.464 1.00 78.93  ? 815  SER   B N   1 
ATOM   6342  C  CA  . SER   B 2 511 ? 15.822  64.184  -22.555 1.00 80.74  ? 815  SER   B CA  1 
ATOM   6343  C  C   . SER   B 2 511 ? 15.212  65.544  -22.287 1.00 82.97  ? 815  SER   B C   1 
ATOM   6344  O  O   . SER   B 2 511 ? 14.059  65.797  -22.646 1.00 86.72  ? 815  SER   B O   1 
ATOM   6345  C  CB  . SER   B 2 511 ? 16.469  64.143  -23.927 1.00 87.85  ? 815  SER   B CB  1 
ATOM   6346  O  OG  . SER   B 2 511 ? 15.493  63.845  -24.912 1.00 88.32  ? 815  SER   B OG  1 
ATOM   6347  N  N   . LEU   B 2 512 ? 15.998  66.421  -21.669 1.00 86.18  ? 816  LEU   B N   1 
ATOM   6348  C  CA  . LEU   B 2 512 ? 15.538  67.746  -21.290 1.00 86.65  ? 816  LEU   B CA  1 
ATOM   6349  C  C   . LEU   B 2 512 ? 16.679  68.741  -21.426 1.00 90.38  ? 816  LEU   B C   1 
ATOM   6350  O  O   . LEU   B 2 512 ? 17.805  68.466  -21.003 1.00 93.51  ? 816  LEU   B O   1 
ATOM   6351  C  CB  . LEU   B 2 512 ? 15.012  67.719  -19.865 1.00 80.22  ? 816  LEU   B CB  1 
ATOM   6352  C  CG  . LEU   B 2 512 ? 14.634  69.028  -19.225 1.00 81.34  ? 816  LEU   B CG  1 
ATOM   6353  C  CD1 . LEU   B 2 512 ? 13.257  69.445  -19.667 1.00 83.43  ? 816  LEU   B CD1 1 
ATOM   6354  C  CD2 . LEU   B 2 512 ? 14.700  68.809  -17.738 1.00 82.17  ? 816  LEU   B CD2 1 
ATOM   6355  N  N   . VAL   B 2 513 ? 16.402  69.890  -22.035 1.00 91.50  ? 817  VAL   B N   1 
ATOM   6356  C  CA  . VAL   B 2 513 ? 17.448  70.889  -22.244 1.00 95.77  ? 817  VAL   B CA  1 
ATOM   6357  C  C   . VAL   B 2 513 ? 16.797  72.269  -22.230 1.00 96.05  ? 817  VAL   B C   1 
ATOM   6358  O  O   . VAL   B 2 513 ? 15.648  72.435  -22.647 1.00 96.21  ? 817  VAL   B O   1 
ATOM   6359  C  CB  . VAL   B 2 513 ? 18.267  70.603  -23.538 1.00 95.19  ? 817  VAL   B CB  1 
ATOM   6360  C  CG1 . VAL   B 2 513 ? 17.384  70.483  -24.778 1.00 93.64  ? 817  VAL   B CG1 1 
ATOM   6361  C  CG2 . VAL   B 2 513 ? 19.408  71.625  -23.742 1.00 99.41  ? 817  VAL   B CG2 1 
ATOM   6362  N  N   . SER   B 2 514 ? 17.512  73.239  -21.662 1.00 99.81  ? 818  SER   B N   1 
ATOM   6363  C  CA  . SER   B 2 514 ? 17.100  74.636  -21.630 1.00 101.93 ? 818  SER   B CA  1 
ATOM   6364  C  C   . SER   B 2 514 ? 18.053  75.386  -22.549 1.00 105.25 ? 818  SER   B C   1 
ATOM   6365  O  O   . SER   B 2 514 ? 19.256  75.433  -22.282 1.00 114.33 ? 818  SER   B O   1 
ATOM   6366  C  CB  . SER   B 2 514 ? 17.145  75.189  -20.204 1.00 101.38 ? 818  SER   B CB  1 
ATOM   6367  O  OG  . SER   B 2 514 ? 16.827  76.569  -20.164 1.00 102.92 ? 818  SER   B OG  1 
ATOM   6368  N  N   . CYS   B 2 515 ? 17.531  75.946  -23.638 1.00 105.50 ? 819  CYS   B N   1 
ATOM   6369  C  CA  . CYS   B 2 515 ? 18.353  76.746  -24.537 1.00 109.50 ? 819  CYS   B CA  1 
ATOM   6370  C  C   . CYS   B 2 515 ? 17.480  77.769  -25.254 1.00 115.36 ? 819  CYS   B C   1 
ATOM   6371  O  O   . CYS   B 2 515 ? 16.267  77.577  -25.410 1.00 113.51 ? 819  CYS   B O   1 
ATOM   6372  C  CB  . CYS   B 2 515 ? 19.095  75.873  -25.560 1.00 109.26 ? 819  CYS   B CB  1 
ATOM   6373  S  SG  . CYS   B 2 515 ? 18.100  75.235  -26.941 1.00 108.26 ? 819  CYS   B SG  1 
ATOM   6374  N  N   . LYS   B 2 516 ? 18.105  78.871  -25.671 1.00 116.08 ? 820  LYS   B N   1 
ATOM   6375  C  CA  . LYS   B 2 516 ? 17.492  79.750  -26.659 1.00 118.13 ? 820  LYS   B CA  1 
ATOM   6376  C  C   . LYS   B 2 516 ? 17.783  79.198  -28.048 1.00 115.29 ? 820  LYS   B C   1 
ATOM   6377  O  O   . LYS   B 2 516 ? 18.888  78.710  -28.328 1.00 111.23 ? 820  LYS   B O   1 
ATOM   6378  C  CB  . LYS   B 2 516 ? 18.006  81.186  -26.526 1.00 111.10 ? 820  LYS   B CB  1 
ATOM   6379  N  N   . LEU   B 2 517 ? 16.784  79.248  -28.917 1.00 110.35 ? 821  LEU   B N   1 
ATOM   6380  C  CA  . LEU   B 2 517 ? 16.891  78.586  -30.203 1.00 114.79 ? 821  LEU   B CA  1 
ATOM   6381  C  C   . LEU   B 2 517 ? 16.680  79.592  -31.317 1.00 125.11 ? 821  LEU   B C   1 
ATOM   6382  O  O   . LEU   B 2 517 ? 15.841  80.493  -31.198 1.00 127.63 ? 821  LEU   B O   1 
ATOM   6383  C  CB  . LEU   B 2 517 ? 15.883  77.447  -30.337 1.00 114.49 ? 821  LEU   B CB  1 
ATOM   6384  C  CG  . LEU   B 2 517 ? 16.395  76.057  -29.967 1.00 109.26 ? 821  LEU   B CG  1 
ATOM   6385  C  CD1 . LEU   B 2 517 ? 15.455  74.988  -30.487 1.00 101.64 ? 821  LEU   B CD1 1 
ATOM   6386  C  CD2 . LEU   B 2 517 ? 17.781  75.869  -30.527 1.00 109.41 ? 821  LEU   B CD2 1 
ATOM   6387  N  N   . GLY   B 2 518 ? 17.463  79.433  -32.385 1.00 143.04 ? 822  GLY   B N   1 
ATOM   6388  C  CA  . GLY   B 2 518 ? 17.310  80.230  -33.595 1.00 144.07 ? 822  GLY   B CA  1 
ATOM   6389  C  C   . GLY   B 2 518 ? 17.636  81.697  -33.392 1.00 143.83 ? 822  GLY   B C   1 
ATOM   6390  O  O   . GLY   B 2 518 ? 18.598  82.073  -32.707 1.00 144.33 ? 822  GLY   B O   1 
ATOM   6391  N  N   . LYS   B 2 519 ? 16.825  82.551  -34.009 1.00 130.49 ? 823  LYS   B N   1 
ATOM   6392  C  CA  . LYS   B 2 519 ? 16.941  83.972  -33.737 1.00 126.94 ? 823  LYS   B CA  1 
ATOM   6393  C  C   . LYS   B 2 519 ? 16.006  84.425  -32.629 1.00 124.11 ? 823  LYS   B C   1 
ATOM   6394  O  O   . LYS   B 2 519 ? 16.253  85.476  -32.026 1.00 126.20 ? 823  LYS   B O   1 
ATOM   6395  C  CB  . LYS   B 2 519 ? 16.687  84.781  -35.013 1.00 123.80 ? 823  LYS   B CB  1 
ATOM   6396  C  CG  . LYS   B 2 519 ? 17.510  84.321  -36.190 1.00 122.66 ? 823  LYS   B CG  1 
ATOM   6397  C  CD  . LYS   B 2 519 ? 18.930  83.946  -35.768 1.00 129.09 ? 823  LYS   B CD  1 
ATOM   6398  C  CE  . LYS   B 2 519 ? 19.718  85.123  -35.191 1.00 127.03 ? 823  LYS   B CE  1 
ATOM   6399  N  NZ  . LYS   B 2 519 ? 21.077  84.687  -34.779 1.00 126.55 ? 823  LYS   B NZ  1 
ATOM   6400  N  N   . ASP   B 2 520 ? 14.957  83.643  -32.341 1.00 121.12 ? 824  ASP   B N   1 
ATOM   6401  C  CA  . ASP   B 2 520 ? 14.001  83.841  -31.257 1.00 116.64 ? 824  ASP   B CA  1 
ATOM   6402  C  C   . ASP   B 2 520 ? 14.733  84.256  -29.977 1.00 114.94 ? 824  ASP   B C   1 
ATOM   6403  O  O   . ASP   B 2 520 ? 15.841  83.765  -29.729 1.00 116.23 ? 824  ASP   B O   1 
ATOM   6404  C  CB  . ASP   B 2 520 ? 13.200  82.546  -31.090 1.00 114.31 ? 824  ASP   B CB  1 
ATOM   6405  C  CG  . ASP   B 2 520 ? 12.038  82.693  -30.149 1.00 113.89 ? 824  ASP   B CG  1 
ATOM   6406  O  OD1 . ASP   B 2 520 ? 12.267  82.702  -28.923 1.00 118.22 ? 824  ASP   B OD1 1 
ATOM   6407  O  OD2 . ASP   B 2 520 ? 10.892  82.816  -30.629 1.00 116.23 ? 824  ASP   B OD2 1 
ATOM   6408  N  N   . PRO   B 2 521 ? 14.194  85.201  -29.163 1.00 113.93 ? 825  PRO   B N   1 
ATOM   6409  C  CA  . PRO   B 2 521 ? 14.935  85.655  -27.978 1.00 111.84 ? 825  PRO   B CA  1 
ATOM   6410  C  C   . PRO   B 2 521 ? 14.540  84.931  -26.698 1.00 117.12 ? 825  PRO   B C   1 
ATOM   6411  O  O   . PRO   B 2 521 ? 15.287  84.950  -25.703 1.00 115.46 ? 825  PRO   B O   1 
ATOM   6412  C  CB  . PRO   B 2 521 ? 14.577  87.135  -27.911 1.00 108.88 ? 825  PRO   B CB  1 
ATOM   6413  C  CG  . PRO   B 2 521 ? 13.149  87.173  -28.408 1.00 112.03 ? 825  PRO   B CG  1 
ATOM   6414  C  CD  . PRO   B 2 521 ? 12.992  86.023  -29.392 1.00 114.34 ? 825  PRO   B CD  1 
ATOM   6415  N  N   . ASN   B 2 522 ? 13.380  84.275  -26.724 1.00 113.92 ? 826  ASN   B N   1 
ATOM   6416  C  CA  . ASN   B 2 522 ? 12.917  83.524  -25.566 1.00 110.53 ? 826  ASN   B CA  1 
ATOM   6417  C  C   . ASN   B 2 522 ? 13.807  82.323  -25.351 1.00 116.47 ? 826  ASN   B C   1 
ATOM   6418  O  O   . ASN   B 2 522 ? 14.133  81.589  -26.294 1.00 116.40 ? 826  ASN   B O   1 
ATOM   6419  C  CB  . ASN   B 2 522 ? 11.493  83.017  -25.736 1.00 109.60 ? 826  ASN   B CB  1 
ATOM   6420  C  CG  . ASN   B 2 522 ? 10.554  84.032  -26.312 1.00 112.43 ? 826  ASN   B CG  1 
ATOM   6421  O  OD1 . ASN   B 2 522 ? 9.749   83.700  -27.177 1.00 111.99 ? 826  ASN   B OD1 1 
ATOM   6422  N  ND2 . ASN   B 2 522 ? 10.616  85.264  -25.823 1.00 121.08 ? 826  ASN   B ND2 1 
ATOM   6423  N  N   . THR   B 2 523 ? 14.154  82.090  -24.098 1.00 117.48 ? 827  THR   B N   1 
ATOM   6424  C  CA  . THR   B 2 523 ? 14.689  80.802  -23.722 1.00 117.50 ? 827  THR   B CA  1 
ATOM   6425  C  C   . THR   B 2 523 ? 13.537  79.832  -23.481 1.00 117.55 ? 827  THR   B C   1 
ATOM   6426  O  O   . THR   B 2 523 ? 12.433  80.224  -23.085 1.00 116.53 ? 827  THR   B O   1 
ATOM   6427  C  CB  . THR   B 2 523 ? 15.542  80.951  -22.481 1.00 118.87 ? 827  THR   B CB  1 
ATOM   6428  O  OG1 . THR   B 2 523 ? 14.867  81.850  -21.594 1.00 119.16 ? 827  THR   B OG1 1 
ATOM   6429  C  CG2 . THR   B 2 523 ? 16.884  81.538  -22.847 1.00 119.18 ? 827  THR   B CG2 1 
ATOM   6430  N  N   . TYR   B 2 524 ? 13.801  78.556  -23.738 1.00 116.95 ? 828  TYR   B N   1 
ATOM   6431  C  CA  . TYR   B 2 524 ? 12.758  77.554  -23.852 1.00 116.00 ? 828  TYR   B CA  1 
ATOM   6432  C  C   . TYR   B 2 524 ? 13.141  76.310  -23.065 1.00 114.08 ? 828  TYR   B C   1 
ATOM   6433  O  O   . TYR   B 2 524 ? 14.301  76.142  -22.677 1.00 116.78 ? 828  TYR   B O   1 
ATOM   6434  C  CB  . TYR   B 2 524 ? 12.524  77.203  -25.319 1.00 116.82 ? 828  TYR   B CB  1 
ATOM   6435  C  CG  . TYR   B 2 524 ? 11.770  78.261  -26.103 1.00 118.57 ? 828  TYR   B CG  1 
ATOM   6436  C  CD1 . TYR   B 2 524 ? 10.679  78.914  -25.545 1.00 116.65 ? 828  TYR   B CD1 1 
ATOM   6437  C  CD2 . TYR   B 2 524 ? 12.139  78.588  -27.406 1.00 117.41 ? 828  TYR   B CD2 1 
ATOM   6438  C  CE1 . TYR   B 2 524 ? 9.983   79.849  -26.253 1.00 117.78 ? 828  TYR   B CE1 1 
ATOM   6439  C  CE2 . TYR   B 2 524 ? 11.447  79.521  -28.120 1.00 116.84 ? 828  TYR   B CE2 1 
ATOM   6440  C  CZ  . TYR   B 2 524 ? 10.370  80.150  -27.539 1.00 119.37 ? 828  TYR   B CZ  1 
ATOM   6441  O  OH  . TYR   B 2 524 ? 9.666   81.094  -28.245 1.00 124.05 ? 828  TYR   B OH  1 
ATOM   6442  N  N   . PHE   B 2 525 ? 12.154  75.426  -22.838 1.00 105.68 ? 829  PHE   B N   1 
ATOM   6443  C  CA  . PHE   B 2 525 ? 12.346  74.125  -22.167 1.00 102.29 ? 829  PHE   B CA  1 
ATOM   6444  C  C   . PHE   B 2 525 ? 12.039  73.010  -23.172 1.00 98.92  ? 829  PHE   B C   1 
ATOM   6445  O  O   . PHE   B 2 525 ? 10.874  72.667  -23.378 1.00 98.30  ? 829  PHE   B O   1 
ATOM   6446  C  CB  . PHE   B 2 525 ? 11.434  73.973  -20.943 1.00 98.53  ? 829  PHE   B CB  1 
ATOM   6447  C  CG  . PHE   B 2 525 ? 12.010  74.481  -19.646 1.00 94.07  ? 829  PHE   B CG  1 
ATOM   6448  C  CD1 . PHE   B 2 525 ? 13.343  74.305  -19.335 1.00 95.79  ? 829  PHE   B CD1 1 
ATOM   6449  C  CD2 . PHE   B 2 525 ? 11.183  75.106  -18.715 1.00 92.21  ? 829  PHE   B CD2 1 
ATOM   6450  C  CE1 . PHE   B 2 525 ? 13.848  74.767  -18.121 1.00 96.76  ? 829  PHE   B CE1 1 
ATOM   6451  C  CE2 . PHE   B 2 525 ? 11.680  75.576  -17.513 1.00 92.13  ? 829  PHE   B CE2 1 
ATOM   6452  C  CZ  . PHE   B 2 525 ? 13.008  75.405  -17.211 1.00 94.37  ? 829  PHE   B CZ  1 
ATOM   6453  N  N   . ILE   B 2 526 ? 13.070  72.413  -23.765 1.00 95.01  ? 830  ILE   B N   1 
ATOM   6454  C  CA  . ILE   B 2 526 ? 12.882  71.369  -24.775 1.00 92.56  ? 830  ILE   B CA  1 
ATOM   6455  C  C   . ILE   B 2 526 ? 13.009  69.999  -24.113 1.00 92.99  ? 830  ILE   B C   1 
ATOM   6456  O  O   . ILE   B 2 526 ? 14.024  69.689  -23.474 1.00 91.22  ? 830  ILE   B O   1 
ATOM   6457  C  CB  . ILE   B 2 526 ? 13.869  71.520  -25.939 1.00 89.82  ? 830  ILE   B CB  1 
ATOM   6458  C  CG1 . ILE   B 2 526 ? 13.899  72.966  -26.414 1.00 95.19  ? 830  ILE   B CG1 1 
ATOM   6459  C  CG2 . ILE   B 2 526 ? 13.462  70.626  -27.091 1.00 88.61  ? 830  ILE   B CG2 1 
ATOM   6460  C  CD1 . ILE   B 2 526 ? 15.190  73.359  -27.123 1.00 93.10  ? 830  ILE   B CD1 1 
ATOM   6461  N  N   . VAL   B 2 527 ? 11.975  69.180  -24.281 1.00 92.45  ? 831  VAL   B N   1 
ATOM   6462  C  CA  . VAL   B 2 527 ? 11.856  67.860  -23.672 1.00 87.69  ? 831  VAL   B CA  1 
ATOM   6463  C  C   . VAL   B 2 527 ? 11.651  66.864  -24.795 1.00 88.58  ? 831  VAL   B C   1 
ATOM   6464  O  O   . VAL   B 2 527 ? 10.682  66.978  -25.556 1.00 93.98  ? 831  VAL   B O   1 
ATOM   6465  C  CB  . VAL   B 2 527 ? 10.669  67.794  -22.697 1.00 86.41  ? 831  VAL   B CB  1 
ATOM   6466  C  CG1 . VAL   B 2 527 ? 10.764  66.570  -21.824 1.00 83.79  ? 831  VAL   B CG1 1 
ATOM   6467  C  CG2 . VAL   B 2 527 ? 10.586  69.053  -21.877 1.00 91.39  ? 831  VAL   B CG2 1 
ATOM   6468  N  N   . GLY   B 2 528 ? 12.554  65.894  -24.910 1.00 87.69  ? 832  GLY   B N   1 
ATOM   6469  C  CA  . GLY   B 2 528 ? 12.375  64.786  -25.835 1.00 85.56  ? 832  GLY   B CA  1 
ATOM   6470  C  C   . GLY   B 2 528 ? 11.844  63.590  -25.068 1.00 82.88  ? 832  GLY   B C   1 
ATOM   6471  O  O   . GLY   B 2 528 ? 12.340  63.262  -23.991 1.00 81.57  ? 832  GLY   B O   1 
ATOM   6472  N  N   . THR   B 2 529 ? 10.805  62.970  -25.616 1.00 84.28  ? 833  THR   B N   1 
ATOM   6473  C  CA  . THR   B 2 529 ? 10.159  61.829  -24.980 1.00 85.25  ? 833  THR   B CA  1 
ATOM   6474  C  C   . THR   B 2 529 ? 10.244  60.597  -25.909 1.00 87.52  ? 833  THR   B C   1 
ATOM   6475  O  O   . THR   B 2 529 ? 10.967  60.597  -26.917 1.00 83.82  ? 833  THR   B O   1 
ATOM   6476  C  CB  . THR   B 2 529 ? 8.718   62.202  -24.591 1.00 86.17  ? 833  THR   B CB  1 
ATOM   6477  O  OG1 . THR   B 2 529 ? 7.843   61.991  -25.699 1.00 91.14  ? 833  THR   B OG1 1 
ATOM   6478  C  CG2 . THR   B 2 529 ? 8.623   63.674  -24.207 1.00 84.32  ? 833  THR   B CG2 1 
ATOM   6479  N  N   . ALA   B 2 530 ? 9.531   59.526  -25.534 1.00 90.60  ? 834  ALA   B N   1 
ATOM   6480  C  CA  . ALA   B 2 530 ? 9.402   58.312  -26.358 1.00 87.86  ? 834  ALA   B CA  1 
ATOM   6481  C  C   . ALA   B 2 530 ? 8.193   57.525  -25.891 1.00 86.85  ? 834  ALA   B C   1 
ATOM   6482  O  O   . ALA   B 2 530 ? 8.107   57.158  -24.715 1.00 88.65  ? 834  ALA   B O   1 
ATOM   6483  C  CB  . ALA   B 2 530 ? 10.644  57.442  -26.280 1.00 85.40  ? 834  ALA   B CB  1 
ATOM   6484  N  N   . MET   B 2 531 ? 7.270   57.250  -26.798 1.00 91.94  ? 835  MET   B N   1 
ATOM   6485  C  CA  . MET   B 2 531 ? 6.074   56.501  -26.442 1.00 95.02  ? 835  MET   B CA  1 
ATOM   6486  C  C   . MET   B 2 531 ? 6.422   55.031  -26.209 1.00 94.51  ? 835  MET   B C   1 
ATOM   6487  O  O   . MET   B 2 531 ? 7.004   54.374  -27.084 1.00 96.15  ? 835  MET   B O   1 
ATOM   6488  C  CB  . MET   B 2 531 ? 5.023   56.655  -27.541 1.00 97.90  ? 835  MET   B CB  1 
ATOM   6489  C  CG  . MET   B 2 531 ? 4.631   58.095  -27.758 1.00 101.09 ? 835  MET   B CG  1 
ATOM   6490  S  SD  . MET   B 2 531 ? 3.881   58.775  -26.286 1.00 90.21  ? 835  MET   B SD  1 
ATOM   6491  C  CE  . MET   B 2 531 ? 2.327   57.866  -26.246 1.00 101.29 ? 835  MET   B CE  1 
ATOM   6492  N  N   . VAL   B 2 532 ? 6.066   54.517  -25.028 1.00 90.98  ? 836  VAL   B N   1 
ATOM   6493  C  CA  . VAL   B 2 532 ? 6.373   53.146  -24.634 1.00 92.53  ? 836  VAL   B CA  1 
ATOM   6494  C  C   . VAL   B 2 532 ? 5.074   52.393  -24.401 1.00 93.17  ? 836  VAL   B C   1 
ATOM   6495  O  O   . VAL   B 2 532 ? 4.129   52.919  -23.807 1.00 95.66  ? 836  VAL   B O   1 
ATOM   6496  C  CB  . VAL   B 2 532 ? 7.264   53.068  -23.369 1.00 94.85  ? 836  VAL   B CB  1 
ATOM   6497  C  CG1 . VAL   B 2 532 ? 8.617   53.753  -23.585 1.00 93.66  ? 836  VAL   B CG1 1 
ATOM   6498  C  CG2 . VAL   B 2 532 ? 6.567   53.668  -22.163 1.00 96.37  ? 836  VAL   B CG2 1 
ATOM   6499  N  N   . TYR   B 2 533 ? 5.038   51.158  -24.872 1.00 93.91  ? 837  TYR   B N   1 
ATOM   6500  C  CA  . TYR   B 2 533 ? 3.950   50.240  -24.602 1.00 95.99  ? 837  TYR   B CA  1 
ATOM   6501  C  C   . TYR   B 2 533 ? 4.576   48.892  -24.276 1.00 97.30  ? 837  TYR   B C   1 
ATOM   6502  O  O   . TYR   B 2 533 ? 5.705   48.613  -24.705 1.00 100.53 ? 837  TYR   B O   1 
ATOM   6503  C  CB  . TYR   B 2 533 ? 2.993   50.121  -25.798 1.00 96.44  ? 837  TYR   B CB  1 
ATOM   6504  C  CG  . TYR   B 2 533 ? 2.493   51.447  -26.351 1.00 96.02  ? 837  TYR   B CG  1 
ATOM   6505  C  CD1 . TYR   B 2 533 ? 1.337   52.039  -25.853 1.00 99.10  ? 837  TYR   B CD1 1 
ATOM   6506  C  CD2 . TYR   B 2 533 ? 3.161   52.092  -27.398 1.00 101.53 ? 837  TYR   B CD2 1 
ATOM   6507  C  CE1 . TYR   B 2 533 ? 0.854   53.262  -26.367 1.00 109.45 ? 837  TYR   B CE1 1 
ATOM   6508  C  CE2 . TYR   B 2 533 ? 2.696   53.316  -27.919 1.00 106.02 ? 837  TYR   B CE2 1 
ATOM   6509  C  CZ  . TYR   B 2 533 ? 1.536   53.900  -27.399 1.00 108.88 ? 837  TYR   B CZ  1 
ATOM   6510  O  OH  . TYR   B 2 533 ? 1.069   55.112  -27.903 1.00 110.53 ? 837  TYR   B OH  1 
ATOM   6511  N  N   . PRO   B 2 534 ? 3.895   48.056  -23.494 1.00 94.14  ? 838  PRO   B N   1 
ATOM   6512  C  CA  . PRO   B 2 534 ? 4.542   46.821  -23.012 1.00 97.05  ? 838  PRO   B CA  1 
ATOM   6513  C  C   . PRO   B 2 534 ? 4.934   45.862  -24.121 1.00 102.67 ? 838  PRO   B C   1 
ATOM   6514  O  O   . PRO   B 2 534 ? 5.930   45.139  -23.982 1.00 107.96 ? 838  PRO   B O   1 
ATOM   6515  C  CB  . PRO   B 2 534 ? 3.483   46.202  -22.094 1.00 101.38 ? 838  PRO   B CB  1 
ATOM   6516  C  CG  . PRO   B 2 534 ? 2.570   47.309  -21.744 1.00 100.32 ? 838  PRO   B CG  1 
ATOM   6517  C  CD  . PRO   B 2 534 ? 2.605   48.313  -22.837 1.00 96.25  ? 838  PRO   B CD  1 
ATOM   6518  N  N   . GLU   B 2 535 ? 4.179   45.831  -25.216 1.00 101.88 ? 839  GLU   B N   1 
ATOM   6519  C  CA  . GLU   B 2 535 ? 4.436   44.928  -26.330 1.00 100.86 ? 839  GLU   B CA  1 
ATOM   6520  C  C   . GLU   B 2 535 ? 5.517   45.457  -27.271 1.00 103.24 ? 839  GLU   B C   1 
ATOM   6521  O  O   . GLU   B 2 535 ? 6.474   44.736  -27.562 1.00 109.24 ? 839  GLU   B O   1 
ATOM   6522  C  CB  . GLU   B 2 535 ? 3.130   44.664  -27.096 1.00 105.64 ? 839  GLU   B CB  1 
ATOM   6523  C  CG  . GLU   B 2 535 ? 2.258   45.902  -27.464 1.00 108.62 ? 839  GLU   B CG  1 
ATOM   6524  C  CD  . GLU   B 2 535 ? 1.488   46.513  -26.287 1.00 102.98 ? 839  GLU   B CD  1 
ATOM   6525  O  OE1 . GLU   B 2 535 ? 2.111   46.775  -25.246 1.00 98.87  ? 839  GLU   B OE1 1 
ATOM   6526  O  OE2 . GLU   B 2 535 ? 0.263   46.742  -26.405 1.00 104.38 ? 839  GLU   B OE2 1 
ATOM   6527  N  N   . GLU   B 2 536 ? 5.374   46.706  -27.748 1.00 102.85 ? 840  GLU   B N   1 
ATOM   6528  C  CA  . GLU   B 2 536 ? 6.363   47.356  -28.604 1.00 99.22  ? 840  GLU   B CA  1 
ATOM   6529  C  C   . GLU   B 2 536 ? 7.659   47.281  -27.807 1.00 99.56  ? 840  GLU   B C   1 
ATOM   6530  O  O   . GLU   B 2 536 ? 7.799   47.907  -26.745 1.00 100.57 ? 840  GLU   B O   1 
ATOM   6531  C  CB  . GLU   B 2 536 ? 5.919   48.774  -28.988 1.00 101.96 ? 840  GLU   B CB  1 
ATOM   6532  N  N   . ALA   B 2 537 ? 8.597   46.481  -28.323 1.00 102.13 ? 841  ALA   B N   1 
ATOM   6533  C  CA  . ALA   B 2 537 ? 9.882   46.273  -27.672 1.00 100.41 ? 841  ALA   B CA  1 
ATOM   6534  C  C   . ALA   B 2 537 ? 10.768  47.462  -28.013 1.00 99.65  ? 841  ALA   B C   1 
ATOM   6535  O  O   . ALA   B 2 537 ? 11.278  48.157  -27.122 1.00 100.86 ? 841  ALA   B O   1 
ATOM   6536  C  CB  . ALA   B 2 537 ? 10.516  44.967  -28.146 1.00 99.54  ? 841  ALA   B CB  1 
ATOM   6537  N  N   . GLU   B 2 538 ? 10.942  47.724  -29.299 1.00 88.26  ? 842  GLU   B N   1 
ATOM   6538  C  CA  . GLU   B 2 538 ? 11.686  48.859  -29.807 1.00 88.00  ? 842  GLU   B CA  1 
ATOM   6539  C  C   . GLU   B 2 538 ? 10.778  50.095  -29.836 1.00 91.47  ? 842  GLU   B C   1 
ATOM   6540  O  O   . GLU   B 2 538 ? 9.586   49.980  -30.154 1.00 88.10  ? 842  GLU   B O   1 
ATOM   6541  C  CB  . GLU   B 2 538 ? 12.227  48.529  -31.199 1.00 91.03  ? 842  GLU   B CB  1 
ATOM   6542  C  CG  . GLU   B 2 538 ? 13.308  49.447  -31.759 1.00 95.31  ? 842  GLU   B CG  1 
ATOM   6543  C  CD  . GLU   B 2 538 ? 14.639  49.381  -31.007 1.00 101.34 ? 842  GLU   B CD  1 
ATOM   6544  O  OE1 . GLU   B 2 538 ? 15.253  48.283  -30.931 1.00 97.04  ? 842  GLU   B OE1 1 
ATOM   6545  O  OE2 . GLU   B 2 538 ? 15.084  50.449  -30.505 1.00 105.92 ? 842  GLU   B OE2 1 
ATOM   6546  N  N   . PRO   B 2 539 ? 11.269  51.278  -29.441 1.00 94.56  ? 843  PRO   B N   1 
ATOM   6547  C  CA  . PRO   B 2 539 ? 10.411  52.478  -29.440 1.00 91.86  ? 843  PRO   B CA  1 
ATOM   6548  C  C   . PRO   B 2 539 ? 10.245  53.029  -30.848 1.00 91.41  ? 843  PRO   B C   1 
ATOM   6549  O  O   . PRO   B 2 539 ? 11.216  53.453  -31.478 1.00 89.36  ? 843  PRO   B O   1 
ATOM   6550  C  CB  . PRO   B 2 539 ? 11.176  53.456  -28.542 1.00 89.22  ? 843  PRO   B CB  1 
ATOM   6551  C  CG  . PRO   B 2 539 ? 12.612  53.067  -28.743 1.00 88.86  ? 843  PRO   B CG  1 
ATOM   6552  C  CD  . PRO   B 2 539 ? 12.618  51.571  -28.904 1.00 92.62  ? 843  PRO   B CD  1 
ATOM   6553  N  N   . LYS   B 2 540 ? 9.008   53.025  -31.350 1.00 94.83  ? 844  LYS   B N   1 
ATOM   6554  C  CA  . LYS   B 2 540 ? 8.771   53.360  -32.754 1.00 95.23  ? 844  LYS   B CA  1 
ATOM   6555  C  C   . LYS   B 2 540 ? 8.050   54.697  -32.943 1.00 94.15  ? 844  LYS   B C   1 
ATOM   6556  O  O   . LYS   B 2 540 ? 7.557   54.965  -34.040 1.00 91.92  ? 844  LYS   B O   1 
ATOM   6557  C  CB  . LYS   B 2 540 ? 8.007   52.232  -33.455 1.00 95.03  ? 844  LYS   B CB  1 
ATOM   6558  N  N   . GLN   B 2 541 ? 7.985   55.538  -31.909 1.00 98.34  ? 845  GLN   B N   1 
ATOM   6559  C  CA  . GLN   B 2 541 ? 7.351   56.846  -32.008 1.00 97.35  ? 845  GLN   B CA  1 
ATOM   6560  C  C   . GLN   B 2 541 ? 7.565   57.605  -30.704 1.00 96.49  ? 845  GLN   B C   1 
ATOM   6561  O  O   . GLN   B 2 541 ? 7.537   57.012  -29.628 1.00 96.93  ? 845  GLN   B O   1 
ATOM   6562  C  CB  . GLN   B 2 541 ? 5.856   56.704  -32.316 1.00 101.60 ? 845  GLN   B CB  1 
ATOM   6563  C  CG  . GLN   B 2 541 ? 5.067   55.875  -31.320 1.00 105.26 ? 845  GLN   B CG  1 
ATOM   6564  C  CD  . GLN   B 2 541 ? 3.620   55.687  -31.757 1.00 111.71 ? 845  GLN   B CD  1 
ATOM   6565  O  OE1 . GLN   B 2 541 ? 3.280   55.900  -32.925 1.00 113.67 ? 845  GLN   B OE1 1 
ATOM   6566  N  NE2 . GLN   B 2 541 ? 2.763   55.280  -30.820 1.00 114.12 ? 845  GLN   B NE2 1 
ATOM   6567  N  N   . GLY   B 2 542 ? 7.755   58.915  -30.813 1.00 104.75 ? 846  GLY   B N   1 
ATOM   6568  C  CA  . GLY   B 2 542 ? 8.031   59.769  -29.665 1.00 103.02 ? 846  GLY   B CA  1 
ATOM   6569  C  C   . GLY   B 2 542 ? 7.533   61.190  -29.966 1.00 105.05 ? 846  GLY   B C   1 
ATOM   6570  O  O   . GLY   B 2 542 ? 6.629   61.374  -30.784 1.00 108.11 ? 846  GLY   B O   1 
ATOM   6571  N  N   . ARG   B 2 543 ? 8.126   62.193  -29.312 1.00 94.78  ? 847  ARG   B N   1 
ATOM   6572  C  CA  . ARG   B 2 543 ? 7.846   63.591  -29.645 1.00 95.09  ? 847  ARG   B CA  1 
ATOM   6573  C  C   . ARG   B 2 543 ? 8.822   64.538  -28.948 1.00 93.82  ? 847  ARG   B C   1 
ATOM   6574  O  O   . ARG   B 2 543 ? 9.114   64.380  -27.763 1.00 93.71  ? 847  ARG   B O   1 
ATOM   6575  C  CB  . ARG   B 2 543 ? 6.407   64.001  -29.282 1.00 94.14  ? 847  ARG   B CB  1 
ATOM   6576  N  N   . ILE   B 2 544 ? 9.296   65.543  -29.693 1.00 95.57  ? 848  ILE   B N   1 
ATOM   6577  C  CA  . ILE   B 2 544 ? 10.026  66.668  -29.109 1.00 93.13  ? 848  ILE   B CA  1 
ATOM   6578  C  C   . ILE   B 2 544 ? 9.021   67.759  -28.808 1.00 92.83  ? 848  ILE   B C   1 
ATOM   6579  O  O   . ILE   B 2 544 ? 8.143   68.056  -29.619 1.00 96.35  ? 848  ILE   B O   1 
ATOM   6580  C  CB  . ILE   B 2 544 ? 11.118  67.182  -30.059 1.00 91.03  ? 848  ILE   B CB  1 
ATOM   6581  C  CG1 . ILE   B 2 544 ? 12.214  66.136  -30.235 1.00 92.04  ? 848  ILE   B CG1 1 
ATOM   6582  C  CG2 . ILE   B 2 544 ? 11.673  68.511  -29.570 1.00 84.68  ? 848  ILE   B CG2 1 
ATOM   6583  C  CD1 . ILE   B 2 544 ? 13.091  66.395  -31.437 1.00 87.10  ? 848  ILE   B CD1 1 
ATOM   6584  N  N   . VAL   B 2 545 ? 9.134   68.340  -27.629 1.00 91.52  ? 849  VAL   B N   1 
ATOM   6585  C  CA  . VAL   B 2 545 ? 8.207   69.348  -27.155 1.00 93.67  ? 849  VAL   B CA  1 
ATOM   6586  C  C   . VAL   B 2 545 ? 9.020   70.579  -26.783 1.00 99.30  ? 849  VAL   B C   1 
ATOM   6587  O  O   . VAL   B 2 545 ? 10.154  70.460  -26.300 1.00 95.73  ? 849  VAL   B O   1 
ATOM   6588  C  CB  . VAL   B 2 545 ? 7.391   68.834  -25.954 1.00 91.98  ? 849  VAL   B CB  1 
ATOM   6589  C  CG1 . VAL   B 2 545 ? 6.378   69.854  -25.510 1.00 94.57  ? 849  VAL   B CG1 1 
ATOM   6590  C  CG2 . VAL   B 2 545 ? 6.710   67.538  -26.325 1.00 95.29  ? 849  VAL   B CG2 1 
ATOM   6591  N  N   . VAL   B 2 546 ? 8.462   71.757  -27.038 1.00 104.49 ? 850  VAL   B N   1 
ATOM   6592  C  CA  . VAL   B 2 546 ? 9.109   73.011  -26.683 1.00 98.15  ? 850  VAL   B CA  1 
ATOM   6593  C  C   . VAL   B 2 546 ? 8.224   73.734  -25.681 1.00 102.43 ? 850  VAL   B C   1 
ATOM   6594  O  O   . VAL   B 2 546 ? 7.040   73.973  -25.957 1.00 104.40 ? 850  VAL   B O   1 
ATOM   6595  C  CB  . VAL   B 2 546 ? 9.367   73.885  -27.913 1.00 95.93  ? 850  VAL   B CB  1 
ATOM   6596  C  CG1 . VAL   B 2 546 ? 10.320  74.996  -27.542 1.00 104.76 ? 850  VAL   B CG1 1 
ATOM   6597  C  CG2 . VAL   B 2 546 ? 9.939   73.060  -29.018 1.00 96.64  ? 850  VAL   B CG2 1 
ATOM   6598  N  N   . PHE   B 2 547 ? 8.787   74.074  -24.519 1.00 101.96 ? 851  PHE   B N   1 
ATOM   6599  C  CA  . PHE   B 2 547 ? 8.062   74.769  -23.458 1.00 100.98 ? 851  PHE   B CA  1 
ATOM   6600  C  C   . PHE   B 2 547 ? 8.623   76.169  -23.258 1.00 106.59 ? 851  PHE   B C   1 
ATOM   6601  O  O   . PHE   B 2 547 ? 9.683   76.533  -23.781 1.00 106.66 ? 851  PHE   B O   1 
ATOM   6602  C  CB  . PHE   B 2 547 ? 8.122   74.010  -22.127 1.00 98.01  ? 851  PHE   B CB  1 
ATOM   6603  C  CG  . PHE   B 2 547 ? 7.326   72.741  -22.102 1.00 97.99  ? 851  PHE   B CG  1 
ATOM   6604  C  CD1 . PHE   B 2 547 ? 5.957   72.765  -21.970 1.00 100.39 ? 851  PHE   B CD1 1 
ATOM   6605  C  CD2 . PHE   B 2 547 ? 7.963   71.515  -22.185 1.00 98.40  ? 851  PHE   B CD2 1 
ATOM   6606  C  CE1 . PHE   B 2 547 ? 5.237   71.587  -21.942 1.00 98.30  ? 851  PHE   B CE1 1 
ATOM   6607  C  CE2 . PHE   B 2 547 ? 7.251   70.345  -22.154 1.00 94.61  ? 851  PHE   B CE2 1 
ATOM   6608  C  CZ  . PHE   B 2 547 ? 5.890   70.379  -22.036 1.00 92.92  ? 851  PHE   B CZ  1 
ATOM   6609  N  N   . GLN   B 2 548 ? 7.890   76.946  -22.458 1.00 108.33 ? 852  GLN   B N   1 
ATOM   6610  C  CA  . GLN   B 2 548 ? 8.255   78.311  -22.108 1.00 107.00 ? 852  GLN   B CA  1 
ATOM   6611  C  C   . GLN   B 2 548 ? 7.617   78.621  -20.762 1.00 109.40 ? 852  GLN   B C   1 
ATOM   6612  O  O   . GLN   B 2 548 ? 6.393   78.541  -20.634 1.00 111.00 ? 852  GLN   B O   1 
ATOM   6613  C  CB  . GLN   B 2 548 ? 7.782   79.283  -23.193 1.00 105.39 ? 852  GLN   B CB  1 
ATOM   6614  C  CG  . GLN   B 2 548 ? 7.741   80.740  -22.786 1.00 109.23 ? 852  GLN   B CG  1 
ATOM   6615  C  CD  . GLN   B 2 548 ? 8.117   81.674  -23.916 1.00 109.94 ? 852  GLN   B CD  1 
ATOM   6616  O  OE1 . GLN   B 2 548 ? 9.250   82.160  -23.979 1.00 113.68 ? 852  GLN   B OE1 1 
ATOM   6617  N  NE2 . GLN   B 2 548 ? 7.167   81.943  -24.810 1.00 108.07 ? 852  GLN   B NE2 1 
ATOM   6618  N  N   . TYR   B 2 549 ? 8.437   78.929  -19.755 1.00 113.86 ? 853  TYR   B N   1 
ATOM   6619  C  CA  . TYR   B 2 549 ? 7.942   79.289  -18.426 1.00 116.56 ? 853  TYR   B CA  1 
ATOM   6620  C  C   . TYR   B 2 549 ? 8.272   80.751  -18.179 1.00 122.71 ? 853  TYR   B C   1 
ATOM   6621  O  O   . TYR   B 2 549 ? 9.398   81.083  -17.798 1.00 123.34 ? 853  TYR   B O   1 
ATOM   6622  C  CB  . TYR   B 2 549 ? 8.556   78.423  -17.339 1.00 106.56 ? 853  TYR   B CB  1 
ATOM   6623  C  CG  . TYR   B 2 549 ? 7.940   78.654  -15.986 1.00 107.92 ? 853  TYR   B CG  1 
ATOM   6624  C  CD1 . TYR   B 2 549 ? 6.723   78.086  -15.667 1.00 114.64 ? 853  TYR   B CD1 1 
ATOM   6625  C  CD2 . TYR   B 2 549 ? 8.572   79.436  -15.023 1.00 110.49 ? 853  TYR   B CD2 1 
ATOM   6626  C  CE1 . TYR   B 2 549 ? 6.143   78.283  -14.418 1.00 116.91 ? 853  TYR   B CE1 1 
ATOM   6627  C  CE2 . TYR   B 2 549 ? 7.999   79.641  -13.764 1.00 110.86 ? 853  TYR   B CE2 1 
ATOM   6628  C  CZ  . TYR   B 2 549 ? 6.783   79.058  -13.473 1.00 112.29 ? 853  TYR   B CZ  1 
ATOM   6629  O  OH  . TYR   B 2 549 ? 6.184   79.237  -12.249 1.00 111.81 ? 853  TYR   B OH  1 
ATOM   6630  N  N   . SER   B 2 550 ? 7.289   81.630  -18.366 1.00 128.44 ? 854  SER   B N   1 
ATOM   6631  C  CA  . SER   B 2 550 ? 7.583   83.041  -18.181 1.00 133.44 ? 854  SER   B CA  1 
ATOM   6632  C  C   . SER   B 2 550 ? 6.492   83.828  -17.471 1.00 137.78 ? 854  SER   B C   1 
ATOM   6633  O  O   . SER   B 2 550 ? 6.717   85.003  -17.150 1.00 135.79 ? 854  SER   B O   1 
ATOM   6634  C  CB  . SER   B 2 550 ? 7.906   83.705  -19.532 1.00 135.61 ? 854  SER   B CB  1 
ATOM   6635  O  OG  . SER   B 2 550 ? 9.226   83.369  -19.953 1.00 132.81 ? 854  SER   B OG  1 
ATOM   6636  N  N   . ASP   B 2 551 ? 5.332   83.231  -17.195 1.00 136.10 ? 855  ASP   B N   1 
ATOM   6637  C  CA  . ASP   B 2 551 ? 4.317   83.887  -16.386 1.00 136.13 ? 855  ASP   B CA  1 
ATOM   6638  C  C   . ASP   B 2 551 ? 3.684   82.837  -15.478 1.00 135.83 ? 855  ASP   B C   1 
ATOM   6639  O  O   . ASP   B 2 551 ? 2.507   82.503  -15.606 1.00 136.13 ? 855  ASP   B O   1 
ATOM   6640  C  CB  . ASP   B 2 551 ? 3.276   84.581  -17.259 1.00 135.55 ? 855  ASP   B CB  1 
ATOM   6641  N  N   . GLY   B 2 552 ? 4.493   82.275  -14.581 1.00 137.81 ? 856  GLY   B N   1 
ATOM   6642  C  CA  . GLY   B 2 552 ? 4.041   81.251  -13.648 1.00 137.47 ? 856  GLY   B CA  1 
ATOM   6643  C  C   . GLY   B 2 552 ? 3.356   80.060  -14.304 1.00 138.96 ? 856  GLY   B C   1 
ATOM   6644  O  O   . GLY   B 2 552 ? 2.820   79.178  -13.616 1.00 135.77 ? 856  GLY   B O   1 
ATOM   6645  N  N   . LYS   B 2 553 ? 3.389   80.013  -15.633 1.00 144.86 ? 857  LYS   B N   1 
ATOM   6646  C  CA  . LYS   B 2 553 ? 2.644   79.031  -16.408 1.00 141.75 ? 857  LYS   B CA  1 
ATOM   6647  C  C   . LYS   B 2 553 ? 3.555   78.450  -17.476 1.00 137.52 ? 857  LYS   B C   1 
ATOM   6648  O  O   . LYS   B 2 553 ? 4.305   79.184  -18.131 1.00 138.19 ? 857  LYS   B O   1 
ATOM   6649  C  CB  . LYS   B 2 553 ? 1.390   79.659  -17.035 1.00 141.20 ? 857  LYS   B CB  1 
ATOM   6650  N  N   . LEU   B 2 554 ? 3.501   77.122  -17.613 1.00 121.28 ? 858  LEU   B N   1 
ATOM   6651  C  CA  . LEU   B 2 554 ? 4.175   76.402  -18.685 1.00 118.04 ? 858  LEU   B CA  1 
ATOM   6652  C  C   . LEU   B 2 554 ? 3.329   76.468  -19.953 1.00 121.07 ? 858  LEU   B C   1 
ATOM   6653  O  O   . LEU   B 2 554 ? 2.150   76.095  -19.949 1.00 124.28 ? 858  LEU   B O   1 
ATOM   6654  C  CB  . LEU   B 2 554 ? 4.405   74.952  -18.269 1.00 111.77 ? 858  LEU   B CB  1 
ATOM   6655  C  CG  . LEU   B 2 554 ? 5.606   74.283  -18.912 1.00 112.28 ? 858  LEU   B CG  1 
ATOM   6656  C  CD1 . LEU   B 2 554 ? 6.849   75.095  -18.665 1.00 112.65 ? 858  LEU   B CD1 1 
ATOM   6657  C  CD2 . LEU   B 2 554 ? 5.778   72.932  -18.310 1.00 111.80 ? 858  LEU   B CD2 1 
ATOM   6658  N  N   . GLN   B 2 555 ? 3.919   76.952  -21.037 1.00 118.44 ? 859  GLN   B N   1 
ATOM   6659  C  CA  . GLN   B 2 555 ? 3.210   77.084  -22.297 1.00 111.46 ? 859  GLN   B CA  1 
ATOM   6660  C  C   . GLN   B 2 555 ? 3.935   76.236  -23.325 1.00 108.23 ? 859  GLN   B C   1 
ATOM   6661  O  O   . GLN   B 2 555 ? 5.155   76.352  -23.465 1.00 107.80 ? 859  GLN   B O   1 
ATOM   6662  C  CB  . GLN   B 2 555 ? 3.149   78.552  -22.725 1.00 114.29 ? 859  GLN   B CB  1 
ATOM   6663  N  N   . THR   B 2 556 ? 3.187   75.379  -24.028 1.00 110.38 ? 860  THR   B N   1 
ATOM   6664  C  CA  . THR   B 2 556 ? 3.743   74.452  -25.024 1.00 114.95 ? 860  THR   B CA  1 
ATOM   6665  C  C   . THR   B 2 556 ? 3.921   75.167  -26.368 1.00 115.88 ? 860  THR   B C   1 
ATOM   6666  O  O   . THR   B 2 556 ? 2.957   75.377  -27.105 1.00 121.03 ? 860  THR   B O   1 
ATOM   6667  C  CB  . THR   B 2 556 ? 2.838   73.230  -25.184 1.00 117.89 ? 860  THR   B CB  1 
ATOM   6668  O  OG1 . THR   B 2 556 ? 2.685   72.556  -23.922 1.00 115.96 ? 860  THR   B OG1 1 
ATOM   6669  C  CG2 . THR   B 2 556 ? 3.414   72.264  -26.231 1.00 114.60 ? 860  THR   B CG2 1 
ATOM   6670  N  N   . VAL   B 2 557 ? 5.165   75.533  -26.703 1.00 110.46 ? 861  VAL   B N   1 
ATOM   6671  C  CA  . VAL   B 2 557 ? 5.487   76.267  -27.928 1.00 110.22 ? 861  VAL   B CA  1 
ATOM   6672  C  C   . VAL   B 2 557 ? 5.679   75.279  -29.092 1.00 117.02 ? 861  VAL   B C   1 
ATOM   6673  O  O   . VAL   B 2 557 ? 6.788   75.129  -29.624 1.00 119.01 ? 861  VAL   B O   1 
ATOM   6674  C  CB  . VAL   B 2 557 ? 6.736   77.154  -27.701 1.00 107.75 ? 861  VAL   B CB  1 
ATOM   6675  C  CG1 . VAL   B 2 557 ? 6.999   78.091  -28.874 1.00 109.24 ? 861  VAL   B CG1 1 
ATOM   6676  C  CG2 . VAL   B 2 557 ? 6.619   77.954  -26.414 1.00 105.54 ? 861  VAL   B CG2 1 
ATOM   6677  N  N   . ALA   B 2 558 ? 4.602   74.579  -29.477 1.00 121.50 ? 862  ALA   B N   1 
ATOM   6678  C  CA  . ALA   B 2 558 ? 4.594   73.561  -30.530 1.00 117.49 ? 862  ALA   B CA  1 
ATOM   6679  C  C   . ALA   B 2 558 ? 5.367   72.289  -30.160 1.00 115.86 ? 862  ALA   B C   1 
ATOM   6680  O  O   . ALA   B 2 558 ? 6.238   72.297  -29.280 1.00 115.16 ? 862  ALA   B O   1 
ATOM   6681  C  CB  . ALA   B 2 558 ? 5.128   74.144  -31.851 1.00 122.66 ? 862  ALA   B CB  1 
ATOM   6682  N  N   . GLU   B 2 559 ? 5.033   71.189  -30.823 1.00 113.78 ? 863  GLU   B N   1 
ATOM   6683  C  CA  . GLU   B 2 559 ? 5.661   69.885  -30.637 1.00 111.39 ? 863  GLU   B CA  1 
ATOM   6684  C  C   . GLU   B 2 559 ? 6.147   69.385  -32.000 1.00 114.44 ? 863  GLU   B C   1 
ATOM   6685  O  O   . GLU   B 2 559 ? 5.997   70.076  -33.016 1.00 120.63 ? 863  GLU   B O   1 
ATOM   6686  C  CB  . GLU   B 2 559 ? 4.675   68.905  -29.991 1.00 112.66 ? 863  GLU   B CB  1 
ATOM   6687  N  N   . LYS   B 2 560 ? 6.756   68.185  -32.014 1.00 104.37 ? 864  LYS   B N   1 
ATOM   6688  C  CA  . LYS   B 2 560 ? 7.239   67.526  -33.241 1.00 100.56 ? 864  LYS   B CA  1 
ATOM   6689  C  C   . LYS   B 2 560 ? 7.240   66.029  -32.968 1.00 99.83  ? 864  LYS   B C   1 
ATOM   6690  O  O   . LYS   B 2 560 ? 8.185   65.524  -32.351 1.00 98.81  ? 864  LYS   B O   1 
ATOM   6691  C  CB  . LYS   B 2 560 ? 8.632   67.988  -33.662 1.00 94.79  ? 864  LYS   B CB  1 
ATOM   6692  N  N   . GLU   B 2 561 ? 6.196   65.332  -33.437 1.00 102.98 ? 865  GLU   B N   1 
ATOM   6693  C  CA  . GLU   B 2 561 ? 6.067   63.890  -33.250 1.00 97.20  ? 865  GLU   B CA  1 
ATOM   6694  C  C   . GLU   B 2 561 ? 7.076   63.155  -34.117 1.00 92.16  ? 865  GLU   B C   1 
ATOM   6695  O  O   . GLU   B 2 561 ? 6.927   63.071  -35.342 1.00 92.85  ? 865  GLU   B O   1 
ATOM   6696  C  CB  . GLU   B 2 561 ? 4.649   63.433  -33.564 1.00 102.15 ? 865  GLU   B CB  1 
ATOM   6697  C  CG  . GLU   B 2 561 ? 4.570   61.935  -33.780 1.00 112.01 ? 865  GLU   B CG  1 
ATOM   6698  C  CD  . GLU   B 2 561 ? 3.366   61.522  -34.603 1.00 122.03 ? 865  GLU   B CD  1 
ATOM   6699  O  OE1 . GLU   B 2 561 ? 2.228   61.904  -34.225 1.00 133.07 ? 865  GLU   B OE1 1 
ATOM   6700  O  OE2 . GLU   B 2 561 ? 3.562   60.817  -35.626 1.00 118.25 ? 865  GLU   B OE2 1 
ATOM   6701  N  N   . VAL   B 2 562 ? 8.103   62.610  -33.478 1.00 92.51  ? 866  VAL   B N   1 
ATOM   6702  C  CA  . VAL   B 2 562 ? 9.149   61.874  -34.143 1.00 91.48  ? 866  VAL   B CA  1 
ATOM   6703  C  C   . VAL   B 2 562 ? 8.779   60.393  -34.159 1.00 91.14  ? 866  VAL   B C   1 
ATOM   6704  O  O   . VAL   B 2 562 ? 7.807   59.968  -33.539 1.00 90.89  ? 866  VAL   B O   1 
ATOM   6705  C  CB  . VAL   B 2 562 ? 10.526  62.131  -33.476 1.00 90.48  ? 866  VAL   B CB  1 
ATOM   6706  C  CG1 . VAL   B 2 562 ? 11.045  63.510  -33.848 1.00 88.45  ? 866  VAL   B CG1 1 
ATOM   6707  C  CG2 . VAL   B 2 562 ? 10.415  61.986  -31.945 1.00 92.26  ? 866  VAL   B CG2 1 
ATOM   6708  N  N   . LYS   B 2 563 ? 9.547   59.596  -34.905 1.00 85.25  ? 867  LYS   B N   1 
ATOM   6709  C  CA  . LYS   B 2 563 ? 9.280   58.164  -35.098 1.00 88.21  ? 867  LYS   B CA  1 
ATOM   6710  C  C   . LYS   B 2 563 ? 10.370  57.349  -34.402 1.00 90.75  ? 867  LYS   B C   1 
ATOM   6711  O  O   . LYS   B 2 563 ? 11.201  56.666  -35.026 1.00 89.31  ? 867  LYS   B O   1 
ATOM   6712  C  CB  . LYS   B 2 563 ? 9.159   57.833  -36.608 1.00 88.99  ? 867  LYS   B CB  1 
ATOM   6713  N  N   . GLY   B 2 564 ? 10.374  57.452  -33.079 1.00 91.88  ? 868  GLY   B N   1 
ATOM   6714  C  CA  . GLY   B 2 564 ? 11.365  56.796  -32.248 1.00 88.20  ? 868  GLY   B CA  1 
ATOM   6715  C  C   . GLY   B 2 564 ? 11.500  57.503  -30.909 1.00 86.88  ? 868  GLY   B C   1 
ATOM   6716  O  O   . GLY   B 2 564 ? 10.643  58.292  -30.510 1.00 86.07  ? 868  GLY   B O   1 
ATOM   6717  N  N   . ALA   B 2 565 ? 12.613  57.198  -30.244 1.00 86.82  ? 869  ALA   B N   1 
ATOM   6718  C  CA  . ALA   B 2 565 ? 12.927  57.699  -28.912 1.00 83.05  ? 869  ALA   B CA  1 
ATOM   6719  C  C   . ALA   B 2 565 ? 13.902  58.859  -29.009 1.00 82.52  ? 869  ALA   B C   1 
ATOM   6720  O  O   . ALA   B 2 565 ? 14.913  58.768  -29.704 1.00 83.30  ? 869  ALA   B O   1 
ATOM   6721  C  CB  . ALA   B 2 565 ? 13.534  56.588  -28.058 1.00 85.52  ? 869  ALA   B CB  1 
ATOM   6722  N  N   . VAL   B 2 566 ? 13.594  59.952  -28.328 1.00 81.81  ? 870  VAL   B N   1 
ATOM   6723  C  CA  . VAL   B 2 566 ? 14.496  61.104  -28.314 1.00 83.21  ? 870  VAL   B CA  1 
ATOM   6724  C  C   . VAL   B 2 566 ? 15.439  60.893  -27.136 1.00 87.00  ? 870  VAL   B C   1 
ATOM   6725  O  O   . VAL   B 2 566 ? 15.288  61.477  -26.066 1.00 88.33  ? 870  VAL   B O   1 
ATOM   6726  C  CB  . VAL   B 2 566 ? 13.725  62.431  -28.233 1.00 84.55  ? 870  VAL   B CB  1 
ATOM   6727  C  CG1 . VAL   B 2 566 ? 14.644  63.599  -28.444 1.00 87.83  ? 870  VAL   B CG1 1 
ATOM   6728  C  CG2 . VAL   B 2 566 ? 12.607  62.469  -29.229 1.00 85.87  ? 870  VAL   B CG2 1 
ATOM   6729  N  N   . TYR   B 2 567 ? 16.444  60.033  -27.341 1.00 88.25  ? 871  TYR   B N   1 
ATOM   6730  C  CA  . TYR   B 2 567 ? 17.308  59.614  -26.235 1.00 86.48  ? 871  TYR   B CA  1 
ATOM   6731  C  C   . TYR   B 2 567 ? 18.071  60.788  -25.629 1.00 91.99  ? 871  TYR   B C   1 
ATOM   6732  O  O   . TYR   B 2 567 ? 18.136  60.937  -24.399 1.00 91.47  ? 871  TYR   B O   1 
ATOM   6733  C  CB  . TYR   B 2 567 ? 18.292  58.547  -26.700 1.00 86.31  ? 871  TYR   B CB  1 
ATOM   6734  C  CG  . TYR   B 2 567 ? 17.674  57.208  -26.917 1.00 83.75  ? 871  TYR   B CG  1 
ATOM   6735  C  CD1 . TYR   B 2 567 ? 17.012  56.553  -25.894 1.00 84.48  ? 871  TYR   B CD1 1 
ATOM   6736  C  CD2 . TYR   B 2 567 ? 17.739  56.608  -28.146 1.00 86.37  ? 871  TYR   B CD2 1 
ATOM   6737  C  CE1 . TYR   B 2 567 ? 16.444  55.324  -26.093 1.00 84.82  ? 871  TYR   B CE1 1 
ATOM   6738  C  CE2 . TYR   B 2 567 ? 17.179  55.379  -28.365 1.00 90.20  ? 871  TYR   B CE2 1 
ATOM   6739  C  CZ  . TYR   B 2 567 ? 16.534  54.733  -27.339 1.00 89.68  ? 871  TYR   B CZ  1 
ATOM   6740  O  OH  . TYR   B 2 567 ? 15.970  53.495  -27.588 1.00 94.96  ? 871  TYR   B OH  1 
ATOM   6741  N  N   . SER   B 2 568 ? 18.673  61.622  -26.477 1.00 99.14  ? 872  SER   B N   1 
ATOM   6742  C  CA  . SER   B 2 568 ? 19.459  62.762  -26.032 1.00 100.72 ? 872  SER   B CA  1 
ATOM   6743  C  C   . SER   B 2 568 ? 19.221  63.938  -26.962 1.00 101.39 ? 872  SER   B C   1 
ATOM   6744  O  O   . SER   B 2 568 ? 18.979  63.766  -28.160 1.00 101.62 ? 872  SER   B O   1 
ATOM   6745  C  CB  . SER   B 2 568 ? 20.969  62.444  -25.984 1.00 99.86  ? 872  SER   B CB  1 
ATOM   6746  O  OG  . SER   B 2 568 ? 21.388  61.909  -24.727 1.00 98.82  ? 872  SER   B OG  1 
ATOM   6747  N  N   . MET   B 2 569 ? 19.292  65.139  -26.394 1.00 98.43  ? 873  MET   B N   1 
ATOM   6748  C  CA  . MET   B 2 569 ? 19.261  66.387  -27.145 1.00 94.70  ? 873  MET   B CA  1 
ATOM   6749  C  C   . MET   B 2 569 ? 20.295  67.332  -26.561 1.00 96.43  ? 873  MET   B C   1 
ATOM   6750  O  O   . MET   B 2 569 ? 20.524  67.349  -25.343 1.00 96.59  ? 873  MET   B O   1 
ATOM   6751  C  CB  . MET   B 2 569 ? 17.886  67.057  -27.107 1.00 86.32  ? 873  MET   B CB  1 
ATOM   6752  C  CG  . MET   B 2 569 ? 16.758  66.101  -27.135 1.00 85.13  ? 873  MET   B CG  1 
ATOM   6753  S  SD  . MET   B 2 569 ? 15.298  66.995  -26.734 1.00 81.91  ? 873  MET   B SD  1 
ATOM   6754  C  CE  . MET   B 2 569 ? 14.979  67.761  -28.301 1.00 91.93  ? 873  MET   B CE  1 
ATOM   6755  N  N   . VAL   B 2 570 ? 20.926  68.107  -27.439 1.00 95.99  ? 874  VAL   B N   1 
ATOM   6756  C  CA  . VAL   B 2 570 ? 21.831  69.177  -27.046 1.00 100.67 ? 874  VAL   B CA  1 
ATOM   6757  C  C   . VAL   B 2 570 ? 21.582  70.354  -27.979 1.00 104.48 ? 874  VAL   B C   1 
ATOM   6758  O  O   . VAL   B 2 570 ? 21.282  70.172  -29.164 1.00 104.03 ? 874  VAL   B O   1 
ATOM   6759  C  CB  . VAL   B 2 570 ? 23.310  68.729  -27.107 1.00 97.10  ? 874  VAL   B CB  1 
ATOM   6760  C  CG1 . VAL   B 2 570 ? 23.524  67.454  -26.330 1.00 90.79  ? 874  VAL   B CG1 1 
ATOM   6761  C  CG2 . VAL   B 2 570 ? 23.732  68.524  -28.532 1.00 98.62  ? 874  VAL   B CG2 1 
ATOM   6762  N  N   . GLU   B 2 571 ? 21.682  71.570  -27.447 1.00 105.76 ? 875  GLU   B N   1 
ATOM   6763  C  CA  . GLU   B 2 571 ? 21.739  72.724  -28.332 1.00 107.51 ? 875  GLU   B CA  1 
ATOM   6764  C  C   . GLU   B 2 571 ? 23.005  72.645  -29.172 1.00 111.17 ? 875  GLU   B C   1 
ATOM   6765  O  O   . GLU   B 2 571 ? 24.067  72.270  -28.673 1.00 115.19 ? 875  GLU   B O   1 
ATOM   6766  C  CB  . GLU   B 2 571 ? 21.730  74.019  -27.535 1.00 108.58 ? 875  GLU   B CB  1 
ATOM   6767  C  CG  . GLU   B 2 571 ? 21.881  75.267  -28.396 1.00 112.20 ? 875  GLU   B CG  1 
ATOM   6768  C  CD  . GLU   B 2 571 ? 23.336  75.653  -28.678 1.00 116.45 ? 875  GLU   B CD  1 
ATOM   6769  O  OE1 . GLU   B 2 571 ? 24.267  75.001  -28.154 1.00 117.86 ? 875  GLU   B OE1 1 
ATOM   6770  O  OE2 . GLU   B 2 571 ? 23.552  76.626  -29.431 1.00 117.49 ? 875  GLU   B OE2 1 
ATOM   6771  N  N   . PHE   B 2 572 ? 22.901  73.012  -30.451 1.00 111.49 ? 876  PHE   B N   1 
ATOM   6772  C  CA  . PHE   B 2 572 ? 24.042  72.978  -31.378 1.00 110.89 ? 876  PHE   B CA  1 
ATOM   6773  C  C   . PHE   B 2 572 ? 24.100  74.305  -32.140 1.00 111.16 ? 876  PHE   B C   1 
ATOM   6774  O  O   . PHE   B 2 572 ? 23.524  74.433  -33.225 1.00 110.52 ? 876  PHE   B O   1 
ATOM   6775  C  CB  . PHE   B 2 572 ? 23.946  71.771  -32.339 1.00 106.98 ? 876  PHE   B CB  1 
ATOM   6776  C  CG  . PHE   B 2 572 ? 25.222  71.492  -33.107 1.00 108.54 ? 876  PHE   B CG  1 
ATOM   6777  C  CD1 . PHE   B 2 572 ? 26.379  71.107  -32.446 1.00 111.42 ? 876  PHE   B CD1 1 
ATOM   6778  C  CD2 . PHE   B 2 572 ? 25.257  71.594  -34.489 1.00 109.81 ? 876  PHE   B CD2 1 
ATOM   6779  C  CE1 . PHE   B 2 572 ? 27.555  70.848  -33.149 1.00 114.39 ? 876  PHE   B CE1 1 
ATOM   6780  C  CE2 . PHE   B 2 572 ? 26.430  71.337  -35.193 1.00 114.51 ? 876  PHE   B CE2 1 
ATOM   6781  C  CZ  . PHE   B 2 572 ? 27.578  70.966  -34.518 1.00 116.20 ? 876  PHE   B CZ  1 
ATOM   6782  N  N   . ASN   B 2 573 ? 24.810  75.283  -31.579 1.00 108.59 ? 877  ASN   B N   1 
ATOM   6783  C  CA  . ASN   B 2 573 ? 25.041  76.574  -32.231 1.00 109.12 ? 877  ASN   B CA  1 
ATOM   6784  C  C   . ASN   B 2 573 ? 23.720  77.238  -32.618 1.00 107.99 ? 877  ASN   B C   1 
ATOM   6785  O  O   . ASN   B 2 573 ? 23.473  77.549  -33.782 1.00 110.64 ? 877  ASN   B O   1 
ATOM   6786  C  CB  . ASN   B 2 573 ? 25.932  76.430  -33.469 1.00 110.03 ? 877  ASN   B CB  1 
ATOM   6787  C  CG  . ASN   B 2 573 ? 27.116  75.503  -33.252 1.00 111.74 ? 877  ASN   B CG  1 
ATOM   6788  O  OD1 . ASN   B 2 573 ? 27.273  74.512  -33.962 1.00 113.85 ? 877  ASN   B OD1 1 
ATOM   6789  N  ND2 . ASN   B 2 573 ? 27.968  75.835  -32.289 1.00 112.86 ? 877  ASN   B ND2 1 
ATOM   6790  N  N   . GLY   B 2 574 ? 22.862  77.447  -31.621 1.00 110.89 ? 878  GLY   B N   1 
ATOM   6791  C  CA  . GLY   B 2 574 ? 21.550  78.006  -31.855 1.00 109.06 ? 878  GLY   B CA  1 
ATOM   6792  C  C   . GLY   B 2 574 ? 20.586  77.077  -32.548 1.00 110.79 ? 878  GLY   B C   1 
ATOM   6793  O  O   . GLY   B 2 574 ? 19.458  77.486  -32.848 1.00 112.61 ? 878  GLY   B O   1 
ATOM   6794  N  N   . LYS   B 2 575 ? 21.004  75.846  -32.830 1.00 110.42 ? 879  LYS   B N   1 
ATOM   6795  C  CA  . LYS   B 2 575 ? 20.157  74.793  -33.363 1.00 106.35 ? 879  LYS   B CA  1 
ATOM   6796  C  C   . LYS   B 2 575 ? 19.896  73.751  -32.265 1.00 103.86 ? 879  LYS   B C   1 
ATOM   6797  O  O   . LYS   B 2 575 ? 20.279  73.912  -31.102 1.00 105.91 ? 879  LYS   B O   1 
ATOM   6798  C  CB  . LYS   B 2 575 ? 20.800  74.187  -34.618 1.00 102.21 ? 879  LYS   B CB  1 
ATOM   6799  N  N   . LEU   B 2 576 ? 19.207  72.678  -32.635 1.00 102.00 ? 880  LEU   B N   1 
ATOM   6800  C  CA  . LEU   B 2 576 ? 18.886  71.593  -31.715 1.00 100.82 ? 880  LEU   B CA  1 
ATOM   6801  C  C   . LEU   B 2 576 ? 19.270  70.286  -32.391 1.00 102.12 ? 880  LEU   B C   1 
ATOM   6802  O  O   . LEU   B 2 576 ? 18.772  69.987  -33.484 1.00 98.52  ? 880  LEU   B O   1 
ATOM   6803  C  CB  . LEU   B 2 576 ? 17.399  71.598  -31.341 1.00 98.99  ? 880  LEU   B CB  1 
ATOM   6804  C  CG  . LEU   B 2 576 ? 16.885  70.554  -30.351 1.00 90.26  ? 880  LEU   B CG  1 
ATOM   6805  C  CD1 . LEU   B 2 576 ? 17.011  71.062  -28.941 1.00 92.61  ? 880  LEU   B CD1 1 
ATOM   6806  C  CD2 . LEU   B 2 576 ? 15.454  70.198  -30.676 1.00 88.53  ? 880  LEU   B CD2 1 
ATOM   6807  N  N   . LEU   B 2 577 ? 20.175  69.524  -31.755 1.00 101.24 ? 881  LEU   B N   1 
ATOM   6808  C  CA  . LEU   B 2 577 ? 20.642  68.222  -32.239 1.00 101.08 ? 881  LEU   B CA  1 
ATOM   6809  C  C   . LEU   B 2 577 ? 19.992  67.135  -31.395 1.00 98.15  ? 881  LEU   B C   1 
ATOM   6810  O  O   . LEU   B 2 577 ? 20.375  66.933  -30.238 1.00 99.90  ? 881  LEU   B O   1 
ATOM   6811  C  CB  . LEU   B 2 577 ? 22.166  68.123  -32.168 1.00 102.80 ? 881  LEU   B CB  1 
ATOM   6812  C  CG  . LEU   B 2 577 ? 22.935  67.033  -32.934 1.00 100.89 ? 881  LEU   B CG  1 
ATOM   6813  C  CD1 . LEU   B 2 577 ? 22.759  67.164  -34.458 1.00 101.13 ? 881  LEU   B CD1 1 
ATOM   6814  C  CD2 . LEU   B 2 577 ? 24.425  67.051  -32.559 1.00 101.39 ? 881  LEU   B CD2 1 
ATOM   6815  N  N   . ALA   B 2 578 ? 19.002  66.452  -31.960 1.00 92.99  ? 882  ALA   B N   1 
ATOM   6816  C  CA  . ALA   B 2 578 ? 18.291  65.382  -31.273 1.00 91.32  ? 882  ALA   B CA  1 
ATOM   6817  C  C   . ALA   B 2 578 ? 18.714  64.042  -31.856 1.00 93.95  ? 882  ALA   B C   1 
ATOM   6818  O  O   . ALA   B 2 578 ? 18.914  63.926  -33.066 1.00 100.36 ? 882  ALA   B O   1 
ATOM   6819  C  CB  . ALA   B 2 578 ? 16.774  65.556  -31.410 1.00 86.64  ? 882  ALA   B CB  1 
ATOM   6820  N  N   . SER   B 2 579 ? 18.875  63.031  -31.011 1.00 92.15  ? 883  SER   B N   1 
ATOM   6821  C  CA  . SER   B 2 579 ? 19.023  61.670  -31.513 1.00 91.04  ? 883  SER   B CA  1 
ATOM   6822  C  C   . SER   B 2 579 ? 17.674  60.971  -31.422 1.00 88.72  ? 883  SER   B C   1 
ATOM   6823  O  O   . SER   B 2 579 ? 16.978  61.067  -30.405 1.00 88.84  ? 883  SER   B O   1 
ATOM   6824  C  CB  . SER   B 2 579 ? 20.114  60.882  -30.771 1.00 92.51  ? 883  SER   B CB  1 
ATOM   6825  O  OG  . SER   B 2 579 ? 20.039  60.987  -29.359 1.00 94.83  ? 883  SER   B OG  1 
ATOM   6826  N  N   . ILE   B 2 580 ? 17.287  60.325  -32.509 1.00 87.22  ? 884  ILE   B N   1 
ATOM   6827  C  CA  . ILE   B 2 580 ? 16.054  59.561  -32.586 1.00 85.84  ? 884  ILE   B CA  1 
ATOM   6828  C  C   . ILE   B 2 580 ? 16.470  58.171  -33.053 1.00 88.77  ? 884  ILE   B C   1 
ATOM   6829  O  O   . ILE   B 2 580 ? 16.777  57.962  -34.236 1.00 90.85  ? 884  ILE   B O   1 
ATOM   6830  C  CB  . ILE   B 2 580 ? 15.027  60.205  -33.523 1.00 84.87  ? 884  ILE   B CB  1 
ATOM   6831  C  CG1 . ILE   B 2 580 ? 14.757  61.642  -33.082 1.00 85.84  ? 884  ILE   B CG1 1 
ATOM   6832  C  CG2 . ILE   B 2 580 ? 13.743  59.407  -33.563 1.00 85.44  ? 884  ILE   B CG2 1 
ATOM   6833  C  CD1 . ILE   B 2 580 ? 15.364  62.678  -34.012 1.00 90.17  ? 884  ILE   B CD1 1 
ATOM   6834  N  N   . ASN   B 2 581 ? 16.526  57.234  -32.109 1.00 86.80  ? 885  ASN   B N   1 
ATOM   6835  C  CA  . ASN   B 2 581 ? 16.922  55.852  -32.342 1.00 85.92  ? 885  ASN   B CA  1 
ATOM   6836  C  C   . ASN   B 2 581 ? 18.321  55.921  -32.924 1.00 89.61  ? 885  ASN   B C   1 
ATOM   6837  O  O   . ASN   B 2 581 ? 19.197  56.526  -32.304 1.00 94.08  ? 885  ASN   B O   1 
ATOM   6838  C  CB  . ASN   B 2 581 ? 15.913  55.175  -33.248 1.00 84.43  ? 885  ASN   B CB  1 
ATOM   6839  C  CG  . ASN   B 2 581 ? 14.624  54.885  -32.515 1.00 85.55  ? 885  ASN   B CG  1 
ATOM   6840  O  OD1 . ASN   B 2 581 ? 14.479  55.241  -31.349 1.00 85.97  ? 885  ASN   B OD1 1 
ATOM   6841  N  ND2 . ASN   B 2 581 ? 13.685  54.240  -33.182 1.00 93.20  ? 885  ASN   B ND2 1 
ATOM   6842  N  N   . SER   B 2 582 ? 18.564  55.351  -34.100 1.00 88.91  ? 886  SER   B N   1 
ATOM   6843  C  CA  . SER   B 2 582 ? 19.897  55.416  -34.686 1.00 91.87  ? 886  SER   B CA  1 
ATOM   6844  C  C   . SER   B 2 582 ? 20.208  56.585  -35.616 1.00 96.14  ? 886  SER   B C   1 
ATOM   6845  O  O   . SER   B 2 582 ? 21.030  56.462  -36.519 1.00 100.46 ? 886  SER   B O   1 
ATOM   6846  C  CB  . SER   B 2 582 ? 20.129  54.102  -35.408 1.00 94.69  ? 886  SER   B CB  1 
ATOM   6847  O  OG  . SER   B 2 582 ? 19.337  54.033  -36.571 1.00 96.65  ? 886  SER   B OG  1 
ATOM   6848  N  N   . THR   B 2 583 ? 19.587  57.736  -35.384 1.00 95.25  ? 887  THR   B N   1 
ATOM   6849  C  CA  . THR   B 2 583 ? 19.702  58.894  -36.264 1.00 96.40  ? 887  THR   B CA  1 
ATOM   6850  C  C   . THR   B 2 583 ? 20.070  60.128  -35.447 1.00 96.24  ? 887  THR   B C   1 
ATOM   6851  O  O   . THR   B 2 583 ? 19.363  60.477  -34.497 1.00 96.45  ? 887  THR   B O   1 
ATOM   6852  C  CB  . THR   B 2 583 ? 18.387  59.125  -37.013 1.00 92.40  ? 887  THR   B CB  1 
ATOM   6853  O  OG1 . THR   B 2 583 ? 18.155  58.037  -37.913 1.00 92.11  ? 887  THR   B OG1 1 
ATOM   6854  C  CG2 . THR   B 2 583 ? 18.425  60.421  -37.794 1.00 97.26  ? 887  THR   B CG2 1 
ATOM   6855  N  N   . VAL   B 2 584 ? 21.163  60.794  -35.814 1.00 97.15  ? 888  VAL   B N   1 
ATOM   6856  C  CA  . VAL   B 2 584 ? 21.500  62.092  -35.241 1.00 94.73  ? 888  VAL   B CA  1 
ATOM   6857  C  C   . VAL   B 2 584 ? 20.934  63.148  -36.185 1.00 100.87 ? 888  VAL   B C   1 
ATOM   6858  O  O   . VAL   B 2 584 ? 21.473  63.382  -37.266 1.00 108.33 ? 888  VAL   B O   1 
ATOM   6859  C  CB  . VAL   B 2 584 ? 23.012  62.268  -35.047 1.00 95.34  ? 888  VAL   B CB  1 
ATOM   6860  C  CG1 . VAL   B 2 584 ? 23.278  63.502  -34.213 1.00 94.75  ? 888  VAL   B CG1 1 
ATOM   6861  C  CG2 . VAL   B 2 584 ? 23.615  61.051  -34.379 1.00 97.09  ? 888  VAL   B CG2 1 
ATOM   6862  N  N   . ARG   B 2 585 ? 19.822  63.759  -35.792 1.00 98.80  ? 889  ARG   B N   1 
ATOM   6863  C  CA  . ARG   B 2 585 ? 19.132  64.754  -36.603 1.00 96.67  ? 889  ARG   B CA  1 
ATOM   6864  C  C   . ARG   B 2 585 ? 19.505  66.144  -36.119 1.00 97.32  ? 889  ARG   B C   1 
ATOM   6865  O  O   . ARG   B 2 585 ? 19.612  66.377  -34.914 1.00 97.88  ? 889  ARG   B O   1 
ATOM   6866  C  CB  . ARG   B 2 585 ? 17.619  64.560  -36.505 1.00 96.13  ? 889  ARG   B CB  1 
ATOM   6867  C  CG  . ARG   B 2 585 ? 16.823  65.481  -37.374 1.00 98.83  ? 889  ARG   B CG  1 
ATOM   6868  C  CD  . ARG   B 2 585 ? 15.385  65.042  -37.419 1.00 96.43  ? 889  ARG   B CD  1 
ATOM   6869  N  NE  . ARG   B 2 585 ? 15.262  63.610  -37.637 1.00 98.55  ? 889  ARG   B NE  1 
ATOM   6870  C  CZ  . ARG   B 2 585 ? 14.134  62.998  -37.965 1.00 98.30  ? 889  ARG   B CZ  1 
ATOM   6871  N  NH1 . ARG   B 2 585 ? 12.995  63.664  -38.079 1.00 97.42  ? 889  ARG   B NH1 1 
ATOM   6872  N  NH2 . ARG   B 2 585 ? 14.152  61.688  -38.200 1.00 98.61  ? 889  ARG   B NH2 1 
ATOM   6873  N  N   . LEU   B 2 586 ? 19.709  67.068  -37.051 1.00 101.97 ? 890  LEU   B N   1 
ATOM   6874  C  CA  . LEU   B 2 586 ? 19.872  68.470  -36.689 1.00 101.54 ? 890  LEU   B CA  1 
ATOM   6875  C  C   . LEU   B 2 586 ? 18.604  69.251  -37.027 1.00 101.20 ? 890  LEU   B C   1 
ATOM   6876  O  O   . LEU   B 2 586 ? 18.003  69.054  -38.087 1.00 100.85 ? 890  LEU   B O   1 
ATOM   6877  C  CB  . LEU   B 2 586 ? 21.080  69.079  -37.390 1.00 101.07 ? 890  LEU   B CB  1 
ATOM   6878  C  CG  . LEU   B 2 586 ? 21.535  70.454  -36.908 1.00 102.90 ? 890  LEU   B CG  1 
ATOM   6879  C  CD1 . LEU   B 2 586 ? 21.543  70.599  -35.385 1.00 99.61  ? 890  LEU   B CD1 1 
ATOM   6880  C  CD2 . LEU   B 2 586 ? 22.920  70.704  -37.475 1.00 114.08 ? 890  LEU   B CD2 1 
ATOM   6881  N  N   . TYR   B 2 587 ? 18.180  70.114  -36.104 1.00 98.64  ? 891  TYR   B N   1 
ATOM   6882  C  CA  . TYR   B 2 587 ? 16.964  70.894  -36.267 1.00 98.82  ? 891  TYR   B CA  1 
ATOM   6883  C  C   . TYR   B 2 587 ? 17.298  72.378  -36.239 1.00 101.01 ? 891  TYR   B C   1 
ATOM   6884  O  O   . TYR   B 2 587 ? 18.299  72.788  -35.650 1.00 102.79 ? 891  TYR   B O   1 
ATOM   6885  C  CB  . TYR   B 2 587 ? 15.958  70.589  -35.172 1.00 95.86  ? 891  TYR   B CB  1 
ATOM   6886  C  CG  . TYR   B 2 587 ? 15.105  69.365  -35.394 1.00 96.23  ? 891  TYR   B CG  1 
ATOM   6887  C  CD1 . TYR   B 2 587 ? 14.029  69.383  -36.262 1.00 101.45 ? 891  TYR   B CD1 1 
ATOM   6888  C  CD2 . TYR   B 2 587 ? 15.360  68.192  -34.706 1.00 101.26 ? 891  TYR   B CD2 1 
ATOM   6889  C  CE1 . TYR   B 2 587 ? 13.229  68.249  -36.449 1.00 103.96 ? 891  TYR   B CE1 1 
ATOM   6890  C  CE2 . TYR   B 2 587 ? 14.568  67.062  -34.883 1.00 100.65 ? 891  TYR   B CE2 1 
ATOM   6891  C  CZ  . TYR   B 2 587 ? 13.509  67.096  -35.749 1.00 97.15  ? 891  TYR   B CZ  1 
ATOM   6892  O  OH  . TYR   B 2 587 ? 12.756  65.959  -35.899 1.00 95.33  ? 891  TYR   B OH  1 
ATOM   6893  N  N   . GLU   B 2 588 ? 16.458  73.184  -36.886 1.00 103.48 ? 892  GLU   B N   1 
ATOM   6894  C  CA  . GLU   B 2 588 ? 16.554  74.633  -36.808 1.00 104.69 ? 892  GLU   B CA  1 
ATOM   6895  C  C   . GLU   B 2 588 ? 15.226  75.178  -36.301 1.00 109.38 ? 892  GLU   B C   1 
ATOM   6896  O  O   . GLU   B 2 588 ? 14.181  74.533  -36.446 1.00 107.15 ? 892  GLU   B O   1 
ATOM   6897  C  CB  . GLU   B 2 588 ? 16.921  75.247  -38.170 1.00 104.44 ? 892  GLU   B CB  1 
ATOM   6898  C  CG  . GLU   B 2 588 ? 18.163  74.625  -38.796 1.00 110.00 ? 892  GLU   B CG  1 
ATOM   6899  C  CD  . GLU   B 2 588 ? 18.676  75.359  -40.034 1.00 120.36 ? 892  GLU   B CD  1 
ATOM   6900  O  OE1 . GLU   B 2 588 ? 17.876  75.631  -40.955 1.00 123.82 ? 892  GLU   B OE1 1 
ATOM   6901  O  OE2 . GLU   B 2 588 ? 19.895  75.651  -40.093 1.00 124.92 ? 892  GLU   B OE2 1 
ATOM   6902  N  N   . TRP   B 2 589 ? 15.280  76.361  -35.680 1.00 110.95 ? 893  TRP   B N   1 
ATOM   6903  C  CA  . TRP   B 2 589 ? 14.093  77.023  -35.139 1.00 116.62 ? 893  TRP   B CA  1 
ATOM   6904  C  C   . TRP   B 2 589 ? 13.620  78.034  -36.177 1.00 124.93 ? 893  TRP   B C   1 
ATOM   6905  O  O   . TRP   B 2 589 ? 14.340  78.990  -36.482 1.00 128.80 ? 893  TRP   B O   1 
ATOM   6906  C  CB  . TRP   B 2 589 ? 14.428  77.687  -33.805 1.00 114.94 ? 893  TRP   B CB  1 
ATOM   6907  C  CG  . TRP   B 2 589 ? 13.276  78.165  -32.943 1.00 115.77 ? 893  TRP   B CG  1 
ATOM   6908  C  CD1 . TRP   B 2 589 ? 13.187  79.371  -32.297 1.00 119.39 ? 893  TRP   B CD1 1 
ATOM   6909  C  CD2 . TRP   B 2 589 ? 12.092  77.444  -32.597 1.00 115.42 ? 893  TRP   B CD2 1 
ATOM   6910  N  NE1 . TRP   B 2 589 ? 12.017  79.446  -31.583 1.00 116.90 ? 893  TRP   B NE1 1 
ATOM   6911  C  CE2 . TRP   B 2 589 ? 11.326  78.278  -31.753 1.00 116.05 ? 893  TRP   B CE2 1 
ATOM   6912  C  CE3 . TRP   B 2 589 ? 11.598  76.182  -32.923 1.00 116.30 ? 893  TRP   B CE3 1 
ATOM   6913  C  CZ2 . TRP   B 2 589 ? 10.099  77.890  -31.238 1.00 117.79 ? 893  TRP   B CZ2 1 
ATOM   6914  C  CZ3 . TRP   B 2 589 ? 10.378  75.802  -32.411 1.00 119.45 ? 893  TRP   B CZ3 1 
ATOM   6915  C  CH2 . TRP   B 2 589 ? 9.638   76.653  -31.580 1.00 118.37 ? 893  TRP   B CH2 1 
ATOM   6916  N  N   . THR   B 2 590 ? 12.428  77.821  -36.738 1.00 130.13 ? 894  THR   B N   1 
ATOM   6917  C  CA  . THR   B 2 590 ? 11.970  78.640  -37.852 1.00 131.89 ? 894  THR   B CA  1 
ATOM   6918  C  C   . THR   B 2 590 ? 11.243  79.883  -37.359 1.00 133.71 ? 894  THR   B C   1 
ATOM   6919  O  O   . THR   B 2 590 ? 10.792  79.968  -36.215 1.00 130.94 ? 894  THR   B O   1 
ATOM   6920  C  CB  . THR   B 2 590 ? 11.054  77.854  -38.795 1.00 134.64 ? 894  THR   B CB  1 
ATOM   6921  O  OG1 . THR   B 2 590 ? 11.077  78.473  -40.083 1.00 140.53 ? 894  THR   B OG1 1 
ATOM   6922  C  CG2 . THR   B 2 590 ? 9.612   77.858  -38.298 1.00 138.76 ? 894  THR   B CG2 1 
ATOM   6923  N  N   . THR   B 2 591 ? 11.132  80.854  -38.263 1.00 136.14 ? 895  THR   B N   1 
ATOM   6924  C  CA  . THR   B 2 591 ? 10.602  82.158  -37.892 1.00 140.24 ? 895  THR   B CA  1 
ATOM   6925  C  C   . THR   B 2 591 ? 9.212   82.043  -37.267 1.00 142.22 ? 895  THR   B C   1 
ATOM   6926  O  O   . THR   B 2 591 ? 8.905   82.751  -36.300 1.00 141.69 ? 895  THR   B O   1 
ATOM   6927  C  CB  . THR   B 2 591 ? 10.601  83.066  -39.120 1.00 139.72 ? 895  THR   B CB  1 
ATOM   6928  O  OG1 . THR   B 2 591 ? 9.690   82.548  -40.092 1.00 142.74 ? 895  THR   B OG1 1 
ATOM   6929  C  CG2 . THR   B 2 591 ? 11.994  83.097  -39.745 1.00 135.40 ? 895  THR   B CG2 1 
ATOM   6930  N  N   . GLU   B 2 592 ? 8.415   81.115  -37.793 1.00 148.42 ? 896  GLU   B N   1 
ATOM   6931  C  CA  . GLU   B 2 592 ? 7.044   80.909  -37.267 1.00 147.20 ? 896  GLU   B CA  1 
ATOM   6932  C  C   . GLU   B 2 592 ? 7.112   79.946  -36.080 1.00 148.05 ? 896  GLU   B C   1 
ATOM   6933  O  O   . GLU   B 2 592 ? 6.122   79.218  -35.865 1.00 147.24 ? 896  GLU   B O   1 
ATOM   6934  C  CB  . GLU   B 2 592 ? 6.154   80.350  -38.372 1.00 150.50 ? 896  GLU   B CB  1 
ATOM   6935  C  CG  . GLU   B 2 592 ? 6.281   81.117  -39.684 1.00 156.42 ? 896  GLU   B CG  1 
ATOM   6936  C  CD  . GLU   B 2 592 ? 7.183   80.456  -40.710 1.00 160.19 ? 896  GLU   B CD  1 
ATOM   6937  O  OE1 . GLU   B 2 592 ? 8.373   80.238  -40.400 1.00 158.20 ? 896  GLU   B OE1 1 
ATOM   6938  O  OE2 . GLU   B 2 592 ? 6.695   80.160  -41.819 1.00 163.39 ? 896  GLU   B OE2 1 
ATOM   6939  N  N   . LYS   B 2 593 ? 8.239   79.932  -35.365 1.00 145.23 ? 897  LYS   B N   1 
ATOM   6940  C  CA  . LYS   B 2 593 ? 8.370   79.088  -34.150 1.00 136.60 ? 897  LYS   B CA  1 
ATOM   6941  C  C   . LYS   B 2 593 ? 8.143   77.583  -34.329 1.00 138.73 ? 897  LYS   B C   1 
ATOM   6942  O  O   . LYS   B 2 593 ? 7.360   77.008  -33.548 1.00 134.65 ? 897  LYS   B O   1 
ATOM   6943  C  CB  . LYS   B 2 593 ? 7.446   79.604  -33.045 1.00 129.59 ? 897  LYS   B CB  1 
ATOM   6944  N  N   . GLU   B 2 594 ? 8.834   76.970  -35.291 1.00 146.71 ? 898  GLU   B N   1 
ATOM   6945  C  CA  . GLU   B 2 594 ? 8.730   75.502  -35.491 1.00 146.27 ? 898  GLU   B CA  1 
ATOM   6946  C  C   . GLU   B 2 594 ? 10.094  74.864  -35.790 1.00 146.16 ? 898  GLU   B C   1 
ATOM   6947  O  O   . GLU   B 2 594 ? 10.936  75.531  -36.415 1.00 147.00 ? 898  GLU   B O   1 
ATOM   6948  C  CB  . GLU   B 2 594 ? 7.747   75.328  -36.649 1.00 148.01 ? 898  GLU   B CB  1 
ATOM   6949  C  CG  . GLU   B 2 594 ? 7.371   73.875  -36.922 1.00 151.26 ? 898  GLU   B CG  1 
ATOM   6950  C  CD  . GLU   B 2 594 ? 7.182   73.010  -35.689 1.00 157.39 ? 898  GLU   B CD  1 
ATOM   6951  O  OE1 . GLU   B 2 594 ? 6.213   73.245  -34.939 1.00 152.10 ? 898  GLU   B OE1 1 
ATOM   6952  O  OE2 . GLU   B 2 594 ? 8.007   72.096  -35.480 1.00 159.42 ? 898  GLU   B OE2 1 
ATOM   6953  N  N   . LEU   B 2 595 ? 10.310  73.632  -35.331 1.00 131.05 ? 899  LEU   B N   1 
ATOM   6954  C  CA  . LEU   B 2 595 ? 11.576  72.918  -35.622 1.00 124.16 ? 899  LEU   B CA  1 
ATOM   6955  C  C   . LEU   B 2 595 ? 11.526  72.422  -37.070 1.00 118.51 ? 899  LEU   B C   1 
ATOM   6956  O  O   . LEU   B 2 595 ? 10.435  72.011  -37.508 1.00 124.28 ? 899  LEU   B O   1 
ATOM   6957  C  CB  . LEU   B 2 595 ? 11.716  71.752  -34.647 1.00 120.87 ? 899  LEU   B CB  1 
ATOM   6958  C  CG  . LEU   B 2 595 ? 11.875  72.103  -33.165 1.00 107.59 ? 899  LEU   B CG  1 
ATOM   6959  C  CD1 . LEU   B 2 595 ? 11.860  70.882  -32.270 1.00 103.92 ? 899  LEU   B CD1 1 
ATOM   6960  C  CD2 . LEU   B 2 595 ? 13.140  72.910  -32.947 1.00 108.15 ? 899  LEU   B CD2 1 
ATOM   6961  N  N   . ARG   B 2 596 ? 12.658  72.442  -37.774 1.00 107.61 ? 900  ARG   B N   1 
ATOM   6962  C  CA  . ARG   B 2 596 ? 12.677  71.887  -39.151 1.00 110.11 ? 900  ARG   B CA  1 
ATOM   6963  C  C   . ARG   B 2 596 ? 13.993  71.147  -39.400 1.00 108.09 ? 900  ARG   B C   1 
ATOM   6964  O  O   . ARG   B 2 596 ? 15.050  71.667  -39.004 1.00 109.66 ? 900  ARG   B O   1 
ATOM   6965  C  CB  . ARG   B 2 596 ? 12.511  72.977  -40.211 1.00 114.23 ? 900  ARG   B CB  1 
ATOM   6966  C  CG  . ARG   B 2 596 ? 11.148  73.648  -40.139 1.00 115.87 ? 900  ARG   B CG  1 
ATOM   6967  C  CD  . ARG   B 2 596 ? 11.030  74.794  -41.133 1.00 119.42 ? 900  ARG   B CD  1 
ATOM   6968  N  NE  . ARG   B 2 596 ? 11.116  74.349  -42.528 1.00 125.15 ? 900  ARG   B NE  1 
ATOM   6969  C  CZ  . ARG   B 2 596 ? 11.155  75.165  -43.573 1.00 116.03 ? 900  ARG   B CZ  1 
ATOM   6970  N  NH1 . ARG   B 2 596 ? 11.080  76.471  -43.397 1.00 104.14 ? 900  ARG   B NH1 1 
ATOM   6971  N  NH2 . ARG   B 2 596 ? 11.266  74.671  -44.792 1.00 118.22 ? 900  ARG   B NH2 1 
ATOM   6972  N  N   . THR   B 2 597 ? 13.916  69.986  -40.048 1.00 107.96 ? 901  THR   B N   1 
ATOM   6973  C  CA  . THR   B 2 597 ? 15.115  69.201  -40.324 1.00 105.75 ? 901  THR   B CA  1 
ATOM   6974  C  C   . THR   B 2 597 ? 16.035  69.934  -41.281 1.00 107.47 ? 901  THR   B C   1 
ATOM   6975  O  O   . THR   B 2 597 ? 15.615  70.325  -42.371 1.00 111.11 ? 901  THR   B O   1 
ATOM   6976  C  CB  . THR   B 2 597 ? 14.746  67.855  -40.947 1.00 108.75 ? 901  THR   B CB  1 
ATOM   6977  O  OG1 . THR   B 2 597 ? 13.673  67.245  -40.210 1.00 110.92 ? 901  THR   B OG1 1 
ATOM   6978  C  CG2 . THR   B 2 597 ? 15.973  66.921  -40.985 1.00 108.94 ? 901  THR   B CG2 1 
ATOM   6979  N  N   . GLU   B 2 598 ? 17.296  70.106  -40.892 1.00 110.37 ? 902  GLU   B N   1 
ATOM   6980  C  CA  . GLU   B 2 598 ? 18.317  70.557  -41.830 1.00 112.56 ? 902  GLU   B CA  1 
ATOM   6981  C  C   . GLU   B 2 598 ? 19.032  69.386  -42.480 1.00 116.77 ? 902  GLU   B C   1 
ATOM   6982  O  O   . GLU   B 2 598 ? 19.103  69.299  -43.708 1.00 121.34 ? 902  GLU   B O   1 
ATOM   6983  C  CB  . GLU   B 2 598 ? 19.347  71.451  -41.138 1.00 108.99 ? 902  GLU   B CB  1 
ATOM   6984  C  CG  . GLU   B 2 598 ? 20.409  71.954  -42.101 1.00 118.36 ? 902  GLU   B CG  1 
ATOM   6985  C  CD  . GLU   B 2 598 ? 21.676  72.472  -41.427 1.00 121.82 ? 902  GLU   B CD  1 
ATOM   6986  O  OE1 . GLU   B 2 598 ? 21.674  72.649  -40.197 1.00 117.00 ? 902  GLU   B OE1 1 
ATOM   6987  O  OE2 . GLU   B 2 598 ? 22.680  72.703  -42.142 1.00 127.91 ? 902  GLU   B OE2 1 
ATOM   6988  N  N   . CYS   B 2 599 ? 19.553  68.476  -41.664 1.00 123.13 ? 903  CYS   B N   1 
ATOM   6989  C  CA  . CYS   B 2 599 ? 20.317  67.338  -42.137 1.00 126.12 ? 903  CYS   B CA  1 
ATOM   6990  C  C   . CYS   B 2 599 ? 20.006  66.131  -41.269 1.00 123.96 ? 903  CYS   B C   1 
ATOM   6991  O  O   . CYS   B 2 599 ? 19.458  66.245  -40.171 1.00 119.96 ? 903  CYS   B O   1 
ATOM   6992  C  CB  . CYS   B 2 599 ? 21.817  67.631  -42.106 1.00 129.45 ? 903  CYS   B CB  1 
ATOM   6993  S  SG  . CYS   B 2 599 ? 22.265  68.615  -40.663 1.00 132.09 ? 903  CYS   B SG  1 
ATOM   6994  N  N   . ASN   B 2 600 ? 20.377  64.968  -41.777 1.00 122.73 ? 904  ASN   B N   1 
ATOM   6995  C  CA  . ASN   B 2 600 ? 20.173  63.720  -41.065 1.00 116.29 ? 904  ASN   B CA  1 
ATOM   6996  C  C   . ASN   B 2 600 ? 21.439  62.890  -41.181 1.00 117.03 ? 904  ASN   B C   1 
ATOM   6997  O  O   . ASN   B 2 600 ? 22.077  62.860  -42.241 1.00 117.95 ? 904  ASN   B O   1 
ATOM   6998  C  CB  . ASN   B 2 600 ? 18.973  62.942  -41.626 1.00 116.80 ? 904  ASN   B CB  1 
ATOM   6999  C  CG  . ASN   B 2 600 ? 17.745  63.062  -40.759 1.00 110.97 ? 904  ASN   B CG  1 
ATOM   7000  O  OD1 . ASN   B 2 600 ? 17.848  63.291  -39.560 1.00 109.26 ? 904  ASN   B OD1 1 
ATOM   7001  N  ND2 . ASN   B 2 600 ? 16.574  62.910  -41.360 1.00 110.30 ? 904  ASN   B ND2 1 
ATOM   7002  N  N   . HIS   B 2 601 ? 21.800  62.226  -40.083 1.00 110.35 ? 905  HIS   B N   1 
ATOM   7003  C  CA  . HIS   B 2 601 ? 22.888  61.252  -40.073 1.00 109.15 ? 905  HIS   B CA  1 
ATOM   7004  C  C   . HIS   B 2 601 ? 22.397  59.963  -39.433 1.00 106.66 ? 905  HIS   B C   1 
ATOM   7005  O  O   . HIS   B 2 601 ? 22.184  59.905  -38.218 1.00 105.12 ? 905  HIS   B O   1 
ATOM   7006  C  CB  . HIS   B 2 601 ? 24.109  61.773  -39.331 1.00 105.38 ? 905  HIS   B CB  1 
ATOM   7007  C  CG  . HIS   B 2 601 ? 25.345  60.972  -39.594 1.00 106.39 ? 905  HIS   B CG  1 
ATOM   7008  N  ND1 . HIS   B 2 601 ? 25.513  59.685  -39.127 1.00 107.75 ? 905  HIS   B ND1 1 
ATOM   7009  C  CD2 . HIS   B 2 601 ? 26.474  61.274  -40.277 1.00 108.24 ? 905  HIS   B CD2 1 
ATOM   7010  C  CE1 . HIS   B 2 601 ? 26.699  59.235  -39.499 1.00 106.46 ? 905  HIS   B CE1 1 
ATOM   7011  N  NE2 . HIS   B 2 601 ? 27.302  60.181  -40.197 1.00 106.52 ? 905  HIS   B NE2 1 
ATOM   7012  N  N   . TYR   B 2 602 ? 22.228  58.930  -40.242 1.00 104.81 ? 906  TYR   B N   1 
ATOM   7013  C  CA  . TYR   B 2 602 ? 21.753  57.657  -39.745 1.00 103.12 ? 906  TYR   B CA  1 
ATOM   7014  C  C   . TYR   B 2 602 ? 22.956  56.791  -39.394 1.00 105.17 ? 906  TYR   B C   1 
ATOM   7015  O  O   . TYR   B 2 602 ? 23.895  56.682  -40.185 1.00 107.22 ? 906  TYR   B O   1 
ATOM   7016  C  CB  . TYR   B 2 602 ? 20.873  56.996  -40.796 1.00 104.24 ? 906  TYR   B CB  1 
ATOM   7017  C  CG  . TYR   B 2 602 ? 19.971  57.967  -41.527 1.00 105.87 ? 906  TYR   B CG  1 
ATOM   7018  C  CD1 . TYR   B 2 602 ? 18.794  58.427  -40.949 1.00 105.17 ? 906  TYR   B CD1 1 
ATOM   7019  C  CD2 . TYR   B 2 602 ? 20.284  58.406  -42.808 1.00 107.99 ? 906  TYR   B CD2 1 
ATOM   7020  C  CE1 . TYR   B 2 602 ? 17.952  59.304  -41.631 1.00 104.15 ? 906  TYR   B CE1 1 
ATOM   7021  C  CE2 . TYR   B 2 602 ? 19.455  59.278  -43.490 1.00 111.03 ? 906  TYR   B CE2 1 
ATOM   7022  C  CZ  . TYR   B 2 602 ? 18.294  59.722  -42.896 1.00 110.13 ? 906  TYR   B CZ  1 
ATOM   7023  O  OH  . TYR   B 2 602 ? 17.477  60.589  -43.579 1.00 120.77 ? 906  TYR   B OH  1 
ATOM   7024  N  N   . ASN   B 2 603 ? 22.946  56.217  -38.195 1.00 108.97 ? 907  ASN   B N   1 
ATOM   7025  C  CA  . ASN   B 2 603 ? 24.043  55.391  -37.707 1.00 106.91 ? 907  ASN   B CA  1 
ATOM   7026  C  C   . ASN   B 2 603 ? 23.634  53.928  -37.678 1.00 103.10 ? 907  ASN   B C   1 
ATOM   7027  O  O   . ASN   B 2 603 ? 22.467  53.572  -37.869 1.00 103.78 ? 907  ASN   B O   1 
ATOM   7028  C  CB  . ASN   B 2 603 ? 24.475  55.800  -36.291 1.00 108.58 ? 907  ASN   B CB  1 
ATOM   7029  C  CG  . ASN   B 2 603 ? 24.702  57.294  -36.144 1.00 107.82 ? 907  ASN   B CG  1 
ATOM   7030  O  OD1 . ASN   B 2 603 ? 24.000  57.969  -35.377 1.00 106.62 ? 907  ASN   B OD1 1 
ATOM   7031  N  ND2 . ASN   B 2 603 ? 25.694  57.816  -36.864 1.00 109.21 ? 907  ASN   B ND2 1 
ATOM   7032  N  N   . ASN   B 2 604 ? 24.627  53.084  -37.392 1.00 100.62 ? 908  ASN   B N   1 
ATOM   7033  C  CA  . ASN   B 2 604 ? 24.452  51.652  -37.190 1.00 97.97  ? 908  ASN   B CA  1 
ATOM   7034  C  C   . ASN   B 2 604 ? 24.427  51.288  -35.714 1.00 100.45 ? 908  ASN   B C   1 
ATOM   7035  O  O   . ASN   B 2 604 ? 24.407  50.103  -35.371 1.00 100.95 ? 908  ASN   B O   1 
ATOM   7036  C  CB  . ASN   B 2 604 ? 25.569  50.882  -37.901 1.00 97.70  ? 908  ASN   B CB  1 
ATOM   7037  C  CG  . ASN   B 2 604 ? 26.958  51.324  -37.450 1.00 101.27 ? 908  ASN   B CG  1 
ATOM   7038  O  OD1 . ASN   B 2 604 ? 27.390  52.455  -37.709 1.00 104.88 ? 908  ASN   B OD1 1 
ATOM   7039  N  ND2 . ASN   B 2 604 ? 27.671  50.425  -36.783 1.00 104.24 ? 908  ASN   B ND2 1 
ATOM   7040  N  N   . ILE   B 2 605 ? 24.446  52.286  -34.837 1.00 102.61 ? 909  ILE   B N   1 
ATOM   7041  C  CA  . ILE   B 2 605 ? 24.307  52.103  -33.403 1.00 100.54 ? 909  ILE   B CA  1 
ATOM   7042  C  C   . ILE   B 2 605 ? 23.143  52.966  -32.936 1.00 103.82 ? 909  ILE   B C   1 
ATOM   7043  O  O   . ILE   B 2 605 ? 22.749  53.934  -33.593 1.00 101.17 ? 909  ILE   B O   1 
ATOM   7044  C  CB  . ILE   B 2 605 ? 25.598  52.479  -32.654 1.00 95.80  ? 909  ILE   B CB  1 
ATOM   7045  C  CG1 . ILE   B 2 605 ? 25.910  53.957  -32.877 1.00 97.27  ? 909  ILE   B CG1 1 
ATOM   7046  C  CG2 . ILE   B 2 605 ? 26.738  51.630  -33.125 1.00 97.36  ? 909  ILE   B CG2 1 
ATOM   7047  C  CD1 . ILE   B 2 605 ? 27.181  54.437  -32.204 1.00 97.76  ? 909  ILE   B CD1 1 
ATOM   7048  N  N   . MET   B 2 606 ? 22.564  52.575  -31.800 1.00 106.69 ? 910  MET   B N   1 
ATOM   7049  C  CA  . MET   B 2 606 ? 21.462  53.381  -31.222 1.00 104.54 ? 910  MET   B CA  1 
ATOM   7050  C  C   . MET   B 2 606 ? 22.086  54.623  -30.576 1.00 103.70 ? 910  MET   B C   1 
ATOM   7051  O  O   . MET   B 2 606 ? 22.808  54.463  -29.570 1.00 104.62 ? 910  MET   B O   1 
ATOM   7052  C  CB  . MET   B 2 606 ? 20.696  52.575  -30.169 1.00 105.38 ? 910  MET   B CB  1 
ATOM   7053  C  CG  . MET   B 2 606 ? 19.412  53.231  -29.714 1.00 109.07 ? 910  MET   B CG  1 
ATOM   7054  S  SD  . MET   B 2 606 ? 17.969  52.180  -29.969 1.00 130.40 ? 910  MET   B SD  1 
ATOM   7055  C  CE  . MET   B 2 606 ? 17.931  52.102  -31.765 1.00 109.55 ? 910  MET   B CE  1 
ATOM   7056  N  N   . ALA   B 2 607 ? 21.849  55.800  -31.158 1.00 96.28  ? 911  ALA   B N   1 
ATOM   7057  C  CA  . ALA   B 2 607 ? 22.448  57.044  -30.621 1.00 91.76  ? 911  ALA   B CA  1 
ATOM   7058  C  C   . ALA   B 2 607 ? 21.929  57.281  -29.201 1.00 93.57  ? 911  ALA   B C   1 
ATOM   7059  O  O   . ALA   B 2 607 ? 20.921  58.002  -29.037 1.00 88.96  ? 911  ALA   B O   1 
ATOM   7060  C  CB  . ALA   B 2 607 ? 22.141  58.201  -31.544 1.00 91.86  ? 911  ALA   B CB  1 
ATOM   7061  N  N   . LEU   B 2 608 ? 22.590  56.681  -28.207 1.00 95.04  ? 912  LEU   B N   1 
ATOM   7062  C  CA  . LEU   B 2 608 ? 22.155  56.822  -26.794 1.00 90.84  ? 912  LEU   B CA  1 
ATOM   7063  C  C   . LEU   B 2 608 ? 22.735  58.118  -26.222 1.00 92.41  ? 912  LEU   B C   1 
ATOM   7064  O  O   . LEU   B 2 608 ? 21.956  58.932  -25.680 1.00 92.85  ? 912  LEU   B O   1 
ATOM   7065  C  CB  . LEU   B 2 608 ? 22.652  55.614  -26.004 1.00 89.93  ? 912  LEU   B CB  1 
ATOM   7066  C  CG  . LEU   B 2 608 ? 22.060  54.260  -26.403 1.00 91.44  ? 912  LEU   B CG  1 
ATOM   7067  C  CD1 . LEU   B 2 608 ? 22.748  53.151  -25.643 1.00 93.74  ? 912  LEU   B CD1 1 
ATOM   7068  C  CD2 . LEU   B 2 608 ? 20.569  54.232  -26.139 1.00 87.79  ? 912  LEU   B CD2 1 
ATOM   7069  N  N   . TYR   B 2 609 ? 24.051  58.296  -26.349 1.00 89.73  ? 913  TYR   B N   1 
ATOM   7070  C  CA  . TYR   B 2 609 ? 24.718  59.485  -25.757 1.00 90.44  ? 913  TYR   B CA  1 
ATOM   7071  C  C   . TYR   B 2 609 ? 24.987  60.513  -26.850 1.00 90.77  ? 913  TYR   B C   1 
ATOM   7072  O  O   . TYR   B 2 609 ? 25.383  60.124  -27.971 1.00 94.53  ? 913  TYR   B O   1 
ATOM   7073  C  CB  . TYR   B 2 609 ? 25.990  58.983  -25.069 1.00 89.81  ? 913  TYR   B CB  1 
ATOM   7074  C  CG  . TYR   B 2 609 ? 25.773  57.774  -24.168 1.00 87.10  ? 913  TYR   B CG  1 
ATOM   7075  C  CD1 . TYR   B 2 609 ? 25.276  57.922  -22.880 1.00 87.80  ? 913  TYR   B CD1 1 
ATOM   7076  C  CD2 . TYR   B 2 609 ? 26.060  56.487  -24.606 1.00 88.06  ? 913  TYR   B CD2 1 
ATOM   7077  C  CE1 . TYR   B 2 609 ? 25.075  56.829  -22.055 1.00 84.81  ? 913  TYR   B CE1 1 
ATOM   7078  C  CE2 . TYR   B 2 609 ? 25.859  55.384  -23.793 1.00 89.01  ? 913  TYR   B CE2 1 
ATOM   7079  C  CZ  . TYR   B 2 609 ? 25.365  55.556  -22.513 1.00 82.89  ? 913  TYR   B CZ  1 
ATOM   7080  O  OH  . TYR   B 2 609 ? 25.162  54.478  -21.704 1.00 81.75  ? 913  TYR   B OH  1 
ATOM   7081  N  N   . LEU   B 2 610 ? 24.775  61.795  -26.535 1.00 91.27  ? 914  LEU   B N   1 
ATOM   7082  C  CA  . LEU   B 2 610 ? 25.025  62.879  -27.519 1.00 90.44  ? 914  LEU   B CA  1 
ATOM   7083  C  C   . LEU   B 2 610 ? 25.833  63.995  -26.842 1.00 92.27  ? 914  LEU   B C   1 
ATOM   7084  O  O   . LEU   B 2 610 ? 25.250  64.720  -26.010 1.00 96.38  ? 914  LEU   B O   1 
ATOM   7085  C  CB  . LEU   B 2 610 ? 23.702  63.405  -28.074 1.00 90.59  ? 914  LEU   B CB  1 
ATOM   7086  C  CG  . LEU   B 2 610 ? 23.694  63.765  -29.562 1.00 92.13  ? 914  LEU   B CG  1 
ATOM   7087  C  CD1 . LEU   B 2 610 ? 24.286  62.635  -30.386 1.00 94.96  ? 914  LEU   B CD1 1 
ATOM   7088  C  CD2 . LEU   B 2 610 ? 22.284  64.086  -30.026 1.00 93.58  ? 914  LEU   B CD2 1 
ATOM   7089  N  N   . LYS   B 2 611 ? 27.122  64.110  -27.169 1.00 93.14  ? 915  LYS   B N   1 
ATOM   7090  C  CA  . LYS   B 2 611 ? 27.953  65.174  -26.616 1.00 97.06  ? 915  LYS   B CA  1 
ATOM   7091  C  C   . LYS   B 2 611 ? 28.535  66.011  -27.750 1.00 102.66 ? 915  LYS   B C   1 
ATOM   7092  O  O   . LYS   B 2 611 ? 28.820  65.501  -28.838 1.00 104.34 ? 915  LYS   B O   1 
ATOM   7093  C  CB  . LYS   B 2 611 ? 29.105  64.631  -25.732 1.00 95.70  ? 915  LYS   B CB  1 
ATOM   7094  C  CG  . LYS   B 2 611 ? 28.686  64.018  -24.383 1.00 91.74  ? 915  LYS   B CG  1 
ATOM   7095  C  CD  . LYS   B 2 611 ? 27.841  64.972  -23.564 1.00 92.27  ? 915  LYS   B CD  1 
ATOM   7096  C  CE  . LYS   B 2 611 ? 26.978  64.261  -22.527 1.00 89.47  ? 915  LYS   B CE  1 
ATOM   7097  N  NZ  . LYS   B 2 611 ? 27.727  63.806  -21.311 1.00 94.37  ? 915  LYS   B NZ  1 
ATOM   7098  N  N   . THR   B 2 612 ? 28.722  67.307  -27.485 1.00 104.55 ? 916  THR   B N   1 
ATOM   7099  C  CA  . THR   B 2 612 ? 29.114  68.257  -28.521 1.00 104.38 ? 916  THR   B CA  1 
ATOM   7100  C  C   . THR   B 2 612 ? 30.056  69.320  -27.969 1.00 103.02 ? 916  THR   B C   1 
ATOM   7101  O  O   . THR   B 2 612 ? 29.803  69.914  -26.912 1.00 103.68 ? 916  THR   B O   1 
ATOM   7102  C  CB  . THR   B 2 612 ? 27.876  68.913  -29.151 1.00 103.41 ? 916  THR   B CB  1 
ATOM   7103  O  OG1 . THR   B 2 612 ? 28.288  69.879  -30.120 1.00 107.69 ? 916  THR   B OG1 1 
ATOM   7104  C  CG2 . THR   B 2 612 ? 27.003  69.585  -28.082 1.00 104.55 ? 916  THR   B CG2 1 
ATOM   7105  N  N   . LYS   B 2 613 ? 31.151  69.552  -28.688 1.00 106.90 ? 917  LYS   B N   1 
ATOM   7106  C  CA  . LYS   B 2 613 ? 32.119  70.594  -28.368 1.00 102.82 ? 917  LYS   B CA  1 
ATOM   7107  C  C   . LYS   B 2 613 ? 32.299  71.400  -29.642 1.00 112.04 ? 917  LYS   B C   1 
ATOM   7108  O  O   . LYS   B 2 613 ? 33.113  71.033  -30.493 1.00 111.23 ? 917  LYS   B O   1 
ATOM   7109  C  CB  . LYS   B 2 613 ? 33.418  70.016  -27.899 1.00 98.28  ? 917  LYS   B CB  1 
ATOM   7110  C  CG  . LYS   B 2 613 ? 34.398  71.042  -27.446 1.00 103.48 ? 917  LYS   B CG  1 
ATOM   7111  C  CD  . LYS   B 2 613 ? 35.801  70.522  -27.592 1.00 108.66 ? 917  LYS   B CD  1 
ATOM   7112  C  CE  . LYS   B 2 613 ? 36.701  71.139  -26.564 1.00 110.45 ? 917  LYS   B CE  1 
ATOM   7113  N  NZ  . LYS   B 2 613 ? 36.329  70.605  -25.226 1.00 115.10 ? 917  LYS   B NZ  1 
ATOM   7114  N  N   . GLY   B 2 614 ? 31.527  72.478  -29.770 1.00 114.38 ? 918  GLY   B N   1 
ATOM   7115  C  CA  . GLY   B 2 614 ? 31.629  73.377  -30.907 1.00 120.06 ? 918  GLY   B CA  1 
ATOM   7116  C  C   . GLY   B 2 614 ? 30.956  72.889  -32.174 1.00 121.29 ? 918  GLY   B C   1 
ATOM   7117  O  O   . GLY   B 2 614 ? 29.790  73.201  -32.428 1.00 119.45 ? 918  GLY   B O   1 
ATOM   7118  N  N   . ASP   B 2 615 ? 31.698  72.147  -32.995 1.00 137.14 ? 919  ASP   B N   1 
ATOM   7119  C  CA  . ASP   B 2 615 ? 31.159  71.563  -34.209 1.00 137.16 ? 919  ASP   B CA  1 
ATOM   7120  C  C   . ASP   B 2 615 ? 31.364  70.056  -34.269 1.00 136.10 ? 919  ASP   B C   1 
ATOM   7121  O  O   . ASP   B 2 615 ? 30.878  69.425  -35.214 1.00 135.93 ? 919  ASP   B O   1 
ATOM   7122  C  CB  . ASP   B 2 615 ? 31.783  72.222  -35.454 1.00 142.75 ? 919  ASP   B CB  1 
ATOM   7123  C  CG  . ASP   B 2 615 ? 31.107  73.555  -35.838 1.00 146.76 ? 919  ASP   B CG  1 
ATOM   7124  O  OD1 . ASP   B 2 615 ? 31.583  74.634  -35.393 1.00 144.23 ? 919  ASP   B OD1 1 
ATOM   7125  O  OD2 . ASP   B 2 615 ? 30.109  73.519  -36.604 1.00 147.09 ? 919  ASP   B OD2 1 
ATOM   7126  N  N   . PHE   B 2 616 ? 32.060  69.467  -33.289 1.00 130.59 ? 920  PHE   B N   1 
ATOM   7127  C  CA  . PHE   B 2 616 ? 32.249  68.020  -33.187 1.00 130.50 ? 920  PHE   B CA  1 
ATOM   7128  C  C   . PHE   B 2 616 ? 31.081  67.382  -32.437 1.00 128.52 ? 920  PHE   B C   1 
ATOM   7129  O  O   . PHE   B 2 616 ? 30.621  67.904  -31.418 1.00 127.85 ? 920  PHE   B O   1 
ATOM   7130  C  CB  . PHE   B 2 616 ? 33.552  67.681  -32.448 1.00 131.20 ? 920  PHE   B CB  1 
ATOM   7131  C  CG  . PHE   B 2 616 ? 34.805  67.713  -33.307 1.00 134.12 ? 920  PHE   B CG  1 
ATOM   7132  C  CD1 . PHE   B 2 616 ? 34.769  68.109  -34.638 1.00 135.34 ? 920  PHE   B CD1 1 
ATOM   7133  C  CD2 . PHE   B 2 616 ? 36.033  67.328  -32.765 1.00 133.08 ? 920  PHE   B CD2 1 
ATOM   7134  C  CE1 . PHE   B 2 616 ? 35.939  68.139  -35.405 1.00 134.79 ? 920  PHE   B CE1 1 
ATOM   7135  C  CE2 . PHE   B 2 616 ? 37.196  67.346  -33.530 1.00 130.51 ? 920  PHE   B CE2 1 
ATOM   7136  C  CZ  . PHE   B 2 616 ? 37.146  67.751  -34.850 1.00 132.93 ? 920  PHE   B CZ  1 
ATOM   7137  N  N   . ILE   B 2 617 ? 30.619  66.234  -32.922 1.00 115.96 ? 921  ILE   B N   1 
ATOM   7138  C  CA  . ILE   B 2 617 ? 29.499  65.525  -32.317 1.00 110.31 ? 921  ILE   B CA  1 
ATOM   7139  C  C   . ILE   B 2 617 ? 29.987  64.156  -31.887 1.00 108.15 ? 921  ILE   B C   1 
ATOM   7140  O  O   . ILE   B 2 617 ? 30.613  63.444  -32.676 1.00 110.23 ? 921  ILE   B O   1 
ATOM   7141  C  CB  . ILE   B 2 617 ? 28.320  65.388  -33.289 1.00 110.84 ? 921  ILE   B CB  1 
ATOM   7142  C  CG1 . ILE   B 2 617 ? 27.768  66.762  -33.648 1.00 110.09 ? 921  ILE   B CG1 1 
ATOM   7143  C  CG2 . ILE   B 2 617 ? 27.257  64.468  -32.721 1.00 107.54 ? 921  ILE   B CG2 1 
ATOM   7144  C  CD1 . ILE   B 2 617 ? 27.637  66.931  -35.115 1.00 114.11 ? 921  ILE   B CD1 1 
ATOM   7145  N  N   . LEU   B 2 618 ? 29.698  63.780  -30.647 1.00 105.51 ? 922  LEU   B N   1 
ATOM   7146  C  CA  . LEU   B 2 618 ? 30.047  62.463  -30.137 1.00 102.23 ? 922  LEU   B CA  1 
ATOM   7147  C  C   . LEU   B 2 618 ? 28.781  61.634  -29.977 1.00 101.26 ? 922  LEU   B C   1 
ATOM   7148  O  O   . LEU   B 2 618 ? 27.787  62.111  -29.420 1.00 102.72 ? 922  LEU   B O   1 
ATOM   7149  C  CB  . LEU   B 2 618 ? 30.792  62.559  -28.806 1.00 98.99  ? 922  LEU   B CB  1 
ATOM   7150  C  CG  . LEU   B 2 618 ? 31.497  61.263  -28.421 1.00 97.86  ? 922  LEU   B CG  1 
ATOM   7151  C  CD1 . LEU   B 2 618 ? 32.176  60.632  -29.633 1.00 100.75 ? 922  LEU   B CD1 1 
ATOM   7152  C  CD2 . LEU   B 2 618 ? 32.497  61.538  -27.322 1.00 97.81  ? 922  LEU   B CD2 1 
ATOM   7153  N  N   . VAL   B 2 619 ? 28.817  60.403  -30.475 1.00 99.68  ? 923  VAL   B N   1 
ATOM   7154  C  CA  . VAL   B 2 619 ? 27.688  59.490  -30.399 1.00 95.21  ? 923  VAL   B CA  1 
ATOM   7155  C  C   . VAL   B 2 619 ? 28.139  58.238  -29.667 1.00 93.09  ? 923  VAL   B C   1 
ATOM   7156  O  O   . VAL   B 2 619 ? 29.275  57.787  -29.825 1.00 95.39  ? 923  VAL   B O   1 
ATOM   7157  C  CB  . VAL   B 2 619 ? 27.140  59.149  -31.798 1.00 97.49  ? 923  VAL   B CB  1 
ATOM   7158  C  CG1 . VAL   B 2 619 ? 26.000  58.161  -31.685 1.00 99.35  ? 923  VAL   B CG1 1 
ATOM   7159  C  CG2 . VAL   B 2 619 ? 26.679  60.410  -32.503 1.00 96.47  ? 923  VAL   B CG2 1 
ATOM   7160  N  N   . GLY   B 2 620 ? 27.246  57.685  -28.853 1.00 89.46  ? 924  GLY   B N   1 
ATOM   7161  C  CA  . GLY   B 2 620 ? 27.589  56.575  -27.997 1.00 90.76  ? 924  GLY   B CA  1 
ATOM   7162  C  C   . GLY   B 2 620 ? 26.433  55.609  -27.883 1.00 95.57  ? 924  GLY   B C   1 
ATOM   7163  O  O   . GLY   B 2 620 ? 25.302  55.905  -28.269 1.00 98.47  ? 924  GLY   B O   1 
ATOM   7164  N  N   . ASP   B 2 621 ? 26.732  54.451  -27.320 1.00 98.31  ? 925  ASP   B N   1 
ATOM   7165  C  CA  . ASP   B 2 621 ? 25.822  53.325  -27.344 1.00 97.82  ? 925  ASP   B CA  1 
ATOM   7166  C  C   . ASP   B 2 621 ? 26.241  52.438  -26.190 1.00 96.70  ? 925  ASP   B C   1 
ATOM   7167  O  O   . ASP   B 2 621 ? 27.434  52.361  -25.907 1.00 98.02  ? 925  ASP   B O   1 
ATOM   7168  C  CB  . ASP   B 2 621 ? 25.938  52.633  -28.703 1.00 100.91 ? 925  ASP   B CB  1 
ATOM   7169  C  CG  . ASP   B 2 621 ? 25.237  51.316  -28.763 1.00 105.61 ? 925  ASP   B CG  1 
ATOM   7170  O  OD1 . ASP   B 2 621 ? 24.122  51.230  -28.206 1.00 108.97 ? 925  ASP   B OD1 1 
ATOM   7171  O  OD2 . ASP   B 2 621 ? 25.779  50.376  -29.403 1.00 104.33 ? 925  ASP   B OD2 1 
ATOM   7172  N  N   . LEU   B 2 622 ? 25.276  51.824  -25.492 1.00 90.10  ? 926  LEU   B N   1 
ATOM   7173  C  CA  . LEU   B 2 622 ? 25.552  51.049  -24.271 1.00 81.54  ? 926  LEU   B CA  1 
ATOM   7174  C  C   . LEU   B 2 622 ? 26.852  50.251  -24.364 1.00 85.15  ? 926  LEU   B C   1 
ATOM   7175  O  O   . LEU   B 2 622 ? 27.581  50.170  -23.377 1.00 89.12  ? 926  LEU   B O   1 
ATOM   7176  C  CB  . LEU   B 2 622 ? 24.378  50.126  -23.914 1.00 76.44  ? 926  LEU   B CB  1 
ATOM   7177  C  CG  . LEU   B 2 622 ? 23.357  50.533  -22.861 1.00 76.05  ? 926  LEU   B CG  1 
ATOM   7178  C  CD1 . LEU   B 2 622 ? 22.690  51.812  -23.465 1.00 90.82  ? 926  LEU   B CD1 1 
ATOM   7179  C  CD2 . LEU   B 2 622 ? 22.303  49.471  -22.698 1.00 77.35  ? 926  LEU   B CD2 1 
ATOM   7180  N  N   . MET   B 2 623 ? 27.142  49.619  -25.504 1.00 86.87  ? 927  MET   B N   1 
ATOM   7181  C  CA  . MET   B 2 623 ? 28.282  48.705  -25.608 1.00 84.86  ? 927  MET   B CA  1 
ATOM   7182  C  C   . MET   B 2 623 ? 29.560  49.369  -26.114 1.00 85.89  ? 927  MET   B C   1 
ATOM   7183  O  O   . MET   B 2 623 ? 30.195  48.920  -27.061 1.00 91.39  ? 927  MET   B O   1 
ATOM   7184  C  CB  . MET   B 2 623 ? 27.871  47.534  -26.501 1.00 85.39  ? 927  MET   B CB  1 
ATOM   7185  C  CG  . MET   B 2 623 ? 26.570  46.893  -26.100 1.00 80.71  ? 927  MET   B CG  1 
ATOM   7186  S  SD  . MET   B 2 623 ? 26.154  45.332  -26.870 1.00 89.80  ? 927  MET   B SD  1 
ATOM   7187  C  CE  . MET   B 2 623 ? 27.263  44.151  -26.140 1.00 83.02  ? 927  MET   B CE  1 
ATOM   7188  N  N   . ARG   B 2 624 ? 29.948  50.441  -25.422 1.00 86.31  ? 928  ARG   B N   1 
ATOM   7189  C  CA  . ARG   B 2 624 ? 31.083  51.285  -25.787 1.00 91.82  ? 928  ARG   B CA  1 
ATOM   7190  C  C   . ARG   B 2 624 ? 31.191  51.461  -27.299 1.00 96.83  ? 928  ARG   B C   1 
ATOM   7191  O  O   . ARG   B 2 624 ? 32.185  51.067  -27.918 1.00 100.57 ? 928  ARG   B O   1 
ATOM   7192  C  CB  . ARG   B 2 624 ? 32.384  50.716  -25.215 1.00 92.29  ? 928  ARG   B CB  1 
ATOM   7193  C  CG  . ARG   B 2 624 ? 33.601  51.584  -25.467 1.00 90.66  ? 928  ARG   B CG  1 
ATOM   7194  C  CD  . ARG   B 2 624 ? 34.481  51.589  -24.293 1.00 94.26  ? 928  ARG   B CD  1 
ATOM   7195  N  NE  . ARG   B 2 624 ? 35.508  50.557  -24.281 1.00 104.10 ? 928  ARG   B NE  1 
ATOM   7196  C  CZ  . ARG   B 2 624 ? 36.656  50.625  -24.939 1.00 109.64 ? 928  ARG   B CZ  1 
ATOM   7197  N  NH1 . ARG   B 2 624 ? 36.883  51.569  -25.844 1.00 108.40 ? 928  ARG   B NH1 1 
ATOM   7198  N  NH2 . ARG   B 2 624 ? 37.594  49.712  -24.696 1.00 116.40 ? 928  ARG   B NH2 1 
ATOM   7199  N  N   . SER   B 2 625 ? 30.162  52.026  -27.919 1.00 97.63  ? 929  SER   B N   1 
ATOM   7200  C  CA  . SER   B 2 625 ? 30.184  52.273  -29.355 1.00 98.35  ? 929  SER   B CA  1 
ATOM   7201  C  C   . SER   B 2 625 ? 30.381  53.775  -29.544 1.00 100.27 ? 929  SER   B C   1 
ATOM   7202  O  O   . SER   B 2 625 ? 29.420  54.528  -29.689 1.00 103.46 ? 929  SER   B O   1 
ATOM   7203  C  CB  . SER   B 2 625 ? 28.886  51.755  -30.045 1.00 94.72  ? 929  SER   B CB  1 
ATOM   7204  O  OG  . SER   B 2 625 ? 28.635  50.389  -29.759 1.00 88.16  ? 929  SER   B OG  1 
ATOM   7205  N  N   . VAL   B 2 626 ? 31.645  54.219  -29.527 1.00 102.38 ? 930  VAL   B N   1 
ATOM   7206  C  CA  . VAL   B 2 626 ? 31.917  55.636  -29.750 1.00 101.24 ? 930  VAL   B CA  1 
ATOM   7207  C  C   . VAL   B 2 626 ? 31.998  55.911  -31.245 1.00 100.73 ? 930  VAL   B C   1 
ATOM   7208  O  O   . VAL   B 2 626 ? 32.296  55.034  -32.062 1.00 101.29 ? 930  VAL   B O   1 
ATOM   7209  C  CB  . VAL   B 2 626 ? 33.192  56.111  -29.036 1.00 97.76  ? 930  VAL   B CB  1 
ATOM   7210  C  CG1 . VAL   B 2 626 ? 32.961  56.210  -27.546 1.00 94.20  ? 930  VAL   B CG1 1 
ATOM   7211  C  CG2 . VAL   B 2 626 ? 34.320  55.151  -29.308 1.00 107.55 ? 930  VAL   B CG2 1 
ATOM   7212  N  N   . LEU   B 2 627 ? 31.752  57.165  -31.586 1.00 100.56 ? 931  LEU   B N   1 
ATOM   7213  C  CA  . LEU   B 2 627 ? 31.548  57.578  -32.963 1.00 104.01 ? 931  LEU   B CA  1 
ATOM   7214  C  C   . LEU   B 2 627 ? 31.588  59.104  -33.041 1.00 109.51 ? 931  LEU   B C   1 
ATOM   7215  O  O   . LEU   B 2 627 ? 30.692  59.785  -32.525 1.00 109.05 ? 931  LEU   B O   1 
ATOM   7216  C  CB  . LEU   B 2 627 ? 30.215  57.038  -33.472 1.00 96.59  ? 931  LEU   B CB  1 
ATOM   7217  C  CG  . LEU   B 2 627 ? 29.757  57.709  -34.753 1.00 97.89  ? 931  LEU   B CG  1 
ATOM   7218  C  CD1 . LEU   B 2 627 ? 30.731  57.369  -35.854 1.00 106.49 ? 931  LEU   B CD1 1 
ATOM   7219  C  CD2 . LEU   B 2 627 ? 28.339  57.323  -35.105 1.00 95.69  ? 931  LEU   B CD2 1 
ATOM   7220  N  N   . LEU   B 2 628 ? 32.615  59.661  -33.669 1.00 109.15 ? 932  LEU   B N   1 
ATOM   7221  C  CA  . LEU   B 2 628 ? 32.771  61.103  -33.737 1.00 106.33 ? 932  LEU   B CA  1 
ATOM   7222  C  C   . LEU   B 2 628 ? 32.325  61.595  -35.112 1.00 107.01 ? 932  LEU   B C   1 
ATOM   7223  O  O   . LEU   B 2 628 ? 32.776  61.073  -36.138 1.00 107.28 ? 932  LEU   B O   1 
ATOM   7224  C  CB  . LEU   B 2 628 ? 34.224  61.483  -33.433 1.00 108.22 ? 932  LEU   B CB  1 
ATOM   7225  C  CG  . LEU   B 2 628 ? 34.559  62.951  -33.123 1.00 116.23 ? 932  LEU   B CG  1 
ATOM   7226  C  CD1 . LEU   B 2 628 ? 33.937  63.415  -31.800 1.00 116.07 ? 932  LEU   B CD1 1 
ATOM   7227  C  CD2 . LEU   B 2 628 ? 36.075  63.236  -33.148 1.00 119.15 ? 932  LEU   B CD2 1 
ATOM   7228  N  N   . LEU   B 2 629 ? 31.404  62.566  -35.122 1.00 109.38 ? 933  LEU   B N   1 
ATOM   7229  C  CA  . LEU   B 2 629 ? 30.884  63.243  -36.325 1.00 110.59 ? 933  LEU   B CA  1 
ATOM   7230  C  C   . LEU   B 2 629 ? 31.312  64.709  -36.346 1.00 111.74 ? 933  LEU   B C   1 
ATOM   7231  O  O   . LEU   B 2 629 ? 31.916  65.229  -35.404 1.00 114.82 ? 933  LEU   B O   1 
ATOM   7232  C  CB  . LEU   B 2 629 ? 29.358  63.188  -36.408 1.00 108.00 ? 933  LEU   B CB  1 
ATOM   7233  C  CG  . LEU   B 2 629 ? 28.586  61.872  -36.408 1.00 107.12 ? 933  LEU   B CG  1 
ATOM   7234  C  CD1 . LEU   B 2 629 ? 27.093  62.188  -36.494 1.00 102.11 ? 933  LEU   B CD1 1 
ATOM   7235  C  CD2 . LEU   B 2 629 ? 29.040  60.899  -37.510 1.00 104.83 ? 933  LEU   B CD2 1 
ATOM   7236  N  N   . ALA   B 2 630 ? 30.953  65.396  -37.428 1.00 109.86 ? 934  ALA   B N   1 
ATOM   7237  C  CA  . ALA   B 2 630 ? 31.282  66.806  -37.575 1.00 114.44 ? 934  ALA   B CA  1 
ATOM   7238  C  C   . ALA   B 2 630 ? 30.346  67.430  -38.603 1.00 118.79 ? 934  ALA   B C   1 
ATOM   7239  O  O   . ALA   B 2 630 ? 30.215  66.911  -39.716 1.00 120.56 ? 934  ALA   B O   1 
ATOM   7240  C  CB  . ALA   B 2 630 ? 32.740  66.986  -37.996 1.00 115.48 ? 934  ALA   B CB  1 
ATOM   7241  N  N   . TYR   B 2 631 ? 29.698  68.530  -38.223 1.00 119.40 ? 935  TYR   B N   1 
ATOM   7242  C  CA  . TYR   B 2 631 ? 28.734  69.201  -39.098 1.00 123.36 ? 935  TYR   B CA  1 
ATOM   7243  C  C   . TYR   B 2 631 ? 29.488  70.175  -39.995 1.00 132.31 ? 935  TYR   B C   1 
ATOM   7244  O  O   . TYR   B 2 631 ? 29.873  71.269  -39.566 1.00 132.39 ? 935  TYR   B O   1 
ATOM   7245  C  CB  . TYR   B 2 631 ? 27.668  69.902  -38.267 1.00 123.55 ? 935  TYR   B CB  1 
ATOM   7246  C  CG  . TYR   B 2 631 ? 26.851  70.938  -39.010 1.00 129.51 ? 935  TYR   B CG  1 
ATOM   7247  C  CD1 . TYR   B 2 631 ? 25.994  70.574  -40.046 1.00 127.62 ? 935  TYR   B CD1 1 
ATOM   7248  C  CD2 . TYR   B 2 631 ? 26.920  72.286  -38.658 1.00 127.24 ? 935  TYR   B CD2 1 
ATOM   7249  C  CE1 . TYR   B 2 631 ? 25.240  71.533  -40.714 1.00 126.89 ? 935  TYR   B CE1 1 
ATOM   7250  C  CE2 . TYR   B 2 631 ? 26.170  73.239  -39.313 1.00 123.28 ? 935  TYR   B CE2 1 
ATOM   7251  C  CZ  . TYR   B 2 631 ? 25.335  72.862  -40.336 1.00 127.45 ? 935  TYR   B CZ  1 
ATOM   7252  O  OH  . TYR   B 2 631 ? 24.597  73.826  -40.980 1.00 132.95 ? 935  TYR   B OH  1 
ATOM   7253  N  N   . LYS   B 2 632 ? 29.715  69.765  -41.242 1.00 145.30 ? 936  LYS   B N   1 
ATOM   7254  C  CA  . LYS   B 2 632 ? 30.380  70.629  -42.208 1.00 145.13 ? 936  LYS   B CA  1 
ATOM   7255  C  C   . LYS   B 2 632 ? 29.478  71.825  -42.491 1.00 146.08 ? 936  LYS   B C   1 
ATOM   7256  O  O   . LYS   B 2 632 ? 28.344  71.637  -42.959 1.00 144.79 ? 936  LYS   B O   1 
ATOM   7257  C  CB  . LYS   B 2 632 ? 30.696  69.863  -43.491 1.00 145.69 ? 936  LYS   B CB  1 
ATOM   7258  N  N   . PRO   B 2 633 ? 29.930  73.063  -42.228 1.00 138.59 ? 937  PRO   B N   1 
ATOM   7259  C  CA  . PRO   B 2 633 ? 29.009  74.210  -42.215 1.00 134.73 ? 937  PRO   B CA  1 
ATOM   7260  C  C   . PRO   B 2 633 ? 28.400  74.528  -43.568 1.00 137.04 ? 937  PRO   B C   1 
ATOM   7261  O  O   . PRO   B 2 633 ? 27.173  74.476  -43.724 1.00 138.26 ? 937  PRO   B O   1 
ATOM   7262  C  CB  . PRO   B 2 633 ? 29.894  75.367  -41.732 1.00 131.93 ? 937  PRO   B CB  1 
ATOM   7263  C  CG  . PRO   B 2 633 ? 31.061  74.711  -41.092 1.00 138.99 ? 937  PRO   B CG  1 
ATOM   7264  C  CD  . PRO   B 2 633 ? 31.298  73.461  -41.875 1.00 138.76 ? 937  PRO   B CD  1 
ATOM   7265  N  N   . MET   B 2 634 ? 29.241  74.887  -44.546 1.00 136.50 ? 938  MET   B N   1 
ATOM   7266  C  CA  . MET   B 2 634 ? 28.712  75.311  -45.839 1.00 131.95 ? 938  MET   B CA  1 
ATOM   7267  C  C   . MET   B 2 634 ? 27.982  74.166  -46.539 1.00 136.30 ? 938  MET   B C   1 
ATOM   7268  O  O   . MET   B 2 634 ? 27.045  74.411  -47.312 1.00 138.09 ? 938  MET   B O   1 
ATOM   7269  C  CB  . MET   B 2 634 ? 29.838  75.879  -46.708 1.00 122.94 ? 938  MET   B CB  1 
ATOM   7270  N  N   . GLU   B 2 635 ? 28.370  72.913  -46.255 1.00 136.12 ? 939  GLU   B N   1 
ATOM   7271  C  CA  . GLU   B 2 635 ? 27.721  71.766  -46.883 1.00 130.40 ? 939  GLU   B CA  1 
ATOM   7272  C  C   . GLU   B 2 635 ? 26.323  71.544  -46.321 1.00 129.78 ? 939  GLU   B C   1 
ATOM   7273  O  O   . GLU   B 2 635 ? 25.404  71.179  -47.061 1.00 129.55 ? 939  GLU   B O   1 
ATOM   7274  C  CB  . GLU   B 2 635 ? 28.579  70.512  -46.706 1.00 126.67 ? 939  GLU   B CB  1 
ATOM   7275  N  N   . GLY   B 2 636 ? 26.137  71.773  -45.020 1.00 131.74 ? 940  GLY   B N   1 
ATOM   7276  C  CA  . GLY   B 2 636 ? 24.857  71.532  -44.389 1.00 127.82 ? 940  GLY   B CA  1 
ATOM   7277  C  C   . GLY   B 2 636 ? 24.546  70.060  -44.210 1.00 125.84 ? 940  GLY   B C   1 
ATOM   7278  O  O   . GLY   B 2 636 ? 23.442  69.621  -44.546 1.00 122.67 ? 940  GLY   B O   1 
ATOM   7279  N  N   . ASN   B 2 637 ? 25.514  69.283  -43.719 1.00 124.68 ? 941  ASN   B N   1 
ATOM   7280  C  CA  . ASN   B 2 637 ? 25.365  67.860  -43.406 1.00 118.88 ? 941  ASN   B CA  1 
ATOM   7281  C  C   . ASN   B 2 637 ? 26.568  67.434  -42.559 1.00 119.26 ? 941  ASN   B C   1 
ATOM   7282  O  O   . ASN   B 2 637 ? 27.586  68.131  -42.503 1.00 121.23 ? 941  ASN   B O   1 
ATOM   7283  C  CB  . ASN   B 2 637 ? 25.232  67.003  -44.684 1.00 119.30 ? 941  ASN   B CB  1 
ATOM   7284  C  CG  . ASN   B 2 637 ? 24.381  65.719  -44.474 1.00 124.23 ? 941  ASN   B CG  1 
ATOM   7285  O  OD1 . ASN   B 2 637 ? 23.143  65.751  -44.510 1.00 126.62 ? 941  ASN   B OD1 1 
ATOM   7286  N  ND2 . ASN   B 2 637 ? 25.055  64.587  -44.283 1.00 121.70 ? 941  ASN   B ND2 1 
ATOM   7287  N  N   . PHE   B 2 638 ? 26.421  66.294  -41.870 1.00 118.48 ? 942  PHE   B N   1 
ATOM   7288  C  CA  . PHE   B 2 638 ? 27.476  65.743  -41.022 1.00 114.51 ? 942  PHE   B CA  1 
ATOM   7289  C  C   . PHE   B 2 638 ? 28.355  64.772  -41.798 1.00 109.61 ? 942  PHE   B C   1 
ATOM   7290  O  O   . PHE   B 2 638 ? 27.899  64.079  -42.712 1.00 111.38 ? 942  PHE   B O   1 
ATOM   7291  C  CB  . PHE   B 2 638 ? 26.938  64.980  -39.803 1.00 110.80 ? 942  PHE   B CB  1 
ATOM   7292  C  CG  . PHE   B 2 638 ? 25.727  65.579  -39.158 1.00 109.07 ? 942  PHE   B CG  1 
ATOM   7293  C  CD1 . PHE   B 2 638 ? 25.855  66.454  -38.098 1.00 110.85 ? 942  PHE   B CD1 1 
ATOM   7294  C  CD2 . PHE   B 2 638 ? 24.463  65.214  -39.576 1.00 110.19 ? 942  PHE   B CD2 1 
ATOM   7295  C  CE1 . PHE   B 2 638 ? 24.743  66.989  -37.486 1.00 110.40 ? 942  PHE   B CE1 1 
ATOM   7296  C  CE2 . PHE   B 2 638 ? 23.355  65.736  -38.979 1.00 112.05 ? 942  PHE   B CE2 1 
ATOM   7297  C  CZ  . PHE   B 2 638 ? 23.493  66.630  -37.925 1.00 112.32 ? 942  PHE   B CZ  1 
ATOM   7298  N  N   . GLU   B 2 639 ? 29.612  64.685  -41.385 1.00 108.00 ? 943  GLU   B N   1 
ATOM   7299  C  CA  . GLU   B 2 639 ? 30.549  63.709  -41.910 1.00 106.58 ? 943  GLU   B CA  1 
ATOM   7300  C  C   . GLU   B 2 639 ? 31.229  63.010  -40.747 1.00 105.55 ? 943  GLU   B C   1 
ATOM   7301  O  O   . GLU   B 2 639 ? 31.541  63.638  -39.732 1.00 108.47 ? 943  GLU   B O   1 
ATOM   7302  C  CB  . GLU   B 2 639 ? 31.593  64.366  -42.816 1.00 107.48 ? 943  GLU   B CB  1 
ATOM   7303  N  N   . GLU   B 2 640 ? 31.452  61.708  -40.891 1.00 101.87 ? 944  GLU   B N   1 
ATOM   7304  C  CA  . GLU   B 2 640 ? 32.039  60.923  -39.816 1.00 103.50 ? 944  GLU   B CA  1 
ATOM   7305  C  C   . GLU   B 2 640 ? 33.536  61.167  -39.718 1.00 103.53 ? 944  GLU   B C   1 
ATOM   7306  O  O   . GLU   B 2 640 ? 34.239  61.120  -40.730 1.00 109.49 ? 944  GLU   B O   1 
ATOM   7307  C  CB  . GLU   B 2 640 ? 31.789  59.442  -40.047 1.00 107.82 ? 944  GLU   B CB  1 
ATOM   7308  C  CG  . GLU   B 2 640 ? 32.710  58.567  -39.215 1.00 113.68 ? 944  GLU   B CG  1 
ATOM   7309  C  CD  . GLU   B 2 640 ? 32.249  57.133  -39.152 1.00 116.28 ? 944  GLU   B CD  1 
ATOM   7310  O  OE1 . GLU   B 2 640 ? 31.069  56.883  -39.482 1.00 116.55 ? 944  GLU   B OE1 1 
ATOM   7311  O  OE2 . GLU   B 2 640 ? 33.062  56.256  -38.772 1.00 121.32 ? 944  GLU   B OE2 1 
ATOM   7312  N  N   . ILE   B 2 641 ? 34.035  61.389  -38.510 1.00 106.38 ? 945  ILE   B N   1 
ATOM   7313  C  CA  . ILE   B 2 641 ? 35.465  61.587  -38.324 1.00 110.14 ? 945  ILE   B CA  1 
ATOM   7314  C  C   . ILE   B 2 641 ? 36.167  60.279  -37.996 1.00 119.75 ? 945  ILE   B C   1 
ATOM   7315  O  O   . ILE   B 2 641 ? 37.190  59.941  -38.598 1.00 124.01 ? 945  ILE   B O   1 
ATOM   7316  C  CB  . ILE   B 2 641 ? 35.725  62.645  -37.234 1.00 114.73 ? 945  ILE   B CB  1 
ATOM   7317  C  CG1 . ILE   B 2 641 ? 34.944  63.933  -37.509 1.00 115.42 ? 945  ILE   B CG1 1 
ATOM   7318  C  CG2 . ILE   B 2 641 ? 37.207  62.959  -37.162 1.00 121.15 ? 945  ILE   B CG2 1 
ATOM   7319  C  CD1 . ILE   B 2 641 ? 35.296  65.064  -36.548 1.00 119.32 ? 945  ILE   B CD1 1 
ATOM   7320  N  N   . ALA   B 2 642 ? 35.632  59.527  -37.031 1.00 121.61 ? 946  ALA   B N   1 
ATOM   7321  C  CA  . ALA   B 2 642 ? 36.192  58.237  -36.644 1.00 123.76 ? 946  ALA   B CA  1 
ATOM   7322  C  C   . ALA   B 2 642 ? 35.172  57.480  -35.802 1.00 117.38 ? 946  ALA   B C   1 
ATOM   7323  O  O   . ALA   B 2 642 ? 34.216  58.053  -35.266 1.00 109.00 ? 946  ALA   B O   1 
ATOM   7324  C  CB  . ALA   B 2 642 ? 37.516  58.396  -35.888 1.00 125.02 ? 946  ALA   B CB  1 
ATOM   7325  N  N   . ARG   B 2 643 ? 35.389  56.172  -35.704 1.00 119.69 ? 947  ARG   B N   1 
ATOM   7326  C  CA  . ARG   B 2 643 ? 34.617  55.290  -34.844 1.00 112.44 ? 947  ARG   B CA  1 
ATOM   7327  C  C   . ARG   B 2 643 ? 35.598  54.408  -34.091 1.00 115.04 ? 947  ARG   B C   1 
ATOM   7328  O  O   . ARG   B 2 643 ? 36.770  54.287  -34.460 1.00 120.69 ? 947  ARG   B O   1 
ATOM   7329  C  CB  . ARG   B 2 643 ? 33.612  54.432  -35.637 1.00 106.02 ? 947  ARG   B CB  1 
ATOM   7330  N  N   . ASP   B 2 644 ? 35.114  53.813  -33.009 1.00 110.87 ? 948  ASP   B N   1 
ATOM   7331  C  CA  . ASP   B 2 644 ? 35.850  52.793  -32.278 1.00 110.19 ? 948  ASP   B CA  1 
ATOM   7332  C  C   . ASP   B 2 644 ? 34.782  51.934  -31.639 1.00 106.46 ? 948  ASP   B C   1 
ATOM   7333  O  O   . ASP   B 2 644 ? 33.854  52.475  -31.033 1.00 107.59 ? 948  ASP   B O   1 
ATOM   7334  C  CB  . ASP   B 2 644 ? 36.794  53.397  -31.230 1.00 117.46 ? 948  ASP   B CB  1 
ATOM   7335  C  CG  . ASP   B 2 644 ? 37.539  52.335  -30.386 1.00 122.95 ? 948  ASP   B CG  1 
ATOM   7336  O  OD1 . ASP   B 2 644 ? 38.411  51.619  -30.935 1.00 124.72 ? 948  ASP   B OD1 1 
ATOM   7337  O  OD2 . ASP   B 2 644 ? 37.282  52.236  -29.155 1.00 123.84 ? 948  ASP   B OD2 1 
ATOM   7338  N  N   . PHE   B 2 645 ? 34.876  50.624  -31.841 1.00 101.80 ? 949  PHE   B N   1 
ATOM   7339  C  CA  . PHE   B 2 645 ? 33.908  49.655  -31.320 1.00 103.62 ? 949  PHE   B CA  1 
ATOM   7340  C  C   . PHE   B 2 645 ? 34.653  48.620  -30.472 1.00 105.28 ? 949  PHE   B C   1 
ATOM   7341  O  O   . PHE   B 2 645 ? 35.195  47.642  -31.007 1.00 108.25 ? 949  PHE   B O   1 
ATOM   7342  C  CB  . PHE   B 2 645 ? 33.136  48.966  -32.456 1.00 104.97 ? 949  PHE   B CB  1 
ATOM   7343  C  CG  . PHE   B 2 645 ? 32.124  49.845  -33.175 1.00 102.44 ? 949  PHE   B CG  1 
ATOM   7344  C  CD1 . PHE   B 2 645 ? 31.797  51.105  -32.700 1.00 107.72 ? 949  PHE   B CD1 1 
ATOM   7345  C  CD2 . PHE   B 2 645 ? 31.489  49.382  -34.325 1.00 94.83  ? 949  PHE   B CD2 1 
ATOM   7346  C  CE1 . PHE   B 2 645 ? 30.860  51.901  -33.368 1.00 106.50 ? 949  PHE   B CE1 1 
ATOM   7347  C  CE2 . PHE   B 2 645 ? 30.556  50.153  -34.993 1.00 99.70  ? 949  PHE   B CE2 1 
ATOM   7348  C  CZ  . PHE   B 2 645 ? 30.237  51.418  -34.520 1.00 107.86 ? 949  PHE   B CZ  1 
ATOM   7349  N  N   . ASN   B 2 646 ? 34.663  48.799  -29.152 1.00 102.86 ? 950  ASN   B N   1 
ATOM   7350  C  CA  . ASN   B 2 646 ? 35.236  47.812  -28.241 1.00 103.22 ? 950  ASN   B CA  1 
ATOM   7351  C  C   . ASN   B 2 646 ? 34.185  47.343  -27.249 1.00 102.24 ? 950  ASN   B C   1 
ATOM   7352  O  O   . ASN   B 2 646 ? 34.066  47.893  -26.146 1.00 104.45 ? 950  ASN   B O   1 
ATOM   7353  C  CB  . ASN   B 2 646 ? 36.454  48.359  -27.517 1.00 106.58 ? 950  ASN   B CB  1 
ATOM   7354  C  CG  . ASN   B 2 646 ? 37.011  47.356  -26.533 1.00 112.14 ? 950  ASN   B CG  1 
ATOM   7355  O  OD1 . ASN   B 2 646 ? 37.126  47.628  -25.334 1.00 120.40 ? 950  ASN   B OD1 1 
ATOM   7356  N  ND2 . ASN   B 2 646 ? 37.294  46.152  -27.026 1.00 107.98 ? 950  ASN   B ND2 1 
ATOM   7357  N  N   . PRO   B 2 647 ? 33.432  46.300  -27.575 1.00 97.26  ? 951  PRO   B N   1 
ATOM   7358  C  CA  . PRO   B 2 647 ? 32.180  46.037  -26.854 1.00 94.75  ? 951  PRO   B CA  1 
ATOM   7359  C  C   . PRO   B 2 647 ? 32.387  45.800  -25.363 1.00 95.16  ? 951  PRO   B C   1 
ATOM   7360  O  O   . PRO   B 2 647 ? 33.239  45.005  -24.960 1.00 98.27  ? 951  PRO   B O   1 
ATOM   7361  C  CB  . PRO   B 2 647 ? 31.643  44.785  -27.549 1.00 95.18  ? 951  PRO   B CB  1 
ATOM   7362  C  CG  . PRO   B 2 647 ? 32.318  44.750  -28.846 1.00 96.49  ? 951  PRO   B CG  1 
ATOM   7363  C  CD  . PRO   B 2 647 ? 33.673  45.331  -28.642 1.00 98.01  ? 951  PRO   B CD  1 
ATOM   7364  N  N   . ASN   B 2 648 ? 31.590  46.512  -24.554 1.00 93.42  ? 952  ASN   B N   1 
ATOM   7365  C  CA  . ASN   B 2 648 ? 31.533  46.457  -23.087 1.00 93.63  ? 952  ASN   B CA  1 
ATOM   7366  C  C   . ASN   B 2 648 ? 30.463  47.462  -22.665 1.00 91.47  ? 952  ASN   B C   1 
ATOM   7367  O  O   . ASN   B 2 648 ? 30.247  48.453  -23.371 1.00 95.12  ? 952  ASN   B O   1 
ATOM   7368  C  CB  . ASN   B 2 648 ? 32.895  46.784  -22.439 1.00 95.17  ? 952  ASN   B CB  1 
ATOM   7369  C  CG  . ASN   B 2 648 ? 32.888  46.647  -20.905 1.00 93.51  ? 952  ASN   B CG  1 
ATOM   7370  O  OD1 . ASN   B 2 648 ? 32.097  45.897  -20.325 1.00 91.10  ? 952  ASN   B OD1 1 
ATOM   7371  N  ND2 . ASN   B 2 648 ? 33.788  47.366  -20.252 1.00 92.10  ? 952  ASN   B ND2 1 
ATOM   7372  N  N   . TRP   B 2 649 ? 29.801  47.246  -21.531 1.00 83.63  ? 953  TRP   B N   1 
ATOM   7373  C  CA  . TRP   B 2 649 ? 28.745  48.155  -21.104 1.00 78.49  ? 953  TRP   B CA  1 
ATOM   7374  C  C   . TRP   B 2 649 ? 29.302  49.540  -20.725 1.00 84.06  ? 953  TRP   B C   1 
ATOM   7375  O  O   . TRP   B 2 649 ? 30.139  49.653  -19.826 1.00 86.73  ? 953  TRP   B O   1 
ATOM   7376  C  CB  . TRP   B 2 649 ? 28.004  47.550  -19.920 1.00 80.72  ? 953  TRP   B CB  1 
ATOM   7377  C  CG  . TRP   B 2 649 ? 27.369  46.239  -20.172 1.00 83.83  ? 953  TRP   B CG  1 
ATOM   7378  C  CD1 . TRP   B 2 649 ? 27.504  45.108  -19.409 1.00 86.63  ? 953  TRP   B CD1 1 
ATOM   7379  C  CD2 . TRP   B 2 649 ? 26.476  45.896  -21.246 1.00 88.91  ? 953  TRP   B CD2 1 
ATOM   7380  N  NE1 . TRP   B 2 649 ? 26.755  44.075  -19.951 1.00 87.91  ? 953  TRP   B NE1 1 
ATOM   7381  C  CE2 . TRP   B 2 649 ? 26.122  44.531  -21.080 1.00 90.41  ? 953  TRP   B CE2 1 
ATOM   7382  C  CE3 . TRP   B 2 649 ? 25.951  46.597  -22.335 1.00 83.11  ? 953  TRP   B CE3 1 
ATOM   7383  C  CZ2 . TRP   B 2 649 ? 25.272  43.865  -21.973 1.00 86.24  ? 953  TRP   B CZ2 1 
ATOM   7384  C  CZ3 . TRP   B 2 649 ? 25.102  45.929  -23.210 1.00 81.01  ? 953  TRP   B CZ3 1 
ATOM   7385  C  CH2 . TRP   B 2 649 ? 24.774  44.588  -23.027 1.00 80.91  ? 953  TRP   B CH2 1 
ATOM   7386  N  N   . MET   B 2 650 ? 28.779  50.593  -21.361 1.00 83.15  ? 954  MET   B N   1 
ATOM   7387  C  CA  . MET   B 2 650 ? 29.125  51.988  -21.105 1.00 78.90  ? 954  MET   B CA  1 
ATOM   7388  C  C   . MET   B 2 650 ? 27.920  52.742  -20.549 1.00 79.71  ? 954  MET   B C   1 
ATOM   7389  O  O   . MET   B 2 650 ? 26.812  52.627  -21.069 1.00 82.72  ? 954  MET   B O   1 
ATOM   7390  C  CB  . MET   B 2 650 ? 29.603  52.670  -22.392 1.00 84.09  ? 954  MET   B CB  1 
ATOM   7391  C  CG  . MET   B 2 650 ? 30.041  54.120  -22.215 1.00 86.64  ? 954  MET   B CG  1 
ATOM   7392  S  SD  . MET   B 2 650 ? 30.839  54.790  -23.688 1.00 87.66  ? 954  MET   B SD  1 
ATOM   7393  C  CE  . MET   B 2 650 ? 29.487  54.724  -24.871 1.00 93.60  ? 954  MET   B CE  1 
ATOM   7394  N  N   . SER   B 2 651 ? 28.140  53.543  -19.507 1.00 82.32  ? 955  SER   B N   1 
ATOM   7395  C  CA  . SER   B 2 651 ? 27.063  54.219  -18.791 1.00 82.32  ? 955  SER   B CA  1 
ATOM   7396  C  C   . SER   B 2 651 ? 27.073  55.738  -18.919 1.00 83.50  ? 955  SER   B C   1 
ATOM   7397  O  O   . SER   B 2 651 ? 26.023  56.364  -18.728 1.00 85.97  ? 955  SER   B O   1 
ATOM   7398  C  CB  . SER   B 2 651 ? 27.114  53.863  -17.299 1.00 82.50  ? 955  SER   B CB  1 
ATOM   7399  O  OG  . SER   B 2 651 ? 28.367  54.244  -16.749 1.00 83.65  ? 955  SER   B OG  1 
ATOM   7400  N  N   . ALA   B 2 652 ? 28.214  56.351  -19.198 1.00 81.75  ? 956  ALA   B N   1 
ATOM   7401  C  CA  . ALA   B 2 652 ? 28.249  57.796  -19.329 1.00 83.60  ? 956  ALA   B CA  1 
ATOM   7402  C  C   . ALA   B 2 652 ? 29.517  58.151  -20.077 1.00 84.49  ? 956  ALA   B C   1 
ATOM   7403  O  O   . ALA   B 2 652 ? 30.483  57.384  -20.076 1.00 83.09  ? 956  ALA   B O   1 
ATOM   7404  C  CB  . ALA   B 2 652 ? 28.194  58.496  -17.967 1.00 81.64  ? 956  ALA   B CB  1 
ATOM   7405  N  N   . VAL   B 2 653 ? 29.502  59.320  -20.718 1.00 88.27  ? 957  VAL   B N   1 
ATOM   7406  C  CA  . VAL   B 2 653 ? 30.574  59.704  -21.624 1.00 90.78  ? 957  VAL   B CA  1 
ATOM   7407  C  C   . VAL   B 2 653 ? 30.558  61.221  -21.774 1.00 94.01  ? 957  VAL   B C   1 
ATOM   7408  O  O   . VAL   B 2 653 ? 29.551  61.877  -21.502 1.00 97.22  ? 957  VAL   B O   1 
ATOM   7409  C  CB  . VAL   B 2 653 ? 30.407  58.975  -22.976 1.00 91.00  ? 957  VAL   B CB  1 
ATOM   7410  C  CG1 . VAL   B 2 653 ? 29.134  59.413  -23.632 1.00 93.83  ? 957  VAL   B CG1 1 
ATOM   7411  C  CG2 . VAL   B 2 653 ? 31.610  59.179  -23.858 1.00 94.36  ? 957  VAL   B CG2 1 
ATOM   7412  N  N   . GLU   B 2 654 ? 31.694  61.784  -22.195 1.00 93.42  ? 958  GLU   B N   1 
ATOM   7413  C  CA  . GLU   B 2 654 ? 31.925  63.223  -22.183 1.00 92.42  ? 958  GLU   B CA  1 
ATOM   7414  C  C   . GLU   B 2 654 ? 33.118  63.539  -23.071 1.00 97.57  ? 958  GLU   B C   1 
ATOM   7415  O  O   . GLU   B 2 654 ? 33.954  62.677  -23.356 1.00 99.20  ? 958  GLU   B O   1 
ATOM   7416  C  CB  . GLU   B 2 654 ? 32.182  63.733  -20.761 1.00 88.75  ? 958  GLU   B CB  1 
ATOM   7417  C  CG  . GLU   B 2 654 ? 32.152  65.232  -20.646 1.00 92.00  ? 958  GLU   B CG  1 
ATOM   7418  C  CD  . GLU   B 2 654 ? 30.826  65.813  -21.117 1.00 96.62  ? 958  GLU   B CD  1 
ATOM   7419  O  OE1 . GLU   B 2 654 ? 29.783  65.147  -20.918 1.00 96.97  ? 958  GLU   B OE1 1 
ATOM   7420  O  OE2 . GLU   B 2 654 ? 30.820  66.934  -21.679 1.00 97.73  ? 958  GLU   B OE2 1 
ATOM   7421  N  N   . ILE   B 2 655 ? 33.199  64.795  -23.497 1.00 100.51 ? 959  ILE   B N   1 
ATOM   7422  C  CA  . ILE   B 2 655 ? 34.318  65.276  -24.293 1.00 101.13 ? 959  ILE   B CA  1 
ATOM   7423  C  C   . ILE   B 2 655 ? 35.280  66.012  -23.366 1.00 101.39 ? 959  ILE   B C   1 
ATOM   7424  O  O   . ILE   B 2 655 ? 34.879  66.924  -22.631 1.00 100.30 ? 959  ILE   B O   1 
ATOM   7425  C  CB  . ILE   B 2 655 ? 33.833  66.170  -25.446 1.00 95.57  ? 959  ILE   B CB  1 
ATOM   7426  C  CG1 . ILE   B 2 655 ? 32.748  65.431  -26.242 1.00 95.29  ? 959  ILE   B CG1 1 
ATOM   7427  C  CG2 . ILE   B 2 655 ? 34.991  66.584  -26.312 1.00 100.41 ? 959  ILE   B CG2 1 
ATOM   7428  C  CD1 . ILE   B 2 655 ? 32.476  65.969  -27.629 1.00 97.13  ? 959  ILE   B CD1 1 
ATOM   7429  N  N   . LEU   B 2 656 ? 36.540  65.580  -23.351 1.00 102.11 ? 960  LEU   B N   1 
ATOM   7430  C  CA  . LEU   B 2 656 ? 37.572  66.366  -22.680 1.00 100.89 ? 960  LEU   B CA  1 
ATOM   7431  C  C   . LEU   B 2 656 ? 37.975  67.540  -23.567 1.00 106.56 ? 960  LEU   B C   1 
ATOM   7432  O  O   . LEU   B 2 656 ? 37.689  68.699  -23.248 1.00 106.41 ? 960  LEU   B O   1 
ATOM   7433  C  CB  . LEU   B 2 656 ? 38.771  65.483  -22.325 1.00 100.35 ? 960  LEU   B CB  1 
ATOM   7434  C  CG  . LEU   B 2 656 ? 38.432  64.349  -21.363 1.00 100.64 ? 960  LEU   B CG  1 
ATOM   7435  C  CD1 . LEU   B 2 656 ? 39.676  63.561  -21.024 1.00 102.31 ? 960  LEU   B CD1 1 
ATOM   7436  C  CD2 . LEU   B 2 656 ? 37.802  64.905  -20.110 1.00 96.82  ? 960  LEU   B CD2 1 
ATOM   7437  N  N   . ASP   B 2 657 ? 38.622  67.250  -24.704 1.00 107.11 ? 961  ASP   B N   1 
ATOM   7438  C  CA  . ASP   B 2 657 ? 38.926  68.265  -25.708 1.00 107.08 ? 961  ASP   B CA  1 
ATOM   7439  C  C   . ASP   B 2 657 ? 38.551  67.754  -27.097 1.00 109.20 ? 961  ASP   B C   1 
ATOM   7440  O  O   . ASP   B 2 657 ? 37.907  66.713  -27.230 1.00 109.96 ? 961  ASP   B O   1 
ATOM   7441  C  CB  . ASP   B 2 657 ? 40.408  68.660  -25.656 1.00 107.41 ? 961  ASP   B CB  1 
ATOM   7442  C  CG  . ASP   B 2 657 ? 41.324  67.494  -25.890 1.00 108.68 ? 961  ASP   B CG  1 
ATOM   7443  O  OD1 . ASP   B 2 657 ? 41.207  66.860  -26.955 1.00 113.97 ? 961  ASP   B OD1 1 
ATOM   7444  O  OD2 . ASP   B 2 657 ? 42.141  67.190  -24.998 1.00 107.64 ? 961  ASP   B OD2 1 
ATOM   7445  N  N   . ASP   B 2 658 ? 38.987  68.463  -28.142 1.00 113.84 ? 962  ASP   B N   1 
ATOM   7446  C  CA  . ASP   B 2 658 ? 38.606  68.104  -29.502 1.00 113.69 ? 962  ASP   B CA  1 
ATOM   7447  C  C   . ASP   B 2 658 ? 39.081  66.717  -29.915 1.00 116.24 ? 962  ASP   B C   1 
ATOM   7448  O  O   . ASP   B 2 658 ? 38.596  66.195  -30.928 1.00 118.93 ? 962  ASP   B O   1 
ATOM   7449  C  CB  . ASP   B 2 658 ? 39.162  69.125  -30.501 1.00 115.85 ? 962  ASP   B CB  1 
ATOM   7450  C  CG  . ASP   B 2 658 ? 38.406  70.440  -30.487 1.00 120.07 ? 962  ASP   B CG  1 
ATOM   7451  O  OD1 . ASP   B 2 658 ? 38.727  71.305  -29.634 1.00 122.94 ? 962  ASP   B OD1 1 
ATOM   7452  O  OD2 . ASP   B 2 658 ? 37.496  70.604  -31.336 1.00 120.24 ? 962  ASP   B OD2 1 
ATOM   7453  N  N   . ASP   B 2 659 ? 40.023  66.118  -29.186 1.00 113.33 ? 963  ASP   B N   1 
ATOM   7454  C  CA  . ASP   B 2 659 ? 40.625  64.846  -29.576 1.00 114.36 ? 963  ASP   B CA  1 
ATOM   7455  C  C   . ASP   B 2 659 ? 40.457  63.747  -28.541 1.00 116.26 ? 963  ASP   B C   1 
ATOM   7456  O  O   . ASP   B 2 659 ? 40.321  62.578  -28.913 1.00 118.97 ? 963  ASP   B O   1 
ATOM   7457  C  CB  . ASP   B 2 659 ? 42.132  65.018  -29.864 1.00 116.49 ? 963  ASP   B CB  1 
ATOM   7458  C  CG  . ASP   B 2 659 ? 42.428  66.112  -30.882 1.00 115.71 ? 963  ASP   B CG  1 
ATOM   7459  O  OD1 . ASP   B 2 659 ? 41.634  67.061  -30.989 1.00 116.10 ? 963  ASP   B OD1 1 
ATOM   7460  O  OD2 . ASP   B 2 659 ? 43.465  66.024  -31.574 1.00 115.38 ? 963  ASP   B OD2 1 
ATOM   7461  N  N   . ASN   B 2 660 ? 40.537  64.118  -27.265 1.00 115.43 ? 964  ASN   B N   1 
ATOM   7462  C  CA  . ASN   B 2 660 ? 40.463  63.100  -26.185 1.00 115.79 ? 964  ASN   B CA  1 
ATOM   7463  C  C   . ASN   B 2 660 ? 39.038  63.058  -25.633 1.00 116.03 ? 964  ASN   B C   1 
ATOM   7464  O  O   . ASN   B 2 660 ? 38.463  64.139  -25.398 1.00 111.39 ? 964  ASN   B O   1 
ATOM   7465  C  CB  . ASN   B 2 660 ? 41.506  63.371  -25.110 1.00 109.36 ? 964  ASN   B CB  1 
ATOM   7466  C  CG  . ASN   B 2 660 ? 42.872  63.610  -25.703 1.00 110.08 ? 964  ASN   B CG  1 
ATOM   7467  O  OD1 . ASN   B 2 660 ? 43.465  62.694  -26.278 1.00 111.94 ? 964  ASN   B OD1 1 
ATOM   7468  N  ND2 . ASN   B 2 660 ? 43.385  64.824  -25.575 1.00 111.71 ? 964  ASN   B ND2 1 
ATOM   7469  N  N   . PHE   B 2 661 ? 38.495  61.854  -25.442 1.00 122.20 ? 965  PHE   B N   1 
ATOM   7470  C  CA  . PHE   B 2 661 ? 37.106  61.698  -24.937 1.00 119.21 ? 965  PHE   B CA  1 
ATOM   7471  C  C   . PHE   B 2 661 ? 37.123  60.756  -23.748 1.00 116.77 ? 965  PHE   B C   1 
ATOM   7472  O  O   . PHE   B 2 661 ? 37.923  59.806  -23.762 1.00 120.04 ? 965  PHE   B O   1 
ATOM   7473  C  CB  . PHE   B 2 661 ? 36.255  61.159  -26.086 1.00 120.97 ? 965  PHE   B CB  1 
ATOM   7474  C  CG  . PHE   B 2 661 ? 36.539  61.826  -27.423 1.00 127.11 ? 965  PHE   B CG  1 
ATOM   7475  C  CD1 . PHE   B 2 661 ? 36.229  63.165  -27.628 1.00 125.72 ? 965  PHE   B CD1 1 
ATOM   7476  C  CD2 . PHE   B 2 661 ? 37.128  61.118  -28.462 1.00 127.67 ? 965  PHE   B CD2 1 
ATOM   7477  C  CE1 . PHE   B 2 661 ? 36.499  63.774  -28.840 1.00 125.40 ? 965  PHE   B CE1 1 
ATOM   7478  C  CE2 . PHE   B 2 661 ? 37.390  61.731  -29.674 1.00 128.26 ? 965  PHE   B CE2 1 
ATOM   7479  C  CZ  . PHE   B 2 661 ? 37.080  63.057  -29.857 1.00 129.20 ? 965  PHE   B CZ  1 
ATOM   7480  N  N   . LEU   B 2 662 ? 36.256  60.988  -22.760 1.00 104.53 ? 966  LEU   B N   1 
ATOM   7481  C  CA  . LEU   B 2 662 ? 36.287  60.172  -21.520 1.00 98.74  ? 966  LEU   B CA  1 
ATOM   7482  C  C   . LEU   B 2 662 ? 34.922  59.521  -21.290 1.00 92.15  ? 966  LEU   B C   1 
ATOM   7483  O  O   . LEU   B 2 662 ? 33.908  60.144  -21.645 1.00 89.68  ? 966  LEU   B O   1 
ATOM   7484  C  CB  . LEU   B 2 662 ? 36.669  61.087  -20.360 1.00 95.95  ? 966  LEU   B CB  1 
ATOM   7485  C  CG  . LEU   B 2 662 ? 36.309  60.618  -18.948 1.00 90.21  ? 966  LEU   B CG  1 
ATOM   7486  C  CD1 . LEU   B 2 662 ? 37.283  59.562  -18.464 1.00 91.08  ? 966  LEU   B CD1 1 
ATOM   7487  C  CD2 . LEU   B 2 662 ? 36.317  61.810  -18.012 1.00 90.85  ? 966  LEU   B CD2 1 
ATOM   7488  N  N   . GLY   B 2 663 ? 34.910  58.321  -20.711 1.00 91.20  ? 967  GLY   B N   1 
ATOM   7489  C  CA  . GLY   B 2 663 ? 33.640  57.651  -20.392 1.00 88.76  ? 967  GLY   B CA  1 
ATOM   7490  C  C   . GLY   B 2 663 ? 33.825  56.622  -19.299 1.00 83.16  ? 967  GLY   B C   1 
ATOM   7491  O  O   . GLY   B 2 663 ? 34.985  56.329  -18.955 1.00 82.12  ? 967  GLY   B O   1 
ATOM   7492  N  N   . ALA   B 2 664 ? 32.730  56.092  -18.747 1.00 77.56  ? 968  ALA   B N   1 
ATOM   7493  C  CA  . ALA   B 2 664 ? 32.830  55.027  -17.719 1.00 81.09  ? 968  ALA   B CA  1 
ATOM   7494  C  C   . ALA   B 2 664 ? 32.280  53.722  -18.293 1.00 84.81  ? 968  ALA   B C   1 
ATOM   7495  O  O   . ALA   B 2 664 ? 31.310  53.791  -19.080 1.00 84.33  ? 968  ALA   B O   1 
ATOM   7496  C  CB  . ALA   B 2 664 ? 32.083  55.438  -16.474 1.00 84.68  ? 968  ALA   B CB  1 
ATOM   7497  N  N   . GLU   B 2 665 ? 32.857  52.575  -17.916 1.00 87.32  ? 969  GLU   B N   1 
ATOM   7498  C  CA  . GLU   B 2 665 ? 32.396  51.313  -18.558 1.00 85.83  ? 969  GLU   B CA  1 
ATOM   7499  C  C   . GLU   B 2 665 ? 32.399  50.112  -17.591 1.00 85.83  ? 969  GLU   B C   1 
ATOM   7500  O  O   . GLU   B 2 665 ? 33.358  49.989  -16.797 1.00 85.53  ? 969  GLU   B O   1 
ATOM   7501  C  CB  . GLU   B 2 665 ? 33.204  51.019  -19.826 1.00 85.91  ? 969  GLU   B CB  1 
ATOM   7502  C  CG  . GLU   B 2 665 ? 34.710  50.918  -19.610 1.00 90.67  ? 969  GLU   B CG  1 
ATOM   7503  C  CD  . GLU   B 2 665 ? 35.417  50.401  -20.850 1.00 98.40  ? 969  GLU   B CD  1 
ATOM   7504  O  OE1 . GLU   B 2 665 ? 34.822  49.552  -21.546 1.00 98.38  ? 969  GLU   B OE1 1 
ATOM   7505  O  OE2 . GLU   B 2 665 ? 36.551  50.842  -21.127 1.00 103.39 ? 969  GLU   B OE2 1 
ATOM   7506  N  N   . ASN   B 2 666 ? 31.350  49.283  -17.646 1.00 90.48  ? 970  ASN   B N   1 
ATOM   7507  C  CA  . ASN   B 2 666 ? 31.256  48.029  -16.840 1.00 92.92  ? 970  ASN   B CA  1 
ATOM   7508  C  C   . ASN   B 2 666 ? 31.567  48.077  -15.344 1.00 94.85  ? 970  ASN   B C   1 
ATOM   7509  O  O   . ASN   B 2 666 ? 30.842  48.777  -14.603 1.00 93.00  ? 970  ASN   B O   1 
ATOM   7510  C  CB  . ASN   B 2 666 ? 32.075  46.898  -17.448 1.00 93.36  ? 970  ASN   B CB  1 
ATOM   7511  C  CG  . ASN   B 2 666 ? 31.373  45.566  -17.334 1.00 98.01  ? 970  ASN   B CG  1 
ATOM   7512  O  OD1 . ASN   B 2 666 ? 30.215  45.437  -17.745 1.00 100.43 ? 970  ASN   B OD1 1 
ATOM   7513  N  ND2 . ASN   B 2 666 ? 32.050  44.571  -16.781 1.00 97.61  ? 970  ASN   B ND2 1 
ATOM   7514  N  N   . ALA   B 2 667 ? 32.594  47.330  -14.922 1.00 92.95  ? 971  ALA   B N   1 
ATOM   7515  C  CA  . ALA   B 2 667 ? 32.914  47.199  -13.480 1.00 88.45  ? 971  ALA   B CA  1 
ATOM   7516  C  C   . ALA   B 2 667 ? 33.684  48.436  -13.024 1.00 89.10  ? 971  ALA   B C   1 
ATOM   7517  O  O   . ALA   B 2 667 ? 34.914  48.324  -12.844 1.00 89.85  ? 971  ALA   B O   1 
ATOM   7518  C  CB  . ALA   B 2 667 ? 33.716  45.944  -13.207 1.00 98.01  ? 971  ALA   B CB  1 
ATOM   7519  N  N   . PHE   B 2 668 ? 32.989  49.561  -12.831 1.00 90.96  ? 972  PHE   B N   1 
ATOM   7520  C  CA  . PHE   B 2 668 ? 33.637  50.768  -12.252 1.00 86.83  ? 972  PHE   B CA  1 
ATOM   7521  C  C   . PHE   B 2 668 ? 34.976  51.003  -12.934 1.00 84.15  ? 972  PHE   B C   1 
ATOM   7522  O  O   . PHE   B 2 668 ? 36.025  50.935  -12.253 1.00 83.68  ? 972  PHE   B O   1 
ATOM   7523  C  CB  . PHE   B 2 668 ? 33.726  50.470  -10.753 1.00 82.73  ? 972  PHE   B CB  1 
ATOM   7524  C  CG  . PHE   B 2 668 ? 32.547  49.658  -10.230 1.00 83.16  ? 972  PHE   B CG  1 
ATOM   7525  C  CD1 . PHE   B 2 668 ? 31.279  50.222  -10.134 1.00 83.15  ? 972  PHE   B CD1 1 
ATOM   7526  C  CD2 . PHE   B 2 668 ? 32.700  48.325  -9.867  1.00 88.30  ? 972  PHE   B CD2 1 
ATOM   7527  C  CE1 . PHE   B 2 668 ? 30.204  49.479  -9.677  1.00 85.20  ? 972  PHE   B CE1 1 
ATOM   7528  C  CE2 . PHE   B 2 668 ? 31.618  47.584  -9.421  1.00 87.66  ? 972  PHE   B CE2 1 
ATOM   7529  C  CZ  . PHE   B 2 668 ? 30.375  48.164  -9.320  1.00 86.22  ? 972  PHE   B CZ  1 
ATOM   7530  N  N   . ASN   B 2 669 ? 34.948  51.310  -14.234 1.00 84.90  ? 973  ASN   B N   1 
ATOM   7531  C  CA  . ASN   B 2 669 ? 36.217  51.466  -14.991 1.00 85.50  ? 973  ASN   B CA  1 
ATOM   7532  C  C   . ASN   B 2 669 ? 36.175  52.697  -15.895 1.00 83.81  ? 973  ASN   B C   1 
ATOM   7533  O  O   . ASN   B 2 669 ? 35.334  52.717  -16.817 1.00 81.24  ? 973  ASN   B O   1 
ATOM   7534  C  CB  . ASN   B 2 669 ? 36.487  50.261  -15.879 1.00 87.98  ? 973  ASN   B CB  1 
ATOM   7535  C  CG  . ASN   B 2 669 ? 37.015  49.069  -15.121 1.00 88.06  ? 973  ASN   B CG  1 
ATOM   7536  O  OD1 . ASN   B 2 669 ? 37.915  49.203  -14.285 1.00 89.36  ? 973  ASN   B OD1 1 
ATOM   7537  N  ND2 . ASN   B 2 669 ? 36.468  47.898  -15.406 1.00 91.20  ? 973  ASN   B ND2 1 
ATOM   7538  N  N   . LEU   B 2 670 ? 37.048  53.680  -15.656 1.00 84.94  ? 974  LEU   B N   1 
ATOM   7539  C  CA  . LEU   B 2 670 ? 37.129  54.809  -16.563 1.00 83.77  ? 974  LEU   B CA  1 
ATOM   7540  C  C   . LEU   B 2 670 ? 38.035  54.461  -17.742 1.00 87.74  ? 974  LEU   B C   1 
ATOM   7541  O  O   . LEU   B 2 670 ? 38.880  53.564  -17.667 1.00 88.37  ? 974  LEU   B O   1 
ATOM   7542  C  CB  . LEU   B 2 670 ? 37.669  56.045  -15.846 1.00 82.76  ? 974  LEU   B CB  1 
ATOM   7543  C  CG  . LEU   B 2 670 ? 36.746  56.811  -14.917 1.00 78.73  ? 974  LEU   B CG  1 
ATOM   7544  C  CD1 . LEU   B 2 670 ? 37.557  57.915  -14.323 1.00 79.94  ? 974  LEU   B CD1 1 
ATOM   7545  C  CD2 . LEU   B 2 670 ? 35.580  57.383  -15.676 1.00 79.61  ? 974  LEU   B CD2 1 
ATOM   7546  N  N   . PHE   B 2 671 ? 37.859  55.195  -18.838 1.00 90.41  ? 975  PHE   B N   1 
ATOM   7547  C  CA  . PHE   B 2 671 ? 38.706  55.027  -20.014 1.00 91.95  ? 975  PHE   B CA  1 
ATOM   7548  C  C   . PHE   B 2 671 ? 38.699  56.314  -20.836 1.00 94.44  ? 975  PHE   B C   1 
ATOM   7549  O  O   . PHE   B 2 671 ? 37.699  57.038  -20.893 1.00 92.71  ? 975  PHE   B O   1 
ATOM   7550  C  CB  . PHE   B 2 671 ? 38.249  53.843  -20.881 1.00 92.54  ? 975  PHE   B CB  1 
ATOM   7551  C  CG  . PHE   B 2 671 ? 37.031  54.148  -21.729 1.00 94.04  ? 975  PHE   B CG  1 
ATOM   7552  C  CD1 . PHE   B 2 671 ? 35.755  53.953  -21.229 1.00 93.37  ? 975  PHE   B CD1 1 
ATOM   7553  C  CD2 . PHE   B 2 671 ? 37.168  54.645  -23.013 1.00 94.66  ? 975  PHE   B CD2 1 
ATOM   7554  C  CE1 . PHE   B 2 671 ? 34.647  54.245  -21.992 1.00 90.78  ? 975  PHE   B CE1 1 
ATOM   7555  C  CE2 . PHE   B 2 671 ? 36.072  54.939  -23.780 1.00 94.24  ? 975  PHE   B CE2 1 
ATOM   7556  C  CZ  . PHE   B 2 671 ? 34.807  54.752  -23.269 1.00 92.00  ? 975  PHE   B CZ  1 
ATOM   7557  N  N   . VAL   B 2 672 ? 39.822  56.577  -21.492 1.00 98.40  ? 976  VAL   B N   1 
ATOM   7558  C  CA  . VAL   B 2 672 ? 39.972  57.718  -22.387 1.00 102.36 ? 976  VAL   B CA  1 
ATOM   7559  C  C   . VAL   B 2 672 ? 40.480  57.206  -23.732 1.00 103.50 ? 976  VAL   B C   1 
ATOM   7560  O  O   . VAL   B 2 672 ? 41.471  56.470  -23.788 1.00 103.45 ? 976  VAL   B O   1 
ATOM   7561  C  CB  . VAL   B 2 672 ? 40.927  58.777  -21.794 1.00 103.56 ? 976  VAL   B CB  1 
ATOM   7562  C  CG1 . VAL   B 2 672 ? 41.087  59.974  -22.733 1.00 105.87 ? 976  VAL   B CG1 1 
ATOM   7563  C  CG2 . VAL   B 2 672 ? 40.428  59.232  -20.432 1.00 100.78 ? 976  VAL   B CG2 1 
ATOM   7564  N  N   . CYS   B 2 673 ? 39.793  57.577  -24.806 1.00 107.48 ? 977  CYS   B N   1 
ATOM   7565  C  CA  . CYS   B 2 673 ? 40.246  57.308  -26.161 1.00 110.33 ? 977  CYS   B CA  1 
ATOM   7566  C  C   . CYS   B 2 673 ? 40.552  58.622  -26.878 1.00 113.87 ? 977  CYS   B C   1 
ATOM   7567  O  O   . CYS   B 2 673 ? 40.151  59.715  -26.452 1.00 112.36 ? 977  CYS   B O   1 
ATOM   7568  C  CB  . CYS   B 2 673 ? 39.196  56.521  -26.936 1.00 109.76 ? 977  CYS   B CB  1 
ATOM   7569  S  SG  . CYS   B 2 673 ? 37.856  57.627  -27.325 1.00 124.90 ? 977  CYS   B SG  1 
ATOM   7570  N  N   . GLN   B 2 674 ? 41.260  58.499  -27.999 1.00 116.38 ? 978  GLN   B N   1 
ATOM   7571  C  CA  . GLN   B 2 674 ? 41.892  59.646  -28.632 1.00 116.89 ? 978  GLN   B CA  1 
ATOM   7572  C  C   . GLN   B 2 674 ? 41.952  59.428  -30.137 1.00 118.79 ? 978  GLN   B C   1 
ATOM   7573  O  O   . GLN   B 2 674 ? 42.007  58.291  -30.609 1.00 122.15 ? 978  GLN   B O   1 
ATOM   7574  C  CB  . GLN   B 2 674 ? 43.289  59.849  -28.039 1.00 113.33 ? 978  GLN   B CB  1 
ATOM   7575  C  CG  . GLN   B 2 674 ? 44.213  60.708  -28.838 1.00 115.56 ? 978  GLN   B CG  1 
ATOM   7576  C  CD  . GLN   B 2 674 ? 45.586  60.762  -28.230 1.00 117.15 ? 978  GLN   B CD  1 
ATOM   7577  O  OE1 . GLN   B 2 674 ? 45.738  60.702  -27.011 1.00 113.26 ? 978  GLN   B OE1 1 
ATOM   7578  N  NE2 . GLN   B 2 674 ? 46.603  60.871  -29.077 1.00 124.82 ? 978  GLN   B NE2 1 
ATOM   7579  N  N   . LYS   B 2 675 ? 41.916  60.525  -30.887 1.00 119.25 ? 979  LYS   B N   1 
ATOM   7580  C  CA  . LYS   B 2 675 ? 42.120  60.484  -32.327 1.00 124.77 ? 979  LYS   B CA  1 
ATOM   7581  C  C   . LYS   B 2 675 ? 43.544  60.927  -32.670 1.00 130.28 ? 979  LYS   B C   1 
ATOM   7582  O  O   . LYS   B 2 675 ? 44.228  61.566  -31.866 1.00 131.39 ? 979  LYS   B O   1 
ATOM   7583  C  CB  . LYS   B 2 675 ? 41.076  61.347  -33.058 1.00 125.53 ? 979  LYS   B CB  1 
ATOM   7584  C  CG  . LYS   B 2 675 ? 40.821  62.744  -32.500 1.00 121.21 ? 979  LYS   B CG  1 
ATOM   7585  C  CD  . LYS   B 2 675 ? 39.913  63.551  -33.439 1.00 117.59 ? 979  LYS   B CD  1 
ATOM   7586  C  CE  . LYS   B 2 675 ? 40.580  63.764  -34.795 1.00 121.32 ? 979  LYS   B CE  1 
ATOM   7587  N  NZ  . LYS   B 2 675 ? 39.976  64.891  -35.560 1.00 127.64 ? 979  LYS   B NZ  1 
ATOM   7588  N  N   . ASP   B 2 676 ? 43.991  60.565  -33.878 1.00 137.47 ? 980  ASP   B N   1 
ATOM   7589  C  CA  . ASP   B 2 676 ? 45.389  60.752  -34.309 1.00 138.27 ? 980  ASP   B CA  1 
ATOM   7590  C  C   . ASP   B 2 676 ? 45.606  62.053  -35.081 1.00 129.78 ? 980  ASP   B C   1 
ATOM   7591  O  O   . ASP   B 2 676 ? 45.203  62.171  -36.241 1.00 125.09 ? 980  ASP   B O   1 
ATOM   7592  C  CB  . ASP   B 2 676 ? 45.836  59.565  -35.173 1.00 145.28 ? 980  ASP   B CB  1 
ATOM   7593  C  CG  . ASP   B 2 676 ? 45.740  58.228  -34.439 1.00 146.31 ? 980  ASP   B CG  1 
ATOM   7594  O  OD1 . ASP   B 2 676 ? 46.439  58.065  -33.415 1.00 143.43 ? 980  ASP   B OD1 1 
ATOM   7595  O  OD2 . ASP   B 2 676 ? 44.962  57.346  -34.879 1.00 151.34 ? 980  ASP   B OD2 1 
ATOM   7596  N  N   . THR   B 2 681 ? 47.840  57.982  -42.054 1.00 180.45 ? 985  THR   B N   1 
ATOM   7597  C  CA  . THR   B 2 681 ? 47.224  57.821  -43.386 1.00 182.76 ? 985  THR   B CA  1 
ATOM   7598  C  C   . THR   B 2 681 ? 45.786  58.261  -43.251 1.00 190.09 ? 985  THR   B C   1 
ATOM   7599  O  O   . THR   B 2 681 ? 45.553  59.487  -43.256 1.00 189.82 ? 985  THR   B O   1 
ATOM   7600  C  CB  . THR   B 2 681 ? 47.348  56.368  -43.841 1.00 181.58 ? 985  THR   B CB  1 
ATOM   7601  O  OG1 . THR   B 2 681 ? 46.634  55.580  -42.896 1.00 182.42 ? 985  THR   B OG1 1 
ATOM   7602  C  CG2 . THR   B 2 681 ? 48.791  55.899  -43.889 1.00 174.98 ? 985  THR   B CG2 1 
ATOM   7603  N  N   . ASP   B 2 682 ? 44.858  57.307  -43.158 1.00 193.73 ? 986  ASP   B N   1 
ATOM   7604  C  CA  . ASP   B 2 682 ? 43.407  57.618  -43.046 1.00 192.88 ? 986  ASP   B CA  1 
ATOM   7605  C  C   . ASP   B 2 682 ? 42.606  56.390  -42.620 1.00 191.21 ? 986  ASP   B C   1 
ATOM   7606  O  O   . ASP   B 2 682 ? 41.551  56.565  -41.979 1.00 191.43 ? 986  ASP   B O   1 
ATOM   7607  C  CB  . ASP   B 2 682 ? 42.852  58.029  -44.399 1.00 190.92 ? 986  ASP   B CB  1 
ATOM   7608  C  CG  . ASP   B 2 682 ? 42.422  59.485  -44.496 1.00 194.63 ? 986  ASP   B CG  1 
ATOM   7609  O  OD1 . ASP   B 2 682 ? 42.499  60.046  -45.608 1.00 196.61 ? 986  ASP   B OD1 1 
ATOM   7610  O  OD2 . ASP   B 2 682 ? 42.021  60.046  -43.455 1.00 192.75 ? 986  ASP   B OD2 1 
ATOM   7611  N  N   . GLU   B 2 683 ? 43.080  55.197  -42.982 1.00 183.29 ? 987  GLU   B N   1 
ATOM   7612  C  CA  . GLU   B 2 683 ? 42.393  53.978  -42.486 1.00 177.67 ? 987  GLU   B CA  1 
ATOM   7613  C  C   . GLU   B 2 683 ? 42.670  54.067  -40.984 1.00 181.73 ? 987  GLU   B C   1 
ATOM   7614  O  O   . GLU   B 2 683 ? 41.865  53.533  -40.194 1.00 176.17 ? 987  GLU   B O   1 
ATOM   7615  C  CB  . GLU   B 2 683 ? 42.962  52.731  -43.165 1.00 169.10 ? 987  GLU   B CB  1 
ATOM   7616  C  CG  . GLU   B 2 683 ? 44.464  52.548  -42.978 1.00 169.25 ? 987  GLU   B CG  1 
ATOM   7617  C  CD  . GLU   B 2 683 ? 45.021  51.374  -43.759 1.00 157.74 ? 987  GLU   B CD  1 
ATOM   7618  O  OE1 . GLU   B 2 683 ? 44.222  50.505  -44.164 1.00 157.07 ? 987  GLU   B OE1 1 
ATOM   7619  O  OE2 . GLU   B 2 683 ? 46.251  51.332  -43.967 1.00 153.48 ? 987  GLU   B OE2 1 
ATOM   7620  N  N   . GLU   B 2 684 ? 43.760  54.744  -40.613 1.00 200.62 ? 988  GLU   B N   1 
ATOM   7621  C  CA  . GLU   B 2 684 ? 44.040  54.953  -39.201 1.00 200.62 ? 988  GLU   B CA  1 
ATOM   7622  C  C   . GLU   B 2 684 ? 43.351  56.145  -38.569 1.00 200.88 ? 988  GLU   B C   1 
ATOM   7623  O  O   . GLU   B 2 684 ? 43.037  56.122  -37.371 1.00 198.70 ? 988  GLU   B O   1 
ATOM   7624  C  CB  . GLU   B 2 684 ? 45.563  55.033  -38.996 1.00 200.82 ? 988  GLU   B CB  1 
ATOM   7625  C  CG  . GLU   B 2 684 ? 46.250  56.126  -39.805 1.00 203.61 ? 988  GLU   B CG  1 
ATOM   7626  C  CD  . GLU   B 2 684 ? 46.523  57.395  -39.006 1.00 204.30 ? 988  GLU   B CD  1 
ATOM   7627  O  OE1 . GLU   B 2 684 ? 46.190  57.434  -37.801 1.00 202.68 ? 988  GLU   B OE1 1 
ATOM   7628  O  OE2 . GLU   B 2 684 ? 47.074  58.360  -39.586 1.00 204.99 ? 988  GLU   B OE2 1 
ATOM   7629  N  N   . ARG   B 2 685 ? 43.090  57.191  -39.358 1.00 185.45 ? 989  ARG   B N   1 
ATOM   7630  C  CA  . ARG   B 2 685 ? 42.471  58.391  -38.814 1.00 177.83 ? 989  ARG   B CA  1 
ATOM   7631  C  C   . ARG   B 2 685 ? 40.996  58.175  -38.514 1.00 166.96 ? 989  ARG   B C   1 
ATOM   7632  O  O   . ARG   B 2 685 ? 40.424  58.902  -37.700 1.00 163.83 ? 989  ARG   B O   1 
ATOM   7633  C  CB  . ARG   B 2 685 ? 42.674  59.554  -39.776 1.00 183.14 ? 989  ARG   B CB  1 
ATOM   7634  C  CG  . ARG   B 2 685 ? 44.144  59.828  -40.024 1.00 187.78 ? 989  ARG   B CG  1 
ATOM   7635  C  CD  . ARG   B 2 685 ? 44.325  60.903  -41.046 1.00 187.54 ? 989  ARG   B CD  1 
ATOM   7636  N  NE  . ARG   B 2 685 ? 43.647  62.125  -40.655 1.00 189.45 ? 989  ARG   B NE  1 
ATOM   7637  C  CZ  . ARG   B 2 685 ? 43.145  62.994  -41.517 1.00 193.41 ? 989  ARG   B CZ  1 
ATOM   7638  N  NH1 . ARG   B 2 685 ? 43.208  62.783  -42.823 1.00 194.11 ? 989  ARG   B NH1 1 
ATOM   7639  N  NH2 . ARG   B 2 685 ? 42.558  64.097  -41.059 1.00 193.81 ? 989  ARG   B NH2 1 
ATOM   7640  N  N   . GLN   B 2 686 ? 40.367  57.192  -39.149 1.00 163.46 ? 990  GLN   B N   1 
ATOM   7641  C  CA  . GLN   B 2 686 ? 39.011  56.805  -38.769 1.00 153.30 ? 990  GLN   B CA  1 
ATOM   7642  C  C   . GLN   B 2 686 ? 39.038  55.737  -37.673 1.00 150.80 ? 990  GLN   B C   1 
ATOM   7643  O  O   . GLN   B 2 686 ? 38.395  54.697  -37.786 1.00 149.32 ? 990  GLN   B O   1 
ATOM   7644  C  CB  . GLN   B 2 686 ? 38.226  56.311  -39.986 1.00 154.09 ? 990  GLN   B CB  1 
ATOM   7645  C  CG  . GLN   B 2 686 ? 38.317  57.208  -41.213 1.00 156.53 ? 990  GLN   B CG  1 
ATOM   7646  C  CD  . GLN   B 2 686 ? 38.630  56.444  -42.492 1.00 166.95 ? 990  GLN   B CD  1 
ATOM   7647  O  OE1 . GLN   B 2 686 ? 39.063  55.292  -42.449 1.00 167.53 ? 990  GLN   B OE1 1 
ATOM   7648  N  NE2 . GLN   B 2 686 ? 38.410  57.086  -43.641 1.00 172.06 ? 990  GLN   B NE2 1 
ATOM   7649  N  N   . HIS   B 2 687 ? 39.807  55.969  -36.610 1.00 146.35 ? 991  HIS   B N   1 
ATOM   7650  C  CA  . HIS   B 2 687 ? 39.736  55.091  -35.451 1.00 138.29 ? 991  HIS   B CA  1 
ATOM   7651  C  C   . HIS   B 2 687 ? 40.334  55.779  -34.227 1.00 139.34 ? 991  HIS   B C   1 
ATOM   7652  O  O   . HIS   B 2 687 ? 41.393  56.417  -34.314 1.00 140.49 ? 991  HIS   B O   1 
ATOM   7653  C  CB  . HIS   B 2 687 ? 40.451  53.757  -35.683 1.00 139.95 ? 991  HIS   B CB  1 
ATOM   7654  C  CG  . HIS   B 2 687 ? 40.679  52.997  -34.417 1.00 138.91 ? 991  HIS   B CG  1 
ATOM   7655  N  ND1 . HIS   B 2 687 ? 41.932  52.796  -33.877 1.00 137.54 ? 991  HIS   B ND1 1 
ATOM   7656  C  CD2 . HIS   B 2 687 ? 39.801  52.452  -33.542 1.00 137.44 ? 991  HIS   B CD2 1 
ATOM   7657  C  CE1 . HIS   B 2 687 ? 41.816  52.128  -32.741 1.00 137.17 ? 991  HIS   B CE1 1 
ATOM   7658  N  NE2 . HIS   B 2 687 ? 40.533  51.909  -32.515 1.00 137.87 ? 991  HIS   B NE2 1 
ATOM   7659  N  N   . LEU   B 2 688 ? 39.660  55.606  -33.085 1.00 136.12 ? 992  LEU   B N   1 
ATOM   7660  C  CA  . LEU   B 2 688 ? 40.090  56.156  -31.801 1.00 128.84 ? 992  LEU   B CA  1 
ATOM   7661  C  C   . LEU   B 2 688 ? 40.833  55.092  -30.999 1.00 128.75 ? 992  LEU   B C   1 
ATOM   7662  O  O   . LEU   B 2 688 ? 40.305  53.998  -30.763 1.00 130.79 ? 992  LEU   B O   1 
ATOM   7663  C  CB  . LEU   B 2 688 ? 38.882  56.653  -31.020 1.00 119.23 ? 992  LEU   B CB  1 
ATOM   7664  C  CG  . LEU   B 2 688 ? 37.819  57.249  -31.916 1.00 116.89 ? 992  LEU   B CG  1 
ATOM   7665  C  CD1 . LEU   B 2 688 ? 36.531  57.305  -31.160 1.00 112.92 ? 992  LEU   B CD1 1 
ATOM   7666  C  CD2 . LEU   B 2 688 ? 38.263  58.629  -32.333 1.00 123.63 ? 992  LEU   B CD2 1 
ATOM   7667  N  N   . GLN   B 2 689 ? 42.045  55.407  -30.565 1.00 124.24 ? 993  GLN   B N   1 
ATOM   7668  C  CA  . GLN   B 2 689 ? 42.845  54.462  -29.798 1.00 123.34 ? 993  GLN   B CA  1 
ATOM   7669  C  C   . GLN   B 2 689 ? 42.754  54.766  -28.308 1.00 120.26 ? 993  GLN   B C   1 
ATOM   7670  O  O   . GLN   B 2 689 ? 42.762  55.932  -27.898 1.00 116.59 ? 993  GLN   B O   1 
ATOM   7671  C  CB  . GLN   B 2 689 ? 44.302  54.495  -30.244 1.00 123.92 ? 993  GLN   B CB  1 
ATOM   7672  C  CG  . GLN   B 2 689 ? 44.500  54.320  -31.734 1.00 131.32 ? 993  GLN   B CG  1 
ATOM   7673  C  CD  . GLN   B 2 689 ? 45.931  54.588  -32.152 1.00 135.53 ? 993  GLN   B CD  1 
ATOM   7674  O  OE1 . GLN   B 2 689 ? 46.689  55.241  -31.429 1.00 137.66 ? 993  GLN   B OE1 1 
ATOM   7675  N  NE2 . GLN   B 2 689 ? 46.313  54.085  -33.321 1.00 136.58 ? 993  GLN   B NE2 1 
ATOM   7676  N  N   . GLU   B 2 690 ? 42.690  53.702  -27.500 1.00 123.40 ? 994  GLU   B N   1 
ATOM   7677  C  CA  . GLU   B 2 690 ? 42.567  53.835  -26.048 1.00 121.06 ? 994  GLU   B CA  1 
ATOM   7678  C  C   . GLU   B 2 690 ? 43.870  54.342  -25.434 1.00 118.12 ? 994  GLU   B C   1 
ATOM   7679  O  O   . GLU   B 2 690 ? 44.939  53.768  -25.654 1.00 117.94 ? 994  GLU   B O   1 
ATOM   7680  C  CB  . GLU   B 2 690 ? 42.189  52.494  -25.420 1.00 121.47 ? 994  GLU   B CB  1 
ATOM   7681  C  CG  . GLU   B 2 690 ? 41.097  51.748  -26.154 1.00 124.40 ? 994  GLU   B CG  1 
ATOM   7682  C  CD  . GLU   B 2 690 ? 40.868  50.353  -25.583 1.00 129.54 ? 994  GLU   B CD  1 
ATOM   7683  O  OE1 . GLU   B 2 690 ? 40.332  50.257  -24.454 1.00 125.48 ? 994  GLU   B OE1 1 
ATOM   7684  O  OE2 . GLU   B 2 690 ? 41.241  49.355  -26.251 1.00 134.28 ? 994  GLU   B OE2 1 
ATOM   7685  N  N   . VAL   B 2 691 ? 43.778  55.407  -24.636 1.00 112.34 ? 995  VAL   B N   1 
ATOM   7686  C  CA  . VAL   B 2 691 ? 44.971  56.064  -24.114 1.00 109.11 ? 995  VAL   B CA  1 
ATOM   7687  C  C   . VAL   B 2 691 ? 44.872  56.311  -22.606 1.00 104.76 ? 995  VAL   B C   1 
ATOM   7688  O  O   . VAL   B 2 691 ? 45.608  57.142  -22.058 1.00 100.67 ? 995  VAL   B O   1 
ATOM   7689  C  CB  . VAL   B 2 691 ? 45.218  57.378  -24.874 1.00 108.62 ? 995  VAL   B CB  1 
ATOM   7690  C  CG1 . VAL   B 2 691 ? 45.373  57.117  -26.364 1.00 109.91 ? 995  VAL   B CG1 1 
ATOM   7691  C  CG2 . VAL   B 2 691 ? 44.067  58.316  -24.638 1.00 112.91 ? 995  VAL   B CG2 1 
ATOM   7692  N  N   . GLY   B 2 692 ? 43.972  55.588  -21.923 1.00 100.32 ? 996  GLY   B N   1 
ATOM   7693  C  CA  . GLY   B 2 692 ? 43.870  55.638  -20.470 1.00 94.80  ? 996  GLY   B CA  1 
ATOM   7694  C  C   . GLY   B 2 692 ? 42.884  54.659  -19.850 1.00 91.93  ? 996  GLY   B C   1 
ATOM   7695  O  O   . GLY   B 2 692 ? 41.737  54.587  -20.290 1.00 95.10  ? 996  GLY   B O   1 
ATOM   7696  N  N   . LEU   B 2 693 ? 43.298  53.906  -18.830 1.00 87.75  ? 997  LEU   B N   1 
ATOM   7697  C  CA  . LEU   B 2 693 ? 42.428  52.933  -18.182 1.00 87.30  ? 997  LEU   B CA  1 
ATOM   7698  C  C   . LEU   B 2 693 ? 42.520  53.082  -16.682 1.00 87.31  ? 997  LEU   B C   1 
ATOM   7699  O  O   . LEU   B 2 693 ? 43.593  53.354  -16.141 1.00 91.59  ? 997  LEU   B O   1 
ATOM   7700  C  CB  . LEU   B 2 693 ? 42.794  51.505  -18.538 1.00 89.59  ? 997  LEU   B CB  1 
ATOM   7701  C  CG  . LEU   B 2 693 ? 42.560  51.179  -20.006 1.00 92.30  ? 997  LEU   B CG  1 
ATOM   7702  C  CD1 . LEU   B 2 693 ? 43.166  49.841  -20.323 1.00 92.57  ? 997  LEU   B CD1 1 
ATOM   7703  C  CD2 . LEU   B 2 693 ? 41.072  51.225  -20.372 1.00 90.51  ? 997  LEU   B CD2 1 
ATOM   7704  N  N   . PHE   B 2 694 ? 41.402  52.842  -16.005 1.00 89.45  ? 998  PHE   B N   1 
ATOM   7705  C  CA  . PHE   B 2 694 ? 41.373  53.099  -14.570 1.00 89.31  ? 998  PHE   B CA  1 
ATOM   7706  C  C   . PHE   B 2 694 ? 40.178  52.459  -13.861 1.00 85.50  ? 998  PHE   B C   1 
ATOM   7707  O  O   . PHE   B 2 694 ? 39.022  52.710  -14.215 1.00 85.47  ? 998  PHE   B O   1 
ATOM   7708  C  CB  . PHE   B 2 694 ? 41.394  54.610  -14.349 1.00 87.64  ? 998  PHE   B CB  1 
ATOM   7709  C  CG  . PHE   B 2 694 ? 41.676  55.005  -12.965 1.00 84.38  ? 998  PHE   B CG  1 
ATOM   7710  C  CD1 . PHE   B 2 694 ? 42.947  54.916  -12.460 1.00 84.62  ? 998  PHE   B CD1 1 
ATOM   7711  C  CD2 . PHE   B 2 694 ? 40.664  55.485  -12.170 1.00 85.64  ? 998  PHE   B CD2 1 
ATOM   7712  C  CE1 . PHE   B 2 694 ? 43.197  55.293  -11.164 1.00 90.29  ? 998  PHE   B CE1 1 
ATOM   7713  C  CE2 . PHE   B 2 694 ? 40.897  55.858  -10.896 1.00 87.33  ? 998  PHE   B CE2 1 
ATOM   7714  C  CZ  . PHE   B 2 694 ? 42.164  55.771  -10.382 1.00 89.07  ? 998  PHE   B CZ  1 
ATOM   7715  N  N   . HIS   B 2 695 ? 40.447  51.620  -12.863 1.00 85.35  ? 999  HIS   B N   1 
ATOM   7716  C  CA  . HIS   B 2 695 ? 39.391  51.138  -11.980 1.00 83.95  ? 999  HIS   B CA  1 
ATOM   7717  C  C   . HIS   B 2 695 ? 39.071  52.265  -11.014 1.00 83.76  ? 999  HIS   B C   1 
ATOM   7718  O  O   . HIS   B 2 695 ? 39.771  52.468  -10.019 1.00 84.88  ? 999  HIS   B O   1 
ATOM   7719  C  CB  . HIS   B 2 695 ? 39.814  49.876  -11.244 1.00 82.56  ? 999  HIS   B CB  1 
ATOM   7720  C  CG  . HIS   B 2 695 ? 38.673  49.140  -10.608 1.00 83.07  ? 999  HIS   B CG  1 
ATOM   7721  N  ND1 . HIS   B 2 695 ? 37.847  48.288  -11.314 1.00 85.02  ? 999  HIS   B ND1 1 
ATOM   7722  C  CD2 . HIS   B 2 695 ? 38.211  49.140  -9.335  1.00 84.54  ? 999  HIS   B CD2 1 
ATOM   7723  C  CE1 . HIS   B 2 695 ? 36.930  47.790  -10.503 1.00 84.92  ? 999  HIS   B CE1 1 
ATOM   7724  N  NE2 . HIS   B 2 695 ? 37.128  48.292  -9.295  1.00 83.00  ? 999  HIS   B NE2 1 
ATOM   7725  N  N   . LEU   B 2 696 ? 38.019  53.023  -11.315 1.00 83.99  ? 1000 LEU   B N   1 
ATOM   7726  C  CA  . LEU   B 2 696 ? 37.614  54.084  -10.404 1.00 82.64  ? 1000 LEU   B CA  1 
ATOM   7727  C  C   . LEU   B 2 696 ? 37.023  53.507  -9.128  1.00 80.17  ? 1000 LEU   B C   1 
ATOM   7728  O  O   . LEU   B 2 696 ? 37.262  54.024  -8.031  1.00 82.18  ? 1000 LEU   B O   1 
ATOM   7729  C  CB  . LEU   B 2 696 ? 36.613  55.002  -11.089 1.00 79.43  ? 1000 LEU   B CB  1 
ATOM   7730  C  CG  . LEU   B 2 696 ? 35.891  55.928  -10.139 1.00 78.33  ? 1000 LEU   B CG  1 
ATOM   7731  C  CD1 . LEU   B 2 696 ? 36.738  57.125  -9.936  1.00 78.97  ? 1000 LEU   B CD1 1 
ATOM   7732  C  CD2 . LEU   B 2 696 ? 34.632  56.303  -10.783 1.00 78.00  ? 1000 LEU   B CD2 1 
ATOM   7733  N  N   . GLY   B 2 697 ? 36.273  52.426  -9.252  1.00 77.56  ? 1001 GLY   B N   1 
ATOM   7734  C  CA  . GLY   B 2 697 ? 35.599  51.854  -8.120  1.00 79.03  ? 1001 GLY   B CA  1 
ATOM   7735  C  C   . GLY   B 2 697 ? 34.191  52.351  -7.925  1.00 82.23  ? 1001 GLY   B C   1 
ATOM   7736  O  O   . GLY   B 2 697 ? 33.551  51.967  -6.942  1.00 85.22  ? 1001 GLY   B O   1 
ATOM   7737  N  N   . GLU   B 2 698 ? 33.686  53.187  -8.825  1.00 83.45  ? 1002 GLU   B N   1 
ATOM   7738  C  CA  . GLU   B 2 698 ? 32.350  53.733  -8.703  1.00 82.19  ? 1002 GLU   B CA  1 
ATOM   7739  C  C   . GLU   B 2 698 ? 31.597  53.554  -10.011 1.00 82.78  ? 1002 GLU   B C   1 
ATOM   7740  O  O   . GLU   B 2 698 ? 32.192  53.261  -11.049 1.00 83.35  ? 1002 GLU   B O   1 
ATOM   7741  C  CB  . GLU   B 2 698 ? 32.403  55.205  -8.323  1.00 83.22  ? 1002 GLU   B CB  1 
ATOM   7742  C  CG  . GLU   B 2 698 ? 32.580  55.424  -6.872  1.00 87.39  ? 1002 GLU   B CG  1 
ATOM   7743  C  CD  . GLU   B 2 698 ? 31.470  54.780  -6.066  1.00 89.81  ? 1002 GLU   B CD  1 
ATOM   7744  O  OE1 . GLU   B 2 698 ? 30.356  54.572  -6.618  1.00 88.31  ? 1002 GLU   B OE1 1 
ATOM   7745  O  OE2 . GLU   B 2 698 ? 31.713  54.484  -4.872  1.00 91.27  ? 1002 GLU   B OE2 1 
ATOM   7746  N  N   . PHE   B 2 699 ? 30.278  53.750  -9.961  1.00 76.99  ? 1003 PHE   B N   1 
ATOM   7747  C  CA  . PHE   B 2 699 ? 29.440  53.640  -11.156 1.00 78.74  ? 1003 PHE   B CA  1 
ATOM   7748  C  C   . PHE   B 2 699 ? 29.019  55.031  -11.590 1.00 80.08  ? 1003 PHE   B C   1 
ATOM   7749  O  O   . PHE   B 2 699 ? 28.127  55.628  -10.981 1.00 80.06  ? 1003 PHE   B O   1 
ATOM   7750  C  CB  . PHE   B 2 699 ? 28.211  52.776  -10.900 1.00 83.60  ? 1003 PHE   B CB  1 
ATOM   7751  C  CG  . PHE   B 2 699 ? 27.553  52.242  -12.165 1.00 81.08  ? 1003 PHE   B CG  1 
ATOM   7752  C  CD1 . PHE   B 2 699 ? 28.000  51.066  -12.748 1.00 84.68  ? 1003 PHE   B CD1 1 
ATOM   7753  C  CD2 . PHE   B 2 699 ? 26.478  52.897  -12.741 1.00 76.78  ? 1003 PHE   B CD2 1 
ATOM   7754  C  CE1 . PHE   B 2 699 ? 27.401  50.578  -13.874 1.00 86.20  ? 1003 PHE   B CE1 1 
ATOM   7755  C  CE2 . PHE   B 2 699 ? 25.874  52.402  -13.873 1.00 74.81  ? 1003 PHE   B CE2 1 
ATOM   7756  C  CZ  . PHE   B 2 699 ? 26.332  51.255  -14.439 1.00 76.36  ? 1003 PHE   B CZ  1 
ATOM   7757  N  N   . VAL   B 2 700 ? 29.635  55.527  -12.662 1.00 80.87  ? 1004 VAL   B N   1 
ATOM   7758  C  CA  . VAL   B 2 700 ? 29.429  56.904  -13.099 1.00 77.76  ? 1004 VAL   B CA  1 
ATOM   7759  C  C   . VAL   B 2 700 ? 28.161  57.005  -13.941 1.00 76.38  ? 1004 VAL   B C   1 
ATOM   7760  O  O   . VAL   B 2 700 ? 27.999  56.293  -14.938 1.00 76.28  ? 1004 VAL   B O   1 
ATOM   7761  C  CB  . VAL   B 2 700 ? 30.651  57.408  -13.874 1.00 77.07  ? 1004 VAL   B CB  1 
ATOM   7762  C  CG1 . VAL   B 2 700 ? 30.336  58.724  -14.527 1.00 77.37  ? 1004 VAL   B CG1 1 
ATOM   7763  C  CG2 . VAL   B 2 700 ? 31.836  57.511  -12.954 1.00 77.43  ? 1004 VAL   B CG2 1 
ATOM   7764  N  N   . ASN   B 2 701 ? 27.273  57.921  -13.556 1.00 76.81  ? 1005 ASN   B N   1 
ATOM   7765  C  CA  . ASN   B 2 701 ? 25.996  58.107  -14.233 1.00 76.23  ? 1005 ASN   B CA  1 
ATOM   7766  C  C   . ASN   B 2 701 ? 25.933  59.355  -15.102 1.00 79.45  ? 1005 ASN   B C   1 
ATOM   7767  O  O   . ASN   B 2 701 ? 25.306  59.309  -16.169 1.00 79.59  ? 1005 ASN   B O   1 
ATOM   7768  C  CB  . ASN   B 2 701 ? 24.861  58.166  -13.216 1.00 76.06  ? 1005 ASN   B CB  1 
ATOM   7769  C  CG  . ASN   B 2 701 ? 24.194  56.844  -13.033 1.00 75.62  ? 1005 ASN   B CG  1 
ATOM   7770  O  OD1 . ASN   B 2 701 ? 24.414  55.932  -13.814 1.00 77.46  ? 1005 ASN   B OD1 1 
ATOM   7771  N  ND2 . ASN   B 2 701 ? 23.367  56.725  -12.007 1.00 75.50  ? 1005 ASN   B ND2 1 
ATOM   7772  N  N   . VAL   B 2 702 ? 26.569  60.455  -14.688 1.00 76.97  ? 1006 VAL   B N   1 
ATOM   7773  C  CA  . VAL   B 2 702 ? 26.583  61.698  -15.451 1.00 77.33  ? 1006 VAL   B CA  1 
ATOM   7774  C  C   . VAL   B 2 702 ? 27.961  62.338  -15.344 1.00 79.58  ? 1006 VAL   B C   1 
ATOM   7775  O  O   . VAL   B 2 702 ? 28.524  62.418  -14.250 1.00 85.36  ? 1006 VAL   B O   1 
ATOM   7776  C  CB  . VAL   B 2 702 ? 25.501  62.672  -14.949 1.00 77.38  ? 1006 VAL   B CB  1 
ATOM   7777  C  CG1 . VAL   B 2 702 ? 25.573  62.823  -13.460 1.00 77.69  ? 1006 VAL   B CG1 1 
ATOM   7778  C  CG2 . VAL   B 2 702 ? 25.619  64.018  -15.633 1.00 79.08  ? 1006 VAL   B CG2 1 
ATOM   7779  N  N   . PHE   B 2 703 ? 28.503  62.789  -16.477 1.00 87.60  ? 1007 PHE   B N   1 
ATOM   7780  C  CA  . PHE   B 2 703 ? 29.637  63.708  -16.532 1.00 85.83  ? 1007 PHE   B CA  1 
ATOM   7781  C  C   . PHE   B 2 703 ? 29.132  65.120  -16.782 1.00 89.05  ? 1007 PHE   B C   1 
ATOM   7782  O  O   . PHE   B 2 703 ? 28.147  65.320  -17.501 1.00 92.20  ? 1007 PHE   B O   1 
ATOM   7783  C  CB  . PHE   B 2 703 ? 30.621  63.365  -17.647 1.00 86.00  ? 1007 PHE   B CB  1 
ATOM   7784  C  CG  . PHE   B 2 703 ? 31.494  62.191  -17.355 1.00 85.59  ? 1007 PHE   B CG  1 
ATOM   7785  C  CD1 . PHE   B 2 703 ? 32.487  62.271  -16.402 1.00 84.71  ? 1007 PHE   B CD1 1 
ATOM   7786  C  CD2 . PHE   B 2 703 ? 31.344  61.016  -18.063 1.00 86.26  ? 1007 PHE   B CD2 1 
ATOM   7787  C  CE1 . PHE   B 2 703 ? 33.301  61.192  -16.151 1.00 85.61  ? 1007 PHE   B CE1 1 
ATOM   7788  C  CE2 . PHE   B 2 703 ? 32.151  59.934  -17.811 1.00 84.90  ? 1007 PHE   B CE2 1 
ATOM   7789  C  CZ  . PHE   B 2 703 ? 33.132  60.020  -16.856 1.00 84.41  ? 1007 PHE   B CZ  1 
ATOM   7790  N  N   . CYS   B 2 704 ? 29.840  66.098  -16.233 1.00 92.40  ? 1008 CYS   B N   1 
ATOM   7791  C  CA  . CYS   B 2 704 ? 29.313  67.455  -16.204 1.00 93.30  ? 1008 CYS   B CA  1 
ATOM   7792  C  C   . CYS   B 2 704 ? 30.479  68.418  -16.095 1.00 95.28  ? 1008 CYS   B C   1 
ATOM   7793  O  O   . CYS   B 2 704 ? 31.188  68.407  -15.085 1.00 94.79  ? 1008 CYS   B O   1 
ATOM   7794  C  CB  . CYS   B 2 704 ? 28.353  67.626  -15.027 1.00 93.36  ? 1008 CYS   B CB  1 
ATOM   7795  S  SG  . CYS   B 2 704 ? 27.467  69.168  -15.051 1.00 99.67  ? 1008 CYS   B SG  1 
ATOM   7796  N  N   . HIS   B 2 705 ? 30.672  69.246  -17.119 1.00 95.85  ? 1009 HIS   B N   1 
ATOM   7797  C  CA  . HIS   B 2 705 ? 31.800  70.175  -17.127 1.00 97.45  ? 1009 HIS   B CA  1 
ATOM   7798  C  C   . HIS   B 2 705 ? 31.563  71.338  -16.173 1.00 96.09  ? 1009 HIS   B C   1 
ATOM   7799  O  O   . HIS   B 2 705 ? 30.472  71.905  -16.125 1.00 96.16  ? 1009 HIS   B O   1 
ATOM   7800  C  CB  . HIS   B 2 705 ? 32.042  70.705  -18.535 1.00 99.44  ? 1009 HIS   B CB  1 
ATOM   7801  C  CG  . HIS   B 2 705 ? 32.934  69.833  -19.359 1.00 101.09 ? 1009 HIS   B CG  1 
ATOM   7802  N  ND1 . HIS   B 2 705 ? 34.309  69.909  -19.297 1.00 103.22 ? 1009 HIS   B ND1 1 
ATOM   7803  C  CD2 . HIS   B 2 705 ? 32.650  68.849  -20.243 1.00 101.13 ? 1009 HIS   B CD2 1 
ATOM   7804  C  CE1 . HIS   B 2 705 ? 34.833  69.020  -20.122 1.00 103.78 ? 1009 HIS   B CE1 1 
ATOM   7805  N  NE2 . HIS   B 2 705 ? 33.848  68.363  -20.708 1.00 100.97 ? 1009 HIS   B NE2 1 
ATOM   7806  N  N   . GLY   B 2 706 ? 32.598  71.708  -15.420 1.00 93.96  ? 1010 GLY   B N   1 
ATOM   7807  C  CA  . GLY   B 2 706 ? 32.460  72.751  -14.422 1.00 95.24  ? 1010 GLY   B CA  1 
ATOM   7808  C  C   . GLY   B 2 706 ? 33.271  72.477  -13.174 1.00 93.21  ? 1010 GLY   B C   1 
ATOM   7809  O  O   . GLY   B 2 706 ? 33.645  71.331  -12.891 1.00 92.23  ? 1010 GLY   B O   1 
ATOM   7810  N  N   . SER   B 2 707 ? 33.576  73.542  -12.439 1.00 94.04  ? 1011 SER   B N   1 
ATOM   7811  C  CA  . SER   B 2 707 ? 34.215  73.442  -11.136 1.00 96.04  ? 1011 SER   B CA  1 
ATOM   7812  C  C   . SER   B 2 707 ? 33.288  73.954  -10.049 1.00 99.06  ? 1011 SER   B C   1 
ATOM   7813  O  O   . SER   B 2 707 ? 32.271  74.602  -10.303 1.00 103.23 ? 1011 SER   B O   1 
ATOM   7814  C  CB  . SER   B 2 707 ? 35.524  74.236  -11.044 1.00 97.46  ? 1011 SER   B CB  1 
ATOM   7815  O  OG  . SER   B 2 707 ? 36.595  73.607  -11.749 1.00 96.30  ? 1011 SER   B OG  1 
ATOM   7816  N  N   . LEU   B 2 708 ? 33.672  73.676  -8.820  1.00 101.17 ? 1012 LEU   B N   1 
ATOM   7817  C  CA  . LEU   B 2 708 ? 32.984  74.218  -7.664  1.00 108.60 ? 1012 LEU   B CA  1 
ATOM   7818  C  C   . LEU   B 2 708 ? 33.907  75.136  -6.879  1.00 111.52 ? 1012 LEU   B C   1 
ATOM   7819  O  O   . LEU   B 2 708 ? 33.666  75.417  -5.698  1.00 110.96 ? 1012 LEU   B O   1 
ATOM   7820  C  CB  . LEU   B 2 708 ? 32.444  73.069  -6.813  1.00 107.71 ? 1012 LEU   B CB  1 
ATOM   7821  C  CG  . LEU   B 2 708 ? 31.694  72.056  -7.684  1.00 97.79  ? 1012 LEU   B CG  1 
ATOM   7822  C  CD1 . LEU   B 2 708 ? 31.255  70.860  -6.875  1.00 91.40  ? 1012 LEU   B CD1 1 
ATOM   7823  C  CD2 . LEU   B 2 708 ? 30.515  72.734  -8.390  1.00 97.04  ? 1012 LEU   B CD2 1 
ATOM   7824  N  N   . VAL   B 2 709 ? 34.974  75.592  -7.531  1.00 110.64 ? 1013 VAL   B N   1 
ATOM   7825  C  CA  . VAL   B 2 709 ? 36.030  76.396  -6.910  1.00 115.43 ? 1013 VAL   B CA  1 
ATOM   7826  C  C   . VAL   B 2 709 ? 36.153  77.652  -7.756  1.00 121.19 ? 1013 VAL   B C   1 
ATOM   7827  O  O   . VAL   B 2 709 ? 35.319  77.889  -8.639  1.00 123.07 ? 1013 VAL   B O   1 
ATOM   7828  C  CB  . VAL   B 2 709 ? 37.353  75.600  -6.930  1.00 114.50 ? 1013 VAL   B CB  1 
ATOM   7829  C  CG1 . VAL   B 2 709 ? 37.403  74.599  -5.764  1.00 108.72 ? 1013 VAL   B CG1 1 
ATOM   7830  C  CG2 . VAL   B 2 709 ? 37.513  74.866  -8.253  1.00 109.70 ? 1013 VAL   B CG2 1 
ATOM   7831  N  N   . MET   B 2 710 ? 37.173  78.481  -7.496  1.00 122.09 ? 1014 MET   B N   1 
ATOM   7832  C  CA  . MET   B 2 710 ? 37.430  79.717  -8.290  1.00 126.61 ? 1014 MET   B CA  1 
ATOM   7833  C  C   . MET   B 2 710 ? 36.317  80.726  -8.001  1.00 125.54 ? 1014 MET   B C   1 
ATOM   7834  O  O   . MET   B 2 710 ? 36.505  81.680  -7.239  1.00 120.97 ? 1014 MET   B O   1 
ATOM   7835  C  CB  . MET   B 2 710 ? 37.533  79.447  -9.817  1.00 128.71 ? 1014 MET   B CB  1 
ATOM   7836  C  CG  . MET   B 2 710 ? 37.195  80.630  -10.763 1.00 125.86 ? 1014 MET   B CG  1 
ATOM   7837  S  SD  . MET   B 2 710 ? 38.365  82.027  -10.861 1.00 142.37 ? 1014 MET   B SD  1 
ATOM   7838  C  CE  . MET   B 2 710 ? 39.860  81.268  -11.493 1.00 130.34 ? 1014 MET   B CE  1 
ATOM   7839  N  N   . PRO   B 2 719 ? 47.542  75.740  -14.259 1.00 154.61 ? 1023 PRO   B N   1 
ATOM   7840  C  CA  . PRO   B 2 719 ? 48.248  74.541  -13.783 1.00 155.63 ? 1023 PRO   B CA  1 
ATOM   7841  C  C   . PRO   B 2 719 ? 47.761  73.263  -14.471 1.00 156.57 ? 1023 PRO   B C   1 
ATOM   7842  O  O   . PRO   B 2 719 ? 48.290  72.888  -15.523 1.00 156.91 ? 1023 PRO   B O   1 
ATOM   7843  C  CB  . PRO   B 2 719 ? 47.922  74.505  -12.281 1.00 152.87 ? 1023 PRO   B CB  1 
ATOM   7844  C  CG  . PRO   B 2 719 ? 46.858  75.592  -12.052 1.00 154.31 ? 1023 PRO   B CG  1 
ATOM   7845  C  CD  . PRO   B 2 719 ? 46.400  76.075  -13.395 1.00 153.88 ? 1023 PRO   B CD  1 
ATOM   7846  N  N   . THR   B 2 720 ? 46.792  72.585  -13.853 1.00 147.51 ? 1024 THR   B N   1 
ATOM   7847  C  CA  . THR   B 2 720 ? 46.092  71.473  -14.487 1.00 134.08 ? 1024 THR   B CA  1 
ATOM   7848  C  C   . THR   B 2 720 ? 44.971  71.990  -15.383 1.00 131.28 ? 1024 THR   B C   1 
ATOM   7849  O  O   . THR   B 2 720 ? 44.340  73.016  -15.100 1.00 135.99 ? 1024 THR   B O   1 
ATOM   7850  C  CB  . THR   B 2 720 ? 45.481  70.540  -13.444 1.00 127.70 ? 1024 THR   B CB  1 
ATOM   7851  O  OG1 . THR   B 2 720 ? 44.622  71.298  -12.583 1.00 128.27 ? 1024 THR   B OG1 1 
ATOM   7852  C  CG2 . THR   B 2 720 ? 46.549  69.863  -12.622 1.00 128.62 ? 1024 THR   B CG2 1 
ATOM   7853  N  N   . GLN   B 2 721 ? 44.688  71.238  -16.441 1.00 124.26 ? 1025 GLN   B N   1 
ATOM   7854  C  CA  . GLN   B 2 721 ? 43.770  71.660  -17.488 1.00 120.61 ? 1025 GLN   B CA  1 
ATOM   7855  C  C   . GLN   B 2 721 ? 42.450  70.907  -17.411 1.00 120.85 ? 1025 GLN   B C   1 
ATOM   7856  O  O   . GLN   B 2 721 ? 42.426  69.698  -17.164 1.00 120.89 ? 1025 GLN   B O   1 
ATOM   7857  C  CB  . GLN   B 2 721 ? 44.393  71.439  -18.863 1.00 121.13 ? 1025 GLN   B CB  1 
ATOM   7858  C  CG  . GLN   B 2 721 ? 45.262  72.572  -19.327 1.00 123.94 ? 1025 GLN   B CG  1 
ATOM   7859  C  CD  . GLN   B 2 721 ? 44.446  73.748  -19.828 1.00 125.40 ? 1025 GLN   B CD  1 
ATOM   7860  O  OE1 . GLN   B 2 721 ? 43.755  74.428  -19.062 1.00 128.15 ? 1025 GLN   B OE1 1 
ATOM   7861  N  NE2 . GLN   B 2 721 ? 44.517  73.989  -21.128 1.00 122.66 ? 1025 GLN   B NE2 1 
ATOM   7862  N  N   . GLY   B 2 722 ? 41.355  71.623  -17.657 1.00 126.32 ? 1026 GLY   B N   1 
ATOM   7863  C  CA  . GLY   B 2 722 ? 40.041  71.021  -17.748 1.00 122.63 ? 1026 GLY   B CA  1 
ATOM   7864  C  C   . GLY   B 2 722 ? 39.358  70.895  -16.399 1.00 120.25 ? 1026 GLY   B C   1 
ATOM   7865  O  O   . GLY   B 2 722 ? 39.967  71.041  -15.338 1.00 127.74 ? 1026 GLY   B O   1 
ATOM   7866  N  N   . SER   B 2 723 ? 38.052  70.642  -16.440 1.00 103.60 ? 1027 SER   B N   1 
ATOM   7867  C  CA  . SER   B 2 723 ? 37.344  70.266  -15.216 1.00 101.15 ? 1027 SER   B CA  1 
ATOM   7868  C  C   . SER   B 2 723 ? 36.086  69.496  -15.571 1.00 99.97  ? 1027 SER   B C   1 
ATOM   7869  O  O   . SER   B 2 723 ? 35.111  70.086  -16.053 1.00 96.24  ? 1027 SER   B O   1 
ATOM   7870  C  CB  . SER   B 2 723 ? 37.003  71.477  -14.366 1.00 96.93  ? 1027 SER   B CB  1 
ATOM   7871  O  OG  . SER   B 2 723 ? 36.198  71.036  -13.289 1.00 90.47  ? 1027 SER   B OG  1 
ATOM   7872  N  N   . VAL   B 2 724 ? 36.087  68.189  -15.303 1.00 97.97  ? 1028 VAL   B N   1 
ATOM   7873  C  CA  . VAL   B 2 724 ? 34.922  67.342  -15.511 1.00 92.74  ? 1028 VAL   B CA  1 
ATOM   7874  C  C   . VAL   B 2 724 ? 34.521  66.724  -14.176 1.00 89.44  ? 1028 VAL   B C   1 
ATOM   7875  O  O   . VAL   B 2 724 ? 35.224  65.857  -13.640 1.00 88.81  ? 1028 VAL   B O   1 
ATOM   7876  C  CB  . VAL   B 2 724 ? 35.173  66.261  -16.566 1.00 92.09  ? 1028 VAL   B CB  1 
ATOM   7877  C  CG1 . VAL   B 2 724 ? 33.888  65.493  -16.822 1.00 95.73  ? 1028 VAL   B CG1 1 
ATOM   7878  C  CG2 . VAL   B 2 724 ? 35.692  66.885  -17.847 1.00 91.72  ? 1028 VAL   B CG2 1 
ATOM   7879  N  N   . LEU   B 2 725 ? 33.395  67.183  -13.640 1.00 89.24  ? 1029 LEU   B N   1 
ATOM   7880  C  CA  . LEU   B 2 725 ? 32.780  66.620  -12.449 1.00 88.38  ? 1029 LEU   B CA  1 
ATOM   7881  C  C   . LEU   B 2 725 ? 31.930  65.420  -12.821 1.00 88.42  ? 1029 LEU   B C   1 
ATOM   7882  O  O   . LEU   B 2 725 ? 31.308  65.394  -13.885 1.00 91.09  ? 1029 LEU   B O   1 
ATOM   7883  C  CB  . LEU   B 2 725 ? 31.885  67.644  -11.758 1.00 84.95  ? 1029 LEU   B CB  1 
ATOM   7884  C  CG  . LEU   B 2 725 ? 32.530  68.761  -10.966 1.00 81.40  ? 1029 LEU   B CG  1 
ATOM   7885  C  CD1 . LEU   B 2 725 ? 31.429  69.550  -10.334 1.00 87.08  ? 1029 LEU   B CD1 1 
ATOM   7886  C  CD2 . LEU   B 2 725 ? 33.423  68.185  -9.914  1.00 86.79  ? 1029 LEU   B CD2 1 
ATOM   7887  N  N   . PHE   B 2 726 ? 31.878  64.432  -11.929 1.00 84.49  ? 1030 PHE   B N   1 
ATOM   7888  C  CA  . PHE   B 2 726 ? 30.969  63.321  -12.148 1.00 79.72  ? 1030 PHE   B CA  1 
ATOM   7889  C  C   . PHE   B 2 726 ? 30.300  62.922  -10.851 1.00 78.78  ? 1030 PHE   B C   1 
ATOM   7890  O  O   . PHE   B 2 726 ? 30.876  63.057  -9.773  1.00 81.91  ? 1030 PHE   B O   1 
ATOM   7891  C  CB  . PHE   B 2 726 ? 31.668  62.105  -12.782 1.00 80.42  ? 1030 PHE   B CB  1 
ATOM   7892  C  CG  . PHE   B 2 726 ? 32.792  61.498  -11.971 1.00 78.90  ? 1030 PHE   B CG  1 
ATOM   7893  C  CD1 . PHE   B 2 726 ? 34.102  61.898  -12.179 1.00 82.68  ? 1030 PHE   B CD1 1 
ATOM   7894  C  CD2 . PHE   B 2 726 ? 32.552  60.459  -11.077 1.00 78.55  ? 1030 PHE   B CD2 1 
ATOM   7895  C  CE1 . PHE   B 2 726 ? 35.162  61.307  -11.472 1.00 81.39  ? 1030 PHE   B CE1 1 
ATOM   7896  C  CE2 . PHE   B 2 726 ? 33.595  59.872  -10.370 1.00 78.73  ? 1030 PHE   B CE2 1 
ATOM   7897  C  CZ  . PHE   B 2 726 ? 34.907  60.296  -10.572 1.00 79.26  ? 1030 PHE   B CZ  1 
ATOM   7898  N  N   . GLY   B 2 727 ? 29.074  62.426  -10.964 1.00 78.19  ? 1031 GLY   B N   1 
ATOM   7899  C  CA  . GLY   B 2 727 ? 28.400  61.819  -9.839  1.00 77.92  ? 1031 GLY   B CA  1 
ATOM   7900  C  C   . GLY   B 2 727 ? 28.138  60.352  -10.111 1.00 78.68  ? 1031 GLY   B C   1 
ATOM   7901  O  O   . GLY   B 2 727 ? 28.107  59.917  -11.270 1.00 77.23  ? 1031 GLY   B O   1 
ATOM   7902  N  N   . THR   B 2 728 ? 27.940  59.578  -9.045  1.00 79.54  ? 1032 THR   B N   1 
ATOM   7903  C  CA  . THR   B 2 728 ? 27.866  58.136  -9.180  1.00 76.82  ? 1032 THR   B CA  1 
ATOM   7904  C  C   . THR   B 2 728 ? 26.632  57.595  -8.473  1.00 76.48  ? 1032 THR   B C   1 
ATOM   7905  O  O   . THR   B 2 728 ? 25.819  58.331  -7.920  1.00 76.57  ? 1032 THR   B O   1 
ATOM   7906  C  CB  . THR   B 2 728 ? 29.120  57.452  -8.624  1.00 76.96  ? 1032 THR   B CB  1 
ATOM   7907  O  OG1 . THR   B 2 728 ? 29.288  57.816  -7.255  1.00 79.05  ? 1032 THR   B OG1 1 
ATOM   7908  C  CG2 . THR   B 2 728 ? 30.356  57.820  -9.432  1.00 77.30  ? 1032 THR   B CG2 1 
ATOM   7909  N  N   . VAL   B 2 729 ? 26.499  56.272  -8.533  1.00 81.42  ? 1033 VAL   B N   1 
ATOM   7910  C  CA  . VAL   B 2 729 ? 25.399  55.574  -7.882  1.00 80.71  ? 1033 VAL   B CA  1 
ATOM   7911  C  C   . VAL   B 2 729 ? 25.558  55.633  -6.375  1.00 79.72  ? 1033 VAL   B C   1 
ATOM   7912  O  O   . VAL   B 2 729 ? 24.577  55.765  -5.638  1.00 83.28  ? 1033 VAL   B O   1 
ATOM   7913  C  CB  . VAL   B 2 729 ? 25.341  54.121  -8.395  1.00 76.89  ? 1033 VAL   B CB  1 
ATOM   7914  C  CG1 . VAL   B 2 729 ? 24.571  53.257  -7.452  1.00 84.60  ? 1033 VAL   B CG1 1 
ATOM   7915  C  CG2 . VAL   B 2 729 ? 24.767  54.058  -9.804  1.00 75.19  ? 1033 VAL   B CG2 1 
ATOM   7916  N  N   . ASN   B 2 730 ? 26.790  55.550  -5.894  1.00 78.46  ? 1034 ASN   B N   1 
ATOM   7917  C  CA  . ASN   B 2 730 ? 27.067  55.578  -4.469  1.00 78.24  ? 1034 ASN   B CA  1 
ATOM   7918  C  C   . ASN   B 2 730 ? 27.140  56.986  -3.916  1.00 81.37  ? 1034 ASN   B C   1 
ATOM   7919  O  O   . ASN   B 2 730 ? 27.628  57.160  -2.792  1.00 83.36  ? 1034 ASN   B O   1 
ATOM   7920  C  CB  . ASN   B 2 730 ? 28.375  54.838  -4.172  1.00 79.97  ? 1034 ASN   B CB  1 
ATOM   7921  C  CG  . ASN   B 2 730 ? 28.249  53.322  -4.318  1.00 87.54  ? 1034 ASN   B CG  1 
ATOM   7922  O  OD1 . ASN   B 2 730 ? 27.826  52.639  -3.382  1.00 90.26  ? 1034 ASN   B OD1 1 
ATOM   7923  N  ND2 . ASN   B 2 730 ? 28.644  52.784  -5.487  1.00 89.36  ? 1034 ASN   B ND2 1 
ATOM   7924  N  N   . GLY   B 2 731 ? 26.675  57.991  -4.667  1.00 87.50  ? 1035 GLY   B N   1 
ATOM   7925  C  CA  . GLY   B 2 731 ? 26.750  59.378  -4.226  1.00 86.67  ? 1035 GLY   B CA  1 
ATOM   7926  C  C   . GLY   B 2 731 ? 28.143  59.974  -4.231  1.00 84.75  ? 1035 GLY   B C   1 
ATOM   7927  O  O   . GLY   B 2 731 ? 28.303  61.142  -3.850  1.00 83.43  ? 1035 GLY   B O   1 
ATOM   7928  N  N   . MET   B 2 732 ? 29.152  59.195  -4.633  1.00 81.80  ? 1036 MET   B N   1 
ATOM   7929  C  CA  . MET   B 2 732 ? 30.508  59.689  -4.806  1.00 78.32  ? 1036 MET   B CA  1 
ATOM   7930  C  C   . MET   B 2 732 ? 30.529  60.769  -5.868  1.00 78.50  ? 1036 MET   B C   1 
ATOM   7931  O  O   . MET   B 2 732 ? 29.962  60.596  -6.950  1.00 79.17  ? 1036 MET   B O   1 
ATOM   7932  C  CB  . MET   B 2 732 ? 31.421  58.531  -5.219  1.00 79.48  ? 1036 MET   B CB  1 
ATOM   7933  C  CG  . MET   B 2 732 ? 32.921  58.831  -5.261  1.00 82.52  ? 1036 MET   B CG  1 
ATOM   7934  S  SD  . MET   B 2 732 ? 33.597  59.382  -6.832  1.00 86.96  ? 1036 MET   B SD  1 
ATOM   7935  C  CE  . MET   B 2 732 ? 35.344  59.022  -6.611  1.00 82.83  ? 1036 MET   B CE  1 
ATOM   7936  N  N   . ILE   B 2 733 ? 31.176  61.885  -5.571  1.00 79.03  ? 1037 ILE   B N   1 
ATOM   7937  C  CA  . ILE   B 2 733 ? 31.364  62.938  -6.558  1.00 81.61  ? 1037 ILE   B CA  1 
ATOM   7938  C  C   . ILE   B 2 733 ? 32.855  63.101  -6.802  1.00 84.03  ? 1037 ILE   B C   1 
ATOM   7939  O  O   . ILE   B 2 733 ? 33.654  63.081  -5.858  1.00 85.63  ? 1037 ILE   B O   1 
ATOM   7940  C  CB  . ILE   B 2 733 ? 30.717  64.264  -6.128  1.00 79.56  ? 1037 ILE   B CB  1 
ATOM   7941  C  CG1 . ILE   B 2 733 ? 29.209  64.057  -5.969  1.00 79.12  ? 1037 ILE   B CG1 1 
ATOM   7942  C  CG2 . ILE   B 2 733 ? 31.027  65.333  -7.147  1.00 79.88  ? 1037 ILE   B CG2 1 
ATOM   7943  C  CD1 . ILE   B 2 733 ? 28.591  64.940  -4.947  1.00 79.35  ? 1037 ILE   B CD1 1 
ATOM   7944  N  N   . GLY   B 2 734 ? 33.224  63.252  -8.075  1.00 82.76  ? 1038 GLY   B N   1 
ATOM   7945  C  CA  . GLY   B 2 734 ? 34.610  63.158  -8.474  1.00 82.73  ? 1038 GLY   B CA  1 
ATOM   7946  C  C   . GLY   B 2 734 ? 34.965  64.181  -9.535  1.00 87.64  ? 1038 GLY   B C   1 
ATOM   7947  O  O   . GLY   B 2 734 ? 34.105  64.803  -10.167 1.00 85.23  ? 1038 GLY   B O   1 
ATOM   7948  N  N   . LEU   B 2 735 ? 36.270  64.311  -9.738  1.00 96.98  ? 1039 LEU   B N   1 
ATOM   7949  C  CA  . LEU   B 2 735 ? 36.865  65.348  -10.563 1.00 95.39  ? 1039 LEU   B CA  1 
ATOM   7950  C  C   . LEU   B 2 735 ? 37.879  64.713  -11.502 1.00 97.06  ? 1039 LEU   B C   1 
ATOM   7951  O  O   . LEU   B 2 735 ? 38.705  63.902  -11.069 1.00 98.25  ? 1039 LEU   B O   1 
ATOM   7952  C  CB  . LEU   B 2 735 ? 37.543  66.378  -9.675  1.00 95.60  ? 1039 LEU   B CB  1 
ATOM   7953  C  CG  . LEU   B 2 735 ? 37.825  67.679  -10.367 1.00 100.27 ? 1039 LEU   B CG  1 
ATOM   7954  C  CD1 . LEU   B 2 735 ? 36.632  67.975  -11.234 1.00 101.22 ? 1039 LEU   B CD1 1 
ATOM   7955  C  CD2 . LEU   B 2 735 ? 38.002  68.758  -9.322  1.00 106.40 ? 1039 LEU   B CD2 1 
ATOM   7956  N  N   . VAL   B 2 736 ? 37.813  65.050  -12.785 1.00 95.06  ? 1040 VAL   B N   1 
ATOM   7957  C  CA  . VAL   B 2 736 ? 38.855  64.666  -13.726 1.00 94.55  ? 1040 VAL   B CA  1 
ATOM   7958  C  C   . VAL   B 2 736 ? 39.421  65.937  -14.327 1.00 101.07 ? 1040 VAL   B C   1 
ATOM   7959  O  O   . VAL   B 2 736 ? 38.661  66.840  -14.699 1.00 98.69  ? 1040 VAL   B O   1 
ATOM   7960  C  CB  . VAL   B 2 736 ? 38.340  63.731  -14.828 1.00 87.63  ? 1040 VAL   B CB  1 
ATOM   7961  C  CG1 . VAL   B 2 736 ? 39.485  63.278  -15.667 1.00 94.06  ? 1040 VAL   B CG1 1 
ATOM   7962  C  CG2 . VAL   B 2 736 ? 37.690  62.559  -14.222 1.00 92.76  ? 1040 VAL   B CG2 1 
ATOM   7963  N  N   . THR   B 2 737 ? 40.753  66.019  -14.396 1.00 106.20 ? 1041 THR   B N   1 
ATOM   7964  C  CA  . THR   B 2 737 ? 41.444  67.106  -15.081 1.00 109.36 ? 1041 THR   B CA  1 
ATOM   7965  C  C   . THR   B 2 737 ? 42.623  66.529  -15.858 1.00 111.62 ? 1041 THR   B C   1 
ATOM   7966  O  O   . THR   B 2 737 ? 43.223  65.526  -15.456 1.00 108.25 ? 1041 THR   B O   1 
ATOM   7967  C  CB  . THR   B 2 737 ? 41.918  68.215  -14.115 1.00 106.82 ? 1041 THR   B CB  1 
ATOM   7968  O  OG1 . THR   B 2 737 ? 42.666  69.186  -14.848 1.00 114.44 ? 1041 THR   B OG1 1 
ATOM   7969  C  CG2 . THR   B 2 737 ? 42.801  67.655  -13.028 1.00 106.44 ? 1041 THR   B CG2 1 
ATOM   7970  N  N   . SER   B 2 738 ? 42.930  67.172  -16.990 1.00 117.51 ? 1042 SER   B N   1 
ATOM   7971  C  CA  . SER   B 2 738 ? 43.958  66.704  -17.915 1.00 116.56 ? 1042 SER   B CA  1 
ATOM   7972  C  C   . SER   B 2 738 ? 45.305  67.314  -17.560 1.00 115.57 ? 1042 SER   B C   1 
ATOM   7973  O  O   . SER   B 2 738 ? 45.386  68.459  -17.109 1.00 118.60 ? 1042 SER   B O   1 
ATOM   7974  C  CB  . SER   B 2 738 ? 43.591  67.069  -19.356 1.00 118.29 ? 1042 SER   B CB  1 
ATOM   7975  O  OG  . SER   B 2 738 ? 42.234  66.755  -19.637 1.00 119.88 ? 1042 SER   B OG  1 
ATOM   7976  N  N   . LEU   B 2 739 ? 46.357  66.547  -17.752 1.00 119.37 ? 1043 LEU   B N   1 
ATOM   7977  C  CA  . LEU   B 2 739 ? 47.674  66.997  -17.349 1.00 127.62 ? 1043 LEU   B CA  1 
ATOM   7978  C  C   . LEU   B 2 739 ? 48.526  67.284  -18.566 1.00 133.62 ? 1043 LEU   B C   1 
ATOM   7979  O  O   . LEU   B 2 739 ? 48.145  67.011  -19.707 1.00 130.56 ? 1043 LEU   B O   1 
ATOM   7980  C  CB  . LEU   B 2 739 ? 48.375  65.951  -16.478 1.00 123.81 ? 1043 LEU   B CB  1 
ATOM   7981  C  CG  . LEU   B 2 739 ? 47.601  65.545  -15.248 1.00 116.06 ? 1043 LEU   B CG  1 
ATOM   7982  C  CD1 . LEU   B 2 739 ? 48.417  64.513  -14.544 1.00 113.93 ? 1043 LEU   B CD1 1 
ATOM   7983  C  CD2 . LEU   B 2 739 ? 47.362  66.759  -14.376 1.00 116.40 ? 1043 LEU   B CD2 1 
ATOM   7984  N  N   . SER   B 2 740 ? 49.710  67.815  -18.291 1.00 140.28 ? 1044 SER   B N   1 
ATOM   7985  C  CA  . SER   B 2 740 ? 50.778  67.873  -19.269 1.00 141.54 ? 1044 SER   B CA  1 
ATOM   7986  C  C   . SER   B 2 740 ? 51.650  66.633  -19.117 1.00 140.18 ? 1044 SER   B C   1 
ATOM   7987  O  O   . SER   B 2 740 ? 51.682  66.000  -18.058 1.00 142.13 ? 1044 SER   B O   1 
ATOM   7988  C  CB  . SER   B 2 740 ? 51.603  69.132  -19.075 1.00 143.19 ? 1044 SER   B CB  1 
ATOM   7989  O  OG  . SER   B 2 740 ? 52.387  68.985  -17.911 1.00 148.00 ? 1044 SER   B OG  1 
ATOM   7990  N  N   . GLU   B 2 741 ? 52.368  66.293  -20.192 1.00 141.57 ? 1045 GLU   B N   1 
ATOM   7991  C  CA  . GLU   B 2 741 ? 53.049  65.004  -20.226 1.00 139.94 ? 1045 GLU   B CA  1 
ATOM   7992  C  C   . GLU   B 2 741 ? 54.094  64.902  -19.133 1.00 140.38 ? 1045 GLU   B C   1 
ATOM   7993  O  O   . GLU   B 2 741 ? 54.306  63.828  -18.563 1.00 138.76 ? 1045 GLU   B O   1 
ATOM   7994  C  CB  . GLU   B 2 741 ? 53.699  64.764  -21.579 1.00 136.76 ? 1045 GLU   B CB  1 
ATOM   7995  C  CG  . GLU   B 2 741 ? 54.199  63.346  -21.702 1.00 137.18 ? 1045 GLU   B CG  1 
ATOM   7996  C  CD  . GLU   B 2 741 ? 54.957  63.110  -22.977 1.00 139.48 ? 1045 GLU   B CD  1 
ATOM   7997  O  OE1 . GLU   B 2 741 ? 55.375  64.117  -23.598 1.00 139.52 ? 1045 GLU   B OE1 1 
ATOM   7998  O  OE2 . GLU   B 2 741 ? 55.129  61.924  -23.353 1.00 139.55 ? 1045 GLU   B OE2 1 
ATOM   7999  N  N   . SER   B 2 742 ? 54.765  66.006  -18.826 1.00 153.95 ? 1046 SER   B N   1 
ATOM   8000  C  CA  . SER   B 2 742 ? 55.736  65.974  -17.742 1.00 153.77 ? 1046 SER   B CA  1 
ATOM   8001  C  C   . SER   B 2 742 ? 55.046  65.729  -16.405 1.00 151.95 ? 1046 SER   B C   1 
ATOM   8002  O  O   . SER   B 2 742 ? 55.473  64.872  -15.620 1.00 148.12 ? 1046 SER   B O   1 
ATOM   8003  C  CB  . SER   B 2 742 ? 56.534  67.275  -17.721 1.00 155.89 ? 1046 SER   B CB  1 
ATOM   8004  O  OG  . SER   B 2 742 ? 55.669  68.387  -17.859 1.00 159.56 ? 1046 SER   B OG  1 
ATOM   8005  N  N   . TRP   B 2 743 ? 53.953  66.458  -16.145 1.00 140.91 ? 1047 TRP   B N   1 
ATOM   8006  C  CA  . TRP   B 2 743 ? 53.288  66.370  -14.848 1.00 137.66 ? 1047 TRP   B CA  1 
ATOM   8007  C  C   . TRP   B 2 743 ? 52.825  64.945  -14.565 1.00 134.97 ? 1047 TRP   B C   1 
ATOM   8008  O  O   . TRP   B 2 743 ? 52.962  64.451  -13.436 1.00 131.73 ? 1047 TRP   B O   1 
ATOM   8009  C  CB  . TRP   B 2 743 ? 52.118  67.360  -14.786 1.00 135.20 ? 1047 TRP   B CB  1 
ATOM   8010  C  CG  . TRP   B 2 743 ? 52.443  68.676  -14.064 1.00 137.79 ? 1047 TRP   B CG  1 
ATOM   8011  C  CD1 . TRP   B 2 743 ? 53.671  69.093  -13.628 1.00 135.13 ? 1047 TRP   B CD1 1 
ATOM   8012  C  CD2 . TRP   B 2 743 ? 51.518  69.718  -13.695 1.00 141.25 ? 1047 TRP   B CD2 1 
ATOM   8013  N  NE1 . TRP   B 2 743 ? 53.572  70.318  -13.019 1.00 128.71 ? 1047 TRP   B NE1 1 
ATOM   8014  C  CE2 . TRP   B 2 743 ? 52.263  70.726  -13.044 1.00 138.76 ? 1047 TRP   B CE2 1 
ATOM   8015  C  CE3 . TRP   B 2 743 ? 50.135  69.896  -13.852 1.00 140.17 ? 1047 TRP   B CE3 1 
ATOM   8016  C  CZ2 . TRP   B 2 743 ? 51.670  71.896  -12.550 1.00 144.09 ? 1047 TRP   B CZ2 1 
ATOM   8017  C  CZ3 . TRP   B 2 743 ? 49.552  71.054  -13.356 1.00 139.18 ? 1047 TRP   B CZ3 1 
ATOM   8018  C  CH2 . TRP   B 2 743 ? 50.317  72.039  -12.716 1.00 140.64 ? 1047 TRP   B CH2 1 
ATOM   8019  N  N   . TYR   B 2 744 ? 52.303  64.259  -15.591 1.00 134.68 ? 1048 TYR   B N   1 
ATOM   8020  C  CA  . TYR   B 2 744 ? 51.913  62.857  -15.458 1.00 126.19 ? 1048 TYR   B CA  1 
ATOM   8021  C  C   . TYR   B 2 744 ? 53.096  62.004  -15.008 1.00 128.27 ? 1048 TYR   B C   1 
ATOM   8022  O  O   . TYR   B 2 744 ? 53.036  61.326  -13.972 1.00 127.41 ? 1048 TYR   B O   1 
ATOM   8023  C  CB  . TYR   B 2 744 ? 51.347  62.354  -16.788 1.00 121.92 ? 1048 TYR   B CB  1 
ATOM   8024  C  CG  . TYR   B 2 744 ? 50.894  60.913  -16.797 1.00 115.04 ? 1048 TYR   B CG  1 
ATOM   8025  C  CD1 . TYR   B 2 744 ? 49.679  60.544  -16.240 1.00 112.59 ? 1048 TYR   B CD1 1 
ATOM   8026  C  CD2 . TYR   B 2 744 ? 51.662  59.928  -17.394 1.00 113.34 ? 1048 TYR   B CD2 1 
ATOM   8027  C  CE1 . TYR   B 2 744 ? 49.244  59.232  -16.261 1.00 108.52 ? 1048 TYR   B CE1 1 
ATOM   8028  C  CE2 . TYR   B 2 744 ? 51.238  58.617  -17.428 1.00 113.69 ? 1048 TYR   B CE2 1 
ATOM   8029  C  CZ  . TYR   B 2 744 ? 50.027  58.266  -16.856 1.00 109.72 ? 1048 TYR   B CZ  1 
ATOM   8030  O  OH  . TYR   B 2 744 ? 49.596  56.947  -16.878 1.00 105.34 ? 1048 TYR   B OH  1 
ATOM   8031  N  N   . ASN   B 2 745 ? 54.193  62.054  -15.778 1.00 130.33 ? 1049 ASN   B N   1 
ATOM   8032  C  CA  . ASN   B 2 745 ? 55.400  61.298  -15.445 1.00 127.74 ? 1049 ASN   B CA  1 
ATOM   8033  C  C   . ASN   B 2 745 ? 55.825  61.533  -14.003 1.00 126.41 ? 1049 ASN   B C   1 
ATOM   8034  O  O   . ASN   B 2 745 ? 56.071  60.578  -13.257 1.00 125.56 ? 1049 ASN   B O   1 
ATOM   8035  C  CB  . ASN   B 2 745 ? 56.552  61.674  -16.381 1.00 128.17 ? 1049 ASN   B CB  1 
ATOM   8036  C  CG  . ASN   B 2 745 ? 56.212  61.506  -17.837 1.00 131.46 ? 1049 ASN   B CG  1 
ATOM   8037  O  OD1 . ASN   B 2 745 ? 55.432  60.632  -18.207 1.00 131.54 ? 1049 ASN   B OD1 1 
ATOM   8038  N  ND2 . ASN   B 2 745 ? 56.829  62.327  -18.684 1.00 135.90 ? 1049 ASN   B ND2 1 
ATOM   8039  N  N   . LEU   B 2 746 ? 55.926  62.806  -13.598 1.00 127.14 ? 1050 LEU   B N   1 
ATOM   8040  C  CA  . LEU   B 2 746 ? 56.368  63.121  -12.244 1.00 126.95 ? 1050 LEU   B CA  1 
ATOM   8041  C  C   . LEU   B 2 746 ? 55.434  62.516  -11.216 1.00 128.20 ? 1050 LEU   B C   1 
ATOM   8042  O  O   . LEU   B 2 746 ? 55.885  61.852  -10.271 1.00 128.01 ? 1050 LEU   B O   1 
ATOM   8043  C  CB  . LEU   B 2 746 ? 56.433  64.619  -12.035 1.00 127.97 ? 1050 LEU   B CB  1 
ATOM   8044  C  CG  . LEU   B 2 746 ? 57.398  65.126  -10.974 1.00 134.05 ? 1050 LEU   B CG  1 
ATOM   8045  C  CD1 . LEU   B 2 746 ? 57.392  66.606  -11.213 1.00 134.28 ? 1050 LEU   B CD1 1 
ATOM   8046  C  CD2 . LEU   B 2 746 ? 57.008  64.799  -9.501  1.00 135.54 ? 1050 LEU   B CD2 1 
ATOM   8047  N  N   . LEU   B 2 747 ? 54.127  62.759  -11.372 1.00 124.87 ? 1051 LEU   B N   1 
ATOM   8048  C  CA  . LEU   B 2 747 ? 53.160  62.210  -10.428 1.00 121.09 ? 1051 LEU   B CA  1 
ATOM   8049  C  C   . LEU   B 2 747 ? 53.193  60.689  -10.421 1.00 124.41 ? 1051 LEU   B C   1 
ATOM   8050  O  O   . LEU   B 2 747 ? 52.976  60.061  -9.375  1.00 125.85 ? 1051 LEU   B O   1 
ATOM   8051  C  CB  . LEU   B 2 747 ? 51.758  62.693  -10.758 1.00 110.97 ? 1051 LEU   B CB  1 
ATOM   8052  C  CG  . LEU   B 2 747 ? 51.447  64.118  -10.369 1.00 111.41 ? 1051 LEU   B CG  1 
ATOM   8053  C  CD1 . LEU   B 2 747 ? 49.998  64.397  -10.682 1.00 113.72 ? 1051 LEU   B CD1 1 
ATOM   8054  C  CD2 . LEU   B 2 747 ? 51.704  64.263  -8.900  1.00 113.17 ? 1051 LEU   B CD2 1 
ATOM   8055  N  N   . LEU   B 2 748 ? 53.445  60.080  -11.582 1.00 124.91 ? 1052 LEU   B N   1 
ATOM   8056  C  CA  . LEU   B 2 748 ? 53.547  58.629  -11.655 1.00 124.22 ? 1052 LEU   B CA  1 
ATOM   8057  C  C   . LEU   B 2 748 ? 54.622  58.102  -10.710 1.00 130.60 ? 1052 LEU   B C   1 
ATOM   8058  O  O   . LEU   B 2 748 ? 54.388  57.155  -9.951  1.00 131.24 ? 1052 LEU   B O   1 
ATOM   8059  C  CB  . LEU   B 2 748 ? 53.824  58.211  -13.094 1.00 123.80 ? 1052 LEU   B CB  1 
ATOM   8060  C  CG  . LEU   B 2 748 ? 52.611  57.579  -13.766 1.00 119.04 ? 1052 LEU   B CG  1 
ATOM   8061  C  CD1 . LEU   B 2 748 ? 51.483  58.578  -13.868 1.00 118.20 ? 1052 LEU   B CD1 1 
ATOM   8062  C  CD2 . LEU   B 2 748 ? 52.981  57.009  -15.116 1.00 118.72 ? 1052 LEU   B CD2 1 
ATOM   8063  N  N   . ASP   B 2 749 ? 55.812  58.706  -10.744 1.00 140.75 ? 1053 ASP   B N   1 
ATOM   8064  C  CA  . ASP   B 2 749 ? 56.854  58.348  -9.785  1.00 142.13 ? 1053 ASP   B CA  1 
ATOM   8065  C  C   . ASP   B 2 749 ? 56.371  58.557  -8.358  1.00 140.87 ? 1053 ASP   B C   1 
ATOM   8066  O  O   . ASP   B 2 749 ? 56.534  57.688  -7.492  1.00 138.26 ? 1053 ASP   B O   1 
ATOM   8067  C  CB  . ASP   B 2 749 ? 58.111  59.176  -10.045 1.00 145.80 ? 1053 ASP   B CB  1 
ATOM   8068  C  CG  . ASP   B 2 749 ? 59.387  58.370  -9.858  1.00 152.66 ? 1053 ASP   B CG  1 
ATOM   8069  O  OD1 . ASP   B 2 749 ? 59.291  57.135  -9.650  1.00 153.79 ? 1053 ASP   B OD1 1 
ATOM   8070  O  OD2 . ASP   B 2 749 ? 60.483  58.973  -9.924  1.00 156.54 ? 1053 ASP   B OD2 1 
ATOM   8071  N  N   . MET   B 2 750 ? 55.765  59.714  -8.102  1.00 129.84 ? 1054 MET   B N   1 
ATOM   8072  C  CA  . MET   B 2 750 ? 55.222  60.008  -6.787  1.00 126.94 ? 1054 MET   B CA  1 
ATOM   8073  C  C   . MET   B 2 750 ? 54.215  58.960  -6.345  1.00 124.53 ? 1054 MET   B C   1 
ATOM   8074  O  O   . MET   B 2 750 ? 54.180  58.576  -5.170  1.00 123.21 ? 1054 MET   B O   1 
ATOM   8075  C  CB  . MET   B 2 750 ? 54.599  61.395  -6.814  1.00 126.26 ? 1054 MET   B CB  1 
ATOM   8076  C  CG  . MET   B 2 750 ? 55.570  62.438  -6.343  1.00 127.63 ? 1054 MET   B CG  1 
ATOM   8077  S  SD  . MET   B 2 750 ? 55.926  61.984  -4.641  1.00 136.36 ? 1054 MET   B SD  1 
ATOM   8078  C  CE  . MET   B 2 750 ? 57.645  61.505  -4.710  1.00 137.17 ? 1054 MET   B CE  1 
ATOM   8079  N  N   . GLN   B 2 751 ? 53.385  58.488  -7.276  1.00 124.32 ? 1055 GLN   B N   1 
ATOM   8080  C  CA  . GLN   B 2 751 ? 52.480  57.381  -6.987  1.00 123.87 ? 1055 GLN   B CA  1 
ATOM   8081  C  C   . GLN   B 2 751 ? 53.242  56.196  -6.401  1.00 128.97 ? 1055 GLN   B C   1 
ATOM   8082  O  O   . GLN   B 2 751 ? 53.011  55.796  -5.253  1.00 129.42 ? 1055 GLN   B O   1 
ATOM   8083  C  CB  . GLN   B 2 751 ? 51.728  56.955  -8.257  1.00 117.43 ? 1055 GLN   B CB  1 
ATOM   8084  C  CG  . GLN   B 2 751 ? 50.714  57.950  -8.798  1.00 110.33 ? 1055 GLN   B CG  1 
ATOM   8085  C  CD  . GLN   B 2 751 ? 49.393  57.293  -9.173  1.00 102.68 ? 1055 GLN   B CD  1 
ATOM   8086  O  OE1 . GLN   B 2 751 ? 48.383  57.489  -8.502  1.00 104.03 ? 1055 GLN   B OE1 1 
ATOM   8087  N  NE2 . GLN   B 2 751 ? 49.399  56.499  -10.236 1.00 102.23 ? 1055 GLN   B NE2 1 
ATOM   8088  N  N   . ASN   B 2 752 ? 54.160  55.622  -7.184  1.00 129.41 ? 1056 ASN   B N   1 
ATOM   8089  C  CA  . ASN   B 2 752 ? 54.905  54.459  -6.717  1.00 129.17 ? 1056 ASN   B CA  1 
ATOM   8090  C  C   . ASN   B 2 752 ? 55.621  54.773  -5.417  1.00 129.05 ? 1056 ASN   B C   1 
ATOM   8091  O  O   . ASN   B 2 752 ? 55.567  53.994  -4.459  1.00 130.00 ? 1056 ASN   B O   1 
ATOM   8092  C  CB  . ASN   B 2 752 ? 55.908  54.000  -7.773  1.00 127.55 ? 1056 ASN   B CB  1 
ATOM   8093  C  CG  . ASN   B 2 752 ? 55.318  53.978  -9.162  1.00 127.57 ? 1056 ASN   B CG  1 
ATOM   8094  O  OD1 . ASN   B 2 752 ? 54.121  53.757  -9.339  1.00 132.27 ? 1056 ASN   B OD1 1 
ATOM   8095  N  ND2 . ASN   B 2 752 ? 56.158  54.209  -10.162 1.00 125.45 ? 1056 ASN   B ND2 1 
ATOM   8096  N  N   . ARG   B 2 753 ? 56.310  55.919  -5.373  1.00 128.12 ? 1057 ARG   B N   1 
ATOM   8097  C  CA  . ARG   B 2 753 ? 57.023  56.296  -4.163  1.00 128.65 ? 1057 ARG   B CA  1 
ATOM   8098  C  C   . ARG   B 2 753 ? 56.070  56.287  -2.980  1.00 129.98 ? 1057 ARG   B C   1 
ATOM   8099  O  O   . ARG   B 2 753 ? 56.371  55.719  -1.924  1.00 130.78 ? 1057 ARG   B O   1 
ATOM   8100  C  CB  . ARG   B 2 753 ? 57.686  57.666  -4.345  1.00 125.57 ? 1057 ARG   B CB  1 
ATOM   8101  N  N   . LEU   B 2 754 ? 54.878  56.855  -3.168  1.00 128.59 ? 1058 LEU   B N   1 
ATOM   8102  C  CA  . LEU   B 2 754 ? 53.912  56.904  -2.081  1.00 126.42 ? 1058 LEU   B CA  1 
ATOM   8103  C  C   . LEU   B 2 754 ? 53.378  55.522  -1.726  1.00 131.52 ? 1058 LEU   B C   1 
ATOM   8104  O  O   . LEU   B 2 754 ? 53.056  55.271  -0.561  1.00 131.14 ? 1058 LEU   B O   1 
ATOM   8105  C  CB  . LEU   B 2 754 ? 52.772  57.840  -2.456  1.00 120.71 ? 1058 LEU   B CB  1 
ATOM   8106  C  CG  . LEU   B 2 754 ? 53.198  59.297  -2.431  1.00 120.45 ? 1058 LEU   B CG  1 
ATOM   8107  C  CD1 . LEU   B 2 754 ? 52.007  60.175  -2.727  1.00 119.14 ? 1058 LEU   B CD1 1 
ATOM   8108  C  CD2 . LEU   B 2 754 ? 53.789  59.624  -1.086  1.00 127.05 ? 1058 LEU   B CD2 1 
ATOM   8109  N  N   . ASN   B 2 755 ? 53.273  54.612  -2.697  1.00 148.59 ? 1059 ASN   B N   1 
ATOM   8110  C  CA  . ASN   B 2 755 ? 52.741  53.284  -2.387  1.00 150.72 ? 1059 ASN   B CA  1 
ATOM   8111  C  C   . ASN   B 2 755 ? 53.635  52.510  -1.432  1.00 149.92 ? 1059 ASN   B C   1 
ATOM   8112  O  O   . ASN   B 2 755 ? 53.165  51.551  -0.803  1.00 149.05 ? 1059 ASN   B O   1 
ATOM   8113  C  CB  . ASN   B 2 755 ? 52.531  52.469  -3.663  1.00 149.71 ? 1059 ASN   B CB  1 
ATOM   8114  C  CG  . ASN   B 2 755 ? 51.374  52.979  -4.482  1.00 148.55 ? 1059 ASN   B CG  1 
ATOM   8115  O  OD1 . ASN   B 2 755 ? 50.356  53.392  -3.930  1.00 148.05 ? 1059 ASN   B OD1 1 
ATOM   8116  N  ND2 . ASN   B 2 755 ? 51.530  52.985  -5.803  1.00 148.35 ? 1059 ASN   B ND2 1 
ATOM   8117  N  N   . LYS   B 2 756 ? 54.907  52.905  -1.319  1.00 137.54 ? 1060 LYS   B N   1 
ATOM   8118  C  CA  . LYS   B 2 756 ? 55.817  52.250  -0.386  1.00 131.86 ? 1060 LYS   B CA  1 
ATOM   8119  C  C   . LYS   B 2 756 ? 55.532  52.673  1.048   1.00 127.39 ? 1060 LYS   B C   1 
ATOM   8120  O  O   . LYS   B 2 756 ? 55.593  51.850  1.966   1.00 129.69 ? 1060 LYS   B O   1 
ATOM   8121  C  CB  . LYS   B 2 756 ? 57.266  52.563  -0.759  1.00 121.32 ? 1060 LYS   B CB  1 
ATOM   8122  N  N   . VAL   B 2 757 ? 55.217  53.946  1.261   1.00 127.68 ? 1061 VAL   B N   1 
ATOM   8123  C  CA  . VAL   B 2 757 ? 55.049  54.458  2.618   1.00 126.55 ? 1061 VAL   B CA  1 
ATOM   8124  C  C   . VAL   B 2 757 ? 53.618  54.255  3.118   1.00 125.43 ? 1061 VAL   B C   1 
ATOM   8125  O  O   . VAL   B 2 757 ? 53.408  53.768  4.233   1.00 124.53 ? 1061 VAL   B O   1 
ATOM   8126  C  CB  . VAL   B 2 757 ? 55.501  55.947  2.711   1.00 123.60 ? 1061 VAL   B CB  1 
ATOM   8127  C  CG1 . VAL   B 2 757 ? 56.958  56.110  2.289   1.00 122.87 ? 1061 VAL   B CG1 1 
ATOM   8128  C  CG2 . VAL   B 2 757 ? 54.641  56.890  1.876   1.00 122.53 ? 1061 VAL   B CG2 1 
ATOM   8129  N  N   . ILE   B 2 758 ? 52.609  54.581  2.308   1.00 123.61 ? 1062 ILE   B N   1 
ATOM   8130  C  CA  . ILE   B 2 758 ? 51.227  54.515  2.775   1.00 120.30 ? 1062 ILE   B CA  1 
ATOM   8131  C  C   . ILE   B 2 758 ? 50.785  53.059  2.809   1.00 124.00 ? 1062 ILE   B C   1 
ATOM   8132  O  O   . ILE   B 2 758 ? 50.779  52.377  1.777   1.00 126.63 ? 1062 ILE   B O   1 
ATOM   8133  C  CB  . ILE   B 2 758 ? 50.299  55.352  1.886   1.00 118.14 ? 1062 ILE   B CB  1 
ATOM   8134  C  CG1 . ILE   B 2 758 ? 50.660  56.842  1.985   1.00 114.73 ? 1062 ILE   B CG1 1 
ATOM   8135  C  CG2 . ILE   B 2 758 ? 48.846  55.079  2.253   1.00 117.23 ? 1062 ILE   B CG2 1 
ATOM   8136  C  CD1 . ILE   B 2 758 ? 51.123  57.451  0.670   1.00 109.91 ? 1062 ILE   B CD1 1 
ATOM   8137  N  N   . LYS   B 2 759 ? 50.412  52.580  3.999   1.00 124.18 ? 1063 LYS   B N   1 
ATOM   8138  C  CA  . LYS   B 2 759 ? 50.043  51.184  4.208   1.00 119.48 ? 1063 LYS   B CA  1 
ATOM   8139  C  C   . LYS   B 2 759 ? 48.564  50.972  3.888   1.00 121.55 ? 1063 LYS   B C   1 
ATOM   8140  O  O   . LYS   B 2 759 ? 47.721  51.820  4.204   1.00 122.70 ? 1063 LYS   B O   1 
ATOM   8141  C  CB  . LYS   B 2 759 ? 50.350  50.763  5.647   1.00 114.90 ? 1063 LYS   B CB  1 
ATOM   8142  N  N   . SER   B 2 760 ? 48.263  49.853  3.222   1.00 113.27 ? 1064 SER   B N   1 
ATOM   8143  C  CA  . SER   B 2 760 ? 46.910  49.511  2.809   1.00 101.31 ? 1064 SER   B CA  1 
ATOM   8144  C  C   . SER   B 2 760 ? 46.154  48.895  3.978   1.00 98.51  ? 1064 SER   B C   1 
ATOM   8145  O  O   . SER   B 2 760 ? 46.750  48.383  4.922   1.00 101.01 ? 1064 SER   B O   1 
ATOM   8146  C  CB  . SER   B 2 760 ? 46.954  48.544  1.627   1.00 97.14  ? 1064 SER   B CB  1 
ATOM   8147  O  OG  . SER   B 2 760 ? 45.677  47.993  1.330   1.00 103.30 ? 1064 SER   B OG  1 
ATOM   8148  N  N   . VAL   B 2 761 ? 44.825  48.945  3.914   1.00 98.55  ? 1065 VAL   B N   1 
ATOM   8149  C  CA  . VAL   B 2 761 ? 44.042  48.434  5.042   1.00 96.75  ? 1065 VAL   B CA  1 
ATOM   8150  C  C   . VAL   B 2 761 ? 43.895  46.912  5.006   1.00 96.31  ? 1065 VAL   B C   1 
ATOM   8151  O  O   . VAL   B 2 761 ? 43.714  46.278  6.053   1.00 100.51 ? 1065 VAL   B O   1 
ATOM   8152  C  CB  . VAL   B 2 761 ? 42.668  49.121  5.093   1.00 95.92  ? 1065 VAL   B CB  1 
ATOM   8153  C  CG1 . VAL   B 2 761 ? 41.819  48.583  6.269   1.00 91.07  ? 1065 VAL   B CG1 1 
ATOM   8154  C  CG2 . VAL   B 2 761 ? 42.862  50.624  5.172   1.00 93.57  ? 1065 VAL   B CG2 1 
ATOM   8155  N  N   . GLY   B 2 762 ? 43.958  46.293  3.841   1.00 94.66  ? 1066 GLY   B N   1 
ATOM   8156  C  CA  . GLY   B 2 762 ? 43.900  44.852  3.796   1.00 96.50  ? 1066 GLY   B CA  1 
ATOM   8157  C  C   . GLY   B 2 762 ? 45.201  44.238  3.375   1.00 95.07  ? 1066 GLY   B C   1 
ATOM   8158  O  O   . GLY   B 2 762 ? 45.234  43.038  3.079   1.00 97.88  ? 1066 GLY   B O   1 
ATOM   8159  N  N   . LYS   B 2 763 ? 46.271  45.033  3.349   1.00 95.30  ? 1067 LYS   B N   1 
ATOM   8160  C  CA  . LYS   B 2 763 ? 47.482  44.722  2.601   1.00 95.43  ? 1067 LYS   B CA  1 
ATOM   8161  C  C   . LYS   B 2 763 ? 47.139  44.534  1.127   1.00 96.95  ? 1067 LYS   B C   1 
ATOM   8162  O  O   . LYS   B 2 763 ? 47.479  43.521  0.516   1.00 99.53  ? 1067 LYS   B O   1 
ATOM   8163  C  CB  . LYS   B 2 763 ? 48.191  43.496  3.179   1.00 99.56  ? 1067 LYS   B CB  1 
ATOM   8164  N  N   . ILE   B 2 764 ? 46.452  45.532  0.564   1.00 98.46  ? 1068 ILE   B N   1 
ATOM   8165  C  CA  . ILE   B 2 764 ? 45.994  45.529  -0.825  1.00 94.60  ? 1068 ILE   B CA  1 
ATOM   8166  C  C   . ILE   B 2 764 ? 46.843  46.511  -1.625  1.00 99.07  ? 1068 ILE   B C   1 
ATOM   8167  O  O   . ILE   B 2 764 ? 46.912  47.703  -1.299  1.00 98.67  ? 1068 ILE   B O   1 
ATOM   8168  C  CB  . ILE   B 2 764 ? 44.505  45.883  -0.938  1.00 90.02  ? 1068 ILE   B CB  1 
ATOM   8169  C  CG1 . ILE   B 2 764 ? 43.689  45.078  0.065   1.00 89.44  ? 1068 ILE   B CG1 1 
ATOM   8170  C  CG2 . ILE   B 2 764 ? 44.008  45.582  -2.341  1.00 89.22  ? 1068 ILE   B CG2 1 
ATOM   8171  C  CD1 . ILE   B 2 764 ? 42.196  45.320  -0.033  1.00 87.85  ? 1068 ILE   B CD1 1 
ATOM   8172  N  N   . GLU   B 2 765 ? 47.458  46.019  -2.695  1.00 104.03 ? 1069 GLU   B N   1 
ATOM   8173  C  CA  . GLU   B 2 765 ? 48.356  46.855  -3.479  1.00 104.91 ? 1069 GLU   B CA  1 
ATOM   8174  C  C   . GLU   B 2 765 ? 47.561  47.839  -4.327  1.00 104.73 ? 1069 GLU   B C   1 
ATOM   8175  O  O   . GLU   B 2 765 ? 46.663  47.436  -5.072  1.00 104.15 ? 1069 GLU   B O   1 
ATOM   8176  C  CB  . GLU   B 2 765 ? 49.245  45.982  -4.365  1.00 105.02 ? 1069 GLU   B CB  1 
ATOM   8177  C  CG  . GLU   B 2 765 ? 49.967  46.764  -5.447  1.00 111.25 ? 1069 GLU   B CG  1 
ATOM   8178  C  CD  . GLU   B 2 765 ? 50.984  47.763  -4.900  1.00 116.67 ? 1069 GLU   B CD  1 
ATOM   8179  O  OE1 . GLU   B 2 765 ? 52.048  47.309  -4.411  1.00 126.54 ? 1069 GLU   B OE1 1 
ATOM   8180  O  OE2 . GLU   B 2 765 ? 50.716  48.995  -4.951  1.00 117.44 ? 1069 GLU   B OE2 1 
ATOM   8181  N  N   . HIS   B 2 766 ? 47.900  49.131  -4.217  1.00 100.69 ? 1070 HIS   B N   1 
ATOM   8182  C  CA  . HIS   B 2 766 ? 47.220  50.164  -5.001  1.00 102.86 ? 1070 HIS   B CA  1 
ATOM   8183  C  C   . HIS   B 2 766 ? 47.111  49.779  -6.470  1.00 104.72 ? 1070 HIS   B C   1 
ATOM   8184  O  O   . HIS   B 2 766 ? 46.068  50.001  -7.099  1.00 104.08 ? 1070 HIS   B O   1 
ATOM   8185  C  CB  . HIS   B 2 766 ? 47.946  51.508  -4.854  1.00 108.52 ? 1070 HIS   B CB  1 
ATOM   8186  C  CG  . HIS   B 2 766 ? 47.567  52.556  -5.878  1.00 109.77 ? 1070 HIS   B CG  1 
ATOM   8187  N  ND1 . HIS   B 2 766 ? 48.046  52.548  -7.175  1.00 112.31 ? 1070 HIS   B ND1 1 
ATOM   8188  C  CD2 . HIS   B 2 766 ? 46.822  53.686  -5.765  1.00 107.73 ? 1070 HIS   B CD2 1 
ATOM   8189  C  CE1 . HIS   B 2 766 ? 47.578  53.600  -7.825  1.00 109.76 ? 1070 HIS   B CE1 1 
ATOM   8190  N  NE2 . HIS   B 2 766 ? 46.838  54.311  -6.991  1.00 106.70 ? 1070 HIS   B NE2 1 
ATOM   8191  N  N   . SER   B 2 767 ? 48.166  49.190  -7.041  1.00 101.83 ? 1071 SER   B N   1 
ATOM   8192  C  CA  . SER   B 2 767 ? 48.129  48.916  -8.474  1.00 99.37  ? 1071 SER   B CA  1 
ATOM   8193  C  C   . SER   B 2 767 ? 47.078  47.865  -8.831  1.00 94.96  ? 1071 SER   B C   1 
ATOM   8194  O  O   . SER   B 2 767 ? 46.471  47.934  -9.907  1.00 92.30  ? 1071 SER   B O   1 
ATOM   8195  C  CB  . SER   B 2 767 ? 49.508  48.505  -8.961  1.00 101.87 ? 1071 SER   B CB  1 
ATOM   8196  O  OG  . SER   B 2 767 ? 49.798  47.177  -8.589  1.00 110.98 ? 1071 SER   B OG  1 
ATOM   8197  N  N   . PHE   B 2 768 ? 46.821  46.910  -7.939  1.00 95.08  ? 1072 PHE   B N   1 
ATOM   8198  C  CA  . PHE   B 2 768 ? 45.752  45.948  -8.180  1.00 91.19  ? 1072 PHE   B CA  1 
ATOM   8199  C  C   . PHE   B 2 768 ? 44.398  46.627  -8.110  1.00 87.09  ? 1072 PHE   B C   1 
ATOM   8200  O  O   . PHE   B 2 768 ? 43.543  46.419  -8.975  1.00 87.79  ? 1072 PHE   B O   1 
ATOM   8201  C  CB  . PHE   B 2 768 ? 45.831  44.807  -7.166  1.00 93.08  ? 1072 PHE   B CB  1 
ATOM   8202  C  CG  . PHE   B 2 768 ? 44.787  43.738  -7.365  1.00 86.78  ? 1072 PHE   B CG  1 
ATOM   8203  C  CD1 . PHE   B 2 768 ? 44.275  43.476  -8.613  1.00 87.30  ? 1072 PHE   B CD1 1 
ATOM   8204  C  CD2 . PHE   B 2 768 ? 44.324  43.002  -6.299  1.00 87.30  ? 1072 PHE   B CD2 1 
ATOM   8205  C  CE1 . PHE   B 2 768 ? 43.324  42.509  -8.804  1.00 88.21  ? 1072 PHE   B CE1 1 
ATOM   8206  C  CE2 . PHE   B 2 768 ? 43.379  42.034  -6.480  1.00 86.11  ? 1072 PHE   B CE2 1 
ATOM   8207  C  CZ  . PHE   B 2 768 ? 42.872  41.787  -7.738  1.00 87.38  ? 1072 PHE   B CZ  1 
ATOM   8208  N  N   . TRP   B 2 769 ? 44.183  47.432  -7.071  1.00 88.20  ? 1073 TRP   B N   1 
ATOM   8209  C  CA  . TRP   B 2 769 ? 42.939  48.181  -6.944  1.00 87.98  ? 1073 TRP   B CA  1 
ATOM   8210  C  C   . TRP   B 2 769 ? 42.583  48.892  -8.237  1.00 89.90  ? 1073 TRP   B C   1 
ATOM   8211  O  O   . TRP   B 2 769 ? 41.454  48.772  -8.735  1.00 88.50  ? 1073 TRP   B O   1 
ATOM   8212  C  CB  . TRP   B 2 769 ? 43.062  49.189  -5.798  1.00 87.75  ? 1073 TRP   B CB  1 
ATOM   8213  C  CG  . TRP   B 2 769 ? 41.899  50.158  -5.601  1.00 86.57  ? 1073 TRP   B CG  1 
ATOM   8214  C  CD1 . TRP   B 2 769 ? 42.005  51.479  -5.288  1.00 86.35  ? 1073 TRP   B CD1 1 
ATOM   8215  C  CD2 . TRP   B 2 769 ? 40.481  49.885  -5.681  1.00 85.15  ? 1073 TRP   B CD2 1 
ATOM   8216  N  NE1 . TRP   B 2 769 ? 40.763  52.047  -5.174  1.00 85.29  ? 1073 TRP   B NE1 1 
ATOM   8217  C  CE2 . TRP   B 2 769 ? 39.811  51.092  -5.410  1.00 83.79  ? 1073 TRP   B CE2 1 
ATOM   8218  C  CE3 . TRP   B 2 769 ? 39.720  48.750  -5.971  1.00 86.54  ? 1073 TRP   B CE3 1 
ATOM   8219  C  CZ2 . TRP   B 2 769 ? 38.423  51.195  -5.411  1.00 82.06  ? 1073 TRP   B CZ2 1 
ATOM   8220  C  CZ3 . TRP   B 2 769 ? 38.339  48.857  -5.964  1.00 85.48  ? 1073 TRP   B CZ3 1 
ATOM   8221  C  CH2 . TRP   B 2 769 ? 37.708  50.069  -5.682  1.00 82.01  ? 1073 TRP   B CH2 1 
ATOM   8222  N  N   . ARG   B 2 770 ? 43.559  49.612  -8.812  1.00 92.08  ? 1074 ARG   B N   1 
ATOM   8223  C  CA  . ARG   B 2 770 ? 43.318  50.531  -9.917  1.00 88.97  ? 1074 ARG   B CA  1 
ATOM   8224  C  C   . ARG   B 2 770 ? 43.309  49.858  -11.280 1.00 89.92  ? 1074 ARG   B C   1 
ATOM   8225  O  O   . ARG   B 2 770 ? 42.723  50.408  -12.217 1.00 88.46  ? 1074 ARG   B O   1 
ATOM   8226  C  CB  . ARG   B 2 770 ? 44.371  51.631  -9.915  1.00 88.12  ? 1074 ARG   B CB  1 
ATOM   8227  C  CG  . ARG   B 2 770 ? 44.216  52.617  -8.791  1.00 91.08  ? 1074 ARG   B CG  1 
ATOM   8228  C  CD  . ARG   B 2 770 ? 42.782  53.050  -8.671  1.00 86.87  ? 1074 ARG   B CD  1 
ATOM   8229  N  NE  . ARG   B 2 770 ? 42.576  54.074  -7.657  1.00 83.90  ? 1074 ARG   B NE  1 
ATOM   8230  C  CZ  . ARG   B 2 770 ? 41.383  54.477  -7.246  1.00 86.90  ? 1074 ARG   B CZ  1 
ATOM   8231  N  NH1 . ARG   B 2 770 ? 40.270  54.009  -7.789  1.00 85.67  ? 1074 ARG   B NH1 1 
ATOM   8232  N  NH2 . ARG   B 2 770 ? 41.301  55.363  -6.258  1.00 91.81  ? 1074 ARG   B NH2 1 
ATOM   8233  N  N   . SER   B 2 771 ? 43.954  48.703  -11.414 1.00 97.26  ? 1075 SER   B N   1 
ATOM   8234  C  CA  . SER   B 2 771 ? 43.993  48.004  -12.693 1.00 98.67  ? 1075 SER   B CA  1 
ATOM   8235  C  C   . SER   B 2 771 ? 42.592  47.767  -13.233 1.00 98.94  ? 1075 SER   B C   1 
ATOM   8236  O  O   . SER   B 2 771 ? 41.693  47.366  -12.500 1.00 101.86 ? 1075 SER   B O   1 
ATOM   8237  C  CB  . SER   B 2 771 ? 44.724  46.668  -12.537 1.00 101.41 ? 1075 SER   B CB  1 
ATOM   8238  O  OG  . SER   B 2 771 ? 46.101  46.888  -12.283 1.00 106.13 ? 1075 SER   B OG  1 
ATOM   8239  N  N   . PHE   B 2 772 ? 42.423  48.005  -14.526 1.00 92.19  ? 1076 PHE   B N   1 
ATOM   8240  C  CA  . PHE   B 2 772 ? 41.130  47.929  -15.210 1.00 92.57  ? 1076 PHE   B CA  1 
ATOM   8241  C  C   . PHE   B 2 772 ? 40.625  46.511  -14.996 1.00 92.03  ? 1076 PHE   B C   1 
ATOM   8242  O  O   . PHE   B 2 772 ? 41.200  45.568  -15.533 1.00 94.05  ? 1076 PHE   B O   1 
ATOM   8243  C  CB  . PHE   B 2 772 ? 41.369  48.295  -16.679 1.00 94.97  ? 1076 PHE   B CB  1 
ATOM   8244  C  CG  . PHE   B 2 772 ? 40.120  48.443  -17.471 1.00 96.59  ? 1076 PHE   B CG  1 
ATOM   8245  C  CD1 . PHE   B 2 772 ? 39.463  47.335  -17.969 1.00 95.73  ? 1076 PHE   B CD1 1 
ATOM   8246  C  CD2 . PHE   B 2 772 ? 39.602  49.699  -17.733 1.00 96.43  ? 1076 PHE   B CD2 1 
ATOM   8247  C  CE1 . PHE   B 2 772 ? 38.309  47.475  -18.699 1.00 96.89  ? 1076 PHE   B CE1 1 
ATOM   8248  C  CE2 . PHE   B 2 772 ? 38.454  49.846  -18.477 1.00 94.18  ? 1076 PHE   B CE2 1 
ATOM   8249  C  CZ  . PHE   B 2 772 ? 37.805  48.730  -18.958 1.00 96.08  ? 1076 PHE   B CZ  1 
ATOM   8250  N  N   . HIS   B 2 773 ? 39.534  46.338  -14.261 1.00 92.44  ? 1077 HIS   B N   1 
ATOM   8251  C  CA  . HIS   B 2 773 ? 39.045  45.007  -13.900 1.00 98.71  ? 1077 HIS   B CA  1 
ATOM   8252  C  C   . HIS   B 2 773 ? 37.685  44.870  -14.546 1.00 104.11 ? 1077 HIS   B C   1 
ATOM   8253  O  O   . HIS   B 2 773 ? 36.796  45.695  -14.323 1.00 102.68 ? 1077 HIS   B O   1 
ATOM   8254  C  CB  . HIS   B 2 773 ? 38.947  44.664  -12.414 1.00 101.32 ? 1077 HIS   B CB  1 
ATOM   8255  C  CG  . HIS   B 2 773 ? 38.257  43.357  -12.151 1.00 106.27 ? 1077 HIS   B CG  1 
ATOM   8256  N  ND1 . HIS   B 2 773 ? 38.607  42.187  -12.794 1.00 111.66 ? 1077 HIS   B ND1 1 
ATOM   8257  C  CD2 . HIS   B 2 773 ? 37.218  43.041  -11.339 1.00 104.34 ? 1077 HIS   B CD2 1 
ATOM   8258  C  CE1 . HIS   B 2 773 ? 37.825  41.206  -12.377 1.00 114.31 ? 1077 HIS   B CE1 1 
ATOM   8259  N  NE2 . HIS   B 2 773 ? 36.974  41.697  -11.492 1.00 110.49 ? 1077 HIS   B NE2 1 
ATOM   8260  N  N   . THR   B 2 774 ? 37.536  43.822  -15.345 1.00 113.12 ? 1078 THR   B N   1 
ATOM   8261  C  CA  . THR   B 2 774 ? 36.268  43.357  -15.881 1.00 115.33 ? 1078 THR   B CA  1 
ATOM   8262  C  C   . THR   B 2 774 ? 36.238  41.872  -15.598 1.00 125.27 ? 1078 THR   B C   1 
ATOM   8263  O  O   . THR   B 2 774 ? 37.278  41.207  -15.686 1.00 125.83 ? 1078 THR   B O   1 
ATOM   8264  C  CB  . THR   B 2 774 ? 36.146  43.620  -17.385 1.00 114.72 ? 1078 THR   B CB  1 
ATOM   8265  O  OG1 . THR   B 2 774 ? 36.070  45.033  -17.600 1.00 108.19 ? 1078 THR   B OG1 1 
ATOM   8266  C  CG2 . THR   B 2 774 ? 34.910  42.940  -17.978 1.00 120.07 ? 1078 THR   B CG2 1 
ATOM   8267  N  N   . GLU   B 2 775 ? 35.067  41.368  -15.216 1.00 140.27 ? 1079 GLU   B N   1 
ATOM   8268  C  CA  . GLU   B 2 775 ? 34.873  39.947  -14.965 1.00 142.61 ? 1079 GLU   B CA  1 
ATOM   8269  C  C   . GLU   B 2 775 ? 35.602  39.148  -16.033 1.00 142.61 ? 1079 GLU   B C   1 
ATOM   8270  O  O   . GLU   B 2 775 ? 36.329  38.195  -15.727 1.00 144.19 ? 1079 GLU   B O   1 
ATOM   8271  C  CB  . GLU   B 2 775 ? 33.385  39.598  -14.956 1.00 143.81 ? 1079 GLU   B CB  1 
ATOM   8272  C  CG  . GLU   B 2 775 ? 32.520  40.629  -14.268 1.00 145.59 ? 1079 GLU   B CG  1 
ATOM   8273  C  CD  . GLU   B 2 775 ? 32.053  41.726  -15.215 1.00 145.40 ? 1079 GLU   B CD  1 
ATOM   8274  O  OE1 . GLU   B 2 775 ? 32.519  41.744  -16.380 1.00 142.04 ? 1079 GLU   B OE1 1 
ATOM   8275  O  OE2 . GLU   B 2 775 ? 31.217  42.563  -14.795 1.00 143.77 ? 1079 GLU   B OE2 1 
ATOM   8276  N  N   . ARG   B 2 776 ? 35.447  39.583  -17.290 1.00 133.75 ? 1080 ARG   B N   1 
ATOM   8277  C  CA  . ARG   B 2 776 ? 36.110  38.933  -18.409 1.00 130.62 ? 1080 ARG   B CA  1 
ATOM   8278  C  C   . ARG   B 2 776 ? 37.630  38.946  -18.238 1.00 133.00 ? 1080 ARG   B C   1 
ATOM   8279  O  O   . ARG   B 2 776 ? 38.256  37.890  -18.104 1.00 132.94 ? 1080 ARG   B O   1 
ATOM   8280  C  CB  . ARG   B 2 776 ? 35.697  39.610  -19.716 1.00 129.18 ? 1080 ARG   B CB  1 
ATOM   8281  N  N   . LYS   B 2 777 ? 38.238  40.136  -18.230 1.00 138.70 ? 1081 LYS   B N   1 
ATOM   8282  C  CA  . LYS   B 2 777 ? 39.690  40.272  -18.179 1.00 135.33 ? 1081 LYS   B CA  1 
ATOM   8283  C  C   . LYS   B 2 777 ? 40.056  41.512  -17.373 1.00 130.00 ? 1081 LYS   B C   1 
ATOM   8284  O  O   . LYS   B 2 777 ? 39.333  42.508  -17.407 1.00 132.87 ? 1081 LYS   B O   1 
ATOM   8285  C  CB  . LYS   B 2 777 ? 40.288  40.363  -19.594 1.00 132.97 ? 1081 LYS   B CB  1 
ATOM   8286  N  N   . THR   B 2 778 ? 41.195  41.445  -16.662 1.00 114.95 ? 1082 THR   B N   1 
ATOM   8287  C  CA  . THR   B 2 778 ? 41.758  42.562  -15.893 1.00 110.45 ? 1082 THR   B CA  1 
ATOM   8288  C  C   . THR   B 2 778 ? 43.138  42.942  -16.446 1.00 105.03 ? 1082 THR   B C   1 
ATOM   8289  O  O   . THR   B 2 778 ? 44.006  42.076  -16.613 1.00 103.58 ? 1082 THR   B O   1 
ATOM   8290  C  CB  . THR   B 2 778 ? 41.804  42.206  -14.378 1.00 109.52 ? 1082 THR   B CB  1 
ATOM   8291  O  OG1 . THR   B 2 778 ? 42.390  43.272  -13.604 1.00 104.78 ? 1082 THR   B OG1 1 
ATOM   8292  C  CG2 . THR   B 2 778 ? 42.557  40.910  -14.119 1.00 109.24 ? 1082 THR   B CG2 1 
ATOM   8293  N  N   . GLU   B 2 779 ? 43.319  44.242  -16.780 1.00 102.60 ? 1083 GLU   B N   1 
ATOM   8294  C  CA  . GLU   B 2 779 ? 44.500  44.914  -17.339 1.00 99.31  ? 1083 GLU   B CA  1 
ATOM   8295  C  C   . GLU   B 2 779 ? 44.961  46.087  -16.469 1.00 99.79  ? 1083 GLU   B C   1 
ATOM   8296  O  O   . GLU   B 2 779 ? 44.149  46.665  -15.735 1.00 100.79 ? 1083 GLU   B O   1 
ATOM   8297  C  CB  . GLU   B 2 779 ? 44.213  45.435  -18.762 1.00 98.09  ? 1083 GLU   B CB  1 
ATOM   8298  N  N   . PRO   B 2 780 ? 46.247  46.473  -16.540 1.00 96.50  ? 1084 PRO   B N   1 
ATOM   8299  C  CA  . PRO   B 2 780 ? 46.770  47.532  -15.655 1.00 92.94  ? 1084 PRO   B CA  1 
ATOM   8300  C  C   . PRO   B 2 780 ? 46.450  48.938  -16.156 1.00 94.52  ? 1084 PRO   B C   1 
ATOM   8301  O  O   . PRO   B 2 780 ? 46.288  49.181  -17.351 1.00 90.11  ? 1084 PRO   B O   1 
ATOM   8302  C  CB  . PRO   B 2 780 ? 48.284  47.307  -15.657 1.00 92.00  ? 1084 PRO   B CB  1 
ATOM   8303  C  CG  . PRO   B 2 780 ? 48.491  45.971  -16.287 1.00 97.27  ? 1084 PRO   B CG  1 
ATOM   8304  C  CD  . PRO   B 2 780 ? 47.338  45.744  -17.204 1.00 98.31  ? 1084 PRO   B CD  1 
ATOM   8305  N  N   . ALA   B 2 781 ? 46.394  49.869  -15.204 1.00 96.34  ? 1085 ALA   B N   1 
ATOM   8306  C  CA  . ALA   B 2 781 ? 45.847  51.193  -15.466 1.00 88.17  ? 1085 ALA   B CA  1 
ATOM   8307  C  C   . ALA   B 2 781 ? 46.871  52.060  -16.184 1.00 91.18  ? 1085 ALA   B C   1 
ATOM   8308  O  O   . ALA   B 2 781 ? 48.063  51.756  -16.210 1.00 94.85  ? 1085 ALA   B O   1 
ATOM   8309  C  CB  . ALA   B 2 781 ? 45.399  51.849  -14.162 1.00 80.74  ? 1085 ALA   B CB  1 
ATOM   8310  N  N   . THR   B 2 782 ? 46.387  53.149  -16.781 1.00 92.89  ? 1086 THR   B N   1 
ATOM   8311  C  CA  . THR   B 2 782 ? 47.212  54.015  -17.614 1.00 90.31  ? 1086 THR   B CA  1 
ATOM   8312  C  C   . THR   B 2 782 ? 46.492  55.328  -17.853 1.00 92.17  ? 1086 THR   B C   1 
ATOM   8313  O  O   . THR   B 2 782 ? 45.265  55.379  -17.884 1.00 95.42  ? 1086 THR   B O   1 
ATOM   8314  C  CB  . THR   B 2 782 ? 47.516  53.366  -18.961 1.00 90.45  ? 1086 THR   B CB  1 
ATOM   8315  O  OG1 . THR   B 2 782 ? 48.116  54.343  -19.808 1.00 96.17  ? 1086 THR   B OG1 1 
ATOM   8316  C  CG2 . THR   B 2 782 ? 46.228  52.868  -19.621 1.00 89.12  ? 1086 THR   B CG2 1 
ATOM   8317  N  N   . GLY   B 2 783 ? 47.267  56.384  -18.055 1.00 94.74  ? 1087 GLY   B N   1 
ATOM   8318  C  CA  . GLY   B 2 783 ? 46.675  57.653  -18.421 1.00 98.48  ? 1087 GLY   B CA  1 
ATOM   8319  C  C   . GLY   B 2 783 ? 45.979  58.342  -17.275 1.00 97.81  ? 1087 GLY   B C   1 
ATOM   8320  O  O   . GLY   B 2 783 ? 45.513  59.474  -17.429 1.00 101.55 ? 1087 GLY   B O   1 
ATOM   8321  N  N   . PHE   B 2 784 ? 45.909  57.678  -16.123 1.00 94.67  ? 1088 PHE   B N   1 
ATOM   8322  C  CA  . PHE   B 2 784 ? 45.224  58.198  -14.955 1.00 95.01  ? 1088 PHE   B CA  1 
ATOM   8323  C  C   . PHE   B 2 784 ? 46.166  58.209  -13.768 1.00 100.30 ? 1088 PHE   B C   1 
ATOM   8324  O  O   . PHE   B 2 784 ? 46.899  57.239  -13.530 1.00 103.75 ? 1088 PHE   B O   1 
ATOM   8325  C  CB  . PHE   B 2 784 ? 43.980  57.375  -14.626 1.00 89.54  ? 1088 PHE   B CB  1 
ATOM   8326  C  CG  . PHE   B 2 784 ? 42.808  57.704  -15.490 1.00 91.00  ? 1088 PHE   B CG  1 
ATOM   8327  C  CD1 . PHE   B 2 784 ? 41.926  58.718  -15.132 1.00 90.94  ? 1088 PHE   B CD1 1 
ATOM   8328  C  CD2 . PHE   B 2 784 ? 42.600  57.026  -16.686 1.00 92.94  ? 1088 PHE   B CD2 1 
ATOM   8329  C  CE1 . PHE   B 2 784 ? 40.851  59.039  -15.941 1.00 91.01  ? 1088 PHE   B CE1 1 
ATOM   8330  C  CE2 . PHE   B 2 784 ? 41.521  57.335  -17.506 1.00 90.79  ? 1088 PHE   B CE2 1 
ATOM   8331  C  CZ  . PHE   B 2 784 ? 40.644  58.339  -17.130 1.00 92.63  ? 1088 PHE   B CZ  1 
ATOM   8332  N  N   . ILE   B 2 785 ? 46.117  59.313  -13.022 1.00 100.37 ? 1089 ILE   B N   1 
ATOM   8333  C  CA  . ILE   B 2 785 ? 46.836  59.462  -11.763 1.00 102.36 ? 1089 ILE   B CA  1 
ATOM   8334  C  C   . ILE   B 2 785 ? 45.811  59.585  -10.653 1.00 100.15 ? 1089 ILE   B C   1 
ATOM   8335  O  O   . ILE   B 2 785 ? 44.902  60.421  -10.732 1.00 98.87  ? 1089 ILE   B O   1 
ATOM   8336  C  CB  . ILE   B 2 785 ? 47.767  60.674  -11.775 1.00 100.35 ? 1089 ILE   B CB  1 
ATOM   8337  C  CG1 . ILE   B 2 785 ? 48.703  60.514  -12.947 1.00 104.19 ? 1089 ILE   B CG1 1 
ATOM   8338  C  CG2 . ILE   B 2 785 ? 48.536  60.762  -10.480 1.00 98.85  ? 1089 ILE   B CG2 1 
ATOM   8339  C  CD1 . ILE   B 2 785 ? 49.626  61.606  -13.074 1.00 112.08 ? 1089 ILE   B CD1 1 
ATOM   8340  N  N   . ASP   B 2 786 ? 45.962  58.754  -9.624  1.00 98.57  ? 1090 ASP   B N   1 
ATOM   8341  C  CA  . ASP   B 2 786 ? 45.056  58.761  -8.486  1.00 97.22  ? 1090 ASP   B CA  1 
ATOM   8342  C  C   . ASP   B 2 786 ? 45.416  59.938  -7.599  1.00 98.93  ? 1090 ASP   B C   1 
ATOM   8343  O  O   . ASP   B 2 786 ? 46.353  59.866  -6.807  1.00 102.84 ? 1090 ASP   B O   1 
ATOM   8344  C  CB  . ASP   B 2 786 ? 45.152  57.449  -7.715  1.00 95.91  ? 1090 ASP   B CB  1 
ATOM   8345  C  CG  . ASP   B 2 786 ? 44.106  57.338  -6.627  1.00 96.21  ? 1090 ASP   B CG  1 
ATOM   8346  O  OD1 . ASP   B 2 786 ? 43.318  58.293  -6.414  1.00 93.22  ? 1090 ASP   B OD1 1 
ATOM   8347  O  OD2 . ASP   B 2 786 ? 44.069  56.269  -5.992  1.00 96.68  ? 1090 ASP   B OD2 1 
ATOM   8348  N  N   . GLY   B 2 787 ? 44.679  61.034  -7.737  1.00 98.00  ? 1091 GLY   B N   1 
ATOM   8349  C  CA  . GLY   B 2 787 ? 44.953  62.191  -6.910  1.00 100.11 ? 1091 GLY   B CA  1 
ATOM   8350  C  C   . GLY   B 2 787 ? 44.799  61.893  -5.434  1.00 100.95 ? 1091 GLY   B C   1 
ATOM   8351  O  O   . GLY   B 2 787 ? 45.561  62.397  -4.609  1.00 103.96 ? 1091 GLY   B O   1 
ATOM   8352  N  N   . ASP   B 2 788 ? 43.825  61.052  -5.083  1.00 103.61 ? 1092 ASP   B N   1 
ATOM   8353  C  CA  . ASP   B 2 788 ? 43.584  60.762  -3.674  1.00 107.75 ? 1092 ASP   B CA  1 
ATOM   8354  C  C   . ASP   B 2 788 ? 44.836  60.213  -3.002  1.00 107.94 ? 1092 ASP   B C   1 
ATOM   8355  O  O   . ASP   B 2 788 ? 45.107  60.517  -1.835  1.00 109.07 ? 1092 ASP   B O   1 
ATOM   8356  C  CB  . ASP   B 2 788 ? 42.412  59.792  -3.541  1.00 107.04 ? 1092 ASP   B CB  1 
ATOM   8357  C  CG  . ASP   B 2 788 ? 41.136  60.354  -4.130  1.00 105.42 ? 1092 ASP   B CG  1 
ATOM   8358  O  OD1 . ASP   B 2 788 ? 40.725  61.455  -3.692  1.00 105.68 ? 1092 ASP   B OD1 1 
ATOM   8359  O  OD2 . ASP   B 2 788 ? 40.569  59.722  -5.053  1.00 100.15 ? 1092 ASP   B OD2 1 
ATOM   8360  N  N   . LEU   B 2 789 ? 45.619  59.419  -3.733  1.00 107.75 ? 1093 LEU   B N   1 
ATOM   8361  C  CA  . LEU   B 2 789 ? 46.927  58.984  -3.258  1.00 102.80 ? 1093 LEU   B CA  1 
ATOM   8362  C  C   . LEU   B 2 789 ? 47.915  60.139  -3.266  1.00 104.22 ? 1093 LEU   B C   1 
ATOM   8363  O  O   . LEU   B 2 789 ? 48.528  60.465  -2.244  1.00 107.59 ? 1093 LEU   B O   1 
ATOM   8364  C  CB  . LEU   B 2 789 ? 47.424  57.854  -4.144  1.00 101.70 ? 1093 LEU   B CB  1 
ATOM   8365  C  CG  . LEU   B 2 789 ? 48.858  57.421  -3.937  1.00 107.62 ? 1093 LEU   B CG  1 
ATOM   8366  C  CD1 . LEU   B 2 789 ? 48.948  56.662  -2.628  1.00 115.69 ? 1093 LEU   B CD1 1 
ATOM   8367  C  CD2 . LEU   B 2 789 ? 49.317  56.553  -5.102  1.00 114.85 ? 1093 LEU   B CD2 1 
ATOM   8368  N  N   . ILE   B 2 790 ? 48.065  60.784  -4.421  1.00 106.30 ? 1094 ILE   B N   1 
ATOM   8369  C  CA  . ILE   B 2 790 ? 48.911  61.966  -4.548  1.00 105.28 ? 1094 ILE   B CA  1 
ATOM   8370  C  C   . ILE   B 2 790 ? 48.610  62.993  -3.458  1.00 106.89 ? 1094 ILE   B C   1 
ATOM   8371  O  O   . ILE   B 2 790 ? 49.517  63.675  -2.968  1.00 110.54 ? 1094 ILE   B O   1 
ATOM   8372  C  CB  . ILE   B 2 790 ? 48.734  62.544  -5.971  1.00 102.50 ? 1094 ILE   B CB  1 
ATOM   8373  C  CG1 . ILE   B 2 790 ? 49.379  61.616  -7.004  1.00 101.94 ? 1094 ILE   B CG1 1 
ATOM   8374  C  CG2 . ILE   B 2 790 ? 49.278  63.945  -6.073  1.00 104.71 ? 1094 ILE   B CG2 1 
ATOM   8375  C  CD1 . ILE   B 2 790 ? 50.849  61.378  -6.772  1.00 106.75 ? 1094 ILE   B CD1 1 
ATOM   8376  N  N   . GLU   B 2 791 ? 47.354  63.101  -3.027  1.00 103.33 ? 1095 GLU   B N   1 
ATOM   8377  C  CA  . GLU   B 2 791 ? 47.021  64.122  -2.044  1.00 104.07 ? 1095 GLU   B CA  1 
ATOM   8378  C  C   . GLU   B 2 791 ? 47.391  63.721  -0.625  1.00 108.04 ? 1095 GLU   B C   1 
ATOM   8379  O  O   . GLU   B 2 791 ? 47.540  64.601  0.225   1.00 111.48 ? 1095 GLU   B O   1 
ATOM   8380  C  CB  . GLU   B 2 791 ? 45.528  64.476  -2.103  1.00 107.03 ? 1095 GLU   B CB  1 
ATOM   8381  C  CG  . GLU   B 2 791 ? 45.105  65.224  -3.373  1.00 107.72 ? 1095 GLU   B CG  1 
ATOM   8382  C  CD  . GLU   B 2 791 ? 43.770  65.944  -3.245  1.00 112.50 ? 1095 GLU   B CD  1 
ATOM   8383  O  OE1 . GLU   B 2 791 ? 42.932  65.556  -2.396  1.00 115.09 ? 1095 GLU   B OE1 1 
ATOM   8384  O  OE2 . GLU   B 2 791 ? 43.565  66.911  -4.007  1.00 113.81 ? 1095 GLU   B OE2 1 
ATOM   8385  N  N   . SER   B 2 792 ? 47.548  62.425  -0.351  1.00 109.91 ? 1096 SER   B N   1 
ATOM   8386  C  CA  . SER   B 2 792 ? 47.849  61.977  1.003   1.00 110.55 ? 1096 SER   B CA  1 
ATOM   8387  C  C   . SER   B 2 792 ? 49.277  62.274  1.416   1.00 117.20 ? 1096 SER   B C   1 
ATOM   8388  O  O   . SER   B 2 792 ? 49.606  62.101  2.590   1.00 121.54 ? 1096 SER   B O   1 
ATOM   8389  C  CB  . SER   B 2 792 ? 47.610  60.482  1.135   1.00 111.35 ? 1096 SER   B CB  1 
ATOM   8390  O  OG  . SER   B 2 792 ? 48.737  59.758  0.667   1.00 115.52 ? 1096 SER   B OG  1 
ATOM   8391  N  N   . PHE   B 2 793 ? 50.138  62.666  0.477   1.00 127.99 ? 1097 PHE   B N   1 
ATOM   8392  C  CA  . PHE   B 2 793 ? 51.472  63.152  0.822   1.00 130.21 ? 1097 PHE   B CA  1 
ATOM   8393  C  C   . PHE   B 2 793 ? 51.415  64.342  1.783   1.00 132.50 ? 1097 PHE   B C   1 
ATOM   8394  O  O   . PHE   B 2 793 ? 52.346  64.562  2.569   1.00 136.03 ? 1097 PHE   B O   1 
ATOM   8395  C  CB  . PHE   B 2 793 ? 52.198  63.514  -0.473  1.00 131.24 ? 1097 PHE   B CB  1 
ATOM   8396  C  CG  . PHE   B 2 793 ? 53.548  64.129  -0.285  1.00 135.46 ? 1097 PHE   B CG  1 
ATOM   8397  C  CD1 . PHE   B 2 793 ? 53.687  65.501  -0.088  1.00 137.88 ? 1097 PHE   B CD1 1 
ATOM   8398  C  CD2 . PHE   B 2 793 ? 54.689  63.349  -0.375  1.00 137.29 ? 1097 PHE   B CD2 1 
ATOM   8399  C  CE1 . PHE   B 2 793 ? 54.938  66.075  0.055   1.00 140.01 ? 1097 PHE   B CE1 1 
ATOM   8400  C  CE2 . PHE   B 2 793 ? 55.935  63.912  -0.233  1.00 141.25 ? 1097 PHE   B CE2 1 
ATOM   8401  C  CZ  . PHE   B 2 793 ? 56.063  65.278  -0.028  1.00 142.30 ? 1097 PHE   B CZ  1 
ATOM   8402  N  N   . LEU   B 2 794 ? 50.341  65.130  1.725   1.00 123.45 ? 1098 LEU   B N   1 
ATOM   8403  C  CA  . LEU   B 2 794 ? 50.171  66.214  2.678   1.00 120.60 ? 1098 LEU   B CA  1 
ATOM   8404  C  C   . LEU   B 2 794 ? 49.866  65.700  4.073   1.00 120.43 ? 1098 LEU   B C   1 
ATOM   8405  O  O   . LEU   B 2 794 ? 50.076  66.430  5.043   1.00 125.81 ? 1098 LEU   B O   1 
ATOM   8406  C  CB  . LEU   B 2 794 ? 49.061  67.152  2.211   1.00 116.37 ? 1098 LEU   B CB  1 
ATOM   8407  C  CG  . LEU   B 2 794 ? 49.232  67.657  0.783   1.00 115.12 ? 1098 LEU   B CG  1 
ATOM   8408  C  CD1 . LEU   B 2 794 ? 48.173  68.668  0.476   1.00 116.95 ? 1098 LEU   B CD1 1 
ATOM   8409  C  CD2 . LEU   B 2 794 ? 50.618  68.248  0.600   1.00 121.21 ? 1098 LEU   B CD2 1 
ATOM   8410  N  N   . ASP   B 2 795 ? 49.387  64.465  4.199   1.00 119.48 ? 1099 ASP   B N   1 
ATOM   8411  C  CA  . ASP   B 2 795 ? 48.966  63.917  5.479   1.00 121.83 ? 1099 ASP   B CA  1 
ATOM   8412  C  C   . ASP   B 2 795 ? 49.986  62.960  6.095   1.00 126.77 ? 1099 ASP   B C   1 
ATOM   8413  O  O   . ASP   B 2 795 ? 49.738  62.457  7.193   1.00 128.17 ? 1099 ASP   B O   1 
ATOM   8414  C  CB  . ASP   B 2 795 ? 47.607  63.201  5.334   1.00 118.66 ? 1099 ASP   B CB  1 
ATOM   8415  C  CG  . ASP   B 2 795 ? 46.498  64.115  4.777   1.00 119.89 ? 1099 ASP   B CG  1 
ATOM   8416  O  OD1 . ASP   B 2 795 ? 46.303  64.144  3.539   1.00 117.86 ? 1099 ASP   B OD1 1 
ATOM   8417  O  OD2 . ASP   B 2 795 ? 45.805  64.790  5.575   1.00 122.15 ? 1099 ASP   B OD2 1 
ATOM   8418  N  N   . ILE   B 2 796 ? 51.126  62.696  5.436   1.00 134.75 ? 1100 ILE   B N   1 
ATOM   8419  C  CA  . ILE   B 2 796 ? 52.115  61.771  5.997   1.00 141.10 ? 1100 ILE   B CA  1 
ATOM   8420  C  C   . ILE   B 2 796 ? 53.105  62.560  6.836   1.00 152.22 ? 1100 ILE   B C   1 
ATOM   8421  O  O   . ILE   B 2 796 ? 53.088  63.796  6.840   1.00 147.99 ? 1100 ILE   B O   1 
ATOM   8422  C  CB  . ILE   B 2 796 ? 52.853  60.939  4.922   1.00 139.25 ? 1100 ILE   B CB  1 
ATOM   8423  C  CG1 . ILE   B 2 796 ? 54.053  61.683  4.337   1.00 148.48 ? 1100 ILE   B CG1 1 
ATOM   8424  C  CG2 . ILE   B 2 796 ? 51.919  60.537  3.794   1.00 132.85 ? 1100 ILE   B CG2 1 
ATOM   8425  C  CD1 . ILE   B 2 796 ? 54.727  60.920  3.197   1.00 144.63 ? 1100 ILE   B CD1 1 
ATOM   8426  N  N   . SER   B 2 797 ? 53.966  61.851  7.560   1.00 175.34 ? 1101 SER   B N   1 
ATOM   8427  C  CA  . SER   B 2 797 ? 54.896  62.507  8.467   1.00 180.05 ? 1101 SER   B CA  1 
ATOM   8428  C  C   . SER   B 2 797 ? 55.956  63.279  7.691   1.00 178.22 ? 1101 SER   B C   1 
ATOM   8429  O  O   . SER   B 2 797 ? 56.282  62.947  6.547   1.00 179.03 ? 1101 SER   B O   1 
ATOM   8430  C  CB  . SER   B 2 797 ? 55.571  61.480  9.370   1.00 181.85 ? 1101 SER   B CB  1 
ATOM   8431  O  OG  . SER   B 2 797 ? 56.427  60.659  8.600   1.00 181.01 ? 1101 SER   B OG  1 
ATOM   8432  N  N   . ARG   B 2 798 ? 56.504  64.314  8.331   1.00 165.06 ? 1102 ARG   B N   1 
ATOM   8433  C  CA  . ARG   B 2 798 ? 57.629  65.034  7.740   1.00 161.63 ? 1102 ARG   B CA  1 
ATOM   8434  C  C   . ARG   B 2 798 ? 58.869  64.165  7.527   1.00 165.40 ? 1102 ARG   B C   1 
ATOM   8435  O  O   . ARG   B 2 798 ? 59.604  64.425  6.558   1.00 164.72 ? 1102 ARG   B O   1 
ATOM   8436  C  CB  . ARG   B 2 798 ? 57.961  66.259  8.600   1.00 158.29 ? 1102 ARG   B CB  1 
ATOM   8437  C  CG  . ARG   B 2 798 ? 58.954  67.218  7.962   1.00 153.58 ? 1102 ARG   B CG  1 
ATOM   8438  C  CD  . ARG   B 2 798 ? 58.672  67.376  6.477   1.00 152.41 ? 1102 ARG   B CD  1 
ATOM   8439  N  NE  . ARG   B 2 798 ? 59.221  68.604  5.919   1.00 151.35 ? 1102 ARG   B NE  1 
ATOM   8440  C  CZ  . ARG   B 2 798 ? 58.542  69.739  5.816   1.00 149.53 ? 1102 ARG   B CZ  1 
ATOM   8441  N  NH1 . ARG   B 2 798 ? 57.309  69.852  6.281   1.00 146.02 ? 1102 ARG   B NH1 1 
ATOM   8442  N  NH2 . ARG   B 2 798 ? 59.110  70.783  5.224   1.00 151.78 ? 1102 ARG   B NH2 1 
ATOM   8443  N  N   . PRO   B 2 799 ? 59.175  63.167  8.369   1.00 171.77 ? 1103 PRO   B N   1 
ATOM   8444  C  CA  . PRO   B 2 799 ? 60.234  62.203  8.020   1.00 172.32 ? 1103 PRO   B CA  1 
ATOM   8445  C  C   . PRO   B 2 799 ? 59.966  61.411  6.749   1.00 170.79 ? 1103 PRO   B C   1 
ATOM   8446  O  O   . PRO   B 2 799 ? 60.797  61.389  5.833   1.00 169.63 ? 1103 PRO   B O   1 
ATOM   8447  C  CB  . PRO   B 2 799 ? 60.261  61.267  9.232   1.00 172.66 ? 1103 PRO   B CB  1 
ATOM   8448  C  CG  . PRO   B 2 799 ? 59.789  62.106  10.361  1.00 170.75 ? 1103 PRO   B CG  1 
ATOM   8449  C  CD  . PRO   B 2 799 ? 58.803  63.080  9.794   1.00 168.15 ? 1103 PRO   B CD  1 
ATOM   8450  N  N   . LYS   B 2 800 ? 58.814  60.729  6.707   1.00 169.07 ? 1104 LYS   B N   1 
ATOM   8451  C  CA  . LYS   B 2 800 ? 58.463  59.917  5.546   1.00 160.19 ? 1104 LYS   B CA  1 
ATOM   8452  C  C   . LYS   B 2 800 ? 58.291  60.771  4.299   1.00 156.36 ? 1104 LYS   B C   1 
ATOM   8453  O  O   . LYS   B 2 800 ? 58.551  60.305  3.185   1.00 151.39 ? 1104 LYS   B O   1 
ATOM   8454  C  CB  . LYS   B 2 800 ? 57.188  59.134  5.833   1.00 158.42 ? 1104 LYS   B CB  1 
ATOM   8455  C  CG  . LYS   B 2 800 ? 57.304  58.142  6.991   1.00 165.83 ? 1104 LYS   B CG  1 
ATOM   8456  C  CD  . LYS   B 2 800 ? 55.928  57.589  7.349   1.00 169.70 ? 1104 LYS   B CD  1 
ATOM   8457  C  CE  . LYS   B 2 800 ? 56.013  56.399  8.286   1.00 165.25 ? 1104 LYS   B CE  1 
ATOM   8458  N  NZ  . LYS   B 2 800 ? 54.641  55.839  8.480   1.00 162.12 ? 1104 LYS   B NZ  1 
ATOM   8459  N  N   . MET   B 2 801 ? 57.841  62.017  4.477   1.00 160.74 ? 1105 MET   B N   1 
ATOM   8460  C  CA  . MET   B 2 801 ? 57.784  62.988  3.390   1.00 155.75 ? 1105 MET   B CA  1 
ATOM   8461  C  C   . MET   B 2 801 ? 59.123  63.108  2.682   1.00 158.58 ? 1105 MET   B C   1 
ATOM   8462  O  O   . MET   B 2 801 ? 59.179  63.364  1.475   1.00 154.70 ? 1105 MET   B O   1 
ATOM   8463  C  CB  . MET   B 2 801 ? 57.361  64.342  3.952   1.00 154.94 ? 1105 MET   B CB  1 
ATOM   8464  C  CG  . MET   B 2 801 ? 56.394  65.110  3.105   1.00 146.58 ? 1105 MET   B CG  1 
ATOM   8465  S  SD  . MET   B 2 801 ? 55.713  66.570  3.898   1.00 144.61 ? 1105 MET   B SD  1 
ATOM   8466  C  CE  . MET   B 2 801 ? 54.801  65.827  5.255   1.00 150.18 ? 1105 MET   B CE  1 
ATOM   8467  N  N   . GLN   B 2 802 ? 60.217  62.928  3.425   1.00 167.89 ? 1106 GLN   B N   1 
ATOM   8468  C  CA  . GLN   B 2 802 ? 61.549  62.943  2.840   1.00 168.46 ? 1106 GLN   B CA  1 
ATOM   8469  C  C   . GLN   B 2 802 ? 61.889  61.611  2.178   1.00 167.31 ? 1106 GLN   B C   1 
ATOM   8470  O  O   . GLN   B 2 802 ? 62.626  61.587  1.185   1.00 168.51 ? 1106 GLN   B O   1 
ATOM   8471  C  CB  . GLN   B 2 802 ? 62.573  63.295  3.921   1.00 169.18 ? 1106 GLN   B CB  1 
ATOM   8472  C  CG  . GLN   B 2 802 ? 62.280  64.615  4.653   1.00 167.98 ? 1106 GLN   B CG  1 
ATOM   8473  C  CD  . GLN   B 2 802 ? 62.921  64.679  6.040   1.00 170.79 ? 1106 GLN   B CD  1 
ATOM   8474  O  OE1 . GLN   B 2 802 ? 63.712  63.802  6.418   1.00 168.46 ? 1106 GLN   B OE1 1 
ATOM   8475  N  NE2 . GLN   B 2 802 ? 62.577  65.719  6.806   1.00 167.16 ? 1106 GLN   B NE2 1 
ATOM   8476  N  N   . GLU   B 2 803 ? 61.342  60.503  2.690   1.00 157.51 ? 1107 GLU   B N   1 
ATOM   8477  C  CA  . GLU   B 2 803 ? 61.642  59.195  2.114   1.00 153.35 ? 1107 GLU   B CA  1 
ATOM   8478  C  C   . GLU   B 2 803 ? 61.120  59.065  0.685   1.00 152.76 ? 1107 GLU   B C   1 
ATOM   8479  O  O   . GLU   B 2 803 ? 61.677  58.298  -0.110  1.00 152.13 ? 1107 GLU   B O   1 
ATOM   8480  C  CB  . GLU   B 2 803 ? 61.069  58.085  2.997   1.00 143.16 ? 1107 GLU   B CB  1 
ATOM   8481  N  N   . VAL   B 2 804 ? 60.076  59.812  0.329   1.00 150.65 ? 1108 VAL   B N   1 
ATOM   8482  C  CA  . VAL   B 2 804 ? 59.464  59.665  -0.987  1.00 143.29 ? 1108 VAL   B CA  1 
ATOM   8483  C  C   . VAL   B 2 804 ? 60.054  60.632  -1.990  1.00 143.76 ? 1108 VAL   B C   1 
ATOM   8484  O  O   . VAL   B 2 804 ? 60.291  60.266  -3.142  1.00 145.86 ? 1108 VAL   B O   1 
ATOM   8485  C  CB  . VAL   B 2 804 ? 57.947  59.850  -0.875  1.00 139.78 ? 1108 VAL   B CB  1 
ATOM   8486  C  CG1 . VAL   B 2 804 ? 57.332  58.597  -0.326  1.00 138.48 ? 1108 VAL   B CG1 1 
ATOM   8487  C  CG2 . VAL   B 2 804 ? 57.646  61.014  0.034   1.00 142.69 ? 1108 VAL   B CG2 1 
ATOM   8488  N  N   . VAL   B 2 805 ? 60.281  61.880  -1.582  1.00 144.58 ? 1109 VAL   B N   1 
ATOM   8489  C  CA  . VAL   B 2 805 ? 60.887  62.850  -2.479  1.00 148.33 ? 1109 VAL   B CA  1 
ATOM   8490  C  C   . VAL   B 2 805 ? 62.345  62.539  -2.759  1.00 153.29 ? 1109 VAL   B C   1 
ATOM   8491  O  O   . VAL   B 2 805 ? 62.947  63.161  -3.648  1.00 154.92 ? 1109 VAL   B O   1 
ATOM   8492  C  CB  . VAL   B 2 805 ? 60.752  64.268  -1.895  1.00 151.97 ? 1109 VAL   B CB  1 
ATOM   8493  C  CG1 . VAL   B 2 805 ? 59.331  64.514  -1.459  1.00 147.54 ? 1109 VAL   B CG1 1 
ATOM   8494  C  CG2 . VAL   B 2 805 ? 61.703  64.458  -0.720  1.00 156.71 ? 1109 VAL   B CG2 1 
ATOM   8495  N  N   . ALA   B 2 806 ? 62.880  61.562  -2.027  1.00 152.29 ? 1110 ALA   B N   1 
ATOM   8496  C  CA  . ALA   B 2 806 ? 64.306  61.192  -2.171  1.00 153.04 ? 1110 ALA   B CA  1 
ATOM   8497  C  C   . ALA   B 2 806 ? 64.683  61.004  -3.640  1.00 159.62 ? 1110 ALA   B C   1 
ATOM   8498  O  O   . ALA   B 2 806 ? 63.908  60.362  -4.376  1.00 160.43 ? 1110 ALA   B O   1 
ATOM   8499  C  CB  . ALA   B 2 806 ? 64.569  59.930  -1.388  1.00 150.86 ? 1110 ALA   B CB  1 
ATOM   8500  N  N   . ASN   B 2 807 ? 65.844  61.531  -4.039  1.00 164.17 ? 1111 ASN   B N   1 
ATOM   8501  C  CA  . ASN   B 2 807 ? 66.350  61.345  -5.428  1.00 162.76 ? 1111 ASN   B CA  1 
ATOM   8502  C  C   . ASN   B 2 807 ? 65.297  61.470  -6.532  1.00 162.41 ? 1111 ASN   B C   1 
ATOM   8503  O  O   . ASN   B 2 807 ? 65.222  60.566  -7.390  1.00 163.14 ? 1111 ASN   B O   1 
ATOM   8504  C  CB  . ASN   B 2 807 ? 67.121  60.037  -5.563  1.00 155.08 ? 1111 ASN   B CB  1 
ATOM   8505  N  N   . LEU   B 2 808 ? 64.542  62.565  -6.531  1.00 157.26 ? 1112 LEU   B N   1 
ATOM   8506  C  CA  . LEU   B 2 808 ? 63.555  62.786  -7.615  1.00 157.38 ? 1112 LEU   B CA  1 
ATOM   8507  C  C   . LEU   B 2 808 ? 64.102  63.605  -8.793  1.00 158.50 ? 1112 LEU   B C   1 
ATOM   8508  O  O   . LEU   B 2 808 ? 64.018  64.848  -8.709  1.00 156.99 ? 1112 LEU   B O   1 
ATOM   8509  C  CB  . LEU   B 2 808 ? 62.361  63.467  -6.952  1.00 162.86 ? 1112 LEU   B CB  1 
ATOM   8510  C  CG  . LEU   B 2 808 ? 61.658  62.670  -5.848  1.00 166.70 ? 1112 LEU   B CG  1 
ATOM   8511  C  CD1 . LEU   B 2 808 ? 60.588  63.510  -5.172  1.00 160.44 ? 1112 LEU   B CD1 1 
ATOM   8512  C  CD2 . LEU   B 2 808 ? 61.066  61.374  -6.374  1.00 162.51 ? 1112 LEU   B CD2 1 
ATOM   8513  N  N   . GLU   B 2 819 ? 67.644  66.627  -7.810  1.00 147.77 ? 1123 GLU   B N   1 
ATOM   8514  C  CA  . GLU   B 2 819 ? 67.202  66.466  -6.430  1.00 149.00 ? 1123 GLU   B CA  1 
ATOM   8515  C  C   . GLU   B 2 819 ? 66.100  67.464  -6.110  1.00 153.31 ? 1123 GLU   B C   1 
ATOM   8516  O  O   . GLU   B 2 819 ? 66.213  68.655  -6.422  1.00 149.44 ? 1123 GLU   B O   1 
ATOM   8517  C  CB  . GLU   B 2 819 ? 68.369  66.636  -5.449  1.00 136.39 ? 1123 GLU   B CB  1 
ATOM   8518  N  N   . ALA   B 2 820 ? 65.028  66.962  -5.497  1.00 156.69 ? 1124 ALA   B N   1 
ATOM   8519  C  CA  . ALA   B 2 820 ? 63.909  67.773  -5.039  1.00 157.25 ? 1124 ALA   B CA  1 
ATOM   8520  C  C   . ALA   B 2 820 ? 63.635  67.458  -3.575  1.00 155.58 ? 1124 ALA   B C   1 
ATOM   8521  O  O   . ALA   B 2 820 ? 63.641  66.293  -3.170  1.00 154.25 ? 1124 ALA   B O   1 
ATOM   8522  C  CB  . ALA   B 2 820 ? 62.653  67.527  -5.886  1.00 155.26 ? 1124 ALA   B CB  1 
ATOM   8523  N  N   . THR   B 2 821 ? 63.416  68.496  -2.777  1.00 155.35 ? 1125 THR   B N   1 
ATOM   8524  C  CA  . THR   B 2 821 ? 63.243  68.309  -1.346  1.00 152.82 ? 1125 THR   B CA  1 
ATOM   8525  C  C   . THR   B 2 821 ? 61.766  68.156  -1.010  1.00 149.70 ? 1125 THR   B C   1 
ATOM   8526  O  O   . THR   B 2 821 ? 60.884  68.376  -1.844  1.00 147.08 ? 1125 THR   B O   1 
ATOM   8527  C  CB  . THR   B 2 821 ? 63.830  69.482  -0.569  1.00 153.12 ? 1125 THR   B CB  1 
ATOM   8528  O  OG1 . THR   B 2 821 ? 62.943  70.601  -0.681  1.00 154.14 ? 1125 THR   B OG1 1 
ATOM   8529  C  CG2 . THR   B 2 821 ? 65.181  69.865  -1.132  1.00 152.32 ? 1125 THR   B CG2 1 
ATOM   8530  N  N   . ALA   B 2 822 ? 61.504  67.796  0.248   1.00 149.17 ? 1126 ALA   B N   1 
ATOM   8531  C  CA  . ALA   B 2 822 ? 60.132  67.590  0.690   1.00 144.87 ? 1126 ALA   B CA  1 
ATOM   8532  C  C   . ALA   B 2 822 ? 59.289  68.849  0.519   1.00 147.88 ? 1126 ALA   B C   1 
ATOM   8533  O  O   . ALA   B 2 822 ? 58.113  68.769  0.149   1.00 148.70 ? 1126 ALA   B O   1 
ATOM   8534  C  CB  . ALA   B 2 822 ? 60.118  67.132  2.150   1.00 148.96 ? 1126 ALA   B CB  1 
ATOM   8535  N  N   . ASP   B 2 823 ? 59.883  70.025  0.766   1.00 154.11 ? 1127 ASP   B N   1 
ATOM   8536  C  CA  . ASP   B 2 823 ? 59.119  71.273  0.814   1.00 152.98 ? 1127 ASP   B CA  1 
ATOM   8537  C  C   . ASP   B 2 823 ? 58.681  71.755  -0.564  1.00 153.36 ? 1127 ASP   B C   1 
ATOM   8538  O  O   . ASP   B 2 823 ? 57.712  72.518  -0.668  1.00 154.66 ? 1127 ASP   B O   1 
ATOM   8539  C  CB  . ASP   B 2 823 ? 59.943  72.367  1.479   1.00 155.59 ? 1127 ASP   B CB  1 
ATOM   8540  C  CG  . ASP   B 2 823 ? 60.401  71.996  2.871   1.00 155.54 ? 1127 ASP   B CG  1 
ATOM   8541  O  OD1 . ASP   B 2 823 ? 60.991  70.896  3.047   1.00 155.31 ? 1127 ASP   B OD1 1 
ATOM   8542  O  OD2 . ASP   B 2 823 ? 60.185  72.825  3.786   1.00 157.67 ? 1127 ASP   B OD2 1 
ATOM   8543  N  N   . ASP   B 2 824 ? 59.411  71.393  -1.620  1.00 149.23 ? 1128 ASP   B N   1 
ATOM   8544  C  CA  . ASP   B 2 824 ? 58.956  71.738  -2.964  1.00 149.15 ? 1128 ASP   B CA  1 
ATOM   8545  C  C   . ASP   B 2 824 ? 57.631  71.063  -3.249  1.00 141.07 ? 1128 ASP   B C   1 
ATOM   8546  O  O   . ASP   B 2 824 ? 56.676  71.688  -3.730  1.00 138.81 ? 1128 ASP   B O   1 
ATOM   8547  C  CB  . ASP   B 2 824 ? 59.975  71.303  -4.018  1.00 151.89 ? 1128 ASP   B CB  1 
ATOM   8548  C  CG  . ASP   B 2 824 ? 61.378  71.747  -3.708  1.00 152.88 ? 1128 ASP   B CG  1 
ATOM   8549  O  OD1 . ASP   B 2 824 ? 61.553  72.831  -3.107  1.00 155.83 ? 1128 ASP   B OD1 1 
ATOM   8550  O  OD2 . ASP   B 2 824 ? 62.306  71.005  -4.091  1.00 150.70 ? 1128 ASP   B OD2 1 
ATOM   8551  N  N   . LEU   B 2 825 ? 57.568  69.773  -2.937  1.00 138.69 ? 1129 LEU   B N   1 
ATOM   8552  C  CA  . LEU   B 2 825 ? 56.451  68.928  -3.316  1.00 134.60 ? 1129 LEU   B CA  1 
ATOM   8553  C  C   . LEU   B 2 825 ? 55.202  69.253  -2.515  1.00 133.16 ? 1129 LEU   B C   1 
ATOM   8554  O  O   . LEU   B 2 825 ? 54.091  69.141  -3.046  1.00 129.84 ? 1129 LEU   B O   1 
ATOM   8555  C  CB  . LEU   B 2 825 ? 56.863  67.478  -3.115  1.00 134.80 ? 1129 LEU   B CB  1 
ATOM   8556  C  CG  . LEU   B 2 825 ? 56.276  66.416  -4.020  1.00 138.08 ? 1129 LEU   B CG  1 
ATOM   8557  C  CD1 . LEU   B 2 825 ? 57.234  65.240  -4.034  1.00 133.62 ? 1129 LEU   B CD1 1 
ATOM   8558  C  CD2 . LEU   B 2 825 ? 54.897  66.010  -3.499  1.00 144.74 ? 1129 LEU   B CD2 1 
ATOM   8559  N  N   . ILE   B 2 826 ? 55.358  69.650  -1.249  1.00 135.74 ? 1130 ILE   B N   1 
ATOM   8560  C  CA  . ILE   B 2 826 ? 54.208  70.096  -0.464  1.00 132.49 ? 1130 ILE   B CA  1 
ATOM   8561  C  C   . ILE   B 2 826 ? 53.506  71.254  -1.163  1.00 132.85 ? 1130 ILE   B C   1 
ATOM   8562  O  O   . ILE   B 2 826 ? 52.275  71.379  -1.118  1.00 130.92 ? 1130 ILE   B O   1 
ATOM   8563  C  CB  . ILE   B 2 826 ? 54.645  70.493  0.955   1.00 131.05 ? 1130 ILE   B CB  1 
ATOM   8564  C  CG1 . ILE   B 2 826 ? 55.236  69.316  1.704   1.00 131.56 ? 1130 ILE   B CG1 1 
ATOM   8565  C  CG2 . ILE   B 2 826 ? 53.469  71.045  1.745   1.00 129.10 ? 1130 ILE   B CG2 1 
ATOM   8566  C  CD1 . ILE   B 2 826 ? 55.733  69.738  3.056   1.00 134.39 ? 1130 ILE   B CD1 1 
ATOM   8567  N  N   . LYS   B 2 827 ? 54.280  72.134  -1.801  1.00 129.12 ? 1131 LYS   B N   1 
ATOM   8568  C  CA  . LYS   B 2 827 ? 53.678  73.226  -2.555  1.00 127.76 ? 1131 LYS   B CA  1 
ATOM   8569  C  C   . LYS   B 2 827 ? 52.873  72.686  -3.726  1.00 127.75 ? 1131 LYS   B C   1 
ATOM   8570  O  O   . LYS   B 2 827 ? 51.763  73.158  -4.001  1.00 130.51 ? 1131 LYS   B O   1 
ATOM   8571  C  CB  . LYS   B 2 827 ? 54.763  74.186  -3.045  1.00 124.80 ? 1131 LYS   B CB  1 
ATOM   8572  N  N   . VAL   B 2 828 ? 53.408  71.668  -4.400  1.00 132.57 ? 1132 VAL   B N   1 
ATOM   8573  C  CA  . VAL   B 2 828 ? 52.783  71.118  -5.601  1.00 128.59 ? 1132 VAL   B CA  1 
ATOM   8574  C  C   . VAL   B 2 828 ? 51.389  70.591  -5.286  1.00 125.85 ? 1132 VAL   B C   1 
ATOM   8575  O  O   . VAL   B 2 828 ? 50.381  71.064  -5.827  1.00 124.95 ? 1132 VAL   B O   1 
ATOM   8576  C  CB  . VAL   B 2 828 ? 53.680  70.022  -6.201  1.00 120.83 ? 1132 VAL   B CB  1 
ATOM   8577  C  CG1 . VAL   B 2 828 ? 53.131  69.569  -7.518  1.00 114.03 ? 1132 VAL   B CG1 1 
ATOM   8578  C  CG2 . VAL   B 2 828 ? 55.096  70.548  -6.362  1.00 126.21 ? 1132 VAL   B CG2 1 
ATOM   8579  N  N   . VAL   B 2 829 ? 51.315  69.602  -4.400  1.00 125.42 ? 1133 VAL   B N   1 
ATOM   8580  C  CA  . VAL   B 2 829 ? 50.027  69.037  -4.016  1.00 124.74 ? 1133 VAL   B CA  1 
ATOM   8581  C  C   . VAL   B 2 829 ? 49.075  70.125  -3.541  1.00 131.08 ? 1133 VAL   B C   1 
ATOM   8582  O  O   . VAL   B 2 829 ? 47.873  70.087  -3.829  1.00 129.43 ? 1133 VAL   B O   1 
ATOM   8583  C  CB  . VAL   B 2 829 ? 50.229  67.963  -2.936  1.00 118.97 ? 1133 VAL   B CB  1 
ATOM   8584  C  CG1 . VAL   B 2 829 ? 48.949  67.221  -2.714  1.00 116.09 ? 1133 VAL   B CG1 1 
ATOM   8585  C  CG2 . VAL   B 2 829 ? 51.337  67.031  -3.352  1.00 118.04 ? 1133 VAL   B CG2 1 
ATOM   8586  N  N   . GLU   B 2 830 ? 49.601  71.117  -2.810  1.00 145.21 ? 1134 GLU   B N   1 
ATOM   8587  C  CA  . GLU   B 2 830 ? 48.748  72.143  -2.219  1.00 146.47 ? 1134 GLU   B CA  1 
ATOM   8588  C  C   . GLU   B 2 830 ? 47.998  72.923  -3.294  1.00 148.20 ? 1134 GLU   B C   1 
ATOM   8589  O  O   . GLU   B 2 830 ? 46.845  73.328  -3.092  1.00 150.28 ? 1134 GLU   B O   1 
ATOM   8590  C  CB  . GLU   B 2 830 ? 49.584  73.079  -1.341  1.00 146.85 ? 1134 GLU   B CB  1 
ATOM   8591  N  N   . GLU   B 2 831 ? 48.635  73.149  -4.443  1.00 129.96 ? 1135 GLU   B N   1 
ATOM   8592  C  CA  . GLU   B 2 831 ? 47.897  73.703  -5.571  1.00 131.31 ? 1135 GLU   B CA  1 
ATOM   8593  C  C   . GLU   B 2 831 ? 46.835  72.721  -6.047  1.00 129.97 ? 1135 GLU   B C   1 
ATOM   8594  O  O   . GLU   B 2 831 ? 45.728  73.124  -6.437  1.00 127.62 ? 1135 GLU   B O   1 
ATOM   8595  C  CB  . GLU   B 2 831 ? 48.856  74.064  -6.706  1.00 131.00 ? 1135 GLU   B CB  1 
ATOM   8596  N  N   . LEU   B 2 832 ? 47.152  71.419  -6.006  1.00 127.89 ? 1136 LEU   B N   1 
ATOM   8597  C  CA  . LEU   B 2 832 ? 46.205  70.405  -6.461  1.00 121.67 ? 1136 LEU   B CA  1 
ATOM   8598  C  C   . LEU   B 2 832 ? 45.022  70.276  -5.512  1.00 122.33 ? 1136 LEU   B C   1 
ATOM   8599  O  O   . LEU   B 2 832 ? 43.906  69.974  -5.955  1.00 120.30 ? 1136 LEU   B O   1 
ATOM   8600  C  CB  . LEU   B 2 832 ? 46.901  69.054  -6.618  1.00 115.74 ? 1136 LEU   B CB  1 
ATOM   8601  C  CG  . LEU   B 2 832 ? 48.045  68.898  -7.624  1.00 112.52 ? 1136 LEU   B CG  1 
ATOM   8602  C  CD1 . LEU   B 2 832 ? 48.444  67.425  -7.762  1.00 107.27 ? 1136 LEU   B CD1 1 
ATOM   8603  C  CD2 . LEU   B 2 832 ? 47.677  69.475  -8.980  1.00 108.70 ? 1136 LEU   B CD2 1 
ATOM   8604  N  N   . THR   B 2 833 ? 45.233  70.484  -4.210  1.00 122.80 ? 1137 THR   B N   1 
ATOM   8605  C  CA  . THR   B 2 833 ? 44.087  70.498  -3.312  1.00 124.03 ? 1137 THR   B CA  1 
ATOM   8606  C  C   . THR   B 2 833 ? 43.159  71.642  -3.665  1.00 123.55 ? 1137 THR   B C   1 
ATOM   8607  O  O   . THR   B 2 833 ? 41.937  71.549  -3.475  1.00 121.82 ? 1137 THR   B O   1 
ATOM   8608  C  CB  . THR   B 2 833 ? 44.537  70.590  -1.858  1.00 123.61 ? 1137 THR   B CB  1 
ATOM   8609  O  OG1 . THR   B 2 833 ? 45.006  71.914  -1.571  1.00 125.77 ? 1137 THR   B OG1 1 
ATOM   8610  C  CG2 . THR   B 2 833 ? 45.649  69.604  -1.621  1.00 120.31 ? 1137 THR   B CG2 1 
ATOM   8611  N  N   . ARG   B 2 834 ? 43.707  72.693  -4.255  1.00 121.91 ? 1138 ARG   B N   1 
ATOM   8612  C  CA  . ARG   B 2 834 ? 42.915  73.864  -4.549  1.00 121.58 ? 1138 ARG   B CA  1 
ATOM   8613  C  C   . ARG   B 2 834 ? 42.128  73.571  -5.820  1.00 118.55 ? 1138 ARG   B C   1 
ATOM   8614  O  O   . ARG   B 2 834 ? 42.084  74.414  -6.713  1.00 120.02 ? 1138 ARG   B O   1 
ATOM   8615  C  CB  . ARG   B 2 834 ? 43.840  75.068  -4.750  1.00 122.97 ? 1138 ARG   B CB  1 
ATOM   8616  N  N   . ILE   B 2 835 ? 41.493  72.406  -5.938  1.00 119.90 ? 1139 ILE   B N   1 
ATOM   8617  C  CA  . ILE   B 2 835 ? 40.649  72.158  -7.098  1.00 119.30 ? 1139 ILE   B CA  1 
ATOM   8618  C  C   . ILE   B 2 835 ? 39.313  71.583  -6.657  1.00 118.67 ? 1139 ILE   B C   1 
ATOM   8619  O  O   . ILE   B 2 835 ? 38.353  71.644  -7.438  1.00 120.32 ? 1139 ILE   B O   1 
ATOM   8620  C  CB  . ILE   B 2 835 ? 41.256  71.277  -8.210  1.00 113.76 ? 1139 ILE   B CB  1 
ATOM   8621  C  CG1 . ILE   B 2 835 ? 41.154  69.801  -7.865  1.00 112.84 ? 1139 ILE   B CG1 1 
ATOM   8622  C  CG2 . ILE   B 2 835 ? 42.681  71.638  -8.460  1.00 114.06 ? 1139 ILE   B CG2 1 
ATOM   8623  C  CD1 . ILE   B 2 835 ? 41.527  68.952  -9.030  1.00 106.63 ? 1139 ILE   B CD1 1 
ATOM   8624  N  N   . HIS   B 2 836 ? 39.184  71.017  -5.463  1.00 118.08 ? 1140 HIS   B N   1 
ATOM   8625  C  CA  . HIS   B 2 836 ? 37.892  70.425  -5.116  1.00 117.55 ? 1140 HIS   B CA  1 
ATOM   8626  C  C   . HIS   B 2 836 ? 37.354  70.924  -3.781  1.00 117.86 ? 1140 HIS   B C   1 
ATOM   8627  O  O   . HIS   B 2 836 ? 36.140  70.896  -3.554  1.00 116.70 ? 1140 HIS   B O   1 
ATOM   8628  C  CB  . HIS   B 2 836 ? 37.976  68.891  -5.110  1.00 115.31 ? 1140 HIS   B CB  1 
ATOM   8629  C  CG  . HIS   B 2 836 ? 39.173  68.354  -4.400  1.00 116.41 ? 1140 HIS   B CG  1 
ATOM   8630  N  ND1 . HIS   B 2 836 ? 39.171  68.054  -3.055  1.00 121.63 ? 1140 HIS   B ND1 1 
ATOM   8631  C  CD2 . HIS   B 2 836 ? 40.417  68.074  -4.848  1.00 117.25 ? 1140 HIS   B CD2 1 
ATOM   8632  C  CE1 . HIS   B 2 836 ? 40.364  67.604  -2.705  1.00 122.00 ? 1140 HIS   B CE1 1 
ATOM   8633  N  NE2 . HIS   B 2 836 ? 41.138  67.609  -3.775  1.00 121.09 ? 1140 HIS   B NE2 1 
ATOM   8634  N  N   . SER   C 3 3   ? 18.509  13.633  -71.348 1.00 104.78 ? 868  SER   C N   1 
ATOM   8635  C  CA  . SER   C 3 3   ? 19.634  13.250  -70.487 1.00 113.37 ? 868  SER   C CA  1 
ATOM   8636  C  C   . SER   C 3 3   ? 20.850  14.184  -70.670 1.00 112.25 ? 868  SER   C C   1 
ATOM   8637  O  O   . SER   C 3 3   ? 21.358  14.734  -69.696 1.00 110.90 ? 868  SER   C O   1 
ATOM   8638  C  CB  . SER   C 3 3   ? 20.051  11.795  -70.749 1.00 117.28 ? 868  SER   C CB  1 
ATOM   8639  O  OG  . SER   C 3 3   ? 19.081  10.888  -70.248 1.00 118.62 ? 868  SER   C OG  1 
ATOM   8640  N  N   . LEU   C 3 4   ? 21.309  14.362  -71.920 1.00 108.59 ? 869  LEU   C N   1 
ATOM   8641  C  CA  . LEU   C 3 4   ? 22.429  15.268  -72.222 1.00 106.24 ? 869  LEU   C CA  1 
ATOM   8642  C  C   . LEU   C 3 4   ? 21.968  16.733  -72.268 1.00 99.74  ? 869  LEU   C C   1 
ATOM   8643  O  O   . LEU   C 3 4   ? 22.667  17.634  -72.718 1.00 92.22  ? 869  LEU   C O   1 
ATOM   8644  C  CB  . LEU   C 3 4   ? 23.094  14.843  -73.539 1.00 107.08 ? 869  LEU   C CB  1 
ATOM   8645  C  CG  . LEU   C 3 4   ? 24.604  15.094  -73.738 1.00 105.39 ? 869  LEU   C CG  1 
ATOM   8646  C  CD1 . LEU   C 3 4   ? 25.445  14.238  -72.786 1.00 104.79 ? 869  LEU   C CD1 1 
ATOM   8647  C  CD2 . LEU   C 3 4   ? 25.053  14.883  -75.198 1.00 97.37  ? 869  LEU   C CD2 1 
ATOM   8648  N  N   . THR   C 3 5   ? 20.734  16.887  -71.814 1.00 100.69 ? 870  THR   C N   1 
ATOM   8649  C  CA  . THR   C 3 5   ? 20.024  18.157  -71.848 1.00 101.41 ? 870  THR   C CA  1 
ATOM   8650  C  C   . THR   C 3 5   ? 19.386  18.487  -70.510 1.00 102.49 ? 870  THR   C C   1 
ATOM   8651  O  O   . THR   C 3 5   ? 18.489  19.340  -70.468 1.00 102.22 ? 870  THR   C O   1 
ATOM   8652  C  CB  . THR   C 3 5   ? 18.960  18.159  -72.938 1.00 103.97 ? 870  THR   C CB  1 
ATOM   8653  O  OG1 . THR   C 3 5   ? 18.200  16.937  -72.874 1.00 102.13 ? 870  THR   C OG1 1 
ATOM   8654  C  CG2 . THR   C 3 5   ? 19.587  18.320  -74.301 1.00 106.41 ? 870  THR   C CG2 1 
ATOM   8655  N  N   . THR   C 3 6   ? 19.791  17.844  -69.433 1.00 103.60 ? 871  THR   C N   1 
ATOM   8656  C  CA  . THR   C 3 6   ? 19.273  18.131  -68.110 1.00 99.36  ? 871  THR   C CA  1 
ATOM   8657  C  C   . THR   C 3 6   ? 20.324  18.931  -67.358 1.00 98.61  ? 871  THR   C C   1 
ATOM   8658  O  O   . THR   C 3 6   ? 21.525  18.712  -67.524 1.00 97.37  ? 871  THR   C O   1 
ATOM   8659  C  CB  . THR   C 3 6   ? 18.923  16.843  -67.369 1.00 103.01 ? 871  THR   C CB  1 
ATOM   8660  O  OG1 . THR   C 3 6   ? 18.425  15.879  -68.304 1.00 104.39 ? 871  THR   C OG1 1 
ATOM   8661  C  CG2 . THR   C 3 6   ? 17.854  17.116  -66.343 1.00 106.31 ? 871  THR   C CG2 1 
ATOM   8662  N  N   . CYS   C 3 7   ? 19.872  19.881  -66.553 1.00 98.34  ? 872  CYS   C N   1 
ATOM   8663  C  CA  . CYS   C 3 7   ? 20.802  20.713  -65.816 1.00 95.07  ? 872  CYS   C CA  1 
ATOM   8664  C  C   . CYS   C 3 7   ? 21.218  20.010  -64.535 1.00 99.10  ? 872  CYS   C C   1 
ATOM   8665  O  O   . CYS   C 3 7   ? 20.367  19.653  -63.714 1.00 100.55 ? 872  CYS   C O   1 
ATOM   8666  C  CB  . CYS   C 3 7   ? 20.172  22.063  -65.487 1.00 93.57  ? 872  CYS   C CB  1 
ATOM   8667  S  SG  . CYS   C 3 7   ? 21.346  23.144  -64.647 1.00 93.25  ? 872  CYS   C SG  1 
ATOM   8668  N  N   . GLU   C 3 8   ? 22.532  19.849  -64.342 1.00 102.98 ? 873  GLU   C N   1 
ATOM   8669  C  CA  . GLU   C 3 8   ? 23.030  19.156  -63.152 1.00 102.61 ? 873  GLU   C CA  1 
ATOM   8670  C  C   . GLU   C 3 8   ? 22.565  19.813  -61.861 1.00 102.55 ? 873  GLU   C C   1 
ATOM   8671  O  O   . GLU   C 3 8   ? 22.434  19.135  -60.837 1.00 104.67 ? 873  GLU   C O   1 
ATOM   8672  C  CB  . GLU   C 3 8   ? 24.554  19.107  -63.159 1.00 106.11 ? 873  GLU   C CB  1 
ATOM   8673  C  CG  . GLU   C 3 8   ? 25.141  18.208  -64.220 1.00 115.43 ? 873  GLU   C CG  1 
ATOM   8674  C  CD  . GLU   C 3 8   ? 25.596  16.864  -63.669 1.00 118.27 ? 873  GLU   C CD  1 
ATOM   8675  O  OE1 . GLU   C 3 8   ? 25.826  16.755  -62.439 1.00 114.29 ? 873  GLU   C OE1 1 
ATOM   8676  O  OE2 . GLU   C 3 8   ? 25.727  15.915  -64.478 1.00 122.27 ? 873  GLU   C OE2 1 
ATOM   8677  N  N   . VAL   C 3 9   ? 22.321  21.121  -61.884 1.00 100.72 ? 874  VAL   C N   1 
ATOM   8678  C  CA  . VAL   C 3 9   ? 22.123  21.893  -60.664 1.00 95.28  ? 874  VAL   C CA  1 
ATOM   8679  C  C   . VAL   C 3 9   ? 20.657  21.997  -60.293 1.00 95.82  ? 874  VAL   C C   1 
ATOM   8680  O  O   . VAL   C 3 9   ? 20.260  21.711  -59.159 1.00 95.85  ? 874  VAL   C O   1 
ATOM   8681  C  CB  . VAL   C 3 9   ? 22.748  23.281  -60.845 1.00 90.75  ? 874  VAL   C CB  1 
ATOM   8682  C  CG1 . VAL   C 3 9   ? 22.394  24.156  -59.690 1.00 95.40  ? 874  VAL   C CG1 1 
ATOM   8683  C  CG2 . VAL   C 3 9   ? 24.222  23.138  -60.960 1.00 94.17  ? 874  VAL   C CG2 1 
ATOM   8684  N  N   . CYS   C 3 10  ? 19.818  22.433  -61.216 1.00 95.84  ? 875  CYS   C N   1 
ATOM   8685  C  CA  . CYS   C 3 10  ? 18.422  22.608  -60.881 1.00 90.10  ? 875  CYS   C CA  1 
ATOM   8686  C  C   . CYS   C 3 10  ? 17.528  21.510  -61.414 1.00 91.93  ? 875  CYS   C C   1 
ATOM   8687  O  O   . CYS   C 3 10  ? 16.399  21.385  -60.938 1.00 92.60  ? 875  CYS   C O   1 
ATOM   8688  C  CB  . CYS   C 3 10  ? 17.918  23.955  -61.400 1.00 91.20  ? 875  CYS   C CB  1 
ATOM   8689  S  SG  . CYS   C 3 10  ? 17.875  24.043  -63.215 1.00 86.54  ? 875  CYS   C SG  1 
ATOM   8690  N  N   . GLY   C 3 11  ? 17.997  20.713  -62.376 1.00 96.36  ? 876  GLY   C N   1 
ATOM   8691  C  CA  . GLY   C 3 11  ? 17.227  19.614  -62.921 1.00 97.86  ? 876  GLY   C CA  1 
ATOM   8692  C  C   . GLY   C 3 11  ? 16.457  19.905  -64.189 1.00 100.27 ? 876  GLY   C C   1 
ATOM   8693  O  O   . GLY   C 3 11  ? 15.709  19.034  -64.645 1.00 100.59 ? 876  GLY   C O   1 
ATOM   8694  N  N   . ALA   C 3 12  ? 16.621  21.090  -64.774 1.00 112.30 ? 877  ALA   C N   1 
ATOM   8695  C  CA  . ALA   C 3 12  ? 15.839  21.477  -65.943 1.00 112.91 ? 877  ALA   C CA  1 
ATOM   8696  C  C   . ALA   C 3 12  ? 16.296  20.699  -67.175 1.00 113.93 ? 877  ALA   C C   1 
ATOM   8697  O  O   . ALA   C 3 12  ? 17.491  20.658  -67.482 1.00 115.43 ? 877  ALA   C O   1 
ATOM   8698  C  CB  . ALA   C 3 12  ? 15.967  22.982  -66.178 1.00 112.65 ? 877  ALA   C CB  1 
ATOM   8699  N  N   . CYS   C 3 13  ? 15.350  20.071  -67.878 1.00 106.52 ? 878  CYS   C N   1 
ATOM   8700  C  CA  . CYS   C 3 13  ? 15.644  19.282  -69.073 1.00 101.08 ? 878  CYS   C CA  1 
ATOM   8701  C  C   . CYS   C 3 13  ? 15.226  20.094  -70.295 1.00 102.20 ? 878  CYS   C C   1 
ATOM   8702  O  O   . CYS   C 3 13  ? 14.031  20.308  -70.523 1.00 98.87  ? 878  CYS   C O   1 
ATOM   8703  C  CB  . CYS   C 3 13  ? 14.926  17.932  -69.041 1.00 99.06  ? 878  CYS   C CB  1 
ATOM   8704  S  SG  . CYS   C 3 13  ? 15.696  16.588  -70.046 1.00 116.57 ? 878  CYS   C SG  1 
ATOM   8705  N  N   . PHE   C 3 14  ? 16.211  20.532  -71.081 1.00 104.32 ? 879  PHE   C N   1 
ATOM   8706  C  CA  . PHE   C 3 14  ? 15.996  21.296  -72.296 1.00 104.92 ? 879  PHE   C CA  1 
ATOM   8707  C  C   . PHE   C 3 14  ? 15.828  20.371  -73.492 1.00 112.70 ? 879  PHE   C C   1 
ATOM   8708  O  O   . PHE   C 3 14  ? 16.121  19.172  -73.434 1.00 108.76 ? 879  PHE   C O   1 
ATOM   8709  C  CB  . PHE   C 3 14  ? 17.156  22.241  -72.540 1.00 103.03 ? 879  PHE   C CB  1 
ATOM   8710  C  CG  . PHE   C 3 14  ? 17.215  23.356  -71.574 1.00 99.28  ? 879  PHE   C CG  1 
ATOM   8711  C  CD1 . PHE   C 3 14  ? 17.871  23.211  -70.383 1.00 97.85  ? 879  PHE   C CD1 1 
ATOM   8712  C  CD2 . PHE   C 3 14  ? 16.594  24.552  -71.852 1.00 101.12 ? 879  PHE   C CD2 1 
ATOM   8713  C  CE1 . PHE   C 3 14  ? 17.923  24.237  -69.500 1.00 99.23  ? 879  PHE   C CE1 1 
ATOM   8714  C  CE2 . PHE   C 3 14  ? 16.645  25.586  -70.974 1.00 90.00  ? 879  PHE   C CE2 1 
ATOM   8715  C  CZ  . PHE   C 3 14  ? 17.304  25.429  -69.799 1.00 96.44  ? 879  PHE   C CZ  1 
ATOM   8716  N  N   . GLU   C 3 15  ? 15.344  20.937  -74.600 1.00 115.64 ? 880  GLU   C N   1 
ATOM   8717  C  CA  . GLU   C 3 15  ? 15.204  20.089  -75.771 1.00 120.10 ? 880  GLU   C CA  1 
ATOM   8718  C  C   . GLU   C 3 15  ? 16.501  20.019  -76.556 1.00 119.48 ? 880  GLU   C C   1 
ATOM   8719  O  O   . GLU   C 3 15  ? 16.758  19.018  -77.239 1.00 119.29 ? 880  GLU   C O   1 
ATOM   8720  C  CB  . GLU   C 3 15  ? 14.056  20.577  -76.636 1.00 125.16 ? 880  GLU   C CB  1 
ATOM   8721  C  CG  . GLU   C 3 15  ? 12.735  20.037  -76.165 1.00 129.22 ? 880  GLU   C CG  1 
ATOM   8722  C  CD  . GLU   C 3 15  ? 11.606  20.421  -77.083 1.00 148.34 ? 880  GLU   C CD  1 
ATOM   8723  O  OE1 . GLU   C 3 15  ? 11.865  20.650  -78.293 1.00 152.44 ? 880  GLU   C OE1 1 
ATOM   8724  O  OE2 . GLU   C 3 15  ? 10.457  20.498  -76.594 1.00 155.30 ? 880  GLU   C OE2 1 
ATOM   8725  N  N   . THR   C 3 16  ? 17.341  21.036  -76.409 1.00 120.28 ? 881  THR   C N   1 
ATOM   8726  C  CA  . THR   C 3 16  ? 18.583  21.174  -77.145 1.00 118.90 ? 881  THR   C CA  1 
ATOM   8727  C  C   . THR   C 3 16  ? 19.741  21.446  -76.200 1.00 117.22 ? 881  THR   C C   1 
ATOM   8728  O  O   . THR   C 3 16  ? 19.634  22.275  -75.291 1.00 116.47 ? 881  THR   C O   1 
ATOM   8729  C  CB  . THR   C 3 16  ? 18.485  22.322  -78.112 1.00 117.49 ? 881  THR   C CB  1 
ATOM   8730  O  OG1 . THR   C 3 16  ? 18.193  23.506  -77.357 1.00 118.91 ? 881  THR   C OG1 1 
ATOM   8731  C  CG2 . THR   C 3 16  ? 17.379  22.061  -79.106 1.00 117.25 ? 881  THR   C CG2 1 
ATOM   8732  N  N   . ARG   C 3 17  ? 20.864  20.775  -76.460 1.00 111.61 ? 882  ARG   C N   1 
ATOM   8733  C  CA  . ARG   C 3 17  ? 22.081  21.036  -75.701 1.00 106.52 ? 882  ARG   C CA  1 
ATOM   8734  C  C   . ARG   C 3 17  ? 22.504  22.500  -75.834 1.00 107.70 ? 882  ARG   C C   1 
ATOM   8735  O  O   . ARG   C 3 17  ? 22.898  23.137  -74.851 1.00 105.06 ? 882  ARG   C O   1 
ATOM   8736  C  CB  . ARG   C 3 17  ? 23.188  20.087  -76.169 1.00 99.71  ? 882  ARG   C CB  1 
ATOM   8737  N  N   . LYS   C 3 18  ? 22.359  23.078  -77.034 1.00 110.57 ? 883  LYS   C N   1 
ATOM   8738  C  CA  . LYS   C 3 18  ? 22.753  24.461  -77.326 1.00 107.65 ? 883  LYS   C CA  1 
ATOM   8739  C  C   . LYS   C 3 18  ? 21.960  25.491  -76.555 1.00 105.99 ? 883  LYS   C C   1 
ATOM   8740  O  O   . LYS   C 3 18  ? 22.292  26.673  -76.863 1.00 105.64 ? 883  LYS   C O   1 
ATOM   8741  C  CB  . LYS   C 3 18  ? 22.710  24.709  -78.839 1.00 110.72 ? 883  LYS   C CB  1 
ATOM   8742  N  N   . GLY   C 3 19  ? 20.992  25.016  -75.750 1.00 99.26  ? 884  GLY   C N   1 
ATOM   8743  C  CA  . GLY   C 3 19  ? 20.122  25.812  -74.903 1.00 98.57  ? 884  GLY   C CA  1 
ATOM   8744  C  C   . GLY   C 3 19  ? 20.409  25.613  -73.435 1.00 99.89  ? 884  GLY   C C   1 
ATOM   8745  O  O   . GLY   C 3 19  ? 20.453  26.568  -72.661 1.00 102.21 ? 884  GLY   C O   1 
ATOM   8746  N  N   . LEU   C 3 20  ? 20.601  24.353  -73.047 1.00 103.76 ? 885  LEU   C N   1 
ATOM   8747  C  CA  . LEU   C 3 20  ? 21.139  24.017  -71.731 1.00 101.52 ? 885  LEU   C CA  1 
ATOM   8748  C  C   . LEU   C 3 20  ? 22.464  24.731  -71.459 1.00 101.48 ? 885  LEU   C C   1 
ATOM   8749  O  O   . LEU   C 3 20  ? 22.824  24.954  -70.298 1.00 97.51  ? 885  LEU   C O   1 
ATOM   8750  C  CB  . LEU   C 3 20  ? 21.282  22.489  -71.658 1.00 95.49  ? 885  LEU   C CB  1 
ATOM   8751  C  CG  . LEU   C 3 20  ? 21.892  21.679  -70.524 1.00 89.26  ? 885  LEU   C CG  1 
ATOM   8752  C  CD1 . LEU   C 3 20  ? 23.405  21.736  -70.547 1.00 89.31  ? 885  LEU   C CD1 1 
ATOM   8753  C  CD2 . LEU   C 3 20  ? 21.336  22.173  -69.226 1.00 94.36  ? 885  LEU   C CD2 1 
ATOM   8754  N  N   . SER   C 3 21  ? 23.194  25.089  -72.513 1.00 100.26 ? 886  SER   C N   1 
ATOM   8755  C  CA  . SER   C 3 21  ? 24.399  25.887  -72.350 1.00 100.86 ? 886  SER   C CA  1 
ATOM   8756  C  C   . SER   C 3 21  ? 24.059  27.315  -71.981 1.00 100.96 ? 886  SER   C C   1 
ATOM   8757  O  O   . SER   C 3 21  ? 24.734  27.924  -71.140 1.00 103.86 ? 886  SER   C O   1 
ATOM   8758  C  CB  . SER   C 3 21  ? 25.187  25.861  -73.642 1.00 102.27 ? 886  SER   C CB  1 
ATOM   8759  O  OG  . SER   C 3 21  ? 24.261  25.849  -74.713 1.00 105.35 ? 886  SER   C OG  1 
ATOM   8760  N  N   . SER   C 3 22  ? 23.032  27.878  -72.612 1.00 98.43  ? 887  SER   C N   1 
ATOM   8761  C  CA  . SER   C 3 22  ? 22.595  29.207  -72.223 1.00 99.49  ? 887  SER   C CA  1 
ATOM   8762  C  C   . SER   C 3 22  ? 22.030  29.210  -70.815 1.00 101.05 ? 887  SER   C C   1 
ATOM   8763  O  O   . SER   C 3 22  ? 22.170  30.206  -70.103 1.00 107.72 ? 887  SER   C O   1 
ATOM   8764  C  CB  . SER   C 3 22  ? 21.552  29.739  -73.192 1.00 100.48 ? 887  SER   C CB  1 
ATOM   8765  O  OG  . SER   C 3 22  ? 20.274  29.335  -72.754 1.00 98.39  ? 887  SER   C OG  1 
ATOM   8766  N  N   . HIS   C 3 23  ? 21.370  28.130  -70.396 1.00 101.29 ? 888  HIS   C N   1 
ATOM   8767  C  CA  . HIS   C 3 23  ? 20.988  28.040  -68.994 1.00 100.09 ? 888  HIS   C CA  1 
ATOM   8768  C  C   . HIS   C 3 23  ? 22.213  27.941  -68.104 1.00 107.51 ? 888  HIS   C C   1 
ATOM   8769  O  O   . HIS   C 3 23  ? 22.231  28.492  -66.997 1.00 111.38 ? 888  HIS   C O   1 
ATOM   8770  C  CB  . HIS   C 3 23  ? 20.084  26.842  -68.749 1.00 95.61  ? 888  HIS   C CB  1 
ATOM   8771  C  CG  . HIS   C 3 23  ? 19.792  26.581  -67.295 1.00 96.86  ? 888  HIS   C CG  1 
ATOM   8772  N  ND1 . HIS   C 3 23  ? 19.385  27.569  -66.421 1.00 101.70 ? 888  HIS   C ND1 1 
ATOM   8773  C  CD2 . HIS   C 3 23  ? 19.832  25.435  -66.566 1.00 99.24  ? 888  HIS   C CD2 1 
ATOM   8774  C  CE1 . HIS   C 3 23  ? 19.195  27.047  -65.220 1.00 100.11 ? 888  HIS   C CE1 1 
ATOM   8775  N  NE2 . HIS   C 3 23  ? 19.468  25.754  -65.279 1.00 96.86  ? 888  HIS   C NE2 1 
ATOM   8776  N  N   . ALA   C 3 24  ? 23.251  27.246  -68.568 1.00 118.96 ? 889  ALA   C N   1 
ATOM   8777  C  CA  . ALA   C 3 24  ? 24.408  27.017  -67.712 1.00 119.63 ? 889  ALA   C CA  1 
ATOM   8778  C  C   . ALA   C 3 24  ? 25.033  28.332  -67.258 1.00 120.91 ? 889  ALA   C C   1 
ATOM   8779  O  O   . ALA   C 3 24  ? 25.567  28.418  -66.144 1.00 122.75 ? 889  ALA   C O   1 
ATOM   8780  C  CB  . ALA   C 3 24  ? 25.422  26.133  -68.445 1.00 120.43 ? 889  ALA   C CB  1 
ATOM   8781  N  N   . ARG   C 3 25  ? 24.951  29.371  -68.096 1.00 111.47 ? 890  ARG   C N   1 
ATOM   8782  C  CA  . ARG   C 3 25  ? 25.367  30.707  -67.678 1.00 111.93 ? 890  ARG   C CA  1 
ATOM   8783  C  C   . ARG   C 3 25  ? 24.631  31.149  -66.416 1.00 113.72 ? 890  ARG   C C   1 
ATOM   8784  O  O   . ARG   C 3 25  ? 25.258  31.586  -65.442 1.00 117.72 ? 890  ARG   C O   1 
ATOM   8785  C  CB  . ARG   C 3 25  ? 25.126  31.711  -68.812 1.00 107.70 ? 890  ARG   C CB  1 
ATOM   8786  N  N   . SER   C 3 26  ? 23.302  31.018  -66.405 1.00 109.76 ? 891  SER   C N   1 
ATOM   8787  C  CA  . SER   C 3 26  ? 22.450  31.623  -65.386 1.00 109.43 ? 891  SER   C CA  1 
ATOM   8788  C  C   . SER   C 3 26  ? 22.846  31.243  -63.948 1.00 112.92 ? 891  SER   C C   1 
ATOM   8789  O  O   . SER   C 3 26  ? 22.431  31.944  -63.010 1.00 112.54 ? 891  SER   C O   1 
ATOM   8790  C  CB  . SER   C 3 26  ? 20.982  31.350  -65.725 1.00 101.08 ? 891  SER   C CB  1 
ATOM   8791  O  OG  . SER   C 3 26  ? 20.505  30.190  -65.067 1.00 96.00  ? 891  SER   C OG  1 
ATOM   8792  N  N   . HIS   C 3 27  ? 23.638  30.190  -63.737 1.00 111.58 ? 892  HIS   C N   1 
ATOM   8793  C  CA  . HIS   C 3 27  ? 24.064  29.811  -62.394 1.00 111.13 ? 892  HIS   C CA  1 
ATOM   8794  C  C   . HIS   C 3 27  ? 25.285  30.517  -61.826 1.00 120.50 ? 892  HIS   C C   1 
ATOM   8795  O  O   . HIS   C 3 27  ? 25.681  30.229  -60.691 1.00 123.35 ? 892  HIS   C O   1 
ATOM   8796  C  CB  . HIS   C 3 27  ? 24.294  28.299  -62.369 1.00 107.95 ? 892  HIS   C CB  1 
ATOM   8797  C  CG  . HIS   C 3 27  ? 23.028  27.497  -62.337 1.00 103.98 ? 892  HIS   C CG  1 
ATOM   8798  N  ND1 . HIS   C 3 27  ? 21.931  27.876  -61.594 1.00 99.67  ? 892  HIS   C ND1 1 
ATOM   8799  C  CD2 . HIS   C 3 27  ? 22.680  26.344  -62.962 1.00 102.46 ? 892  HIS   C CD2 1 
ATOM   8800  C  CE1 . HIS   C 3 27  ? 20.962  26.992  -61.762 1.00 99.30  ? 892  HIS   C CE1 1 
ATOM   8801  N  NE2 . HIS   C 3 27  ? 21.388  26.053  -62.590 1.00 98.97  ? 892  HIS   C NE2 1 
ATOM   8802  N  N   . LEU   C 3 28  ? 25.902  31.411  -62.588 1.00 126.47 ? 893  LEU   C N   1 
ATOM   8803  C  CA  . LEU   C 3 28  ? 26.957  32.268  -62.056 1.00 131.41 ? 893  LEU   C CA  1 
ATOM   8804  C  C   . LEU   C 3 28  ? 26.798  33.674  -62.637 1.00 122.63 ? 893  LEU   C C   1 
ATOM   8805  O  O   . LEU   C 3 28  ? 25.866  34.395  -62.277 1.00 119.10 ? 893  LEU   C O   1 
ATOM   8806  C  CB  . LEU   C 3 28  ? 28.352  31.694  -62.363 1.00 131.60 ? 893  LEU   C CB  1 
ATOM   8807  C  CG  . LEU   C 3 28  ? 29.052  30.796  -61.329 1.00 124.02 ? 893  LEU   C CG  1 
ATOM   8808  C  CD1 . LEU   C 3 28  ? 30.319  30.238  -61.948 1.00 126.25 ? 893  LEU   C CD1 1 
ATOM   8809  C  CD2 . LEU   C 3 28  ? 29.385  31.544  -60.042 1.00 117.41 ? 893  LEU   C CD2 1 
ATOM   8810  N  N   . ASP   D 1 6   ? 17.638  -35.492 -14.011 1.00 136.34 ? 75   ASP   D N   1 
ATOM   8811  C  CA  . ASP   D 1 6   ? 16.203  -35.765 -14.064 1.00 146.50 ? 75   ASP   D CA  1 
ATOM   8812  C  C   . ASP   D 1 6   ? 15.549  -34.810 -13.073 1.00 148.91 ? 75   ASP   D C   1 
ATOM   8813  O  O   . ASP   D 1 6   ? 16.262  -34.151 -12.309 1.00 143.17 ? 75   ASP   D O   1 
ATOM   8814  C  CB  . ASP   D 1 6   ? 15.915  -37.246 -13.728 1.00 145.56 ? 75   ASP   D CB  1 
ATOM   8815  C  CG  . ASP   D 1 6   ? 14.564  -37.765 -14.292 1.00 145.27 ? 75   ASP   D CG  1 
ATOM   8816  O  OD1 . ASP   D 1 6   ? 13.595  -37.922 -13.505 1.00 136.32 ? 75   ASP   D OD1 1 
ATOM   8817  O  OD2 . ASP   D 1 6   ? 14.480  -38.046 -15.515 1.00 144.31 ? 75   ASP   D OD2 1 
ATOM   8818  N  N   . ASP   D 1 7   ? 14.197  -34.730 -13.093 1.00 166.13 ? 76   ASP   D N   1 
ATOM   8819  C  CA  . ASP   D 1 7   ? 13.436  -33.887 -12.161 1.00 166.56 ? 76   ASP   D CA  1 
ATOM   8820  C  C   . ASP   D 1 7   ? 12.087  -34.519 -11.789 1.00 161.11 ? 76   ASP   D C   1 
ATOM   8821  O  O   . ASP   D 1 7   ? 11.120  -33.790 -11.540 1.00 162.19 ? 76   ASP   D O   1 
ATOM   8822  C  CB  . ASP   D 1 7   ? 13.186  -32.471 -12.736 1.00 171.18 ? 76   ASP   D CB  1 
ATOM   8823  C  CG  . ASP   D 1 7   ? 14.457  -31.734 -13.109 1.00 175.43 ? 76   ASP   D CG  1 
ATOM   8824  O  OD1 . ASP   D 1 7   ? 15.172  -31.289 -12.189 1.00 174.90 ? 76   ASP   D OD1 1 
ATOM   8825  O  OD2 . ASP   D 1 7   ? 14.715  -31.571 -14.324 1.00 176.30 ? 76   ASP   D OD2 1 
ATOM   8826  N  N   . SER   D 1 8   ? 12.010  -35.850 -11.724 1.00 147.04 ? 77   SER   D N   1 
ATOM   8827  C  CA  . SER   D 1 8   ? 10.732  -36.519 -11.486 1.00 147.57 ? 77   SER   D CA  1 
ATOM   8828  C  C   . SER   D 1 8   ? 10.292  -36.383 -10.029 1.00 145.52 ? 77   SER   D C   1 
ATOM   8829  O  O   . SER   D 1 8   ? 11.106  -36.226 -9.113  1.00 137.11 ? 77   SER   D O   1 
ATOM   8830  C  CB  . SER   D 1 8   ? 10.802  -38.004 -11.867 1.00 140.05 ? 77   SER   D CB  1 
ATOM   8831  O  OG  . SER   D 1 8   ? 9.519   -38.627 -11.820 1.00 130.58 ? 77   SER   D OG  1 
ATOM   8832  N  N   . CYS   D 1 9   ? 8.977   -36.435 -9.824  1.00 154.49 ? 78   CYS   D N   1 
ATOM   8833  C  CA  . CYS   D 1 9   ? 8.365   -36.384 -8.500  1.00 154.99 ? 78   CYS   D CA  1 
ATOM   8834  C  C   . CYS   D 1 9   ? 7.783   -37.772 -8.262  1.00 156.06 ? 78   CYS   D C   1 
ATOM   8835  O  O   . CYS   D 1 9   ? 6.621   -38.027 -8.575  1.00 158.14 ? 78   CYS   D O   1 
ATOM   8836  C  CB  . CYS   D 1 9   ? 7.281   -35.307 -8.402  1.00 156.33 ? 78   CYS   D CB  1 
ATOM   8837  S  SG  . CYS   D 1 9   ? 7.784   -33.731 -9.060  1.00 168.57 ? 78   CYS   D SG  1 
ATOM   8838  N  N   . GLN   D 1 10  ? 8.608   -38.667 -7.732  1.00 135.57 ? 79   GLN   D N   1 
ATOM   8839  C  CA  . GLN   D 1 10  ? 8.212   -40.043 -7.481  1.00 129.48 ? 79   GLN   D CA  1 
ATOM   8840  C  C   . GLN   D 1 10  ? 7.936   -40.237 -5.995  1.00 119.98 ? 79   GLN   D C   1 
ATOM   8841  O  O   . GLN   D 1 10  ? 8.165   -39.352 -5.175  1.00 121.26 ? 79   GLN   D O   1 
ATOM   8842  C  CB  . GLN   D 1 10  ? 9.313   -40.986 -7.985  1.00 128.59 ? 79   GLN   D CB  1 
ATOM   8843  C  CG  . GLN   D 1 10  ? 9.681   -40.720 -9.445  1.00 131.99 ? 79   GLN   D CG  1 
ATOM   8844  C  CD  . GLN   D 1 10  ? 10.850  -41.570 -9.950  1.00 135.04 ? 79   GLN   D CD  1 
ATOM   8845  O  OE1 . GLN   D 1 10  ? 11.812  -41.847 -9.223  1.00 131.82 ? 79   GLN   D OE1 1 
ATOM   8846  N  NE2 . GLN   D 1 10  ? 10.775  -41.973 -11.214 1.00 140.23 ? 79   GLN   D NE2 1 
ATOM   8847  N  N   . VAL   D 1 11  ? 7.413   -41.407 -5.655  1.00 119.06 ? 80   VAL   D N   1 
ATOM   8848  C  CA  . VAL   D 1 11  ? 7.055   -41.733 -4.280  1.00 119.18 ? 80   VAL   D CA  1 
ATOM   8849  C  C   . VAL   D 1 11  ? 7.679   -43.077 -3.943  1.00 117.16 ? 80   VAL   D C   1 
ATOM   8850  O  O   . VAL   D 1 11  ? 7.172   -44.126 -4.360  1.00 116.94 ? 80   VAL   D O   1 
ATOM   8851  C  CB  . VAL   D 1 11  ? 5.538   -41.773 -4.064  1.00 122.37 ? 80   VAL   D CB  1 
ATOM   8852  C  CG1 . VAL   D 1 11  ? 5.220   -41.951 -2.566  1.00 119.83 ? 80   VAL   D CG1 1 
ATOM   8853  C  CG2 . VAL   D 1 11  ? 4.884   -40.518 -4.635  1.00 120.67 ? 80   VAL   D CG2 1 
ATOM   8854  N  N   . ILE   D 1 12  ? 8.741   -43.050 -3.150  1.00 117.35 ? 81   ILE   D N   1 
ATOM   8855  C  CA  . ILE   D 1 12  ? 9.598   -44.208 -2.913  1.00 117.33 ? 81   ILE   D CA  1 
ATOM   8856  C  C   . ILE   D 1 12  ? 9.480   -44.640 -1.456  1.00 118.90 ? 81   ILE   D C   1 
ATOM   8857  O  O   . ILE   D 1 12  ? 9.334   -43.788 -0.567  1.00 121.42 ? 81   ILE   D O   1 
ATOM   8858  C  CB  . ILE   D 1 12  ? 11.053  -43.867 -3.284  1.00 118.79 ? 81   ILE   D CB  1 
ATOM   8859  C  CG1 . ILE   D 1 12  ? 11.144  -43.490 -4.770  1.00 119.89 ? 81   ILE   D CG1 1 
ATOM   8860  C  CG2 . ILE   D 1 12  ? 12.014  -45.000 -2.912  1.00 117.61 ? 81   ILE   D CG2 1 
ATOM   8861  C  CD1 . ILE   D 1 12  ? 12.256  -42.515 -5.089  1.00 118.49 ? 81   ILE   D CD1 1 
ATOM   8862  N  N   . PRO   D 1 13  ? 9.507   -45.934 -1.162  1.00 116.24 ? 82   PRO   D N   1 
ATOM   8863  C  CA  . PRO   D 1 13  ? 9.529   -46.379 0.237   1.00 118.01 ? 82   PRO   D CA  1 
ATOM   8864  C  C   . PRO   D 1 13  ? 10.894  -46.192 0.873   1.00 114.89 ? 82   PRO   D C   1 
ATOM   8865  O  O   . PRO   D 1 13  ? 11.930  -46.307 0.221   1.00 116.41 ? 82   PRO   D O   1 
ATOM   8866  C  CB  . PRO   D 1 13  ? 9.181   -47.865 0.135   1.00 115.53 ? 82   PRO   D CB  1 
ATOM   8867  C  CG  . PRO   D 1 13  ? 9.631   -48.242 -1.243  1.00 120.76 ? 82   PRO   D CG  1 
ATOM   8868  C  CD  . PRO   D 1 13  ? 9.317   -47.050 -2.097  1.00 116.18 ? 82   PRO   D CD  1 
ATOM   8869  N  N   . VAL   D 1 14  ? 10.876  -45.932 2.175   1.00 116.29 ? 83   VAL   D N   1 
ATOM   8870  C  CA  . VAL   D 1 14  ? 12.063  -45.543 2.930   1.00 122.95 ? 83   VAL   D CA  1 
ATOM   8871  C  C   . VAL   D 1 14  ? 12.553  -46.725 3.744   1.00 131.41 ? 83   VAL   D C   1 
ATOM   8872  O  O   . VAL   D 1 14  ? 11.758  -47.374 4.428   1.00 138.91 ? 83   VAL   D O   1 
ATOM   8873  C  CB  . VAL   D 1 14  ? 11.764  -44.372 3.877   1.00 126.62 ? 83   VAL   D CB  1 
ATOM   8874  C  CG1 . VAL   D 1 14  ? 13.023  -44.000 4.667   1.00 125.75 ? 83   VAL   D CG1 1 
ATOM   8875  C  CG2 . VAL   D 1 14  ? 11.208  -43.200 3.111   1.00 127.08 ? 83   VAL   D CG2 1 
ATOM   8876  N  N   . LEU   D 1 15  ? 13.866  -46.970 3.713   1.00 127.13 ? 84   LEU   D N   1 
ATOM   8877  C  CA  . LEU   D 1 15  ? 14.462  -47.865 4.693   1.00 135.28 ? 84   LEU   D CA  1 
ATOM   8878  C  C   . LEU   D 1 15  ? 14.096  -47.349 6.078   1.00 143.50 ? 84   LEU   D C   1 
ATOM   8879  O  O   . LEU   D 1 15  ? 14.560  -46.274 6.471   1.00 145.57 ? 84   LEU   D O   1 
ATOM   8880  C  CB  . LEU   D 1 15  ? 15.980  -47.935 4.531   1.00 131.89 ? 84   LEU   D CB  1 
ATOM   8881  C  CG  . LEU   D 1 15  ? 16.617  -49.181 3.899   1.00 123.18 ? 84   LEU   D CG  1 
ATOM   8882  C  CD1 . LEU   D 1 15  ? 18.125  -49.128 4.106   1.00 117.56 ? 84   LEU   D CD1 1 
ATOM   8883  C  CD2 . LEU   D 1 15  ? 16.040  -50.497 4.444   1.00 118.11 ? 84   LEU   D CD2 1 
ATOM   8884  N  N   . PRO   D 1 16  ? 13.267  -48.047 6.895   1.00 160.63 ? 85   PRO   D N   1 
ATOM   8885  C  CA  . PRO   D 1 16  ? 12.833  -47.478 8.165   1.00 165.63 ? 85   PRO   D CA  1 
ATOM   8886  C  C   . PRO   D 1 16  ? 13.883  -46.951 9.128   1.00 165.06 ? 85   PRO   D C   1 
ATOM   8887  O  O   . PRO   D 1 16  ? 13.813  -45.785 9.560   1.00 165.80 ? 85   PRO   D O   1 
ATOM   8888  C  CB  . PRO   D 1 16  ? 12.141  -48.658 8.855   1.00 167.91 ? 85   PRO   D CB  1 
ATOM   8889  C  CG  . PRO   D 1 16  ? 11.595  -49.467 7.710   1.00 167.37 ? 85   PRO   D CG  1 
ATOM   8890  C  CD  . PRO   D 1 16  ? 12.735  -49.416 6.715   1.00 163.68 ? 85   PRO   D CD  1 
ATOM   8891  N  N   . GLN   D 1 17  ? 14.822  -47.815 9.504   1.00 154.89 ? 86   GLN   D N   1 
ATOM   8892  C  CA  . GLN   D 1 17  ? 15.852  -47.398 10.483  1.00 150.07 ? 86   GLN   D CA  1 
ATOM   8893  C  C   . GLN   D 1 17  ? 17.034  -47.001 9.594   1.00 153.35 ? 86   GLN   D C   1 
ATOM   8894  O  O   . GLN   D 1 17  ? 17.843  -47.886 9.247   1.00 152.93 ? 86   GLN   D O   1 
ATOM   8895  C  CB  . GLN   D 1 17  ? 16.208  -48.507 11.470  1.00 146.44 ? 86   GLN   D CB  1 
ATOM   8896  C  CG  . GLN   D 1 17  ? 15.031  -49.403 11.837  1.00 145.58 ? 86   GLN   D CG  1 
ATOM   8897  C  CD  . GLN   D 1 17  ? 15.161  -50.025 13.210  1.00 138.31 ? 86   GLN   D CD  1 
ATOM   8898  O  OE1 . GLN   D 1 17  ? 16.259  -50.373 13.660  1.00 138.55 ? 86   GLN   D OE1 1 
ATOM   8899  N  NE2 . GLN   D 1 17  ? 14.035  -50.172 13.892  1.00 134.03 ? 86   GLN   D NE2 1 
ATOM   8900  N  N   . VAL   D 1 18  ? 17.109  -45.722 9.231   1.00 158.93 ? 87   VAL   D N   1 
ATOM   8901  C  CA  . VAL   D 1 18  ? 18.215  -45.238 8.357   1.00 155.46 ? 87   VAL   D CA  1 
ATOM   8902  C  C   . VAL   D 1 18  ? 18.709  -43.854 8.798   1.00 155.17 ? 87   VAL   D C   1 
ATOM   8903  O  O   . VAL   D 1 18  ? 17.876  -43.051 9.266   1.00 155.40 ? 87   VAL   D O   1 
ATOM   8904  C  CB  . VAL   D 1 18  ? 17.748  -45.105 6.897   1.00 155.69 ? 87   VAL   D CB  1 
ATOM   8905  C  CG1 . VAL   D 1 18  ? 17.004  -43.801 6.640   1.00 155.64 ? 87   VAL   D CG1 1 
ATOM   8906  C  CG2 . VAL   D 1 18  ? 18.894  -45.285 5.910   1.00 151.57 ? 87   VAL   D CG2 1 
ATOM   8907  N  N   . MET   D 1 19  ? 20.012  -43.608 8.672   1.00 147.08 ? 88   MET   D N   1 
ATOM   8908  C  CA  . MET   D 1 19  ? 20.592  -42.324 9.095   1.00 144.60 ? 88   MET   D CA  1 
ATOM   8909  C  C   . MET   D 1 19  ? 21.806  -41.972 8.202   1.00 138.56 ? 88   MET   D C   1 
ATOM   8910  O  O   . MET   D 1 19  ? 22.507  -40.986 8.505   1.00 136.88 ? 88   MET   D O   1 
ATOM   8911  C  CB  . MET   D 1 19  ? 20.942  -42.431 10.571  1.00 145.13 ? 88   MET   D CB  1 
ATOM   8912  C  CG  . MET   D 1 19  ? 22.052  -43.422 10.871  1.00 144.91 ? 88   MET   D CG  1 
ATOM   8913  S  SD  . MET   D 1 19  ? 22.181  -43.826 12.625  1.00 148.89 ? 88   MET   D SD  1 
ATOM   8914  C  CE  . MET   D 1 19  ? 21.027  -45.199 12.741  1.00 149.38 ? 88   MET   D CE  1 
ATOM   8915  N  N   . MET   D 1 20  ? 22.022  -42.749 7.142   1.00 136.39 ? 89   MET   D N   1 
ATOM   8916  C  CA  . MET   D 1 20  ? 23.231  -42.563 6.333   1.00 131.81 ? 89   MET   D CA  1 
ATOM   8917  C  C   . MET   D 1 20  ? 23.217  -41.445 5.259   1.00 127.79 ? 89   MET   D C   1 
ATOM   8918  O  O   . MET   D 1 20  ? 22.139  -40.863 5.028   1.00 128.60 ? 89   MET   D O   1 
ATOM   8919  C  CB  . MET   D 1 20  ? 23.495  -43.890 5.621   1.00 129.41 ? 89   MET   D CB  1 
ATOM   8920  C  CG  . MET   D 1 20  ? 24.815  -43.965 4.880   1.00 130.61 ? 89   MET   D CG  1 
ATOM   8921  S  SD  . MET   D 1 20  ? 25.108  -45.598 4.175   1.00 134.66 ? 89   MET   D SD  1 
ATOM   8922  C  CE  . MET   D 1 20  ? 25.633  -46.513 5.630   1.00 132.26 ? 89   MET   D CE  1 
ATOM   8923  N  N   . ILE   D 1 21  ? 24.374  -41.157 4.664   1.00 120.58 ? 90   ILE   D N   1 
ATOM   8924  C  CA  . ILE   D 1 21  ? 24.443  -40.173 3.550   1.00 112.46 ? 90   ILE   D CA  1 
ATOM   8925  C  C   . ILE   D 1 21  ? 24.997  -41.015 2.394   1.00 110.41 ? 90   ILE   D C   1 
ATOM   8926  O  O   . ILE   D 1 21  ? 26.214  -40.952 2.144   1.00 109.45 ? 90   ILE   D O   1 
ATOM   8927  C  CB  . ILE   D 1 21  ? 25.364  -38.997 3.912   1.00 108.85 ? 90   ILE   D CB  1 
ATOM   8928  C  CG1 . ILE   D 1 21  ? 25.349  -38.705 5.410   1.00 104.56 ? 90   ILE   D CG1 1 
ATOM   8929  C  CG2 . ILE   D 1 21  ? 25.010  -37.758 3.093   1.00 107.00 ? 90   ILE   D CG2 1 
ATOM   8930  C  CD1 . ILE   D 1 21  ? 24.452  -37.546 5.801   1.00 100.20 ? 90   ILE   D CD1 1 
ATOM   8931  N  N   . LEU   D 1 22  ? 24.139  -41.801 1.745   1.00 108.00 ? 91   LEU   D N   1 
ATOM   8932  C  CA  . LEU   D 1 22  ? 24.610  -42.704 0.665   1.00 102.38 ? 91   LEU   D CA  1 
ATOM   8933  C  C   . LEU   D 1 22  ? 25.000  -41.713 -0.431  1.00 96.15  ? 91   LEU   D C   1 
ATOM   8934  O  O   . LEU   D 1 22  ? 24.108  -41.032 -0.954  1.00 94.85  ? 91   LEU   D O   1 
ATOM   8935  C  CB  . LEU   D 1 22  ? 23.529  -43.701 0.260   1.00 100.41 ? 91   LEU   D CB  1 
ATOM   8936  C  CG  . LEU   D 1 22  ? 24.028  -44.946 -0.476  1.00 98.84  ? 91   LEU   D CG  1 
ATOM   8937  C  CD1 . LEU   D 1 22  ? 25.237  -45.510 0.242   1.00 102.47 ? 91   LEU   D CD1 1 
ATOM   8938  C  CD2 . LEU   D 1 22  ? 22.927  -45.979 -0.538  1.00 98.89  ? 91   LEU   D CD2 1 
ATOM   8939  N  N   . ILE   D 1 23  ? 26.285  -41.639 -0.756  1.00 94.60  ? 92   ILE   D N   1 
ATOM   8940  C  CA  . ILE   D 1 23  ? 26.698  -40.767 -1.888  1.00 96.51  ? 92   ILE   D CA  1 
ATOM   8941  C  C   . ILE   D 1 23  ? 26.454  -41.664 -3.105  1.00 100.01 ? 92   ILE   D C   1 
ATOM   8942  O  O   . ILE   D 1 23  ? 26.931  -42.814 -3.096  1.00 99.86  ? 92   ILE   D O   1 
ATOM   8943  C  CB  . ILE   D 1 23  ? 28.168  -40.339 -1.770  1.00 96.84  ? 92   ILE   D CB  1 
ATOM   8944  C  CG1 . ILE   D 1 23  ? 28.382  -39.403 -0.592  1.00 92.03  ? 92   ILE   D CG1 1 
ATOM   8945  C  CG2 . ILE   D 1 23  ? 28.667  -39.721 -3.076  1.00 93.29  ? 92   ILE   D CG2 1 
ATOM   8946  C  CD1 . ILE   D 1 23  ? 29.790  -38.851 -0.510  1.00 89.84  ? 92   ILE   D CD1 1 
ATOM   8947  N  N   . PRO   D 1 24  ? 25.703  -41.204 -4.123  1.00 98.73  ? 93   PRO   D N   1 
ATOM   8948  C  CA  . PRO   D 1 24  ? 25.401  -42.039 -5.268  1.00 90.51  ? 93   PRO   D CA  1 
ATOM   8949  C  C   . PRO   D 1 24  ? 26.612  -42.852 -5.643  1.00 95.20  ? 93   PRO   D C   1 
ATOM   8950  O  O   . PRO   D 1 24  ? 27.665  -42.270 -5.940  1.00 96.55  ? 93   PRO   D O   1 
ATOM   8951  C  CB  . PRO   D 1 24  ? 25.071  -40.989 -6.314  1.00 85.92  ? 93   PRO   D CB  1 
ATOM   8952  C  CG  . PRO   D 1 24  ? 24.388  -39.903 -5.529  1.00 88.62  ? 93   PRO   D CG  1 
ATOM   8953  C  CD  . PRO   D 1 24  ? 25.113  -39.882 -4.197  1.00 95.85  ? 93   PRO   D CD  1 
ATOM   8954  N  N   . GLY   D 1 25  ? 26.476  -44.176 -5.635  1.00 103.68 ? 94   GLY   D N   1 
ATOM   8955  C  CA  . GLY   D 1 25  ? 27.589  -45.038 -6.071  1.00 107.37 ? 94   GLY   D CA  1 
ATOM   8956  C  C   . GLY   D 1 25  ? 28.073  -45.923 -4.945  1.00 109.76 ? 94   GLY   D C   1 
ATOM   8957  O  O   . GLY   D 1 25  ? 28.396  -47.098 -5.204  1.00 108.36 ? 94   GLY   D O   1 
ATOM   8958  N  N   . GLN   D 1 26  ? 28.125  -45.379 -3.732  1.00 107.63 ? 95   GLN   D N   1 
ATOM   8959  C  CA  . GLN   D 1 26  ? 28.553  -46.186 -2.568  1.00 106.11 ? 95   GLN   D CA  1 
ATOM   8960  C  C   . GLN   D 1 26  ? 27.608  -47.378 -2.422  1.00 105.82 ? 95   GLN   D C   1 
ATOM   8961  O  O   . GLN   D 1 26  ? 26.403  -47.223 -2.709  1.00 107.17 ? 95   GLN   D O   1 
ATOM   8962  C  CB  . GLN   D 1 26  ? 28.487  -45.398 -1.263  1.00 111.07 ? 95   GLN   D CB  1 
ATOM   8963  C  CG  . GLN   D 1 26  ? 29.398  -44.180 -1.188  1.00 112.94 ? 95   GLN   D CG  1 
ATOM   8964  C  CD  . GLN   D 1 26  ? 29.278  -43.459 0.135   1.00 109.83 ? 95   GLN   D CD  1 
ATOM   8965  O  OE1 . GLN   D 1 26  ? 28.206  -42.967 0.505   1.00 109.25 ? 95   GLN   D OE1 1 
ATOM   8966  N  NE2 . GLN   D 1 26  ? 30.374  -43.407 0.876   1.00 103.75 ? 95   GLN   D NE2 1 
ATOM   8967  N  N   . THR   D 1 27  ? 28.134  -48.515 -1.972  1.00 99.13  ? 96   THR   D N   1 
ATOM   8968  C  CA  . THR   D 1 27  ? 27.269  -49.678 -1.719  1.00 96.25  ? 96   THR   D CA  1 
ATOM   8969  C  C   . THR   D 1 27  ? 26.874  -49.648 -0.266  1.00 96.08  ? 96   THR   D C   1 
ATOM   8970  O  O   . THR   D 1 27  ? 27.740  -49.354 0.575   1.00 98.21  ? 96   THR   D O   1 
ATOM   8971  C  CB  . THR   D 1 27  ? 28.034  -50.946 -2.070  1.00 96.25  ? 96   THR   D CB  1 
ATOM   8972  O  OG1 . THR   D 1 27  ? 28.941  -51.131 -0.989  1.00 106.53 ? 96   THR   D OG1 1 
ATOM   8973  C  CG2 . THR   D 1 27  ? 28.795  -50.812 -3.376  1.00 97.16  ? 96   THR   D CG2 1 
ATOM   8974  N  N   . LEU   D 1 28  ? 25.604  -49.914 0.021   1.00 93.34  ? 97   LEU   D N   1 
ATOM   8975  C  CA  . LEU   D 1 28  ? 25.117  -49.899 1.420   1.00 93.69  ? 97   LEU   D CA  1 
ATOM   8976  C  C   . LEU   D 1 28  ? 24.882  -51.342 1.867   1.00 96.58  ? 97   LEU   D C   1 
ATOM   8977  O  O   . LEU   D 1 28  ? 23.905  -51.957 1.404   1.00 100.96 ? 97   LEU   D O   1 
ATOM   8978  C  CB  . LEU   D 1 28  ? 23.839  -49.072 1.521   1.00 92.82  ? 97   LEU   D CB  1 
ATOM   8979  C  CG  . LEU   D 1 28  ? 23.077  -49.155 2.847   1.00 91.01  ? 97   LEU   D CG  1 
ATOM   8980  C  CD1 . LEU   D 1 28  ? 23.218  -47.861 3.621   1.00 95.34  ? 97   LEU   D CD1 1 
ATOM   8981  C  CD2 . LEU   D 1 28  ? 21.616  -49.452 2.575   1.00 93.43  ? 97   LEU   D CD2 1 
ATOM   8982  N  N   . PRO   D 1 29  ? 25.741  -51.912 2.733   1.00 94.28  ? 98   PRO   D N   1 
ATOM   8983  C  CA  . PRO   D 1 29  ? 25.501  -53.250 3.241   1.00 93.09  ? 98   PRO   D CA  1 
ATOM   8984  C  C   . PRO   D 1 29  ? 24.318  -53.207 4.179   1.00 95.84  ? 98   PRO   D C   1 
ATOM   8985  O  O   . PRO   D 1 29  ? 24.052  -52.147 4.769   1.00 98.02  ? 98   PRO   D O   1 
ATOM   8986  C  CB  . PRO   D 1 29  ? 26.803  -53.564 3.960   1.00 94.68  ? 98   PRO   D CB  1 
ATOM   8987  C  CG  . PRO   D 1 29  ? 27.328  -52.212 4.377   1.00 99.36  ? 98   PRO   D CG  1 
ATOM   8988  C  CD  . PRO   D 1 29  ? 26.950  -51.291 3.234   1.00 95.33  ? 98   PRO   D CD  1 
ATOM   8989  N  N   . LEU   D 1 30  ? 23.625  -54.334 4.332   1.00 96.53  ? 99   LEU   D N   1 
ATOM   8990  C  CA  . LEU   D 1 30  ? 22.400  -54.339 5.165   1.00 102.30 ? 99   LEU   D CA  1 
ATOM   8991  C  C   . LEU   D 1 30  ? 22.070  -55.769 5.608   1.00 113.11 ? 99   LEU   D C   1 
ATOM   8992  O  O   . LEU   D 1 30  ? 22.290  -56.694 4.807   1.00 115.33 ? 99   LEU   D O   1 
ATOM   8993  C  CB  . LEU   D 1 30  ? 21.282  -53.744 4.317   1.00 104.19 ? 99   LEU   D CB  1 
ATOM   8994  C  CG  . LEU   D 1 30  ? 20.213  -52.945 5.065   1.00 103.80 ? 99   LEU   D CG  1 
ATOM   8995  C  CD1 . LEU   D 1 30  ? 20.804  -51.664 5.617   1.00 105.22 ? 99   LEU   D CD1 1 
ATOM   8996  C  CD2 . LEU   D 1 30  ? 19.084  -52.637 4.105   1.00 96.71  ? 99   LEU   D CD2 1 
ATOM   8997  N  N   . GLN   D 1 31  ? 21.572  -55.935 6.837   1.00 117.36 ? 100  GLN   D N   1 
ATOM   8998  C  CA  . GLN   D 1 31  ? 21.158  -57.271 7.340   1.00 118.43 ? 100  GLN   D CA  1 
ATOM   8999  C  C   . GLN   D 1 31  ? 19.813  -57.108 8.054   1.00 123.56 ? 100  GLN   D C   1 
ATOM   9000  O  O   . GLN   D 1 31  ? 19.813  -56.653 9.213   1.00 126.95 ? 100  GLN   D O   1 
ATOM   9001  C  CB  . GLN   D 1 31  ? 22.185  -57.853 8.307   1.00 110.63 ? 100  GLN   D CB  1 
ATOM   9002  N  N   . LEU   D 1 32  ? 18.717  -57.467 7.390   1.00 127.56 ? 101  LEU   D N   1 
ATOM   9003  C  CA  . LEU   D 1 32  ? 17.373  -57.240 7.977   1.00 131.04 ? 101  LEU   D CA  1 
ATOM   9004  C  C   . LEU   D 1 32  ? 16.868  -58.459 8.758   1.00 139.67 ? 101  LEU   D C   1 
ATOM   9005  O  O   . LEU   D 1 32  ? 17.374  -59.572 8.507   1.00 144.52 ? 101  LEU   D O   1 
ATOM   9006  C  CB  . LEU   D 1 32  ? 16.390  -57.080 6.823   1.00 133.90 ? 101  LEU   D CB  1 
ATOM   9007  C  CG  . LEU   D 1 32  ? 16.603  -55.851 5.935   1.00 126.97 ? 101  LEU   D CG  1 
ATOM   9008  C  CD1 . LEU   D 1 32  ? 15.661  -55.887 4.748   1.00 121.37 ? 101  LEU   D CD1 1 
ATOM   9009  C  CD2 . LEU   D 1 32  ? 16.391  -54.586 6.743   1.00 125.54 ? 101  LEU   D CD2 1 
ATOM   9010  N  N   . PHE   D 1 33  ? 15.899  -58.248 9.655   1.00 146.83 ? 102  PHE   D N   1 
ATOM   9011  C  CA  . PHE   D 1 33  ? 15.344  -59.351 10.484  1.00 148.51 ? 102  PHE   D CA  1 
ATOM   9012  C  C   . PHE   D 1 33  ? 13.831  -59.212 10.650  1.00 153.07 ? 102  PHE   D C   1 
ATOM   9013  O  O   . PHE   D 1 33  ? 13.086  -60.157 10.327  1.00 153.28 ? 102  PHE   D O   1 
ATOM   9014  C  CB  . PHE   D 1 33  ? 16.076  -59.219 11.822  1.00 145.44 ? 102  PHE   D CB  1 
ATOM   9015  N  N   . HIS   D 1 34  ? 13.382  -58.056 11.143  1.00 158.41 ? 103  HIS   D N   1 
ATOM   9016  C  CA  . HIS   D 1 34  ? 11.928  -57.828 11.361  1.00 157.65 ? 103  HIS   D CA  1 
ATOM   9017  C  C   . HIS   D 1 34  ? 11.175  -58.049 10.047  1.00 160.34 ? 103  HIS   D C   1 
ATOM   9018  O  O   . HIS   D 1 34  ? 11.651  -57.610 8.980   1.00 158.85 ? 103  HIS   D O   1 
ATOM   9019  C  CB  . HIS   D 1 34  ? 11.684  -56.436 11.951  1.00 147.05 ? 103  HIS   D CB  1 
ATOM   9020  N  N   . PRO   D 1 35  ? 9.997   -58.706 10.076  1.00 162.78 ? 104  PRO   D N   1 
ATOM   9021  C  CA  . PRO   D 1 35  ? 9.270   -59.023 8.851   1.00 161.78 ? 104  PRO   D CA  1 
ATOM   9022  C  C   . PRO   D 1 35  ? 8.920   -57.896 7.895   1.00 162.14 ? 104  PRO   D C   1 
ATOM   9023  O  O   . PRO   D 1 35  ? 9.233   -58.015 6.697   1.00 158.62 ? 104  PRO   D O   1 
ATOM   9024  C  CB  . PRO   D 1 35  ? 7.960   -59.612 9.397   1.00 159.40 ? 104  PRO   D CB  1 
ATOM   9025  C  CG  . PRO   D 1 35  ? 8.355   -60.189 10.733  1.00 167.83 ? 104  PRO   D CG  1 
ATOM   9026  C  CD  . PRO   D 1 35  ? 9.340   -59.175 11.281  1.00 167.22 ? 104  PRO   D CD  1 
ATOM   9027  N  N   . GLN   D 1 36  ? 8.255   -56.851 8.394   1.00 171.91 ? 105  GLN   D N   1 
ATOM   9028  C  CA  . GLN   D 1 36  ? 7.813   -55.727 7.528   1.00 169.60 ? 105  GLN   D CA  1 
ATOM   9029  C  C   . GLN   D 1 36  ? 8.926   -55.245 6.591   1.00 167.86 ? 105  GLN   D C   1 
ATOM   9030  O  O   . GLN   D 1 36  ? 8.611   -54.841 5.453   1.00 165.98 ? 105  GLN   D O   1 
ATOM   9031  C  CB  . GLN   D 1 36  ? 7.508   -54.515 8.407   1.00 164.54 ? 105  GLN   D CB  1 
ATOM   9032  N  N   . GLU   D 1 37  ? 10.171  -55.271 7.064   1.00 158.29 ? 106  GLU   D N   1 
ATOM   9033  C  CA  . GLU   D 1 37  ? 11.320  -54.846 6.228   1.00 152.17 ? 106  GLU   D CA  1 
ATOM   9034  C  C   . GLU   D 1 37  ? 11.377  -55.852 5.076   1.00 150.16 ? 106  GLU   D C   1 
ATOM   9035  O  O   . GLU   D 1 37  ? 11.160  -55.450 3.916   1.00 145.67 ? 106  GLU   D O   1 
ATOM   9036  C  CB  . GLU   D 1 37  ? 12.591  -54.961 7.065   1.00 144.29 ? 106  GLU   D CB  1 
ATOM   9037  N  N   . VAL   D 1 38  ? 11.665  -57.112 5.397   1.00 150.90 ? 107  VAL   D N   1 
ATOM   9038  C  CA  . VAL   D 1 38  ? 11.804  -58.154 4.340   1.00 145.53 ? 107  VAL   D CA  1 
ATOM   9039  C  C   . VAL   D 1 38  ? 10.596  -58.091 3.397   1.00 143.81 ? 107  VAL   D C   1 
ATOM   9040  O  O   . VAL   D 1 38  ? 10.801  -58.120 2.172   1.00 138.99 ? 107  VAL   D O   1 
ATOM   9041  C  CB  . VAL   D 1 38  ? 11.934  -59.536 5.000   1.00 140.60 ? 107  VAL   D CB  1 
ATOM   9042  C  CG1 . VAL   D 1 38  ? 12.504  -60.566 4.035   1.00 134.09 ? 107  VAL   D CG1 1 
ATOM   9043  C  CG2 . VAL   D 1 38  ? 12.766  -59.471 6.275   1.00 143.20 ? 107  VAL   D CG2 1 
ATOM   9044  N  N   . SER   D 1 39  ? 9.386   -58.034 3.949   1.00 147.43 ? 108  SER   D N   1 
ATOM   9045  C  CA  . SER   D 1 39  ? 8.178   -58.047 3.090   1.00 144.20 ? 108  SER   D CA  1 
ATOM   9046  C  C   . SER   D 1 39  ? 8.323   -56.963 2.020   1.00 142.45 ? 108  SER   D C   1 
ATOM   9047  O  O   . SER   D 1 39  ? 8.167   -57.275 0.819   1.00 138.61 ? 108  SER   D O   1 
ATOM   9048  C  CB  . SER   D 1 39  ? 6.945   -57.834 3.909   1.00 148.91 ? 108  SER   D CB  1 
ATOM   9049  O  OG  . SER   D 1 39  ? 7.173   -58.177 5.268   1.00 151.71 ? 108  SER   D OG  1 
ATOM   9050  N  N   . MET   D 1 40  ? 8.613   -55.738 2.451   1.00 145.88 ? 109  MET   D N   1 
ATOM   9051  C  CA  . MET   D 1 40  ? 8.799   -54.623 1.492   1.00 147.57 ? 109  MET   D CA  1 
ATOM   9052  C  C   . MET   D 1 40  ? 9.906   -55.007 0.505   1.00 145.66 ? 109  MET   D C   1 
ATOM   9053  O  O   . MET   D 1 40  ? 9.664   -54.937 -0.716  1.00 143.49 ? 109  MET   D O   1 
ATOM   9054  C  CB  . MET   D 1 40  ? 9.207   -53.342 2.225   1.00 146.54 ? 109  MET   D CB  1 
ATOM   9055  N  N   . VAL   D 1 41  ? 11.072  -55.392 1.028   1.00 142.51 ? 110  VAL   D N   1 
ATOM   9056  C  CA  . VAL   D 1 41  ? 12.215  -55.778 0.151   1.00 136.89 ? 110  VAL   D CA  1 
ATOM   9057  C  C   . VAL   D 1 41  ? 11.689  -56.716 -0.942  1.00 137.04 ? 110  VAL   D C   1 
ATOM   9058  O  O   . VAL   D 1 41  ? 11.877  -56.403 -2.125  1.00 133.45 ? 110  VAL   D O   1 
ATOM   9059  C  CB  . VAL   D 1 41  ? 13.344  -56.441 0.959   1.00 134.83 ? 110  VAL   D CB  1 
ATOM   9060  C  CG1 . VAL   D 1 41  ? 14.512  -56.845 0.072   1.00 128.31 ? 110  VAL   D CG1 1 
ATOM   9061  C  CG2 . VAL   D 1 41  ? 13.828  -55.544 2.090   1.00 133.38 ? 110  VAL   D CG2 1 
ATOM   9062  N  N   . ARG   D 1 42  ? 11.051  -57.816 -0.547  1.00 139.79 ? 111  ARG   D N   1 
ATOM   9063  C  CA  . ARG   D 1 42  ? 10.544  -58.798 -1.536  1.00 137.93 ? 111  ARG   D CA  1 
ATOM   9064  C  C   . ARG   D 1 42  ? 9.821   -58.040 -2.655  1.00 139.97 ? 111  ARG   D C   1 
ATOM   9065  O  O   . ARG   D 1 42  ? 10.251  -58.137 -3.825  1.00 140.89 ? 111  ARG   D O   1 
ATOM   9066  C  CB  . ARG   D 1 42  ? 9.615   -59.804 -0.852  1.00 133.60 ? 111  ARG   D CB  1 
ATOM   9067  N  N   . ASN   D 1 43  ? 8.759   -57.318 -2.302  1.00 140.63 ? 112  ASN   D N   1 
ATOM   9068  C  CA  . ASN   D 1 43  ? 7.979   -56.586 -3.333  1.00 141.93 ? 112  ASN   D CA  1 
ATOM   9069  C  C   . ASN   D 1 43  ? 8.949   -55.733 -4.152  1.00 143.18 ? 112  ASN   D C   1 
ATOM   9070  O  O   . ASN   D 1 43  ? 8.903   -55.805 -5.395  1.00 141.15 ? 112  ASN   D O   1 
ATOM   9071  C  CB  . ASN   D 1 43  ? 6.868   -55.753 -2.710  1.00 140.27 ? 112  ASN   D CB  1 
ATOM   9072  C  CG  . ASN   D 1 43  ? 5.885   -55.264 -3.745  1.00 140.12 ? 112  ASN   D CG  1 
ATOM   9073  O  OD1 . ASN   D 1 43  ? 5.723   -55.894 -4.795  1.00 140.41 ? 112  ASN   D OD1 1 
ATOM   9074  N  ND2 . ASN   D 1 43  ? 5.222   -54.151 -3.471  1.00 142.63 ? 112  ASN   D ND2 1 
ATOM   9075  N  N   . LEU   D 1 44  ? 9.798   -54.962 -3.472  1.00 143.19 ? 113  LEU   D N   1 
ATOM   9076  C  CA  . LEU   D 1 44  ? 10.749  -54.071 -4.181  1.00 138.78 ? 113  LEU   D CA  1 
ATOM   9077  C  C   . LEU   D 1 44  ? 11.521  -54.884 -5.230  1.00 138.70 ? 113  LEU   D C   1 
ATOM   9078  O  O   . LEU   D 1 44  ? 11.477  -54.502 -6.412  1.00 139.69 ? 113  LEU   D O   1 
ATOM   9079  C  CB  . LEU   D 1 44  ? 11.684  -53.408 -3.173  1.00 134.26 ? 113  LEU   D CB  1 
ATOM   9080  C  CG  . LEU   D 1 44  ? 11.374  -51.948 -2.832  1.00 131.00 ? 113  LEU   D CG  1 
ATOM   9081  C  CD1 . LEU   D 1 44  ? 12.567  -51.307 -2.152  1.00 123.94 ? 113  LEU   D CD1 1 
ATOM   9082  C  CD2 . LEU   D 1 44  ? 11.002  -51.183 -4.087  1.00 130.36 ? 113  LEU   D CD2 1 
ATOM   9083  N  N   . ILE   D 1 45  ? 12.203  -55.956 -4.819  1.00 139.36 ? 114  ILE   D N   1 
ATOM   9084  C  CA  . ILE   D 1 45  ? 13.035  -56.734 -5.786  1.00 134.38 ? 114  ILE   D CA  1 
ATOM   9085  C  C   . ILE   D 1 45  ? 12.181  -57.019 -7.027  1.00 138.29 ? 114  ILE   D C   1 
ATOM   9086  O  O   . ILE   D 1 45  ? 12.699  -56.864 -8.150  1.00 141.25 ? 114  ILE   D O   1 
ATOM   9087  C  CB  . ILE   D 1 45  ? 13.554  -58.042 -5.171  1.00 123.45 ? 114  ILE   D CB  1 
ATOM   9088  C  CG1 . ILE   D 1 45  ? 14.151  -57.825 -3.794  1.00 125.69 ? 114  ILE   D CG1 1 
ATOM   9089  C  CG2 . ILE   D 1 45  ? 14.551  -58.725 -6.108  1.00 113.07 ? 114  ILE   D CG2 1 
ATOM   9090  C  CD1 . ILE   D 1 45  ? 13.929  -58.999 -2.864  1.00 123.84 ? 114  ILE   D CD1 1 
ATOM   9091  N  N   . GLN   D 1 46  ? 10.920  -57.402 -6.825  1.00 136.55 ? 115  GLN   D N   1 
ATOM   9092  C  CA  . GLN   D 1 46  ? 10.035  -57.744 -7.967  1.00 135.70 ? 115  GLN   D CA  1 
ATOM   9093  C  C   . GLN   D 1 46  ? 9.537   -56.499 -8.714  1.00 140.67 ? 115  GLN   D C   1 
ATOM   9094  O  O   . GLN   D 1 46  ? 8.672   -56.653 -9.600  1.00 142.29 ? 115  GLN   D O   1 
ATOM   9095  C  CB  . GLN   D 1 46  ? 8.946   -58.708 -7.501  1.00 129.56 ? 115  GLN   D CB  1 
ATOM   9096  N  N   . LYS   D 1 47  ? 10.067  -55.322 -8.375  1.00 141.24 ? 116  LYS   D N   1 
ATOM   9097  C  CA  . LYS   D 1 47  ? 9.672   -54.068 -9.036  1.00 143.97 ? 116  LYS   D CA  1 
ATOM   9098  C  C   . LYS   D 1 47  ? 10.838  -53.152 -9.421  1.00 146.38 ? 116  LYS   D C   1 
ATOM   9099  O  O   . LYS   D 1 47  ? 11.595  -53.513 -10.343 1.00 145.87 ? 116  LYS   D O   1 
ATOM   9100  C  CB  . LYS   D 1 47  ? 8.740   -53.382 -8.028  1.00 140.74 ? 116  LYS   D CB  1 
ATOM   9101  N  N   . ASP   D 1 48  ? 10.983  -52.023 -8.724  1.00 151.66 ? 117  ASP   D N   1 
ATOM   9102  C  CA  . ASP   D 1 48  ? 12.094  -51.069 -9.008  1.00 150.73 ? 117  ASP   D CA  1 
ATOM   9103  C  C   . ASP   D 1 48  ? 13.290  -51.423 -8.160  1.00 152.34 ? 117  ASP   D C   1 
ATOM   9104  O  O   . ASP   D 1 48  ? 14.386  -50.904 -8.449  1.00 152.92 ? 117  ASP   D O   1 
ATOM   9105  C  CB  . ASP   D 1 48  ? 11.654  -49.633 -8.755  1.00 149.94 ? 117  ASP   D CB  1 
ATOM   9106  C  CG  . ASP   D 1 48  ? 10.979  -49.410 -7.410  1.00 154.79 ? 117  ASP   D CG  1 
ATOM   9107  O  OD1 . ASP   D 1 48  ? 9.846   -49.903 -7.236  1.00 157.90 ? 117  ASP   D OD1 1 
ATOM   9108  O  OD2 . ASP   D 1 48  ? 11.596  -48.753 -6.548  1.00 156.25 ? 117  ASP   D OD2 1 
ATOM   9109  N  N   . ARG   D 1 49  ? 13.087  -52.241 -7.126  1.00 144.63 ? 118  ARG   D N   1 
ATOM   9110  C  CA  . ARG   D 1 49  ? 14.197  -52.669 -6.236  1.00 138.04 ? 118  ARG   D CA  1 
ATOM   9111  C  C   . ARG   D 1 49  ? 14.940  -51.438 -5.703  1.00 135.93 ? 118  ARG   D C   1 
ATOM   9112  O  O   . ARG   D 1 49  ? 16.162  -51.545 -5.492  1.00 134.18 ? 118  ARG   D O   1 
ATOM   9113  C  CB  . ARG   D 1 49  ? 15.153  -53.596 -6.993  1.00 137.91 ? 118  ARG   D CB  1 
ATOM   9114  N  N   . THR   D 1 50  ? 14.234  -50.329 -5.477  1.00 134.84 ? 119  THR   D N   1 
ATOM   9115  C  CA  . THR   D 1 50  ? 14.918  -49.091 -5.052  1.00 128.43 ? 119  THR   D CA  1 
ATOM   9116  C  C   . THR   D 1 50  ? 14.225  -48.508 -3.844  1.00 125.73 ? 119  THR   D C   1 
ATOM   9117  O  O   . THR   D 1 50  ? 13.034  -48.165 -3.957  1.00 128.60 ? 119  THR   D O   1 
ATOM   9118  C  CB  . THR   D 1 50  ? 14.943  -48.100 -6.212  1.00 128.22 ? 119  THR   D CB  1 
ATOM   9119  O  OG1 . THR   D 1 50  ? 15.504  -48.802 -7.316  1.00 130.98 ? 119  THR   D OG1 1 
ATOM   9120  C  CG2 . THR   D 1 50  ? 15.797  -46.883 -5.912  1.00 120.97 ? 119  THR   D CG2 1 
ATOM   9121  N  N   . PHE   D 1 51  ? 14.938  -48.402 -2.722  1.00 117.37 ? 120  PHE   D N   1 
ATOM   9122  C  CA  . PHE   D 1 51  ? 14.356  -47.756 -1.519  1.00 111.36 ? 120  PHE   D CA  1 
ATOM   9123  C  C   . PHE   D 1 51  ? 14.993  -46.388 -1.372  1.00 110.30 ? 120  PHE   D C   1 
ATOM   9124  O  O   . PHE   D 1 51  ? 15.790  -46.001 -2.245  1.00 109.52 ? 120  PHE   D O   1 
ATOM   9125  C  CB  . PHE   D 1 51  ? 14.552  -48.594 -0.254  1.00 107.90 ? 120  PHE   D CB  1 
ATOM   9126  C  CG  . PHE   D 1 51  ? 15.954  -49.127 -0.004  1.00 105.37 ? 120  PHE   D CG  1 
ATOM   9127  C  CD1 . PHE   D 1 51  ? 16.984  -48.280 0.381   1.00 108.15 ? 120  PHE   D CD1 1 
ATOM   9128  C  CD2 . PHE   D 1 51  ? 16.228  -50.483 -0.127  1.00 105.04 ? 120  PHE   D CD2 1 
ATOM   9129  C  CE1 . PHE   D 1 51  ? 18.253  -48.775 0.618   1.00 107.07 ? 120  PHE   D CE1 1 
ATOM   9130  C  CE2 . PHE   D 1 51  ? 17.500  -50.972 0.112   1.00 103.78 ? 120  PHE   D CE2 1 
ATOM   9131  C  CZ  . PHE   D 1 51  ? 18.507  -50.118 0.487   1.00 103.77 ? 120  PHE   D CZ  1 
ATOM   9132  N  N   . ALA   D 1 52  ? 14.671  -45.683 -0.289  1.00 111.71 ? 121  ALA   D N   1 
ATOM   9133  C  CA  . ALA   D 1 52  ? 15.188  -44.309 -0.109  1.00 104.81 ? 121  ALA   D CA  1 
ATOM   9134  C  C   . ALA   D 1 52  ? 16.017  -44.212 1.168   1.00 110.08 ? 121  ALA   D C   1 
ATOM   9135  O  O   . ALA   D 1 52  ? 15.479  -44.481 2.257   1.00 120.28 ? 121  ALA   D O   1 
ATOM   9136  C  CB  . ALA   D 1 52  ? 14.032  -43.349 -0.068  1.00 101.94 ? 121  ALA   D CB  1 
ATOM   9137  N  N   . VAL   D 1 53  ? 17.289  -43.838 1.037   1.00 103.50 ? 122  VAL   D N   1 
ATOM   9138  C  CA  . VAL   D 1 53  ? 18.137  -43.622 2.243   1.00 110.68 ? 122  VAL   D CA  1 
ATOM   9139  C  C   . VAL   D 1 53  ? 17.975  -42.149 2.628   1.00 116.72 ? 122  VAL   D C   1 
ATOM   9140  O  O   . VAL   D 1 53  ? 18.254  -41.292 1.772   1.00 112.37 ? 122  VAL   D O   1 
ATOM   9141  C  CB  . VAL   D 1 53  ? 19.609  -43.975 1.974   1.00 109.44 ? 122  VAL   D CB  1 
ATOM   9142  C  CG1 . VAL   D 1 53  ? 20.546  -43.361 3.007   1.00 118.10 ? 122  VAL   D CG1 1 
ATOM   9143  C  CG2 . VAL   D 1 53  ? 19.817  -45.481 1.886   1.00 109.64 ? 122  VAL   D CG2 1 
ATOM   9144  N  N   . LEU   D 1 54  ? 17.517  -41.877 3.849   1.00 126.26 ? 123  LEU   D N   1 
ATOM   9145  C  CA  . LEU   D 1 54  ? 17.252  -40.480 4.272   1.00 126.88 ? 123  LEU   D CA  1 
ATOM   9146  C  C   . LEU   D 1 54  ? 18.462  -39.925 5.027   1.00 135.20 ? 123  LEU   D C   1 
ATOM   9147  O  O   . LEU   D 1 54  ? 19.224  -40.728 5.601   1.00 137.65 ? 123  LEU   D O   1 
ATOM   9148  C  CB  . LEU   D 1 54  ? 16.008  -40.466 5.152   1.00 126.59 ? 123  LEU   D CB  1 
ATOM   9149  C  CG  . LEU   D 1 54  ? 14.700  -40.866 4.465   1.00 123.33 ? 123  LEU   D CG  1 
ATOM   9150  C  CD1 . LEU   D 1 54  ? 13.562  -40.957 5.469   1.00 128.40 ? 123  LEU   D CD1 1 
ATOM   9151  C  CD2 . LEU   D 1 54  ? 14.381  -39.857 3.383   1.00 118.38 ? 123  LEU   D CD2 1 
ATOM   9152  N  N   . ALA   D 1 55  ? 18.610  -38.600 5.034   1.00 149.58 ? 124  ALA   D N   1 
ATOM   9153  C  CA  . ALA   D 1 55  ? 19.727  -37.957 5.762   1.00 152.73 ? 124  ALA   D CA  1 
ATOM   9154  C  C   . ALA   D 1 55  ? 19.177  -36.794 6.586   1.00 156.65 ? 124  ALA   D C   1 
ATOM   9155  O  O   . ALA   D 1 55  ? 18.168  -36.191 6.162   1.00 156.56 ? 124  ALA   D O   1 
ATOM   9156  C  CB  . ALA   D 1 55  ? 20.764  -37.489 4.777   1.00 146.76 ? 124  ALA   D CB  1 
ATOM   9157  N  N   . TYR   D 1 56  ? 19.809  -36.488 7.722   1.00 149.52 ? 125  TYR   D N   1 
ATOM   9158  C  CA  . TYR   D 1 56  ? 19.318  -35.422 8.605   1.00 150.77 ? 125  TYR   D CA  1 
ATOM   9159  C  C   . TYR   D 1 56  ? 20.433  -34.453 9.007   1.00 151.67 ? 125  TYR   D C   1 
ATOM   9160  O  O   . TYR   D 1 56  ? 20.406  -33.866 10.090  1.00 152.77 ? 125  TYR   D O   1 
ATOM   9161  C  CB  . TYR   D 1 56  ? 18.666  -36.015 9.857   1.00 151.27 ? 125  TYR   D CB  1 
ATOM   9162  C  CG  . TYR   D 1 56  ? 18.075  -37.389 9.628   1.00 153.01 ? 125  TYR   D CG  1 
ATOM   9163  C  CD1 . TYR   D 1 56  ? 16.889  -37.545 8.926   1.00 152.52 ? 125  TYR   D CD1 1 
ATOM   9164  C  CD2 . TYR   D 1 56  ? 18.709  -38.535 10.110  1.00 151.49 ? 125  TYR   D CD2 1 
ATOM   9165  C  CE1 . TYR   D 1 56  ? 16.347  -38.806 8.710   1.00 149.91 ? 125  TYR   D CE1 1 
ATOM   9166  C  CE2 . TYR   D 1 56  ? 18.175  -39.795 9.904   1.00 145.49 ? 125  TYR   D CE2 1 
ATOM   9167  C  CZ  . TYR   D 1 56  ? 16.996  -39.926 9.202   1.00 148.07 ? 125  TYR   D CZ  1 
ATOM   9168  O  OH  . TYR   D 1 56  ? 16.469  -41.182 8.997   1.00 149.79 ? 125  TYR   D OH  1 
ATOM   9169  N  N   . ALA   D 1 64  ? 16.364  -33.869 9.091   1.00 152.15 ? 133  ALA   D N   1 
ATOM   9170  C  CA  . ALA   D 1 64  ? 16.287  -33.013 7.903   1.00 155.12 ? 133  ALA   D CA  1 
ATOM   9171  C  C   . ALA   D 1 64  ? 15.519  -33.670 6.713   1.00 156.84 ? 133  ALA   D C   1 
ATOM   9172  O  O   . ALA   D 1 64  ? 14.788  -34.662 6.901   1.00 155.04 ? 133  ALA   D O   1 
ATOM   9173  C  CB  . ALA   D 1 64  ? 17.692  -32.591 7.471   1.00 154.66 ? 133  ALA   D CB  1 
ATOM   9174  N  N   . GLN   D 1 65  ? 15.712  -33.128 5.482   1.00 145.90 ? 134  GLN   D N   1 
ATOM   9175  C  CA  . GLN   D 1 65  ? 14.739  -33.287 4.399   1.00 133.13 ? 134  GLN   D CA  1 
ATOM   9176  C  C   . GLN   D 1 65  ? 15.361  -33.630 3.038   1.00 127.64 ? 134  GLN   D C   1 
ATOM   9177  O  O   . GLN   D 1 65  ? 14.840  -33.208 2.002   1.00 122.44 ? 134  GLN   D O   1 
ATOM   9178  C  CB  . GLN   D 1 65  ? 13.896  -32.007 4.254   1.00 130.50 ? 134  GLN   D CB  1 
ATOM   9179  C  CG  . GLN   D 1 65  ? 14.690  -30.675 4.354   1.00 133.77 ? 134  GLN   D CG  1 
ATOM   9180  C  CD  . GLN   D 1 65  ? 14.409  -29.885 5.643   1.00 138.78 ? 134  GLN   D CD  1 
ATOM   9181  O  OE1 . GLN   D 1 65  ? 14.724  -30.336 6.743   1.00 142.81 ? 134  GLN   D OE1 1 
ATOM   9182  N  NE2 . GLN   D 1 65  ? 13.821  -28.699 5.502   1.00 132.79 ? 134  GLN   D NE2 1 
ATOM   9183  N  N   . PHE   D 1 66  ? 16.451  -34.402 3.003   1.00 131.34 ? 135  PHE   D N   1 
ATOM   9184  C  CA  . PHE   D 1 66  ? 17.061  -34.848 1.745   1.00 127.96 ? 135  PHE   D CA  1 
ATOM   9185  C  C   . PHE   D 1 66  ? 17.477  -36.311 1.871   1.00 128.29 ? 135  PHE   D C   1 
ATOM   9186  O  O   . PHE   D 1 66  ? 17.535  -36.874 2.973   1.00 128.71 ? 135  PHE   D O   1 
ATOM   9187  C  CB  . PHE   D 1 66  ? 18.294  -34.015 1.354   1.00 128.64 ? 135  PHE   D CB  1 
ATOM   9188  C  CG  . PHE   D 1 66  ? 17.984  -32.640 0.814   1.00 129.45 ? 135  PHE   D CG  1 
ATOM   9189  C  CD1 . PHE   D 1 66  ? 17.629  -31.605 1.659   1.00 129.65 ? 135  PHE   D CD1 1 
ATOM   9190  C  CD2 . PHE   D 1 66  ? 18.104  -32.371 -0.540  1.00 127.78 ? 135  PHE   D CD2 1 
ATOM   9191  C  CE1 . PHE   D 1 66  ? 17.372  -30.342 1.157   1.00 130.64 ? 135  PHE   D CE1 1 
ATOM   9192  C  CE2 . PHE   D 1 66  ? 17.850  -31.101 -1.047  1.00 125.95 ? 135  PHE   D CE2 1 
ATOM   9193  C  CZ  . PHE   D 1 66  ? 17.486  -30.092 -0.199  1.00 127.68 ? 135  PHE   D CZ  1 
ATOM   9194  N  N   . GLY   D 1 67  ? 17.803  -36.923 0.734   1.00 114.28 ? 136  GLY   D N   1 
ATOM   9195  C  CA  . GLY   D 1 67  ? 18.215  -38.315 0.750   1.00 111.70 ? 136  GLY   D CA  1 
ATOM   9196  C  C   . GLY   D 1 67  ? 18.658  -38.777 -0.620  1.00 103.72 ? 136  GLY   D C   1 
ATOM   9197  O  O   . GLY   D 1 67  ? 18.697  -38.005 -1.577  1.00 106.68 ? 136  GLY   D O   1 
ATOM   9198  N  N   . THR   D 1 68  ? 18.994  -40.063 -0.700  1.00 99.17  ? 137  THR   D N   1 
ATOM   9199  C  CA  . THR   D 1 68  ? 19.451  -40.692 -1.931  1.00 96.59  ? 137  THR   D CA  1 
ATOM   9200  C  C   . THR   D 1 68  ? 18.762  -42.031 -2.065  1.00 101.32 ? 137  THR   D C   1 
ATOM   9201  O  O   . THR   D 1 68  ? 18.747  -42.803 -1.103  1.00 105.94 ? 137  THR   D O   1 
ATOM   9202  C  CB  . THR   D 1 68  ? 20.950  -40.944 -1.915  1.00 95.38  ? 137  THR   D CB  1 
ATOM   9203  O  OG1 . THR   D 1 68  ? 21.626  -39.799 -1.391  1.00 97.63  ? 137  THR   D OG1 1 
ATOM   9204  C  CG2 . THR   D 1 68  ? 21.441  -41.264 -3.314  1.00 92.40  ? 137  THR   D CG2 1 
ATOM   9205  N  N   . THR   D 1 69  ? 18.221  -42.324 -3.249  1.00 100.47 ? 138  THR   D N   1 
ATOM   9206  C  CA  . THR   D 1 69  ? 17.696  -43.662 -3.474  1.00 95.63  ? 138  THR   D CA  1 
ATOM   9207  C  C   . THR   D 1 69  ? 18.829  -44.665 -3.519  1.00 94.42  ? 138  THR   D C   1 
ATOM   9208  O  O   . THR   D 1 69  ? 19.987  -44.319 -3.743  1.00 96.90  ? 138  THR   D O   1 
ATOM   9209  C  CB  . THR   D 1 69  ? 16.935  -43.751 -4.775  1.00 93.08  ? 138  THR   D CB  1 
ATOM   9210  O  OG1 . THR   D 1 69  ? 17.789  -43.324 -5.834  1.00 91.86  ? 138  THR   D OG1 1 
ATOM   9211  C  CG2 . THR   D 1 69  ? 15.720  -42.885 -4.711  1.00 101.44 ? 138  THR   D CG2 1 
ATOM   9212  N  N   . ALA   D 1 70  ? 18.479  -45.927 -3.306  1.00 96.85  ? 139  ALA   D N   1 
ATOM   9213  C  CA  . ALA   D 1 70  ? 19.468  -46.993 -3.308  1.00 96.21  ? 139  ALA   D CA  1 
ATOM   9214  C  C   . ALA   D 1 70  ? 18.849  -48.242 -3.904  1.00 101.22 ? 139  ALA   D C   1 
ATOM   9215  O  O   . ALA   D 1 70  ? 17.766  -48.650 -3.476  1.00 105.34 ? 139  ALA   D O   1 
ATOM   9216  C  CB  . ALA   D 1 70  ? 19.970  -47.288 -1.902  1.00 97.69  ? 139  ALA   D CB  1 
ATOM   9217  N  N   . GLU   D 1 71  ? 19.535  -48.847 -4.877  1.00 97.49  ? 140  GLU   D N   1 
ATOM   9218  C  CA  . GLU   D 1 71  ? 19.000  -49.985 -5.622  1.00 102.10 ? 140  GLU   D CA  1 
ATOM   9219  C  C   . GLU   D 1 71  ? 19.607  -51.287 -5.110  1.00 100.10 ? 140  GLU   D C   1 
ATOM   9220  O  O   . GLU   D 1 71  ? 20.829  -51.471 -5.159  1.00 95.98  ? 140  GLU   D O   1 
ATOM   9221  C  CB  . GLU   D 1 71  ? 19.260  -49.847 -7.123  1.00 99.22  ? 140  GLU   D CB  1 
ATOM   9222  C  CG  . GLU   D 1 71  ? 18.685  -50.998 -7.934  1.00 101.64 ? 140  GLU   D CG  1 
ATOM   9223  C  CD  . GLU   D 1 71  ? 19.128  -50.977 -9.376  1.00 100.31 ? 140  GLU   D CD  1 
ATOM   9224  O  OE1 . GLU   D 1 71  ? 19.691  -49.948 -9.786  1.00 94.13  ? 140  GLU   D OE1 1 
ATOM   9225  O  OE2 . GLU   D 1 71  ? 18.933  -51.987 -10.098 1.00 106.45 ? 140  GLU   D OE2 1 
ATOM   9226  N  N   . ILE   D 1 72  ? 18.743  -52.193 -4.648  1.00 102.48 ? 141  ILE   D N   1 
ATOM   9227  C  CA  . ILE   D 1 72  ? 19.184  -53.514 -4.224  1.00 100.17 ? 141  ILE   D CA  1 
ATOM   9228  C  C   . ILE   D 1 72  ? 19.799  -54.238 -5.423  1.00 99.45  ? 141  ILE   D C   1 
ATOM   9229  O  O   . ILE   D 1 72  ? 19.203  -54.299 -6.508  1.00 103.10 ? 141  ILE   D O   1 
ATOM   9230  C  CB  . ILE   D 1 72  ? 18.010  -54.287 -3.610  1.00 98.19  ? 141  ILE   D CB  1 
ATOM   9231  C  CG1 . ILE   D 1 72  ? 17.092  -53.332 -2.849  1.00 102.01 ? 141  ILE   D CG1 1 
ATOM   9232  C  CG2 . ILE   D 1 72  ? 18.505  -55.323 -2.644  1.00 98.84  ? 141  ILE   D CG2 1 
ATOM   9233  C  CD1 . ILE   D 1 72  ? 15.873  -53.995 -2.248  1.00 110.29 ? 141  ILE   D CD1 1 
ATOM   9234  N  N   . TYR   D 1 73  ? 21.023  -54.750 -5.248  1.00 94.54  ? 142  TYR   D N   1 
ATOM   9235  C  CA  . TYR   D 1 73  ? 21.692  -55.544 -6.266  1.00 94.29  ? 142  TYR   D CA  1 
ATOM   9236  C  C   . TYR   D 1 73  ? 22.189  -56.885 -5.735  1.00 98.96  ? 142  TYR   D C   1 
ATOM   9237  O  O   . TYR   D 1 73  ? 22.808  -57.647 -6.489  1.00 104.27 ? 142  TYR   D O   1 
ATOM   9238  C  CB  . TYR   D 1 73  ? 22.862  -54.761 -6.899  1.00 94.59  ? 142  TYR   D CB  1 
ATOM   9239  C  CG  . TYR   D 1 73  ? 24.069  -54.521 -6.006  1.00 94.12  ? 142  TYR   D CG  1 
ATOM   9240  C  CD1 . TYR   D 1 73  ? 25.145  -55.400 -5.995  1.00 96.66  ? 142  TYR   D CD1 1 
ATOM   9241  C  CD2 . TYR   D 1 73  ? 24.138  -53.401 -5.191  1.00 94.31  ? 142  TYR   D CD2 1 
ATOM   9242  C  CE1 . TYR   D 1 73  ? 26.241  -55.176 -5.176  1.00 96.65  ? 142  TYR   D CE1 1 
ATOM   9243  C  CE2 . TYR   D 1 73  ? 25.229  -53.171 -4.374  1.00 93.64  ? 142  TYR   D CE2 1 
ATOM   9244  C  CZ  . TYR   D 1 73  ? 26.276  -54.056 -4.368  1.00 94.65  ? 142  TYR   D CZ  1 
ATOM   9245  O  OH  . TYR   D 1 73  ? 27.353  -53.807 -3.549  1.00 95.70  ? 142  TYR   D OH  1 
ATOM   9246  N  N   . ALA   D 1 74  ? 21.932  -57.202 -4.466  1.00 98.24  ? 143  ALA   D N   1 
ATOM   9247  C  CA  . ALA   D 1 74  ? 22.195  -58.536 -3.948  1.00 99.58  ? 143  ALA   D CA  1 
ATOM   9248  C  C   . ALA   D 1 74  ? 21.099  -58.879 -2.950  1.00 100.36 ? 143  ALA   D C   1 
ATOM   9249  O  O   . ALA   D 1 74  ? 20.523  -57.995 -2.327  1.00 104.89 ? 143  ALA   D O   1 
ATOM   9250  C  CB  . ALA   D 1 74  ? 23.586  -58.612 -3.316  1.00 97.75  ? 143  ALA   D CB  1 
ATOM   9251  N  N   . TYR   D 1 75  ? 20.776  -60.166 -2.825  1.00 104.76 ? 144  TYR   D N   1 
ATOM   9252  C  CA  . TYR   D 1 75  ? 19.750  -60.594 -1.876  1.00 106.68 ? 144  TYR   D CA  1 
ATOM   9253  C  C   . TYR   D 1 75  ? 20.079  -62.012 -1.428  1.00 114.90 ? 144  TYR   D C   1 
ATOM   9254  O  O   . TYR   D 1 75  ? 20.054  -62.938 -2.245  1.00 116.23 ? 144  TYR   D O   1 
ATOM   9255  C  CB  . TYR   D 1 75  ? 18.350  -60.516 -2.502  1.00 101.09 ? 144  TYR   D CB  1 
ATOM   9256  C  CG  . TYR   D 1 75  ? 17.234  -60.931 -1.574  1.00 107.80 ? 144  TYR   D CG  1 
ATOM   9257  C  CD1 . TYR   D 1 75  ? 16.503  -59.988 -0.876  1.00 113.52 ? 144  TYR   D CD1 1 
ATOM   9258  C  CD2 . TYR   D 1 75  ? 16.912  -62.274 -1.388  1.00 111.95 ? 144  TYR   D CD2 1 
ATOM   9259  C  CE1 . TYR   D 1 75  ? 15.465  -60.367 -0.016  1.00 116.33 ? 144  TYR   D CE1 1 
ATOM   9260  C  CE2 . TYR   D 1 75  ? 15.887  -62.662 -0.532  1.00 113.02 ? 144  TYR   D CE2 1 
ATOM   9261  C  CZ  . TYR   D 1 75  ? 15.166  -61.701 0.152   1.00 116.02 ? 144  TYR   D CZ  1 
ATOM   9262  O  OH  . TYR   D 1 75  ? 14.144  -62.059 1.003   1.00 126.72 ? 144  TYR   D OH  1 
ATOM   9263  N  N   . ARG   D 1 76  ? 20.404  -62.186 -0.143  1.00 115.39 ? 145  ARG   D N   1 
ATOM   9264  C  CA  . ARG   D 1 76  ? 20.752  -63.490 0.420   1.00 123.82 ? 145  ARG   D CA  1 
ATOM   9265  C  C   . ARG   D 1 76  ? 19.967  -63.717 1.705   1.00 132.35 ? 145  ARG   D C   1 
ATOM   9266  O  O   . ARG   D 1 76  ? 20.091  -62.936 2.655   1.00 134.53 ? 145  ARG   D O   1 
ATOM   9267  C  CB  . ARG   D 1 76  ? 22.258  -63.586 0.691   1.00 123.40 ? 145  ARG   D CB  1 
ATOM   9268  N  N   . GLU   D 1 77  ? 19.168  -64.795 1.731   1.00 136.59 ? 146  GLU   D N   1 
ATOM   9269  C  CA  . GLU   D 1 77  ? 18.433  -65.248 2.912   1.00 141.37 ? 146  GLU   D CA  1 
ATOM   9270  C  C   . GLU   D 1 77  ? 19.217  -66.358 3.621   1.00 149.02 ? 146  GLU   D C   1 
ATOM   9271  O  O   . GLU   D 1 77  ? 19.430  -67.431 3.043   1.00 143.28 ? 146  GLU   D O   1 
ATOM   9272  C  CB  . GLU   D 1 77  ? 17.051  -65.777 2.520   1.00 132.70 ? 146  GLU   D CB  1 
ATOM   9273  C  CG  . GLU   D 1 77  ? 16.002  -64.730 2.209   1.00 132.21 ? 146  GLU   D CG  1 
ATOM   9274  C  CD  . GLU   D 1 77  ? 14.586  -65.261 2.361   1.00 134.76 ? 146  GLU   D CD  1 
ATOM   9275  O  OE1 . GLU   D 1 77  ? 14.354  -66.057 3.288   1.00 135.43 ? 146  GLU   D OE1 1 
ATOM   9276  O  OE2 . GLU   D 1 77  ? 13.704  -64.893 1.554   1.00 133.17 ? 146  GLU   D OE2 1 
ATOM   9277  N  N   . GLU   D 1 78  ? 19.620  -66.114 4.879   1.00 151.83 ? 147  GLU   D N   1 
ATOM   9278  C  CA  . GLU   D 1 78  ? 20.336  -67.114 5.697   1.00 151.21 ? 147  GLU   D CA  1 
ATOM   9279  C  C   . GLU   D 1 78  ? 19.526  -67.546 6.924   1.00 156.31 ? 147  GLU   D C   1 
ATOM   9280  O  O   . GLU   D 1 78  ? 20.094  -67.861 7.973   1.00 157.49 ? 147  GLU   D O   1 
ATOM   9281  C  CB  . GLU   D 1 78  ? 21.700  -66.574 6.149   1.00 146.04 ? 147  GLU   D CB  1 
ATOM   9282  C  CG  . GLU   D 1 78  ? 22.827  -66.752 5.146   1.00 146.73 ? 147  GLU   D CG  1 
ATOM   9283  C  CD  . GLU   D 1 78  ? 22.837  -65.683 4.072   1.00 153.78 ? 147  GLU   D CD  1 
ATOM   9284  O  OE1 . GLU   D 1 78  ? 22.929  -64.482 4.422   1.00 156.75 ? 147  GLU   D OE1 1 
ATOM   9285  O  OE2 . GLU   D 1 78  ? 22.748  -66.037 2.872   1.00 156.33 ? 147  GLU   D OE2 1 
ATOM   9286  N  N   . GLY   D 1 82  ? 20.012  -67.560 13.847  1.00 162.19 ? 151  GLY   D N   1 
ATOM   9287  C  CA  . GLY   D 1 82  ? 19.096  -68.682 13.970  1.00 164.22 ? 151  GLY   D CA  1 
ATOM   9288  C  C   . GLY   D 1 82  ? 17.667  -68.312 13.620  1.00 164.22 ? 151  GLY   D C   1 
ATOM   9289  O  O   . GLY   D 1 82  ? 16.734  -69.090 13.844  1.00 164.15 ? 151  GLY   D O   1 
ATOM   9290  N  N   . ILE   D 1 83  ? 17.488  -67.116 13.068  1.00 161.86 ? 152  ILE   D N   1 
ATOM   9291  C  CA  . ILE   D 1 83  ? 16.162  -66.672 12.655  1.00 162.24 ? 152  ILE   D CA  1 
ATOM   9292  C  C   . ILE   D 1 83  ? 16.160  -66.478 11.143  1.00 164.74 ? 152  ILE   D C   1 
ATOM   9293  O  O   . ILE   D 1 83  ? 17.062  -66.958 10.440  1.00 164.12 ? 152  ILE   D O   1 
ATOM   9294  C  CB  . ILE   D 1 83  ? 15.763  -65.368 13.368  1.00 160.13 ? 152  ILE   D CB  1 
ATOM   9295  C  CG1 . ILE   D 1 83  ? 16.900  -64.356 13.261  1.00 165.19 ? 152  ILE   D CG1 1 
ATOM   9296  C  CG2 . ILE   D 1 83  ? 15.422  -65.626 14.820  1.00 154.14 ? 152  ILE   D CG2 1 
ATOM   9297  C  CD1 . ILE   D 1 83  ? 16.435  -62.916 13.082  1.00 164.67 ? 152  ILE   D CD1 1 
ATOM   9298  N  N   . GLU   D 1 84  ? 15.148  -65.766 10.634  1.00 165.79 ? 153  GLU   D N   1 
ATOM   9299  C  CA  . GLU   D 1 84  ? 15.056  -65.414 9.212   1.00 164.47 ? 153  GLU   D CA  1 
ATOM   9300  C  C   . GLU   D 1 84  ? 15.998  -64.245 8.925   1.00 163.35 ? 153  GLU   D C   1 
ATOM   9301  O  O   . GLU   D 1 84  ? 15.597  -63.078 8.859   1.00 156.03 ? 153  GLU   D O   1 
ATOM   9302  C  CB  . GLU   D 1 84  ? 13.614  -65.094 8.830   1.00 155.52 ? 153  GLU   D CB  1 
ATOM   9303  N  N   . ILE   D 1 85  ? 17.281  -64.581 8.773   1.00 171.28 ? 154  ILE   D N   1 
ATOM   9304  C  CA  . ILE   D 1 85  ? 18.347  -63.612 8.515   1.00 167.83 ? 154  ILE   D CA  1 
ATOM   9305  C  C   . ILE   D 1 85  ? 18.387  -63.299 7.023   1.00 164.08 ? 154  ILE   D C   1 
ATOM   9306  O  O   . ILE   D 1 85  ? 18.595  -64.194 6.197   1.00 165.31 ? 154  ILE   D O   1 
ATOM   9307  C  CB  . ILE   D 1 85  ? 19.707  -64.153 8.987   1.00 166.48 ? 154  ILE   D CB  1 
ATOM   9308  C  CG1 . ILE   D 1 85  ? 19.657  -64.554 10.466  1.00 163.77 ? 154  ILE   D CG1 1 
ATOM   9309  C  CG2 . ILE   D 1 85  ? 20.782  -63.125 8.702   1.00 163.60 ? 154  ILE   D CG2 1 
ATOM   9310  C  CD1 . ILE   D 1 85  ? 20.214  -65.956 10.760  1.00 160.30 ? 154  ILE   D CD1 1 
ATOM   9311  N  N   . VAL   D 1 86  ? 18.198  -62.032 6.677   1.00 145.76 ? 155  VAL   D N   1 
ATOM   9312  C  CA  . VAL   D 1 86  ? 18.201  -61.588 5.290   1.00 138.94 ? 155  VAL   D CA  1 
ATOM   9313  C  C   . VAL   D 1 86  ? 19.250  -60.505 5.153   1.00 134.40 ? 155  VAL   D C   1 
ATOM   9314  O  O   . VAL   D 1 86  ? 19.217  -59.507 5.880   1.00 135.49 ? 155  VAL   D O   1 
ATOM   9315  C  CB  . VAL   D 1 86  ? 16.833  -61.058 4.846   1.00 135.90 ? 155  VAL   D CB  1 
ATOM   9316  C  CG1 . VAL   D 1 86  ? 16.866  -60.715 3.368   1.00 127.31 ? 155  VAL   D CG1 1 
ATOM   9317  C  CG2 . VAL   D 1 86  ? 15.743  -62.066 5.155   1.00 141.23 ? 155  VAL   D CG2 1 
ATOM   9318  N  N   . LYS   D 1 87  ? 20.162  -60.680 4.211   1.00 126.37 ? 156  LYS   D N   1 
ATOM   9319  C  CA  . LYS   D 1 87  ? 21.216  -59.708 3.981   1.00 118.38 ? 156  LYS   D CA  1 
ATOM   9320  C  C   . LYS   D 1 87  ? 21.105  -59.222 2.541   1.00 117.51 ? 156  LYS   D C   1 
ATOM   9321  O  O   . LYS   D 1 87  ? 21.375  -59.987 1.606   1.00 118.16 ? 156  LYS   D O   1 
ATOM   9322  C  CB  . LYS   D 1 87  ? 22.580  -60.328 4.269   1.00 119.27 ? 156  LYS   D CB  1 
ATOM   9323  N  N   . VAL   D 1 88  ? 20.699  -57.966 2.356   1.00 113.48 ? 157  VAL   D N   1 
ATOM   9324  C  CA  . VAL   D 1 88  ? 20.678  -57.345 1.040   1.00 103.98 ? 157  VAL   D CA  1 
ATOM   9325  C  C   . VAL   D 1 88  ? 21.819  -56.337 0.955   1.00 99.83  ? 157  VAL   D C   1 
ATOM   9326  O  O   . VAL   D 1 88  ? 22.418  -55.951 1.951   1.00 104.59 ? 157  VAL   D O   1 
ATOM   9327  C  CB  . VAL   D 1 88  ? 19.330  -56.670 0.724   1.00 100.46 ? 157  VAL   D CB  1 
ATOM   9328  C  CG1 . VAL   D 1 88  ? 18.186  -57.652 0.875   1.00 108.97 ? 157  VAL   D CG1 1 
ATOM   9329  C  CG2 . VAL   D 1 88  ? 19.133  -55.470 1.596   1.00 100.84 ? 157  VAL   D CG2 1 
ATOM   9330  N  N   . LYS   D 1 89  ? 22.126  -55.922 -0.264  1.00 99.29  ? 158  LYS   D N   1 
ATOM   9331  C  CA  . LYS   D 1 89  ? 23.096  -54.874 -0.512  1.00 92.08  ? 158  LYS   D CA  1 
ATOM   9332  C  C   . LYS   D 1 89  ? 22.502  -53.978 -1.576  1.00 93.20  ? 158  LYS   D C   1 
ATOM   9333  O  O   . LYS   D 1 89  ? 21.839  -54.455 -2.496  1.00 96.45  ? 158  LYS   D O   1 
ATOM   9334  C  CB  . LYS   D 1 89  ? 24.450  -55.427 -0.964  1.00 87.81  ? 158  LYS   D CB  1 
ATOM   9335  N  N   . ALA   D 1 90  ? 22.714  -52.675 -1.426  1.00 92.55  ? 159  ALA   D N   1 
ATOM   9336  C  CA  . ALA   D 1 90  ? 22.138  -51.693 -2.322  1.00 89.30  ? 159  ALA   D CA  1 
ATOM   9337  C  C   . ALA   D 1 90  ? 23.207  -50.685 -2.689  1.00 90.28  ? 159  ALA   D C   1 
ATOM   9338  O  O   . ALA   D 1 90  ? 24.239  -50.582 -2.029  1.00 92.74  ? 159  ALA   D O   1 
ATOM   9339  C  CB  . ALA   D 1 90  ? 20.938  -50.987 -1.690  1.00 93.34  ? 159  ALA   D CB  1 
ATOM   9340  N  N   . ILE   D 1 91  ? 22.936  -49.914 -3.733  1.00 93.71  ? 160  ILE   D N   1 
ATOM   9341  C  CA  . ILE   D 1 91  ? 23.865  -48.922 -4.242  1.00 90.94  ? 160  ILE   D CA  1 
ATOM   9342  C  C   . ILE   D 1 91  ? 23.111  -47.618 -4.456  1.00 92.77  ? 160  ILE   D C   1 
ATOM   9343  O  O   . ILE   D 1 91  ? 21.932  -47.634 -4.838  1.00 90.10  ? 160  ILE   D O   1 
ATOM   9344  C  CB  . ILE   D 1 91  ? 24.521  -49.403 -5.546  1.00 88.60  ? 160  ILE   D CB  1 
ATOM   9345  C  CG1 . ILE   D 1 91  ? 25.426  -48.332 -6.132  1.00 90.73  ? 160  ILE   D CG1 1 
ATOM   9346  C  CG2 . ILE   D 1 91  ? 23.456  -49.838 -6.535  1.00 93.19  ? 160  ILE   D CG2 1 
ATOM   9347  C  CD1 . ILE   D 1 91  ? 26.359  -48.844 -7.175  1.00 85.25  ? 160  ILE   D CD1 1 
ATOM   9348  N  N   . GLY   D 1 92  ? 23.798  -46.501 -4.205  1.00 96.56  ? 161  GLY   D N   1 
ATOM   9349  C  CA  . GLY   D 1 92  ? 23.180  -45.176 -4.293  1.00 96.31  ? 161  GLY   D CA  1 
ATOM   9350  C  C   . GLY   D 1 92  ? 22.857  -44.750 -5.718  1.00 91.60  ? 161  GLY   D C   1 
ATOM   9351  O  O   . GLY   D 1 92  ? 23.766  -44.622 -6.554  1.00 90.43  ? 161  GLY   D O   1 
ATOM   9352  N  N   . ARG   D 1 93  ? 21.588  -44.523 -6.002  1.00 89.05  ? 162  ARG   D N   1 
ATOM   9353  C  CA  . ARG   D 1 93  ? 21.202  -44.177 -7.352  1.00 88.19  ? 162  ARG   D CA  1 
ATOM   9354  C  C   . ARG   D 1 93  ? 21.065  -42.693 -7.662  1.00 92.58  ? 162  ARG   D C   1 
ATOM   9355  O  O   . ARG   D 1 93  ? 21.904  -42.127 -8.365  1.00 92.27  ? 162  ARG   D O   1 
ATOM   9356  C  CB  . ARG   D 1 93  ? 19.870  -44.843 -7.704  1.00 91.98  ? 162  ARG   D CB  1 
ATOM   9357  C  CG  . ARG   D 1 93  ? 20.015  -46.326 -8.047  1.00 87.43  ? 162  ARG   D CG  1 
ATOM   9358  C  CD  . ARG   D 1 93  ? 21.180  -46.574 -9.026  1.00 89.50  ? 162  ARG   D CD  1 
ATOM   9359  N  NE  . ARG   D 1 93  ? 21.291  -47.963 -9.473  1.00 88.91  ? 162  ARG   D NE  1 
ATOM   9360  C  CZ  . ARG   D 1 93  ? 22.422  -48.545 -9.852  1.00 87.93  ? 162  ARG   D CZ  1 
ATOM   9361  N  NH1 . ARG   D 1 93  ? 23.583  -47.913 -9.777  1.00 86.20  ? 162  ARG   D NH1 1 
ATOM   9362  N  NH2 . ARG   D 1 93  ? 22.391  -49.802 -10.285 1.00 93.57  ? 162  ARG   D NH2 1 
ATOM   9363  N  N   . GLN   D 1 94  ? 20.007  -42.058 -7.182  1.00 99.12  ? 163  GLN   D N   1 
ATOM   9364  C  CA  . GLN   D 1 94  ? 19.734  -40.683 -7.536  1.00 99.58  ? 163  GLN   D CA  1 
ATOM   9365  C  C   . GLN   D 1 94  ? 19.435  -39.954 -6.229  1.00 103.16 ? 163  GLN   D C   1 
ATOM   9366  O  O   . GLN   D 1 94  ? 18.936  -40.548 -5.267  1.00 103.29 ? 163  GLN   D O   1 
ATOM   9367  C  CB  . GLN   D 1 94  ? 18.608  -40.529 -8.570  1.00 100.66 ? 163  GLN   D CB  1 
ATOM   9368  C  CG  . GLN   D 1 94  ? 17.528  -41.619 -8.438  1.00 106.09 ? 163  GLN   D CG  1 
ATOM   9369  C  CD  . GLN   D 1 94  ? 16.707  -41.834 -9.709  1.00 113.22 ? 163  GLN   D CD  1 
ATOM   9370  O  OE1 . GLN   D 1 94  ? 17.168  -41.550 -10.820 1.00 116.58 ? 163  GLN   D OE1 1 
ATOM   9371  N  NE2 . GLN   D 1 94  ? 15.482  -42.342 -9.546  1.00 113.00 ? 163  GLN   D NE2 1 
ATOM   9372  N  N   . ARG   D 1 95  ? 19.794  -38.668 -6.182  1.00 99.65  ? 164  ARG   D N   1 
ATOM   9373  C  CA  . ARG   D 1 95  ? 19.583  -37.841 -4.999  1.00 97.68  ? 164  ARG   D CA  1 
ATOM   9374  C  C   . ARG   D 1 95  ? 18.194  -37.214 -5.052  1.00 99.88  ? 164  ARG   D C   1 
ATOM   9375  O  O   . ARG   D 1 95  ? 17.555  -37.165 -6.106  1.00 106.68 ? 164  ARG   D O   1 
ATOM   9376  C  CB  . ARG   D 1 95  ? 20.644  -36.746 -4.900  1.00 92.89  ? 164  ARG   D CB  1 
ATOM   9377  C  CG  . ARG   D 1 95  ? 22.089  -37.225 -4.795  1.00 88.22  ? 164  ARG   D CG  1 
ATOM   9378  C  CD  . ARG   D 1 95  ? 22.972  -36.309 -5.602  1.00 86.51  ? 164  ARG   D CD  1 
ATOM   9379  N  NE  . ARG   D 1 95  ? 22.209  -35.719 -6.699  1.00 91.48  ? 164  ARG   D NE  1 
ATOM   9380  C  CZ  . ARG   D 1 95  ? 22.579  -34.655 -7.401  1.00 94.29  ? 164  ARG   D CZ  1 
ATOM   9381  N  NH1 . ARG   D 1 95  ? 23.682  -33.985 -7.112  1.00 90.70  ? 164  ARG   D NH1 1 
ATOM   9382  N  NH2 . ARG   D 1 95  ? 21.824  -34.259 -8.420  1.00 99.85  ? 164  ARG   D NH2 1 
ATOM   9383  N  N   . PHE   D 1 96  ? 17.722  -36.737 -3.902  1.00 100.76 ? 165  PHE   D N   1 
ATOM   9384  C  CA  . PHE   D 1 96  ? 16.333  -36.314 -3.803  1.00 105.45 ? 165  PHE   D CA  1 
ATOM   9385  C  C   . PHE   D 1 96  ? 16.105  -35.441 -2.563  1.00 111.32 ? 165  PHE   D C   1 
ATOM   9386  O  O   . PHE   D 1 96  ? 16.787  -35.572 -1.536  1.00 112.80 ? 165  PHE   D O   1 
ATOM   9387  C  CB  . PHE   D 1 96  ? 15.373  -37.531 -3.831  1.00 105.51 ? 165  PHE   D CB  1 
ATOM   9388  C  CG  . PHE   D 1 96  ? 15.399  -38.401 -2.604  1.00 101.39 ? 165  PHE   D CG  1 
ATOM   9389  C  CD1 . PHE   D 1 96  ? 14.782  -37.992 -1.450  1.00 103.52 ? 165  PHE   D CD1 1 
ATOM   9390  C  CD2 . PHE   D 1 96  ? 16.001  -39.643 -2.616  1.00 100.89 ? 165  PHE   D CD2 1 
ATOM   9391  C  CE1 . PHE   D 1 96  ? 14.794  -38.764 -0.332  1.00 105.63 ? 165  PHE   D CE1 1 
ATOM   9392  C  CE2 . PHE   D 1 96  ? 16.002  -40.436 -1.495  1.00 101.12 ? 165  PHE   D CE2 1 
ATOM   9393  C  CZ  . PHE   D 1 96  ? 15.401  -39.991 -0.349  1.00 104.60 ? 165  PHE   D CZ  1 
ATOM   9394  N  N   . LYS   D 1 97  ? 15.081  -34.592 -2.671  1.00 109.11 ? 166  LYS   D N   1 
ATOM   9395  C  CA  . LYS   D 1 97  ? 14.667  -33.769 -1.513  1.00 109.51 ? 166  LYS   D CA  1 
ATOM   9396  C  C   . LYS   D 1 97  ? 13.275  -34.266 -1.122  1.00 108.73 ? 166  LYS   D C   1 
ATOM   9397  O  O   . LYS   D 1 97  ? 12.463  -34.513 -2.034  1.00 108.35 ? 166  LYS   D O   1 
ATOM   9398  C  CB  . LYS   D 1 97  ? 14.561  -32.293 -1.893  1.00 106.71 ? 166  LYS   D CB  1 
ATOM   9399  N  N   . VAL   D 1 98  ? 13.015  -34.429 0.172   1.00 111.71 ? 167  VAL   D N   1 
ATOM   9400  C  CA  . VAL   D 1 98  ? 11.706  -35.012 0.576   1.00 109.30 ? 167  VAL   D CA  1 
ATOM   9401  C  C   . VAL   D 1 98  ? 10.647  -33.905 0.525   1.00 108.55 ? 167  VAL   D C   1 
ATOM   9402  O  O   . VAL   D 1 98  ? 10.986  -32.736 0.798   1.00 103.46 ? 167  VAL   D O   1 
ATOM   9403  C  CB  . VAL   D 1 98  ? 11.772  -35.699 1.952   1.00 109.62 ? 167  VAL   D CB  1 
ATOM   9404  C  CG1 . VAL   D 1 98  ? 13.115  -36.381 2.174   1.00 112.51 ? 167  VAL   D CG1 1 
ATOM   9405  C  CG2 . VAL   D 1 98  ? 11.452  -34.751 3.101   1.00 120.41 ? 167  VAL   D CG2 1 
ATOM   9406  N  N   . LEU   D 1 99  ? 9.429   -34.262 0.130   1.00 110.73 ? 168  LEU   D N   1 
ATOM   9407  C  CA  . LEU   D 1 99  ? 8.322   -33.279 0.088   1.00 107.01 ? 168  LEU   D CA  1 
ATOM   9408  C  C   . LEU   D 1 99  ? 7.263   -33.747 1.085   1.00 107.52 ? 168  LEU   D C   1 
ATOM   9409  O  O   . LEU   D 1 99  ? 7.067   -33.058 2.104   1.00 109.83 ? 168  LEU   D O   1 
ATOM   9410  C  CB  . LEU   D 1 99  ? 7.770   -33.226 -1.331  1.00 107.96 ? 168  LEU   D CB  1 
ATOM   9411  C  CG  . LEU   D 1 99  ? 8.730   -32.700 -2.401  1.00 104.89 ? 168  LEU   D CG  1 
ATOM   9412  C  CD1 . LEU   D 1 99  ? 8.110   -32.838 -3.777  1.00 105.53 ? 168  LEU   D CD1 1 
ATOM   9413  C  CD2 . LEU   D 1 99  ? 9.052   -31.249 -2.103  1.00 105.49 ? 168  LEU   D CD2 1 
ATOM   9414  N  N   . GLU   D 1 100 ? 6.619   -34.878 0.800   1.00 111.01 ? 169  GLU   D N   1 
ATOM   9415  C  CA  . GLU   D 1 100 ? 5.644   -35.455 1.759   1.00 115.09 ? 169  GLU   D CA  1 
ATOM   9416  C  C   . GLU   D 1 100 ? 6.268   -36.725 2.348   1.00 118.65 ? 169  GLU   D C   1 
ATOM   9417  O  O   . GLU   D 1 100 ? 7.182   -37.281 1.704   1.00 116.49 ? 169  GLU   D O   1 
ATOM   9418  C  CB  . GLU   D 1 100 ? 4.308   -35.774 1.092   1.00 109.38 ? 169  GLU   D CB  1 
ATOM   9419  N  N   . LEU   D 1 101 ? 5.792   -37.162 3.514   1.00 122.69 ? 170  LEU   D N   1 
ATOM   9420  C  CA  . LEU   D 1 101 ? 6.410   -38.334 4.182   1.00 126.94 ? 170  LEU   D CA  1 
ATOM   9421  C  C   . LEU   D 1 101 ? 5.353   -39.090 5.000   1.00 135.44 ? 170  LEU   D C   1 
ATOM   9422  O  O   . LEU   D 1 101 ? 5.677   -39.526 6.123   1.00 138.95 ? 170  LEU   D O   1 
ATOM   9423  C  CB  . LEU   D 1 101 ? 7.546   -37.827 5.066   1.00 124.61 ? 170  LEU   D CB  1 
ATOM   9424  C  CG  . LEU   D 1 101 ? 8.959   -38.244 4.650   1.00 124.80 ? 170  LEU   D CG  1 
ATOM   9425  C  CD1 . LEU   D 1 101 ? 9.988   -37.432 5.413   1.00 122.69 ? 170  LEU   D CD1 1 
ATOM   9426  C  CD2 . LEU   D 1 101 ? 9.170   -39.726 4.891   1.00 125.33 ? 170  LEU   D CD2 1 
ATOM   9427  N  N   . ARG   D 1 102 ? 4.144   -39.248 4.454   1.00 148.23 ? 171  ARG   D N   1 
ATOM   9428  C  CA  . ARG   D 1 102 ? 3.095   -39.961 5.185   1.00 149.43 ? 171  ARG   D CA  1 
ATOM   9429  C  C   . ARG   D 1 102 ? 3.605   -41.317 5.678   1.00 152.06 ? 171  ARG   D C   1 
ATOM   9430  O  O   . ARG   D 1 102 ? 4.310   -42.021 4.951   1.00 153.04 ? 171  ARG   D O   1 
ATOM   9431  C  CB  . ARG   D 1 102 ? 1.867   -40.137 4.283   1.00 147.43 ? 171  ARG   D CB  1 
ATOM   9432  N  N   . THR   D 1 103 ? 3.273   -41.668 6.935   1.00 148.84 ? 172  THR   D N   1 
ATOM   9433  C  CA  . THR   D 1 103 ? 3.726   -42.931 7.568   1.00 141.48 ? 172  THR   D CA  1 
ATOM   9434  C  C   . THR   D 1 103 ? 2.582   -43.946 7.711   1.00 133.00 ? 172  THR   D C   1 
ATOM   9435  O  O   . THR   D 1 103 ? 2.675   -45.078 7.226   1.00 128.61 ? 172  THR   D O   1 
ATOM   9436  C  CB  . THR   D 1 103 ? 4.355   -42.700 8.982   1.00 132.88 ? 172  THR   D CB  1 
ATOM   9437  O  OG1 . THR   D 1 103 ? 5.286   -41.610 8.941   1.00 135.14 ? 172  THR   D OG1 1 
ATOM   9438  C  CG2 . THR   D 1 103 ? 5.074   -43.959 9.452   1.00 126.50 ? 172  THR   D CG2 1 
ATOM   9439  N  N   . ILE   D 1 108 ? 6.331   -49.556 8.255   1.00 172.84 ? 177  ILE   D N   1 
ATOM   9440  C  CA  . ILE   D 1 108 ? 7.340   -48.925 7.407   1.00 166.46 ? 177  ILE   D CA  1 
ATOM   9441  C  C   . ILE   D 1 108 ? 6.920   -47.484 7.083   1.00 162.14 ? 177  ILE   D C   1 
ATOM   9442  O  O   . ILE   D 1 108 ? 6.126   -46.890 7.828   1.00 163.06 ? 177  ILE   D O   1 
ATOM   9443  C  CB  . ILE   D 1 108 ? 7.582   -49.763 6.138   1.00 166.26 ? 177  ILE   D CB  1 
ATOM   9444  C  CG1 . ILE   D 1 108 ? 6.253   -50.133 5.466   1.00 170.01 ? 177  ILE   D CG1 1 
ATOM   9445  C  CG2 . ILE   D 1 108 ? 8.355   -51.034 6.482   1.00 164.61 ? 177  ILE   D CG2 1 
ATOM   9446  C  CD1 . ILE   D 1 108 ? 6.395   -51.060 4.245   1.00 167.86 ? 177  ILE   D CD1 1 
ATOM   9447  N  N   . GLN   D 1 109 ? 7.441   -46.921 5.986   1.00 151.19 ? 178  GLN   D N   1 
ATOM   9448  C  CA  . GLN   D 1 109 ? 7.185   -45.520 5.656   1.00 140.44 ? 178  GLN   D CA  1 
ATOM   9449  C  C   . GLN   D 1 109 ? 7.467   -45.269 4.183   1.00 133.07 ? 178  GLN   D C   1 
ATOM   9450  O  O   . GLN   D 1 109 ? 8.521   -45.670 3.689   1.00 135.34 ? 178  GLN   D O   1 
ATOM   9451  C  CB  . GLN   D 1 109 ? 8.062   -44.604 6.512   1.00 136.31 ? 178  GLN   D CB  1 
ATOM   9452  C  CG  . GLN   D 1 109 ? 7.795   -43.135 6.334   1.00 133.99 ? 178  GLN   D CG  1 
ATOM   9453  C  CD  . GLN   D 1 109 ? 8.346   -42.326 7.483   1.00 134.58 ? 178  GLN   D CD  1 
ATOM   9454  O  OE1 . GLN   D 1 109 ? 7.793   -41.289 7.843   1.00 133.53 ? 178  GLN   D OE1 1 
ATOM   9455  N  NE2 . GLN   D 1 109 ? 9.440   -42.800 8.073   1.00 132.15 ? 178  GLN   D NE2 1 
ATOM   9456  N  N   . GLN   D 1 110 ? 6.545   -44.599 3.490   1.00 130.27 ? 179  GLN   D N   1 
ATOM   9457  C  CA  . GLN   D 1 110 ? 6.779   -44.146 2.121   1.00 130.20 ? 179  GLN   D CA  1 
ATOM   9458  C  C   . GLN   D 1 110 ? 7.197   -42.672 2.130   1.00 130.88 ? 179  GLN   D C   1 
ATOM   9459  O  O   . GLN   D 1 110 ? 7.182   -42.007 3.170   1.00 135.18 ? 179  GLN   D O   1 
ATOM   9460  C  CB  . GLN   D 1 110 ? 5.537   -44.362 1.246   1.00 129.97 ? 179  GLN   D CB  1 
ATOM   9461  N  N   . ALA   D 1 111 ? 7.584   -42.156 0.961   1.00 126.13 ? 180  ALA   D N   1 
ATOM   9462  C  CA  . ALA   D 1 111 ? 8.056   -40.777 0.909   1.00 120.99 ? 180  ALA   D CA  1 
ATOM   9463  C  C   . ALA   D 1 111 ? 7.869   -40.200 -0.482  1.00 119.38 ? 180  ALA   D C   1 
ATOM   9464  O  O   . ALA   D 1 111 ? 8.291   -40.803 -1.472  1.00 118.09 ? 180  ALA   D O   1 
ATOM   9465  C  CB  . ALA   D 1 111 ? 9.526   -40.677 1.321   1.00 119.22 ? 180  ALA   D CB  1 
ATOM   9466  N  N   . LYS   D 1 112 ? 7.218   -39.040 -0.547  1.00 117.88 ? 181  LYS   D N   1 
ATOM   9467  C  CA  . LYS   D 1 112 ? 7.192   -38.261 -1.772  1.00 113.53 ? 181  LYS   D CA  1 
ATOM   9468  C  C   . LYS   D 1 112 ? 8.526   -37.559 -1.918  1.00 115.65 ? 181  LYS   D C   1 
ATOM   9469  O  O   . LYS   D 1 112 ? 9.086   -37.030 -0.952  1.00 114.39 ? 181  LYS   D O   1 
ATOM   9470  C  CB  . LYS   D 1 112 ? 6.056   -37.240 -1.770  1.00 110.48 ? 181  LYS   D CB  1 
ATOM   9471  N  N   . VAL   D 1 113 ? 9.019   -37.541 -3.145  1.00 120.52 ? 182  VAL   D N   1 
ATOM   9472  C  CA  . VAL   D 1 113 ? 10.439  -37.384 -3.427  1.00 118.35 ? 182  VAL   D CA  1 
ATOM   9473  C  C   . VAL   D 1 113 ? 10.568  -36.541 -4.690  1.00 119.32 ? 182  VAL   D C   1 
ATOM   9474  O  O   . VAL   D 1 113 ? 9.829   -36.743 -5.659  1.00 122.82 ? 182  VAL   D O   1 
ATOM   9475  C  CB  . VAL   D 1 113 ? 11.106  -38.777 -3.572  1.00 117.46 ? 182  VAL   D CB  1 
ATOM   9476  C  CG1 . VAL   D 1 113 ? 12.354  -38.702 -4.415  1.00 117.76 ? 182  VAL   D CG1 1 
ATOM   9477  C  CG2 . VAL   D 1 113 ? 11.418  -39.378 -2.199  1.00 114.93 ? 182  VAL   D CG2 1 
ATOM   9478  N  N   . GLN   D 1 114 ? 11.456  -35.547 -4.663  1.00 112.46 ? 183  GLN   D N   1 
ATOM   9479  C  CA  . GLN   D 1 114 ? 11.751  -34.746 -5.849  1.00 111.50 ? 183  GLN   D CA  1 
ATOM   9480  C  C   . GLN   D 1 114 ? 13.188  -35.061 -6.216  1.00 109.90 ? 183  GLN   D C   1 
ATOM   9481  O  O   . GLN   D 1 114 ? 14.109  -34.659 -5.503  1.00 111.45 ? 183  GLN   D O   1 
ATOM   9482  C  CB  . GLN   D 1 114 ? 11.555  -33.244 -5.605  1.00 106.65 ? 183  GLN   D CB  1 
ATOM   9483  N  N   . ILE   D 1 115 ? 13.388  -35.799 -7.306  1.00 113.03 ? 184  ILE   D N   1 
ATOM   9484  C  CA  . ILE   D 1 115 ? 14.742  -36.184 -7.673  1.00 113.07 ? 184  ILE   D CA  1 
ATOM   9485  C  C   . ILE   D 1 115 ? 15.557  -34.929 -7.939  1.00 114.57 ? 184  ILE   D C   1 
ATOM   9486  O  O   . ILE   D 1 115 ? 15.106  -34.015 -8.638  1.00 123.60 ? 184  ILE   D O   1 
ATOM   9487  C  CB  . ILE   D 1 115 ? 14.728  -37.123 -8.887  1.00 119.07 ? 184  ILE   D CB  1 
ATOM   9488  C  CG1 . ILE   D 1 115 ? 14.013  -38.427 -8.545  1.00 112.95 ? 184  ILE   D CG1 1 
ATOM   9489  C  CG2 . ILE   D 1 115 ? 16.143  -37.430 -9.317  1.00 116.70 ? 184  ILE   D CG2 1 
ATOM   9490  C  CD1 . ILE   D 1 115 ? 14.682  -39.197 -7.440  1.00 103.95 ? 184  ILE   D CD1 1 
ATOM   9491  N  N   . LEU   D 1 116 ? 16.746  -34.857 -7.350  1.00 109.35 ? 185  LEU   D N   1 
ATOM   9492  C  CA  . LEU   D 1 116 ? 17.568  -33.674 -7.544  1.00 112.19 ? 185  LEU   D CA  1 
ATOM   9493  C  C   . LEU   D 1 116 ? 18.147  -33.671 -8.960  1.00 118.33 ? 185  LEU   D C   1 
ATOM   9494  O  O   . LEU   D 1 116 ? 18.260  -34.725 -9.602  1.00 117.15 ? 185  LEU   D O   1 
ATOM   9495  C  CB  . LEU   D 1 116 ? 18.696  -33.606 -6.509  1.00 107.40 ? 185  LEU   D CB  1 
ATOM   9496  C  CG  . LEU   D 1 116 ? 18.421  -33.345 -5.020  1.00 102.92 ? 185  LEU   D CG  1 
ATOM   9497  C  CD1 . LEU   D 1 116 ? 19.679  -32.731 -4.407  1.00 95.64  ? 185  LEU   D CD1 1 
ATOM   9498  C  CD2 . LEU   D 1 116 ? 17.199  -32.465 -4.758  1.00 102.54 ? 185  LEU   D CD2 1 
ATOM   9499  N  N   . PRO   D 1 117 ? 18.500  -32.495 -9.478  1.00 130.42 ? 186  PRO   D N   1 
ATOM   9500  C  CA  . PRO   D 1 117 ? 18.947  -32.396 -10.878 1.00 130.63 ? 186  PRO   D CA  1 
ATOM   9501  C  C   . PRO   D 1 117 ? 20.408  -32.795 -11.049 1.00 128.31 ? 186  PRO   D C   1 
ATOM   9502  O  O   . PRO   D 1 117 ? 21.274  -32.350 -10.289 1.00 126.03 ? 186  PRO   D O   1 
ATOM   9503  C  CB  . PRO   D 1 117 ? 18.745  -30.912 -11.197 1.00 132.38 ? 186  PRO   D CB  1 
ATOM   9504  C  CG  . PRO   D 1 117 ? 18.898  -30.229 -9.853  1.00 130.01 ? 186  PRO   D CG  1 
ATOM   9505  C  CD  . PRO   D 1 117 ? 18.290  -31.173 -8.863  1.00 128.07 ? 186  PRO   D CD  1 
ATOM   9506  N  N   . GLU   D 1 118 ? 20.684  -33.625 -12.068 1.00 116.84 ? 187  GLU   D N   1 
ATOM   9507  C  CA  . GLU   D 1 118 ? 22.055  -33.895 -12.520 1.00 110.57 ? 187  GLU   D CA  1 
ATOM   9508  C  C   . GLU   D 1 118 ? 22.182  -33.385 -13.951 1.00 107.89 ? 187  GLU   D C   1 
ATOM   9509  O  O   . GLU   D 1 118 ? 21.846  -34.102 -14.901 1.00 109.87 ? 187  GLU   D O   1 
ATOM   9510  C  CB  . GLU   D 1 118 ? 22.427  -35.377 -12.438 1.00 108.23 ? 187  GLU   D CB  1 
ATOM   9511  C  CG  . GLU   D 1 118 ? 23.838  -35.701 -12.996 1.00 101.07 ? 187  GLU   D CG  1 
ATOM   9512  C  CD  . GLU   D 1 118 ? 24.971  -35.434 -12.003 1.00 97.41  ? 187  GLU   D CD  1 
ATOM   9513  O  OE1 . GLU   D 1 118 ? 24.871  -35.884 -10.846 1.00 95.76  ? 187  GLU   D OE1 1 
ATOM   9514  O  OE2 . GLU   D 1 118 ? 25.967  -34.780 -12.380 1.00 95.33  ? 187  GLU   D OE2 1 
ATOM   9515  N  N   . CYS   D 1 119 ? 22.700  -32.161 -14.096 1.00 108.36 ? 188  CYS   D N   1 
ATOM   9516  C  CA  . CYS   D 1 119 ? 22.644  -31.409 -15.349 1.00 104.10 ? 188  CYS   D CA  1 
ATOM   9517  C  C   . CYS   D 1 119 ? 23.847  -31.749 -16.218 1.00 98.83  ? 188  CYS   D C   1 
ATOM   9518  O  O   . CYS   D 1 119 ? 24.982  -31.383 -15.891 1.00 92.58  ? 188  CYS   D O   1 
ATOM   9519  C  CB  . CYS   D 1 119 ? 22.598  -29.912 -15.063 1.00 104.37 ? 188  CYS   D CB  1 
ATOM   9520  S  SG  . CYS   D 1 119 ? 21.734  -29.504 -13.528 1.00 111.89 ? 188  CYS   D SG  1 
ATOM   9521  N  N   . VAL   D 1 120 ? 23.601  -32.430 -17.334 1.00 99.45  ? 189  VAL   D N   1 
ATOM   9522  C  CA  . VAL   D 1 120 ? 24.671  -32.856 -18.226 1.00 93.14  ? 189  VAL   D CA  1 
ATOM   9523  C  C   . VAL   D 1 120 ? 24.859  -31.783 -19.285 1.00 92.66  ? 189  VAL   D C   1 
ATOM   9524  O  O   . VAL   D 1 120 ? 23.904  -31.388 -19.959 1.00 96.84  ? 189  VAL   D O   1 
ATOM   9525  C  CB  . VAL   D 1 120 ? 24.364  -34.216 -18.860 1.00 86.56  ? 189  VAL   D CB  1 
ATOM   9526  C  CG1 . VAL   D 1 120 ? 25.409  -34.531 -19.888 1.00 88.03  ? 189  VAL   D CG1 1 
ATOM   9527  C  CG2 . VAL   D 1 120 ? 24.327  -35.292 -17.783 1.00 92.08  ? 189  VAL   D CG2 1 
ATOM   9528  N  N   . LEU   D 1 121 ? 26.081  -31.304 -19.425 1.00 93.31  ? 190  LEU   D N   1 
ATOM   9529  C  CA  . LEU   D 1 121 ? 26.323  -30.160 -20.283 1.00 90.53  ? 190  LEU   D CA  1 
ATOM   9530  C  C   . LEU   D 1 121 ? 27.146  -30.537 -21.513 1.00 90.75  ? 190  LEU   D C   1 
ATOM   9531  O  O   . LEU   D 1 121 ? 27.941  -31.480 -21.487 1.00 93.87  ? 190  LEU   D O   1 
ATOM   9532  C  CB  . LEU   D 1 121 ? 27.057  -29.054 -19.513 1.00 88.42  ? 190  LEU   D CB  1 
ATOM   9533  C  CG  . LEU   D 1 121 ? 26.214  -28.042 -18.734 1.00 83.43  ? 190  LEU   D CG  1 
ATOM   9534  C  CD1 . LEU   D 1 121 ? 25.566  -28.675 -17.508 1.00 87.23  ? 190  LEU   D CD1 1 
ATOM   9535  C  CD2 . LEU   D 1 121 ? 27.035  -26.806 -18.389 1.00 74.58  ? 190  LEU   D CD2 1 
ATOM   9536  N  N   . PRO   D 1 122 ? 26.988  -29.804 -22.593 1.00 89.57  ? 191  PRO   D N   1 
ATOM   9537  C  CA  . PRO   D 1 122 ? 27.838  -29.994 -23.771 1.00 92.32  ? 191  PRO   D CA  1 
ATOM   9538  C  C   . PRO   D 1 122 ? 29.229  -29.402 -23.558 1.00 89.49  ? 191  PRO   D C   1 
ATOM   9539  O  O   . PRO   D 1 122 ? 29.505  -28.720 -22.574 1.00 86.28  ? 191  PRO   D O   1 
ATOM   9540  C  CB  . PRO   D 1 122 ? 27.087  -29.242 -24.872 1.00 97.42  ? 191  PRO   D CB  1 
ATOM   9541  C  CG  . PRO   D 1 122 ? 26.310  -28.194 -24.142 1.00 97.00  ? 191  PRO   D CG  1 
ATOM   9542  C  CD  . PRO   D 1 122 ? 25.933  -28.801 -22.812 1.00 91.96  ? 191  PRO   D CD  1 
ATOM   9543  N  N   . SER   D 1 123 ? 30.106  -29.676 -24.517 1.00 89.02  ? 192  SER   D N   1 
ATOM   9544  C  CA  . SER   D 1 123 ? 31.418  -29.062 -24.498 1.00 87.92  ? 192  SER   D CA  1 
ATOM   9545  C  C   . SER   D 1 123 ? 31.273  -27.556 -24.627 1.00 89.25  ? 192  SER   D C   1 
ATOM   9546  O  O   . SER   D 1 123 ? 30.428  -27.073 -25.383 1.00 94.85  ? 192  SER   D O   1 
ATOM   9547  C  CB  . SER   D 1 123 ? 32.263  -29.614 -25.637 1.00 92.33  ? 192  SER   D CB  1 
ATOM   9548  O  OG  . SER   D 1 123 ? 33.323  -28.731 -25.914 1.00 95.52  ? 192  SER   D OG  1 
ATOM   9549  N  N   . THR   D 1 124 ? 32.093  -26.812 -23.872 1.00 90.59  ? 193  THR   D N   1 
ATOM   9550  C  CA  . THR   D 1 124 ? 32.008  -25.349 -23.884 1.00 90.54  ? 193  THR   D CA  1 
ATOM   9551  C  C   . THR   D 1 124 ? 32.089  -24.789 -25.301 1.00 91.78  ? 193  THR   D C   1 
ATOM   9552  O  O   . THR   D 1 124 ? 31.523  -23.727 -25.578 1.00 91.00  ? 193  THR   D O   1 
ATOM   9553  C  CB  . THR   D 1 124 ? 33.110  -24.706 -22.997 1.00 89.36  ? 193  THR   D CB  1 
ATOM   9554  O  OG1 . THR   D 1 124 ? 34.358  -25.415 -23.118 1.00 89.66  ? 193  THR   D OG1 1 
ATOM   9555  C  CG2 . THR   D 1 124 ? 32.696  -24.686 -21.541 1.00 85.06  ? 193  THR   D CG2 1 
ATOM   9556  N  N   . MET   D 1 125 ? 32.750  -25.502 -26.218 1.00 94.42  ? 194  MET   D N   1 
ATOM   9557  C  CA  . MET   D 1 125 ? 32.966  -25.013 -27.579 1.00 99.05  ? 194  MET   D CA  1 
ATOM   9558  C  C   . MET   D 1 125 ? 31.923  -25.489 -28.579 1.00 101.35 ? 194  MET   D C   1 
ATOM   9559  O  O   . MET   D 1 125 ? 31.959  -25.053 -29.735 1.00 104.19 ? 194  MET   D O   1 
ATOM   9560  C  CB  . MET   D 1 125 ? 34.358  -25.432 -28.090 1.00 98.64  ? 194  MET   D CB  1 
ATOM   9561  C  CG  . MET   D 1 125 ? 35.523  -24.865 -27.292 1.00 93.09  ? 194  MET   D CG  1 
ATOM   9562  S  SD  . MET   D 1 125 ? 35.636  -23.074 -27.425 1.00 88.59  ? 194  MET   D SD  1 
ATOM   9563  C  CE  . MET   D 1 125 ? 34.740  -22.501 -25.988 1.00 87.44  ? 194  MET   D CE  1 
ATOM   9564  N  N   . SER   D 1 126 ? 31.016  -26.380 -28.177 1.00 100.18 ? 195  SER   D N   1 
ATOM   9565  C  CA  . SER   D 1 126 ? 30.096  -26.965 -29.141 1.00 99.11  ? 195  SER   D CA  1 
ATOM   9566  C  C   . SER   D 1 126 ? 29.283  -25.890 -29.844 1.00 104.43 ? 195  SER   D C   1 
ATOM   9567  O  O   . SER   D 1 126 ? 28.979  -26.022 -31.033 1.00 110.92 ? 195  SER   D O   1 
ATOM   9568  C  CB  . SER   D 1 126 ? 29.180  -27.964 -28.445 1.00 97.84  ? 195  SER   D CB  1 
ATOM   9569  O  OG  . SER   D 1 126 ? 28.279  -27.283 -27.591 1.00 99.86  ? 195  SER   D OG  1 
ATOM   9570  N  N   . ALA   D 1 127 ? 28.941  -24.808 -29.131 1.00 104.18 ? 196  ALA   D N   1 
ATOM   9571  C  CA  . ALA   D 1 127 ? 28.168  -23.715 -29.726 1.00 104.33 ? 196  ALA   D CA  1 
ATOM   9572  C  C   . ALA   D 1 127 ? 28.961  -22.977 -30.802 1.00 107.68 ? 196  ALA   D C   1 
ATOM   9573  O  O   . ALA   D 1 127 ? 28.469  -22.747 -31.916 1.00 107.29 ? 196  ALA   D O   1 
ATOM   9574  C  CB  . ALA   D 1 127 ? 27.735  -22.734 -28.640 1.00 103.12 ? 196  ALA   D CB  1 
ATOM   9575  N  N   . VAL   D 1 128 ? 30.192  -22.575 -30.476 1.00 117.38 ? 197  VAL   D N   1 
ATOM   9576  C  CA  . VAL   D 1 128 ? 31.004  -21.804 -31.407 1.00 119.08 ? 197  VAL   D CA  1 
ATOM   9577  C  C   . VAL   D 1 128 ? 31.826  -22.676 -32.344 1.00 119.35 ? 197  VAL   D C   1 
ATOM   9578  O  O   . VAL   D 1 128 ? 32.556  -22.140 -33.189 1.00 120.36 ? 197  VAL   D O   1 
ATOM   9579  C  CB  . VAL   D 1 128 ? 31.941  -20.856 -30.638 1.00 118.58 ? 197  VAL   D CB  1 
ATOM   9580  C  CG1 . VAL   D 1 128 ? 31.126  -19.780 -29.938 1.00 115.38 ? 197  VAL   D CG1 1 
ATOM   9581  C  CG2 . VAL   D 1 128 ? 32.773  -21.651 -29.638 1.00 116.09 ? 197  VAL   D CG2 1 
ATOM   9582  N  N   . GLN   D 1 129 ? 31.738  -23.998 -32.221 1.00 113.63 ? 198  GLN   D N   1 
ATOM   9583  C  CA  . GLN   D 1 129 ? 32.566  -24.889 -33.023 1.00 113.37 ? 198  GLN   D CA  1 
ATOM   9584  C  C   . GLN   D 1 129 ? 32.367  -24.609 -34.510 1.00 118.00 ? 198  GLN   D C   1 
ATOM   9585  O  O   . GLN   D 1 129 ? 31.259  -24.796 -35.036 1.00 121.81 ? 198  GLN   D O   1 
ATOM   9586  C  CB  . GLN   D 1 129 ? 32.250  -26.351 -32.686 1.00 111.30 ? 198  GLN   D CB  1 
ATOM   9587  C  CG  . GLN   D 1 129 ? 33.294  -27.348 -33.167 1.00 112.79 ? 198  GLN   D CG  1 
ATOM   9588  C  CD  . GLN   D 1 129 ? 34.697  -27.005 -32.720 1.00 112.20 ? 198  GLN   D CD  1 
ATOM   9589  O  OE1 . GLN   D 1 129 ? 35.387  -26.219 -33.364 1.00 109.61 ? 198  GLN   D OE1 1 
ATOM   9590  N  NE2 . GLN   D 1 129 ? 35.131  -27.601 -31.618 1.00 113.89 ? 198  GLN   D NE2 1 
ATOM   9591  N  N   . LEU   D 1 130 ? 33.422  -24.127 -35.180 1.00 115.61 ? 199  LEU   D N   1 
ATOM   9592  C  CA  . LEU   D 1 130 ? 33.363  -23.896 -36.622 1.00 113.74 ? 199  LEU   D CA  1 
ATOM   9593  C  C   . LEU   D 1 130 ? 33.205  -25.208 -37.375 1.00 115.39 ? 199  LEU   D C   1 
ATOM   9594  O  O   . LEU   D 1 130 ? 33.884  -26.195 -37.090 1.00 117.15 ? 199  LEU   D O   1 
ATOM   9595  C  CB  . LEU   D 1 130 ? 34.619  -23.192 -37.118 1.00 109.54 ? 199  LEU   D CB  1 
ATOM   9596  C  CG  . LEU   D 1 130 ? 34.755  -21.724 -36.786 1.00 106.71 ? 199  LEU   D CG  1 
ATOM   9597  C  CD1 . LEU   D 1 130 ? 35.782  -21.615 -35.698 1.00 106.61 ? 199  LEU   D CD1 1 
ATOM   9598  C  CD2 . LEU   D 1 130 ? 35.166  -20.948 -38.028 1.00 103.52 ? 199  LEU   D CD2 1 
ATOM   9599  N  N   . GLU   D 1 131 ? 32.323  -25.203 -38.372 1.00 116.89 ? 200  GLU   D N   1 
ATOM   9600  C  CA  . GLU   D 1 131 ? 31.983  -26.442 -39.059 1.00 118.81 ? 200  GLU   D CA  1 
ATOM   9601  C  C   . GLU   D 1 131 ? 33.186  -27.050 -39.781 1.00 120.70 ? 200  GLU   D C   1 
ATOM   9602  O  O   . GLU   D 1 131 ? 33.287  -28.279 -39.876 1.00 123.48 ? 200  GLU   D O   1 
ATOM   9603  C  CB  . GLU   D 1 131 ? 30.820  -26.196 -40.023 1.00 119.93 ? 200  GLU   D CB  1 
ATOM   9604  C  CG  . GLU   D 1 131 ? 29.445  -26.095 -39.340 1.00 118.48 ? 200  GLU   D CG  1 
ATOM   9605  C  CD  . GLU   D 1 131 ? 29.316  -24.877 -38.433 1.00 120.02 ? 200  GLU   D CD  1 
ATOM   9606  O  OE1 . GLU   D 1 131 ? 29.805  -23.793 -38.828 1.00 118.44 ? 200  GLU   D OE1 1 
ATOM   9607  O  OE2 . GLU   D 1 131 ? 28.738  -25.005 -37.326 1.00 119.92 ? 200  GLU   D OE2 1 
ATOM   9608  N  N   . SER   D 1 132 ? 34.116  -26.222 -40.275 1.00 116.40 ? 201  SER   D N   1 
ATOM   9609  C  CA  . SER   D 1 132 ? 35.292  -26.769 -40.950 1.00 115.64 ? 201  SER   D CA  1 
ATOM   9610  C  C   . SER   D 1 132 ? 36.264  -27.390 -39.957 1.00 120.23 ? 201  SER   D C   1 
ATOM   9611  O  O   . SER   D 1 132 ? 37.019  -28.298 -40.326 1.00 122.54 ? 201  SER   D O   1 
ATOM   9612  C  CB  . SER   D 1 132 ? 35.987  -25.695 -41.791 1.00 106.24 ? 201  SER   D CB  1 
ATOM   9613  O  OG  . SER   D 1 132 ? 36.766  -24.813 -41.014 1.00 100.80 ? 201  SER   D OG  1 
ATOM   9614  N  N   . LEU   D 1 133 ? 36.236  -26.929 -38.693 1.00 119.79 ? 202  LEU   D N   1 
ATOM   9615  C  CA  . LEU   D 1 133 ? 37.056  -27.458 -37.601 1.00 116.67 ? 202  LEU   D CA  1 
ATOM   9616  C  C   . LEU   D 1 133 ? 36.437  -28.671 -36.916 1.00 122.54 ? 202  LEU   D C   1 
ATOM   9617  O  O   . LEU   D 1 133 ? 37.151  -29.403 -36.222 1.00 129.85 ? 202  LEU   D O   1 
ATOM   9618  C  CB  . LEU   D 1 133 ? 37.285  -26.380 -36.543 1.00 112.92 ? 202  LEU   D CB  1 
ATOM   9619  C  CG  . LEU   D 1 133 ? 38.395  -25.344 -36.691 1.00 112.87 ? 202  LEU   D CG  1 
ATOM   9620  C  CD1 . LEU   D 1 133 ? 38.370  -24.661 -38.058 1.00 109.98 ? 202  LEU   D CD1 1 
ATOM   9621  C  CD2 . LEU   D 1 133 ? 38.246  -24.326 -35.559 1.00 112.10 ? 202  LEU   D CD2 1 
ATOM   9622  N  N   . ASN   D 1 134 ? 35.122  -28.868 -37.051 1.00 124.67 ? 203  ASN   D N   1 
ATOM   9623  C  CA  . ASN   D 1 134 ? 34.457  -30.096 -36.633 1.00 125.82 ? 203  ASN   D CA  1 
ATOM   9624  C  C   . ASN   D 1 134 ? 35.277  -31.315 -37.041 1.00 135.07 ? 203  ASN   D C   1 
ATOM   9625  O  O   . ASN   D 1 134 ? 35.395  -32.274 -36.273 1.00 139.87 ? 203  ASN   D O   1 
ATOM   9626  C  CB  . ASN   D 1 134 ? 33.058  -30.196 -37.263 1.00 124.21 ? 203  ASN   D CB  1 
ATOM   9627  C  CG  . ASN   D 1 134 ? 32.003  -29.341 -36.555 1.00 123.01 ? 203  ASN   D CG  1 
ATOM   9628  O  OD1 . ASN   D 1 134 ? 32.131  -29.024 -35.371 1.00 122.41 ? 203  ASN   D OD1 1 
ATOM   9629  N  ND2 . ASN   D 1 134 ? 30.935  -28.988 -37.286 1.00 120.88 ? 203  ASN   D ND2 1 
ATOM   9630  N  N   . LYS   D 1 135 ? 35.863  -31.257 -38.245 1.00 143.35 ? 204  LYS   D N   1 
ATOM   9631  C  CA  . LYS   D 1 135 ? 36.458  -32.427 -38.900 1.00 144.34 ? 204  LYS   D CA  1 
ATOM   9632  C  C   . LYS   D 1 135 ? 37.509  -33.105 -38.031 1.00 144.47 ? 204  LYS   D C   1 
ATOM   9633  O  O   . LYS   D 1 135 ? 37.468  -34.322 -37.827 1.00 140.81 ? 204  LYS   D O   1 
ATOM   9634  C  CB  . LYS   D 1 135 ? 37.064  -32.024 -40.252 1.00 139.42 ? 204  LYS   D CB  1 
ATOM   9635  C  CG  . LYS   D 1 135 ? 36.048  -31.805 -41.355 1.00 133.07 ? 204  LYS   D CG  1 
ATOM   9636  C  CD  . LYS   D 1 135 ? 36.459  -30.682 -42.284 1.00 133.15 ? 204  LYS   D CD  1 
ATOM   9637  C  CE  . LYS   D 1 135 ? 35.210  -30.082 -42.910 1.00 134.97 ? 204  LYS   D CE  1 
ATOM   9638  N  NZ  . LYS   D 1 135 ? 35.454  -28.830 -43.684 1.00 134.59 ? 204  LYS   D NZ  1 
ATOM   9639  N  N   . CYS   D 1 136 ? 38.471  -32.337 -37.516 1.00 174.73 ? 205  CYS   D N   1 
ATOM   9640  C  CA  . CYS   D 1 136 ? 39.536  -32.899 -36.696 1.00 176.96 ? 205  CYS   D CA  1 
ATOM   9641  C  C   . CYS   D 1 136 ? 39.359  -32.562 -35.214 1.00 173.64 ? 205  CYS   D C   1 
ATOM   9642  O  O   . CYS   D 1 136 ? 40.333  -32.441 -34.467 1.00 173.72 ? 205  CYS   D O   1 
ATOM   9643  C  CB  . CYS   D 1 136 ? 40.904  -32.447 -37.207 1.00 179.70 ? 205  CYS   D CB  1 
ATOM   9644  S  SG  . CYS   D 1 136 ? 42.230  -33.638 -36.721 1.00 188.35 ? 205  CYS   D SG  1 
ATOM   9645  N  N   . GLN   D 1 137 ? 38.110  -32.421 -34.773 1.00 148.56 ? 206  GLN   D N   1 
ATOM   9646  C  CA  . GLN   D 1 137 ? 37.842  -32.260 -33.354 1.00 142.15 ? 206  GLN   D CA  1 
ATOM   9647  C  C   . GLN   D 1 137 ? 38.145  -33.538 -32.573 1.00 143.23 ? 206  GLN   D C   1 
ATOM   9648  O  O   . GLN   D 1 137 ? 38.253  -33.489 -31.344 1.00 145.09 ? 206  GLN   D O   1 
ATOM   9649  C  CB  . GLN   D 1 137 ? 36.385  -31.792 -33.169 1.00 133.05 ? 206  GLN   D CB  1 
ATOM   9650  C  CG  . GLN   D 1 137 ? 36.017  -31.185 -31.801 1.00 129.56 ? 206  GLN   D CG  1 
ATOM   9651  C  CD  . GLN   D 1 137 ? 36.986  -30.125 -31.286 1.00 123.18 ? 206  GLN   D CD  1 
ATOM   9652  O  OE1 . GLN   D 1 137 ? 37.187  -29.997 -30.070 1.00 117.88 ? 206  GLN   D OE1 1 
ATOM   9653  N  NE2 . GLN   D 1 137 ? 37.576  -29.355 -32.196 1.00 120.63 ? 206  GLN   D NE2 1 
ATOM   9654  N  N   . ILE   D 1 138 ? 38.320  -34.666 -33.257 1.00 140.25 ? 207  ILE   D N   1 
ATOM   9655  C  CA  . ILE   D 1 138 ? 38.721  -35.917 -32.628 1.00 140.94 ? 207  ILE   D CA  1 
ATOM   9656  C  C   . ILE   D 1 138 ? 40.242  -35.940 -32.519 1.00 144.76 ? 207  ILE   D C   1 
ATOM   9657  O  O   . ILE   D 1 138 ? 40.944  -35.695 -33.509 1.00 147.31 ? 207  ILE   D O   1 
ATOM   9658  C  CB  . ILE   D 1 138 ? 38.194  -37.119 -33.429 1.00 135.63 ? 207  ILE   D CB  1 
ATOM   9659  C  CG1 . ILE   D 1 138 ? 36.735  -37.395 -33.065 1.00 135.65 ? 207  ILE   D CG1 1 
ATOM   9660  C  CG2 . ILE   D 1 138 ? 39.064  -38.361 -33.224 1.00 139.77 ? 207  ILE   D CG2 1 
ATOM   9661  C  CD1 . ILE   D 1 138 ? 36.214  -38.716 -33.580 1.00 130.00 ? 207  ILE   D CD1 1 
ATOM   9662  N  N   . PHE   D 1 139 ? 40.761  -36.222 -31.302 1.00 148.78 ? 208  PHE   D N   1 
ATOM   9663  C  CA  . PHE   D 1 139 ? 42.192  -36.236 -30.984 1.00 149.57 ? 208  PHE   D CA  1 
ATOM   9664  C  C   . PHE   D 1 139 ? 42.736  -37.660 -30.954 1.00 151.30 ? 208  PHE   D C   1 
ATOM   9665  O  O   . PHE   D 1 139 ? 42.051  -38.572 -30.479 1.00 156.13 ? 208  PHE   D O   1 
ATOM   9666  C  CB  . PHE   D 1 139 ? 42.469  -35.583 -29.627 1.00 147.82 ? 208  PHE   D CB  1 
ATOM   9667  C  CG  . PHE   D 1 139 ? 41.560  -34.431 -29.305 1.00 150.58 ? 208  PHE   D CG  1 
ATOM   9668  C  CD1 . PHE   D 1 139 ? 41.632  -33.245 -30.029 1.00 148.88 ? 208  PHE   D CD1 1 
ATOM   9669  C  CD2 . PHE   D 1 139 ? 40.639  -34.532 -28.267 1.00 147.70 ? 208  PHE   D CD2 1 
ATOM   9670  C  CE1 . PHE   D 1 139 ? 40.792  -32.191 -29.733 1.00 144.66 ? 208  PHE   D CE1 1 
ATOM   9671  C  CE2 . PHE   D 1 139 ? 39.794  -33.481 -27.958 1.00 143.18 ? 208  PHE   D CE2 1 
ATOM   9672  C  CZ  . PHE   D 1 139 ? 39.870  -32.307 -28.691 1.00 143.46 ? 208  PHE   D CZ  1 
ATOM   9673  N  N   . PRO   D 1 140 ? 43.960  -37.900 -31.430 1.00 141.20 ? 209  PRO   D N   1 
ATOM   9674  C  CA  . PRO   D 1 140 ? 44.541  -39.242 -31.310 1.00 146.34 ? 209  PRO   D CA  1 
ATOM   9675  C  C   . PRO   D 1 140 ? 44.709  -39.653 -29.852 1.00 149.92 ? 209  PRO   D C   1 
ATOM   9676  O  O   . PRO   D 1 140 ? 44.592  -38.854 -28.915 1.00 143.64 ? 209  PRO   D O   1 
ATOM   9677  C  CB  . PRO   D 1 140 ? 45.893  -39.119 -32.024 1.00 137.30 ? 209  PRO   D CB  1 
ATOM   9678  C  CG  . PRO   D 1 140 ? 45.722  -37.987 -32.934 1.00 130.49 ? 209  PRO   D CG  1 
ATOM   9679  C  CD  . PRO   D 1 140 ? 44.817  -37.017 -32.234 1.00 133.41 ? 209  PRO   D CD  1 
ATOM   9680  N  N   . SER   D 1 141 ? 45.002  -40.944 -29.678 1.00 142.39 ? 210  SER   D N   1 
ATOM   9681  C  CA  . SER   D 1 141 ? 45.059  -41.563 -28.359 1.00 146.08 ? 210  SER   D CA  1 
ATOM   9682  C  C   . SER   D 1 141 ? 46.115  -40.879 -27.491 1.00 147.55 ? 210  SER   D C   1 
ATOM   9683  O  O   . SER   D 1 141 ? 47.123  -40.367 -27.991 1.00 146.79 ? 210  SER   D O   1 
ATOM   9684  C  CB  . SER   D 1 141 ? 45.355  -43.064 -28.511 1.00 148.81 ? 210  SER   D CB  1 
ATOM   9685  O  OG  . SER   D 1 141 ? 44.826  -43.847 -27.446 1.00 148.96 ? 210  SER   D OG  1 
ATOM   9686  N  N   . LYS   D 1 142 ? 45.868  -40.878 -26.169 1.00 156.40 ? 211  LYS   D N   1 
ATOM   9687  C  CA  . LYS   D 1 142 ? 46.700  -40.157 -25.207 1.00 154.76 ? 211  LYS   D CA  1 
ATOM   9688  C  C   . LYS   D 1 142 ? 47.753  -41.079 -24.599 1.00 171.42 ? 211  LYS   D C   1 
ATOM   9689  O  O   . LYS   D 1 142 ? 47.401  -41.945 -23.780 1.00 173.49 ? 211  LYS   D O   1 
ATOM   9690  C  CB  . LYS   D 1 142 ? 45.834  -39.559 -24.105 1.00 140.92 ? 211  LYS   D CB  1 
ATOM   9691  N  N   . PRO   D 1 143 ? 49.041  -40.915 -24.927 1.00 191.73 ? 212  PRO   D N   1 
ATOM   9692  C  CA  . PRO   D 1 143 ? 50.073  -41.803 -24.368 1.00 192.25 ? 212  PRO   D CA  1 
ATOM   9693  C  C   . PRO   D 1 143 ? 50.370  -41.515 -22.899 1.00 191.56 ? 212  PRO   D C   1 
ATOM   9694  O  O   . PRO   D 1 143 ? 50.284  -40.379 -22.427 1.00 190.28 ? 212  PRO   D O   1 
ATOM   9695  C  CB  . PRO   D 1 143 ? 51.305  -41.514 -25.241 1.00 191.47 ? 212  PRO   D CB  1 
ATOM   9696  C  CG  . PRO   D 1 143 ? 50.783  -40.779 -26.448 1.00 187.46 ? 212  PRO   D CG  1 
ATOM   9697  C  CD  . PRO   D 1 143 ? 49.588  -40.018 -25.958 1.00 185.40 ? 212  PRO   D CD  1 
ATOM   9698  N  N   . VAL   D 1 144 ? 50.743  -42.567 -22.173 1.00 179.51 ? 213  VAL   D N   1 
ATOM   9699  C  CA  . VAL   D 1 144 ? 51.119  -42.417 -20.766 1.00 175.52 ? 213  VAL   D CA  1 
ATOM   9700  C  C   . VAL   D 1 144 ? 52.638  -42.325 -20.625 1.00 171.89 ? 213  VAL   D C   1 
ATOM   9701  O  O   . VAL   D 1 144 ? 53.180  -41.275 -20.276 1.00 168.41 ? 213  VAL   D O   1 
ATOM   9702  C  CB  . VAL   D 1 144 ? 50.569  -43.569 -19.900 1.00 169.77 ? 213  VAL   D CB  1 
ATOM   9703  C  CG1 . VAL   D 1 144 ? 49.050  -43.612 -19.968 1.00 166.47 ? 213  VAL   D CG1 1 
ATOM   9704  C  CG2 . VAL   D 1 144 ? 51.180  -44.896 -20.337 1.00 168.89 ? 213  VAL   D CG2 1 
ATOM   9705  N  N   . SER   D 1 151 ? 53.584  -37.358 -22.554 1.00 144.02 ? 220  SER   D N   1 
ATOM   9706  C  CA  . SER   D 1 151 ? 53.752  -36.651 -21.288 1.00 147.30 ? 220  SER   D CA  1 
ATOM   9707  C  C   . SER   D 1 151 ? 52.575  -35.733 -20.945 1.00 149.58 ? 220  SER   D C   1 
ATOM   9708  O  O   . SER   D 1 151 ? 51.421  -36.048 -21.247 1.00 144.14 ? 220  SER   D O   1 
ATOM   9709  C  CB  . SER   D 1 151 ? 55.034  -35.833 -21.321 1.00 145.59 ? 220  SER   D CB  1 
ATOM   9710  O  OG  . SER   D 1 151 ? 55.264  -35.251 -20.053 1.00 149.64 ? 220  SER   D OG  1 
ATOM   9711  N  N   . TYR   D 1 152 ? 52.871  -34.600 -20.303 1.00 160.32 ? 221  TYR   D N   1 
ATOM   9712  C  CA  . TYR   D 1 152 ? 51.870  -33.586 -19.995 1.00 160.06 ? 221  TYR   D CA  1 
ATOM   9713  C  C   . TYR   D 1 152 ? 51.756  -32.516 -21.076 1.00 157.61 ? 221  TYR   D C   1 
ATOM   9714  O  O   . TYR   D 1 152 ? 50.827  -31.702 -21.022 1.00 156.14 ? 221  TYR   D O   1 
ATOM   9715  C  CB  . TYR   D 1 152 ? 52.173  -32.917 -18.656 1.00 161.41 ? 221  TYR   D CB  1 
ATOM   9716  N  N   . LYS   D 1 153 ? 52.671  -32.499 -22.052 1.00 143.56 ? 222  LYS   D N   1 
ATOM   9717  C  CA  . LYS   D 1 153 ? 52.533  -31.612 -23.202 1.00 133.89 ? 222  LYS   D CA  1 
ATOM   9718  C  C   . LYS   D 1 153 ? 51.369  -32.034 -24.095 1.00 127.72 ? 222  LYS   D C   1 
ATOM   9719  O  O   . LYS   D 1 153 ? 50.944  -31.253 -24.960 1.00 123.82 ? 222  LYS   D O   1 
ATOM   9720  C  CB  . LYS   D 1 153 ? 53.838  -31.589 -24.000 1.00 130.31 ? 222  LYS   D CB  1 
ATOM   9721  N  N   . TRP   D 1 154 ? 50.863  -33.256 -23.917 1.00 127.99 ? 223  TRP   D N   1 
ATOM   9722  C  CA  . TRP   D 1 154 ? 49.589  -33.634 -24.520 1.00 121.34 ? 223  TRP   D CA  1 
ATOM   9723  C  C   . TRP   D 1 154 ? 48.482  -32.680 -24.079 1.00 120.02 ? 223  TRP   D C   1 
ATOM   9724  O  O   . TRP   D 1 154 ? 47.713  -32.174 -24.903 1.00 116.63 ? 223  TRP   D O   1 
ATOM   9725  C  CB  . TRP   D 1 154 ? 49.254  -35.077 -24.141 1.00 116.55 ? 223  TRP   D CB  1 
ATOM   9726  C  CG  . TRP   D 1 154 ? 48.070  -35.668 -24.841 1.00 115.37 ? 223  TRP   D CG  1 
ATOM   9727  C  CD1 . TRP   D 1 154 ? 48.085  -36.413 -25.989 1.00 121.96 ? 223  TRP   D CD1 1 
ATOM   9728  C  CD2 . TRP   D 1 154 ? 46.702  -35.612 -24.415 1.00 112.69 ? 223  TRP   D CD2 1 
ATOM   9729  N  NE1 . TRP   D 1 154 ? 46.806  -36.803 -26.314 1.00 126.48 ? 223  TRP   D NE1 1 
ATOM   9730  C  CE2 . TRP   D 1 154 ? 45.939  -36.327 -25.364 1.00 119.80 ? 223  TRP   D CE2 1 
ATOM   9731  C  CE3 . TRP   D 1 154 ? 46.047  -35.022 -23.329 1.00 106.76 ? 223  TRP   D CE3 1 
ATOM   9732  C  CZ2 . TRP   D 1 154 ? 44.552  -36.465 -25.257 1.00 115.00 ? 223  TRP   D CZ2 1 
ATOM   9733  C  CZ3 . TRP   D 1 154 ? 44.675  -35.159 -23.228 1.00 108.08 ? 223  TRP   D CZ3 1 
ATOM   9734  C  CH2 . TRP   D 1 154 ? 43.941  -35.875 -24.185 1.00 108.61 ? 223  TRP   D CH2 1 
ATOM   9735  N  N   . TRP   D 1 155 ? 48.407  -32.401 -22.772 1.00 121.27 ? 224  TRP   D N   1 
ATOM   9736  C  CA  . TRP   D 1 155 ? 47.345  -31.566 -22.226 1.00 112.14 ? 224  TRP   D CA  1 
ATOM   9737  C  C   . TRP   D 1 155 ? 47.515  -30.097 -22.576 1.00 112.35 ? 224  TRP   D C   1 
ATOM   9738  O  O   . TRP   D 1 155 ? 46.593  -29.307 -22.342 1.00 112.94 ? 224  TRP   D O   1 
ATOM   9739  C  CB  . TRP   D 1 155 ? 47.303  -31.727 -20.714 1.00 110.90 ? 224  TRP   D CB  1 
ATOM   9740  C  CG  . TRP   D 1 155 ? 46.796  -33.030 -20.288 1.00 104.14 ? 224  TRP   D CG  1 
ATOM   9741  C  CD1 . TRP   D 1 155 ? 47.527  -34.128 -19.970 1.00 105.20 ? 224  TRP   D CD1 1 
ATOM   9742  C  CD2 . TRP   D 1 155 ? 45.427  -33.387 -20.119 1.00 100.57 ? 224  TRP   D CD2 1 
ATOM   9743  N  NE1 . TRP   D 1 155 ? 46.696  -35.153 -19.608 1.00 100.25 ? 224  TRP   D NE1 1 
ATOM   9744  C  CE2 . TRP   D 1 155 ? 45.398  -34.724 -19.693 1.00 101.26 ? 224  TRP   D CE2 1 
ATOM   9745  C  CE3 . TRP   D 1 155 ? 44.220  -32.703 -20.279 1.00 99.20  ? 224  TRP   D CE3 1 
ATOM   9746  C  CZ2 . TRP   D 1 155 ? 44.207  -35.398 -19.426 1.00 102.98 ? 224  TRP   D CZ2 1 
ATOM   9747  C  CZ3 . TRP   D 1 155 ? 43.033  -33.376 -20.012 1.00 98.08  ? 224  TRP   D CZ3 1 
ATOM   9748  C  CH2 . TRP   D 1 155 ? 43.037  -34.707 -19.592 1.00 99.74  ? 224  TRP   D CH2 1 
ATOM   9749  N  N   . GLN   D 1 156 ? 48.686  -29.702 -23.079 1.00 118.03 ? 225  GLN   D N   1 
ATOM   9750  C  CA  . GLN   D 1 156 ? 48.819  -28.373 -23.662 1.00 119.76 ? 225  GLN   D CA  1 
ATOM   9751  C  C   . GLN   D 1 156 ? 48.278  -28.356 -25.091 1.00 118.57 ? 225  GLN   D C   1 
ATOM   9752  O  O   . GLN   D 1 156 ? 47.503  -27.466 -25.460 1.00 116.67 ? 225  GLN   D O   1 
ATOM   9753  C  CB  . GLN   D 1 156 ? 50.281  -27.926 -23.622 1.00 121.14 ? 225  GLN   D CB  1 
ATOM   9754  C  CG  . GLN   D 1 156 ? 50.914  -28.052 -22.260 1.00 127.58 ? 225  GLN   D CG  1 
ATOM   9755  C  CD  . GLN   D 1 156 ? 50.051  -27.448 -21.153 1.00 131.35 ? 225  GLN   D CD  1 
ATOM   9756  O  OE1 . GLN   D 1 156 ? 49.793  -26.234 -21.138 1.00 125.24 ? 225  GLN   D OE1 1 
ATOM   9757  N  NE2 . GLN   D 1 156 ? 49.604  -28.297 -20.214 1.00 130.67 ? 225  GLN   D NE2 1 
ATOM   9758  N  N   . LYS   D 1 157 ? 48.673  -29.345 -25.902 1.00 116.35 ? 226  LYS   D N   1 
ATOM   9759  C  CA  . LYS   D 1 157 ? 48.058  -29.523 -27.213 1.00 105.86 ? 226  LYS   D CA  1 
ATOM   9760  C  C   . LYS   D 1 157 ? 46.555  -29.719 -27.076 1.00 99.74  ? 226  LYS   D C   1 
ATOM   9761  O  O   . LYS   D 1 157 ? 45.776  -29.123 -27.821 1.00 96.53  ? 226  LYS   D O   1 
ATOM   9762  C  CB  . LYS   D 1 157 ? 48.696  -30.713 -27.925 1.00 107.25 ? 226  LYS   D CB  1 
ATOM   9763  N  N   . TYR   D 1 158 ? 46.134  -30.521 -26.100 1.00 101.70 ? 227  TYR   D N   1 
ATOM   9764  C  CA  . TYR   D 1 158 ? 44.711  -30.704 -25.827 1.00 99.81  ? 227  TYR   D CA  1 
ATOM   9765  C  C   . TYR   D 1 158 ? 43.996  -29.365 -25.723 1.00 98.62  ? 227  TYR   D C   1 
ATOM   9766  O  O   . TYR   D 1 158 ? 43.025  -29.109 -26.450 1.00 98.56  ? 227  TYR   D O   1 
ATOM   9767  C  CB  . TYR   D 1 158 ? 44.554  -31.537 -24.548 1.00 100.70 ? 227  TYR   D CB  1 
ATOM   9768  C  CG  . TYR   D 1 158 ? 43.136  -31.730 -24.068 1.00 95.61  ? 227  TYR   D CG  1 
ATOM   9769  C  CD1 . TYR   D 1 158 ? 42.359  -32.786 -24.530 1.00 98.66  ? 227  TYR   D CD1 1 
ATOM   9770  C  CD2 . TYR   D 1 158 ? 42.579  -30.854 -23.144 1.00 96.64  ? 227  TYR   D CD2 1 
ATOM   9771  C  CE1 . TYR   D 1 158 ? 41.058  -32.961 -24.082 1.00 103.18 ? 227  TYR   D CE1 1 
ATOM   9772  C  CE2 . TYR   D 1 158 ? 41.281  -31.018 -22.692 1.00 95.18  ? 227  TYR   D CE2 1 
ATOM   9773  C  CZ  . TYR   D 1 158 ? 40.523  -32.074 -23.165 1.00 96.55  ? 227  TYR   D CZ  1 
ATOM   9774  O  OH  . TYR   D 1 158 ? 39.228  -32.251 -22.728 1.00 97.86  ? 227  TYR   D OH  1 
ATOM   9775  N  N   . GLN   D 1 159 ? 44.496  -28.466 -24.862 1.00 98.65  ? 228  GLN   D N   1 
ATOM   9776  C  CA  . GLN   D 1 159 ? 43.859  -27.161 -24.691 1.00 96.72  ? 228  GLN   D CA  1 
ATOM   9777  C  C   . GLN   D 1 159 ? 43.873  -26.344 -25.988 1.00 96.87  ? 228  GLN   D C   1 
ATOM   9778  O  O   . GLN   D 1 159 ? 42.857  -25.726 -26.339 1.00 95.89  ? 228  GLN   D O   1 
ATOM   9779  C  CB  . GLN   D 1 159 ? 44.529  -26.369 -23.561 1.00 95.17  ? 228  GLN   D CB  1 
ATOM   9780  C  CG  . GLN   D 1 159 ? 44.106  -24.885 -23.556 1.00 95.54  ? 228  GLN   D CG  1 
ATOM   9781  C  CD  . GLN   D 1 159 ? 44.744  -24.037 -22.457 1.00 93.58  ? 228  GLN   D CD  1 
ATOM   9782  O  OE1 . GLN   D 1 159 ? 44.369  -24.125 -21.284 1.00 92.29  ? 228  GLN   D OE1 1 
ATOM   9783  N  NE2 . GLN   D 1 159 ? 45.685  -23.174 -22.849 1.00 96.84  ? 228  GLN   D NE2 1 
ATOM   9784  N  N   . LYS   D 1 160 ? 45.005  -26.316 -26.707 1.00 98.76  ? 229  LYS   D N   1 
ATOM   9785  C  CA  . LYS   D 1 160 ? 45.090  -25.505 -27.919 1.00 91.57  ? 229  LYS   D CA  1 
ATOM   9786  C  C   . LYS   D 1 160 ? 44.084  -25.963 -28.971 1.00 91.83  ? 229  LYS   D C   1 
ATOM   9787  O  O   . LYS   D 1 160 ? 43.436  -25.134 -29.616 1.00 96.42  ? 229  LYS   D O   1 
ATOM   9788  C  CB  . LYS   D 1 160 ? 46.511  -25.525 -28.473 1.00 90.30  ? 229  LYS   D CB  1 
ATOM   9789  N  N   . ARG   D 1 161 ? 43.897  -27.275 -29.136 1.00 93.69  ? 230  ARG   D N   1 
ATOM   9790  C  CA  . ARG   D 1 161 ? 42.966  -27.745 -30.164 1.00 93.29  ? 230  ARG   D CA  1 
ATOM   9791  C  C   . ARG   D 1 161 ? 41.504  -27.644 -29.713 1.00 96.21  ? 230  ARG   D C   1 
ATOM   9792  O  O   . ARG   D 1 161 ? 40.695  -26.997 -30.390 1.00 97.00  ? 230  ARG   D O   1 
ATOM   9793  C  CB  . ARG   D 1 161 ? 43.312  -29.181 -30.582 1.00 88.90  ? 230  ARG   D CB  1 
ATOM   9794  N  N   . LYS   D 1 162 ? 41.153  -28.247 -28.559 1.00 95.89  ? 231  LYS   D N   1 
ATOM   9795  C  CA  . LYS   D 1 162 ? 39.746  -28.364 -28.145 1.00 96.30  ? 231  LYS   D CA  1 
ATOM   9796  C  C   . LYS   D 1 162 ? 39.086  -27.004 -27.957 1.00 94.86  ? 231  LYS   D C   1 
ATOM   9797  O  O   . LYS   D 1 162 ? 37.913  -26.809 -28.311 1.00 94.18  ? 231  LYS   D O   1 
ATOM   9798  C  CB  . LYS   D 1 162 ? 39.636  -29.163 -26.848 1.00 90.81  ? 231  LYS   D CB  1 
ATOM   9799  C  CG  . LYS   D 1 162 ? 38.210  -29.467 -26.447 1.00 90.79  ? 231  LYS   D CG  1 
ATOM   9800  C  CD  . LYS   D 1 162 ? 38.109  -30.244 -25.137 1.00 93.80  ? 231  LYS   D CD  1 
ATOM   9801  C  CE  . LYS   D 1 162 ? 36.693  -30.820 -24.974 1.00 98.40  ? 231  LYS   D CE  1 
ATOM   9802  N  NZ  . LYS   D 1 162 ? 36.428  -31.580 -23.717 1.00 97.63  ? 231  LYS   D NZ  1 
ATOM   9803  N  N   . PHE   D 1 163 ? 39.809  -26.067 -27.353 1.00 92.32  ? 232  PHE   D N   1 
ATOM   9804  C  CA  . PHE   D 1 163 ? 39.315  -24.720 -27.096 1.00 89.26  ? 232  PHE   D CA  1 
ATOM   9805  C  C   . PHE   D 1 163 ? 39.888  -23.718 -28.091 1.00 97.08  ? 232  PHE   D C   1 
ATOM   9806  O  O   . PHE   D 1 163 ? 40.249  -22.594 -27.717 1.00 98.94  ? 232  PHE   D O   1 
ATOM   9807  C  CB  . PHE   D 1 163 ? 39.644  -24.322 -25.666 1.00 86.48  ? 232  PHE   D CB  1 
ATOM   9808  C  CG  . PHE   D 1 163 ? 39.160  -25.311 -24.642 1.00 84.67  ? 232  PHE   D CG  1 
ATOM   9809  C  CD1 . PHE   D 1 163 ? 37.830  -25.329 -24.246 1.00 84.42  ? 232  PHE   D CD1 1 
ATOM   9810  C  CD2 . PHE   D 1 163 ? 40.023  -26.228 -24.082 1.00 83.77  ? 232  PHE   D CD2 1 
ATOM   9811  C  CE1 . PHE   D 1 163 ? 37.379  -26.234 -23.297 1.00 80.30  ? 232  PHE   D CE1 1 
ATOM   9812  C  CE2 . PHE   D 1 163 ? 39.571  -27.136 -23.141 1.00 81.69  ? 232  PHE   D CE2 1 
ATOM   9813  C  CZ  . PHE   D 1 163 ? 38.251  -27.137 -22.754 1.00 79.68  ? 232  PHE   D CZ  1 
ATOM   9814  N  N   . HIS   D 1 164 ? 39.981  -24.107 -29.371 1.00 97.20  ? 233  HIS   D N   1 
ATOM   9815  C  CA  . HIS   D 1 164 ? 40.520  -23.234 -30.410 1.00 90.48  ? 233  HIS   D CA  1 
ATOM   9816  C  C   . HIS   D 1 164 ? 39.537  -22.097 -30.664 1.00 88.99  ? 233  HIS   D C   1 
ATOM   9817  O  O   . HIS   D 1 164 ? 39.842  -20.925 -30.395 1.00 87.09  ? 233  HIS   D O   1 
ATOM   9818  C  CB  . HIS   D 1 164 ? 40.757  -23.995 -31.701 1.00 88.75  ? 233  HIS   D CB  1 
ATOM   9819  C  CG  . HIS   D 1 164 ? 41.330  -23.154 -32.801 1.00 95.61  ? 233  HIS   D CG  1 
ATOM   9820  N  ND1 . HIS   D 1 164 ? 40.620  -22.798 -33.933 1.00 99.02  ? 233  HIS   D ND1 1 
ATOM   9821  C  CD2 . HIS   D 1 164 ? 42.564  -22.615 -32.950 1.00 96.93  ? 233  HIS   D CD2 1 
ATOM   9822  C  CE1 . HIS   D 1 164 ? 41.388  -22.065 -34.723 1.00 96.69  ? 233  HIS   D CE1 1 
ATOM   9823  N  NE2 . HIS   D 1 164 ? 42.571  -21.938 -34.148 1.00 96.64  ? 233  HIS   D NE2 1 
ATOM   9824  N  N   . CYS   D 1 165 ? 38.340  -22.411 -31.166 1.00 96.24  ? 234  CYS   D N   1 
ATOM   9825  C  CA  . CYS   D 1 165 ? 37.359  -21.341 -31.492 1.00 97.92  ? 234  CYS   D CA  1 
ATOM   9826  C  C   . CYS   D 1 165 ? 36.859  -20.981 -30.084 1.00 95.22  ? 234  CYS   D C   1 
ATOM   9827  O  O   . CYS   D 1 165 ? 35.674  -21.153 -29.742 1.00 93.85  ? 234  CYS   D O   1 
ATOM   9828  C  CB  . CYS   D 1 165 ? 36.159  -21.917 -32.281 1.00 102.05 ? 234  CYS   D CB  1 
ATOM   9829  S  SG  . CYS   D 1 165 ? 35.738  -23.576 -31.802 1.00 115.01 ? 234  CYS   D SG  1 
ATOM   9830  N  N   . ALA   D 1 166 ? 37.763  -20.615 -29.201 1.00 85.98  ? 235  ALA   D N   1 
ATOM   9831  C  CA  . ALA   D 1 166 ? 37.306  -19.912 -27.998 1.00 85.57  ? 235  ALA   D CA  1 
ATOM   9832  C  C   . ALA   D 1 166 ? 37.714  -18.517 -28.374 1.00 84.73  ? 235  ALA   D C   1 
ATOM   9833  O  O   . ALA   D 1 166 ? 37.550  -17.611 -27.574 1.00 83.41  ? 235  ALA   D O   1 
ATOM   9834  C  CB  . ALA   D 1 166 ? 38.105  -20.419 -26.806 1.00 90.88  ? 235  ALA   D CB  1 
ATOM   9835  N  N   . ASN   D 1 167 ? 38.308  -18.344 -29.571 1.00 84.87  ? 236  ASN   D N   1 
ATOM   9836  C  CA  . ASN   D 1 167 ? 38.649  -17.017 -30.064 1.00 83.21  ? 236  ASN   D CA  1 
ATOM   9837  C  C   . ASN   D 1 167 ? 37.426  -16.270 -30.554 1.00 80.11  ? 236  ASN   D C   1 
ATOM   9838  O  O   . ASN   D 1 167 ? 37.391  -15.037 -30.504 1.00 80.75  ? 236  ASN   D O   1 
ATOM   9839  C  CB  . ASN   D 1 167 ? 39.688  -17.141 -31.153 1.00 82.29  ? 236  ASN   D CB  1 
ATOM   9840  C  CG  . ASN   D 1 167 ? 40.946  -17.672 -30.630 1.00 85.06  ? 236  ASN   D CG  1 
ATOM   9841  O  OD1 . ASN   D 1 167 ? 41.630  -18.435 -31.276 1.00 93.49  ? 236  ASN   D OD1 1 
ATOM   9842  N  ND2 . ASN   D 1 167 ? 41.277  -17.258 -29.428 1.00 88.33  ? 236  ASN   D ND2 1 
ATOM   9843  N  N   . LEU   D 1 168 ? 36.402  -17.000 -30.974 1.00 81.58  ? 237  LEU   D N   1 
ATOM   9844  C  CA  . LEU   D 1 168 ? 35.151  -16.370 -31.343 1.00 83.85  ? 237  LEU   D CA  1 
ATOM   9845  C  C   . LEU   D 1 168 ? 34.449  -15.750 -30.140 1.00 82.29  ? 237  LEU   D C   1 
ATOM   9846  O  O   . LEU   D 1 168 ? 33.570  -14.895 -30.308 1.00 77.89  ? 237  LEU   D O   1 
ATOM   9847  C  CB  . LEU   D 1 168 ? 34.275  -17.417 -32.014 1.00 85.50  ? 237  LEU   D CB  1 
ATOM   9848  C  CG  . LEU   D 1 168 ? 35.025  -18.156 -33.103 1.00 79.21  ? 237  LEU   D CG  1 
ATOM   9849  C  CD1 . LEU   D 1 168 ? 34.197  -19.317 -33.444 1.00 95.23  ? 237  LEU   D CD1 1 
ATOM   9850  C  CD2 . LEU   D 1 168 ? 35.152  -17.274 -34.297 1.00 75.93  ? 237  LEU   D CD2 1 
ATOM   9851  N  N   . THR   D 1 169 ? 34.855  -16.139 -28.941 1.00 82.02  ? 238  THR   D N   1 
ATOM   9852  C  CA  . THR   D 1 169 ? 34.208  -15.808 -27.690 1.00 80.09  ? 238  THR   D CA  1 
ATOM   9853  C  C   . THR   D 1 169 ? 35.046  -14.782 -26.956 1.00 78.96  ? 238  THR   D C   1 
ATOM   9854  O  O   . THR   D 1 169 ? 36.161  -14.466 -27.366 1.00 78.58  ? 238  THR   D O   1 
ATOM   9855  C  CB  . THR   D 1 169 ? 34.026  -17.075 -26.849 1.00 83.66  ? 238  THR   D CB  1 
ATOM   9856  O  OG1 . THR   D 1 169 ? 35.283  -17.453 -26.284 1.00 84.59  ? 238  THR   D OG1 1 
ATOM   9857  C  CG2 . THR   D 1 169 ? 33.571  -18.220 -27.727 1.00 84.86  ? 238  THR   D CG2 1 
ATOM   9858  N  N   . SER   D 1 170 ? 34.496  -14.249 -25.862 1.00 88.93  ? 239  SER   D N   1 
ATOM   9859  C  CA  . SER   D 1 170 ? 35.127  -13.140 -25.148 1.00 89.92  ? 239  SER   D CA  1 
ATOM   9860  C  C   . SER   D 1 170 ? 35.976  -13.607 -23.975 1.00 89.65  ? 239  SER   D C   1 
ATOM   9861  O  O   . SER   D 1 170 ? 36.320  -12.794 -23.115 1.00 89.66  ? 239  SER   D O   1 
ATOM   9862  C  CB  . SER   D 1 170 ? 34.079  -12.125 -24.673 1.00 89.87  ? 239  SER   D CB  1 
ATOM   9863  O  OG  . SER   D 1 170 ? 33.134  -12.751 -23.821 1.00 91.12  ? 239  SER   D OG  1 
ATOM   9864  N  N   . TRP   D 1 171 ? 36.318  -14.896 -23.932 1.00 81.66  ? 240  TRP   D N   1 
ATOM   9865  C  CA  . TRP   D 1 171 ? 37.119  -15.506 -22.880 1.00 77.71  ? 240  TRP   D CA  1 
ATOM   9866  C  C   . TRP   D 1 171 ? 38.266  -16.302 -23.495 1.00 79.30  ? 240  TRP   D C   1 
ATOM   9867  O  O   . TRP   D 1 171 ? 38.183  -16.715 -24.661 1.00 79.91  ? 240  TRP   D O   1 
ATOM   9868  C  CB  . TRP   D 1 171 ? 36.270  -16.433 -22.000 1.00 75.37  ? 240  TRP   D CB  1 
ATOM   9869  C  CG  . TRP   D 1 171 ? 35.172  -15.738 -21.260 1.00 76.67  ? 240  TRP   D CG  1 
ATOM   9870  C  CD1 . TRP   D 1 171 ? 33.838  -15.966 -21.389 1.00 78.38  ? 240  TRP   D CD1 1 
ATOM   9871  C  CD2 . TRP   D 1 171 ? 35.310  -14.709 -20.259 1.00 78.16  ? 240  TRP   D CD2 1 
ATOM   9872  N  NE1 . TRP   D 1 171 ? 33.138  -15.144 -20.539 1.00 81.27  ? 240  TRP   D NE1 1 
ATOM   9873  C  CE2 . TRP   D 1 171 ? 34.019  -14.366 -19.834 1.00 80.00  ? 240  TRP   D CE2 1 
ATOM   9874  C  CE3 . TRP   D 1 171 ? 36.399  -14.051 -19.682 1.00 77.83  ? 240  TRP   D CE3 1 
ATOM   9875  C  CZ2 . TRP   D 1 171 ? 33.786  -13.397 -18.861 1.00 80.34  ? 240  TRP   D CZ2 1 
ATOM   9876  C  CZ3 . TRP   D 1 171 ? 36.161  -13.085 -18.723 1.00 74.40  ? 240  TRP   D CZ3 1 
ATOM   9877  C  CH2 . TRP   D 1 171 ? 34.870  -12.767 -18.326 1.00 76.84  ? 240  TRP   D CH2 1 
ATOM   9878  N  N   . PRO   D 1 172 ? 39.352  -16.522 -22.744 1.00 78.63  ? 241  PRO   D N   1 
ATOM   9879  C  CA  . PRO   D 1 172 ? 40.498  -17.267 -23.271 1.00 79.98  ? 241  PRO   D CA  1 
ATOM   9880  C  C   . PRO   D 1 172 ? 40.430  -18.759 -22.987 1.00 83.18  ? 241  PRO   D C   1 
ATOM   9881  O  O   . PRO   D 1 172 ? 39.730  -19.225 -22.086 1.00 82.20  ? 241  PRO   D O   1 
ATOM   9882  C  CB  . PRO   D 1 172 ? 41.699  -16.660 -22.527 1.00 79.33  ? 241  PRO   D CB  1 
ATOM   9883  C  CG  . PRO   D 1 172 ? 41.148  -15.844 -21.429 1.00 80.63  ? 241  PRO   D CG  1 
ATOM   9884  C  CD  . PRO   D 1 172 ? 39.652  -16.008 -21.400 1.00 80.03  ? 241  PRO   D CD  1 
ATOM   9885  N  N   . ARG   D 1 173 ? 41.221  -19.488 -23.779 1.00 86.53  ? 242  ARG   D N   1 
ATOM   9886  C  CA  . ARG   D 1 173 ? 41.388  -20.929 -23.666 1.00 88.51  ? 242  ARG   D CA  1 
ATOM   9887  C  C   . ARG   D 1 173 ? 41.442  -21.397 -22.222 1.00 87.16  ? 242  ARG   D C   1 
ATOM   9888  O  O   . ARG   D 1 173 ? 40.624  -22.213 -21.786 1.00 87.74  ? 242  ARG   D O   1 
ATOM   9889  C  CB  . ARG   D 1 173 ? 42.674  -21.344 -24.384 1.00 92.64  ? 242  ARG   D CB  1 
ATOM   9890  C  CG  . ARG   D 1 173 ? 42.463  -21.920 -25.755 1.00 95.34  ? 242  ARG   D CG  1 
ATOM   9891  C  CD  . ARG   D 1 173 ? 43.773  -22.386 -26.359 1.00 97.96  ? 242  ARG   D CD  1 
ATOM   9892  N  NE  . ARG   D 1 173 ? 44.496  -21.346 -27.084 1.00 108.18 ? 242  ARG   D NE  1 
ATOM   9893  C  CZ  . ARG   D 1 173 ? 45.822  -21.298 -27.175 1.00 116.50 ? 242  ARG   D CZ  1 
ATOM   9894  N  NH1 . ARG   D 1 173 ? 46.586  -22.219 -26.596 1.00 112.35 ? 242  ARG   D NH1 1 
ATOM   9895  N  NH2 . ARG   D 1 173 ? 46.399  -20.288 -27.837 1.00 117.29 ? 242  ARG   D NH2 1 
ATOM   9896  N  N   . TRP   D 1 174 ? 42.416  -20.883 -21.471 1.00 80.87  ? 243  TRP   D N   1 
ATOM   9897  C  CA  . TRP   D 1 174 ? 42.690  -21.432 -20.150 1.00 81.49  ? 243  TRP   D CA  1 
ATOM   9898  C  C   . TRP   D 1 174 ? 41.482  -21.360 -19.231 1.00 82.78  ? 243  TRP   D C   1 
ATOM   9899  O  O   . TRP   D 1 174 ? 41.398  -22.149 -18.278 1.00 87.32  ? 243  TRP   D O   1 
ATOM   9900  C  CB  . TRP   D 1 174 ? 43.888  -20.726 -19.494 1.00 84.99  ? 243  TRP   D CB  1 
ATOM   9901  C  CG  . TRP   D 1 174 ? 43.943  -19.187 -19.505 1.00 83.24  ? 243  TRP   D CG  1 
ATOM   9902  C  CD1 . TRP   D 1 174 ? 44.657  -18.405 -20.378 1.00 84.44  ? 243  TRP   D CD1 1 
ATOM   9903  C  CD2 . TRP   D 1 174 ? 43.334  -18.280 -18.570 1.00 79.02  ? 243  TRP   D CD2 1 
ATOM   9904  N  NE1 . TRP   D 1 174 ? 44.504  -17.078 -20.066 1.00 83.94  ? 243  TRP   D NE1 1 
ATOM   9905  C  CE2 . TRP   D 1 174 ? 43.695  -16.973 -18.963 1.00 83.25  ? 243  TRP   D CE2 1 
ATOM   9906  C  CE3 . TRP   D 1 174 ? 42.499  -18.443 -17.463 1.00 77.89  ? 243  TRP   D CE3 1 
ATOM   9907  C  CZ2 . TRP   D 1 174 ? 43.257  -15.837 -18.274 1.00 84.82  ? 243  TRP   D CZ2 1 
ATOM   9908  C  CZ3 . TRP   D 1 174 ? 42.066  -17.320 -16.787 1.00 79.42  ? 243  TRP   D CZ3 1 
ATOM   9909  C  CH2 . TRP   D 1 174 ? 42.450  -16.033 -17.188 1.00 82.11  ? 243  TRP   D CH2 1 
ATOM   9910  N  N   . LEU   D 1 175 ? 40.550  -20.424 -19.478 1.00 80.42  ? 244  LEU   D N   1 
ATOM   9911  C  CA  . LEU   D 1 175 ? 39.362  -20.351 -18.632 1.00 77.03  ? 244  LEU   D CA  1 
ATOM   9912  C  C   . LEU   D 1 175 ? 38.366  -21.449 -18.994 1.00 79.68  ? 244  LEU   D C   1 
ATOM   9913  O  O   . LEU   D 1 175 ? 37.735  -22.036 -18.109 1.00 81.00  ? 244  LEU   D O   1 
ATOM   9914  C  CB  . LEU   D 1 175 ? 38.711  -18.971 -18.713 1.00 73.27  ? 244  LEU   D CB  1 
ATOM   9915  C  CG  . LEU   D 1 175 ? 37.317  -18.953 -18.074 1.00 73.13  ? 244  LEU   D CG  1 
ATOM   9916  C  CD1 . LEU   D 1 175 ? 37.331  -18.889 -16.549 1.00 79.50  ? 244  LEU   D CD1 1 
ATOM   9917  C  CD2 . LEU   D 1 175 ? 36.462  -17.864 -18.627 1.00 79.22  ? 244  LEU   D CD2 1 
ATOM   9918  N  N   . TYR   D 1 176 ? 38.230  -21.771 -20.283 1.00 81.26  ? 245  TYR   D N   1 
ATOM   9919  C  CA  . TYR   D 1 176 ? 37.365  -22.880 -20.663 1.00 79.60  ? 245  TYR   D CA  1 
ATOM   9920  C  C   . TYR   D 1 176 ? 37.938  -24.206 -20.203 1.00 80.45  ? 245  TYR   D C   1 
ATOM   9921  O  O   . TYR   D 1 176 ? 37.177  -25.166 -20.037 1.00 83.89  ? 245  TYR   D O   1 
ATOM   9922  C  CB  . TYR   D 1 176 ? 37.134  -22.894 -22.183 1.00 81.27  ? 245  TYR   D CB  1 
ATOM   9923  C  CG  . TYR   D 1 176 ? 36.337  -21.710 -22.689 1.00 79.26  ? 245  TYR   D CG  1 
ATOM   9924  C  CD1 . TYR   D 1 176 ? 34.969  -21.650 -22.504 1.00 79.27  ? 245  TYR   D CD1 1 
ATOM   9925  C  CD2 . TYR   D 1 176 ? 36.960  -20.643 -23.333 1.00 76.53  ? 245  TYR   D CD2 1 
ATOM   9926  C  CE1 . TYR   D 1 176 ? 34.246  -20.567 -22.943 1.00 82.72  ? 245  TYR   D CE1 1 
ATOM   9927  C  CE2 . TYR   D 1 176 ? 36.249  -19.570 -23.768 1.00 75.95  ? 245  TYR   D CE2 1 
ATOM   9928  C  CZ  . TYR   D 1 176 ? 34.886  -19.526 -23.577 1.00 77.67  ? 245  TYR   D CZ  1 
ATOM   9929  O  OH  . TYR   D 1 176 ? 34.142  -18.443 -24.016 1.00 74.54  ? 245  TYR   D OH  1 
ATOM   9930  N  N   . SER   D 1 177 ? 39.260  -24.279 -20.002 1.00 80.11  ? 246  SER   D N   1 
ATOM   9931  C  CA  . SER   D 1 177 ? 39.866  -25.456 -19.383 1.00 79.10  ? 246  SER   D CA  1 
ATOM   9932  C  C   . SER   D 1 177 ? 39.441  -25.583 -17.925 1.00 81.17  ? 246  SER   D C   1 
ATOM   9933  O  O   . SER   D 1 177 ? 39.210  -26.694 -17.430 1.00 82.84  ? 246  SER   D O   1 
ATOM   9934  C  CB  . SER   D 1 177 ? 41.395  -25.378 -19.482 1.00 78.45  ? 246  SER   D CB  1 
ATOM   9935  O  OG  . SER   D 1 177 ? 41.846  -25.543 -20.806 1.00 75.11  ? 246  SER   D OG  1 
ATOM   9936  N  N   . LEU   D 1 178 ? 39.318  -24.449 -17.229 1.00 82.19  ? 247  LEU   D N   1 
ATOM   9937  C  CA  . LEU   D 1 178 ? 38.933  -24.471 -15.824 1.00 79.07  ? 247  LEU   D CA  1 
ATOM   9938  C  C   . LEU   D 1 178 ? 37.587  -25.153 -15.638 1.00 77.63  ? 247  LEU   D C   1 
ATOM   9939  O  O   . LEU   D 1 178 ? 37.396  -25.905 -14.681 1.00 82.05  ? 247  LEU   D O   1 
ATOM   9940  C  CB  . LEU   D 1 178 ? 38.916  -23.051 -15.247 1.00 74.42  ? 247  LEU   D CB  1 
ATOM   9941  C  CG  . LEU   D 1 178 ? 40.250  -22.306 -15.239 1.00 74.00  ? 247  LEU   D CG  1 
ATOM   9942  C  CD1 . LEU   D 1 178 ? 40.156  -21.089 -14.396 1.00 73.85  ? 247  LEU   D CD1 1 
ATOM   9943  C  CD2 . LEU   D 1 178 ? 41.367  -23.197 -14.765 1.00 76.94  ? 247  LEU   D CD2 1 
ATOM   9944  N  N   . TYR   D 1 179 ? 36.654  -24.945 -16.569 1.00 76.02  ? 248  TYR   D N   1 
ATOM   9945  C  CA  . TYR   D 1 179 ? 35.338  -25.562 -16.508 1.00 75.73  ? 248  TYR   D CA  1 
ATOM   9946  C  C   . TYR   D 1 179 ? 35.222  -26.818 -17.370 1.00 77.75  ? 248  TYR   D C   1 
ATOM   9947  O  O   . TYR   D 1 179 ? 34.105  -27.227 -17.692 1.00 82.02  ? 248  TYR   D O   1 
ATOM   9948  C  CB  . TYR   D 1 179 ? 34.261  -24.559 -16.924 1.00 77.21  ? 248  TYR   D CB  1 
ATOM   9949  C  CG  . TYR   D 1 179 ? 34.084  -23.363 -16.003 1.00 79.82  ? 248  TYR   D CG  1 
ATOM   9950  C  CD1 . TYR   D 1 179 ? 34.742  -22.172 -16.263 1.00 81.64  ? 248  TYR   D CD1 1 
ATOM   9951  C  CD2 . TYR   D 1 179 ? 33.230  -23.408 -14.897 1.00 80.84  ? 248  TYR   D CD2 1 
ATOM   9952  C  CE1 . TYR   D 1 179 ? 34.583  -21.059 -15.441 1.00 84.36  ? 248  TYR   D CE1 1 
ATOM   9953  C  CE2 . TYR   D 1 179 ? 33.058  -22.300 -14.063 1.00 82.57  ? 248  TYR   D CE2 1 
ATOM   9954  C  CZ  . TYR   D 1 179 ? 33.744  -21.123 -14.341 1.00 86.61  ? 248  TYR   D CZ  1 
ATOM   9955  O  OH  . TYR   D 1 179 ? 33.617  -19.990 -13.546 1.00 91.54  ? 248  TYR   D OH  1 
ATOM   9956  N  N   . ASP   D 1 180 ? 36.330  -27.454 -17.750 1.00 78.10  ? 249  ASP   D N   1 
ATOM   9957  C  CA  . ASP   D 1 180 ? 36.280  -28.605 -18.652 1.00 82.35  ? 249  ASP   D CA  1 
ATOM   9958  C  C   . ASP   D 1 180 ? 36.329  -29.921 -17.885 1.00 85.19  ? 249  ASP   D C   1 
ATOM   9959  O  O   . ASP   D 1 180 ? 37.279  -30.162 -17.132 1.00 88.75  ? 249  ASP   D O   1 
ATOM   9960  C  CB  . ASP   D 1 180 ? 37.428  -28.548 -19.652 1.00 84.64  ? 249  ASP   D CB  1 
ATOM   9961  C  CG  . ASP   D 1 180 ? 37.464  -29.759 -20.553 1.00 89.17  ? 249  ASP   D CG  1 
ATOM   9962  O  OD1 . ASP   D 1 180 ? 36.384  -30.192 -21.041 1.00 89.02  ? 249  ASP   D OD1 1 
ATOM   9963  O  OD2 . ASP   D 1 180 ? 38.582  -30.263 -20.781 1.00 89.59  ? 249  ASP   D OD2 1 
ATOM   9964  N  N   . ALA   D 1 181 ? 35.328  -30.782 -18.103 1.00 82.35  ? 250  ALA   D N   1 
ATOM   9965  C  CA  . ALA   D 1 181 ? 35.237  -32.030 -17.357 1.00 82.28  ? 250  ALA   D CA  1 
ATOM   9966  C  C   . ALA   D 1 181 ? 36.535  -32.820 -17.427 1.00 91.91  ? 250  ALA   D C   1 
ATOM   9967  O  O   . ALA   D 1 181 ? 37.141  -33.128 -16.401 1.00 93.57  ? 250  ALA   D O   1 
ATOM   9968  C  CB  . ALA   D 1 181 ? 34.078  -32.872 -17.881 1.00 88.18  ? 250  ALA   D CB  1 
ATOM   9969  N  N   . GLU   D 1 182 ? 36.992  -33.143 -18.639 1.00 105.39 ? 251  GLU   D N   1 
ATOM   9970  C  CA  . GLU   D 1 182 ? 38.154  -34.025 -18.773 1.00 108.50 ? 251  GLU   D CA  1 
ATOM   9971  C  C   . GLU   D 1 182 ? 39.410  -33.407 -18.155 1.00 106.31 ? 251  GLU   D C   1 
ATOM   9972  O  O   . GLU   D 1 182 ? 40.207  -34.112 -17.524 1.00 106.14 ? 251  GLU   D O   1 
ATOM   9973  C  CB  . GLU   D 1 182 ? 38.390  -34.384 -20.245 1.00 110.27 ? 251  GLU   D CB  1 
ATOM   9974  C  CG  . GLU   D 1 182 ? 37.127  -34.492 -21.107 1.00 112.73 ? 251  GLU   D CG  1 
ATOM   9975  C  CD  . GLU   D 1 182 ? 36.171  -35.600 -20.664 1.00 121.83 ? 251  GLU   D CD  1 
ATOM   9976  O  OE1 . GLU   D 1 182 ? 36.643  -36.735 -20.410 1.00 126.42 ? 251  GLU   D OE1 1 
ATOM   9977  O  OE2 . GLU   D 1 182 ? 34.944  -35.336 -20.581 1.00 120.79 ? 251  GLU   D OE2 1 
ATOM   9978  N  N   . THR   D 1 183 ? 39.607  -32.095 -18.323 1.00 93.64  ? 252  THR   D N   1 
ATOM   9979  C  CA  . THR   D 1 183 ? 40.741  -31.427 -17.686 1.00 89.08  ? 252  THR   D CA  1 
ATOM   9980  C  C   . THR   D 1 183 ? 40.642  -31.528 -16.176 1.00 88.77  ? 252  THR   D C   1 
ATOM   9981  O  O   . THR   D 1 183 ? 41.613  -31.876 -15.500 1.00 89.09  ? 252  THR   D O   1 
ATOM   9982  C  CB  . THR   D 1 183 ? 40.799  -29.953 -18.088 1.00 88.75  ? 252  THR   D CB  1 
ATOM   9983  O  OG1 . THR   D 1 183 ? 41.103  -29.832 -19.482 1.00 89.81  ? 252  THR   D OG1 1 
ATOM   9984  C  CG2 . THR   D 1 183 ? 41.858  -29.200 -17.245 1.00 88.70  ? 252  THR   D CG2 1 
ATOM   9985  N  N   . LEU   D 1 184 ? 39.465  -31.214 -15.631 1.00 88.06  ? 253  LEU   D N   1 
ATOM   9986  C  CA  . LEU   D 1 184 ? 39.268  -31.254 -14.186 1.00 85.37  ? 253  LEU   D CA  1 
ATOM   9987  C  C   . LEU   D 1 184 ? 39.572  -32.640 -13.633 1.00 85.09  ? 253  LEU   D C   1 
ATOM   9988  O  O   . LEU   D 1 184 ? 40.391  -32.789 -12.718 1.00 86.22  ? 253  LEU   D O   1 
ATOM   9989  C  CB  . LEU   D 1 184 ? 37.838  -30.825 -13.834 1.00 79.76  ? 253  LEU   D CB  1 
ATOM   9990  C  CG  . LEU   D 1 184 ? 37.491  -29.341 -14.023 1.00 75.73  ? 253  LEU   D CG  1 
ATOM   9991  C  CD1 . LEU   D 1 184 ? 35.996  -29.093 -13.872 1.00 74.97  ? 253  LEU   D CD1 1 
ATOM   9992  C  CD2 . LEU   D 1 184 ? 38.311  -28.436 -13.099 1.00 78.32  ? 253  LEU   D CD2 1 
ATOM   9993  N  N   . MET   D 1 185 ? 38.945  -33.673 -14.203 1.00 84.34  ? 254  MET   D N   1 
ATOM   9994  C  CA  . MET   D 1 185 ? 39.142  -35.029 -13.705 1.00 80.85  ? 254  MET   D CA  1 
ATOM   9995  C  C   . MET   D 1 185 ? 40.619  -35.431 -13.708 1.00 87.08  ? 254  MET   D C   1 
ATOM   9996  O  O   . MET   D 1 185 ? 41.093  -36.054 -12.748 1.00 88.98  ? 254  MET   D O   1 
ATOM   9997  C  CB  . MET   D 1 185 ? 38.303  -35.986 -14.533 1.00 79.81  ? 254  MET   D CB  1 
ATOM   9998  C  CG  . MET   D 1 185 ? 36.839  -35.719 -14.400 1.00 82.49  ? 254  MET   D CG  1 
ATOM   9999  S  SD  . MET   D 1 185 ? 35.943  -36.695 -15.611 1.00 90.90  ? 254  MET   D SD  1 
ATOM   10000 C  CE  . MET   D 1 185 ? 36.672  -38.309 -15.257 1.00 95.03  ? 254  MET   D CE  1 
ATOM   10001 N  N   . ASP   D 1 186 ? 41.374  -35.063 -14.750 1.00 89.03  ? 255  ASP   D N   1 
ATOM   10002 C  CA  . ASP   D 1 186 ? 42.812  -35.349 -14.763 1.00 88.43  ? 255  ASP   D CA  1 
ATOM   10003 C  C   . ASP   D 1 186 ? 43.539  -34.677 -13.589 1.00 86.35  ? 255  ASP   D C   1 
ATOM   10004 O  O   . ASP   D 1 186 ? 44.434  -35.278 -12.985 1.00 87.95  ? 255  ASP   D O   1 
ATOM   10005 C  CB  . ASP   D 1 186 ? 43.395  -34.920 -16.113 1.00 92.85  ? 255  ASP   D CB  1 
ATOM   10006 C  CG  . ASP   D 1 186 ? 44.927  -34.904 -16.132 1.00 97.46  ? 255  ASP   D CG  1 
ATOM   10007 O  OD1 . ASP   D 1 186 ? 45.513  -35.961 -16.497 1.00 94.32  ? 255  ASP   D OD1 1 
ATOM   10008 O  OD2 . ASP   D 1 186 ? 45.536  -33.832 -15.818 1.00 92.60  ? 255  ASP   D OD2 1 
ATOM   10009 N  N   . ARG   D 1 187 ? 43.136  -33.452 -13.223 1.00 87.26  ? 256  ARG   D N   1 
ATOM   10010 C  CA  . ARG   D 1 187 ? 43.769  -32.715 -12.119 1.00 89.61  ? 256  ARG   D CA  1 
ATOM   10011 C  C   . ARG   D 1 187 ? 43.491  -33.365 -10.772 1.00 87.03  ? 256  ARG   D C   1 
ATOM   10012 O  O   . ARG   D 1 187 ? 44.385  -33.458 -9.919  1.00 90.44  ? 256  ARG   D O   1 
ATOM   10013 C  CB  . ARG   D 1 187 ? 43.262  -31.269 -12.078 1.00 90.91  ? 256  ARG   D CB  1 
ATOM   10014 C  CG  . ARG   D 1 187 ? 43.857  -30.321 -13.080 1.00 93.10  ? 256  ARG   D CG  1 
ATOM   10015 C  CD  . ARG   D 1 187 ? 42.953  -29.150 -13.280 1.00 88.21  ? 256  ARG   D CD  1 
ATOM   10016 N  NE  . ARG   D 1 187 ? 42.885  -28.287 -12.113 1.00 93.20  ? 256  ARG   D NE  1 
ATOM   10017 C  CZ  . ARG   D 1 187 ? 42.228  -27.138 -12.095 1.00 95.46  ? 256  ARG   D CZ  1 
ATOM   10018 N  NH1 . ARG   D 1 187 ? 41.566  -26.709 -13.156 1.00 95.40  ? 256  ARG   D NH1 1 
ATOM   10019 N  NH2 . ARG   D 1 187 ? 42.241  -26.397 -10.992 1.00 95.28  ? 256  ARG   D NH2 1 
ATOM   10020 N  N   . ILE   D 1 188 ? 42.232  -33.738 -10.535 1.00 83.01  ? 257  ILE   D N   1 
ATOM   10021 C  CA  . ILE   D 1 188 ? 41.867  -34.462 -9.322  1.00 80.21  ? 257  ILE   D CA  1 
ATOM   10022 C  C   . ILE   D 1 188 ? 42.678  -35.746 -9.213  1.00 82.10  ? 257  ILE   D C   1 
ATOM   10023 O  O   . ILE   D 1 188 ? 43.201  -36.083 -8.150  1.00 85.10  ? 257  ILE   D O   1 
ATOM   10024 C  CB  . ILE   D 1 188 ? 40.354  -34.728 -9.314  1.00 76.87  ? 257  ILE   D CB  1 
ATOM   10025 C  CG1 . ILE   D 1 188 ? 39.635  -33.390 -9.276  1.00 76.53  ? 257  ILE   D CG1 1 
ATOM   10026 C  CG2 . ILE   D 1 188 ? 39.964  -35.658 -8.184  1.00 80.38  ? 257  ILE   D CG2 1 
ATOM   10027 C  CD1 . ILE   D 1 188 ? 38.160  -33.475 -9.109  1.00 76.48  ? 257  ILE   D CD1 1 
ATOM   10028 N  N   . LYS   D 1 189 ? 42.810  -36.474 -10.317 1.00 81.25  ? 258  LYS   D N   1 
ATOM   10029 C  CA  . LYS   D 1 189 ? 43.601  -37.696 -10.288 1.00 78.76  ? 258  LYS   D CA  1 
ATOM   10030 C  C   . LYS   D 1 189 ? 45.033  -37.403 -9.877  1.00 80.75  ? 258  LYS   D C   1 
ATOM   10031 O  O   . LYS   D 1 189 ? 45.570  -38.058 -8.983  1.00 84.08  ? 258  LYS   D O   1 
ATOM   10032 C  CB  . LYS   D 1 189 ? 43.558  -38.381 -11.650 1.00 85.08  ? 258  LYS   D CB  1 
ATOM   10033 C  CG  . LYS   D 1 189 ? 42.202  -38.983 -12.007 1.00 88.47  ? 258  LYS   D CG  1 
ATOM   10034 C  CD  . LYS   D 1 189 ? 42.019  -39.109 -13.508 1.00 88.57  ? 258  LYS   D CD  1 
ATOM   10035 C  CE  . LYS   D 1 189 ? 43.294  -39.587 -14.154 1.00 94.95  ? 258  LYS   D CE  1 
ATOM   10036 N  NZ  . LYS   D 1 189 ? 43.012  -40.082 -15.509 1.00 107.11 ? 258  LYS   D NZ  1 
ATOM   10037 N  N   . LYS   D 1 190 ? 45.659  -36.400 -10.498 1.00 84.97  ? 259  LYS   D N   1 
ATOM   10038 C  CA  . LYS   D 1 190 ? 47.050  -36.068 -10.187 1.00 84.83  ? 259  LYS   D CA  1 
ATOM   10039 C  C   . LYS   D 1 190 ? 47.253  -35.883 -8.685  1.00 88.77  ? 259  LYS   D C   1 
ATOM   10040 O  O   . LYS   D 1 190 ? 48.224  -36.391 -8.109  1.00 91.47  ? 259  LYS   D O   1 
ATOM   10041 C  CB  . LYS   D 1 190 ? 47.473  -34.807 -10.952 1.00 78.96  ? 259  LYS   D CB  1 
ATOM   10042 N  N   . GLN   D 1 191 ? 46.309  -35.194 -8.031  1.00 89.81  ? 260  GLN   D N   1 
ATOM   10043 C  CA  . GLN   D 1 191 ? 46.376  -34.966 -6.587  1.00 90.40  ? 260  GLN   D CA  1 
ATOM   10044 C  C   . GLN   D 1 191 ? 46.185  -36.257 -5.808  1.00 91.62  ? 260  GLN   D C   1 
ATOM   10045 O  O   . GLN   D 1 191 ? 46.872  -36.505 -4.809  1.00 91.86  ? 260  GLN   D O   1 
ATOM   10046 C  CB  . GLN   D 1 191 ? 45.315  -33.963 -6.163  1.00 88.27  ? 260  GLN   D CB  1 
ATOM   10047 C  CG  . GLN   D 1 191 ? 45.530  -32.576 -6.678  1.00 91.96  ? 260  GLN   D CG  1 
ATOM   10048 C  CD  . GLN   D 1 191 ? 45.468  -31.572 -5.564  1.00 98.85  ? 260  GLN   D CD  1 
ATOM   10049 O  OE1 . GLN   D 1 191 ? 45.526  -31.930 -4.378  1.00 95.64  ? 260  GLN   D OE1 1 
ATOM   10050 N  NE2 . GLN   D 1 191 ? 45.347  -30.300 -5.927  1.00 107.08 ? 260  GLN   D NE2 1 
ATOM   10051 N  N   . LEU   D 1 192 ? 45.199  -37.063 -6.221  1.00 91.31  ? 261  LEU   D N   1 
ATOM   10052 C  CA  . LEU   D 1 192 ? 45.019  -38.398 -5.663  1.00 89.02  ? 261  LEU   D CA  1 
ATOM   10053 C  C   . LEU   D 1 192 ? 46.300  -39.229 -5.786  1.00 93.84  ? 261  LEU   D C   1 
ATOM   10054 O  O   . LEU   D 1 192 ? 46.647  -39.983 -4.869  1.00 99.24  ? 261  LEU   D O   1 
ATOM   10055 C  CB  . LEU   D 1 192 ? 43.832  -39.079 -6.357  1.00 81.72  ? 261  LEU   D CB  1 
ATOM   10056 C  CG  . LEU   D 1 192 ? 42.457  -38.408 -6.163  1.00 80.15  ? 261  LEU   D CG  1 
ATOM   10057 C  CD1 . LEU   D 1 192 ? 41.338  -39.050 -7.004  1.00 78.32  ? 261  LEU   D CD1 1 
ATOM   10058 C  CD2 . LEU   D 1 192 ? 42.082  -38.387 -4.691  1.00 82.00  ? 261  LEU   D CD2 1 
ATOM   10059 N  N   . ARG   D 1 193 ? 47.039  -39.070 -6.895  1.00 93.59  ? 262  ARG   D N   1 
ATOM   10060 C  CA  . ARG   D 1 193 ? 48.271  -39.833 -7.103  1.00 97.11  ? 262  ARG   D CA  1 
ATOM   10061 C  C   . ARG   D 1 193 ? 49.292  -39.597 -5.995  1.00 101.68 ? 262  ARG   D C   1 
ATOM   10062 O  O   . ARG   D 1 193 ? 50.106  -40.483 -5.708  1.00 106.39 ? 262  ARG   D O   1 
ATOM   10063 C  CB  . ARG   D 1 193 ? 48.897  -39.490 -8.459  1.00 89.69  ? 262  ARG   D CB  1 
ATOM   10064 N  N   . GLU   D 1 194 ? 49.278  -38.425 -5.355  1.00 101.58 ? 263  GLU   D N   1 
ATOM   10065 C  CA  . GLU   D 1 194 ? 50.229  -38.216 -4.275  1.00 104.30 ? 263  GLU   D CA  1 
ATOM   10066 C  C   . GLU   D 1 194 ? 49.849  -38.978 -3.005  1.00 102.78 ? 263  GLU   D C   1 
ATOM   10067 O  O   . GLU   D 1 194 ? 50.695  -39.123 -2.112  1.00 105.41 ? 263  GLU   D O   1 
ATOM   10068 C  CB  . GLU   D 1 194 ? 50.366  -36.737 -3.952  1.00 104.13 ? 263  GLU   D CB  1 
ATOM   10069 C  CG  . GLU   D 1 194 ? 50.761  -35.892 -5.100  1.00 104.68 ? 263  GLU   D CG  1 
ATOM   10070 C  CD  . GLU   D 1 194 ? 50.014  -34.585 -5.095  1.00 110.51 ? 263  GLU   D CD  1 
ATOM   10071 O  OE1 . GLU   D 1 194 ? 49.284  -34.306 -4.111  1.00 111.37 ? 263  GLU   D OE1 1 
ATOM   10072 O  OE2 . GLU   D 1 194 ? 50.145  -33.832 -6.083  1.00 115.48 ? 263  GLU   D OE2 1 
ATOM   10073 N  N   . TRP   D 1 195 ? 48.601  -39.441 -2.887  1.00 98.37  ? 264  TRP   D N   1 
ATOM   10074 C  CA  . TRP   D 1 195 ? 48.202  -40.256 -1.742  1.00 96.72  ? 264  TRP   D CA  1 
ATOM   10075 C  C   . TRP   D 1 195 ? 48.259  -41.781 -1.855  1.00 107.95 ? 264  TRP   D C   1 
ATOM   10076 O  O   . TRP   D 1 195 ? 48.867  -42.459 -1.018  1.00 111.24 ? 264  TRP   D O   1 
ATOM   10077 C  CB  . TRP   D 1 195 ? 46.729  -40.006 -1.384  1.00 92.00  ? 264  TRP   D CB  1 
ATOM   10078 C  CG  . TRP   D 1 195 ? 46.434  -38.547 -1.044  1.00 91.78  ? 264  TRP   D CG  1 
ATOM   10079 C  CD1 . TRP   D 1 195 ? 47.346  -37.576 -0.739  1.00 95.04  ? 264  TRP   D CD1 1 
ATOM   10080 C  CD2 . TRP   D 1 195 ? 45.151  -37.905 -0.989  1.00 86.73  ? 264  TRP   D CD2 1 
ATOM   10081 N  NE1 . TRP   D 1 195 ? 46.717  -36.373 -0.497  1.00 84.86  ? 264  TRP   D NE1 1 
ATOM   10082 C  CE2 . TRP   D 1 195 ? 45.370  -36.549 -0.645  1.00 82.25  ? 264  TRP   D CE2 1 
ATOM   10083 C  CE3 . TRP   D 1 195 ? 43.840  -38.342 -1.195  1.00 85.22  ? 264  TRP   D CE3 1 
ATOM   10084 C  CZ2 . TRP   D 1 195 ? 44.329  -35.635 -0.500  1.00 81.05  ? 264  TRP   D CZ2 1 
ATOM   10085 C  CZ3 . TRP   D 1 195 ? 42.802  -37.421 -1.049  1.00 83.44  ? 264  TRP   D CZ3 1 
ATOM   10086 C  CH2 . TRP   D 1 195 ? 43.054  -36.088 -0.708  1.00 79.03  ? 264  TRP   D CH2 1 
ATOM   10087 N  N   . ASP   D 1 196 ? 47.644  -42.325 -2.900  1.00 109.63 ? 265  ASP   D N   1 
ATOM   10088 C  CA  . ASP   D 1 196 ? 47.630  -43.766 -3.145  1.00 111.29 ? 265  ASP   D CA  1 
ATOM   10089 C  C   . ASP   D 1 196 ? 48.331  -43.862 -4.492  1.00 118.83 ? 265  ASP   D C   1 
ATOM   10090 O  O   . ASP   D 1 196 ? 47.689  -43.845 -5.537  1.00 129.97 ? 265  ASP   D O   1 
ATOM   10091 C  CB  . ASP   D 1 196 ? 46.246  -44.392 -3.215  1.00 113.90 ? 265  ASP   D CB  1 
ATOM   10092 C  CG  . ASP   D 1 196 ? 46.296  -45.868 -3.449  1.00 123.50 ? 265  ASP   D CG  1 
ATOM   10093 O  OD1 . ASP   D 1 196 ? 47.400  -46.432 -3.325  1.00 128.85 ? 265  ASP   D OD1 1 
ATOM   10094 O  OD2 . ASP   D 1 196 ? 45.232  -46.457 -3.755  1.00 125.23 ? 265  ASP   D OD2 1 
ATOM   10095 N  N   . GLU   D 1 197 ? 49.660  -43.991 -4.485  1.00 119.52 ? 266  GLU   D N   1 
ATOM   10096 C  CA  . GLU   D 1 197 ? 50.368  -44.134 -5.755  1.00 126.08 ? 266  GLU   D CA  1 
ATOM   10097 C  C   . GLU   D 1 197 ? 49.752  -45.467 -6.164  1.00 133.74 ? 266  GLU   D C   1 
ATOM   10098 O  O   . GLU   D 1 197 ? 49.895  -46.483 -5.473  1.00 130.66 ? 266  GLU   D O   1 
ATOM   10099 C  CB  . GLU   D 1 197 ? 51.878  -44.043 -5.569  1.00 124.28 ? 266  GLU   D CB  1 
ATOM   10100 C  CG  . GLU   D 1 197 ? 52.286  -42.724 -4.922  1.00 128.00 ? 266  GLU   D CG  1 
ATOM   10101 C  CD  . GLU   D 1 197 ? 53.664  -42.773 -4.247  1.00 140.47 ? 266  GLU   D CD  1 
ATOM   10102 O  OE1 . GLU   D 1 197 ? 54.594  -43.380 -4.837  1.00 143.73 ? 266  GLU   D OE1 1 
ATOM   10103 O  OE2 . GLU   D 1 197 ? 53.814  -42.213 -3.125  1.00 141.01 ? 266  GLU   D OE2 1 
ATOM   10104 N  N   . ASN   D 1 198 ? 49.049  -45.458 -7.296  1.00 150.50 ? 267  ASN   D N   1 
ATOM   10105 C  CA  . ASN   D 1 198 ? 48.266  -46.620 -7.697  1.00 156.36 ? 267  ASN   D CA  1 
ATOM   10106 C  C   . ASN   D 1 198 ? 47.658  -46.158 -9.031  1.00 157.82 ? 267  ASN   D C   1 
ATOM   10107 O  O   . ASN   D 1 198 ? 48.032  -45.101 -9.537  1.00 162.43 ? 267  ASN   D O   1 
ATOM   10108 C  CB  . ASN   D 1 198 ? 47.080  -47.073 -6.857  1.00 158.36 ? 267  ASN   D CB  1 
ATOM   10109 C  CG  . ASN   D 1 198 ? 47.387  -48.348 -6.012  1.00 159.88 ? 267  ASN   D CG  1 
ATOM   10110 O  OD1 . ASN   D 1 198 ? 48.552  -48.646 -5.721  1.00 156.45 ? 267  ASN   D OD1 1 
ATOM   10111 N  ND2 . ASN   D 1 198 ? 46.341  -49.129 -5.688  1.00 160.26 ? 267  ASN   D ND2 1 
ATOM   10112 N  N   . LEU   D 1 199 ? 46.725  -46.908 -9.607  1.00 142.74 ? 268  LEU   D N   1 
ATOM   10113 C  CA  . LEU   D 1 199 ? 46.417  -46.767 -11.022 1.00 138.90 ? 268  LEU   D CA  1 
ATOM   10114 C  C   . LEU   D 1 199 ? 45.382  -45.787 -11.547 1.00 141.13 ? 268  LEU   D C   1 
ATOM   10115 O  O   . LEU   D 1 199 ? 44.482  -45.382 -10.812 1.00 145.44 ? 268  LEU   D O   1 
ATOM   10116 C  CB  . LEU   D 1 199 ? 45.924  -48.200 -11.247 1.00 140.87 ? 268  LEU   D CB  1 
ATOM   10117 C  CG  . LEU   D 1 199 ? 46.871  -49.409 -11.106 1.00 144.58 ? 268  LEU   D CG  1 
ATOM   10118 C  CD1 . LEU   D 1 199 ? 46.128  -50.749 -11.232 1.00 143.31 ? 268  LEU   D CD1 1 
ATOM   10119 C  CD2 . LEU   D 1 199 ? 48.036  -49.347 -12.107 1.00 134.85 ? 268  LEU   D CD2 1 
ATOM   10120 N  N   . LYS   D 1 200 ? 45.519  -45.407 -12.821 1.00 143.04 ? 269  LYS   D N   1 
ATOM   10121 C  CA  . LYS   D 1 200 ? 44.568  -44.455 -13.450 1.00 135.99 ? 269  LYS   D CA  1 
ATOM   10122 C  C   . LYS   D 1 200 ? 43.655  -45.240 -14.393 1.00 138.27 ? 269  LYS   D C   1 
ATOM   10123 O  O   . LYS   D 1 200 ? 42.994  -44.613 -15.242 1.00 133.71 ? 269  LYS   D O   1 
ATOM   10124 C  CB  . LYS   D 1 200 ? 45.303  -43.407 -14.289 1.00 122.00 ? 269  LYS   D CB  1 
ATOM   10125 N  N   . ASP   D 1 201 ? 43.635  -46.562 -14.243 1.00 145.12 ? 270  ASP   D N   1 
ATOM   10126 C  CA  . ASP   D 1 201 ? 42.807  -47.410 -15.137 1.00 150.14 ? 270  ASP   D CA  1 
ATOM   10127 C  C   . ASP   D 1 201 ? 41.439  -47.633 -14.496 1.00 150.18 ? 270  ASP   D C   1 
ATOM   10128 O  O   . ASP   D 1 201 ? 40.799  -46.637 -14.108 1.00 147.68 ? 270  ASP   D O   1 
ATOM   10129 C  CB  . ASP   D 1 201 ? 43.488  -48.722 -15.481 1.00 151.35 ? 270  ASP   D CB  1 
ATOM   10130 C  CG  . ASP   D 1 201 ? 44.664  -48.606 -16.436 1.00 157.73 ? 270  ASP   D CG  1 
ATOM   10131 O  OD1 . ASP   D 1 201 ? 44.797  -47.540 -17.071 1.00 158.22 ? 270  ASP   D OD1 1 
ATOM   10132 O  OD2 . ASP   D 1 201 ? 45.430  -49.586 -16.538 1.00 162.87 ? 270  ASP   D OD2 1 
ATOM   10133 N  N   . ASP   D 1 202 ? 41.024  -48.895 -14.384 1.00 165.78 ? 271  ASP   D N   1 
ATOM   10134 C  CA  . ASP   D 1 202 ? 39.709  -49.220 -13.772 1.00 166.08 ? 271  ASP   D CA  1 
ATOM   10135 C  C   . ASP   D 1 202 ? 39.480  -48.537 -12.426 1.00 164.24 ? 271  ASP   D C   1 
ATOM   10136 O  O   . ASP   D 1 202 ? 38.305  -48.418 -12.026 1.00 164.11 ? 271  ASP   D O   1 
ATOM   10137 C  CB  . ASP   D 1 202 ? 39.659  -50.683 -13.371 1.00 169.10 ? 271  ASP   D CB  1 
ATOM   10138 N  N   . SER   D 1 203 ? 40.558  -48.116 -11.768 1.00 141.61 ? 272  SER   D N   1 
ATOM   10139 C  CA  . SER   D 1 203 ? 40.472  -47.423 -10.458 1.00 132.94 ? 272  SER   D CA  1 
ATOM   10140 C  C   . SER   D 1 203 ? 39.332  -46.399 -10.379 1.00 128.98 ? 272  SER   D C   1 
ATOM   10141 O  O   . SER   D 1 203 ? 38.496  -46.526 -9.463  1.00 127.96 ? 272  SER   D O   1 
ATOM   10142 C  CB  . SER   D 1 203 ? 41.755  -46.669 -10.342 1.00 131.62 ? 272  SER   D CB  1 
ATOM   10143 O  OG  . SER   D 1 203 ? 42.166  -46.194 -11.616 1.00 134.34 ? 272  SER   D OG  1 
ATOM   10144 N  N   . LEU   D 1 204 ? 39.309  -45.418 -11.283 1.00 125.52 ? 273  LEU   D N   1 
ATOM   10145 C  CA  . LEU   D 1 204 ? 38.309  -44.326 -11.172 1.00 111.42 ? 273  LEU   D CA  1 
ATOM   10146 C  C   . LEU   D 1 204 ? 37.449  -44.353 -12.439 1.00 113.91 ? 273  LEU   D C   1 
ATOM   10147 O  O   . LEU   D 1 204 ? 37.975  -44.710 -13.508 1.00 121.87 ? 273  LEU   D O   1 
ATOM   10148 C  CB  . LEU   D 1 204 ? 39.004  -42.983 -10.984 1.00 105.04 ? 273  LEU   D CB  1 
ATOM   10149 C  CG  . LEU   D 1 204 ? 39.818  -42.830 -9.697  1.00 101.56 ? 273  LEU   D CG  1 
ATOM   10150 C  CD1 . LEU   D 1 204 ? 41.025  -41.946 -9.938  1.00 90.35  ? 273  LEU   D CD1 1 
ATOM   10151 C  CD2 . LEU   D 1 204 ? 38.946  -42.263 -8.595  1.00 103.04 ? 273  LEU   D CD2 1 
ATOM   10152 N  N   . PRO   D 1 205 ? 36.155  -43.978 -12.363 1.00 109.05 ? 274  PRO   D N   1 
ATOM   10153 C  CA  . PRO   D 1 205 ? 35.246  -44.035 -13.516 1.00 104.63 ? 274  PRO   D CA  1 
ATOM   10154 C  C   . PRO   D 1 205 ? 35.515  -42.902 -14.497 1.00 98.35  ? 274  PRO   D C   1 
ATOM   10155 O  O   . PRO   D 1 205 ? 36.317  -42.005 -14.258 1.00 96.27  ? 274  PRO   D O   1 
ATOM   10156 C  CB  . PRO   D 1 205 ? 33.855  -43.897 -12.886 1.00 99.02  ? 274  PRO   D CB  1 
ATOM   10157 C  CG  . PRO   D 1 205 ? 34.099  -43.122 -11.649 1.00 97.50  ? 274  PRO   D CG  1 
ATOM   10158 C  CD  . PRO   D 1 205 ? 35.451  -43.545 -11.141 1.00 104.34 ? 274  PRO   D CD  1 
ATOM   10159 N  N   . SER   D 1 206 ? 34.791  -42.956 -15.610 1.00 104.65 ? 275  SER   D N   1 
ATOM   10160 C  CA  . SER   D 1 206 ? 35.029  -42.072 -16.739 1.00 104.32 ? 275  SER   D CA  1 
ATOM   10161 C  C   . SER   D 1 206 ? 33.934  -41.024 -16.841 1.00 103.02 ? 275  SER   D C   1 
ATOM   10162 O  O   . SER   D 1 206 ? 34.224  -39.829 -16.740 1.00 105.61 ? 275  SER   D O   1 
ATOM   10163 C  CB  . SER   D 1 206 ? 35.118  -42.878 -18.034 1.00 108.25 ? 275  SER   D CB  1 
ATOM   10164 O  OG  . SER   D 1 206 ? 33.899  -43.558 -18.310 1.00 108.37 ? 275  SER   D OG  1 
ATOM   10165 N  N   . ASN   D 1 207 ? 32.688  -41.456 -17.057 1.00 96.88  ? 276  ASN   D N   1 
ATOM   10166 C  CA  . ASN   D 1 207 ? 31.564  -40.540 -17.122 1.00 95.61  ? 276  ASN   D CA  1 
ATOM   10167 C  C   . ASN   D 1 207 ? 31.613  -39.597 -15.924 1.00 94.54  ? 276  ASN   D C   1 
ATOM   10168 O  O   . ASN   D 1 207 ? 31.505  -40.064 -14.783 1.00 95.81  ? 276  ASN   D O   1 
ATOM   10169 C  CB  . ASN   D 1 207 ? 30.248  -41.323 -17.158 1.00 95.20  ? 276  ASN   D CB  1 
ATOM   10170 C  CG  . ASN   D 1 207 ? 29.022  -40.421 -17.057 1.00 100.69 ? 276  ASN   D CG  1 
ATOM   10171 O  OD1 . ASN   D 1 207 ? 28.429  -40.301 -15.988 1.00 98.28  ? 276  ASN   D OD1 1 
ATOM   10172 N  ND2 . ASN   D 1 207 ? 28.626  -39.800 -18.174 1.00 106.07 ? 276  ASN   D ND2 1 
ATOM   10173 N  N   . PRO   D 1 208 ? 31.812  -38.287 -16.126 1.00 97.49  ? 277  PRO   D N   1 
ATOM   10174 C  CA  . PRO   D 1 208 ? 32.101  -37.404 -14.985 1.00 97.27  ? 277  PRO   D CA  1 
ATOM   10175 C  C   . PRO   D 1 208 ? 30.999  -37.353 -13.952 1.00 97.27  ? 277  PRO   D C   1 
ATOM   10176 O  O   . PRO   D 1 208 ? 31.266  -36.942 -12.812 1.00 96.67  ? 277  PRO   D O   1 
ATOM   10177 C  CB  . PRO   D 1 208 ? 32.307  -36.029 -15.646 1.00 94.22  ? 277  PRO   D CB  1 
ATOM   10178 C  CG  . PRO   D 1 208 ? 32.667  -36.322 -17.023 1.00 96.42  ? 277  PRO   D CG  1 
ATOM   10179 C  CD  . PRO   D 1 208 ? 31.848  -37.535 -17.388 1.00 101.69 ? 277  PRO   D CD  1 
ATOM   10180 N  N   . ILE   D 1 209 ? 29.771  -37.749 -14.296 1.00 93.77  ? 278  ILE   D N   1 
ATOM   10181 C  CA  . ILE   D 1 209 ? 28.735  -37.840 -13.272 1.00 91.46  ? 278  ILE   D CA  1 
ATOM   10182 C  C   . ILE   D 1 209 ? 29.183  -38.790 -12.161 1.00 91.09  ? 278  ILE   D C   1 
ATOM   10183 O  O   . ILE   D 1 209 ? 29.082  -38.471 -10.972 1.00 88.88  ? 278  ILE   D O   1 
ATOM   10184 C  CB  . ILE   D 1 209 ? 27.393  -38.264 -13.893 1.00 92.64  ? 278  ILE   D CB  1 
ATOM   10185 C  CG1 . ILE   D 1 209 ? 26.846  -37.152 -14.804 1.00 96.70  ? 278  ILE   D CG1 1 
ATOM   10186 C  CG2 . ILE   D 1 209 ? 26.388  -38.611 -12.805 1.00 90.93  ? 278  ILE   D CG2 1 
ATOM   10187 C  CD1 . ILE   D 1 209 ? 27.330  -37.205 -16.276 1.00 94.68  ? 278  ILE   D CD1 1 
ATOM   10188 N  N   . ASP   D 1 210 ? 29.739  -39.953 -12.540 1.00 93.48  ? 279  ASP   D N   1 
ATOM   10189 C  CA  . ASP   D 1 210 ? 30.182  -40.951 -11.564 1.00 89.48  ? 279  ASP   D CA  1 
ATOM   10190 C  C   . ASP   D 1 210 ? 31.528  -40.595 -10.942 1.00 89.25  ? 279  ASP   D C   1 
ATOM   10191 O  O   . ASP   D 1 210 ? 31.754  -40.867 -9.760  1.00 90.16  ? 279  ASP   D O   1 
ATOM   10192 C  CB  . ASP   D 1 210 ? 30.285  -42.330 -12.214 1.00 88.73  ? 279  ASP   D CB  1 
ATOM   10193 C  CG  . ASP   D 1 210 ? 29.140  -42.621 -13.141 1.00 90.20  ? 279  ASP   D CG  1 
ATOM   10194 O  OD1 . ASP   D 1 210 ? 27.977  -42.554 -12.692 1.00 90.79  ? 279  ASP   D OD1 1 
ATOM   10195 O  OD2 . ASP   D 1 210 ? 29.409  -42.918 -14.327 1.00 95.08  ? 279  ASP   D OD2 1 
ATOM   10196 N  N   . PHE   D 1 211 ? 32.453  -40.039 -11.730 1.00 93.20  ? 280  PHE   D N   1 
ATOM   10197 C  CA  . PHE   D 1 211 ? 33.747  -39.653 -11.172 1.00 90.98  ? 280  PHE   D CA  1 
ATOM   10198 C  C   . PHE   D 1 211 ? 33.557  -38.688 -10.019 1.00 88.89  ? 280  PHE   D C   1 
ATOM   10199 O  O   . PHE   D 1 211 ? 34.173  -38.846 -8.957  1.00 91.76  ? 280  PHE   D O   1 
ATOM   10200 C  CB  . PHE   D 1 211 ? 34.632  -39.022 -12.254 1.00 90.62  ? 280  PHE   D CB  1 
ATOM   10201 C  CG  . PHE   D 1 211 ? 36.047  -38.735 -11.798 1.00 88.03  ? 280  PHE   D CG  1 
ATOM   10202 C  CD1 . PHE   D 1 211 ? 36.362  -37.548 -11.140 1.00 86.14  ? 280  PHE   D CD1 1 
ATOM   10203 C  CD2 . PHE   D 1 211 ? 37.061  -39.650 -12.035 1.00 88.72  ? 280  PHE   D CD2 1 
ATOM   10204 C  CE1 . PHE   D 1 211 ? 37.667  -37.291 -10.719 1.00 85.42  ? 280  PHE   D CE1 1 
ATOM   10205 C  CE2 . PHE   D 1 211 ? 38.355  -39.395 -11.625 1.00 88.23  ? 280  PHE   D CE2 1 
ATOM   10206 C  CZ  . PHE   D 1 211 ? 38.660  -38.218 -10.964 1.00 86.54  ? 280  PHE   D CZ  1 
ATOM   10207 N  N   . SER   D 1 212 ? 32.688  -37.695 -10.203 1.00 86.92  ? 281  SER   D N   1 
ATOM   10208 C  CA  . SER   D 1 212 ? 32.428  -36.724 -9.150  1.00 83.87  ? 281  SER   D CA  1 
ATOM   10209 C  C   . SER   D 1 212 ? 31.941  -37.402 -7.871  1.00 86.50  ? 281  SER   D C   1 
ATOM   10210 O  O   . SER   D 1 212 ? 32.435  -37.109 -6.778  1.00 86.15  ? 281  SER   D O   1 
ATOM   10211 C  CB  . SER   D 1 212 ? 31.418  -35.695 -9.637  1.00 80.48  ? 281  SER   D CB  1 
ATOM   10212 O  OG  . SER   D 1 212 ? 30.124  -36.243 -9.624  1.00 84.17  ? 281  SER   D OG  1 
ATOM   10213 N  N   . TYR   D 1 213 ? 30.980  -38.322 -7.981  1.00 88.45  ? 282  TYR   D N   1 
ATOM   10214 C  CA  . TYR   D 1 213 ? 30.485  -38.983 -6.779  1.00 86.38  ? 282  TYR   D CA  1 
ATOM   10215 C  C   . TYR   D 1 213 ? 31.503  -39.937 -6.186  1.00 87.38  ? 282  TYR   D C   1 
ATOM   10216 O  O   . TYR   D 1 213 ? 31.439  -40.228 -4.987  1.00 90.80  ? 282  TYR   D O   1 
ATOM   10217 C  CB  . TYR   D 1 213 ? 29.189  -39.736 -7.077  1.00 86.35  ? 282  TYR   D CB  1 
ATOM   10218 C  CG  . TYR   D 1 213 ? 28.058  -38.801 -7.384  1.00 84.84  ? 282  TYR   D CG  1 
ATOM   10219 C  CD1 . TYR   D 1 213 ? 27.812  -37.708 -6.580  1.00 83.44  ? 282  TYR   D CD1 1 
ATOM   10220 C  CD2 . TYR   D 1 213 ? 27.256  -38.993 -8.497  1.00 87.36  ? 282  TYR   D CD2 1 
ATOM   10221 C  CE1 . TYR   D 1 213 ? 26.794  -36.843 -6.858  1.00 82.28  ? 282  TYR   D CE1 1 
ATOM   10222 C  CE2 . TYR   D 1 213 ? 26.234  -38.132 -8.789  1.00 84.95  ? 282  TYR   D CE2 1 
ATOM   10223 C  CZ  . TYR   D 1 213 ? 26.009  -37.059 -7.961  1.00 84.99  ? 282  TYR   D CZ  1 
ATOM   10224 O  OH  . TYR   D 1 213 ? 24.990  -36.188 -8.239  1.00 93.19  ? 282  TYR   D OH  1 
ATOM   10225 N  N   . ARG   D 1 214 ? 32.432  -40.438 -6.988  1.00 96.20  ? 283  ARG   D N   1 
ATOM   10226 C  CA  . ARG   D 1 214 ? 33.450  -41.300 -6.419  1.00 98.39  ? 283  ARG   D CA  1 
ATOM   10227 C  C   . ARG   D 1 214 ? 34.515  -40.500 -5.673  1.00 98.49  ? 283  ARG   D C   1 
ATOM   10228 O  O   . ARG   D 1 214 ? 35.041  -40.973 -4.657  1.00 99.68  ? 283  ARG   D O   1 
ATOM   10229 C  CB  . ARG   D 1 214 ? 34.069  -42.149 -7.521  1.00 101.30 ? 283  ARG   D CB  1 
ATOM   10230 C  CG  . ARG   D 1 214 ? 35.262  -42.907 -7.049  1.00 105.90 ? 283  ARG   D CG  1 
ATOM   10231 C  CD  . ARG   D 1 214 ? 34.861  -44.102 -6.249  1.00 108.33 ? 283  ARG   D CD  1 
ATOM   10232 N  NE  . ARG   D 1 214 ? 35.955  -45.059 -6.268  1.00 117.01 ? 283  ARG   D NE  1 
ATOM   10233 C  CZ  . ARG   D 1 214 ? 36.317  -45.747 -7.342  1.00 117.06 ? 283  ARG   D CZ  1 
ATOM   10234 N  NH1 . ARG   D 1 214 ? 35.661  -45.637 -8.491  1.00 113.00 ? 283  ARG   D NH1 1 
ATOM   10235 N  NH2 . ARG   D 1 214 ? 37.368  -46.561 -7.267  1.00 123.32 ? 283  ARG   D NH2 1 
ATOM   10236 N  N   . VAL   D 1 215 ? 34.811  -39.281 -6.120  1.00 88.53  ? 284  VAL   D N   1 
ATOM   10237 C  CA  . VAL   D 1 215 ? 35.762  -38.464 -5.379  1.00 83.20  ? 284  VAL   D CA  1 
ATOM   10238 C  C   . VAL   D 1 215 ? 35.172  -38.002 -4.057  1.00 82.46  ? 284  VAL   D C   1 
ATOM   10239 O  O   . VAL   D 1 215 ? 35.907  -37.811 -3.087  1.00 84.49  ? 284  VAL   D O   1 
ATOM   10240 C  CB  . VAL   D 1 215 ? 36.236  -37.282 -6.235  1.00 80.35  ? 284  VAL   D CB  1 
ATOM   10241 C  CG1 . VAL   D 1 215 ? 36.953  -36.239 -5.383  1.00 84.51  ? 284  VAL   D CG1 1 
ATOM   10242 C  CG2 . VAL   D 1 215 ? 37.163  -37.784 -7.321  1.00 81.01  ? 284  VAL   D CG2 1 
ATOM   10243 N  N   . ALA   D 1 216 ? 33.853  -37.842 -3.971  1.00 82.90  ? 285  ALA   D N   1 
ATOM   10244 C  CA  . ALA   D 1 216 ? 33.269  -37.369 -2.724  1.00 82.11  ? 285  ALA   D CA  1 
ATOM   10245 C  C   . ALA   D 1 216 ? 33.301  -38.443 -1.645  1.00 90.92  ? 285  ALA   D C   1 
ATOM   10246 O  O   . ALA   D 1 216 ? 33.363  -38.120 -0.445  1.00 91.80  ? 285  ALA   D O   1 
ATOM   10247 C  CB  . ALA   D 1 216 ? 31.844  -36.886 -2.961  1.00 78.88  ? 285  ALA   D CB  1 
ATOM   10248 N  N   . ALA   D 1 217 ? 33.294  -39.717 -2.038  1.00 86.61  ? 286  ALA   D N   1 
ATOM   10249 C  CA  . ALA   D 1 217 ? 33.411  -40.758 -1.034  1.00 88.52  ? 286  ALA   D CA  1 
ATOM   10250 C  C   . ALA   D 1 217 ? 34.846  -41.221 -0.796  1.00 92.14  ? 286  ALA   D C   1 
ATOM   10251 O  O   . ALA   D 1 217 ? 35.064  -42.051 0.090   1.00 97.35  ? 286  ALA   D O   1 
ATOM   10252 C  CB  . ALA   D 1 217 ? 32.528  -41.947 -1.402  1.00 96.81  ? 286  ALA   D CB  1 
ATOM   10253 N  N   . CYS   D 1 218 ? 35.830  -40.718 -1.543  1.00 99.12  ? 287  CYS   D N   1 
ATOM   10254 C  CA  . CYS   D 1 218 ? 37.229  -41.002 -1.233  1.00 99.01  ? 287  CYS   D CA  1 
ATOM   10255 C  C   . CYS   D 1 218 ? 37.928  -39.862 -0.520  1.00 98.49  ? 287  CYS   D C   1 
ATOM   10256 O  O   . CYS   D 1 218 ? 39.024  -40.068 0.006   1.00 99.18  ? 287  CYS   D O   1 
ATOM   10257 C  CB  . CYS   D 1 218 ? 38.018  -41.335 -2.499  1.00 101.34 ? 287  CYS   D CB  1 
ATOM   10258 S  SG  . CYS   D 1 218 ? 38.016  -43.113 -2.909  1.00 140.68 ? 287  CYS   D SG  1 
ATOM   10259 N  N   . LEU   D 1 219 ? 37.340  -38.687 -0.505  1.00 88.53  ? 288  LEU   D N   1 
ATOM   10260 C  CA  . LEU   D 1 219 ? 37.935  -37.546 0.161   1.00 80.28  ? 288  LEU   D CA  1 
ATOM   10261 C  C   . LEU   D 1 219 ? 37.728  -37.672 1.663   1.00 83.86  ? 288  LEU   D C   1 
ATOM   10262 O  O   . LEU   D 1 219 ? 36.654  -38.096 2.105   1.00 86.55  ? 288  LEU   D O   1 
ATOM   10263 C  CB  . LEU   D 1 219 ? 37.320  -36.238 -0.347  1.00 78.76  ? 288  LEU   D CB  1 
ATOM   10264 C  CG  . LEU   D 1 219 ? 38.041  -35.623 -1.555  1.00 78.34  ? 288  LEU   D CG  1 
ATOM   10265 C  CD1 . LEU   D 1 219 ? 37.342  -34.407 -2.156  1.00 77.89  ? 288  LEU   D CD1 1 
ATOM   10266 C  CD2 . LEU   D 1 219 ? 39.465  -35.281 -1.173  1.00 83.54  ? 288  LEU   D CD2 1 
ATOM   10267 N  N   . PRO   D 1 220 ? 38.749  -37.323 2.463   1.00 82.84  ? 289  PRO   D N   1 
ATOM   10268 C  CA  . PRO   D 1 220 ? 38.561  -37.215 3.917   1.00 80.22  ? 289  PRO   D CA  1 
ATOM   10269 C  C   . PRO   D 1 220 ? 37.777  -35.968 4.302   1.00 81.70  ? 289  PRO   D C   1 
ATOM   10270 O  O   . PRO   D 1 220 ? 38.363  -34.995 4.790   1.00 84.81  ? 289  PRO   D O   1 
ATOM   10271 C  CB  . PRO   D 1 220 ? 39.999  -37.155 4.444   1.00 80.44  ? 289  PRO   D CB  1 
ATOM   10272 C  CG  . PRO   D 1 220 ? 40.780  -36.545 3.318   1.00 80.00  ? 289  PRO   D CG  1 
ATOM   10273 C  CD  . PRO   D 1 220 ? 40.145  -37.062 2.060   1.00 79.72  ? 289  PRO   D CD  1 
ATOM   10274 N  N   . ILE   D 1 221 ? 36.465  -35.967 4.063   1.00 82.13  ? 290  ILE   D N   1 
ATOM   10275 C  CA  . ILE   D 1 221 ? 35.619  -34.812 4.326   1.00 83.34  ? 290  ILE   D CA  1 
ATOM   10276 C  C   . ILE   D 1 221 ? 34.503  -35.240 5.259   1.00 84.27  ? 290  ILE   D C   1 
ATOM   10277 O  O   . ILE   D 1 221 ? 34.092  -36.403 5.281   1.00 86.53  ? 290  ILE   D O   1 
ATOM   10278 C  CB  . ILE   D 1 221 ? 35.016  -34.183 3.038   1.00 82.46  ? 290  ILE   D CB  1 
ATOM   10279 C  CG1 . ILE   D 1 221 ? 34.372  -35.251 2.164   1.00 87.18  ? 290  ILE   D CG1 1 
ATOM   10280 C  CG2 . ILE   D 1 221 ? 36.047  -33.437 2.223   1.00 82.39  ? 290  ILE   D CG2 1 
ATOM   10281 C  CD1 . ILE   D 1 221 ? 34.098  -34.765 0.767   1.00 84.74  ? 290  ILE   D CD1 1 
ATOM   10282 N  N   . ASP   D 1 222 ? 34.009  -34.278 6.023   1.00 88.66  ? 291  ASP   D N   1 
ATOM   10283 C  CA  . ASP   D 1 222 ? 32.921  -34.474 6.963   1.00 93.46  ? 291  ASP   D CA  1 
ATOM   10284 C  C   . ASP   D 1 222 ? 31.587  -34.495 6.216   1.00 93.51  ? 291  ASP   D C   1 
ATOM   10285 O  O   . ASP   D 1 222 ? 31.512  -34.219 5.013   1.00 93.18  ? 291  ASP   D O   1 
ATOM   10286 C  CB  . ASP   D 1 222 ? 32.954  -33.376 8.023   1.00 94.98  ? 291  ASP   D CB  1 
ATOM   10287 C  CG  . ASP   D 1 222 ? 33.036  -31.991 7.406   1.00 97.30  ? 291  ASP   D CG  1 
ATOM   10288 O  OD1 . ASP   D 1 222 ? 32.961  -31.920 6.164   1.00 95.83  ? 291  ASP   D OD1 1 
ATOM   10289 O  OD2 . ASP   D 1 222 ? 33.179  -30.981 8.135   1.00 102.37 ? 291  ASP   D OD2 1 
ATOM   10290 N  N   . ASP   D 1 223 ? 30.512  -34.785 6.961   1.00 92.35  ? 292  ASP   D N   1 
ATOM   10291 C  CA  . ASP   D 1 223 ? 29.199  -34.970 6.349   1.00 92.64  ? 292  ASP   D CA  1 
ATOM   10292 C  C   . ASP   D 1 223 ? 28.633  -33.667 5.759   1.00 90.84  ? 292  ASP   D C   1 
ATOM   10293 O  O   . ASP   D 1 223 ? 27.864  -33.709 4.793   1.00 89.22  ? 292  ASP   D O   1 
ATOM   10294 C  CB  . ASP   D 1 223 ? 28.238  -35.610 7.372   1.00 91.43  ? 292  ASP   D CB  1 
ATOM   10295 C  CG  . ASP   D 1 223 ? 28.335  -37.158 7.395   1.00 93.45  ? 292  ASP   D CG  1 
ATOM   10296 O  OD1 . ASP   D 1 223 ? 28.842  -37.730 6.405   1.00 95.74  ? 292  ASP   D OD1 1 
ATOM   10297 O  OD2 . ASP   D 1 223 ? 27.889  -37.814 8.370   1.00 87.39  ? 292  ASP   D OD2 1 
ATOM   10298 N  N   . VAL   D 1 224 ? 29.008  -32.498 6.284   1.00 94.20  ? 293  VAL   D N   1 
ATOM   10299 C  CA  . VAL   D 1 224 ? 28.454  -31.275 5.701   1.00 93.57  ? 293  VAL   D CA  1 
ATOM   10300 C  C   . VAL   D 1 224 ? 29.019  -31.043 4.309   1.00 91.00  ? 293  VAL   D C   1 
ATOM   10301 O  O   . VAL   D 1 224 ? 28.302  -30.606 3.403   1.00 93.98  ? 293  VAL   D O   1 
ATOM   10302 C  CB  . VAL   D 1 224 ? 28.683  -30.059 6.613   1.00 97.01  ? 293  VAL   D CB  1 
ATOM   10303 C  CG1 . VAL   D 1 224 ? 27.830  -30.203 7.842   1.00 100.65 ? 293  VAL   D CG1 1 
ATOM   10304 C  CG2 . VAL   D 1 224 ? 30.151  -29.898 6.972   1.00 94.86  ? 293  VAL   D CG2 1 
ATOM   10305 N  N   . LEU   D 1 225 ? 30.300  -31.335 4.103   1.00 91.75  ? 294  LEU   D N   1 
ATOM   10306 C  CA  . LEU   D 1 225 ? 30.834  -31.242 2.755   1.00 87.43  ? 294  LEU   D CA  1 
ATOM   10307 C  C   . LEU   D 1 225 ? 30.181  -32.279 1.865   1.00 86.64  ? 294  LEU   D C   1 
ATOM   10308 O  O   . LEU   D 1 225 ? 29.822  -31.979 0.724   1.00 85.89  ? 294  LEU   D O   1 
ATOM   10309 C  CB  . LEU   D 1 225 ? 32.351  -31.406 2.762   1.00 85.24  ? 294  LEU   D CB  1 
ATOM   10310 C  CG  . LEU   D 1 225 ? 33.140  -30.107 2.647   1.00 79.49  ? 294  LEU   D CG  1 
ATOM   10311 C  CD1 . LEU   D 1 225 ? 32.571  -29.040 3.564   1.00 78.07  ? 294  LEU   D CD1 1 
ATOM   10312 C  CD2 . LEU   D 1 225 ? 34.583  -30.378 2.982   1.00 83.09  ? 294  LEU   D CD2 1 
ATOM   10313 N  N   . ARG   D 1 226 ? 29.974  -33.492 2.387   1.00 88.31  ? 295  ARG   D N   1 
ATOM   10314 C  CA  . ARG   D 1 226 ? 29.344  -34.538 1.588   1.00 85.77  ? 295  ARG   D CA  1 
ATOM   10315 C  C   . ARG   D 1 226 ? 27.952  -34.120 1.120   1.00 87.76  ? 295  ARG   D C   1 
ATOM   10316 O  O   . ARG   D 1 226 ? 27.624  -34.267 -0.062  1.00 87.57  ? 295  ARG   D O   1 
ATOM   10317 C  CB  . ARG   D 1 226 ? 29.292  -35.847 2.370   1.00 87.43  ? 295  ARG   D CB  1 
ATOM   10318 C  CG  . ARG   D 1 226 ? 30.595  -36.637 2.298   1.00 85.12  ? 295  ARG   D CG  1 
ATOM   10319 C  CD  . ARG   D 1 226 ? 30.525  -37.972 3.019   1.00 85.93  ? 295  ARG   D CD  1 
ATOM   10320 N  NE  . ARG   D 1 226 ? 31.713  -38.764 2.723   1.00 87.48  ? 295  ARG   D NE  1 
ATOM   10321 C  CZ  . ARG   D 1 226 ? 31.827  -40.068 2.953   1.00 93.81  ? 295  ARG   D CZ  1 
ATOM   10322 N  NH1 . ARG   D 1 226 ? 30.852  -40.764 3.525   1.00 93.67  ? 295  ARG   D NH1 1 
ATOM   10323 N  NH2 . ARG   D 1 226 ? 32.944  -40.694 2.591   1.00 96.24  ? 295  ARG   D NH2 1 
ATOM   10324 N  N   . ILE   D 1 227 ? 27.127  -33.560 2.011   1.00 87.42  ? 296  ILE   D N   1 
ATOM   10325 C  CA  . ILE   D 1 227 ? 25.789  -33.173 1.566   1.00 86.17  ? 296  ILE   D CA  1 
ATOM   10326 C  C   . ILE   D 1 227 ? 25.817  -31.905 0.721   1.00 83.10  ? 296  ILE   D C   1 
ATOM   10327 O  O   . ILE   D 1 227 ? 24.833  -31.599 0.037   1.00 83.27  ? 296  ILE   D O   1 
ATOM   10328 C  CB  . ILE   D 1 227 ? 24.802  -33.009 2.740   1.00 85.93  ? 296  ILE   D CB  1 
ATOM   10329 C  CG1 . ILE   D 1 227 ? 25.103  -31.758 3.553   1.00 94.03  ? 296  ILE   D CG1 1 
ATOM   10330 C  CG2 . ILE   D 1 227 ? 24.853  -34.197 3.630   1.00 84.45  ? 296  ILE   D CG2 1 
ATOM   10331 C  CD1 . ILE   D 1 227 ? 24.130  -31.547 4.698   1.00 98.58  ? 296  ILE   D CD1 1 
ATOM   10332 N  N   . GLN   D 1 228 ? 26.913  -31.152 0.747   1.00 82.32  ? 297  GLN   D N   1 
ATOM   10333 C  CA  . GLN   D 1 228 ? 27.007  -29.990 -0.126  1.00 85.01  ? 297  GLN   D CA  1 
ATOM   10334 C  C   . GLN   D 1 228 ? 27.309  -30.415 -1.559  1.00 81.79  ? 297  GLN   D C   1 
ATOM   10335 O  O   . GLN   D 1 228 ? 26.693  -29.920 -2.506  1.00 82.45  ? 297  GLN   D O   1 
ATOM   10336 C  CB  . GLN   D 1 228 ? 28.081  -29.030 0.379   1.00 88.24  ? 297  GLN   D CB  1 
ATOM   10337 C  CG  . GLN   D 1 228 ? 27.692  -28.063 1.477   1.00 90.52  ? 297  GLN   D CG  1 
ATOM   10338 C  CD  . GLN   D 1 228 ? 28.731  -26.938 1.603   1.00 102.00 ? 297  GLN   D CD  1 
ATOM   10339 O  OE1 . GLN   D 1 228 ? 29.232  -26.636 2.700   1.00 102.19 ? 297  GLN   D OE1 1 
ATOM   10340 N  NE2 . GLN   D 1 228 ? 29.064  -26.317 0.462   1.00 102.23 ? 297  GLN   D NE2 1 
ATOM   10341 N  N   . LEU   D 1 229 ? 28.274  -31.316 -1.738  1.00 80.41  ? 298  LEU   D N   1 
ATOM   10342 C  CA  . LEU   D 1 229 ? 28.553  -31.846 -3.066  1.00 77.31  ? 298  LEU   D CA  1 
ATOM   10343 C  C   . LEU   D 1 229 ? 27.324  -32.541 -3.633  1.00 83.82  ? 298  LEU   D C   1 
ATOM   10344 O  O   . LEU   D 1 229 ? 27.045  -32.434 -4.836  1.00 85.62  ? 298  LEU   D O   1 
ATOM   10345 C  CB  . LEU   D 1 229 ? 29.731  -32.817 -3.002  1.00 77.47  ? 298  LEU   D CB  1 
ATOM   10346 C  CG  . LEU   D 1 229 ? 31.083  -32.247 -2.615  1.00 77.32  ? 298  LEU   D CG  1 
ATOM   10347 C  CD1 . LEU   D 1 229 ? 32.085  -33.360 -2.465  1.00 77.59  ? 298  LEU   D CD1 1 
ATOM   10348 C  CD2 . LEU   D 1 229 ? 31.497  -31.267 -3.660  1.00 76.85  ? 298  LEU   D CD2 1 
ATOM   10349 N  N   . LEU   D 1 230 ? 26.571  -33.252 -2.772  1.00 82.58  ? 299  LEU   D N   1 
ATOM   10350 C  CA  . LEU   D 1 230 ? 25.355  -33.936 -3.210  1.00 78.56  ? 299  LEU   D CA  1 
ATOM   10351 C  C   . LEU   D 1 230 ? 24.308  -32.950 -3.708  1.00 80.87  ? 299  LEU   D C   1 
ATOM   10352 O  O   . LEU   D 1 230 ? 23.614  -33.213 -4.697  1.00 81.70  ? 299  LEU   D O   1 
ATOM   10353 C  CB  . LEU   D 1 230 ? 24.787  -34.777 -2.076  1.00 78.79  ? 299  LEU   D CB  1 
ATOM   10354 C  CG  . LEU   D 1 230 ? 25.651  -35.953 -1.649  1.00 84.09  ? 299  LEU   D CG  1 
ATOM   10355 C  CD1 . LEU   D 1 230 ? 24.900  -36.879 -0.719  1.00 91.78  ? 299  LEU   D CD1 1 
ATOM   10356 C  CD2 . LEU   D 1 230 ? 26.147  -36.711 -2.855  1.00 86.62  ? 299  LEU   D CD2 1 
ATOM   10357 N  N   . LYS   D 1 231 ? 24.191  -31.803 -3.051  1.00 81.25  ? 300  LYS   D N   1 
ATOM   10358 C  CA  . LYS   D 1 231 ? 23.217  -30.806 -3.459  1.00 82.06  ? 300  LYS   D CA  1 
ATOM   10359 C  C   . LYS   D 1 231 ? 23.661  -30.003 -4.685  1.00 85.62  ? 300  LYS   D C   1 
ATOM   10360 O  O   . LYS   D 1 231 ? 22.803  -29.390 -5.333  1.00 87.23  ? 300  LYS   D O   1 
ATOM   10361 C  CB  . LYS   D 1 231 ? 22.913  -29.895 -2.265  1.00 83.73  ? 300  LYS   D CB  1 
ATOM   10362 C  CG  . LYS   D 1 231 ? 22.135  -30.607 -1.164  1.00 84.85  ? 300  LYS   D CG  1 
ATOM   10363 C  CD  . LYS   D 1 231 ? 21.428  -29.657 -0.231  1.00 93.15  ? 300  LYS   D CD  1 
ATOM   10364 C  CE  . LYS   D 1 231 ? 22.043  -29.707 1.150   1.00 96.20  ? 300  LYS   D CE  1 
ATOM   10365 N  NZ  . LYS   D 1 231 ? 23.514  -29.491 1.056   1.00 97.69  ? 300  LYS   D NZ  1 
ATOM   10366 N  N   . ILE   D 1 232 ? 24.964  -30.015 -5.027  1.00 86.22  ? 301  ILE   D N   1 
ATOM   10367 C  CA  . ILE   D 1 232 ? 25.473  -29.355 -6.238  1.00 83.25  ? 301  ILE   D CA  1 
ATOM   10368 C  C   . ILE   D 1 232 ? 24.850  -30.002 -7.474  1.00 89.80  ? 301  ILE   D C   1 
ATOM   10369 O  O   . ILE   D 1 232 ? 24.931  -31.225 -7.665  1.00 87.97  ? 301  ILE   D O   1 
ATOM   10370 C  CB  . ILE   D 1 232 ? 27.016  -29.434 -6.296  1.00 79.79  ? 301  ILE   D CB  1 
ATOM   10371 C  CG1 . ILE   D 1 232 ? 27.702  -28.361 -5.458  1.00 78.92  ? 301  ILE   D CG1 1 
ATOM   10372 C  CG2 . ILE   D 1 232 ? 27.540  -29.280 -7.700  1.00 84.63  ? 301  ILE   D CG2 1 
ATOM   10373 C  CD1 . ILE   D 1 232 ? 29.225  -28.283 -5.684  1.00 75.89  ? 301  ILE   D CD1 1 
ATOM   10374 N  N   . GLY   D 1 233 ? 24.242  -29.176 -8.336  1.00 97.61  ? 302  GLY   D N   1 
ATOM   10375 C  CA  . GLY   D 1 233 ? 23.554  -29.650 -9.528  1.00 98.88  ? 302  GLY   D CA  1 
ATOM   10376 C  C   . GLY   D 1 233 ? 24.416  -30.370 -10.552 1.00 98.88  ? 302  GLY   D C   1 
ATOM   10377 O  O   . GLY   D 1 233 ? 24.232  -31.562 -10.787 1.00 102.69 ? 302  GLY   D O   1 
ATOM   10378 N  N   . SER   D 1 234 ? 25.366  -29.679 -11.159 1.00 88.25  ? 303  SER   D N   1 
ATOM   10379 C  CA  . SER   D 1 234 ? 26.179  -30.267 -12.212 1.00 85.32  ? 303  SER   D CA  1 
ATOM   10380 C  C   . SER   D 1 234 ? 27.401  -30.996 -11.660 1.00 85.74  ? 303  SER   D C   1 
ATOM   10381 O  O   . SER   D 1 234 ? 27.961  -30.627 -10.625 1.00 84.94  ? 303  SER   D O   1 
ATOM   10382 C  CB  . SER   D 1 234 ? 26.656  -29.188 -13.178 1.00 88.58  ? 303  SER   D CB  1 
ATOM   10383 O  OG  . SER   D 1 234 ? 27.783  -28.503 -12.644 1.00 89.33  ? 303  SER   D OG  1 
ATOM   10384 N  N   . ALA   D 1 235 ? 27.838  -32.018 -12.397 1.00 86.23  ? 304  ALA   D N   1 
ATOM   10385 C  CA  . ALA   D 1 235 ? 29.063  -32.726 -12.052 1.00 80.43  ? 304  ALA   D CA  1 
ATOM   10386 C  C   . ALA   D 1 235 ? 30.299  -31.853 -12.213 1.00 77.48  ? 304  ALA   D C   1 
ATOM   10387 O  O   . ALA   D 1 235 ? 31.267  -32.027 -11.472 1.00 80.18  ? 304  ALA   D O   1 
ATOM   10388 C  CB  . ALA   D 1 235 ? 29.189  -33.989 -12.899 1.00 85.38  ? 304  ALA   D CB  1 
ATOM   10389 N  N   . ILE   D 1 236 ? 30.292  -30.908 -13.156 1.00 83.96  ? 305  ILE   D N   1 
ATOM   10390 C  CA  . ILE   D 1 236 ? 31.463  -30.044 -13.338 1.00 86.26  ? 305  ILE   D CA  1 
ATOM   10391 C  C   . ILE   D 1 236 ? 31.612  -29.107 -12.145 1.00 86.25  ? 305  ILE   D C   1 
ATOM   10392 O  O   . ILE   D 1 236 ? 32.723  -28.894 -11.644 1.00 86.85  ? 305  ILE   D O   1 
ATOM   10393 C  CB  . ILE   D 1 236 ? 31.398  -29.266 -14.678 1.00 85.42  ? 305  ILE   D CB  1 
ATOM   10394 C  CG1 . ILE   D 1 236 ? 31.767  -30.162 -15.861 1.00 83.55  ? 305  ILE   D CG1 1 
ATOM   10395 C  CG2 . ILE   D 1 236 ? 32.366  -28.075 -14.696 1.00 83.16  ? 305  ILE   D CG2 1 
ATOM   10396 C  CD1 . ILE   D 1 236 ? 32.003  -29.410 -17.158 1.00 81.73  ? 305  ILE   D CD1 1 
ATOM   10397 N  N   . GLN   D 1 237 ? 30.500  -28.544 -11.656 1.00 84.04  ? 306  GLN   D N   1 
ATOM   10398 C  CA  . GLN   D 1 237 ? 30.565  -27.755 -10.429 1.00 83.11  ? 306  GLN   D CA  1 
ATOM   10399 C  C   . GLN   D 1 237 ? 31.012  -28.613 -9.234  1.00 85.63  ? 306  GLN   D C   1 
ATOM   10400 O  O   . GLN   D 1 237 ? 31.714  -28.117 -8.338  1.00 86.76  ? 306  GLN   D O   1 
ATOM   10401 C  CB  . GLN   D 1 237 ? 29.208  -27.084 -10.179 1.00 81.43  ? 306  GLN   D CB  1 
ATOM   10402 C  CG  . GLN   D 1 237 ? 28.940  -25.853 -11.041 1.00 79.30  ? 306  GLN   D CG  1 
ATOM   10403 C  CD  . GLN   D 1 237 ? 27.461  -25.488 -11.120 1.00 79.86  ? 306  GLN   D CD  1 
ATOM   10404 O  OE1 . GLN   D 1 237 ? 26.582  -26.354 -11.047 1.00 76.40  ? 306  GLN   D OE1 1 
ATOM   10405 N  NE2 . GLN   D 1 237 ? 27.183  -24.195 -11.266 1.00 83.58  ? 306  GLN   D NE2 1 
ATOM   10406 N  N   . ARG   D 1 238 ? 30.669  -29.911 -9.232  1.00 80.93  ? 307  ARG   D N   1 
ATOM   10407 C  CA  . ARG   D 1 238 ? 31.060  -30.796 -8.135  1.00 78.67  ? 307  ARG   D CA  1 
ATOM   10408 C  C   . ARG   D 1 238 ? 32.551  -31.143 -8.186  1.00 79.61  ? 307  ARG   D C   1 
ATOM   10409 O  O   . ARG   D 1 238 ? 33.210  -31.194 -7.139  1.00 77.97  ? 307  ARG   D O   1 
ATOM   10410 C  CB  . ARG   D 1 238 ? 30.204  -32.056 -8.178  1.00 78.24  ? 307  ARG   D CB  1 
ATOM   10411 C  CG  . ARG   D 1 238 ? 30.197  -32.929 -6.955  1.00 77.08  ? 307  ARG   D CG  1 
ATOM   10412 C  CD  . ARG   D 1 238 ? 29.240  -34.096 -7.165  1.00 78.06  ? 307  ARG   D CD  1 
ATOM   10413 N  NE  . ARG   D 1 238 ? 27.902  -33.632 -7.530  1.00 82.52  ? 307  ARG   D NE  1 
ATOM   10414 C  CZ  . ARG   D 1 238 ? 27.316  -33.825 -8.710  1.00 86.13  ? 307  ARG   D CZ  1 
ATOM   10415 N  NH1 . ARG   D 1 238 ? 27.884  -34.553 -9.657  1.00 86.36  ? 307  ARG   D NH1 1 
ATOM   10416 N  NH2 . ARG   D 1 238 ? 26.129  -33.273 -8.944  1.00 84.72  ? 307  ARG   D NH2 1 
ATOM   10417 N  N   . LEU   D 1 239 ? 33.102  -31.402 -9.389  1.00 79.75  ? 308  LEU   D N   1 
ATOM   10418 C  CA  . LEU   D 1 239 ? 34.556  -31.550 -9.549  1.00 76.54  ? 308  LEU   D CA  1 
ATOM   10419 C  C   . LEU   D 1 239 ? 35.290  -30.234 -9.293  1.00 77.32  ? 308  LEU   D C   1 
ATOM   10420 O  O   . LEU   D 1 239 ? 36.394  -30.223 -8.731  1.00 75.73  ? 308  LEU   D O   1 
ATOM   10421 C  CB  . LEU   D 1 239 ? 34.898  -32.030 -10.959 1.00 75.84  ? 308  LEU   D CB  1 
ATOM   10422 C  CG  . LEU   D 1 239 ? 34.239  -33.250 -11.564 1.00 76.06  ? 308  LEU   D CG  1 
ATOM   10423 C  CD1 . LEU   D 1 239 ? 34.682  -33.382 -12.973 1.00 75.97  ? 308  LEU   D CD1 1 
ATOM   10424 C  CD2 . LEU   D 1 239 ? 34.638  -34.470 -10.799 1.00 82.81  ? 308  LEU   D CD2 1 
ATOM   10425 N  N   . ARG   D 1 240 ? 34.722  -29.122 -9.755  1.00 77.93  ? 309  ARG   D N   1 
ATOM   10426 C  CA  . ARG   D 1 240 ? 35.319  -27.835 -9.445  1.00 77.57  ? 309  ARG   D CA  1 
ATOM   10427 C  C   . ARG   D 1 240 ? 35.325  -27.602 -7.951  1.00 82.89  ? 309  ARG   D C   1 
ATOM   10428 O  O   . ARG   D 1 240 ? 36.221  -26.927 -7.427  1.00 84.81  ? 309  ARG   D O   1 
ATOM   10429 C  CB  . ARG   D 1 240 ? 34.578  -26.707 -10.167 1.00 77.26  ? 309  ARG   D CB  1 
ATOM   10430 C  CG  . ARG   D 1 240 ? 35.215  -26.400 -11.490 1.00 75.97  ? 309  ARG   D CG  1 
ATOM   10431 C  CD  . ARG   D 1 240 ? 34.426  -25.455 -12.312 1.00 76.81  ? 309  ARG   D CD  1 
ATOM   10432 N  NE  . ARG   D 1 240 ? 34.253  -24.180 -11.641 1.00 83.63  ? 309  ARG   D NE  1 
ATOM   10433 C  CZ  . ARG   D 1 240 ? 35.153  -23.209 -11.610 1.00 84.84  ? 309  ARG   D CZ  1 
ATOM   10434 N  NH1 . ARG   D 1 240 ? 36.352  -23.350 -12.162 1.00 78.16  ? 309  ARG   D NH1 1 
ATOM   10435 N  NH2 . ARG   D 1 240 ? 34.839  -22.067 -11.007 1.00 88.25  ? 309  ARG   D NH2 1 
ATOM   10436 N  N   . CYS   D 1 241 ? 34.365  -28.184 -7.240  1.00 83.81  ? 310  CYS   D N   1 
ATOM   10437 C  CA  . CYS   D 1 241 ? 34.318  -27.953 -5.809  1.00 83.26  ? 310  CYS   D CA  1 
ATOM   10438 C  C   . CYS   D 1 241 ? 35.206  -28.929 -5.049  1.00 76.00  ? 310  CYS   D C   1 
ATOM   10439 O  O   . CYS   D 1 241 ? 35.928  -28.513 -4.140  1.00 76.10  ? 310  CYS   D O   1 
ATOM   10440 C  CB  . CYS   D 1 241 ? 32.882  -28.022 -5.310  1.00 83.60  ? 310  CYS   D CB  1 
ATOM   10441 S  SG  . CYS   D 1 241 ? 32.831  -27.496 -3.621  1.00 87.50  ? 310  CYS   D SG  1 
ATOM   10442 N  N   . GLU   D 1 242 ? 35.177  -30.219 -5.406  1.00 76.22  ? 311  GLU   D N   1 
ATOM   10443 C  CA  . GLU   D 1 242 ? 36.101  -31.168 -4.784  1.00 76.71  ? 311  GLU   D CA  1 
ATOM   10444 C  C   . GLU   D 1 242 ? 37.538  -30.736 -5.002  1.00 76.48  ? 311  GLU   D C   1 
ATOM   10445 O  O   . GLU   D 1 242 ? 38.399  -30.887 -4.122  1.00 76.72  ? 311  GLU   D O   1 
ATOM   10446 C  CB  . GLU   D 1 242 ? 35.896  -32.562 -5.363  1.00 76.77  ? 311  GLU   D CB  1 
ATOM   10447 C  CG  . GLU   D 1 242 ? 34.598  -33.159 -5.005  1.00 76.97  ? 311  GLU   D CG  1 
ATOM   10448 C  CD  . GLU   D 1 242 ? 34.139  -34.076 -6.065  1.00 77.01  ? 311  GLU   D CD  1 
ATOM   10449 O  OE1 . GLU   D 1 242 ? 34.796  -34.080 -7.109  1.00 76.83  ? 311  GLU   D OE1 1 
ATOM   10450 O  OE2 . GLU   D 1 242 ? 33.151  -34.801 -5.856  1.00 77.25  ? 311  GLU   D OE2 1 
ATOM   10451 N  N   . LEU   D 1 243 ? 37.813  -30.213 -6.183  1.00 76.18  ? 312  LEU   D N   1 
ATOM   10452 C  CA  . LEU   D 1 243 ? 39.137  -29.701 -6.444  1.00 76.11  ? 312  LEU   D CA  1 
ATOM   10453 C  C   . LEU   D 1 243 ? 39.444  -28.520 -5.535  1.00 80.44  ? 312  LEU   D C   1 
ATOM   10454 O  O   . LEU   D 1 243 ? 40.611  -28.276 -5.205  1.00 86.18  ? 312  LEU   D O   1 
ATOM   10455 C  CB  . LEU   D 1 243 ? 39.226  -29.329 -7.918  1.00 75.82  ? 312  LEU   D CB  1 
ATOM   10456 C  CG  . LEU   D 1 243 ? 40.575  -29.389 -8.596  1.00 76.60  ? 312  LEU   D CG  1 
ATOM   10457 C  CD1 . LEU   D 1 243 ? 41.414  -30.508 -8.038  1.00 77.65  ? 312  LEU   D CD1 1 
ATOM   10458 C  CD2 . LEU   D 1 243 ? 40.327  -29.552 -10.085 1.00 82.42  ? 312  LEU   D CD2 1 
ATOM   10459 N  N   . ASP   D 1 244 ? 38.416  -27.784 -5.104  1.00 80.64  ? 313  ASP   D N   1 
ATOM   10460 C  CA  . ASP   D 1 244 ? 38.657  -26.698 -4.163  1.00 79.96  ? 313  ASP   D CA  1 
ATOM   10461 C  C   . ASP   D 1 244 ? 38.858  -27.232 -2.760  1.00 79.64  ? 313  ASP   D C   1 
ATOM   10462 O  O   . ASP   D 1 244 ? 39.667  -26.698 -1.997  1.00 78.36  ? 313  ASP   D O   1 
ATOM   10463 C  CB  . ASP   D 1 244 ? 37.498  -25.701 -4.186  1.00 80.85  ? 313  ASP   D CB  1 
ATOM   10464 C  CG  . ASP   D 1 244 ? 37.978  -24.276 -4.155  1.00 84.43  ? 313  ASP   D CG  1 
ATOM   10465 O  OD1 . ASP   D 1 244 ? 39.073  -24.045 -4.706  1.00 87.02  ? 313  ASP   D OD1 1 
ATOM   10466 O  OD2 . ASP   D 1 244 ? 37.285  -23.396 -3.597  1.00 84.07  ? 313  ASP   D OD2 1 
ATOM   10467 N  N   . ILE   D 1 245 ? 38.141  -28.289 -2.409  1.00 80.58  ? 314  ILE   D N   1 
ATOM   10468 C  CA  . ILE   D 1 245 ? 38.314  -28.897 -1.103  1.00 78.28  ? 314  ILE   D CA  1 
ATOM   10469 C  C   . ILE   D 1 245 ? 39.776  -29.288 -0.914  1.00 79.90  ? 314  ILE   D C   1 
ATOM   10470 O  O   . ILE   D 1 245 ? 40.467  -28.740 -0.053  1.00 81.77  ? 314  ILE   D O   1 
ATOM   10471 C  CB  . ILE   D 1 245 ? 37.339  -30.077 -0.945  1.00 77.17  ? 314  ILE   D CB  1 
ATOM   10472 C  CG1 . ILE   D 1 245 ? 35.967  -29.525 -0.597  1.00 77.08  ? 314  ILE   D CG1 1 
ATOM   10473 C  CG2 . ILE   D 1 245 ? 37.799  -31.046 0.100   1.00 79.47  ? 314  ILE   D CG2 1 
ATOM   10474 C  CD1 . ILE   D 1 245 ? 34.845  -30.259 -1.210  1.00 77.08  ? 314  ILE   D CD1 1 
ATOM   10475 N  N   . MET   D 1 246 ? 40.298  -30.160 -1.788  1.00 79.10  ? 315  MET   D N   1 
ATOM   10476 C  CA  . MET   D 1 246 ? 41.687  -30.613 -1.654  1.00 80.53  ? 315  MET   D CA  1 
ATOM   10477 C  C   . MET   D 1 246 ? 42.677  -29.455 -1.681  1.00 83.31  ? 315  MET   D C   1 
ATOM   10478 O  O   . MET   D 1 246 ? 43.717  -29.498 -1.015  1.00 89.10  ? 315  MET   D O   1 
ATOM   10479 C  CB  . MET   D 1 246 ? 42.047  -31.581 -2.773  1.00 77.85  ? 315  MET   D CB  1 
ATOM   10480 C  CG  . MET   D 1 246 ? 40.978  -32.519 -3.129  1.00 77.48  ? 315  MET   D CG  1 
ATOM   10481 S  SD  . MET   D 1 246 ? 41.552  -33.332 -4.593  1.00 79.64  ? 315  MET   D SD  1 
ATOM   10482 C  CE  . MET   D 1 246 ? 41.865  -35.005 -4.002  1.00 86.08  ? 315  MET   D CE  1 
ATOM   10483 N  N   . ASN   D 1 247 ? 42.412  -28.444 -2.493  1.00 82.21  ? 316  ASN   D N   1 
ATOM   10484 C  CA  . ASN   D 1 247 ? 43.366  -27.354 -2.597  1.00 84.62  ? 316  ASN   D CA  1 
ATOM   10485 C  C   . ASN   D 1 247 ? 43.290  -26.381 -1.418  1.00 85.39  ? 316  ASN   D C   1 
ATOM   10486 O  O   . ASN   D 1 247 ? 44.298  -25.727 -1.120  1.00 83.39  ? 316  ASN   D O   1 
ATOM   10487 C  CB  . ASN   D 1 247 ? 43.155  -26.596 -3.916  1.00 91.24  ? 316  ASN   D CB  1 
ATOM   10488 C  CG  . ASN   D 1 247 ? 43.817  -27.271 -5.116  1.00 92.02  ? 316  ASN   D CG  1 
ATOM   10489 O  OD1 . ASN   D 1 247 ? 43.666  -28.469 -5.347  1.00 88.08  ? 316  ASN   D OD1 1 
ATOM   10490 N  ND2 . ASN   D 1 247 ? 44.540  -26.481 -5.896  1.00 101.47 ? 316  ASN   D ND2 1 
ATOM   10491 N  N   . LYS   D 1 248 ? 42.135  -26.278 -0.734  1.00 85.56  ? 317  LYS   D N   1 
ATOM   10492 C  CA  . LYS   D 1 248 ? 41.895  -25.264 0.290   1.00 82.72  ? 317  LYS   D CA  1 
ATOM   10493 C  C   . LYS   D 1 248 ? 41.684  -25.806 1.706   1.00 84.72  ? 317  LYS   D C   1 
ATOM   10494 O  O   . LYS   D 1 248 ? 42.038  -25.113 2.654   1.00 85.44  ? 317  LYS   D O   1 
ATOM   10495 C  CB  . LYS   D 1 248 ? 40.663  -24.415 -0.089  1.00 85.31  ? 317  LYS   D CB  1 
ATOM   10496 C  CG  . LYS   D 1 248 ? 40.896  -23.242 -1.082  1.00 83.00  ? 317  LYS   D CG  1 
ATOM   10497 C  CD  . LYS   D 1 248 ? 39.802  -22.152 -0.913  1.00 89.86  ? 317  LYS   D CD  1 
ATOM   10498 C  CE  . LYS   D 1 248 ? 39.778  -21.128 -2.054  1.00 93.23  ? 317  LYS   D CE  1 
ATOM   10499 N  NZ  . LYS   D 1 248 ? 38.680  -21.370 -3.062  1.00 87.98  ? 317  LYS   D NZ  1 
ATOM   10500 N  N   . CYS   D 1 249 ? 41.087  -26.993 1.877   1.00 89.53  ? 318  CYS   D N   1 
ATOM   10501 C  CA  . CYS   D 1 249 ? 40.934  -27.648 3.193   1.00 85.14  ? 318  CYS   D CA  1 
ATOM   10502 C  C   . CYS   D 1 249 ? 42.130  -28.550 3.446   1.00 81.87  ? 318  CYS   D C   1 
ATOM   10503 O  O   . CYS   D 1 249 ? 42.061  -29.777 3.317   1.00 84.67  ? 318  CYS   D O   1 
ATOM   10504 C  CB  . CYS   D 1 249 ? 39.655  -28.470 3.259   1.00 80.85  ? 318  CYS   D CB  1 
ATOM   10505 S  SG  . CYS   D 1 249 ? 38.209  -27.541 3.007   1.00 82.90  ? 318  CYS   D SG  1 
ATOM   10506 N  N   . THR   D 1 250 ? 43.235  -27.928 3.836   1.00 82.06  ? 319  THR   D N   1 
ATOM   10507 C  CA  . THR   D 1 250 ? 44.521  -28.603 3.915   1.00 86.55  ? 319  THR   D CA  1 
ATOM   10508 C  C   . THR   D 1 250 ? 44.876  -29.038 5.326   1.00 89.23  ? 319  THR   D C   1 
ATOM   10509 O  O   . THR   D 1 250 ? 45.931  -29.649 5.530   1.00 90.53  ? 319  THR   D O   1 
ATOM   10510 C  CB  . THR   D 1 250 ? 45.609  -27.692 3.351   1.00 88.51  ? 319  THR   D CB  1 
ATOM   10511 O  OG1 . THR   D 1 250 ? 45.655  -26.458 4.089   1.00 87.27  ? 319  THR   D OG1 1 
ATOM   10512 C  CG2 . THR   D 1 250 ? 45.312  -27.399 1.902   1.00 86.99  ? 319  THR   D CG2 1 
ATOM   10513 N  N   . SER   D 1 251 ? 43.992  -28.779 6.284   1.00 89.67  ? 320  SER   D N   1 
ATOM   10514 C  CA  . SER   D 1 251 ? 44.198  -29.047 7.699   1.00 91.71  ? 320  SER   D CA  1 
ATOM   10515 C  C   . SER   D 1 251 ? 42.985  -29.805 8.235   1.00 91.28  ? 320  SER   D C   1 
ATOM   10516 O  O   . SER   D 1 251 ? 41.843  -29.373 8.033   1.00 89.63  ? 320  SER   D O   1 
ATOM   10517 C  CB  . SER   D 1 251 ? 44.403  -27.715 8.445   1.00 95.29  ? 320  SER   D CB  1 
ATOM   10518 O  OG  . SER   D 1 251 ? 44.592  -27.883 9.836   1.00 99.64  ? 320  SER   D OG  1 
ATOM   10519 N  N   . LEU   D 1 252 ? 43.224  -30.934 8.907   1.00 92.50  ? 321  LEU   D N   1 
ATOM   10520 C  CA  . LEU   D 1 252 ? 42.153  -31.771 9.442   1.00 94.50  ? 321  LEU   D CA  1 
ATOM   10521 C  C   . LEU   D 1 252 ? 42.074  -31.627 10.964  1.00 94.17  ? 321  LEU   D C   1 
ATOM   10522 O  O   . LEU   D 1 252 ? 43.080  -31.787 11.664  1.00 93.69  ? 321  LEU   D O   1 
ATOM   10523 C  CB  . LEU   D 1 252 ? 42.362  -33.233 9.030   1.00 90.72  ? 321  LEU   D CB  1 
ATOM   10524 C  CG  . LEU   D 1 252 ? 42.113  -33.590 7.558   1.00 84.62  ? 321  LEU   D CG  1 
ATOM   10525 C  CD1 . LEU   D 1 252 ? 42.654  -34.968 7.259   1.00 82.90  ? 321  LEU   D CD1 1 
ATOM   10526 C  CD2 . LEU   D 1 252 ? 40.630  -33.506 7.191   1.00 86.20  ? 321  LEU   D CD2 1 
ATOM   10527 N  N   . CYS   D 1 253 ? 40.875  -31.328 11.468  1.00 94.63  ? 322  CYS   D N   1 
ATOM   10528 C  CA  . CYS   D 1 253 ? 40.642  -30.927 12.851  1.00 95.89  ? 322  CYS   D CA  1 
ATOM   10529 C  C   . CYS   D 1 253 ? 39.649  -31.855 13.540  1.00 96.13  ? 322  CYS   D C   1 
ATOM   10530 O  O   . CYS   D 1 253 ? 38.939  -32.630 12.896  1.00 98.59  ? 322  CYS   D O   1 
ATOM   10531 C  CB  . CYS   D 1 253 ? 40.112  -29.495 12.907  1.00 97.13  ? 322  CYS   D CB  1 
ATOM   10532 S  SG  . CYS   D 1 253 ? 41.302  -28.280 12.375  1.00 95.99  ? 322  CYS   D SG  1 
ATOM   10533 N  N   . CYS   D 1 254 ? 39.591  -31.751 14.870  1.00 96.66  ? 323  CYS   D N   1 
ATOM   10534 C  CA  . CYS   D 1 254 ? 38.607  -32.500 15.646  1.00 97.37  ? 323  CYS   D CA  1 
ATOM   10535 C  C   . CYS   D 1 254 ? 37.201  -31.989 15.348  1.00 100.12 ? 323  CYS   D C   1 
ATOM   10536 O  O   . CYS   D 1 254 ? 36.949  -30.785 15.405  1.00 102.28 ? 323  CYS   D O   1 
ATOM   10537 C  CB  . CYS   D 1 254 ? 38.905  -32.372 17.135  1.00 95.98  ? 323  CYS   D CB  1 
ATOM   10538 S  SG  . CYS   D 1 254 ? 37.811  -33.297 18.207  1.00 111.30 ? 323  CYS   D SG  1 
ATOM   10539 N  N   . LYS   D 1 255 ? 36.276  -32.899 15.023  1.00 100.42 ? 324  LYS   D N   1 
ATOM   10540 C  CA  . LYS   D 1 255 ? 34.935  -32.461 14.642  1.00 100.80 ? 324  LYS   D CA  1 
ATOM   10541 C  C   . LYS   D 1 255 ? 34.170  -31.897 15.832  1.00 104.46 ? 324  LYS   D C   1 
ATOM   10542 O  O   . LYS   D 1 255 ? 33.343  -30.992 15.664  1.00 99.42  ? 324  LYS   D O   1 
ATOM   10543 C  CB  . LYS   D 1 255 ? 34.158  -33.619 14.009  1.00 100.22 ? 324  LYS   D CB  1 
ATOM   10544 C  CG  . LYS   D 1 255 ? 33.034  -33.170 13.065  1.00 100.21 ? 324  LYS   D CG  1 
ATOM   10545 C  CD  . LYS   D 1 255 ? 32.187  -34.330 12.564  1.00 99.11  ? 324  LYS   D CD  1 
ATOM   10546 C  CE  . LYS   D 1 255 ? 31.296  -34.876 13.669  1.00 107.28 ? 324  LYS   D CE  1 
ATOM   10547 N  NZ  . LYS   D 1 255 ? 30.624  -36.134 13.285  1.00 111.40 ? 324  LYS   D NZ  1 
ATOM   10548 N  N   . GLN   D 1 256 ? 34.465  -32.403 17.038  1.00 115.07 ? 325  GLN   D N   1 
ATOM   10549 C  CA  . GLN   D 1 256 ? 33.678  -32.134 18.241  1.00 114.92 ? 325  GLN   D CA  1 
ATOM   10550 C  C   . GLN   D 1 256 ? 33.973  -30.764 18.835  1.00 111.66 ? 325  GLN   D C   1 
ATOM   10551 O  O   . GLN   D 1 256 ? 33.061  -30.070 19.302  1.00 111.81 ? 325  GLN   D O   1 
ATOM   10552 C  CB  . GLN   D 1 256 ? 33.953  -33.220 19.283  1.00 113.86 ? 325  GLN   D CB  1 
ATOM   10553 C  CG  . GLN   D 1 256 ? 33.340  -34.538 18.925  1.00 117.46 ? 325  GLN   D CG  1 
ATOM   10554 C  CD  . GLN   D 1 256 ? 31.848  -34.487 19.072  1.00 123.58 ? 325  GLN   D CD  1 
ATOM   10555 O  OE1 . GLN   D 1 256 ? 31.110  -35.147 18.337  1.00 130.59 ? 325  GLN   D OE1 1 
ATOM   10556 N  NE2 . GLN   D 1 256 ? 31.385  -33.673 20.027  1.00 125.30 ? 325  GLN   D NE2 1 
ATOM   10557 N  N   . CYS   D 1 257 ? 35.236  -30.362 18.832  1.00 105.37 ? 326  CYS   D N   1 
ATOM   10558 C  CA  . CYS   D 1 257 ? 35.633  -29.110 19.430  1.00 98.78  ? 326  CYS   D CA  1 
ATOM   10559 C  C   . CYS   D 1 257 ? 36.160  -28.071 18.437  1.00 106.11 ? 326  CYS   D C   1 
ATOM   10560 O  O   . CYS   D 1 257 ? 36.193  -26.893 18.783  1.00 111.89 ? 326  CYS   D O   1 
ATOM   10561 C  CB  . CYS   D 1 257 ? 36.689  -29.371 20.513  1.00 99.93  ? 326  CYS   D CB  1 
ATOM   10562 S  SG  . CYS   D 1 257 ? 38.388  -29.616 19.907  1.00 95.60  ? 326  CYS   D SG  1 
ATOM   10563 N  N   . GLN   D 1 258 ? 36.537  -28.466 17.212  1.00 107.39 ? 327  GLN   D N   1 
ATOM   10564 C  CA  . GLN   D 1 258 ? 36.977  -27.547 16.135  1.00 103.69 ? 327  GLN   D CA  1 
ATOM   10565 C  C   . GLN   D 1 258 ? 38.062  -26.580 16.574  1.00 104.58 ? 327  GLN   D C   1 
ATOM   10566 O  O   . GLN   D 1 258 ? 38.008  -25.386 16.277  1.00 108.49 ? 327  GLN   D O   1 
ATOM   10567 C  CB  . GLN   D 1 258 ? 35.822  -26.743 15.559  1.00 102.99 ? 327  GLN   D CB  1 
ATOM   10568 C  CG  . GLN   D 1 258 ? 34.667  -27.529 15.064  1.00 108.93 ? 327  GLN   D CG  1 
ATOM   10569 C  CD  . GLN   D 1 258 ? 33.554  -26.604 14.693  1.00 116.60 ? 327  GLN   D CD  1 
ATOM   10570 O  OE1 . GLN   D 1 258 ? 33.727  -25.382 14.734  1.00 117.10 ? 327  GLN   D OE1 1 
ATOM   10571 N  NE2 . GLN   D 1 258 ? 32.401  -27.163 14.333  1.00 123.25 ? 327  GLN   D NE2 1 
ATOM   10572 N  N   . GLU   D 1 259 ? 39.087  -27.092 17.238  1.00 108.03 ? 328  GLU   D N   1 
ATOM   10573 C  CA  . GLU   D 1 259 ? 40.088  -26.196 17.785  1.00 108.33 ? 328  GLU   D CA  1 
ATOM   10574 C  C   . GLU   D 1 259 ? 41.468  -26.792 17.617  1.00 110.52 ? 328  GLU   D C   1 
ATOM   10575 O  O   . GLU   D 1 259 ? 42.454  -26.073 17.441  1.00 116.07 ? 328  GLU   D O   1 
ATOM   10576 C  CB  . GLU   D 1 259 ? 39.816  -25.920 19.263  1.00 109.26 ? 328  GLU   D CB  1 
ATOM   10577 N  N   . THR   D 1 260 ? 41.552  -28.103 17.685  1.00 120.26 ? 329  THR   D N   1 
ATOM   10578 C  CA  . THR   D 1 260 ? 42.825  -28.775 17.513  1.00 120.46 ? 329  THR   D CA  1 
ATOM   10579 C  C   . THR   D 1 260 ? 42.987  -29.270 16.080  1.00 119.06 ? 329  THR   D C   1 
ATOM   10580 O  O   . THR   D 1 260 ? 42.110  -29.954 15.534  1.00 119.29 ? 329  THR   D O   1 
ATOM   10581 C  CB  . THR   D 1 260 ? 42.941  -29.915 18.507  1.00 122.48 ? 329  THR   D CB  1 
ATOM   10582 O  OG1 . THR   D 1 260 ? 41.797  -30.769 18.398  1.00 127.51 ? 329  THR   D OG1 1 
ATOM   10583 C  CG2 . THR   D 1 260 ? 42.985  -29.341 19.853  1.00 123.02 ? 329  THR   D CG2 1 
ATOM   10584 N  N   . GLU   D 1 261 ? 44.110  -28.899 15.479  1.00 108.83 ? 330  GLU   D N   1 
ATOM   10585 C  CA  . GLU   D 1 261 ? 44.536  -29.437 14.200  1.00 102.10 ? 330  GLU   D CA  1 
ATOM   10586 C  C   . GLU   D 1 261 ? 45.092  -30.841 14.405  1.00 101.32 ? 330  GLU   D C   1 
ATOM   10587 O  O   . GLU   D 1 261 ? 46.107  -31.021 15.091  1.00 100.90 ? 330  GLU   D O   1 
ATOM   10588 C  CB  . GLU   D 1 261 ? 45.597  -28.512 13.608  1.00 106.07 ? 330  GLU   D CB  1 
ATOM   10589 C  CG  . GLU   D 1 261 ? 46.438  -29.115 12.472  1.00 109.35 ? 330  GLU   D CG  1 
ATOM   10590 C  CD  . GLU   D 1 261 ? 47.522  -28.163 11.949  1.00 112.06 ? 330  GLU   D CD  1 
ATOM   10591 O  OE1 . GLU   D 1 261 ? 48.350  -27.678 12.757  1.00 109.39 ? 330  GLU   D OE1 1 
ATOM   10592 O  OE2 . GLU   D 1 261 ? 47.540  -27.906 10.722  1.00 113.91 ? 330  GLU   D OE2 1 
ATOM   10593 N  N   . ILE   D 1 262 ? 44.438  -31.840 13.813  1.00 98.99  ? 331  ILE   D N   1 
ATOM   10594 C  CA  . ILE   D 1 262 ? 44.888  -33.215 13.989  1.00 97.36  ? 331  ILE   D CA  1 
ATOM   10595 C  C   . ILE   D 1 262 ? 46.008  -33.546 13.000  1.00 96.95  ? 331  ILE   D C   1 
ATOM   10596 O  O   . ILE   D 1 262 ? 47.118  -33.920 13.397  1.00 101.40 ? 331  ILE   D O   1 
ATOM   10597 C  CB  . ILE   D 1 262 ? 43.696  -34.181 13.886  1.00 94.10  ? 331  ILE   D CB  1 
ATOM   10598 C  CG1 . ILE   D 1 262 ? 42.556  -33.652 14.751  1.00 91.98  ? 331  ILE   D CG1 1 
ATOM   10599 C  CG2 . ILE   D 1 262 ? 44.095  -35.564 14.393  1.00 93.56  ? 331  ILE   D CG2 1 
ATOM   10600 C  CD1 . ILE   D 1 262 ? 42.800  -33.813 16.194  1.00 92.62  ? 331  ILE   D CD1 1 
ATOM   10601 N  N   . THR   D 1 263 ? 45.761  -33.376 11.705  1.00 94.07  ? 332  THR   D N   1 
ATOM   10602 C  CA  . THR   D 1 263 ? 46.783  -33.685 10.713  1.00 94.22  ? 332  THR   D CA  1 
ATOM   10603 C  C   . THR   D 1 263 ? 46.636  -32.703 9.546   1.00 96.70  ? 332  THR   D C   1 
ATOM   10604 O  O   . THR   D 1 263 ? 45.867  -31.736 9.616   1.00 94.64  ? 332  THR   D O   1 
ATOM   10605 C  CB  . THR   D 1 263 ? 46.669  -35.164 10.308  1.00 93.80  ? 332  THR   D CB  1 
ATOM   10606 O  OG1 . THR   D 1 263 ? 47.828  -35.570 9.563   1.00 93.39  ? 332  THR   D OG1 1 
ATOM   10607 C  CG2 . THR   D 1 263 ? 45.435  -35.381 9.468   1.00 93.49  ? 332  THR   D CG2 1 
ATOM   10608 N  N   . THR   D 1 264 ? 47.383  -32.951 8.469   1.00 98.98  ? 333  THR   D N   1 
ATOM   10609 C  CA  . THR   D 1 264 ? 47.455  -32.040 7.340   1.00 96.30  ? 333  THR   D CA  1 
ATOM   10610 C  C   . THR   D 1 264 ? 47.601  -32.847 6.059   1.00 96.46  ? 333  THR   D C   1 
ATOM   10611 O  O   . THR   D 1 264 ? 48.088  -33.973 6.071   1.00 99.14  ? 333  THR   D O   1 
ATOM   10612 C  CB  . THR   D 1 264 ? 48.614  -31.058 7.503   1.00 95.88  ? 333  THR   D CB  1 
ATOM   10613 O  OG1 . THR   D 1 264 ? 48.725  -30.269 6.327   1.00 102.14 ? 333  THR   D OG1 1 
ATOM   10614 C  CG2 . THR   D 1 264 ? 49.915  -31.785 7.682   1.00 96.47  ? 333  THR   D CG2 1 
ATOM   10615 N  N   . LYS   D 1 265 ? 47.182  -32.240 4.945   1.00 98.13  ? 334  LYS   D N   1 
ATOM   10616 C  CA  . LYS   D 1 265 ? 47.048  -32.957 3.677   1.00 100.81 ? 334  LYS   D CA  1 
ATOM   10617 C  C   . LYS   D 1 265 ? 48.317  -33.727 3.325   1.00 103.62 ? 334  LYS   D C   1 
ATOM   10618 O  O   . LYS   D 1 265 ? 48.273  -34.934 3.042   1.00 98.54  ? 334  LYS   D O   1 
ATOM   10619 C  CB  . LYS   D 1 265 ? 46.691  -31.970 2.561   1.00 94.54  ? 334  LYS   D CB  1 
ATOM   10620 N  N   . ASN   D 1 266 ? 49.465  -33.043 3.370   1.00 112.54 ? 335  ASN   D N   1 
ATOM   10621 C  CA  . ASN   D 1 266 ? 50.705  -33.599 2.839   1.00 113.69 ? 335  ASN   D CA  1 
ATOM   10622 C  C   . ASN   D 1 266 ? 51.172  -34.855 3.577   1.00 114.68 ? 335  ASN   D C   1 
ATOM   10623 O  O   . ASN   D 1 266 ? 52.037  -35.566 3.061   1.00 118.93 ? 335  ASN   D O   1 
ATOM   10624 C  CB  . ASN   D 1 266 ? 51.791  -32.537 2.887   1.00 113.99 ? 335  ASN   D CB  1 
ATOM   10625 C  CG  . ASN   D 1 266 ? 51.951  -31.964 4.275   1.00 118.04 ? 335  ASN   D CG  1 
ATOM   10626 O  OD1 . ASN   D 1 266 ? 52.226  -32.691 5.239   1.00 120.46 ? 335  ASN   D OD1 1 
ATOM   10627 N  ND2 . ASN   D 1 266 ? 51.699  -30.668 4.404   1.00 123.22 ? 335  ASN   D ND2 1 
ATOM   10628 N  N   . GLU   D 1 267 ? 50.639  -35.140 4.767   1.00 104.28 ? 336  GLU   D N   1 
ATOM   10629 C  CA  . GLU   D 1 267 ? 50.932  -36.398 5.454   1.00 101.14 ? 336  GLU   D CA  1 
ATOM   10630 C  C   . GLU   D 1 267 ? 50.003  -37.537 5.033   1.00 97.20  ? 336  GLU   D C   1 
ATOM   10631 O  O   . GLU   D 1 267 ? 50.194  -38.671 5.492   1.00 96.58  ? 336  GLU   D O   1 
ATOM   10632 C  CB  . GLU   D 1 267 ? 50.839  -36.256 6.990   1.00 98.66  ? 336  GLU   D CB  1 
ATOM   10633 C  CG  . GLU   D 1 267 ? 51.328  -34.963 7.632   1.00 98.56  ? 336  GLU   D CG  1 
ATOM   10634 C  CD  . GLU   D 1 267 ? 52.841  -34.815 7.685   1.00 103.31 ? 336  GLU   D CD  1 
ATOM   10635 O  OE1 . GLU   D 1 267 ? 53.569  -35.768 7.330   1.00 98.50  ? 336  GLU   D OE1 1 
ATOM   10636 O  OE2 . GLU   D 1 267 ? 53.305  -33.721 8.091   1.00 107.71 ? 336  GLU   D OE2 1 
ATOM   10637 N  N   . ILE   D 1 268 ? 48.997  -37.281 4.204   1.00 94.88  ? 337  ILE   D N   1 
ATOM   10638 C  CA  . ILE   D 1 268 ? 48.093  -38.359 3.831   1.00 94.02  ? 337  ILE   D CA  1 
ATOM   10639 C  C   . ILE   D 1 268 ? 48.838  -39.359 2.958   1.00 94.64  ? 337  ILE   D C   1 
ATOM   10640 O  O   . ILE   D 1 268 ? 49.559  -38.971 2.026   1.00 95.00  ? 337  ILE   D O   1 
ATOM   10641 C  CB  . ILE   D 1 268 ? 46.865  -37.805 3.115   1.00 90.52  ? 337  ILE   D CB  1 
ATOM   10642 C  CG1 . ILE   D 1 268 ? 46.135  -36.884 4.065   1.00 87.14  ? 337  ILE   D CG1 1 
ATOM   10643 C  CG2 . ILE   D 1 268 ? 45.963  -38.935 2.682   1.00 87.29  ? 337  ILE   D CG2 1 
ATOM   10644 C  CD1 . ILE   D 1 268 ? 44.860  -36.445 3.522   1.00 83.74  ? 337  ILE   D CD1 1 
ATOM   10645 N  N   . PHE   D 1 269 ? 48.672  -40.648 3.262   1.00 93.36  ? 338  PHE   D N   1 
ATOM   10646 C  CA  . PHE   D 1 269 ? 49.390  -41.717 2.583   1.00 92.29  ? 338  PHE   D CA  1 
ATOM   10647 C  C   . PHE   D 1 269 ? 48.589  -43.009 2.633   1.00 94.53  ? 338  PHE   D C   1 
ATOM   10648 O  O   . PHE   D 1 269 ? 47.746  -43.219 3.509   1.00 95.75  ? 338  PHE   D O   1 
ATOM   10649 C  CB  . PHE   D 1 269 ? 50.780  -41.960 3.186   1.00 90.58  ? 338  PHE   D CB  1 
ATOM   10650 C  CG  . PHE   D 1 269 ? 50.832  -43.027 4.276   1.00 94.81  ? 338  PHE   D CG  1 
ATOM   10651 C  CD1 . PHE   D 1 269 ? 50.341  -42.782 5.553   1.00 98.63  ? 338  PHE   D CD1 1 
ATOM   10652 C  CD2 . PHE   D 1 269 ? 51.425  -44.255 4.036   1.00 97.20  ? 338  PHE   D CD2 1 
ATOM   10653 C  CE1 . PHE   D 1 269 ? 50.416  -43.768 6.551   1.00 98.42  ? 338  PHE   D CE1 1 
ATOM   10654 C  CE2 . PHE   D 1 269 ? 51.502  -45.226 5.021   1.00 98.94  ? 338  PHE   D CE2 1 
ATOM   10655 C  CZ  . PHE   D 1 269 ? 51.002  -44.985 6.274   1.00 99.14  ? 338  PHE   D CZ  1 
ATOM   10656 N  N   . SER   D 1 270 ? 48.917  -43.905 1.720   1.00 97.74  ? 339  SER   D N   1 
ATOM   10657 C  CA  . SER   D 1 270 ? 48.185  -45.154 1.565   1.00 103.80 ? 339  SER   D CA  1 
ATOM   10658 C  C   . SER   D 1 270 ? 49.105  -46.297 1.945   1.00 109.46 ? 339  SER   D C   1 
ATOM   10659 O  O   . SER   D 1 270 ? 50.027  -46.648 1.203   1.00 113.04 ? 339  SER   D O   1 
ATOM   10660 C  CB  . SER   D 1 270 ? 47.674  -45.308 0.148   1.00 111.26 ? 339  SER   D CB  1 
ATOM   10661 O  OG  . SER   D 1 270 ? 46.702  -44.330 -0.148  1.00 110.44 ? 339  SER   D OG  1 
ATOM   10662 N  N   . LEU   D 1 271 ? 48.853  -46.866 3.113   1.00 113.35 ? 340  LEU   D N   1 
ATOM   10663 C  CA  . LEU   D 1 271 ? 49.577  -48.056 3.519   1.00 117.88 ? 340  LEU   D CA  1 
ATOM   10664 C  C   . LEU   D 1 271 ? 49.196  -49.221 2.631   1.00 125.20 ? 340  LEU   D C   1 
ATOM   10665 O  O   . LEU   D 1 271 ? 50.042  -49.839 1.979   1.00 126.19 ? 340  LEU   D O   1 
ATOM   10666 C  CB  . LEU   D 1 271 ? 49.267  -48.372 4.977   1.00 111.27 ? 340  LEU   D CB  1 
ATOM   10667 C  CG  . LEU   D 1 271 ? 50.199  -49.430 5.530   1.00 113.54 ? 340  LEU   D CG  1 
ATOM   10668 C  CD1 . LEU   D 1 271 ? 51.502  -48.784 5.979   1.00 110.88 ? 340  LEU   D CD1 1 
ATOM   10669 C  CD2 . LEU   D 1 271 ? 49.521  -50.183 6.651   1.00 112.61 ? 340  LEU   D CD2 1 
ATOM   10670 N  N   . SER   D 1 272 ? 47.909  -49.521 2.591   1.00 156.16 ? 341  SER   D N   1 
ATOM   10671 C  CA  . SER   D 1 272 ? 47.399  -50.571 1.746   1.00 158.50 ? 341  SER   D CA  1 
ATOM   10672 C  C   . SER   D 1 272 ? 47.304  -50.088 0.307   1.00 159.61 ? 341  SER   D C   1 
ATOM   10673 O  O   . SER   D 1 272 ? 47.365  -48.891 0.014   1.00 160.96 ? 341  SER   D O   1 
ATOM   10674 C  CB  . SER   D 1 272 ? 46.032  -51.023 2.253   1.00 161.25 ? 341  SER   D CB  1 
ATOM   10675 O  OG  . SER   D 1 272 ? 45.420  -51.899 1.329   1.00 166.56 ? 341  SER   D OG  1 
ATOM   10676 N  N   . LEU   D 1 273 ? 47.167  -51.044 -0.606  1.00 148.53 ? 342  LEU   D N   1 
ATOM   10677 C  CA  . LEU   D 1 273 ? 46.750  -50.698 -1.956  1.00 148.60 ? 342  LEU   D CA  1 
ATOM   10678 C  C   . LEU   D 1 273 ? 45.339  -50.114 -1.977  1.00 149.13 ? 342  LEU   D C   1 
ATOM   10679 O  O   . LEU   D 1 273 ? 44.985  -49.404 -2.927  1.00 146.13 ? 342  LEU   D O   1 
ATOM   10680 C  CB  . LEU   D 1 273 ? 46.826  -51.940 -2.838  1.00 149.10 ? 342  LEU   D CB  1 
ATOM   10681 C  CG  . LEU   D 1 273 ? 46.097  -53.161 -2.260  1.00 149.97 ? 342  LEU   D CG  1 
ATOM   10682 C  CD1 . LEU   D 1 273 ? 44.660  -53.272 -2.782  1.00 151.68 ? 342  LEU   D CD1 1 
ATOM   10683 C  CD2 . LEU   D 1 273 ? 46.872  -54.447 -2.522  1.00 145.71 ? 342  LEU   D CD2 1 
ATOM   10684 N  N   . CYS   D 1 274 ? 44.540  -50.388 -0.934  1.00 149.81 ? 343  CYS   D N   1 
ATOM   10685 C  CA  . CYS   D 1 274 ? 43.098  -50.151 -0.986  1.00 147.88 ? 343  CYS   D CA  1 
ATOM   10686 C  C   . CYS   D 1 274 ? 42.755  -48.665 -1.060  1.00 142.82 ? 343  CYS   D C   1 
ATOM   10687 O  O   . CYS   D 1 274 ? 41.728  -48.290 -1.635  1.00 143.32 ? 343  CYS   D O   1 
ATOM   10688 C  CB  . CYS   D 1 274 ? 42.411  -50.787 0.224   1.00 149.56 ? 343  CYS   D CB  1 
ATOM   10689 S  SG  . CYS   D 1 274 ? 42.253  -52.604 0.209   1.00 160.39 ? 343  CYS   D SG  1 
ATOM   10690 N  N   . GLY   D 1 275 ? 43.580  -47.806 -0.473  1.00 134.55 ? 344  GLY   D N   1 
ATOM   10691 C  CA  . GLY   D 1 275 ? 43.311  -46.393 -0.499  1.00 113.07 ? 344  GLY   D CA  1 
ATOM   10692 C  C   . GLY   D 1 275 ? 44.118  -45.686 0.552   1.00 102.89 ? 344  GLY   D C   1 
ATOM   10693 O  O   . GLY   D 1 275 ? 44.860  -46.307 1.318   1.00 108.54 ? 344  GLY   D O   1 
ATOM   10694 N  N   . PRO   D 1 276 ? 44.015  -44.363 0.593   1.00 98.01  ? 345  PRO   D N   1 
ATOM   10695 C  CA  . PRO   D 1 276 ? 44.524  -43.636 1.757   1.00 96.60  ? 345  PRO   D CA  1 
ATOM   10696 C  C   . PRO   D 1 276 ? 43.488  -43.709 2.859   1.00 92.22  ? 345  PRO   D C   1 
ATOM   10697 O  O   . PRO   D 1 276 ? 43.776  -44.127 3.986   1.00 90.71  ? 345  PRO   D O   1 
ATOM   10698 C  CB  . PRO   D 1 276 ? 44.740  -42.211 1.228   1.00 90.82  ? 345  PRO   D CB  1 
ATOM   10699 C  CG  . PRO   D 1 276 ? 43.810  -42.068 0.104   1.00 92.57  ? 345  PRO   D CG  1 
ATOM   10700 C  CD  . PRO   D 1 276 ? 43.500  -43.447 -0.439  1.00 101.98 ? 345  PRO   D CD  1 
ATOM   10701 N  N   . MET   D 1 277 ? 42.262  -43.341 2.512   1.00 91.34  ? 346  MET   D N   1 
ATOM   10702 C  CA  . MET   D 1 277 ? 41.083  -43.639 3.304   1.00 85.62  ? 346  MET   D CA  1 
ATOM   10703 C  C   . MET   D 1 277 ? 40.374  -44.804 2.628   1.00 91.35  ? 346  MET   D C   1 
ATOM   10704 O  O   . MET   D 1 277 ? 40.075  -44.741 1.428   1.00 96.62  ? 346  MET   D O   1 
ATOM   10705 C  CB  . MET   D 1 277 ? 40.188  -42.415 3.385   1.00 82.45  ? 346  MET   D CB  1 
ATOM   10706 C  CG  . MET   D 1 277 ? 39.046  -42.494 4.312   1.00 81.86  ? 346  MET   D CG  1 
ATOM   10707 S  SD  . MET   D 1 277 ? 38.269  -40.914 4.083   1.00 81.25  ? 346  MET   D SD  1 
ATOM   10708 C  CE  . MET   D 1 277 ? 36.889  -41.433 3.096   1.00 85.49  ? 346  MET   D CE  1 
ATOM   10709 N  N   . ALA   D 1 278 ? 40.195  -45.890 3.370   1.00 89.39  ? 347  ALA   D N   1 
ATOM   10710 C  CA  . ALA   D 1 278 ? 39.445  -47.050 2.922   1.00 87.87  ? 347  ALA   D CA  1 
ATOM   10711 C  C   . ALA   D 1 278 ? 38.604  -47.487 4.106   1.00 90.11  ? 347  ALA   D C   1 
ATOM   10712 O  O   . ALA   D 1 278 ? 38.897  -47.120 5.241   1.00 94.93  ? 347  ALA   D O   1 
ATOM   10713 C  CB  . ALA   D 1 278 ? 40.370  -48.166 2.440   1.00 95.43  ? 347  ALA   D CB  1 
ATOM   10714 N  N   . ALA   D 1 279 ? 37.553  -48.256 3.856   1.00 89.73  ? 348  ALA   D N   1 
ATOM   10715 C  CA  . ALA   D 1 279 ? 36.542  -48.528 4.881   1.00 92.25  ? 348  ALA   D CA  1 
ATOM   10716 C  C   . ALA   D 1 279 ? 36.762  -49.884 5.552   1.00 93.49  ? 348  ALA   D C   1 
ATOM   10717 O  O   . ALA   D 1 279 ? 36.378  -50.918 4.998   1.00 101.70 ? 348  ALA   D O   1 
ATOM   10718 C  CB  . ALA   D 1 279 ? 35.153  -48.473 4.256   1.00 95.85  ? 348  ALA   D CB  1 
ATOM   10719 N  N   . TYR   D 1 280 ? 37.313  -49.887 6.760   1.00 84.88  ? 349  TYR   D N   1 
ATOM   10720 C  CA  . TYR   D 1 280 ? 37.604  -51.134 7.457   1.00 88.84  ? 349  TYR   D CA  1 
ATOM   10721 C  C   . TYR   D 1 280 ? 36.500  -51.482 8.474   1.00 91.55  ? 349  TYR   D C   1 
ATOM   10722 O  O   . TYR   D 1 280 ? 35.742  -50.620 8.920   1.00 90.66  ? 349  TYR   D O   1 
ATOM   10723 C  CB  . TYR   D 1 280 ? 38.962  -51.048 8.165   1.00 93.80  ? 349  TYR   D CB  1 
ATOM   10724 C  CG  . TYR   D 1 280 ? 40.126  -50.573 7.311   1.00 90.00  ? 349  TYR   D CG  1 
ATOM   10725 C  CD1 . TYR   D 1 280 ? 40.223  -49.243 6.915   1.00 95.49  ? 349  TYR   D CD1 1 
ATOM   10726 C  CD2 . TYR   D 1 280 ? 41.143  -51.438 6.936   1.00 89.84  ? 349  TYR   D CD2 1 
ATOM   10727 C  CE1 . TYR   D 1 280 ? 41.294  -48.782 6.134   1.00 96.53  ? 349  TYR   D CE1 1 
ATOM   10728 C  CE2 . TYR   D 1 280 ? 42.214  -50.998 6.168   1.00 94.69  ? 349  TYR   D CE2 1 
ATOM   10729 C  CZ  . TYR   D 1 280 ? 42.286  -49.667 5.764   1.00 99.51  ? 349  TYR   D CZ  1 
ATOM   10730 O  OH  . TYR   D 1 280 ? 43.341  -49.210 4.985   1.00 107.46 ? 349  TYR   D OH  1 
ATOM   10731 N  N   . VAL   D 1 281 ? 36.422  -52.764 8.843   1.00 91.02  ? 350  VAL   D N   1 
ATOM   10732 C  CA  . VAL   D 1 281 ? 35.387  -53.250 9.761   1.00 93.48  ? 350  VAL   D CA  1 
ATOM   10733 C  C   . VAL   D 1 281 ? 36.035  -53.786 11.037  1.00 100.58 ? 350  VAL   D C   1 
ATOM   10734 O  O   . VAL   D 1 281 ? 36.887  -54.684 10.989  1.00 101.41 ? 350  VAL   D O   1 
ATOM   10735 C  CB  . VAL   D 1 281 ? 34.511  -54.332 9.111   1.00 91.17  ? 350  VAL   D CB  1 
ATOM   10736 C  CG1 . VAL   D 1 281 ? 33.247  -54.551 9.933   1.00 90.15  ? 350  VAL   D CG1 1 
ATOM   10737 C  CG2 . VAL   D 1 281 ? 34.170  -53.945 7.718   1.00 94.24  ? 350  VAL   D CG2 1 
ATOM   10738 N  N   . ASN   D 1 282 ? 35.594  -53.246 12.183  1.00 98.78  ? 351  ASN   D N   1 
ATOM   10739 C  CA  . ASN   D 1 282 ? 36.042  -53.680 13.497  1.00 98.92  ? 351  ASN   D CA  1 
ATOM   10740 C  C   . ASN   D 1 282 ? 35.323  -54.967 13.884  1.00 104.29 ? 351  ASN   D C   1 
ATOM   10741 O  O   . ASN   D 1 282 ? 34.300  -55.313 13.290  1.00 103.63 ? 351  ASN   D O   1 
ATOM   10742 C  CB  . ASN   D 1 282 ? 35.777  -52.572 14.524  1.00 98.93  ? 351  ASN   D CB  1 
ATOM   10743 C  CG  . ASN   D 1 282 ? 34.431  -52.708 15.254  1.00 98.96  ? 351  ASN   D CG  1 
ATOM   10744 O  OD1 . ASN   D 1 282 ? 33.476  -53.293 14.752  1.00 102.22 ? 351  ASN   D OD1 1 
ATOM   10745 N  ND2 . ASN   D 1 282 ? 34.348  -52.104 16.430  1.00 94.34  ? 351  ASN   D ND2 1 
ATOM   10746 N  N   . PRO   D 1 283 ? 35.813  -55.678 14.913  1.00 107.42 ? 352  PRO   D N   1 
ATOM   10747 C  CA  . PRO   D 1 283 ? 35.248  -57.003 15.192  1.00 103.40 ? 352  PRO   D CA  1 
ATOM   10748 C  C   . PRO   D 1 283 ? 33.796  -56.989 15.635  1.00 99.89  ? 352  PRO   D C   1 
ATOM   10749 O  O   . PRO   D 1 283 ? 33.239  -58.057 15.874  1.00 105.91 ? 352  PRO   D O   1 
ATOM   10750 C  CB  . PRO   D 1 283 ? 36.233  -57.585 16.211  1.00 102.22 ? 352  PRO   D CB  1 
ATOM   10751 C  CG  . PRO   D 1 283 ? 36.814  -56.425 16.861  1.00 105.17 ? 352  PRO   D CG  1 
ATOM   10752 C  CD  . PRO   D 1 283 ? 36.932  -55.376 15.820  1.00 106.64 ? 352  PRO   D CD  1 
ATOM   10753 N  N   . HIS   D 1 284 ? 33.168  -55.826 15.754  1.00 98.00  ? 353  HIS   D N   1 
ATOM   10754 C  CA  . HIS   D 1 284 ? 31.767  -55.745 16.132  1.00 97.40  ? 353  HIS   D CA  1 
ATOM   10755 C  C   . HIS   D 1 284 ? 30.821  -55.257 15.052  1.00 96.00  ? 353  HIS   D C   1 
ATOM   10756 O  O   . HIS   D 1 284 ? 29.628  -55.080 15.328  1.00 93.28  ? 353  HIS   D O   1 
ATOM   10757 C  CB  . HIS   D 1 284 ? 31.667  -54.801 17.340  1.00 103.70 ? 353  HIS   D CB  1 
ATOM   10758 C  CG  . HIS   D 1 284 ? 32.144  -55.380 18.642  1.00 105.41 ? 353  HIS   D CG  1 
ATOM   10759 N  ND1 . HIS   D 1 284 ? 31.314  -56.079 19.495  1.00 104.87 ? 353  HIS   D ND1 1 
ATOM   10760 C  CD2 . HIS   D 1 284 ? 33.342  -55.292 19.273  1.00 104.51 ? 353  HIS   D CD2 1 
ATOM   10761 C  CE1 . HIS   D 1 284 ? 31.993  -56.433 20.572  1.00 109.60 ? 353  HIS   D CE1 1 
ATOM   10762 N  NE2 . HIS   D 1 284 ? 33.225  -55.966 20.464  1.00 107.83 ? 353  HIS   D NE2 1 
ATOM   10763 N  N   . GLY   D 1 285 ? 31.318  -54.988 13.834  1.00 96.56  ? 354  GLY   D N   1 
ATOM   10764 C  CA  . GLY   D 1 285 ? 30.508  -54.525 12.716  1.00 97.91  ? 354  GLY   D CA  1 
ATOM   10765 C  C   . GLY   D 1 285 ? 30.714  -53.058 12.342  1.00 96.09  ? 354  GLY   D C   1 
ATOM   10766 O  O   . GLY   D 1 285 ? 30.435  -52.684 11.186  1.00 94.17  ? 354  GLY   D O   1 
ATOM   10767 N  N   . TYR   D 1 286 ? 31.146  -52.235 13.270  1.00 92.57  ? 355  TYR   D N   1 
ATOM   10768 C  CA  . TYR   D 1 286 ? 31.392  -50.831 12.975  1.00 93.16  ? 355  TYR   D CA  1 
ATOM   10769 C  C   . TYR   D 1 286 ? 32.388  -50.701 11.819  1.00 91.54  ? 355  TYR   D C   1 
ATOM   10770 O  O   . TYR   D 1 286 ? 33.456  -51.315 11.842  1.00 93.60  ? 355  TYR   D O   1 
ATOM   10771 C  CB  . TYR   D 1 286 ? 31.905  -50.135 14.254  1.00 92.32  ? 355  TYR   D CB  1 
ATOM   10772 C  CG  . TYR   D 1 286 ? 30.882  -50.165 15.373  1.00 90.48  ? 355  TYR   D CG  1 
ATOM   10773 C  CD1 . TYR   D 1 286 ? 30.772  -51.274 16.193  1.00 94.98  ? 355  TYR   D CD1 1 
ATOM   10774 C  CD2 . TYR   D 1 286 ? 29.999  -49.108 15.579  1.00 88.76  ? 355  TYR   D CD2 1 
ATOM   10775 C  CE1 . TYR   D 1 286 ? 29.821  -51.337 17.202  1.00 98.18  ? 355  TYR   D CE1 1 
ATOM   10776 C  CE2 . TYR   D 1 286 ? 29.041  -49.157 16.593  1.00 91.41  ? 355  TYR   D CE2 1 
ATOM   10777 C  CZ  . TYR   D 1 286 ? 28.962  -50.276 17.399  1.00 98.49  ? 355  TYR   D CZ  1 
ATOM   10778 O  OH  . TYR   D 1 286 ? 28.024  -50.336 18.403  1.00 110.34 ? 355  TYR   D OH  1 
ATOM   10779 N  N   . VAL   D 1 287 ? 32.038  -49.922 10.800  1.00 86.74  ? 356  VAL   D N   1 
ATOM   10780 C  CA  . VAL   D 1 287 ? 32.941  -49.670 9.682   1.00 86.13  ? 356  VAL   D CA  1 
ATOM   10781 C  C   . VAL   D 1 287 ? 33.568  -48.294 9.843   1.00 85.94  ? 356  VAL   D C   1 
ATOM   10782 O  O   . VAL   D 1 287 ? 32.849  -47.301 10.021  1.00 86.12  ? 356  VAL   D O   1 
ATOM   10783 C  CB  . VAL   D 1 287 ? 32.200  -49.780 8.346   1.00 93.12  ? 356  VAL   D CB  1 
ATOM   10784 C  CG1 . VAL   D 1 287 ? 33.188  -49.734 7.152   1.00 92.73  ? 356  VAL   D CG1 1 
ATOM   10785 C  CG2 . VAL   D 1 287 ? 31.377  -51.041 8.353   1.00 97.70  ? 356  VAL   D CG2 1 
ATOM   10786 N  N   . HIS   D 1 288 ? 34.903  -48.233 9.762   1.00 85.52  ? 357  HIS   D N   1 
ATOM   10787 C  CA  . HIS   D 1 288 ? 35.670  -47.000 9.971   1.00 85.16  ? 357  HIS   D CA  1 
ATOM   10788 C  C   . HIS   D 1 288 ? 36.433  -46.627 8.711   1.00 89.01  ? 357  HIS   D C   1 
ATOM   10789 O  O   . HIS   D 1 288 ? 37.517  -47.169 8.471   1.00 89.07  ? 357  HIS   D O   1 
ATOM   10790 C  CB  . HIS   D 1 288 ? 36.672  -47.146 11.102  1.00 86.17  ? 357  HIS   D CB  1 
ATOM   10791 C  CG  . HIS   D 1 288 ? 36.071  -47.218 12.472  1.00 86.23  ? 357  HIS   D CG  1 
ATOM   10792 N  ND1 . HIS   D 1 288 ? 36.067  -46.142 13.336  1.00 86.25  ? 357  HIS   D ND1 1 
ATOM   10793 C  CD2 . HIS   D 1 288 ? 35.506  -48.250 13.143  1.00 86.88  ? 357  HIS   D CD2 1 
ATOM   10794 C  CE1 . HIS   D 1 288 ? 35.501  -46.506 14.472  1.00 91.57  ? 357  HIS   D CE1 1 
ATOM   10795 N  NE2 . HIS   D 1 288 ? 35.153  -47.780 14.378  1.00 87.28  ? 357  HIS   D NE2 1 
ATOM   10796 N  N   . GLU   D 1 289 ? 35.917  -45.672 7.934   1.00 95.79  ? 358  GLU   D N   1 
ATOM   10797 C  CA  . GLU   D 1 289 ? 36.774  -45.078 6.917   1.00 95.60  ? 358  GLU   D CA  1 
ATOM   10798 C  C   . GLU   D 1 289 ? 37.906  -44.497 7.748   1.00 97.02  ? 358  GLU   D C   1 
ATOM   10799 O  O   . GLU   D 1 289 ? 37.676  -43.572 8.533   1.00 99.52  ? 358  GLU   D O   1 
ATOM   10800 C  CB  . GLU   D 1 289 ? 36.058  -44.023 6.066   1.00 95.05  ? 358  GLU   D CB  1 
ATOM   10801 C  CG  . GLU   D 1 289 ? 34.765  -44.433 5.430   1.00 95.57  ? 358  GLU   D CG  1 
ATOM   10802 C  CD  . GLU   D 1 289 ? 33.606  -43.639 5.989   1.00 99.00  ? 358  GLU   D CD  1 
ATOM   10803 O  OE1 . GLU   D 1 289 ? 33.449  -43.639 7.244   1.00 100.33 ? 358  GLU   D OE1 1 
ATOM   10804 O  OE2 . GLU   D 1 289 ? 32.872  -43.003 5.179   1.00 98.18  ? 358  GLU   D OE2 1 
ATOM   10805 N  N   . THR   D 1 290 ? 39.119  -45.041 7.620   1.00 88.71  ? 359  THR   D N   1 
ATOM   10806 C  CA  . THR   D 1 290 ? 40.267  -44.582 8.408   1.00 88.33  ? 359  THR   D CA  1 
ATOM   10807 C  C   . THR   D 1 290 ? 41.305  -44.075 7.409   1.00 85.26  ? 359  THR   D C   1 
ATOM   10808 O  O   . THR   D 1 290 ? 42.036  -44.854 6.792   1.00 85.91  ? 359  THR   D O   1 
ATOM   10809 C  CB  . THR   D 1 290 ? 40.871  -45.635 9.330   1.00 88.68  ? 359  THR   D CB  1 
ATOM   10810 O  OG1 . THR   D 1 290 ? 41.343  -46.745 8.561   1.00 94.19  ? 359  THR   D OG1 1 
ATOM   10811 C  CG2 . THR   D 1 290 ? 39.847  -46.121 10.302  1.00 85.96  ? 359  THR   D CG2 1 
ATOM   10812 N  N   . LEU   D 1 291 ? 41.354  -42.756 7.273   1.00 84.06  ? 360  LEU   D N   1 
ATOM   10813 C  CA  . LEU   D 1 291 ? 42.452  -42.116 6.574   1.00 84.74  ? 360  LEU   D CA  1 
ATOM   10814 C  C   . LEU   D 1 291 ? 43.761  -42.430 7.293   1.00 84.33  ? 360  LEU   D C   1 
ATOM   10815 O  O   . LEU   D 1 291 ? 43.871  -42.254 8.506   1.00 85.39  ? 360  LEU   D O   1 
ATOM   10816 C  CB  . LEU   D 1 291 ? 42.197  -40.608 6.526   1.00 82.16  ? 360  LEU   D CB  1 
ATOM   10817 C  CG  . LEU   D 1 291 ? 43.216  -39.818 5.740   1.00 81.79  ? 360  LEU   D CG  1 
ATOM   10818 C  CD1 . LEU   D 1 291 ? 43.039  -40.133 4.292   1.00 83.37  ? 360  LEU   D CD1 1 
ATOM   10819 C  CD2 . LEU   D 1 291 ? 43.055  -38.341 6.002   1.00 85.08  ? 360  LEU   D CD2 1 
ATOM   10820 N  N   . THR   D 1 292 ? 44.735  -42.946 6.554   1.00 88.54  ? 361  THR   D N   1 
ATOM   10821 C  CA  . THR   D 1 292 ? 46.064  -43.206 7.093   1.00 87.63  ? 361  THR   D CA  1 
ATOM   10822 C  C   . THR   D 1 292 ? 46.941  -41.971 6.862   1.00 87.67  ? 361  THR   D C   1 
ATOM   10823 O  O   . THR   D 1 292 ? 47.126  -41.534 5.724   1.00 88.89  ? 361  THR   D O   1 
ATOM   10824 C  CB  . THR   D 1 292 ? 46.666  -44.478 6.468   1.00 88.97  ? 361  THR   D CB  1 
ATOM   10825 O  OG1 . THR   D 1 292 ? 46.443  -44.512 5.053   1.00 90.69  ? 361  THR   D OG1 1 
ATOM   10826 C  CG2 . THR   D 1 292 ? 46.036  -45.723 7.049   1.00 89.48  ? 361  THR   D CG2 1 
ATOM   10827 N  N   . VAL   D 1 293 ? 47.437  -41.367 7.948   1.00 90.70  ? 362  VAL   D N   1 
ATOM   10828 C  CA  . VAL   D 1 293 ? 48.366  -40.241 7.866   1.00 92.20  ? 362  VAL   D CA  1 
ATOM   10829 C  C   . VAL   D 1 293 ? 49.699  -40.649 8.492   1.00 92.34  ? 362  VAL   D C   1 
ATOM   10830 O  O   . VAL   D 1 293 ? 49.779  -41.574 9.305   1.00 93.40  ? 362  VAL   D O   1 
ATOM   10831 C  CB  . VAL   D 1 293 ? 47.828  -38.941 8.529   1.00 90.48  ? 362  VAL   D CB  1 
ATOM   10832 C  CG1 . VAL   D 1 293 ? 46.479  -38.584 7.964   1.00 91.87  ? 362  VAL   D CG1 1 
ATOM   10833 C  CG2 . VAL   D 1 293 ? 47.755  -39.046 10.031  1.00 89.75  ? 362  VAL   D CG2 1 
ATOM   10834 N  N   . TYR   D 1 294 ? 50.756  -39.926 8.103   1.00 91.82  ? 363  TYR   D N   1 
ATOM   10835 C  CA  . TYR   D 1 294 ? 52.116  -40.252 8.536   1.00 94.52  ? 363  TYR   D CA  1 
ATOM   10836 C  C   . TYR   D 1 294 ? 52.408  -39.759 9.949   1.00 93.93  ? 363  TYR   D C   1 
ATOM   10837 O  O   . TYR   D 1 294 ? 53.025  -40.472 10.756  1.00 90.27  ? 363  TYR   D O   1 
ATOM   10838 C  CB  . TYR   D 1 294 ? 53.133  -39.656 7.552   1.00 97.99  ? 363  TYR   D CB  1 
ATOM   10839 C  CG  . TYR   D 1 294 ? 53.579  -40.617 6.468   1.00 94.68  ? 363  TYR   D CG  1 
ATOM   10840 C  CD1 . TYR   D 1 294 ? 53.993  -41.943 6.804   1.00 97.13  ? 363  TYR   D CD1 1 
ATOM   10841 C  CD2 . TYR   D 1 294 ? 53.534  -40.231 5.116   1.00 93.49  ? 363  TYR   D CD2 1 
ATOM   10842 C  CE1 . TYR   D 1 294 ? 54.368  -42.832 5.835   1.00 98.22  ? 363  TYR   D CE1 1 
ATOM   10843 C  CE2 . TYR   D 1 294 ? 53.891  -41.110 4.126   1.00 97.13  ? 363  TYR   D CE2 1 
ATOM   10844 C  CZ  . TYR   D 1 294 ? 54.334  -42.404 4.498   1.00 98.84  ? 363  TYR   D CZ  1 
ATOM   10845 O  OH  . TYR   D 1 294 ? 54.707  -43.315 3.539   1.00 104.99 ? 363  TYR   D OH  1 
ATOM   10846 N  N   . LYS   D 1 295 ? 52.002  -38.525 10.238  1.00 93.84  ? 364  LYS   D N   1 
ATOM   10847 C  CA  . LYS   D 1 295 ? 52.230  -37.891 11.526  1.00 95.49  ? 364  LYS   D CA  1 
ATOM   10848 C  C   . LYS   D 1 295 ? 50.943  -37.166 11.900  1.00 97.94  ? 364  LYS   D C   1 
ATOM   10849 O  O   . LYS   D 1 295 ? 50.501  -36.281 11.160  1.00 99.27  ? 364  LYS   D O   1 
ATOM   10850 C  CB  . LYS   D 1 295 ? 53.421  -36.916 11.447  1.00 93.63  ? 364  LYS   D CB  1 
ATOM   10851 N  N   . ALA   D 1 296 ? 50.319  -37.555 13.016  1.00 99.05  ? 365  ALA   D N   1 
ATOM   10852 C  CA  . ALA   D 1 296 ? 49.183  -36.831 13.575  1.00 99.17  ? 365  ALA   D CA  1 
ATOM   10853 C  C   . ALA   D 1 296 ? 49.588  -36.100 14.855  1.00 99.41  ? 365  ALA   D C   1 
ATOM   10854 O  O   . ALA   D 1 296 ? 50.572  -36.453 15.513  1.00 95.39  ? 365  ALA   D O   1 
ATOM   10855 C  CB  . ALA   D 1 296 ? 48.009  -37.775 13.848  1.00 94.85  ? 365  ALA   D CB  1 
ATOM   10856 N  N   . CYS   D 1 297 ? 48.825  -35.059 15.208  1.00 106.18 ? 366  CYS   D N   1 
ATOM   10857 C  CA  . CYS   D 1 297 ? 49.169  -34.183 16.328  1.00 106.32 ? 366  CYS   D CA  1 
ATOM   10858 C  C   . CYS   D 1 297 ? 47.943  -33.889 17.189  1.00 104.77 ? 366  CYS   D C   1 
ATOM   10859 O  O   . CYS   D 1 297 ? 46.803  -34.025 16.738  1.00 107.55 ? 366  CYS   D O   1 
ATOM   10860 C  CB  . CYS   D 1 297 ? 49.780  -32.871 15.839  1.00 105.26 ? 366  CYS   D CB  1 
ATOM   10861 S  SG  . CYS   D 1 297 ? 51.553  -33.034 15.573  1.00 127.19 ? 366  CYS   D SG  1 
ATOM   10862 N  N   . ASN   D 1 298 ? 48.189  -33.492 18.444  1.00 97.63  ? 367  ASN   D N   1 
ATOM   10863 C  CA  . ASN   D 1 298 ? 47.123  -33.163 19.390  1.00 99.30  ? 367  ASN   D CA  1 
ATOM   10864 C  C   . ASN   D 1 298 ? 46.275  -34.373 19.751  1.00 99.38  ? 367  ASN   D C   1 
ATOM   10865 O  O   . ASN   D 1 298 ? 45.080  -34.256 20.028  1.00 98.43  ? 367  ASN   D O   1 
ATOM   10866 C  CB  . ASN   D 1 298 ? 46.222  -32.054 18.858  1.00 97.86  ? 367  ASN   D CB  1 
ATOM   10867 C  CG  . ASN   D 1 298 ? 46.951  -30.803 18.675  1.00 101.45 ? 367  ASN   D CG  1 
ATOM   10868 O  OD1 . ASN   D 1 298 ? 47.765  -30.434 19.519  1.00 108.35 ? 367  ASN   D OD1 1 
ATOM   10869 N  ND2 . ASN   D 1 298 ? 46.695  -30.125 17.573  1.00 105.89 ? 367  ASN   D ND2 1 
ATOM   10870 N  N   . LEU   D 1 299 ? 46.855  -35.554 19.739  1.00 101.18 ? 368  LEU   D N   1 
ATOM   10871 C  CA  . LEU   D 1 299 ? 46.100  -36.737 20.101  1.00 99.42  ? 368  LEU   D CA  1 
ATOM   10872 C  C   . LEU   D 1 299 ? 46.665  -37.305 21.388  1.00 98.10  ? 368  LEU   D C   1 
ATOM   10873 O  O   . LEU   D 1 299 ? 47.877  -37.278 21.610  1.00 100.13 ? 368  LEU   D O   1 
ATOM   10874 C  CB  . LEU   D 1 299 ? 46.115  -37.774 18.973  1.00 96.95  ? 368  LEU   D CB  1 
ATOM   10875 C  CG  . LEU   D 1 299 ? 45.403  -37.230 17.724  1.00 99.01  ? 368  LEU   D CG  1 
ATOM   10876 C  CD1 . LEU   D 1 299 ? 45.352  -38.274 16.656  1.00 99.28  ? 368  LEU   D CD1 1 
ATOM   10877 C  CD2 . LEU   D 1 299 ? 43.999  -36.727 18.014  1.00 98.98  ? 368  LEU   D CD2 1 
ATOM   10878 N  N   . ASN   D 1 300 ? 45.781  -37.768 22.253  1.00 95.27  ? 369  ASN   D N   1 
ATOM   10879 C  CA  . ASN   D 1 300 ? 46.182  -38.474 23.450  1.00 95.38  ? 369  ASN   D CA  1 
ATOM   10880 C  C   . ASN   D 1 300 ? 45.862  -39.945 23.283  1.00 95.37  ? 369  ASN   D C   1 
ATOM   10881 O  O   . ASN   D 1 300 ? 44.749  -40.302 22.883  1.00 93.00  ? 369  ASN   D O   1 
ATOM   10882 C  CB  . ASN   D 1 300 ? 45.493  -37.903 24.676  1.00 97.75  ? 369  ASN   D CB  1 
ATOM   10883 C  CG  . ASN   D 1 300 ? 46.240  -36.742 25.231  1.00 99.23  ? 369  ASN   D CG  1 
ATOM   10884 O  OD1 . ASN   D 1 300 ? 47.344  -36.435 24.773  1.00 102.11 ? 369  ASN   D OD1 1 
ATOM   10885 N  ND2 . ASN   D 1 300 ? 45.662  -36.080 26.221  1.00 96.41  ? 369  ASN   D ND2 1 
ATOM   10886 N  N   . LEU   D 1 301 ? 46.851  -40.779 23.582  1.00 103.02 ? 370  LEU   D N   1 
ATOM   10887 C  CA  . LEU   D 1 301 ? 46.707  -42.226 23.496  1.00 105.33 ? 370  LEU   D CA  1 
ATOM   10888 C  C   . LEU   D 1 301 ? 46.006  -42.780 24.736  1.00 108.61 ? 370  LEU   D C   1 
ATOM   10889 O  O   . LEU   D 1 301 ? 46.318  -42.398 25.867  1.00 112.32 ? 370  LEU   D O   1 
ATOM   10890 C  CB  . LEU   D 1 301 ? 48.085  -42.878 23.343  1.00 103.99 ? 370  LEU   D CB  1 
ATOM   10891 C  CG  . LEU   D 1 301 ? 48.723  -42.868 21.953  1.00 103.52 ? 370  LEU   D CG  1 
ATOM   10892 C  CD1 . LEU   D 1 301 ? 47.760  -43.513 20.986  1.00 105.63 ? 370  LEU   D CD1 1 
ATOM   10893 C  CD2 . LEU   D 1 301 ? 49.094  -41.471 21.473  1.00 103.68 ? 370  LEU   D CD2 1 
ATOM   10894 N  N   . ILE   D 1 302 ? 45.060  -43.692 24.519  1.00 98.58  ? 371  ILE   D N   1 
ATOM   10895 C  CA  . ILE   D 1 302 ? 44.281  -44.323 25.581  1.00 94.70  ? 371  ILE   D CA  1 
ATOM   10896 C  C   . ILE   D 1 302 ? 44.639  -45.802 25.597  1.00 99.56  ? 371  ILE   D C   1 
ATOM   10897 O  O   . ILE   D 1 302 ? 44.319  -46.543 24.656  1.00 104.21 ? 371  ILE   D O   1 
ATOM   10898 C  CB  . ILE   D 1 302 ? 42.769  -44.116 25.382  1.00 91.89  ? 371  ILE   D CB  1 
ATOM   10899 C  CG1 . ILE   D 1 302 ? 42.363  -42.671 25.635  1.00 92.95  ? 371  ILE   D CG1 1 
ATOM   10900 C  CG2 . ILE   D 1 302 ? 41.986  -44.995 26.291  1.00 92.64  ? 371  ILE   D CG2 1 
ATOM   10901 C  CD1 . ILE   D 1 302 ? 42.807  -42.145 26.952  1.00 98.17  ? 371  ILE   D CD1 1 
ATOM   10902 N  N   . GLY   D 1 303 ? 45.329  -46.237 26.652  1.00 100.68 ? 372  GLY   D N   1 
ATOM   10903 C  CA  . GLY   D 1 303 ? 45.626  -47.657 26.863  1.00 101.33 ? 372  GLY   D CA  1 
ATOM   10904 C  C   . GLY   D 1 303 ? 47.019  -48.083 26.453  1.00 107.03 ? 372  GLY   D C   1 
ATOM   10905 O  O   . GLY   D 1 303 ? 47.972  -47.302 26.489  1.00 103.40 ? 372  GLY   D O   1 
ATOM   10906 N  N   . ARG   D 1 304 ? 47.162  -49.347 26.048  1.00 111.03 ? 373  ARG   D N   1 
ATOM   10907 C  CA  . ARG   D 1 304 ? 48.446  -49.873 25.615  1.00 108.42 ? 373  ARG   D CA  1 
ATOM   10908 C  C   . ARG   D 1 304 ? 48.292  -50.520 24.245  1.00 107.58 ? 373  ARG   D C   1 
ATOM   10909 O  O   . ARG   D 1 304 ? 47.202  -51.017 23.918  1.00 105.58 ? 373  ARG   D O   1 
ATOM   10910 C  CB  . ARG   D 1 304 ? 48.989  -50.867 26.634  1.00 108.36 ? 373  ARG   D CB  1 
ATOM   10911 N  N   . PRO   D 1 305 ? 49.368  -50.533 23.425  1.00 107.13 ? 374  PRO   D N   1 
ATOM   10912 C  CA  . PRO   D 1 305 ? 49.271  -51.085 22.066  1.00 105.71 ? 374  PRO   D CA  1 
ATOM   10913 C  C   . PRO   D 1 305 ? 48.718  -52.501 22.064  1.00 108.75 ? 374  PRO   D C   1 
ATOM   10914 O  O   . PRO   D 1 305 ? 48.983  -53.289 22.962  1.00 112.40 ? 374  PRO   D O   1 
ATOM   10915 C  CB  . PRO   D 1 305 ? 50.688  -51.020 21.554  1.00 105.00 ? 374  PRO   D CB  1 
ATOM   10916 C  CG  . PRO   D 1 305 ? 51.304  -49.878 22.288  1.00 106.41 ? 374  PRO   D CG  1 
ATOM   10917 C  CD  . PRO   D 1 305 ? 50.676  -49.940 23.666  1.00 109.01 ? 374  PRO   D CD  1 
ATOM   10918 N  N   . SER   D 1 306 ? 47.941  -52.833 21.015  1.00 102.87 ? 375  SER   D N   1 
ATOM   10919 C  CA  . SER   D 1 306 ? 47.304  -54.145 20.884  1.00 106.02 ? 375  SER   D CA  1 
ATOM   10920 C  C   . SER   D 1 306 ? 47.300  -54.542 19.405  1.00 109.88 ? 375  SER   D C   1 
ATOM   10921 O  O   . SER   D 1 306 ? 47.424  -53.698 18.508  1.00 109.73 ? 375  SER   D O   1 
ATOM   10922 C  CB  . SER   D 1 306 ? 45.876  -54.100 21.464  1.00 103.01 ? 375  SER   D CB  1 
ATOM   10923 O  OG  . SER   D 1 306 ? 45.128  -55.278 21.191  1.00 107.10 ? 375  SER   D OG  1 
ATOM   10924 N  N   . THR   D 1 307 ? 47.170  -55.847 19.146  1.00 111.86 ? 376  THR   D N   1 
ATOM   10925 C  CA  . THR   D 1 307 ? 47.116  -56.346 17.778  1.00 107.80 ? 376  THR   D CA  1 
ATOM   10926 C  C   . THR   D 1 307 ? 45.917  -57.251 17.518  1.00 112.65 ? 376  THR   D C   1 
ATOM   10927 O  O   . THR   D 1 307 ? 45.877  -57.908 16.479  1.00 116.75 ? 376  THR   D O   1 
ATOM   10928 C  CB  . THR   D 1 307 ? 48.405  -57.086 17.421  1.00 104.95 ? 376  THR   D CB  1 
ATOM   10929 O  OG1 . THR   D 1 307 ? 48.717  -58.005 18.469  1.00 105.86 ? 376  THR   D OG1 1 
ATOM   10930 C  CG2 . THR   D 1 307 ? 49.543  -56.106 17.258  1.00 104.98 ? 376  THR   D CG2 1 
ATOM   10931 N  N   . GLU   D 1 308 ? 44.948  -57.319 18.426  1.00 123.53 ? 377  GLU   D N   1 
ATOM   10932 C  CA  . GLU   D 1 308 ? 43.703  -58.017 18.128  1.00 125.92 ? 377  GLU   D CA  1 
ATOM   10933 C  C   . GLU   D 1 308 ? 43.006  -57.370 16.944  1.00 126.28 ? 377  GLU   D C   1 
ATOM   10934 O  O   . GLU   D 1 308 ? 42.677  -56.187 16.989  1.00 125.85 ? 377  GLU   D O   1 
ATOM   10935 C  CB  . GLU   D 1 308 ? 42.746  -57.963 19.308  1.00 128.43 ? 377  GLU   D CB  1 
ATOM   10936 C  CG  . GLU   D 1 308 ? 43.239  -58.508 20.606  1.00 131.23 ? 377  GLU   D CG  1 
ATOM   10937 C  CD  . GLU   D 1 308 ? 42.205  -58.244 21.684  1.00 135.60 ? 377  GLU   D CD  1 
ATOM   10938 O  OE1 . GLU   D 1 308 ? 41.693  -57.092 21.742  1.00 129.20 ? 377  GLU   D OE1 1 
ATOM   10939 O  OE2 . GLU   D 1 308 ? 41.871  -59.188 22.439  1.00 138.19 ? 377  GLU   D OE2 1 
ATOM   10940 N  N   . HIS   D 1 309 ? 42.750  -58.154 15.900  1.00 129.55 ? 378  HIS   D N   1 
ATOM   10941 C  CA  . HIS   D 1 309 ? 41.922  -57.694 14.784  1.00 131.10 ? 378  HIS   D CA  1 
ATOM   10942 C  C   . HIS   D 1 309 ? 42.475  -56.404 14.167  1.00 126.86 ? 378  HIS   D C   1 
ATOM   10943 O  O   . HIS   D 1 309 ? 41.729  -55.511 13.758  1.00 125.67 ? 378  HIS   D O   1 
ATOM   10944 C  CB  . HIS   D 1 309 ? 40.461  -57.510 15.239  1.00 132.04 ? 378  HIS   D CB  1 
ATOM   10945 C  CG  . HIS   D 1 309 ? 39.440  -57.620 14.136  1.00 135.16 ? 378  HIS   D CG  1 
ATOM   10946 N  ND1 . HIS   D 1 309 ? 38.669  -58.748 13.942  1.00 136.44 ? 378  HIS   D ND1 1 
ATOM   10947 C  CD2 . HIS   D 1 309 ? 39.046  -56.734 13.185  1.00 130.65 ? 378  HIS   D CD2 1 
ATOM   10948 C  CE1 . HIS   D 1 309 ? 37.853  -58.557 12.918  1.00 130.90 ? 378  HIS   D CE1 1 
ATOM   10949 N  NE2 . HIS   D 1 309 ? 38.062  -57.343 12.440  1.00 127.63 ? 378  HIS   D NE2 1 
ATOM   10950 N  N   . SER   D 1 310 ? 43.799  -56.288 14.118  1.00 115.15 ? 379  SER   D N   1 
ATOM   10951 C  CA  . SER   D 1 310 ? 44.411  -55.117 13.505  1.00 111.02 ? 379  SER   D CA  1 
ATOM   10952 C  C   . SER   D 1 310 ? 44.129  -55.098 12.003  1.00 111.15 ? 379  SER   D C   1 
ATOM   10953 O  O   . SER   D 1 310 ? 44.243  -56.125 11.316  1.00 108.73 ? 379  SER   D O   1 
ATOM   10954 C  CB  . SER   D 1 310 ? 45.916  -55.100 13.770  1.00 108.58 ? 379  SER   D CB  1 
ATOM   10955 O  OG  . SER   D 1 310 ? 46.510  -53.946 13.201  1.00 99.82  ? 379  SER   D OG  1 
ATOM   10956 N  N   . TRP   D 1 311 ? 43.750  -53.924 11.493  1.00 106.58 ? 380  TRP   D N   1 
ATOM   10957 C  CA  . TRP   D 1 311 ? 43.467  -53.800 10.072  1.00 101.62 ? 380  TRP   D CA  1 
ATOM   10958 C  C   . TRP   D 1 311 ? 44.730  -53.714 9.250   1.00 100.31 ? 380  TRP   D C   1 
ATOM   10959 O  O   . TRP   D 1 311 ? 44.691  -53.955 8.039   1.00 106.05 ? 380  TRP   D O   1 
ATOM   10960 C  CB  . TRP   D 1 311 ? 42.595  -52.582 9.813   1.00 98.00  ? 380  TRP   D CB  1 
ATOM   10961 C  CG  . TRP   D 1 311 ? 41.248  -52.712 10.440  1.00 99.85  ? 380  TRP   D CG  1 
ATOM   10962 C  CD1 . TRP   D 1 311 ? 40.505  -53.852 10.577  1.00 101.29 ? 380  TRP   D CD1 1 
ATOM   10963 C  CD2 . TRP   D 1 311 ? 40.488  -51.666 11.033  1.00 98.80  ? 380  TRP   D CD2 1 
ATOM   10964 N  NE1 . TRP   D 1 311 ? 39.319  -53.572 11.209  1.00 97.71  ? 380  TRP   D NE1 1 
ATOM   10965 C  CE2 . TRP   D 1 311 ? 39.284  -52.233 11.496  1.00 97.91  ? 380  TRP   D CE2 1 
ATOM   10966 C  CE3 . TRP   D 1 311 ? 40.703  -50.297 11.208  1.00 95.05  ? 380  TRP   D CE3 1 
ATOM   10967 C  CZ2 . TRP   D 1 311 ? 38.313  -51.481 12.131  1.00 96.52  ? 380  TRP   D CZ2 1 
ATOM   10968 C  CZ3 . TRP   D 1 311 ? 39.750  -49.563 11.831  1.00 92.79  ? 380  TRP   D CZ3 1 
ATOM   10969 C  CH2 . TRP   D 1 311 ? 38.566  -50.149 12.292  1.00 95.03  ? 380  TRP   D CH2 1 
ATOM   10970 N  N   . PHE   D 1 312 ? 45.848  -53.395 9.879   1.00 101.47 ? 381  PHE   D N   1 
ATOM   10971 C  CA  . PHE   D 1 312 ? 47.133  -53.354 9.197   1.00 104.22 ? 381  PHE   D CA  1 
ATOM   10972 C  C   . PHE   D 1 312 ? 48.028  -54.377 9.866   1.00 105.50 ? 381  PHE   D C   1 
ATOM   10973 O  O   . PHE   D 1 312 ? 48.633  -54.088 10.912  1.00 106.99 ? 381  PHE   D O   1 
ATOM   10974 C  CB  . PHE   D 1 312 ? 47.737  -51.953 9.263   1.00 99.69  ? 381  PHE   D CB  1 
ATOM   10975 C  CG  . PHE   D 1 312 ? 46.772  -50.896 8.875   1.00 95.16  ? 381  PHE   D CG  1 
ATOM   10976 C  CD1 . PHE   D 1 312 ? 46.526  -50.630 7.547   1.00 100.59 ? 381  PHE   D CD1 1 
ATOM   10977 C  CD2 . PHE   D 1 312 ? 46.064  -50.211 9.831   1.00 98.61  ? 381  PHE   D CD2 1 
ATOM   10978 C  CE1 . PHE   D 1 312 ? 45.630  -49.672 7.171   1.00 100.86 ? 381  PHE   D CE1 1 
ATOM   10979 C  CE2 . PHE   D 1 312 ? 45.157  -49.255 9.468   1.00 100.28 ? 381  PHE   D CE2 1 
ATOM   10980 C  CZ  . PHE   D 1 312 ? 44.938  -48.985 8.128   1.00 100.06 ? 381  PHE   D CZ  1 
ATOM   10981 N  N   . PRO   D 1 313 ? 48.090  -55.599 9.341   1.00 105.12 ? 382  PRO   D N   1 
ATOM   10982 C  CA  . PRO   D 1 313 ? 48.867  -56.654 9.997   1.00 106.19 ? 382  PRO   D CA  1 
ATOM   10983 C  C   . PRO   D 1 313 ? 50.320  -56.245 10.220  1.00 108.56 ? 382  PRO   D C   1 
ATOM   10984 O  O   . PRO   D 1 313 ? 50.921  -55.515 9.419   1.00 105.33 ? 382  PRO   D O   1 
ATOM   10985 C  CB  . PRO   D 1 313 ? 48.742  -57.831 9.023   1.00 106.35 ? 382  PRO   D CB  1 
ATOM   10986 C  CG  . PRO   D 1 313 ? 47.413  -57.620 8.374   1.00 109.92 ? 382  PRO   D CG  1 
ATOM   10987 C  CD  . PRO   D 1 313 ? 47.281  -56.119 8.224   1.00 106.91 ? 382  PRO   D CD  1 
ATOM   10988 N  N   . GLY   D 1 314 ? 50.878  -56.729 11.337  1.00 108.09 ? 383  GLY   D N   1 
ATOM   10989 C  CA  . GLY   D 1 314 ? 52.204  -56.348 11.774  1.00 110.26 ? 383  GLY   D CA  1 
ATOM   10990 C  C   . GLY   D 1 314 ? 52.272  -55.014 12.486  1.00 115.91 ? 383  GLY   D C   1 
ATOM   10991 O  O   . GLY   D 1 314 ? 53.346  -54.649 12.998  1.00 114.48 ? 383  GLY   D O   1 
ATOM   10992 N  N   . TYR   D 1 315 ? 51.165  -54.272 12.520  1.00 116.05 ? 384  TYR   D N   1 
ATOM   10993 C  CA  . TYR   D 1 315 ? 51.043  -53.013 13.236  1.00 112.05 ? 384  TYR   D CA  1 
ATOM   10994 C  C   . TYR   D 1 315 ? 50.156  -53.215 14.458  1.00 108.57 ? 384  TYR   D C   1 
ATOM   10995 O  O   . TYR   D 1 315 ? 49.331  -54.136 14.511  1.00 106.14 ? 384  TYR   D O   1 
ATOM   10996 C  CB  . TYR   D 1 315 ? 50.498  -51.901 12.316  1.00 105.13 ? 384  TYR   D CB  1 
ATOM   10997 C  CG  . TYR   D 1 315 ? 51.517  -51.442 11.296  1.00 101.50 ? 384  TYR   D CG  1 
ATOM   10998 C  CD1 . TYR   D 1 315 ? 52.476  -50.490 11.622  1.00 104.95 ? 384  TYR   D CD1 1 
ATOM   10999 C  CD2 . TYR   D 1 315 ? 51.547  -51.989 10.025  1.00 104.23 ? 384  TYR   D CD2 1 
ATOM   11000 C  CE1 . TYR   D 1 315 ? 53.422  -50.079 10.700  1.00 105.56 ? 384  TYR   D CE1 1 
ATOM   11001 C  CE2 . TYR   D 1 315 ? 52.493  -51.583 9.089   1.00 109.15 ? 384  TYR   D CE2 1 
ATOM   11002 C  CZ  . TYR   D 1 315 ? 53.428  -50.626 9.436   1.00 107.31 ? 384  TYR   D CZ  1 
ATOM   11003 O  OH  . TYR   D 1 315 ? 54.372  -50.206 8.525   1.00 109.25 ? 384  TYR   D OH  1 
ATOM   11004 N  N   . ALA   D 1 316 ? 50.378  -52.371 15.462  1.00 104.50 ? 385  ALA   D N   1 
ATOM   11005 C  CA  . ALA   D 1 316 ? 49.666  -52.437 16.724  1.00 102.00 ? 385  ALA   D CA  1 
ATOM   11006 C  C   . ALA   D 1 316 ? 48.962  -51.115 16.951  1.00 104.16 ? 385  ALA   D C   1 
ATOM   11007 O  O   . ALA   D 1 316 ? 49.587  -50.058 16.845  1.00 107.37 ? 385  ALA   D O   1 
ATOM   11008 C  CB  . ALA   D 1 316 ? 50.617  -52.725 17.876  1.00 106.95 ? 385  ALA   D CB  1 
ATOM   11009 N  N   . TRP   D 1 317 ? 47.678  -51.181 17.297  1.00 102.99 ? 386  TRP   D N   1 
ATOM   11010 C  CA  . TRP   D 1 317 ? 46.819  -50.008 17.409  1.00 103.73 ? 386  TRP   D CA  1 
ATOM   11011 C  C   . TRP   D 1 317 ? 46.626  -49.592 18.863  1.00 97.95  ? 386  TRP   D C   1 
ATOM   11012 O  O   . TRP   D 1 317 ? 46.185  -50.394 19.689  1.00 98.04  ? 386  TRP   D O   1 
ATOM   11013 C  CB  . TRP   D 1 317 ? 45.458  -50.298 16.788  1.00 102.22 ? 386  TRP   D CB  1 
ATOM   11014 C  CG  . TRP   D 1 317 ? 44.839  -51.520 17.339  1.00 96.82  ? 386  TRP   D CG  1 
ATOM   11015 C  CD1 . TRP   D 1 317 ? 45.029  -52.784 16.906  1.00 100.12 ? 386  TRP   D CD1 1 
ATOM   11016 C  CD2 . TRP   D 1 317 ? 43.936  -51.600 18.445  1.00 99.45  ? 386  TRP   D CD2 1 
ATOM   11017 N  NE1 . TRP   D 1 317 ? 44.294  -53.657 17.661  1.00 107.16 ? 386  TRP   D NE1 1 
ATOM   11018 C  CE2 . TRP   D 1 317 ? 43.610  -52.953 18.615  1.00 105.37 ? 386  TRP   D CE2 1 
ATOM   11019 C  CE3 . TRP   D 1 317 ? 43.359  -50.656 19.300  1.00 97.75  ? 386  TRP   D CE3 1 
ATOM   11020 C  CZ2 . TRP   D 1 317 ? 42.739  -53.396 19.609  1.00 109.70 ? 386  TRP   D CZ2 1 
ATOM   11021 C  CZ3 . TRP   D 1 317 ? 42.493  -51.097 20.290  1.00 99.44  ? 386  TRP   D CZ3 1 
ATOM   11022 C  CH2 . TRP   D 1 317 ? 42.190  -52.454 20.433  1.00 106.43 ? 386  TRP   D CH2 1 
ATOM   11023 N  N   . THR   D 1 318 ? 46.948  -48.340 19.170  1.00 95.72  ? 387  THR   D N   1 
ATOM   11024 C  CA  . THR   D 1 318 ? 46.556  -47.722 20.433  1.00 101.08 ? 387  THR   D CA  1 
ATOM   11025 C  C   . THR   D 1 318 ? 45.470  -46.697 20.118  1.00 95.66  ? 387  THR   D C   1 
ATOM   11026 O  O   . THR   D 1 318 ? 45.624  -45.915 19.177  1.00 95.04  ? 387  THR   D O   1 
ATOM   11027 C  CB  . THR   D 1 318 ? 47.748  -47.069 21.161  1.00 97.34  ? 387  THR   D CB  1 
ATOM   11028 O  OG1 . THR   D 1 318 ? 48.913  -47.900 21.088  1.00 98.24  ? 387  THR   D OG1 1 
ATOM   11029 C  CG2 . THR   D 1 318 ? 47.410  -46.911 22.614  1.00 97.66  ? 387  THR   D CG2 1 
ATOM   11030 N  N   . VAL   D 1 319 ? 44.356  -46.731 20.864  1.00 92.37  ? 388  VAL   D N   1 
ATOM   11031 C  CA  . VAL   D 1 319 ? 43.265  -45.793 20.601  1.00 89.78  ? 388  VAL   D CA  1 
ATOM   11032 C  C   . VAL   D 1 319 ? 43.754  -44.378 20.867  1.00 90.16  ? 388  VAL   D C   1 
ATOM   11033 O  O   . VAL   D 1 319 ? 44.516  -44.136 21.808  1.00 94.08  ? 388  VAL   D O   1 
ATOM   11034 C  CB  . VAL   D 1 319 ? 42.026  -46.123 21.452  1.00 90.25  ? 388  VAL   D CB  1 
ATOM   11035 C  CG1 . VAL   D 1 319 ? 40.975  -45.052 21.307  1.00 89.79  ? 388  VAL   D CG1 1 
ATOM   11036 C  CG2 . VAL   D 1 319 ? 41.426  -47.447 21.038  1.00 90.41  ? 388  VAL   D CG2 1 
ATOM   11037 N  N   . ALA   D 1 320 ? 43.340  -43.437 20.015  1.00 90.17  ? 389  ALA   D N   1 
ATOM   11038 C  CA  . ALA   D 1 320 ? 43.671  -42.030 20.184  1.00 90.14  ? 389  ALA   D CA  1 
ATOM   11039 C  C   . ALA   D 1 320 ? 42.397  -41.198 20.256  1.00 93.54  ? 389  ALA   D C   1 
ATOM   11040 O  O   . ALA   D 1 320 ? 41.326  -41.611 19.781  1.00 91.23  ? 389  ALA   D O   1 
ATOM   11041 C  CB  . ALA   D 1 320 ? 44.567  -41.500 19.057  1.00 87.89  ? 389  ALA   D CB  1 
ATOM   11042 N  N   . GLN   D 1 321 ? 42.534  -40.029 20.882  1.00 96.05  ? 390  GLN   D N   1 
ATOM   11043 C  CA  . GLN   D 1 321 ? 41.427  -39.129 21.129  1.00 91.67  ? 390  GLN   D CA  1 
ATOM   11044 C  C   . GLN   D 1 321 ? 41.974  -37.724 21.244  1.00 91.61  ? 390  GLN   D C   1 
ATOM   11045 O  O   . GLN   D 1 321 ? 43.170  -37.509 21.447  1.00 93.64  ? 390  GLN   D O   1 
ATOM   11046 C  CB  . GLN   D 1 321 ? 40.664  -39.490 22.405  1.00 92.16  ? 390  GLN   D CB  1 
ATOM   11047 C  CG  . GLN   D 1 321 ? 41.520  -39.503 23.672  1.00 93.35  ? 390  GLN   D CG  1 
ATOM   11048 C  CD  . GLN   D 1 321 ? 40.679  -39.505 24.948  1.00 95.61  ? 390  GLN   D CD  1 
ATOM   11049 O  OE1 . GLN   D 1 321 ? 39.498  -39.889 24.932  1.00 94.22  ? 390  GLN   D OE1 1 
ATOM   11050 N  NE2 . GLN   D 1 321 ? 41.282  -39.063 26.060  1.00 94.86  ? 390  GLN   D NE2 1 
ATOM   11051 N  N   . CYS   D 1 322 ? 41.061  -36.771 21.187  1.00 89.61  ? 391  CYS   D N   1 
ATOM   11052 C  CA  . CYS   D 1 322 ? 41.428  -35.370 21.151  1.00 87.50  ? 391  CYS   D CA  1 
ATOM   11053 C  C   . CYS   D 1 322 ? 42.084  -34.948 22.462  1.00 90.67  ? 391  CYS   D C   1 
ATOM   11054 O  O   . CYS   D 1 322 ? 41.607  -35.287 23.553  1.00 92.26  ? 391  CYS   D O   1 
ATOM   11055 C  CB  . CYS   D 1 322 ? 40.174  -34.562 20.869  1.00 87.61  ? 391  CYS   D CB  1 
ATOM   11056 S  SG  . CYS   D 1 322 ? 40.426  -32.806 20.890  1.00 86.23  ? 391  CYS   D SG  1 
ATOM   11057 N  N   . LYS   D 1 323 ? 43.207  -34.227 22.351  1.00 92.32  ? 392  LYS   D N   1 
ATOM   11058 C  CA  . LYS   D 1 323 ? 43.939  -33.700 23.495  1.00 88.21  ? 392  LYS   D CA  1 
ATOM   11059 C  C   . LYS   D 1 323 ? 43.082  -32.716 24.282  1.00 88.32  ? 392  LYS   D C   1 
ATOM   11060 O  O   . LYS   D 1 323 ? 43.515  -32.231 25.336  1.00 88.86  ? 392  LYS   D O   1 
ATOM   11061 C  CB  . LYS   D 1 323 ? 45.236  -33.032 23.033  1.00 87.99  ? 392  LYS   D CB  1 
ATOM   11062 N  N   . ILE   D 1 324 ? 41.858  -32.450 23.824  1.00 87.86  ? 393  ILE   D N   1 
ATOM   11063 C  CA  . ILE   D 1 324 ? 41.040  -31.386 24.395  1.00 87.86  ? 393  ILE   D CA  1 
ATOM   11064 C  C   . ILE   D 1 324 ? 39.651  -31.867 24.813  1.00 88.09  ? 393  ILE   D C   1 
ATOM   11065 O  O   . ILE   D 1 324 ? 39.319  -31.874 26.008  1.00 89.66  ? 393  ILE   D O   1 
ATOM   11066 C  CB  . ILE   D 1 324 ? 40.922  -30.227 23.400  1.00 87.03  ? 393  ILE   D CB  1 
ATOM   11067 C  CG1 . ILE   D 1 324 ? 42.313  -29.717 23.003  1.00 87.24  ? 393  ILE   D CG1 1 
ATOM   11068 C  CG2 . ILE   D 1 324 ? 40.028  -29.144 23.997  1.00 87.05  ? 393  ILE   D CG2 1 
ATOM   11069 C  CD1 . ILE   D 1 324 ? 43.007  -28.968 24.117  1.00 87.72  ? 393  ILE   D CD1 1 
ATOM   11070 N  N   . CYS   D 1 325 ? 38.808  -32.206 23.842  1.00 87.57  ? 394  CYS   D N   1 
ATOM   11071 C  CA  . CYS   D 1 325 ? 37.455  -32.674 24.121  1.00 87.78  ? 394  CYS   D CA  1 
ATOM   11072 C  C   . CYS   D 1 325 ? 37.409  -34.177 24.382  1.00 88.30  ? 394  CYS   D C   1 
ATOM   11073 O  O   . CYS   D 1 325 ? 36.350  -34.713 24.739  1.00 88.62  ? 394  CYS   D O   1 
ATOM   11074 C  CB  . CYS   D 1 325 ? 36.544  -32.316 22.952  1.00 89.19  ? 394  CYS   D CB  1 
ATOM   11075 S  SG  . CYS   D 1 325 ? 37.112  -33.096 21.432  1.00 86.40  ? 394  CYS   D SG  1 
ATOM   11076 N  N   . ALA   D 1 326 ? 38.545  -34.854 24.199  1.00 88.41  ? 395  ALA   D N   1 
ATOM   11077 C  CA  . ALA   D 1 326 ? 38.695  -36.297 24.433  1.00 88.93  ? 395  ALA   D CA  1 
ATOM   11078 C  C   . ALA   D 1 326 ? 37.688  -37.110 23.628  1.00 91.81  ? 395  ALA   D C   1 
ATOM   11079 O  O   . ALA   D 1 326 ? 37.136  -38.106 24.097  1.00 93.83  ? 395  ALA   D O   1 
ATOM   11080 C  CB  . ALA   D 1 326 ? 38.621  -36.633 25.911  1.00 89.87  ? 395  ALA   D CB  1 
ATOM   11081 N  N   . SER   D 1 327 ? 37.482  -36.681 22.384  1.00 90.11  ? 396  SER   D N   1 
ATOM   11082 C  CA  . SER   D 1 327 ? 36.662  -37.412 21.445  1.00 92.63  ? 396  SER   D CA  1 
ATOM   11083 C  C   . SER   D 1 327 ? 37.540  -38.360 20.656  1.00 93.71  ? 396  SER   D C   1 
ATOM   11084 O  O   . SER   D 1 327 ? 38.680  -38.040 20.313  1.00 91.39  ? 396  SER   D O   1 
ATOM   11085 C  CB  . SER   D 1 327 ? 35.921  -36.460 20.519  1.00 95.25  ? 396  SER   D CB  1 
ATOM   11086 O  OG  . SER   D 1 327 ? 34.853  -35.887 21.246  1.00 96.62  ? 396  SER   D OG  1 
ATOM   11087 N  N   . HIS   D 1 328 ? 37.013  -39.537 20.404  1.00 95.67  ? 397  HIS   D N   1 
ATOM   11088 C  CA  . HIS   D 1 328 ? 37.781  -40.524 19.687  1.00 93.25  ? 397  HIS   D CA  1 
ATOM   11089 C  C   . HIS   D 1 328 ? 38.083  -40.007 18.300  1.00 93.15  ? 397  HIS   D C   1 
ATOM   11090 O  O   . HIS   D 1 328 ? 37.173  -39.620 17.567  1.00 101.48 ? 397  HIS   D O   1 
ATOM   11091 C  CB  . HIS   D 1 328 ? 36.989  -41.809 19.634  1.00 96.15  ? 397  HIS   D CB  1 
ATOM   11092 C  CG  . HIS   D 1 328 ? 37.607  -42.843 18.772  1.00 94.55  ? 397  HIS   D CG  1 
ATOM   11093 N  ND1 . HIS   D 1 328 ? 37.072  -43.205 17.559  1.00 96.61  ? 397  HIS   D ND1 1 
ATOM   11094 C  CD2 . HIS   D 1 328 ? 38.739  -43.569 18.925  1.00 91.33  ? 397  HIS   D CD2 1 
ATOM   11095 C  CE1 . HIS   D 1 328 ? 37.837  -44.133 17.012  1.00 94.66  ? 397  HIS   D CE1 1 
ATOM   11096 N  NE2 . HIS   D 1 328 ? 38.856  -44.370 17.819  1.00 90.17  ? 397  HIS   D NE2 1 
ATOM   11097 N  N   . ILE   D 1 329 ? 39.362  -39.944 17.953  1.00 90.98  ? 398  ILE   D N   1 
ATOM   11098 C  CA  . ILE   D 1 329 ? 39.777  -39.569 16.607  1.00 91.05  ? 398  ILE   D CA  1 
ATOM   11099 C  C   . ILE   D 1 329 ? 40.177  -40.795 15.788  1.00 88.14  ? 398  ILE   D C   1 
ATOM   11100 O  O   . ILE   D 1 329 ? 39.767  -40.948 14.638  1.00 87.83  ? 398  ILE   D O   1 
ATOM   11101 C  CB  . ILE   D 1 329 ? 40.910  -38.521 16.681  1.00 85.73  ? 398  ILE   D CB  1 
ATOM   11102 C  CG1 . ILE   D 1 329 ? 40.387  -37.261 17.346  1.00 91.00  ? 398  ILE   D CG1 1 
ATOM   11103 C  CG2 . ILE   D 1 329 ? 41.427  -38.139 15.324  1.00 84.92  ? 398  ILE   D CG2 1 
ATOM   11104 C  CD1 . ILE   D 1 329 ? 39.129  -36.711 16.693  1.00 92.31  ? 398  ILE   D CD1 1 
ATOM   11105 N  N   . GLY   D 1 330 ? 40.939  -41.703 16.371  1.00 89.69  ? 399  GLY   D N   1 
ATOM   11106 C  CA  . GLY   D 1 330 ? 41.356  -42.892 15.666  1.00 88.05  ? 399  GLY   D CA  1 
ATOM   11107 C  C   . GLY   D 1 330 ? 42.268  -43.783 16.487  1.00 89.05  ? 399  GLY   D C   1 
ATOM   11108 O  O   . GLY   D 1 330 ? 41.946  -44.109 17.639  1.00 88.74  ? 399  GLY   D O   1 
ATOM   11109 N  N   . TRP   D 1 331 ? 43.417  -44.153 15.903  1.00 88.50  ? 400  TRP   D N   1 
ATOM   11110 C  CA  . TRP   D 1 331 ? 44.379  -45.097 16.472  1.00 89.76  ? 400  TRP   D CA  1 
ATOM   11111 C  C   . TRP   D 1 331 ? 45.793  -44.727 16.035  1.00 89.51  ? 400  TRP   D C   1 
ATOM   11112 O  O   . TRP   D 1 331 ? 46.005  -44.301 14.899  1.00 98.41  ? 400  TRP   D O   1 
ATOM   11113 C  CB  . TRP   D 1 331 ? 44.081  -46.534 16.015  1.00 93.65  ? 400  TRP   D CB  1 
ATOM   11114 C  CG  . TRP   D 1 331 ? 42.684  -47.004 16.293  1.00 89.68  ? 400  TRP   D CG  1 
ATOM   11115 C  CD1 . TRP   D 1 331 ? 42.269  -47.737 17.357  1.00 88.67  ? 400  TRP   D CD1 1 
ATOM   11116 C  CD2 . TRP   D 1 331 ? 41.529  -46.772 15.488  1.00 87.45  ? 400  TRP   D CD2 1 
ATOM   11117 N  NE1 . TRP   D 1 331 ? 40.927  -47.973 17.271  1.00 88.69  ? 400  TRP   D NE1 1 
ATOM   11118 C  CE2 . TRP   D 1 331 ? 40.449  -47.390 16.130  1.00 87.90  ? 400  TRP   D CE2 1 
ATOM   11119 C  CE3 . TRP   D 1 331 ? 41.306  -46.103 14.286  1.00 86.70  ? 400  TRP   D CE3 1 
ATOM   11120 C  CZ2 . TRP   D 1 331 ? 39.166  -47.364 15.614  1.00 92.37  ? 400  TRP   D CZ2 1 
ATOM   11121 C  CZ3 . TRP   D 1 331 ? 40.028  -46.070 13.775  1.00 86.97  ? 400  TRP   D CZ3 1 
ATOM   11122 C  CH2 . TRP   D 1 331 ? 38.974  -46.698 14.434  1.00 89.49  ? 400  TRP   D CH2 1 
ATOM   11123 N  N   . LYS   D 1 332 ? 46.767  -44.930 16.915  1.00 88.06  ? 401  LYS   D N   1 
ATOM   11124 C  CA  . LYS   D 1 332 ? 48.169  -44.820 16.533  1.00 91.12  ? 401  LYS   D CA  1 
ATOM   11125 C  C   . LYS   D 1 332 ? 48.736  -46.222 16.335  1.00 98.65  ? 401  LYS   D C   1 
ATOM   11126 O  O   . LYS   D 1 332 ? 48.672  -47.066 17.242  1.00 97.81  ? 401  LYS   D O   1 
ATOM   11127 C  CB  . LYS   D 1 332 ? 48.973  -44.045 17.572  1.00 94.59  ? 401  LYS   D CB  1 
ATOM   11128 C  CG  . LYS   D 1 332 ? 50.414  -43.747 17.188  1.00 93.65  ? 401  LYS   D CG  1 
ATOM   11129 C  CD  . LYS   D 1 332 ? 51.179  -43.285 18.431  1.00 94.73  ? 401  LYS   D CD  1 
ATOM   11130 C  CE  . LYS   D 1 332 ? 52.668  -43.086 18.183  1.00 91.79  ? 401  LYS   D CE  1 
ATOM   11131 N  NZ  . LYS   D 1 332 ? 53.283  -42.140 19.170  1.00 100.71 ? 401  LYS   D NZ  1 
ATOM   11132 N  N   . PHE   D 1 333 ? 49.288  -46.464 15.148  1.00 100.61 ? 402  PHE   D N   1 
ATOM   11133 C  CA  . PHE   D 1 333 ? 49.704  -47.792 14.734  1.00 101.55 ? 402  PHE   D CA  1 
ATOM   11134 C  C   . PHE   D 1 333 ? 51.220  -47.928 14.789  1.00 105.07 ? 402  PHE   D C   1 
ATOM   11135 O  O   . PHE   D 1 333 ? 51.944  -47.231 14.068  1.00 101.97 ? 402  PHE   D O   1 
ATOM   11136 C  CB  . PHE   D 1 333 ? 49.183  -48.101 13.339  1.00 96.73  ? 402  PHE   D CB  1 
ATOM   11137 C  CG  . PHE   D 1 333 ? 47.728  -48.453 13.308  1.00 97.80  ? 402  PHE   D CG  1 
ATOM   11138 C  CD1 . PHE   D 1 333 ? 47.307  -49.759 13.526  1.00 98.77  ? 402  PHE   D CD1 1 
ATOM   11139 C  CD2 . PHE   D 1 333 ? 46.773  -47.479 13.066  1.00 96.92  ? 402  PHE   D CD2 1 
ATOM   11140 C  CE1 . PHE   D 1 333 ? 45.963  -50.086 13.488  1.00 96.90  ? 402  PHE   D CE1 1 
ATOM   11141 C  CE2 . PHE   D 1 333 ? 45.429  -47.796 13.035  1.00 93.84  ? 402  PHE   D CE2 1 
ATOM   11142 C  CZ  . PHE   D 1 333 ? 45.021  -49.103 13.249  1.00 93.78  ? 402  PHE   D CZ  1 
ATOM   11143 N  N   . THR   D 1 334 ? 51.677  -48.873 15.610  1.00 111.63 ? 403  THR   D N   1 
ATOM   11144 C  CA  . THR   D 1 334 ? 53.079  -49.120 15.900  1.00 112.99 ? 403  THR   D CA  1 
ATOM   11145 C  C   . THR   D 1 334 ? 53.467  -50.478 15.332  1.00 114.74 ? 403  THR   D C   1 
ATOM   11146 O  O   . THR   D 1 334 ? 52.706  -51.450 15.443  1.00 114.57 ? 403  THR   D O   1 
ATOM   11147 C  CB  . THR   D 1 334 ? 53.321  -49.081 17.418  1.00 112.03 ? 403  THR   D CB  1 
ATOM   11148 O  OG1 . THR   D 1 334 ? 52.958  -50.337 18.015  1.00 118.16 ? 403  THR   D OG1 1 
ATOM   11149 C  CG2 . THR   D 1 334 ? 52.462  -47.974 18.055  1.00 108.94 ? 403  THR   D CG2 1 
ATOM   11150 N  N   . ALA   D 1 335 ? 54.649  -50.545 14.728  1.00 114.43 ? 404  ALA   D N   1 
ATOM   11151 C  CA  . ALA   D 1 335 ? 55.104  -51.751 14.049  1.00 116.50 ? 404  ALA   D CA  1 
ATOM   11152 C  C   . ALA   D 1 335 ? 55.578  -52.805 15.047  1.00 117.49 ? 404  ALA   D C   1 
ATOM   11153 O  O   . ALA   D 1 335 ? 56.396  -52.501 15.921  1.00 118.87 ? 404  ALA   D O   1 
ATOM   11154 C  CB  . ALA   D 1 335 ? 56.235  -51.388 13.093  1.00 118.05 ? 404  ALA   D CB  1 
ATOM   11155 N  N   . THR   D 1 336 ? 55.091  -54.051 14.902  1.00 115.08 ? 405  THR   D N   1 
ATOM   11156 C  CA  . THR   D 1 336 ? 55.619  -55.161 15.710  1.00 120.66 ? 405  THR   D CA  1 
ATOM   11157 C  C   . THR   D 1 336 ? 57.100  -55.363 15.400  1.00 127.47 ? 405  THR   D C   1 
ATOM   11158 O  O   . THR   D 1 336 ? 57.963  -55.068 16.237  1.00 127.11 ? 405  THR   D O   1 
ATOM   11159 C  CB  . THR   D 1 336 ? 54.864  -56.496 15.498  1.00 115.40 ? 405  THR   D CB  1 
ATOM   11160 O  OG1 . THR   D 1 336 ? 54.975  -56.937 14.139  1.00 124.80 ? 405  THR   D OG1 1 
ATOM   11161 C  CG2 . THR   D 1 336 ? 53.427  -56.384 15.882  1.00 112.57 ? 405  THR   D CG2 1 
ATOM   11162 N  N   . LYS   D 1 337 ? 57.417  -55.827 14.191  1.00 133.13 ? 406  LYS   D N   1 
ATOM   11163 C  CA  . LYS   D 1 337 ? 58.812  -56.036 13.824  1.00 134.39 ? 406  LYS   D CA  1 
ATOM   11164 C  C   . LYS   D 1 337 ? 59.490  -54.682 13.637  1.00 137.25 ? 406  LYS   D C   1 
ATOM   11165 O  O   . LYS   D 1 337 ? 58.881  -53.624 13.812  1.00 137.25 ? 406  LYS   D O   1 
ATOM   11166 C  CB  . LYS   D 1 337 ? 58.918  -56.894 12.567  1.00 141.19 ? 406  LYS   D CB  1 
ATOM   11167 N  N   . LYS   D 1 338 ? 60.782  -54.713 13.298  1.00 141.74 ? 407  LYS   D N   1 
ATOM   11168 C  CA  . LYS   D 1 338 ? 61.558  -53.496 13.108  1.00 141.37 ? 407  LYS   D CA  1 
ATOM   11169 C  C   . LYS   D 1 338 ? 61.819  -53.171 11.649  1.00 152.97 ? 407  LYS   D C   1 
ATOM   11170 O  O   . LYS   D 1 338 ? 62.065  -52.004 11.333  1.00 149.59 ? 407  LYS   D O   1 
ATOM   11171 C  CB  . LYS   D 1 338 ? 62.908  -53.607 13.822  1.00 134.94 ? 407  LYS   D CB  1 
ATOM   11172 C  CG  . LYS   D 1 338 ? 62.904  -54.645 14.924  1.00 128.60 ? 407  LYS   D CG  1 
ATOM   11173 C  CD  . LYS   D 1 338 ? 62.348  -54.070 16.203  1.00 129.76 ? 407  LYS   D CD  1 
ATOM   11174 C  CE  . LYS   D 1 338 ? 62.420  -55.086 17.312  1.00 117.00 ? 407  LYS   D CE  1 
ATOM   11175 N  NZ  . LYS   D 1 338 ? 61.869  -54.500 18.562  1.00 110.09 ? 407  LYS   D NZ  1 
ATOM   11176 N  N   . ASP   D 1 339 ? 61.767  -54.174 10.763  1.00 180.54 ? 408  ASP   D N   1 
ATOM   11177 C  CA  . ASP   D 1 339 ? 61.932  -53.934 9.334   1.00 183.76 ? 408  ASP   D CA  1 
ATOM   11178 C  C   . ASP   D 1 339 ? 60.807  -53.070 8.768   1.00 181.35 ? 408  ASP   D C   1 
ATOM   11179 O  O   . ASP   D 1 339 ? 61.034  -52.324 7.808   1.00 181.21 ? 408  ASP   D O   1 
ATOM   11180 C  CB  . ASP   D 1 339 ? 62.006  -55.275 8.599   1.00 186.28 ? 408  ASP   D CB  1 
ATOM   11181 C  CG  . ASP   D 1 339 ? 60.980  -56.285 9.114   1.00 185.89 ? 408  ASP   D CG  1 
ATOM   11182 O  OD1 . ASP   D 1 339 ? 60.268  -55.959 10.084  1.00 183.30 ? 408  ASP   D OD1 1 
ATOM   11183 O  OD2 . ASP   D 1 339 ? 60.880  -57.400 8.555   1.00 184.94 ? 408  ASP   D OD2 1 
ATOM   11184 N  N   . MET   D 1 340 ? 59.604  -53.139 9.365   1.00 160.70 ? 409  MET   D N   1 
ATOM   11185 C  CA  . MET   D 1 340 ? 58.420  -52.432 8.877   1.00 144.72 ? 409  MET   D CA  1 
ATOM   11186 C  C   . MET   D 1 340 ? 58.735  -50.975 8.537   1.00 133.17 ? 409  MET   D C   1 
ATOM   11187 O  O   . MET   D 1 340 ? 59.478  -50.296 9.253   1.00 131.74 ? 409  MET   D O   1 
ATOM   11188 C  CB  . MET   D 1 340 ? 57.298  -52.487 9.925   1.00 134.67 ? 409  MET   D CB  1 
ATOM   11189 C  CG  . MET   D 1 340 ? 57.071  -53.855 10.566  1.00 133.85 ? 409  MET   D CG  1 
ATOM   11190 S  SD  . MET   D 1 340 ? 55.994  -54.909 9.577   1.00 137.87 ? 409  MET   D SD  1 
ATOM   11191 C  CE  . MET   D 1 340 ? 54.399  -54.162 9.903   1.00 120.67 ? 409  MET   D CE  1 
ATOM   11192 N  N   . SER   D 1 341 ? 58.175  -50.503 7.433   1.00 129.63 ? 410  SER   D N   1 
ATOM   11193 C  CA  . SER   D 1 341 ? 58.360  -49.131 6.988   1.00 122.23 ? 410  SER   D CA  1 
ATOM   11194 C  C   . SER   D 1 341 ? 57.051  -48.729 6.322   1.00 117.09 ? 410  SER   D C   1 
ATOM   11195 O  O   . SER   D 1 341 ? 56.607  -49.424 5.398   1.00 110.50 ? 410  SER   D O   1 
ATOM   11196 C  CB  . SER   D 1 341 ? 59.570  -49.033 6.047   1.00 122.19 ? 410  SER   D CB  1 
ATOM   11197 O  OG  . SER   D 1 341 ? 59.604  -47.832 5.304   1.00 118.06 ? 410  SER   D OG  1 
ATOM   11198 N  N   . PRO   D 1 342 ? 56.358  -47.672 6.816   1.00 117.88 ? 411  PRO   D N   1 
ATOM   11199 C  CA  . PRO   D 1 342 ? 56.752  -46.779 7.911   1.00 114.89 ? 411  PRO   D CA  1 
ATOM   11200 C  C   . PRO   D 1 342 ? 56.670  -47.440 9.283   1.00 113.08 ? 411  PRO   D C   1 
ATOM   11201 O  O   . PRO   D 1 342 ? 55.855  -48.329 9.511   1.00 111.79 ? 411  PRO   D O   1 
ATOM   11202 C  CB  . PRO   D 1 342 ? 55.753  -45.627 7.765   1.00 108.04 ? 411  PRO   D CB  1 
ATOM   11203 C  CG  . PRO   D 1 342 ? 54.501  -46.303 7.322   1.00 107.45 ? 411  PRO   D CG  1 
ATOM   11204 C  CD  . PRO   D 1 342 ? 54.962  -47.419 6.406   1.00 113.61 ? 411  PRO   D CD  1 
ATOM   11205 N  N   . GLN   D 1 343 ? 57.522  -47.017 10.222  1.00 110.60 ? 412  GLN   D N   1 
ATOM   11206 C  CA  . GLN   D 1 343 ? 57.545  -47.652 11.536  1.00 115.61 ? 412  GLN   D CA  1 
ATOM   11207 C  C   . GLN   D 1 343 ? 56.293  -47.339 12.346  1.00 113.33 ? 412  GLN   D C   1 
ATOM   11208 O  O   . GLN   D 1 343 ? 55.815  -48.190 13.109  1.00 112.52 ? 412  GLN   D O   1 
ATOM   11209 C  CB  . GLN   D 1 343 ? 58.804  -47.226 12.297  1.00 117.21 ? 412  GLN   D CB  1 
ATOM   11210 C  CG  . GLN   D 1 343 ? 60.022  -48.115 12.051  1.00 116.10 ? 412  GLN   D CG  1 
ATOM   11211 C  CD  . GLN   D 1 343 ? 59.823  -49.490 12.617  1.00 122.19 ? 412  GLN   D CD  1 
ATOM   11212 O  OE1 . GLN   D 1 343 ? 59.604  -49.650 13.819  1.00 122.85 ? 412  GLN   D OE1 1 
ATOM   11213 N  NE2 . GLN   D 1 343 ? 59.834  -50.493 11.750  1.00 131.15 ? 412  GLN   D NE2 1 
ATOM   11214 N  N   . LYS   D 1 344 ? 55.723  -46.145 12.157  1.00 109.99 ? 413  LYS   D N   1 
ATOM   11215 C  CA  . LYS   D 1 344 ? 54.571  -45.660 12.901  1.00 106.24 ? 413  LYS   D CA  1 
ATOM   11216 C  C   . LYS   D 1 344 ? 53.648  -44.880 11.974  1.00 104.86 ? 413  LYS   D C   1 
ATOM   11217 O  O   . LYS   D 1 344 ? 54.115  -44.175 11.072  1.00 106.91 ? 413  LYS   D O   1 
ATOM   11218 C  CB  . LYS   D 1 344 ? 55.010  -44.756 14.050  1.00 105.94 ? 413  LYS   D CB  1 
ATOM   11219 N  N   . PHE   D 1 345 ? 52.342  -44.983 12.202  1.00 103.05 ? 414  PHE   D N   1 
ATOM   11220 C  CA  . PHE   D 1 345 ? 51.410  -44.113 11.505  1.00 100.89 ? 414  PHE   D CA  1 
ATOM   11221 C  C   . PHE   D 1 345 ? 50.156  -43.973 12.351  1.00 98.67  ? 414  PHE   D C   1 
ATOM   11222 O  O   . PHE   D 1 345 ? 50.001  -44.643 13.379  1.00 99.58  ? 414  PHE   D O   1 
ATOM   11223 C  CB  . PHE   D 1 345 ? 51.083  -44.638 10.101  1.00 102.87 ? 414  PHE   D CB  1 
ATOM   11224 C  CG  . PHE   D 1 345 ? 50.407  -45.976 10.081  1.00 102.26 ? 414  PHE   D CG  1 
ATOM   11225 C  CD1 . PHE   D 1 345 ? 51.143  -47.144 10.130  1.00 98.64  ? 414  PHE   D CD1 1 
ATOM   11226 C  CD2 . PHE   D 1 345 ? 49.030  -46.063 9.972   1.00 101.32 ? 414  PHE   D CD2 1 
ATOM   11227 C  CE1 . PHE   D 1 345 ? 50.513  -48.372 10.078  1.00 99.93  ? 414  PHE   D CE1 1 
ATOM   11228 C  CE2 . PHE   D 1 345 ? 48.394  -47.290 9.928   1.00 98.88  ? 414  PHE   D CE2 1 
ATOM   11229 C  CZ  . PHE   D 1 345 ? 49.136  -48.448 9.977   1.00 100.22 ? 414  PHE   D CZ  1 
ATOM   11230 N  N   . TRP   D 1 346 ? 49.259  -43.081 11.920  1.00 93.38  ? 415  TRP   D N   1 
ATOM   11231 C  CA  . TRP   D 1 346 ? 47.954  -42.912 12.550  1.00 93.01  ? 415  TRP   D CA  1 
ATOM   11232 C  C   . TRP   D 1 346 ? 46.832  -43.277 11.585  1.00 91.60  ? 415  TRP   D C   1 
ATOM   11233 O  O   . TRP   D 1 346 ? 46.924  -43.036 10.380  1.00 94.91  ? 415  TRP   D O   1 
ATOM   11234 C  CB  . TRP   D 1 346 ? 47.752  -41.476 13.046  1.00 93.59  ? 415  TRP   D CB  1 
ATOM   11235 C  CG  . TRP   D 1 346 ? 48.780  -41.056 14.039  1.00 94.18  ? 415  TRP   D CG  1 
ATOM   11236 C  CD1 . TRP   D 1 346 ? 50.064  -40.701 13.773  1.00 96.00  ? 415  TRP   D CD1 1 
ATOM   11237 C  CD2 . TRP   D 1 346 ? 48.619  -40.944 15.455  1.00 92.56  ? 415  TRP   D CD2 1 
ATOM   11238 N  NE1 . TRP   D 1 346 ? 50.722  -40.372 14.936  1.00 94.16  ? 415  TRP   D NE1 1 
ATOM   11239 C  CE2 . TRP   D 1 346 ? 49.855  -40.514 15.985  1.00 92.80  ? 415  TRP   D CE2 1 
ATOM   11240 C  CE3 . TRP   D 1 346 ? 47.553  -41.155 16.327  1.00 92.94  ? 415  TRP   D CE3 1 
ATOM   11241 C  CZ2 . TRP   D 1 346 ? 50.052  -40.290 17.349  1.00 94.47  ? 415  TRP   D CZ2 1 
ATOM   11242 C  CZ3 . TRP   D 1 346 ? 47.749  -40.927 17.691  1.00 96.25  ? 415  TRP   D CZ3 1 
ATOM   11243 C  CH2 . TRP   D 1 346 ? 48.993  -40.508 18.185  1.00 94.80  ? 415  TRP   D CH2 1 
ATOM   11244 N  N   . GLY   D 1 347 ? 45.769  -43.864 12.122  1.00 85.64  ? 416  GLY   D N   1 
ATOM   11245 C  CA  . GLY   D 1 347 ? 44.588  -44.157 11.335  1.00 85.13  ? 416  GLY   D CA  1 
ATOM   11246 C  C   . GLY   D 1 347 ? 43.392  -43.437 11.908  1.00 86.67  ? 416  GLY   D C   1 
ATOM   11247 O  O   . GLY   D 1 347 ? 42.818  -43.900 12.892  1.00 89.26  ? 416  GLY   D O   1 
ATOM   11248 N  N   . LEU   D 1 348 ? 43.013  -42.305 11.306  1.00 89.31  ? 417  LEU   D N   1 
ATOM   11249 C  CA  . LEU   D 1 348 ? 41.998  -41.391 11.837  1.00 86.31  ? 417  LEU   D CA  1 
ATOM   11250 C  C   . LEU   D 1 348 ? 40.675  -41.625 11.120  1.00 84.02  ? 417  LEU   D C   1 
ATOM   11251 O  O   . LEU   D 1 348 ? 40.613  -41.507 9.894   1.00 85.58  ? 417  LEU   D O   1 
ATOM   11252 C  CB  . LEU   D 1 348 ? 42.428  -39.937 11.641  1.00 85.08  ? 417  LEU   D CB  1 
ATOM   11253 C  CG  . LEU   D 1 348 ? 43.932  -39.676 11.717  1.00 85.54  ? 417  LEU   D CG  1 
ATOM   11254 C  CD1 . LEU   D 1 348 ? 44.291  -38.228 11.386  1.00 83.56  ? 417  LEU   D CD1 1 
ATOM   11255 C  CD2 . LEU   D 1 348 ? 44.449  -40.092 13.089  1.00 89.34  ? 417  LEU   D CD2 1 
ATOM   11256 N  N   . THR   D 1 349 ? 39.623  -41.947 11.872  1.00 84.59  ? 418  THR   D N   1 
ATOM   11257 C  CA  . THR   D 1 349 ? 38.370  -42.279 11.211  1.00 86.63  ? 418  THR   D CA  1 
ATOM   11258 C  C   . THR   D 1 349 ? 37.680  -41.023 10.704  1.00 87.83  ? 418  THR   D C   1 
ATOM   11259 O  O   . THR   D 1 349 ? 37.889  -39.920 11.218  1.00 89.53  ? 418  THR   D O   1 
ATOM   11260 C  CB  . THR   D 1 349 ? 37.413  -43.061 12.115  1.00 86.24  ? 418  THR   D CB  1 
ATOM   11261 O  OG1 . THR   D 1 349 ? 36.137  -43.145 11.461  1.00 86.78  ? 418  THR   D OG1 1 
ATOM   11262 C  CG2 . THR   D 1 349 ? 37.250  -42.414 13.479  1.00 90.93  ? 418  THR   D CG2 1 
ATOM   11263 N  N   . ARG   D 1 350 ? 36.844  -41.211 9.682   1.00 88.11  ? 419  ARG   D N   1 
ATOM   11264 C  CA  . ARG   D 1 350 ? 36.344  -40.074 8.918   1.00 87.70  ? 419  ARG   D CA  1 
ATOM   11265 C  C   . ARG   D 1 350 ? 35.340  -39.257 9.717   1.00 91.10  ? 419  ARG   D C   1 
ATOM   11266 O  O   . ARG   D 1 350 ? 35.346  -38.019 9.663   1.00 87.05  ? 419  ARG   D O   1 
ATOM   11267 C  CB  . ARG   D 1 350 ? 35.709  -40.566 7.631   1.00 83.29  ? 419  ARG   D CB  1 
ATOM   11268 C  CG  . ARG   D 1 350 ? 35.773  -39.572 6.573   1.00 81.66  ? 419  ARG   D CG  1 
ATOM   11269 C  CD  . ARG   D 1 350 ? 34.703  -39.852 5.634   1.00 87.11  ? 419  ARG   D CD  1 
ATOM   11270 N  NE  . ARG   D 1 350 ? 33.482  -39.159 6.010   1.00 87.82  ? 419  ARG   D NE  1 
ATOM   11271 C  CZ  . ARG   D 1 350 ? 32.392  -39.755 6.458   1.00 87.27  ? 419  ARG   D CZ  1 
ATOM   11272 N  NH1 . ARG   D 1 350 ? 32.368  -41.050 6.706   1.00 89.68  ? 419  ARG   D NH1 1 
ATOM   11273 N  NH2 . ARG   D 1 350 ? 31.289  -39.037 6.636   1.00 90.42  ? 419  ARG   D NH2 1 
ATOM   11274 N  N   . SER   D 1 351 ? 34.468  -39.945 10.465  1.00 93.62  ? 420  SER   D N   1 
ATOM   11275 C  CA  . SER   D 1 351 ? 33.402  -39.304 11.219  1.00 89.99  ? 420  SER   D CA  1 
ATOM   11276 C  C   . SER   D 1 351 ? 33.940  -38.366 12.276  1.00 94.98  ? 420  SER   D C   1 
ATOM   11277 O  O   . SER   D 1 351 ? 33.235  -37.442 12.695  1.00 99.32  ? 420  SER   D O   1 
ATOM   11278 C  CB  . SER   D 1 351 ? 32.539  -40.379 11.859  1.00 84.63  ? 420  SER   D CB  1 
ATOM   11279 O  OG  . SER   D 1 351 ? 33.365  -41.424 12.326  1.00 95.52  ? 420  SER   D OG  1 
ATOM   11280 N  N   . ALA   D 1 352 ? 35.168  -38.596 12.717  1.00 93.89  ? 421  ALA   D N   1 
ATOM   11281 C  CA  . ALA   D 1 352 ? 35.787  -37.831 13.779  1.00 95.78  ? 421  ALA   D CA  1 
ATOM   11282 C  C   . ALA   D 1 352 ? 36.497  -36.587 13.280  1.00 96.29  ? 421  ALA   D C   1 
ATOM   11283 O  O   . ALA   D 1 352 ? 36.989  -35.815 14.106  1.00 98.50  ? 421  ALA   D O   1 
ATOM   11284 C  CB  . ALA   D 1 352 ? 36.784  -38.711 14.531  1.00 98.76  ? 421  ALA   D CB  1 
ATOM   11285 N  N   . LEU   D 1 353 ? 36.559  -36.368 11.967  1.00 97.15  ? 422  LEU   D N   1 
ATOM   11286 C  CA  . LEU   D 1 353 ? 37.399  -35.320 11.405  1.00 93.78  ? 422  LEU   D CA  1 
ATOM   11287 C  C   . LEU   D 1 353 ? 36.565  -34.222 10.763  1.00 92.69  ? 422  LEU   D C   1 
ATOM   11288 O  O   . LEU   D 1 353 ? 35.380  -34.382 10.464  1.00 90.84  ? 422  LEU   D O   1 
ATOM   11289 C  CB  . LEU   D 1 353 ? 38.381  -35.886 10.375  1.00 93.43  ? 422  LEU   D CB  1 
ATOM   11290 C  CG  . LEU   D 1 353 ? 39.493  -36.789 10.909  1.00 92.07  ? 422  LEU   D CG  1 
ATOM   11291 C  CD1 . LEU   D 1 353 ? 40.365  -37.312 9.774   1.00 88.01  ? 422  LEU   D CD1 1 
ATOM   11292 C  CD2 . LEU   D 1 353 ? 40.323  -36.039 11.929  1.00 87.07  ? 422  LEU   D CD2 1 
ATOM   11293 N  N   . LEU   D 1 354 ? 37.214  -33.104 10.551  1.00 99.59  ? 423  LEU   D N   1 
ATOM   11294 C  CA  . LEU   D 1 354 ? 36.562  -31.917 10.021  1.00 101.45 ? 423  LEU   D CA  1 
ATOM   11295 C  C   . LEU   D 1 354 ? 37.570  -31.079 9.244   1.00 103.95 ? 423  LEU   D C   1 
ATOM   11296 O  O   . LEU   D 1 354 ? 38.493  -30.511 9.843   1.00 103.64 ? 423  LEU   D O   1 
ATOM   11297 C  CB  . LEU   D 1 354 ? 35.946  -31.102 11.157  1.00 101.98 ? 423  LEU   D CB  1 
ATOM   11298 C  CG  . LEU   D 1 354 ? 35.336  -29.751 10.786  1.00 106.15 ? 423  LEU   D CG  1 
ATOM   11299 C  CD1 . LEU   D 1 354 ? 33.973  -29.572 11.444  1.00 108.36 ? 423  LEU   D CD1 1 
ATOM   11300 C  CD2 . LEU   D 1 354 ? 36.266  -28.661 11.222  1.00 107.56 ? 423  LEU   D CD2 1 
ATOM   11301 N  N   . PRO   D 1 355 ? 37.431  -30.981 7.921   1.00 104.54 ? 424  PRO   D N   1 
ATOM   11302 C  CA  . PRO   D 1 355 ? 38.400  -30.221 7.124   1.00 104.97 ? 424  PRO   D CA  1 
ATOM   11303 C  C   . PRO   D 1 355 ? 38.236  -28.721 7.313   1.00 106.62 ? 424  PRO   D C   1 
ATOM   11304 O  O   . PRO   D 1 355 ? 37.123  -28.208 7.474   1.00 106.80 ? 424  PRO   D O   1 
ATOM   11305 C  CB  . PRO   D 1 355 ? 38.066  -30.625 5.683   1.00 105.61 ? 424  PRO   D CB  1 
ATOM   11306 C  CG  . PRO   D 1 355 ? 37.210  -31.842 5.802   1.00 105.27 ? 424  PRO   D CG  1 
ATOM   11307 C  CD  . PRO   D 1 355 ? 36.452  -31.664 7.071   1.00 104.10 ? 424  PRO   D CD  1 
ATOM   11308 N  N   . THR   D 1 356 ? 39.368  -28.010 7.255   1.00 99.60  ? 425  THR   D N   1 
ATOM   11309 C  CA  . THR   D 1 356 ? 39.396  -26.578 7.540   1.00 96.98  ? 425  THR   D CA  1 
ATOM   11310 C  C   . THR   D 1 356 ? 40.424  -25.871 6.663   1.00 94.52  ? 425  THR   D C   1 
ATOM   11311 O  O   . THR   D 1 356 ? 41.371  -26.482 6.160   1.00 93.35  ? 425  THR   D O   1 
ATOM   11312 C  CB  . THR   D 1 356 ? 39.720  -26.303 9.009   1.00 100.54 ? 425  THR   D CB  1 
ATOM   11313 O  OG1 . THR   D 1 356 ? 40.751  -27.201 9.448   1.00 97.96  ? 425  THR   D OG1 1 
ATOM   11314 C  CG2 . THR   D 1 356 ? 38.492  -26.483 9.873   1.00 102.39 ? 425  THR   D CG2 1 
ATOM   11315 N  N   . ILE   D 1 357 ? 40.242  -24.562 6.521   1.00 97.95  ? 426  ILE   D N   1 
ATOM   11316 C  CA  . ILE   D 1 357 ? 41.054  -23.709 5.662   1.00 96.43  ? 426  ILE   D CA  1 
ATOM   11317 C  C   . ILE   D 1 357 ? 41.935  -22.835 6.553   1.00 98.10  ? 426  ILE   D C   1 
ATOM   11318 O  O   . ILE   D 1 357 ? 41.429  -21.883 7.165   1.00 103.76 ? 426  ILE   D O   1 
ATOM   11319 C  CB  . ILE   D 1 357 ? 40.186  -22.829 4.754   1.00 96.19  ? 426  ILE   D CB  1 
ATOM   11320 C  CG1 . ILE   D 1 357 ? 39.238  -23.659 3.877   1.00 96.16  ? 426  ILE   D CG1 1 
ATOM   11321 C  CG2 . ILE   D 1 357 ? 41.077  -21.937 3.914   1.00 98.46  ? 426  ILE   D CG2 1 
ATOM   11322 C  CD1 . ILE   D 1 357 ? 38.262  -22.788 3.119   1.00 100.34 ? 426  ILE   D CD1 1 
ATOM   11323 N  N   . PRO   D 1 358 ? 43.251  -23.087 6.639   1.00 88.23  ? 427  PRO   D N   1 
ATOM   11324 C  CA  . PRO   D 1 358 ? 44.261  -22.282 7.353   1.00 86.51  ? 427  PRO   D CA  1 
ATOM   11325 C  C   . PRO   D 1 358 ? 44.135  -20.736 7.254   1.00 88.54  ? 427  PRO   D C   1 
ATOM   11326 O  O   . PRO   D 1 358 ? 44.421  -19.966 8.201   1.00 84.73  ? 427  PRO   D O   1 
ATOM   11327 C  CB  . PRO   D 1 358 ? 45.553  -22.762 6.703   1.00 79.39  ? 427  PRO   D CB  1 
ATOM   11328 C  CG  . PRO   D 1 358 ? 45.297  -24.245 6.461   1.00 85.67  ? 427  PRO   D CG  1 
ATOM   11329 C  CD  . PRO   D 1 358 ? 43.802  -24.390 6.227   1.00 89.40  ? 427  PRO   D CD  1 
ATOM   11330 N  N   . VAL   D 1 369 ? 38.499  -16.631 2.562   1.00 123.54 ? 438  VAL   D N   1 
ATOM   11331 C  CA  . VAL   D 1 369 ? 38.407  -17.715 1.576   1.00 124.32 ? 438  VAL   D CA  1 
ATOM   11332 C  C   . VAL   D 1 369 ? 37.108  -18.488 1.738   1.00 126.17 ? 438  VAL   D C   1 
ATOM   11333 O  O   . VAL   D 1 369 ? 36.648  -18.721 2.861   1.00 125.56 ? 438  VAL   D O   1 
ATOM   11334 C  CB  . VAL   D 1 369 ? 39.586  -18.666 1.697   1.00 120.30 ? 438  VAL   D CB  1 
ATOM   11335 C  CG1 . VAL   D 1 369 ? 40.771  -18.096 0.983   1.00 118.78 ? 438  VAL   D CG1 1 
ATOM   11336 C  CG2 . VAL   D 1 369 ? 39.914  -18.829 3.155   1.00 121.56 ? 438  VAL   D CG2 1 
ATOM   11337 N  N   . ILE   D 1 370 ? 36.521  -18.892 0.613   1.00 117.51 ? 439  ILE   D N   1 
ATOM   11338 C  CA  . ILE   D 1 370 ? 35.301  -19.694 0.596   1.00 109.95 ? 439  ILE   D CA  1 
ATOM   11339 C  C   . ILE   D 1 370 ? 35.498  -20.812 -0.417  1.00 103.72 ? 439  ILE   D C   1 
ATOM   11340 O  O   . ILE   D 1 370 ? 36.277  -20.680 -1.364  1.00 106.52 ? 439  ILE   D O   1 
ATOM   11341 C  CB  . ILE   D 1 370 ? 34.058  -18.839 0.256   1.00 103.53 ? 439  ILE   D CB  1 
ATOM   11342 C  CG1 . ILE   D 1 370 ? 33.827  -17.800 1.339   1.00 109.41 ? 439  ILE   D CG1 1 
ATOM   11343 C  CG2 . ILE   D 1 370 ? 32.819  -19.690 0.139   1.00 103.02 ? 439  ILE   D CG2 1 
ATOM   11344 C  CD1 . ILE   D 1 370 ? 32.564  -17.015 1.135   1.00 111.41 ? 439  ILE   D CD1 1 
ATOM   11345 N  N   . LEU   D 1 371 ? 34.844  -21.945 -0.174  1.00 98.44  ? 440  LEU   D N   1 
ATOM   11346 C  CA  . LEU   D 1 371 ? 34.923  -23.074 -1.127  1.00 94.08  ? 440  LEU   D CA  1 
ATOM   11347 C  C   . LEU   D 1 371 ? 34.089  -22.707 -2.357  1.00 98.11  ? 440  LEU   D C   1 
ATOM   11348 O  O   . LEU   D 1 371 ? 32.864  -22.543 -2.202  1.00 96.75  ? 440  LEU   D O   1 
ATOM   11349 C  CB  . LEU   D 1 371 ? 34.399  -24.312 -0.412  1.00 93.18  ? 440  LEU   D CB  1 
ATOM   11350 C  CG  . LEU   D 1 371 ? 35.231  -24.789 0.778   1.00 89.42  ? 440  LEU   D CG  1 
ATOM   11351 C  CD1 . LEU   D 1 371 ? 34.456  -25.915 1.411   1.00 87.87  ? 440  LEU   D CD1 1 
ATOM   11352 C  CD2 . LEU   D 1 371 ? 36.589  -25.283 0.319   1.00 93.60  ? 440  LEU   D CD2 1 
ATOM   11353 N  N   . CYS   D 1 372 ? 34.724  -22.585 -3.524  1.00 99.24  ? 441  CYS   D N   1 
ATOM   11354 C  CA  . CYS   D 1 372 ? 33.995  -22.123 -4.734  1.00 100.88 ? 441  CYS   D CA  1 
ATOM   11355 C  C   . CYS   D 1 372 ? 33.553  -23.303 -5.609  1.00 99.09  ? 441  CYS   D C   1 
ATOM   11356 O  O   . CYS   D 1 372 ? 33.876  -24.454 -5.260  1.00 99.49  ? 441  CYS   D O   1 
ATOM   11357 C  CB  . CYS   D 1 372 ? 34.864  -21.185 -5.558  1.00 100.67 ? 441  CYS   D CB  1 
ATOM   11358 S  SG  . CYS   D 1 372 ? 35.462  -19.763 -4.611  1.00 109.45 ? 441  CYS   D SG  1 
ATOM   11359 N  N   . LEU   D 1 373 ? 32.840  -23.013 -6.701  1.00 102.32 ? 442  LEU   D N   1 
ATOM   11360 C  CA  . LEU   D 1 373 ? 32.336  -24.082 -7.601  1.00 99.84  ? 442  LEU   D CA  1 
ATOM   11361 C  C   . LEU   D 1 373 ? 32.285  -23.572 -9.051  1.00 99.27  ? 442  LEU   D C   1 
ATOM   11362 O  O   . LEU   D 1 373 ? 31.678  -24.232 -9.880  1.00 97.28  ? 442  LEU   D O   1 
ATOM   11363 C  CB  . LEU   D 1 373 ? 30.960  -24.545 -7.127  1.00 98.01  ? 442  LEU   D CB  1 
ATOM   11364 C  CG  . LEU   D 1 373 ? 29.850  -23.491 -7.132  1.00 98.53  ? 442  LEU   D CG  1 
ATOM   11365 C  CD1 . LEU   D 1 373 ? 29.290  -23.312 -8.530  1.00 101.16 ? 442  LEU   D CD1 1 
ATOM   11366 C  CD2 . LEU   D 1 373 ? 28.754  -23.895 -6.164  1.00 95.28  ? 442  LEU   D CD2 1 
ATOM   11367 O  OXT . LEU   D 1 373 ? 32.866  -22.514 -9.318  1.00 96.73  ? 442  LEU   D OXT 1 
ATOM   11368 N  N   . SER   E 2 2   ? 9.828   -9.035  -16.358 1.00 107.93 ? 2    SER   E N   1 
ATOM   11369 C  CA  . SER   E 2 2   ? 9.336   -8.073  -17.338 1.00 108.20 ? 2    SER   E CA  1 
ATOM   11370 C  C   . SER   E 2 2   ? 9.054   -8.730  -18.690 1.00 109.52 ? 2    SER   E C   1 
ATOM   11371 O  O   . SER   E 2 2   ? 8.975   -9.964  -18.813 1.00 105.38 ? 2    SER   E O   1 
ATOM   11372 C  CB  . SER   E 2 2   ? 10.340  -6.930  -17.527 1.00 99.80  ? 2    SER   E CB  1 
ATOM   11373 O  OG  . SER   E 2 2   ? 11.606  -7.426  -17.927 1.00 92.24  ? 2    SER   E OG  1 
ATOM   11374 N  N   . TYR   E 2 3   ? 8.913   -7.873  -19.702 1.00 106.23 ? 3    TYR   E N   1 
ATOM   11375 C  CA  . TYR   E 2 3   ? 8.624   -8.285  -21.064 1.00 102.76 ? 3    TYR   E CA  1 
ATOM   11376 C  C   . TYR   E 2 3   ? 9.521   -7.503  -22.002 1.00 103.92 ? 3    TYR   E C   1 
ATOM   11377 O  O   . TYR   E 2 3   ? 9.674   -6.287  -21.853 1.00 107.45 ? 3    TYR   E O   1 
ATOM   11378 C  CB  . TYR   E 2 3   ? 7.171   -8.026  -21.401 1.00 104.24 ? 3    TYR   E CB  1 
ATOM   11379 C  CG  . TYR   E 2 3   ? 6.273   -8.406  -20.271 1.00 103.29 ? 3    TYR   E CG  1 
ATOM   11380 C  CD1 . TYR   E 2 3   ? 6.069   -9.737  -19.959 1.00 104.05 ? 3    TYR   E CD1 1 
ATOM   11381 C  CD2 . TYR   E 2 3   ? 5.651   -7.439  -19.495 1.00 107.97 ? 3    TYR   E CD2 1 
ATOM   11382 C  CE1 . TYR   E 2 3   ? 5.251   -10.106 -18.919 1.00 107.87 ? 3    TYR   E CE1 1 
ATOM   11383 C  CE2 . TYR   E 2 3   ? 4.826   -7.791  -18.449 1.00 110.93 ? 3    TYR   E CE2 1 
ATOM   11384 C  CZ  . TYR   E 2 3   ? 4.627   -9.133  -18.165 1.00 110.35 ? 3    TYR   E CZ  1 
ATOM   11385 O  OH  . TYR   E 2 3   ? 3.804   -9.514  -17.126 1.00 108.50 ? 3    TYR   E OH  1 
ATOM   11386 N  N   . ASN   E 2 4   ? 10.102  -8.196  -22.973 1.00 99.71  ? 4    ASN   E N   1 
ATOM   11387 C  CA  . ASN   E 2 4   ? 11.082  -7.567  -23.824 1.00 99.74  ? 4    ASN   E CA  1 
ATOM   11388 C  C   . ASN   E 2 4   ? 10.822  -7.954  -25.264 1.00 101.14 ? 4    ASN   E C   1 
ATOM   11389 O  O   . ASN   E 2 4   ? 9.981   -8.803  -25.573 1.00 103.24 ? 4    ASN   E O   1 
ATOM   11390 C  CB  . ASN   E 2 4   ? 12.499  -7.926  -23.383 1.00 99.40  ? 4    ASN   E CB  1 
ATOM   11391 C  CG  . ASN   E 2 4   ? 12.742  -7.584  -21.936 1.00 97.45  ? 4    ASN   E CG  1 
ATOM   11392 O  OD1 . ASN   E 2 4   ? 13.170  -6.481  -21.619 1.00 94.02  ? 4    ASN   E OD1 1 
ATOM   11393 N  ND2 . ASN   E 2 4   ? 12.431  -8.517  -21.043 1.00 97.17  ? 4    ASN   E ND2 1 
ATOM   11394 N  N   . TYR   E 2 5   ? 11.577  -7.319  -26.145 1.00 98.33  ? 5    TYR   E N   1 
ATOM   11395 C  CA  . TYR   E 2 5   ? 11.264  -7.308  -27.560 1.00 95.98  ? 5    TYR   E CA  1 
ATOM   11396 C  C   . TYR   E 2 5   ? 12.618  -7.346  -28.263 1.00 94.89  ? 5    TYR   E C   1 
ATOM   11397 O  O   . TYR   E 2 5   ? 13.350  -6.359  -28.226 1.00 94.92  ? 5    TYR   E O   1 
ATOM   11398 C  CB  . TYR   E 2 5   ? 10.462  -6.049  -27.883 1.00 93.58  ? 5    TYR   E CB  1 
ATOM   11399 C  CG  . TYR   E 2 5   ? 10.271  -5.659  -29.331 1.00 91.13  ? 5    TYR   E CG  1 
ATOM   11400 C  CD1 . TYR   E 2 5   ? 11.207  -4.877  -29.987 1.00 91.74  ? 5    TYR   E CD1 1 
ATOM   11401 C  CD2 . TYR   E 2 5   ? 9.124   -6.008  -30.021 1.00 93.52  ? 5    TYR   E CD2 1 
ATOM   11402 C  CE1 . TYR   E 2 5   ? 11.030  -4.487  -31.312 1.00 92.24  ? 5    TYR   E CE1 1 
ATOM   11403 C  CE2 . TYR   E 2 5   ? 8.929   -5.622  -31.350 1.00 95.95  ? 5    TYR   E CE2 1 
ATOM   11404 C  CZ  . TYR   E 2 5   ? 9.890   -4.857  -31.995 1.00 93.87  ? 5    TYR   E CZ  1 
ATOM   11405 O  OH  . TYR   E 2 5   ? 9.725   -4.464  -33.319 1.00 91.47  ? 5    TYR   E OH  1 
ATOM   11406 N  N   . VAL   E 2 6   ? 12.972  -8.508  -28.840 1.00 91.31  ? 6    VAL   E N   1 
ATOM   11407 C  CA  . VAL   E 2 6   ? 14.228  -8.621  -29.583 1.00 88.64  ? 6    VAL   E CA  1 
ATOM   11408 C  C   . VAL   E 2 6   ? 13.943  -8.294  -31.038 1.00 86.85  ? 6    VAL   E C   1 
ATOM   11409 O  O   . VAL   E 2 6   ? 12.933  -8.735  -31.597 1.00 88.39  ? 6    VAL   E O   1 
ATOM   11410 C  CB  . VAL   E 2 6   ? 14.851  -10.021 -29.438 1.00 84.70  ? 6    VAL   E CB  1 
ATOM   11411 C  CG1 . VAL   E 2 6   ? 15.493  -10.203 -28.061 1.00 82.06  ? 6    VAL   E CG1 1 
ATOM   11412 C  CG2 . VAL   E 2 6   ? 13.793  -11.064 -29.656 1.00 88.03  ? 6    VAL   E CG2 1 
ATOM   11413 N  N   . VAL   E 2 7   ? 14.816  -7.492  -31.649 1.00 84.10  ? 7    VAL   E N   1 
ATOM   11414 C  CA  . VAL   E 2 7   ? 14.767  -7.244  -33.083 1.00 86.34  ? 7    VAL   E CA  1 
ATOM   11415 C  C   . VAL   E 2 7   ? 16.192  -7.273  -33.629 1.00 86.74  ? 7    VAL   E C   1 
ATOM   11416 O  O   . VAL   E 2 7   ? 17.175  -7.126  -32.893 1.00 84.65  ? 7    VAL   E O   1 
ATOM   11417 C  CB  . VAL   E 2 7   ? 14.046  -5.912  -33.452 1.00 85.84  ? 7    VAL   E CB  1 
ATOM   11418 C  CG1 . VAL   E 2 7   ? 14.896  -4.703  -33.115 1.00 86.09  ? 7    VAL   E CG1 1 
ATOM   11419 C  CG2 . VAL   E 2 7   ? 13.599  -5.896  -34.933 1.00 87.89  ? 7    VAL   E CG2 1 
ATOM   11420 N  N   . THR   E 2 8   ? 16.285  -7.494  -34.942 1.00 88.03  ? 8    THR   E N   1 
ATOM   11421 C  CA  . THR   E 2 8   ? 17.552  -7.627  -35.647 1.00 85.32  ? 8    THR   E CA  1 
ATOM   11422 C  C   . THR   E 2 8   ? 17.893  -6.311  -36.334 1.00 85.07  ? 8    THR   E C   1 
ATOM   11423 O  O   . THR   E 2 8   ? 17.163  -5.871  -37.232 1.00 90.56  ? 8    THR   E O   1 
ATOM   11424 C  CB  . THR   E 2 8   ? 17.479  -8.758  -36.669 1.00 82.93  ? 8    THR   E CB  1 
ATOM   11425 O  OG1 . THR   E 2 8   ? 17.201  -9.989  -35.983 1.00 87.41  ? 8    THR   E OG1 1 
ATOM   11426 C  CG2 . THR   E 2 8   ? 18.779  -8.868  -37.436 1.00 80.37  ? 8    THR   E CG2 1 
ATOM   11427 N  N   . ALA   E 2 9   ? 18.997  -5.687  -35.909 1.00 79.66  ? 9    ALA   E N   1 
ATOM   11428 C  CA  . ALA   E 2 9   ? 19.529  -4.507  -36.582 1.00 82.20  ? 9    ALA   E CA  1 
ATOM   11429 C  C   . ALA   E 2 9   ? 20.537  -4.854  -37.663 1.00 82.05  ? 9    ALA   E C   1 
ATOM   11430 O  O   . ALA   E 2 9   ? 20.908  -3.985  -38.459 1.00 84.67  ? 9    ALA   E O   1 
ATOM   11431 C  CB  . ALA   E 2 9   ? 20.199  -3.570  -35.577 1.00 82.38  ? 9    ALA   E CB  1 
ATOM   11432 N  N   . GLN   E 2 10  ? 20.994  -6.095  -37.701 1.00 80.38  ? 10   GLN   E N   1 
ATOM   11433 C  CA  . GLN   E 2 10  ? 21.970  -6.526  -38.683 1.00 79.46  ? 10   GLN   E CA  1 
ATOM   11434 C  C   . GLN   E 2 10  ? 21.843  -8.035  -38.777 1.00 80.65  ? 10   GLN   E C   1 
ATOM   11435 O  O   . GLN   E 2 10  ? 21.801  -8.709  -37.749 1.00 83.71  ? 10   GLN   E O   1 
ATOM   11436 C  CB  . GLN   E 2 10  ? 23.389  -6.115  -38.270 1.00 78.38  ? 10   GLN   E CB  1 
ATOM   11437 C  CG  . GLN   E 2 10  ? 24.491  -6.810  -39.046 1.00 79.62  ? 10   GLN   E CG  1 
ATOM   11438 C  CD  . GLN   E 2 10  ? 24.448  -6.498  -40.521 1.00 84.23  ? 10   GLN   E CD  1 
ATOM   11439 O  OE1 . GLN   E 2 10  ? 24.365  -5.341  -40.921 1.00 88.67  ? 10   GLN   E OE1 1 
ATOM   11440 N  NE2 . GLN   E 2 10  ? 24.488  -7.535  -41.341 1.00 88.53  ? 10   GLN   E NE2 1 
ATOM   11441 N  N   . LYS   E 2 11  ? 21.730  -8.557  -39.989 1.00 80.35  ? 11   LYS   E N   1 
ATOM   11442 C  CA  . LYS   E 2 11  ? 21.647  -9.989  -40.171 1.00 78.98  ? 11   LYS   E CA  1 
ATOM   11443 C  C   . LYS   E 2 11  ? 23.034  -10.596 -39.940 1.00 80.82  ? 11   LYS   E C   1 
ATOM   11444 O  O   . LYS   E 2 11  ? 24.026  -9.876  -39.853 1.00 82.26  ? 11   LYS   E O   1 
ATOM   11445 C  CB  . LYS   E 2 11  ? 21.090  -10.297 -41.565 1.00 81.25  ? 11   LYS   E CB  1 
ATOM   11446 N  N   . PRO   E 2 12  ? 23.121  -11.912 -39.758 1.00 81.12  ? 12   PRO   E N   1 
ATOM   11447 C  CA  . PRO   E 2 12  ? 24.426  -12.586 -39.762 1.00 79.75  ? 12   PRO   E CA  1 
ATOM   11448 C  C   . PRO   E 2 12  ? 25.265  -12.215 -40.975 1.00 78.78  ? 12   PRO   E C   1 
ATOM   11449 O  O   . PRO   E 2 12  ? 24.803  -12.279 -42.107 1.00 82.73  ? 12   PRO   E O   1 
ATOM   11450 C  CB  . PRO   E 2 12  ? 24.044  -14.067 -39.819 1.00 84.28  ? 12   PRO   E CB  1 
ATOM   11451 C  CG  . PRO   E 2 12  ? 22.681  -14.149 -39.226 1.00 84.38  ? 12   PRO   E CG  1 
ATOM   11452 C  CD  . PRO   E 2 12  ? 22.023  -12.815 -39.371 1.00 84.47  ? 12   PRO   E CD  1 
ATOM   11453 N  N   . THR   E 2 13  ? 26.522  -11.877 -40.750 1.00 78.92  ? 13   THR   E N   1 
ATOM   11454 C  CA  . THR   E 2 13  ? 27.391  -11.529 -41.860 1.00 78.61  ? 13   THR   E CA  1 
ATOM   11455 C  C   . THR   E 2 13  ? 28.383  -12.617 -42.225 1.00 87.83  ? 13   THR   E C   1 
ATOM   11456 O  O   . THR   E 2 13  ? 28.958  -12.565 -43.321 1.00 91.40  ? 13   THR   E O   1 
ATOM   11457 C  CB  . THR   E 2 13  ? 28.181  -10.268 -41.532 1.00 80.82  ? 13   THR   E CB  1 
ATOM   11458 O  OG1 . THR   E 2 13  ? 29.271  -10.626 -40.680 1.00 83.84  ? 13   THR   E OG1 1 
ATOM   11459 C  CG2 . THR   E 2 13  ? 27.296  -9.298  -40.794 1.00 83.12  ? 13   THR   E CG2 1 
ATOM   11460 N  N   . ALA   E 2 14  ? 28.611  -13.583 -41.336 1.00 89.08  ? 14   ALA   E N   1 
ATOM   11461 C  CA  . ALA   E 2 14  ? 29.607  -14.613 -41.561 1.00 85.45  ? 14   ALA   E CA  1 
ATOM   11462 C  C   . ALA   E 2 14  ? 28.997  -15.729 -42.382 1.00 84.01  ? 14   ALA   E C   1 
ATOM   11463 O  O   . ALA   E 2 14  ? 27.814  -16.044 -42.234 1.00 83.17  ? 14   ALA   E O   1 
ATOM   11464 C  CB  . ALA   E 2 14  ? 30.137  -15.144 -40.235 1.00 88.09  ? 14   ALA   E CB  1 
ATOM   11465 N  N   . VAL   E 2 15  ? 29.808  -16.291 -43.274 1.00 88.59  ? 15   VAL   E N   1 
ATOM   11466 C  CA  . VAL   E 2 15  ? 29.389  -17.327 -44.211 1.00 87.24  ? 15   VAL   E CA  1 
ATOM   11467 C  C   . VAL   E 2 15  ? 29.818  -18.680 -43.672 1.00 91.49  ? 15   VAL   E C   1 
ATOM   11468 O  O   . VAL   E 2 15  ? 31.010  -18.908 -43.422 1.00 90.86  ? 15   VAL   E O   1 
ATOM   11469 C  CB  . VAL   E 2 15  ? 29.994  -17.096 -45.598 1.00 83.32  ? 15   VAL   E CB  1 
ATOM   11470 C  CG1 . VAL   E 2 15  ? 29.626  -18.229 -46.494 1.00 87.01  ? 15   VAL   E CG1 1 
ATOM   11471 C  CG2 . VAL   E 2 15  ? 29.504  -15.791 -46.139 1.00 86.87  ? 15   VAL   E CG2 1 
ATOM   11472 N  N   . ASN   E 2 16  ? 28.851  -19.587 -43.508 1.00 96.12  ? 16   ASN   E N   1 
ATOM   11473 C  CA  . ASN   E 2 16  ? 29.136  -20.919 -42.998 1.00 100.29 ? 16   ASN   E CA  1 
ATOM   11474 C  C   . ASN   E 2 16  ? 28.945  -22.014 -44.036 1.00 99.46  ? 16   ASN   E C   1 
ATOM   11475 O  O   . ASN   E 2 16  ? 29.419  -23.133 -43.829 1.00 102.96 ? 16   ASN   E O   1 
ATOM   11476 C  CB  . ASN   E 2 16  ? 28.262  -21.223 -41.769 1.00 102.13 ? 16   ASN   E CB  1 
ATOM   11477 C  CG  . ASN   E 2 16  ? 26.783  -21.155 -42.074 1.00 100.88 ? 16   ASN   E CG  1 
ATOM   11478 O  OD1 . ASN   E 2 16  ? 26.281  -20.113 -42.484 1.00 100.54 ? 16   ASN   E OD1 1 
ATOM   11479 N  ND2 . ASN   E 2 16  ? 26.071  -22.259 -41.853 1.00 100.37 ? 16   ASN   E ND2 1 
ATOM   11480 N  N   . GLY   E 2 17  ? 28.276  -21.718 -45.139 1.00 91.57  ? 17   GLY   E N   1 
ATOM   11481 C  CA  . GLY   E 2 17  ? 28.051  -22.715 -46.165 1.00 93.10  ? 17   GLY   E CA  1 
ATOM   11482 C  C   . GLY   E 2 17  ? 27.853  -22.043 -47.500 1.00 93.68  ? 17   GLY   E C   1 
ATOM   11483 O  O   . GLY   E 2 17  ? 27.290  -20.946 -47.583 1.00 95.06  ? 17   GLY   E O   1 
ATOM   11484 N  N   . CYS   E 2 18  ? 28.337  -22.697 -48.554 1.00 93.84  ? 18   CYS   E N   1 
ATOM   11485 C  CA  . CYS   E 2 18  ? 28.223  -22.145 -49.898 1.00 92.54  ? 18   CYS   E CA  1 
ATOM   11486 C  C   . CYS   E 2 18  ? 28.415  -23.273 -50.892 1.00 94.01  ? 18   CYS   E C   1 
ATOM   11487 O  O   . CYS   E 2 18  ? 29.386  -24.029 -50.786 1.00 99.69  ? 18   CYS   E O   1 
ATOM   11488 C  CB  . CYS   E 2 18  ? 29.240  -21.019 -50.147 1.00 96.84  ? 18   CYS   E CB  1 
ATOM   11489 S  SG  . CYS   E 2 18  ? 31.033  -21.370 -49.881 1.00 107.76 ? 18   CYS   E SG  1 
ATOM   11490 N  N   . VAL   E 2 19  ? 27.482  -23.384 -51.842 1.00 96.92  ? 19   VAL   E N   1 
ATOM   11491 C  CA  . VAL   E 2 19  ? 27.490  -24.417 -52.866 1.00 90.85  ? 19   VAL   E CA  1 
ATOM   11492 C  C   . VAL   E 2 19  ? 27.139  -23.790 -54.213 1.00 89.44  ? 19   VAL   E C   1 
ATOM   11493 O  O   . VAL   E 2 19  ? 26.485  -22.749 -54.290 1.00 90.81  ? 19   VAL   E O   1 
ATOM   11494 C  CB  . VAL   E 2 19  ? 26.501  -25.556 -52.529 1.00 88.62  ? 19   VAL   E CB  1 
ATOM   11495 C  CG1 . VAL   E 2 19  ? 27.041  -26.417 -51.398 1.00 94.04  ? 19   VAL   E CG1 1 
ATOM   11496 C  CG2 . VAL   E 2 19  ? 25.150  -24.980 -52.161 1.00 87.14  ? 19   VAL   E CG2 1 
ATOM   11497 N  N   . THR   E 2 20  ? 27.573  -24.452 -55.276 1.00 90.72  ? 20   THR   E N   1 
ATOM   11498 C  CA  . THR   E 2 20  ? 27.220  -24.129 -56.648 1.00 90.01  ? 20   THR   E CA  1 
ATOM   11499 C  C   . THR   E 2 20  ? 26.126  -25.072 -57.158 1.00 94.30  ? 20   THR   E C   1 
ATOM   11500 O  O   . THR   E 2 20  ? 25.855  -26.125 -56.582 1.00 95.95  ? 20   THR   E O   1 
ATOM   11501 C  CB  . THR   E 2 20  ? 28.456  -24.221 -57.551 1.00 94.17  ? 20   THR   E CB  1 
ATOM   11502 O  OG1 . THR   E 2 20  ? 29.294  -25.324 -57.142 1.00 89.95  ? 20   THR   E OG1 1 
ATOM   11503 C  CG2 . THR   E 2 20  ? 29.242  -22.934 -57.489 1.00 93.94  ? 20   THR   E CG2 1 
ATOM   11504 N  N   . GLY   E 2 21  ? 25.489  -24.680 -58.252 1.00 102.66 ? 21   GLY   E N   1 
ATOM   11505 C  CA  . GLY   E 2 21  ? 24.493  -25.555 -58.840 1.00 103.66 ? 21   GLY   E CA  1 
ATOM   11506 C  C   . GLY   E 2 21  ? 23.599  -24.793 -59.808 1.00 105.30 ? 21   GLY   E C   1 
ATOM   11507 O  O   . GLY   E 2 21  ? 23.982  -23.757 -60.353 1.00 104.59 ? 21   GLY   E O   1 
ATOM   11508 N  N   . HIS   E 2 22  ? 22.409  -25.356 -60.019 1.00 107.33 ? 22   HIS   E N   1 
ATOM   11509 C  CA  . HIS   E 2 22  ? 21.449  -24.844 -60.991 1.00 107.78 ? 22   HIS   E CA  1 
ATOM   11510 C  C   . HIS   E 2 22  ? 20.062  -24.932 -60.349 1.00 108.99 ? 22   HIS   E C   1 
ATOM   11511 O  O   . HIS   E 2 22  ? 19.242  -25.790 -60.664 1.00 109.32 ? 22   HIS   E O   1 
ATOM   11512 C  CB  . HIS   E 2 22  ? 21.543  -25.622 -62.298 1.00 109.41 ? 22   HIS   E CB  1 
ATOM   11513 C  CG  . HIS   E 2 22  ? 22.951  -25.944 -62.692 1.00 107.98 ? 22   HIS   E CG  1 
ATOM   11514 N  ND1 . HIS   E 2 22  ? 23.817  -24.997 -63.198 1.00 109.75 ? 22   HIS   E ND1 1 
ATOM   11515 C  CD2 . HIS   E 2 22  ? 23.657  -27.098 -62.616 1.00 105.00 ? 22   HIS   E CD2 1 
ATOM   11516 C  CE1 . HIS   E 2 22  ? 24.990  -25.559 -63.437 1.00 106.85 ? 22   HIS   E CE1 1 
ATOM   11517 N  NE2 . HIS   E 2 22  ? 24.919  -26.834 -63.094 1.00 102.81 ? 22   HIS   E NE2 1 
ATOM   11518 N  N   . PHE   E 2 23  ? 19.818  -24.026 -59.408 1.00 110.99 ? 23   PHE   E N   1 
ATOM   11519 C  CA  . PHE   E 2 23  ? 18.648  -24.101 -58.547 1.00 112.63 ? 23   PHE   E CA  1 
ATOM   11520 C  C   . PHE   E 2 23  ? 17.463  -23.340 -59.136 1.00 117.07 ? 23   PHE   E C   1 
ATOM   11521 O  O   . PHE   E 2 23  ? 16.310  -23.792 -59.027 1.00 116.93 ? 23   PHE   E O   1 
ATOM   11522 C  CB  . PHE   E 2 23  ? 19.019  -23.565 -57.151 1.00 107.27 ? 23   PHE   E CB  1 
ATOM   11523 C  CG  . PHE   E 2 23  ? 17.923  -23.692 -56.136 1.00 106.18 ? 23   PHE   E CG  1 
ATOM   11524 C  CD1 . PHE   E 2 23  ? 17.122  -24.828 -56.103 1.00 109.28 ? 23   PHE   E CD1 1 
ATOM   11525 C  CD2 . PHE   E 2 23  ? 17.696  -22.684 -55.211 1.00 102.37 ? 23   PHE   E CD2 1 
ATOM   11526 C  CE1 . PHE   E 2 23  ? 16.111  -24.956 -55.174 1.00 107.80 ? 23   PHE   E CE1 1 
ATOM   11527 C  CE2 . PHE   E 2 23  ? 16.682  -22.797 -54.280 1.00 105.60 ? 23   PHE   E CE2 1 
ATOM   11528 C  CZ  . PHE   E 2 23  ? 15.889  -23.938 -54.259 1.00 109.07 ? 23   PHE   E CZ  1 
ATOM   11529 N  N   . THR   E 2 24  ? 17.747  -22.209 -59.796 1.00 117.44 ? 24   THR   E N   1 
ATOM   11530 C  CA  . THR   E 2 24  ? 16.712  -21.354 -60.373 1.00 121.59 ? 24   THR   E CA  1 
ATOM   11531 C  C   . THR   E 2 24  ? 16.285  -21.833 -61.764 1.00 121.60 ? 24   THR   E C   1 
ATOM   11532 O  O   . THR   E 2 24  ? 15.087  -21.932 -62.057 1.00 121.10 ? 24   THR   E O   1 
ATOM   11533 C  CB  . THR   E 2 24  ? 17.218  -19.909 -60.429 1.00 119.90 ? 24   THR   E CB  1 
ATOM   11534 O  OG1 . THR   E 2 24  ? 18.347  -19.830 -61.312 1.00 119.48 ? 24   THR   E OG1 1 
ATOM   11535 C  CG2 . THR   E 2 24  ? 17.650  -19.444 -59.051 1.00 112.72 ? 24   THR   E CG2 1 
ATOM   11536 N  N   . SER   E 2 25  ? 17.252  -22.122 -62.634 1.00 120.57 ? 25   SER   E N   1 
ATOM   11537 C  CA  . SER   E 2 25  ? 16.984  -22.681 -63.951 1.00 122.45 ? 25   SER   E CA  1 
ATOM   11538 C  C   . SER   E 2 25  ? 18.154  -23.560 -64.347 1.00 123.01 ? 25   SER   E C   1 
ATOM   11539 O  O   . SER   E 2 25  ? 19.301  -23.218 -64.050 1.00 122.73 ? 25   SER   E O   1 
ATOM   11540 C  CB  . SER   E 2 25  ? 16.791  -21.599 -65.007 1.00 128.71 ? 25   SER   E CB  1 
ATOM   11541 O  OG  . SER   E 2 25  ? 16.439  -22.204 -66.234 1.00 136.97 ? 25   SER   E OG  1 
ATOM   11542 N  N   . ALA   E 2 26  ? 17.871  -24.672 -65.036 1.00 127.98 ? 26   ALA   E N   1 
ATOM   11543 C  CA  . ALA   E 2 26  ? 18.929  -25.635 -65.348 1.00 127.79 ? 26   ALA   E CA  1 
ATOM   11544 C  C   . ALA   E 2 26  ? 20.091  -25.025 -66.143 1.00 131.41 ? 26   ALA   E C   1 
ATOM   11545 O  O   . ALA   E 2 26  ? 21.162  -25.650 -66.220 1.00 121.74 ? 26   ALA   E O   1 
ATOM   11546 C  CB  . ALA   E 2 26  ? 18.344  -26.836 -66.097 1.00 118.96 ? 26   ALA   E CB  1 
ATOM   11547 N  N   . GLU   E 2 27  ? 19.913  -23.822 -66.708 1.00 142.29 ? 27   GLU   E N   1 
ATOM   11548 C  CA  . GLU   E 2 27  ? 20.925  -23.126 -67.504 1.00 142.02 ? 27   GLU   E CA  1 
ATOM   11549 C  C   . GLU   E 2 27  ? 21.512  -21.906 -66.795 1.00 143.06 ? 27   GLU   E C   1 
ATOM   11550 O  O   . GLU   E 2 27  ? 22.148  -21.065 -67.447 1.00 145.30 ? 27   GLU   E O   1 
ATOM   11551 C  CB  . GLU   E 2 27  ? 20.335  -22.695 -68.847 1.00 143.83 ? 27   GLU   E CB  1 
ATOM   11552 C  CG  . GLU   E 2 27  ? 19.220  -21.660 -68.730 1.00 147.11 ? 27   GLU   E CG  1 
ATOM   11553 C  CD  . GLU   E 2 27  ? 17.825  -22.274 -68.799 1.00 153.60 ? 27   GLU   E CD  1 
ATOM   11554 O  OE1 . GLU   E 2 27  ? 17.714  -23.524 -68.788 1.00 156.03 ? 27   GLU   E OE1 1 
ATOM   11555 O  OE2 . GLU   E 2 27  ? 16.839  -21.501 -68.860 1.00 154.95 ? 27   GLU   E OE2 1 
ATOM   11556 N  N   . ASP   E 2 28  ? 21.296  -21.779 -65.486 1.00 133.13 ? 28   ASP   E N   1 
ATOM   11557 C  CA  . ASP   E 2 28  ? 21.889  -20.744 -64.652 1.00 119.99 ? 28   ASP   E CA  1 
ATOM   11558 C  C   . ASP   E 2 28  ? 22.989  -21.355 -63.789 1.00 110.02 ? 28   ASP   E C   1 
ATOM   11559 O  O   . ASP   E 2 28  ? 22.857  -22.487 -63.313 1.00 109.59 ? 28   ASP   E O   1 
ATOM   11560 C  CB  . ASP   E 2 28  ? 20.823  -20.099 -63.747 1.00 117.73 ? 28   ASP   E CB  1 
ATOM   11561 C  CG  . ASP   E 2 28  ? 19.848  -19.212 -64.514 1.00 118.92 ? 28   ASP   E CG  1 
ATOM   11562 O  OD1 . ASP   E 2 28  ? 20.081  -18.993 -65.720 1.00 127.80 ? 28   ASP   E OD1 1 
ATOM   11563 O  OD2 . ASP   E 2 28  ? 18.858  -18.726 -63.908 1.00 111.53 ? 28   ASP   E OD2 1 
ATOM   11564 N  N   . LEU   E 2 29  ? 24.075  -20.607 -63.587 1.00 106.96 ? 29   LEU   E N   1 
ATOM   11565 C  CA  . LEU   E 2 29  ? 25.082  -20.955 -62.585 1.00 102.95 ? 29   LEU   E CA  1 
ATOM   11566 C  C   . LEU   E 2 29  ? 24.752  -20.214 -61.295 1.00 104.61 ? 29   LEU   E C   1 
ATOM   11567 O  O   . LEU   E 2 29  ? 24.999  -19.011 -61.165 1.00 104.44 ? 29   LEU   E O   1 
ATOM   11568 C  CB  . LEU   E 2 29  ? 26.492  -20.611 -63.051 1.00 99.25  ? 29   LEU   E CB  1 
ATOM   11569 C  CG  . LEU   E 2 29  ? 27.463  -21.166 -62.019 1.00 97.28  ? 29   LEU   E CG  1 
ATOM   11570 C  CD1 . LEU   E 2 29  ? 27.180  -22.662 -61.821 1.00 97.18  ? 29   LEU   E CD1 1 
ATOM   11571 C  CD2 . LEU   E 2 29  ? 28.908  -20.886 -62.412 1.00 98.47  ? 29   LEU   E CD2 1 
ATOM   11572 N  N   . ASN   E 2 30  ? 24.190  -20.933 -60.334 1.00 105.24 ? 30   ASN   E N   1 
ATOM   11573 C  CA  . ASN   E 2 30  ? 23.791  -20.331 -59.078 1.00 100.93 ? 30   ASN   E CA  1 
ATOM   11574 C  C   . ASN   E 2 30  ? 24.900  -20.468 -58.055 1.00 97.71  ? 30   ASN   E C   1 
ATOM   11575 O  O   . ASN   E 2 30  ? 25.593  -21.487 -58.003 1.00 97.47  ? 30   ASN   E O   1 
ATOM   11576 C  CB  . ASN   E 2 30  ? 22.514  -20.978 -58.551 1.00 101.29 ? 30   ASN   E CB  1 
ATOM   11577 C  CG  . ASN   E 2 30  ? 21.295  -20.572 -59.349 1.00 105.09 ? 30   ASN   E CG  1 
ATOM   11578 O  OD1 . ASN   E 2 30  ? 20.490  -21.417 -59.745 1.00 104.75 ? 30   ASN   E OD1 1 
ATOM   11579 N  ND2 . ASN   E 2 30  ? 21.154  -19.266 -59.594 1.00 103.44 ? 30   ASN   E ND2 1 
ATOM   11580 N  N   . LEU   E 2 31  ? 25.079  -19.426 -57.259 1.00 96.58  ? 31   LEU   E N   1 
ATOM   11581 C  CA  . LEU   E 2 31  ? 25.861  -19.512 -56.037 1.00 93.84  ? 31   LEU   E CA  1 
ATOM   11582 C  C   . LEU   E 2 31  ? 24.890  -19.353 -54.875 1.00 92.12  ? 31   LEU   E C   1 
ATOM   11583 O  O   . LEU   E 2 31  ? 24.154  -18.366 -54.815 1.00 95.14  ? 31   LEU   E O   1 
ATOM   11584 C  CB  . LEU   E 2 31  ? 26.967  -18.457 -56.008 1.00 92.55  ? 31   LEU   E CB  1 
ATOM   11585 C  CG  . LEU   E 2 31  ? 27.940  -18.572 -54.828 1.00 90.72  ? 31   LEU   E CG  1 
ATOM   11586 C  CD1 . LEU   E 2 31  ? 28.394  -20.010 -54.652 1.00 91.32  ? 31   LEU   E CD1 1 
ATOM   11587 C  CD2 . LEU   E 2 31  ? 29.143  -17.622 -54.946 1.00 91.12  ? 31   LEU   E CD2 1 
ATOM   11588 N  N   . LEU   E 2 32  ? 24.848  -20.343 -53.993 1.00 88.21  ? 32   LEU   E N   1 
ATOM   11589 C  CA  . LEU   E 2 32  ? 23.947  -20.338 -52.847 1.00 87.78  ? 32   LEU   E CA  1 
ATOM   11590 C  C   . LEU   E 2 32  ? 24.772  -20.144 -51.588 1.00 90.43  ? 32   LEU   E C   1 
ATOM   11591 O  O   . LEU   E 2 32  ? 25.567  -21.016 -51.230 1.00 95.93  ? 32   LEU   E O   1 
ATOM   11592 C  CB  . LEU   E 2 32  ? 23.170  -21.642 -52.768 1.00 86.69  ? 32   LEU   E CB  1 
ATOM   11593 C  CG  . LEU   E 2 32  ? 21.716  -21.550 -53.177 1.00 88.85  ? 32   LEU   E CG  1 
ATOM   11594 C  CD1 . LEU   E 2 32  ? 21.632  -21.268 -54.658 1.00 97.37  ? 32   LEU   E CD1 1 
ATOM   11595 C  CD2 . LEU   E 2 32  ? 21.038  -22.840 -52.793 1.00 85.91  ? 32   LEU   E CD2 1 
ATOM   11596 N  N   . ILE   E 2 33  ? 24.585  -19.027 -50.892 1.00 90.33  ? 33   ILE   E N   1 
ATOM   11597 C  CA  . ILE   E 2 33  ? 25.323  -18.774 -49.663 1.00 91.58  ? 33   ILE   E CA  1 
ATOM   11598 C  C   . ILE   E 2 33  ? 24.376  -18.900 -48.474 1.00 91.75  ? 33   ILE   E C   1 
ATOM   11599 O  O   . ILE   E 2 33  ? 23.235  -18.408 -48.513 1.00 87.97  ? 33   ILE   E O   1 
ATOM   11600 C  CB  . ILE   E 2 33  ? 26.035  -17.413 -49.687 1.00 89.16  ? 33   ILE   E CB  1 
ATOM   11601 C  CG1 . ILE   E 2 33  ? 27.087  -17.421 -50.777 1.00 89.85  ? 33   ILE   E CG1 1 
ATOM   11602 C  CG2 . ILE   E 2 33  ? 26.738  -17.147 -48.381 1.00 86.32  ? 33   ILE   E CG2 1 
ATOM   11603 C  CD1 . ILE   E 2 33  ? 27.597  -16.054 -51.065 1.00 94.32  ? 33   ILE   E CD1 1 
ATOM   11604 N  N   . ALA   E 2 34  ? 24.853  -19.597 -47.439 1.00 91.36  ? 34   ALA   E N   1 
ATOM   11605 C  CA  . ALA   E 2 34  ? 24.203  -19.728 -46.143 1.00 87.43  ? 34   ALA   E CA  1 
ATOM   11606 C  C   . ALA   E 2 34  ? 24.975  -18.900 -45.121 1.00 89.15  ? 34   ALA   E C   1 
ATOM   11607 O  O   . ALA   E 2 34  ? 26.193  -19.082 -44.980 1.00 89.25  ? 34   ALA   E O   1 
ATOM   11608 C  CB  . ALA   E 2 34  ? 24.157  -21.186 -45.694 1.00 81.08  ? 34   ALA   E CB  1 
ATOM   11609 N  N   . LYS   E 2 35  ? 24.235  -18.053 -44.405 1.00 88.80  ? 35   LYS   E N   1 
ATOM   11610 C  CA  . LYS   E 2 35  ? 24.817  -17.237 -43.318 1.00 87.37  ? 35   LYS   E CA  1 
ATOM   11611 C  C   . LYS   E 2 35  ? 23.942  -17.484 -42.085 1.00 85.42  ? 35   LYS   E C   1 
ATOM   11612 O  O   . LYS   E 2 35  ? 23.092  -16.624 -41.792 1.00 85.50  ? 35   LYS   E O   1 
ATOM   11613 C  CB  . LYS   E 2 35  ? 24.823  -15.772 -43.751 1.00 87.21  ? 35   LYS   E CB  1 
ATOM   11614 C  CG  . LYS   E 2 35  ? 25.604  -15.465 -45.015 1.00 83.76  ? 35   LYS   E CG  1 
ATOM   11615 C  CD  . LYS   E 2 35  ? 26.325  -14.127 -44.926 1.00 85.61  ? 35   LYS   E CD  1 
ATOM   11616 C  CE  . LYS   E 2 35  ? 25.887  -13.173 -45.988 1.00 89.97  ? 35   LYS   E CE  1 
ATOM   11617 N  NZ  . LYS   E 2 35  ? 26.294  -13.628 -47.319 1.00 92.39  ? 35   LYS   E NZ  1 
ATOM   11618 N  N   . ASN   E 2 36  ? 24.087  -18.650 -41.455 1.00 84.60  ? 36   ASN   E N   1 
ATOM   11619 C  CA  . ASN   E 2 36  ? 23.315  -19.007 -40.232 1.00 85.73  ? 36   ASN   E CA  1 
ATOM   11620 C  C   . ASN   E 2 36  ? 21.824  -19.157 -40.533 1.00 85.58  ? 36   ASN   E C   1 
ATOM   11621 O  O   . ASN   E 2 36  ? 21.406  -20.282 -40.847 1.00 86.69  ? 36   ASN   E O   1 
ATOM   11622 C  CB  . ASN   E 2 36  ? 23.523  -18.011 -39.101 1.00 88.02  ? 36   ASN   E CB  1 
ATOM   11623 C  CG  . ASN   E 2 36  ? 23.183  -18.633 -37.773 1.00 85.98  ? 36   ASN   E CG  1 
ATOM   11624 O  OD1 . ASN   E 2 36  ? 23.315  -19.850 -37.623 1.00 85.29  ? 36   ASN   E OD1 1 
ATOM   11625 N  ND2 . ASN   E 2 36  ? 22.739  -17.835 -36.815 1.00 87.04  ? 36   ASN   E ND2 1 
ATOM   11626 N  N   . THR   E 2 37  ? 21.052  -18.079 -40.408 1.00 88.77  ? 37   THR   E N   1 
ATOM   11627 C  CA  . THR   E 2 37  ? 19.587  -18.178 -40.575 1.00 88.17  ? 37   THR   E CA  1 
ATOM   11628 C  C   . THR   E 2 37  ? 19.193  -17.709 -41.950 1.00 95.38  ? 37   THR   E C   1 
ATOM   11629 O  O   . THR   E 2 37  ? 18.007  -17.858 -42.300 1.00 96.12  ? 37   THR   E O   1 
ATOM   11630 C  CB  . THR   E 2 37  ? 18.917  -17.323 -39.506 1.00 85.93  ? 37   THR   E CB  1 
ATOM   11631 O  OG1 . THR   E 2 37  ? 19.269  -15.986 -39.841 1.00 84.40  ? 37   THR   E OG1 1 
ATOM   11632 C  CG2 . THR   E 2 37  ? 19.404  -17.654 -38.107 1.00 91.87  ? 37   THR   E CG2 1 
ATOM   11633 N  N   . ARG   E 2 38  ? 20.137  -17.158 -42.710 1.00 98.65  ? 38   ARG   E N   1 
ATOM   11634 C  CA  . ARG   E 2 38  ? 19.779  -16.580 -44.027 1.00 98.63  ? 38   ARG   E CA  1 
ATOM   11635 C  C   . ARG   E 2 38  ? 20.365  -17.418 -45.163 1.00 99.34  ? 38   ARG   E C   1 
ATOM   11636 O  O   . ARG   E 2 38  ? 21.425  -18.032 -44.956 1.00 99.69  ? 38   ARG   E O   1 
ATOM   11637 C  CB  . ARG   E 2 38  ? 20.288  -15.141 -44.145 1.00 99.85  ? 38   ARG   E CB  1 
ATOM   11638 C  CG  . ARG   E 2 38  ? 19.629  -14.154 -43.194 1.00 101.62 ? 38   ARG   E CG  1 
ATOM   11639 C  CD  . ARG   E 2 38  ? 20.137  -12.742 -43.426 1.00 104.42 ? 38   ARG   E CD  1 
ATOM   11640 N  NE  . ARG   E 2 38  ? 19.534  -11.772 -42.506 1.00 107.72 ? 38   ARG   E NE  1 
ATOM   11641 C  CZ  . ARG   E 2 38  ? 18.352  -11.206 -42.694 1.00 108.07 ? 38   ARG   E CZ  1 
ATOM   11642 N  NH1 . ARG   E 2 38  ? 17.701  -11.399 -43.826 1.00 108.18 ? 38   ARG   E NH1 1 
ATOM   11643 N  NH2 . ARG   E 2 38  ? 17.825  -10.452 -41.747 1.00 107.14 ? 38   ARG   E NH2 1 
ATOM   11644 N  N   . LEU   E 2 39  ? 19.704  -17.419 -46.316 1.00 97.72  ? 39   LEU   E N   1 
ATOM   11645 C  CA  . LEU   E 2 39  ? 20.155  -18.155 -47.480 1.00 92.23  ? 39   LEU   E CA  1 
ATOM   11646 C  C   . LEU   E 2 39  ? 20.172  -17.185 -48.636 1.00 94.61  ? 39   LEU   E C   1 
ATOM   11647 O  O   . LEU   E 2 39  ? 19.122  -16.654 -49.005 1.00 98.69  ? 39   LEU   E O   1 
ATOM   11648 C  CB  . LEU   E 2 39  ? 19.229  -19.324 -47.778 1.00 92.16  ? 39   LEU   E CB  1 
ATOM   11649 C  CG  . LEU   E 2 39  ? 19.420  -19.859 -49.185 1.00 92.70  ? 39   LEU   E CG  1 
ATOM   11650 C  CD1 . LEU   E 2 39  ? 20.822  -20.406 -49.390 1.00 92.73  ? 39   LEU   E CD1 1 
ATOM   11651 C  CD2 . LEU   E 2 39  ? 18.396  -20.911 -49.426 1.00 91.71  ? 39   LEU   E CD2 1 
ATOM   11652 N  N   . GLU   E 2 40  ? 21.353  -16.940 -49.189 1.00 94.25  ? 40   GLU   E N   1 
ATOM   11653 C  CA  . GLU   E 2 40  ? 21.495  -16.032 -50.319 1.00 96.41  ? 40   GLU   E CA  1 
ATOM   11654 C  C   . GLU   E 2 40  ? 21.589  -16.837 -51.604 1.00 99.81  ? 40   GLU   E C   1 
ATOM   11655 O  O   . GLU   E 2 40  ? 22.287  -17.854 -51.657 1.00 97.79  ? 40   GLU   E O   1 
ATOM   11656 C  CB  . GLU   E 2 40  ? 22.726  -15.149 -50.156 1.00 95.53  ? 40   GLU   E CB  1 
ATOM   11657 C  CG  . GLU   E 2 40  ? 22.807  -14.594 -48.773 1.00 97.54  ? 40   GLU   E CG  1 
ATOM   11658 C  CD  . GLU   E 2 40  ? 23.214  -13.145 -48.756 1.00 98.88  ? 40   GLU   E CD  1 
ATOM   11659 O  OE1 . GLU   E 2 40  ? 23.758  -12.698 -49.788 1.00 107.41 ? 40   GLU   E OE1 1 
ATOM   11660 O  OE2 . GLU   E 2 40  ? 22.986  -12.463 -47.721 1.00 96.74  ? 40   GLU   E OE2 1 
ATOM   11661 N  N   . ILE   E 2 41  ? 20.851  -16.393 -52.628 1.00 98.11  ? 41   ILE   E N   1 
ATOM   11662 C  CA  . ILE   E 2 41  ? 20.820  -17.039 -53.939 1.00 96.63  ? 41   ILE   E CA  1 
ATOM   11663 C  C   . ILE   E 2 41  ? 21.347  -16.060 -54.970 1.00 100.60 ? 41   ILE   E C   1 
ATOM   11664 O  O   . ILE   E 2 41  ? 20.806  -14.955 -55.119 1.00 102.49 ? 41   ILE   E O   1 
ATOM   11665 C  CB  . ILE   E 2 41  ? 19.412  -17.489 -54.338 1.00 94.60  ? 41   ILE   E CB  1 
ATOM   11666 C  CG1 . ILE   E 2 41  ? 18.927  -18.599 -53.412 1.00 96.60  ? 41   ILE   E CG1 1 
ATOM   11667 C  CG2 . ILE   E 2 41  ? 19.440  -17.929 -55.774 1.00 96.76  ? 41   ILE   E CG2 1 
ATOM   11668 C  CD1 . ILE   E 2 41  ? 17.436  -18.578 -53.178 1.00 99.30  ? 41   ILE   E CD1 1 
ATOM   11669 N  N   . TYR   E 2 42  ? 22.373  -16.472 -55.702 1.00 99.83  ? 42   TYR   E N   1 
ATOM   11670 C  CA  . TYR   E 2 42  ? 23.006  -15.629 -56.698 1.00 99.68  ? 42   TYR   E CA  1 
ATOM   11671 C  C   . TYR   E 2 42  ? 23.035  -16.366 -58.029 1.00 99.05  ? 42   TYR   E C   1 
ATOM   11672 O  O   . TYR   E 2 42  ? 22.997  -17.599 -58.075 1.00 97.44  ? 42   TYR   E O   1 
ATOM   11673 C  CB  . TYR   E 2 42  ? 24.437  -15.223 -56.258 1.00 97.16  ? 42   TYR   E CB  1 
ATOM   11674 C  CG  . TYR   E 2 42  ? 24.474  -14.119 -55.222 1.00 93.33  ? 42   TYR   E CG  1 
ATOM   11675 C  CD1 . TYR   E 2 42  ? 24.222  -14.381 -53.879 1.00 94.01  ? 42   TYR   E CD1 1 
ATOM   11676 C  CD2 . TYR   E 2 42  ? 24.745  -12.811 -55.590 1.00 99.78  ? 42   TYR   E CD2 1 
ATOM   11677 C  CE1 . TYR   E 2 42  ? 24.238  -13.362 -52.922 1.00 98.67  ? 42   TYR   E CE1 1 
ATOM   11678 C  CE2 . TYR   E 2 42  ? 24.766  -11.781 -54.645 1.00 99.20  ? 42   TYR   E CE2 1 
ATOM   11679 C  CZ  . TYR   E 2 42  ? 24.513  -12.064 -53.317 1.00 97.12  ? 42   TYR   E CZ  1 
ATOM   11680 O  OH  . TYR   E 2 42  ? 24.537  -11.033 -52.407 1.00 97.33  ? 42   TYR   E OH  1 
ATOM   11681 N  N   . VAL   E 2 43  ? 23.061  -15.597 -59.110 1.00 101.34 ? 43   VAL   E N   1 
ATOM   11682 C  CA  . VAL   E 2 43  ? 23.381  -16.115 -60.433 1.00 101.83 ? 43   VAL   E CA  1 
ATOM   11683 C  C   . VAL   E 2 43  ? 24.786  -15.658 -60.791 1.00 102.36 ? 43   VAL   E C   1 
ATOM   11684 O  O   . VAL   E 2 43  ? 25.102  -14.460 -60.730 1.00 102.26 ? 43   VAL   E O   1 
ATOM   11685 C  CB  . VAL   E 2 43  ? 22.367  -15.652 -61.492 1.00 101.18 ? 43   VAL   E CB  1 
ATOM   11686 C  CG1 . VAL   E 2 43  ? 22.919  -15.941 -62.873 1.00 103.02 ? 43   VAL   E CG1 1 
ATOM   11687 C  CG2 . VAL   E 2 43  ? 21.060  -16.375 -61.320 1.00 102.13 ? 43   VAL   E CG2 1 
ATOM   11688 N  N   . VAL   E 2 44  ? 25.634  -16.609 -61.158 1.00 100.49 ? 44   VAL   E N   1 
ATOM   11689 C  CA  . VAL   E 2 44  ? 27.021  -16.300 -61.486 1.00 101.45 ? 44   VAL   E CA  1 
ATOM   11690 C  C   . VAL   E 2 44  ? 27.062  -15.681 -62.876 1.00 108.27 ? 44   VAL   E C   1 
ATOM   11691 O  O   . VAL   E 2 44  ? 27.068  -16.393 -63.886 1.00 112.12 ? 44   VAL   E O   1 
ATOM   11692 C  CB  . VAL   E 2 44  ? 27.906  -17.556 -61.399 1.00 98.24  ? 44   VAL   E CB  1 
ATOM   11693 C  CG1 . VAL   E 2 44  ? 29.350  -17.236 -61.777 1.00 94.86  ? 44   VAL   E CG1 1 
ATOM   11694 C  CG2 . VAL   E 2 44  ? 27.840  -18.137 -60.000 1.00 101.12 ? 44   VAL   E CG2 1 
ATOM   11695 N  N   . THR   E 2 45  ? 27.065  -14.352 -62.944 1.00 108.77 ? 45   THR   E N   1 
ATOM   11696 C  CA  . THR   E 2 45  ? 27.226  -13.717 -64.241 1.00 111.27 ? 45   THR   E CA  1 
ATOM   11697 C  C   . THR   E 2 45  ? 28.691  -13.758 -64.662 1.00 115.73 ? 45   THR   E C   1 
ATOM   11698 O  O   . THR   E 2 45  ? 29.591  -13.973 -63.845 1.00 118.00 ? 45   THR   E O   1 
ATOM   11699 C  CB  . THR   E 2 45  ? 26.722  -12.283 -64.210 1.00 111.18 ? 45   THR   E CB  1 
ATOM   11700 O  OG1 . THR   E 2 45  ? 27.680  -11.449 -63.547 1.00 116.38 ? 45   THR   E OG1 1 
ATOM   11701 C  CG2 . THR   E 2 45  ? 25.399  -12.225 -63.471 1.00 109.71 ? 45   THR   E CG2 1 
ATOM   11702 N  N   . ALA   E 2 46  ? 28.916  -13.574 -65.965 1.00 118.76 ? 46   ALA   E N   1 
ATOM   11703 C  CA  . ALA   E 2 46  ? 30.281  -13.528 -66.481 1.00 121.79 ? 46   ALA   E CA  1 
ATOM   11704 C  C   . ALA   E 2 46  ? 31.079  -12.411 -65.815 1.00 126.05 ? 46   ALA   E C   1 
ATOM   11705 O  O   . ALA   E 2 46  ? 32.235  -12.620 -65.411 1.00 129.95 ? 46   ALA   E O   1 
ATOM   11706 C  CB  . ALA   E 2 46  ? 30.252  -13.349 -67.999 1.00 122.32 ? 46   ALA   E CB  1 
ATOM   11707 N  N   . GLU   E 2 47  ? 30.457  -11.234 -65.644 1.00 127.27 ? 47   GLU   E N   1 
ATOM   11708 C  CA  . GLU   E 2 47  ? 31.109  -10.107 -64.975 1.00 124.53 ? 47   GLU   E CA  1 
ATOM   11709 C  C   . GLU   E 2 47  ? 31.312  -10.382 -63.482 1.00 125.43 ? 47   GLU   E C   1 
ATOM   11710 O  O   . GLU   E 2 47  ? 32.426  -10.233 -62.960 1.00 125.72 ? 47   GLU   E O   1 
ATOM   11711 C  CB  . GLU   E 2 47  ? 30.293  -8.828  -65.183 1.00 123.70 ? 47   GLU   E CB  1 
ATOM   11712 N  N   . GLY   E 2 48  ? 30.247  -10.773 -62.776 1.00 121.73 ? 48   GLY   E N   1 
ATOM   11713 C  CA  . GLY   E 2 48  ? 30.329  -11.054 -61.356 1.00 115.06 ? 48   GLY   E CA  1 
ATOM   11714 C  C   . GLY   E 2 48  ? 29.135  -11.851 -60.859 1.00 108.01 ? 48   GLY   E C   1 
ATOM   11715 O  O   . GLY   E 2 48  ? 28.942  -12.994 -61.268 1.00 107.44 ? 48   GLY   E O   1 
ATOM   11716 N  N   . LEU   E 2 49  ? 28.317  -11.256 -60.001 1.00 106.72 ? 49   LEU   E N   1 
ATOM   11717 C  CA  . LEU   E 2 49  ? 27.218  -11.972 -59.369 1.00 105.23 ? 49   LEU   E CA  1 
ATOM   11718 C  C   . LEU   E 2 49  ? 25.958  -11.121 -59.353 1.00 104.88 ? 49   LEU   E C   1 
ATOM   11719 O  O   . LEU   E 2 49  ? 26.005  -9.948  -58.970 1.00 106.13 ? 49   LEU   E O   1 
ATOM   11720 C  CB  . LEU   E 2 49  ? 27.597  -12.345 -57.928 1.00 100.38 ? 49   LEU   E CB  1 
ATOM   11721 C  CG  . LEU   E 2 49  ? 28.451  -13.587 -57.732 1.00 92.83  ? 49   LEU   E CG  1 
ATOM   11722 C  CD1 . LEU   E 2 49  ? 28.939  -13.656 -56.321 1.00 89.63  ? 49   LEU   E CD1 1 
ATOM   11723 C  CD2 . LEU   E 2 49  ? 27.621  -14.789 -58.035 1.00 100.00 ? 49   LEU   E CD2 1 
ATOM   11724 N  N   . ARG   E 2 50  ? 24.833  -11.721 -59.736 1.00 103.26 ? 50   ARG   E N   1 
ATOM   11725 C  CA  . ARG   E 2 50  ? 23.554  -11.021 -59.763 1.00 100.13 ? 50   ARG   E CA  1 
ATOM   11726 C  C   . ARG   E 2 50  ? 22.655  -11.556 -58.665 1.00 100.47 ? 50   ARG   E C   1 
ATOM   11727 O  O   . ARG   E 2 50  ? 22.367  -12.763 -58.647 1.00 103.53 ? 50   ARG   E O   1 
ATOM   11728 C  CB  . ARG   E 2 50  ? 22.886  -11.186 -61.133 1.00 103.43 ? 50   ARG   E CB  1 
ATOM   11729 C  CG  . ARG   E 2 50  ? 21.441  -10.706 -61.228 1.00 101.11 ? 50   ARG   E CG  1 
ATOM   11730 C  CD  . ARG   E 2 50  ? 20.948  -10.710 -62.677 1.00 102.07 ? 50   ARG   E CD  1 
ATOM   11731 N  NE  . ARG   E 2 50  ? 20.995  -12.031 -63.304 1.00 103.14 ? 50   ARG   E NE  1 
ATOM   11732 C  CZ  . ARG   E 2 50  ? 19.966  -12.869 -63.390 1.00 104.84 ? 50   ARG   E CZ  1 
ATOM   11733 N  NH1 . ARG   E 2 50  ? 18.778  -12.573 -62.879 1.00 100.49 ? 50   ARG   E NH1 1 
ATOM   11734 N  NH2 . ARG   E 2 50  ? 20.130  -14.035 -64.011 1.00 108.17 ? 50   ARG   E NH2 1 
ATOM   11735 N  N   . PRO   E 2 51  ? 22.203  -10.704 -57.741 1.00 99.57  ? 51   PRO   E N   1 
ATOM   11736 C  CA  . PRO   E 2 51  ? 21.243  -11.144 -56.718 1.00 99.05  ? 51   PRO   E CA  1 
ATOM   11737 C  C   . PRO   E 2 51  ? 19.986  -11.750 -57.328 1.00 104.84 ? 51   PRO   E C   1 
ATOM   11738 O  O   . PRO   E 2 51  ? 19.532  -11.361 -58.409 1.00 108.41 ? 51   PRO   E O   1 
ATOM   11739 C  CB  . PRO   E 2 51  ? 20.910  -9.847  -55.970 1.00 91.52  ? 51   PRO   E CB  1 
ATOM   11740 C  CG  . PRO   E 2 51  ? 22.138  -9.043  -56.106 1.00 99.59  ? 51   PRO   E CG  1 
ATOM   11741 C  CD  . PRO   E 2 51  ? 22.672  -9.334  -57.490 1.00 101.69 ? 51   PRO   E CD  1 
ATOM   11742 N  N   . VAL   E 2 52  ? 19.412  -12.706 -56.607 1.00 101.90 ? 52   VAL   E N   1 
ATOM   11743 C  CA  . VAL   E 2 52  ? 18.277  -13.458 -57.116 1.00 101.35 ? 52   VAL   E CA  1 
ATOM   11744 C  C   . VAL   E 2 52  ? 17.178  -13.518 -56.068 1.00 102.89 ? 52   VAL   E C   1 
ATOM   11745 O  O   . VAL   E 2 52  ? 16.008  -13.245 -56.372 1.00 100.71 ? 52   VAL   E O   1 
ATOM   11746 C  CB  . VAL   E 2 52  ? 18.718  -14.866 -57.539 1.00 107.28 ? 52   VAL   E CB  1 
ATOM   11747 C  CG1 . VAL   E 2 52  ? 17.504  -15.725 -57.866 1.00 112.79 ? 52   VAL   E CG1 1 
ATOM   11748 C  CG2 . VAL   E 2 52  ? 19.664  -14.754 -58.724 1.00 106.32 ? 52   VAL   E CG2 1 
ATOM   11749 N  N   . LYS   E 2 53  ? 17.552  -13.876 -54.839 1.00 104.14 ? 53   LYS   E N   1 
ATOM   11750 C  CA  . LYS   E 2 53  ? 16.667  -13.953 -53.677 1.00 106.43 ? 53   LYS   E CA  1 
ATOM   11751 C  C   . LYS   E 2 53  ? 17.521  -14.153 -52.432 1.00 103.78 ? 53   LYS   E C   1 
ATOM   11752 O  O   . LYS   E 2 53  ? 18.619  -14.712 -52.506 1.00 103.06 ? 53   LYS   E O   1 
ATOM   11753 C  CB  . LYS   E 2 53  ? 15.653  -15.102 -53.817 1.00 108.93 ? 53   LYS   E CB  1 
ATOM   11754 C  CG  . LYS   E 2 53  ? 14.618  -15.234 -52.700 1.00 106.41 ? 53   LYS   E CG  1 
ATOM   11755 C  CD  . LYS   E 2 53  ? 13.244  -14.651 -53.070 1.00 112.48 ? 53   LYS   E CD  1 
ATOM   11756 C  CE  . LYS   E 2 53  ? 12.144  -15.348 -52.264 1.00 116.49 ? 53   LYS   E CE  1 
ATOM   11757 N  NZ  . LYS   E 2 53  ? 10.839  -14.634 -52.253 1.00 122.10 ? 53   LYS   E NZ  1 
ATOM   11758 N  N   . GLU   E 2 54  ? 17.018  -13.677 -51.296 1.00 107.81 ? 54   GLU   E N   1 
ATOM   11759 C  CA  . GLU   E 2 54  ? 17.554  -14.063 -50.000 1.00 108.98 ? 54   GLU   E CA  1 
ATOM   11760 C  C   . GLU   E 2 54  ? 16.388  -14.397 -49.084 1.00 109.82 ? 54   GLU   E C   1 
ATOM   11761 O  O   . GLU   E 2 54  ? 15.561  -13.531 -48.781 1.00 112.58 ? 54   GLU   E O   1 
ATOM   11762 C  CB  . GLU   E 2 54  ? 18.421  -12.959 -49.390 1.00 107.11 ? 54   GLU   E CB  1 
ATOM   11763 C  CG  . GLU   E 2 54  ? 18.773  -13.266 -47.969 1.00 104.83 ? 54   GLU   E CG  1 
ATOM   11764 C  CD  . GLU   E 2 54  ? 18.821  -12.029 -47.126 1.00 111.68 ? 54   GLU   E CD  1 
ATOM   11765 O  OE1 . GLU   E 2 54  ? 19.554  -11.085 -47.502 1.00 114.91 ? 54   GLU   E OE1 1 
ATOM   11766 O  OE2 . GLU   E 2 54  ? 18.109  -11.991 -46.099 1.00 113.25 ? 54   GLU   E OE2 1 
ATOM   11767 N  N   . VAL   E 2 55  ? 16.303  -15.651 -48.672 1.00 102.40 ? 55   VAL   E N   1 
ATOM   11768 C  CA  . VAL   E 2 55  ? 15.229  -16.100 -47.825 1.00 100.32 ? 55   VAL   E CA  1 
ATOM   11769 C  C   . VAL   E 2 55  ? 15.727  -16.164 -46.389 1.00 105.87 ? 55   VAL   E C   1 
ATOM   11770 O  O   . VAL   E 2 55  ? 16.915  -16.024 -46.111 1.00 109.22 ? 55   VAL   E O   1 
ATOM   11771 C  CB  . VAL   E 2 55  ? 14.699  -17.460 -48.265 1.00 99.03  ? 55   VAL   E CB  1 
ATOM   11772 C  CG1 . VAL   E 2 55  ? 14.341  -17.407 -49.712 1.00 109.90 ? 55   VAL   E CG1 1 
ATOM   11773 C  CG2 . VAL   E 2 55  ? 15.759  -18.505 -48.010 1.00 96.31  ? 55   VAL   E CG2 1 
ATOM   11774 N  N   . GLY   E 2 56  ? 14.811  -16.411 -45.463 1.00 106.85 ? 56   GLY   E N   1 
ATOM   11775 C  CA  . GLY   E 2 56  ? 15.171  -16.525 -44.068 1.00 104.83 ? 56   GLY   E CA  1 
ATOM   11776 C  C   . GLY   E 2 56  ? 14.466  -17.700 -43.439 1.00 105.33 ? 56   GLY   E C   1 
ATOM   11777 O  O   . GLY   E 2 56  ? 13.230  -17.799 -43.482 1.00 104.54 ? 56   GLY   E O   1 
ATOM   11778 N  N   . MET   E 2 57  ? 15.251  -18.588 -42.843 1.00 105.08 ? 57   MET   E N   1 
ATOM   11779 C  CA  . MET   E 2 57  ? 14.755  -19.837 -42.286 1.00 105.64 ? 57   MET   E CA  1 
ATOM   11780 C  C   . MET   E 2 57  ? 14.556  -19.732 -40.777 1.00 102.58 ? 57   MET   E C   1 
ATOM   11781 O  O   . MET   E 2 57  ? 15.278  -18.999 -40.094 1.00 99.90  ? 57   MET   E O   1 
ATOM   11782 C  CB  . MET   E 2 57  ? 15.737  -20.965 -42.589 1.00 107.62 ? 57   MET   E CB  1 
ATOM   11783 C  CG  . MET   E 2 57  ? 16.054  -21.142 -44.043 1.00 106.63 ? 57   MET   E CG  1 
ATOM   11784 S  SD  . MET   E 2 57  ? 16.220  -22.902 -44.289 1.00 113.97 ? 57   MET   E SD  1 
ATOM   11785 C  CE  . MET   E 2 57  ? 14.707  -23.482 -43.493 1.00 108.51 ? 57   MET   E CE  1 
ATOM   11786 N  N   . TYR   E 2 58  ? 13.580  -20.487 -40.262 1.00 94.30  ? 58   TYR   E N   1 
ATOM   11787 C  CA  . TYR   E 2 58  ? 13.356  -20.613 -38.819 1.00 87.98  ? 58   TYR   E CA  1 
ATOM   11788 C  C   . TYR   E 2 58  ? 14.239  -21.703 -38.235 1.00 87.87  ? 58   TYR   E C   1 
ATOM   11789 O  O   . TYR   E 2 58  ? 13.787  -22.575 -37.502 1.00 91.54  ? 58   TYR   E O   1 
ATOM   11790 C  CB  . TYR   E 2 58  ? 11.891  -20.907 -38.526 1.00 92.05  ? 58   TYR   E CB  1 
ATOM   11791 C  CG  . TYR   E 2 58  ? 10.944  -19.759 -38.772 1.00 94.87  ? 58   TYR   E CG  1 
ATOM   11792 C  CD1 . TYR   E 2 58  ? 10.559  -19.411 -40.064 1.00 100.94 ? 58   TYR   E CD1 1 
ATOM   11793 C  CD2 . TYR   E 2 58  ? 10.409  -19.040 -37.716 1.00 94.56  ? 58   TYR   E CD2 1 
ATOM   11794 C  CE1 . TYR   E 2 58  ? 9.680   -18.360 -40.292 1.00 101.52 ? 58   TYR   E CE1 1 
ATOM   11795 C  CE2 . TYR   E 2 58  ? 9.534   -17.996 -37.931 1.00 94.85  ? 58   TYR   E CE2 1 
ATOM   11796 C  CZ  . TYR   E 2 58  ? 9.169   -17.657 -39.213 1.00 96.97  ? 58   TYR   E CZ  1 
ATOM   11797 O  OH  . TYR   E 2 58  ? 8.288   -16.606 -39.406 1.00 102.91 ? 58   TYR   E OH  1 
ATOM   11798 N  N   . GLY   E 2 59  ? 15.511  -21.676 -38.586 1.00 87.37  ? 59   GLY   E N   1 
ATOM   11799 C  CA  . GLY   E 2 59  ? 16.452  -22.645 -38.060 1.00 88.29  ? 59   GLY   E CA  1 
ATOM   11800 C  C   . GLY   E 2 59  ? 17.841  -22.193 -38.437 1.00 86.54  ? 59   GLY   E C   1 
ATOM   11801 O  O   . GLY   E 2 59  ? 18.021  -21.291 -39.261 1.00 84.04  ? 59   GLY   E O   1 
ATOM   11802 N  N   . LYS   E 2 60  ? 18.832  -22.815 -37.813 1.00 86.30  ? 60   LYS   E N   1 
ATOM   11803 C  CA  . LYS   E 2 60  ? 20.207  -22.587 -38.230 1.00 85.39  ? 60   LYS   E CA  1 
ATOM   11804 C  C   . LYS   E 2 60  ? 20.530  -23.598 -39.325 1.00 84.51  ? 60   LYS   E C   1 
ATOM   11805 O  O   . LYS   E 2 60  ? 20.474  -24.810 -39.089 1.00 83.37  ? 60   LYS   E O   1 
ATOM   11806 C  CB  . LYS   E 2 60  ? 21.170  -22.682 -37.045 1.00 81.06  ? 60   LYS   E CB  1 
ATOM   11807 C  CG  . LYS   E 2 60  ? 21.053  -21.522 -36.088 1.00 77.27  ? 60   LYS   E CG  1 
ATOM   11808 C  CD  . LYS   E 2 60  ? 21.872  -21.773 -34.854 1.00 82.16  ? 60   LYS   E CD  1 
ATOM   11809 C  CE  . LYS   E 2 60  ? 23.359  -21.778 -35.166 1.00 84.64  ? 60   LYS   E CE  1 
ATOM   11810 N  NZ  . LYS   E 2 60  ? 23.946  -20.394 -35.186 1.00 82.76  ? 60   LYS   E NZ  1 
ATOM   11811 N  N   . ILE   E 2 61  ? 20.801  -23.098 -40.535 1.00 84.36  ? 61   ILE   E N   1 
ATOM   11812 C  CA  . ILE   E 2 61  ? 21.165  -23.936 -41.670 1.00 82.55  ? 61   ILE   E CA  1 
ATOM   11813 C  C   . ILE   E 2 61  ? 22.367  -24.690 -41.138 1.00 84.60  ? 61   ILE   E C   1 
ATOM   11814 O  O   . ILE   E 2 61  ? 23.400  -24.082 -40.841 1.00 84.95  ? 61   ILE   E O   1 
ATOM   11815 C  CB  . ILE   E 2 61  ? 21.435  -23.108 -42.940 1.00 83.41  ? 61   ILE   E CB  1 
ATOM   11816 C  CG1 . ILE   E 2 61  ? 20.232  -22.224 -43.285 1.00 86.57  ? 61   ILE   E CG1 1 
ATOM   11817 C  CG2 . ILE   E 2 61  ? 21.710  -24.021 -44.097 1.00 87.74  ? 61   ILE   E CG2 1 
ATOM   11818 C  CD1 . ILE   E 2 61  ? 20.521  -21.142 -44.295 1.00 84.25  ? 61   ILE   E CD1 1 
ATOM   11819 N  N   . ALA   E 2 62  ? 22.219  -26.004 -40.964 1.00 86.01  ? 62   ALA   E N   1 
ATOM   11820 C  CA  . ALA   E 2 62  ? 23.288  -26.856 -40.456 1.00 84.03  ? 62   ALA   E CA  1 
ATOM   11821 C  C   . ALA   E 2 62  ? 23.815  -27.704 -41.589 1.00 85.78  ? 62   ALA   E C   1 
ATOM   11822 O  O   . ALA   E 2 62  ? 25.003  -28.039 -41.600 1.00 85.29  ? 62   ALA   E O   1 
ATOM   11823 C  CB  . ALA   E 2 62  ? 22.830  -27.785 -39.335 1.00 82.99  ? 62   ALA   E CB  1 
ATOM   11824 N  N   . VAL   E 2 63  ? 22.944  -28.057 -42.527 1.00 90.72  ? 63   VAL   E N   1 
ATOM   11825 C  CA  . VAL   E 2 63  ? 23.312  -28.742 -43.758 1.00 92.05  ? 63   VAL   E CA  1 
ATOM   11826 C  C   . VAL   E 2 63  ? 22.642  -28.008 -44.919 1.00 92.20  ? 63   VAL   E C   1 
ATOM   11827 O  O   . VAL   E 2 63  ? 21.521  -27.498 -44.785 1.00 89.83  ? 63   VAL   E O   1 
ATOM   11828 C  CB  . VAL   E 2 63  ? 22.904  -30.232 -43.728 1.00 90.94  ? 63   VAL   E CB  1 
ATOM   11829 C  CG1 . VAL   E 2 63  ? 23.310  -30.917 -45.005 1.00 95.56  ? 63   VAL   E CG1 1 
ATOM   11830 C  CG2 . VAL   E 2 63  ? 23.538  -30.925 -42.557 1.00 89.44  ? 63   VAL   E CG2 1 
ATOM   11831 N  N   . MET   E 2 64  ? 23.343  -27.933 -46.051 1.00 89.28  ? 64   MET   E N   1 
ATOM   11832 C  CA  . MET   E 2 64  ? 22.808  -27.283 -47.242 1.00 91.10  ? 64   MET   E CA  1 
ATOM   11833 C  C   . MET   E 2 64  ? 23.496  -27.902 -48.444 1.00 95.46  ? 64   MET   E C   1 
ATOM   11834 O  O   . MET   E 2 64  ? 24.695  -27.684 -48.655 1.00 93.67  ? 64   MET   E O   1 
ATOM   11835 C  CB  . MET   E 2 64  ? 23.025  -25.777 -47.211 1.00 91.61  ? 64   MET   E CB  1 
ATOM   11836 C  CG  . MET   E 2 64  ? 22.519  -25.064 -48.446 1.00 88.39  ? 64   MET   E CG  1 
ATOM   11837 S  SD  . MET   E 2 64  ? 23.154  -23.391 -48.565 1.00 83.33  ? 64   MET   E SD  1 
ATOM   11838 C  CE  . MET   E 2 64  ? 24.906  -23.652 -48.791 1.00 88.40  ? 64   MET   E CE  1 
ATOM   11839 N  N   . GLU   E 2 65  ? 22.728  -28.658 -49.225 1.00 102.92 ? 65   GLU   E N   1 
ATOM   11840 C  CA  . GLU   E 2 65  ? 23.260  -29.378 -50.366 1.00 104.71 ? 65   GLU   E CA  1 
ATOM   11841 C  C   . GLU   E 2 65  ? 22.262  -29.327 -51.506 1.00 103.90 ? 65   GLU   E C   1 
ATOM   11842 O  O   . GLU   E 2 65  ? 21.052  -29.449 -51.287 1.00 103.30 ? 65   GLU   E O   1 
ATOM   11843 C  CB  . GLU   E 2 65  ? 23.588  -30.827 -49.999 1.00 106.33 ? 65   GLU   E CB  1 
ATOM   11844 C  CG  . GLU   E 2 65  ? 24.946  -30.996 -49.340 1.00 107.57 ? 65   GLU   E CG  1 
ATOM   11845 C  CD  . GLU   E 2 65  ? 26.047  -30.258 -50.087 1.00 116.30 ? 65   GLU   E CD  1 
ATOM   11846 O  OE1 . GLU   E 2 65  ? 26.005  -30.211 -51.346 1.00 113.26 ? 65   GLU   E OE1 1 
ATOM   11847 O  OE2 . GLU   E 2 65  ? 26.957  -29.717 -49.412 1.00 120.46 ? 65   GLU   E OE2 1 
ATOM   11848 N  N   . LEU   E 2 66  ? 22.785  -29.114 -52.712 1.00 102.15 ? 66   LEU   E N   1 
ATOM   11849 C  CA  . LEU   E 2 66  ? 22.012  -29.180 -53.944 1.00 102.12 ? 66   LEU   E CA  1 
ATOM   11850 C  C   . LEU   E 2 66  ? 22.057  -30.590 -54.529 1.00 102.89 ? 66   LEU   E C   1 
ATOM   11851 O  O   . LEU   E 2 66  ? 23.021  -31.331 -54.324 1.00 101.64 ? 66   LEU   E O   1 
ATOM   11852 C  CB  . LEU   E 2 66  ? 22.550  -28.178 -54.966 1.00 99.07  ? 66   LEU   E CB  1 
ATOM   11853 C  CG  . LEU   E 2 66  ? 22.065  -26.748 -54.804 1.00 95.16  ? 66   LEU   E CG  1 
ATOM   11854 C  CD1 . LEU   E 2 66  ? 22.646  -25.901 -55.907 1.00 94.95  ? 66   LEU   E CD1 1 
ATOM   11855 C  CD2 . LEU   E 2 66  ? 20.555  -26.718 -54.842 1.00 98.45  ? 66   LEU   E CD2 1 
ATOM   11856 N  N   . PHE   E 2 67  ? 20.995  -30.951 -55.255 1.00 108.90 ? 67   PHE   E N   1 
ATOM   11857 C  CA  . PHE   E 2 67  ? 20.894  -32.236 -55.938 1.00 107.51 ? 67   PHE   E CA  1 
ATOM   11858 C  C   . PHE   E 2 67  ? 19.745  -32.167 -56.933 1.00 109.44 ? 67   PHE   E C   1 
ATOM   11859 O  O   . PHE   E 2 67  ? 18.809  -31.381 -56.762 1.00 106.87 ? 67   PHE   E O   1 
ATOM   11860 C  CB  . PHE   E 2 67  ? 20.684  -33.392 -54.953 1.00 104.30 ? 67   PHE   E CB  1 
ATOM   11861 C  CG  . PHE   E 2 67  ? 19.363  -33.362 -54.249 1.00 100.68 ? 67   PHE   E CG  1 
ATOM   11862 C  CD1 . PHE   E 2 67  ? 19.111  -32.415 -53.286 1.00 100.16 ? 67   PHE   E CD1 1 
ATOM   11863 C  CD2 . PHE   E 2 67  ? 18.385  -34.292 -54.540 1.00 104.39 ? 67   PHE   E CD2 1 
ATOM   11864 C  CE1 . PHE   E 2 67  ? 17.910  -32.382 -52.635 1.00 101.87 ? 67   PHE   E CE1 1 
ATOM   11865 C  CE2 . PHE   E 2 67  ? 17.182  -34.268 -53.894 1.00 99.41  ? 67   PHE   E CE2 1 
ATOM   11866 C  CZ  . PHE   E 2 67  ? 16.942  -33.316 -52.938 1.00 100.05 ? 67   PHE   E CZ  1 
ATOM   11867 N  N   . ARG   E 2 68  ? 19.832  -32.993 -57.979 1.00 119.85 ? 68   ARG   E N   1 
ATOM   11868 C  CA  . ARG   E 2 68  ? 18.781  -33.118 -58.995 1.00 123.06 ? 68   ARG   E CA  1 
ATOM   11869 C  C   . ARG   E 2 68  ? 18.373  -34.579 -59.139 1.00 123.47 ? 68   ARG   E C   1 
ATOM   11870 O  O   . ARG   E 2 68  ? 19.110  -35.370 -59.753 1.00 122.60 ? 68   ARG   E O   1 
ATOM   11871 C  CB  . ARG   E 2 68  ? 19.246  -32.560 -60.343 1.00 119.18 ? 68   ARG   E CB  1 
ATOM   11872 C  CG  . ARG   E 2 68  ? 18.142  -32.477 -61.379 1.00 122.03 ? 68   ARG   E CG  1 
ATOM   11873 C  CD  . ARG   E 2 68  ? 18.620  -31.923 -62.707 1.00 120.84 ? 68   ARG   E CD  1 
ATOM   11874 N  NE  . ARG   E 2 68  ? 19.256  -30.618 -62.589 1.00 119.19 ? 68   ARG   E NE  1 
ATOM   11875 C  CZ  . ARG   E 2 68  ? 19.215  -29.686 -63.533 1.00 118.08 ? 68   ARG   E CZ  1 
ATOM   11876 N  NH1 . ARG   E 2 68  ? 18.507  -29.853 -64.639 1.00 122.98 ? 68   ARG   E NH1 1 
ATOM   11877 N  NH2 . ARG   E 2 68  ? 19.890  -28.553 -63.360 1.00 118.21 ? 68   ARG   E NH2 1 
ATOM   11878 N  N   . PRO   E 2 69  ? 17.215  -34.990 -58.598 1.00 126.18 ? 69   PRO   E N   1 
ATOM   11879 C  CA  . PRO   E 2 69  ? 16.821  -36.404 -58.643 1.00 125.61 ? 69   PRO   E CA  1 
ATOM   11880 C  C   . PRO   E 2 69  ? 16.608  -36.883 -60.070 1.00 133.86 ? 69   PRO   E C   1 
ATOM   11881 O  O   . PRO   E 2 69  ? 16.560  -36.100 -61.026 1.00 134.51 ? 69   PRO   E O   1 
ATOM   11882 C  CB  . PRO   E 2 69  ? 15.510  -36.440 -57.849 1.00 123.82 ? 69   PRO   E CB  1 
ATOM   11883 C  CG  . PRO   E 2 69  ? 15.520  -35.207 -57.033 1.00 123.25 ? 69   PRO   E CG  1 
ATOM   11884 C  CD  . PRO   E 2 69  ? 16.253  -34.183 -57.829 1.00 125.52 ? 69   PRO   E CD  1 
ATOM   11885 N  N   . LYS   E 2 70  ? 16.478  -38.207 -60.198 1.00 143.27 ? 70   LYS   E N   1 
ATOM   11886 C  CA  . LYS   E 2 70  ? 16.241  -38.841 -61.491 1.00 143.30 ? 70   LYS   E CA  1 
ATOM   11887 C  C   . LYS   E 2 70  ? 15.003  -38.255 -62.163 1.00 139.97 ? 70   LYS   E C   1 
ATOM   11888 O  O   . LYS   E 2 70  ? 13.898  -38.298 -61.607 1.00 137.63 ? 70   LYS   E O   1 
ATOM   11889 C  CB  . LYS   E 2 70  ? 16.086  -40.357 -61.310 1.00 141.15 ? 70   LYS   E CB  1 
ATOM   11890 N  N   . GLY   E 2 71  ? 15.194  -37.702 -63.363 1.00 138.80 ? 71   GLY   E N   1 
ATOM   11891 C  CA  . GLY   E 2 71  ? 14.125  -37.002 -64.046 1.00 134.76 ? 71   GLY   E CA  1 
ATOM   11892 C  C   . GLY   E 2 71  ? 13.580  -35.766 -63.358 1.00 136.31 ? 71   GLY   E C   1 
ATOM   11893 O  O   . GLY   E 2 71  ? 12.417  -35.747 -62.937 1.00 133.83 ? 71   GLY   E O   1 
ATOM   11894 N  N   . GLU   E 2 72  ? 14.416  -34.735 -63.230 1.00 133.32 ? 72   GLU   E N   1 
ATOM   11895 C  CA  . GLU   E 2 72  ? 14.032  -33.467 -62.621 1.00 132.42 ? 72   GLU   E CA  1 
ATOM   11896 C  C   . GLU   E 2 72  ? 14.510  -32.283 -63.452 1.00 130.67 ? 72   GLU   E C   1 
ATOM   11897 O  O   . GLU   E 2 72  ? 15.661  -32.262 -63.893 1.00 132.45 ? 72   GLU   E O   1 
ATOM   11898 C  CB  . GLU   E 2 72  ? 14.641  -33.433 -61.215 1.00 132.12 ? 72   GLU   E CB  1 
ATOM   11899 C  CG  . GLU   E 2 72  ? 13.807  -34.164 -60.193 1.00 133.85 ? 72   GLU   E CG  1 
ATOM   11900 C  CD  . GLU   E 2 72  ? 12.436  -33.539 -60.039 1.00 139.29 ? 72   GLU   E CD  1 
ATOM   11901 O  OE1 . GLU   E 2 72  ? 12.344  -32.425 -59.460 1.00 138.07 ? 72   GLU   E OE1 1 
ATOM   11902 O  OE2 . GLU   E 2 72  ? 11.453  -34.153 -60.520 1.00 145.66 ? 72   GLU   E OE2 1 
ATOM   11903 N  N   . SER   E 2 73  ? 13.622  -31.299 -63.662 1.00 125.06 ? 73   SER   E N   1 
ATOM   11904 C  CA  . SER   E 2 73  ? 13.923  -30.210 -64.594 1.00 121.01 ? 73   SER   E CA  1 
ATOM   11905 C  C   . SER   E 2 73  ? 15.155  -29.417 -64.159 1.00 122.41 ? 73   SER   E C   1 
ATOM   11906 O  O   . SER   E 2 73  ? 16.014  -29.099 -64.994 1.00 120.97 ? 73   SER   E O   1 
ATOM   11907 C  CB  . SER   E 2 73  ? 12.695  -29.295 -64.777 1.00 119.51 ? 73   SER   E CB  1 
ATOM   11908 O  OG  . SER   E 2 73  ? 12.391  -28.456 -63.670 1.00 120.65 ? 73   SER   E OG  1 
ATOM   11909 N  N   . LYS   E 2 74  ? 15.274  -29.110 -62.857 1.00 124.09 ? 74   LYS   E N   1 
ATOM   11910 C  CA  . LYS   E 2 74  ? 16.399  -28.336 -62.322 1.00 120.96 ? 74   LYS   E CA  1 
ATOM   11911 C  C   . LYS   E 2 74  ? 16.791  -28.864 -60.935 1.00 118.23 ? 74   LYS   E C   1 
ATOM   11912 O  O   . LYS   E 2 74  ? 16.172  -29.789 -60.397 1.00 116.39 ? 74   LYS   E O   1 
ATOM   11913 C  CB  . LYS   E 2 74  ? 16.067  -26.834 -62.280 1.00 115.27 ? 74   LYS   E CB  1 
ATOM   11914 C  CG  . LYS   E 2 74  ? 14.911  -26.491 -61.366 1.00 114.02 ? 74   LYS   E CG  1 
ATOM   11915 C  CD  . LYS   E 2 74  ? 14.170  -25.264 -61.861 1.00 119.61 ? 74   LYS   E CD  1 
ATOM   11916 C  CE  . LYS   E 2 74  ? 12.858  -25.093 -61.102 1.00 125.84 ? 74   LYS   E CE  1 
ATOM   11917 N  NZ  . LYS   E 2 74  ? 12.054  -23.903 -61.516 1.00 124.12 ? 74   LYS   E NZ  1 
ATOM   11918 N  N   . ASP   E 2 75  ? 17.836  -28.259 -60.355 1.00 117.72 ? 75   ASP   E N   1 
ATOM   11919 C  CA  . ASP   E 2 75  ? 18.385  -28.719 -59.083 1.00 111.81 ? 75   ASP   E CA  1 
ATOM   11920 C  C   . ASP   E 2 75  ? 17.409  -28.452 -57.938 1.00 110.31 ? 75   ASP   E C   1 
ATOM   11921 O  O   . ASP   E 2 75  ? 16.594  -27.520 -57.984 1.00 109.77 ? 75   ASP   E O   1 
ATOM   11922 C  CB  . ASP   E 2 75  ? 19.732  -28.032 -58.777 1.00 106.14 ? 75   ASP   E CB  1 
ATOM   11923 C  CG  . ASP   E 2 75  ? 20.906  -28.570 -59.623 1.00 107.65 ? 75   ASP   E CG  1 
ATOM   11924 O  OD1 . ASP   E 2 75  ? 20.868  -29.740 -60.080 1.00 110.17 ? 75   ASP   E OD1 1 
ATOM   11925 O  OD2 . ASP   E 2 75  ? 21.893  -27.814 -59.798 1.00 104.73 ? 75   ASP   E OD2 1 
ATOM   11926 N  N   . LEU   E 2 76  ? 17.494  -29.304 -56.908 1.00 108.57 ? 76   LEU   E N   1 
ATOM   11927 C  CA  . LEU   E 2 76  ? 16.735  -29.164 -55.670 1.00 104.48 ? 76   LEU   E CA  1 
ATOM   11928 C  C   . LEU   E 2 76  ? 17.666  -28.932 -54.488 1.00 103.29 ? 76   LEU   E C   1 
ATOM   11929 O  O   . LEU   E 2 76  ? 18.815  -29.376 -54.488 1.00 104.04 ? 76   LEU   E O   1 
ATOM   11930 C  CB  . LEU   E 2 76  ? 15.894  -30.400 -55.386 1.00 100.65 ? 76   LEU   E CB  1 
ATOM   11931 C  CG  . LEU   E 2 76  ? 14.795  -30.572 -56.401 1.00 103.99 ? 76   LEU   E CG  1 
ATOM   11932 C  CD1 . LEU   E 2 76  ? 13.905  -31.680 -55.922 1.00 105.28 ? 76   LEU   E CD1 1 
ATOM   11933 C  CD2 . LEU   E 2 76  ? 14.050  -29.245 -56.535 1.00 110.30 ? 76   LEU   E CD2 1 
ATOM   11934 N  N   . LEU   E 2 77  ? 17.143  -28.285 -53.449 1.00 102.36 ? 77   LEU   E N   1 
ATOM   11935 C  CA  . LEU   E 2 77  ? 17.944  -27.867 -52.307 1.00 97.09  ? 77   LEU   E CA  1 
ATOM   11936 C  C   . LEU   E 2 77  ? 17.587  -28.686 -51.077 1.00 96.78  ? 77   LEU   E C   1 
ATOM   11937 O  O   . LEU   E 2 77  ? 16.425  -28.699 -50.661 1.00 96.70  ? 77   LEU   E O   1 
ATOM   11938 C  CB  . LEU   E 2 77  ? 17.715  -26.395 -52.020 1.00 94.59  ? 77   LEU   E CB  1 
ATOM   11939 C  CG  . LEU   E 2 77  ? 18.677  -25.890 -50.976 1.00 88.75  ? 77   LEU   E CG  1 
ATOM   11940 C  CD1 . LEU   E 2 77  ? 20.086  -26.172 -51.433 1.00 94.64  ? 77   LEU   E CD1 1 
ATOM   11941 C  CD2 . LEU   E 2 77  ? 18.460  -24.433 -50.809 1.00 86.43  ? 77   LEU   E CD2 1 
ATOM   11942 N  N   . PHE   E 2 78  ? 18.583  -29.343 -50.477 1.00 96.20  ? 78   PHE   E N   1 
ATOM   11943 C  CA  . PHE   E 2 78  ? 18.390  -29.986 -49.180 1.00 95.62  ? 78   PHE   E CA  1 
ATOM   11944 C  C   . PHE   E 2 78  ? 19.021  -29.159 -48.070 1.00 92.50  ? 78   PHE   E C   1 
ATOM   11945 O  O   . PHE   E 2 78  ? 20.186  -28.753 -48.175 1.00 90.68  ? 78   PHE   E O   1 
ATOM   11946 C  CB  . PHE   E 2 78  ? 18.952  -31.402 -49.105 1.00 92.05  ? 78   PHE   E CB  1 
ATOM   11947 C  CG  . PHE   E 2 78  ? 18.723  -32.035 -47.766 1.00 88.87  ? 78   PHE   E CG  1 
ATOM   11948 C  CD1 . PHE   E 2 78  ? 17.503  -32.618 -47.464 1.00 90.33  ? 78   PHE   E CD1 1 
ATOM   11949 C  CD2 . PHE   E 2 78  ? 19.697  -31.986 -46.787 1.00 86.96  ? 78   PHE   E CD2 1 
ATOM   11950 C  CE1 . PHE   E 2 78  ? 17.275  -33.178 -46.226 1.00 88.83  ? 78   PHE   E CE1 1 
ATOM   11951 C  CE2 . PHE   E 2 78  ? 19.472  -32.545 -45.542 1.00 87.51  ? 78   PHE   E CE2 1 
ATOM   11952 C  CZ  . PHE   E 2 78  ? 18.259  -33.144 -45.263 1.00 87.00  ? 78   PHE   E CZ  1 
ATOM   11953 N  N   . ILE   E 2 79  ? 18.258  -28.952 -46.999 1.00 90.54  ? 79   ILE   E N   1 
ATOM   11954 C  CA  . ILE   E 2 79  ? 18.658  -28.104 -45.888 1.00 88.44  ? 79   ILE   E CA  1 
ATOM   11955 C  C   . ILE   E 2 79  ? 18.216  -28.792 -44.602 1.00 91.40  ? 79   ILE   E C   1 
ATOM   11956 O  O   . ILE   E 2 79  ? 17.037  -29.132 -44.442 1.00 92.87  ? 79   ILE   E O   1 
ATOM   11957 C  CB  . ILE   E 2 79  ? 18.061  -26.692 -45.983 1.00 85.23  ? 79   ILE   E CB  1 
ATOM   11958 C  CG1 . ILE   E 2 79  ? 18.894  -25.815 -46.920 1.00 86.34  ? 79   ILE   E CG1 1 
ATOM   11959 C  CG2 . ILE   E 2 79  ? 18.012  -26.058 -44.640 1.00 88.66  ? 79   ILE   E CG2 1 
ATOM   11960 C  CD1 . ILE   E 2 79  ? 18.286  -24.461 -47.163 1.00 84.61  ? 79   ILE   E CD1 1 
ATOM   11961 N  N   . LEU   E 2 80  ? 19.165  -29.034 -43.707 1.00 90.67  ? 80   LEU   E N   1 
ATOM   11962 C  CA  . LEU   E 2 80  ? 18.902  -29.644 -42.413 1.00 86.06  ? 80   LEU   E CA  1 
ATOM   11963 C  C   . LEU   E 2 80  ? 19.282  -28.617 -41.362 1.00 87.28  ? 80   LEU   E C   1 
ATOM   11964 O  O   . LEU   E 2 80  ? 20.452  -28.243 -41.263 1.00 86.74  ? 80   LEU   E O   1 
ATOM   11965 C  CB  . LEU   E 2 80  ? 19.702  -30.924 -42.240 1.00 82.29  ? 80   LEU   E CB  1 
ATOM   11966 C  CG  . LEU   E 2 80  ? 19.490  -31.514 -40.861 1.00 85.65  ? 80   LEU   E CG  1 
ATOM   11967 C  CD1 . LEU   E 2 80  ? 18.028  -31.738 -40.610 1.00 88.28  ? 80   LEU   E CD1 1 
ATOM   11968 C  CD2 . LEU   E 2 80  ? 20.232  -32.806 -40.744 1.00 88.84  ? 80   LEU   E CD2 1 
ATOM   11969 N  N   . THR   E 2 81  ? 18.299  -28.147 -40.593 1.00 87.78  ? 81   THR   E N   1 
ATOM   11970 C  CA  . THR   E 2 81  ? 18.561  -27.079 -39.640 1.00 85.18  ? 81   THR   E CA  1 
ATOM   11971 C  C   . THR   E 2 81  ? 19.173  -27.650 -38.368 1.00 87.04  ? 81   THR   E C   1 
ATOM   11972 O  O   . THR   E 2 81  ? 19.108  -28.854 -38.109 1.00 87.33  ? 81   THR   E O   1 
ATOM   11973 C  CB  . THR   E 2 81  ? 17.282  -26.308 -39.280 1.00 86.53  ? 81   THR   E CB  1 
ATOM   11974 O  OG1 . THR   E 2 81  ? 16.471  -27.099 -38.409 1.00 87.62  ? 81   THR   E OG1 1 
ATOM   11975 C  CG2 . THR   E 2 81  ? 16.481  -25.959 -40.511 1.00 86.42  ? 81   THR   E CG2 1 
ATOM   11976 N  N   . ALA   E 2 82  ? 19.767  -26.755 -37.564 1.00 87.63  ? 82   ALA   E N   1 
ATOM   11977 C  CA  . ALA   E 2 82  ? 20.372  -27.170 -36.297 1.00 85.26  ? 82   ALA   E CA  1 
ATOM   11978 C  C   . ALA   E 2 82  ? 19.373  -27.883 -35.383 1.00 88.22  ? 82   ALA   E C   1 
ATOM   11979 O  O   . ALA   E 2 82  ? 19.748  -28.832 -34.686 1.00 89.46  ? 82   ALA   E O   1 
ATOM   11980 C  CB  . ALA   E 2 82  ? 20.979  -25.959 -35.583 1.00 83.60  ? 82   ALA   E CB  1 
ATOM   11981 N  N   . LYS   E 2 83  ? 18.097  -27.451 -35.370 1.00 90.18  ? 83   LYS   E N   1 
ATOM   11982 C  CA  . LYS   E 2 83  ? 17.021  -28.109 -34.612 1.00 88.29  ? 83   LYS   E CA  1 
ATOM   11983 C  C   . LYS   E 2 83  ? 16.643  -29.454 -35.161 1.00 89.59  ? 83   LYS   E C   1 
ATOM   11984 O  O   . LYS   E 2 83  ? 15.693  -30.027 -34.646 1.00 91.48  ? 83   LYS   E O   1 
ATOM   11985 C  CB  . LYS   E 2 83  ? 15.789  -27.211 -34.540 1.00 89.21  ? 83   LYS   E CB  1 
ATOM   11986 C  CG  . LYS   E 2 83  ? 16.002  -25.907 -33.823 1.00 92.56  ? 83   LYS   E CG  1 
ATOM   11987 C  CD  . LYS   E 2 83  ? 15.462  -25.930 -32.402 1.00 89.01  ? 83   LYS   E CD  1 
ATOM   11988 C  CE  . LYS   E 2 83  ? 15.444  -24.525 -31.822 1.00 84.96  ? 83   LYS   E CE  1 
ATOM   11989 N  NZ  . LYS   E 2 83  ? 14.279  -24.288 -30.935 1.00 86.51  ? 83   LYS   E NZ  1 
ATOM   11990 N  N   . TYR   E 2 84  ? 17.353  -29.936 -36.178 1.00 89.37  ? 84   TYR   E N   1 
ATOM   11991 C  CA  . TYR   E 2 84  ? 17.092  -31.199 -36.854 1.00 92.26  ? 84   TYR   E CA  1 
ATOM   11992 C  C   . TYR   E 2 84  ? 15.900  -31.095 -37.801 1.00 93.53  ? 84   TYR   E C   1 
ATOM   11993 O  O   . TYR   E 2 84  ? 15.282  -32.112 -38.143 1.00 96.82  ? 84   TYR   E O   1 
ATOM   11994 C  CB  . TYR   E 2 84  ? 16.910  -32.356 -35.864 1.00 98.44  ? 84   TYR   E CB  1 
ATOM   11995 C  CG  . TYR   E 2 84  ? 18.184  -32.693 -35.124 1.00 100.83 ? 84   TYR   E CG  1 
ATOM   11996 C  CD1 . TYR   E 2 84  ? 19.240  -33.320 -35.774 1.00 102.02 ? 84   TYR   E CD1 1 
ATOM   11997 C  CD2 . TYR   E 2 84  ? 18.347  -32.376 -33.783 1.00 106.66 ? 84   TYR   E CD2 1 
ATOM   11998 C  CE1 . TYR   E 2 84  ? 20.429  -33.636 -35.106 1.00 101.57 ? 84   TYR   E CE1 1 
ATOM   11999 C  CE2 . TYR   E 2 84  ? 19.544  -32.693 -33.098 1.00 107.46 ? 84   TYR   E CE2 1 
ATOM   12000 C  CZ  . TYR   E 2 84  ? 20.575  -33.325 -33.777 1.00 101.18 ? 84   TYR   E CZ  1 
ATOM   12001 O  OH  . TYR   E 2 84  ? 21.757  -33.651 -33.151 1.00 94.09  ? 84   TYR   E OH  1 
ATOM   12002 N  N   . ASN   E 2 85  ? 15.549  -29.887 -38.236 1.00 91.78  ? 85   ASN   E N   1 
ATOM   12003 C  CA  . ASN   E 2 85  ? 14.512  -29.736 -39.247 1.00 90.99  ? 85   ASN   E CA  1 
ATOM   12004 C  C   . ASN   E 2 85  ? 15.132  -30.005 -40.613 1.00 90.20  ? 85   ASN   E C   1 
ATOM   12005 O  O   . ASN   E 2 85  ? 16.166  -29.430 -40.958 1.00 89.02  ? 85   ASN   E O   1 
ATOM   12006 C  CB  . ASN   E 2 85  ? 13.883  -28.336 -39.206 1.00 87.62  ? 85   ASN   E CB  1 
ATOM   12007 C  CG  . ASN   E 2 85  ? 13.575  -27.859 -37.785 1.00 88.78  ? 85   ASN   E CG  1 
ATOM   12008 O  OD1 . ASN   E 2 85  ? 13.965  -26.747 -37.379 1.00 89.40  ? 85   ASN   E OD1 1 
ATOM   12009 N  ND2 . ASN   E 2 85  ? 12.878  -28.698 -37.023 1.00 84.12  ? 85   ASN   E ND2 1 
ATOM   12010 N  N   . ALA   E 2 86  ? 14.522  -30.897 -41.376 1.00 94.92  ? 86   ALA   E N   1 
ATOM   12011 C  CA  . ALA   E 2 86  ? 14.966  -31.172 -42.727 1.00 92.36  ? 86   ALA   E CA  1 
ATOM   12012 C  C   . ALA   E 2 86  ? 13.904  -30.701 -43.702 1.00 94.93  ? 86   ALA   E C   1 
ATOM   12013 O  O   . ALA   E 2 86  ? 12.711  -30.658 -43.386 1.00 93.02  ? 86   ALA   E O   1 
ATOM   12014 C  CB  . ALA   E 2 86  ? 15.249  -32.657 -42.937 1.00 93.24  ? 86   ALA   E CB  1 
ATOM   12015 N  N   . CYS   E 2 87  ? 14.359  -30.333 -44.891 1.00 95.22  ? 87   CYS   E N   1 
ATOM   12016 C  CA  . CYS   E 2 87  ? 13.458  -29.835 -45.917 1.00 100.72 ? 87   CYS   E CA  1 
ATOM   12017 C  C   . CYS   E 2 87  ? 14.127  -30.010 -47.272 1.00 99.85  ? 87   CYS   E C   1 
ATOM   12018 O  O   . CYS   E 2 87  ? 15.359  -30.054 -47.371 1.00 99.11  ? 87   CYS   E O   1 
ATOM   12019 C  CB  . CYS   E 2 87  ? 13.085  -28.359 -45.689 1.00 100.06 ? 87   CYS   E CB  1 
ATOM   12020 S  SG  . CYS   E 2 87  ? 14.485  -27.212 -45.728 1.00 99.64  ? 87   CYS   E SG  1 
ATOM   12021 N  N   . ILE   E 2 88  ? 13.300  -30.107 -48.311 1.00 97.99  ? 88   ILE   E N   1 
ATOM   12022 C  CA  . ILE   E 2 88  ? 13.762  -30.090 -49.690 1.00 99.43  ? 88   ILE   E CA  1 
ATOM   12023 C  C   . ILE   E 2 88  ? 13.006  -28.996 -50.426 1.00 102.90 ? 88   ILE   E C   1 
ATOM   12024 O  O   . ILE   E 2 88  ? 11.768  -28.989 -50.442 1.00 103.54 ? 88   ILE   E O   1 
ATOM   12025 C  CB  . ILE   E 2 88  ? 13.574  -31.445 -50.382 1.00 98.03  ? 88   ILE   E CB  1 
ATOM   12026 C  CG1 . ILE   E 2 88  ? 14.331  -32.523 -49.623 1.00 96.64  ? 88   ILE   E CG1 1 
ATOM   12027 C  CG2 . ILE   E 2 88  ? 14.079  -31.368 -51.806 1.00 96.20  ? 88   ILE   E CG2 1 
ATOM   12028 C  CD1 . ILE   E 2 88  ? 14.039  -33.896 -50.129 1.00 97.33  ? 88   ILE   E CD1 1 
ATOM   12029 N  N   . LEU   E 2 89  ? 13.760  -28.094 -51.057 1.00 105.47 ? 89   LEU   E N   1 
ATOM   12030 C  CA  . LEU   E 2 89  ? 13.259  -26.828 -51.569 1.00 105.92 ? 89   LEU   E CA  1 
ATOM   12031 C  C   . LEU   E 2 89  ? 13.444  -26.741 -53.078 1.00 108.23 ? 89   LEU   E C   1 
ATOM   12032 O  O   . LEU   E 2 89  ? 14.471  -27.183 -53.613 1.00 105.62 ? 89   LEU   E O   1 
ATOM   12033 C  CB  . LEU   E 2 89  ? 13.993  -25.671 -50.906 1.00 100.86 ? 89   LEU   E CB  1 
ATOM   12034 C  CG  . LEU   E 2 89  ? 14.191  -25.719 -49.402 1.00 96.19  ? 89   LEU   E CG  1 
ATOM   12035 C  CD1 . LEU   E 2 89  ? 15.061  -24.556 -49.072 1.00 92.28  ? 89   LEU   E CD1 1 
ATOM   12036 C  CD2 . LEU   E 2 89  ? 12.873  -25.598 -48.677 1.00 100.75 ? 89   LEU   E CD2 1 
ATOM   12037 N  N   . GLU   E 2 90  ? 12.456  -26.138 -53.753 1.00 112.97 ? 90   GLU   E N   1 
ATOM   12038 C  CA  . GLU   E 2 90  ? 12.528  -25.873 -55.184 1.00 117.34 ? 90   GLU   E CA  1 
ATOM   12039 C  C   . GLU   E 2 90  ? 12.313  -24.392 -55.456 1.00 116.79 ? 90   GLU   E C   1 
ATOM   12040 O  O   . GLU   E 2 90  ? 11.552  -23.723 -54.755 1.00 115.09 ? 90   GLU   E O   1 
ATOM   12041 C  CB  . GLU   E 2 90  ? 11.494  -26.680 -55.956 1.00 122.64 ? 90   GLU   E CB  1 
ATOM   12042 C  CG  . GLU   E 2 90  ? 11.538  -26.463 -57.450 1.00 127.21 ? 90   GLU   E CG  1 
ATOM   12043 C  CD  . GLU   E 2 90  ? 10.297  -26.998 -58.119 1.00 132.57 ? 90   GLU   E CD  1 
ATOM   12044 O  OE1 . GLU   E 2 90  ? 9.449   -27.565 -57.386 1.00 132.21 ? 90   GLU   E OE1 1 
ATOM   12045 O  OE2 . GLU   E 2 90  ? 10.175  -26.857 -59.361 1.00 137.40 ? 90   GLU   E OE2 1 
ATOM   12046 N  N   . TYR   E 2 91  ? 12.983  -23.889 -56.494 1.00 132.82 ? 91   TYR   E N   1 
ATOM   12047 C  CA  . TYR   E 2 91  ? 12.837  -22.505 -56.934 1.00 135.51 ? 91   TYR   E CA  1 
ATOM   12048 C  C   . TYR   E 2 91  ? 11.643  -22.391 -57.887 1.00 142.95 ? 91   TYR   E C   1 
ATOM   12049 O  O   . TYR   E 2 91  ? 11.594  -23.090 -58.910 1.00 143.33 ? 91   TYR   E O   1 
ATOM   12050 C  CB  . TYR   E 2 91  ? 14.126  -22.045 -57.615 1.00 132.10 ? 91   TYR   E CB  1 
ATOM   12051 C  CG  . TYR   E 2 91  ? 14.183  -20.579 -57.952 1.00 132.75 ? 91   TYR   E CG  1 
ATOM   12052 C  CD1 . TYR   E 2 91  ? 13.619  -20.093 -59.121 1.00 135.26 ? 91   TYR   E CD1 1 
ATOM   12053 C  CD2 . TYR   E 2 91  ? 14.814  -19.686 -57.102 1.00 132.64 ? 91   TYR   E CD2 1 
ATOM   12054 C  CE1 . TYR   E 2 91  ? 13.672  -18.762 -59.431 1.00 137.17 ? 91   TYR   E CE1 1 
ATOM   12055 C  CE2 . TYR   E 2 91  ? 14.873  -18.346 -57.400 1.00 134.41 ? 91   TYR   E CE2 1 
ATOM   12056 C  CZ  . TYR   E 2 91  ? 14.302  -17.890 -58.567 1.00 138.26 ? 91   TYR   E CZ  1 
ATOM   12057 O  OH  . TYR   E 2 91  ? 14.358  -16.550 -58.860 1.00 140.93 ? 91   TYR   E OH  1 
ATOM   12058 N  N   . LYS   E 2 92  ? 10.687  -21.508 -57.560 1.00 140.79 ? 92   LYS   E N   1 
ATOM   12059 C  CA  . LYS   E 2 92  ? 9.499   -21.278 -58.385 1.00 136.61 ? 92   LYS   E CA  1 
ATOM   12060 C  C   . LYS   E 2 92  ? 9.361   -19.788 -58.662 1.00 135.58 ? 92   LYS   E C   1 
ATOM   12061 O  O   . LYS   E 2 92  ? 9.156   -18.999 -57.736 1.00 135.97 ? 92   LYS   E O   1 
ATOM   12062 C  CB  . LYS   E 2 92  ? 8.231   -21.812 -57.712 1.00 129.87 ? 92   LYS   E CB  1 
ATOM   12063 N  N   . GLN   E 2 93  ? 9.447   -19.411 -59.935 1.00 140.05 ? 93   GLN   E N   1 
ATOM   12064 C  CA  . GLN   E 2 93  ? 9.420   -18.013 -60.347 1.00 144.57 ? 93   GLN   E CA  1 
ATOM   12065 C  C   . GLN   E 2 93  ? 8.227   -17.805 -61.282 1.00 149.80 ? 93   GLN   E C   1 
ATOM   12066 O  O   . GLN   E 2 93  ? 8.184   -18.382 -62.376 1.00 150.83 ? 93   GLN   E O   1 
ATOM   12067 C  CB  . GLN   E 2 93  ? 10.737  -17.618 -61.012 1.00 142.06 ? 93   GLN   E CB  1 
ATOM   12068 C  CG  . GLN   E 2 93  ? 10.841  -16.141 -61.339 1.00 140.18 ? 93   GLN   E CG  1 
ATOM   12069 C  CD  . GLN   E 2 93  ? 12.217  -15.773 -61.836 1.00 144.13 ? 93   GLN   E CD  1 
ATOM   12070 O  OE1 . GLN   E 2 93  ? 13.127  -16.604 -61.851 1.00 143.09 ? 93   GLN   E OE1 1 
ATOM   12071 N  NE2 . GLN   E 2 93  ? 12.383  -14.514 -62.236 1.00 146.84 ? 93   GLN   E NE2 1 
ATOM   12072 N  N   . SER   E 2 94  ? 7.266   -16.997 -60.845 1.00 151.66 ? 94   SER   E N   1 
ATOM   12073 C  CA  . SER   E 2 94  ? 6.057   -16.727 -61.613 1.00 150.26 ? 94   SER   E CA  1 
ATOM   12074 C  C   . SER   E 2 94  ? 6.063   -15.293 -62.134 1.00 155.55 ? 94   SER   E C   1 
ATOM   12075 O  O   . SER   E 2 94  ? 5.153   -14.495 -61.881 1.00 156.85 ? 94   SER   E O   1 
ATOM   12076 C  CB  . SER   E 2 94  ? 4.819   -16.989 -60.759 1.00 145.45 ? 94   SER   E CB  1 
ATOM   12077 O  OG  . SER   E 2 94  ? 4.303   -15.770 -60.246 1.00 146.69 ? 94   SER   E OG  1 
ATOM   12078 N  N   . GLY   E 2 95  ? 7.135   -14.974 -62.873 1.00 152.53 ? 95   GLY   E N   1 
ATOM   12079 C  CA  . GLY   E 2 95  ? 7.305   -13.655 -63.447 1.00 148.70 ? 95   GLY   E CA  1 
ATOM   12080 C  C   . GLY   E 2 95  ? 7.921   -12.644 -62.500 1.00 143.41 ? 95   GLY   E C   1 
ATOM   12081 O  O   . GLY   E 2 95  ? 9.046   -12.196 -62.726 1.00 142.44 ? 95   GLY   E O   1 
ATOM   12082 N  N   . GLU   E 2 96  ? 7.192   -12.243 -61.458 1.00 151.76 ? 96   GLU   E N   1 
ATOM   12083 C  CA  . GLU   E 2 96  ? 7.728   -11.347 -60.440 1.00 147.86 ? 96   GLU   E CA  1 
ATOM   12084 C  C   . GLU   E 2 96  ? 7.615   -11.907 -59.034 1.00 152.33 ? 96   GLU   E C   1 
ATOM   12085 O  O   . GLU   E 2 96  ? 8.167   -11.307 -58.105 1.00 147.01 ? 96   GLU   E O   1 
ATOM   12086 C  CB  . GLU   E 2 96  ? 7.018   -9.986  -60.486 1.00 137.77 ? 96   GLU   E CB  1 
ATOM   12087 N  N   . SER   E 2 97  ? 6.925   -13.031 -58.850 1.00 165.55 ? 97   SER   E N   1 
ATOM   12088 C  CA  . SER   E 2 97  ? 6.711   -13.652 -57.543 1.00 165.35 ? 97   SER   E CA  1 
ATOM   12089 C  C   . SER   E 2 97  ? 7.710   -14.790 -57.384 1.00 162.33 ? 97   SER   E C   1 
ATOM   12090 O  O   . SER   E 2 97  ? 7.445   -15.937 -57.751 1.00 161.99 ? 97   SER   E O   1 
ATOM   12091 C  CB  . SER   E 2 97  ? 5.274   -14.148 -57.407 1.00 167.85 ? 97   SER   E CB  1 
ATOM   12092 O  OG  . SER   E 2 97  ? 5.152   -15.055 -56.326 1.00 170.57 ? 97   SER   E OG  1 
ATOM   12093 N  N   . ILE   E 2 98  ? 8.869   -14.470 -56.828 1.00 143.50 ? 98   ILE   E N   1 
ATOM   12094 C  CA  . ILE   E 2 98  ? 9.840   -15.496 -56.476 1.00 135.69 ? 98   ILE   E CA  1 
ATOM   12095 C  C   . ILE   E 2 98  ? 9.419   -16.116 -55.161 1.00 134.76 ? 98   ILE   E C   1 
ATOM   12096 O  O   . ILE   E 2 98  ? 9.158   -15.405 -54.183 1.00 139.86 ? 98   ILE   E O   1 
ATOM   12097 C  CB  . ILE   E 2 98  ? 11.246  -14.904 -56.362 1.00 131.25 ? 98   ILE   E CB  1 
ATOM   12098 C  CG1 . ILE   E 2 98  ? 11.731  -14.416 -57.710 1.00 134.51 ? 98   ILE   E CG1 1 
ATOM   12099 C  CG2 . ILE   E 2 98  ? 12.194  -15.939 -55.819 1.00 130.42 ? 98   ILE   E CG2 1 
ATOM   12100 C  CD1 . ILE   E 2 98  ? 12.985  -13.596 -57.589 1.00 130.03 ? 98   ILE   E CD1 1 
ATOM   12101 N  N   . ASP   E 2 99  ? 9.372   -17.438 -55.122 1.00 129.88 ? 99   ASP   E N   1 
ATOM   12102 C  CA  . ASP   E 2 99  ? 9.043   -18.129 -53.887 1.00 128.34 ? 99   ASP   E CA  1 
ATOM   12103 C  C   . ASP   E 2 99  ? 9.790   -19.451 -53.851 1.00 125.22 ? 99   ASP   E C   1 
ATOM   12104 O  O   . ASP   E 2 99  ? 10.046  -20.067 -54.889 1.00 123.12 ? 99   ASP   E O   1 
ATOM   12105 C  CB  . ASP   E 2 99  ? 7.535   -18.351 -53.753 1.00 130.55 ? 99   ASP   E CB  1 
ATOM   12106 C  CG  . ASP   E 2 99  ? 6.821   -17.140 -53.204 1.00 139.24 ? 99   ASP   E CG  1 
ATOM   12107 O  OD1 . ASP   E 2 99  ? 7.279   -16.590 -52.169 1.00 143.65 ? 99   ASP   E OD1 1 
ATOM   12108 O  OD2 . ASP   E 2 99  ? 5.813   -16.730 -53.820 1.00 141.68 ? 99   ASP   E OD2 1 
ATOM   12109 N  N   . ILE   E 2 100 ? 10.144  -19.876 -52.641 1.00 122.57 ? 100  ILE   E N   1 
ATOM   12110 C  CA  . ILE   E 2 100 ? 10.833  -21.141 -52.433 1.00 114.68 ? 100  ILE   E CA  1 
ATOM   12111 C  C   . ILE   E 2 100 ? 9.846   -22.126 -51.830 1.00 110.50 ? 100  ILE   E C   1 
ATOM   12112 O  O   . ILE   E 2 100 ? 9.483   -22.025 -50.656 1.00 110.14 ? 100  ILE   E O   1 
ATOM   12113 C  CB  . ILE   E 2 100 ? 12.062  -20.982 -51.536 1.00 110.62 ? 100  ILE   E CB  1 
ATOM   12114 C  CG1 . ILE   E 2 100 ? 13.018  -19.939 -52.108 1.00 112.45 ? 100  ILE   E CG1 1 
ATOM   12115 C  CG2 . ILE   E 2 100 ? 12.765  -22.311 -51.448 1.00 108.89 ? 100  ILE   E CG2 1 
ATOM   12116 C  CD1 . ILE   E 2 100 ? 13.751  -20.411 -53.347 1.00 118.68 ? 100  ILE   E CD1 1 
ATOM   12117 N  N   . ILE   E 2 101 ? 9.440   -23.101 -52.620 1.00 108.78 ? 101  ILE   E N   1 
ATOM   12118 C  CA  . ILE   E 2 101 ? 8.432   -24.054 -52.185 1.00 107.66 ? 101  ILE   E CA  1 
ATOM   12119 C  C   . ILE   E 2 101 ? 9.090   -25.200 -51.431 1.00 109.41 ? 101  ILE   E C   1 
ATOM   12120 O  O   . ILE   E 2 101 ? 10.276  -25.498 -51.594 1.00 108.41 ? 101  ILE   E O   1 
ATOM   12121 C  CB  . ILE   E 2 101 ? 7.628   -24.556 -53.383 1.00 107.67 ? 101  ILE   E CB  1 
ATOM   12122 C  CG1 . ILE   E 2 101 ? 8.435   -25.591 -54.191 1.00 115.06 ? 101  ILE   E CG1 1 
ATOM   12123 C  CG2 . ILE   E 2 101 ? 7.300   -23.359 -54.243 1.00 108.93 ? 101  ILE   E CG2 1 
ATOM   12124 C  CD1 . ILE   E 2 101 ? 8.154   -27.088 -53.876 1.00 115.50 ? 101  ILE   E CD1 1 
ATOM   12125 N  N   . THR   E 2 102 ? 8.297   -25.856 -50.592 1.00 109.03 ? 102  THR   E N   1 
ATOM   12126 C  CA  . THR   E 2 102 ? 8.784   -26.916 -49.716 1.00 105.67 ? 102  THR   E CA  1 
ATOM   12127 C  C   . THR   E 2 102 ? 8.227   -28.226 -50.254 1.00 105.68 ? 102  THR   E C   1 
ATOM   12128 O  O   . THR   E 2 102 ? 7.141   -28.657 -49.867 1.00 107.81 ? 102  THR   E O   1 
ATOM   12129 C  CB  . THR   E 2 102 ? 8.373   -26.683 -48.248 1.00 104.65 ? 102  THR   E CB  1 
ATOM   12130 O  OG1 . THR   E 2 102 ? 8.365   -25.270 -47.953 1.00 104.60 ? 102  THR   E OG1 1 
ATOM   12131 C  CG2 . THR   E 2 102 ? 9.354   -27.400 -47.317 1.00 100.79 ? 102  THR   E CG2 1 
ATOM   12132 N  N   . ARG   E 2 103 ? 8.987   -28.861 -51.150 1.00 102.35 ? 103  ARG   E N   1 
ATOM   12133 C  CA  . ARG   E 2 103 ? 8.557   -30.132 -51.718 1.00 102.11 ? 103  ARG   E CA  1 
ATOM   12134 C  C   . ARG   E 2 103 ? 8.491   -31.241 -50.661 1.00 107.79 ? 103  ARG   E C   1 
ATOM   12135 O  O   . ARG   E 2 103 ? 7.668   -32.158 -50.779 1.00 112.50 ? 103  ARG   E O   1 
ATOM   12136 C  CB  . ARG   E 2 103 ? 9.494   -30.521 -52.860 1.00 101.22 ? 103  ARG   E CB  1 
ATOM   12137 N  N   . ALA   E 2 104 ? 9.332   -31.182 -49.629 1.00 105.85 ? 104  ALA   E N   1 
ATOM   12138 C  CA  . ALA   E 2 104 ? 9.274   -32.151 -48.539 1.00 105.97 ? 104  ALA   E CA  1 
ATOM   12139 C  C   . ALA   E 2 104 ? 9.865   -31.520 -47.289 1.00 106.12 ? 104  ALA   E C   1 
ATOM   12140 O  O   . ALA   E 2 104 ? 10.736  -30.651 -47.386 1.00 107.11 ? 104  ALA   E O   1 
ATOM   12141 C  CB  . ALA   E 2 104 ? 10.029  -33.441 -48.878 1.00 109.71 ? 104  ALA   E CB  1 
ATOM   12142 N  N   . HIS   E 2 105 ? 9.395   -31.958 -46.116 1.00 104.89 ? 105  HIS   E N   1 
ATOM   12143 C  CA  . HIS   E 2 105 ? 9.853   -31.389 -44.850 1.00 101.19 ? 105  HIS   E CA  1 
ATOM   12144 C  C   . HIS   E 2 105 ? 9.557   -32.353 -43.718 1.00 102.69 ? 105  HIS   E C   1 
ATOM   12145 O  O   . HIS   E 2 105 ? 8.527   -33.031 -43.709 1.00 105.45 ? 105  HIS   E O   1 
ATOM   12146 C  CB  . HIS   E 2 105 ? 9.204   -30.034 -44.528 1.00 100.55 ? 105  HIS   E CB  1 
ATOM   12147 C  CG  . HIS   E 2 105 ? 7.744   -30.106 -44.185 1.00 95.44  ? 105  HIS   E CG  1 
ATOM   12148 N  ND1 . HIS   E 2 105 ? 7.238   -29.624 -42.998 1.00 94.35  ? 105  HIS   E ND1 1 
ATOM   12149 C  CD2 . HIS   E 2 105 ? 6.679   -30.555 -44.893 1.00 99.11  ? 105  HIS   E CD2 1 
ATOM   12150 C  CE1 . HIS   E 2 105 ? 5.927   -29.782 -42.984 1.00 95.77  ? 105  HIS   E CE1 1 
ATOM   12151 N  NE2 . HIS   E 2 105 ? 5.562   -30.347 -44.121 1.00 97.52  ? 105  HIS   E NE2 1 
ATOM   12152 N  N   . GLY   E 2 106 ? 10.462  -32.381 -42.752 1.00 110.92 ? 106  GLY   E N   1 
ATOM   12153 C  CA  . GLY   E 2 106 ? 10.253  -33.187 -41.566 1.00 112.40 ? 106  GLY   E CA  1 
ATOM   12154 C  C   . GLY   E 2 106 ? 11.356  -32.931 -40.564 1.00 107.62 ? 106  GLY   E C   1 
ATOM   12155 O  O   . GLY   E 2 106 ? 12.322  -32.206 -40.829 1.00 106.54 ? 106  GLY   E O   1 
ATOM   12156 N  N   . ASN   E 2 107 ? 11.204  -33.554 -39.409 1.00 96.65  ? 107  ASN   E N   1 
ATOM   12157 C  CA  . ASN   E 2 107 ? 12.180  -33.439 -38.347 1.00 99.38  ? 107  ASN   E CA  1 
ATOM   12158 C  C   . ASN   E 2 107 ? 12.831  -34.792 -38.103 1.00 99.51  ? 107  ASN   E C   1 
ATOM   12159 O  O   . ASN   E 2 107 ? 12.151  -35.764 -37.757 1.00 102.21 ? 107  ASN   E O   1 
ATOM   12160 C  CB  . ASN   E 2 107 ? 11.529  -32.907 -37.082 1.00 100.95 ? 107  ASN   E CB  1 
ATOM   12161 C  CG  . ASN   E 2 107 ? 12.533  -32.441 -36.090 1.00 99.75  ? 107  ASN   E CG  1 
ATOM   12162 O  OD1 . ASN   E 2 107 ? 13.634  -32.992 -35.988 1.00 102.28 ? 107  ASN   E OD1 1 
ATOM   12163 N  ND2 . ASN   E 2 107 ? 12.174  -31.410 -35.347 1.00 98.89  ? 107  ASN   E ND2 1 
ATOM   12164 N  N   . VAL   E 2 108 ? 14.139  -34.846 -38.250 1.00 99.69  ? 108  VAL   E N   1 
ATOM   12165 C  CA  . VAL   E 2 108 ? 14.880  -36.081 -38.151 1.00 106.72 ? 108  VAL   E CA  1 
ATOM   12166 C  C   . VAL   E 2 108 ? 15.450  -36.289 -36.743 1.00 115.02 ? 108  VAL   E C   1 
ATOM   12167 O  O   . VAL   E 2 108 ? 16.384  -37.074 -36.561 1.00 115.17 ? 108  VAL   E O   1 
ATOM   12168 C  CB  . VAL   E 2 108 ? 15.990  -36.140 -39.208 1.00 105.21 ? 108  VAL   E CB  1 
ATOM   12169 C  CG1 . VAL   E 2 108 ? 15.400  -36.234 -40.590 1.00 98.62  ? 108  VAL   E CG1 1 
ATOM   12170 C  CG2 . VAL   E 2 108 ? 16.886  -34.915 -39.069 1.00 105.01 ? 108  VAL   E CG2 1 
ATOM   12171 N  N   . GLN   E 2 109 ? 14.909  -35.606 -35.747 1.00 135.81 ? 109  GLN   E N   1 
ATOM   12172 C  CA  . GLN   E 2 109 ? 15.399  -35.776 -34.384 1.00 137.11 ? 109  GLN   E CA  1 
ATOM   12173 C  C   . GLN   E 2 109 ? 15.043  -37.167 -33.867 1.00 140.51 ? 109  GLN   E C   1 
ATOM   12174 O  O   . GLN   E 2 109 ? 13.887  -37.589 -33.960 1.00 143.65 ? 109  GLN   E O   1 
ATOM   12175 C  CB  . GLN   E 2 109 ? 14.807  -34.703 -33.480 1.00 136.45 ? 109  GLN   E CB  1 
ATOM   12176 C  CG  . GLN   E 2 109 ? 15.062  -34.948 -32.022 1.00 142.65 ? 109  GLN   E CG  1 
ATOM   12177 C  CD  . GLN   E 2 109 ? 16.469  -34.571 -31.612 1.00 144.96 ? 109  GLN   E CD  1 
ATOM   12178 O  OE1 . GLN   E 2 109 ? 17.361  -35.427 -31.510 1.00 146.75 ? 109  GLN   E OE1 1 
ATOM   12179 N  NE2 . GLN   E 2 109 ? 16.675  -33.278 -31.357 1.00 142.09 ? 109  GLN   E NE2 1 
ATOM   12180 N  N   . ASP   E 2 110 ? 16.034  -37.891 -33.341 1.00 131.16 ? 110  ASP   E N   1 
ATOM   12181 C  CA  . ASP   E 2 110 ? 15.782  -39.168 -32.670 1.00 128.56 ? 110  ASP   E CA  1 
ATOM   12182 C  C   . ASP   E 2 110 ? 15.650  -38.915 -31.174 1.00 132.53 ? 110  ASP   E C   1 
ATOM   12183 O  O   . ASP   E 2 110 ? 16.305  -38.022 -30.632 1.00 132.36 ? 110  ASP   E O   1 
ATOM   12184 C  CB  . ASP   E 2 110 ? 16.908  -40.174 -32.947 1.00 123.49 ? 110  ASP   E CB  1 
ATOM   12185 C  CG  . ASP   E 2 110 ? 16.997  -40.562 -34.412 1.00 119.60 ? 110  ASP   E CG  1 
ATOM   12186 O  OD1 . ASP   E 2 110 ? 15.943  -40.581 -35.080 1.00 120.67 ? 110  ASP   E OD1 1 
ATOM   12187 O  OD2 . ASP   E 2 110 ? 18.115  -40.834 -34.903 1.00 116.69 ? 110  ASP   E OD2 1 
ATOM   12188 N  N   . ARG   E 2 111 ? 14.788  -39.699 -30.511 1.00 134.41 ? 111  ARG   E N   1 
ATOM   12189 C  CA  . ARG   E 2 111 ? 14.537  -39.496 -29.084 1.00 132.46 ? 111  ARG   E CA  1 
ATOM   12190 C  C   . ARG   E 2 111 ? 15.810  -39.683 -28.276 1.00 132.62 ? 111  ARG   E C   1 
ATOM   12191 O  O   . ARG   E 2 111 ? 16.282  -38.765 -27.598 1.00 135.24 ? 111  ARG   E O   1 
ATOM   12192 C  CB  . ARG   E 2 111 ? 13.464  -40.462 -28.590 1.00 133.27 ? 111  ARG   E CB  1 
ATOM   12193 C  CG  . ARG   E 2 111 ? 12.396  -40.763 -29.618 1.00 138.31 ? 111  ARG   E CG  1 
ATOM   12194 C  CD  . ARG   E 2 111 ? 11.556  -41.942 -29.163 1.00 144.33 ? 111  ARG   E CD  1 
ATOM   12195 N  NE  . ARG   E 2 111 ? 12.397  -43.037 -28.683 1.00 148.63 ? 111  ARG   E NE  1 
ATOM   12196 C  CZ  . ARG   E 2 111 ? 12.755  -44.099 -29.397 1.00 150.47 ? 111  ARG   E CZ  1 
ATOM   12197 N  NH1 . ARG   E 2 111 ? 12.316  -44.288 -30.632 1.00 155.35 ? 111  ARG   E NH1 1 
ATOM   12198 N  NH2 . ARG   E 2 111 ? 13.566  -45.004 -28.851 1.00 146.17 ? 111  ARG   E NH2 1 
ATOM   12199 N  N   . ILE   E 2 112 ? 16.370  -40.860 -28.338 1.00 134.09 ? 112  ILE   E N   1 
ATOM   12200 C  CA  . ILE   E 2 112 ? 17.655  -41.139 -27.723 1.00 133.76 ? 112  ILE   E CA  1 
ATOM   12201 C  C   . ILE   E 2 112 ? 18.736  -41.052 -28.790 1.00 136.59 ? 112  ILE   E C   1 
ATOM   12202 O  O   . ILE   E 2 112 ? 18.502  -41.322 -29.980 1.00 135.77 ? 112  ILE   E O   1 
ATOM   12203 C  CB  . ILE   E 2 112 ? 17.651  -42.519 -27.043 1.00 137.78 ? 112  ILE   E CB  1 
ATOM   12204 C  CG1 . ILE   E 2 112 ? 17.915  -43.622 -28.079 1.00 140.63 ? 112  ILE   E CG1 1 
ATOM   12205 C  CG2 . ILE   E 2 112 ? 16.318  -42.753 -26.367 1.00 140.01 ? 112  ILE   E CG2 1 
ATOM   12206 C  CD1 . ILE   E 2 112 ? 18.372  -44.939 -27.496 1.00 136.62 ? 112  ILE   E CD1 1 
ATOM   12207 N  N   . GLY   E 2 113 ? 19.936  -40.662 -28.364 1.00 132.12 ? 113  GLY   E N   1 
ATOM   12208 C  CA  . GLY   E 2 113 ? 21.074  -40.639 -29.265 1.00 124.03 ? 113  GLY   E CA  1 
ATOM   12209 C  C   . GLY   E 2 113 ? 22.117  -39.623 -28.859 1.00 117.71 ? 113  GLY   E C   1 
ATOM   12210 O  O   . GLY   E 2 113 ? 21.763  -38.531 -28.400 1.00 112.95 ? 113  GLY   E O   1 
ATOM   12211 N  N   . ARG   E 2 114 ? 23.404  -39.975 -29.029 1.00 116.14 ? 114  ARG   E N   1 
ATOM   12212 C  CA  . ARG   E 2 114 ? 24.517  -39.111 -28.639 1.00 113.10 ? 114  ARG   E CA  1 
ATOM   12213 C  C   . ARG   E 2 114 ? 24.924  -38.238 -29.820 1.00 111.96 ? 114  ARG   E C   1 
ATOM   12214 O  O   . ARG   E 2 114 ? 25.438  -38.770 -30.816 1.00 110.92 ? 114  ARG   E O   1 
ATOM   12215 C  CB  . ARG   E 2 114 ? 25.707  -39.943 -28.151 1.00 114.35 ? 114  ARG   E CB  1 
ATOM   12216 N  N   . PRO   E 2 115 ? 24.694  -36.912 -29.774 1.00 108.07 ? 115  PRO   E N   1 
ATOM   12217 C  CA  . PRO   E 2 115 ? 25.162  -36.030 -30.856 1.00 105.62 ? 115  PRO   E CA  1 
ATOM   12218 C  C   . PRO   E 2 115 ? 26.652  -36.162 -31.102 1.00 106.50 ? 115  PRO   E C   1 
ATOM   12219 O  O   . PRO   E 2 115 ? 27.452  -35.901 -30.203 1.00 110.40 ? 115  PRO   E O   1 
ATOM   12220 C  CB  . PRO   E 2 115 ? 24.800  -34.634 -30.348 1.00 104.20 ? 115  PRO   E CB  1 
ATOM   12221 C  CG  . PRO   E 2 115 ? 23.593  -34.861 -29.495 1.00 107.27 ? 115  PRO   E CG  1 
ATOM   12222 C  CD  . PRO   E 2 115 ? 23.829  -36.199 -28.817 1.00 108.45 ? 115  PRO   E CD  1 
ATOM   12223 N  N   . SER   E 2 116 ? 27.033  -36.569 -32.308 1.00 104.23 ? 116  SER   E N   1 
ATOM   12224 C  CA  . SER   E 2 116 ? 28.402  -36.998 -32.539 1.00 108.27 ? 116  SER   E CA  1 
ATOM   12225 C  C   . SER   E 2 116 ? 29.385  -35.845 -32.355 1.00 114.70 ? 116  SER   E C   1 
ATOM   12226 O  O   . SER   E 2 116 ? 29.052  -34.668 -32.553 1.00 113.23 ? 116  SER   E O   1 
ATOM   12227 C  CB  . SER   E 2 116 ? 28.533  -37.604 -33.934 1.00 112.12 ? 116  SER   E CB  1 
ATOM   12228 O  OG  . SER   E 2 116 ? 29.809  -38.206 -34.139 1.00 115.12 ? 116  SER   E OG  1 
ATOM   12229 N  N   . GLU   E 2 117 ? 30.611  -36.212 -31.959 1.00 115.57 ? 117  GLU   E N   1 
ATOM   12230 C  CA  . GLU   E 2 117 ? 31.634  -35.227 -31.627 1.00 116.05 ? 117  GLU   E CA  1 
ATOM   12231 C  C   . GLU   E 2 117 ? 32.005  -34.376 -32.837 1.00 118.63 ? 117  GLU   E C   1 
ATOM   12232 O  O   . GLU   E 2 117 ? 32.012  -33.143 -32.756 1.00 122.64 ? 117  GLU   E O   1 
ATOM   12233 C  CB  . GLU   E 2 117 ? 32.869  -35.929 -31.055 1.00 117.26 ? 117  GLU   E CB  1 
ATOM   12234 N  N   . THR   E 2 118 ? 32.301  -35.013 -33.974 1.00 131.48 ? 118  THR   E N   1 
ATOM   12235 C  CA  . THR   E 2 118 ? 32.686  -34.298 -35.187 1.00 133.57 ? 118  THR   E CA  1 
ATOM   12236 C  C   . THR   E 2 118 ? 31.524  -33.558 -35.867 1.00 132.45 ? 118  THR   E C   1 
ATOM   12237 O  O   . THR   E 2 118 ? 31.769  -32.900 -36.879 1.00 133.39 ? 118  THR   E O   1 
ATOM   12238 C  CB  . THR   E 2 118 ? 33.354  -35.259 -36.188 1.00 132.95 ? 118  THR   E CB  1 
ATOM   12239 O  OG1 . THR   E 2 118 ? 32.521  -36.407 -36.401 1.00 133.94 ? 118  THR   E OG1 1 
ATOM   12240 C  CG2 . THR   E 2 118 ? 34.716  -35.710 -35.680 1.00 130.51 ? 118  THR   E CG2 1 
ATOM   12241 N  N   . GLY   E 2 119 ? 30.287  -33.617 -35.364 1.00 116.90 ? 119  GLY   E N   1 
ATOM   12242 C  CA  . GLY   E 2 119 ? 29.217  -32.769 -35.872 1.00 109.78 ? 119  GLY   E CA  1 
ATOM   12243 C  C   . GLY   E 2 119 ? 28.341  -33.448 -36.912 1.00 101.57 ? 119  GLY   E C   1 
ATOM   12244 O  O   . GLY   E 2 119 ? 28.527  -34.614 -37.270 1.00 101.57 ? 119  GLY   E O   1 
ATOM   12245 N  N   . ILE   E 2 120 ? 27.363  -32.685 -37.412 1.00 98.67  ? 120  ILE   E N   1 
ATOM   12246 C  CA  . ILE   E 2 120 ? 26.366  -33.204 -38.357 1.00 94.36  ? 120  ILE   E CA  1 
ATOM   12247 C  C   . ILE   E 2 120 ? 26.985  -33.321 -39.743 1.00 91.55  ? 120  ILE   E C   1 
ATOM   12248 O  O   . ILE   E 2 120 ? 27.426  -32.318 -40.317 1.00 93.27  ? 120  ILE   E O   1 
ATOM   12249 C  CB  . ILE   E 2 120 ? 25.121  -32.302 -38.425 1.00 86.45  ? 120  ILE   E CB  1 
ATOM   12250 C  CG1 . ILE   E 2 120 ? 24.426  -32.175 -37.081 1.00 86.95  ? 120  ILE   E CG1 1 
ATOM   12251 C  CG2 . ILE   E 2 120 ? 24.149  -32.855 -39.429 1.00 81.54  ? 120  ILE   E CG2 1 
ATOM   12252 C  CD1 . ILE   E 2 120 ? 23.129  -31.395 -37.184 1.00 83.42  ? 120  ILE   E CD1 1 
ATOM   12253 N  N   . ILE   E 2 121 ? 26.975  -34.528 -40.308 1.00 88.02  ? 121  ILE   E N   1 
ATOM   12254 C  CA  . ILE   E 2 121 ? 27.424  -34.744 -41.681 1.00 85.37  ? 121  ILE   E CA  1 
ATOM   12255 C  C   . ILE   E 2 121 ? 26.205  -35.113 -42.514 1.00 83.64  ? 121  ILE   E C   1 
ATOM   12256 O  O   . ILE   E 2 121 ? 25.602  -36.174 -42.307 1.00 90.73  ? 121  ILE   E O   1 
ATOM   12257 C  CB  . ILE   E 2 121 ? 28.503  -35.832 -41.771 1.00 85.92  ? 121  ILE   E CB  1 
ATOM   12258 C  CG1 . ILE   E 2 121 ? 29.666  -35.527 -40.823 1.00 90.27  ? 121  ILE   E CG1 1 
ATOM   12259 C  CG2 . ILE   E 2 121 ? 29.031  -35.969 -43.196 1.00 84.66  ? 121  ILE   E CG2 1 
ATOM   12260 C  CD1 . ILE   E 2 121 ? 30.980  -36.238 -41.199 1.00 94.66  ? 121  ILE   E CD1 1 
ATOM   12261 N  N   . GLY   E 2 122 ? 25.827  -34.235 -43.440 1.00 81.28  ? 122  GLY   E N   1 
ATOM   12262 C  CA  . GLY   E 2 122 ? 24.830  -34.552 -44.450 1.00 80.89  ? 122  GLY   E CA  1 
ATOM   12263 C  C   . GLY   E 2 122 ? 25.517  -34.850 -45.769 1.00 82.86  ? 122  GLY   E C   1 
ATOM   12264 O  O   . GLY   E 2 122 ? 26.413  -34.116 -46.196 1.00 90.00  ? 122  GLY   E O   1 
ATOM   12265 N  N   . ILE   E 2 123 ? 25.104  -35.951 -46.394 1.00 84.61  ? 123  ILE   E N   1 
ATOM   12266 C  CA  . ILE   E 2 123 ? 25.629  -36.389 -47.681 1.00 91.65  ? 123  ILE   E CA  1 
ATOM   12267 C  C   . ILE   E 2 123 ? 24.471  -36.959 -48.495 1.00 98.86  ? 123  ILE   E C   1 
ATOM   12268 O  O   . ILE   E 2 123 ? 23.500  -37.482 -47.936 1.00 98.45  ? 123  ILE   E O   1 
ATOM   12269 C  CB  . ILE   E 2 123 ? 26.764  -37.440 -47.523 1.00 97.48  ? 123  ILE   E CB  1 
ATOM   12270 C  CG1 . ILE   E 2 123 ? 26.453  -38.434 -46.398 1.00 94.39  ? 123  ILE   E CG1 1 
ATOM   12271 C  CG2 . ILE   E 2 123 ? 28.109  -36.770 -47.319 1.00 95.55  ? 123  ILE   E CG2 1 
ATOM   12272 C  CD1 . ILE   E 2 123 ? 27.563  -39.432 -46.139 1.00 96.72  ? 123  ILE   E CD1 1 
ATOM   12273 N  N   . ILE   E 2 124 ? 24.574  -36.851 -49.825 1.00 104.49 ? 124  ILE   E N   1 
ATOM   12274 C  CA  . ILE   E 2 124 ? 23.529  -37.404 -50.739 1.00 110.34 ? 124  ILE   E CA  1 
ATOM   12275 C  C   . ILE   E 2 124 ? 24.240  -38.287 -51.776 1.00 117.97 ? 124  ILE   E C   1 
ATOM   12276 O  O   . ILE   E 2 124 ? 25.316  -37.878 -52.254 1.00 113.76 ? 124  ILE   E O   1 
ATOM   12277 C  CB  . ILE   E 2 124 ? 22.726  -36.272 -51.404 1.00 105.10 ? 124  ILE   E CB  1 
ATOM   12278 C  CG1 . ILE   E 2 124 ? 21.997  -35.420 -50.371 1.00 96.60  ? 124  ILE   E CG1 1 
ATOM   12279 C  CG2 . ILE   E 2 124 ? 21.762  -36.821 -52.456 1.00 111.65 ? 124  ILE   E CG2 1 
ATOM   12280 C  CD1 . ILE   E 2 124 ? 20.961  -34.485 -50.964 1.00 96.18  ? 124  ILE   E CD1 1 
ATOM   12281 N  N   . ASP   E 2 125 ? 23.674  -39.451 -52.104 1.00 142.34 ? 125  ASP   E N   1 
ATOM   12282 C  CA  . ASP   E 2 125 ? 24.363  -40.402 -53.023 1.00 143.42 ? 125  ASP   E CA  1 
ATOM   12283 C  C   . ASP   E 2 125 ? 24.512  -39.777 -54.410 1.00 143.59 ? 125  ASP   E C   1 
ATOM   12284 O  O   . ASP   E 2 125 ? 23.556  -39.140 -54.881 1.00 143.89 ? 125  ASP   E O   1 
ATOM   12285 C  CB  . ASP   E 2 125 ? 23.658  -41.749 -53.056 1.00 144.73 ? 125  ASP   E CB  1 
ATOM   12286 C  CG  . ASP   E 2 125 ? 23.984  -42.636 -54.247 1.00 147.68 ? 125  ASP   E CG  1 
ATOM   12287 O  OD1 . ASP   E 2 125 ? 24.998  -43.361 -54.178 1.00 147.15 ? 125  ASP   E OD1 1 
ATOM   12288 O  OD2 . ASP   E 2 125 ? 23.220  -42.597 -55.232 1.00 147.40 ? 125  ASP   E OD2 1 
ATOM   12289 N  N   . PRO   E 2 126 ? 25.675  -39.926 -55.076 1.00 128.83 ? 126  PRO   E N   1 
ATOM   12290 C  CA  . PRO   E 2 126 ? 25.852  -39.410 -56.424 1.00 124.04 ? 126  PRO   E CA  1 
ATOM   12291 C  C   . PRO   E 2 126 ? 24.634  -39.559 -57.318 1.00 125.16 ? 126  PRO   E C   1 
ATOM   12292 O  O   . PRO   E 2 126 ? 24.194  -38.563 -57.919 1.00 121.81 ? 126  PRO   E O   1 
ATOM   12293 C  CB  . PRO   E 2 126 ? 26.986  -40.313 -56.898 1.00 117.68 ? 126  PRO   E CB  1 
ATOM   12294 C  CG  . PRO   E 2 126 ? 27.859  -40.452 -55.678 1.00 120.13 ? 126  PRO   E CG  1 
ATOM   12295 C  CD  . PRO   E 2 126 ? 26.864  -40.566 -54.542 1.00 126.84 ? 126  PRO   E CD  1 
ATOM   12296 N  N   . GLU   E 2 127 ? 24.099  -40.775 -57.415 1.00 127.62 ? 127  GLU   E N   1 
ATOM   12297 C  CA  . GLU   E 2 127 ? 22.895  -41.022 -58.248 1.00 124.03 ? 127  GLU   E CA  1 
ATOM   12298 C  C   . GLU   E 2 127 ? 21.642  -40.718 -57.421 1.00 126.84 ? 127  GLU   E C   1 
ATOM   12299 O  O   . GLU   E 2 127 ? 20.689  -41.516 -57.481 1.00 126.27 ? 127  GLU   E O   1 
ATOM   12300 C  CB  . GLU   E 2 127 ? 22.883  -42.458 -58.763 1.00 113.80 ? 127  GLU   E CB  1 
ATOM   12301 N  N   . CYS   E 2 128 ? 21.650  -39.606 -56.689 1.00 123.48 ? 128  CYS   E N   1 
ATOM   12302 C  CA  . CYS   E 2 128 ? 20.513  -39.274 -55.792 1.00 121.40 ? 128  CYS   E CA  1 
ATOM   12303 C  C   . CYS   E 2 128 ? 20.247  -40.571 -55.009 1.00 124.77 ? 128  CYS   E C   1 
ATOM   12304 O  O   . CYS   E 2 128 ? 21.130  -40.936 -54.219 1.00 122.39 ? 128  CYS   E O   1 
ATOM   12305 C  CB  . CYS   E 2 128 ? 19.346  -38.649 -56.538 1.00 117.40 ? 128  CYS   E CB  1 
ATOM   12306 S  SG  . CYS   E 2 128 ? 19.705  -36.923 -56.952 1.00 120.43 ? 128  CYS   E SG  1 
ATOM   12307 N  N   . ARG   E 2 129 ? 19.085  -41.205 -55.176 1.00 125.80 ? 129  ARG   E N   1 
ATOM   12308 C  CA  . ARG   E 2 129 ? 18.799  -42.507 -54.507 1.00 123.86 ? 129  ARG   E CA  1 
ATOM   12309 C  C   . ARG   E 2 129 ? 18.542  -42.234 -53.009 1.00 124.46 ? 129  ARG   E C   1 
ATOM   12310 O  O   . ARG   E 2 129 ? 17.437  -42.590 -52.548 1.00 120.90 ? 129  ARG   E O   1 
ATOM   12311 C  CB  . ARG   E 2 129 ? 19.888  -43.568 -54.709 1.00 116.14 ? 129  ARG   E CB  1 
ATOM   12312 N  N   . MET   E 2 130 ? 19.502  -41.660 -52.269 1.00 123.97 ? 130  MET   E N   1 
ATOM   12313 C  CA  . MET   E 2 130 ? 19.278  -41.489 -50.807 1.00 117.66 ? 130  MET   E CA  1 
ATOM   12314 C  C   . MET   E 2 130 ? 20.053  -40.314 -50.192 1.00 109.63 ? 130  MET   E C   1 
ATOM   12315 O  O   . MET   E 2 130 ? 21.073  -39.901 -50.781 1.00 111.26 ? 130  MET   E O   1 
ATOM   12316 C  CB  . MET   E 2 130 ? 19.688  -42.779 -50.085 1.00 116.05 ? 130  MET   E CB  1 
ATOM   12317 C  CG  . MET   E 2 130 ? 21.167  -43.096 -50.123 1.00 118.56 ? 130  MET   E CG  1 
ATOM   12318 S  SD  . MET   E 2 130 ? 21.498  -44.534 -49.089 1.00 115.98 ? 130  MET   E SD  1 
ATOM   12319 C  CE  . MET   E 2 130 ? 21.438  -43.686 -47.507 1.00 114.56 ? 130  MET   E CE  1 
ATOM   12320 N  N   . ILE   E 2 131 ? 19.555  -39.779 -49.074 1.00 106.24 ? 131  ILE   E N   1 
ATOM   12321 C  CA  . ILE   E 2 131 ? 20.235  -38.732 -48.310 1.00 103.54 ? 131  ILE   E CA  1 
ATOM   12322 C  C   . ILE   E 2 131 ? 20.828  -39.388 -47.067 1.00 104.37 ? 131  ILE   E C   1 
ATOM   12323 O  O   . ILE   E 2 131 ? 20.101  -40.038 -46.300 1.00 106.35 ? 131  ILE   E O   1 
ATOM   12324 C  CB  . ILE   E 2 131 ? 19.271  -37.603 -47.915 1.00 100.29 ? 131  ILE   E CB  1 
ATOM   12325 C  CG1 . ILE   E 2 131 ? 18.672  -36.941 -49.145 1.00 101.75 ? 131  ILE   E CG1 1 
ATOM   12326 C  CG2 . ILE   E 2 131 ? 19.968  -36.571 -47.073 1.00 95.35  ? 131  ILE   E CG2 1 
ATOM   12327 C  CD1 . ILE   E 2 131 ? 17.837  -35.759 -48.811 1.00 98.36  ? 131  ILE   E CD1 1 
ATOM   12328 N  N   . GLY   E 2 132 ? 22.136  -39.231 -46.867 1.00 97.89  ? 132  GLY   E N   1 
ATOM   12329 C  CA  . GLY   E 2 132 ? 22.819  -39.824 -45.728 1.00 94.47  ? 132  GLY   E CA  1 
ATOM   12330 C  C   . GLY   E 2 132 ? 23.136  -38.772 -44.681 1.00 93.26  ? 132  GLY   E C   1 
ATOM   12331 O  O   . GLY   E 2 132 ? 23.805  -37.781 -44.971 1.00 97.09  ? 132  GLY   E O   1 
ATOM   12332 N  N   . LEU   E 2 133 ? 22.650  -39.005 -43.454 1.00 93.67  ? 133  LEU   E N   1 
ATOM   12333 C  CA  . LEU   E 2 133 ? 22.826  -38.097 -42.321 1.00 88.22  ? 133  LEU   E CA  1 
ATOM   12334 C  C   . LEU   E 2 133 ? 23.550  -38.809 -41.187 1.00 91.94  ? 133  LEU   E C   1 
ATOM   12335 O  O   . LEU   E 2 133 ? 23.138  -39.900 -40.788 1.00 102.36 ? 133  LEU   E O   1 
ATOM   12336 C  CB  . LEU   E 2 133 ? 21.475  -37.593 -41.804 1.00 88.10  ? 133  LEU   E CB  1 
ATOM   12337 C  CG  . LEU   E 2 133 ? 20.567  -36.803 -42.737 1.00 89.65  ? 133  LEU   E CG  1 
ATOM   12338 C  CD1 . LEU   E 2 133 ? 19.343  -36.283 -41.985 1.00 87.90  ? 133  LEU   E CD1 1 
ATOM   12339 C  CD2 . LEU   E 2 133 ? 21.330  -35.668 -43.391 1.00 88.33  ? 133  LEU   E CD2 1 
ATOM   12340 N  N   . ARG   E 2 134 ? 24.611  -38.205 -40.651 1.00 89.03  ? 134  ARG   E N   1 
ATOM   12341 C  CA  . ARG   E 2 134 ? 25.246  -38.723 -39.434 1.00 93.76  ? 134  ARG   E CA  1 
ATOM   12342 C  C   . ARG   E 2 134 ? 24.862  -37.815 -38.281 1.00 99.17  ? 134  ARG   E C   1 
ATOM   12343 O  O   . ARG   E 2 134 ? 25.519  -36.798 -38.043 1.00 99.32  ? 134  ARG   E O   1 
ATOM   12344 C  CB  . ARG   E 2 134 ? 26.764  -38.803 -39.543 1.00 89.60  ? 134  ARG   E CB  1 
ATOM   12345 C  CG  . ARG   E 2 134 ? 27.367  -39.759 -38.508 1.00 97.31  ? 134  ARG   E CG  1 
ATOM   12346 C  CD  . ARG   E 2 134 ? 27.476  -39.164 -37.110 1.00 99.68  ? 134  ARG   E CD  1 
ATOM   12347 N  NE  . ARG   E 2 134 ? 28.343  -37.999 -37.144 1.00 100.39 ? 134  ARG   E NE  1 
ATOM   12348 C  CZ  . ARG   E 2 134 ? 29.661  -38.033 -37.000 1.00 102.00 ? 134  ARG   E CZ  1 
ATOM   12349 N  NH1 . ARG   E 2 134 ? 30.300  -39.159 -36.728 1.00 101.48 ? 134  ARG   E NH1 1 
ATOM   12350 N  NH2 . ARG   E 2 134 ? 30.354  -36.906 -37.120 1.00 107.54 ? 134  ARG   E NH2 1 
ATOM   12351 N  N   . LEU   E 2 135 ? 23.839  -38.206 -37.529 1.00 98.35  ? 135  LEU   E N   1 
ATOM   12352 C  CA  . LEU   E 2 135 ? 23.414  -37.390 -36.406 1.00 100.11 ? 135  LEU   E CA  1 
ATOM   12353 C  C   . LEU   E 2 135 ? 24.041  -37.833 -35.099 1.00 106.22 ? 135  LEU   E C   1 
ATOM   12354 O  O   . LEU   E 2 135 ? 24.376  -36.987 -34.262 1.00 107.24 ? 135  LEU   E O   1 
ATOM   12355 C  CB  . LEU   E 2 135 ? 21.889  -37.412 -36.269 1.00 101.08 ? 135  LEU   E CB  1 
ATOM   12356 C  CG  . LEU   E 2 135 ? 21.146  -36.826 -37.467 1.00 97.55  ? 135  LEU   E CG  1 
ATOM   12357 C  CD1 . LEU   E 2 135 ? 19.678  -36.587 -37.118 1.00 96.39  ? 135  LEU   E CD1 1 
ATOM   12358 C  CD2 . LEU   E 2 135 ? 21.850  -35.556 -37.978 1.00 94.72  ? 135  LEU   E CD2 1 
ATOM   12359 N  N   . TYR   E 2 136 ? 24.208  -39.140 -34.902 1.00 109.63 ? 136  TYR   E N   1 
ATOM   12360 C  CA  . TYR   E 2 136 ? 24.590  -39.666 -33.601 1.00 109.47 ? 136  TYR   E CA  1 
ATOM   12361 C  C   . TYR   E 2 136 ? 25.682  -40.717 -33.758 1.00 108.24 ? 136  TYR   E C   1 
ATOM   12362 O  O   . TYR   E 2 136 ? 25.915  -41.246 -34.847 1.00 106.64 ? 136  TYR   E O   1 
ATOM   12363 C  CB  . TYR   E 2 136 ? 23.362  -40.237 -32.855 1.00 109.12 ? 136  TYR   E CB  1 
ATOM   12364 C  CG  . TYR   E 2 136 ? 22.154  -39.297 -32.853 1.00 109.84 ? 136  TYR   E CG  1 
ATOM   12365 C  CD1 . TYR   E 2 136 ? 22.136  -38.155 -32.063 1.00 107.63 ? 136  TYR   E CD1 1 
ATOM   12366 C  CD2 . TYR   E 2 136 ? 21.035  -39.554 -33.639 1.00 111.91 ? 136  TYR   E CD2 1 
ATOM   12367 C  CE1 . TYR   E 2 136 ? 21.051  -37.298 -32.060 1.00 106.52 ? 136  TYR   E CE1 1 
ATOM   12368 C  CE2 . TYR   E 2 136 ? 19.943  -38.693 -33.635 1.00 110.79 ? 136  TYR   E CE2 1 
ATOM   12369 C  CZ  . TYR   E 2 136 ? 19.962  -37.569 -32.842 1.00 106.88 ? 136  TYR   E CZ  1 
ATOM   12370 O  OH  . TYR   E 2 136 ? 18.892  -36.706 -32.824 1.00 113.00 ? 136  TYR   E OH  1 
ATOM   12371 N  N   . ASP   E 2 137 ? 26.370  -40.988 -32.648 1.00 107.59 ? 137  ASP   E N   1 
ATOM   12372 C  CA  . ASP   E 2 137 ? 27.445  -41.972 -32.638 1.00 106.89 ? 137  ASP   E CA  1 
ATOM   12373 C  C   . ASP   E 2 137 ? 26.859  -43.366 -32.732 1.00 111.70 ? 137  ASP   E C   1 
ATOM   12374 O  O   . ASP   E 2 137 ? 25.933  -43.707 -31.992 1.00 111.81 ? 137  ASP   E O   1 
ATOM   12375 C  CB  . ASP   E 2 137 ? 28.278  -41.857 -31.366 1.00 112.89 ? 137  ASP   E CB  1 
ATOM   12376 C  CG  . ASP   E 2 137 ? 29.326  -40.760 -31.444 1.00 117.46 ? 137  ASP   E CG  1 
ATOM   12377 O  OD1 . ASP   E 2 137 ? 29.886  -40.555 -32.546 1.00 119.08 ? 137  ASP   E OD1 1 
ATOM   12378 O  OD2 . ASP   E 2 137 ? 29.601  -40.110 -30.402 1.00 115.50 ? 137  ASP   E OD2 1 
ATOM   12379 N  N   . GLY   E 2 138 ? 27.389  -44.169 -33.651 1.00 115.88 ? 138  GLY   E N   1 
ATOM   12380 C  CA  . GLY   E 2 138 ? 26.879  -45.501 -33.876 1.00 112.78 ? 138  GLY   E CA  1 
ATOM   12381 C  C   . GLY   E 2 138 ? 25.711  -45.599 -34.835 1.00 115.40 ? 138  GLY   E C   1 
ATOM   12382 O  O   . GLY   E 2 138 ? 25.296  -46.717 -35.156 1.00 118.55 ? 138  GLY   E O   1 
ATOM   12383 N  N   . LEU   E 2 139 ? 25.180  -44.476 -35.325 1.00 115.84 ? 139  LEU   E N   1 
ATOM   12384 C  CA  . LEU   E 2 139 ? 23.962  -44.465 -36.127 1.00 113.99 ? 139  LEU   E CA  1 
ATOM   12385 C  C   . LEU   E 2 139 ? 24.189  -43.754 -37.453 1.00 107.53 ? 139  LEU   E C   1 
ATOM   12386 O  O   . LEU   E 2 139 ? 25.033  -42.861 -37.558 1.00 107.54 ? 139  LEU   E O   1 
ATOM   12387 C  CB  . LEU   E 2 139 ? 22.805  -43.778 -35.375 1.00 113.95 ? 139  LEU   E CB  1 
ATOM   12388 C  CG  . LEU   E 2 139 ? 22.002  -44.623 -34.388 1.00 112.85 ? 139  LEU   E CG  1 
ATOM   12389 C  CD1 . LEU   E 2 139 ? 20.844  -43.818 -33.853 1.00 111.18 ? 139  LEU   E CD1 1 
ATOM   12390 C  CD2 . LEU   E 2 139 ? 21.492  -45.849 -35.094 1.00 113.59 ? 139  LEU   E CD2 1 
ATOM   12391 N  N   . PHE   E 2 140 ? 23.400  -44.142 -38.459 1.00 105.32 ? 140  PHE   E N   1 
ATOM   12392 C  CA  . PHE   E 2 140 ? 23.477  -43.552 -39.800 1.00 104.34 ? 140  PHE   E CA  1 
ATOM   12393 C  C   . PHE   E 2 140 ? 22.064  -43.451 -40.374 1.00 104.68 ? 140  PHE   E C   1 
ATOM   12394 O  O   . PHE   E 2 140 ? 21.544  -44.426 -40.916 1.00 108.88 ? 140  PHE   E O   1 
ATOM   12395 C  CB  . PHE   E 2 140 ? 24.382  -44.372 -40.717 1.00 103.67 ? 140  PHE   E CB  1 
ATOM   12396 C  CG  . PHE   E 2 140 ? 24.665  -43.712 -42.047 1.00 102.53 ? 140  PHE   E CG  1 
ATOM   12397 C  CD1 . PHE   E 2 140 ? 25.342  -42.506 -42.109 1.00 99.11  ? 140  PHE   E CD1 1 
ATOM   12398 C  CD2 . PHE   E 2 140 ? 24.269  -44.305 -43.232 1.00 107.57 ? 140  PHE   E CD2 1 
ATOM   12399 C  CE1 . PHE   E 2 140 ? 25.614  -41.899 -43.318 1.00 98.01  ? 140  PHE   E CE1 1 
ATOM   12400 C  CE2 . PHE   E 2 140 ? 24.539  -43.699 -44.455 1.00 105.80 ? 140  PHE   E CE2 1 
ATOM   12401 C  CZ  . PHE   E 2 140 ? 25.211  -42.495 -44.494 1.00 100.84 ? 140  PHE   E CZ  1 
ATOM   12402 N  N   . LYS   E 2 141 ? 21.456  -42.273 -40.275 1.00 103.87 ? 141  LYS   E N   1 
ATOM   12403 C  CA  . LYS   E 2 141 ? 20.125  -42.057 -40.830 1.00 102.31 ? 141  LYS   E CA  1 
ATOM   12404 C  C   . LYS   E 2 141 ? 20.176  -42.078 -42.352 1.00 102.26 ? 141  LYS   E C   1 
ATOM   12405 O  O   . LYS   E 2 141 ? 21.166  -41.672 -42.967 1.00 98.37  ? 141  LYS   E O   1 
ATOM   12406 C  CB  . LYS   E 2 141 ? 19.562  -40.723 -40.330 1.00 104.23 ? 141  LYS   E CB  1 
ATOM   12407 C  CG  . LYS   E 2 141 ? 18.041  -40.624 -40.266 1.00 108.03 ? 141  LYS   E CG  1 
ATOM   12408 C  CD  . LYS   E 2 141 ? 17.546  -40.071 -38.916 1.00 108.00 ? 141  LYS   E CD  1 
ATOM   12409 C  CE  . LYS   E 2 141 ? 16.055  -39.719 -38.981 1.00 109.62 ? 141  LYS   E CE  1 
ATOM   12410 N  NZ  . LYS   E 2 141 ? 15.274  -39.983 -37.729 1.00 112.92 ? 141  LYS   E NZ  1 
ATOM   12411 N  N   . VAL   E 2 142 ? 19.111  -42.593 -42.958 1.00 108.07 ? 142  VAL   E N   1 
ATOM   12412 C  CA  . VAL   E 2 142 ? 18.992  -42.696 -44.407 1.00 107.94 ? 142  VAL   E CA  1 
ATOM   12413 C  C   . VAL   E 2 142 ? 17.604  -42.191 -44.777 1.00 111.10 ? 142  VAL   E C   1 
ATOM   12414 O  O   . VAL   E 2 142 ? 16.599  -42.759 -44.339 1.00 112.18 ? 142  VAL   E O   1 
ATOM   12415 C  CB  . VAL   E 2 142 ? 19.201  -44.136 -44.913 1.00 105.28 ? 142  VAL   E CB  1 
ATOM   12416 C  CG1 . VAL   E 2 142 ? 18.905  -44.217 -46.400 1.00 113.39 ? 142  VAL   E CG1 1 
ATOM   12417 C  CG2 . VAL   E 2 142 ? 20.606  -44.609 -44.633 1.00 102.01 ? 142  VAL   E CG2 1 
ATOM   12418 N  N   . ILE   E 2 143 ? 17.546  -41.102 -45.534 1.00 109.04 ? 143  ILE   E N   1 
ATOM   12419 C  CA  . ILE   E 2 143 ? 16.263  -40.649 -46.056 1.00 106.42 ? 143  ILE   E CA  1 
ATOM   12420 C  C   . ILE   E 2 143 ? 16.154  -41.197 -47.458 1.00 111.94 ? 143  ILE   E C   1 
ATOM   12421 O  O   . ILE   E 2 143 ? 16.840  -40.706 -48.360 1.00 115.80 ? 143  ILE   E O   1 
ATOM   12422 C  CB  . ILE   E 2 143 ? 16.133  -39.129 -46.099 1.00 103.66 ? 143  ILE   E CB  1 
ATOM   12423 C  CG1 . ILE   E 2 143 ? 16.347  -38.531 -44.727 1.00 102.78 ? 143  ILE   E CG1 1 
ATOM   12424 C  CG2 . ILE   E 2 143 ? 14.777  -38.768 -46.639 1.00 108.28 ? 143  ILE   E CG2 1 
ATOM   12425 C  CD1 . ILE   E 2 143 ? 17.713  -38.016 -44.574 1.00 104.96 ? 143  ILE   E CD1 1 
ATOM   12426 N  N   . PRO   E 2 144 ? 15.336  -42.216 -47.692 1.00 112.16 ? 144  PRO   E N   1 
ATOM   12427 C  CA  . PRO   E 2 144 ? 15.212  -42.742 -49.054 1.00 116.63 ? 144  PRO   E CA  1 
ATOM   12428 C  C   . PRO   E 2 144 ? 14.628  -41.682 -49.978 1.00 118.76 ? 144  PRO   E C   1 
ATOM   12429 O  O   . PRO   E 2 144 ? 13.559  -41.119 -49.713 1.00 117.04 ? 144  PRO   E O   1 
ATOM   12430 C  CB  . PRO   E 2 144 ? 14.281  -43.948 -48.875 1.00 117.67 ? 144  PRO   E CB  1 
ATOM   12431 C  CG  . PRO   E 2 144 ? 14.428  -44.323 -47.418 1.00 113.56 ? 144  PRO   E CG  1 
ATOM   12432 C  CD  . PRO   E 2 144 ? 14.585  -43.011 -46.713 1.00 111.97 ? 144  PRO   E CD  1 
ATOM   12433 N  N   . LEU   E 2 145 ? 15.353  -41.398 -51.063 1.00 120.31 ? 145  LEU   E N   1 
ATOM   12434 C  CA  . LEU   E 2 145 ? 14.949  -40.380 -52.039 1.00 125.08 ? 145  LEU   E CA  1 
ATOM   12435 C  C   . LEU   E 2 145 ? 13.965  -40.986 -53.033 1.00 133.15 ? 145  LEU   E C   1 
ATOM   12436 O  O   . LEU   E 2 145 ? 14.294  -41.291 -54.187 1.00 136.10 ? 145  LEU   E O   1 
ATOM   12437 C  CB  . LEU   E 2 145 ? 16.166  -39.801 -52.750 1.00 123.18 ? 145  LEU   E CB  1 
ATOM   12438 C  CG  . LEU   E 2 145 ? 17.004  -38.721 -52.048 1.00 118.16 ? 145  LEU   E CG  1 
ATOM   12439 C  CD1 . LEU   E 2 145 ? 18.249  -38.375 -52.856 1.00 113.92 ? 145  LEU   E CD1 1 
ATOM   12440 C  CD2 . LEU   E 2 145 ? 16.185  -37.462 -51.770 1.00 111.39 ? 145  LEU   E CD2 1 
ATOM   12441 N  N   . ASP   E 2 146 ? 12.730  -41.173 -52.573 1.00 145.63 ? 146  ASP   E N   1 
ATOM   12442 C  CA  . ASP   E 2 146 ? 11.628  -41.597 -53.422 1.00 145.33 ? 146  ASP   E CA  1 
ATOM   12443 C  C   . ASP   E 2 146 ? 10.575  -40.495 -53.463 1.00 147.37 ? 146  ASP   E C   1 
ATOM   12444 O  O   . ASP   E 2 146 ? 10.320  -39.839 -52.447 1.00 146.60 ? 146  ASP   E O   1 
ATOM   12445 C  CB  . ASP   E 2 146 ? 11.013  -42.903 -52.934 1.00 140.05 ? 146  ASP   E CB  1 
ATOM   12446 C  CG  . ASP   E 2 146 ? 10.073  -43.507 -53.957 1.00 147.77 ? 146  ASP   E CG  1 
ATOM   12447 O  OD1 . ASP   E 2 146 ? 9.121   -42.815 -54.397 1.00 147.79 ? 146  ASP   E OD1 1 
ATOM   12448 O  OD2 . ASP   E 2 146 ? 10.306  -44.667 -54.357 1.00 152.77 ? 146  ASP   E OD2 1 
ATOM   12449 N  N   . ARG   E 2 147 ? 9.962   -40.298 -54.644 1.00 148.90 ? 147  ARG   E N   1 
ATOM   12450 C  CA  . ARG   E 2 147 ? 9.029   -39.187 -54.849 1.00 147.88 ? 147  ARG   E CA  1 
ATOM   12451 C  C   . ARG   E 2 147 ? 7.910   -39.177 -53.811 1.00 148.50 ? 147  ARG   E C   1 
ATOM   12452 O  O   . ARG   E 2 147 ? 7.334   -38.117 -53.526 1.00 150.52 ? 147  ARG   E O   1 
ATOM   12453 C  CB  . ARG   E 2 147 ? 8.428   -39.245 -56.260 1.00 145.75 ? 147  ARG   E CB  1 
ATOM   12454 N  N   . ASP   E 2 148 ? 7.586   -40.337 -53.240 1.00 155.23 ? 148  ASP   E N   1 
ATOM   12455 C  CA  . ASP   E 2 148 ? 6.543   -40.374 -52.222 1.00 155.61 ? 148  ASP   E CA  1 
ATOM   12456 C  C   . ASP   E 2 148 ? 6.992   -39.670 -50.943 1.00 153.58 ? 148  ASP   E C   1 
ATOM   12457 O  O   . ASP   E 2 148 ? 6.198   -38.940 -50.336 1.00 155.92 ? 148  ASP   E O   1 
ATOM   12458 C  CB  . ASP   E 2 148 ? 6.138   -41.821 -51.932 1.00 157.79 ? 148  ASP   E CB  1 
ATOM   12459 C  CG  . ASP   E 2 148 ? 4.630   -41.985 -51.771 1.00 159.11 ? 148  ASP   E CG  1 
ATOM   12460 O  OD1 . ASP   E 2 148 ? 4.051   -41.349 -50.857 1.00 158.42 ? 148  ASP   E OD1 1 
ATOM   12461 O  OD2 . ASP   E 2 148 ? 4.031   -42.747 -52.570 1.00 158.09 ? 148  ASP   E OD2 1 
ATOM   12462 N  N   . ASN   E 2 149 ? 8.252   -39.860 -50.524 1.00 144.70 ? 149  ASN   E N   1 
ATOM   12463 C  CA  . ASN   E 2 149 ? 8.739   -39.304 -49.258 1.00 132.20 ? 149  ASN   E CA  1 
ATOM   12464 C  C   . ASN   E 2 149 ? 8.465   -37.806 -49.371 1.00 125.82 ? 149  ASN   E C   1 
ATOM   12465 O  O   . ASN   E 2 149 ? 9.058   -37.107 -50.205 1.00 119.97 ? 149  ASN   E O   1 
ATOM   12466 C  CB  . ASN   E 2 149 ? 10.199  -39.707 -49.004 1.00 124.74 ? 149  ASN   E CB  1 
ATOM   12467 C  CG  . ASN   E 2 149 ? 10.503  -39.978 -47.518 1.00 115.94 ? 149  ASN   E CG  1 
ATOM   12468 O  OD1 . ASN   E 2 149 ? 9.643   -39.836 -46.648 1.00 113.36 ? 149  ASN   E OD1 1 
ATOM   12469 N  ND2 . ASN   E 2 149 ? 11.736  -40.393 -47.237 1.00 113.33 ? 149  ASN   E ND2 1 
ATOM   12470 N  N   . LYS   E 2 150 ? 7.530   -37.318 -48.560 1.00 122.30 ? 150  LYS   E N   1 
ATOM   12471 C  CA  . LYS   E 2 150 ? 7.249   -35.900 -48.465 1.00 117.42 ? 150  LYS   E CA  1 
ATOM   12472 C  C   . LYS   E 2 150 ? 7.480   -35.517 -47.014 1.00 113.01 ? 150  LYS   E C   1 
ATOM   12473 O  O   . LYS   E 2 150 ? 8.019   -34.442 -46.740 1.00 111.48 ? 150  LYS   E O   1 
ATOM   12474 C  CB  . LYS   E 2 150 ? 5.831   -35.502 -48.894 1.00 116.70 ? 150  LYS   E CB  1 
ATOM   12475 N  N   . GLU   E 2 151 ? 7.128   -36.388 -46.076 1.00 109.19 ? 151  GLU   E N   1 
ATOM   12476 C  CA  . GLU   E 2 151 ? 7.467   -36.147 -44.688 1.00 110.37 ? 151  GLU   E CA  1 
ATOM   12477 C  C   . GLU   E 2 151 ? 8.886   -36.590 -44.367 1.00 109.91 ? 151  GLU   E C   1 
ATOM   12478 O  O   . GLU   E 2 151 ? 9.263   -36.601 -43.192 1.00 111.99 ? 151  GLU   E O   1 
ATOM   12479 C  CB  . GLU   E 2 151 ? 6.469   -36.846 -43.767 1.00 115.34 ? 151  GLU   E CB  1 
ATOM   12480 C  CG  . GLU   E 2 151 ? 5.152   -36.085 -43.613 1.00 123.99 ? 151  GLU   E CG  1 
ATOM   12481 C  CD  . GLU   E 2 151 ? 3.946   -37.009 -43.496 1.00 132.72 ? 151  GLU   E CD  1 
ATOM   12482 O  OE1 . GLU   E 2 151 ? 4.109   -38.235 -43.678 1.00 126.41 ? 151  GLU   E OE1 1 
ATOM   12483 O  OE2 . GLU   E 2 151 ? 2.829   -36.512 -43.228 1.00 138.53 ? 151  GLU   E OE2 1 
ATOM   12484 N  N   . LEU   E 2 152 ? 9.676   -36.945 -45.384 1.00 111.13 ? 152  LEU   E N   1 
ATOM   12485 C  CA  . LEU   E 2 152 ? 11.071  -37.358 -45.204 1.00 109.83 ? 152  LEU   E CA  1 
ATOM   12486 C  C   . LEU   E 2 152 ? 11.196  -38.451 -44.141 1.00 111.06 ? 152  LEU   E C   1 
ATOM   12487 O  O   . LEU   E 2 152 ? 11.944  -38.334 -43.166 1.00 107.05 ? 152  LEU   E O   1 
ATOM   12488 C  CB  . LEU   E 2 152 ? 11.947  -36.154 -44.868 1.00 106.14 ? 152  LEU   E CB  1 
ATOM   12489 C  CG  . LEU   E 2 152 ? 12.018  -35.046 -45.917 1.00 103.71 ? 152  LEU   E CG  1 
ATOM   12490 C  CD1 . LEU   E 2 152 ? 12.416  -33.725 -45.277 1.00 103.78 ? 152  LEU   E CD1 1 
ATOM   12491 C  CD2 . LEU   E 2 152 ? 13.008  -35.439 -46.991 1.00 91.60  ? 152  LEU   E CD2 1 
ATOM   12492 N  N   . LYS   E 2 153 ? 10.441  -39.533 -44.342 1.00 110.57 ? 153  LYS   E N   1 
ATOM   12493 C  CA  . LYS   E 2 153 ? 10.600  -40.715 -43.510 1.00 109.51 ? 153  LYS   E CA  1 
ATOM   12494 C  C   . LYS   E 2 153 ? 12.032  -41.238 -43.618 1.00 112.75 ? 153  LYS   E C   1 
ATOM   12495 O  O   . LYS   E 2 153 ? 12.645  -41.186 -44.694 1.00 113.39 ? 153  LYS   E O   1 
ATOM   12496 C  CB  . LYS   E 2 153 ? 9.588   -41.782 -43.936 1.00 105.49 ? 153  LYS   E CB  1 
ATOM   12497 N  N   . ALA   E 2 154 ? 12.582  -41.727 -42.497 1.00 115.16 ? 154  ALA   E N   1 
ATOM   12498 C  CA  . ALA   E 2 154 ? 13.969  -42.185 -42.449 1.00 116.81 ? 154  ALA   E CA  1 
ATOM   12499 C  C   . ALA   E 2 154 ? 14.126  -43.430 -41.581 1.00 120.44 ? 154  ALA   E C   1 
ATOM   12500 O  O   . ALA   E 2 154 ? 13.304  -43.710 -40.703 1.00 122.23 ? 154  ALA   E O   1 
ATOM   12501 C  CB  . ALA   E 2 154 ? 14.898  -41.095 -41.920 1.00 112.99 ? 154  ALA   E CB  1 
ATOM   12502 N  N   . PHE   E 2 155 ? 15.226  -44.161 -41.819 1.00 124.03 ? 155  PHE   E N   1 
ATOM   12503 C  CA  . PHE   E 2 155 ? 15.564  -45.364 -41.061 1.00 120.46 ? 155  PHE   E CA  1 
ATOM   12504 C  C   . PHE   E 2 155 ? 17.049  -45.358 -40.712 1.00 115.73 ? 155  PHE   E C   1 
ATOM   12505 O  O   . PHE   E 2 155 ? 17.888  -45.021 -41.552 1.00 116.62 ? 155  PHE   E O   1 
ATOM   12506 C  CB  . PHE   E 2 155 ? 15.187  -46.649 -41.833 1.00 123.32 ? 155  PHE   E CB  1 
ATOM   12507 C  CG  . PHE   E 2 155 ? 15.965  -46.882 -43.112 1.00 124.71 ? 155  PHE   E CG  1 
ATOM   12508 C  CD1 . PHE   E 2 155 ? 17.169  -47.570 -43.092 1.00 124.33 ? 155  PHE   E CD1 1 
ATOM   12509 C  CD2 . PHE   E 2 155 ? 15.461  -46.465 -44.336 1.00 122.58 ? 155  PHE   E CD2 1 
ATOM   12510 C  CE1 . PHE   E 2 155 ? 17.870  -47.800 -44.256 1.00 125.33 ? 155  PHE   E CE1 1 
ATOM   12511 C  CE2 . PHE   E 2 155 ? 16.157  -46.696 -45.506 1.00 122.29 ? 155  PHE   E CE2 1 
ATOM   12512 C  CZ  . PHE   E 2 155 ? 17.362  -47.366 -45.464 1.00 124.90 ? 155  PHE   E CZ  1 
ATOM   12513 N  N   . ASN   E 2 156 ? 17.359  -45.714 -39.469 1.00 111.72 ? 156  ASN   E N   1 
ATOM   12514 C  CA  . ASN   E 2 156 ? 18.731  -45.784 -38.988 1.00 111.31 ? 156  ASN   E CA  1 
ATOM   12515 C  C   . ASN   E 2 156 ? 19.340  -47.162 -39.245 1.00 114.87 ? 156  ASN   E C   1 
ATOM   12516 O  O   . ASN   E 2 156 ? 18.668  -48.192 -39.122 1.00 117.13 ? 156  ASN   E O   1 
ATOM   12517 C  CB  . ASN   E 2 156 ? 18.785  -45.477 -37.489 1.00 111.61 ? 156  ASN   E CB  1 
ATOM   12518 C  CG  . ASN   E 2 156 ? 18.756  -43.993 -37.186 1.00 113.49 ? 156  ASN   E CG  1 
ATOM   12519 O  OD1 . ASN   E 2 156 ? 19.536  -43.213 -37.742 1.00 117.35 ? 156  ASN   E OD1 1 
ATOM   12520 N  ND2 . ASN   E 2 156 ? 17.852  -43.592 -36.303 1.00 114.20 ? 156  ASN   E ND2 1 
ATOM   12521 N  N   . ILE   E 2 157 ? 20.629  -47.164 -39.590 1.00 115.75 ? 157  ILE   E N   1 
ATOM   12522 C  CA  . ILE   E 2 157 ? 21.455  -48.371 -39.630 1.00 119.24 ? 157  ILE   E CA  1 
ATOM   12523 C  C   . ILE   E 2 157 ? 22.423  -48.310 -38.456 1.00 118.21 ? 157  ILE   E C   1 
ATOM   12524 O  O   . ILE   E 2 157 ? 23.075  -47.281 -38.232 1.00 117.55 ? 157  ILE   E O   1 
ATOM   12525 C  CB  . ILE   E 2 157 ? 22.221  -48.491 -40.963 1.00 117.05 ? 157  ILE   E CB  1 
ATOM   12526 C  CG1 . ILE   E 2 157 ? 21.376  -47.985 -42.125 1.00 115.74 ? 157  ILE   E CG1 1 
ATOM   12527 C  CG2 . ILE   E 2 157 ? 22.630  -49.934 -41.220 1.00 120.26 ? 157  ILE   E CG2 1 
ATOM   12528 C  CD1 . ILE   E 2 157 ? 22.178  -47.782 -43.387 1.00 114.80 ? 157  ILE   E CD1 1 
ATOM   12529 N  N   . ARG   E 2 158 ? 22.503  -49.391 -37.688 1.00 119.93 ? 158  ARG   E N   1 
ATOM   12530 C  CA  . ARG   E 2 158 ? 23.519  -49.441 -36.650 1.00 118.70 ? 158  ARG   E CA  1 
ATOM   12531 C  C   . ARG   E 2 158 ? 24.886  -49.379 -37.302 1.00 119.99 ? 158  ARG   E C   1 
ATOM   12532 O  O   . ARG   E 2 158 ? 25.105  -49.949 -38.378 1.00 120.01 ? 158  ARG   E O   1 
ATOM   12533 C  CB  . ARG   E 2 158 ? 23.408  -50.707 -35.802 1.00 123.62 ? 158  ARG   E CB  1 
ATOM   12534 C  CG  . ARG   E 2 158 ? 22.003  -51.111 -35.402 1.00 131.44 ? 158  ARG   E CG  1 
ATOM   12535 C  CD  . ARG   E 2 158 ? 21.264  -50.007 -34.635 1.00 131.06 ? 158  ARG   E CD  1 
ATOM   12536 N  NE  . ARG   E 2 158 ? 19.929  -50.398 -34.176 1.00 134.42 ? 158  ARG   E NE  1 
ATOM   12537 C  CZ  . ARG   E 2 158 ? 18.843  -50.473 -34.943 1.00 134.70 ? 158  ARG   E CZ  1 
ATOM   12538 N  NH1 . ARG   E 2 158 ? 18.902  -50.292 -36.256 1.00 128.21 ? 158  ARG   E NH1 1 
ATOM   12539 N  NH2 . ARG   E 2 158 ? 17.666  -50.741 -34.380 1.00 137.39 ? 158  ARG   E NH2 1 
ATOM   12540 N  N   . LEU   E 2 159 ? 25.793  -48.639 -36.668 1.00 121.27 ? 159  LEU   E N   1 
ATOM   12541 C  CA  . LEU   E 2 159 ? 27.160  -48.463 -37.159 1.00 124.53 ? 159  LEU   E CA  1 
ATOM   12542 C  C   . LEU   E 2 159 ? 28.100  -48.954 -36.063 1.00 126.33 ? 159  LEU   E C   1 
ATOM   12543 O  O   . LEU   E 2 159 ? 28.190  -48.338 -34.997 1.00 124.29 ? 159  LEU   E O   1 
ATOM   12544 C  CB  . LEU   E 2 159 ? 27.451  -47.002 -37.555 1.00 122.11 ? 159  LEU   E CB  1 
ATOM   12545 C  CG  . LEU   E 2 159 ? 28.623  -46.751 -38.536 1.00 125.35 ? 159  LEU   E CG  1 
ATOM   12546 C  CD1 . LEU   E 2 159 ? 28.519  -45.373 -39.132 1.00 117.20 ? 159  LEU   E CD1 1 
ATOM   12547 C  CD2 . LEU   E 2 159 ? 29.974  -46.911 -37.859 1.00 135.11 ? 159  LEU   E CD2 1 
ATOM   12548 N  N   . GLU   E 2 160 ? 28.805  -50.062 -36.332 1.00 142.48 ? 160  GLU   E N   1 
ATOM   12549 C  CA  . GLU   E 2 160 ? 29.669  -50.659 -35.316 1.00 144.09 ? 160  GLU   E CA  1 
ATOM   12550 C  C   . GLU   E 2 160 ? 30.758  -49.689 -34.880 1.00 143.03 ? 160  GLU   E C   1 
ATOM   12551 O  O   . GLU   E 2 160 ? 31.041  -49.568 -33.681 1.00 144.47 ? 160  GLU   E O   1 
ATOM   12552 C  CB  . GLU   E 2 160 ? 30.276  -51.965 -35.837 1.00 147.70 ? 160  GLU   E CB  1 
ATOM   12553 C  CG  . GLU   E 2 160 ? 29.248  -53.041 -36.190 1.00 154.14 ? 160  GLU   E CG  1 
ATOM   12554 C  CD  . GLU   E 2 160 ? 28.997  -54.010 -35.050 1.00 157.38 ? 160  GLU   E CD  1 
ATOM   12555 O  OE1 . GLU   E 2 160 ? 29.286  -53.652 -33.884 1.00 155.19 ? 160  GLU   E OE1 1 
ATOM   12556 O  OE2 . GLU   E 2 160 ? 28.528  -55.137 -35.329 1.00 156.64 ? 160  GLU   E OE2 1 
ATOM   12557 N  N   . GLU   E 2 161 ? 31.371  -48.983 -35.835 1.00 129.04 ? 161  GLU   E N   1 
ATOM   12558 C  CA  . GLU   E 2 161 ? 32.318  -47.920 -35.522 1.00 125.52 ? 161  GLU   E CA  1 
ATOM   12559 C  C   . GLU   E 2 161 ? 31.532  -46.721 -35.031 1.00 124.74 ? 161  GLU   E C   1 
ATOM   12560 O  O   . GLU   E 2 161 ? 30.541  -46.346 -35.655 1.00 127.88 ? 161  GLU   E O   1 
ATOM   12561 C  CB  . GLU   E 2 161 ? 33.126  -47.537 -36.763 1.00 121.00 ? 161  GLU   E CB  1 
ATOM   12562 C  CG  . GLU   E 2 161 ? 34.007  -48.660 -37.305 1.00 119.27 ? 161  GLU   E CG  1 
ATOM   12563 C  CD  . GLU   E 2 161 ? 33.326  -49.521 -38.395 1.00 124.74 ? 161  GLU   E CD  1 
ATOM   12564 O  OE1 . GLU   E 2 161 ? 32.086  -49.699 -38.311 1.00 127.62 ? 161  GLU   E OE1 1 
ATOM   12565 O  OE2 . GLU   E 2 161 ? 34.022  -50.020 -39.331 1.00 120.85 ? 161  GLU   E OE2 1 
ATOM   12566 N  N   . LEU   E 2 162 ? 31.963  -46.127 -33.912 1.00 123.82 ? 162  LEU   E N   1 
ATOM   12567 C  CA  . LEU   E 2 162 ? 31.248  -45.005 -33.324 1.00 121.22 ? 162  LEU   E CA  1 
ATOM   12568 C  C   . LEU   E 2 162 ? 32.050  -43.713 -33.341 1.00 118.80 ? 162  LEU   E C   1 
ATOM   12569 O  O   . LEU   E 2 162 ? 31.621  -42.727 -32.735 1.00 121.26 ? 162  LEU   E O   1 
ATOM   12570 C  CB  . LEU   E 2 162 ? 30.824  -45.337 -31.885 1.00 121.92 ? 162  LEU   E CB  1 
ATOM   12571 C  CG  . LEU   E 2 162 ? 29.984  -46.618 -31.768 1.00 119.28 ? 162  LEU   E CG  1 
ATOM   12572 C  CD1 . LEU   E 2 162 ? 30.786  -47.783 -31.186 1.00 118.73 ? 162  LEU   E CD1 1 
ATOM   12573 C  CD2 . LEU   E 2 162 ? 28.717  -46.391 -30.982 1.00 114.53 ? 162  LEU   E CD2 1 
ATOM   12574 N  N   . HIS   E 2 163 ? 33.165  -43.660 -34.082 1.00 115.08 ? 163  HIS   E N   1 
ATOM   12575 C  CA  . HIS   E 2 163 ? 34.062  -42.501 -34.070 1.00 116.95 ? 163  HIS   E CA  1 
ATOM   12576 C  C   . HIS   E 2 163 ? 34.440  -42.115 -35.500 1.00 115.29 ? 163  HIS   E C   1 
ATOM   12577 O  O   . HIS   E 2 163 ? 35.591  -42.225 -35.931 1.00 114.79 ? 163  HIS   E O   1 
ATOM   12578 C  CB  . HIS   E 2 163 ? 35.291  -42.782 -33.211 1.00 120.15 ? 163  HIS   E CB  1 
ATOM   12579 C  CG  . HIS   E 2 163 ? 34.964  -42.866 -31.758 1.00 124.31 ? 163  HIS   E CG  1 
ATOM   12580 N  ND1 . HIS   E 2 163 ? 34.104  -41.979 -31.146 1.00 126.87 ? 163  HIS   E ND1 1 
ATOM   12581 C  CD2 . HIS   E 2 163 ? 35.331  -43.755 -30.806 1.00 128.78 ? 163  HIS   E CD2 1 
ATOM   12582 C  CE1 . HIS   E 2 163 ? 33.973  -42.303 -29.872 1.00 131.18 ? 163  HIS   E CE1 1 
ATOM   12583 N  NE2 . HIS   E 2 163 ? 34.706  -43.379 -29.641 1.00 133.83 ? 163  HIS   E NE2 1 
ATOM   12584 N  N   . VAL   E 2 164 ? 33.446  -41.619 -36.226 1.00 115.12 ? 164  VAL   E N   1 
ATOM   12585 C  CA  . VAL   E 2 164 ? 33.584  -41.279 -37.634 1.00 108.35 ? 164  VAL   E CA  1 
ATOM   12586 C  C   . VAL   E 2 164 ? 34.085  -39.848 -37.765 1.00 109.17 ? 164  VAL   E C   1 
ATOM   12587 O  O   . VAL   E 2 164 ? 33.402  -38.904 -37.360 1.00 112.31 ? 164  VAL   E O   1 
ATOM   12588 C  CB  . VAL   E 2 164 ? 32.254  -41.453 -38.374 1.00 100.23 ? 164  VAL   E CB  1 
ATOM   12589 C  CG1 . VAL   E 2 164 ? 32.438  -41.053 -39.807 1.00 101.19 ? 164  VAL   E CG1 1 
ATOM   12590 C  CG2 . VAL   E 2 164 ? 31.761  -42.892 -38.257 1.00 104.77 ? 164  VAL   E CG2 1 
ATOM   12591 N  N   . ILE   E 2 165 ? 35.263  -39.689 -38.370 1.00 110.74 ? 165  ILE   E N   1 
ATOM   12592 C  CA  . ILE   E 2 165 ? 35.799  -38.360 -38.658 1.00 107.17 ? 165  ILE   E CA  1 
ATOM   12593 C  C   . ILE   E 2 165 ? 34.986  -37.677 -39.762 1.00 104.43 ? 165  ILE   E C   1 
ATOM   12594 O  O   . ILE   E 2 165 ? 34.364  -36.633 -39.533 1.00 107.44 ? 165  ILE   E O   1 
ATOM   12595 C  CB  . ILE   E 2 165 ? 37.291  -38.457 -39.025 1.00 102.68 ? 165  ILE   E CB  1 
ATOM   12596 C  CG1 . ILE   E 2 165 ? 38.034  -39.320 -38.014 1.00 107.27 ? 165  ILE   E CG1 1 
ATOM   12597 C  CG2 . ILE   E 2 165 ? 37.923  -37.103 -39.050 1.00 107.79 ? 165  ILE   E CG2 1 
ATOM   12598 C  CD1 . ILE   E 2 165 ? 37.826  -38.884 -36.593 1.00 112.26 ? 165  ILE   E CD1 1 
ATOM   12599 N  N   . ASP   E 2 166 ? 34.974  -38.260 -40.970 1.00 99.49  ? 166  ASP   E N   1 
ATOM   12600 C  CA  . ASP   E 2 166 ? 34.335  -37.704 -42.169 1.00 97.72  ? 166  ASP   E CA  1 
ATOM   12601 C  C   . ASP   E 2 166 ? 33.818  -38.863 -43.018 1.00 99.11  ? 166  ASP   E C   1 
ATOM   12602 O  O   . ASP   E 2 166 ? 34.565  -39.816 -43.264 1.00 103.81 ? 166  ASP   E O   1 
ATOM   12603 C  CB  . ASP   E 2 166 ? 35.347  -36.856 -42.981 1.00 98.29  ? 166  ASP   E CB  1 
ATOM   12604 C  CG  . ASP   E 2 166 ? 34.690  -35.817 -43.917 1.00 100.07 ? 166  ASP   E CG  1 
ATOM   12605 O  OD1 . ASP   E 2 166 ? 33.454  -35.859 -44.112 1.00 98.20  ? 166  ASP   E OD1 1 
ATOM   12606 O  OD2 . ASP   E 2 166 ? 35.430  -34.944 -44.457 1.00 98.47  ? 166  ASP   E OD2 1 
ATOM   12607 N  N   . VAL   E 2 167 ? 32.556  -38.797 -43.459 1.00 97.64  ? 167  VAL   E N   1 
ATOM   12608 C  CA  . VAL   E 2 167 ? 31.989  -39.780 -44.380 1.00 98.14  ? 167  VAL   E CA  1 
ATOM   12609 C  C   . VAL   E 2 167 ? 31.444  -39.061 -45.608 1.00 101.81 ? 167  VAL   E C   1 
ATOM   12610 O  O   . VAL   E 2 167 ? 30.807  -38.007 -45.501 1.00 106.37 ? 167  VAL   E O   1 
ATOM   12611 C  CB  . VAL   E 2 167 ? 30.887  -40.640 -43.728 1.00 92.90  ? 167  VAL   E CB  1 
ATOM   12612 C  CG1 . VAL   E 2 167 ? 29.882  -39.766 -43.047 1.00 88.67  ? 167  VAL   E CG1 1 
ATOM   12613 C  CG2 . VAL   E 2 167 ? 30.204  -41.523 -44.779 1.00 96.59  ? 167  VAL   E CG2 1 
ATOM   12614 N  N   . LYS   E 2 168 ? 31.694  -39.635 -46.776 1.00 97.69  ? 168  LYS   E N   1 
ATOM   12615 C  CA  . LYS   E 2 168 ? 31.241  -39.066 -48.034 1.00 101.87 ? 168  LYS   E CA  1 
ATOM   12616 C  C   . LYS   E 2 168 ? 30.873  -40.224 -48.952 1.00 105.85 ? 168  LYS   E C   1 
ATOM   12617 O  O   . LYS   E 2 168 ? 31.659  -41.166 -49.082 1.00 108.82 ? 168  LYS   E O   1 
ATOM   12618 C  CB  . LYS   E 2 168 ? 32.348  -38.199 -48.646 1.00 101.27 ? 168  LYS   E CB  1 
ATOM   12619 C  CG  . LYS   E 2 168 ? 32.075  -36.710 -48.677 1.00 98.30  ? 168  LYS   E CG  1 
ATOM   12620 C  CD  . LYS   E 2 168 ? 32.398  -36.040 -47.366 1.00 101.12 ? 168  LYS   E CD  1 
ATOM   12621 C  CE  . LYS   E 2 168 ? 32.259  -34.523 -47.482 1.00 105.27 ? 168  LYS   E CE  1 
ATOM   12622 N  NZ  . LYS   E 2 168 ? 32.412  -33.810 -46.174 1.00 110.66 ? 168  LYS   E NZ  1 
ATOM   12623 N  N   . PHE   E 2 169 ? 29.684  -40.183 -49.561 1.00 102.65 ? 169  PHE   E N   1 
ATOM   12624 C  CA  . PHE   E 2 169 ? 29.300  -41.204 -50.537 1.00 103.36 ? 169  PHE   E CA  1 
ATOM   12625 C  C   . PHE   E 2 169 ? 30.322  -41.288 -51.673 1.00 107.98 ? 169  PHE   E C   1 
ATOM   12626 O  O   . PHE   E 2 169 ? 30.917  -40.287 -52.074 1.00 107.29 ? 169  PHE   E O   1 
ATOM   12627 C  CB  . PHE   E 2 169 ? 27.946  -40.879 -51.146 1.00 108.79 ? 169  PHE   E CB  1 
ATOM   12628 C  CG  . PHE   E 2 169 ? 26.780  -41.299 -50.323 1.00 110.73 ? 169  PHE   E CG  1 
ATOM   12629 C  CD1 . PHE   E 2 169 ? 26.490  -42.632 -50.147 1.00 115.22 ? 169  PHE   E CD1 1 
ATOM   12630 C  CD2 . PHE   E 2 169 ? 25.927  -40.355 -49.784 1.00 110.03 ? 169  PHE   E CD2 1 
ATOM   12631 C  CE1 . PHE   E 2 169 ? 25.385  -43.017 -49.414 1.00 116.68 ? 169  PHE   E CE1 1 
ATOM   12632 C  CE2 . PHE   E 2 169 ? 24.826  -40.732 -49.056 1.00 108.15 ? 169  PHE   E CE2 1 
ATOM   12633 C  CZ  . PHE   E 2 169 ? 24.556  -42.060 -48.869 1.00 111.57 ? 169  PHE   E CZ  1 
ATOM   12634 N  N   . LEU   E 2 170 ? 30.475  -42.479 -52.245 1.00 112.25 ? 170  LEU   E N   1 
ATOM   12635 C  CA  . LEU   E 2 170 ? 31.503  -42.720 -53.251 1.00 110.59 ? 170  LEU   E CA  1 
ATOM   12636 C  C   . LEU   E 2 170 ? 30.945  -42.665 -54.676 1.00 114.23 ? 170  LEU   E C   1 
ATOM   12637 O  O   . LEU   E 2 170 ? 29.833  -43.130 -54.952 1.00 111.11 ? 170  LEU   E O   1 
ATOM   12638 C  CB  . LEU   E 2 170 ? 32.186  -44.066 -52.999 1.00 108.14 ? 170  LEU   E CB  1 
ATOM   12639 C  CG  . LEU   E 2 170 ? 33.286  -43.946 -51.954 1.00 107.74 ? 170  LEU   E CG  1 
ATOM   12640 C  CD1 . LEU   E 2 170 ? 34.055  -45.239 -51.786 1.00 109.24 ? 170  LEU   E CD1 1 
ATOM   12641 C  CD2 . LEU   E 2 170 ? 34.211  -42.802 -52.344 1.00 112.42 ? 170  LEU   E CD2 1 
ATOM   12642 N  N   . TYR   E 2 171 ? 31.727  -42.071 -55.575 1.00 112.00 ? 171  TYR   E N   1 
ATOM   12643 C  CA  . TYR   E 2 171 ? 31.411  -42.104 -56.991 1.00 110.34 ? 171  TYR   E CA  1 
ATOM   12644 C  C   . TYR   E 2 171 ? 31.875  -43.426 -57.585 1.00 120.74 ? 171  TYR   E C   1 
ATOM   12645 O  O   . TYR   E 2 171 ? 32.854  -44.021 -57.122 1.00 123.48 ? 171  TYR   E O   1 
ATOM   12646 C  CB  . TYR   E 2 171 ? 32.110  -40.962 -57.723 1.00 109.33 ? 171  TYR   E CB  1 
ATOM   12647 C  CG  . TYR   E 2 171 ? 31.573  -39.556 -57.531 1.00 108.21 ? 171  TYR   E CG  1 
ATOM   12648 C  CD1 . TYR   E 2 171 ? 30.321  -39.178 -58.011 1.00 108.22 ? 171  TYR   E CD1 1 
ATOM   12649 C  CD2 . TYR   E 2 171 ? 32.351  -38.582 -56.920 1.00 111.50 ? 171  TYR   E CD2 1 
ATOM   12650 C  CE1 . TYR   E 2 171 ? 29.851  -37.866 -57.859 1.00 108.36 ? 171  TYR   E CE1 1 
ATOM   12651 C  CE2 . TYR   E 2 171 ? 31.897  -37.269 -56.768 1.00 109.76 ? 171  TYR   E CE2 1 
ATOM   12652 C  CZ  . TYR   E 2 171 ? 30.650  -36.916 -57.233 1.00 110.46 ? 171  TYR   E CZ  1 
ATOM   12653 O  OH  . TYR   E 2 171 ? 30.220  -35.613 -57.061 1.00 107.69 ? 171  TYR   E OH  1 
ATOM   12654 N  N   . GLY   E 2 172 ? 31.184  -43.881 -58.634 1.00 120.52 ? 172  GLY   E N   1 
ATOM   12655 C  CA  . GLY   E 2 172 ? 31.613  -45.074 -59.348 1.00 127.21 ? 172  GLY   E CA  1 
ATOM   12656 C  C   . GLY   E 2 172 ? 31.181  -46.402 -58.753 1.00 136.15 ? 172  GLY   E C   1 
ATOM   12657 O  O   . GLY   E 2 172 ? 31.439  -47.452 -59.359 1.00 137.71 ? 172  GLY   E O   1 
ATOM   12658 N  N   . CYS   E 2 173 ? 30.538  -46.390 -57.595 1.00 142.51 ? 173  CYS   E N   1 
ATOM   12659 C  CA  . CYS   E 2 173 ? 30.079  -47.612 -56.960 1.00 138.62 ? 173  CYS   E CA  1 
ATOM   12660 C  C   . CYS   E 2 173 ? 28.916  -48.206 -57.740 1.00 139.22 ? 173  CYS   E C   1 
ATOM   12661 O  O   . CYS   E 2 173 ? 28.135  -47.489 -58.367 1.00 141.44 ? 173  CYS   E O   1 
ATOM   12662 C  CB  . CYS   E 2 173 ? 29.634  -47.294 -55.542 1.00 141.65 ? 173  CYS   E CB  1 
ATOM   12663 S  SG  . CYS   E 2 173 ? 28.387  -45.943 -55.506 1.00 152.33 ? 173  CYS   E SG  1 
ATOM   12664 N  N   . GLN   E 2 174 ? 28.796  -49.533 -57.687 1.00 129.55 ? 174  GLN   E N   1 
ATOM   12665 C  CA  . GLN   E 2 174 ? 27.649  -50.190 -58.306 1.00 127.46 ? 174  GLN   E CA  1 
ATOM   12666 C  C   . GLN   E 2 174 ? 26.362  -49.894 -57.537 1.00 127.00 ? 174  GLN   E C   1 
ATOM   12667 O  O   . GLN   E 2 174 ? 25.382  -49.397 -58.107 1.00 122.49 ? 174  GLN   E O   1 
ATOM   12668 C  CB  . GLN   E 2 174 ? 27.900  -51.693 -58.387 1.00 129.38 ? 174  GLN   E CB  1 
ATOM   12669 C  CG  . GLN   E 2 174 ? 28.282  -52.304 -57.044 1.00 128.12 ? 174  GLN   E CG  1 
ATOM   12670 C  CD  . GLN   E 2 174 ? 28.796  -53.710 -57.165 1.00 127.78 ? 174  GLN   E CD  1 
ATOM   12671 O  OE1 . GLN   E 2 174 ? 29.020  -54.207 -58.274 1.00 130.00 ? 174  GLN   E OE1 1 
ATOM   12672 N  NE2 . GLN   E 2 174 ? 28.998  -54.367 -56.023 1.00 120.17 ? 174  GLN   E NE2 1 
ATOM   12673 N  N   . ALA   E 2 175 ? 26.349  -50.196 -56.243 1.00 127.05 ? 175  ALA   E N   1 
ATOM   12674 C  CA  . ALA   E 2 175 ? 25.301  -49.883 -55.295 1.00 122.72 ? 175  ALA   E CA  1 
ATOM   12675 C  C   . ALA   E 2 175 ? 25.795  -48.778 -54.378 1.00 123.14 ? 175  ALA   E C   1 
ATOM   12676 O  O   . ALA   E 2 175 ? 27.003  -48.551 -54.292 1.00 129.84 ? 175  ALA   E O   1 
ATOM   12677 C  CB  . ALA   E 2 175 ? 24.944  -51.130 -54.480 1.00 121.98 ? 175  ALA   E CB  1 
ATOM   12678 N  N   . PRO   E 2 176 ? 24.908  -48.058 -53.689 1.00 118.21 ? 176  PRO   E N   1 
ATOM   12679 C  CA  . PRO   E 2 176 ? 25.360  -46.905 -52.883 1.00 120.97 ? 176  PRO   E CA  1 
ATOM   12680 C  C   . PRO   E 2 176 ? 26.396  -47.297 -51.827 1.00 121.51 ? 176  PRO   E C   1 
ATOM   12681 O  O   . PRO   E 2 176 ? 26.221  -48.273 -51.093 1.00 122.79 ? 176  PRO   E O   1 
ATOM   12682 C  CB  . PRO   E 2 176 ? 24.062  -46.397 -52.239 1.00 118.22 ? 176  PRO   E CB  1 
ATOM   12683 C  CG  . PRO   E 2 176 ? 22.983  -46.871 -53.146 1.00 121.10 ? 176  PRO   E CG  1 
ATOM   12684 C  CD  . PRO   E 2 176 ? 23.440  -48.193 -53.683 1.00 116.69 ? 176  PRO   E CD  1 
ATOM   12685 N  N   . THR   E 2 177 ? 27.479  -46.512 -51.751 1.00 118.45 ? 177  THR   E N   1 
ATOM   12686 C  CA  . THR   E 2 177 ? 28.629  -46.834 -50.906 1.00 117.55 ? 177  THR   E CA  1 
ATOM   12687 C  C   . THR   E 2 177 ? 29.196  -45.588 -50.225 1.00 116.65 ? 177  THR   E C   1 
ATOM   12688 O  O   . THR   E 2 177 ? 29.414  -44.553 -50.864 1.00 114.96 ? 177  THR   E O   1 
ATOM   12689 C  CB  . THR   E 2 177 ? 29.741  -47.508 -51.718 1.00 118.44 ? 177  THR   E CB  1 
ATOM   12690 O  OG1 . THR   E 2 177 ? 29.197  -48.599 -52.460 1.00 120.34 ? 177  THR   E OG1 1 
ATOM   12691 C  CG2 . THR   E 2 177 ? 30.830  -48.043 -50.792 1.00 122.22 ? 177  THR   E CG2 1 
ATOM   12692 N  N   . ILE   E 2 178 ? 29.472  -45.713 -48.926 1.00 116.22 ? 178  ILE   E N   1 
ATOM   12693 C  CA  . ILE   E 2 178 ? 30.012  -44.626 -48.115 1.00 111.22 ? 178  ILE   E CA  1 
ATOM   12694 C  C   . ILE   E 2 178 ? 31.427  -44.965 -47.694 1.00 111.59 ? 178  ILE   E C   1 
ATOM   12695 O  O   . ILE   E 2 178 ? 31.722  -46.090 -47.272 1.00 115.25 ? 178  ILE   E O   1 
ATOM   12696 C  CB  . ILE   E 2 178 ? 29.163  -44.334 -46.869 1.00 108.73 ? 178  ILE   E CB  1 
ATOM   12697 C  CG1 . ILE   E 2 178 ? 28.929  -45.617 -46.086 1.00 108.95 ? 178  ILE   E CG1 1 
ATOM   12698 C  CG2 . ILE   E 2 178 ? 27.861  -43.670 -47.238 1.00 108.73 ? 178  ILE   E CG2 1 
ATOM   12699 C  CD1 . ILE   E 2 178 ? 28.641  -45.382 -44.660 1.00 106.58 ? 178  ILE   E CD1 1 
ATOM   12700 N  N   . CYS   E 2 179 ? 32.285  -43.964 -47.752 1.00 109.17 ? 179  CYS   E N   1 
ATOM   12701 C  CA  . CYS   E 2 179 ? 33.673  -44.061 -47.343 1.00 107.51 ? 179  CYS   E CA  1 
ATOM   12702 C  C   . CYS   E 2 179 ? 33.847  -43.173 -46.118 1.00 104.41 ? 179  CYS   E C   1 
ATOM   12703 O  O   . CYS   E 2 179 ? 33.647  -41.958 -46.198 1.00 100.91 ? 179  CYS   E O   1 
ATOM   12704 C  CB  . CYS   E 2 179 ? 34.570  -43.630 -48.499 1.00 107.12 ? 179  CYS   E CB  1 
ATOM   12705 S  SG  . CYS   E 2 179 ? 36.295  -43.726 -48.183 1.00 116.19 ? 179  CYS   E SG  1 
ATOM   12706 N  N   . PHE   E 2 180 ? 34.171  -43.779 -44.984 1.00 109.24 ? 180  PHE   E N   1 
ATOM   12707 C  CA  . PHE   E 2 180 ? 34.294  -43.052 -43.731 1.00 107.62 ? 180  PHE   E CA  1 
ATOM   12708 C  C   . PHE   E 2 180 ? 35.660  -43.313 -43.111 1.00 110.71 ? 180  PHE   E C   1 
ATOM   12709 O  O   . PHE   E 2 180 ? 36.184  -44.426 -43.204 1.00 116.48 ? 180  PHE   E O   1 
ATOM   12710 C  CB  . PHE   E 2 180 ? 33.166  -43.442 -42.750 1.00 107.92 ? 180  PHE   E CB  1 
ATOM   12711 C  CG  . PHE   E 2 180 ? 33.094  -44.904 -42.460 1.00 112.72 ? 180  PHE   E CG  1 
ATOM   12712 C  CD1 . PHE   E 2 180 ? 32.560  -45.783 -43.388 1.00 116.26 ? 180  PHE   E CD1 1 
ATOM   12713 C  CD2 . PHE   E 2 180 ? 33.563  -45.404 -41.257 1.00 114.20 ? 180  PHE   E CD2 1 
ATOM   12714 C  CE1 . PHE   E 2 180 ? 32.502  -47.132 -43.126 1.00 120.66 ? 180  PHE   E CE1 1 
ATOM   12715 C  CE2 . PHE   E 2 180 ? 33.507  -46.747 -40.983 1.00 118.64 ? 180  PHE   E CE2 1 
ATOM   12716 C  CZ  . PHE   E 2 180 ? 32.974  -47.616 -41.915 1.00 121.64 ? 180  PHE   E CZ  1 
ATOM   12717 N  N   . VAL   E 2 181 ? 36.244  -42.255 -42.527 1.00 105.89 ? 181  VAL   E N   1 
ATOM   12718 C  CA  . VAL   E 2 181 ? 37.447  -42.340 -41.690 1.00 110.08 ? 181  VAL   E CA  1 
ATOM   12719 C  C   . VAL   E 2 181 ? 36.995  -42.509 -40.250 1.00 110.45 ? 181  VAL   E C   1 
ATOM   12720 O  O   . VAL   E 2 181 ? 36.099  -41.797 -39.790 1.00 112.69 ? 181  VAL   E O   1 
ATOM   12721 C  CB  . VAL   E 2 181 ? 38.328  -41.084 -41.839 1.00 104.95 ? 181  VAL   E CB  1 
ATOM   12722 C  CG1 . VAL   E 2 181 ? 39.421  -41.040 -40.767 1.00 104.63 ? 181  VAL   E CG1 1 
ATOM   12723 C  CG2 . VAL   E 2 181 ? 38.956  -41.034 -43.209 1.00 104.89 ? 181  VAL   E CG2 1 
ATOM   12724 N  N   . TYR   E 2 182 ? 37.610  -43.455 -39.535 1.00 112.48 ? 182  TYR   E N   1 
ATOM   12725 C  CA  . TYR   E 2 182 ? 37.274  -43.716 -38.146 1.00 112.38 ? 182  TYR   E CA  1 
ATOM   12726 C  C   . TYR   E 2 182 ? 38.550  -43.871 -37.335 1.00 113.02 ? 182  TYR   E C   1 
ATOM   12727 O  O   . TYR   E 2 182 ? 39.628  -44.120 -37.874 1.00 119.89 ? 182  TYR   E O   1 
ATOM   12728 C  CB  . TYR   E 2 182 ? 36.361  -44.956 -37.998 1.00 113.50 ? 182  TYR   E CB  1 
ATOM   12729 C  CG  . TYR   E 2 182 ? 36.960  -46.266 -38.451 1.00 116.27 ? 182  TYR   E CG  1 
ATOM   12730 C  CD1 . TYR   E 2 182 ? 37.121  -46.560 -39.800 1.00 114.69 ? 182  TYR   E CD1 1 
ATOM   12731 C  CD2 . TYR   E 2 182 ? 37.334  -47.221 -37.525 1.00 119.61 ? 182  TYR   E CD2 1 
ATOM   12732 C  CE1 . TYR   E 2 182 ? 37.658  -47.753 -40.201 1.00 118.13 ? 182  TYR   E CE1 1 
ATOM   12733 C  CE2 . TYR   E 2 182 ? 37.868  -48.414 -37.916 1.00 119.64 ? 182  TYR   E CE2 1 
ATOM   12734 C  CZ  . TYR   E 2 182 ? 38.029  -48.681 -39.247 1.00 119.07 ? 182  TYR   E CZ  1 
ATOM   12735 O  OH  . TYR   E 2 182 ? 38.567  -49.893 -39.594 1.00 124.70 ? 182  TYR   E OH  1 
ATOM   12736 N  N   . GLN   E 2 183 ? 38.427  -43.675 -36.033 1.00 110.63 ? 183  GLN   E N   1 
ATOM   12737 C  CA  . GLN   E 2 183 ? 39.555  -43.773 -35.128 1.00 118.90 ? 183  GLN   E CA  1 
ATOM   12738 C  C   . GLN   E 2 183 ? 39.121  -44.675 -33.987 1.00 125.66 ? 183  GLN   E C   1 
ATOM   12739 O  O   . GLN   E 2 183 ? 38.161  -44.357 -33.279 1.00 128.52 ? 183  GLN   E O   1 
ATOM   12740 C  CB  . GLN   E 2 183 ? 39.976  -42.387 -34.624 1.00 123.61 ? 183  GLN   E CB  1 
ATOM   12741 N  N   . ASP   E 2 184 ? 39.773  -45.824 -33.850 1.00 125.32 ? 184  ASP   E N   1 
ATOM   12742 C  CA  . ASP   E 2 184 ? 39.513  -46.678 -32.698 1.00 130.64 ? 184  ASP   E CA  1 
ATOM   12743 C  C   . ASP   E 2 184 ? 40.828  -46.806 -31.937 1.00 135.14 ? 184  ASP   E C   1 
ATOM   12744 O  O   . ASP   E 2 184 ? 41.823  -46.224 -32.378 1.00 138.53 ? 184  ASP   E O   1 
ATOM   12745 C  CB  . ASP   E 2 184 ? 38.937  -48.029 -33.129 1.00 129.99 ? 184  ASP   E CB  1 
ATOM   12746 C  CG  . ASP   E 2 184 ? 39.916  -48.855 -33.922 1.00 138.29 ? 184  ASP   E CG  1 
ATOM   12747 O  OD1 . ASP   E 2 184 ? 40.997  -48.341 -34.281 1.00 141.78 ? 184  ASP   E OD1 1 
ATOM   12748 O  OD2 . ASP   E 2 184 ? 39.597  -50.036 -34.184 1.00 142.08 ? 184  ASP   E OD2 1 
ATOM   12749 N  N   . PRO   E 2 185 ? 40.878  -47.506 -30.777 1.00 138.84 ? 185  PRO   E N   1 
ATOM   12750 C  CA  . PRO   E 2 185 ? 42.158  -47.689 -30.070 1.00 142.78 ? 185  PRO   E CA  1 
ATOM   12751 C  C   . PRO   E 2 185 ? 43.379  -47.979 -30.938 1.00 146.70 ? 185  PRO   E C   1 
ATOM   12752 O  O   . PRO   E 2 185 ? 44.470  -47.479 -30.639 1.00 144.07 ? 185  PRO   E O   1 
ATOM   12753 C  CB  . PRO   E 2 185 ? 41.850  -48.866 -29.145 1.00 142.26 ? 185  PRO   E CB  1 
ATOM   12754 C  CG  . PRO   E 2 185 ? 40.406  -48.628 -28.757 1.00 139.69 ? 185  PRO   E CG  1 
ATOM   12755 C  CD  . PRO   E 2 185 ? 39.742  -47.924 -29.932 1.00 139.09 ? 185  PRO   E CD  1 
ATOM   12756 N  N   . GLN   E 2 186 ? 43.173  -48.781 -31.982 1.00 155.91 ? 186  GLN   E N   1 
ATOM   12757 C  CA  . GLN   E 2 186 ? 44.299  -49.201 -32.851 1.00 157.38 ? 186  GLN   E CA  1 
ATOM   12758 C  C   . GLN   E 2 186 ? 44.858  -47.986 -33.600 1.00 155.70 ? 186  GLN   E C   1 
ATOM   12759 O  O   . GLN   E 2 186 ? 46.066  -47.986 -33.907 1.00 155.83 ? 186  GLN   E O   1 
ATOM   12760 C  CB  . GLN   E 2 186 ? 43.776  -50.268 -33.811 1.00 155.59 ? 186  GLN   E CB  1 
ATOM   12761 C  CG  . GLN   E 2 186 ? 43.649  -51.655 -33.191 1.00 158.39 ? 186  GLN   E CG  1 
ATOM   12762 C  CD  . GLN   E 2 186 ? 42.611  -51.739 -32.093 1.00 161.71 ? 186  GLN   E CD  1 
ATOM   12763 O  OE1 . GLN   E 2 186 ? 41.576  -51.065 -32.129 1.00 157.98 ? 186  GLN   E OE1 1 
ATOM   12764 N  NE2 . GLN   E 2 186 ? 42.887  -52.563 -31.094 1.00 164.72 ? 186  GLN   E NE2 1 
ATOM   12765 N  N   . GLY   E 2 187 ? 44.007  -47.000 -33.885 1.00 147.27 ? 187  GLY   E N   1 
ATOM   12766 C  CA  . GLY   E 2 187 ? 44.468  -45.786 -34.579 1.00 140.00 ? 187  GLY   E CA  1 
ATOM   12767 C  C   . GLY   E 2 187 ? 43.437  -45.283 -35.566 1.00 136.04 ? 187  GLY   E C   1 
ATOM   12768 O  O   . GLY   E 2 187 ? 42.255  -45.655 -35.428 1.00 133.39 ? 187  GLY   E O   1 
ATOM   12769 N  N   . ARG   E 2 188 ? 43.869  -44.465 -36.527 1.00 130.76 ? 188  ARG   E N   1 
ATOM   12770 C  CA  . ARG   E 2 188 ? 42.936  -43.898 -37.531 1.00 128.09 ? 188  ARG   E CA  1 
ATOM   12771 C  C   . ARG   E 2 188 ? 43.001  -44.759 -38.795 1.00 134.12 ? 188  ARG   E C   1 
ATOM   12772 O  O   . ARG   E 2 188 ? 44.117  -44.969 -39.313 1.00 132.65 ? 188  ARG   E O   1 
ATOM   12773 C  CB  . ARG   E 2 188 ? 43.295  -42.443 -37.840 1.00 119.37 ? 188  ARG   E CB  1 
ATOM   12774 N  N   . HIS   E 2 189 ? 41.847  -45.242 -39.257 1.00 141.30 ? 189  HIS   E N   1 
ATOM   12775 C  CA  . HIS   E 2 189 ? 41.811  -46.118 -40.455 1.00 139.95 ? 189  HIS   E CA  1 
ATOM   12776 C  C   . HIS   E 2 189 ? 40.636  -45.729 -41.353 1.00 137.68 ? 189  HIS   E C   1 
ATOM   12777 O  O   . HIS   E 2 189 ? 39.788  -44.924 -40.920 1.00 137.81 ? 189  HIS   E O   1 
ATOM   12778 C  CB  . HIS   E 2 189 ? 41.701  -47.588 -40.044 1.00 140.57 ? 189  HIS   E CB  1 
ATOM   12779 C  CG  . HIS   E 2 189 ? 42.105  -47.886 -38.643 1.00 142.84 ? 189  HIS   E CG  1 
ATOM   12780 N  ND1 . HIS   E 2 189 ? 43.425  -47.998 -38.266 1.00 147.20 ? 189  HIS   E ND1 1 
ATOM   12781 C  CD2 . HIS   E 2 189 ? 41.384  -48.106 -37.541 1.00 144.07 ? 189  HIS   E CD2 1 
ATOM   12782 C  CE1 . HIS   E 2 189 ? 43.486  -48.280 -36.975 1.00 148.40 ? 189  HIS   E CE1 1 
ATOM   12783 N  NE2 . HIS   E 2 189 ? 42.257  -48.344 -36.514 1.00 148.64 ? 189  HIS   E NE2 1 
ATOM   12784 N  N   . VAL   E 2 190 ? 40.585  -46.287 -42.564 1.00 131.58 ? 190  VAL   E N   1 
ATOM   12785 C  CA  . VAL   E 2 190 ? 39.510  -46.010 -43.509 1.00 123.95 ? 190  VAL   E CA  1 
ATOM   12786 C  C   . VAL   E 2 190 ? 38.766  -47.308 -43.812 1.00 125.91 ? 190  VAL   E C   1 
ATOM   12787 O  O   . VAL   E 2 190 ? 39.396  -48.345 -44.044 1.00 130.22 ? 190  VAL   E O   1 
ATOM   12788 C  CB  . VAL   E 2 190 ? 40.050  -45.379 -44.807 1.00 121.06 ? 190  VAL   E CB  1 
ATOM   12789 C  CG1 . VAL   E 2 190 ? 38.901  -44.861 -45.637 1.00 118.09 ? 190  VAL   E CG1 1 
ATOM   12790 C  CG2 . VAL   E 2 190 ? 41.046  -44.262 -44.511 1.00 121.69 ? 190  VAL   E CG2 1 
ATOM   12791 N  N   . LYS   E 2 191 ? 37.427  -47.253 -43.811 1.00 122.23 ? 191  LYS   E N   1 
ATOM   12792 C  CA  . LYS   E 2 191 ? 36.591  -48.385 -44.231 1.00 121.27 ? 191  LYS   E CA  1 
ATOM   12793 C  C   . LYS   E 2 191 ? 35.425  -47.896 -45.090 1.00 119.64 ? 191  LYS   E C   1 
ATOM   12794 O  O   . LYS   E 2 191 ? 35.076  -46.713 -45.086 1.00 117.53 ? 191  LYS   E O   1 
ATOM   12795 C  CB  . LYS   E 2 191 ? 36.045  -49.192 -43.042 1.00 114.50 ? 191  LYS   E CB  1 
ATOM   12796 N  N   . THR   E 2 192 ? 34.821  -48.827 -45.828 1.00 126.32 ? 192  THR   E N   1 
ATOM   12797 C  CA  . THR   E 2 192 ? 33.719  -48.532 -46.734 1.00 126.59 ? 192  THR   E CA  1 
ATOM   12798 C  C   . THR   E 2 192 ? 32.619  -49.561 -46.551 1.00 127.52 ? 192  THR   E C   1 
ATOM   12799 O  O   . THR   E 2 192 ? 32.881  -50.768 -46.516 1.00 127.02 ? 192  THR   E O   1 
ATOM   12800 C  CB  . THR   E 2 192 ? 34.128  -48.536 -48.232 1.00 127.41 ? 192  THR   E CB  1 
ATOM   12801 O  OG1 . THR   E 2 192 ? 34.573  -49.841 -48.615 1.00 128.85 ? 192  THR   E OG1 1 
ATOM   12802 C  CG2 . THR   E 2 192 ? 35.215  -47.528 -48.508 1.00 129.22 ? 192  THR   E CG2 1 
ATOM   12803 N  N   . TYR   E 2 193 ? 31.391  -49.075 -46.448 1.00 123.35 ? 193  TYR   E N   1 
ATOM   12804 C  CA  . TYR   E 2 193 ? 30.213  -49.922 -46.408 1.00 121.56 ? 193  TYR   E CA  1 
ATOM   12805 C  C   . TYR   E 2 193 ? 29.306  -49.572 -47.575 1.00 118.62 ? 193  TYR   E C   1 
ATOM   12806 O  O   . TYR   E 2 193 ? 29.294  -48.435 -48.048 1.00 116.31 ? 193  TYR   E O   1 
ATOM   12807 C  CB  . TYR   E 2 193 ? 29.433  -49.758 -45.098 1.00 120.96 ? 193  TYR   E CB  1 
ATOM   12808 C  CG  . TYR   E 2 193 ? 30.166  -50.242 -43.879 1.00 117.19 ? 193  TYR   E CG  1 
ATOM   12809 C  CD1 . TYR   E 2 193 ? 31.333  -50.984 -43.997 1.00 118.86 ? 193  TYR   E CD1 1 
ATOM   12810 C  CD2 . TYR   E 2 193 ? 29.691  -49.970 -42.607 1.00 120.90 ? 193  TYR   E CD2 1 
ATOM   12811 C  CE1 . TYR   E 2 193 ? 32.016  -51.437 -42.890 1.00 123.78 ? 193  TYR   E CE1 1 
ATOM   12812 C  CE2 . TYR   E 2 193 ? 30.371  -50.424 -41.475 1.00 124.31 ? 193  TYR   E CE2 1 
ATOM   12813 C  CZ  . TYR   E 2 193 ? 31.537  -51.159 -41.630 1.00 124.98 ? 193  TYR   E CZ  1 
ATOM   12814 O  OH  . TYR   E 2 193 ? 32.238  -51.619 -40.541 1.00 120.41 ? 193  TYR   E OH  1 
ATOM   12815 N  N   . GLU   E 2 194 ? 28.528  -50.555 -48.013 1.00 125.79 ? 194  GLU   E N   1 
ATOM   12816 C  CA  . GLU   E 2 194 ? 27.483  -50.368 -49.011 1.00 127.15 ? 194  GLU   E CA  1 
ATOM   12817 C  C   . GLU   E 2 194 ? 26.120  -50.285 -48.323 1.00 127.43 ? 194  GLU   E C   1 
ATOM   12818 O  O   . GLU   E 2 194 ? 25.930  -50.791 -47.215 1.00 129.81 ? 194  GLU   E O   1 
ATOM   12819 C  CB  . GLU   E 2 194 ? 27.482  -51.507 -50.045 1.00 128.91 ? 194  GLU   E CB  1 
ATOM   12820 C  CG  . GLU   E 2 194 ? 28.716  -51.580 -50.952 1.00 128.72 ? 194  GLU   E CG  1 
ATOM   12821 C  CD  . GLU   E 2 194 ? 28.393  -52.066 -52.371 1.00 130.95 ? 194  GLU   E CD  1 
ATOM   12822 O  OE1 . GLU   E 2 194 ? 27.909  -53.208 -52.543 1.00 130.02 ? 194  GLU   E OE1 1 
ATOM   12823 O  OE2 . GLU   E 2 194 ? 28.603  -51.288 -53.327 1.00 133.11 ? 194  GLU   E OE2 1 
ATOM   12824 N  N   . VAL   E 2 195 ? 25.159  -49.654 -49.003 1.00 123.86 ? 195  VAL   E N   1 
ATOM   12825 C  CA  . VAL   E 2 195 ? 23.864  -49.323 -48.414 1.00 124.14 ? 195  VAL   E CA  1 
ATOM   12826 C  C   . VAL   E 2 195 ? 22.752  -49.978 -49.220 1.00 128.45 ? 195  VAL   E C   1 
ATOM   12827 O  O   . VAL   E 2 195 ? 22.530  -49.624 -50.389 1.00 125.29 ? 195  VAL   E O   1 
ATOM   12828 C  CB  . VAL   E 2 195 ? 23.644  -47.807 -48.345 1.00 120.77 ? 195  VAL   E CB  1 
ATOM   12829 C  CG1 . VAL   E 2 195 ? 22.256  -47.505 -47.827 1.00 119.18 ? 195  VAL   E CG1 1 
ATOM   12830 C  CG2 . VAL   E 2 195 ? 24.690  -47.177 -47.470 1.00 121.28 ? 195  VAL   E CG2 1 
ATOM   12831 N  N   . SER   E 2 196 ? 22.033  -50.905 -48.586 1.00 127.12 ? 196  SER   E N   1 
ATOM   12832 C  CA  . SER   E 2 196 ? 20.878  -51.566 -49.190 1.00 132.54 ? 196  SER   E CA  1 
ATOM   12833 C  C   . SER   E 2 196 ? 19.623  -50.975 -48.560 1.00 131.20 ? 196  SER   E C   1 
ATOM   12834 O  O   . SER   E 2 196 ? 19.351  -51.196 -47.375 1.00 130.07 ? 196  SER   E O   1 
ATOM   12835 C  CB  . SER   E 2 196 ? 20.939  -53.087 -49.001 1.00 138.35 ? 196  SER   E CB  1 
ATOM   12836 O  OG  . SER   E 2 196 ? 19.952  -53.785 -49.763 1.00 138.15 ? 196  SER   E OG  1 
ATOM   12837 N  N   . LEU   E 2 197 ? 18.868  -50.210 -49.351 1.00 130.87 ? 197  LEU   E N   1 
ATOM   12838 C  CA  . LEU   E 2 197 ? 17.594  -49.704 -48.862 1.00 130.71 ? 197  LEU   E CA  1 
ATOM   12839 C  C   . LEU   E 2 197 ? 16.586  -50.838 -48.705 1.00 137.22 ? 197  LEU   E C   1 
ATOM   12840 O  O   . LEU   E 2 197 ? 15.826  -50.867 -47.731 1.00 137.50 ? 197  LEU   E O   1 
ATOM   12841 C  CB  . LEU   E 2 197 ? 17.062  -48.618 -49.798 1.00 123.89 ? 197  LEU   E CB  1 
ATOM   12842 C  CG  . LEU   E 2 197 ? 18.007  -47.455 -50.114 1.00 123.29 ? 197  LEU   E CG  1 
ATOM   12843 C  CD1 . LEU   E 2 197 ? 18.937  -47.808 -51.261 1.00 127.67 ? 197  LEU   E CD1 1 
ATOM   12844 C  CD2 . LEU   E 2 197 ? 17.218  -46.201 -50.444 1.00 119.77 ? 197  LEU   E CD2 1 
ATOM   12845 N  N   . ARG   E 2 198 ? 16.585  -51.797 -49.640 1.00 137.86 ? 198  ARG   E N   1 
ATOM   12846 C  CA  . ARG   E 2 198 ? 15.640  -52.908 -49.551 1.00 139.01 ? 198  ARG   E CA  1 
ATOM   12847 C  C   . ARG   E 2 198 ? 15.973  -53.826 -48.380 1.00 137.30 ? 198  ARG   E C   1 
ATOM   12848 O  O   . ARG   E 2 198 ? 15.074  -54.252 -47.643 1.00 135.08 ? 198  ARG   E O   1 
ATOM   12849 C  CB  . ARG   E 2 198 ? 15.620  -53.682 -50.870 1.00 143.58 ? 198  ARG   E CB  1 
ATOM   12850 C  CG  . ARG   E 2 198 ? 16.990  -54.069 -51.393 1.00 148.66 ? 198  ARG   E CG  1 
ATOM   12851 C  CD  . ARG   E 2 198 ? 16.935  -55.426 -52.110 1.00 153.66 ? 198  ARG   E CD  1 
ATOM   12852 N  NE  . ARG   E 2 198 ? 16.500  -56.501 -51.222 1.00 151.83 ? 198  ARG   E NE  1 
ATOM   12853 C  CZ  . ARG   E 2 198 ? 17.310  -57.196 -50.433 1.00 151.89 ? 198  ARG   E CZ  1 
ATOM   12854 N  NH1 . ARG   E 2 198 ? 18.613  -56.961 -50.399 1.00 153.28 ? 198  ARG   E NH1 1 
ATOM   12855 N  NH2 . ARG   E 2 198 ? 16.802  -58.148 -49.653 1.00 150.34 ? 198  ARG   E NH2 1 
ATOM   12856 N  N   . GLU   E 2 199 ? 17.250  -54.145 -48.190 1.00 145.16 ? 199  GLU   E N   1 
ATOM   12857 C  CA  . GLU   E 2 199 ? 17.654  -54.865 -46.992 1.00 150.21 ? 199  GLU   E CA  1 
ATOM   12858 C  C   . GLU   E 2 199 ? 17.680  -53.964 -45.753 1.00 151.42 ? 199  GLU   E C   1 
ATOM   12859 O  O   . GLU   E 2 199 ? 17.817  -54.479 -44.636 1.00 155.21 ? 199  GLU   E O   1 
ATOM   12860 C  CB  . GLU   E 2 199 ? 19.025  -55.520 -47.230 1.00 153.02 ? 199  GLU   E CB  1 
ATOM   12861 C  CG  . GLU   E 2 199 ? 19.461  -56.579 -46.193 1.00 156.74 ? 199  GLU   E CG  1 
ATOM   12862 C  CD  . GLU   E 2 199 ? 20.948  -56.461 -45.811 1.00 157.35 ? 199  GLU   E CD  1 
ATOM   12863 O  OE1 . GLU   E 2 199 ? 21.674  -55.699 -46.491 1.00 159.92 ? 199  GLU   E OE1 1 
ATOM   12864 O  OE2 . GLU   E 2 199 ? 21.389  -57.113 -44.829 1.00 155.77 ? 199  GLU   E OE2 1 
ATOM   12865 N  N   . LYS   E 2 200 ? 17.537  -52.641 -45.922 1.00 140.47 ? 200  LYS   E N   1 
ATOM   12866 C  CA  . LYS   E 2 200 ? 17.553  -51.668 -44.816 1.00 131.73 ? 200  LYS   E CA  1 
ATOM   12867 C  C   . LYS   E 2 200 ? 18.721  -51.895 -43.871 1.00 129.91 ? 200  LYS   E C   1 
ATOM   12868 O  O   . LYS   E 2 200 ? 18.619  -51.620 -42.681 1.00 131.30 ? 200  LYS   E O   1 
ATOM   12869 C  CB  . LYS   E 2 200 ? 16.249  -51.679 -44.015 1.00 131.06 ? 200  LYS   E CB  1 
ATOM   12870 C  CG  . LYS   E 2 200 ? 14.977  -51.486 -44.832 1.00 135.49 ? 200  LYS   E CG  1 
ATOM   12871 C  CD  . LYS   E 2 200 ? 14.352  -50.102 -44.625 1.00 131.38 ? 200  LYS   E CD  1 
ATOM   12872 C  CE  . LYS   E 2 200 ? 13.048  -49.975 -45.436 1.00 135.17 ? 200  LYS   E CE  1 
ATOM   12873 N  NZ  . LYS   E 2 200 ? 12.640  -48.569 -45.767 1.00 129.38 ? 200  LYS   E NZ  1 
ATOM   12874 N  N   . GLU   E 2 201 ? 19.833  -52.423 -44.365 1.00 136.71 ? 201  GLU   E N   1 
ATOM   12875 C  CA  . GLU   E 2 201 ? 21.007  -52.602 -43.527 1.00 136.35 ? 201  GLU   E CA  1 
ATOM   12876 C  C   . GLU   E 2 201 ? 22.233  -52.286 -44.379 1.00 136.66 ? 201  GLU   E C   1 
ATOM   12877 O  O   . GLU   E 2 201 ? 22.125  -51.722 -45.475 1.00 131.54 ? 201  GLU   E O   1 
ATOM   12878 C  CB  . GLU   E 2 201 ? 21.026  -54.012 -42.917 1.00 137.50 ? 201  GLU   E CB  1 
ATOM   12879 N  N   . PHE   E 2 202 ? 23.405  -52.657 -43.872 1.00 132.28 ? 202  PHE   E N   1 
ATOM   12880 C  CA  . PHE   E 2 202 ? 24.673  -52.449 -44.559 1.00 133.43 ? 202  PHE   E CA  1 
ATOM   12881 C  C   . PHE   E 2 202 ? 25.133  -53.716 -45.274 1.00 136.45 ? 202  PHE   E C   1 
ATOM   12882 O  O   . PHE   E 2 202 ? 24.671  -54.825 -44.988 1.00 142.20 ? 202  PHE   E O   1 
ATOM   12883 C  CB  . PHE   E 2 202 ? 25.755  -51.996 -43.573 1.00 133.44 ? 202  PHE   E CB  1 
ATOM   12884 C  CG  . PHE   E 2 202 ? 25.824  -50.505 -43.387 1.00 131.26 ? 202  PHE   E CG  1 
ATOM   12885 C  CD1 . PHE   E 2 202 ? 25.905  -49.662 -44.477 1.00 131.15 ? 202  PHE   E CD1 1 
ATOM   12886 C  CD2 . PHE   E 2 202 ? 25.799  -49.952 -42.122 1.00 126.39 ? 202  PHE   E CD2 1 
ATOM   12887 C  CE1 . PHE   E 2 202 ? 25.958  -48.306 -44.310 1.00 129.73 ? 202  PHE   E CE1 1 
ATOM   12888 C  CE2 . PHE   E 2 202 ? 25.844  -48.596 -41.953 1.00 126.03 ? 202  PHE   E CE2 1 
ATOM   12889 C  CZ  . PHE   E 2 202 ? 25.929  -47.770 -43.048 1.00 127.74 ? 202  PHE   E CZ  1 
ATOM   12890 N  N   . ASN   E 2 203 ? 26.049  -53.528 -46.227 1.00 138.34 ? 203  ASN   E N   1 
ATOM   12891 C  CA  . ASN   E 2 203 ? 26.749  -54.608 -46.912 1.00 139.15 ? 203  ASN   E CA  1 
ATOM   12892 C  C   . ASN   E 2 203 ? 28.226  -54.239 -47.013 1.00 137.61 ? 203  ASN   E C   1 
ATOM   12893 O  O   . ASN   E 2 203 ? 28.566  -53.066 -47.177 1.00 135.97 ? 203  ASN   E O   1 
ATOM   12894 C  CB  . ASN   E 2 203 ? 26.166  -54.874 -48.319 1.00 138.35 ? 203  ASN   E CB  1 
ATOM   12895 C  CG  . ASN   E 2 203 ? 24.863  -55.690 -48.292 1.00 143.32 ? 203  ASN   E CG  1 
ATOM   12896 O  OD1 . ASN   E 2 203 ? 24.622  -56.486 -47.374 1.00 146.44 ? 203  ASN   E OD1 1 
ATOM   12897 N  ND2 . ASN   E 2 203 ? 24.029  -55.506 -49.323 1.00 141.58 ? 203  ASN   E ND2 1 
ATOM   12898 N  N   . LYS   E 2 204 ? 29.104  -55.243 -46.908 1.00 127.89 ? 204  LYS   E N   1 
ATOM   12899 C  CA  . LYS   E 2 204 ? 30.547  -55.001 -46.858 1.00 125.68 ? 204  LYS   E CA  1 
ATOM   12900 C  C   . LYS   E 2 204 ? 31.051  -54.298 -48.121 1.00 124.41 ? 204  LYS   E C   1 
ATOM   12901 O  O   . LYS   E 2 204 ? 30.790  -54.747 -49.239 1.00 125.38 ? 204  LYS   E O   1 
ATOM   12902 C  CB  . LYS   E 2 204 ? 31.290  -56.323 -46.660 1.00 120.68 ? 204  LYS   E CB  1 
ATOM   12903 N  N   . GLY   E 2 205 ? 31.799  -53.202 -47.943 1.00 119.01 ? 205  GLY   E N   1 
ATOM   12904 C  CA  . GLY   E 2 205 ? 32.203  -52.372 -49.058 1.00 119.81 ? 205  GLY   E CA  1 
ATOM   12905 C  C   . GLY   E 2 205 ? 33.379  -52.940 -49.832 1.00 119.11 ? 205  GLY   E C   1 
ATOM   12906 O  O   . GLY   E 2 205 ? 33.974  -53.968 -49.467 1.00 120.19 ? 205  GLY   E O   1 
ATOM   12907 N  N   . PRO   E 2 206 ? 33.731  -52.265 -50.945 1.00 117.11 ? 206  PRO   E N   1 
ATOM   12908 C  CA  . PRO   E 2 206 ? 34.873  -52.715 -51.754 1.00 117.94 ? 206  PRO   E CA  1 
ATOM   12909 C  C   . PRO   E 2 206 ? 36.273  -52.702 -51.155 1.00 125.07 ? 206  PRO   E C   1 
ATOM   12910 O  O   . PRO   E 2 206 ? 36.964  -53.724 -51.238 1.00 134.35 ? 206  PRO   E O   1 
ATOM   12911 C  CB  . PRO   E 2 206 ? 34.870  -51.742 -52.940 1.00 116.25 ? 206  PRO   E CB  1 
ATOM   12912 C  CG  . PRO   E 2 206 ? 33.945  -50.654 -52.567 1.00 115.77 ? 206  PRO   E CG  1 
ATOM   12913 C  CD  . PRO   E 2 206 ? 32.944  -51.245 -51.655 1.00 117.15 ? 206  PRO   E CD  1 
ATOM   12914 N  N   . TRP   E 2 207 ? 36.718  -51.592 -50.557 1.00 123.07 ? 207  TRP   E N   1 
ATOM   12915 C  CA  . TRP   E 2 207 ? 38.113  -51.434 -50.146 1.00 126.49 ? 207  TRP   E CA  1 
ATOM   12916 C  C   . TRP   E 2 207 ? 38.171  -50.888 -48.715 1.00 127.29 ? 207  TRP   E C   1 
ATOM   12917 O  O   . TRP   E 2 207 ? 37.235  -50.239 -48.236 1.00 127.08 ? 207  TRP   E O   1 
ATOM   12918 C  CB  . TRP   E 2 207 ? 38.958  -50.551 -51.082 1.00 131.98 ? 207  TRP   E CB  1 
ATOM   12919 C  CG  . TRP   E 2 207 ? 38.264  -49.295 -51.561 1.00 127.41 ? 207  TRP   E CG  1 
ATOM   12920 C  CD1 . TRP   E 2 207 ? 37.378  -49.189 -52.600 1.00 123.27 ? 207  TRP   E CD1 1 
ATOM   12921 C  CD2 . TRP   E 2 207 ? 38.415  -47.968 -51.024 1.00 125.88 ? 207  TRP   E CD2 1 
ATOM   12922 N  NE1 . TRP   E 2 207 ? 36.967  -47.883 -52.735 1.00 124.22 ? 207  TRP   E NE1 1 
ATOM   12923 C  CE2 . TRP   E 2 207 ? 37.587  -47.115 -51.780 1.00 123.84 ? 207  TRP   E CE2 1 
ATOM   12924 C  CE3 . TRP   E 2 207 ? 39.168  -47.421 -49.975 1.00 123.48 ? 207  TRP   E CE3 1 
ATOM   12925 C  CZ2 . TRP   E 2 207 ? 37.492  -45.740 -51.519 1.00 117.41 ? 207  TRP   E CZ2 1 
ATOM   12926 C  CZ3 . TRP   E 2 207 ? 39.070  -46.056 -49.720 1.00 115.43 ? 207  TRP   E CZ3 1 
ATOM   12927 C  CH2 . TRP   E 2 207 ? 38.241  -45.236 -50.488 1.00 114.57 ? 207  TRP   E CH2 1 
ATOM   12928 N  N   . LYS   E 2 208 ? 39.286  -51.172 -48.031 1.00 130.94 ? 208  LYS   E N   1 
ATOM   12929 C  CA  . LYS   E 2 208 ? 39.535  -50.671 -46.680 1.00 131.16 ? 208  LYS   E CA  1 
ATOM   12930 C  C   . LYS   E 2 208 ? 41.034  -50.451 -46.522 1.00 135.52 ? 208  LYS   E C   1 
ATOM   12931 O  O   . LYS   E 2 208 ? 41.845  -50.996 -47.272 1.00 135.14 ? 208  LYS   E O   1 
ATOM   12932 C  CB  . LYS   E 2 208 ? 38.984  -51.623 -45.598 1.00 120.47 ? 208  LYS   E CB  1 
ATOM   12933 C  CG  . LYS   E 2 208 ? 40.006  -52.539 -44.944 1.00 125.79 ? 208  LYS   E CG  1 
ATOM   12934 C  CD  . LYS   E 2 208 ? 39.351  -53.779 -44.324 1.00 123.64 ? 208  LYS   E CD  1 
ATOM   12935 C  CE  . LYS   E 2 208 ? 38.645  -54.637 -45.372 1.00 122.82 ? 208  LYS   E CE  1 
ATOM   12936 N  NZ  . LYS   E 2 208 ? 38.218  -55.976 -44.859 1.00 124.89 ? 208  LYS   E NZ  1 
ATOM   12937 N  N   . GLN   E 2 209 ? 41.401  -49.620 -45.549 1.00 147.46 ? 209  GLN   E N   1 
ATOM   12938 C  CA  . GLN   E 2 209 ? 42.795  -49.270 -45.312 1.00 148.94 ? 209  GLN   E CA  1 
ATOM   12939 C  C   . GLN   E 2 209 ? 43.075  -49.391 -43.825 1.00 149.17 ? 209  GLN   E C   1 
ATOM   12940 O  O   . GLN   E 2 209 ? 42.455  -48.696 -43.015 1.00 148.27 ? 209  GLN   E O   1 
ATOM   12941 C  CB  . GLN   E 2 209 ? 43.111  -47.859 -45.812 1.00 151.66 ? 209  GLN   E CB  1 
ATOM   12942 C  CG  . GLN   E 2 209 ? 44.435  -47.295 -45.300 1.00 151.84 ? 209  GLN   E CG  1 
ATOM   12943 C  CD  . GLN   E 2 209 ? 45.642  -48.023 -45.863 1.00 153.31 ? 209  GLN   E CD  1 
ATOM   12944 O  OE1 . GLN   E 2 209 ? 46.300  -48.803 -45.158 1.00 154.44 ? 209  GLN   E OE1 1 
ATOM   12945 N  NE2 . GLN   E 2 209 ? 45.950  -47.764 -47.138 1.00 149.51 ? 209  GLN   E NE2 1 
ATOM   12946 N  N   . GLU   E 2 210 ? 44.024  -50.261 -43.478 1.00 150.04 ? 210  GLU   E N   1 
ATOM   12947 C  CA  . GLU   E 2 210 ? 44.183  -50.680 -42.092 1.00 152.40 ? 210  GLU   E CA  1 
ATOM   12948 C  C   . GLU   E 2 210 ? 44.717  -49.559 -41.213 1.00 148.34 ? 210  GLU   E C   1 
ATOM   12949 O  O   . GLU   E 2 210 ? 44.417  -49.528 -40.016 1.00 145.42 ? 210  GLU   E O   1 
ATOM   12950 C  CB  . GLU   E 2 210 ? 45.110  -51.898 -42.015 1.00 153.21 ? 210  GLU   E CB  1 
ATOM   12951 C  CG  . GLU   E 2 210 ? 44.863  -52.971 -43.091 1.00 152.71 ? 210  GLU   E CG  1 
ATOM   12952 C  CD  . GLU   E 2 210 ? 43.677  -53.872 -42.783 1.00 149.64 ? 210  GLU   E CD  1 
ATOM   12953 O  OE1 . GLU   E 2 210 ? 43.164  -53.817 -41.647 1.00 146.51 ? 210  GLU   E OE1 1 
ATOM   12954 O  OE2 . GLU   E 2 210 ? 43.262  -54.635 -43.683 1.00 153.66 ? 210  GLU   E OE2 1 
ATOM   12955 N  N   . ASN   E 2 211 ? 45.507  -48.644 -41.769 1.00 140.93 ? 211  ASN   E N   1 
ATOM   12956 C  CA  . ASN   E 2 211 ? 46.188  -47.664 -40.930 1.00 136.80 ? 211  ASN   E CA  1 
ATOM   12957 C  C   . ASN   E 2 211 ? 46.627  -46.490 -41.785 1.00 133.46 ? 211  ASN   E C   1 
ATOM   12958 O  O   . ASN   E 2 211 ? 47.454  -46.669 -42.686 1.00 135.54 ? 211  ASN   E O   1 
ATOM   12959 C  CB  . ASN   E 2 211 ? 47.386  -48.292 -40.242 1.00 135.74 ? 211  ASN   E CB  1 
ATOM   12960 C  CG  . ASN   E 2 211 ? 47.387  -48.039 -38.758 1.00 138.74 ? 211  ASN   E CG  1 
ATOM   12961 O  OD1 . ASN   E 2 211 ? 46.448  -47.453 -38.217 1.00 143.63 ? 211  ASN   E OD1 1 
ATOM   12962 N  ND2 . ASN   E 2 211 ? 48.440  -48.486 -38.082 1.00 138.75 ? 211  ASN   E ND2 1 
ATOM   12963 N  N   . VAL   E 2 212 ? 46.085  -45.305 -41.496 1.00 132.25 ? 212  VAL   E N   1 
ATOM   12964 C  CA  . VAL   E 2 212 ? 46.345  -44.093 -42.265 1.00 125.78 ? 212  VAL   E CA  1 
ATOM   12965 C  C   . VAL   E 2 212 ? 46.764  -43.015 -41.261 1.00 120.86 ? 212  VAL   E C   1 
ATOM   12966 O  O   . VAL   E 2 212 ? 46.804  -43.250 -40.053 1.00 122.48 ? 212  VAL   E O   1 
ATOM   12967 C  CB  . VAL   E 2 212 ? 45.108  -43.695 -43.136 1.00 117.90 ? 212  VAL   E CB  1 
ATOM   12968 C  CG1 . VAL   E 2 212 ? 44.016  -43.036 -42.329 1.00 118.10 ? 212  VAL   E CG1 1 
ATOM   12969 C  CG2 . VAL   E 2 212 ? 45.497  -42.873 -44.377 1.00 115.02 ? 212  VAL   E CG2 1 
ATOM   12970 N  N   . GLU   E 2 213 ? 47.134  -41.835 -41.782 1.00 116.30 ? 213  GLU   E N   1 
ATOM   12971 C  CA  . GLU   E 2 213 ? 47.710  -40.773 -40.959 1.00 114.10 ? 213  GLU   E CA  1 
ATOM   12972 C  C   . GLU   E 2 213 ? 46.870  -40.515 -39.721 1.00 113.88 ? 213  GLU   E C   1 
ATOM   12973 O  O   . GLU   E 2 213 ? 45.639  -40.539 -39.773 1.00 113.66 ? 213  GLU   E O   1 
ATOM   12974 C  CB  . GLU   E 2 213 ? 47.852  -39.479 -41.769 1.00 116.42 ? 213  GLU   E CB  1 
ATOM   12975 C  CG  . GLU   E 2 213 ? 48.150  -38.223 -40.942 1.00 115.35 ? 213  GLU   E CG  1 
ATOM   12976 C  CD  . GLU   E 2 213 ? 48.760  -37.085 -41.761 1.00 117.11 ? 213  GLU   E CD  1 
ATOM   12977 O  OE1 . GLU   E 2 213 ? 48.500  -37.003 -42.983 1.00 117.65 ? 213  GLU   E OE1 1 
ATOM   12978 O  OE2 . GLU   E 2 213 ? 49.514  -36.272 -41.180 1.00 117.78 ? 213  GLU   E OE2 1 
ATOM   12979 N  N   . ALA   E 2 214 ? 47.553  -40.281 -38.595 1.00 121.61 ? 214  ALA   E N   1 
ATOM   12980 C  CA  . ALA   E 2 214 ? 46.873  -40.092 -37.315 1.00 123.49 ? 214  ALA   E CA  1 
ATOM   12981 C  C   . ALA   E 2 214 ? 46.029  -38.823 -37.273 1.00 122.57 ? 214  ALA   E C   1 
ATOM   12982 O  O   . ALA   E 2 214 ? 45.140  -38.717 -36.422 1.00 121.86 ? 214  ALA   E O   1 
ATOM   12983 C  CB  . ALA   E 2 214 ? 47.889  -40.072 -36.168 1.00 126.58 ? 214  ALA   E CB  1 
ATOM   12984 N  N   . GLU   E 2 215 ? 46.292  -37.859 -38.152 1.00 121.06 ? 215  GLU   E N   1 
ATOM   12985 C  CA  . GLU   E 2 215 ? 45.472  -36.661 -38.284 1.00 122.24 ? 215  GLU   E CA  1 
ATOM   12986 C  C   . GLU   E 2 215 ? 44.758  -36.637 -39.632 1.00 121.50 ? 215  GLU   E C   1 
ATOM   12987 O  O   . GLU   E 2 215 ? 44.620  -35.589 -40.267 1.00 120.88 ? 215  GLU   E O   1 
ATOM   12988 C  CB  . GLU   E 2 215 ? 46.308  -35.400 -38.094 1.00 128.12 ? 215  GLU   E CB  1 
ATOM   12989 C  CG  . GLU   E 2 215 ? 47.092  -35.366 -36.800 1.00 129.74 ? 215  GLU   E CG  1 
ATOM   12990 C  CD  . GLU   E 2 215 ? 46.206  -35.216 -35.580 1.00 129.32 ? 215  GLU   E CD  1 
ATOM   12991 O  OE1 . GLU   E 2 215 ? 45.002  -34.900 -35.739 1.00 131.09 ? 215  GLU   E OE1 1 
ATOM   12992 O  OE2 . GLU   E 2 215 ? 46.727  -35.410 -34.459 1.00 129.67 ? 215  GLU   E OE2 1 
ATOM   12993 N  N   . ALA   E 2 216 ? 44.322  -37.813 -40.081 1.00 118.52 ? 216  ALA   E N   1 
ATOM   12994 C  CA  . ALA   E 2 216 ? 43.362  -37.915 -41.169 1.00 109.54 ? 216  ALA   E CA  1 
ATOM   12995 C  C   . ALA   E 2 216 ? 42.040  -37.290 -40.749 1.00 108.48 ? 216  ALA   E C   1 
ATOM   12996 O  O   . ALA   E 2 216 ? 41.475  -37.649 -39.710 1.00 110.45 ? 216  ALA   E O   1 
ATOM   12997 C  CB  . ALA   E 2 216 ? 43.154  -39.379 -41.543 1.00 111.35 ? 216  ALA   E CB  1 
ATOM   12998 N  N   . SER   E 2 217 ? 41.537  -36.362 -41.564 1.00 106.28 ? 217  SER   E N   1 
ATOM   12999 C  CA  . SER   E 2 217 ? 40.363  -35.580 -41.183 1.00 106.39 ? 217  SER   E CA  1 
ATOM   13000 C  C   . SER   E 2 217 ? 39.346  -35.339 -42.290 1.00 105.96 ? 217  SER   E C   1 
ATOM   13001 O  O   . SER   E 2 217 ? 38.206  -34.992 -41.968 1.00 110.54 ? 217  SER   E O   1 
ATOM   13002 C  CB  . SER   E 2 217 ? 40.802  -34.224 -40.626 1.00 115.36 ? 217  SER   E CB  1 
ATOM   13003 O  OG  . SER   E 2 217 ? 41.869  -33.687 -41.391 1.00 109.65 ? 217  SER   E OG  1 
ATOM   13004 N  N   . MET   E 2 218 ? 39.684  -35.511 -43.568 1.00 101.88 ? 218  MET   E N   1 
ATOM   13005 C  CA  . MET   E 2 218 ? 38.839  -35.065 -44.664 1.00 96.65  ? 218  MET   E CA  1 
ATOM   13006 C  C   . MET   E 2 218 ? 38.703  -36.171 -45.701 1.00 101.71 ? 218  MET   E C   1 
ATOM   13007 O  O   . MET   E 2 218 ? 39.706  -36.784 -46.093 1.00 103.50 ? 218  MET   E O   1 
ATOM   13008 C  CB  . MET   E 2 218 ? 39.443  -33.812 -45.281 1.00 98.44  ? 218  MET   E CB  1 
ATOM   13009 C  CG  . MET   E 2 218 ? 38.535  -33.003 -46.168 1.00 104.12 ? 218  MET   E CG  1 
ATOM   13010 S  SD  . MET   E 2 218 ? 39.437  -31.589 -46.879 1.00 105.11 ? 218  MET   E SD  1 
ATOM   13011 C  CE  . MET   E 2 218 ? 39.501  -30.532 -45.418 1.00 101.46 ? 218  MET   E CE  1 
ATOM   13012 N  N   . VAL   E 2 219 ? 37.472  -36.427 -46.144 1.00 103.71 ? 219  VAL   E N   1 
ATOM   13013 C  CA  . VAL   E 2 219 ? 37.185  -37.443 -47.153 1.00 99.83  ? 219  VAL   E CA  1 
ATOM   13014 C  C   . VAL   E 2 219 ? 36.596  -36.768 -48.372 1.00 100.73 ? 219  VAL   E C   1 
ATOM   13015 O  O   . VAL   E 2 219 ? 35.560  -36.098 -48.287 1.00 100.62 ? 219  VAL   E O   1 
ATOM   13016 C  CB  . VAL   E 2 219 ? 36.219  -38.511 -46.644 1.00 99.43  ? 219  VAL   E CB  1 
ATOM   13017 C  CG1 . VAL   E 2 219 ? 35.778  -39.392 -47.810 1.00 103.43 ? 219  VAL   E CG1 1 
ATOM   13018 C  CG2 . VAL   E 2 219 ? 36.885  -39.314 -45.573 1.00 102.64 ? 219  VAL   E CG2 1 
ATOM   13019 N  N   . ILE   E 2 220 ? 37.230  -36.977 -49.512 1.00 102.40 ? 220  ILE   E N   1 
ATOM   13020 C  CA  . ILE   E 2 220 ? 36.805  -36.376 -50.763 1.00 102.06 ? 220  ILE   E CA  1 
ATOM   13021 C  C   . ILE   E 2 220 ? 36.499  -37.498 -51.735 1.00 105.97 ? 220  ILE   E C   1 
ATOM   13022 O  O   . ILE   E 2 220 ? 37.349  -38.361 -51.976 1.00 108.31 ? 220  ILE   E O   1 
ATOM   13023 C  CB  . ILE   E 2 220 ? 37.886  -35.451 -51.332 1.00 99.57  ? 220  ILE   E CB  1 
ATOM   13024 C  CG1 . ILE   E 2 220 ? 38.165  -34.318 -50.358 1.00 99.09  ? 220  ILE   E CG1 1 
ATOM   13025 C  CG2 . ILE   E 2 220 ? 37.457  -34.901 -52.662 1.00 101.51 ? 220  ILE   E CG2 1 
ATOM   13026 C  CD1 . ILE   E 2 220 ? 39.327  -33.481 -50.784 1.00 100.59 ? 220  ILE   E CD1 1 
ATOM   13027 N  N   . ALA   E 2 221 ? 35.297  -37.487 -52.291 1.00 103.27 ? 221  ALA   E N   1 
ATOM   13028 C  CA  . ALA   E 2 221 ? 34.926  -38.495 -53.269 1.00 104.83 ? 221  ALA   E CA  1 
ATOM   13029 C  C   . ALA   E 2 221 ? 35.401  -38.066 -54.655 1.00 106.87 ? 221  ALA   E C   1 
ATOM   13030 O  O   . ALA   E 2 221 ? 34.975  -37.028 -55.167 1.00 108.91 ? 221  ALA   E O   1 
ATOM   13031 C  CB  . ALA   E 2 221 ? 33.417  -38.704 -53.238 1.00 103.71 ? 221  ALA   E CB  1 
ATOM   13032 N  N   . VAL   E 2 222 ? 36.290  -38.848 -55.254 1.00 110.44 ? 222  VAL   E N   1 
ATOM   13033 C  CA  . VAL   E 2 222 ? 36.790  -38.529 -56.595 1.00 112.41 ? 222  VAL   E CA  1 
ATOM   13034 C  C   . VAL   E 2 222 ? 35.723  -38.916 -57.615 1.00 113.18 ? 222  VAL   E C   1 
ATOM   13035 O  O   . VAL   E 2 222 ? 35.152  -40.017 -57.509 1.00 111.14 ? 222  VAL   E O   1 
ATOM   13036 C  CB  . VAL   E 2 222 ? 38.108  -39.251 -56.864 1.00 114.10 ? 222  VAL   E CB  1 
ATOM   13037 C  CG1 . VAL   E 2 222 ? 38.827  -38.648 -58.058 1.00 114.04 ? 222  VAL   E CG1 1 
ATOM   13038 C  CG2 . VAL   E 2 222 ? 38.998  -39.139 -55.658 1.00 113.28 ? 222  VAL   E CG2 1 
ATOM   13039 N  N   . PRO   E 2 223 ? 35.415  -38.042 -58.583 1.00 114.89 ? 223  PRO   E N   1 
ATOM   13040 C  CA  . PRO   E 2 223 ? 34.307  -38.301 -59.513 1.00 114.68 ? 223  PRO   E CA  1 
ATOM   13041 C  C   . PRO   E 2 223 ? 34.601  -39.452 -60.463 1.00 119.51 ? 223  PRO   E C   1 
ATOM   13042 O  O   . PRO   E 2 223 ? 35.705  -40.002 -60.532 1.00 118.52 ? 223  PRO   E O   1 
ATOM   13043 C  CB  . PRO   E 2 223 ? 34.148  -36.989 -60.289 1.00 112.60 ? 223  PRO   E CB  1 
ATOM   13044 C  CG  . PRO   E 2 223 ? 34.882  -35.998 -59.533 1.00 114.75 ? 223  PRO   E CG  1 
ATOM   13045 C  CD  . PRO   E 2 223 ? 35.969  -36.697 -58.781 1.00 115.55 ? 223  PRO   E CD  1 
ATOM   13046 N  N   . GLU   E 2 224 ? 33.566  -39.770 -61.236 1.00 117.55 ? 224  GLU   E N   1 
ATOM   13047 C  CA  . GLU   E 2 224 ? 33.426  -40.951 -62.074 1.00 116.49 ? 224  GLU   E CA  1 
ATOM   13048 C  C   . GLU   E 2 224 ? 34.662  -41.333 -62.884 1.00 121.39 ? 224  GLU   E C   1 
ATOM   13049 O  O   . GLU   E 2 224 ? 34.917  -42.531 -63.066 1.00 122.52 ? 224  GLU   E O   1 
ATOM   13050 C  CB  . GLU   E 2 224 ? 32.232  -40.742 -62.995 1.00 120.97 ? 224  GLU   E CB  1 
ATOM   13051 C  CG  . GLU   E 2 224 ? 30.987  -41.421 -62.496 1.00 126.83 ? 224  GLU   E CG  1 
ATOM   13052 C  CD  . GLU   E 2 224 ? 31.000  -42.902 -62.818 1.00 137.00 ? 224  GLU   E CD  1 
ATOM   13053 O  OE1 . GLU   E 2 224 ? 31.553  -43.682 -62.009 1.00 137.79 ? 224  GLU   E OE1 1 
ATOM   13054 O  OE2 . GLU   E 2 224 ? 30.476  -43.284 -63.894 1.00 136.80 ? 224  GLU   E OE2 1 
ATOM   13055 N  N   . PRO   E 2 225 ? 35.447  -40.375 -63.412 1.00 126.21 ? 225  PRO   E N   1 
ATOM   13056 C  CA  . PRO   E 2 225 ? 36.715  -40.766 -64.055 1.00 124.87 ? 225  PRO   E CA  1 
ATOM   13057 C  C   . PRO   E 2 225 ? 37.673  -41.650 -63.247 1.00 119.79 ? 225  PRO   E C   1 
ATOM   13058 O  O   . PRO   E 2 225 ? 37.976  -42.768 -63.674 1.00 112.02 ? 225  PRO   E O   1 
ATOM   13059 C  CB  . PRO   E 2 225 ? 37.382  -39.412 -64.341 1.00 128.32 ? 225  PRO   E CB  1 
ATOM   13060 C  CG  . PRO   E 2 225 ? 36.217  -38.469 -64.577 1.00 126.39 ? 225  PRO   E CG  1 
ATOM   13061 C  CD  . PRO   E 2 225 ? 35.106  -38.955 -63.679 1.00 126.20 ? 225  PRO   E CD  1 
ATOM   13062 N  N   . PHE   E 2 226 ? 38.136  -41.182 -62.076 1.00 125.99 ? 226  PHE   E N   1 
ATOM   13063 C  CA  . PHE   E 2 226 ? 39.166  -41.892 -61.310 1.00 120.71 ? 226  PHE   E CA  1 
ATOM   13064 C  C   . PHE   E 2 226 ? 38.484  -42.858 -60.343 1.00 119.83 ? 226  PHE   E C   1 
ATOM   13065 O  O   . PHE   E 2 226 ? 38.851  -44.037 -60.270 1.00 118.60 ? 226  PHE   E O   1 
ATOM   13066 C  CB  . PHE   E 2 226 ? 40.074  -40.951 -60.494 1.00 120.50 ? 226  PHE   E CB  1 
ATOM   13067 C  CG  . PHE   E 2 226 ? 40.763  -39.862 -61.291 1.00 122.02 ? 226  PHE   E CG  1 
ATOM   13068 C  CD1 . PHE   E 2 226 ? 40.138  -38.631 -61.493 1.00 127.40 ? 226  PHE   E CD1 1 
ATOM   13069 C  CD2 . PHE   E 2 226 ? 42.052  -40.037 -61.771 1.00 122.21 ? 226  PHE   E CD2 1 
ATOM   13070 C  CE1 . PHE   E 2 226 ? 40.767  -37.611 -62.199 1.00 125.12 ? 226  PHE   E CE1 1 
ATOM   13071 C  CE2 . PHE   E 2 226 ? 42.688  -39.023 -62.477 1.00 127.36 ? 226  PHE   E CE2 1 
ATOM   13072 C  CZ  . PHE   E 2 226 ? 42.046  -37.807 -62.689 1.00 126.58 ? 226  PHE   E CZ  1 
ATOM   13073 N  N   . GLY   E 2 227 ? 37.533  -42.355 -59.550 1.00 120.76 ? 227  GLY   E N   1 
ATOM   13074 C  CA  . GLY   E 2 227 ? 36.877  -43.130 -58.517 1.00 118.26 ? 227  GLY   E CA  1 
ATOM   13075 C  C   . GLY   E 2 227 ? 37.628  -43.089 -57.198 1.00 116.64 ? 227  GLY   E C   1 
ATOM   13076 O  O   . GLY   E 2 227 ? 38.772  -42.645 -57.103 1.00 116.09 ? 227  GLY   E O   1 
ATOM   13077 N  N   . GLY   E 2 228 ? 36.972  -43.570 -56.154 1.00 118.10 ? 228  GLY   E N   1 
ATOM   13078 C  CA  . GLY   E 2 228 ? 37.673  -43.686 -54.892 1.00 119.96 ? 228  GLY   E CA  1 
ATOM   13079 C  C   . GLY   E 2 228 ? 37.563  -42.411 -54.074 1.00 119.88 ? 228  GLY   E C   1 
ATOM   13080 O  O   . GLY   E 2 228 ? 36.722  -41.548 -54.348 1.00 119.73 ? 228  GLY   E O   1 
ATOM   13081 N  N   . ALA   E 2 229 ? 38.431  -42.299 -53.062 1.00 117.03 ? 229  ALA   E N   1 
ATOM   13082 C  CA  . ALA   E 2 229 ? 38.411  -41.165 -52.149 1.00 113.30 ? 229  ALA   E CA  1 
ATOM   13083 C  C   . ALA   E 2 229 ? 39.832  -40.705 -51.836 1.00 113.70 ? 229  ALA   E C   1 
ATOM   13084 O  O   . ALA   E 2 229 ? 40.765  -41.509 -51.768 1.00 111.67 ? 229  ALA   E O   1 
ATOM   13085 C  CB  . ALA   E 2 229 ? 37.659  -41.500 -50.851 1.00 110.13 ? 229  ALA   E CB  1 
ATOM   13086 N  N   . ILE   E 2 230 ? 39.983  -39.387 -51.663 1.00 111.62 ? 230  ILE   E N   1 
ATOM   13087 C  CA  . ILE   E 2 230 ? 41.226  -38.765 -51.209 1.00 111.11 ? 230  ILE   E CA  1 
ATOM   13088 C  C   . ILE   E 2 230 ? 41.082  -38.454 -49.723 1.00 111.35 ? 230  ILE   E C   1 
ATOM   13089 O  O   . ILE   E 2 230 ? 40.079  -37.860 -49.301 1.00 105.74 ? 230  ILE   E O   1 
ATOM   13090 C  CB  . ILE   E 2 230 ? 41.548  -37.481 -51.998 1.00 104.93 ? 230  ILE   E CB  1 
ATOM   13091 C  CG1 . ILE   E 2 230 ? 41.232  -37.656 -53.476 1.00 110.67 ? 230  ILE   E CG1 1 
ATOM   13092 C  CG2 . ILE   E 2 230 ? 43.006  -37.124 -51.886 1.00 104.17 ? 230  ILE   E CG2 1 
ATOM   13093 C  CD1 . ILE   E 2 230 ? 41.606  -36.453 -54.328 1.00 108.58 ? 230  ILE   E CD1 1 
ATOM   13094 N  N   . ILE   E 2 231 ? 42.077  -38.864 -48.928 1.00 114.86 ? 231  ILE   E N   1 
ATOM   13095 C  CA  . ILE   E 2 231 ? 42.105  -38.647 -47.483 1.00 112.98 ? 231  ILE   E CA  1 
ATOM   13096 C  C   . ILE   E 2 231 ? 43.183  -37.601 -47.211 1.00 111.87 ? 231  ILE   E C   1 
ATOM   13097 O  O   . ILE   E 2 231 ? 44.384  -37.902 -47.269 1.00 112.26 ? 231  ILE   E O   1 
ATOM   13098 C  CB  . ILE   E 2 231 ? 42.376  -39.945 -46.707 1.00 112.98 ? 231  ILE   E CB  1 
ATOM   13099 C  CG1 . ILE   E 2 231 ? 41.370  -41.020 -47.088 1.00 109.82 ? 231  ILE   E CG1 1 
ATOM   13100 C  CG2 . ILE   E 2 231 ? 42.276  -39.712 -45.212 1.00 110.07 ? 231  ILE   E CG2 1 
ATOM   13101 C  CD1 . ILE   E 2 231 ? 39.988  -40.686 -46.652 1.00 106.74 ? 231  ILE   E CD1 1 
ATOM   13102 N  N   . ILE   E 2 232 ? 42.764  -36.372 -46.906 1.00 113.20 ? 232  ILE   E N   1 
ATOM   13103 C  CA  . ILE   E 2 232 ? 43.688  -35.284 -46.591 1.00 110.38 ? 232  ILE   E CA  1 
ATOM   13104 C  C   . ILE   E 2 232 ? 43.894  -35.250 -45.085 1.00 103.76 ? 232  ILE   E C   1 
ATOM   13105 O  O   . ILE   E 2 232 ? 42.934  -35.133 -44.320 1.00 102.15 ? 232  ILE   E O   1 
ATOM   13106 C  CB  . ILE   E 2 232 ? 43.175  -33.926 -47.094 1.00 105.60 ? 232  ILE   E CB  1 
ATOM   13107 C  CG1 . ILE   E 2 232 ? 42.892  -33.946 -48.593 1.00 102.81 ? 232  ILE   E CG1 1 
ATOM   13108 C  CG2 . ILE   E 2 232 ? 44.197  -32.852 -46.814 1.00 103.64 ? 232  ILE   E CG2 1 
ATOM   13109 C  CD1 . ILE   E 2 232 ? 42.424  -32.612 -49.117 1.00 95.86  ? 232  ILE   E CD1 1 
ATOM   13110 N  N   . GLY   E 2 233 ? 45.142  -35.356 -44.662 1.00 103.16 ? 233  GLY   E N   1 
ATOM   13111 C  CA  . GLY   E 2 233 ? 45.410  -35.341 -43.245 1.00 110.94 ? 233  GLY   E CA  1 
ATOM   13112 C  C   . GLY   E 2 233 ? 46.064  -34.071 -42.748 1.00 111.78 ? 233  GLY   E C   1 
ATOM   13113 O  O   . GLY   E 2 233 ? 45.649  -32.952 -43.062 1.00 109.82 ? 233  GLY   E O   1 
ATOM   13114 N  N   . GLN   E 2 234 ? 47.096  -34.247 -41.937 1.00 113.69 ? 234  GLN   E N   1 
ATOM   13115 C  CA  . GLN   E 2 234 ? 47.867  -33.125 -41.432 1.00 115.70 ? 234  GLN   E CA  1 
ATOM   13116 C  C   . GLN   E 2 234 ? 48.935  -32.740 -42.447 1.00 115.14 ? 234  GLN   E C   1 
ATOM   13117 O  O   . GLN   E 2 234 ? 48.892  -31.650 -43.033 1.00 115.64 ? 234  GLN   E O   1 
ATOM   13118 C  CB  . GLN   E 2 234 ? 48.477  -33.514 -40.078 1.00 118.54 ? 234  GLN   E CB  1 
ATOM   13119 C  CG  . GLN   E 2 234 ? 49.286  -32.465 -39.387 1.00 121.15 ? 234  GLN   E CG  1 
ATOM   13120 C  CD  . GLN   E 2 234 ? 48.460  -31.275 -38.975 1.00 123.10 ? 234  GLN   E CD  1 
ATOM   13121 O  OE1 . GLN   E 2 234 ? 48.629  -30.188 -39.530 1.00 124.21 ? 234  GLN   E OE1 1 
ATOM   13122 N  NE2 . GLN   E 2 234 ? 47.580  -31.458 -37.980 1.00 121.70 ? 234  GLN   E NE2 1 
ATOM   13123 N  N   . GLU   E 2 235 ? 49.862  -33.663 -42.697 1.00 114.38 ? 235  GLU   E N   1 
ATOM   13124 C  CA  . GLU   E 2 235 ? 51.042  -33.428 -43.515 1.00 117.44 ? 235  GLU   E CA  1 
ATOM   13125 C  C   . GLU   E 2 235 ? 51.094  -34.336 -44.741 1.00 114.27 ? 235  GLU   E C   1 
ATOM   13126 O  O   . GLU   E 2 235 ? 52.098  -34.320 -45.470 1.00 114.96 ? 235  GLU   E O   1 
ATOM   13127 C  CB  . GLU   E 2 235 ? 52.299  -33.620 -42.656 1.00 114.93 ? 235  GLU   E CB  1 
ATOM   13128 N  N   . SER   E 2 236 ? 50.044  -35.126 -44.985 1.00 115.02 ? 236  SER   E N   1 
ATOM   13129 C  CA  . SER   E 2 236 ? 50.065  -36.131 -46.045 1.00 117.03 ? 236  SER   E CA  1 
ATOM   13130 C  C   . SER   E 2 236 ? 48.673  -36.316 -46.634 1.00 112.97 ? 236  SER   E C   1 
ATOM   13131 O  O   . SER   E 2 236 ? 47.733  -36.693 -45.923 1.00 110.40 ? 236  SER   E O   1 
ATOM   13132 C  CB  . SER   E 2 236 ? 50.598  -37.471 -45.523 1.00 118.02 ? 236  SER   E CB  1 
ATOM   13133 O  OG  . SER   E 2 236 ? 49.587  -38.222 -44.868 1.00 110.73 ? 236  SER   E OG  1 
ATOM   13134 N  N   . ILE   E 2 237 ? 48.563  -36.068 -47.937 1.00 111.82 ? 237  ILE   E N   1 
ATOM   13135 C  CA  . ILE   E 2 237 ? 47.362  -36.344 -48.723 1.00 115.64 ? 237  ILE   E CA  1 
ATOM   13136 C  C   . ILE   E 2 237 ? 47.535  -37.704 -49.396 1.00 118.57 ? 237  ILE   E C   1 
ATOM   13137 O  O   . ILE   E 2 237 ? 48.551  -37.957 -50.061 1.00 118.10 ? 237  ILE   E O   1 
ATOM   13138 C  CB  . ILE   E 2 237 ? 47.114  -35.237 -49.768 1.00 110.84 ? 237  ILE   E CB  1 
ATOM   13139 C  CG1 . ILE   E 2 237 ? 47.152  -33.865 -49.104 1.00 110.42 ? 237  ILE   E CG1 1 
ATOM   13140 C  CG2 . ILE   E 2 237 ? 45.780  -35.413 -50.467 1.00 107.36 ? 237  ILE   E CG2 1 
ATOM   13141 C  CD1 . ILE   E 2 237 ? 47.889  -32.833 -49.924 1.00 108.88 ? 237  ILE   E CD1 1 
ATOM   13142 N  N   . THR   E 2 238 ? 46.550  -38.580 -49.220 1.00 127.33 ? 238  THR   E N   1 
ATOM   13143 C  CA  . THR   E 2 238 ? 46.619  -39.950 -49.706 1.00 126.23 ? 238  THR   E CA  1 
ATOM   13144 C  C   . THR   E 2 238 ? 45.360  -40.287 -50.492 1.00 127.83 ? 238  THR   E C   1 
ATOM   13145 O  O   . THR   E 2 238 ? 44.244  -40.024 -50.032 1.00 128.51 ? 238  THR   E O   1 
ATOM   13146 C  CB  . THR   E 2 238 ? 46.822  -40.934 -48.540 1.00 128.64 ? 238  THR   E CB  1 
ATOM   13147 O  OG1 . THR   E 2 238 ? 45.906  -40.645 -47.469 1.00 130.44 ? 238  THR   E OG1 1 
ATOM   13148 C  CG2 . THR   E 2 238 ? 48.226  -40.810 -48.014 1.00 126.96 ? 238  THR   E CG2 1 
ATOM   13149 N  N   . TYR   E 2 239 ? 45.545  -40.851 -51.687 1.00 121.05 ? 239  TYR   E N   1 
ATOM   13150 C  CA  . TYR   E 2 239 ? 44.452  -41.321 -52.532 1.00 119.28 ? 239  TYR   E CA  1 
ATOM   13151 C  C   . TYR   E 2 239 ? 44.309  -42.840 -52.433 1.00 124.78 ? 239  TYR   E C   1 
ATOM   13152 O  O   . TYR   E 2 239 ? 45.306  -43.570 -52.475 1.00 127.50 ? 239  TYR   E O   1 
ATOM   13153 C  CB  . TYR   E 2 239 ? 44.697  -40.929 -53.993 1.00 116.04 ? 239  TYR   E CB  1 
ATOM   13154 C  CG  . TYR   E 2 239 ? 43.731  -41.555 -54.975 1.00 116.30 ? 239  TYR   E CG  1 
ATOM   13155 C  CD1 . TYR   E 2 239 ? 42.453  -41.041 -55.140 1.00 119.49 ? 239  TYR   E CD1 1 
ATOM   13156 C  CD2 . TYR   E 2 239 ? 44.099  -42.645 -55.748 1.00 116.21 ? 239  TYR   E CD2 1 
ATOM   13157 C  CE1 . TYR   E 2 239 ? 41.566  -41.599 -56.042 1.00 116.98 ? 239  TYR   E CE1 1 
ATOM   13158 C  CE2 . TYR   E 2 239 ? 43.211  -43.214 -56.652 1.00 116.74 ? 239  TYR   E CE2 1 
ATOM   13159 C  CZ  . TYR   E 2 239 ? 41.944  -42.680 -56.793 1.00 114.30 ? 239  TYR   E CZ  1 
ATOM   13160 O  OH  . TYR   E 2 239 ? 41.030  -43.210 -57.675 1.00 117.09 ? 239  TYR   E OH  1 
ATOM   13161 N  N   . HIS   E 2 240 ? 43.069  -43.316 -52.297 1.00 124.51 ? 240  HIS   E N   1 
ATOM   13162 C  CA  . HIS   E 2 240 ? 42.799  -44.741 -52.207 1.00 123.10 ? 240  HIS   E CA  1 
ATOM   13163 C  C   . HIS   E 2 240 ? 41.664  -45.082 -53.157 1.00 124.36 ? 240  HIS   E C   1 
ATOM   13164 O  O   . HIS   E 2 240 ? 40.736  -44.287 -53.326 1.00 121.72 ? 240  HIS   E O   1 
ATOM   13165 C  CB  . HIS   E 2 240 ? 42.427  -45.176 -50.780 1.00 123.65 ? 240  HIS   E CB  1 
ATOM   13166 C  CG  . HIS   E 2 240 ? 43.321  -44.620 -49.710 1.00 124.80 ? 240  HIS   E CG  1 
ATOM   13167 N  ND1 . HIS   E 2 240 ? 44.296  -45.368 -49.088 1.00 127.52 ? 240  HIS   E ND1 1 
ATOM   13168 C  CD2 . HIS   E 2 240 ? 43.369  -43.394 -49.135 1.00 124.69 ? 240  HIS   E CD2 1 
ATOM   13169 C  CE1 . HIS   E 2 240 ? 44.909  -44.627 -48.183 1.00 128.52 ? 240  HIS   E CE1 1 
ATOM   13170 N  NE2 . HIS   E 2 240 ? 44.368  -43.423 -48.193 1.00 125.09 ? 240  HIS   E NE2 1 
ATOM   13171 N  N   . ASN   E 2 241 ? 41.757  -46.261 -53.790 1.00 131.25 ? 241  ASN   E N   1 
ATOM   13172 C  CA  . ASN   E 2 241 ? 40.679  -46.799 -54.618 1.00 133.47 ? 241  ASN   E CA  1 
ATOM   13173 C  C   . ASN   E 2 241 ? 40.887  -48.282 -54.910 1.00 139.44 ? 241  ASN   E C   1 
ATOM   13174 O  O   . ASN   E 2 241 ? 41.419  -48.638 -55.963 1.00 141.67 ? 241  ASN   E O   1 
ATOM   13175 C  CB  . ASN   E 2 241 ? 40.567  -46.023 -55.933 1.00 127.23 ? 241  ASN   E CB  1 
ATOM   13176 C  CG  . ASN   E 2 241 ? 39.236  -46.257 -56.649 1.00 125.80 ? 241  ASN   E CG  1 
ATOM   13177 O  OD1 . ASN   E 2 241 ? 38.321  -46.909 -56.128 1.00 124.14 ? 241  ASN   E OD1 1 
ATOM   13178 N  ND2 . ASN   E 2 241 ? 39.123  -45.705 -57.854 1.00 124.32 ? 241  ASN   E ND2 1 
ATOM   13179 N  N   . GLY   E 2 242 ? 40.459  -49.155 -54.001 1.00 158.05 ? 242  GLY   E N   1 
ATOM   13180 C  CA  . GLY   E 2 242 ? 40.706  -50.580 -54.189 1.00 162.15 ? 242  GLY   E CA  1 
ATOM   13181 C  C   . GLY   E 2 242 ? 42.174  -50.901 -53.961 1.00 168.30 ? 242  GLY   E C   1 
ATOM   13182 O  O   . GLY   E 2 242 ? 42.762  -50.517 -52.939 1.00 169.34 ? 242  GLY   E O   1 
ATOM   13183 N  N   . ASP   E 2 243 ? 42.781  -51.602 -54.926 1.00 160.66 ? 243  ASP   E N   1 
ATOM   13184 C  CA  . ASP   E 2 243 ? 44.215  -51.870 -54.855 1.00 161.86 ? 243  ASP   E CA  1 
ATOM   13185 C  C   . ASP   E 2 243 ? 45.019  -50.575 -54.930 1.00 161.74 ? 243  ASP   E C   1 
ATOM   13186 O  O   . ASP   E 2 243 ? 46.095  -50.466 -54.327 1.00 166.28 ? 243  ASP   E O   1 
ATOM   13187 C  CB  . ASP   E 2 243 ? 44.630  -52.822 -55.975 1.00 164.10 ? 243  ASP   E CB  1 
ATOM   13188 N  N   . LYS   E 2 244 ? 44.498  -49.578 -55.652 1.00 156.25 ? 244  LYS   E N   1 
ATOM   13189 C  CA  . LYS   E 2 244 ? 45.206  -48.318 -55.860 1.00 149.06 ? 244  LYS   E CA  1 
ATOM   13190 C  C   . LYS   E 2 244 ? 45.403  -47.564 -54.546 1.00 143.07 ? 244  LYS   E C   1 
ATOM   13191 O  O   . LYS   E 2 244 ? 44.475  -47.433 -53.741 1.00 141.56 ? 244  LYS   E O   1 
ATOM   13192 C  CB  . LYS   E 2 244 ? 44.440  -47.446 -56.857 1.00 136.61 ? 244  LYS   E CB  1 
ATOM   13193 N  N   . TYR   E 2 245 ? 46.622  -47.063 -54.339 1.00 138.15 ? 245  TYR   E N   1 
ATOM   13194 C  CA  . TYR   E 2 245 ? 46.969  -46.297 -53.141 1.00 134.37 ? 245  TYR   E CA  1 
ATOM   13195 C  C   . TYR   E 2 245 ? 48.145  -45.393 -53.472 1.00 135.15 ? 245  TYR   E C   1 
ATOM   13196 O  O   . TYR   E 2 245 ? 49.244  -45.893 -53.741 1.00 136.70 ? 245  TYR   E O   1 
ATOM   13197 C  CB  . TYR   E 2 245 ? 47.310  -47.213 -51.974 1.00 136.36 ? 245  TYR   E CB  1 
ATOM   13198 C  CG  . TYR   E 2 245 ? 48.014  -46.497 -50.846 1.00 133.35 ? 245  TYR   E CG  1 
ATOM   13199 C  CD1 . TYR   E 2 245 ? 47.422  -45.409 -50.221 1.00 130.70 ? 245  TYR   E CD1 1 
ATOM   13200 C  CD2 . TYR   E 2 245 ? 49.269  -46.903 -50.405 1.00 137.49 ? 245  TYR   E CD2 1 
ATOM   13201 C  CE1 . TYR   E 2 245 ? 48.054  -44.740 -49.190 1.00 132.83 ? 245  TYR   E CE1 1 
ATOM   13202 C  CE2 . TYR   E 2 245 ? 49.915  -46.242 -49.368 1.00 137.86 ? 245  TYR   E CE2 1 
ATOM   13203 C  CZ  . TYR   E 2 245 ? 49.296  -45.155 -48.762 1.00 138.43 ? 245  TYR   E CZ  1 
ATOM   13204 O  OH  . TYR   E 2 245 ? 49.897  -44.466 -47.725 1.00 141.91 ? 245  TYR   E OH  1 
ATOM   13205 N  N   . LEU   E 2 246 ? 47.919  -44.073 -53.455 1.00 131.02 ? 246  LEU   E N   1 
ATOM   13206 C  CA  . LEU   E 2 246 ? 48.932  -43.053 -53.715 1.00 124.41 ? 246  LEU   E CA  1 
ATOM   13207 C  C   . LEU   E 2 246 ? 49.007  -42.097 -52.519 1.00 128.17 ? 246  LEU   E C   1 
ATOM   13208 O  O   . LEU   E 2 246 ? 47.982  -41.776 -51.912 1.00 129.41 ? 246  LEU   E O   1 
ATOM   13209 C  CB  . LEU   E 2 246 ? 48.585  -42.300 -55.020 1.00 123.84 ? 246  LEU   E CB  1 
ATOM   13210 C  CG  . LEU   E 2 246 ? 49.529  -41.290 -55.682 1.00 126.89 ? 246  LEU   E CG  1 
ATOM   13211 C  CD1 . LEU   E 2 246 ? 50.910  -41.891 -55.950 1.00 127.80 ? 246  LEU   E CD1 1 
ATOM   13212 C  CD2 . LEU   E 2 246 ? 48.910  -40.733 -56.978 1.00 120.08 ? 246  LEU   E CD2 1 
ATOM   13213 N  N   . ALA   E 2 247 ? 50.228  -41.649 -52.170 1.00 126.20 ? 247  ALA   E N   1 
ATOM   13214 C  CA  . ALA   E 2 247 ? 50.469  -40.816 -50.983 1.00 125.14 ? 247  ALA   E CA  1 
ATOM   13215 C  C   . ALA   E 2 247 ? 51.521  -39.746 -51.279 1.00 129.56 ? 247  ALA   E C   1 
ATOM   13216 O  O   . ALA   E 2 247 ? 52.642  -40.082 -51.671 1.00 132.72 ? 247  ALA   E O   1 
ATOM   13217 C  CB  . ALA   E 2 247 ? 50.929  -41.673 -49.795 1.00 117.35 ? 247  ALA   E CB  1 
ATOM   13218 N  N   . ILE   E 2 248 ? 51.191  -38.461 -51.090 1.00 126.52 ? 248  ILE   E N   1 
ATOM   13219 C  CA  . ILE   E 2 248 ? 52.208  -37.409 -51.087 1.00 122.86 ? 248  ILE   E CA  1 
ATOM   13220 C  C   . ILE   E 2 248 ? 52.362  -36.862 -49.679 1.00 120.89 ? 248  ILE   E C   1 
ATOM   13221 O  O   . ILE   E 2 248 ? 51.434  -36.888 -48.864 1.00 117.06 ? 248  ILE   E O   1 
ATOM   13222 C  CB  . ILE   E 2 248 ? 51.907  -36.249 -52.068 1.00 118.93 ? 248  ILE   E CB  1 
ATOM   13223 C  CG1 . ILE   E 2 248 ? 50.435  -35.879 -52.052 1.00 116.02 ? 248  ILE   E CG1 1 
ATOM   13224 C  CG2 . ILE   E 2 248 ? 52.354  -36.571 -53.473 1.00 122.72 ? 248  ILE   E CG2 1 
ATOM   13225 C  CD1 . ILE   E 2 248 ? 50.130  -34.723 -52.945 1.00 115.61 ? 248  ILE   E CD1 1 
ATOM   13226 N  N   . ALA   E 2 249 ? 53.552  -36.346 -49.388 1.00 121.19 ? 249  ALA   E N   1 
ATOM   13227 C  CA  . ALA   E 2 249 ? 53.806  -35.621 -48.146 1.00 121.82 ? 249  ALA   E CA  1 
ATOM   13228 C  C   . ALA   E 2 249 ? 54.369  -34.256 -48.514 1.00 125.75 ? 249  ALA   E C   1 
ATOM   13229 O  O   . ALA   E 2 249 ? 55.529  -33.951 -48.203 1.00 127.23 ? 249  ALA   E O   1 
ATOM   13230 C  CB  . ALA   E 2 249 ? 54.764  -36.380 -47.231 1.00 122.35 ? 249  ALA   E CB  1 
ATOM   13231 N  N   . PRO   E 2 250 ? 53.579  -33.418 -49.182 1.00 130.05 ? 250  PRO   E N   1 
ATOM   13232 C  CA  . PRO   E 2 250 ? 54.085  -32.132 -49.651 1.00 128.72 ? 250  PRO   E CA  1 
ATOM   13233 C  C   . PRO   E 2 250 ? 54.557  -31.289 -48.486 1.00 128.43 ? 250  PRO   E C   1 
ATOM   13234 O  O   . PRO   E 2 250 ? 53.925  -31.266 -47.419 1.00 129.16 ? 250  PRO   E O   1 
ATOM   13235 C  CB  . PRO   E 2 250 ? 52.868  -31.493 -50.331 1.00 129.97 ? 250  PRO   E CB  1 
ATOM   13236 C  CG  . PRO   E 2 250 ? 51.902  -32.588 -50.541 1.00 130.03 ? 250  PRO   E CG  1 
ATOM   13237 C  CD  . PRO   E 2 250 ? 52.132  -33.544 -49.426 1.00 129.93 ? 250  PRO   E CD  1 
ATOM   13238 N  N   . PRO   E 2 251 ? 55.680  -30.598 -48.650 1.00 119.80 ? 251  PRO   E N   1 
ATOM   13239 C  CA  . PRO   E 2 251 ? 56.205  -29.798 -47.535 1.00 120.49 ? 251  PRO   E CA  1 
ATOM   13240 C  C   . PRO   E 2 251 ? 55.431  -28.512 -47.292 1.00 119.89 ? 251  PRO   E C   1 
ATOM   13241 O  O   . PRO   E 2 251 ? 55.427  -28.010 -46.158 1.00 121.09 ? 251  PRO   E O   1 
ATOM   13242 C  CB  . PRO   E 2 251 ? 57.653  -29.520 -47.963 1.00 118.02 ? 251  PRO   E CB  1 
ATOM   13243 C  CG  . PRO   E 2 251 ? 57.658  -29.700 -49.443 1.00 116.16 ? 251  PRO   E CG  1 
ATOM   13244 C  CD  . PRO   E 2 251 ? 56.647  -30.746 -49.749 1.00 117.01 ? 251  PRO   E CD  1 
ATOM   13245 N  N   . ILE   E 2 252 ? 54.768  -27.972 -48.315 1.00 117.36 ? 252  ILE   E N   1 
ATOM   13246 C  CA  . ILE   E 2 252 ? 54.098  -26.690 -48.164 1.00 114.82 ? 252  ILE   E CA  1 
ATOM   13247 C  C   . ILE   E 2 252 ? 52.907  -26.815 -47.215 1.00 118.82 ? 252  ILE   E C   1 
ATOM   13248 O  O   . ILE   E 2 252 ? 52.745  -26.012 -46.287 1.00 119.92 ? 252  ILE   E O   1 
ATOM   13249 C  CB  . ILE   E 2 252 ? 53.708  -26.144 -49.551 1.00 109.98 ? 252  ILE   E CB  1 
ATOM   13250 C  CG1 . ILE   E 2 252 ? 52.764  -24.944 -49.449 1.00 114.26 ? 252  ILE   E CG1 1 
ATOM   13251 C  CG2 . ILE   E 2 252 ? 53.132  -27.241 -50.396 1.00 117.15 ? 252  ILE   E CG2 1 
ATOM   13252 C  CD1 . ILE   E 2 252 ? 53.337  -23.732 -48.726 1.00 119.20 ? 252  ILE   E CD1 1 
ATOM   13253 N  N   . ILE   E 2 253 ? 52.085  -27.849 -47.397 1.00 117.69 ? 253  ILE   E N   1 
ATOM   13254 C  CA  . ILE   E 2 253 ? 50.923  -28.048 -46.535 1.00 120.83 ? 253  ILE   E CA  1 
ATOM   13255 C  C   . ILE   E 2 253 ? 51.283  -28.486 -45.122 1.00 123.61 ? 253  ILE   E C   1 
ATOM   13256 O  O   . ILE   E 2 253 ? 50.391  -28.574 -44.262 1.00 122.90 ? 253  ILE   E O   1 
ATOM   13257 C  CB  . ILE   E 2 253 ? 49.993  -29.117 -47.123 1.00 122.02 ? 253  ILE   E CB  1 
ATOM   13258 C  CG1 . ILE   E 2 253 ? 50.619  -30.492 -46.884 1.00 123.54 ? 253  ILE   E CG1 1 
ATOM   13259 C  CG2 . ILE   E 2 253 ? 49.740  -28.832 -48.604 1.00 117.74 ? 253  ILE   E CG2 1 
ATOM   13260 C  CD1 . ILE   E 2 253 ? 49.610  -31.594 -46.890 1.00 123.01 ? 253  ILE   E CD1 1 
ATOM   13261 N  N   . LYS   E 2 254 ? 52.560  -28.794 -44.865 1.00 127.15 ? 254  LYS   E N   1 
ATOM   13262 C  CA  . LYS   E 2 254 ? 53.022  -29.189 -43.533 1.00 129.79 ? 254  LYS   E CA  1 
ATOM   13263 C  C   . LYS   E 2 254 ? 53.256  -27.940 -42.672 1.00 131.11 ? 254  LYS   E C   1 
ATOM   13264 O  O   . LYS   E 2 254 ? 54.265  -27.841 -41.963 1.00 133.11 ? 254  LYS   E O   1 
ATOM   13265 C  CB  . LYS   E 2 254 ? 54.316  -30.016 -43.642 1.00 124.89 ? 254  LYS   E CB  1 
ATOM   13266 N  N   . GLN   E 2 255 ? 52.345  -26.972 -42.746 1.00 122.01 ? 255  GLN   E N   1 
ATOM   13267 C  CA  . GLN   E 2 255 ? 52.476  -25.716 -42.006 1.00 120.53 ? 255  GLN   E CA  1 
ATOM   13268 C  C   . GLN   E 2 255 ? 51.150  -25.216 -41.437 1.00 124.34 ? 255  GLN   E C   1 
ATOM   13269 O  O   . GLN   E 2 255 ? 51.168  -24.329 -40.572 1.00 122.49 ? 255  GLN   E O   1 
ATOM   13270 C  CB  . GLN   E 2 255 ? 53.102  -24.615 -42.874 1.00 117.40 ? 255  GLN   E CB  1 
ATOM   13271 N  N   . SER   E 2 256 ? 50.010  -25.724 -41.904 1.00 122.80 ? 256  SER   E N   1 
ATOM   13272 C  CA  . SER   E 2 256 ? 48.702  -25.565 -41.280 1.00 117.39 ? 256  SER   E CA  1 
ATOM   13273 C  C   . SER   E 2 256 ? 47.822  -26.657 -41.869 1.00 114.08 ? 256  SER   E C   1 
ATOM   13274 O  O   . SER   E 2 256 ? 48.182  -27.285 -42.868 1.00 112.29 ? 256  SER   E O   1 
ATOM   13275 C  CB  . SER   E 2 256 ? 48.095  -24.171 -41.511 1.00 112.42 ? 256  SER   E CB  1 
ATOM   13276 O  OG  . SER   E 2 256 ? 46.826  -24.034 -40.882 1.00 106.78 ? 256  SER   E OG  1 
ATOM   13277 N  N   . THR   E 2 257 ? 46.675  -26.894 -41.237 1.00 108.37 ? 257  THR   E N   1 
ATOM   13278 C  CA  . THR   E 2 257 ? 45.800  -27.977 -41.667 1.00 103.72 ? 257  THR   E CA  1 
ATOM   13279 C  C   . THR   E 2 257 ? 44.791  -27.471 -42.692 1.00 99.16  ? 257  THR   E C   1 
ATOM   13280 O  O   . THR   E 2 257 ? 44.236  -26.379 -42.550 1.00 96.12  ? 257  THR   E O   1 
ATOM   13281 C  CB  . THR   E 2 257 ? 45.049  -28.592 -40.486 1.00 97.86  ? 257  THR   E CB  1 
ATOM   13282 O  OG1 . THR   E 2 257 ? 44.108  -27.637 -40.014 1.00 99.48  ? 257  THR   E OG1 1 
ATOM   13283 C  CG2 . THR   E 2 257 ? 45.966  -28.929 -39.357 1.00 101.23 ? 257  THR   E CG2 1 
ATOM   13284 N  N   . ILE   E 2 258 ? 44.554  -28.283 -43.718 1.00 99.00  ? 258  ILE   E N   1 
ATOM   13285 C  CA  . ILE   E 2 258 ? 43.513  -28.030 -44.705 1.00 93.97  ? 258  ILE   E CA  1 
ATOM   13286 C  C   . ILE   E 2 258 ? 42.155  -28.227 -44.040 1.00 93.12  ? 258  ILE   E C   1 
ATOM   13287 O  O   . ILE   E 2 258 ? 41.854  -29.311 -43.529 1.00 93.82  ? 258  ILE   E O   1 
ATOM   13288 C  CB  . ILE   E 2 258 ? 43.688  -28.964 -45.911 1.00 92.73  ? 258  ILE   E CB  1 
ATOM   13289 C  CG1 . ILE   E 2 258 ? 45.173  -29.147 -46.247 1.00 93.84  ? 258  ILE   E CG1 1 
ATOM   13290 C  CG2 . ILE   E 2 258 ? 42.953  -28.441 -47.125 1.00 97.73  ? 258  ILE   E CG2 1 
ATOM   13291 C  CD1 . ILE   E 2 258 ? 45.798  -27.966 -46.969 1.00 93.70  ? 258  ILE   E CD1 1 
ATOM   13292 N  N   . VAL   E 2 259 ? 41.326  -27.189 -44.034 1.00 94.73  ? 259  VAL   E N   1 
ATOM   13293 C  CA  . VAL   E 2 259 ? 40.029  -27.293 -43.394 1.00 97.62  ? 259  VAL   E CA  1 
ATOM   13294 C  C   . VAL   E 2 259 ? 38.870  -27.326 -44.387 1.00 100.20 ? 259  VAL   E C   1 
ATOM   13295 O  O   . VAL   E 2 259 ? 37.838  -27.945 -44.096 1.00 104.58 ? 259  VAL   E O   1 
ATOM   13296 C  CB  . VAL   E 2 259 ? 39.829  -26.162 -42.374 1.00 96.14  ? 259  VAL   E CB  1 
ATOM   13297 C  CG1 . VAL   E 2 259 ? 40.699  -26.433 -41.190 1.00 95.36  ? 259  VAL   E CG1 1 
ATOM   13298 C  CG2 . VAL   E 2 259 ? 40.138  -24.789 -43.002 1.00 93.75  ? 259  VAL   E CG2 1 
ATOM   13299 N  N   . CYS   E 2 260 ? 39.001  -26.708 -45.555 1.00 95.02  ? 260  CYS   E N   1 
ATOM   13300 C  CA  . CYS   E 2 260 ? 37.917  -26.745 -46.526 1.00 97.73  ? 260  CYS   E CA  1 
ATOM   13301 C  C   . CYS   E 2 260 ? 38.449  -27.131 -47.897 1.00 98.84  ? 260  CYS   E C   1 
ATOM   13302 O  O   . CYS   E 2 260 ? 39.582  -26.795 -48.268 1.00 96.62  ? 260  CYS   E O   1 
ATOM   13303 C  CB  . CYS   E 2 260 ? 37.186  -25.408 -46.603 1.00 96.76  ? 260  CYS   E CB  1 
ATOM   13304 S  SG  . CYS   E 2 260 ? 38.287  -24.020 -46.756 1.00 94.94  ? 260  CYS   E SG  1 
ATOM   13305 N  N   . HIS   E 2 261 ? 37.614  -27.851 -48.641 1.00 98.96  ? 261  HIS   E N   1 
ATOM   13306 C  CA  . HIS   E 2 261 ? 37.952  -28.295 -49.983 1.00 97.01  ? 261  HIS   E CA  1 
ATOM   13307 C  C   . HIS   E 2 261 ? 36.791  -27.958 -50.899 1.00 98.50  ? 261  HIS   E C   1 
ATOM   13308 O  O   . HIS   E 2 261 ? 35.701  -27.594 -50.440 1.00 97.58  ? 261  HIS   E O   1 
ATOM   13309 C  CB  . HIS   E 2 261 ? 38.261  -29.803 -50.048 1.00 97.32  ? 261  HIS   E CB  1 
ATOM   13310 C  CG  . HIS   E 2 261 ? 37.041  -30.674 -49.982 1.00 97.37  ? 261  HIS   E CG  1 
ATOM   13311 N  ND1 . HIS   E 2 261 ? 36.354  -30.906 -48.806 1.00 98.22  ? 261  HIS   E ND1 1 
ATOM   13312 C  CD2 . HIS   E 2 261 ? 36.380  -31.359 -50.946 1.00 92.99  ? 261  HIS   E CD2 1 
ATOM   13313 C  CE1 . HIS   E 2 261 ? 35.327  -31.702 -49.048 1.00 97.29  ? 261  HIS   E CE1 1 
ATOM   13314 N  NE2 . HIS   E 2 261 ? 35.321  -31.992 -50.338 1.00 94.21  ? 261  HIS   E NE2 1 
ATOM   13315 N  N   . ASN   E 2 262 ? 37.058  -28.073 -52.198 1.00 96.33  ? 262  ASN   E N   1 
ATOM   13316 C  CA  . ASN   E 2 262 ? 36.087  -27.796 -53.243 1.00 97.19  ? 262  ASN   E CA  1 
ATOM   13317 C  C   . ASN   E 2 262 ? 36.635  -28.386 -54.530 1.00 104.87 ? 262  ASN   E C   1 
ATOM   13318 O  O   . ASN   E 2 262 ? 37.834  -28.261 -54.808 1.00 102.81 ? 262  ASN   E O   1 
ATOM   13319 C  CB  . ASN   E 2 262 ? 35.838  -26.292 -53.401 1.00 93.64  ? 262  ASN   E CB  1 
ATOM   13320 C  CG  . ASN   E 2 262 ? 34.991  -25.968 -54.617 1.00 99.23  ? 262  ASN   E CG  1 
ATOM   13321 O  OD1 . ASN   E 2 262 ? 35.489  -25.443 -55.615 1.00 101.01 ? 262  ASN   E OD1 1 
ATOM   13322 N  ND2 . ASN   E 2 262 ? 33.707  -26.287 -54.545 1.00 97.01  ? 262  ASN   E ND2 1 
ATOM   13323 N  N   . ARG   E 2 263 ? 35.763  -29.033 -55.305 1.00 107.37 ? 263  ARG   E N   1 
ATOM   13324 C  CA  . ARG   E 2 263 ? 36.163  -29.623 -56.576 1.00 110.06 ? 263  ARG   E CA  1 
ATOM   13325 C  C   . ARG   E 2 263 ? 36.020  -28.592 -57.685 1.00 112.82 ? 263  ARG   E C   1 
ATOM   13326 O  O   . ARG   E 2 263 ? 34.936  -28.033 -57.873 1.00 109.44 ? 263  ARG   E O   1 
ATOM   13327 C  CB  . ARG   E 2 263 ? 35.327  -30.855 -56.897 1.00 115.08 ? 263  ARG   E CB  1 
ATOM   13328 C  CG  . ARG   E 2 263 ? 35.931  -31.670 -58.026 1.00 118.93 ? 263  ARG   E CG  1 
ATOM   13329 C  CD  . ARG   E 2 263 ? 35.013  -32.769 -58.443 1.00 117.15 ? 263  ARG   E CD  1 
ATOM   13330 N  NE  . ARG   E 2 263 ? 33.775  -32.241 -58.996 1.00 121.22 ? 263  ARG   E NE  1 
ATOM   13331 C  CZ  . ARG   E 2 263 ? 32.566  -32.498 -58.515 1.00 122.64 ? 263  ARG   E CZ  1 
ATOM   13332 N  NH1 . ARG   E 2 263 ? 32.393  -33.304 -57.470 1.00 111.13 ? 263  ARG   E NH1 1 
ATOM   13333 N  NH2 . ARG   E 2 263 ? 31.505  -31.940 -59.100 1.00 124.18 ? 263  ARG   E NH2 1 
ATOM   13334 N  N   . VAL   E 2 264 ? 37.106  -28.345 -58.417 1.00 119.17 ? 264  VAL   E N   1 
ATOM   13335 C  CA  . VAL   E 2 264 ? 37.081  -27.361 -59.492 1.00 124.64 ? 264  VAL   E CA  1 
ATOM   13336 C  C   . VAL   E 2 264 ? 36.346  -27.845 -60.728 1.00 137.51 ? 264  VAL   E C   1 
ATOM   13337 O  O   . VAL   E 2 264 ? 35.262  -27.350 -61.047 1.00 136.35 ? 264  VAL   E O   1 
ATOM   13338 C  CB  . VAL   E 2 264 ? 38.495  -26.949 -59.945 1.00 121.91 ? 264  VAL   E CB  1 
ATOM   13339 C  CG1 . VAL   E 2 264 ? 38.411  -25.793 -60.886 1.00 118.98 ? 264  VAL   E CG1 1 
ATOM   13340 C  CG2 . VAL   E 2 264 ? 39.355  -26.578 -58.755 1.00 117.69 ? 264  VAL   E CG2 1 
ATOM   13341 N  N   . ASP   E 2 265 ? 36.923  -28.815 -61.429 1.00 166.15 ? 265  ASP   E N   1 
ATOM   13342 C  CA  . ASP   E 2 265 ? 36.221  -29.334 -62.589 1.00 165.97 ? 265  ASP   E CA  1 
ATOM   13343 C  C   . ASP   E 2 265 ? 35.404  -30.500 -62.046 1.00 165.66 ? 265  ASP   E C   1 
ATOM   13344 O  O   . ASP   E 2 265 ? 35.864  -31.213 -61.151 1.00 165.74 ? 265  ASP   E O   1 
ATOM   13345 C  CB  . ASP   E 2 265 ? 37.167  -29.827 -63.685 1.00 166.72 ? 265  ASP   E CB  1 
ATOM   13346 C  CG  . ASP   E 2 265 ? 38.392  -30.539 -63.125 1.00 168.18 ? 265  ASP   E CG  1 
ATOM   13347 O  OD1 . ASP   E 2 265 ? 38.242  -31.677 -62.628 1.00 168.06 ? 265  ASP   E OD1 1 
ATOM   13348 O  OD2 . ASP   E 2 265 ? 39.501  -29.957 -63.180 1.00 168.51 ? 265  ASP   E OD2 1 
ATOM   13349 N  N   . PRO   E 2 266 ? 34.193  -30.703 -62.541 1.00 141.95 ? 266  PRO   E N   1 
ATOM   13350 C  CA  . PRO   E 2 266 ? 33.422  -31.882 -62.126 1.00 138.95 ? 266  PRO   E CA  1 
ATOM   13351 C  C   . PRO   E 2 266 ? 34.049  -33.216 -62.514 1.00 133.58 ? 266  PRO   E C   1 
ATOM   13352 O  O   . PRO   E 2 266 ? 33.500  -34.280 -62.208 1.00 126.22 ? 266  PRO   E O   1 
ATOM   13353 C  CB  . PRO   E 2 266 ? 32.052  -31.632 -62.759 1.00 136.28 ? 266  PRO   E CB  1 
ATOM   13354 C  CG  . PRO   E 2 266 ? 31.953  -30.152 -62.792 1.00 133.33 ? 266  PRO   E CG  1 
ATOM   13355 C  CD  . PRO   E 2 266 ? 33.329  -29.662 -63.121 1.00 138.45 ? 266  PRO   E CD  1 
ATOM   13356 N  N   . ASN   E 2 267 ? 35.206  -33.165 -63.174 1.00 133.16 ? 267  ASN   E N   1 
ATOM   13357 C  CA  . ASN   E 2 267 ? 35.944  -34.371 -63.523 1.00 133.91 ? 267  ASN   E CA  1 
ATOM   13358 C  C   . ASN   E 2 267 ? 36.706  -34.979 -62.343 1.00 131.03 ? 267  ASN   E C   1 
ATOM   13359 O  O   . ASN   E 2 267 ? 36.743  -36.206 -62.180 1.00 126.16 ? 267  ASN   E O   1 
ATOM   13360 C  CB  . ASN   E 2 267 ? 36.889  -34.041 -64.684 1.00 137.39 ? 267  ASN   E CB  1 
ATOM   13361 C  CG  . ASN   E 2 267 ? 37.472  -35.271 -65.335 1.00 137.37 ? 267  ASN   E CG  1 
ATOM   13362 O  OD1 . ASN   E 2 267 ? 37.009  -35.714 -66.392 1.00 136.13 ? 267  ASN   E OD1 1 
ATOM   13363 N  ND2 . ASN   E 2 267 ? 38.513  -35.824 -64.717 1.00 138.52 ? 267  ASN   E ND2 1 
ATOM   13364 N  N   . GLY   E 2 268 ? 37.316  -34.137 -61.514 1.00 135.65 ? 268  GLY   E N   1 
ATOM   13365 C  CA  . GLY   E 2 268 ? 38.108  -34.582 -60.388 1.00 130.13 ? 268  GLY   E CA  1 
ATOM   13366 C  C   . GLY   E 2 268 ? 39.590  -34.314 -60.498 1.00 131.51 ? 268  GLY   E C   1 
ATOM   13367 O  O   . GLY   E 2 268 ? 40.328  -34.659 -59.570 1.00 127.33 ? 268  GLY   E O   1 
ATOM   13368 N  N   . SER   E 2 269 ? 40.051  -33.701 -61.588 1.00 137.08 ? 269  SER   E N   1 
ATOM   13369 C  CA  . SER   E 2 269 ? 41.485  -33.540 -61.789 1.00 137.80 ? 269  SER   E CA  1 
ATOM   13370 C  C   . SER   E 2 269 ? 42.051  -32.412 -60.941 1.00 139.02 ? 269  SER   E C   1 
ATOM   13371 O  O   . SER   E 2 269 ? 43.129  -32.565 -60.358 1.00 139.35 ? 269  SER   E O   1 
ATOM   13372 C  CB  . SER   E 2 269 ? 41.789  -33.296 -63.267 1.00 142.96 ? 269  SER   E CB  1 
ATOM   13373 O  OG  . SER   E 2 269 ? 41.786  -31.912 -63.592 1.00 152.79 ? 269  SER   E OG  1 
ATOM   13374 N  N   . ARG   E 2 270 ? 41.345  -31.283 -60.848 1.00 132.21 ? 270  ARG   E N   1 
ATOM   13375 C  CA  . ARG   E 2 270 ? 41.817  -30.129 -60.096 1.00 124.66 ? 270  ARG   E CA  1 
ATOM   13376 C  C   . ARG   E 2 270 ? 40.873  -29.860 -58.927 1.00 121.08 ? 270  ARG   E C   1 
ATOM   13377 O  O   . ARG   E 2 270 ? 39.653  -29.792 -59.113 1.00 123.96 ? 270  ARG   E O   1 
ATOM   13378 C  CB  . ARG   E 2 270 ? 41.951  -28.901 -61.005 1.00 129.87 ? 270  ARG   E CB  1 
ATOM   13379 C  CG  . ARG   E 2 270 ? 42.831  -29.138 -62.253 1.00 135.38 ? 270  ARG   E CG  1 
ATOM   13380 C  CD  . ARG   E 2 270 ? 43.820  -28.000 -62.548 1.00 133.76 ? 270  ARG   E CD  1 
ATOM   13381 N  NE  . ARG   E 2 270 ? 43.207  -26.686 -62.402 1.00 135.49 ? 270  ARG   E NE  1 
ATOM   13382 C  CZ  . ARG   E 2 270 ? 42.422  -26.117 -63.308 1.00 146.39 ? 270  ARG   E CZ  1 
ATOM   13383 N  NH1 . ARG   E 2 270 ? 42.162  -26.707 -64.467 1.00 150.42 ? 270  ARG   E NH1 1 
ATOM   13384 N  NH2 . ARG   E 2 270 ? 41.877  -24.929 -63.043 1.00 146.52 ? 270  ARG   E NH2 1 
ATOM   13385 N  N   . TYR   E 2 271 ? 41.451  -29.731 -57.725 1.00 115.51 ? 271  TYR   E N   1 
ATOM   13386 C  CA  . TYR   E 2 271 ? 40.755  -29.528 -56.460 1.00 105.76 ? 271  TYR   E CA  1 
ATOM   13387 C  C   . TYR   E 2 271 ? 41.359  -28.321 -55.751 1.00 104.93 ? 271  TYR   E C   1 
ATOM   13388 O  O   . TYR   E 2 271 ? 42.539  -28.016 -55.928 1.00 109.07 ? 271  TYR   E O   1 
ATOM   13389 C  CB  . TYR   E 2 271 ? 40.886  -30.765 -55.564 1.00 104.45 ? 271  TYR   E CB  1 
ATOM   13390 C  CG  . TYR   E 2 271 ? 39.815  -31.810 -55.754 1.00 106.95 ? 271  TYR   E CG  1 
ATOM   13391 C  CD1 . TYR   E 2 271 ? 38.599  -31.683 -55.111 1.00 105.83 ? 271  TYR   E CD1 1 
ATOM   13392 C  CD2 . TYR   E 2 271 ? 40.026  -32.928 -56.552 1.00 108.68 ? 271  TYR   E CD2 1 
ATOM   13393 C  CE1 . TYR   E 2 271 ? 37.626  -32.618 -55.256 1.00 105.62 ? 271  TYR   E CE1 1 
ATOM   13394 C  CE2 . TYR   E 2 271 ? 39.052  -33.873 -56.711 1.00 106.37 ? 271  TYR   E CE2 1 
ATOM   13395 C  CZ  . TYR   E 2 271 ? 37.848  -33.708 -56.057 1.00 106.84 ? 271  TYR   E CZ  1 
ATOM   13396 O  OH  . TYR   E 2 271 ? 36.842  -34.629 -56.187 1.00 109.00 ? 271  TYR   E OH  1 
ATOM   13397 N  N   . LEU   E 2 272 ? 40.560  -27.638 -54.934 1.00 102.76 ? 272  LEU   E N   1 
ATOM   13398 C  CA  . LEU   E 2 272 ? 41.003  -26.431 -54.239 1.00 98.69  ? 272  LEU   E CA  1 
ATOM   13399 C  C   . LEU   E 2 272 ? 41.072  -26.659 -52.735 1.00 92.80  ? 272  LEU   E C   1 
ATOM   13400 O  O   . LEU   E 2 272 ? 40.130  -27.192 -52.143 1.00 93.50  ? 272  LEU   E O   1 
ATOM   13401 C  CB  . LEU   E 2 272 ? 40.063  -25.265 -54.538 1.00 99.77  ? 272  LEU   E CB  1 
ATOM   13402 C  CG  . LEU   E 2 272 ? 40.484  -24.378 -55.706 1.00 97.31  ? 272  LEU   E CG  1 
ATOM   13403 C  CD1 . LEU   E 2 272 ? 39.429  -23.328 -55.986 1.00 93.90  ? 272  LEU   E CD1 1 
ATOM   13404 C  CD2 . LEU   E 2 272 ? 41.817  -23.744 -55.376 1.00 98.42  ? 272  LEU   E CD2 1 
ATOM   13405 N  N   . LEU   E 2 273 ? 42.168  -26.220 -52.116 1.00 94.78  ? 273  LEU   E N   1 
ATOM   13406 C  CA  . LEU   E 2 273 ? 42.423  -26.457 -50.700 1.00 97.22  ? 273  LEU   E CA  1 
ATOM   13407 C  C   . LEU   E 2 273 ? 42.637  -25.156 -49.943 1.00 93.20  ? 273  LEU   E C   1 
ATOM   13408 O  O   . LEU   E 2 273 ? 43.286  -24.232 -50.431 1.00 94.95  ? 273  LEU   E O   1 
ATOM   13409 C  CB  . LEU   E 2 273 ? 43.651  -27.341 -50.492 1.00 96.58  ? 273  LEU   E CB  1 
ATOM   13410 C  CG  . LEU   E 2 273 ? 43.506  -28.758 -51.023 1.00 95.84  ? 273  LEU   E CG  1 
ATOM   13411 C  CD1 . LEU   E 2 273 ? 44.757  -29.582 -50.734 1.00 95.46  ? 273  LEU   E CD1 1 
ATOM   13412 C  CD2 . LEU   E 2 273 ? 42.236  -29.390 -50.450 1.00 93.22  ? 273  LEU   E CD2 1 
ATOM   13413 N  N   . GLY   E 2 274 ? 42.126  -25.103 -48.731 1.00 92.27  ? 274  GLY   E N   1 
ATOM   13414 C  CA  . GLY   E 2 274 ? 42.368  -23.938 -47.920 1.00 95.93  ? 274  GLY   E CA  1 
ATOM   13415 C  C   . GLY   E 2 274 ? 42.689  -24.307 -46.492 1.00 93.24  ? 274  GLY   E C   1 
ATOM   13416 O  O   . GLY   E 2 274 ? 42.063  -25.210 -45.926 1.00 91.68  ? 274  GLY   E O   1 
ATOM   13417 N  N   . ASP   E 2 275 ? 43.655  -23.613 -45.894 1.00 91.98  ? 275  ASP   E N   1 
ATOM   13418 C  CA  . ASP   E 2 275 ? 44.042  -23.882 -44.520 1.00 96.51  ? 275  ASP   E CA  1 
ATOM   13419 C  C   . ASP   E 2 275 ? 43.526  -22.777 -43.589 1.00 96.79  ? 275  ASP   E C   1 
ATOM   13420 O  O   . ASP   E 2 275 ? 42.773  -21.879 -43.993 1.00 97.14  ? 275  ASP   E O   1 
ATOM   13421 C  CB  . ASP   E 2 275 ? 45.564  -24.100 -44.416 1.00 97.37  ? 275  ASP   E CB  1 
ATOM   13422 C  CG  . ASP   E 2 275 ? 46.390  -22.835 -44.610 1.00 98.40  ? 275  ASP   E CG  1 
ATOM   13423 O  OD1 . ASP   E 2 275 ? 45.851  -21.712 -44.693 1.00 101.64 ? 275  ASP   E OD1 1 
ATOM   13424 O  OD2 . ASP   E 2 275 ? 47.624  -22.984 -44.675 1.00 99.38  ? 275  ASP   E OD2 1 
ATOM   13425 N  N   . MET   E 2 276 ? 43.918  -22.848 -42.324 1.00 91.78  ? 276  MET   E N   1 
ATOM   13426 C  CA  . MET   E 2 276 ? 43.363  -21.951 -41.334 1.00 94.21  ? 276  MET   E CA  1 
ATOM   13427 C  C   . MET   E 2 276 ? 44.115  -20.639 -41.249 1.00 99.43  ? 276  MET   E C   1 
ATOM   13428 O  O   . MET   E 2 276 ? 43.901  -19.880 -40.300 1.00 101.20 ? 276  MET   E O   1 
ATOM   13429 C  CB  . MET   E 2 276 ? 43.350  -22.631 -39.978 1.00 96.10  ? 276  MET   E CB  1 
ATOM   13430 C  CG  . MET   E 2 276 ? 42.974  -24.079 -40.062 1.00 98.77  ? 276  MET   E CG  1 
ATOM   13431 S  SD  . MET   E 2 276 ? 43.343  -25.000 -38.555 1.00 97.30  ? 276  MET   E SD  1 
ATOM   13432 C  CE  . MET   E 2 276 ? 41.791  -25.023 -37.696 1.00 92.41  ? 276  MET   E CE  1 
ATOM   13433 N  N   . GLU   E 2 277 ? 45.009  -20.365 -42.198 1.00 99.41  ? 277  GLU   E N   1 
ATOM   13434 C  CA  . GLU   E 2 277 ? 45.711  -19.089 -42.249 1.00 99.87  ? 277  GLU   E CA  1 
ATOM   13435 C  C   . GLU   E 2 277 ? 45.565  -18.440 -43.615 1.00 100.06 ? 277  GLU   E C   1 
ATOM   13436 O  O   . GLU   E 2 277 ? 46.378  -17.588 -43.987 1.00 101.38 ? 277  GLU   E O   1 
ATOM   13437 C  CB  . GLU   E 2 277 ? 47.192  -19.254 -41.891 1.00 103.90 ? 277  GLU   E CB  1 
ATOM   13438 C  CG  . GLU   E 2 277 ? 47.464  -20.371 -40.878 1.00 104.99 ? 277  GLU   E CG  1 
ATOM   13439 C  CD  . GLU   E 2 277 ? 48.937  -20.525 -40.556 1.00 115.16 ? 277  GLU   E CD  1 
ATOM   13440 O  OE1 . GLU   E 2 277 ? 49.692  -19.546 -40.769 1.00 120.74 ? 277  GLU   E OE1 1 
ATOM   13441 O  OE2 . GLU   E 2 277 ? 49.343  -21.618 -40.093 1.00 114.33 ? 277  GLU   E OE2 1 
ATOM   13442 N  N   . GLY   E 2 278 ? 44.549  -18.838 -44.372 1.00 112.29 ? 278  GLY   E N   1 
ATOM   13443 C  CA  . GLY   E 2 278 ? 44.205  -18.173 -45.604 1.00 114.31 ? 278  GLY   E CA  1 
ATOM   13444 C  C   . GLY   E 2 278 ? 44.888  -18.699 -46.845 1.00 114.74 ? 278  GLY   E C   1 
ATOM   13445 O  O   . GLY   E 2 278 ? 44.625  -18.185 -47.941 1.00 115.14 ? 278  GLY   E O   1 
ATOM   13446 N  N   . ARG   E 2 279 ? 45.751  -19.700 -46.721 1.00 102.86 ? 279  ARG   E N   1 
ATOM   13447 C  CA  . ARG   E 2 279 ? 46.460  -20.185 -47.891 1.00 97.85  ? 279  ARG   E CA  1 
ATOM   13448 C  C   . ARG   E 2 279 ? 45.525  -21.002 -48.771 1.00 101.08 ? 279  ARG   E C   1 
ATOM   13449 O  O   . ARG   E 2 279 ? 44.792  -21.874 -48.292 1.00 101.26 ? 279  ARG   E O   1 
ATOM   13450 C  CB  . ARG   E 2 279 ? 47.672  -21.004 -47.474 1.00 93.16  ? 279  ARG   E CB  1 
ATOM   13451 C  CG  . ARG   E 2 279 ? 48.687  -20.175 -46.779 1.00 96.32  ? 279  ARG   E CG  1 
ATOM   13452 C  CD  . ARG   E 2 279 ? 49.999  -20.891 -46.649 1.00 100.37 ? 279  ARG   E CD  1 
ATOM   13453 N  NE  . ARG   E 2 279 ? 50.052  -21.690 -45.433 1.00 106.95 ? 279  ARG   E NE  1 
ATOM   13454 C  CZ  . ARG   E 2 279 ? 50.578  -21.278 -44.288 1.00 109.29 ? 279  ARG   E CZ  1 
ATOM   13455 N  NH1 . ARG   E 2 279 ? 51.114  -20.074 -44.168 1.00 110.07 ? 279  ARG   E NH1 1 
ATOM   13456 N  NH2 . ARG   E 2 279 ? 50.567  -22.096 -43.239 1.00 113.87 ? 279  ARG   E NH2 1 
ATOM   13457 N  N   . LEU   E 2 280 ? 45.551  -20.706 -50.062 1.00 101.96 ? 280  LEU   E N   1 
ATOM   13458 C  CA  . LEU   E 2 280 ? 44.750  -21.390 -51.071 1.00 100.09 ? 280  LEU   E CA  1 
ATOM   13459 C  C   . LEU   E 2 280 ? 45.686  -22.272 -51.898 1.00 101.47 ? 280  LEU   E C   1 
ATOM   13460 O  O   . LEU   E 2 280 ? 46.445  -21.766 -52.731 1.00 101.48 ? 280  LEU   E O   1 
ATOM   13461 C  CB  . LEU   E 2 280 ? 44.018  -20.368 -51.941 1.00 93.26  ? 280  LEU   E CB  1 
ATOM   13462 C  CG  . LEU   E 2 280 ? 43.052  -20.809 -53.039 1.00 85.07  ? 280  LEU   E CG  1 
ATOM   13463 C  CD1 . LEU   E 2 280 ? 41.885  -21.580 -52.488 1.00 87.28  ? 280  LEU   E CD1 1 
ATOM   13464 C  CD2 . LEU   E 2 280 ? 42.547  -19.603 -53.784 1.00 88.83  ? 280  LEU   E CD2 1 
ATOM   13465 N  N   . PHE   E 2 281 ? 45.643  -23.587 -51.662 1.00 106.05 ? 281  PHE   E N   1 
ATOM   13466 C  CA  . PHE   E 2 281 ? 46.394  -24.524 -52.489 1.00 106.09 ? 281  PHE   E CA  1 
ATOM   13467 C  C   . PHE   E 2 281 ? 45.519  -25.175 -53.558 1.00 106.33 ? 281  PHE   E C   1 
ATOM   13468 O  O   . PHE   E 2 281 ? 44.291  -25.258 -53.452 1.00 105.64 ? 281  PHE   E O   1 
ATOM   13469 C  CB  . PHE   E 2 281 ? 47.037  -25.648 -51.680 1.00 103.52 ? 281  PHE   E CB  1 
ATOM   13470 C  CG  . PHE   E 2 281 ? 47.603  -25.219 -50.393 1.00 103.09 ? 281  PHE   E CG  1 
ATOM   13471 C  CD1 . PHE   E 2 281 ? 48.885  -24.741 -50.315 1.00 106.25 ? 281  PHE   E CD1 1 
ATOM   13472 C  CD2 . PHE   E 2 281 ? 46.857  -25.336 -49.247 1.00 104.20 ? 281  PHE   E CD2 1 
ATOM   13473 C  CE1 . PHE   E 2 281 ? 49.410  -24.359 -49.114 1.00 108.50 ? 281  PHE   E CE1 1 
ATOM   13474 C  CE2 . PHE   E 2 281 ? 47.372  -24.967 -48.045 1.00 109.15 ? 281  PHE   E CE2 1 
ATOM   13475 C  CZ  . PHE   E 2 281 ? 48.658  -24.474 -47.974 1.00 112.11 ? 281  PHE   E CZ  1 
ATOM   13476 N  N   . MET   E 2 282 ? 46.188  -25.698 -54.575 1.00 107.08 ? 282  MET   E N   1 
ATOM   13477 C  CA  . MET   E 2 282 ? 45.534  -26.383 -55.680 1.00 108.80 ? 282  MET   E CA  1 
ATOM   13478 C  C   . MET   E 2 282 ? 46.027  -27.827 -55.701 1.00 109.95 ? 282  MET   E C   1 
ATOM   13479 O  O   . MET   E 2 282 ? 47.216  -28.078 -55.908 1.00 109.34 ? 282  MET   E O   1 
ATOM   13480 C  CB  . MET   E 2 282 ? 45.831  -25.651 -56.988 1.00 111.15 ? 282  MET   E CB  1 
ATOM   13481 C  CG  . MET   E 2 282 ? 45.387  -26.338 -58.271 1.00 114.04 ? 282  MET   E CG  1 
ATOM   13482 S  SD  . MET   E 2 282 ? 43.615  -26.439 -58.619 1.00 120.35 ? 282  MET   E SD  1 
ATOM   13483 C  CE  . MET   E 2 282 ? 43.045  -24.767 -58.435 1.00 115.37 ? 282  MET   E CE  1 
ATOM   13484 N  N   . LEU   E 2 283 ? 45.127  -28.773 -55.440 1.00 107.42 ? 283  LEU   E N   1 
ATOM   13485 C  CA  . LEU   E 2 283 ? 45.436  -30.189 -55.578 1.00 105.64 ? 283  LEU   E CA  1 
ATOM   13486 C  C   . LEU   E 2 283 ? 45.165  -30.597 -57.022 1.00 114.18 ? 283  LEU   E C   1 
ATOM   13487 O  O   . LEU   E 2 283 ? 44.026  -30.502 -57.491 1.00 115.97 ? 283  LEU   E O   1 
ATOM   13488 C  CB  . LEU   E 2 283 ? 44.604  -31.034 -54.613 1.00 98.52  ? 283  LEU   E CB  1 
ATOM   13489 C  CG  . LEU   E 2 283 ? 44.944  -32.529 -54.597 1.00 97.66  ? 283  LEU   E CG  1 
ATOM   13490 C  CD1 . LEU   E 2 283 ? 46.276  -32.806 -53.925 1.00 96.89  ? 283  LEU   E CD1 1 
ATOM   13491 C  CD2 . LEU   E 2 283 ? 43.849  -33.325 -53.946 1.00 97.34  ? 283  LEU   E CD2 1 
ATOM   13492 N  N   . LEU   E 2 284 ? 46.202  -31.056 -57.726 1.00 115.84 ? 284  LEU   E N   1 
ATOM   13493 C  CA  . LEU   E 2 284 ? 46.051  -31.601 -59.073 1.00 113.74 ? 284  LEU   E CA  1 
ATOM   13494 C  C   . LEU   E 2 284 ? 46.202  -33.118 -59.020 1.00 114.62 ? 284  LEU   E C   1 
ATOM   13495 O  O   . LEU   E 2 284 ? 47.100  -33.635 -58.344 1.00 111.36 ? 284  LEU   E O   1 
ATOM   13496 C  CB  . LEU   E 2 284 ? 47.072  -30.988 -60.042 1.00 111.71 ? 284  LEU   E CB  1 
ATOM   13497 C  CG  . LEU   E 2 284 ? 47.115  -29.457 -60.149 1.00 111.23 ? 284  LEU   E CG  1 
ATOM   13498 C  CD1 . LEU   E 2 284 ? 48.384  -28.926 -59.529 1.00 111.58 ? 284  LEU   E CD1 1 
ATOM   13499 C  CD2 . LEU   E 2 284 ? 46.993  -28.962 -61.577 1.00 119.91 ? 284  LEU   E CD2 1 
ATOM   13500 N  N   . LEU   E 2 285 ? 45.308  -33.825 -59.708 1.00 117.31 ? 285  LEU   E N   1 
ATOM   13501 C  CA  . LEU   E 2 285 ? 45.425  -35.270 -59.906 1.00 117.11 ? 285  LEU   E CA  1 
ATOM   13502 C  C   . LEU   E 2 285 ? 45.992  -35.483 -61.305 1.00 121.06 ? 285  LEU   E C   1 
ATOM   13503 O  O   . LEU   E 2 285 ? 45.257  -35.507 -62.292 1.00 127.63 ? 285  LEU   E O   1 
ATOM   13504 C  CB  . LEU   E 2 285 ? 44.075  -35.964 -59.736 1.00 117.73 ? 285  LEU   E CB  1 
ATOM   13505 C  CG  . LEU   E 2 285 ? 43.490  -36.103 -58.326 1.00 118.14 ? 285  LEU   E CG  1 
ATOM   13506 C  CD1 . LEU   E 2 285 ? 42.952  -34.777 -57.812 1.00 118.55 ? 285  LEU   E CD1 1 
ATOM   13507 C  CD2 . LEU   E 2 285 ? 42.401  -37.169 -58.268 1.00 115.26 ? 285  LEU   E CD2 1 
ATOM   13508 N  N   . GLU   E 2 286 ? 47.318  -35.625 -61.392 1.00 121.83 ? 286  GLU   E N   1 
ATOM   13509 C  CA  . GLU   E 2 286 ? 47.992  -35.844 -62.670 1.00 128.86 ? 286  GLU   E CA  1 
ATOM   13510 C  C   . GLU   E 2 286 ? 47.531  -37.168 -63.286 1.00 136.94 ? 286  GLU   E C   1 
ATOM   13511 O  O   . GLU   E 2 286 ? 47.802  -38.242 -62.734 1.00 136.46 ? 286  GLU   E O   1 
ATOM   13512 C  CB  . GLU   E 2 286 ? 49.511  -35.813 -62.477 1.00 120.86 ? 286  GLU   E CB  1 
ATOM   13513 N  N   . LYS   E 2 287 ? 46.797  -37.103 -64.403 1.00 141.95 ? 287  LYS   E N   1 
ATOM   13514 C  CA  . LYS   E 2 287 ? 46.125  -38.263 -64.976 1.00 145.43 ? 287  LYS   E CA  1 
ATOM   13515 C  C   . LYS   E 2 287 ? 46.937  -38.833 -66.145 1.00 161.59 ? 287  LYS   E C   1 
ATOM   13516 O  O   . LYS   E 2 287 ? 47.961  -38.274 -66.547 1.00 162.73 ? 287  LYS   E O   1 
ATOM   13517 C  CB  . LYS   E 2 287 ? 44.703  -37.886 -65.402 1.00 139.23 ? 287  LYS   E CB  1 
ATOM   13518 N  N   . GLU   E 2 288 ? 46.469  -39.956 -66.709 1.00 182.45 ? 288  GLU   E N   1 
ATOM   13519 C  CA  . GLU   E 2 288 ? 47.257  -40.728 -67.682 1.00 186.64 ? 288  GLU   E CA  1 
ATOM   13520 C  C   . GLU   E 2 288 ? 46.336  -41.435 -68.675 1.00 187.67 ? 288  GLU   E C   1 
ATOM   13521 O  O   . GLU   E 2 288 ? 45.662  -42.398 -68.307 1.00 186.49 ? 288  GLU   E O   1 
ATOM   13522 C  CB  . GLU   E 2 288 ? 48.155  -41.740 -66.959 1.00 189.06 ? 288  GLU   E CB  1 
ATOM   13523 C  CG  . GLU   E 2 288 ? 49.052  -42.603 -67.859 1.00 194.66 ? 288  GLU   E CG  1 
ATOM   13524 C  CD  . GLU   E 2 288 ? 50.103  -43.398 -67.079 1.00 197.35 ? 288  GLU   E CD  1 
ATOM   13525 O  OE1 . GLU   E 2 288 ? 49.761  -43.970 -66.020 1.00 199.63 ? 288  GLU   E OE1 1 
ATOM   13526 O  OE2 . GLU   E 2 288 ? 51.271  -43.452 -67.531 1.00 194.74 ? 288  GLU   E OE2 1 
ATOM   13527 N  N   . GLU   E 2 289 ? 46.360  -41.000 -69.942 1.00 179.28 ? 289  GLU   E N   1 
ATOM   13528 C  CA  . GLU   E 2 289 ? 45.483  -41.518 -71.000 1.00 175.54 ? 289  GLU   E CA  1 
ATOM   13529 C  C   . GLU   E 2 289 ? 46.121  -42.723 -71.685 1.00 175.93 ? 289  GLU   E C   1 
ATOM   13530 O  O   . GLU   E 2 289 ? 46.933  -42.575 -72.603 1.00 174.83 ? 289  GLU   E O   1 
ATOM   13531 C  CB  . GLU   E 2 289 ? 45.200  -40.430 -72.034 1.00 168.29 ? 289  GLU   E CB  1 
ATOM   13532 C  CG  . GLU   E 2 289 ? 44.425  -39.237 -71.512 1.00 165.77 ? 289  GLU   E CG  1 
ATOM   13533 C  CD  . GLU   E 2 289 ? 44.624  -37.991 -72.377 1.00 164.98 ? 289  GLU   E CD  1 
ATOM   13534 O  OE1 . GLU   E 2 289 ? 45.165  -38.108 -73.509 1.00 161.33 ? 289  GLU   E OE1 1 
ATOM   13535 O  OE2 . GLU   E 2 289 ? 44.242  -36.890 -71.916 1.00 167.29 ? 289  GLU   E OE2 1 
ATOM   13536 N  N   . GLN   E 2 290 ? 45.828  -43.929 -71.206 1.00 171.41 ? 290  GLN   E N   1 
ATOM   13537 C  CA  . GLN   E 2 290 ? 46.526  -45.092 -71.813 1.00 165.74 ? 290  GLN   E CA  1 
ATOM   13538 C  C   . GLN   E 2 290 ? 46.046  -45.245 -73.265 1.00 163.96 ? 290  GLN   E C   1 
ATOM   13539 O  O   . GLN   E 2 290 ? 44.940  -44.755 -73.574 1.00 163.72 ? 290  GLN   E O   1 
ATOM   13540 C  CB  . GLN   E 2 290 ? 46.310  -46.347 -70.967 1.00 164.56 ? 290  GLN   E CB  1 
ATOM   13541 C  CG  . GLN   E 2 290 ? 46.332  -46.091 -69.463 1.00 170.73 ? 290  GLN   E CG  1 
ATOM   13542 C  CD  . GLN   E 2 290 ? 47.722  -45.966 -68.879 1.00 179.11 ? 290  GLN   E CD  1 
ATOM   13543 O  OE1 . GLN   E 2 290 ? 48.712  -45.761 -69.589 1.00 180.72 ? 290  GLN   E OE1 1 
ATOM   13544 N  NE2 . GLN   E 2 290 ? 47.809  -46.090 -67.563 1.00 177.18 ? 290  GLN   E NE2 1 
ATOM   13545 N  N   . MET   E 2 291 ? 46.855  -45.867 -74.129 1.00 166.84 ? 291  MET   E N   1 
ATOM   13546 C  CA  . MET   E 2 291 ? 46.408  -46.126 -75.524 1.00 160.02 ? 291  MET   E CA  1 
ATOM   13547 C  C   . MET   E 2 291 ? 45.041  -46.808 -75.438 1.00 155.08 ? 291  MET   E C   1 
ATOM   13548 O  O   . MET   E 2 291 ? 44.077  -46.276 -76.024 1.00 153.92 ? 291  MET   E O   1 
ATOM   13549 C  CB  . MET   E 2 291 ? 47.398  -47.018 -76.275 1.00 146.72 ? 291  MET   E CB  1 
ATOM   13550 C  CG  . MET   E 2 291 ? 48.741  -46.359 -76.500 1.00 145.04 ? 291  MET   E CG  1 
ATOM   13551 S  SD  . MET   E 2 291 ? 48.560  -44.849 -77.468 1.00 133.81 ? 291  MET   E SD  1 
ATOM   13552 C  CE  . MET   E 2 291 ? 48.036  -45.532 -79.046 1.00 146.16 ? 291  MET   E CE  1 
ATOM   13553 N  N   . ASP   E 2 292 ? 44.963  -47.943 -74.741 1.00 152.52 ? 292  ASP   E N   1 
ATOM   13554 C  CA  . ASP   E 2 292 ? 43.624  -48.544 -74.514 1.00 149.89 ? 292  ASP   E CA  1 
ATOM   13555 C  C   . ASP   E 2 292 ? 42.904  -47.370 -73.852 1.00 158.28 ? 292  ASP   E C   1 
ATOM   13556 O  O   . ASP   E 2 292 ? 43.605  -46.566 -73.209 1.00 157.98 ? 292  ASP   E O   1 
ATOM   13557 C  CB  . ASP   E 2 292 ? 43.728  -49.904 -73.844 1.00 145.71 ? 292  ASP   E CB  1 
ATOM   13558 C  CG  . ASP   E 2 292 ? 42.422  -50.657 -73.647 1.00 149.04 ? 292  ASP   E CG  1 
ATOM   13559 O  OD1 . ASP   E 2 292 ? 41.372  -50.123 -74.061 1.00 152.89 ? 292  ASP   E OD1 1 
ATOM   13560 O  OD2 . ASP   E 2 292 ? 42.470  -51.767 -73.080 1.00 145.81 ? 292  ASP   E OD2 1 
ATOM   13561 N  N   . GLY   E 2 293 ? 41.585  -47.249 -74.020 1.00 181.92 ? 293  GLY   E N   1 
ATOM   13562 C  CA  . GLY   E 2 293 ? 40.819  -46.094 -73.495 1.00 181.25 ? 293  GLY   E CA  1 
ATOM   13563 C  C   . GLY   E 2 293 ? 41.121  -45.830 -72.030 1.00 182.80 ? 293  GLY   E C   1 
ATOM   13564 O  O   . GLY   E 2 293 ? 40.901  -44.684 -71.597 1.00 181.81 ? 293  GLY   E O   1 
ATOM   13565 N  N   . THR   E 2 294 ? 41.580  -46.839 -71.288 1.00 162.95 ? 294  THR   E N   1 
ATOM   13566 C  CA  . THR   E 2 294 ? 41.880  -46.723 -69.844 1.00 162.37 ? 294  THR   E CA  1 
ATOM   13567 C  C   . THR   E 2 294 ? 42.706  -45.528 -69.422 1.00 164.52 ? 294  THR   E C   1 
ATOM   13568 O  O   . THR   E 2 294 ? 43.785  -45.310 -70.004 1.00 163.38 ? 294  THR   E O   1 
ATOM   13569 C  CB  . THR   E 2 294 ? 42.700  -47.948 -69.448 1.00 163.75 ? 294  THR   E CB  1 
ATOM   13570 O  OG1 . THR   E 2 294 ? 41.819  -49.047 -69.658 1.00 163.39 ? 294  THR   E OG1 1 
ATOM   13571 C  CG2 . THR   E 2 294 ? 43.154  -47.920 -68.000 1.00 157.02 ? 294  THR   E CG2 1 
ATOM   13572 N  N   . VAL   E 2 295 ? 42.211  -44.767 -68.448 1.00 170.58 ? 295  VAL   E N   1 
ATOM   13573 C  CA  . VAL   E 2 295 ? 42.915  -43.656 -67.823 1.00 166.70 ? 295  VAL   E CA  1 
ATOM   13574 C  C   . VAL   E 2 295 ? 43.224  -43.985 -66.364 1.00 161.63 ? 295  VAL   E C   1 
ATOM   13575 O  O   . VAL   E 2 295 ? 42.386  -44.567 -65.667 1.00 157.16 ? 295  VAL   E O   1 
ATOM   13576 C  CB  . VAL   E 2 295 ? 42.061  -42.374 -67.948 1.00 161.62 ? 295  VAL   E CB  1 
ATOM   13577 C  CG1 . VAL   E 2 295 ? 42.913  -41.142 -67.730 1.00 162.81 ? 295  VAL   E CG1 1 
ATOM   13578 C  CG2 . VAL   E 2 295 ? 41.364  -42.295 -69.316 1.00 156.81 ? 295  VAL   E CG2 1 
ATOM   13579 N  N   . THR   E 2 296 ? 44.434  -43.649 -65.912 1.00 159.29 ? 296  THR   E N   1 
ATOM   13580 C  CA  . THR   E 2 296 ? 44.877  -43.954 -64.554 1.00 158.44 ? 296  THR   E CA  1 
ATOM   13581 C  C   . THR   E 2 296 ? 45.447  -42.697 -63.903 1.00 155.72 ? 296  THR   E C   1 
ATOM   13582 O  O   . THR   E 2 296 ? 45.505  -41.628 -64.520 1.00 155.12 ? 296  THR   E O   1 
ATOM   13583 C  CB  . THR   E 2 296 ? 45.920  -45.083 -64.542 1.00 163.45 ? 296  THR   E CB  1 
ATOM   13584 O  OG1 . THR   E 2 296 ? 47.019  -44.734 -65.393 1.00 168.24 ? 296  THR   E OG1 1 
ATOM   13585 C  CG2 . THR   E 2 296 ? 45.302  -46.396 -65.019 1.00 164.75 ? 296  THR   E CG2 1 
ATOM   13586 N  N   . LEU   E 2 297 ? 45.871  -42.831 -62.634 1.00 151.07 ? 297  LEU   E N   1 
ATOM   13587 C  CA  . LEU   E 2 297 ? 46.381  -41.715 -61.833 1.00 142.83 ? 297  LEU   E CA  1 
ATOM   13588 C  C   . LEU   E 2 297 ? 47.893  -41.833 -61.707 1.00 137.19 ? 297  LEU   E C   1 
ATOM   13589 O  O   . LEU   E 2 297 ? 48.396  -42.729 -61.020 1.00 125.99 ? 297  LEU   E O   1 
ATOM   13590 C  CB  . LEU   E 2 297 ? 45.733  -41.669 -60.451 1.00 135.57 ? 297  LEU   E CB  1 
ATOM   13591 C  CG  . LEU   E 2 297 ? 45.947  -40.377 -59.666 1.00 127.30 ? 297  LEU   E CG  1 
ATOM   13592 C  CD1 . LEU   E 2 297 ? 45.407  -39.197 -60.439 1.00 128.40 ? 297  LEU   E CD1 1 
ATOM   13593 C  CD2 . LEU   E 2 297 ? 45.261  -40.496 -58.334 1.00 121.65 ? 297  LEU   E CD2 1 
ATOM   13594 N  N   . LYS   E 2 298 ? 48.603  -40.917 -62.373 1.00 141.89 ? 298  LYS   E N   1 
ATOM   13595 C  CA  . LYS   E 2 298 ? 50.059  -40.846 -62.284 1.00 140.24 ? 298  LYS   E CA  1 
ATOM   13596 C  C   . LYS   E 2 298 ? 50.494  -40.424 -60.887 1.00 137.51 ? 298  LYS   E C   1 
ATOM   13597 O  O   . LYS   E 2 298 ? 51.152  -41.186 -60.165 1.00 136.25 ? 298  LYS   E O   1 
ATOM   13598 C  CB  . LYS   E 2 298 ? 50.609  -39.857 -63.329 1.00 144.97 ? 298  LYS   E CB  1 
ATOM   13599 C  CG  . LYS   E 2 298 ? 51.079  -40.456 -64.671 1.00 159.17 ? 298  LYS   E CG  1 
ATOM   13600 C  CD  . LYS   E 2 298 ? 51.432  -39.364 -65.713 1.00 166.94 ? 298  LYS   E CD  1 
ATOM   13601 C  CE  . LYS   E 2 298 ? 51.958  -39.968 -67.031 1.00 173.60 ? 298  LYS   E CE  1 
ATOM   13602 N  NZ  . LYS   E 2 298 ? 51.744  -39.102 -68.234 1.00 167.29 ? 298  LYS   E NZ  1 
ATOM   13603 N  N   . ASP   E 2 299 ? 50.129  -39.209 -60.486 1.00 130.44 ? 299  ASP   E N   1 
ATOM   13604 C  CA  . ASP   E 2 299 ? 50.680  -38.616 -59.280 1.00 123.49 ? 299  ASP   E CA  1 
ATOM   13605 C  C   . ASP   E 2 299 ? 49.646  -37.682 -58.666 1.00 116.45 ? 299  ASP   E C   1 
ATOM   13606 O  O   . ASP   E 2 299 ? 48.476  -37.664 -59.060 1.00 115.62 ? 299  ASP   E O   1 
ATOM   13607 C  CB  . ASP   E 2 299 ? 51.998  -37.891 -59.594 1.00 120.47 ? 299  ASP   E CB  1 
ATOM   13608 C  CG  . ASP   E 2 299 ? 53.015  -37.983 -58.455 1.00 118.58 ? 299  ASP   E CG  1 
ATOM   13609 O  OD1 . ASP   E 2 299 ? 53.144  -39.062 -57.835 1.00 122.03 ? 299  ASP   E OD1 1 
ATOM   13610 O  OD2 . ASP   E 2 299 ? 53.717  -36.981 -58.205 1.00 115.68 ? 299  ASP   E OD2 1 
ATOM   13611 N  N   . LEU   E 2 300 ? 50.096  -36.922 -57.676 1.00 115.82 ? 300  LEU   E N   1 
ATOM   13612 C  CA  . LEU   E 2 300 ? 49.304  -35.928 -56.974 1.00 113.00 ? 300  LEU   E CA  1 
ATOM   13613 C  C   . LEU   E 2 300 ? 50.215  -34.753 -56.660 1.00 112.67 ? 300  LEU   E C   1 
ATOM   13614 O  O   . LEU   E 2 300 ? 51.255  -34.929 -56.012 1.00 114.72 ? 300  LEU   E O   1 
ATOM   13615 C  CB  . LEU   E 2 300 ? 48.719  -36.501 -55.680 1.00 112.89 ? 300  LEU   E CB  1 
ATOM   13616 C  CG  . LEU   E 2 300 ? 47.420  -37.276 -55.760 1.00 108.65 ? 300  LEU   E CG  1 
ATOM   13617 C  CD1 . LEU   E 2 300 ? 47.174  -37.862 -54.398 1.00 106.35 ? 300  LEU   E CD1 1 
ATOM   13618 C  CD2 . LEU   E 2 300 ? 46.309  -36.335 -56.170 1.00 108.92 ? 300  LEU   E CD2 1 
ATOM   13619 N  N   . ARG   E 2 301 ? 49.828  -33.562 -57.113 1.00 106.40 ? 301  ARG   E N   1 
ATOM   13620 C  CA  . ARG   E 2 301 ? 50.617  -32.358 -56.908 1.00 108.19 ? 301  ARG   E CA  1 
ATOM   13621 C  C   . ARG   E 2 301 ? 49.818  -31.330 -56.120 1.00 112.60 ? 301  ARG   E C   1 
ATOM   13622 O  O   . ARG   E 2 301 ? 48.584  -31.347 -56.104 1.00 111.78 ? 301  ARG   E O   1 
ATOM   13623 C  CB  . ARG   E 2 301 ? 51.060  -31.749 -58.239 1.00 111.39 ? 301  ARG   E CB  1 
ATOM   13624 C  CG  . ARG   E 2 301 ? 52.250  -30.795 -58.144 1.00 114.70 ? 301  ARG   E CG  1 
ATOM   13625 C  CD  . ARG   E 2 301 ? 53.011  -30.755 -59.470 1.00 115.51 ? 301  ARG   E CD  1 
ATOM   13626 N  NE  . ARG   E 2 301 ? 52.157  -30.374 -60.586 1.00 111.90 ? 301  ARG   E NE  1 
ATOM   13627 C  CZ  . ARG   E 2 301 ? 51.841  -29.121 -60.873 1.00 116.62 ? 301  ARG   E CZ  1 
ATOM   13628 N  NH1 . ARG   E 2 301 ? 52.319  -28.110 -60.159 1.00 116.77 ? 301  ARG   E NH1 1 
ATOM   13629 N  NH2 . ARG   E 2 301 ? 51.018  -28.875 -61.893 1.00 117.76 ? 301  ARG   E NH2 1 
ATOM   13630 N  N   . VAL   E 2 302 ? 50.546  -30.429 -55.455 1.00 118.70 ? 302  VAL   E N   1 
ATOM   13631 C  CA  . VAL   E 2 302 ? 49.961  -29.374 -54.636 1.00 116.55 ? 302  VAL   E CA  1 
ATOM   13632 C  C   . VAL   E 2 302 ? 50.659  -28.055 -54.945 1.00 116.81 ? 302  VAL   E C   1 
ATOM   13633 O  O   . VAL   E 2 302 ? 51.890  -27.974 -54.898 1.00 114.77 ? 302  VAL   E O   1 
ATOM   13634 C  CB  . VAL   E 2 302 ? 50.062  -29.702 -53.137 1.00 109.70 ? 302  VAL   E CB  1 
ATOM   13635 C  CG1 . VAL   E 2 302 ? 49.819  -28.456 -52.324 1.00 113.04 ? 302  VAL   E CG1 1 
ATOM   13636 C  CG2 . VAL   E 2 302 ? 49.075  -30.807 -52.775 1.00 106.84 ? 302  VAL   E CG2 1 
ATOM   13637 N  N   . GLU   E 2 303 ? 49.869  -27.028 -55.257 1.00 125.17 ? 303  GLU   E N   1 
ATOM   13638 C  CA  . GLU   E 2 303 ? 50.371  -25.702 -55.597 1.00 125.76 ? 303  GLU   E CA  1 
ATOM   13639 C  C   . GLU   E 2 303 ? 49.738  -24.666 -54.683 1.00 123.14 ? 303  GLU   E C   1 
ATOM   13640 O  O   . GLU   E 2 303 ? 48.523  -24.693 -54.465 1.00 122.89 ? 303  GLU   E O   1 
ATOM   13641 C  CB  . GLU   E 2 303 ? 50.069  -25.344 -57.056 1.00 129.61 ? 303  GLU   E CB  1 
ATOM   13642 C  CG  . GLU   E 2 303 ? 51.121  -25.806 -58.046 1.00 135.67 ? 303  GLU   E CG  1 
ATOM   13643 C  CD  . GLU   E 2 303 ? 52.410  -25.003 -57.968 1.00 137.96 ? 303  GLU   E CD  1 
ATOM   13644 O  OE1 . GLU   E 2 303 ? 52.345  -23.780 -57.689 1.00 136.69 ? 303  GLU   E OE1 1 
ATOM   13645 O  OE2 . GLU   E 2 303 ? 53.487  -25.610 -58.181 1.00 139.57 ? 303  GLU   E OE2 1 
ATOM   13646 N  N   . LEU   E 2 304 ? 50.559  -23.743 -54.181 1.00 112.51 ? 304  LEU   E N   1 
ATOM   13647 C  CA  . LEU   E 2 304 ? 50.102  -22.659 -53.317 1.00 106.82 ? 304  LEU   E CA  1 
ATOM   13648 C  C   . LEU   E 2 304 ? 49.815  -21.428 -54.168 1.00 104.84 ? 304  LEU   E C   1 
ATOM   13649 O  O   . LEU   E 2 304 ? 50.740  -20.746 -54.616 1.00 102.96 ? 304  LEU   E O   1 
ATOM   13650 C  CB  . LEU   E 2 304 ? 51.142  -22.352 -52.244 1.00 103.89 ? 304  LEU   E CB  1 
ATOM   13651 C  CG  . LEU   E 2 304 ? 50.868  -21.105 -51.397 1.00 100.53 ? 304  LEU   E CG  1 
ATOM   13652 C  CD1 . LEU   E 2 304 ? 49.481  -21.168 -50.767 1.00 103.77 ? 304  LEU   E CD1 1 
ATOM   13653 C  CD2 . LEU   E 2 304 ? 51.936  -20.896 -50.339 1.00 96.33  ? 304  LEU   E CD2 1 
ATOM   13654 N  N   . LEU   E 2 305 ? 48.530  -21.124 -54.360 1.00 104.85 ? 305  LEU   E N   1 
ATOM   13655 C  CA  . LEU   E 2 305 ? 48.136  -20.024 -55.233 1.00 103.79 ? 305  LEU   E CA  1 
ATOM   13656 C  C   . LEU   E 2 305 ? 48.372  -18.672 -54.574 1.00 105.10 ? 305  LEU   E C   1 
ATOM   13657 O  O   . LEU   E 2 305 ? 49.010  -17.795 -55.160 1.00 107.63 ? 305  LEU   E O   1 
ATOM   13658 C  CB  . LEU   E 2 305 ? 46.674  -20.176 -55.628 1.00 100.80 ? 305  LEU   E CB  1 
ATOM   13659 C  CG  . LEU   E 2 305 ? 46.257  -21.541 -56.149 1.00 101.64 ? 305  LEU   E CG  1 
ATOM   13660 C  CD1 . LEU   E 2 305 ? 44.850  -21.500 -56.666 1.00 96.78  ? 305  LEU   E CD1 1 
ATOM   13661 C  CD2 . LEU   E 2 305 ? 47.193  -21.941 -57.243 1.00 112.91 ? 305  LEU   E CD2 1 
ATOM   13662 N  N   . GLY   E 2 306 ? 47.866  -18.491 -53.360 1.00 105.10 ? 306  GLY   E N   1 
ATOM   13663 C  CA  . GLY   E 2 306 ? 48.065  -17.241 -52.651 1.00 105.65 ? 306  GLY   E CA  1 
ATOM   13664 C  C   . GLY   E 2 306 ? 47.508  -17.286 -51.246 1.00 102.51 ? 306  GLY   E C   1 
ATOM   13665 O  O   . GLY   E 2 306 ? 47.430  -18.343 -50.619 1.00 100.67 ? 306  GLY   E O   1 
ATOM   13666 N  N   . GLU   E 2 307 ? 47.140  -16.113 -50.747 1.00 105.43 ? 307  GLU   E N   1 
ATOM   13667 C  CA  . GLU   E 2 307 ? 46.469  -15.985 -49.465 1.00 101.62 ? 307  GLU   E CA  1 
ATOM   13668 C  C   . GLU   E 2 307 ? 45.127  -15.319 -49.698 1.00 100.40 ? 307  GLU   E C   1 
ATOM   13669 O  O   . GLU   E 2 307 ? 45.028  -14.364 -50.470 1.00 101.48 ? 307  GLU   E O   1 
ATOM   13670 C  CB  . GLU   E 2 307 ? 47.303  -15.175 -48.479 1.00 104.24 ? 307  GLU   E CB  1 
ATOM   13671 C  CG  . GLU   E 2 307 ? 47.179  -15.693 -47.065 1.00 109.64 ? 307  GLU   E CG  1 
ATOM   13672 C  CD  . GLU   E 2 307 ? 48.082  -14.972 -46.084 1.00 111.64 ? 307  GLU   E CD  1 
ATOM   13673 O  OE1 . GLU   E 2 307 ? 48.621  -13.905 -46.461 1.00 112.85 ? 307  GLU   E OE1 1 
ATOM   13674 O  OE2 . GLU   E 2 307 ? 48.253  -15.481 -44.944 1.00 109.56 ? 307  GLU   E OE2 1 
ATOM   13675 N  N   . THR   E 2 308 ? 44.088  -15.845 -49.059 1.00 96.71  ? 308  THR   E N   1 
ATOM   13676 C  CA  . THR   E 2 308 ? 42.766  -15.238 -49.140 1.00 96.90  ? 308  THR   E CA  1 
ATOM   13677 C  C   . THR   E 2 308 ? 42.369  -14.989 -47.696 1.00 96.00  ? 308  THR   E C   1 
ATOM   13678 O  O   . THR   E 2 308 ? 43.230  -14.947 -46.815 1.00 101.47 ? 308  THR   E O   1 
ATOM   13679 C  CB  . THR   E 2 308 ? 41.737  -16.185 -49.772 1.00 94.05  ? 308  THR   E CB  1 
ATOM   13680 O  OG1 . THR   E 2 308 ? 41.529  -17.330 -48.932 1.00 90.03  ? 308  THR   E OG1 1 
ATOM   13681 C  CG2 . THR   E 2 308 ? 42.192  -16.636 -51.148 1.00 93.60  ? 308  THR   E CG2 1 
ATOM   13682 N  N   . SER   E 2 309 ? 41.085  -14.813 -47.435 1.00 91.58  ? 309  SER   E N   1 
ATOM   13683 C  CA  . SER   E 2 309 ? 40.614  -14.846 -46.065 1.00 93.21  ? 309  SER   E CA  1 
ATOM   13684 C  C   . SER   E 2 309 ? 40.572  -16.233 -45.449 1.00 94.43  ? 309  SER   E C   1 
ATOM   13685 O  O   . SER   E 2 309 ? 40.461  -17.240 -46.152 1.00 96.39  ? 309  SER   E O   1 
ATOM   13686 C  CB  . SER   E 2 309 ? 39.241  -14.193 -45.948 1.00 91.10  ? 309  SER   E CB  1 
ATOM   13687 O  OG  . SER   E 2 309 ? 39.319  -12.829 -46.269 1.00 91.46  ? 309  SER   E OG  1 
ATOM   13688 N  N   . ILE   E 2 310 ? 40.660  -16.266 -44.122 1.00 97.15  ? 310  ILE   E N   1 
ATOM   13689 C  CA  . ILE   E 2 310 ? 40.580  -17.502 -43.358 1.00 97.72  ? 310  ILE   E CA  1 
ATOM   13690 C  C   . ILE   E 2 310 ? 39.226  -18.059 -43.785 1.00 96.41  ? 310  ILE   E C   1 
ATOM   13691 O  O   . ILE   E 2 310 ? 38.167  -17.506 -43.461 1.00 95.75  ? 310  ILE   E O   1 
ATOM   13692 C  CB  . ILE   E 2 310 ? 40.738  -17.223 -41.857 1.00 96.28  ? 310  ILE   E CB  1 
ATOM   13693 C  CG1 . ILE   E 2 310 ? 41.955  -16.333 -41.652 1.00 95.83  ? 310  ILE   E CG1 1 
ATOM   13694 C  CG2 . ILE   E 2 310 ? 40.933  -18.510 -41.092 1.00 99.11  ? 310  ILE   E CG2 1 
ATOM   13695 C  CD1 . ILE   E 2 310 ? 42.313  -16.115 -40.207 1.00 96.54  ? 310  ILE   E CD1 1 
ATOM   13696 N  N   . ALA   E 2 311 ? 39.271  -19.154 -44.532 1.00 91.76  ? 311  ALA   E N   1 
ATOM   13697 C  CA  . ALA   E 2 311 ? 38.130  -19.560 -45.326 1.00 88.65  ? 311  ALA   E CA  1 
ATOM   13698 C  C   . ALA   E 2 311 ? 37.411  -20.629 -44.538 1.00 90.42  ? 311  ALA   E C   1 
ATOM   13699 O  O   . ALA   E 2 311 ? 38.028  -21.577 -44.041 1.00 91.89  ? 311  ALA   E O   1 
ATOM   13700 C  CB  . ALA   E 2 311 ? 38.505  -20.091 -46.702 1.00 91.22  ? 311  ALA   E CB  1 
ATOM   13701 N  N   . GLU   E 2 312 ? 36.105  -20.446 -44.399 1.00 91.64  ? 312  GLU   E N   1 
ATOM   13702 C  CA  . GLU   E 2 312 ? 35.237  -21.457 -43.832 1.00 91.13  ? 312  GLU   E CA  1 
ATOM   13703 C  C   . GLU   E 2 312 ? 34.777  -22.407 -44.916 1.00 90.67  ? 312  GLU   E C   1 
ATOM   13704 O  O   . GLU   E 2 312 ? 35.021  -23.611 -44.834 1.00 95.44  ? 312  GLU   E O   1 
ATOM   13705 C  CB  . GLU   E 2 312 ? 34.042  -20.795 -43.136 1.00 90.72  ? 312  GLU   E CB  1 
ATOM   13706 C  CG  . GLU   E 2 312 ? 33.132  -21.739 -42.406 1.00 91.08  ? 312  GLU   E CG  1 
ATOM   13707 C  CD  . GLU   E 2 312 ? 33.832  -22.554 -41.340 1.00 100.68 ? 312  GLU   E CD  1 
ATOM   13708 O  OE1 . GLU   E 2 312 ? 35.031  -22.323 -41.057 1.00 102.20 ? 312  GLU   E OE1 1 
ATOM   13709 O  OE2 . GLU   E 2 312 ? 33.166  -23.437 -40.764 1.00 108.66 ? 312  GLU   E OE2 1 
ATOM   13710 N  N   . CYS   E 2 313 ? 34.137  -21.873 -45.943 1.00 90.25  ? 313  CYS   E N   1 
ATOM   13711 C  CA  . CYS   E 2 313 ? 33.704  -22.653 -47.088 1.00 92.90  ? 313  CYS   E CA  1 
ATOM   13712 C  C   . CYS   E 2 313 ? 34.358  -22.071 -48.336 1.00 95.18  ? 313  CYS   E C   1 
ATOM   13713 O  O   . CYS   E 2 313 ? 34.554  -20.853 -48.424 1.00 94.70  ? 313  CYS   E O   1 
ATOM   13714 C  CB  . CYS   E 2 313 ? 32.167  -22.638 -47.207 1.00 96.19  ? 313  CYS   E CB  1 
ATOM   13715 S  SG  . CYS   E 2 313 ? 31.474  -21.070 -47.852 1.00 105.64 ? 313  CYS   E SG  1 
ATOM   13716 N  N   . LEU   E 2 314 ? 34.709  -22.932 -49.294 1.00 93.22  ? 314  LEU   E N   1 
ATOM   13717 C  CA  . LEU   E 2 314 ? 35.272  -22.492 -50.563 1.00 89.52  ? 314  LEU   E CA  1 
ATOM   13718 C  C   . LEU   E 2 314 ? 34.440  -23.019 -51.716 1.00 93.18  ? 314  LEU   E C   1 
ATOM   13719 O  O   . LEU   E 2 314 ? 33.910  -24.128 -51.658 1.00 96.98  ? 314  LEU   E O   1 
ATOM   13720 C  CB  . LEU   E 2 314 ? 36.704  -22.970 -50.764 1.00 88.06  ? 314  LEU   E CB  1 
ATOM   13721 C  CG  . LEU   E 2 314 ? 37.790  -22.069 -50.204 1.00 87.98  ? 314  LEU   E CG  1 
ATOM   13722 C  CD1 . LEU   E 2 314 ? 39.155  -22.606 -50.599 1.00 86.90  ? 314  LEU   E CD1 1 
ATOM   13723 C  CD2 . LEU   E 2 314 ? 37.572  -20.630 -50.662 1.00 87.28  ? 314  LEU   E CD2 1 
ATOM   13724 N  N   . THR   E 2 315 ? 34.354  -22.236 -52.783 1.00 95.33  ? 315  THR   E N   1 
ATOM   13725 C  CA  . THR   E 2 315 ? 33.625  -22.690 -53.957 1.00 96.49  ? 315  THR   E CA  1 
ATOM   13726 C  C   . THR   E 2 315 ? 34.182  -21.962 -55.174 1.00 96.62  ? 315  THR   E C   1 
ATOM   13727 O  O   . THR   E 2 315 ? 34.296  -20.732 -55.165 1.00 97.52  ? 315  THR   E O   1 
ATOM   13728 C  CB  . THR   E 2 315 ? 32.100  -22.485 -53.766 1.00 94.99  ? 315  THR   E CB  1 
ATOM   13729 O  OG1 . THR   E 2 315 ? 31.390  -22.795 -54.971 1.00 97.73  ? 315  THR   E OG1 1 
ATOM   13730 C  CG2 . THR   E 2 315 ? 31.736  -21.086 -53.299 1.00 93.59  ? 315  THR   E CG2 1 
ATOM   13731 N  N   . TYR   E 2 316 ? 34.606  -22.723 -56.183 1.00 95.16  ? 316  TYR   E N   1 
ATOM   13732 C  CA  . TYR   E 2 316 ? 35.078  -22.116 -57.414 1.00 95.42  ? 316  TYR   E CA  1 
ATOM   13733 C  C   . TYR   E 2 316 ? 33.877  -21.836 -58.286 1.00 97.69  ? 316  TYR   E C   1 
ATOM   13734 O  O   . TYR   E 2 316 ? 32.991  -22.687 -58.418 1.00 99.44  ? 316  TYR   E O   1 
ATOM   13735 C  CB  . TYR   E 2 316 ? 36.064  -23.024 -58.143 1.00 101.74 ? 316  TYR   E CB  1 
ATOM   13736 C  CG  . TYR   E 2 316 ? 36.378  -22.603 -59.576 1.00 105.72 ? 316  TYR   E CG  1 
ATOM   13737 C  CD1 . TYR   E 2 316 ? 37.062  -21.425 -59.847 1.00 105.81 ? 316  TYR   E CD1 1 
ATOM   13738 C  CD2 . TYR   E 2 316 ? 36.016  -23.405 -60.658 1.00 107.58 ? 316  TYR   E CD2 1 
ATOM   13739 C  CE1 . TYR   E 2 316 ? 37.361  -21.051 -61.159 1.00 110.49 ? 316  TYR   E CE1 1 
ATOM   13740 C  CE2 . TYR   E 2 316 ? 36.311  -23.035 -61.964 1.00 107.33 ? 316  TYR   E CE2 1 
ATOM   13741 C  CZ  . TYR   E 2 316 ? 36.981  -21.862 -62.206 1.00 111.07 ? 316  TYR   E CZ  1 
ATOM   13742 O  OH  . TYR   E 2 316 ? 37.272  -21.497 -63.497 1.00 117.84 ? 316  TYR   E OH  1 
ATOM   13743 N  N   . LEU   E 2 317 ? 33.838  -20.637 -58.860 1.00 98.23  ? 317  LEU   E N   1 
ATOM   13744 C  CA  . LEU   E 2 317 ? 32.720  -20.250 -59.709 1.00 100.34 ? 317  LEU   E CA  1 
ATOM   13745 C  C   . LEU   E 2 317 ? 32.919  -20.525 -61.200 1.00 109.44 ? 317  LEU   E C   1 
ATOM   13746 O  O   . LEU   E 2 317 ? 32.306  -21.450 -61.751 1.00 109.93 ? 317  LEU   E O   1 
ATOM   13747 C  CB  . LEU   E 2 317 ? 32.410  -18.766 -59.523 1.00 97.81  ? 317  LEU   E CB  1 
ATOM   13748 C  CG  . LEU   E 2 317 ? 32.080  -18.338 -58.088 1.00 96.71  ? 317  LEU   E CG  1 
ATOM   13749 C  CD1 . LEU   E 2 317 ? 31.692  -16.865 -58.011 1.00 94.15  ? 317  LEU   E CD1 1 
ATOM   13750 C  CD2 . LEU   E 2 317 ? 30.984  -19.207 -57.492 1.00 94.62  ? 317  LEU   E CD2 1 
ATOM   13751 N  N   . ASP   E 2 318 ? 33.770  -19.739 -61.860 1.00 119.22 ? 318  ASP   E N   1 
ATOM   13752 C  CA  . ASP   E 2 318 ? 34.065  -19.920 -63.280 1.00 118.37 ? 318  ASP   E CA  1 
ATOM   13753 C  C   . ASP   E 2 318 ? 34.988  -18.799 -63.727 1.00 118.72 ? 318  ASP   E C   1 
ATOM   13754 O  O   . ASP   E 2 318 ? 35.091  -17.757 -63.079 1.00 118.73 ? 318  ASP   E O   1 
ATOM   13755 C  CB  . ASP   E 2 318 ? 32.841  -19.971 -64.186 1.00 119.27 ? 318  ASP   E CB  1 
ATOM   13756 C  CG  . ASP   E 2 318 ? 33.066  -20.840 -65.374 1.00 125.96 ? 318  ASP   E CG  1 
ATOM   13757 O  OD1 . ASP   E 2 318 ? 34.028  -21.638 -65.310 1.00 127.37 ? 318  ASP   E OD1 1 
ATOM   13758 O  OD2 . ASP   E 2 318 ? 32.312  -20.726 -66.365 1.00 134.07 ? 318  ASP   E OD2 1 
ATOM   13759 N  N   . ASN   E 2 319 ? 35.660  -19.026 -64.856 1.00 116.36 ? 319  ASN   E N   1 
ATOM   13760 C  CA  . ASN   E 2 319 ? 36.521  -18.005 -65.453 1.00 118.11 ? 319  ASN   E CA  1 
ATOM   13761 C  C   . ASN   E 2 319 ? 37.576  -17.518 -64.466 1.00 115.82 ? 319  ASN   E C   1 
ATOM   13762 O  O   . ASN   E 2 319 ? 38.041  -16.378 -64.534 1.00 112.53 ? 319  ASN   E O   1 
ATOM   13763 C  CB  . ASN   E 2 319 ? 35.680  -16.840 -65.967 1.00 121.20 ? 319  ASN   E CB  1 
ATOM   13764 C  CG  . ASN   E 2 319 ? 34.527  -17.310 -66.810 1.00 122.47 ? 319  ASN   E CG  1 
ATOM   13765 O  OD1 . ASN   E 2 319 ? 34.629  -18.329 -67.491 1.00 123.49 ? 319  ASN   E OD1 1 
ATOM   13766 N  ND2 . ASN   E 2 319 ? 33.415  -16.584 -66.762 1.00 123.00 ? 319  ASN   E ND2 1 
ATOM   13767 N  N   . GLY   E 2 320 ? 37.921  -18.377 -63.514 1.00 116.29 ? 320  GLY   E N   1 
ATOM   13768 C  CA  . GLY   E 2 320 ? 38.983  -18.121 -62.575 1.00 114.62 ? 320  GLY   E CA  1 
ATOM   13769 C  C   . GLY   E 2 320 ? 38.542  -17.645 -61.210 1.00 107.69 ? 320  GLY   E C   1 
ATOM   13770 O  O   . GLY   E 2 320 ? 39.380  -17.603 -60.301 1.00 109.02 ? 320  GLY   E O   1 
ATOM   13771 N  N   . VAL   E 2 321 ? 37.269  -17.298 -61.021 1.00 107.25 ? 321  VAL   E N   1 
ATOM   13772 C  CA  . VAL   E 2 321 ? 36.848  -16.591 -59.813 1.00 103.12 ? 321  VAL   E CA  1 
ATOM   13773 C  C   . VAL   E 2 321 ? 36.350  -17.574 -58.755 1.00 100.92 ? 321  VAL   E C   1 
ATOM   13774 O  O   . VAL   E 2 321 ? 35.375  -18.306 -58.969 1.00 99.39  ? 321  VAL   E O   1 
ATOM   13775 C  CB  . VAL   E 2 321 ? 35.788  -15.531 -60.127 1.00 101.08 ? 321  VAL   E CB  1 
ATOM   13776 C  CG1 . VAL   E 2 321 ? 35.706  -14.555 -58.990 1.00 100.43 ? 321  VAL   E CG1 1 
ATOM   13777 C  CG2 . VAL   E 2 321 ? 36.163  -14.807 -61.380 1.00 111.80 ? 321  VAL   E CG2 1 
ATOM   13778 N  N   . VAL   E 2 322 ? 37.020  -17.566 -57.602 1.00 97.56  ? 322  VAL   E N   1 
ATOM   13779 C  CA  . VAL   E 2 322 ? 36.722  -18.428 -56.465 1.00 93.70  ? 322  VAL   E CA  1 
ATOM   13780 C  C   . VAL   E 2 322 ? 35.975  -17.612 -55.424 1.00 90.49  ? 322  VAL   E C   1 
ATOM   13781 O  O   . VAL   E 2 322 ? 36.399  -16.496 -55.102 1.00 94.17  ? 322  VAL   E O   1 
ATOM   13782 C  CB  . VAL   E 2 322 ? 38.016  -18.982 -55.846 1.00 92.14  ? 322  VAL   E CB  1 
ATOM   13783 C  CG1 . VAL   E 2 322 ? 37.690  -20.083 -54.885 1.00 91.56  ? 322  VAL   E CG1 1 
ATOM   13784 C  CG2 . VAL   E 2 322 ? 38.965  -19.449 -56.915 1.00 94.97  ? 322  VAL   E CG2 1 
ATOM   13785 N  N   . PHE   E 2 323 ? 34.898  -18.162 -54.870 1.00 87.07  ? 323  PHE   E N   1 
ATOM   13786 C  CA  . PHE   E 2 323 ? 34.239  -17.503 -53.747 1.00 87.49  ? 323  PHE   E CA  1 
ATOM   13787 C  C   . PHE   E 2 323 ? 34.836  -18.028 -52.450 1.00 88.14  ? 323  PHE   E C   1 
ATOM   13788 O  O   . PHE   E 2 323 ? 34.921  -19.241 -52.247 1.00 90.76  ? 323  PHE   E O   1 
ATOM   13789 C  CB  . PHE   E 2 323 ? 32.722  -17.699 -53.742 1.00 85.41  ? 323  PHE   E CB  1 
ATOM   13790 C  CG  . PHE   E 2 323 ? 32.061  -17.158 -52.488 1.00 88.87  ? 323  PHE   E CG  1 
ATOM   13791 C  CD1 . PHE   E 2 323 ? 32.226  -15.830 -52.112 1.00 88.33  ? 323  PHE   E CD1 1 
ATOM   13792 C  CD2 . PHE   E 2 323 ? 31.301  -17.974 -51.669 1.00 88.96  ? 323  PHE   E CD2 1 
ATOM   13793 C  CE1 . PHE   E 2 323 ? 31.635  -15.336 -50.954 1.00 81.87  ? 323  PHE   E CE1 1 
ATOM   13794 C  CE2 . PHE   E 2 323 ? 30.711  -17.468 -50.508 1.00 86.80  ? 323  PHE   E CE2 1 
ATOM   13795 C  CZ  . PHE   E 2 323 ? 30.882  -16.154 -50.160 1.00 79.95  ? 323  PHE   E CZ  1 
ATOM   13796 N  N   . VAL   E 2 324 ? 35.258  -17.114 -51.585 1.00 86.78  ? 324  VAL   E N   1 
ATOM   13797 C  CA  . VAL   E 2 324 ? 35.809  -17.450 -50.281 1.00 84.88  ? 324  VAL   E CA  1 
ATOM   13798 C  C   . VAL   E 2 324 ? 34.745  -17.100 -49.249 1.00 84.44  ? 324  VAL   E C   1 
ATOM   13799 O  O   . VAL   E 2 324 ? 34.413  -15.928 -49.057 1.00 87.65  ? 324  VAL   E O   1 
ATOM   13800 C  CB  . VAL   E 2 324 ? 37.132  -16.714 -50.023 1.00 80.40  ? 324  VAL   E CB  1 
ATOM   13801 C  CG1 . VAL   E 2 324 ? 37.853  -17.280 -48.825 1.00 80.97  ? 324  VAL   E CG1 1 
ATOM   13802 C  CG2 . VAL   E 2 324 ? 38.015  -16.800 -51.237 1.00 84.20  ? 324  VAL   E CG2 1 
ATOM   13803 N  N   . GLY   E 2 325 ? 34.174  -18.120 -48.613 1.00 84.57  ? 325  GLY   E N   1 
ATOM   13804 C  CA  . GLY   E 2 325 ? 33.260  -17.911 -47.506 1.00 84.60  ? 325  GLY   E CA  1 
ATOM   13805 C  C   . GLY   E 2 325 ? 34.043  -17.889 -46.215 1.00 86.26  ? 325  GLY   E C   1 
ATOM   13806 O  O   . GLY   E 2 325 ? 34.760  -18.849 -45.915 1.00 88.44  ? 325  GLY   E O   1 
ATOM   13807 N  N   . SER   E 2 326 ? 33.943  -16.797 -45.454 1.00 85.02  ? 326  SER   E N   1 
ATOM   13808 C  CA  . SER   E 2 326 ? 34.799  -16.583 -44.292 1.00 85.77  ? 326  SER   E CA  1 
ATOM   13809 C  C   . SER   E 2 326 ? 33.953  -16.262 -43.074 1.00 87.43  ? 326  SER   E C   1 
ATOM   13810 O  O   . SER   E 2 326 ? 33.035  -15.428 -43.154 1.00 81.74  ? 326  SER   E O   1 
ATOM   13811 C  CB  . SER   E 2 326 ? 35.808  -15.452 -44.534 1.00 86.75  ? 326  SER   E CB  1 
ATOM   13812 O  OG  . SER   E 2 326 ? 36.799  -15.404 -43.516 1.00 86.79  ? 326  SER   E OG  1 
ATOM   13813 N  N   . ARG   E 2 327 ? 34.288  -16.925 -41.951 1.00 88.12  ? 327  ARG   E N   1 
ATOM   13814 C  CA  . ARG   E 2 327 ? 33.689  -16.707 -40.641 1.00 86.06  ? 327  ARG   E CA  1 
ATOM   13815 C  C   . ARG   E 2 327 ? 34.490  -15.760 -39.758 1.00 83.72  ? 327  ARG   E C   1 
ATOM   13816 O  O   . ARG   E 2 327 ? 33.925  -15.188 -38.815 1.00 81.22  ? 327  ARG   E O   1 
ATOM   13817 C  CB  . ARG   E 2 327 ? 33.526  -18.038 -39.901 1.00 87.87  ? 327  ARG   E CB  1 
ATOM   13818 C  CG  . ARG   E 2 327 ? 32.242  -18.778 -40.226 1.00 92.79  ? 327  ARG   E CG  1 
ATOM   13819 C  CD  . ARG   E 2 327 ? 31.064  -18.306 -39.368 1.00 95.40  ? 327  ARG   E CD  1 
ATOM   13820 N  NE  . ARG   E 2 327 ? 31.292  -18.529 -37.944 1.00 98.87  ? 327  ARG   E NE  1 
ATOM   13821 C  CZ  . ARG   E 2 327 ? 31.268  -19.726 -37.372 1.00 104.72 ? 327  ARG   E CZ  1 
ATOM   13822 N  NH1 . ARG   E 2 327 ? 31.007  -20.825 -38.069 1.00 104.78 ? 327  ARG   E NH1 1 
ATOM   13823 N  NH2 . ARG   E 2 327 ? 31.523  -19.829 -36.072 1.00 103.37 ? 327  ARG   E NH2 1 
ATOM   13824 N  N   . LEU   E 2 328 ? 35.781  -15.587 -40.039 1.00 84.35  ? 328  LEU   E N   1 
ATOM   13825 C  CA  . LEU   E 2 328 ? 36.656  -14.706 -39.273 1.00 83.88  ? 328  LEU   E CA  1 
ATOM   13826 C  C   . LEU   E 2 328 ? 36.862  -13.337 -39.915 1.00 85.08  ? 328  LEU   E C   1 
ATOM   13827 O  O   . LEU   E 2 328 ? 36.856  -12.322 -39.217 1.00 86.63  ? 328  LEU   E O   1 
ATOM   13828 C  CB  . LEU   E 2 328 ? 38.014  -15.374 -39.069 1.00 82.81  ? 328  LEU   E CB  1 
ATOM   13829 C  CG  . LEU   E 2 328 ? 37.924  -16.658 -38.269 1.00 75.83  ? 328  LEU   E CG  1 
ATOM   13830 C  CD1 . LEU   E 2 328 ? 39.303  -17.103 -37.851 1.00 77.89  ? 328  LEU   E CD1 1 
ATOM   13831 C  CD2 . LEU   E 2 328 ? 37.038  -16.404 -37.084 1.00 75.06  ? 328  LEU   E CD2 1 
ATOM   13832 N  N   . GLY   E 2 329 ? 37.047  -13.275 -41.229 1.00 86.00  ? 329  GLY   E N   1 
ATOM   13833 C  CA  . GLY   E 2 329 ? 37.170  -11.986 -41.883 1.00 86.97  ? 329  GLY   E CA  1 
ATOM   13834 C  C   . GLY   E 2 329 ? 36.100  -11.743 -42.924 1.00 86.68  ? 329  GLY   E C   1 
ATOM   13835 O  O   . GLY   E 2 329 ? 35.050  -12.384 -42.912 1.00 85.15  ? 329  GLY   E O   1 
ATOM   13836 N  N   . ASP   E 2 330 ? 36.349  -10.819 -43.834 1.00 94.58  ? 330  ASP   E N   1 
ATOM   13837 C  CA  . ASP   E 2 330 ? 35.402  -10.614 -44.910 1.00 94.24  ? 330  ASP   E CA  1 
ATOM   13838 C  C   . ASP   E 2 330 ? 35.387  -11.829 -45.823 1.00 95.06  ? 330  ASP   E C   1 
ATOM   13839 O  O   . ASP   E 2 330 ? 36.427  -12.434 -46.097 1.00 96.11  ? 330  ASP   E O   1 
ATOM   13840 C  CB  . ASP   E 2 330 ? 35.758  -9.366  -45.701 1.00 97.51  ? 330  ASP   E CB  1 
ATOM   13841 C  CG  . ASP   E 2 330 ? 35.509  -8.097  -44.920 1.00 99.16  ? 330  ASP   E CG  1 
ATOM   13842 O  OD1 . ASP   E 2 330 ? 34.782  -8.167  -43.898 1.00 99.96  ? 330  ASP   E OD1 1 
ATOM   13843 O  OD2 . ASP   E 2 330 ? 36.050  -7.036  -45.319 1.00 100.97 ? 330  ASP   E OD2 1 
ATOM   13844 N  N   . SER   E 2 331 ? 34.192  -12.218 -46.251 1.00 92.13  ? 331  SER   E N   1 
ATOM   13845 C  CA  . SER   E 2 331 ? 34.076  -13.095 -47.393 1.00 77.68  ? 331  SER   E CA  1 
ATOM   13846 C  C   . SER   E 2 331 ? 34.515  -12.333 -48.623 1.00 82.51  ? 331  SER   E C   1 
ATOM   13847 O  O   . SER   E 2 331 ? 34.495  -11.104 -48.656 1.00 90.28  ? 331  SER   E O   1 
ATOM   13848 C  CB  . SER   E 2 331 ? 32.639  -13.562 -47.548 1.00 78.58  ? 331  SER   E CB  1 
ATOM   13849 O  OG  . SER   E 2 331 ? 32.048  -13.803 -46.276 1.00 86.11  ? 331  SER   E OG  1 
ATOM   13850 N  N   . GLN   E 2 332 ? 34.896  -13.062 -49.659 1.00 85.03  ? 332  GLN   E N   1 
ATOM   13851 C  CA  . GLN   E 2 332 ? 35.475  -12.353 -50.786 1.00 87.43  ? 332  GLN   E CA  1 
ATOM   13852 C  C   . GLN   E 2 332 ? 35.493  -13.220 -52.044 1.00 90.78  ? 332  GLN   E C   1 
ATOM   13853 O  O   . GLN   E 2 332 ? 35.548  -14.449 -51.962 1.00 89.99  ? 332  GLN   E O   1 
ATOM   13854 C  CB  . GLN   E 2 332 ? 36.884  -11.899 -50.428 1.00 84.22  ? 332  GLN   E CB  1 
ATOM   13855 C  CG  . GLN   E 2 332 ? 37.705  -12.999 -49.892 1.00 84.23  ? 332  GLN   E CG  1 
ATOM   13856 C  CD  . GLN   E 2 332 ? 39.157  -12.698 -50.019 1.00 88.84  ? 332  GLN   E CD  1 
ATOM   13857 O  OE1 . GLN   E 2 332 ? 40.015  -13.487 -49.611 1.00 93.00  ? 332  GLN   E OE1 1 
ATOM   13858 N  NE2 . GLN   E 2 332 ? 39.458  -11.541 -50.594 1.00 92.37  ? 332  GLN   E NE2 1 
ATOM   13859 N  N   . LEU   E 2 333 ? 35.432  -12.544 -53.201 1.00 97.04  ? 333  LEU   E N   1 
ATOM   13860 C  CA  . LEU   E 2 333 ? 35.703  -13.128 -54.510 1.00 92.11  ? 333  LEU   E CA  1 
ATOM   13861 C  C   . LEU   E 2 333 ? 37.170  -12.938 -54.845 1.00 93.99  ? 333  LEU   E C   1 
ATOM   13862 O  O   . LEU   E 2 333 ? 37.729  -11.865 -54.625 1.00 101.19 ? 333  LEU   E O   1 
ATOM   13863 C  CB  . LEU   E 2 333 ? 34.857  -12.459 -55.596 1.00 95.59  ? 333  LEU   E CB  1 
ATOM   13864 C  CG  . LEU   E 2 333 ? 33.403  -12.904 -55.700 1.00 91.16  ? 333  LEU   E CG  1 
ATOM   13865 C  CD1 . LEU   E 2 333 ? 32.695  -12.175 -56.808 1.00 85.92  ? 333  LEU   E CD1 1 
ATOM   13866 C  CD2 . LEU   E 2 333 ? 33.327  -14.401 -55.911 1.00 90.97  ? 333  LEU   E CD2 1 
ATOM   13867 N  N   . VAL   E 2 334 ? 37.795  -13.976 -55.384 1.00 92.75  ? 334  VAL   E N   1 
ATOM   13868 C  CA  . VAL   E 2 334 ? 39.169  -13.875 -55.851 1.00 98.37  ? 334  VAL   E CA  1 
ATOM   13869 C  C   . VAL   E 2 334 ? 39.252  -14.414 -57.276 1.00 100.80 ? 334  VAL   E C   1 
ATOM   13870 O  O   . VAL   E 2 334 ? 38.666  -15.454 -57.592 1.00 101.34 ? 334  VAL   E O   1 
ATOM   13871 C  CB  . VAL   E 2 334 ? 40.170  -14.607 -54.922 1.00 93.91  ? 334  VAL   E CB  1 
ATOM   13872 C  CG1 . VAL   E 2 334 ? 40.375  -13.838 -53.652 1.00 94.50  ? 334  VAL   E CG1 1 
ATOM   13873 C  CG2 . VAL   E 2 334 ? 39.710  -16.018 -54.591 1.00 95.66  ? 334  VAL   E CG2 1 
ATOM   13874 N  N   . LYS   E 2 335 ? 39.944  -13.687 -58.136 1.00 102.45 ? 335  LYS   E N   1 
ATOM   13875 C  CA  . LYS   E 2 335 ? 40.319  -14.181 -59.449 1.00 105.67 ? 335  LYS   E CA  1 
ATOM   13876 C  C   . LYS   E 2 335 ? 41.646  -14.920 -59.336 1.00 108.80 ? 335  LYS   E C   1 
ATOM   13877 O  O   . LYS   E 2 335 ? 42.571  -14.441 -58.675 1.00 111.21 ? 335  LYS   E O   1 
ATOM   13878 C  CB  . LYS   E 2 335 ? 40.444  -13.015 -60.428 1.00 111.37 ? 335  LYS   E CB  1 
ATOM   13879 C  CG  . LYS   E 2 335 ? 41.025  -13.374 -61.780 1.00 112.03 ? 335  LYS   E CG  1 
ATOM   13880 C  CD  . LYS   E 2 335 ? 39.993  -14.078 -62.623 1.00 113.21 ? 335  LYS   E CD  1 
ATOM   13881 C  CE  . LYS   E 2 335 ? 40.595  -14.556 -63.904 1.00 117.34 ? 335  LYS   E CE  1 
ATOM   13882 N  NZ  . LYS   E 2 335 ? 41.799  -15.361 -63.607 1.00 125.75 ? 335  LYS   E NZ  1 
ATOM   13883 N  N   . LEU   E 2 336 ? 41.738  -16.086 -59.966 1.00 111.98 ? 336  LEU   E N   1 
ATOM   13884 C  CA  . LEU   E 2 336 ? 42.983  -16.853 -60.008 1.00 115.39 ? 336  LEU   E CA  1 
ATOM   13885 C  C   . LEU   E 2 336 ? 43.641  -16.615 -61.367 1.00 126.23 ? 336  LEU   E C   1 
ATOM   13886 O  O   . LEU   E 2 336 ? 43.204  -17.157 -62.386 1.00 130.95 ? 336  LEU   E O   1 
ATOM   13887 C  CB  . LEU   E 2 336 ? 42.730  -18.340 -59.770 1.00 113.51 ? 336  LEU   E CB  1 
ATOM   13888 C  CG  . LEU   E 2 336 ? 41.951  -18.762 -58.532 1.00 104.38 ? 336  LEU   E CG  1 
ATOM   13889 C  CD1 . LEU   E 2 336 ? 42.124  -20.236 -58.239 1.00 96.81  ? 336  LEU   E CD1 1 
ATOM   13890 C  CD2 . LEU   E 2 336 ? 42.380  -17.941 -57.359 1.00 106.11 ? 336  LEU   E CD2 1 
ATOM   13891 N  N   . ASN   E 2 337 ? 44.694  -15.807 -61.387 1.00 135.32 ? 337  ASN   E N   1 
ATOM   13892 C  CA  . ASN   E 2 337 ? 45.467  -15.625 -62.609 1.00 137.96 ? 337  ASN   E CA  1 
ATOM   13893 C  C   . ASN   E 2 337 ? 46.463  -16.769 -62.781 1.00 142.92 ? 337  ASN   E C   1 
ATOM   13894 O  O   . ASN   E 2 337 ? 46.889  -17.399 -61.808 1.00 144.50 ? 337  ASN   E O   1 
ATOM   13895 C  CB  . ASN   E 2 337 ? 46.201  -14.288 -62.583 1.00 139.62 ? 337  ASN   E CB  1 
ATOM   13896 C  CG  . ASN   E 2 337 ? 45.254  -13.114 -62.550 1.00 140.27 ? 337  ASN   E CG  1 
ATOM   13897 O  OD1 . ASN   E 2 337 ? 44.217  -13.115 -63.224 1.00 141.72 ? 337  ASN   E OD1 1 
ATOM   13898 N  ND2 . ASN   E 2 337 ? 45.594  -12.106 -61.759 1.00 137.72 ? 337  ASN   E ND2 1 
ATOM   13899 N  N   . VAL   E 2 338 ? 46.827  -17.051 -64.037 1.00 150.90 ? 338  VAL   E N   1 
ATOM   13900 C  CA  . VAL   E 2 338 ? 47.806  -18.105 -64.316 1.00 151.23 ? 338  VAL   E CA  1 
ATOM   13901 C  C   . VAL   E 2 338 ? 49.202  -17.502 -64.292 1.00 154.07 ? 338  VAL   E C   1 
ATOM   13902 O  O   . VAL   E 2 338 ? 50.175  -18.151 -64.693 1.00 154.84 ? 338  VAL   E O   1 
ATOM   13903 C  CB  . VAL   E 2 338 ? 47.559  -18.817 -65.662 1.00 147.47 ? 338  VAL   E CB  1 
ATOM   13904 C  CG1 . VAL   E 2 338 ? 46.214  -19.476 -65.679 1.00 150.03 ? 338  VAL   E CG1 1 
ATOM   13905 C  CG2 . VAL   E 2 338 ? 47.688  -17.849 -66.817 1.00 145.27 ? 338  VAL   E CG2 1 
ATOM   13906 N  N   . ASP   E 2 339 ? 49.311  -16.257 -63.834 1.00 157.76 ? 339  ASP   E N   1 
ATOM   13907 C  CA  . ASP   E 2 339 ? 50.584  -15.555 -63.786 1.00 160.12 ? 339  ASP   E CA  1 
ATOM   13908 C  C   . ASP   E 2 339 ? 50.800  -14.968 -62.401 1.00 161.08 ? 339  ASP   E C   1 
ATOM   13909 O  O   . ASP   E 2 339 ? 49.938  -14.251 -61.882 1.00 158.42 ? 339  ASP   E O   1 
ATOM   13910 C  CB  . ASP   E 2 339 ? 50.642  -14.457 -64.844 1.00 164.10 ? 339  ASP   E CB  1 
ATOM   13911 C  CG  . ASP   E 2 339 ? 50.942  -15.004 -66.228 1.00 168.99 ? 339  ASP   E CG  1 
ATOM   13912 O  OD1 . ASP   E 2 339 ? 50.038  -15.621 -66.836 1.00 168.77 ? 339  ASP   E OD1 1 
ATOM   13913 O  OD2 . ASP   E 2 339 ? 52.089  -14.832 -66.699 1.00 172.15 ? 339  ASP   E OD2 1 
ATOM   13914 N  N   . SER   E 2 340 ? 51.953  -15.286 -61.807 1.00 157.25 ? 340  SER   E N   1 
ATOM   13915 C  CA  . SER   E 2 340 ? 52.323  -14.734 -60.511 1.00 154.79 ? 340  SER   E CA  1 
ATOM   13916 C  C   . SER   E 2 340 ? 52.395  -13.218 -60.581 1.00 157.27 ? 340  SER   E C   1 
ATOM   13917 O  O   . SER   E 2 340 ? 52.892  -12.644 -61.555 1.00 159.00 ? 340  SER   E O   1 
ATOM   13918 C  CB  . SER   E 2 340 ? 53.670  -15.302 -60.057 1.00 156.00 ? 340  SER   E CB  1 
ATOM   13919 O  OG  . SER   E 2 340 ? 54.661  -15.143 -61.064 1.00 156.20 ? 340  SER   E OG  1 
ATOM   13920 N  N   . ASN   E 2 341 ? 51.904  -12.564 -59.537 1.00 157.58 ? 341  ASN   E N   1 
ATOM   13921 C  CA  . ASN   E 2 341 ? 51.928  -11.110 -59.498 1.00 160.41 ? 341  ASN   E CA  1 
ATOM   13922 C  C   . ASN   E 2 341 ? 53.200  -10.643 -58.780 1.00 166.06 ? 341  ASN   E C   1 
ATOM   13923 O  O   . ASN   E 2 341 ? 54.181  -11.387 -58.687 1.00 164.55 ? 341  ASN   E O   1 
ATOM   13924 C  CB  . ASN   E 2 341 ? 50.622  -10.582 -58.871 1.00 154.21 ? 341  ASN   E CB  1 
ATOM   13925 C  CG  . ASN   E 2 341 ? 50.444  -10.988 -57.414 1.00 153.56 ? 341  ASN   E CG  1 
ATOM   13926 O  OD1 . ASN   E 2 341 ? 51.405  -11.265 -56.704 1.00 161.03 ? 341  ASN   E OD1 1 
ATOM   13927 N  ND2 . ASN   E 2 341 ? 49.195  -10.999 -56.957 1.00 142.87 ? 341  ASN   E ND2 1 
ATOM   13928 N  N   . GLU   E 2 342 ? 53.196  -9.398  -58.291 1.00 177.69 ? 342  GLU   E N   1 
ATOM   13929 C  CA  . GLU   E 2 342 ? 54.347  -8.875  -57.557 1.00 180.50 ? 342  GLU   E CA  1 
ATOM   13930 C  C   . GLU   E 2 342 ? 54.632  -9.717  -56.316 1.00 184.05 ? 342  GLU   E C   1 
ATOM   13931 O  O   . GLU   E 2 342 ? 55.774  -10.127 -56.073 1.00 186.36 ? 342  GLU   E O   1 
ATOM   13932 C  CB  . GLU   E 2 342 ? 54.107  -7.410  -57.178 1.00 176.63 ? 342  GLU   E CB  1 
ATOM   13933 N  N   . GLN   E 2 343 ? 53.594  -9.995  -55.520 1.00 169.44 ? 343  GLN   E N   1 
ATOM   13934 C  CA  . GLN   E 2 343 ? 53.696  -10.844 -54.341 1.00 164.73 ? 343  GLN   E CA  1 
ATOM   13935 C  C   . GLN   E 2 343 ? 53.747  -12.339 -54.678 1.00 161.90 ? 343  GLN   E C   1 
ATOM   13936 O  O   . GLN   E 2 343 ? 53.589  -13.157 -53.764 1.00 161.40 ? 343  GLN   E O   1 
ATOM   13937 C  CB  . GLN   E 2 343 ? 52.518  -10.565 -53.399 1.00 157.33 ? 343  GLN   E CB  1 
ATOM   13938 N  N   . GLY   E 2 344 ? 53.963  -12.711 -55.942 1.00 161.76 ? 344  GLY   E N   1 
ATOM   13939 C  CA  . GLY   E 2 344 ? 53.952  -14.115 -56.347 1.00 158.49 ? 344  GLY   E CA  1 
ATOM   13940 C  C   . GLY   E 2 344 ? 52.665  -14.860 -56.047 1.00 155.44 ? 344  GLY   E C   1 
ATOM   13941 O  O   . GLY   E 2 344 ? 52.699  -16.071 -55.810 1.00 152.83 ? 344  GLY   E O   1 
ATOM   13942 N  N   . SER   E 2 345 ? 51.530  -14.164 -56.043 1.00 148.09 ? 345  SER   E N   1 
ATOM   13943 C  CA  . SER   E 2 345 ? 50.234  -14.710 -55.650 1.00 134.30 ? 345  SER   E CA  1 
ATOM   13944 C  C   . SER   E 2 345 ? 49.362  -14.772 -56.901 1.00 130.94 ? 345  SER   E C   1 
ATOM   13945 O  O   . SER   E 2 345 ? 48.808  -13.759 -57.336 1.00 133.29 ? 345  SER   E O   1 
ATOM   13946 C  CB  . SER   E 2 345 ? 49.604  -13.849 -54.549 1.00 132.07 ? 345  SER   E CB  1 
ATOM   13947 O  OG  . SER   E 2 345 ? 48.312  -14.284 -54.132 1.00 118.05 ? 345  SER   E OG  1 
ATOM   13948 N  N   . TYR   E 2 346 ? 49.239  -15.969 -57.481 1.00 125.96 ? 346  TYR   E N   1 
ATOM   13949 C  CA  . TYR   E 2 346 ? 48.281  -16.178 -58.566 1.00 127.77 ? 346  TYR   E CA  1 
ATOM   13950 C  C   . TYR   E 2 346 ? 46.854  -15.799 -58.162 1.00 120.95 ? 346  TYR   E C   1 
ATOM   13951 O  O   . TYR   E 2 346 ? 46.014  -15.555 -59.036 1.00 120.13 ? 346  TYR   E O   1 
ATOM   13952 C  CB  . TYR   E 2 346 ? 48.353  -17.642 -59.023 1.00 125.31 ? 346  TYR   E CB  1 
ATOM   13953 C  CG  . TYR   E 2 346 ? 49.708  -18.010 -59.560 1.00 134.54 ? 346  TYR   E CG  1 
ATOM   13954 C  CD1 . TYR   E 2 346 ? 50.766  -18.270 -58.703 1.00 136.48 ? 346  TYR   E CD1 1 
ATOM   13955 C  CD2 . TYR   E 2 346 ? 49.943  -18.062 -60.922 1.00 145.97 ? 346  TYR   E CD2 1 
ATOM   13956 C  CE1 . TYR   E 2 346 ? 52.020  -18.588 -59.184 1.00 144.45 ? 346  TYR   E CE1 1 
ATOM   13957 C  CE2 . TYR   E 2 346 ? 51.198  -18.382 -61.421 1.00 151.53 ? 346  TYR   E CE2 1 
ATOM   13958 C  CZ  . TYR   E 2 346 ? 52.232  -18.644 -60.546 1.00 150.07 ? 346  TYR   E CZ  1 
ATOM   13959 O  OH  . TYR   E 2 346 ? 53.475  -18.959 -61.040 1.00 153.54 ? 346  TYR   E OH  1 
ATOM   13960 N  N   . VAL   E 2 347 ? 46.563  -15.749 -56.860 1.00 118.47 ? 347  VAL   E N   1 
ATOM   13961 C  CA  . VAL   E 2 347 ? 45.285  -15.243 -56.377 1.00 111.53 ? 347  VAL   E CA  1 
ATOM   13962 C  C   . VAL   E 2 347 ? 45.334  -13.729 -56.330 1.00 110.55 ? 347  VAL   E C   1 
ATOM   13963 O  O   . VAL   E 2 347 ? 46.316  -13.139 -55.872 1.00 112.59 ? 347  VAL   E O   1 
ATOM   13964 C  CB  . VAL   E 2 347 ? 44.953  -15.800 -54.989 1.00 107.18 ? 347  VAL   E CB  1 
ATOM   13965 C  CG1 . VAL   E 2 347 ? 43.518  -15.441 -54.623 1.00 102.53 ? 347  VAL   E CG1 1 
ATOM   13966 C  CG2 . VAL   E 2 347 ? 45.157  -17.264 -54.947 1.00 105.76 ? 347  VAL   E CG2 1 
ATOM   13967 N  N   . VAL   E 2 348 ? 44.266  -13.100 -56.793 1.00 107.00 ? 348  VAL   E N   1 
ATOM   13968 C  CA  . VAL   E 2 348 ? 44.083  -11.657 -56.720 1.00 102.82 ? 348  VAL   E CA  1 
ATOM   13969 C  C   . VAL   E 2 348 ? 42.670  -11.421 -56.220 1.00 102.98 ? 348  VAL   E C   1 
ATOM   13970 O  O   . VAL   E 2 348 ? 41.737  -12.086 -56.682 1.00 105.77 ? 348  VAL   E O   1 
ATOM   13971 C  CB  . VAL   E 2 348 ? 44.275  -10.995 -58.092 1.00 102.99 ? 348  VAL   E CB  1 
ATOM   13972 C  CG1 . VAL   E 2 348 ? 44.298  -9.507  -57.936 1.00 104.81 ? 348  VAL   E CG1 1 
ATOM   13973 C  CG2 . VAL   E 2 348 ? 45.535  -11.521 -58.764 1.00 112.82 ? 348  VAL   E CG2 1 
ATOM   13974 N  N   . ALA   E 2 349 ? 42.501  -10.513 -55.267 1.00 102.91 ? 349  ALA   E N   1 
ATOM   13975 C  CA  . ALA   E 2 349 ? 41.159  -10.308 -54.756 1.00 104.60 ? 349  ALA   E CA  1 
ATOM   13976 C  C   . ALA   E 2 349 ? 40.351  -9.457  -55.727 1.00 108.41 ? 349  ALA   E C   1 
ATOM   13977 O  O   . ALA   E 2 349 ? 40.868  -8.562  -56.394 1.00 108.84 ? 349  ALA   E O   1 
ATOM   13978 C  CB  . ALA   E 2 349 ? 41.185  -9.671  -53.367 1.00 106.84 ? 349  ALA   E CB  1 
ATOM   13979 N  N   . MET   E 2 350 ? 39.059  -9.765  -55.809 1.00 119.78 ? 350  MET   E N   1 
ATOM   13980 C  CA  . MET   E 2 350 ? 38.190  -9.228  -56.852 1.00 121.29 ? 350  MET   E CA  1 
ATOM   13981 C  C   . MET   E 2 350 ? 37.009  -8.490  -56.251 1.00 121.00 ? 350  MET   E C   1 
ATOM   13982 O  O   . MET   E 2 350 ? 36.479  -7.565  -56.874 1.00 124.81 ? 350  MET   E O   1 
ATOM   13983 C  CB  . MET   E 2 350 ? 37.714  -10.351 -57.757 1.00 122.01 ? 350  MET   E CB  1 
ATOM   13984 C  CG  . MET   E 2 350 ? 37.047  -9.917  -59.042 1.00 127.55 ? 350  MET   E CG  1 
ATOM   13985 S  SD  . MET   E 2 350 ? 36.460  -11.327 -60.028 1.00 137.93 ? 350  MET   E SD  1 
ATOM   13986 C  CE  . MET   E 2 350 ? 36.034  -10.538 -61.597 1.00 130.70 ? 350  MET   E CE  1 
ATOM   13987 N  N   . GLU   E 2 351 ? 36.590  -8.899  -55.059 1.00 119.57 ? 351  GLU   E N   1 
ATOM   13988 C  CA  . GLU   E 2 351 ? 35.560  -8.213  -54.294 1.00 116.14 ? 351  GLU   E CA  1 
ATOM   13989 C  C   . GLU   E 2 351 ? 35.749  -8.612  -52.842 1.00 114.53 ? 351  GLU   E C   1 
ATOM   13990 O  O   . GLU   E 2 351 ? 36.544  -9.496  -52.527 1.00 115.98 ? 351  GLU   E O   1 
ATOM   13991 C  CB  . GLU   E 2 351 ? 34.172  -8.570  -54.809 1.00 116.05 ? 351  GLU   E CB  1 
ATOM   13992 C  CG  . GLU   E 2 351 ? 33.223  -7.402  -54.828 1.00 120.77 ? 351  GLU   E CG  1 
ATOM   13993 C  CD  . GLU   E 2 351 ? 31.951  -7.716  -55.584 1.00 127.16 ? 351  GLU   E CD  1 
ATOM   13994 O  OE1 . GLU   E 2 351 ? 32.033  -8.444  -56.597 1.00 131.37 ? 351  GLU   E OE1 1 
ATOM   13995 O  OE2 . GLU   E 2 351 ? 30.865  -7.260  -55.157 1.00 130.57 ? 351  GLU   E OE2 1 
ATOM   13996 N  N   . THR   E 2 352 ? 35.024  -7.945  -51.955 1.00 98.11  ? 352  THR   E N   1 
ATOM   13997 C  CA  . THR   E 2 352 ? 35.097  -8.294  -50.545 1.00 93.72  ? 352  THR   E CA  1 
ATOM   13998 C  C   . THR   E 2 352 ? 33.732  -8.049  -49.933 1.00 90.58  ? 352  THR   E C   1 
ATOM   13999 O  O   . THR   E 2 352 ? 33.161  -6.974  -50.113 1.00 95.93  ? 352  THR   E O   1 
ATOM   14000 C  CB  . THR   E 2 352 ? 36.165  -7.467  -49.820 1.00 94.97  ? 352  THR   E CB  1 
ATOM   14001 O  OG1 . THR   E 2 352 ? 36.175  -6.147  -50.354 1.00 108.49 ? 352  THR   E OG1 1 
ATOM   14002 C  CG2 . THR   E 2 352 ? 37.556  -8.062  -49.981 1.00 96.83  ? 352  THR   E CG2 1 
ATOM   14003 N  N   . PHE   E 2 353 ? 33.218  -9.030  -49.211 1.00 87.20  ? 353  PHE   E N   1 
ATOM   14004 C  CA  . PHE   E 2 353 ? 31.881  -8.944  -48.634 1.00 88.25  ? 353  PHE   E CA  1 
ATOM   14005 C  C   . PHE   E 2 353 ? 31.987  -8.873  -47.116 1.00 88.03  ? 353  PHE   E C   1 
ATOM   14006 O  O   . PHE   E 2 353 ? 32.536  -9.783  -46.485 1.00 88.50  ? 353  PHE   E O   1 
ATOM   14007 C  CB  . PHE   E 2 353 ? 31.025  -10.127 -49.079 1.00 88.13  ? 353  PHE   E CB  1 
ATOM   14008 C  CG  . PHE   E 2 353 ? 31.097  -10.383 -50.550 1.00 87.74  ? 353  PHE   E CG  1 
ATOM   14009 C  CD1 . PHE   E 2 353 ? 30.299  -9.687  -51.435 1.00 91.64  ? 353  PHE   E CD1 1 
ATOM   14010 C  CD2 . PHE   E 2 353 ? 31.986  -11.309 -51.051 1.00 90.68  ? 353  PHE   E CD2 1 
ATOM   14011 C  CE1 . PHE   E 2 353 ? 30.374  -9.921  -52.791 1.00 92.19  ? 353  PHE   E CE1 1 
ATOM   14012 C  CE2 . PHE   E 2 353 ? 32.070  -11.557 -52.410 1.00 94.03  ? 353  PHE   E CE2 1 
ATOM   14013 C  CZ  . PHE   E 2 353 ? 31.261  -10.861 -53.283 1.00 95.13  ? 353  PHE   E CZ  1 
ATOM   14014 N  N   . THR   E 2 354 ? 31.436  -7.804  -46.541 1.00 89.26  ? 354  THR   E N   1 
ATOM   14015 C  CA  . THR   E 2 354 ? 31.675  -7.471  -45.143 1.00 85.11  ? 354  THR   E CA  1 
ATOM   14016 C  C   . THR   E 2 354 ? 31.245  -8.606  -44.234 1.00 84.71  ? 354  THR   E C   1 
ATOM   14017 O  O   . THR   E 2 354 ? 30.212  -9.244  -44.456 1.00 85.44  ? 354  THR   E O   1 
ATOM   14018 C  CB  . THR   E 2 354 ? 30.916  -6.199  -44.751 1.00 81.34  ? 354  THR   E CB  1 
ATOM   14019 O  OG1 . THR   E 2 354 ? 30.972  -5.260  -45.820 1.00 82.87  ? 354  THR   E OG1 1 
ATOM   14020 C  CG2 . THR   E 2 354 ? 31.565  -5.556  -43.563 1.00 84.37  ? 354  THR   E CG2 1 
ATOM   14021 N  N   . ASN   E 2 355 ? 32.058  -8.855  -43.207 1.00 84.00  ? 355  ASN   E N   1 
ATOM   14022 C  CA  . ASN   E 2 355 ? 31.718  -9.791  -42.141 1.00 82.78  ? 355  ASN   E CA  1 
ATOM   14023 C  C   . ASN   E 2 355 ? 32.098  -9.161  -40.809 1.00 82.00  ? 355  ASN   E C   1 
ATOM   14024 O  O   . ASN   E 2 355 ? 33.282  -8.937  -40.528 1.00 80.91  ? 355  ASN   E O   1 
ATOM   14025 C  CB  . ASN   E 2 355 ? 32.408  -11.140 -42.317 1.00 87.20  ? 355  ASN   E CB  1 
ATOM   14026 C  CG  . ASN   E 2 355 ? 32.162  -12.085 -41.139 1.00 87.96  ? 355  ASN   E CG  1 
ATOM   14027 O  OD1 . ASN   E 2 355 ? 31.088  -12.081 -40.521 1.00 83.38  ? 355  ASN   E OD1 1 
ATOM   14028 N  ND2 . ASN   E 2 355 ? 33.163  -12.907 -40.828 1.00 90.39  ? 355  ASN   E ND2 1 
ATOM   14029 N  N   . LEU   E 2 356 ? 31.080  -8.888  -39.995 1.00 82.71  ? 356  LEU   E N   1 
ATOM   14030 C  CA  . LEU   E 2 356 ? 31.280  -8.311  -38.677 1.00 81.12  ? 356  LEU   E CA  1 
ATOM   14031 C  C   . LEU   E 2 356 ? 31.763  -9.336  -37.653 1.00 86.70  ? 356  LEU   E C   1 
ATOM   14032 O  O   . LEU   E 2 356 ? 32.480  -8.964  -36.720 1.00 89.22  ? 356  LEU   E O   1 
ATOM   14033 C  CB  . LEU   E 2 356 ? 29.981  -7.667  -38.206 1.00 78.54  ? 356  LEU   E CB  1 
ATOM   14034 C  CG  . LEU   E 2 356 ? 29.535  -6.516  -39.097 1.00 75.49  ? 356  LEU   E CG  1 
ATOM   14035 C  CD1 . LEU   E 2 356 ? 28.336  -5.767  -38.538 1.00 74.04  ? 356  LEU   E CD1 1 
ATOM   14036 C  CD2 . LEU   E 2 356 ? 30.695  -5.571  -39.347 1.00 80.40  ? 356  LEU   E CD2 1 
ATOM   14037 N  N   . GLY   E 2 357 ? 31.412  -10.615 -37.808 1.00 88.11  ? 357  GLY   E N   1 
ATOM   14038 C  CA  . GLY   E 2 357 ? 31.750  -11.624 -36.828 1.00 87.37  ? 357  GLY   E CA  1 
ATOM   14039 C  C   . GLY   E 2 357 ? 33.203  -12.064 -36.891 1.00 88.06  ? 357  GLY   E C   1 
ATOM   14040 O  O   . GLY   E 2 357 ? 33.897  -11.853 -37.891 1.00 89.57  ? 357  GLY   E O   1 
ATOM   14041 N  N   . PRO   E 2 358 ? 33.706  -12.631 -35.778 1.00 83.54  ? 358  PRO   E N   1 
ATOM   14042 C  CA  . PRO   E 2 358 ? 33.065  -12.645 -34.465 1.00 81.75  ? 358  PRO   E CA  1 
ATOM   14043 C  C   . PRO   E 2 358 ? 33.136  -11.245 -33.906 1.00 81.80  ? 358  PRO   E C   1 
ATOM   14044 O  O   . PRO   E 2 358 ? 34.140  -10.551 -34.097 1.00 78.71  ? 358  PRO   E O   1 
ATOM   14045 C  CB  . PRO   E 2 358 ? 33.915  -13.638 -33.671 1.00 77.79  ? 358  PRO   E CB  1 
ATOM   14046 C  CG  . PRO   E 2 358 ? 35.278  -13.494 -34.279 1.00 76.06  ? 358  PRO   E CG  1 
ATOM   14047 C  CD  . PRO   E 2 358 ? 35.000  -13.337 -35.749 1.00 81.24  ? 358  PRO   E CD  1 
ATOM   14048 N  N   . ILE   E 2 359 ? 32.072  -10.790 -33.258 1.00 81.52  ? 359  ILE   E N   1 
ATOM   14049 C  CA  . ILE   E 2 359 ? 32.097  -9.546  -32.503 1.00 78.41  ? 359  ILE   E CA  1 
ATOM   14050 C  C   . ILE   E 2 359 ? 32.327  -9.914  -31.044 1.00 79.77  ? 359  ILE   E C   1 
ATOM   14051 O  O   . ILE   E 2 359 ? 31.438  -10.465 -30.383 1.00 79.26  ? 359  ILE   E O   1 
ATOM   14052 C  CB  . ILE   E 2 359 ? 30.813  -8.735  -32.692 1.00 76.76  ? 359  ILE   E CB  1 
ATOM   14053 C  CG1 . ILE   E 2 359 ? 30.712  -8.278  -34.150 1.00 76.30  ? 359  ILE   E CG1 1 
ATOM   14054 C  CG2 . ILE   E 2 359 ? 30.834  -7.539  -31.758 1.00 79.06  ? 359  ILE   E CG2 1 
ATOM   14055 C  CD1 . ILE   E 2 359 ? 29.416  -7.588  -34.524 1.00 73.91  ? 359  ILE   E CD1 1 
ATOM   14056 N  N   . VAL   E 2 360 ? 33.534  -9.628  -30.553 1.00 77.64  ? 360  VAL   E N   1 
ATOM   14057 C  CA  . VAL   E 2 360 ? 33.933  -10.011 -29.207 1.00 77.28  ? 360  VAL   E CA  1 
ATOM   14058 C  C   . VAL   E 2 360 ? 33.797  -8.851  -28.216 1.00 83.49  ? 360  VAL   E C   1 
ATOM   14059 O  O   . VAL   E 2 360 ? 33.707  -9.092  -26.996 1.00 84.19  ? 360  VAL   E O   1 
ATOM   14060 C  CB  . VAL   E 2 360 ? 35.369  -10.564 -29.229 1.00 73.55  ? 360  VAL   E CB  1 
ATOM   14061 C  CG1 . VAL   E 2 360 ? 35.469  -11.661 -30.242 1.00 73.29  ? 360  VAL   E CG1 1 
ATOM   14062 C  CG2 . VAL   E 2 360 ? 36.353  -9.470  -29.551 1.00 79.29  ? 360  VAL   E CG2 1 
ATOM   14063 N  N   . ASP   E 2 361 ? 33.757  -7.611  -28.701 1.00 84.34  ? 361  ASP   E N   1 
ATOM   14064 C  CA  . ASP   E 2 361 ? 33.476  -6.458  -27.861 1.00 85.61  ? 361  ASP   E CA  1 
ATOM   14065 C  C   . ASP   E 2 361 ? 32.854  -5.371  -28.737 1.00 84.04  ? 361  ASP   E C   1 
ATOM   14066 O  O   . ASP   E 2 361 ? 32.911  -5.426  -29.970 1.00 82.92  ? 361  ASP   E O   1 
ATOM   14067 C  CB  . ASP   E 2 361 ? 34.746  -5.956  -27.151 1.00 85.04  ? 361  ASP   E CB  1 
ATOM   14068 C  CG  . ASP   E 2 361 ? 34.444  -5.287  -25.808 1.00 87.73  ? 361  ASP   E CG  1 
ATOM   14069 O  OD1 . ASP   E 2 361 ? 33.249  -5.237  -25.400 1.00 86.66  ? 361  ASP   E OD1 1 
ATOM   14070 O  OD2 . ASP   E 2 361 ? 35.408  -4.821  -25.153 1.00 87.95  ? 361  ASP   E OD2 1 
ATOM   14071 N  N   . MET   E 2 362 ? 32.258  -4.379  -28.088 1.00 81.35  ? 362  MET   E N   1 
ATOM   14072 C  CA  . MET   E 2 362 ? 31.716  -3.261  -28.836 1.00 77.48  ? 362  MET   E CA  1 
ATOM   14073 C  C   . MET   E 2 362 ? 31.366  -2.157  -27.860 1.00 82.32  ? 362  MET   E C   1 
ATOM   14074 O  O   . MET   E 2 362 ? 31.216  -2.402  -26.660 1.00 91.25  ? 362  MET   E O   1 
ATOM   14075 C  CB  . MET   E 2 362 ? 30.485  -3.670  -29.620 1.00 78.77  ? 362  MET   E CB  1 
ATOM   14076 C  CG  . MET   E 2 362 ? 29.345  -4.071  -28.745 1.00 79.44  ? 362  MET   E CG  1 
ATOM   14077 S  SD  . MET   E 2 362 ? 27.841  -4.221  -29.744 1.00 87.75  ? 362  MET   E SD  1 
ATOM   14078 C  CE  . MET   E 2 362 ? 28.473  -5.118  -31.137 1.00 78.18  ? 362  MET   E CE  1 
ATOM   14079 N  N   . CYS   E 2 363 ? 31.257  -0.937  -28.384 1.00 80.94  ? 363  CYS   E N   1 
ATOM   14080 C  CA  . CYS   E 2 363 ? 30.766  0.203   -27.619 1.00 82.96  ? 363  CYS   E CA  1 
ATOM   14081 C  C   . CYS   E 2 363 ? 30.088  1.189   -28.565 1.00 85.27  ? 363  CYS   E C   1 
ATOM   14082 O  O   . CYS   E 2 363 ? 30.311  1.181   -29.782 1.00 83.37  ? 363  CYS   E O   1 
ATOM   14083 C  CB  . CYS   E 2 363 ? 31.885  0.899   -26.825 1.00 86.44  ? 363  CYS   E CB  1 
ATOM   14084 S  SG  . CYS   E 2 363 ? 33.297  1.475   -27.803 1.00 85.03  ? 363  CYS   E SG  1 
ATOM   14085 N  N   . VAL   E 2 364 ? 29.247  2.038   -27.983 1.00 83.95  ? 364  VAL   E N   1 
ATOM   14086 C  CA  . VAL   E 2 364 ? 28.489  3.032   -28.726 1.00 83.12  ? 364  VAL   E CA  1 
ATOM   14087 C  C   . VAL   E 2 364 ? 29.139  4.391   -28.509 1.00 89.22  ? 364  VAL   E C   1 
ATOM   14088 O  O   . VAL   E 2 364 ? 29.226  4.863   -27.372 1.00 94.44  ? 364  VAL   E O   1 
ATOM   14089 C  CB  . VAL   E 2 364 ? 27.024  3.054   -28.276 1.00 84.46  ? 364  VAL   E CB  1 
ATOM   14090 C  CG1 . VAL   E 2 364 ? 26.185  3.883   -29.244 1.00 97.15  ? 364  VAL   E CG1 1 
ATOM   14091 C  CG2 . VAL   E 2 364 ? 26.499  1.653   -28.146 1.00 84.57  ? 364  VAL   E CG2 1 
ATOM   14092 N  N   . VAL   E 2 365 ? 29.586  5.032   -29.582 1.00 93.64  ? 365  VAL   E N   1 
ATOM   14093 C  CA  . VAL   E 2 365 ? 30.261  6.325   -29.508 1.00 97.33  ? 365  VAL   E CA  1 
ATOM   14094 C  C   . VAL   E 2 365 ? 29.608  7.247   -30.529 1.00 107.76 ? 365  VAL   E C   1 
ATOM   14095 O  O   . VAL   E 2 365 ? 29.589  6.933   -31.723 1.00 114.24 ? 365  VAL   E O   1 
ATOM   14096 C  CB  . VAL   E 2 365 ? 31.776  6.207   -29.771 1.00 91.90  ? 365  VAL   E CB  1 
ATOM   14097 C  CG1 . VAL   E 2 365 ? 32.466  7.496   -29.472 1.00 95.07  ? 365  VAL   E CG1 1 
ATOM   14098 C  CG2 . VAL   E 2 365 ? 32.389  5.111   -28.928 1.00 91.79  ? 365  VAL   E CG2 1 
ATOM   14099 N  N   . ASP   E 2 366 ? 29.066  8.373   -30.064 1.00 117.16 ? 366  ASP   E N   1 
ATOM   14100 C  CA  . ASP   E 2 366 ? 28.481  9.391   -30.948 1.00 122.18 ? 366  ASP   E CA  1 
ATOM   14101 C  C   . ASP   E 2 366 ? 29.606  10.233  -31.565 1.00 120.77 ? 366  ASP   E C   1 
ATOM   14102 O  O   . ASP   E 2 366 ? 29.799  11.408  -31.240 1.00 125.32 ? 366  ASP   E O   1 
ATOM   14103 C  CB  . ASP   E 2 366 ? 27.493  10.255  -30.167 1.00 125.11 ? 366  ASP   E CB  1 
ATOM   14104 C  CG  . ASP   E 2 366 ? 26.678  11.162  -31.054 1.00 129.01 ? 366  ASP   E CG  1 
ATOM   14105 O  OD1 . ASP   E 2 366 ? 26.795  11.041  -32.292 1.00 132.35 ? 366  ASP   E OD1 1 
ATOM   14106 O  OD2 . ASP   E 2 366 ? 25.922  11.989  -30.509 1.00 127.04 ? 366  ASP   E OD2 1 
ATOM   14107 N  N   . LEU   E 2 367 ? 30.347  9.609   -32.495 1.00 115.82 ? 367  LEU   E N   1 
ATOM   14108 C  CA  . LEU   E 2 367 ? 31.651  10.144  -32.888 1.00 111.54 ? 367  LEU   E CA  1 
ATOM   14109 C  C   . LEU   E 2 367 ? 31.542  11.511  -33.548 1.00 115.79 ? 367  LEU   E C   1 
ATOM   14110 O  O   . LEU   E 2 367 ? 32.469  12.322  -33.445 1.00 113.39 ? 367  LEU   E O   1 
ATOM   14111 C  CB  . LEU   E 2 367 ? 32.359  9.163   -33.824 1.00 108.78 ? 367  LEU   E CB  1 
ATOM   14112 C  CG  . LEU   E 2 367 ? 33.199  8.054   -33.178 1.00 100.72 ? 367  LEU   E CG  1 
ATOM   14113 C  CD1 . LEU   E 2 367 ? 33.590  6.995   -34.196 1.00 100.59 ? 367  LEU   E CD1 1 
ATOM   14114 C  CD2 . LEU   E 2 367 ? 34.441  8.589   -32.475 1.00 97.49  ? 367  LEU   E CD2 1 
ATOM   14115 N  N   . GLU   E 2 368 ? 30.444  11.773  -34.249 1.00 119.60 ? 368  GLU   E N   1 
ATOM   14116 C  CA  . GLU   E 2 368 ? 30.204  13.076  -34.858 1.00 120.10 ? 368  GLU   E CA  1 
ATOM   14117 C  C   . GLU   E 2 368 ? 29.306  13.961  -34.007 1.00 126.21 ? 368  GLU   E C   1 
ATOM   14118 O  O   . GLU   E 2 368 ? 29.035  15.104  -34.392 1.00 128.39 ? 368  GLU   E O   1 
ATOM   14119 C  CB  . GLU   E 2 368 ? 29.613  12.901  -36.258 1.00 115.45 ? 368  GLU   E CB  1 
ATOM   14120 C  CG  . GLU   E 2 368 ? 30.342  11.823  -37.023 1.00 113.81 ? 368  GLU   E CG  1 
ATOM   14121 C  CD  . GLU   E 2 368 ? 30.104  11.874  -38.506 1.00 114.56 ? 368  GLU   E CD  1 
ATOM   14122 O  OE1 . GLU   E 2 368 ? 29.119  12.521  -38.933 1.00 114.27 ? 368  GLU   E OE1 1 
ATOM   14123 O  OE2 . GLU   E 2 368 ? 30.914  11.268  -39.240 1.00 114.70 ? 368  GLU   E OE2 1 
ATOM   14124 N  N   . ARG   E 2 369 ? 28.860  13.462  -32.854 1.00 128.06 ? 369  ARG   E N   1 
ATOM   14125 C  CA  . ARG   E 2 369 ? 28.126  14.250  -31.864 1.00 129.42 ? 369  ARG   E CA  1 
ATOM   14126 C  C   . ARG   E 2 369 ? 26.809  14.778  -32.425 1.00 130.80 ? 369  ARG   E C   1 
ATOM   14127 O  O   . ARG   E 2 369 ? 26.330  15.834  -32.004 1.00 130.00 ? 369  ARG   E O   1 
ATOM   14128 C  CB  . ARG   E 2 369 ? 28.984  15.397  -31.317 1.00 127.33 ? 369  ARG   E CB  1 
ATOM   14129 N  N   . GLN   E 2 370 ? 26.216  14.037  -33.371 1.00 133.21 ? 370  GLN   E N   1 
ATOM   14130 C  CA  . GLN   E 2 370 ? 24.929  14.384  -33.966 1.00 133.53 ? 370  GLN   E CA  1 
ATOM   14131 C  C   . GLN   E 2 370 ? 23.760  13.700  -33.265 1.00 135.61 ? 370  GLN   E C   1 
ATOM   14132 O  O   . GLN   E 2 370 ? 22.730  13.457  -33.904 1.00 132.67 ? 370  GLN   E O   1 
ATOM   14133 C  CB  . GLN   E 2 370 ? 24.912  14.042  -35.459 1.00 131.59 ? 370  GLN   E CB  1 
ATOM   14134 C  CG  . GLN   E 2 370 ? 25.853  14.871  -36.364 1.00 131.64 ? 370  GLN   E CG  1 
ATOM   14135 C  CD  . GLN   E 2 370 ? 25.843  14.433  -37.830 1.00 133.72 ? 370  GLN   E CD  1 
ATOM   14136 O  OE1 . GLN   E 2 370 ? 25.533  13.288  -38.139 1.00 133.35 ? 370  GLN   E OE1 1 
ATOM   14137 N  NE2 . GLN   E 2 370 ? 26.194  15.344  -38.734 1.00 136.22 ? 370  GLN   E NE2 1 
ATOM   14138 N  N   . GLY   E 2 371 ? 23.904  13.365  -31.977 1.00 137.69 ? 371  GLY   E N   1 
ATOM   14139 C  CA  . GLY   E 2 371 ? 22.877  12.677  -31.217 1.00 139.00 ? 371  GLY   E CA  1 
ATOM   14140 C  C   . GLY   E 2 371 ? 22.576  11.273  -31.679 1.00 142.38 ? 371  GLY   E C   1 
ATOM   14141 O  O   . GLY   E 2 371 ? 21.877  10.540  -30.965 1.00 138.76 ? 371  GLY   E O   1 
ATOM   14142 N  N   . GLN   E 2 372 ? 23.083  10.873  -32.848 1.00 159.37 ? 372  GLN   E N   1 
ATOM   14143 C  CA  . GLN   E 2 372 ? 22.818  9.578   -33.459 1.00 155.90 ? 372  GLN   E CA  1 
ATOM   14144 C  C   . GLN   E 2 372 ? 23.455  8.322   -32.887 1.00 154.00 ? 372  GLN   E C   1 
ATOM   14145 O  O   . GLN   E 2 372 ? 22.774  7.314   -32.668 1.00 154.38 ? 372  GLN   E O   1 
ATOM   14146 C  CB  . GLN   E 2 372 ? 23.326  9.573   -34.910 1.00 157.08 ? 372  GLN   E CB  1 
ATOM   14147 C  CG  . GLN   E 2 372 ? 23.138  8.271   -35.682 1.00 156.12 ? 372  GLN   E CG  1 
ATOM   14148 C  CD  . GLN   E 2 372 ? 21.725  8.080   -36.189 1.00 156.67 ? 372  GLN   E CD  1 
ATOM   14149 O  OE1 . GLN   E 2 372 ? 20.743  8.446   -35.521 1.00 156.93 ? 372  GLN   E OE1 1 
ATOM   14150 N  NE2 . GLN   E 2 372 ? 21.609  7.498   -37.383 1.00 155.16 ? 372  GLN   E NE2 1 
ATOM   14151 N  N   . GLY   E 2 373 ? 24.754  8.385   -32.619 1.00 134.24 ? 373  GLY   E N   1 
ATOM   14152 C  CA  . GLY   E 2 373 ? 25.482  7.218   -32.174 1.00 124.68 ? 373  GLY   E CA  1 
ATOM   14153 C  C   . GLY   E 2 373 ? 25.983  6.391   -33.339 1.00 117.74 ? 373  GLY   E C   1 
ATOM   14154 O  O   . GLY   E 2 373 ? 25.337  6.286   -34.388 1.00 115.89 ? 373  GLY   E O   1 
ATOM   14155 N  N   . GLN   E 2 374 ? 27.157  5.814   -33.163 1.00 114.46 ? 374  GLN   E N   1 
ATOM   14156 C  CA  . GLN   E 2 374 ? 27.735  4.882   -34.111 1.00 111.90 ? 374  GLN   E CA  1 
ATOM   14157 C  C   . GLN   E 2 374 ? 28.040  3.697   -33.197 1.00 106.37 ? 374  GLN   E C   1 
ATOM   14158 O  O   . GLN   E 2 374 ? 27.919  3.794   -31.977 1.00 105.68 ? 374  GLN   E O   1 
ATOM   14159 C  CB  . GLN   E 2 374 ? 28.979  5.402   -34.840 1.00 112.18 ? 374  GLN   E CB  1 
ATOM   14160 C  CG  . GLN   E 2 374 ? 28.788  6.851   -35.297 1.00 116.01 ? 374  GLN   E CG  1 
ATOM   14161 C  CD  . GLN   E 2 374 ? 29.819  7.314   -36.300 1.00 118.94 ? 374  GLN   E CD  1 
ATOM   14162 O  OE1 . GLN   E 2 374 ? 29.503  8.039   -37.257 1.00 122.68 ? 374  GLN   E OE1 1 
ATOM   14163 N  NE2 . GLN   E 2 374 ? 31.064  6.903   -36.092 1.00 116.00 ? 374  GLN   E NE2 1 
ATOM   14164 N  N   . LEU   E 2 375 ? 28.412  2.564   -33.786 1.00 92.87  ? 375  LEU   E N   1 
ATOM   14165 C  CA  . LEU   E 2 375 ? 28.845  1.402   -33.022 1.00 89.51  ? 375  LEU   E CA  1 
ATOM   14166 C  C   . LEU   E 2 375 ? 30.238  1.008   -33.483 1.00 85.08  ? 375  LEU   E C   1 
ATOM   14167 O  O   . LEU   E 2 375 ? 30.455  0.838   -34.680 1.00 87.56  ? 375  LEU   E O   1 
ATOM   14168 C  CB  . LEU   E 2 375 ? 27.862  0.242   -33.215 1.00 92.03  ? 375  LEU   E CB  1 
ATOM   14169 C  CG  . LEU   E 2 375 ? 27.935  -1.020  -32.334 1.00 87.22  ? 375  LEU   E CG  1 
ATOM   14170 C  CD1 . LEU   E 2 375 ? 27.750  -0.749  -30.851 1.00 82.55  ? 375  LEU   E CD1 1 
ATOM   14171 C  CD2 . LEU   E 2 375 ? 26.886  -1.990  -32.809 1.00 83.53  ? 375  LEU   E CD2 1 
ATOM   14172 N  N   . VAL   E 2 376 ? 31.174  0.852   -32.553 1.00 77.10  ? 376  VAL   E N   1 
ATOM   14173 C  CA  . VAL   E 2 376 ? 32.515  0.372   -32.882 1.00 80.80  ? 376  VAL   E CA  1 
ATOM   14174 C  C   . VAL   E 2 376 ? 32.717  -0.991  -32.232 1.00 86.35  ? 376  VAL   E C   1 
ATOM   14175 O  O   . VAL   E 2 376 ? 32.398  -1.167  -31.048 1.00 89.82  ? 376  VAL   E O   1 
ATOM   14176 C  CB  . VAL   E 2 376 ? 33.612  1.358   -32.436 1.00 84.01  ? 376  VAL   E CB  1 
ATOM   14177 C  CG1 . VAL   E 2 376 ? 34.989  0.892   -32.912 1.00 79.75  ? 376  VAL   E CG1 1 
ATOM   14178 C  CG2 . VAL   E 2 376 ? 33.313  2.741   -32.974 1.00 86.77  ? 376  VAL   E CG2 1 
ATOM   14179 N  N   . THR   E 2 377 ? 33.279  -1.951  -33.003 1.00 85.75  ? 377  THR   E N   1 
ATOM   14180 C  CA  . THR   E 2 377 ? 33.359  -3.368  -32.631 1.00 81.63  ? 377  THR   E CA  1 
ATOM   14181 C  C   . THR   E 2 377 ? 34.769  -3.926  -32.813 1.00 79.36  ? 377  THR   E C   1 
ATOM   14182 O  O   . THR   E 2 377 ? 35.457  -3.587  -33.784 1.00 76.29  ? 377  THR   E O   1 
ATOM   14183 C  CB  . THR   E 2 377 ? 32.410  -4.215  -33.482 1.00 78.61  ? 377  THR   E CB  1 
ATOM   14184 O  OG1 . THR   E 2 377 ? 32.807  -4.094  -34.851 1.00 78.83  ? 377  THR   E OG1 1 
ATOM   14185 C  CG2 . THR   E 2 377 ? 30.960  -3.755  -33.334 1.00 79.57  ? 377  THR   E CG2 1 
ATOM   14186 N  N   . CYS   E 2 378 ? 35.181  -4.795  -31.875 1.00 80.40  ? 378  CYS   E N   1 
ATOM   14187 C  CA  . CYS   E 2 378 ? 36.369  -5.647  -32.013 1.00 78.34  ? 378  CYS   E CA  1 
ATOM   14188 C  C   . CYS   E 2 378 ? 35.948  -6.864  -32.814 1.00 78.96  ? 378  CYS   E C   1 
ATOM   14189 O  O   . CYS   E 2 378 ? 35.438  -7.842  -32.267 1.00 79.91  ? 378  CYS   E O   1 
ATOM   14190 C  CB  . CYS   E 2 378 ? 36.922  -6.071  -30.660 1.00 78.29  ? 378  CYS   E CB  1 
ATOM   14191 S  SG  . CYS   E 2 378 ? 37.556  -4.749  -29.621 1.00 83.44  ? 378  CYS   E SG  1 
ATOM   14192 N  N   . SER   E 2 379 ? 36.159  -6.807  -34.126 1.00 78.01  ? 379  SER   E N   1 
ATOM   14193 C  CA  . SER   E 2 379 ? 35.648  -7.802  -35.052 1.00 76.85  ? 379  SER   E CA  1 
ATOM   14194 C  C   . SER   E 2 379 ? 36.750  -8.692  -35.612 1.00 80.45  ? 379  SER   E C   1 
ATOM   14195 O  O   . SER   E 2 379 ? 37.897  -8.265  -35.792 1.00 80.01  ? 379  SER   E O   1 
ATOM   14196 C  CB  . SER   E 2 379 ? 34.922  -7.121  -36.204 1.00 77.31  ? 379  SER   E CB  1 
ATOM   14197 O  OG  . SER   E 2 379 ? 33.650  -6.699  -35.776 1.00 79.85  ? 379  SER   E OG  1 
ATOM   14198 N  N   . GLY   E 2 380 ? 36.375  -9.942  -35.892 1.00 80.70  ? 380  GLY   E N   1 
ATOM   14199 C  CA  . GLY   E 2 380 ? 37.271  -10.871 -36.536 1.00 76.50  ? 380  GLY   E CA  1 
ATOM   14200 C  C   . GLY   E 2 380 ? 38.280  -11.441 -35.568 1.00 77.58  ? 380  GLY   E C   1 
ATOM   14201 O  O   . GLY   E 2 380 ? 38.284  -11.178 -34.366 1.00 76.30  ? 380  GLY   E O   1 
ATOM   14202 N  N   . ALA   E 2 381 ? 39.218  -12.191 -36.146 1.00 81.76  ? 381  ALA   E N   1 
ATOM   14203 C  CA  . ALA   E 2 381 ? 40.303  -12.780 -35.338 1.00 79.22  ? 381  ALA   E CA  1 
ATOM   14204 C  C   . ALA   E 2 381 ? 41.540  -12.943 -36.217 1.00 75.71  ? 381  ALA   E C   1 
ATOM   14205 O  O   . ALA   E 2 381 ? 41.411  -12.875 -37.453 1.00 75.40  ? 381  ALA   E O   1 
ATOM   14206 C  CB  . ALA   E 2 381 ? 39.856  -14.102 -34.782 1.00 75.25  ? 381  ALA   E CB  1 
ATOM   14207 N  N   . PHE   E 2 382 ? 42.702  -13.126 -35.595 1.00 79.93  ? 382  PHE   E N   1 
ATOM   14208 C  CA  . PHE   E 2 382 ? 43.968  -13.347 -36.343 1.00 81.65  ? 382  PHE   E CA  1 
ATOM   14209 C  C   . PHE   E 2 382 ? 44.155  -12.274 -37.404 1.00 83.70  ? 382  PHE   E C   1 
ATOM   14210 O  O   . PHE   E 2 382 ? 43.830  -11.100 -37.153 1.00 83.68  ? 382  PHE   E O   1 
ATOM   14211 C  CB  . PHE   E 2 382 ? 43.968  -14.758 -36.931 1.00 83.43  ? 382  PHE   E CB  1 
ATOM   14212 C  CG  . PHE   E 2 382 ? 43.532  -15.842 -35.956 1.00 85.12  ? 382  PHE   E CG  1 
ATOM   14213 C  CD1 . PHE   E 2 382 ? 44.021  -15.875 -34.656 1.00 84.36  ? 382  PHE   E CD1 1 
ATOM   14214 C  CD2 . PHE   E 2 382 ? 42.632  -16.826 -36.345 1.00 84.16  ? 382  PHE   E CD2 1 
ATOM   14215 C  CE1 . PHE   E 2 382 ? 43.618  -16.861 -33.773 1.00 84.96  ? 382  PHE   E CE1 1 
ATOM   14216 C  CE2 . PHE   E 2 382 ? 42.235  -17.811 -35.458 1.00 85.52  ? 382  PHE   E CE2 1 
ATOM   14217 C  CZ  . PHE   E 2 382 ? 42.729  -17.827 -34.177 1.00 84.76  ? 382  PHE   E CZ  1 
ATOM   14218 N  N   . LYS   E 2 383 ? 44.669  -12.658 -38.571 1.00 80.57  ? 383  LYS   E N   1 
ATOM   14219 C  CA  . LYS   E 2 383 ? 44.980  -11.661 -39.627 1.00 80.75  ? 383  LYS   E CA  1 
ATOM   14220 C  C   . LYS   E 2 383 ? 43.734  -10.853 -39.990 1.00 82.00  ? 383  LYS   E C   1 
ATOM   14221 O  O   . LYS   E 2 383 ? 43.886  -9.743  -40.525 1.00 83.54  ? 383  LYS   E O   1 
ATOM   14222 C  CB  . LYS   E 2 383 ? 45.506  -12.358 -40.883 1.00 86.86  ? 383  LYS   E CB  1 
ATOM   14223 C  CG  . LYS   E 2 383 ? 45.955  -11.454 -42.017 1.00 92.44  ? 383  LYS   E CG  1 
ATOM   14224 C  CD  . LYS   E 2 383 ? 46.347  -12.232 -43.266 1.00 96.73  ? 383  LYS   E CD  1 
ATOM   14225 C  CE  . LYS   E 2 383 ? 47.077  -11.402 -44.275 1.00 96.87  ? 383  LYS   E CE  1 
ATOM   14226 N  NZ  . LYS   E 2 383 ? 46.287  -10.253 -44.724 1.00 96.17  ? 383  LYS   E NZ  1 
ATOM   14227 N  N   . GLU   E 2 384 ? 42.552  -11.397 -39.731 1.00 80.55  ? 384  GLU   E N   1 
ATOM   14228 C  CA  . GLU   E 2 384 ? 41.317  -10.700 -40.148 1.00 80.39  ? 384  GLU   E CA  1 
ATOM   14229 C  C   . GLU   E 2 384 ? 40.860  -9.752  -39.035 1.00 79.93  ? 384  GLU   E C   1 
ATOM   14230 O  O   . GLU   E 2 384 ? 39.771  -9.167  -39.174 1.00 80.78  ? 384  GLU   E O   1 
ATOM   14231 C  CB  . GLU   E 2 384 ? 40.267  -11.757 -40.465 1.00 82.54  ? 384  GLU   E CB  1 
ATOM   14232 C  CG  . GLU   E 2 384 ? 40.813  -12.914 -41.294 1.00 86.40  ? 384  GLU   E CG  1 
ATOM   14233 C  CD  . GLU   E 2 384 ? 41.029  -12.598 -42.761 1.00 92.67  ? 384  GLU   E CD  1 
ATOM   14234 O  OE1 . GLU   E 2 384 ? 40.414  -11.641 -43.270 1.00 95.80  ? 384  GLU   E OE1 1 
ATOM   14235 O  OE2 . GLU   E 2 384 ? 41.820  -13.319 -43.399 1.00 93.60  ? 384  GLU   E OE2 1 
ATOM   14236 N  N   . GLY   E 2 385 ? 41.654  -9.602  -37.977 1.00 76.38  ? 385  GLY   E N   1 
ATOM   14237 C  CA  . GLY   E 2 385 ? 41.191  -8.757  -36.888 1.00 77.62  ? 385  GLY   E CA  1 
ATOM   14238 C  C   . GLY   E 2 385 ? 40.983  -7.329  -37.354 1.00 77.91  ? 385  GLY   E C   1 
ATOM   14239 O  O   . GLY   E 2 385 ? 41.852  -6.743  -38.011 1.00 83.04  ? 385  GLY   E O   1 
ATOM   14240 N  N   . SER   E 2 386 ? 39.828  -6.760  -37.025 1.00 75.96  ? 386  SER   E N   1 
ATOM   14241 C  CA  . SER   E 2 386 ? 39.447  -5.468  -37.577 1.00 75.55  ? 386  SER   E CA  1 
ATOM   14242 C  C   . SER   E 2 386 ? 38.703  -4.651  -36.534 1.00 80.19  ? 386  SER   E C   1 
ATOM   14243 O  O   . SER   E 2 386 ? 38.327  -5.152  -35.468 1.00 84.04  ? 386  SER   E O   1 
ATOM   14244 C  CB  . SER   E 2 386 ? 38.571  -5.633  -38.822 1.00 75.12  ? 386  SER   E CB  1 
ATOM   14245 O  OG  . SER   E 2 386 ? 37.279  -6.129  -38.510 1.00 74.74  ? 386  SER   E OG  1 
ATOM   14246 N  N   . LEU   E 2 387 ? 38.513  -3.368  -36.842 1.00 79.90  ? 387  LEU   E N   1 
ATOM   14247 C  CA  . LEU   E 2 387 ? 37.573  -2.503  -36.135 1.00 79.54  ? 387  LEU   E CA  1 
ATOM   14248 C  C   . LEU   E 2 387 ? 36.487  -2.069  -37.108 1.00 80.91  ? 387  LEU   E C   1 
ATOM   14249 O  O   . LEU   E 2 387 ? 36.790  -1.543  -38.184 1.00 82.39  ? 387  LEU   E O   1 
ATOM   14250 C  CB  . LEU   E 2 387 ? 38.264  -1.269  -35.556 1.00 76.93  ? 387  LEU   E CB  1 
ATOM   14251 C  CG  . LEU   E 2 387 ? 39.081  -1.525  -34.309 1.00 74.08  ? 387  LEU   E CG  1 
ATOM   14252 C  CD1 . LEU   E 2 387 ? 39.403  -0.209  -33.683 1.00 76.99  ? 387  LEU   E CD1 1 
ATOM   14253 C  CD2 . LEU   E 2 387 ? 38.305  -2.421  -33.362 1.00 76.67  ? 387  LEU   E CD2 1 
ATOM   14254 N  N   . ARG   E 2 388 ? 35.228  -2.284  -36.742 1.00 78.41  ? 388  ARG   E N   1 
ATOM   14255 C  CA  . ARG   E 2 388 ? 34.110  -1.930  -37.607 1.00 80.57  ? 388  ARG   E CA  1 
ATOM   14256 C  C   . ARG   E 2 388 ? 33.322  -0.794  -36.961 1.00 86.56  ? 388  ARG   E C   1 
ATOM   14257 O  O   . ARG   E 2 388 ? 33.030  -0.855  -35.760 1.00 90.90  ? 388  ARG   E O   1 
ATOM   14258 C  CB  . ARG   E 2 388 ? 33.223  -3.154  -37.849 1.00 81.44  ? 388  ARG   E CB  1 
ATOM   14259 C  CG  . ARG   E 2 388 ? 33.961  -4.415  -38.342 1.00 80.41  ? 388  ARG   E CG  1 
ATOM   14260 C  CD  . ARG   E 2 388 ? 34.680  -4.216  -39.684 1.00 80.36  ? 388  ARG   E CD  1 
ATOM   14261 N  NE  . ARG   E 2 388 ? 35.364  -5.425  -40.148 1.00 81.75  ? 388  ARG   E NE  1 
ATOM   14262 C  CZ  . ARG   E 2 388 ? 35.220  -5.991  -41.346 1.00 83.90  ? 388  ARG   E CZ  1 
ATOM   14263 N  NH1 . ARG   E 2 388 ? 34.421  -5.482  -42.268 1.00 84.82  ? 388  ARG   E NH1 1 
ATOM   14264 N  NH2 . ARG   E 2 388 ? 35.913  -7.088  -41.633 1.00 85.47  ? 388  ARG   E NH2 1 
ATOM   14265 N  N   . ILE   E 2 389 ? 32.989  0.249   -37.740 1.00 85.54  ? 389  ILE   E N   1 
ATOM   14266 C  CA  . ILE   E 2 389 ? 32.219  1.393   -37.233 1.00 87.58  ? 389  ILE   E CA  1 
ATOM   14267 C  C   . ILE   E 2 389 ? 30.919  1.499   -38.023 1.00 92.40  ? 389  ILE   E C   1 
ATOM   14268 O  O   . ILE   E 2 389 ? 30.935  1.795   -39.222 1.00 96.65  ? 389  ILE   E O   1 
ATOM   14269 C  CB  . ILE   E 2 389 ? 32.998  2.716   -37.281 1.00 88.06  ? 389  ILE   E CB  1 
ATOM   14270 C  CG1 . ILE   E 2 389 ? 34.377  2.584   -36.629 1.00 86.20  ? 389  ILE   E CG1 1 
ATOM   14271 C  CG2 . ILE   E 2 389 ? 32.242  3.784   -36.498 1.00 91.61  ? 389  ILE   E CG2 1 
ATOM   14272 C  CD1 . ILE   E 2 389 ? 35.490  2.372   -37.606 1.00 84.71  ? 389  ILE   E CD1 1 
ATOM   14273 N  N   . ILE   E 2 390 ? 29.795  1.308   -37.331 1.00 95.62  ? 390  ILE   E N   1 
ATOM   14274 C  CA  . ILE   E 2 390 ? 28.503  1.001   -37.934 1.00 99.35  ? 390  ILE   E CA  1 
ATOM   14275 C  C   . ILE   E 2 390 ? 27.534  2.120   -37.615 1.00 104.94 ? 390  ILE   E C   1 
ATOM   14276 O  O   . ILE   E 2 390 ? 27.305  2.411   -36.440 1.00 110.02 ? 390  ILE   E O   1 
ATOM   14277 C  CB  . ILE   E 2 390 ? 27.944  -0.326  -37.399 1.00 98.54  ? 390  ILE   E CB  1 
ATOM   14278 C  CG1 . ILE   E 2 390 ? 28.923  -1.489  -37.653 1.00 92.45  ? 390  ILE   E CG1 1 
ATOM   14279 C  CG2 . ILE   E 2 390 ? 26.541  -0.553  -37.947 1.00 103.02 ? 390  ILE   E CG2 1 
ATOM   14280 C  CD1 . ILE   E 2 390 ? 29.027  -2.477  -36.500 1.00 85.88  ? 390  ILE   E CD1 1 
ATOM   14281 N  N   . ARG   E 2 391 ? 26.907  2.693   -38.639 1.00 122.70 ? 391  ARG   E N   1 
ATOM   14282 C  CA  . ARG   E 2 391 ? 26.008  3.819   -38.421 1.00 123.48 ? 391  ARG   E CA  1 
ATOM   14283 C  C   . ARG   E 2 391 ? 24.805  3.751   -39.357 1.00 125.30 ? 391  ARG   E C   1 
ATOM   14284 O  O   . ARG   E 2 391 ? 24.840  3.122   -40.415 1.00 126.81 ? 391  ARG   E O   1 
ATOM   14285 C  CB  . ARG   E 2 391 ? 26.749  5.153   -38.603 1.00 127.47 ? 391  ARG   E CB  1 
ATOM   14286 C  CG  . ARG   E 2 391 ? 25.875  6.384   -38.366 1.00 131.52 ? 391  ARG   E CG  1 
ATOM   14287 C  CD  . ARG   E 2 391 ? 26.716  7.630   -38.498 1.00 136.01 ? 391  ARG   E CD  1 
ATOM   14288 N  NE  . ARG   E 2 391 ? 27.209  7.782   -39.865 1.00 139.62 ? 391  ARG   E NE  1 
ATOM   14289 C  CZ  . ARG   E 2 391 ? 26.515  8.320   -40.863 1.00 142.86 ? 391  ARG   E CZ  1 
ATOM   14290 N  NH1 . ARG   E 2 391 ? 25.278  8.759   -40.684 1.00 145.63 ? 391  ARG   E NH1 1 
ATOM   14291 N  NH2 . ARG   E 2 391 ? 27.069  8.415   -42.072 1.00 141.65 ? 391  ARG   E NH2 1 
ATOM   14292 N  N   . ASN   E 2 392 ? 23.738  4.432   -38.963 1.00 122.59 ? 392  ASN   E N   1 
ATOM   14293 C  CA  . ASN   E 2 392 ? 22.564  4.533   -39.809 1.00 121.59 ? 392  ASN   E CA  1 
ATOM   14294 C  C   . ASN   E 2 392 ? 22.669  5.726   -40.763 1.00 124.19 ? 392  ASN   E C   1 
ATOM   14295 O  O   . ASN   E 2 392 ? 21.882  5.863   -41.706 1.00 118.88 ? 392  ASN   E O   1 
ATOM   14296 C  CB  . ASN   E 2 392 ? 21.302  4.643   -38.954 1.00 120.78 ? 392  ASN   E CB  1 
ATOM   14297 C  CG  . ASN   E 2 392 ? 20.743  3.293   -38.562 1.00 116.87 ? 392  ASN   E CG  1 
ATOM   14298 O  OD1 . ASN   E 2 392 ? 20.166  2.587   -39.393 1.00 121.24 ? 392  ASN   E OD1 1 
ATOM   14299 N  ND2 . ASN   E 2 392 ? 20.889  2.933   -37.293 1.00 112.94 ? 392  ASN   E ND2 1 
ATOM   14300 N  N   . LEU   E 2 406 ? 22.342  1.120   -42.833 1.00 125.51 ? 710  LEU   E N   1 
ATOM   14301 C  CA  . LEU   E 2 406 ? 23.557  0.792   -42.081 1.00 128.01 ? 710  LEU   E CA  1 
ATOM   14302 C  C   . LEU   E 2 406 ? 24.808  0.904   -42.931 1.00 137.52 ? 710  LEU   E C   1 
ATOM   14303 O  O   . LEU   E 2 406 ? 24.824  0.420   -44.065 1.00 141.85 ? 710  LEU   E O   1 
ATOM   14304 C  CB  . LEU   E 2 406 ? 23.487  -0.618  -41.506 1.00 117.29 ? 710  LEU   E CB  1 
ATOM   14305 C  CG  . LEU   E 2 406 ? 22.897  -0.731  -40.101 1.00 112.48 ? 710  LEU   E CG  1 
ATOM   14306 C  CD1 . LEU   E 2 406 ? 23.327  -2.019  -39.453 1.00 92.75  ? 710  LEU   E CD1 1 
ATOM   14307 C  CD2 . LEU   E 2 406 ? 23.282  0.460   -39.236 1.00 122.11 ? 710  LEU   E CD2 1 
ATOM   14308 N  N   . HIS   E 2 407 ? 25.861  1.512   -42.373 1.00 146.23 ? 711  HIS   E N   1 
ATOM   14309 C  CA  . HIS   E 2 407 ? 27.087  1.807   -43.110 1.00 149.82 ? 711  HIS   E CA  1 
ATOM   14310 C  C   . HIS   E 2 407 ? 28.289  1.453   -42.243 1.00 145.44 ? 711  HIS   E C   1 
ATOM   14311 O  O   . HIS   E 2 407 ? 28.352  1.878   -41.087 1.00 143.65 ? 711  HIS   E O   1 
ATOM   14312 C  CB  . HIS   E 2 407 ? 27.124  3.289   -43.523 1.00 156.15 ? 711  HIS   E CB  1 
ATOM   14313 C  CG  . HIS   E 2 407 ? 25.777  3.851   -43.887 1.00 160.07 ? 711  HIS   E CG  1 
ATOM   14314 N  ND1 . HIS   E 2 407 ? 25.182  4.880   -43.186 1.00 161.33 ? 711  HIS   E ND1 1 
ATOM   14315 C  CD2 . HIS   E 2 407 ? 24.904  3.517   -44.870 1.00 159.29 ? 711  HIS   E CD2 1 
ATOM   14316 C  CE1 . HIS   E 2 407 ? 24.006  5.160   -43.724 1.00 160.76 ? 711  HIS   E CE1 1 
ATOM   14317 N  NE2 . HIS   E 2 407 ? 23.812  4.345   -44.746 1.00 160.58 ? 711  HIS   E NE2 1 
ATOM   14318 N  N   . ILE   E 2 408 ? 29.240  0.691   -42.802 1.00 119.16 ? 712  ILE   E N   1 
ATOM   14319 C  CA  . ILE   E 2 408 ? 30.303  0.010   -42.048 1.00 102.97 ? 712  ILE   E CA  1 
ATOM   14320 C  C   . ILE   E 2 408 ? 31.669  0.403   -42.602 1.00 95.47  ? 712  ILE   E C   1 
ATOM   14321 O  O   . ILE   E 2 408 ? 31.973  0.119   -43.767 1.00 97.16  ? 712  ILE   E O   1 
ATOM   14322 C  CB  . ILE   E 2 408 ? 30.156  -1.523  -42.101 1.00 100.99 ? 712  ILE   E CB  1 
ATOM   14323 C  CG1 . ILE   E 2 408 ? 28.868  -1.996  -41.421 1.00 105.88 ? 712  ILE   E CG1 1 
ATOM   14324 C  CG2 . ILE   E 2 408 ? 31.365  -2.205  -41.493 1.00 92.73  ? 712  ILE   E CG2 1 
ATOM   14325 C  CD1 . ILE   E 2 408 ? 27.897  -2.720  -42.371 1.00 111.61 ? 712  ILE   E CD1 1 
ATOM   14326 N  N   . ARG   E 2 409 ? 32.500  1.012   -41.758 1.00 89.45  ? 713  ARG   E N   1 
ATOM   14327 C  CA  . ARG   E 2 409 ? 33.891  1.331   -42.068 1.00 84.80  ? 713  ARG   E CA  1 
ATOM   14328 C  C   . ARG   E 2 409 ? 34.785  0.291   -41.408 1.00 81.36  ? 713  ARG   E C   1 
ATOM   14329 O  O   . ARG   E 2 409 ? 34.553  -0.085  -40.257 1.00 84.13  ? 713  ARG   E O   1 
ATOM   14330 C  CB  . ARG   E 2 409 ? 34.235  2.741   -41.564 1.00 90.03  ? 713  ARG   E CB  1 
ATOM   14331 C  CG  . ARG   E 2 409 ? 35.695  3.213   -41.697 1.00 90.87  ? 713  ARG   E CG  1 
ATOM   14332 C  CD  . ARG   E 2 409 ? 35.845  4.633   -41.146 1.00 90.69  ? 713  ARG   E CD  1 
ATOM   14333 N  NE  . ARG   E 2 409 ? 37.192  5.188   -41.268 1.00 98.30  ? 713  ARG   E NE  1 
ATOM   14334 C  CZ  . ARG   E 2 409 ? 37.556  6.376   -40.791 1.00 104.38 ? 713  ARG   E CZ  1 
ATOM   14335 N  NH1 . ARG   E 2 409 ? 36.707  7.143   -40.125 1.00 107.10 ? 713  ARG   E NH1 1 
ATOM   14336 N  NH2 . ARG   E 2 409 ? 38.799  6.815   -40.995 1.00 102.08 ? 713  ARG   E NH2 1 
ATOM   14337 N  N   . THR   E 2 410 ? 35.785  -0.194  -42.133 1.00 77.52  ? 714  THR   E N   1 
ATOM   14338 C  CA  . THR   E 2 410 ? 36.604  -1.299  -41.650 1.00 76.48  ? 714  THR   E CA  1 
ATOM   14339 C  C   . THR   E 2 410 ? 38.024  -0.836  -41.396 1.00 75.33  ? 714  THR   E C   1 
ATOM   14340 O  O   . THR   E 2 410 ? 38.655  -0.268  -42.289 1.00 80.26  ? 714  THR   E O   1 
ATOM   14341 C  CB  . THR   E 2 410 ? 36.657  -2.443  -42.657 1.00 81.55  ? 714  THR   E CB  1 
ATOM   14342 O  OG1 . THR   E 2 410 ? 35.385  -3.105  -42.726 1.00 86.78  ? 714  THR   E OG1 1 
ATOM   14343 C  CG2 . THR   E 2 410 ? 37.759  -3.423  -42.269 1.00 78.50  ? 714  THR   E CG2 1 
ATOM   14344 N  N   . VAL   E 2 411 ? 38.523  -1.091  -40.192 1.00 75.05  ? 715  VAL   E N   1 
ATOM   14345 C  CA  . VAL   E 2 411 ? 39.908  -0.808  -39.825 1.00 75.19  ? 715  VAL   E CA  1 
ATOM   14346 C  C   . VAL   E 2 411 ? 40.608  -2.148  -39.680 1.00 75.86  ? 715  VAL   E C   1 
ATOM   14347 O  O   . VAL   E 2 411 ? 40.490  -2.800  -38.638 1.00 78.69  ? 715  VAL   E O   1 
ATOM   14348 C  CB  . VAL   E 2 411 ? 40.018  0.010   -38.519 1.00 74.84  ? 715  VAL   E CB  1 
ATOM   14349 C  CG1 . VAL   E 2 411 ? 41.424  0.460   -38.304 1.00 75.07  ? 715  VAL   E CG1 1 
ATOM   14350 C  CG2 . VAL   E 2 411 ? 39.131  1.221   -38.557 1.00 74.67  ? 715  VAL   E CG2 1 
ATOM   14351 N  N   . PRO   E 2 412 ? 41.300  -2.619  -40.702 1.00 77.75  ? 716  PRO   E N   1 
ATOM   14352 C  CA  . PRO   E 2 412 ? 42.131  -3.816  -40.533 1.00 81.48  ? 716  PRO   E CA  1 
ATOM   14353 C  C   . PRO   E 2 412 ? 43.215  -3.572  -39.499 1.00 83.29  ? 716  PRO   E C   1 
ATOM   14354 O  O   . PRO   E 2 412 ? 43.825  -2.497  -39.448 1.00 83.36  ? 716  PRO   E O   1 
ATOM   14355 C  CB  . PRO   E 2 412 ? 42.724  -4.033  -41.927 1.00 86.66  ? 716  PRO   E CB  1 
ATOM   14356 C  CG  . PRO   E 2 412 ? 42.738  -2.655  -42.520 1.00 85.49  ? 716  PRO   E CG  1 
ATOM   14357 C  CD  . PRO   E 2 412 ? 41.470  -2.016  -42.029 1.00 80.79  ? 716  PRO   E CD  1 
ATOM   14358 N  N   . LEU   E 2 413 ? 43.430  -4.587  -38.651 1.00 84.12  ? 717  LEU   E N   1 
ATOM   14359 C  CA  . LEU   E 2 413 ? 44.489  -4.583  -37.653 1.00 82.09  ? 717  LEU   E CA  1 
ATOM   14360 C  C   . LEU   E 2 413 ? 45.472  -5.726  -37.822 1.00 81.83  ? 717  LEU   E C   1 
ATOM   14361 O  O   . LEU   E 2 413 ? 46.573  -5.658  -37.264 1.00 83.04  ? 717  LEU   E O   1 
ATOM   14362 C  CB  . LEU   E 2 413 ? 43.887  -4.637  -36.240 1.00 76.50  ? 717  LEU   E CB  1 
ATOM   14363 C  CG  . LEU   E 2 413 ? 43.021  -3.408  -35.949 1.00 74.88  ? 717  LEU   E CG  1 
ATOM   14364 C  CD1 . LEU   E 2 413 ? 41.744  -3.718  -35.212 1.00 74.43  ? 717  LEU   E CD1 1 
ATOM   14365 C  CD2 . LEU   E 2 413 ? 43.823  -2.355  -35.216 1.00 74.88  ? 717  LEU   E CD2 1 
ATOM   14366 N  N   . TYR   E 2 414 ? 45.103  -6.776  -38.550 1.00 83.89  ? 718  TYR   E N   1 
ATOM   14367 C  CA  . TYR   E 2 414 ? 45.987  -7.890  -38.873 1.00 84.66  ? 718  TYR   E CA  1 
ATOM   14368 C  C   . TYR   E 2 414 ? 46.409  -8.692  -37.647 1.00 83.45  ? 718  TYR   E C   1 
ATOM   14369 O  O   . TYR   E 2 414 ? 47.348  -9.504  -37.730 1.00 81.51  ? 718  TYR   E O   1 
ATOM   14370 C  CB  . TYR   E 2 414 ? 47.201  -7.372  -39.639 1.00 87.30  ? 718  TYR   E CB  1 
ATOM   14371 C  CG  . TYR   E 2 414 ? 46.803  -6.656  -40.922 1.00 83.97  ? 718  TYR   E CG  1 
ATOM   14372 C  CD1 . TYR   E 2 414 ? 45.891  -7.230  -41.800 1.00 87.28  ? 718  TYR   E CD1 1 
ATOM   14373 C  CD2 . TYR   E 2 414 ? 47.327  -5.423  -41.249 1.00 80.10  ? 718  TYR   E CD2 1 
ATOM   14374 C  CE1 . TYR   E 2 414 ? 45.529  -6.601  -42.970 1.00 84.56  ? 718  TYR   E CE1 1 
ATOM   14375 C  CE2 . TYR   E 2 414 ? 46.971  -4.791  -42.412 1.00 84.05  ? 718  TYR   E CE2 1 
ATOM   14376 C  CZ  . TYR   E 2 414 ? 46.069  -5.381  -43.274 1.00 83.96  ? 718  TYR   E CZ  1 
ATOM   14377 O  OH  . TYR   E 2 414 ? 45.707  -4.747  -44.452 1.00 85.66  ? 718  TYR   E OH  1 
ATOM   14378 N  N   . GLU   E 2 415 ? 45.733  -8.457  -36.515 1.00 82.85  ? 719  GLU   E N   1 
ATOM   14379 C  CA  . GLU   E 2 415 ? 45.851  -9.200  -35.267 1.00 82.15  ? 719  GLU   E CA  1 
ATOM   14380 C  C   . GLU   E 2 415 ? 44.504  -9.116  -34.556 1.00 79.59  ? 719  GLU   E C   1 
ATOM   14381 O  O   . GLU   E 2 415 ? 43.633  -8.333  -34.937 1.00 78.31  ? 719  GLU   E O   1 
ATOM   14382 C  CB  . GLU   E 2 415 ? 46.980  -8.651  -34.391 1.00 82.07  ? 719  GLU   E CB  1 
ATOM   14383 C  CG  . GLU   E 2 415 ? 46.705  -7.288  -33.805 1.00 81.57  ? 719  GLU   E CG  1 
ATOM   14384 C  CD  . GLU   E 2 415 ? 47.909  -6.738  -33.087 1.00 86.68  ? 719  GLU   E CD  1 
ATOM   14385 O  OE1 . GLU   E 2 415 ? 48.944  -6.518  -33.748 1.00 90.96  ? 719  GLU   E OE1 1 
ATOM   14386 O  OE2 . GLU   E 2 415 ? 47.841  -6.545  -31.854 1.00 89.60  ? 719  GLU   E OE2 1 
ATOM   14387 N  N   . SER   E 2 416 ? 44.335  -9.917  -33.507 1.00 80.05  ? 720  SER   E N   1 
ATOM   14388 C  CA  . SER   E 2 416 ? 43.011  -10.074 -32.902 1.00 78.15  ? 720  SER   E CA  1 
ATOM   14389 C  C   . SER   E 2 416 ? 42.733  -8.942  -31.909 1.00 77.39  ? 720  SER   E C   1 
ATOM   14390 O  O   . SER   E 2 416 ? 43.494  -8.778  -30.947 1.00 78.50  ? 720  SER   E O   1 
ATOM   14391 C  CB  . SER   E 2 416 ? 42.917  -11.439 -32.213 1.00 77.72  ? 720  SER   E CB  1 
ATOM   14392 O  OG  . SER   E 2 416 ? 43.251  -12.495 -33.109 1.00 79.34  ? 720  SER   E OG  1 
ATOM   14393 N  N   . PRO   E 2 417 ? 41.687  -8.125  -32.114 1.00 74.57  ? 721  PRO   E N   1 
ATOM   14394 C  CA  . PRO   E 2 417 ? 41.222  -7.245  -31.039 1.00 73.63  ? 721  PRO   E CA  1 
ATOM   14395 C  C   . PRO   E 2 417 ? 40.320  -7.999  -30.079 1.00 76.55  ? 721  PRO   E C   1 
ATOM   14396 O  O   . PRO   E 2 417 ? 39.457  -8.780  -30.496 1.00 77.77  ? 721  PRO   E O   1 
ATOM   14397 C  CB  . PRO   E 2 417 ? 40.439  -6.161  -31.779 1.00 73.56  ? 721  PRO   E CB  1 
ATOM   14398 C  CG  . PRO   E 2 417 ? 39.917  -6.859  -32.950 1.00 74.16  ? 721  PRO   E CG  1 
ATOM   14399 C  CD  . PRO   E 2 417 ? 40.997  -7.818  -33.378 1.00 74.95  ? 721  PRO   E CD  1 
ATOM   14400 N  N   . ARG   E 2 418 ? 40.518  -7.742  -28.785 1.00 74.15  ? 722  ARG   E N   1 
ATOM   14401 C  CA  . ARG   E 2 418 ? 39.790  -8.403  -27.709 1.00 73.35  ? 722  ARG   E CA  1 
ATOM   14402 C  C   . ARG   E 2 418 ? 38.821  -7.489  -26.966 1.00 79.35  ? 722  ARG   E C   1 
ATOM   14403 O  O   . ARG   E 2 418 ? 37.643  -7.853  -26.834 1.00 79.98  ? 722  ARG   E O   1 
ATOM   14404 C  CB  . ARG   E 2 418 ? 40.785  -9.020  -26.728 1.00 76.41  ? 722  ARG   E CB  1 
ATOM   14405 C  CG  . ARG   E 2 418 ? 41.763  -10.006 -27.378 1.00 81.09  ? 722  ARG   E CG  1 
ATOM   14406 C  CD  . ARG   E 2 418 ? 41.068  -11.202 -28.010 1.00 84.88  ? 722  ARG   E CD  1 
ATOM   14407 N  NE  . ARG   E 2 418 ? 40.210  -11.918 -27.066 1.00 86.31  ? 722  ARG   E NE  1 
ATOM   14408 C  CZ  . ARG   E 2 418 ? 39.239  -12.756 -27.415 1.00 79.87  ? 722  ARG   E CZ  1 
ATOM   14409 N  NH1 . ARG   E 2 418 ? 38.964  -13.014 -28.688 1.00 80.50  ? 722  ARG   E NH1 1 
ATOM   14410 N  NH2 . ARG   E 2 418 ? 38.520  -13.343 -26.465 1.00 78.92  ? 722  ARG   E NH2 1 
ATOM   14411 N  N   . LYS   E 2 419 ? 39.249  -6.311  -26.485 1.00 75.43  ? 723  LYS   E N   1 
ATOM   14412 C  CA  . LYS   E 2 419 ? 38.328  -5.413  -25.783 1.00 77.85  ? 723  LYS   E CA  1 
ATOM   14413 C  C   . LYS   E 2 419 ? 38.571  -3.967  -26.190 1.00 80.89  ? 723  LYS   E C   1 
ATOM   14414 O  O   . LYS   E 2 419 ? 39.676  -3.600  -26.583 1.00 83.19  ? 723  LYS   E O   1 
ATOM   14415 C  CB  . LYS   E 2 419 ? 38.452  -5.538  -24.262 1.00 80.52  ? 723  LYS   E CB  1 
ATOM   14416 C  CG  . LYS   E 2 419 ? 38.335  -6.966  -23.696 1.00 78.87  ? 723  LYS   E CG  1 
ATOM   14417 C  CD  . LYS   E 2 419 ? 36.902  -7.406  -23.508 1.00 79.49  ? 723  LYS   E CD  1 
ATOM   14418 C  CE  . LYS   E 2 419 ? 36.816  -8.852  -23.049 1.00 81.84  ? 723  LYS   E CE  1 
ATOM   14419 N  NZ  . LYS   E 2 419 ? 35.522  -9.137  -22.343 1.00 92.52  ? 723  LYS   E NZ  1 
ATOM   14420 N  N   . ILE   E 2 420 ? 37.524  -3.131  -26.066 1.00 84.36  ? 724  ILE   E N   1 
ATOM   14421 C  CA  . ILE   E 2 420 ? 37.510  -1.768  -26.606 1.00 85.08  ? 724  ILE   E CA  1 
ATOM   14422 C  C   . ILE   E 2 420 ? 36.771  -0.804  -25.680 1.00 89.88  ? 724  ILE   E C   1 
ATOM   14423 O  O   . ILE   E 2 420 ? 35.778  -1.156  -25.032 1.00 89.86  ? 724  ILE   E O   1 
ATOM   14424 C  CB  . ILE   E 2 420 ? 36.862  -1.701  -28.016 1.00 85.69  ? 724  ILE   E CB  1 
ATOM   14425 C  CG1 . ILE   E 2 420 ? 37.235  -0.408  -28.730 1.00 85.66  ? 724  ILE   E CG1 1 
ATOM   14426 C  CG2 . ILE   E 2 420 ? 35.333  -1.773  -27.941 1.00 83.95  ? 724  ILE   E CG2 1 
ATOM   14427 C  CD1 . ILE   E 2 420 ? 36.655  -0.302  -30.112 1.00 82.38  ? 724  ILE   E CD1 1 
ATOM   14428 N  N   . CYS   E 2 421 ? 37.242  0.442   -25.667 1.00 98.61  ? 725  CYS   E N   1 
ATOM   14429 C  CA  . CYS   E 2 421 ? 36.636  1.518   -24.893 1.00 98.60  ? 725  CYS   E CA  1 
ATOM   14430 C  C   . CYS   E 2 421 ? 37.040  2.846   -25.516 1.00 100.15 ? 725  CYS   E C   1 
ATOM   14431 O  O   . CYS   E 2 421 ? 38.033  2.931   -26.250 1.00 98.40  ? 725  CYS   E O   1 
ATOM   14432 C  CB  . CYS   E 2 421 ? 37.089  1.483   -23.441 1.00 95.56  ? 725  CYS   E CB  1 
ATOM   14433 S  SG  . CYS   E 2 421 ? 38.835  1.921   -23.408 1.00 100.66 ? 725  CYS   E SG  1 
ATOM   14434 N  N   . TYR   E 2 422 ? 36.287  3.894   -25.174 1.00 95.26  ? 726  TYR   E N   1 
ATOM   14435 C  CA  . TYR   E 2 422 ? 36.440  5.209   -25.777 1.00 93.49  ? 726  TYR   E CA  1 
ATOM   14436 C  C   . TYR   E 2 422 ? 36.723  6.264   -24.720 1.00 98.04  ? 726  TYR   E C   1 
ATOM   14437 O  O   . TYR   E 2 422 ? 36.061  6.307   -23.679 1.00 100.41 ? 726  TYR   E O   1 
ATOM   14438 C  CB  . TYR   E 2 422 ? 35.195  5.589   -26.548 1.00 91.97  ? 726  TYR   E CB  1 
ATOM   14439 C  CG  . TYR   E 2 422 ? 35.254  6.957   -27.163 1.00 93.78  ? 726  TYR   E CG  1 
ATOM   14440 C  CD1 . TYR   E 2 422 ? 36.193  7.255   -28.137 1.00 95.44  ? 726  TYR   E CD1 1 
ATOM   14441 C  CD2 . TYR   E 2 422 ? 34.361  7.953   -26.783 1.00 97.52  ? 726  TYR   E CD2 1 
ATOM   14442 C  CE1 . TYR   E 2 422 ? 36.249  8.519   -28.724 1.00 98.34  ? 726  TYR   E CE1 1 
ATOM   14443 C  CE2 . TYR   E 2 422 ? 34.406  9.223   -27.362 1.00 97.34  ? 726  TYR   E CE2 1 
ATOM   14444 C  CZ  . TYR   E 2 422 ? 35.354  9.500   -28.335 1.00 98.00  ? 726  TYR   E CZ  1 
ATOM   14445 O  OH  . TYR   E 2 422 ? 35.421  10.748  -28.921 1.00 100.53 ? 726  TYR   E OH  1 
ATOM   14446 N  N   . GLN   E 2 423 ? 37.696  7.128   -25.014 1.00 98.49  ? 727  GLN   E N   1 
ATOM   14447 C  CA  . GLN   E 2 423 ? 38.189  8.151   -24.097 1.00 99.57  ? 727  GLN   E CA  1 
ATOM   14448 C  C   . GLN   E 2 423 ? 38.010  9.492   -24.800 1.00 104.53 ? 727  GLN   E C   1 
ATOM   14449 O  O   . GLN   E 2 423 ? 38.877  9.891   -25.590 1.00 105.27 ? 727  GLN   E O   1 
ATOM   14450 C  CB  . GLN   E 2 423 ? 39.655  7.892   -23.739 1.00 100.29 ? 727  GLN   E CB  1 
ATOM   14451 C  CG  . GLN   E 2 423 ? 40.249  8.861   -22.732 1.00 103.61 ? 727  GLN   E CG  1 
ATOM   14452 C  CD  . GLN   E 2 423 ? 41.358  8.232   -21.893 1.00 104.74 ? 727  GLN   E CD  1 
ATOM   14453 O  OE1 . GLN   E 2 423 ? 42.539  8.591   -22.009 1.00 108.55 ? 727  GLN   E OE1 1 
ATOM   14454 N  NE2 . GLN   E 2 423 ? 40.975  7.297   -21.025 1.00 105.08 ? 727  GLN   E NE2 1 
ATOM   14455 N  N   . GLU   E 2 424 ? 36.884  10.175  -24.529 1.00 106.37 ? 728  GLU   E N   1 
ATOM   14456 C  CA  . GLU   E 2 424 ? 36.608  11.455  -25.184 1.00 105.13 ? 728  GLU   E CA  1 
ATOM   14457 C  C   . GLU   E 2 424 ? 37.692  12.482  -24.859 1.00 106.89 ? 728  GLU   E C   1 
ATOM   14458 O  O   . GLU   E 2 424 ? 38.246  13.123  -25.757 1.00 106.96 ? 728  GLU   E O   1 
ATOM   14459 C  CB  . GLU   E 2 424 ? 35.225  11.970  -24.780 1.00 99.45  ? 728  GLU   E CB  1 
ATOM   14460 N  N   . VAL   E 2 425 ? 38.022  12.629  -23.577 1.00 106.32 ? 729  VAL   E N   1 
ATOM   14461 C  CA  . VAL   E 2 425 ? 39.113  13.476  -23.093 1.00 108.29 ? 729  VAL   E CA  1 
ATOM   14462 C  C   . VAL   E 2 425 ? 40.374  13.366  -23.949 1.00 111.25 ? 729  VAL   E C   1 
ATOM   14463 O  O   . VAL   E 2 425 ? 41.064  14.367  -24.176 1.00 117.89 ? 729  VAL   E O   1 
ATOM   14464 C  CB  . VAL   E 2 425 ? 39.445  13.124  -21.630 1.00 112.26 ? 729  VAL   E CB  1 
ATOM   14465 C  CG1 . VAL   E 2 425 ? 40.921  13.435  -21.290 1.00 113.79 ? 729  VAL   E CG1 1 
ATOM   14466 C  CG2 . VAL   E 2 425 ? 38.499  13.837  -20.688 1.00 110.84 ? 729  VAL   E CG2 1 
ATOM   14467 N  N   . SER   E 2 426 ? 40.711  12.162  -24.400 1.00 111.54 ? 730  SER   E N   1 
ATOM   14468 C  CA  . SER   E 2 426 ? 41.869  11.973  -25.255 1.00 110.44 ? 730  SER   E CA  1 
ATOM   14469 C  C   . SER   E 2 426 ? 41.507  11.879  -26.729 1.00 109.37 ? 730  SER   E C   1 
ATOM   14470 O  O   . SER   E 2 426 ? 42.407  11.841  -27.564 1.00 110.55 ? 730  SER   E O   1 
ATOM   14471 C  CB  . SER   E 2 426 ? 42.637  10.725  -24.838 1.00 115.35 ? 730  SER   E CB  1 
ATOM   14472 O  OG  . SER   E 2 426 ? 43.056  10.818  -23.486 1.00 123.27 ? 730  SER   E OG  1 
ATOM   14473 N  N   . GLN   E 2 427 ? 40.215  11.827  -27.063 1.00 115.18 ? 731  GLN   E N   1 
ATOM   14474 C  CA  . GLN   E 2 427 ? 39.759  11.731  -28.459 1.00 117.75 ? 731  GLN   E CA  1 
ATOM   14475 C  C   . GLN   E 2 427 ? 40.294  10.478  -29.147 1.00 117.30 ? 731  GLN   E C   1 
ATOM   14476 O  O   . GLN   E 2 427 ? 40.593  10.472  -30.343 1.00 115.48 ? 731  GLN   E O   1 
ATOM   14477 C  CB  . GLN   E 2 427 ? 40.146  12.977  -29.262 1.00 119.32 ? 731  GLN   E CB  1 
ATOM   14478 C  CG  . GLN   E 2 427 ? 39.374  14.235  -28.944 1.00 121.11 ? 731  GLN   E CG  1 
ATOM   14479 C  CD  . GLN   E 2 427 ? 37.900  14.082  -29.242 1.00 125.11 ? 731  GLN   E CD  1 
ATOM   14480 O  OE1 . GLN   E 2 427 ? 37.468  14.207  -30.392 1.00 127.18 ? 731  GLN   E OE1 1 
ATOM   14481 N  NE2 . GLN   E 2 427 ? 37.113  13.797  -28.205 1.00 126.46 ? 731  GLN   E NE2 1 
ATOM   14482 N  N   . CYS   E 2 428 ? 40.399  9.392   -28.389 1.00 107.20 ? 732  CYS   E N   1 
ATOM   14483 C  CA  . CYS   E 2 428 ? 40.954  8.166   -28.921 1.00 98.82  ? 732  CYS   E CA  1 
ATOM   14484 C  C   . CYS   E 2 428 ? 40.277  6.978   -28.259 1.00 94.10  ? 732  CYS   E C   1 
ATOM   14485 O  O   . CYS   E 2 428 ? 39.520  7.111   -27.291 1.00 92.86  ? 732  CYS   E O   1 
ATOM   14486 C  CB  . CYS   E 2 428 ? 42.464  8.110   -28.716 1.00 98.18  ? 732  CYS   E CB  1 
ATOM   14487 S  SG  . CYS   E 2 428 ? 42.891  7.812   -27.009 1.00 117.38 ? 732  CYS   E SG  1 
ATOM   14488 N  N   . PHE   E 2 429 ? 40.553  5.810   -28.814 1.00 94.06  ? 733  PHE   E N   1 
ATOM   14489 C  CA  . PHE   E 2 429 ? 40.022  4.551   -28.324 1.00 91.68  ? 733  PHE   E CA  1 
ATOM   14490 C  C   . PHE   E 2 429 ? 41.141  3.743   -27.689 1.00 96.24  ? 733  PHE   E C   1 
ATOM   14491 O  O   . PHE   E 2 429 ? 42.288  3.786   -28.153 1.00 94.34  ? 733  PHE   E O   1 
ATOM   14492 C  CB  . PHE   E 2 429 ? 39.413  3.734   -29.454 1.00 89.67  ? 733  PHE   E CB  1 
ATOM   14493 C  CG  . PHE   E 2 429 ? 38.127  4.262   -29.969 1.00 92.92  ? 733  PHE   E CG  1 
ATOM   14494 C  CD1 . PHE   E 2 429 ? 38.097  5.141   -31.049 1.00 95.70  ? 733  PHE   E CD1 1 
ATOM   14495 C  CD2 . PHE   E 2 429 ? 36.938  3.875   -29.389 1.00 91.55  ? 733  PHE   E CD2 1 
ATOM   14496 C  CE1 . PHE   E 2 429 ? 36.890  5.617   -31.544 1.00 89.66  ? 733  PHE   E CE1 1 
ATOM   14497 C  CE2 . PHE   E 2 429 ? 35.735  4.337   -29.874 1.00 89.77  ? 733  PHE   E CE2 1 
ATOM   14498 C  CZ  . PHE   E 2 429 ? 35.707  5.207   -30.950 1.00 89.98  ? 733  PHE   E CZ  1 
ATOM   14499 N  N   . GLY   E 2 430 ? 40.803  2.995   -26.632 1.00 97.05  ? 734  GLY   E N   1 
ATOM   14500 C  CA  . GLY   E 2 430 ? 41.699  2.011   -26.069 1.00 95.12  ? 734  GLY   E CA  1 
ATOM   14501 C  C   . GLY   E 2 430 ? 41.303  0.610   -26.501 1.00 94.79  ? 734  GLY   E C   1 
ATOM   14502 O  O   . GLY   E 2 430 ? 40.199  0.153   -26.200 1.00 94.67  ? 734  GLY   E O   1 
ATOM   14503 N  N   . VAL   E 2 431 ? 42.207  -0.117  -27.145 1.00 84.45  ? 735  VAL   E N   1 
ATOM   14504 C  CA  . VAL   E 2 431 ? 41.881  -1.449  -27.622 1.00 83.19  ? 735  VAL   E CA  1 
ATOM   14505 C  C   . VAL   E 2 431 ? 42.940  -2.436  -27.139 1.00 81.38  ? 735  VAL   E C   1 
ATOM   14506 O  O   . VAL   E 2 431 ? 44.140  -2.159  -27.238 1.00 83.91  ? 735  VAL   E O   1 
ATOM   14507 C  CB  . VAL   E 2 431 ? 41.766  -1.486  -29.163 1.00 84.60  ? 735  VAL   E CB  1 
ATOM   14508 C  CG1 . VAL   E 2 431 ? 41.683  -2.923  -29.648 1.00 84.91  ? 735  VAL   E CG1 1 
ATOM   14509 C  CG2 . VAL   E 2 431 ? 40.554  -0.735  -29.632 1.00 82.60  ? 735  VAL   E CG2 1 
ATOM   14510 N  N   . LEU   E 2 432 ? 42.495  -3.570  -26.604 1.00 79.44  ? 736  LEU   E N   1 
ATOM   14511 C  CA  . LEU   E 2 432 ? 43.381  -4.654  -26.200 1.00 78.05  ? 736  LEU   E CA  1 
ATOM   14512 C  C   . LEU   E 2 432 ? 43.490  -5.663  -27.333 1.00 78.44  ? 736  LEU   E C   1 
ATOM   14513 O  O   . LEU   E 2 432 ? 42.485  -6.052  -27.927 1.00 81.52  ? 736  LEU   E O   1 
ATOM   14514 C  CB  . LEU   E 2 432 ? 42.866  -5.357  -24.933 1.00 77.89  ? 736  LEU   E CB  1 
ATOM   14515 C  CG  . LEU   E 2 432 ? 42.994  -4.696  -23.552 1.00 76.53  ? 736  LEU   E CG  1 
ATOM   14516 C  CD1 . LEU   E 2 432 ? 42.515  -5.620  -22.403 1.00 76.61  ? 736  LEU   E CD1 1 
ATOM   14517 C  CD2 . LEU   E 2 432 ? 44.425  -4.200  -23.326 1.00 79.52  ? 736  LEU   E CD2 1 
ATOM   14518 N  N   . SER   E 2 433 ? 44.714  -6.091  -27.625 1.00 79.11  ? 737  SER   E N   1 
ATOM   14519 C  CA  . SER   E 2 433 ? 44.974  -6.951  -28.761 1.00 79.31  ? 737  SER   E CA  1 
ATOM   14520 C  C   . SER   E 2 433 ? 45.888  -8.087  -28.342 1.00 82.55  ? 737  SER   E C   1 
ATOM   14521 O  O   . SER   E 2 433 ? 46.532  -8.037  -27.289 1.00 84.40  ? 737  SER   E O   1 
ATOM   14522 C  CB  . SER   E 2 433 ? 45.624  -6.174  -29.904 1.00 81.34  ? 737  SER   E CB  1 
ATOM   14523 O  OG  . SER   E 2 433 ? 46.957  -5.806  -29.566 1.00 81.82  ? 737  SER   E OG  1 
ATOM   14524 N  N   . SER   E 2 434 ? 45.932  -9.117  -29.190 1.00 81.06  ? 738  SER   E N   1 
ATOM   14525 C  CA  . SER   E 2 434 ? 46.881  -10.212 -29.028 1.00 82.00  ? 738  SER   E CA  1 
ATOM   14526 C  C   . SER   E 2 434 ? 47.405  -10.599 -30.397 1.00 83.02  ? 738  SER   E C   1 
ATOM   14527 O  O   . SER   E 2 434 ? 46.636  -10.735 -31.356 1.00 83.67  ? 738  SER   E O   1 
ATOM   14528 C  CB  . SER   E 2 434 ? 46.257  -11.425 -28.321 1.00 85.89  ? 738  SER   E CB  1 
ATOM   14529 O  OG  . SER   E 2 434 ? 45.163  -11.990 -29.034 1.00 91.12  ? 738  SER   E OG  1 
ATOM   14530 N  N   . ARG   E 2 435 ? 48.719  -10.752 -30.477 1.00 85.16  ? 739  ARG   E N   1 
ATOM   14531 C  CA  . ARG   E 2 435 ? 49.414  -11.064 -31.714 1.00 86.92  ? 739  ARG   E CA  1 
ATOM   14532 C  C   . ARG   E 2 435 ? 50.102  -12.400 -31.523 1.00 88.18  ? 739  ARG   E C   1 
ATOM   14533 O  O   . ARG   E 2 435 ? 50.516  -12.738 -30.416 1.00 90.81  ? 739  ARG   E O   1 
ATOM   14534 C  CB  . ARG   E 2 435 ? 50.422  -9.964  -32.058 1.00 86.56  ? 739  ARG   E CB  1 
ATOM   14535 C  CG  . ARG   E 2 435 ? 51.395  -10.254 -33.181 1.00 94.37  ? 739  ARG   E CG  1 
ATOM   14536 C  CD  . ARG   E 2 435 ? 52.515  -9.219  -33.150 1.00 98.19  ? 739  ARG   E CD  1 
ATOM   14537 N  NE  . ARG   E 2 435 ? 53.371  -9.321  -31.969 1.00 98.25  ? 739  ARG   E NE  1 
ATOM   14538 C  CZ  . ARG   E 2 435 ? 53.833  -8.285  -31.280 1.00 94.92  ? 739  ARG   E CZ  1 
ATOM   14539 N  NH1 . ARG   E 2 435 ? 53.431  -7.055  -31.534 1.00 100.80 ? 739  ARG   E NH1 1 
ATOM   14540 N  NH2 . ARG   E 2 435 ? 54.729  -8.487  -30.322 1.00 95.42  ? 739  ARG   E NH2 1 
ATOM   14541 N  N   . ILE   E 2 436 ? 50.176  -13.187 -32.574 1.00 90.28  ? 740  ILE   E N   1 
ATOM   14542 C  CA  . ILE   E 2 436 ? 50.768  -14.506 -32.472 1.00 93.87  ? 740  ILE   E CA  1 
ATOM   14543 C  C   . ILE   E 2 436 ? 52.138  -14.447 -33.124 1.00 99.49  ? 740  ILE   E C   1 
ATOM   14544 O  O   . ILE   E 2 436 ? 52.280  -14.016 -34.276 1.00 98.02  ? 740  ILE   E O   1 
ATOM   14545 C  CB  . ILE   E 2 436 ? 49.881  -15.582 -33.105 1.00 94.54  ? 740  ILE   E CB  1 
ATOM   14546 C  CG1 . ILE   E 2 436 ? 48.485  -15.541 -32.459 1.00 93.93  ? 740  ILE   E CG1 1 
ATOM   14547 C  CG2 . ILE   E 2 436 ? 50.570  -16.957 -32.974 1.00 99.51  ? 740  ILE   E CG2 1 
ATOM   14548 C  CD1 . ILE   E 2 436 ? 47.511  -14.456 -33.019 1.00 91.56  ? 740  ILE   E CD1 1 
ATOM   14549 N  N   . GLU   E 2 437 ? 53.144  -14.831 -32.351 1.00 105.55 ? 741  GLU   E N   1 
ATOM   14550 C  CA  . GLU   E 2 437 ? 54.516  -14.948 -32.803 1.00 109.11 ? 741  GLU   E CA  1 
ATOM   14551 C  C   . GLU   E 2 437 ? 54.978  -16.380 -32.613 1.00 110.50 ? 741  GLU   E C   1 
ATOM   14552 O  O   . GLU   E 2 437 ? 54.405  -17.142 -31.835 1.00 112.12 ? 741  GLU   E O   1 
ATOM   14553 C  CB  . GLU   E 2 437 ? 55.435  -14.005 -32.031 1.00 111.18 ? 741  GLU   E CB  1 
ATOM   14554 C  CG  . GLU   E 2 437 ? 55.034  -12.553 -32.124 1.00 109.18 ? 741  GLU   E CG  1 
ATOM   14555 C  CD  . GLU   E 2 437 ? 56.174  -11.604 -31.787 1.00 111.71 ? 741  GLU   E CD  1 
ATOM   14556 O  OE1 . GLU   E 2 437 ? 57.206  -12.060 -31.248 1.00 113.00 ? 741  GLU   E OE1 1 
ATOM   14557 O  OE2 . GLU   E 2 437 ? 56.036  -10.398 -32.071 1.00 111.96 ? 741  GLU   E OE2 1 
ATOM   14558 N  N   . VAL   E 2 438 ? 56.027  -16.740 -33.333 1.00 111.27 ? 742  VAL   E N   1 
ATOM   14559 C  CA  . VAL   E 2 438 ? 56.646  -18.048 -33.221 1.00 118.62 ? 742  VAL   E CA  1 
ATOM   14560 C  C   . VAL   E 2 438 ? 58.041  -17.855 -32.658 1.00 124.25 ? 742  VAL   E C   1 
ATOM   14561 O  O   . VAL   E 2 438 ? 58.750  -16.926 -33.056 1.00 127.26 ? 742  VAL   E O   1 
ATOM   14562 C  CB  . VAL   E 2 438 ? 56.681  -18.761 -34.581 1.00 121.52 ? 742  VAL   E CB  1 
ATOM   14563 C  CG1 . VAL   E 2 438 ? 57.634  -19.945 -34.534 1.00 128.21 ? 742  VAL   E CG1 1 
ATOM   14564 C  CG2 . VAL   E 2 438 ? 55.289  -19.217 -34.947 1.00 121.07 ? 742  VAL   E CG2 1 
ATOM   14565 N  N   . GLN   E 2 439 ? 58.424  -18.711 -31.720 1.00 130.74 ? 743  GLN   E N   1 
ATOM   14566 C  CA  . GLN   E 2 439 ? 59.756  -18.679 -31.133 1.00 134.86 ? 743  GLN   E CA  1 
ATOM   14567 C  C   . GLN   E 2 439 ? 60.876  -18.686 -32.178 1.00 135.24 ? 743  GLN   E C   1 
ATOM   14568 O  O   . GLN   E 2 439 ? 61.058  -19.666 -32.904 1.00 135.74 ? 743  GLN   E O   1 
ATOM   14569 C  CB  . GLN   E 2 439 ? 59.933  -19.869 -30.198 1.00 141.23 ? 743  GLN   E CB  1 
ATOM   14570 C  CG  . GLN   E 2 439 ? 61.296  -19.930 -29.553 1.00 150.79 ? 743  GLN   E CG  1 
ATOM   14571 C  CD  . GLN   E 2 439 ? 61.373  -19.076 -28.315 1.00 150.49 ? 743  GLN   E CD  1 
ATOM   14572 O  OE1 . GLN   E 2 439 ? 60.815  -17.973 -28.262 1.00 139.52 ? 743  GLN   E OE1 1 
ATOM   14573 N  NE2 . GLN   E 2 439 ? 62.058  -19.587 -27.297 1.00 160.30 ? 743  GLN   E NE2 1 
ATOM   14574 N  N   . THR   E 2 441 ? 64.180  -18.405 -33.389 1.00 140.85 ? 745  THR   E N   1 
ATOM   14575 C  CA  . THR   E 2 441 ? 65.361  -19.251 -33.192 1.00 146.83 ? 745  THR   E CA  1 
ATOM   14576 C  C   . THR   E 2 441 ? 66.362  -18.645 -32.205 1.00 148.99 ? 745  THR   E C   1 
ATOM   14577 O  O   . THR   E 2 441 ? 66.874  -19.352 -31.335 1.00 151.96 ? 745  THR   E O   1 
ATOM   14578 C  CB  . THR   E 2 441 ? 66.121  -19.544 -34.528 1.00 146.24 ? 745  THR   E CB  1 
ATOM   14579 O  OG1 . THR   E 2 441 ? 66.394  -18.321 -35.222 1.00 147.45 ? 745  THR   E OG1 1 
ATOM   14580 C  CG2 . THR   E 2 441 ? 65.306  -20.452 -35.424 1.00 149.72 ? 745  THR   E CG2 1 
ATOM   14581 N  N   . SER   E 2 442 ? 66.646  -17.346 -32.341 1.00 147.46 ? 746  SER   E N   1 
ATOM   14582 C  CA  . SER   E 2 442 ? 67.697  -16.706 -31.545 1.00 146.77 ? 746  SER   E CA  1 
ATOM   14583 C  C   . SER   E 2 442 ? 67.184  -16.390 -30.138 1.00 145.50 ? 746  SER   E C   1 
ATOM   14584 O  O   . SER   E 2 442 ? 67.157  -15.241 -29.682 1.00 146.61 ? 746  SER   E O   1 
ATOM   14585 C  CB  . SER   E 2 442 ? 68.214  -15.451 -32.248 1.00 142.56 ? 746  SER   E CB  1 
ATOM   14586 O  OG  . SER   E 2 442 ? 67.214  -14.458 -32.329 1.00 145.77 ? 746  SER   E OG  1 
ATOM   14587 N  N   . GLY   E 2 443 ? 66.781  -17.453 -29.437 1.00 145.08 ? 747  GLY   E N   1 
ATOM   14588 C  CA  . GLY   E 2 443 ? 66.199  -17.350 -28.123 1.00 146.60 ? 747  GLY   E CA  1 
ATOM   14589 C  C   . GLY   E 2 443 ? 65.093  -16.320 -28.054 1.00 143.98 ? 747  GLY   E C   1 
ATOM   14590 O  O   . GLY   E 2 443 ? 64.985  -15.583 -27.068 1.00 142.50 ? 747  GLY   E O   1 
ATOM   14591 N  N   . GLY   E 2 444 ? 64.287  -16.221 -29.104 1.00 143.53 ? 748  GLY   E N   1 
ATOM   14592 C  CA  . GLY   E 2 444 ? 63.304  -15.157 -29.159 1.00 135.18 ? 748  GLY   E CA  1 
ATOM   14593 C  C   . GLY   E 2 444 ? 62.221  -15.448 -30.164 1.00 133.45 ? 748  GLY   E C   1 
ATOM   14594 O  O   . GLY   E 2 444 ? 62.401  -16.213 -31.117 1.00 134.00 ? 748  GLY   E O   1 
ATOM   14595 N  N   . THR   E 2 445 ? 61.091  -14.783 -29.944 1.00 131.42 ? 749  THR   E N   1 
ATOM   14596 C  CA  . THR   E 2 445 ? 59.927  -14.881 -30.808 1.00 124.11 ? 749  THR   E CA  1 
ATOM   14597 C  C   . THR   E 2 445 ? 59.980  -13.814 -31.893 1.00 120.13 ? 749  THR   E C   1 
ATOM   14598 O  O   . THR   E 2 445 ? 60.345  -12.661 -31.646 1.00 119.17 ? 749  THR   E O   1 
ATOM   14599 C  CB  . THR   E 2 445 ? 58.638  -14.716 -30.001 1.00 120.04 ? 749  THR   E CB  1 
ATOM   14600 O  OG1 . THR   E 2 445 ? 58.558  -13.376 -29.491 1.00 116.42 ? 749  THR   E OG1 1 
ATOM   14601 C  CG2 . THR   E 2 445 ? 58.599  -15.703 -28.844 1.00 124.82 ? 749  THR   E CG2 1 
ATOM   14602 N  N   . THR   E 2 446 ? 59.600  -14.211 -33.095 1.00 119.48 ? 750  THR   E N   1 
ATOM   14603 C  CA  . THR   E 2 446 ? 59.523  -13.332 -34.245 1.00 118.15 ? 750  THR   E CA  1 
ATOM   14604 C  C   . THR   E 2 446 ? 58.073  -13.271 -34.704 1.00 117.20 ? 750  THR   E C   1 
ATOM   14605 O  O   . THR   E 2 446 ? 57.371  -14.285 -34.687 1.00 118.42 ? 750  THR   E O   1 
ATOM   14606 C  CB  . THR   E 2 446 ? 60.435  -13.836 -35.380 1.00 121.57 ? 750  THR   E CB  1 
ATOM   14607 O  OG1 . THR   E 2 446 ? 60.428  -12.890 -36.455 1.00 131.69 ? 750  THR   E OG1 1 
ATOM   14608 C  CG2 . THR   E 2 446 ? 59.989  -15.218 -35.905 1.00 117.01 ? 750  THR   E CG2 1 
ATOM   14609 N  N   . ALA   E 2 447 ? 57.610  -12.083 -35.086 1.00 113.36 ? 751  ALA   E N   1 
ATOM   14610 C  CA  . ALA   E 2 447 ? 56.233  -11.958 -35.547 1.00 110.79 ? 751  ALA   E CA  1 
ATOM   14611 C  C   . ALA   E 2 447 ? 56.029  -12.725 -36.866 1.00 109.81 ? 751  ALA   E C   1 
ATOM   14612 O  O   . ALA   E 2 447 ? 56.983  -13.161 -37.523 1.00 106.19 ? 751  ALA   E O   1 
ATOM   14613 C  CB  . ALA   E 2 447 ? 55.856  -10.485 -35.699 1.00 110.49 ? 751  ALA   E CB  1 
ATOM   14614 N  N   . LEU   E 2 448 ? 54.754  -12.901 -37.250 1.00 108.96 ? 752  LEU   E N   1 
ATOM   14615 C  CA  . LEU   E 2 448 ? 54.393  -13.627 -38.465 1.00 101.77 ? 752  LEU   E CA  1 
ATOM   14616 C  C   . LEU   E 2 448 ? 53.918  -12.737 -39.591 1.00 97.79  ? 752  LEU   E C   1 
ATOM   14617 O  O   . LEU   E 2 448 ? 53.987  -13.151 -40.749 1.00 94.39  ? 752  LEU   E O   1 
ATOM   14618 C  CB  . LEU   E 2 448 ? 53.279  -14.649 -38.179 1.00 103.00 ? 752  LEU   E CB  1 
ATOM   14619 C  CG  . LEU   E 2 448 ? 53.373  -15.605 -36.980 1.00 106.69 ? 752  LEU   E CG  1 
ATOM   14620 C  CD1 . LEU   E 2 448 ? 52.203  -16.573 -36.988 1.00 104.10 ? 752  LEU   E CD1 1 
ATOM   14621 C  CD2 . LEU   E 2 448 ? 54.685  -16.380 -36.938 1.00 108.49 ? 752  LEU   E CD2 1 
ATOM   14622 N  N   . ARG   E 2 449 ? 53.425  -11.532 -39.281 1.00 100.57 ? 753  ARG   E N   1 
ATOM   14623 C  CA  . ARG   E 2 449 ? 52.771  -10.617 -40.201 1.00 100.23 ? 753  ARG   E CA  1 
ATOM   14624 C  C   . ARG   E 2 449 ? 52.778  -9.238  -39.556 1.00 101.05 ? 753  ARG   E C   1 
ATOM   14625 O  O   . ARG   E 2 449 ? 52.666  -9.142  -38.323 1.00 103.37 ? 753  ARG   E O   1 
ATOM   14626 C  CB  . ARG   E 2 449 ? 51.336  -11.056 -40.522 1.00 101.12 ? 753  ARG   E CB  1 
ATOM   14627 C  CG  . ARG   E 2 449 ? 50.411  -11.046 -39.305 1.00 101.26 ? 753  ARG   E CG  1 
ATOM   14628 C  CD  . ARG   E 2 449 ? 49.067  -11.654 -39.595 1.00 97.66  ? 753  ARG   E CD  1 
ATOM   14629 N  NE  . ARG   E 2 449 ? 49.074  -13.110 -39.512 1.00 98.14  ? 753  ARG   E NE  1 
ATOM   14630 C  CZ  . ARG   E 2 449 ? 49.142  -13.908 -40.567 1.00 98.48  ? 753  ARG   E CZ  1 
ATOM   14631 N  NH1 . ARG   E 2 449 ? 49.303  -13.416 -41.788 1.00 97.80  ? 753  ARG   E NH1 1 
ATOM   14632 N  NH2 . ARG   E 2 449 ? 49.023  -15.229 -40.395 1.00 100.12 ? 753  ARG   E NH2 1 
ATOM   14633 N  N   . PRO   E 2 450 ? 52.891  -8.168  -40.333 1.00 100.36 ? 754  PRO   E N   1 
ATOM   14634 C  CA  . PRO   E 2 450 ? 52.933  -6.821  -39.757 1.00 97.24  ? 754  PRO   E CA  1 
ATOM   14635 C  C   . PRO   E 2 450 ? 51.600  -6.385  -39.197 1.00 94.35  ? 754  PRO   E C   1 
ATOM   14636 O  O   . PRO   E 2 450 ? 50.885  -5.648  -39.869 1.00 96.36  ? 754  PRO   E O   1 
ATOM   14637 C  CB  . PRO   E 2 450 ? 53.303  -5.957  -40.957 1.00 102.96 ? 754  PRO   E CB  1 
ATOM   14638 C  CG  . PRO   E 2 450 ? 52.651  -6.694  -42.115 1.00 103.26 ? 754  PRO   E CG  1 
ATOM   14639 C  CD  . PRO   E 2 450 ? 52.877  -8.141  -41.806 1.00 101.54 ? 754  PRO   E CD  1 
ATOM   14640 N  N   . SER   E 2 451 ? 51.249  -6.782  -37.990 1.00 93.15  ? 755  SER   E N   1 
ATOM   14641 C  CA  . SER   E 2 451 ? 49.946  -6.425  -37.450 1.00 90.53  ? 755  SER   E CA  1 
ATOM   14642 C  C   . SER   E 2 451 ? 49.974  -4.982  -36.912 1.00 92.41  ? 755  SER   E C   1 
ATOM   14643 O  O   . SER   E 2 451 ? 50.908  -4.223  -37.170 1.00 99.08  ? 755  SER   E O   1 
ATOM   14644 C  CB  . SER   E 2 451 ? 49.543  -7.477  -36.427 1.00 93.13  ? 755  SER   E CB  1 
ATOM   14645 O  OG  . SER   E 2 451 ? 50.496  -7.560  -35.379 1.00 97.70  ? 755  SER   E OG  1 
ATOM   14646 N  N   . ALA   E 2 452 ? 48.936  -4.562  -36.179 1.00 91.87  ? 756  ALA   E N   1 
ATOM   14647 C  CA  . ALA   E 2 452 ? 48.819  -3.158  -35.756 1.00 93.25  ? 756  ALA   E CA  1 
ATOM   14648 C  C   . ALA   E 2 452 ? 49.782  -2.793  -34.643 1.00 95.82  ? 756  ALA   E C   1 
ATOM   14649 O  O   . ALA   E 2 452 ? 50.209  -1.639  -34.554 1.00 99.41  ? 756  ALA   E O   1 
ATOM   14650 C  CB  . ALA   E 2 452 ? 47.402  -2.834  -35.275 1.00 87.28  ? 756  ALA   E CB  1 
ATOM   14651 N  N   . SER   E 2 453 ? 50.092  -3.740  -33.762 1.00 97.13  ? 757  SER   E N   1 
ATOM   14652 C  CA  . SER   E 2 453 ? 50.986  -3.444  -32.656 1.00 96.62  ? 757  SER   E CA  1 
ATOM   14653 C  C   . SER   E 2 453 ? 52.421  -3.356  -33.139 1.00 100.00 ? 757  SER   E C   1 
ATOM   14654 O  O   . SER   E 2 453 ? 53.182  -2.520  -32.643 1.00 104.60 ? 757  SER   E O   1 
ATOM   14655 C  CB  . SER   E 2 453 ? 50.834  -4.490  -31.546 1.00 94.72  ? 757  SER   E CB  1 
ATOM   14656 O  OG  . SER   E 2 453 ? 50.868  -5.812  -32.060 1.00 92.81  ? 757  SER   E OG  1 
ATOM   14657 N  N   . THR   E 2 454 ? 52.807  -4.164  -34.131 1.00 98.95  ? 758  THR   E N   1 
ATOM   14658 C  CA  . THR   E 2 454 ? 54.170  -4.048  -34.639 1.00 107.62 ? 758  THR   E CA  1 
ATOM   14659 C  C   . THR   E 2 454 ? 54.384  -2.692  -35.315 1.00 114.16 ? 758  THR   E C   1 
ATOM   14660 O  O   . THR   E 2 454 ? 55.353  -1.989  -35.009 1.00 115.22 ? 758  THR   E O   1 
ATOM   14661 C  CB  . THR   E 2 454 ? 54.515  -5.223  -35.566 1.00 106.95 ? 758  THR   E CB  1 
ATOM   14662 O  OG1 . THR   E 2 454 ? 53.912  -5.058  -36.850 1.00 108.27 ? 758  THR   E OG1 1 
ATOM   14663 C  CG2 . THR   E 2 454 ? 54.028  -6.520  -34.962 1.00 104.51 ? 758  THR   E CG2 1 
ATOM   14664 N  N   . GLN   E 2 455 ? 53.452  -2.269  -36.177 1.00 122.95 ? 759  GLN   E N   1 
ATOM   14665 C  CA  . GLN   E 2 455 ? 53.596  -0.999  -36.907 1.00 125.35 ? 759  GLN   E CA  1 
ATOM   14666 C  C   . GLN   E 2 455 ? 52.843  0.151   -36.216 1.00 124.77 ? 759  GLN   E C   1 
ATOM   14667 O  O   . GLN   E 2 455 ? 51.986  0.809   -36.805 1.00 126.74 ? 759  GLN   E O   1 
ATOM   14668 C  CB  . GLN   E 2 455 ? 53.116  -1.149  -38.349 1.00 127.24 ? 759  GLN   E CB  1 
ATOM   14669 C  CG  . GLN   E 2 455 ? 53.273  -2.518  -38.956 1.00 128.84 ? 759  GLN   E CG  1 
ATOM   14670 C  CD  . GLN   E 2 455 ? 54.721  -2.853  -39.267 1.00 135.66 ? 759  GLN   E CD  1 
ATOM   14671 O  OE1 . GLN   E 2 455 ? 55.396  -2.119  -39.994 1.00 139.05 ? 759  GLN   E OE1 1 
ATOM   14672 N  NE2 . GLN   E 2 455 ? 55.213  -3.964  -38.702 1.00 135.65 ? 759  GLN   E NE2 1 
ATOM   14673 N  N   . ALA   E 2 456 ? 53.178  0.413   -34.957 1.00 115.65 ? 760  ALA   E N   1 
ATOM   14674 C  CA  . ALA   E 2 456 ? 52.598  1.554   -34.260 1.00 108.06 ? 760  ALA   E CA  1 
ATOM   14675 C  C   . ALA   E 2 456 ? 53.571  2.729   -34.320 1.00 112.73 ? 760  ALA   E C   1 
ATOM   14676 O  O   . ALA   E 2 456 ? 54.726  2.576   -34.715 1.00 116.51 ? 760  ALA   E O   1 
ATOM   14677 C  CB  . ALA   E 2 456 ? 52.265  1.208   -32.808 1.00 99.92  ? 760  ALA   E CB  1 
ATOM   14678 N  N   . LEU   E 2 457 ? 53.071  3.914   -33.937 1.00 112.71 ? 761  LEU   E N   1 
ATOM   14679 C  CA  . LEU   E 2 457 ? 53.893  5.132   -33.909 1.00 106.66 ? 761  LEU   E CA  1 
ATOM   14680 C  C   . LEU   E 2 457 ? 54.724  5.194   -32.626 1.00 104.93 ? 761  LEU   E C   1 
ATOM   14681 O  O   . LEU   E 2 457 ? 55.951  5.069   -32.662 1.00 108.41 ? 761  LEU   E O   1 
ATOM   14682 C  CB  . LEU   E 2 457 ? 53.013  6.382   -34.064 1.00 102.03 ? 761  LEU   E CB  1 
ATOM   14683 C  CG  . LEU   E 2 457 ? 52.068  6.445   -35.277 1.00 103.83 ? 761  LEU   E CG  1 
ATOM   14684 C  CD1 . LEU   E 2 457 ? 51.361  7.794   -35.405 1.00 104.47 ? 761  LEU   E CD1 1 
ATOM   14685 C  CD2 . LEU   E 2 457 ? 52.783  6.101   -36.565 1.00 104.83 ? 761  LEU   E CD2 1 
ATOM   14686 N  N   . SER   E 2 458 ? 54.074  5.390   -31.480 1.00 106.95 ? 762  SER   E N   1 
ATOM   14687 C  CA  . SER   E 2 458 ? 54.749  5.169   -30.209 1.00 106.71 ? 762  SER   E CA  1 
ATOM   14688 C  C   . SER   E 2 458 ? 54.707  3.680   -29.887 1.00 105.24 ? 762  SER   E C   1 
ATOM   14689 O  O   . SER   E 2 458 ? 53.816  2.955   -30.340 1.00 105.88 ? 762  SER   E O   1 
ATOM   14690 C  CB  . SER   E 2 458 ? 54.082  5.958   -29.063 1.00 107.76 ? 762  SER   E CB  1 
ATOM   14691 O  OG  . SER   E 2 458 ? 53.629  7.256   -29.422 1.00 107.46 ? 762  SER   E OG  1 
ATOM   14692 N  N   . SER   E 2 459 ? 55.679  3.214   -29.107 1.00 96.90  ? 763  SER   E N   1 
ATOM   14693 C  CA  . SER   E 2 459 ? 55.594  1.853   -28.593 1.00 96.91  ? 763  SER   E CA  1 
ATOM   14694 C  C   . SER   E 2 459 ? 56.335  1.754   -27.268 1.00 99.06  ? 763  SER   E C   1 
ATOM   14695 O  O   . SER   E 2 459 ? 57.556  1.944   -27.229 1.00 104.32 ? 763  SER   E O   1 
ATOM   14696 C  CB  . SER   E 2 459 ? 56.141  0.845   -29.617 1.00 100.47 ? 763  SER   E CB  1 
ATOM   14697 O  OG  . SER   E 2 459 ? 57.473  0.456   -29.326 1.00 103.22 ? 763  SER   E OG  1 
ATOM   14698 N  N   . SER   E 2 460 ? 55.595  1.444   -26.196 1.00 100.00 ? 764  SER   E N   1 
ATOM   14699 C  CA  . SER   E 2 460 ? 56.128  1.219   -24.855 1.00 98.37  ? 764  SER   E CA  1 
ATOM   14700 C  C   . SER   E 2 460 ? 56.096  -0.266  -24.500 1.00 101.13 ? 764  SER   E C   1 
ATOM   14701 O  O   . SER   E 2 460 ? 55.218  -1.006  -24.942 1.00 101.71 ? 764  SER   E O   1 
ATOM   14702 C  CB  . SER   E 2 460 ? 55.328  2.002   -23.813 1.00 98.04  ? 764  SER   E CB  1 
ATOM   14703 O  OG  . SER   E 2 460 ? 53.934  1.769   -23.930 1.00 97.35  ? 764  SER   E OG  1 
ATOM   14704 N  N   . VAL   E 2 461 ? 57.071  -0.697  -23.695 1.00 101.98 ? 765  VAL   E N   1 
ATOM   14705 C  CA  . VAL   E 2 461 ? 57.157  -2.079  -23.227 1.00 102.25 ? 765  VAL   E CA  1 
ATOM   14706 C  C   . VAL   E 2 461 ? 57.187  -2.083  -21.707 1.00 103.07 ? 765  VAL   E C   1 
ATOM   14707 O  O   . VAL   E 2 461 ? 58.041  -1.430  -21.100 1.00 104.77 ? 765  VAL   E O   1 
ATOM   14708 C  CB  . VAL   E 2 461 ? 58.386  -2.809  -23.797 1.00 101.22 ? 765  VAL   E CB  1 
ATOM   14709 C  CG1 . VAL   E 2 461 ? 58.686  -4.046  -22.968 1.00 104.77 ? 765  VAL   E CG1 1 
ATOM   14710 C  CG2 . VAL   E 2 461 ? 58.124  -3.205  -25.246 1.00 102.37 ? 765  VAL   E CG2 1 
ATOM   14711 N  N   . SER   E 2 462 ? 56.269  -2.835  -21.101 1.00 106.82 ? 766  SER   E N   1 
ATOM   14712 C  CA  . SER   E 2 462 ? 56.037  -2.735  -19.670 1.00 106.72 ? 766  SER   E CA  1 
ATOM   14713 C  C   . SER   E 2 462 ? 57.220  -3.254  -18.879 1.00 115.51 ? 766  SER   E C   1 
ATOM   14714 O  O   . SER   E 2 462 ? 57.944  -4.162  -19.305 1.00 111.87 ? 766  SER   E O   1 
ATOM   14715 C  CB  . SER   E 2 462 ? 54.792  -3.507  -19.250 1.00 103.36 ? 766  SER   E CB  1 
ATOM   14716 O  OG  . SER   E 2 462 ? 54.227  -2.908  -18.101 1.00 101.39 ? 766  SER   E OG  1 
ATOM   14717 N  N   . SER   E 2 463 ? 57.377  -2.680  -17.688 1.00 125.67 ? 767  SER   E N   1 
ATOM   14718 C  CA  . SER   E 2 463 ? 58.521  -2.948  -16.823 1.00 130.77 ? 767  SER   E CA  1 
ATOM   14719 C  C   . SER   E 2 463 ? 58.033  -2.864  -15.380 1.00 132.15 ? 767  SER   E C   1 
ATOM   14720 O  O   . SER   E 2 463 ? 57.828  -1.762  -14.864 1.00 131.87 ? 767  SER   E O   1 
ATOM   14721 C  CB  . SER   E 2 463 ? 59.640  -1.955  -17.088 1.00 133.55 ? 767  SER   E CB  1 
ATOM   14722 O  OG  . SER   E 2 463 ? 60.378  -1.733  -15.905 1.00 136.20 ? 767  SER   E OG  1 
ATOM   14723 N  N   . SER   E 2 464 ? 57.839  -4.023  -14.745 1.00 136.12 ? 768  SER   E N   1 
ATOM   14724 C  CA  . SER   E 2 464 ? 57.417  -4.107  -13.347 1.00 140.43 ? 768  SER   E CA  1 
ATOM   14725 C  C   . SER   E 2 464 ? 58.395  -4.860  -12.463 1.00 151.16 ? 768  SER   E C   1 
ATOM   14726 O  O   . SER   E 2 464 ? 58.642  -4.438  -11.325 1.00 150.55 ? 768  SER   E O   1 
ATOM   14727 C  CB  . SER   E 2 464 ? 56.045  -4.794  -13.229 1.00 133.32 ? 768  SER   E CB  1 
ATOM   14728 O  OG  . SER   E 2 464 ? 55.027  -4.049  -13.862 1.00 129.06 ? 768  SER   E OG  1 
ATOM   14729 N  N   . LYS   E 2 465 ? 58.939  -5.978  -12.954 1.00 160.62 ? 769  LYS   E N   1 
ATOM   14730 C  CA  . LYS   E 2 465 ? 59.737  -6.895  -12.141 1.00 164.30 ? 769  LYS   E CA  1 
ATOM   14731 C  C   . LYS   E 2 465 ? 58.991  -7.268  -10.859 1.00 169.59 ? 769  LYS   E C   1 
ATOM   14732 O  O   . LYS   E 2 465 ? 59.577  -7.368  -9.778  1.00 172.27 ? 769  LYS   E O   1 
ATOM   14733 C  CB  . LYS   E 2 465 ? 61.119  -6.307  -11.834 1.00 159.80 ? 769  LYS   E CB  1 
ATOM   14734 N  N   . LEU   E 2 466 ? 57.672  -7.454  -10.979 1.00 161.12 ? 770  LEU   E N   1 
ATOM   14735 C  CA  . LEU   E 2 466 ? 56.832  -7.823  -9.846  1.00 157.46 ? 770  LEU   E CA  1 
ATOM   14736 C  C   . LEU   E 2 466 ? 56.721  -9.333  -9.664  1.00 157.61 ? 770  LEU   E C   1 
ATOM   14737 O  O   . LEU   E 2 466 ? 56.235  -9.782  -8.618  1.00 153.40 ? 770  LEU   E O   1 
ATOM   14738 C  CB  . LEU   E 2 466 ? 55.430  -7.213  -10.001 1.00 150.18 ? 770  LEU   E CB  1 
ATOM   14739 N  N   . PHE   E 2 467 ? 57.164  -10.116 -10.651 1.00 156.69 ? 771  PHE   E N   1 
ATOM   14740 C  CA  . PHE   E 2 467 ? 57.045  -11.575 -10.619 1.00 156.65 ? 771  PHE   E CA  1 
ATOM   14741 C  C   . PHE   E 2 467 ? 58.248  -12.252 -11.284 1.00 155.97 ? 771  PHE   E C   1 
ATOM   14742 O  O   . PHE   E 2 467 ? 59.399  -12.000 -10.925 1.00 158.03 ? 771  PHE   E O   1 
ATOM   14743 C  CB  . PHE   E 2 467 ? 55.748  -12.026 -11.309 1.00 153.04 ? 771  PHE   E CB  1 
ATOM   14744 C  CG  . PHE   E 2 467 ? 54.571  -11.121 -11.053 1.00 151.16 ? 771  PHE   E CG  1 
ATOM   14745 C  CD1 . PHE   E 2 467 ? 53.762  -11.305 -9.939  1.00 147.81 ? 771  PHE   E CD1 1 
ATOM   14746 C  CD2 . PHE   E 2 467 ? 54.282  -10.081 -11.921 1.00 147.66 ? 771  PHE   E CD2 1 
ATOM   14747 C  CE1 . PHE   E 2 467 ? 52.685  -10.479 -9.701  1.00 143.99 ? 771  PHE   E CE1 1 
ATOM   14748 C  CE2 . PHE   E 2 467 ? 53.205  -9.245  -11.689 1.00 145.42 ? 771  PHE   E CE2 1 
ATOM   14749 C  CZ  . PHE   E 2 467 ? 52.406  -9.444  -10.576 1.00 143.67 ? 771  PHE   E CZ  1 
ATOM   14750 N  N   . THR   E 2 476 ? 61.485  -22.205 -22.104 1.00 192.29 ? 780  THR   E N   1 
ATOM   14751 C  CA  . THR   E 2 476 ? 60.664  -23.383 -21.856 1.00 192.64 ? 780  THR   E CA  1 
ATOM   14752 C  C   . THR   E 2 476 ? 59.917  -23.763 -23.147 1.00 198.20 ? 780  THR   E C   1 
ATOM   14753 O  O   . THR   E 2 476 ? 59.381  -24.868 -23.255 1.00 197.89 ? 780  THR   E O   1 
ATOM   14754 C  CB  . THR   E 2 476 ? 59.669  -23.141 -20.676 1.00 189.79 ? 780  THR   E CB  1 
ATOM   14755 O  OG1 . THR   E 2 476 ? 60.350  -22.482 -19.599 1.00 181.39 ? 780  THR   E OG1 1 
ATOM   14756 C  CG2 . THR   E 2 476 ? 59.098  -24.454 -20.146 1.00 188.79 ? 780  THR   E CG2 1 
ATOM   14757 N  N   . SER   E 2 477 ? 59.904  -22.857 -24.130 1.00 205.63 ? 781  SER   E N   1 
ATOM   14758 C  CA  . SER   E 2 477 ? 59.282  -23.096 -25.430 1.00 204.46 ? 781  SER   E CA  1 
ATOM   14759 C  C   . SER   E 2 477 ? 60.346  -23.215 -26.517 1.00 200.89 ? 781  SER   E C   1 
ATOM   14760 O  O   . SER   E 2 477 ? 61.327  -22.461 -26.523 1.00 201.23 ? 781  SER   E O   1 
ATOM   14761 C  CB  . SER   E 2 477 ? 58.299  -21.979 -25.790 1.00 201.34 ? 781  SER   E CB  1 
ATOM   14762 O  OG  . SER   E 2 477 ? 57.984  -22.020 -27.171 1.00 198.87 ? 781  SER   E OG  1 
ATOM   14763 N  N   . PHE   E 2 478 ? 60.144  -24.153 -27.451 1.00 178.29 ? 782  PHE   E N   1 
ATOM   14764 C  CA  . PHE   E 2 478 ? 61.170  -24.515 -28.432 1.00 167.14 ? 782  PHE   E CA  1 
ATOM   14765 C  C   . PHE   E 2 478 ? 60.601  -24.521 -29.853 1.00 156.05 ? 782  PHE   E C   1 
ATOM   14766 O  O   . PHE   E 2 478 ? 60.705  -25.507 -30.582 1.00 148.46 ? 782  PHE   E O   1 
ATOM   14767 C  CB  . PHE   E 2 478 ? 61.779  -25.875 -28.108 1.00 157.53 ? 782  PHE   E CB  1 
ATOM   14768 N  N   . GLY   E 2 479 ? 60.025  -23.392 -30.272 1.00 153.65 ? 783  GLY   E N   1 
ATOM   14769 C  CA  . GLY   E 2 479 ? 59.566  -23.223 -31.638 1.00 146.84 ? 783  GLY   E CA  1 
ATOM   14770 C  C   . GLY   E 2 479 ? 58.066  -23.080 -31.818 1.00 141.70 ? 783  GLY   E C   1 
ATOM   14771 O  O   . GLY   E 2 479 ? 57.611  -22.923 -32.961 1.00 128.11 ? 783  GLY   E O   1 
ATOM   14772 N  N   . GLU   E 2 480 ? 57.283  -23.112 -30.733 1.00 140.52 ? 784  GLU   E N   1 
ATOM   14773 C  CA  . GLU   E 2 480 ? 55.826  -23.124 -30.811 1.00 132.03 ? 784  GLU   E CA  1 
ATOM   14774 C  C   . GLU   E 2 480 ? 55.300  -21.705 -31.024 1.00 127.43 ? 784  GLU   E C   1 
ATOM   14775 O  O   . GLU   E 2 480 ? 56.065  -20.804 -31.371 1.00 127.04 ? 784  GLU   E O   1 
ATOM   14776 C  CB  . GLU   E 2 480 ? 55.235  -23.767 -29.546 1.00 132.58 ? 784  GLU   E CB  1 
ATOM   14777 N  N   . GLU   E 2 481 ? 53.996  -21.499 -30.834 1.00 120.51 ? 785  GLU   E N   1 
ATOM   14778 C  CA  . GLU   E 2 481 ? 53.383  -20.182 -30.949 1.00 112.05 ? 785  GLU   E CA  1 
ATOM   14779 C  C   . GLU   E 2 481 ? 53.216  -19.551 -29.574 1.00 105.66 ? 785  GLU   E C   1 
ATOM   14780 O  O   . GLU   E 2 481 ? 53.107  -20.235 -28.557 1.00 105.83 ? 785  GLU   E O   1 
ATOM   14781 C  CB  . GLU   E 2 481 ? 52.014  -20.263 -31.632 1.00 114.72 ? 785  GLU   E CB  1 
ATOM   14782 C  CG  . GLU   E 2 481 ? 51.842  -21.380 -32.656 1.00 124.18 ? 785  GLU   E CG  1 
ATOM   14783 C  CD  . GLU   E 2 481 ? 50.445  -21.383 -33.274 1.00 127.22 ? 785  GLU   E CD  1 
ATOM   14784 O  OE1 . GLU   E 2 481 ? 49.460  -21.299 -32.512 1.00 130.00 ? 785  GLU   E OE1 1 
ATOM   14785 O  OE2 . GLU   E 2 481 ? 50.326  -21.461 -34.519 1.00 128.05 ? 785  GLU   E OE2 1 
ATOM   14786 N  N   . VAL   E 2 482 ? 53.157  -18.219 -29.550 1.00 108.36 ? 786  VAL   E N   1 
ATOM   14787 C  CA  . VAL   E 2 482 ? 53.032  -17.477 -28.300 1.00 99.19  ? 786  VAL   E CA  1 
ATOM   14788 C  C   . VAL   E 2 482 ? 52.208  -16.224 -28.538 1.00 93.83  ? 786  VAL   E C   1 
ATOM   14789 O  O   . VAL   E 2 482 ? 52.094  -15.725 -29.658 1.00 94.96  ? 786  VAL   E O   1 
ATOM   14790 C  CB  . VAL   E 2 482 ? 54.409  -17.115 -27.706 1.00 98.06  ? 786  VAL   E CB  1 
ATOM   14791 C  CG1 . VAL   E 2 482 ? 54.983  -15.904 -28.396 1.00 99.02  ? 786  VAL   E CG1 1 
ATOM   14792 C  CG2 . VAL   E 2 482 ? 54.279  -16.859 -26.234 1.00 104.70 ? 786  VAL   E CG2 1 
ATOM   14793 N  N   . GLU   E 2 483 ? 51.607  -15.724 -27.470 1.00 89.41  ? 787  GLU   E N   1 
ATOM   14794 C  CA  . GLU   E 2 483 ? 50.758  -14.546 -27.542 1.00 90.83  ? 787  GLU   E CA  1 
ATOM   14795 C  C   . GLU   E 2 483 ? 51.503  -13.335 -27.012 1.00 90.84  ? 787  GLU   E C   1 
ATOM   14796 O  O   . GLU   E 2 483 ? 52.385  -13.448 -26.157 1.00 90.48  ? 787  GLU   E O   1 
ATOM   14797 C  CB  . GLU   E 2 483 ? 49.461  -14.746 -26.755 1.00 90.41  ? 787  GLU   E CB  1 
ATOM   14798 C  CG  . GLU   E 2 483 ? 48.263  -15.060 -27.645 1.00 94.37  ? 787  GLU   E CG  1 
ATOM   14799 C  CD  . GLU   E 2 483 ? 46.985  -15.366 -26.862 1.00 97.80  ? 787  GLU   E CD  1 
ATOM   14800 O  OE1 . GLU   E 2 483 ? 47.084  -15.869 -25.719 1.00 97.32  ? 787  GLU   E OE1 1 
ATOM   14801 O  OE2 . GLU   E 2 483 ? 45.878  -15.113 -27.399 1.00 100.95 ? 787  GLU   E OE2 1 
ATOM   14802 N  N   . VAL   E 2 484 ? 51.135  -12.164 -27.536 1.00 90.94  ? 788  VAL   E N   1 
ATOM   14803 C  CA  . VAL   E 2 484 ? 51.749  -10.890 -27.179 1.00 89.98  ? 788  VAL   E CA  1 
ATOM   14804 C  C   . VAL   E 2 484 ? 50.654  -9.845  -27.014 1.00 87.88  ? 788  VAL   E C   1 
ATOM   14805 O  O   . VAL   E 2 484 ? 50.278  -9.172  -27.979 1.00 89.67  ? 788  VAL   E O   1 
ATOM   14806 C  CB  . VAL   E 2 484 ? 52.775  -10.431 -28.233 1.00 91.03  ? 788  VAL   E CB  1 
ATOM   14807 C  CG1 . VAL   E 2 484 ? 53.475  -9.190  -27.734 1.00 99.14  ? 788  VAL   E CG1 1 
ATOM   14808 C  CG2 . VAL   E 2 484 ? 53.764  -11.554 -28.605 1.00 86.14  ? 788  VAL   E CG2 1 
ATOM   14809 N  N   . HIS   E 2 485 ? 50.179  -9.640  -25.787 1.00 88.69  ? 789  HIS   E N   1 
ATOM   14810 C  CA  . HIS   E 2 485 ? 49.054  -8.735  -25.561 1.00 86.94  ? 789  HIS   E CA  1 
ATOM   14811 C  C   . HIS   E 2 485 ? 49.535  -7.287  -25.477 1.00 88.29  ? 789  HIS   E C   1 
ATOM   14812 O  O   . HIS   E 2 485 ? 50.480  -6.984  -24.743 1.00 95.17  ? 789  HIS   E O   1 
ATOM   14813 C  CB  . HIS   E 2 485 ? 48.288  -9.134  -24.293 1.00 85.12  ? 789  HIS   E CB  1 
ATOM   14814 C  CG  . HIS   E 2 485 ? 47.529  -10.413 -24.437 1.00 85.61  ? 789  HIS   E CG  1 
ATOM   14815 N  ND1 . HIS   E 2 485 ? 48.159  -11.624 -24.633 1.00 89.95  ? 789  HIS   E ND1 1 
ATOM   14816 C  CD2 . HIS   E 2 485 ? 46.199  -10.667 -24.475 1.00 87.89  ? 789  HIS   E CD2 1 
ATOM   14817 C  CE1 . HIS   E 2 485 ? 47.252  -12.573 -24.770 1.00 90.04  ? 789  HIS   E CE1 1 
ATOM   14818 N  NE2 . HIS   E 2 485 ? 46.054  -12.019 -24.681 1.00 91.08  ? 789  HIS   E NE2 1 
ATOM   14819 N  N   . ASN   E 2 486 ? 48.916  -6.397  -26.249 1.00 83.44  ? 790  ASN   E N   1 
ATOM   14820 C  CA  . ASN   E 2 486 ? 49.213  -4.974  -26.123 1.00 87.55  ? 790  ASN   E CA  1 
ATOM   14821 C  C   . ASN   E 2 486 ? 47.919  -4.202  -25.890 1.00 88.03  ? 790  ASN   E C   1 
ATOM   14822 O  O   . ASN   E 2 486 ? 46.826  -4.675  -26.201 1.00 86.76  ? 790  ASN   E O   1 
ATOM   14823 C  CB  . ASN   E 2 486 ? 49.955  -4.407  -27.349 1.00 88.06  ? 790  ASN   E CB  1 
ATOM   14824 C  CG  . ASN   E 2 486 ? 50.998  -5.370  -27.911 1.00 94.00  ? 790  ASN   E CG  1 
ATOM   14825 O  OD1 . ASN   E 2 486 ? 52.204  -5.276  -27.615 1.00 94.92  ? 790  ASN   E OD1 1 
ATOM   14826 N  ND2 . ASN   E 2 486 ? 50.536  -6.295  -28.752 1.00 93.96  ? 790  ASN   E ND2 1 
ATOM   14827 N  N   . LEU   E 2 487 ? 48.051  -3.034  -25.265 1.00 91.21  ? 791  LEU   E N   1 
ATOM   14828 C  CA  . LEU   E 2 487 ? 47.034  -1.996  -25.299 1.00 84.74  ? 791  LEU   E CA  1 
ATOM   14829 C  C   . LEU   E 2 487 ? 47.366  -1.102  -26.484 1.00 87.78  ? 791  LEU   E C   1 
ATOM   14830 O  O   . LEU   E 2 487 ? 48.524  -0.695  -26.655 1.00 87.99  ? 791  LEU   E O   1 
ATOM   14831 C  CB  . LEU   E 2 487 ? 47.004  -1.197  -23.994 1.00 81.88  ? 791  LEU   E CB  1 
ATOM   14832 C  CG  . LEU   E 2 487 ? 46.239  0.132   -23.946 1.00 81.84  ? 791  LEU   E CG  1 
ATOM   14833 C  CD1 . LEU   E 2 487 ? 44.758  -0.061  -24.164 1.00 83.21  ? 791  LEU   E CD1 1 
ATOM   14834 C  CD2 . LEU   E 2 487 ? 46.465  0.800   -22.619 1.00 85.11  ? 791  LEU   E CD2 1 
ATOM   14835 N  N   . LEU   E 2 488 ? 46.367  -0.850  -27.326 1.00 87.92  ? 792  LEU   E N   1 
ATOM   14836 C  CA  . LEU   E 2 488 ? 46.510  0.005   -28.497 1.00 87.66  ? 792  LEU   E CA  1 
ATOM   14837 C  C   . LEU   E 2 488 ? 45.798  1.319   -28.230 1.00 89.00  ? 792  LEU   E C   1 
ATOM   14838 O  O   . LEU   E 2 488 ? 44.642  1.326   -27.784 1.00 89.83  ? 792  LEU   E O   1 
ATOM   14839 C  CB  . LEU   E 2 488 ? 45.934  -0.660  -29.757 1.00 83.95  ? 792  LEU   E CB  1 
ATOM   14840 C  CG  . LEU   E 2 488 ? 46.489  -1.991  -30.272 1.00 82.80  ? 792  LEU   E CG  1 
ATOM   14841 C  CD1 . LEU   E 2 488 ? 46.043  -2.220  -31.700 1.00 82.15  ? 792  LEU   E CD1 1 
ATOM   14842 C  CD2 . LEU   E 2 488 ? 48.017  -2.089  -30.166 1.00 91.77  ? 792  LEU   E CD2 1 
ATOM   14843 N  N   . ILE   E 2 489 ? 46.488  2.424   -28.472 1.00 94.63  ? 793  ILE   E N   1 
ATOM   14844 C  CA  . ILE   E 2 489 ? 45.872  3.743   -28.452 1.00 96.84  ? 793  ILE   E CA  1 
ATOM   14845 C  C   . ILE   E 2 489 ? 45.557  4.093   -29.899 1.00 97.52  ? 793  ILE   E C   1 
ATOM   14846 O  O   . ILE   E 2 489 ? 46.467  4.305   -30.710 1.00 98.47  ? 793  ILE   E O   1 
ATOM   14847 C  CB  . ILE   E 2 489 ? 46.780  4.798   -27.803 1.00 98.47  ? 793  ILE   E CB  1 
ATOM   14848 C  CG1 . ILE   E 2 489 ? 47.269  4.318   -26.434 1.00 96.24  ? 793  ILE   E CG1 1 
ATOM   14849 C  CG2 . ILE   E 2 489 ? 46.020  6.102   -27.664 1.00 102.87 ? 793  ILE   E CG2 1 
ATOM   14850 C  CD1 . ILE   E 2 489 ? 46.208  4.382   -25.360 1.00 96.36  ? 793  ILE   E CD1 1 
ATOM   14851 N  N   . ILE   E 2 490 ? 44.272  4.125   -30.238 1.00 94.89  ? 794  ILE   E N   1 
ATOM   14852 C  CA  . ILE   E 2 490 ? 43.830  4.312   -31.612 1.00 95.71  ? 794  ILE   E CA  1 
ATOM   14853 C  C   . ILE   E 2 490 ? 43.065  5.624   -31.703 1.00 98.41  ? 794  ILE   E C   1 
ATOM   14854 O  O   . ILE   E 2 490 ? 42.203  5.908   -30.859 1.00 100.48 ? 794  ILE   E O   1 
ATOM   14855 C  CB  . ILE   E 2 490 ? 42.986  3.123   -32.099 1.00 93.57  ? 794  ILE   E CB  1 
ATOM   14856 C  CG1 . ILE   E 2 490 ? 43.856  1.867   -32.059 1.00 92.17  ? 794  ILE   E CG1 1 
ATOM   14857 C  CG2 . ILE   E 2 490 ? 42.447  3.383   -33.498 1.00 91.48  ? 794  ILE   E CG2 1 
ATOM   14858 C  CD1 . ILE   E 2 490 ? 43.161  0.613   -32.479 1.00 88.02  ? 794  ILE   E CD1 1 
ATOM   14859 N  N   . ASP   E 2 491 ? 43.386  6.417   -32.721 1.00 98.64  ? 795  ASP   E N   1 
ATOM   14860 C  CA  . ASP   E 2 491 ? 42.957  7.806   -32.797 1.00 95.35  ? 795  ASP   E CA  1 
ATOM   14861 C  C   . ASP   E 2 491 ? 41.618  7.899   -33.504 1.00 93.59  ? 795  ASP   E C   1 
ATOM   14862 O  O   . ASP   E 2 491 ? 41.509  7.546   -34.680 1.00 93.75  ? 795  ASP   E O   1 
ATOM   14863 C  CB  . ASP   E 2 491 ? 43.997  8.634   -33.531 1.00 95.02  ? 795  ASP   E CB  1 
ATOM   14864 C  CG  . ASP   E 2 491 ? 43.451  9.945   -33.969 1.00 99.68  ? 795  ASP   E CG  1 
ATOM   14865 O  OD1 . ASP   E 2 491 ? 43.485  10.886  -33.149 1.00 102.01 ? 795  ASP   E OD1 1 
ATOM   14866 O  OD2 . ASP   E 2 491 ? 42.963  10.027  -35.119 1.00 100.28 ? 795  ASP   E OD2 1 
ATOM   14867 N  N   . GLN   E 2 492 ? 40.617  8.426   -32.808 1.00 98.18  ? 796  GLN   E N   1 
ATOM   14868 C  CA  . GLN   E 2 492 ? 39.249  8.320   -33.293 1.00 99.44  ? 796  GLN   E CA  1 
ATOM   14869 C  C   . GLN   E 2 492 ? 39.082  8.846   -34.712 1.00 93.20  ? 796  GLN   E C   1 
ATOM   14870 O  O   . GLN   E 2 492 ? 38.168  8.420   -35.420 1.00 86.91  ? 796  GLN   E O   1 
ATOM   14871 C  CB  . GLN   E 2 492 ? 38.293  9.037   -32.324 1.00 103.81 ? 796  GLN   E CB  1 
ATOM   14872 C  CG  . GLN   E 2 492 ? 38.207  10.553  -32.445 1.00 102.70 ? 796  GLN   E CG  1 
ATOM   14873 C  CD  . GLN   E 2 492 ? 37.175  11.138  -31.489 1.00 104.02 ? 796  GLN   E CD  1 
ATOM   14874 O  OE1 . GLN   E 2 492 ? 37.266  10.950  -30.277 1.00 101.10 ? 796  GLN   E OE1 1 
ATOM   14875 N  NE2 . GLN   E 2 492 ? 36.181  11.838  -32.036 1.00 104.52 ? 796  GLN   E NE2 1 
ATOM   14876 N  N   . HIS   E 2 493 ? 39.957  9.722   -35.174 1.00 95.30  ? 797  HIS   E N   1 
ATOM   14877 C  CA  . HIS   E 2 493 ? 39.700  10.264  -36.497 1.00 96.18  ? 797  HIS   E CA  1 
ATOM   14878 C  C   . HIS   E 2 493 ? 40.366  9.435   -37.579 1.00 95.17  ? 797  HIS   E C   1 
ATOM   14879 O  O   . HIS   E 2 493 ? 39.712  9.017   -38.542 1.00 97.98  ? 797  HIS   E O   1 
ATOM   14880 C  CB  . HIS   E 2 493 ? 40.191  11.708  -36.587 1.00 98.46  ? 797  HIS   E CB  1 
ATOM   14881 C  CG  . HIS   E 2 493 ? 39.556  12.632  -35.595 1.00 98.76  ? 797  HIS   E CG  1 
ATOM   14882 N  ND1 . HIS   E 2 493 ? 40.193  13.037  -34.441 1.00 101.67 ? 797  HIS   E ND1 1 
ATOM   14883 C  CD2 . HIS   E 2 493 ? 38.348  13.246  -35.596 1.00 101.71 ? 797  HIS   E CD2 1 
ATOM   14884 C  CE1 . HIS   E 2 493 ? 39.403  13.861  -33.773 1.00 108.20 ? 797  HIS   E CE1 1 
ATOM   14885 N  NE2 . HIS   E 2 493 ? 38.276  14.002  -34.451 1.00 106.00 ? 797  HIS   E NE2 1 
ATOM   14886 N  N   . THR   E 2 494 ? 41.668  9.198   -37.420 1.00 95.00  ? 798  THR   E N   1 
ATOM   14887 C  CA  . THR   E 2 494 ? 42.437  8.458   -38.413 1.00 99.43  ? 798  THR   E CA  1 
ATOM   14888 C  C   . THR   E 2 494 ? 42.241  6.945   -38.281 1.00 94.84  ? 798  THR   E C   1 
ATOM   14889 O  O   . THR   E 2 494 ? 42.349  6.225   -39.276 1.00 92.37  ? 798  THR   E O   1 
ATOM   14890 C  CB  . THR   E 2 494 ? 43.934  8.808   -38.300 1.00 99.90  ? 798  THR   E CB  1 
ATOM   14891 O  OG1 . THR   E 2 494 ? 44.491  8.198   -37.130 1.00 103.01 ? 798  THR   E OG1 1 
ATOM   14892 C  CG2 . THR   E 2 494 ? 44.159  10.304  -38.187 1.00 97.48  ? 798  THR   E CG2 1 
ATOM   14893 N  N   . PHE   E 2 495 ? 41.918  6.460   -37.079 1.00 94.51  ? 799  PHE   E N   1 
ATOM   14894 C  CA  . PHE   E 2 495 ? 41.968  5.039   -36.741 1.00 89.20  ? 799  PHE   E CA  1 
ATOM   14895 C  C   . PHE   E 2 495 ? 43.353  4.467   -37.026 1.00 96.97  ? 799  PHE   E C   1 
ATOM   14896 O  O   . PHE   E 2 495 ? 43.530  3.442   -37.696 1.00 102.12 ? 799  PHE   E O   1 
ATOM   14897 C  CB  . PHE   E 2 495 ? 40.860  4.269   -37.438 1.00 82.85  ? 799  PHE   E CB  1 
ATOM   14898 C  CG  . PHE   E 2 495 ? 39.540  4.503   -36.820 1.00 85.98  ? 799  PHE   E CG  1 
ATOM   14899 C  CD1 . PHE   E 2 495 ? 39.342  4.193   -35.484 1.00 89.15  ? 799  PHE   E CD1 1 
ATOM   14900 C  CD2 . PHE   E 2 495 ? 38.503  5.071   -37.535 1.00 88.74  ? 799  PHE   E CD2 1 
ATOM   14901 C  CE1 . PHE   E 2 495 ? 38.114  4.415   -34.870 1.00 88.73  ? 799  PHE   E CE1 1 
ATOM   14902 C  CE2 . PHE   E 2 495 ? 37.273  5.294   -36.934 1.00 89.85  ? 799  PHE   E CE2 1 
ATOM   14903 C  CZ  . PHE   E 2 495 ? 37.075  4.963   -35.596 1.00 87.32  ? 799  PHE   E CZ  1 
ATOM   14904 N  N   . GLU   E 2 496 ? 44.345  5.152   -36.481 1.00 97.40  ? 800  GLU   E N   1 
ATOM   14905 C  CA  . GLU   E 2 496 ? 45.740  4.796   -36.613 1.00 97.94  ? 800  GLU   E CA  1 
ATOM   14906 C  C   . GLU   E 2 496 ? 46.267  4.478   -35.227 1.00 100.35 ? 800  GLU   E C   1 
ATOM   14907 O  O   . GLU   E 2 496 ? 45.824  5.060   -34.232 1.00 99.89  ? 800  GLU   E O   1 
ATOM   14908 C  CB  . GLU   E 2 496 ? 46.506  5.950   -37.249 1.00 103.10 ? 800  GLU   E CB  1 
ATOM   14909 C  CG  . GLU   E 2 496 ? 47.991  5.765   -37.397 1.00 110.99 ? 800  GLU   E CG  1 
ATOM   14910 C  CD  . GLU   E 2 496 ? 48.661  7.041   -37.882 1.00 116.51 ? 800  GLU   E CD  1 
ATOM   14911 O  OE1 . GLU   E 2 496 ? 48.421  8.117   -37.270 1.00 113.91 ? 800  GLU   E OE1 1 
ATOM   14912 O  OE2 . GLU   E 2 496 ? 49.400  6.965   -38.893 1.00 120.30 ? 800  GLU   E OE2 1 
ATOM   14913 N  N   . VAL   E 2 497 ? 47.205  3.533   -35.167 1.00 103.93 ? 801  VAL   E N   1 
ATOM   14914 C  CA  . VAL   E 2 497 ? 47.745  3.027   -33.905 1.00 100.58 ? 801  VAL   E CA  1 
ATOM   14915 C  C   . VAL   E 2 497 ? 48.767  4.044   -33.389 1.00 98.52  ? 801  VAL   E C   1 
ATOM   14916 O  O   . VAL   E 2 497 ? 49.880  4.134   -33.911 1.00 96.13  ? 801  VAL   E O   1 
ATOM   14917 C  CB  . VAL   E 2 497 ? 48.350  1.634   -34.076 1.00 98.80  ? 801  VAL   E CB  1 
ATOM   14918 C  CG1 . VAL   E 2 497 ? 48.653  1.000   -32.732 1.00 97.86  ? 801  VAL   E CG1 1 
ATOM   14919 C  CG2 . VAL   E 2 497 ? 47.418  0.739   -34.902 1.00 90.61  ? 801  VAL   E CG2 1 
ATOM   14920 N  N   . LEU   E 2 498 ? 48.402  4.806   -32.349 1.00 98.02  ? 802  LEU   E N   1 
ATOM   14921 C  CA  . LEU   E 2 498 ? 49.267  5.869   -31.835 1.00 97.45  ? 802  LEU   E CA  1 
ATOM   14922 C  C   . LEU   E 2 498 ? 50.358  5.321   -30.929 1.00 101.70 ? 802  LEU   E C   1 
ATOM   14923 O  O   . LEU   E 2 498 ? 51.520  5.720   -31.044 1.00 103.32 ? 802  LEU   E O   1 
ATOM   14924 C  CB  . LEU   E 2 498 ? 48.463  6.899   -31.048 1.00 100.69 ? 802  LEU   E CB  1 
ATOM   14925 C  CG  . LEU   E 2 498 ? 47.200  7.554   -31.591 1.00 102.77 ? 802  LEU   E CG  1 
ATOM   14926 C  CD1 . LEU   E 2 498 ? 46.587  8.510   -30.544 1.00 104.40 ? 802  LEU   E CD1 1 
ATOM   14927 C  CD2 . LEU   E 2 498 ? 47.495  8.267   -32.897 1.00 100.12 ? 802  LEU   E CD2 1 
ATOM   14928 N  N   . HIS   E 2 499 ? 49.976  4.466   -29.973 1.00 100.74 ? 803  HIS   E N   1 
ATOM   14929 C  CA  . HIS   E 2 499 ? 50.867  3.826   -29.014 1.00 97.85  ? 803  HIS   E CA  1 
ATOM   14930 C  C   . HIS   E 2 499 ? 50.573  2.335   -29.008 1.00 96.44  ? 803  HIS   E C   1 
ATOM   14931 O  O   . HIS   E 2 499 ? 49.512  1.895   -29.465 1.00 95.39  ? 803  HIS   E O   1 
ATOM   14932 C  CB  . HIS   E 2 499 ? 50.667  4.392   -27.600 1.00 100.32 ? 803  HIS   E CB  1 
ATOM   14933 C  CG  . HIS   E 2 499 ? 51.932  4.525   -26.810 1.00 103.71 ? 803  HIS   E CG  1 
ATOM   14934 N  ND1 . HIS   E 2 499 ? 52.799  3.475   -26.587 1.00 99.99  ? 803  HIS   E ND1 1 
ATOM   14935 C  CD2 . HIS   E 2 499 ? 52.474  5.598   -26.185 1.00 108.50 ? 803  HIS   E CD2 1 
ATOM   14936 C  CE1 . HIS   E 2 499 ? 53.821  3.900   -25.864 1.00 100.73 ? 803  HIS   E CE1 1 
ATOM   14937 N  NE2 . HIS   E 2 499 ? 53.646  5.182   -25.602 1.00 105.68 ? 803  HIS   E NE2 1 
ATOM   14938 N  N   . ALA   E 2 500 ? 51.514  1.547   -28.479 1.00 94.50  ? 804  ALA   E N   1 
ATOM   14939 C  CA  . ALA   E 2 500 ? 51.289  0.096   -28.394 1.00 94.42  ? 804  ALA   E CA  1 
ATOM   14940 C  C   . ALA   E 2 500 ? 52.091  -0.446  -27.214 1.00 97.77  ? 804  ALA   E C   1 
ATOM   14941 O  O   . ALA   E 2 500 ? 53.260  -0.809  -27.367 1.00 98.23  ? 804  ALA   E O   1 
ATOM   14942 C  CB  . ALA   E 2 500 ? 51.676  -0.609  -29.689 1.00 94.52  ? 804  ALA   E CB  1 
ATOM   14943 N  N   . HIS   E 2 501 ? 51.435  -0.543  -26.051 1.00 95.80  ? 805  HIS   E N   1 
ATOM   14944 C  CA  . HIS   E 2 501 ? 52.109  -0.938  -24.821 1.00 95.54  ? 805  HIS   E CA  1 
ATOM   14945 C  C   . HIS   E 2 501 ? 52.086  -2.448  -24.673 1.00 95.99  ? 805  HIS   E C   1 
ATOM   14946 O  O   . HIS   E 2 501 ? 51.036  -3.021  -24.392 1.00 98.75  ? 805  HIS   E O   1 
ATOM   14947 C  CB  . HIS   E 2 501 ? 51.465  -0.315  -23.597 1.00 95.12  ? 805  HIS   E CB  1 
ATOM   14948 C  CG  . HIS   E 2 501 ? 52.128  -0.728  -22.331 1.00 96.51  ? 805  HIS   E CG  1 
ATOM   14949 N  ND1 . HIS   E 2 501 ? 53.374  -0.266  -21.971 1.00 99.37  ? 805  HIS   E ND1 1 
ATOM   14950 C  CD2 . HIS   E 2 501 ? 51.750  -1.590  -21.363 1.00 96.61  ? 805  HIS   E CD2 1 
ATOM   14951 C  CE1 . HIS   E 2 501 ? 53.718  -0.796  -20.814 1.00 100.75 ? 805  HIS   E CE1 1 
ATOM   14952 N  NE2 . HIS   E 2 501 ? 52.753  -1.609  -20.427 1.00 99.53  ? 805  HIS   E NE2 1 
ATOM   14953 N  N   . GLN   E 2 502 ? 53.243  -3.087  -24.812 1.00 109.62 ? 806  GLN   E N   1 
ATOM   14954 C  CA  . GLN   E 2 502 ? 53.327  -4.539  -24.680 1.00 109.32 ? 806  GLN   E CA  1 
ATOM   14955 C  C   . GLN   E 2 502 ? 53.392  -4.938  -23.212 1.00 107.11 ? 806  GLN   E C   1 
ATOM   14956 O  O   . GLN   E 2 502 ? 54.380  -4.659  -22.526 1.00 107.06 ? 806  GLN   E O   1 
ATOM   14957 C  CB  . GLN   E 2 502 ? 54.542  -5.099  -25.409 1.00 110.65 ? 806  GLN   E CB  1 
ATOM   14958 C  CG  . GLN   E 2 502 ? 54.563  -6.614  -25.370 1.00 109.52 ? 806  GLN   E CG  1 
ATOM   14959 C  CD  . GLN   E 2 502 ? 55.959  -7.192  -25.460 1.00 112.88 ? 806  GLN   E CD  1 
ATOM   14960 O  OE1 . GLN   E 2 502 ? 56.677  -6.968  -26.437 1.00 113.43 ? 806  GLN   E OE1 1 
ATOM   14961 N  NE2 . GLN   E 2 502 ? 56.352  -7.948  -24.433 1.00 112.52 ? 806  GLN   E NE2 1 
ATOM   14962 N  N   . PHE   E 2 503 ? 52.355  -5.620  -22.745 1.00 100.55 ? 807  PHE   E N   1 
ATOM   14963 C  CA  . PHE   E 2 503 ? 52.304  -6.045  -21.363 1.00 98.74  ? 807  PHE   E CA  1 
ATOM   14964 C  C   . PHE   E 2 503 ? 53.377  -7.089  -21.081 1.00 102.10 ? 807  PHE   E C   1 
ATOM   14965 O  O   . PHE   E 2 503 ? 54.067  -7.587  -21.981 1.00 104.92 ? 807  PHE   E O   1 
ATOM   14966 C  CB  . PHE   E 2 503 ? 50.939  -6.616  -21.030 1.00 92.03  ? 807  PHE   E CB  1 
ATOM   14967 C  CG  . PHE   E 2 503 ? 49.883  -5.599  -20.907 1.00 87.51  ? 807  PHE   E CG  1 
ATOM   14968 C  CD1 . PHE   E 2 503 ? 49.701  -4.925  -19.715 1.00 90.05  ? 807  PHE   E CD1 1 
ATOM   14969 C  CD2 . PHE   E 2 503 ? 49.054  -5.325  -21.970 1.00 85.42  ? 807  PHE   E CD2 1 
ATOM   14970 C  CE1 . PHE   E 2 503 ? 48.710  -3.985  -19.584 1.00 86.86  ? 807  PHE   E CE1 1 
ATOM   14971 C  CE2 . PHE   E 2 503 ? 48.064  -4.391  -21.850 1.00 89.36  ? 807  PHE   E CE2 1 
ATOM   14972 C  CZ  . PHE   E 2 503 ? 47.894  -3.712  -20.650 1.00 87.98  ? 807  PHE   E CZ  1 
ATOM   14973 N  N   . LEU   E 2 504 ? 53.459  -7.465  -19.806 1.00 99.83  ? 808  LEU   E N   1 
ATOM   14974 C  CA  . LEU   E 2 504 ? 54.530  -8.322  -19.322 1.00 104.06 ? 808  LEU   E CA  1 
ATOM   14975 C  C   . LEU   E 2 504 ? 54.502  -9.687  -19.998 1.00 108.11 ? 808  LEU   E C   1 
ATOM   14976 O  O   . LEU   E 2 504 ? 53.464  -10.159 -20.473 1.00 106.14 ? 808  LEU   E O   1 
ATOM   14977 C  CB  . LEU   E 2 504 ? 54.426  -8.491  -17.815 1.00 101.37 ? 808  LEU   E CB  1 
ATOM   14978 C  CG  . LEU   E 2 504 ? 54.685  -7.198  -17.069 1.00 99.54  ? 808  LEU   E CG  1 
ATOM   14979 C  CD1 . LEU   E 2 504 ? 54.221  -7.368  -15.648 1.00 102.23 ? 808  LEU   E CD1 1 
ATOM   14980 C  CD2 . LEU   E 2 504 ? 56.166  -6.881  -17.140 1.00 104.68 ? 808  LEU   E CD2 1 
ATOM   14981 N  N   . GLN   E 2 505 ? 55.674  -10.311 -20.052 1.00 114.13 ? 809  GLN   E N   1 
ATOM   14982 C  CA  . GLN   E 2 505 ? 55.790  -11.615 -20.678 1.00 116.11 ? 809  GLN   E CA  1 
ATOM   14983 C  C   . GLN   E 2 505 ? 55.016  -12.636 -19.861 1.00 114.40 ? 809  GLN   E C   1 
ATOM   14984 O  O   . GLN   E 2 505 ? 55.132  -12.681 -18.632 1.00 113.48 ? 809  GLN   E O   1 
ATOM   14985 C  CB  . GLN   E 2 505 ? 57.253  -12.017 -20.817 1.00 120.23 ? 809  GLN   E CB  1 
ATOM   14986 C  CG  . GLN   E 2 505 ? 57.537  -12.856 -22.060 1.00 121.80 ? 809  GLN   E CG  1 
ATOM   14987 C  CD  . GLN   E 2 505 ? 57.632  -14.347 -21.765 1.00 127.70 ? 809  GLN   E CD  1 
ATOM   14988 O  OE1 . GLN   E 2 505 ? 58.403  -14.772 -20.895 1.00 132.17 ? 809  GLN   E OE1 1 
ATOM   14989 N  NE2 . GLN   E 2 505 ? 56.854  -15.153 -22.497 1.00 126.95 ? 809  GLN   E NE2 1 
ATOM   14990 N  N   . ASN   E 2 506 ? 54.211  -13.441 -20.547 1.00 107.30 ? 810  ASN   E N   1 
ATOM   14991 C  CA  . ASN   E 2 506 ? 53.229  -14.341 -19.962 1.00 104.04 ? 810  ASN   E CA  1 
ATOM   14992 C  C   . ASN   E 2 506 ? 52.089  -13.629 -19.264 1.00 100.34 ? 810  ASN   E C   1 
ATOM   14993 O  O   . ASN   E 2 506 ? 51.281  -14.290 -18.601 1.00 96.15  ? 810  ASN   E O   1 
ATOM   14994 C  CB  . ASN   E 2 506 ? 53.846  -15.307 -18.958 1.00 102.65 ? 810  ASN   E CB  1 
ATOM   14995 C  CG  . ASN   E 2 506 ? 54.263  -16.565 -19.597 1.00 104.81 ? 810  ASN   E CG  1 
ATOM   14996 O  OD1 . ASN   E 2 506 ? 55.440  -16.881 -19.609 1.00 107.35 ? 810  ASN   E OD1 1 
ATOM   14997 N  ND2 . ASN   E 2 506 ? 53.307  -17.294 -20.178 1.00 103.98 ? 810  ASN   E ND2 1 
ATOM   14998 N  N   . GLU   E 2 507 ? 52.019  -12.308 -19.331 1.00 99.80  ? 811  GLU   E N   1 
ATOM   14999 C  CA  . GLU   E 2 507 ? 50.864  -11.620 -18.802 1.00 94.97  ? 811  GLU   E CA  1 
ATOM   15000 C  C   . GLU   E 2 507 ? 49.757  -11.636 -19.838 1.00 90.56  ? 811  GLU   E C   1 
ATOM   15001 O  O   . GLU   E 2 507 ? 50.001  -11.526 -21.043 1.00 90.62  ? 811  GLU   E O   1 
ATOM   15002 C  CB  . GLU   E 2 507 ? 51.208  -10.190 -18.414 1.00 97.41  ? 811  GLU   E CB  1 
ATOM   15003 C  CG  . GLU   E 2 507 ? 50.064  -9.430  -17.755 1.00 94.54  ? 811  GLU   E CG  1 
ATOM   15004 C  CD  . GLU   E 2 507 ? 50.497  -8.045  -17.300 1.00 96.23  ? 811  GLU   E CD  1 
ATOM   15005 O  OE1 . GLU   E 2 507 ? 51.350  -7.432  -17.979 1.00 98.66  ? 811  GLU   E OE1 1 
ATOM   15006 O  OE2 . GLU   E 2 507 ? 50.007  -7.568  -16.256 1.00 96.04  ? 811  GLU   E OE2 1 
ATOM   15007 N  N   . TYR   E 2 508 ? 48.541  -11.795 -19.357 1.00 90.26  ? 812  TYR   E N   1 
ATOM   15008 C  CA  . TYR   E 2 508 ? 47.365  -11.913 -20.193 1.00 89.81  ? 812  TYR   E CA  1 
ATOM   15009 C  C   . TYR   E 2 508 ? 46.431  -10.776 -19.814 1.00 88.87  ? 812  TYR   E C   1 
ATOM   15010 O  O   . TYR   E 2 508 ? 46.130  -10.605 -18.631 1.00 87.63  ? 812  TYR   E O   1 
ATOM   15011 C  CB  . TYR   E 2 508 ? 46.703  -13.277 -19.970 1.00 92.01  ? 812  TYR   E CB  1 
ATOM   15012 C  CG  . TYR   E 2 508 ? 45.842  -13.715 -21.108 1.00 90.67  ? 812  TYR   E CG  1 
ATOM   15013 C  CD1 . TYR   E 2 508 ? 44.631  -13.076 -21.364 1.00 90.29  ? 812  TYR   E CD1 1 
ATOM   15014 C  CD2 . TYR   E 2 508 ? 46.238  -14.744 -21.948 1.00 89.48  ? 812  TYR   E CD2 1 
ATOM   15015 C  CE1 . TYR   E 2 508 ? 43.830  -13.447 -22.423 1.00 89.87  ? 812  TYR   E CE1 1 
ATOM   15016 C  CE2 . TYR   E 2 508 ? 45.435  -15.132 -23.020 1.00 93.93  ? 812  TYR   E CE2 1 
ATOM   15017 C  CZ  . TYR   E 2 508 ? 44.230  -14.470 -23.249 1.00 93.18  ? 812  TYR   E CZ  1 
ATOM   15018 O  OH  . TYR   E 2 508 ? 43.413  -14.816 -24.307 1.00 97.82  ? 812  TYR   E OH  1 
ATOM   15019 N  N   . ALA   E 2 509 ? 45.996  -9.991  -20.803 1.00 94.04  ? 813  ALA   E N   1 
ATOM   15020 C  CA  . ALA   E 2 509 ? 45.129  -8.836  -20.540 1.00 95.13  ? 813  ALA   E CA  1 
ATOM   15021 C  C   . ALA   E 2 509 ? 43.653  -9.212  -20.698 1.00 95.47  ? 813  ALA   E C   1 
ATOM   15022 O  O   . ALA   E 2 509 ? 43.254  -9.699  -21.761 1.00 98.19  ? 813  ALA   E O   1 
ATOM   15023 C  CB  . ALA   E 2 509 ? 45.483  -7.674  -21.482 1.00 90.52  ? 813  ALA   E CB  1 
ATOM   15024 N  N   . LEU   E 2 510 ? 42.838  -8.970  -19.654 1.00 86.52  ? 814  LEU   E N   1 
ATOM   15025 C  CA  . LEU   E 2 510 ? 41.441  -9.405  -19.644 1.00 83.27  ? 814  LEU   E CA  1 
ATOM   15026 C  C   . LEU   E 2 510 ? 40.437  -8.264  -19.637 1.00 86.36  ? 814  LEU   E C   1 
ATOM   15027 O  O   . LEU   E 2 510 ? 39.494  -8.270  -20.437 1.00 92.17  ? 814  LEU   E O   1 
ATOM   15028 C  CB  . LEU   E 2 510 ? 41.159  -10.309 -18.443 1.00 80.92  ? 814  LEU   E CB  1 
ATOM   15029 C  CG  . LEU   E 2 510 ? 42.156  -11.439 -18.210 1.00 86.76  ? 814  LEU   E CG  1 
ATOM   15030 C  CD1 . LEU   E 2 510 ? 41.970  -12.096 -16.849 1.00 87.79  ? 814  LEU   E CD1 1 
ATOM   15031 C  CD2 . LEU   E 2 510 ? 42.013  -12.468 -19.289 1.00 86.39  ? 814  LEU   E CD2 1 
ATOM   15032 N  N   . SER   E 2 511 ? 40.567  -7.305  -18.734 1.00 84.96  ? 815  SER   E N   1 
ATOM   15033 C  CA  . SER   E 2 511 ? 39.564  -6.261  -18.612 1.00 83.39  ? 815  SER   E CA  1 
ATOM   15034 C  C   . SER   E 2 511 ? 40.139  -4.909  -19.010 1.00 86.22  ? 815  SER   E C   1 
ATOM   15035 O  O   . SER   E 2 511 ? 41.337  -4.651  -18.873 1.00 87.81  ? 815  SER   E O   1 
ATOM   15036 C  CB  . SER   E 2 511 ? 38.999  -6.200  -17.192 1.00 86.46  ? 815  SER   E CB  1 
ATOM   15037 O  OG  . SER   E 2 511 ? 40.028  -6.199  -16.222 1.00 88.89  ? 815  SER   E OG  1 
ATOM   15038 N  N   . LEU   E 2 512 ? 39.264  -4.054  -19.529 1.00 89.24  ? 816  LEU   E N   1 
ATOM   15039 C  CA  . LEU   E 2 512 ? 39.636  -2.708  -19.933 1.00 86.22  ? 816  LEU   E CA  1 
ATOM   15040 C  C   . LEU   E 2 512 ? 38.505  -1.765  -19.566 1.00 89.91  ? 816  LEU   E C   1 
ATOM   15041 O  O   . LEU   E 2 512 ? 37.324  -2.142  -19.529 1.00 86.62  ? 816  LEU   E O   1 
ATOM   15042 C  CB  . LEU   E 2 512 ? 39.932  -2.617  -21.431 1.00 79.72  ? 816  LEU   E CB  1 
ATOM   15043 C  CG  . LEU   E 2 512 ? 40.655  -1.390  -21.966 1.00 80.29  ? 816  LEU   E CG  1 
ATOM   15044 C  CD1 . LEU   E 2 512 ? 42.065  -1.350  -21.473 1.00 83.31  ? 816  LEU   E CD1 1 
ATOM   15045 C  CD2 . LEU   E 2 512 ? 40.646  -1.404  -23.467 1.00 82.36  ? 816  LEU   E CD2 1 
ATOM   15046 N  N   . VAL   E 2 513 ? 38.887  -0.528  -19.268 1.00 92.39  ? 817  VAL   E N   1 
ATOM   15047 C  CA  . VAL   E 2 513 ? 37.928  0.483   -18.857 1.00 97.65  ? 817  VAL   E CA  1 
ATOM   15048 C  C   . VAL   E 2 513 ? 38.600  1.841   -19.021 1.00 98.98  ? 817  VAL   E C   1 
ATOM   15049 O  O   . VAL   E 2 513 ? 39.834  1.945   -19.054 1.00 96.39  ? 817  VAL   E O   1 
ATOM   15050 C  CB  . VAL   E 2 513 ? 37.431  0.207   -17.410 1.00 95.07  ? 817  VAL   E CB  1 
ATOM   15051 C  CG1 . VAL   E 2 513 ? 38.601  0.040   -16.460 1.00 91.94  ? 817  VAL   E CG1 1 
ATOM   15052 C  CG2 . VAL   E 2 513 ? 36.441  1.279   -16.933 1.00 97.43  ? 817  VAL   E CG2 1 
ATOM   15053 N  N   . SER   E 2 514 ? 37.780  2.875   -19.206 1.00 101.82 ? 818  SER   E N   1 
ATOM   15054 C  CA  . SER   E 2 514 ? 38.218  4.261   -19.255 1.00 101.58 ? 818  SER   E CA  1 
ATOM   15055 C  C   . SER   E 2 514 ? 37.333  5.041   -18.301 1.00 100.71 ? 818  SER   E C   1 
ATOM   15056 O  O   . SER   E 2 514 ? 36.104  4.984   -18.408 1.00 101.40 ? 818  SER   E O   1 
ATOM   15057 C  CB  . SER   E 2 514 ? 38.129  4.824   -20.677 1.00 102.98 ? 818  SER   E CB  1 
ATOM   15058 O  OG  . SER   E 2 514 ? 38.608  6.156   -20.751 1.00 101.93 ? 818  SER   E OG  1 
ATOM   15059 N  N   . CYS   E 2 515 ? 37.950  5.735   -17.351 1.00 107.58 ? 819  CYS   E N   1 
ATOM   15060 C  CA  . CYS   E 2 515 ? 37.199  6.566   -16.412 1.00 111.56 ? 819  CYS   E CA  1 
ATOM   15061 C  C   . CYS   E 2 515 ? 38.149  7.537   -15.709 1.00 110.57 ? 819  CYS   E C   1 
ATOM   15062 O  O   . CYS   E 2 515 ? 39.378  7.434   -15.792 1.00 104.14 ? 819  CYS   E O   1 
ATOM   15063 C  CB  . CYS   E 2 515 ? 36.440  5.710   -15.393 1.00 107.30 ? 819  CYS   E CB  1 
ATOM   15064 S  SG  . CYS   E 2 515 ? 37.524  4.617   -14.487 1.00 101.99 ? 819  CYS   E SG  1 
ATOM   15065 N  N   . LYS   E 2 516 ? 37.540  8.515   -15.034 1.00 113.44 ? 820  LYS   E N   1 
ATOM   15066 C  CA  . LYS   E 2 516 ? 38.210  9.383   -14.081 1.00 113.06 ? 820  LYS   E CA  1 
ATOM   15067 C  C   . LYS   E 2 516 ? 37.785  8.903   -12.695 1.00 113.98 ? 820  LYS   E C   1 
ATOM   15068 O  O   . LYS   E 2 516 ? 36.587  8.832   -12.397 1.00 111.99 ? 820  LYS   E O   1 
ATOM   15069 C  CB  . LYS   E 2 516 ? 37.866  10.860  -14.318 1.00 107.84 ? 820  LYS   E CB  1 
ATOM   15070 N  N   . LEU   E 2 517 ? 38.762  8.541   -11.865 1.00 113.69 ? 821  LEU   E N   1 
ATOM   15071 C  CA  . LEU   E 2 517 ? 38.528  7.945   -10.557 1.00 112.77 ? 821  LEU   E CA  1 
ATOM   15072 C  C   . LEU   E 2 517 ? 38.829  8.950   -9.450  1.00 113.89 ? 821  LEU   E C   1 
ATOM   15073 O  O   . LEU   E 2 517 ? 39.745  9.769   -9.566  1.00 116.72 ? 821  LEU   E O   1 
ATOM   15074 C  CB  . LEU   E 2 517 ? 39.406  6.699   -10.361 1.00 111.85 ? 821  LEU   E CB  1 
ATOM   15075 C  CG  . LEU   E 2 517 ? 39.191  5.473   -11.243 1.00 110.00 ? 821  LEU   E CG  1 
ATOM   15076 C  CD1 . LEU   E 2 517 ? 40.255  4.436   -10.933 1.00 110.06 ? 821  LEU   E CD1 1 
ATOM   15077 C  CD2 . LEU   E 2 517 ? 37.810  4.919   -11.005 1.00 111.74 ? 821  LEU   E CD2 1 
ATOM   15078 N  N   . GLY   E 2 518 ? 38.072  8.854   -8.352  1.00 110.96 ? 822  GLY   E N   1 
ATOM   15079 C  CA  . GLY   E 2 518 ? 38.260  9.779   -7.249  1.00 115.91 ? 822  GLY   E CA  1 
ATOM   15080 C  C   . GLY   E 2 518 ? 37.888  11.204  -7.633  1.00 117.80 ? 822  GLY   E C   1 
ATOM   15081 O  O   . GLY   E 2 518 ? 36.983  11.456  -8.435  1.00 117.37 ? 822  GLY   E O   1 
ATOM   15082 N  N   . LYS   E 2 519 ? 38.588  12.157  -7.032  1.00 119.54 ? 823  LYS   E N   1 
ATOM   15083 C  CA  . LYS   E 2 519 ? 38.452  13.543  -7.445  1.00 121.68 ? 823  LYS   E CA  1 
ATOM   15084 C  C   . LYS   E 2 519 ? 39.474  13.934  -8.505  1.00 122.77 ? 823  LYS   E C   1 
ATOM   15085 O  O   . LYS   E 2 519 ? 39.379  15.036  -9.054  1.00 122.03 ? 823  LYS   E O   1 
ATOM   15086 C  CB  . LYS   E 2 519 ? 38.551  14.472  -6.226  1.00 117.26 ? 823  LYS   E CB  1 
ATOM   15087 C  CG  . LYS   E 2 519 ? 37.442  14.201  -5.196  1.00 120.21 ? 823  LYS   E CG  1 
ATOM   15088 C  CD  . LYS   E 2 519 ? 36.086  13.963  -5.930  1.00 125.55 ? 823  LYS   E CD  1 
ATOM   15089 C  CE  . LYS   E 2 519 ? 34.847  14.343  -5.084  1.00 125.30 ? 823  LYS   E CE  1 
ATOM   15090 N  NZ  . LYS   E 2 519 ? 33.737  14.990  -5.879  1.00 103.90 ? 823  LYS   E NZ  1 
ATOM   15091 N  N   . ASP   E 2 520 ? 40.419  13.047  -8.805  1.00 124.63 ? 824  ASP   E N   1 
ATOM   15092 C  CA  . ASP   E 2 520 ? 41.404  13.246  -9.859  1.00 123.19 ? 824  ASP   E CA  1 
ATOM   15093 C  C   . ASP   E 2 520 ? 40.718  13.701  -11.146 1.00 125.76 ? 824  ASP   E C   1 
ATOM   15094 O  O   . ASP   E 2 520 ? 39.734  13.080  -11.570 1.00 128.10 ? 824  ASP   E O   1 
ATOM   15095 C  CB  . ASP   E 2 520 ? 42.136  11.925  -10.093 1.00 122.96 ? 824  ASP   E CB  1 
ATOM   15096 C  CG  . ASP   E 2 520 ? 43.441  12.104  -10.815 1.00 125.25 ? 824  ASP   E CG  1 
ATOM   15097 O  OD1 . ASP   E 2 520 ? 43.470  12.776  -11.872 1.00 124.69 ? 824  ASP   E OD1 1 
ATOM   15098 O  OD2 . ASP   E 2 520 ? 44.440  11.538  -10.327 1.00 130.78 ? 824  ASP   E OD2 1 
ATOM   15099 N  N   . PRO   E 2 521 ? 41.210  14.762  -11.804 1.00 122.70 ? 825  PRO   E N   1 
ATOM   15100 C  CA  . PRO   E 2 521 ? 40.502  15.283  -12.980 1.00 121.38 ? 825  PRO   E CA  1 
ATOM   15101 C  C   . PRO   E 2 521 ? 40.812  14.490  -14.230 1.00 123.39 ? 825  PRO   E C   1 
ATOM   15102 O  O   . PRO   E 2 521 ? 39.992  14.426  -15.160 1.00 122.32 ? 825  PRO   E O   1 
ATOM   15103 C  CB  . PRO   E 2 521 ? 41.034  16.709  -13.096 1.00 125.41 ? 825  PRO   E CB  1 
ATOM   15104 C  CG  . PRO   E 2 521 ? 42.449  16.581  -12.598 1.00 125.82 ? 825  PRO   E CG  1 
ATOM   15105 C  CD  . PRO   E 2 521 ? 42.403  15.567  -11.480 1.00 124.61 ? 825  PRO   E CD  1 
ATOM   15106 N  N   . ASN   E 2 522 ? 41.994  13.899  -14.265 1.00 122.08 ? 826  ASN   E N   1 
ATOM   15107 C  CA  . ASN   E 2 522 ? 42.449  13.186  -15.444 1.00 122.25 ? 826  ASN   E CA  1 
ATOM   15108 C  C   . ASN   E 2 522 ? 41.669  11.886  -15.616 1.00 122.28 ? 826  ASN   E C   1 
ATOM   15109 O  O   . ASN   E 2 522 ? 41.167  11.297  -14.651 1.00 119.83 ? 826  ASN   E O   1 
ATOM   15110 C  CB  . ASN   E 2 522 ? 43.944  12.901  -15.332 1.00 119.57 ? 826  ASN   E CB  1 
ATOM   15111 C  CG  . ASN   E 2 522 ? 44.678  13.957  -14.530 1.00 122.23 ? 826  ASN   E CG  1 
ATOM   15112 O  OD1 . ASN   E 2 522 ? 44.624  15.154  -14.840 1.00 127.47 ? 826  ASN   E OD1 1 
ATOM   15113 N  ND2 . ASN   E 2 522 ? 45.374  13.518  -13.485 1.00 123.09 ? 826  ASN   E ND2 1 
ATOM   15114 N  N   . THR   E 2 523 ? 41.555  11.454  -16.872 1.00 124.74 ? 827  THR   E N   1 
ATOM   15115 C  CA  . THR   E 2 523 ? 40.911  10.198  -17.221 1.00 121.59 ? 827  THR   E CA  1 
ATOM   15116 C  C   . THR   E 2 523 ? 41.981  9.160   -17.529 1.00 118.73 ? 827  THR   E C   1 
ATOM   15117 O  O   . THR   E 2 523 ? 42.963  9.451   -18.222 1.00 121.62 ? 827  THR   E O   1 
ATOM   15118 C  CB  . THR   E 2 523 ? 39.978  10.370  -18.420 1.00 119.12 ? 827  THR   E CB  1 
ATOM   15119 O  OG1 . THR   E 2 523 ? 39.176  11.538  -18.230 1.00 121.10 ? 827  THR   E OG1 1 
ATOM   15120 C  CG2 . THR   E 2 523 ? 39.068  9.196   -18.514 1.00 116.51 ? 827  THR   E CG2 1 
ATOM   15121 N  N   . TYR   E 2 524 ? 41.807  7.952   -16.989 1.00 112.31 ? 828  TYR   E N   1 
ATOM   15122 C  CA  . TYR   E 2 524 ? 42.844  6.934   -17.070 1.00 113.00 ? 828  TYR   E CA  1 
ATOM   15123 C  C   . TYR   E 2 524 ? 42.315  5.651   -17.698 1.00 113.46 ? 828  TYR   E C   1 
ATOM   15124 O  O   . TYR   E 2 524 ? 41.155  5.289   -17.499 1.00 113.58 ? 828  TYR   E O   1 
ATOM   15125 C  CB  . TYR   E 2 524 ? 43.402  6.626   -15.702 1.00 111.67 ? 828  TYR   E CB  1 
ATOM   15126 C  CG  . TYR   E 2 524 ? 43.992  7.812   -14.987 1.00 117.54 ? 828  TYR   E CG  1 
ATOM   15127 C  CD1 . TYR   E 2 524 ? 45.242  8.308   -15.341 1.00 116.81 ? 828  TYR   E CD1 1 
ATOM   15128 C  CD2 . TYR   E 2 524 ? 43.309  8.430   -13.937 1.00 121.30 ? 828  TYR   E CD2 1 
ATOM   15129 C  CE1 . TYR   E 2 524 ? 45.808  9.397   -14.671 1.00 120.70 ? 828  TYR   E CE1 1 
ATOM   15130 C  CE2 . TYR   E 2 524 ? 43.860  9.510   -13.259 1.00 124.32 ? 828  TYR   E CE2 1 
ATOM   15131 C  CZ  . TYR   E 2 524 ? 45.110  9.992   -13.631 1.00 124.00 ? 828  TYR   E CZ  1 
ATOM   15132 O  OH  . TYR   E 2 524 ? 45.660  11.069  -12.969 1.00 122.09 ? 828  TYR   E OH  1 
ATOM   15133 N  N   . PHE   E 2 525 ? 43.181  4.974   -18.465 1.00 109.56 ? 829  PHE   E N   1 
ATOM   15134 C  CA  . PHE   E 2 525 ? 42.914  3.656   -19.046 1.00 100.17 ? 829  PHE   E CA  1 
ATOM   15135 C  C   . PHE   E 2 525 ? 43.344  2.605   -18.028 1.00 99.34  ? 829  PHE   E C   1 
ATOM   15136 O  O   . PHE   E 2 525 ? 44.546  2.390   -17.835 1.00 98.77  ? 829  PHE   E O   1 
ATOM   15137 C  CB  . PHE   E 2 525 ? 43.705  3.451   -20.340 1.00 98.39  ? 829  PHE   E CB  1 
ATOM   15138 C  CG  . PHE   E 2 525 ? 43.118  4.106   -21.569 1.00 99.22  ? 829  PHE   E CG  1 
ATOM   15139 C  CD1 . PHE   E 2 525 ? 41.777  3.960   -21.898 1.00 100.80 ? 829  PHE   E CD1 1 
ATOM   15140 C  CD2 . PHE   E 2 525 ? 43.931  4.853   -22.420 1.00 97.53  ? 829  PHE   E CD2 1 
ATOM   15141 C  CE1 . PHE   E 2 525 ? 41.263  4.557   -23.055 1.00 97.44  ? 829  PHE   E CE1 1 
ATOM   15142 C  CE2 . PHE   E 2 525 ? 43.415  5.453   -23.563 1.00 96.66  ? 829  PHE   E CE2 1 
ATOM   15143 C  CZ  . PHE   E 2 525 ? 42.087  5.303   -23.877 1.00 94.48  ? 829  PHE   E CZ  1 
ATOM   15144 N  N   . ILE   E 2 526 ? 42.389  1.934   -17.384 1.00 99.36  ? 830  ILE   E N   1 
ATOM   15145 C  CA  . ILE   E 2 526 ? 42.714  0.894   -16.408 1.00 97.08  ? 830  ILE   E CA  1 
ATOM   15146 C  C   . ILE   E 2 526 ? 42.523  -0.480  -17.045 1.00 93.37  ? 830  ILE   E C   1 
ATOM   15147 O  O   . ILE   E 2 526 ? 41.479  -0.772  -17.649 1.00 88.98  ? 830  ILE   E O   1 
ATOM   15148 C  CB  . ILE   E 2 526 ? 41.892  1.042   -15.116 1.00 92.21  ? 830  ILE   E CB  1 
ATOM   15149 C  CG1 . ILE   E 2 526 ? 41.982  2.469   -14.601 1.00 89.55  ? 830  ILE   E CG1 1 
ATOM   15150 C  CG2 . ILE   E 2 526 ? 42.417  0.109   -14.044 1.00 89.09  ? 830  ILE   E CG2 1 
ATOM   15151 C  CD1 . ILE   E 2 526 ? 40.647  3.119   -14.483 1.00 90.98  ? 830  ILE   E CD1 1 
ATOM   15152 N  N   . VAL   E 2 527 ? 43.553  -1.310  -16.921 1.00 90.16  ? 831  VAL   E N   1 
ATOM   15153 C  CA  . VAL   E 2 527 ? 43.621  -2.641  -17.496 1.00 86.41  ? 831  VAL   E CA  1 
ATOM   15154 C  C   . VAL   E 2 527 ? 43.617  -3.651  -16.352 1.00 89.92  ? 831  VAL   E C   1 
ATOM   15155 O  O   . VAL   E 2 527 ? 44.139  -3.390  -15.261 1.00 91.12  ? 831  VAL   E O   1 
ATOM   15156 C  CB  . VAL   E 2 527 ? 44.893  -2.769  -18.367 1.00 86.33  ? 831  VAL   E CB  1 
ATOM   15157 C  CG1 . VAL   E 2 527 ? 45.043  -4.175  -18.928 1.00 88.18  ? 831  VAL   E CG1 1 
ATOM   15158 C  CG2 . VAL   E 2 527 ? 44.888  -1.723  -19.464 1.00 83.58  ? 831  VAL   E CG2 1 
ATOM   15159 N  N   . GLY   E 2 528 ? 43.010  -4.802  -16.591 1.00 90.81  ? 832  GLY   E N   1 
ATOM   15160 C  CA  . GLY   E 2 528 ? 43.074  -5.925  -15.662 1.00 89.01  ? 832  GLY   E CA  1 
ATOM   15161 C  C   . GLY   E 2 528 ? 43.703  -7.122  -16.344 1.00 86.44  ? 832  GLY   E C   1 
ATOM   15162 O  O   . GLY   E 2 528 ? 43.434  -7.384  -17.513 1.00 86.09  ? 832  GLY   E O   1 
ATOM   15163 N  N   . THR   E 2 529 ? 44.575  -7.818  -15.628 1.00 92.55  ? 833  THR   E N   1 
ATOM   15164 C  CA  . THR   E 2 529 ? 45.404  -8.826  -16.269 1.00 94.49  ? 833  THR   E CA  1 
ATOM   15165 C  C   . THR   E 2 529 ? 45.464  -10.098 -15.419 1.00 95.85  ? 833  THR   E C   1 
ATOM   15166 O  O   . THR   E 2 529 ? 44.902  -10.178 -14.318 1.00 94.70  ? 833  THR   E O   1 
ATOM   15167 C  CB  . THR   E 2 529 ? 46.817  -8.287  -16.538 1.00 96.08  ? 833  THR   E CB  1 
ATOM   15168 O  OG1 . THR   E 2 529 ? 47.620  -8.451  -15.361 1.00 100.26 ? 833  THR   E OG1 1 
ATOM   15169 C  CG2 . THR   E 2 529 ? 46.781  -6.799  -16.918 1.00 93.49  ? 833  THR   E CG2 1 
ATOM   15170 N  N   . ALA   E 2 530 ? 46.139  -11.111 -15.964 1.00 94.09  ? 834  ALA   E N   1 
ATOM   15171 C  CA  . ALA   E 2 530 ? 46.405  -12.352 -15.243 1.00 93.52  ? 834  ALA   E CA  1 
ATOM   15172 C  C   . ALA   E 2 530 ? 47.722  -12.939 -15.738 1.00 95.94  ? 834  ALA   E C   1 
ATOM   15173 O  O   . ALA   E 2 530 ? 47.893  -13.162 -16.939 1.00 93.55  ? 834  ALA   E O   1 
ATOM   15174 C  CB  . ALA   E 2 530 ? 45.259  -13.341 -15.436 1.00 93.22  ? 834  ALA   E CB  1 
ATOM   15175 N  N   . MET   E 2 531 ? 48.666  -13.168 -14.830 1.00 101.37 ? 835  MET   E N   1 
ATOM   15176 C  CA  . MET   E 2 531 ? 49.866  -13.920 -15.187 1.00 101.47 ? 835  MET   E CA  1 
ATOM   15177 C  C   . MET   E 2 531 ? 49.486  -15.382 -15.333 1.00 102.56 ? 835  MET   E C   1 
ATOM   15178 O  O   . MET   E 2 531 ? 48.989  -15.989 -14.376 1.00 107.56 ? 835  MET   E O   1 
ATOM   15179 C  CB  . MET   E 2 531 ? 50.960  -13.770 -14.129 1.00 102.13 ? 835  MET   E CB  1 
ATOM   15180 C  CG  . MET   E 2 531 ? 51.320  -12.344 -13.764 1.00 107.76 ? 835  MET   E CG  1 
ATOM   15181 S  SD  . MET   E 2 531 ? 51.825  -11.377 -15.188 1.00 105.12 ? 835  MET   E SD  1 
ATOM   15182 C  CE  . MET   E 2 531 ? 53.136  -12.378 -15.852 1.00 102.66 ? 835  MET   E CE  1 
ATOM   15183 N  N   . VAL   E 2 532 ? 49.711  -15.954 -16.518 1.00 100.40 ? 836  VAL   E N   1 
ATOM   15184 C  CA  . VAL   E 2 532 ? 49.286  -17.321 -16.807 1.00 102.24 ? 836  VAL   E CA  1 
ATOM   15185 C  C   . VAL   E 2 532 ? 50.474  -18.132 -17.299 1.00 103.02 ? 836  VAL   E C   1 
ATOM   15186 O  O   . VAL   E 2 532 ? 51.299  -17.630 -18.073 1.00 103.02 ? 836  VAL   E O   1 
ATOM   15187 C  CB  . VAL   E 2 532 ? 48.131  -17.357 -17.836 1.00 99.62  ? 836  VAL   E CB  1 
ATOM   15188 C  CG1 . VAL   E 2 532 ? 46.891  -16.671 -17.271 1.00 96.74  ? 836  VAL   E CG1 1 
ATOM   15189 C  CG2 . VAL   E 2 532 ? 48.545  -16.717 -19.157 1.00 98.92  ? 836  VAL   E CG2 1 
ATOM   15190 N  N   . TYR   E 2 533 ? 50.553  -19.387 -16.856 1.00 107.71 ? 837  TYR   E N   1 
ATOM   15191 C  CA  . TYR   E 2 533 ? 51.637  -20.306 -17.185 1.00 109.53 ? 837  TYR   E CA  1 
ATOM   15192 C  C   . TYR   E 2 533 ? 51.048  -21.682 -17.459 1.00 116.56 ? 837  TYR   E C   1 
ATOM   15193 O  O   . TYR   E 2 533 ? 49.992  -22.027 -16.913 1.00 120.60 ? 837  TYR   E O   1 
ATOM   15194 C  CB  . TYR   E 2 533 ? 52.678  -20.390 -16.053 1.00 108.47 ? 837  TYR   E CB  1 
ATOM   15195 C  CG  . TYR   E 2 533 ? 53.152  -19.026 -15.565 1.00 104.72 ? 837  TYR   E CG  1 
ATOM   15196 C  CD1 . TYR   E 2 533 ? 54.179  -18.345 -16.211 1.00 103.25 ? 837  TYR   E CD1 1 
ATOM   15197 C  CD2 . TYR   E 2 533 ? 52.562  -18.418 -14.463 1.00 106.71 ? 837  TYR   E CD2 1 
ATOM   15198 C  CE1 . TYR   E 2 533 ? 54.609  -17.094 -15.769 1.00 101.85 ? 837  TYR   E CE1 1 
ATOM   15199 C  CE2 . TYR   E 2 533 ? 52.977  -17.173 -14.013 1.00 106.11 ? 837  TYR   E CE2 1 
ATOM   15200 C  CZ  . TYR   E 2 533 ? 54.004  -16.513 -14.667 1.00 105.09 ? 837  TYR   E CZ  1 
ATOM   15201 O  OH  . TYR   E 2 533 ? 54.420  -15.272 -14.211 1.00 110.09 ? 837  TYR   E OH  1 
ATOM   15202 N  N   . PRO   E 2 534 ? 51.706  -22.487 -18.304 1.00 116.07 ? 838  PRO   E N   1 
ATOM   15203 C  CA  . PRO   E 2 534 ? 51.053  -23.704 -18.810 1.00 120.73 ? 838  PRO   E CA  1 
ATOM   15204 C  C   . PRO   E 2 534 ? 50.783  -24.729 -17.736 1.00 126.74 ? 838  PRO   E C   1 
ATOM   15205 O  O   . PRO   E 2 534 ? 49.864  -25.540 -17.890 1.00 126.45 ? 838  PRO   E O   1 
ATOM   15206 C  CB  . PRO   E 2 534 ? 52.054  -24.233 -19.843 1.00 123.08 ? 838  PRO   E CB  1 
ATOM   15207 C  CG  . PRO   E 2 534 ? 52.985  -23.115 -20.101 1.00 120.81 ? 838  PRO   E CG  1 
ATOM   15208 C  CD  . PRO   E 2 534 ? 53.064  -22.346 -18.839 1.00 114.88 ? 838  PRO   E CD  1 
ATOM   15209 N  N   . GLU   E 2 535 ? 51.559  -24.709 -16.652 1.00 131.46 ? 839  GLU   E N   1 
ATOM   15210 C  CA  . GLU   E 2 535 ? 51.359  -25.609 -15.519 1.00 134.32 ? 839  GLU   E CA  1 
ATOM   15211 C  C   . GLU   E 2 535 ? 50.286  -25.076 -14.573 1.00 131.45 ? 839  GLU   E C   1 
ATOM   15212 O  O   . GLU   E 2 535 ? 49.382  -25.818 -14.166 1.00 130.19 ? 839  GLU   E O   1 
ATOM   15213 C  CB  . GLU   E 2 535 ? 52.687  -25.804 -14.772 1.00 136.94 ? 839  GLU   E CB  1 
ATOM   15214 C  CG  . GLU   E 2 535 ? 53.921  -26.130 -15.670 1.00 140.42 ? 839  GLU   E CG  1 
ATOM   15215 C  CD  . GLU   E 2 535 ? 54.568  -24.897 -16.358 1.00 137.58 ? 839  GLU   E CD  1 
ATOM   15216 O  OE1 . GLU   E 2 535 ? 53.993  -23.788 -16.284 1.00 135.53 ? 839  GLU   E OE1 1 
ATOM   15217 O  OE2 . GLU   E 2 535 ? 55.656  -25.035 -16.977 1.00 138.40 ? 839  GLU   E OE2 1 
ATOM   15218 N  N   . GLU   E 2 536 ? 50.375  -23.791 -14.217 1.00 148.28 ? 840  GLU   E N   1 
ATOM   15219 C  CA  . GLU   E 2 536 ? 49.387  -23.143 -13.365 1.00 148.11 ? 840  GLU   E CA  1 
ATOM   15220 C  C   . GLU   E 2 536 ? 48.010  -23.250 -14.002 1.00 146.51 ? 840  GLU   E C   1 
ATOM   15221 O  O   . GLU   E 2 536 ? 47.748  -22.654 -15.055 1.00 145.33 ? 840  GLU   E O   1 
ATOM   15222 C  CB  . GLU   E 2 536 ? 49.743  -21.671 -13.109 1.00 150.96 ? 840  GLU   E CB  1 
ATOM   15223 C  CG  . GLU   E 2 536 ? 48.919  -20.973 -11.991 1.00 151.02 ? 840  GLU   E CG  1 
ATOM   15224 C  CD  . GLU   E 2 536 ? 48.594  -19.477 -12.289 1.00 153.31 ? 840  GLU   E CD  1 
ATOM   15225 O  OE1 . GLU   E 2 536 ? 48.433  -19.104 -13.486 1.00 154.03 ? 840  GLU   E OE1 1 
ATOM   15226 O  OE2 . GLU   E 2 536 ? 48.487  -18.677 -11.320 1.00 150.61 ? 840  GLU   E OE2 1 
ATOM   15227 N  N   . ALA   E 2 537 ? 47.134  -24.020 -13.368 1.00 123.62 ? 841  ALA   E N   1 
ATOM   15228 C  CA  . ALA   E 2 537 ? 45.784  -24.198 -13.853 1.00 114.04 ? 841  ALA   E CA  1 
ATOM   15229 C  C   . ALA   E 2 537 ? 44.920  -22.950 -13.571 1.00 108.59 ? 841  ALA   E C   1 
ATOM   15230 O  O   . ALA   E 2 537 ? 44.550  -22.212 -14.499 1.00 106.31 ? 841  ALA   E O   1 
ATOM   15231 C  CB  . ALA   E 2 537 ? 45.133  -25.424 -13.190 1.00 109.88 ? 841  ALA   E CB  1 
ATOM   15232 N  N   . GLU   E 2 538 ? 44.606  -22.714 -12.282 1.00 105.04 ? 842  GLU   E N   1 
ATOM   15233 C  CA  . GLU   E 2 538 ? 43.856  -21.551 -11.853 1.00 97.71  ? 842  GLU   E CA  1 
ATOM   15234 C  C   . GLU   E 2 538 ? 44.790  -20.360 -11.715 1.00 104.79 ? 842  GLU   E C   1 
ATOM   15235 O  O   . GLU   E 2 538 ? 45.902  -20.525 -11.224 1.00 111.43 ? 842  GLU   E O   1 
ATOM   15236 C  CB  . GLU   E 2 538 ? 43.164  -21.783 -10.505 1.00 93.70  ? 842  GLU   E CB  1 
ATOM   15237 C  CG  . GLU   E 2 538 ? 41.730  -22.226 -10.636 1.00 99.44  ? 842  GLU   E CG  1 
ATOM   15238 C  CD  . GLU   E 2 538 ? 41.425  -23.400 -9.714  1.00 113.84 ? 842  GLU   E CD  1 
ATOM   15239 O  OE1 . GLU   E 2 538 ? 42.236  -23.606 -8.783  1.00 119.70 ? 842  GLU   E OE1 1 
ATOM   15240 O  OE2 . GLU   E 2 538 ? 40.400  -24.115 -9.898  1.00 105.56 ? 842  GLU   E OE2 1 
ATOM   15241 N  N   . PRO   E 2 539 ? 44.369  -19.157 -12.105 1.00 101.35 ? 843  PRO   E N   1 
ATOM   15242 C  CA  . PRO   E 2 539 ? 45.277  -18.003 -12.029 1.00 103.91 ? 843  PRO   E CA  1 
ATOM   15243 C  C   . PRO   E 2 539 ? 45.433  -17.506 -10.593 1.00 107.44 ? 843  PRO   E C   1 
ATOM   15244 O  O   . PRO   E 2 539 ? 44.440  -17.257 -9.903  1.00 104.53 ? 843  PRO   E O   1 
ATOM   15245 C  CB  . PRO   E 2 539 ? 44.586  -16.960 -12.909 1.00 99.38  ? 843  PRO   E CB  1 
ATOM   15246 C  CG  . PRO   E 2 539 ? 43.129  -17.280 -12.734 1.00 95.87  ? 843  PRO   E CG  1 
ATOM   15247 C  CD  . PRO   E 2 539 ? 43.030  -18.778 -12.592 1.00 95.93  ? 843  PRO   E CD  1 
ATOM   15248 N  N   . LYS   E 2 540 ? 46.689  -17.333 -10.144 1.00 109.63 ? 844  LYS   E N   1 
ATOM   15249 C  CA  . LYS   E 2 540 ? 46.951  -16.910 -8.769  1.00 102.89 ? 844  LYS   E CA  1 
ATOM   15250 C  C   . LYS   E 2 540 ? 47.705  -15.587 -8.628  1.00 103.27 ? 844  LYS   E C   1 
ATOM   15251 O  O   . LYS   E 2 540 ? 47.965  -15.159 -7.500  1.00 103.46 ? 844  LYS   E O   1 
ATOM   15252 C  CB  . LYS   E 2 540 ? 47.699  -18.022 -8.026  1.00 100.30 ? 844  LYS   E CB  1 
ATOM   15253 C  CG  . LYS   E 2 540 ? 46.776  -19.177 -7.722  1.00 104.61 ? 844  LYS   E CG  1 
ATOM   15254 C  CD  . LYS   E 2 540 ? 47.547  -20.430 -7.359  1.00 115.40 ? 844  LYS   E CD  1 
ATOM   15255 C  CE  . LYS   E 2 540 ? 46.626  -21.642 -7.271  1.00 124.67 ? 844  LYS   E CE  1 
ATOM   15256 N  NZ  . LYS   E 2 540 ? 47.277  -22.851 -6.670  1.00 145.85 ? 844  LYS   E NZ  1 
ATOM   15257 N  N   . GLN   E 2 541 ? 48.053  -14.910 -9.716  1.00 103.64 ? 845  GLN   E N   1 
ATOM   15258 C  CA  . GLN   E 2 541 ? 48.571  -13.554 -9.603  1.00 102.09 ? 845  GLN   E CA  1 
ATOM   15259 C  C   . GLN   E 2 541 ? 48.243  -12.820 -10.889 1.00 101.62 ? 845  GLN   E C   1 
ATOM   15260 O  O   . GLN   E 2 541 ? 48.203  -13.423 -11.961 1.00 105.46 ? 845  GLN   E O   1 
ATOM   15261 C  CB  . GLN   E 2 541 ? 50.079  -13.527 -9.340  1.00 107.34 ? 845  GLN   E CB  1 
ATOM   15262 C  CG  . GLN   E 2 541 ? 50.869  -14.324 -10.357 1.00 117.57 ? 845  GLN   E CG  1 
ATOM   15263 C  CD  . GLN   E 2 541 ? 52.357  -14.271 -10.116 1.00 125.93 ? 845  GLN   E CD  1 
ATOM   15264 O  OE1 . GLN   E 2 541 ? 52.807  -14.045 -8.989  1.00 129.36 ? 845  GLN   E OE1 1 
ATOM   15265 N  NE2 . GLN   E 2 541 ? 53.138  -14.473 -11.180 1.00 127.48 ? 845  GLN   E NE2 1 
ATOM   15266 N  N   . GLY   E 2 542 ? 47.985  -11.528 -10.775 1.00 103.38 ? 846  GLY   E N   1 
ATOM   15267 C  CA  . GLY   E 2 542 ? 47.609  -10.706 -11.901 1.00 100.79 ? 846  GLY   E CA  1 
ATOM   15268 C  C   . GLY   E 2 542 ? 47.904  -9.275  -11.556 1.00 101.06 ? 846  GLY   E C   1 
ATOM   15269 O  O   . GLY   E 2 542 ? 48.631  -8.992  -10.603 1.00 105.68 ? 846  GLY   E O   1 
ATOM   15270 N  N   . ARG   E 2 543 ? 47.298  -8.352  -12.302 1.00 94.75  ? 847  ARG   E N   1 
ATOM   15271 C  CA  . ARG   E 2 543 ? 47.752  -6.969  -12.211 1.00 95.01  ? 847  ARG   E CA  1 
ATOM   15272 C  C   . ARG   E 2 543 ? 46.662  -6.000  -12.647 1.00 95.59  ? 847  ARG   E C   1 
ATOM   15273 O  O   . ARG   E 2 543 ? 46.096  -6.146  -13.738 1.00 97.82  ? 847  ARG   E O   1 
ATOM   15274 C  CB  . ARG   E 2 543 ? 49.021  -6.785  -13.067 1.00 93.96  ? 847  ARG   E CB  1 
ATOM   15275 C  CG  . ARG   E 2 543 ? 49.694  -5.438  -12.968 1.00 93.73  ? 847  ARG   E CG  1 
ATOM   15276 C  CD  . ARG   E 2 543 ? 51.142  -5.553  -13.382 1.00 96.65  ? 847  ARG   E CD  1 
ATOM   15277 N  NE  . ARG   E 2 543 ? 51.280  -5.754  -14.817 1.00 96.45  ? 847  ARG   E NE  1 
ATOM   15278 C  CZ  . ARG   E 2 543 ? 51.782  -4.853  -15.651 1.00 99.35  ? 847  ARG   E CZ  1 
ATOM   15279 N  NH1 . ARG   E 2 543 ? 52.230  -3.686  -15.221 1.00 101.87 ? 847  ARG   E NH1 1 
ATOM   15280 N  NH2 . ARG   E 2 543 ? 51.854  -5.137  -16.948 1.00 100.66 ? 847  ARG   E NH2 1 
ATOM   15281 N  N   . ILE   E 2 544 ? 46.397  -4.995  -11.814 1.00 93.67  ? 848  ILE   E N   1 
ATOM   15282 C  CA  . ILE   E 2 544 ? 45.642  -3.813  -12.218 1.00 89.84  ? 848  ILE   E CA  1 
ATOM   15283 C  C   . ILE   E 2 544 ? 46.637  -2.692  -12.459 1.00 93.74  ? 848  ILE   E C   1 
ATOM   15284 O  O   . ILE   E 2 544 ? 47.454  -2.382  -11.584 1.00 96.07  ? 848  ILE   E O   1 
ATOM   15285 C  CB  . ILE   E 2 544 ? 44.617  -3.408  -11.157 1.00 86.91  ? 848  ILE   E CB  1 
ATOM   15286 C  CG1 . ILE   E 2 544 ? 43.732  -4.588  -10.815 1.00 90.59  ? 848  ILE   E CG1 1 
ATOM   15287 C  CG2 . ILE   E 2 544 ? 43.796  -2.240  -11.656 1.00 86.13  ? 848  ILE   E CG2 1 
ATOM   15288 C  CD1 . ILE   E 2 544 ? 42.867  -4.347  -9.626  1.00 89.45  ? 848  ILE   E CD1 1 
ATOM   15289 N  N   . VAL   E 2 545 ? 46.588  -2.100  -13.650 1.00 92.86  ? 849  VAL   E N   1 
ATOM   15290 C  CA  . VAL   E 2 545 ? 47.506  -1.039  -14.056 1.00 92.13  ? 849  VAL   E CA  1 
ATOM   15291 C  C   . VAL   E 2 545 ? 46.699  0.147   -14.543 1.00 94.66  ? 849  VAL   E C   1 
ATOM   15292 O  O   . VAL   E 2 545 ? 45.738  -0.010  -15.305 1.00 94.55  ? 849  VAL   E O   1 
ATOM   15293 C  CB  . VAL   E 2 545 ? 48.477  -1.478  -15.164 1.00 90.41  ? 849  VAL   E CB  1 
ATOM   15294 C  CG1 . VAL   E 2 545 ? 49.600  -2.233  -14.585 1.00 94.46  ? 849  VAL   E CG1 1 
ATOM   15295 C  CG2 . VAL   E 2 545 ? 47.767  -2.350  -16.134 1.00 96.21  ? 849  VAL   E CG2 1 
ATOM   15296 N  N   . VAL   E 2 546 ? 47.112  1.336   -14.124 1.00 97.14  ? 850  VAL   E N   1 
ATOM   15297 C  CA  . VAL   E 2 546 ? 46.481  2.585   -14.527 1.00 97.46  ? 850  VAL   E CA  1 
ATOM   15298 C  C   . VAL   E 2 546 ? 47.402  3.294   -15.504 1.00 100.80 ? 850  VAL   E C   1 
ATOM   15299 O  O   . VAL   E 2 546 ? 48.588  3.474   -15.216 1.00 103.78 ? 850  VAL   E O   1 
ATOM   15300 C  CB  . VAL   E 2 546 ? 46.189  3.476   -13.316 1.00 95.07  ? 850  VAL   E CB  1 
ATOM   15301 C  CG1 . VAL   E 2 546 ? 45.294  4.598   -13.725 1.00 96.82  ? 850  VAL   E CG1 1 
ATOM   15302 C  CG2 . VAL   E 2 546 ? 45.563  2.661   -12.230 1.00 94.30  ? 850  VAL   E CG2 1 
ATOM   15303 N  N   . PHE   E 2 547 ? 46.860  3.701   -16.652 1.00 103.02 ? 851  PHE   E N   1 
ATOM   15304 C  CA  . PHE   E 2 547 ? 47.613  4.394   -17.686 1.00 102.25 ? 851  PHE   E CA  1 
ATOM   15305 C  C   . PHE   E 2 547 ? 47.050  5.803   -17.874 1.00 106.46 ? 851  PHE   E C   1 
ATOM   15306 O  O   . PHE   E 2 547 ? 46.059  6.190   -17.246 1.00 105.53 ? 851  PHE   E O   1 
ATOM   15307 C  CB  . PHE   E 2 547 ? 47.572  3.623   -19.013 1.00 102.57 ? 851  PHE   E CB  1 
ATOM   15308 C  CG  . PHE   E 2 547 ? 48.265  2.272   -18.971 1.00 103.13 ? 851  PHE   E CG  1 
ATOM   15309 C  CD1 . PHE   E 2 547 ? 47.578  1.130   -18.563 1.00 98.93  ? 851  PHE   E CD1 1 
ATOM   15310 C  CD2 . PHE   E 2 547 ? 49.596  2.136   -19.365 1.00 103.86 ? 851  PHE   E CD2 1 
ATOM   15311 C  CE1 . PHE   E 2 547 ? 48.207  -0.103  -18.528 1.00 97.79  ? 851  PHE   E CE1 1 
ATOM   15312 C  CE2 . PHE   E 2 547 ? 50.230  0.883   -19.333 1.00 97.55  ? 851  PHE   E CE2 1 
ATOM   15313 C  CZ  . PHE   E 2 547 ? 49.531  -0.228  -18.913 1.00 95.16  ? 851  PHE   E CZ  1 
ATOM   15314 N  N   . GLN   E 2 548 ? 47.704  6.556   -18.759 1.00 116.75 ? 852  GLN   E N   1 
ATOM   15315 C  CA  . GLN   E 2 548 ? 47.201  7.842   -19.232 1.00 120.75 ? 852  GLN   E CA  1 
ATOM   15316 C  C   . GLN   E 2 548 ? 47.795  8.149   -20.605 1.00 124.20 ? 852  GLN   E C   1 
ATOM   15317 O  O   . GLN   E 2 548 ? 49.021  8.238   -20.744 1.00 121.59 ? 852  GLN   E O   1 
ATOM   15318 C  CB  . GLN   E 2 548 ? 47.541  8.949   -18.243 1.00 119.25 ? 852  GLN   E CB  1 
ATOM   15319 C  CG  . GLN   E 2 548 ? 47.094  10.316  -18.700 1.00 127.49 ? 852  GLN   E CG  1 
ATOM   15320 C  CD  . GLN   E 2 548 ? 47.311  11.372  -17.633 1.00 125.27 ? 852  GLN   E CD  1 
ATOM   15321 O  OE1 . GLN   E 2 548 ? 46.358  11.856  -17.013 1.00 123.89 ? 852  GLN   E OE1 1 
ATOM   15322 N  NE2 . GLN   E 2 548 ? 48.570  11.736  -17.411 1.00 125.72 ? 852  GLN   E NE2 1 
ATOM   15323 N  N   . TYR   E 2 549 ? 46.944  8.330   -21.614 1.00 127.70 ? 853  TYR   E N   1 
ATOM   15324 C  CA  . TYR   E 2 549 ? 47.495  8.758   -22.927 1.00 126.48 ? 853  TYR   E CA  1 
ATOM   15325 C  C   . TYR   E 2 549 ? 47.356  10.259  -22.981 1.00 130.35 ? 853  TYR   E C   1 
ATOM   15326 O  O   . TYR   E 2 549 ? 48.274  10.907  -23.507 1.00 131.24 ? 853  TYR   E O   1 
ATOM   15327 C  CB  . TYR   E 2 549 ? 46.835  8.182   -24.180 1.00 117.11 ? 853  TYR   E CB  1 
ATOM   15328 C  CG  . TYR   E 2 549 ? 47.695  8.407   -25.415 1.00 116.92 ? 853  TYR   E CG  1 
ATOM   15329 C  CD1 . TYR   E 2 549 ? 48.840  7.653   -25.633 1.00 119.76 ? 853  TYR   E CD1 1 
ATOM   15330 C  CD2 . TYR   E 2 549 ? 47.383  9.395   -26.340 1.00 112.69 ? 853  TYR   E CD2 1 
ATOM   15331 C  CE1 . TYR   E 2 549 ? 49.636  7.857   -26.746 1.00 117.92 ? 853  TYR   E CE1 1 
ATOM   15332 C  CE2 . TYR   E 2 549 ? 48.175  9.612   -27.454 1.00 112.15 ? 853  TYR   E CE2 1 
ATOM   15333 C  CZ  . TYR   E 2 549 ? 49.303  8.840   -27.658 1.00 117.20 ? 853  TYR   E CZ  1 
ATOM   15334 O  OH  . TYR   E 2 549 ? 50.089  9.046   -28.754 1.00 117.12 ? 853  TYR   E OH  1 
ATOM   15335 N  N   . SER   E 2 550 ? 46.252  10.783  -22.442 1.00 139.99 ? 854  SER   E N   1 
ATOM   15336 C  CA  . SER   E 2 550 ? 46.011  12.249  -22.419 1.00 144.14 ? 854  SER   E CA  1 
ATOM   15337 C  C   . SER   E 2 550 ? 47.322  12.982  -22.117 1.00 147.04 ? 854  SER   E C   1 
ATOM   15338 O  O   . SER   E 2 550 ? 47.531  13.324  -20.933 1.00 148.34 ? 854  SER   E O   1 
ATOM   15339 C  CB  . SER   E 2 550 ? 44.944  12.616  -21.419 1.00 142.08 ? 854  SER   E CB  1 
ATOM   15340 O  OG  . SER   E 2 550 ? 44.180  11.478  -21.047 1.00 140.77 ? 854  SER   E OG  1 
ATOM   15341 N  N   . ASP   E 2 551 ? 48.131  13.249  -23.147 1.00 140.19 ? 855  ASP   E N   1 
ATOM   15342 C  CA  . ASP   E 2 551 ? 49.453  13.900  -22.966 1.00 139.37 ? 855  ASP   E CA  1 
ATOM   15343 C  C   . ASP   E 2 551 ? 50.169  13.892  -24.311 1.00 137.46 ? 855  ASP   E C   1 
ATOM   15344 O  O   . ASP   E 2 551 ? 50.398  14.980  -24.876 1.00 138.35 ? 855  ASP   E O   1 
ATOM   15345 C  CB  . ASP   E 2 551 ? 50.315  13.145  -21.970 1.00 135.33 ? 855  ASP   E CB  1 
ATOM   15346 N  N   . GLY   E 2 552 ? 50.493  12.699  -24.802 1.00 132.50 ? 856  GLY   E N   1 
ATOM   15347 C  CA  . GLY   E 2 552 ? 51.232  12.564  -26.068 1.00 127.20 ? 856  GLY   E CA  1 
ATOM   15348 C  C   . GLY   E 2 552 ? 51.832  11.179  -26.108 1.00 131.29 ? 856  GLY   E C   1 
ATOM   15349 O  O   . GLY   E 2 552 ? 52.195  10.719  -27.208 1.00 131.90 ? 856  GLY   E O   1 
ATOM   15350 N  N   . LYS   E 2 553 ? 51.912  10.530  -24.945 1.00 130.26 ? 857  LYS   E N   1 
ATOM   15351 C  CA  . LYS   E 2 553 ? 52.440  9.146   -24.876 1.00 129.77 ? 857  LYS   E CA  1 
ATOM   15352 C  C   . LYS   E 2 553 ? 51.732  8.395   -23.741 1.00 128.73 ? 857  LYS   E C   1 
ATOM   15353 O  O   . LYS   E 2 553 ? 50.908  9.020   -23.043 1.00 129.01 ? 857  LYS   E O   1 
ATOM   15354 C  CB  . LYS   E 2 553 ? 53.956  9.167   -24.669 1.00 131.14 ? 857  LYS   E CB  1 
ATOM   15355 N  N   . LEU   E 2 554 ? 52.043  7.108   -23.570 1.00 121.16 ? 858  LEU   E N   1 
ATOM   15356 C  CA  . LEU   E 2 554 ? 51.381  6.281   -22.531 1.00 117.27 ? 858  LEU   E CA  1 
ATOM   15357 C  C   . LEU   E 2 554 ? 52.277  6.219   -21.293 1.00 119.43 ? 858  LEU   E C   1 
ATOM   15358 O  O   . LEU   E 2 554 ? 53.460  5.853   -21.435 1.00 116.21 ? 858  LEU   E O   1 
ATOM   15359 C  CB  . LEU   E 2 554 ? 51.111  4.885   -23.081 1.00 111.67 ? 858  LEU   E CB  1 
ATOM   15360 C  CG  . LEU   E 2 554 ? 49.928  4.136   -22.466 1.00 104.05 ? 858  LEU   E CG  1 
ATOM   15361 C  CD1 . LEU   E 2 554 ? 48.755  5.079   -22.298 1.00 110.53 ? 858  LEU   E CD1 1 
ATOM   15362 C  CD2 . LEU   E 2 554 ? 49.552  2.972   -23.361 1.00 100.62 ? 858  LEU   E CD2 1 
ATOM   15363 N  N   . GLN   E 2 555 ? 51.726  6.560   -20.131 1.00 117.84 ? 859  GLN   E N   1 
ATOM   15364 C  CA  . GLN   E 2 555 ? 52.474  6.508   -18.882 1.00 114.49 ? 859  GLN   E CA  1 
ATOM   15365 C  C   . GLN   E 2 555 ? 51.710  5.661   -17.877 1.00 109.09 ? 859  GLN   E C   1 
ATOM   15366 O  O   . GLN   E 2 555 ? 50.496  5.824   -17.712 1.00 106.81 ? 859  GLN   E O   1 
ATOM   15367 C  CB  . GLN   E 2 555 ? 52.744  7.917   -18.314 1.00 111.35 ? 859  GLN   E CB  1 
ATOM   15368 N  N   . THR   E 2 556 ? 52.432  4.760   -17.211 1.00 108.55 ? 860  THR   E N   1 
ATOM   15369 C  CA  . THR   E 2 556 ? 51.876  3.915   -16.158 1.00 105.33 ? 860  THR   E CA  1 
ATOM   15370 C  C   . THR   E 2 556 ? 51.723  4.727   -14.864 1.00 105.02 ? 860  THR   E C   1 
ATOM   15371 O  O   . THR   E 2 556 ? 52.716  5.165   -14.279 1.00 109.19 ? 860  THR   E O   1 
ATOM   15372 C  CB  . THR   E 2 556 ? 52.777  2.699   -15.941 1.00 108.49 ? 860  THR   E CB  1 
ATOM   15373 O  OG1 . THR   E 2 556 ? 53.312  2.257   -17.204 1.00 110.19 ? 860  THR   E OG1 1 
ATOM   15374 C  CG2 . THR   E 2 556 ? 51.983  1.566   -15.303 1.00 109.69 ? 860  THR   E CG2 1 
ATOM   15375 N  N   . VAL   E 2 557 ? 50.485  4.915   -14.401 1.00 106.55 ? 861  VAL   E N   1 
ATOM   15376 C  CA  . VAL   E 2 557 ? 50.228  5.736   -13.220 1.00 102.69 ? 861  VAL   E CA  1 
ATOM   15377 C  C   . VAL   E 2 557 ? 50.178  4.932   -11.898 1.00 103.56 ? 861  VAL   E C   1 
ATOM   15378 O  O   . VAL   E 2 557 ? 50.322  5.532   -10.826 1.00 105.03 ? 861  VAL   E O   1 
ATOM   15379 C  CB  . VAL   E 2 557 ? 48.937  6.556   -13.464 1.00 100.78 ? 861  VAL   E CB  1 
ATOM   15380 C  CG1 . VAL   E 2 557 ? 48.645  7.527   -12.342 1.00 102.78 ? 861  VAL   E CG1 1 
ATOM   15381 C  CG2 . VAL   E 2 557 ? 49.070  7.343   -14.760 1.00 104.57 ? 861  VAL   E CG2 1 
ATOM   15382 N  N   . ALA   E 2 558 ? 50.036  3.598   -11.949 1.00 103.93 ? 862  ALA   E N   1 
ATOM   15383 C  CA  . ALA   E 2 558 ? 49.998  2.712   -10.774 1.00 102.00 ? 862  ALA   E CA  1 
ATOM   15384 C  C   . ALA   E 2 558 ? 49.908  1.257   -11.221 1.00 99.59  ? 862  ALA   E C   1 
ATOM   15385 O  O   . ALA   E 2 558 ? 49.504  0.965   -12.346 1.00 99.16  ? 862  ALA   E O   1 
ATOM   15386 C  CB  . ALA   E 2 558 ? 48.818  3.023   -9.836  1.00 101.32 ? 862  ALA   E CB  1 
ATOM   15387 N  N   . GLU   E 2 559 ? 50.280  0.341   -10.320 1.00 105.68 ? 863  GLU   E N   1 
ATOM   15388 C  CA  . GLU   E 2 559 ? 50.128  -1.099  -10.569 1.00 104.98 ? 863  GLU   E CA  1 
ATOM   15389 C  C   . GLU   E 2 559 ? 49.825  -1.777  -9.234  1.00 106.41 ? 863  GLU   E C   1 
ATOM   15390 O  O   . GLU   E 2 559 ? 50.739  -1.985  -8.434  1.00 110.99 ? 863  GLU   E O   1 
ATOM   15391 C  CB  . GLU   E 2 559 ? 51.373  -1.711  -11.197 1.00 106.87 ? 863  GLU   E CB  1 
ATOM   15392 C  CG  . GLU   E 2 559 ? 52.111  -0.873  -12.246 1.00 115.54 ? 863  GLU   E CG  1 
ATOM   15393 C  CD  . GLU   E 2 559 ? 53.503  -1.428  -12.530 1.00 118.78 ? 863  GLU   E CD  1 
ATOM   15394 O  OE1 . GLU   E 2 559 ? 53.780  -2.552  -12.043 1.00 114.76 ? 863  GLU   E OE1 1 
ATOM   15395 O  OE2 . GLU   E 2 559 ? 54.310  -0.761  -13.231 1.00 125.82 ? 863  GLU   E OE2 1 
ATOM   15396 N  N   . LYS   E 2 560 ? 48.562  -2.122  -8.999  1.00 101.93 ? 864  LYS   E N   1 
ATOM   15397 C  CA  . LYS   E 2 560 ? 48.213  -2.901  -7.816  1.00 98.15  ? 864  LYS   E CA  1 
ATOM   15398 C  C   . LYS   E 2 560 ? 48.272  -4.372  -8.196  1.00 99.09  ? 864  LYS   E C   1 
ATOM   15399 O  O   . LYS   E 2 560 ? 47.524  -4.820  -9.069  1.00 99.39  ? 864  LYS   E O   1 
ATOM   15400 C  CB  . LYS   E 2 560 ? 46.831  -2.538  -7.278  1.00 98.57  ? 864  LYS   E CB  1 
ATOM   15401 C  CG  . LYS   E 2 560 ? 46.551  -3.158  -5.928  1.00 103.24 ? 864  LYS   E CG  1 
ATOM   15402 C  CD  . LYS   E 2 560 ? 46.889  -2.206  -4.785  1.00 111.02 ? 864  LYS   E CD  1 
ATOM   15403 C  CE  . LYS   E 2 560 ? 47.167  -2.986  -3.510  1.00 113.02 ? 864  LYS   E CE  1 
ATOM   15404 N  NZ  . LYS   E 2 560 ? 48.574  -3.431  -3.465  1.00 107.30 ? 864  LYS   E NZ  1 
ATOM   15405 N  N   . GLU   E 2 561 ? 49.199  -5.101  -7.574  1.00 99.95  ? 865  GLU   E N   1 
ATOM   15406 C  CA  . GLU   E 2 561 ? 49.300  -6.540  -7.757  1.00 96.81  ? 865  GLU   E CA  1 
ATOM   15407 C  C   . GLU   E 2 561 ? 48.138  -7.209  -7.041  1.00 100.26 ? 865  GLU   E C   1 
ATOM   15408 O  O   . GLU   E 2 561 ? 47.847  -6.882  -5.886  1.00 103.71 ? 865  GLU   E O   1 
ATOM   15409 C  CB  . GLU   E 2 561 ? 50.633  -7.042  -7.208  1.00 106.04 ? 865  GLU   E CB  1 
ATOM   15410 C  CG  . GLU   E 2 561 ? 50.741  -8.559  -7.081  1.00 116.24 ? 865  GLU   E CG  1 
ATOM   15411 C  CD  . GLU   E 2 561 ? 52.014  -9.023  -6.363  1.00 124.30 ? 865  GLU   E CD  1 
ATOM   15412 O  OE1 . GLU   E 2 561 ? 52.671  -8.189  -5.693  1.00 118.74 ? 865  GLU   E OE1 1 
ATOM   15413 O  OE2 . GLU   E 2 561 ? 52.355  -10.227 -6.471  1.00 131.77 ? 865  GLU   E OE2 1 
ATOM   15414 N  N   . VAL   E 2 562 ? 47.441  -8.106  -7.742  1.00 100.34 ? 866  VAL   E N   1 
ATOM   15415 C  CA  . VAL   E 2 562 ? 46.329  -8.869  -7.183  1.00 97.87  ? 866  VAL   E CA  1 
ATOM   15416 C  C   . VAL   E 2 562 ? 46.666  -10.343 -7.331  1.00 96.39  ? 866  VAL   E C   1 
ATOM   15417 O  O   . VAL   E 2 562 ? 47.372  -10.735 -8.265  1.00 100.80 ? 866  VAL   E O   1 
ATOM   15418 C  CB  . VAL   E 2 562 ? 44.980  -8.531  -7.865  1.00 94.77  ? 866  VAL   E CB  1 
ATOM   15419 C  CG1 . VAL   E 2 562 ? 44.520  -7.108  -7.501  1.00 90.84  ? 866  VAL   E CG1 1 
ATOM   15420 C  CG2 . VAL   E 2 562 ? 45.100  -8.655  -9.355  1.00 97.88  ? 866  VAL   E CG2 1 
ATOM   15421 N  N   . LYS   E 2 563 ? 46.176  -11.161 -6.395  1.00 96.78  ? 867  LYS   E N   1 
ATOM   15422 C  CA  . LYS   E 2 563 ? 46.558  -12.571 -6.329  1.00 97.84  ? 867  LYS   E CA  1 
ATOM   15423 C  C   . LYS   E 2 563 ? 45.536  -13.426 -7.082  1.00 96.79  ? 867  LYS   E C   1 
ATOM   15424 O  O   . LYS   E 2 563 ? 44.927  -14.340 -6.548  1.00 96.14  ? 867  LYS   E O   1 
ATOM   15425 C  CB  . LYS   E 2 563 ? 46.710  -13.030 -4.874  1.00 93.14  ? 867  LYS   E CB  1 
ATOM   15426 N  N   . GLY   E 2 564 ? 45.361  -13.081 -8.354  1.00 100.94 ? 868  GLY   E N   1 
ATOM   15427 C  CA  . GLY   E 2 564 ? 44.446  -13.806 -9.214  1.00 100.82 ? 868  GLY   E CA  1 
ATOM   15428 C  C   . GLY   E 2 564 ? 44.227  -13.037 -10.502 1.00 99.49  ? 868  GLY   E C   1 
ATOM   15429 O  O   . GLY   E 2 564 ? 44.940  -12.077 -10.807 1.00 100.40 ? 868  GLY   E O   1 
ATOM   15430 N  N   . ALA   E 2 565 ? 43.227  -13.490 -11.254 1.00 93.34  ? 869  ALA   E N   1 
ATOM   15431 C  CA  . ALA   E 2 565 ? 42.898  -12.892 -12.538 1.00 87.57  ? 869  ALA   E CA  1 
ATOM   15432 C  C   . ALA   E 2 565 ? 41.926  -11.751 -12.313 1.00 85.09  ? 869  ALA   E C   1 
ATOM   15433 O  O   . ALA   E 2 565 ? 40.999  -11.875 -11.512 1.00 88.29  ? 869  ALA   E O   1 
ATOM   15434 C  CB  . ALA   E 2 565 ? 42.284  -13.929 -13.482 1.00 85.50  ? 869  ALA   E CB  1 
ATOM   15435 N  N   . VAL   E 2 566 ? 42.133  -10.638 -13.006 1.00 83.50  ? 870  VAL   E N   1 
ATOM   15436 C  CA  . VAL   E 2 566 ? 41.181  -9.533  -12.946 1.00 85.43  ? 870  VAL   E CA  1 
ATOM   15437 C  C   . VAL   E 2 566 ? 40.240  -9.709  -14.135 1.00 86.78  ? 870  VAL   E C   1 
ATOM   15438 O  O   . VAL   E 2 566 ? 40.501  -9.230  -15.234 1.00 87.22  ? 870  VAL   E O   1 
ATOM   15439 C  CB  . VAL   E 2 566 ? 41.875  -8.180  -12.945 1.00 86.34  ? 870  VAL   E CB  1 
ATOM   15440 C  CG1 . VAL   E 2 566 ? 40.847  -7.089  -12.760 1.00 88.59  ? 870  VAL   E CG1 1 
ATOM   15441 C  CG2 . VAL   E 2 566 ? 42.884  -8.136  -11.849 1.00 85.04  ? 870  VAL   E CG2 1 
ATOM   15442 N  N   . TYR   E 2 567 ? 39.116  -10.399 -13.909 1.00 84.58  ? 871  TYR   E N   1 
ATOM   15443 C  CA  . TYR   E 2 567 ? 38.232  -10.756 -15.017 1.00 79.27  ? 871  TYR   E CA  1 
ATOM   15444 C  C   . TYR   E 2 567 ? 37.431  -9.569  -15.519 1.00 80.12  ? 871  TYR   E C   1 
ATOM   15445 O  O   . TYR   E 2 567 ? 37.104  -9.502  -16.701 1.00 88.34  ? 871  TYR   E O   1 
ATOM   15446 C  CB  . TYR   E 2 567 ? 37.275  -11.867 -14.617 1.00 80.91  ? 871  TYR   E CB  1 
ATOM   15447 C  CG  . TYR   E 2 567 ? 37.953  -13.184 -14.420 1.00 80.87  ? 871  TYR   E CG  1 
ATOM   15448 C  CD1 . TYR   E 2 567 ? 38.522  -13.849 -15.481 1.00 83.06  ? 871  TYR   E CD1 1 
ATOM   15449 C  CD2 . TYR   E 2 567 ? 38.025  -13.764 -13.169 1.00 83.18  ? 871  TYR   E CD2 1 
ATOM   15450 C  CE1 . TYR   E 2 567 ? 39.143  -15.061 -15.302 1.00 82.55  ? 871  TYR   E CE1 1 
ATOM   15451 C  CE2 . TYR   E 2 567 ? 38.641  -14.956 -12.981 1.00 85.25  ? 871  TYR   E CE2 1 
ATOM   15452 C  CZ  . TYR   E 2 567 ? 39.201  -15.602 -14.048 1.00 82.84  ? 871  TYR   E CZ  1 
ATOM   15453 O  OH  . TYR   E 2 567 ? 39.824  -16.804 -13.840 1.00 85.48  ? 871  TYR   E OH  1 
ATOM   15454 N  N   . SER   E 2 568 ? 37.091  -8.631  -14.656 1.00 84.78  ? 872  SER   E N   1 
ATOM   15455 C  CA  . SER   E 2 568 ? 36.212  -7.562  -15.090 1.00 87.42  ? 872  SER   E CA  1 
ATOM   15456 C  C   . SER   E 2 568 ? 36.520  -6.318  -14.265 1.00 92.04  ? 872  SER   E C   1 
ATOM   15457 O  O   . SER   E 2 568 ? 37.170  -6.396  -13.218 1.00 92.58  ? 872  SER   E O   1 
ATOM   15458 C  CB  . SER   E 2 568 ? 34.745  -8.007  -14.961 1.00 87.75  ? 872  SER   E CB  1 
ATOM   15459 O  OG  . SER   E 2 568 ? 33.880  -7.267  -15.807 1.00 89.98  ? 872  SER   E OG  1 
ATOM   15460 N  N   . MET   E 2 569 ? 36.063  -5.158  -14.755 1.00 92.31  ? 873  MET   E N   1 
ATOM   15461 C  CA  . MET   E 2 569 ? 36.062  -3.913  -13.987 1.00 93.27  ? 873  MET   E CA  1 
ATOM   15462 C  C   . MET   E 2 569 ? 34.872  -3.059  -14.395 1.00 95.48  ? 873  MET   E C   1 
ATOM   15463 O  O   . MET   E 2 569 ? 34.510  -3.001  -15.575 1.00 98.49  ? 873  MET   E O   1 
ATOM   15464 C  CB  . MET   E 2 569 ? 37.336  -3.089  -14.191 1.00 90.21  ? 873  MET   E CB  1 
ATOM   15465 C  CG  . MET   E 2 569 ? 38.560  -3.595  -13.491 1.00 87.71  ? 873  MET   E CG  1 
ATOM   15466 S  SD  . MET   E 2 569 ? 39.984  -3.114  -14.476 1.00 83.25  ? 873  MET   E SD  1 
ATOM   15467 C  CE  . MET   E 2 569 ? 41.270  -3.914  -13.534 1.00 90.21  ? 873  MET   E CE  1 
ATOM   15468 N  N   . VAL   E 2 570 ? 34.264  -2.397  -13.421 1.00 95.55  ? 874  VAL   E N   1 
ATOM   15469 C  CA  . VAL   E 2 570 ? 33.252  -1.387  -13.689 1.00 100.46 ? 874  VAL   E CA  1 
ATOM   15470 C  C   . VAL   E 2 570 ? 33.550  -0.195  -12.790 1.00 105.78 ? 874  VAL   E C   1 
ATOM   15471 O  O   . VAL   E 2 570 ? 33.803  -0.363  -11.591 1.00 103.98 ? 874  VAL   E O   1 
ATOM   15472 C  CB  . VAL   E 2 570 ? 31.813  -1.913  -13.472 1.00 98.23  ? 874  VAL   E CB  1 
ATOM   15473 C  CG1 . VAL   E 2 570 ? 31.513  -3.034  -14.421 1.00 96.88  ? 874  VAL   E CG1 1 
ATOM   15474 C  CG2 . VAL   E 2 570 ? 31.629  -2.421  -12.087 1.00 100.40 ? 874  VAL   E CG2 1 
ATOM   15475 N  N   . GLU   E 2 571 ? 33.586  0.996   -13.379 1.00 114.48 ? 875  GLU   E N   1 
ATOM   15476 C  CA  . GLU   E 2 571 ? 33.661  2.225   -12.595 1.00 112.80 ? 875  GLU   E CA  1 
ATOM   15477 C  C   . GLU   E 2 571 ? 32.374  2.343   -11.791 1.00 114.63 ? 875  GLU   E C   1 
ATOM   15478 O  O   . GLU   E 2 571 ? 31.293  2.568   -12.352 1.00 114.27 ? 875  GLU   E O   1 
ATOM   15479 C  CB  . GLU   E 2 571 ? 33.872  3.428   -13.507 1.00 114.92 ? 875  GLU   E CB  1 
ATOM   15480 C  CG  . GLU   E 2 571 ? 34.204  4.726   -12.782 1.00 117.58 ? 875  GLU   E CG  1 
ATOM   15481 C  CD  . GLU   E 2 571 ? 33.071  5.733   -12.842 1.00 122.33 ? 875  GLU   E CD  1 
ATOM   15482 O  OE1 . GLU   E 2 571 ? 31.988  5.373   -13.357 1.00 125.15 ? 875  GLU   E OE1 1 
ATOM   15483 O  OE2 . GLU   E 2 571 ? 33.262  6.883   -12.380 1.00 124.30 ? 875  GLU   E OE2 1 
ATOM   15484 N  N   . PHE   E 2 572 ? 32.483  2.164   -10.478 1.00 111.71 ? 876  PHE   E N   1 
ATOM   15485 C  CA  . PHE   E 2 572 ? 31.330  2.055   -9.587  1.00 109.43 ? 876  PHE   E CA  1 
ATOM   15486 C  C   . PHE   E 2 572 ? 31.308  3.275   -8.672  1.00 108.69 ? 876  PHE   E C   1 
ATOM   15487 O  O   . PHE   E 2 572 ? 31.883  3.256   -7.587  1.00 109.38 ? 876  PHE   E O   1 
ATOM   15488 C  CB  . PHE   E 2 572 ? 31.396  0.770   -8.790  1.00 106.62 ? 876  PHE   E CB  1 
ATOM   15489 C  CG  . PHE   E 2 572 ? 30.196  0.529   -7.952  1.00 105.21 ? 876  PHE   E CG  1 
ATOM   15490 C  CD1 . PHE   E 2 572 ? 29.039  0.051   -8.524  1.00 104.37 ? 876  PHE   E CD1 1 
ATOM   15491 C  CD2 . PHE   E 2 572 ? 30.222  0.784   -6.593  1.00 104.01 ? 876  PHE   E CD2 1 
ATOM   15492 C  CE1 . PHE   E 2 572 ? 27.933  -0.187  -7.759  1.00 105.13 ? 876  PHE   E CE1 1 
ATOM   15493 C  CE2 . PHE   E 2 572 ? 29.114  0.559   -5.822  1.00 105.11 ? 876  PHE   E CE2 1 
ATOM   15494 C  CZ  . PHE   E 2 572 ? 27.960  0.076   -6.405  1.00 103.56 ? 876  PHE   E CZ  1 
ATOM   15495 N  N   . ASN   E 2 573 ? 30.636  4.333   -9.126  1.00 117.63 ? 877  ASN   E N   1 
ATOM   15496 C  CA  . ASN   E 2 573 ? 30.475  5.570   -8.358  1.00 120.63 ? 877  ASN   E CA  1 
ATOM   15497 C  C   . ASN   E 2 573 ? 31.828  6.208   -8.041  1.00 117.39 ? 877  ASN   E C   1 
ATOM   15498 O  O   . ASN   E 2 573 ? 32.236  6.331   -6.881  1.00 115.51 ? 877  ASN   E O   1 
ATOM   15499 C  CB  . ASN   E 2 573 ? 29.674  5.329   -7.071  1.00 120.22 ? 877  ASN   E CB  1 
ATOM   15500 C  CG  . ASN   E 2 573 ? 28.300  4.739   -7.329  1.00 120.12 ? 877  ASN   E CG  1 
ATOM   15501 O  OD1 . ASN   E 2 573 ? 27.767  4.834   -8.440  1.00 121.60 ? 877  ASN   E OD1 1 
ATOM   15502 N  ND2 . ASN   E 2 573 ? 27.711  4.135   -6.294  1.00 118.12 ? 877  ASN   E ND2 1 
ATOM   15503 N  N   . GLY   E 2 574 ? 32.535  6.620   -9.097  1.00 114.02 ? 878  GLY   E N   1 
ATOM   15504 C  CA  . GLY   E 2 574 ? 33.832  7.252   -8.961  1.00 111.97 ? 878  GLY   E CA  1 
ATOM   15505 C  C   . GLY   E 2 574 ? 34.942  6.364   -8.446  1.00 109.41 ? 878  GLY   E C   1 
ATOM   15506 O  O   . GLY   E 2 574 ? 36.108  6.778   -8.484  1.00 108.36 ? 878  GLY   E O   1 
ATOM   15507 N  N   . LYS   E 2 575 ? 34.625  5.174   -7.956  1.00 108.73 ? 879  LYS   E N   1 
ATOM   15508 C  CA  . LYS   E 2 575 ? 35.594  4.167   -7.557  1.00 107.41 ? 879  LYS   E CA  1 
ATOM   15509 C  C   . LYS   E 2 575 ? 35.569  3.031   -8.565  1.00 106.71 ? 879  LYS   E C   1 
ATOM   15510 O  O   . LYS   E 2 575 ? 34.650  2.916   -9.379  1.00 109.00 ? 879  LYS   E O   1 
ATOM   15511 C  CB  . LYS   E 2 575 ? 35.285  3.638   -6.156  1.00 104.28 ? 879  LYS   E CB  1 
ATOM   15512 C  CG  . LYS   E 2 575 ? 34.453  4.587   -5.320  1.00 106.26 ? 879  LYS   E CG  1 
ATOM   15513 C  CD  . LYS   E 2 575 ? 34.272  4.075   -3.908  1.00 103.95 ? 879  LYS   E CD  1 
ATOM   15514 C  CE  . LYS   E 2 575 ? 33.178  4.818   -3.191  1.00 101.44 ? 879  LYS   E CE  1 
ATOM   15515 N  NZ  . LYS   E 2 575 ? 33.039  4.293   -1.814  1.00 100.28 ? 879  LYS   E NZ  1 
ATOM   15516 N  N   . LEU   E 2 576 ? 36.594  2.187   -8.506  1.00 103.94 ? 880  LEU   E N   1 
ATOM   15517 C  CA  . LEU   E 2 576 ? 36.737  1.052   -9.415  1.00 103.51 ? 880  LEU   E CA  1 
ATOM   15518 C  C   . LEU   E 2 576 ? 36.272  -0.221  -8.709  1.00 103.39 ? 880  LEU   E C   1 
ATOM   15519 O  O   . LEU   E 2 576 ? 36.671  -0.485  -7.566  1.00 103.47 ? 880  LEU   E O   1 
ATOM   15520 C  CB  . LEU   E 2 576 ? 38.194  0.922   -9.890  1.00 101.51 ? 880  LEU   E CB  1 
ATOM   15521 C  CG  . LEU   E 2 576 ? 38.667  -0.162  -10.864 1.00 98.52  ? 880  LEU   E CG  1 
ATOM   15522 C  CD1 . LEU   E 2 576 ? 39.322  0.464   -12.074 1.00 99.08  ? 880  LEU   E CD1 1 
ATOM   15523 C  CD2 . LEU   E 2 576 ? 39.654  -1.092  -10.179 1.00 94.17  ? 880  LEU   E CD2 1 
ATOM   15524 N  N   . LEU   E 2 577 ? 35.402  -0.989  -9.374  1.00 101.29 ? 881  LEU   E N   1 
ATOM   15525 C  CA  . LEU   E 2 577 ? 34.919  -2.269  -8.864  1.00 96.46  ? 881  LEU   E CA  1 
ATOM   15526 C  C   . LEU   E 2 577 ? 35.477  -3.365  -9.760  1.00 97.38  ? 881  LEU   E C   1 
ATOM   15527 O  O   . LEU   E 2 577 ? 35.042  -3.515  -10.905 1.00 99.70  ? 881  LEU   E O   1 
ATOM   15528 C  CB  . LEU   E 2 577 ? 33.395  -2.307  -8.837  1.00 95.28  ? 881  LEU   E CB  1 
ATOM   15529 C  CG  . LEU   E 2 577 ? 32.771  -3.614  -8.376  1.00 91.36  ? 881  LEU   E CG  1 
ATOM   15530 C  CD1 . LEU   E 2 577 ? 33.327  -3.931  -7.024  1.00 96.70  ? 881  LEU   E CD1 1 
ATOM   15531 C  CD2 . LEU   E 2 577 ? 31.273  -3.427  -8.305  1.00 91.33  ? 881  LEU   E CD2 1 
ATOM   15532 N  N   . ALA   E 2 578 ? 36.441  -4.119  -9.250  1.00 95.05  ? 882  ALA   E N   1 
ATOM   15533 C  CA  . ALA   E 2 578 ? 37.103  -5.165  -10.008 1.00 91.55  ? 882  ALA   E CA  1 
ATOM   15534 C  C   . ALA   E 2 578 ? 36.745  -6.519  -9.419  1.00 92.28  ? 882  ALA   E C   1 
ATOM   15535 O  O   . ALA   E 2 578 ? 36.414  -6.629  -8.236  1.00 94.53  ? 882  ALA   E O   1 
ATOM   15536 C  CB  . ALA   E 2 578 ? 38.625  -4.973  -9.997  1.00 90.96  ? 882  ALA   E CB  1 
ATOM   15537 N  N   . SER   E 2 579 ? 36.795  -7.553  -10.251 1.00 90.59  ? 883  SER   E N   1 
ATOM   15538 C  CA  . SER   E 2 579 ? 36.722  -8.918  -9.758  1.00 91.17  ? 883  SER   E CA  1 
ATOM   15539 C  C   . SER   E 2 579 ? 38.086  -9.581  -9.910  1.00 90.86  ? 883  SER   E C   1 
ATOM   15540 O  O   . SER   E 2 579 ? 38.798  -9.349  -10.896 1.00 84.80  ? 883  SER   E O   1 
ATOM   15541 C  CB  . SER   E 2 579 ? 35.629  -9.728  -10.466 1.00 87.44  ? 883  SER   E CB  1 
ATOM   15542 O  OG  . SER   E 2 579 ? 35.660  -9.592  -11.869 1.00 85.83  ? 883  SER   E OG  1 
ATOM   15543 N  N   . ILE   E 2 580 ? 38.465  -10.354 -8.886  1.00 94.03  ? 884  ILE   E N   1 
ATOM   15544 C  CA  . ILE   E 2 580 ? 39.681  -11.174 -8.875  1.00 90.54  ? 884  ILE   E CA  1 
ATOM   15545 C  C   . ILE   E 2 580 ? 39.233  -12.587 -8.513  1.00 89.37  ? 884  ILE   E C   1 
ATOM   15546 O  O   . ILE   E 2 580 ? 38.963  -12.874 -7.343  1.00 94.28  ? 884  ILE   E O   1 
ATOM   15547 C  CB  . ILE   E 2 580 ? 40.746  -10.658 -7.893  1.00 82.66  ? 884  ILE   E CB  1 
ATOM   15548 C  CG1 . ILE   E 2 580 ? 41.050  -9.183  -8.139  1.00 83.63  ? 884  ILE   E CG1 1 
ATOM   15549 C  CG2 . ILE   E 2 580 ? 42.013  -11.466 -8.008  1.00 82.68  ? 884  ILE   E CG2 1 
ATOM   15550 C  CD1 . ILE   E 2 580 ? 40.216  -8.255  -7.309  1.00 86.54  ? 884  ILE   E CD1 1 
ATOM   15551 N  N   . ASN   E 2 581 ? 39.107  -13.457 -9.514  1.00 85.59  ? 885  ASN   E N   1 
ATOM   15552 C  CA  . ASN   E 2 581 ? 38.729  -14.849 -9.291  1.00 86.33  ? 885  ASN   E CA  1 
ATOM   15553 C  C   . ASN   E 2 581 ? 37.410  -14.684 -8.537  1.00 88.05  ? 885  ASN   E C   1 
ATOM   15554 O  O   . ASN   E 2 581 ? 36.520  -13.961 -8.988  1.00 88.94  ? 885  ASN   E O   1 
ATOM   15555 C  CB  . ASN   E 2 581 ? 39.802  -15.557 -8.464  1.00 89.90  ? 885  ASN   E CB  1 
ATOM   15556 C  CG  . ASN   E 2 581 ? 41.132  -15.642 -9.187  1.00 92.37  ? 885  ASN   E CG  1 
ATOM   15557 O  OD1 . ASN   E 2 581 ? 41.236  -15.294 -10.364 1.00 92.62  ? 885  ASN   E OD1 1 
ATOM   15558 N  ND2 . ASN   E 2 581 ? 42.160  -16.102 -8.485  1.00 93.79  ? 885  ASN   E ND2 1 
ATOM   15559 N  N   . SER   E 2 582 ? 37.254  -15.344 -7.399  1.00 90.83  ? 886  SER   E N   1 
ATOM   15560 C  CA  . SER   E 2 582 ? 36.043  -15.180 -6.611  1.00 90.98  ? 886  SER   E CA  1 
ATOM   15561 C  C   . SER   E 2 582 ? 35.692  -13.888 -5.911  1.00 95.16  ? 886  SER   E C   1 
ATOM   15562 O  O   . SER   E 2 582 ? 34.574  -13.756 -5.403  1.00 99.27  ? 886  SER   E O   1 
ATOM   15563 C  CB  . SER   E 2 582 ? 36.061  -16.312 -5.592  1.00 94.22  ? 886  SER   E CB  1 
ATOM   15564 O  OG  . SER   E 2 582 ? 36.294  -17.515 -6.279  1.00 102.77 ? 886  SER   E OG  1 
ATOM   15565 N  N   . THR   E 2 583 ? 36.608  -12.931 -5.889  1.00 94.55  ? 887  THR   E N   1 
ATOM   15566 C  CA  . THR   E 2 583 ? 36.535  -11.773 -5.014  1.00 96.34  ? 887  THR   E CA  1 
ATOM   15567 C  C   . THR   E 2 583 ? 36.076  -10.556 -5.805  1.00 97.98  ? 887  THR   E C   1 
ATOM   15568 O  O   . THR   E 2 583 ? 36.781  -10.102 -6.713  1.00 95.31  ? 887  THR   E O   1 
ATOM   15569 C  CB  . THR   E 2 583 ? 37.896  -11.489 -4.377  1.00 94.36  ? 887  THR   E CB  1 
ATOM   15570 O  OG1 . THR   E 2 583 ? 38.436  -12.690 -3.803  1.00 91.61  ? 887  THR   E OG1 1 
ATOM   15571 C  CG2 . THR   E 2 583 ? 37.760  -10.417 -3.318  1.00 98.77  ? 887  THR   E CG2 1 
ATOM   15572 N  N   . VAL   E 2 584 ? 34.922  -10.011 -5.436  1.00 100.67 ? 888  VAL   E N   1 
ATOM   15573 C  CA  . VAL   E 2 584 ? 34.499  -8.704  -5.933  1.00 99.67  ? 888  VAL   E CA  1 
ATOM   15574 C  C   . VAL   E 2 584 ? 34.979  -7.632  -4.953  1.00 98.60  ? 888  VAL   E C   1 
ATOM   15575 O  O   . VAL   E 2 584 ? 34.620  -7.646  -3.772  1.00 102.63 ? 888  VAL   E O   1 
ATOM   15576 C  CB  . VAL   E 2 584 ? 32.979  -8.649  -6.127  1.00 97.12  ? 888  VAL   E CB  1 
ATOM   15577 C  CG1 . VAL   E 2 584 ? 32.518  -7.211  -6.232  1.00 92.49  ? 888  VAL   E CG1 1 
ATOM   15578 C  CG2 . VAL   E 2 584 ? 32.590  -9.462  -7.366  1.00 91.71  ? 888  VAL   E CG2 1 
ATOM   15579 N  N   . ARG   E 2 585 ? 35.798  -6.705  -5.452  1.00 97.32  ? 889  ARG   E N   1 
ATOM   15580 C  CA  . ARG   E 2 585 ? 36.551  -5.761  -4.631  1.00 100.29 ? 889  ARG   E CA  1 
ATOM   15581 C  C   . ARG   E 2 585 ? 36.315  -4.339  -5.120  1.00 101.95 ? 889  ARG   E C   1 
ATOM   15582 O  O   . ARG   E 2 585 ? 36.413  -4.059  -6.321  1.00 101.95 ? 889  ARG   E O   1 
ATOM   15583 C  CB  . ARG   E 2 585 ? 38.051  -6.091  -4.661  1.00 94.95  ? 889  ARG   E CB  1 
ATOM   15584 C  CG  . ARG   E 2 585 ? 38.995  -4.974  -4.296  1.00 89.90  ? 889  ARG   E CG  1 
ATOM   15585 C  CD  . ARG   E 2 585 ? 40.342  -5.584  -4.148  1.00 89.13  ? 889  ARG   E CD  1 
ATOM   15586 N  NE  . ARG   E 2 585 ? 40.282  -6.670  -3.180  1.00 94.71  ? 889  ARG   E NE  1 
ATOM   15587 C  CZ  . ARG   E 2 585 ? 41.213  -7.602  -3.018  1.00 95.53  ? 889  ARG   E CZ  1 
ATOM   15588 N  NH1 . ARG   E 2 585 ? 42.276  -7.660  -3.799  1.00 90.98  ? 889  ARG   E NH1 1 
ATOM   15589 N  NH2 . ARG   E 2 585 ? 41.071  -8.499  -2.042  1.00 99.65  ? 889  ARG   E NH2 1 
ATOM   15590 N  N   . LEU   E 2 586 ? 36.012  -3.447  -4.190  1.00 100.72 ? 890  LEU   E N   1 
ATOM   15591 C  CA  . LEU   E 2 586 ? 35.830  -2.041  -4.496  1.00 97.30  ? 890  LEU   E CA  1 
ATOM   15592 C  C   . LEU   E 2 586 ? 37.138  -1.343  -4.146  1.00 99.66  ? 890  LEU   E C   1 
ATOM   15593 O  O   . LEU   E 2 586 ? 37.534  -1.288  -2.977  1.00 101.85 ? 890  LEU   E O   1 
ATOM   15594 C  CB  . LEU   E 2 586 ? 34.636  -1.475  -3.731  1.00 98.27  ? 890  LEU   E CB  1 
ATOM   15595 C  CG  . LEU   E 2 586 ? 34.148  -0.061  -4.036  1.00 101.34 ? 890  LEU   E CG  1 
ATOM   15596 C  CD1 . LEU   E 2 586 ? 34.285  0.276   -5.532  1.00 101.82 ? 890  LEU   E CD1 1 
ATOM   15597 C  CD2 . LEU   E 2 586 ? 32.707  0.073   -3.582  1.00 101.53 ? 890  LEU   E CD2 1 
ATOM   15598 N  N   . TYR   E 2 587 ? 37.831  -0.860  -5.162  1.00 98.71  ? 891  TYR   E N   1 
ATOM   15599 C  CA  . TYR   E 2 587 ? 39.035  -0.084  -4.957  1.00 97.61  ? 891  TYR   E CA  1 
ATOM   15600 C  C   . TYR   E 2 587 ? 38.698  1.404   -4.895  1.00 97.14  ? 891  TYR   E C   1 
ATOM   15601 O  O   . TYR   E 2 587 ? 37.633  1.838   -5.335  1.00 95.01  ? 891  TYR   E O   1 
ATOM   15602 C  CB  . TYR   E 2 587 ? 40.026  -0.341  -6.081  1.00 94.97  ? 891  TYR   E CB  1 
ATOM   15603 C  CG  . TYR   E 2 587 ? 40.885  -1.559  -5.913  1.00 94.90  ? 891  TYR   E CG  1 
ATOM   15604 C  CD1 . TYR   E 2 587 ? 41.803  -1.655  -4.872  1.00 101.71 ? 891  TYR   E CD1 1 
ATOM   15605 C  CD2 . TYR   E 2 587 ? 40.805  -2.600  -6.821  1.00 96.45  ? 891  TYR   E CD2 1 
ATOM   15606 C  CE1 . TYR   E 2 587 ? 42.609  -2.767  -4.742  1.00 104.67 ? 891  TYR   E CE1 1 
ATOM   15607 C  CE2 . TYR   E 2 587 ? 41.596  -3.706  -6.703  1.00 96.93  ? 891  TYR   E CE2 1 
ATOM   15608 C  CZ  . TYR   E 2 587 ? 42.502  -3.790  -5.676  1.00 101.53 ? 891  TYR   E CZ  1 
ATOM   15609 O  OH  . TYR   E 2 587 ? 43.275  -4.925  -5.594  1.00 101.02 ? 891  TYR   E OH  1 
ATOM   15610 N  N   . GLU   E 2 588 ? 39.643  2.186   -4.372  1.00 98.64  ? 892  GLU   E N   1 
ATOM   15611 C  CA  . GLU   E 2 588 ? 39.488  3.626   -4.240  1.00 97.21  ? 892  GLU   E CA  1 
ATOM   15612 C  C   . GLU   E 2 588 ? 40.758  4.335   -4.674  1.00 102.21 ? 892  GLU   E C   1 
ATOM   15613 O  O   . GLU   E 2 588 ? 41.869  3.825   -4.478  1.00 102.40 ? 892  GLU   E O   1 
ATOM   15614 C  CB  . GLU   E 2 588 ? 39.168  4.033   -2.812  1.00 101.02 ? 892  GLU   E CB  1 
ATOM   15615 C  CG  . GLU   E 2 588 ? 37.727  4.406   -2.591  1.00 104.66 ? 892  GLU   E CG  1 
ATOM   15616 C  CD  . GLU   E 2 588 ? 37.389  4.497   -1.111  1.00 109.48 ? 892  GLU   E CD  1 
ATOM   15617 O  OE1 . GLU   E 2 588 ? 38.239  4.113   -0.260  1.00 106.74 ? 892  GLU   E OE1 1 
ATOM   15618 O  OE2 . GLU   E 2 588 ? 36.267  4.955   -0.801  1.00 111.12 ? 892  GLU   E OE2 1 
ATOM   15619 N  N   . TRP   E 2 589 ? 40.580  5.529   -5.252  1.00 109.64 ? 893  TRP   E N   1 
ATOM   15620 C  CA  . TRP   E 2 589 ? 41.665  6.336   -5.806  1.00 111.26 ? 893  TRP   E CA  1 
ATOM   15621 C  C   . TRP   E 2 589 ? 42.112  7.341   -4.747  1.00 114.63 ? 893  TRP   E C   1 
ATOM   15622 O  O   . TRP   E 2 589 ? 41.382  8.283   -4.440  1.00 116.28 ? 893  TRP   E O   1 
ATOM   15623 C  CB  . TRP   E 2 589 ? 41.207  7.046   -7.081  1.00 108.29 ? 893  TRP   E CB  1 
ATOM   15624 C  CG  . TRP   E 2 589 ? 42.314  7.558   -7.945  1.00 108.59 ? 893  TRP   E CG  1 
ATOM   15625 C  CD1 . TRP   E 2 589 ? 42.424  8.810   -8.475  1.00 113.80 ? 893  TRP   E CD1 1 
ATOM   15626 C  CD2 . TRP   E 2 589 ? 43.479  6.839   -8.370  1.00 111.01 ? 893  TRP   E CD2 1 
ATOM   15627 N  NE1 . TRP   E 2 589 ? 43.580  8.914   -9.215  1.00 114.83 ? 893  TRP   E NE1 1 
ATOM   15628 C  CE2 . TRP   E 2 589 ? 44.246  7.718   -9.166  1.00 114.05 ? 893  TRP   E CE2 1 
ATOM   15629 C  CE3 . TRP   E 2 589 ? 43.945  5.536   -8.165  1.00 111.28 ? 893  TRP   E CE3 1 
ATOM   15630 C  CZ2 . TRP   E 2 589 ? 45.453  7.335   -9.756  1.00 113.96 ? 893  TRP   E CZ2 1 
ATOM   15631 C  CZ3 . TRP   E 2 589 ? 45.147  5.159   -8.745  1.00 112.06 ? 893  TRP   E CZ3 1 
ATOM   15632 C  CH2 . TRP   E 2 589 ? 45.886  6.055   -9.532  1.00 111.41 ? 893  TRP   E CH2 1 
ATOM   15633 N  N   . THR   E 2 590 ? 43.315  7.141   -4.200  1.00 119.21 ? 894  THR   E N   1 
ATOM   15634 C  CA  . THR   E 2 590 ? 43.837  8.015   -3.162  1.00 122.34 ? 894  THR   E CA  1 
ATOM   15635 C  C   . THR   E 2 590 ? 44.282  9.337   -3.770  1.00 124.69 ? 894  THR   E C   1 
ATOM   15636 O  O   . THR   E 2 590 ? 44.639  9.435   -4.951  1.00 118.77 ? 894  THR   E O   1 
ATOM   15637 C  CB  . THR   E 2 590 ? 45.019  7.389   -2.393  1.00 124.41 ? 894  THR   E CB  1 
ATOM   15638 O  OG1 . THR   E 2 590 ? 46.218  7.426   -3.185  1.00 127.40 ? 894  THR   E OG1 1 
ATOM   15639 C  CG2 . THR   E 2 590 ? 44.725  5.944   -1.966  1.00 119.98 ? 894  THR   E CG2 1 
ATOM   15640 N  N   . THR   E 2 591 ? 44.219  10.372  -2.928  1.00 132.67 ? 895  THR   E N   1 
ATOM   15641 C  CA  . THR   E 2 591 ? 44.849  11.645  -3.237  1.00 132.14 ? 895  THR   E CA  1 
ATOM   15642 C  C   . THR   E 2 591 ? 46.311  11.444  -3.639  1.00 131.60 ? 895  THR   E C   1 
ATOM   15643 O  O   . THR   E 2 591 ? 46.862  12.256  -4.393  1.00 129.79 ? 895  THR   E O   1 
ATOM   15644 C  CB  . THR   E 2 591 ? 44.703  12.568  -2.028  1.00 127.91 ? 895  THR   E CB  1 
ATOM   15645 O  OG1 . THR   E 2 591 ? 45.237  11.905  -0.876  1.00 132.37 ? 895  THR   E OG1 1 
ATOM   15646 C  CG2 . THR   E 2 591 ? 43.233  12.841  -1.751  1.00 119.07 ? 895  THR   E CG2 1 
ATOM   15647 N  N   . GLU   E 2 592 ? 46.935  10.341  -3.186  1.00 136.38 ? 896  GLU   E N   1 
ATOM   15648 C  CA  . GLU   E 2 592 ? 48.301  9.949   -3.524  1.00 136.58 ? 896  GLU   E CA  1 
ATOM   15649 C  C   . GLU   E 2 592 ? 48.397  9.179   -4.831  1.00 137.22 ? 896  GLU   E C   1 
ATOM   15650 O  O   . GLU   E 2 592 ? 49.432  8.529   -5.081  1.00 135.35 ? 896  GLU   E O   1 
ATOM   15651 C  CB  . GLU   E 2 592 ? 48.894  9.103   -2.390  1.00 135.07 ? 896  GLU   E CB  1 
ATOM   15652 C  CG  . GLU   E 2 592 ? 48.650  9.679   -1.019  1.00 136.19 ? 896  GLU   E CG  1 
ATOM   15653 C  CD  . GLU   E 2 592 ? 49.414  10.981  -0.783  1.00 147.54 ? 896  GLU   E CD  1 
ATOM   15654 O  OE1 . GLU   E 2 592 ? 50.333  10.982  0.075   1.00 157.25 ? 896  GLU   E OE1 1 
ATOM   15655 O  OE2 . GLU   E 2 592 ? 49.094  12.005  -1.445  1.00 148.69 ? 896  GLU   E OE2 1 
ATOM   15656 N  N   . LYS   E 2 593 ? 47.332  9.230   -5.640  1.00 126.72 ? 897  LYS   E N   1 
ATOM   15657 C  CA  . LYS   E 2 593 ? 47.270  8.573   -6.936  1.00 119.76 ? 897  LYS   E CA  1 
ATOM   15658 C  C   . LYS   E 2 593 ? 47.689  7.103   -6.818  1.00 123.07 ? 897  LYS   E C   1 
ATOM   15659 O  O   . LYS   E 2 593 ? 48.567  6.605   -7.534  1.00 120.67 ? 897  LYS   E O   1 
ATOM   15660 C  CB  . LYS   E 2 593 ? 48.127  9.339   -7.947  1.00 109.86 ? 897  LYS   E CB  1 
ATOM   15661 N  N   . GLU   E 2 594 ? 47.048  6.408   -5.871  1.00 121.49 ? 898  GLU   E N   1 
ATOM   15662 C  CA  . GLU   E 2 594 ? 47.280  4.991   -5.628  1.00 118.66 ? 898  GLU   E CA  1 
ATOM   15663 C  C   . GLU   E 2 594 ? 45.937  4.273   -5.474  1.00 116.54 ? 898  GLU   E C   1 
ATOM   15664 O  O   . GLU   E 2 594 ? 44.874  4.896   -5.400  1.00 115.57 ? 898  GLU   E O   1 
ATOM   15665 C  CB  . GLU   E 2 594 ? 48.174  4.771   -4.391  1.00 116.29 ? 898  GLU   E CB  1 
ATOM   15666 N  N   . LEU   E 2 595 ? 45.981  2.942   -5.411  1.00 114.15 ? 899  LEU   E N   1 
ATOM   15667 C  CA  . LEU   E 2 595 ? 44.781  2.118   -5.290  1.00 110.57 ? 899  LEU   E CA  1 
ATOM   15668 C  C   . LEU   E 2 595 ? 44.739  1.484   -3.904  1.00 113.38 ? 899  LEU   E C   1 
ATOM   15669 O  O   . LEU   E 2 595 ? 45.595  0.652   -3.572  1.00 115.07 ? 899  LEU   E O   1 
ATOM   15670 C  CB  . LEU   E 2 595 ? 44.722  1.038   -6.376  1.00 107.39 ? 899  LEU   E CB  1 
ATOM   15671 C  CG  . LEU   E 2 595 ? 44.185  1.445   -7.756  1.00 100.50 ? 899  LEU   E CG  1 
ATOM   15672 C  CD1 . LEU   E 2 595 ? 44.562  0.402   -8.780  1.00 95.38  ? 899  LEU   E CD1 1 
ATOM   15673 C  CD2 . LEU   E 2 595 ? 42.680  1.648   -7.746  1.00 96.52  ? 899  LEU   E CD2 1 
ATOM   15674 N  N   . ARG   E 2 596 ? 43.734  1.877   -3.110  1.00 111.33 ? 900  ARG   E N   1 
ATOM   15675 C  CA  . ARG   E 2 596 ? 43.459  1.318   -1.788  1.00 112.76 ? 900  ARG   E CA  1 
ATOM   15676 C  C   . ARG   E 2 596 ? 42.129  0.569   -1.829  1.00 108.61 ? 900  ARG   E C   1 
ATOM   15677 O  O   . ARG   E 2 596 ? 41.146  1.070   -2.385  1.00 104.76 ? 900  ARG   E O   1 
ATOM   15678 C  CB  . ARG   E 2 596 ? 43.423  2.418   -0.717  1.00 109.37 ? 900  ARG   E CB  1 
ATOM   15679 N  N   . THR   E 2 597 ? 42.093  -0.620  -1.232  1.00 108.81 ? 901  THR   E N   1 
ATOM   15680 C  CA  . THR   E 2 597 ? 40.885  -1.427  -1.256  1.00 106.23 ? 901  THR   E CA  1 
ATOM   15681 C  C   . THR   E 2 597 ? 39.915  -0.960  -0.179  1.00 108.29 ? 901  THR   E C   1 
ATOM   15682 O  O   . THR   E 2 597 ? 40.274  -0.899  1.002   1.00 107.79 ? 901  THR   E O   1 
ATOM   15683 C  CB  . THR   E 2 597 ? 41.214  -2.901  -1.058  1.00 108.00 ? 901  THR   E CB  1 
ATOM   15684 O  OG1 . THR   E 2 597 ? 39.994  -3.622  -0.882  1.00 111.49 ? 901  THR   E OG1 1 
ATOM   15685 C  CG2 . THR   E 2 597 ? 42.062  -3.126  0.174   1.00 112.66 ? 901  THR   E CG2 1 
ATOM   15686 N  N   . GLU   E 2 598 ? 38.684  -0.629  -0.587  1.00 106.48 ? 902  GLU   E N   1 
ATOM   15687 C  CA  . GLU   E 2 598 ? 37.690  -0.186  0.396   1.00 107.14 ? 902  GLU   E CA  1 
ATOM   15688 C  C   . GLU   E 2 598 ? 37.085  -1.368  1.143   1.00 109.03 ? 902  GLU   E C   1 
ATOM   15689 O  O   . GLU   E 2 598 ? 37.338  -1.558  2.335   1.00 114.38 ? 902  GLU   E O   1 
ATOM   15690 C  CB  . GLU   E 2 598 ? 36.588  0.657   -0.254  1.00 105.78 ? 902  GLU   E CB  1 
ATOM   15691 C  CG  . GLU   E 2 598 ? 35.545  1.068   0.817   1.00 109.48 ? 902  GLU   E CG  1 
ATOM   15692 C  CD  . GLU   E 2 598 ? 34.369  1.941   0.336   1.00 109.42 ? 902  GLU   E CD  1 
ATOM   15693 O  OE1 . GLU   E 2 598 ? 34.400  2.496   -0.792  1.00 106.61 ? 902  GLU   E OE1 1 
ATOM   15694 O  OE2 . GLU   E 2 598 ? 33.403  2.075   1.126   1.00 109.97 ? 902  GLU   E OE2 1 
ATOM   15695 N  N   . CYS   E 2 599 ? 36.274  -2.176  0.452   1.00 110.55 ? 903  CYS   E N   1 
ATOM   15696 C  CA  . CYS   E 2 599 ? 35.591  -3.307  1.066   1.00 111.80 ? 903  CYS   E CA  1 
ATOM   15697 C  C   . CYS   E 2 599 ? 35.661  -4.513  0.139   1.00 111.85 ? 903  CYS   E C   1 
ATOM   15698 O  O   . CYS   E 2 599 ? 35.862  -4.387  -1.075  1.00 107.05 ? 903  CYS   E O   1 
ATOM   15699 C  CB  . CYS   E 2 599 ? 34.142  -2.961  1.374   1.00 110.15 ? 903  CYS   E CB  1 
ATOM   15700 S  SG  . CYS   E 2 599 ? 33.423  -2.165  -0.031  1.00 101.46 ? 903  CYS   E SG  1 
ATOM   15701 N  N   . ASN   E 2 600 ? 35.478  -5.696  0.724   1.00 112.37 ? 904  ASN   E N   1 
ATOM   15702 C  CA  . ASN   E 2 600 ? 35.588  -6.933  -0.028  1.00 111.73 ? 904  ASN   E CA  1 
ATOM   15703 C  C   . ASN   E 2 600 ? 34.314  -7.753  0.061   1.00 111.09 ? 904  ASN   E C   1 
ATOM   15704 O  O   . ASN   E 2 600 ? 33.496  -7.592  0.976   1.00 112.70 ? 904  ASN   E O   1 
ATOM   15705 C  CB  . ASN   E 2 600 ? 36.756  -7.784  0.453   1.00 109.20 ? 904  ASN   E CB  1 
ATOM   15706 C  CG  . ASN   E 2 600 ? 37.988  -7.559  -0.362  1.00 109.53 ? 904  ASN   E CG  1 
ATOM   15707 O  OD1 . ASN   E 2 600 ? 37.926  -6.975  -1.446  1.00 110.34 ? 904  ASN   E OD1 1 
ATOM   15708 N  ND2 . ASN   E 2 600 ? 39.123  -8.015  0.145   1.00 111.69 ? 904  ASN   E ND2 1 
ATOM   15709 N  N   . HIS   E 2 601 ? 34.172  -8.643  -0.921  1.00 109.97 ? 905  HIS   E N   1 
ATOM   15710 C  CA  . HIS   E 2 601 ? 33.137  -9.668  -0.921  1.00 107.21 ? 905  HIS   E CA  1 
ATOM   15711 C  C   . HIS   E 2 601 ? 33.704  -10.921 -1.564  1.00 104.47 ? 905  HIS   E C   1 
ATOM   15712 O  O   . HIS   E 2 601 ? 34.132  -10.884 -2.722  1.00 100.65 ? 905  HIS   E O   1 
ATOM   15713 C  CB  . HIS   E 2 601 ? 31.893  -9.210  -1.664  1.00 98.36  ? 905  HIS   E CB  1 
ATOM   15714 C  CG  . HIS   E 2 601 ? 30.677  -9.969  -1.274  1.00 98.40  ? 905  HIS   E CG  1 
ATOM   15715 N  ND1 . HIS   E 2 601 ? 30.466  -11.275 -1.652  1.00 101.80 ? 905  HIS   E ND1 1 
ATOM   15716 C  CD2 . HIS   E 2 601 ? 29.627  -9.629  -0.495  1.00 102.21 ? 905  HIS   E CD2 1 
ATOM   15717 C  CE1 . HIS   E 2 601 ? 29.322  -11.699 -1.148  1.00 103.76 ? 905  HIS   E CE1 1 
ATOM   15718 N  NE2 . HIS   E 2 601 ? 28.791  -10.718 -0.442  1.00 104.51 ? 905  HIS   E NE2 1 
ATOM   15719 N  N   . TYR   E 2 602 ? 33.698  -12.023 -0.819  1.00 103.72 ? 906  TYR   E N   1 
ATOM   15720 C  CA  . TYR   E 2 602 ? 34.216  -13.297 -1.301  1.00 101.93 ? 906  TYR   E CA  1 
ATOM   15721 C  C   . TYR   E 2 602 ? 33.056  -14.228 -1.634  1.00 102.45 ? 906  TYR   E C   1 
ATOM   15722 O  O   . TYR   E 2 602 ? 32.163  -14.443 -0.806  1.00 104.44 ? 906  TYR   E O   1 
ATOM   15723 C  CB  . TYR   E 2 602 ? 35.138  -13.926 -0.262  1.00 106.01 ? 906  TYR   E CB  1 
ATOM   15724 C  CG  . TYR   E 2 602 ? 36.279  -13.022 0.095   1.00 104.08 ? 906  TYR   E CG  1 
ATOM   15725 C  CD1 . TYR   E 2 602 ? 36.087  -11.924 0.932   1.00 105.09 ? 906  TYR   E CD1 1 
ATOM   15726 C  CD2 . TYR   E 2 602 ? 37.541  -13.253 -0.418  1.00 104.96 ? 906  TYR   E CD2 1 
ATOM   15727 C  CE1 . TYR   E 2 602 ? 37.115  -11.095 1.249   1.00 105.43 ? 906  TYR   E CE1 1 
ATOM   15728 C  CE2 . TYR   E 2 602 ? 38.585  -12.425 -0.103  1.00 105.09 ? 906  TYR   E CE2 1 
ATOM   15729 C  CZ  . TYR   E 2 602 ? 38.362  -11.347 0.729   1.00 106.60 ? 906  TYR   E CZ  1 
ATOM   15730 O  OH  . TYR   E 2 602 ? 39.399  -10.510 1.040   1.00 116.64 ? 906  TYR   E OH  1 
ATOM   15731 N  N   . ASN   E 2 603 ? 33.077  -14.776 -2.841  1.00 101.58 ? 907  ASN   E N   1 
ATOM   15732 C  CA  . ASN   E 2 603 ? 31.973  -15.542 -3.392  1.00 99.92  ? 907  ASN   E CA  1 
ATOM   15733 C  C   . ASN   E 2 603 ? 32.353  -17.015 -3.495  1.00 100.54 ? 907  ASN   E C   1 
ATOM   15734 O  O   . ASN   E 2 603 ? 33.517  -17.391 -3.312  1.00 102.33 ? 907  ASN   E O   1 
ATOM   15735 C  CB  . ASN   E 2 603 ? 31.583  -14.975 -4.762  1.00 98.13  ? 907  ASN   E CB  1 
ATOM   15736 C  CG  . ASN   E 2 603 ? 31.353  -13.468 -4.722  1.00 101.78 ? 907  ASN   E CG  1 
ATOM   15737 O  OD1 . ASN   E 2 603 ? 30.446  -12.997 -4.039  1.00 102.37 ? 907  ASN   E OD1 1 
ATOM   15738 N  ND2 . ASN   E 2 603 ? 32.175  -12.707 -5.452  1.00 100.36 ? 907  ASN   E ND2 1 
ATOM   15739 N  N   . ASN   E 2 604 ? 31.338  -17.853 -3.763  1.00 97.85  ? 908  ASN   E N   1 
ATOM   15740 C  CA  . ASN   E 2 604 ? 31.514  -19.267 -4.085  1.00 96.97  ? 908  ASN   E CA  1 
ATOM   15741 C  C   . ASN   E 2 604 ? 31.445  -19.538 -5.580  1.00 95.67  ? 908  ASN   E C   1 
ATOM   15742 O  O   . ASN   E 2 604 ? 31.617  -20.682 -6.001  1.00 96.54  ? 908  ASN   E O   1 
ATOM   15743 C  CB  . ASN   E 2 604 ? 30.465  -20.127 -3.379  1.00 99.13  ? 908  ASN   E CB  1 
ATOM   15744 C  CG  . ASN   E 2 604 ? 29.067  -19.845 -3.876  1.00 102.25 ? 908  ASN   E CG  1 
ATOM   15745 O  OD1 . ASN   E 2 604 ? 28.758  -18.709 -4.229  1.00 104.95 ? 908  ASN   E OD1 1 
ATOM   15746 N  ND2 . ASN   E 2 604 ? 28.216  -20.873 -3.920  1.00 100.31 ? 908  ASN   E ND2 1 
ATOM   15747 N  N   . ILE   E 2 605 ? 31.166  -18.522 -6.381  1.00 95.30  ? 909  ILE   E N   1 
ATOM   15748 C  CA  . ILE   E 2 605 ? 31.325  -18.590 -7.821  1.00 93.64  ? 909  ILE   E CA  1 
ATOM   15749 C  C   . ILE   E 2 605 ? 32.534  -17.746 -8.206  1.00 94.73  ? 909  ILE   E C   1 
ATOM   15750 O  O   . ILE   E 2 605 ? 33.046  -16.929 -7.424  1.00 97.04  ? 909  ILE   E O   1 
ATOM   15751 C  CB  . ILE   E 2 605 ? 30.061  -18.122 -8.561  1.00 90.68  ? 909  ILE   E CB  1 
ATOM   15752 C  CG1 . ILE   E 2 605 ? 29.843  -16.626 -8.325  1.00 89.80  ? 909  ILE   E CG1 1 
ATOM   15753 C  CG2 . ILE   E 2 605 ? 28.876  -18.910 -8.066  1.00 93.99  ? 909  ILE   E CG2 1 
ATOM   15754 C  CD1 . ILE   E 2 605 ? 28.598  -16.053 -8.955  1.00 90.16  ? 909  ILE   E CD1 1 
ATOM   15755 N  N   . MET   E 2 606 ? 33.018  -17.976 -9.418  1.00 89.22  ? 910  MET   E N   1 
ATOM   15756 C  CA  . MET   E 2 606 ? 34.086  -17.163 -9.970  1.00 84.14  ? 910  MET   E CA  1 
ATOM   15757 C  C   . MET   E 2 606 ? 33.469  -15.927 -10.612 1.00 88.53  ? 910  MET   E C   1 
ATOM   15758 O  O   . MET   E 2 606 ? 32.559  -16.048 -11.435 1.00 94.62  ? 910  MET   E O   1 
ATOM   15759 C  CB  . MET   E 2 606 ? 34.855  -17.983 -10.989 1.00 82.99  ? 910  MET   E CB  1 
ATOM   15760 C  CG  . MET   E 2 606 ? 36.047  -17.335 -11.569 1.00 84.99  ? 910  MET   E CG  1 
ATOM   15761 S  SD  . MET   E 2 606 ? 36.647  -18.466 -12.856 1.00 88.14  ? 910  MET   E SD  1 
ATOM   15762 C  CE  . MET   E 2 606 ? 37.719  -19.531 -11.830 1.00 97.98  ? 910  MET   E CE  1 
ATOM   15763 N  N   . ALA   E 2 607 ? 33.923  -14.736 -10.214 1.00 87.71  ? 911  ALA   E N   1 
ATOM   15764 C  CA  . ALA   E 2 607 ? 33.340  -13.485 -10.717 1.00 83.86  ? 911  ALA   E CA  1 
ATOM   15765 C  C   . ALA   E 2 607 ? 33.856  -13.206 -12.130 1.00 85.05  ? 911  ALA   E C   1 
ATOM   15766 O  O   . ALA   E 2 607 ? 34.738  -12.368 -12.364 1.00 83.12  ? 911  ALA   E O   1 
ATOM   15767 C  CB  . ALA   E 2 607 ? 33.630  -12.336 -9.767  1.00 87.31  ? 911  ALA   E CB  1 
ATOM   15768 N  N   . LEU   E 2 608 ? 33.299  -13.952 -13.095 1.00 84.20  ? 912  LEU   E N   1 
ATOM   15769 C  CA  . LEU   E 2 608 ? 33.571  -13.752 -14.515 1.00 81.02  ? 912  LEU   E CA  1 
ATOM   15770 C  C   . LEU   E 2 608 ? 32.881  -12.504 -15.043 1.00 80.57  ? 912  LEU   E C   1 
ATOM   15771 O  O   . LEU   E 2 608 ? 33.505  -11.675 -15.716 1.00 84.02  ? 912  LEU   E O   1 
ATOM   15772 C  CB  . LEU   E 2 608 ? 33.106  -14.967 -15.338 1.00 82.76  ? 912  LEU   E CB  1 
ATOM   15773 C  CG  . LEU   E 2 608 ? 34.068  -16.141 -15.565 1.00 82.28  ? 912  LEU   E CG  1 
ATOM   15774 C  CD1 . LEU   E 2 608 ? 35.269  -15.787 -16.439 1.00 76.82  ? 912  LEU   E CD1 1 
ATOM   15775 C  CD2 . LEU   E 2 608 ? 34.508  -16.541 -14.219 1.00 89.09  ? 912  LEU   E CD2 1 
ATOM   15776 N  N   . TYR   E 2 609 ? 31.576  -12.403 -14.816 1.00 79.84  ? 913  TYR   E N   1 
ATOM   15777 C  CA  . TYR   E 2 609 ? 30.801  -11.264 -15.288 1.00 82.55  ? 913  TYR   E CA  1 
ATOM   15778 C  C   . TYR   E 2 609 ? 30.535  -10.297 -14.139 1.00 87.18  ? 913  TYR   E C   1 
ATOM   15779 O  O   . TYR   E 2 609 ? 30.284  -10.706 -12.996 1.00 84.40  ? 913  TYR   E O   1 
ATOM   15780 C  CB  . TYR   E 2 609 ? 29.499  -11.736 -15.941 1.00 77.64  ? 913  TYR   E CB  1 
ATOM   15781 C  CG  . TYR   E 2 609 ? 29.767  -12.751 -17.028 1.00 79.64  ? 913  TYR   E CG  1 
ATOM   15782 C  CD1 . TYR   E 2 609 ? 30.156  -12.363 -18.307 1.00 78.01  ? 913  TYR   E CD1 1 
ATOM   15783 C  CD2 . TYR   E 2 609 ? 29.664  -14.110 -16.767 1.00 85.72  ? 913  TYR   E CD2 1 
ATOM   15784 C  CE1 . TYR   E 2 609 ? 30.415  -13.305 -19.306 1.00 77.92  ? 913  TYR   E CE1 1 
ATOM   15785 C  CE2 . TYR   E 2 609 ? 29.921  -15.056 -17.754 1.00 83.25  ? 913  TYR   E CE2 1 
ATOM   15786 C  CZ  . TYR   E 2 609 ? 30.295  -14.647 -19.019 1.00 79.57  ? 913  TYR   E CZ  1 
ATOM   15787 O  OH  . TYR   E 2 609 ? 30.533  -15.590 -19.996 1.00 82.56  ? 913  TYR   E OH  1 
ATOM   15788 N  N   . LEU   E 2 610 ? 30.637  -9.002  -14.460 1.00 87.96  ? 914  LEU   E N   1 
ATOM   15789 C  CA  . LEU   E 2 610 ? 30.511  -7.903  -13.518 1.00 84.71  ? 914  LEU   E CA  1 
ATOM   15790 C  C   . LEU   E 2 610 ? 29.801  -6.777  -14.234 1.00 82.29  ? 914  LEU   E C   1 
ATOM   15791 O  O   . LEU   E 2 610 ? 30.316  -6.278  -15.236 1.00 87.61  ? 914  LEU   E O   1 
ATOM   15792 C  CB  . LEU   E 2 610 ? 31.890  -7.437  -13.045 1.00 88.59  ? 914  LEU   E CB  1 
ATOM   15793 C  CG  . LEU   E 2 610 ? 31.987  -6.672  -11.735 1.00 90.27  ? 914  LEU   E CG  1 
ATOM   15794 C  CD1 . LEU   E 2 610 ? 31.409  -7.523  -10.602 1.00 87.42  ? 914  LEU   E CD1 1 
ATOM   15795 C  CD2 . LEU   E 2 610 ? 33.445  -6.343  -11.474 1.00 87.69  ? 914  LEU   E CD2 1 
ATOM   15796 N  N   . LYS   E 2 611 ? 28.632  -6.386  -13.740 1.00 84.99  ? 915  LYS   E N   1 
ATOM   15797 C  CA  . LYS   E 2 611 ? 27.881  -5.256  -14.280 1.00 92.17  ? 915  LYS   E CA  1 
ATOM   15798 C  C   . LYS   E 2 611 ? 27.149  -4.550  -13.140 1.00 96.24  ? 915  LYS   E C   1 
ATOM   15799 O  O   . LYS   E 2 611 ? 26.624  -5.200  -12.231 1.00 95.19  ? 915  LYS   E O   1 
ATOM   15800 C  CB  . LYS   E 2 611 ? 26.862  -5.684  -15.362 1.00 87.41  ? 915  LYS   E CB  1 
ATOM   15801 C  CG  . LYS   E 2 611 ? 27.470  -6.275  -16.638 1.00 83.59  ? 915  LYS   E CG  1 
ATOM   15802 C  CD  . LYS   E 2 611 ? 27.386  -5.335  -17.846 1.00 87.89  ? 915  LYS   E CD  1 
ATOM   15803 C  CE  . LYS   E 2 611 ? 28.352  -5.728  -18.975 1.00 87.66  ? 915  LYS   E CE  1 
ATOM   15804 N  NZ  . LYS   E 2 611 ? 28.048  -7.019  -19.628 1.00 84.49  ? 915  LYS   E NZ  1 
ATOM   15805 N  N   . THR   E 2 612 ? 27.096  -3.213  -13.210 1.00 110.93 ? 916  THR   E N   1 
ATOM   15806 C  CA  . THR   E 2 612 ? 26.513  -2.378  -12.170 1.00 109.19 ? 916  THR   E CA  1 
ATOM   15807 C  C   . THR   E 2 612 ? 25.521  -1.386  -12.751 1.00 109.80 ? 916  THR   E C   1 
ATOM   15808 O  O   . THR   E 2 612 ? 25.760  -0.804  -13.816 1.00 110.30 ? 916  THR   E O   1 
ATOM   15809 C  CB  . THR   E 2 612 ? 27.571  -1.591  -11.402 1.00 109.60 ? 916  THR   E CB  1 
ATOM   15810 O  OG1 . THR   E 2 612 ? 28.363  -0.826  -12.321 1.00 110.98 ? 916  THR   E OG1 1 
ATOM   15811 C  CG2 . THR   E 2 612 ? 28.456  -2.535  -10.635 1.00 110.83 ? 916  THR   E CG2 1 
ATOM   15812 N  N   . LYS   E 2 613 ? 24.411  -1.204  -12.048 1.00 100.67 ? 917  LYS   E N   1 
ATOM   15813 C  CA  . LYS   E 2 613 ? 23.511  -0.074  -12.278 1.00 100.82 ? 917  LYS   E CA  1 
ATOM   15814 C  C   . LYS   E 2 613 ? 23.512  0.739   -10.986 1.00 106.48 ? 917  LYS   E C   1 
ATOM   15815 O  O   . LYS   E 2 613 ? 22.759  0.440   -10.052 1.00 105.02 ? 917  LYS   E O   1 
ATOM   15816 C  CB  . LYS   E 2 613 ? 22.101  -0.511  -12.662 1.00 90.13  ? 917  LYS   E CB  1 
ATOM   15817 N  N   . GLY   E 2 614 ? 24.367  1.774   -10.955 1.00 108.26 ? 918  GLY   E N   1 
ATOM   15818 C  CA  . GLY   E 2 614 ? 24.513  2.618   -9.791  1.00 100.62 ? 918  GLY   E CA  1 
ATOM   15819 C  C   . GLY   E 2 614 ? 24.893  1.681   -8.668  1.00 103.37 ? 918  GLY   E C   1 
ATOM   15820 O  O   . GLY   E 2 614 ? 25.979  1.106   -8.695  1.00 106.31 ? 918  GLY   E O   1 
ATOM   15821 N  N   . ASP   E 2 615 ? 24.006  1.540   -7.673  1.00 103.32 ? 919  ASP   E N   1 
ATOM   15822 C  CA  . ASP   E 2 615 ? 24.237  0.793   -6.438  1.00 103.73 ? 919  ASP   E CA  1 
ATOM   15823 C  C   . ASP   E 2 615 ? 24.288  -0.717  -6.436  1.00 100.15 ? 919  ASP   E C   1 
ATOM   15824 O  O   . ASP   E 2 615 ? 24.869  -1.304  -5.522  1.00 97.43  ? 919  ASP   E O   1 
ATOM   15825 C  CB  . ASP   E 2 615 ? 23.112  1.220   -5.480  1.00 110.65 ? 919  ASP   E CB  1 
ATOM   15826 C  CG  . ASP   E 2 615 ? 21.691  0.877   -6.020  1.00 112.53 ? 919  ASP   E CG  1 
ATOM   15827 O  OD1 . ASP   E 2 615 ? 21.524  0.751   -7.258  1.00 111.50 ? 919  ASP   E OD1 1 
ATOM   15828 O  OD2 . ASP   E 2 615 ? 20.736  0.747   -5.206  1.00 111.97 ? 919  ASP   E OD2 1 
ATOM   15829 N  N   . PHE   E 2 616 ? 23.668  -1.346  -7.431  1.00 103.55 ? 920  PHE   E N   1 
ATOM   15830 C  CA  . PHE   E 2 616 ? 23.598  -2.789  -7.554  1.00 104.60 ? 920  PHE   E CA  1 
ATOM   15831 C  C   . PHE   E 2 616 ? 24.732  -3.304  -8.429  1.00 103.39 ? 920  PHE   E C   1 
ATOM   15832 O  O   . PHE   E 2 616 ? 25.193  -2.626  -9.354  1.00 103.42 ? 920  PHE   E O   1 
ATOM   15833 C  CB  . PHE   E 2 616 ? 22.246  -3.200  -8.136  1.00 106.97 ? 920  PHE   E CB  1 
ATOM   15834 C  CG  . PHE   E 2 616 ? 21.078  -2.918  -7.216  1.00 110.86 ? 920  PHE   E CG  1 
ATOM   15835 C  CD1 . PHE   E 2 616 ? 21.232  -2.948  -5.829  1.00 109.70 ? 920  PHE   E CD1 1 
ATOM   15836 C  CD2 . PHE   E 2 616 ? 19.821  -2.611  -7.733  1.00 116.75 ? 920  PHE   E CD2 1 
ATOM   15837 C  CE1 . PHE   E 2 616 ? 20.153  -2.675  -4.977  1.00 106.23 ? 920  PHE   E CE1 1 
ATOM   15838 C  CE2 . PHE   E 2 616 ? 18.736  -2.340  -6.883  1.00 116.09 ? 920  PHE   E CE2 1 
ATOM   15839 C  CZ  . PHE   E 2 616 ? 18.908  -2.372  -5.507  1.00 112.59 ? 920  PHE   E CZ  1 
ATOM   15840 N  N   . ILE   E 2 617 ? 25.172  -4.524  -8.127  1.00 98.49  ? 921  ILE   E N   1 
ATOM   15841 C  CA  . ILE   E 2 617 ? 26.237  -5.209  -8.846  1.00 96.39  ? 921  ILE   E CA  1 
ATOM   15842 C  C   . ILE   E 2 617 ? 25.732  -6.604  -9.210  1.00 96.19  ? 921  ILE   E C   1 
ATOM   15843 O  O   . ILE   E 2 617 ? 25.227  -7.327  -8.345  1.00 97.94  ? 921  ILE   E O   1 
ATOM   15844 C  CB  . ILE   E 2 617 ? 27.519  -5.294  -7.998  1.00 95.16  ? 921  ILE   E CB  1 
ATOM   15845 C  CG1 . ILE   E 2 617 ? 27.863  -3.943  -7.391  1.00 93.50  ? 921  ILE   E CG1 1 
ATOM   15846 C  CG2 . ILE   E 2 617 ? 28.679  -5.776  -8.830  1.00 97.18  ? 921  ILE   E CG2 1 
ATOM   15847 C  CD1 . ILE   E 2 617 ? 27.835  -3.932  -5.888  1.00 100.23 ? 921  ILE   E CD1 1 
ATOM   15848 N  N   . LEU   E 2 618 ? 25.862  -6.982  -10.485 1.00 92.52  ? 922  LEU   E N   1 
ATOM   15849 C  CA  . LEU   E 2 618 ? 25.466  -8.301  -10.966 1.00 90.57  ? 922  LEU   E CA  1 
ATOM   15850 C  C   . LEU   E 2 618 ? 26.694  -9.124  -11.337 1.00 90.10  ? 922  LEU   E C   1 
ATOM   15851 O  O   . LEU   E 2 618 ? 27.442  -8.757  -12.251 1.00 91.26  ? 922  LEU   E O   1 
ATOM   15852 C  CB  . LEU   E 2 618 ? 24.539  -8.173  -12.169 1.00 87.68  ? 922  LEU   E CB  1 
ATOM   15853 C  CG  . LEU   E 2 618 ? 24.213  -9.550  -12.720 1.00 84.34  ? 922  LEU   E CG  1 
ATOM   15854 C  CD1 . LEU   E 2 618 ? 23.521  -10.385 -11.655 1.00 89.90  ? 922  LEU   E CD1 1 
ATOM   15855 C  CD2 . LEU   E 2 618 ? 23.358  -9.421  -13.939 1.00 82.56  ? 922  LEU   E CD2 1 
ATOM   15856 N  N   . VAL   E 2 619 ? 26.889  -10.251 -10.657 1.00 87.23  ? 923  VAL   E N   1 
ATOM   15857 C  CA  . VAL   E 2 619 ? 28.056  -11.099 -10.855 1.00 86.35  ? 923  VAL   E CA  1 
ATOM   15858 C  C   . VAL   E 2 619 ? 27.655  -12.416 -11.511 1.00 90.68  ? 923  VAL   E C   1 
ATOM   15859 O  O   . VAL   E 2 619 ? 26.628  -13.008 -11.157 1.00 93.43  ? 923  VAL   E O   1 
ATOM   15860 C  CB  . VAL   E 2 619 ? 28.771  -11.359 -9.522  1.00 89.23  ? 923  VAL   E CB  1 
ATOM   15861 C  CG1 . VAL   E 2 619 ? 30.043  -12.138 -9.762  1.00 93.31  ? 923  VAL   E CG1 1 
ATOM   15862 C  CG2 . VAL   E 2 619 ? 29.041  -10.062 -8.800  1.00 91.56  ? 923  VAL   E CG2 1 
ATOM   15863 N  N   . GLY   E 2 620 ? 28.490  -12.897 -12.431 1.00 89.19  ? 924  GLY   E N   1 
ATOM   15864 C  CA  . GLY   E 2 620 ? 28.158  -14.068 -13.220 1.00 85.16  ? 924  GLY   E CA  1 
ATOM   15865 C  C   . GLY   E 2 620 ? 29.352  -14.982 -13.409 1.00 88.15  ? 924  GLY   E C   1 
ATOM   15866 O  O   . GLY   E 2 620 ? 30.511  -14.582 -13.271 1.00 87.73  ? 924  GLY   E O   1 
ATOM   15867 N  N   . ASP   E 2 621 ? 29.035  -16.211 -13.792 1.00 100.20 ? 925  ASP   E N   1 
ATOM   15868 C  CA  . ASP   E 2 621 ? 29.931  -17.357 -13.738 1.00 99.30  ? 925  ASP   E CA  1 
ATOM   15869 C  C   . ASP   E 2 621 ? 29.590  -18.220 -14.940 1.00 99.51  ? 925  ASP   E C   1 
ATOM   15870 O  O   . ASP   E 2 621 ? 28.416  -18.314 -15.303 1.00 101.05 ? 925  ASP   E O   1 
ATOM   15871 C  CB  . ASP   E 2 621 ? 29.722  -18.078 -12.394 1.00 101.27 ? 925  ASP   E CB  1 
ATOM   15872 C  CG  . ASP   E 2 621 ? 30.410  -19.422 -12.295 1.00 106.31 ? 925  ASP   E CG  1 
ATOM   15873 O  OD1 . ASP   E 2 621 ? 31.649  -19.445 -12.118 1.00 109.39 ? 925  ASP   E OD1 1 
ATOM   15874 O  OD2 . ASP   E 2 621 ? 29.697  -20.456 -12.318 1.00 106.41 ? 925  ASP   E OD2 1 
ATOM   15875 N  N   . LEU   E 2 622 ? 30.597  -18.819 -15.580 1.00 90.02  ? 926  LEU   E N   1 
ATOM   15876 C  CA  . LEU   E 2 622 ? 30.386  -19.449 -16.889 1.00 86.59  ? 926  LEU   E CA  1 
ATOM   15877 C  C   . LEU   E 2 622 ? 29.095  -20.256 -16.925 1.00 87.97  ? 926  LEU   E C   1 
ATOM   15878 O  O   . LEU   E 2 622 ? 28.437  -20.304 -17.969 1.00 84.89  ? 926  LEU   E O   1 
ATOM   15879 C  CB  . LEU   E 2 622 ? 31.635  -20.182 -17.354 1.00 81.98  ? 926  LEU   E CB  1 
ATOM   15880 C  CG  . LEU   E 2 622 ? 32.431  -19.336 -18.332 1.00 80.50  ? 926  LEU   E CG  1 
ATOM   15881 C  CD1 . LEU   E 2 622 ? 32.889  -18.105 -17.607 1.00 94.13  ? 926  LEU   E CD1 1 
ATOM   15882 C  CD2 . LEU   E 2 622 ? 33.601  -20.085 -18.869 1.00 75.95  ? 926  LEU   E CD2 1 
ATOM   15883 N  N   . MET   E 2 623 ? 28.743  -20.924 -15.819 1.00 92.34  ? 927  MET   E N   1 
ATOM   15884 C  CA  . MET   E 2 623 ? 27.529  -21.734 -15.767 1.00 87.49  ? 927  MET   E CA  1 
ATOM   15885 C  C   . MET   E 2 623 ? 26.274  -21.074 -15.185 1.00 86.03  ? 927  MET   E C   1 
ATOM   15886 O  O   . MET   E 2 623 ? 25.702  -21.548 -14.198 1.00 85.90  ? 927  MET   E O   1 
ATOM   15887 C  CB  . MET   E 2 623 ? 27.955  -22.997 -14.998 1.00 87.08  ? 927  MET   E CB  1 
ATOM   15888 C  CG  . MET   E 2 623 ? 29.354  -23.532 -15.416 1.00 86.64  ? 927  MET   E CG  1 
ATOM   15889 S  SD  . MET   E 2 623 ? 29.899  -25.201 -14.932 1.00 90.67  ? 927  MET   E SD  1 
ATOM   15890 C  CE  . MET   E 2 623 ? 28.499  -26.222 -15.308 1.00 80.60  ? 927  MET   E CE  1 
ATOM   15891 N  N   . ARG   E 2 624 ? 25.852  -19.970 -15.817 1.00 87.15  ? 928  ARG   E N   1 
ATOM   15892 C  CA  . ARG   E 2 624 ? 24.643  -19.203 -15.523 1.00 88.05  ? 928  ARG   E CA  1 
ATOM   15893 C  C   . ARG   E 2 624 ? 24.456  -19.026 -14.019 1.00 93.23  ? 928  ARG   E C   1 
ATOM   15894 O  O   . ARG   E 2 624 ? 23.325  -18.953 -13.524 1.00 94.01  ? 928  ARG   E O   1 
ATOM   15895 C  CB  . ARG   E 2 624 ? 23.413  -19.858 -16.170 1.00 88.89  ? 928  ARG   E CB  1 
ATOM   15896 C  CG  . ARG   E 2 624 ? 22.212  -18.929 -16.423 1.00 91.30  ? 928  ARG   E CG  1 
ATOM   15897 C  CD  . ARG   E 2 624 ? 20.949  -19.786 -16.620 1.00 96.00  ? 928  ARG   E CD  1 
ATOM   15898 N  NE  . ARG   E 2 624 ? 19.657  -19.113 -16.462 1.00 100.06 ? 928  ARG   E NE  1 
ATOM   15899 C  CZ  . ARG   E 2 624 ? 19.189  -18.600 -15.324 1.00 105.04 ? 928  ARG   E CZ  1 
ATOM   15900 N  NH1 . ARG   E 2 624 ? 19.949  -18.482 -14.243 1.00 102.44 ? 928  ARG   E NH1 1 
ATOM   15901 N  NH2 . ARG   E 2 624 ? 17.922  -18.194 -15.266 1.00 107.84 ? 928  ARG   E NH2 1 
ATOM   15902 N  N   . SER   E 2 625 ? 25.561  -18.948 -13.283 1.00 95.64  ? 929  SER   E N   1 
ATOM   15903 C  CA  . SER   E 2 625 ? 25.508  -18.626 -11.864 1.00 93.50  ? 929  SER   E CA  1 
ATOM   15904 C  C   . SER   E 2 625 ? 25.375  -17.117 -11.771 1.00 91.93  ? 929  SER   E C   1 
ATOM   15905 O  O   . SER   E 2 625 ? 26.358  -16.392 -11.917 1.00 93.68  ? 929  SER   E O   1 
ATOM   15906 C  CB  . SER   E 2 625 ? 26.755  -19.129 -11.144 1.00 96.65  ? 929  SER   E CB  1 
ATOM   15907 O  OG  . SER   E 2 625 ? 27.055  -20.486 -11.453 1.00 95.91  ? 929  SER   E OG  1 
ATOM   15908 N  N   . VAL   E 2 626 ? 24.154  -16.626 -11.566 1.00 96.74  ? 930  VAL   E N   1 
ATOM   15909 C  CA  . VAL   E 2 626 ? 23.944  -15.204 -11.307 1.00 98.96  ? 930  VAL   E CA  1 
ATOM   15910 C  C   . VAL   E 2 626 ? 23.798  -14.987 -9.805  1.00 104.65 ? 930  VAL   E C   1 
ATOM   15911 O  O   . VAL   E 2 626 ? 23.605  -15.923 -9.010  1.00 101.55 ? 930  VAL   E O   1 
ATOM   15912 C  CB  . VAL   E 2 626 ? 22.745  -14.568 -12.061 1.00 90.90  ? 930  VAL   E CB  1 
ATOM   15913 C  CG1 . VAL   E 2 626 ? 22.973  -14.630 -13.539 1.00 87.40  ? 930  VAL   E CG1 1 
ATOM   15914 C  CG2 . VAL   E 2 626 ? 21.416  -15.208 -11.663 1.00 99.24  ? 930  VAL   E CG2 1 
ATOM   15915 N  N   . LEU   E 2 627 ? 23.862  -13.712 -9.428  1.00 107.43 ? 931  LEU   E N   1 
ATOM   15916 C  CA  . LEU   E 2 627 ? 24.170  -13.298 -8.071  1.00 106.65 ? 931  LEU   E CA  1 
ATOM   15917 C  C   . LEU   E 2 627 ? 24.031  -11.785 -8.154  1.00 105.84 ? 931  LEU   E C   1 
ATOM   15918 O  O   . LEU   E 2 627 ? 24.572  -11.153 -9.071  1.00 104.34 ? 931  LEU   E O   1 
ATOM   15919 C  CB  . LEU   E 2 627 ? 25.529  -13.856 -7.651  1.00 104.57 ? 931  LEU   E CB  1 
ATOM   15920 C  CG  . LEU   E 2 627 ? 26.094  -13.233 -6.392  1.00 108.27 ? 931  LEU   E CG  1 
ATOM   15921 C  CD1 . LEU   E 2 627 ? 25.071  -13.382 -5.273  1.00 111.94 ? 931  LEU   E CD1 1 
ATOM   15922 C  CD2 . LEU   E 2 627 ? 27.427  -13.878 -6.040  1.00 109.65 ? 931  LEU   E CD2 1 
ATOM   15923 N  N   . LEU   E 2 628 ? 23.297  -11.197 -7.215  1.00 105.07 ? 932  LEU   E N   1 
ATOM   15924 C  CA  . LEU   E 2 628 ? 23.027  -9.769  -7.211  1.00 99.67  ? 932  LEU   E CA  1 
ATOM   15925 C  C   . LEU   E 2 628 ? 23.508  -9.305  -5.840  1.00 102.92 ? 932  LEU   E C   1 
ATOM   15926 O  O   . LEU   E 2 628 ? 23.118  -9.882  -4.816  1.00 102.38 ? 932  LEU   E O   1 
ATOM   15927 C  CB  . LEU   E 2 628 ? 21.566  -9.392  -7.458  1.00 93.62  ? 932  LEU   E CB  1 
ATOM   15928 C  CG  . LEU   E 2 628 ? 21.243  -7.909  -7.602  1.00 94.28  ? 932  LEU   E CG  1 
ATOM   15929 C  CD1 . LEU   E 2 628 ? 21.964  -7.290  -8.784  1.00 98.02  ? 932  LEU   E CD1 1 
ATOM   15930 C  CD2 . LEU   E 2 628 ? 19.754  -7.715  -7.719  1.00 94.72  ? 932  LEU   E CD2 1 
ATOM   15931 N  N   . LEU   E 2 629 ? 24.386  -8.288  -5.829  1.00 104.62 ? 933  LEU   E N   1 
ATOM   15932 C  CA  . LEU   E 2 629 ? 24.926  -7.668  -4.620  1.00 102.83 ? 933  LEU   E CA  1 
ATOM   15933 C  C   . LEU   E 2 629 ? 24.572  -6.183  -4.576  1.00 104.45 ? 933  LEU   E C   1 
ATOM   15934 O  O   . LEU   E 2 629 ? 24.272  -5.553  -5.598  1.00 102.70 ? 933  LEU   E O   1 
ATOM   15935 C  CB  . LEU   E 2 629 ? 26.457  -7.808  -4.529  1.00 98.59  ? 933  LEU   E CB  1 
ATOM   15936 C  CG  . LEU   E 2 629 ? 27.087  -9.189  -4.663  1.00 96.95  ? 933  LEU   E CG  1 
ATOM   15937 C  CD1 . LEU   E 2 629 ? 28.575  -9.059  -4.850  1.00 98.05  ? 933  LEU   E CD1 1 
ATOM   15938 C  CD2 . LEU   E 2 629 ? 26.783  -10.039 -3.450  1.00 102.74 ? 933  LEU   E CD2 1 
ATOM   15939 N  N   . ALA   E 2 630 ? 24.646  -5.625  -3.364  1.00 111.53 ? 934  ALA   E N   1 
ATOM   15940 C  CA  . ALA   E 2 630 ? 24.345  -4.220  -3.099  1.00 112.62 ? 934  ALA   E CA  1 
ATOM   15941 C  C   . ALA   E 2 630 ? 25.401  -3.653  -2.162  1.00 116.72 ? 934  ALA   E C   1 
ATOM   15942 O  O   . ALA   E 2 630 ? 25.561  -4.147  -1.037  1.00 117.45 ? 934  ALA   E O   1 
ATOM   15943 C  CB  . ALA   E 2 630 ? 22.959  -4.050  -2.475  1.00 112.29 ? 934  ALA   E CB  1 
ATOM   15944 N  N   . TYR   E 2 631 ? 26.116  -2.619  -2.632  1.00 113.06 ? 935  TYR   E N   1 
ATOM   15945 C  CA  . TYR   E 2 631 ? 27.068  -1.866  -1.813  1.00 111.54 ? 935  TYR   E CA  1 
ATOM   15946 C  C   . TYR   E 2 631 ? 26.271  -1.017  -0.823  1.00 112.90 ? 935  TYR   E C   1 
ATOM   15947 O  O   . TYR   E 2 631 ? 25.667  -0.013  -1.198  1.00 111.69 ? 935  TYR   E O   1 
ATOM   15948 C  CB  . TYR   E 2 631 ? 27.974  -1.013  -2.701  1.00 107.00 ? 935  TYR   E CB  1 
ATOM   15949 C  CG  . TYR   E 2 631 ? 28.886  -0.030  -1.958  1.00 109.07 ? 935  TYR   E CG  1 
ATOM   15950 C  CD1 . TYR   E 2 631 ? 29.673  -0.446  -0.886  1.00 112.88 ? 935  TYR   E CD1 1 
ATOM   15951 C  CD2 . TYR   E 2 631 ? 28.971  1.312   -2.340  1.00 110.34 ? 935  TYR   E CD2 1 
ATOM   15952 C  CE1 . TYR   E 2 631 ? 30.505  0.454   -0.204  1.00 117.55 ? 935  TYR   E CE1 1 
ATOM   15953 C  CE2 . TYR   E 2 631 ? 29.798  2.212   -1.668  1.00 107.66 ? 935  TYR   E CE2 1 
ATOM   15954 C  CZ  . TYR   E 2 631 ? 30.564  1.780   -0.601  1.00 113.00 ? 935  TYR   E CZ  1 
ATOM   15955 O  OH  . TYR   E 2 631 ? 31.388  2.662   0.070   1.00 111.52 ? 935  TYR   E OH  1 
ATOM   15956 N  N   . LYS   E 2 632 ? 26.226  -1.440  0.444   1.00 112.92 ? 936  LYS   E N   1 
ATOM   15957 C  CA  . LYS   E 2 632 ? 25.535  -0.650  1.448   1.00 112.84 ? 936  LYS   E CA  1 
ATOM   15958 C  C   . LYS   E 2 632 ? 26.462  0.505   1.801   1.00 118.63 ? 936  LYS   E C   1 
ATOM   15959 O  O   . LYS   E 2 632 ? 27.508  0.270   2.420   1.00 123.68 ? 936  LYS   E O   1 
ATOM   15960 C  CB  . LYS   E 2 632 ? 25.204  -1.491  2.685   1.00 114.18 ? 936  LYS   E CB  1 
ATOM   15961 C  CG  . LYS   E 2 632 ? 24.626  -2.871  2.387   1.00 111.05 ? 936  LYS   E CG  1 
ATOM   15962 C  CD  . LYS   E 2 632 ? 23.320  -2.802  1.619   1.00 109.29 ? 936  LYS   E CD  1 
ATOM   15963 C  CE  . LYS   E 2 632 ? 22.136  -2.975  2.543   1.00 111.55 ? 936  LYS   E CE  1 
ATOM   15964 N  NZ  . LYS   E 2 632 ? 20.886  -3.287  1.799   1.00 115.78 ? 936  LYS   E NZ  1 
ATOM   15965 N  N   . PRO   E 2 633 ? 26.141  1.764   1.399   1.00 118.70 ? 937  PRO   E N   1 
ATOM   15966 C  CA  . PRO   E 2 633 ? 27.115  2.855   1.582   1.00 119.43 ? 937  PRO   E CA  1 
ATOM   15967 C  C   . PRO   E 2 633 ? 27.436  3.053   3.056   1.00 128.33 ? 937  PRO   E C   1 
ATOM   15968 O  O   . PRO   E 2 633 ? 28.604  2.963   3.465   1.00 127.07 ? 937  PRO   E O   1 
ATOM   15969 C  CB  . PRO   E 2 633 ? 26.415  4.081   0.976   1.00 104.85 ? 937  PRO   E CB  1 
ATOM   15970 C  CG  . PRO   E 2 633 ? 25.165  3.576   0.333   1.00 103.87 ? 937  PRO   E CG  1 
ATOM   15971 C  CD  . PRO   E 2 633 ? 24.826  2.262   0.966   1.00 112.47 ? 937  PRO   E CD  1 
ATOM   15972 N  N   . MET   E 2 634 ? 26.386  3.314   3.850   1.00 125.06 ? 938  MET   E N   1 
ATOM   15973 C  CA  . MET   E 2 634 ? 26.508  3.508   5.287   1.00 126.80 ? 938  MET   E CA  1 
ATOM   15974 C  C   . MET   E 2 634 ? 27.401  2.448   5.925   1.00 125.55 ? 938  MET   E C   1 
ATOM   15975 O  O   . MET   E 2 634 ? 28.473  2.760   6.448   1.00 128.50 ? 938  MET   E O   1 
ATOM   15976 C  CB  . MET   E 2 634 ? 25.109  3.522   5.916   1.00 126.77 ? 938  MET   E CB  1 
ATOM   15977 N  N   . GLU   E 2 635 ? 26.991  1.173   5.852   1.00 126.75 ? 939  GLU   E N   1 
ATOM   15978 C  CA  . GLU   E 2 635 ? 27.793  0.093   6.421   1.00 129.56 ? 939  GLU   E CA  1 
ATOM   15979 C  C   . GLU   E 2 635 ? 29.192  0.037   5.804   1.00 134.55 ? 939  GLU   E C   1 
ATOM   15980 O  O   . GLU   E 2 635 ? 30.174  -0.250  6.508   1.00 132.53 ? 939  GLU   E O   1 
ATOM   15981 C  CB  . GLU   E 2 635 ? 27.065  -1.241  6.251   1.00 128.92 ? 939  GLU   E CB  1 
ATOM   15982 N  N   . GLY   E 2 636 ? 29.307  0.308   4.510   1.00 151.75 ? 940  GLY   E N   1 
ATOM   15983 C  CA  . GLY   E 2 636 ? 30.615  0.240   3.851   1.00 150.08 ? 940  GLY   E CA  1 
ATOM   15984 C  C   . GLY   E 2 636 ? 31.090  -1.147  3.467   1.00 151.15 ? 940  GLY   E C   1 
ATOM   15985 O  O   . GLY   E 2 636 ? 32.302  -1.397  3.455   1.00 151.65 ? 940  GLY   E O   1 
ATOM   15986 N  N   . ASN   E 2 637 ? 30.168  -2.073  3.183   1.00 128.02 ? 941  ASN   E N   1 
ATOM   15987 C  CA  . ASN   E 2 637 ? 30.515  -3.392  2.677   1.00 119.38 ? 941  ASN   E CA  1 
ATOM   15988 C  C   . ASN   E 2 637 ? 29.384  -3.842  1.766   1.00 118.59 ? 941  ASN   E C   1 
ATOM   15989 O  O   . ASN   E 2 637 ? 28.253  -3.369  1.893   1.00 119.93 ? 941  ASN   E O   1 
ATOM   15990 C  CB  . ASN   E 2 637 ? 30.739  -4.398  3.820   1.00 119.86 ? 941  ASN   E CB  1 
ATOM   15991 C  CG  . ASN   E 2 637 ? 31.237  -5.776  3.326   1.00 120.98 ? 941  ASN   E CG  1 
ATOM   15992 O  OD1 . ASN   E 2 637 ? 30.453  -6.722  3.195   1.00 115.69 ? 941  ASN   E OD1 1 
ATOM   15993 N  ND2 . ASN   E 2 637 ? 32.542  -5.882  3.044   1.00 119.68 ? 941  ASN   E ND2 1 
ATOM   15994 N  N   . PHE   E 2 638 ? 29.695  -4.760  0.845   1.00 117.83 ? 942  PHE   E N   1 
ATOM   15995 C  CA  . PHE   E 2 638 ? 28.677  -5.339  -0.024  1.00 113.75 ? 942  PHE   E CA  1 
ATOM   15996 C  C   . PHE   E 2 638 ? 27.760  -6.272  0.770   1.00 111.72 ? 942  PHE   E C   1 
ATOM   15997 O  O   . PHE   E 2 638 ? 28.219  -7.029  1.634   1.00 109.72 ? 942  PHE   E O   1 
ATOM   15998 C  CB  . PHE   E 2 638 ? 29.327  -6.122  -1.171  1.00 109.49 ? 942  PHE   E CB  1 
ATOM   15999 C  CG  . PHE   E 2 638 ? 30.392  -5.371  -1.919  1.00 101.05 ? 942  PHE   E CG  1 
ATOM   16000 C  CD1 . PHE   E 2 638 ? 30.062  -4.514  -2.959  1.00 102.08 ? 942  PHE   E CD1 1 
ATOM   16001 C  CD2 . PHE   E 2 638 ? 31.727  -5.549  -1.598  1.00 102.70 ? 942  PHE   E CD2 1 
ATOM   16002 C  CE1 . PHE   E 2 638 ? 31.054  -3.837  -3.664  1.00 104.54 ? 942  PHE   E CE1 1 
ATOM   16003 C  CE2 . PHE   E 2 638 ? 32.719  -4.882  -2.288  1.00 105.28 ? 942  PHE   E CE2 1 
ATOM   16004 C  CZ  . PHE   E 2 638 ? 32.387  -4.023  -3.327  1.00 103.75 ? 942  PHE   E CZ  1 
ATOM   16005 N  N   . GLU   E 2 639 ? 26.464  -6.243  0.444   1.00 107.20 ? 943  GLU   E N   1 
ATOM   16006 C  CA  . GLU   E 2 639 ? 25.471  -7.123  1.052   1.00 105.09 ? 943  GLU   E CA  1 
ATOM   16007 C  C   . GLU   E 2 639 ? 24.752  -7.897  -0.040  1.00 107.12 ? 943  GLU   E C   1 
ATOM   16008 O  O   . GLU   E 2 639 ? 24.205  -7.288  -0.964  1.00 109.88 ? 943  GLU   E O   1 
ATOM   16009 C  CB  . GLU   E 2 639 ? 24.450  -6.329  1.866   1.00 105.38 ? 943  GLU   E CB  1 
ATOM   16010 N  N   . GLU   E 2 640 ? 24.743  -9.230  0.073   1.00 105.58 ? 944  GLU   E N   1 
ATOM   16011 C  CA  . GLU   E 2 640 ? 24.078  -10.074 -0.919  1.00 105.04 ? 944  GLU   E CA  1 
ATOM   16012 C  C   . GLU   E 2 640 ? 22.565  -9.878  -0.883  1.00 103.55 ? 944  GLU   E C   1 
ATOM   16013 O  O   . GLU   E 2 640 ? 21.961  -9.763  0.181   1.00 104.62 ? 944  GLU   E O   1 
ATOM   16014 C  CB  . GLU   E 2 640 ? 24.395  -11.551 -0.688  1.00 104.78 ? 944  GLU   E CB  1 
ATOM   16015 C  CG  . GLU   E 2 640 ? 24.071  -12.423 -1.918  1.00 109.68 ? 944  GLU   E CG  1 
ATOM   16016 C  CD  . GLU   E 2 640 ? 23.492  -13.810 -1.601  1.00 114.45 ? 944  GLU   E CD  1 
ATOM   16017 O  OE1 . GLU   E 2 640 ? 22.261  -13.924 -1.342  1.00 112.88 ? 944  GLU   E OE1 1 
ATOM   16018 O  OE2 . GLU   E 2 640 ? 24.270  -14.796 -1.645  1.00 114.11 ? 944  GLU   E OE2 1 
ATOM   16019 N  N   . ILE   E 2 641 ? 21.953  -9.874  -2.061  1.00 103.38 ? 945  ILE   E N   1 
ATOM   16020 C  CA  . ILE   E 2 641 ? 20.527  -9.620  -2.164  1.00 101.30 ? 945  ILE   E CA  1 
ATOM   16021 C  C   . ILE   E 2 641 ? 19.820  -10.917 -2.535  1.00 111.95 ? 945  ILE   E C   1 
ATOM   16022 O  O   . ILE   E 2 641 ? 18.945  -11.385 -1.801  1.00 117.02 ? 945  ILE   E O   1 
ATOM   16023 C  CB  . ILE   E 2 641 ? 20.238  -8.531  -3.201  1.00 100.77 ? 945  ILE   E CB  1 
ATOM   16024 C  CG1 . ILE   E 2 641 ? 21.238  -7.379  -3.094  1.00 104.10 ? 945  ILE   E CG1 1 
ATOM   16025 C  CG2 . ILE   E 2 641 ? 18.842  -8.032  -3.034  1.00 106.08 ? 945  ILE   E CG2 1 
ATOM   16026 C  CD1 . ILE   E 2 641 ? 21.078  -6.328  -4.178  1.00 106.69 ? 945  ILE   E CD1 1 
ATOM   16027 N  N   . ALA   E 2 642 ? 20.192  -11.477 -3.684  1.00 112.63 ? 946  ALA   E N   1 
ATOM   16028 C  CA  . ALA   E 2 642 ? 19.574  -12.685 -4.203  1.00 111.84 ? 946  ALA   E CA  1 
ATOM   16029 C  C   . ALA   E 2 642 ? 20.547  -13.360 -5.163  1.00 109.42 ? 946  ALA   E C   1 
ATOM   16030 O  O   . ALA   E 2 642 ? 21.644  -12.857 -5.441  1.00 106.24 ? 946  ALA   E O   1 
ATOM   16031 C  CB  . ALA   E 2 642 ? 18.252  -12.357 -4.892  1.00 110.98 ? 946  ALA   E CB  1 
ATOM   16032 N  N   . ARG   E 2 643 ? 20.117  -14.510 -5.679  1.00 112.49 ? 947  ARG   E N   1 
ATOM   16033 C  CA  . ARG   E 2 643 ? 20.876  -15.269 -6.664  1.00 109.39 ? 947  ARG   E CA  1 
ATOM   16034 C  C   . ARG   E 2 643 ? 19.977  -16.338 -7.274  1.00 110.43 ? 947  ARG   E C   1 
ATOM   16035 O  O   . ARG   E 2 643 ? 18.866  -16.598 -6.798  1.00 112.73 ? 947  ARG   E O   1 
ATOM   16036 C  CB  . ARG   E 2 643 ? 22.117  -15.893 -6.026  1.00 105.79 ? 947  ARG   E CB  1 
ATOM   16037 C  CG  . ARG   E 2 643 ? 21.821  -16.648 -4.766  1.00 107.73 ? 947  ARG   E CG  1 
ATOM   16038 C  CD  . ARG   E 2 643 ? 22.979  -17.528 -4.395  1.00 111.91 ? 947  ARG   E CD  1 
ATOM   16039 N  NE  . ARG   E 2 643 ? 24.216  -16.770 -4.265  1.00 112.47 ? 947  ARG   E NE  1 
ATOM   16040 C  CZ  . ARG   E 2 643 ? 25.400  -17.305 -3.993  1.00 113.73 ? 947  ARG   E CZ  1 
ATOM   16041 N  NH1 . ARG   E 2 643 ? 25.545  -18.609 -3.795  1.00 114.63 ? 947  ARG   E NH1 1 
ATOM   16042 N  NH2 . ARG   E 2 643 ? 26.470  -16.513 -3.921  1.00 114.71 ? 947  ARG   E NH2 1 
ATOM   16043 N  N   . ASP   E 2 644 ? 20.479  -16.957 -8.341  1.00 106.46 ? 948  ASP   E N   1 
ATOM   16044 C  CA  . ASP   E 2 644 ? 19.870  -18.147 -8.921  1.00 105.71 ? 948  ASP   E CA  1 
ATOM   16045 C  C   . ASP   E 2 644 ? 20.960  -18.923 -9.640  1.00 105.67 ? 948  ASP   E C   1 
ATOM   16046 O  O   . ASP   E 2 644 ? 21.716  -18.339 -10.421 1.00 104.03 ? 948  ASP   E O   1 
ATOM   16047 C  CB  . ASP   E 2 644 ? 18.729  -17.804 -9.890  1.00 107.86 ? 948  ASP   E CB  1 
ATOM   16048 C  CG  . ASP   E 2 644 ? 18.033  -19.053 -10.470 1.00 111.06 ? 948  ASP   E CG  1 
ATOM   16049 O  OD1 . ASP   E 2 644 ? 17.606  -19.939 -9.689  1.00 111.64 ? 948  ASP   E OD1 1 
ATOM   16050 O  OD2 . ASP   E 2 644 ? 17.888  -19.129 -11.715 1.00 111.67 ? 948  ASP   E OD2 1 
ATOM   16051 N  N   . PHE   E 2 645 ? 21.053  -20.223 -9.344  1.00 108.42 ? 949  PHE   E N   1 
ATOM   16052 C  CA  . PHE   E 2 645 ? 21.981  -21.146 -9.997  1.00 108.02 ? 949  PHE   E CA  1 
ATOM   16053 C  C   . PHE   E 2 645 ? 21.171  -22.133 -10.835 1.00 104.49 ? 949  PHE   E C   1 
ATOM   16054 O  O   . PHE   E 2 645 ? 20.433  -22.969 -10.294 1.00 104.48 ? 949  PHE   E O   1 
ATOM   16055 C  CB  . PHE   E 2 645 ? 22.851  -21.891 -8.983  1.00 107.81 ? 949  PHE   E CB  1 
ATOM   16056 C  CG  . PHE   E 2 645 ? 23.828  -21.015 -8.256  1.00 109.04 ? 949  PHE   E CG  1 
ATOM   16057 C  CD1 . PHE   E 2 645 ? 24.139  -19.750 -8.737  1.00 106.94 ? 949  PHE   E CD1 1 
ATOM   16058 C  CD2 . PHE   E 2 645 ? 24.442  -21.454 -7.087  1.00 111.36 ? 949  PHE   E CD2 1 
ATOM   16059 C  CE1 . PHE   E 2 645 ? 25.047  -18.932 -8.067  1.00 107.98 ? 949  PHE   E CE1 1 
ATOM   16060 C  CE2 . PHE   E 2 645 ? 25.353  -20.645 -6.406  1.00 110.02 ? 949  PHE   E CE2 1 
ATOM   16061 C  CZ  . PHE   E 2 645 ? 25.657  -19.384 -6.897  1.00 106.66 ? 949  PHE   E CZ  1 
ATOM   16062 N  N   . ASN   E 2 646 ? 21.309  -22.035 -12.153 1.00 100.95 ? 950  ASN   E N   1 
ATOM   16063 C  CA  . ASN   E 2 646 ? 20.719  -23.001 -13.075 1.00 96.90  ? 950  ASN   E CA  1 
ATOM   16064 C  C   . ASN   E 2 646 ? 21.811  -23.350 -14.064 1.00 92.08  ? 950  ASN   E C   1 
ATOM   16065 O  O   . ASN   E 2 646 ? 22.014  -22.627 -15.055 1.00 91.85  ? 950  ASN   E O   1 
ATOM   16066 C  CB  . ASN   E 2 646 ? 19.491  -22.461 -13.783 1.00 98.40  ? 950  ASN   E CB  1 
ATOM   16067 C  CG  . ASN   E 2 646 ? 18.725  -23.545 -14.463 1.00 100.05 ? 950  ASN   E CG  1 
ATOM   16068 O  OD1 . ASN   E 2 646 ? 19.084  -23.973 -15.557 1.00 104.44 ? 950  ASN   E OD1 1 
ATOM   16069 N  ND2 . ASN   E 2 646 ? 17.686  -24.038 -13.803 1.00 101.46 ? 950  ASN   E ND2 1 
ATOM   16070 N  N   . PRO   E 2 647 ? 22.529  -24.439 -13.830 1.00 90.32  ? 951  PRO   E N   1 
ATOM   16071 C  CA  . PRO   E 2 647 ? 23.824  -24.635 -14.494 1.00 90.07  ? 951  PRO   E CA  1 
ATOM   16072 C  C   . PRO   E 2 647 ? 23.655  -24.846 -15.992 1.00 90.64  ? 951  PRO   E C   1 
ATOM   16073 O  O   . PRO   E 2 647 ? 22.930  -25.742 -16.444 1.00 92.48  ? 951  PRO   E O   1 
ATOM   16074 C  CB  . PRO   E 2 647 ? 24.398  -25.878 -13.797 1.00 84.96  ? 951  PRO   E CB  1 
ATOM   16075 C  CG  . PRO   E 2 647 ? 23.347  -26.313 -12.799 1.00 89.63  ? 951  PRO   E CG  1 
ATOM   16076 C  CD  . PRO   E 2 647 ? 22.064  -25.647 -13.147 1.00 90.02  ? 951  PRO   E CD  1 
ATOM   16077 N  N   . ASN   E 2 648 ? 24.350  -24.016 -16.757 1.00 83.97  ? 952  ASN   E N   1 
ATOM   16078 C  CA  . ASN   E 2 648 ? 24.280  -23.996 -18.205 1.00 83.80  ? 952  ASN   E CA  1 
ATOM   16079 C  C   . ASN   E 2 648 ? 25.279  -22.954 -18.667 1.00 84.41  ? 952  ASN   E C   1 
ATOM   16080 O  O   . ASN   E 2 648 ? 25.491  -21.960 -17.980 1.00 87.80  ? 952  ASN   E O   1 
ATOM   16081 C  CB  . ASN   E 2 648 ? 22.864  -23.656 -18.685 1.00 86.75  ? 952  ASN   E CB  1 
ATOM   16082 C  CG  . ASN   E 2 648 ? 22.754  -23.603 -20.190 1.00 87.40  ? 952  ASN   E CG  1 
ATOM   16083 O  OD1 . ASN   E 2 648 ? 22.342  -22.598 -20.746 1.00 89.34  ? 952  ASN   E OD1 1 
ATOM   16084 N  ND2 . ASN   E 2 648 ? 23.123  -24.688 -20.859 1.00 91.35  ? 952  ASN   E ND2 1 
ATOM   16085 N  N   . TRP   E 2 649 ? 25.909  -23.193 -19.808 1.00 83.17  ? 953  TRP   E N   1 
ATOM   16086 C  CA  . TRP   E 2 649 ? 26.929  -22.262 -20.261 1.00 81.58  ? 953  TRP   E CA  1 
ATOM   16087 C  C   . TRP   E 2 649 ? 26.298  -20.895 -20.535 1.00 82.60  ? 953  TRP   E C   1 
ATOM   16088 O  O   . TRP   E 2 649 ? 25.229  -20.815 -21.147 1.00 84.84  ? 953  TRP   E O   1 
ATOM   16089 C  CB  . TRP   E 2 649 ? 27.626  -22.826 -21.507 1.00 83.84  ? 953  TRP   E CB  1 
ATOM   16090 C  CG  . TRP   E 2 649 ? 28.275  -24.212 -21.328 1.00 79.13  ? 953  TRP   E CG  1 
ATOM   16091 C  CD1 . TRP   E 2 649 ? 28.094  -25.299 -22.119 1.00 84.38  ? 953  TRP   E CD1 1 
ATOM   16092 C  CD2 . TRP   E 2 649 ? 29.198  -24.623 -20.306 1.00 79.29  ? 953  TRP   E CD2 1 
ATOM   16093 N  NE1 . TRP   E 2 649 ? 28.837  -26.357 -21.663 1.00 82.77  ? 953  TRP   E NE1 1 
ATOM   16094 C  CE2 . TRP   E 2 649 ? 29.522  -25.964 -20.548 1.00 78.40  ? 953  TRP   E CE2 1 
ATOM   16095 C  CE3 . TRP   E 2 649 ? 29.780  -23.983 -19.209 1.00 85.74  ? 953  TRP   E CE3 1 
ATOM   16096 C  CZ2 . TRP   E 2 649 ? 30.389  -26.680 -19.734 1.00 82.12  ? 953  TRP   E CZ2 1 
ATOM   16097 C  CZ3 . TRP   E 2 649 ? 30.657  -24.701 -18.402 1.00 81.01  ? 953  TRP   E CZ3 1 
ATOM   16098 C  CH2 . TRP   E 2 649 ? 30.947  -26.031 -18.667 1.00 79.57  ? 953  TRP   E CH2 1 
ATOM   16099 N  N   . MET   E 2 650 ? 26.948  -19.823 -20.050 1.00 80.39  ? 954  MET   E N   1 
ATOM   16100 C  CA  . MET   E 2 650 ? 26.456  -18.442 -20.158 1.00 80.55  ? 954  MET   E CA  1 
ATOM   16101 C  C   . MET   E 2 650 ? 27.569  -17.533 -20.660 1.00 80.15  ? 954  MET   E C   1 
ATOM   16102 O  O   . MET   E 2 650 ? 28.574  -17.345 -19.968 1.00 82.18  ? 954  MET   E O   1 
ATOM   16103 C  CB  . MET   E 2 650 ? 25.944  -17.911 -18.814 1.00 80.20  ? 954  MET   E CB  1 
ATOM   16104 C  CG  . MET   E 2 650 ? 25.394  -16.509 -18.902 1.00 75.61  ? 954  MET   E CG  1 
ATOM   16105 S  SD  . MET   E 2 650 ? 24.989  -15.867 -17.265 1.00 80.58  ? 954  MET   E SD  1 
ATOM   16106 C  CE  . MET   E 2 650 ? 26.608  -15.904 -16.487 1.00 84.64  ? 954  MET   E CE  1 
ATOM   16107 N  N   . SER   E 2 651 ? 27.371  -16.927 -21.830 1.00 82.10  ? 955  SER   E N   1 
ATOM   16108 C  CA  . SER   E 2 651 ? 28.454  -16.249 -22.539 1.00 80.58  ? 955  SER   E CA  1 
ATOM   16109 C  C   . SER   E 2 651 ? 28.479  -14.738 -22.350 1.00 77.76  ? 955  SER   E C   1 
ATOM   16110 O  O   . SER   E 2 651 ? 29.477  -14.108 -22.719 1.00 77.53  ? 955  SER   E O   1 
ATOM   16111 C  CB  . SER   E 2 651 ? 28.377  -16.551 -24.046 1.00 81.89  ? 955  SER   E CB  1 
ATOM   16112 O  OG  . SER   E 2 651 ? 27.151  -16.103 -24.607 1.00 82.90  ? 955  SER   E OG  1 
ATOM   16113 N  N   . ALA   E 2 652 ? 27.414  -14.147 -21.821 1.00 75.18  ? 956  ALA   E N   1 
ATOM   16114 C  CA  . ALA   E 2 652 ? 27.345  -12.701 -21.688 1.00 74.60  ? 956  ALA   E CA  1 
ATOM   16115 C  C   . ALA   E 2 652 ? 26.074  -12.345 -20.941 1.00 72.22  ? 956  ALA   E C   1 
ATOM   16116 O  O   . ALA   E 2 652 ? 25.051  -12.991 -21.137 1.00 74.39  ? 956  ALA   E O   1 
ATOM   16117 C  CB  . ALA   E 2 652 ? 27.351  -12.024 -23.061 1.00 79.37  ? 956  ALA   E CB  1 
ATOM   16118 N  N   . VAL   E 2 653 ? 26.154  -11.308 -20.105 1.00 74.93  ? 957  VAL   E N   1 
ATOM   16119 C  CA  . VAL   E 2 653 ? 25.060  -10.904 -19.219 1.00 79.53  ? 957  VAL   E CA  1 
ATOM   16120 C  C   . VAL   E 2 653 ? 25.042  -9.380  -19.113 1.00 76.74  ? 957  VAL   E C   1 
ATOM   16121 O  O   . VAL   E 2 653 ? 26.023  -8.705  -19.427 1.00 76.61  ? 957  VAL   E O   1 
ATOM   16122 C  CB  . VAL   E 2 653 ? 25.182  -11.544 -17.809 1.00 77.75  ? 957  VAL   E CB  1 
ATOM   16123 C  CG1 . VAL   E 2 653 ? 26.238  -10.807 -16.941 1.00 75.82  ? 957  VAL   E CG1 1 
ATOM   16124 C  CG2 . VAL   E 2 653 ? 23.826  -11.583 -17.132 1.00 74.10  ? 957  VAL   E CG2 1 
ATOM   16125 N  N   . GLU   E 2 654 ? 23.910  -8.849  -18.644 1.00 74.42  ? 958  GLU   E N   1 
ATOM   16126 C  CA  . GLU   E 2 654 ? 23.669  -7.409  -18.623 1.00 80.97  ? 958  GLU   E CA  1 
ATOM   16127 C  C   . GLU   E 2 654 ? 22.475  -7.108  -17.720 1.00 80.66  ? 958  GLU   E C   1 
ATOM   16128 O  O   . GLU   E 2 654 ? 21.502  -7.868  -17.704 1.00 79.79  ? 958  GLU   E O   1 
ATOM   16129 C  CB  . GLU   E 2 654 ? 23.413  -6.896  -20.056 1.00 86.28  ? 958  GLU   E CB  1 
ATOM   16130 C  CG  . GLU   E 2 654 ? 23.110  -5.400  -20.217 1.00 82.44  ? 958  GLU   E CG  1 
ATOM   16131 C  CD  . GLU   E 2 654 ? 24.287  -4.533  -19.882 1.00 83.63  ? 958  GLU   E CD  1 
ATOM   16132 O  OE1 . GLU   E 2 654 ? 25.090  -4.251  -20.799 1.00 85.03  ? 958  GLU   E OE1 1 
ATOM   16133 O  OE2 . GLU   E 2 654 ? 24.414  -4.145  -18.698 1.00 81.51  ? 958  GLU   E OE2 1 
ATOM   16134 N  N   . ILE   E 2 655 ? 22.557  -6.005  -16.972 1.00 82.89  ? 959  ILE   E N   1 
ATOM   16135 C  CA  . ILE   E 2 655 ? 21.427  -5.532  -16.172 1.00 87.40  ? 959  ILE   E CA  1 
ATOM   16136 C  C   . ILE   E 2 655 ? 20.463  -4.808  -17.101 1.00 85.72  ? 959  ILE   E C   1 
ATOM   16137 O  O   . ILE   E 2 655 ? 20.890  -4.007  -17.940 1.00 82.85  ? 959  ILE   E O   1 
ATOM   16138 C  CB  . ILE   E 2 655 ? 21.898  -4.611  -15.025 1.00 88.36  ? 959  ILE   E CB  1 
ATOM   16139 C  CG1 . ILE   E 2 655 ? 23.014  -5.266  -14.196 1.00 85.74  ? 959  ILE   E CG1 1 
ATOM   16140 C  CG2 . ILE   E 2 655 ? 20.737  -4.218  -14.124 1.00 84.96  ? 959  ILE   E CG2 1 
ATOM   16141 C  CD1 . ILE   E 2 655 ? 23.548  -4.380  -13.131 1.00 83.09  ? 959  ILE   E CD1 1 
ATOM   16142 N  N   . LEU   E 2 656 ? 19.165  -5.114  -16.984 1.00 88.57  ? 960  LEU   E N   1 
ATOM   16143 C  CA  . LEU   E 2 656 ? 18.140  -4.442  -17.783 1.00 89.23  ? 960  LEU   E CA  1 
ATOM   16144 C  C   . LEU   E 2 656 ? 17.563  -3.242  -17.046 1.00 96.72  ? 960  LEU   E C   1 
ATOM   16145 O  O   . LEU   E 2 656 ? 17.378  -2.165  -17.627 1.00 94.44  ? 960  LEU   E O   1 
ATOM   16146 C  CB  . LEU   E 2 656 ? 17.007  -5.409  -18.136 1.00 85.94  ? 960  LEU   E CB  1 
ATOM   16147 C  CG  . LEU   E 2 656 ? 17.176  -6.286  -19.364 1.00 83.63  ? 960  LEU   E CG  1 
ATOM   16148 C  CD1 . LEU   E 2 656 ? 16.000  -7.232  -19.513 1.00 84.98  ? 960  LEU   E CD1 1 
ATOM   16149 C  CD2 . LEU   E 2 656 ? 17.366  -5.423  -20.601 1.00 83.01  ? 960  LEU   E CD2 1 
ATOM   16150 N  N   . ASP   E 2 657 ? 17.229  -3.458  -15.778 1.00 103.38 ? 961  ASP   E N   1 
ATOM   16151 C  CA  . ASP   E 2 657 ? 16.747  -2.451  -14.845 1.00 103.22 ? 961  ASP   E CA  1 
ATOM   16152 C  C   . ASP   E 2 657 ? 16.911  -3.058  -13.457 1.00 105.77 ? 961  ASP   E C   1 
ATOM   16153 O  O   . ASP   E 2 657 ? 17.396  -4.180  -13.314 1.00 105.65 ? 961  ASP   E O   1 
ATOM   16154 C  CB  . ASP   E 2 657 ? 15.297  -2.040  -15.140 1.00 103.62 ? 961  ASP   E CB  1 
ATOM   16155 C  CG  . ASP   E 2 657 ? 14.260  -3.088  -14.698 1.00 108.61 ? 961  ASP   E CG  1 
ATOM   16156 O  OD1 . ASP   E 2 657 ? 14.005  -3.249  -13.479 1.00 112.01 ? 961  ASP   E OD1 1 
ATOM   16157 O  OD2 . ASP   E 2 657 ? 13.659  -3.733  -15.587 1.00 110.48 ? 961  ASP   E OD2 1 
ATOM   16158 N  N   . ASP   E 2 658 ? 16.474  -2.312  -12.437 1.00 111.20 ? 962  ASP   E N   1 
ATOM   16159 C  CA  . ASP   E 2 658 ? 16.661  -2.712  -11.043 1.00 110.91 ? 962  ASP   E CA  1 
ATOM   16160 C  C   . ASP   E 2 658 ? 16.143  -4.120  -10.751 1.00 111.52 ? 962  ASP   E C   1 
ATOM   16161 O  O   . ASP   E 2 658 ? 16.587  -4.754  -9.779  1.00 110.44 ? 962  ASP   E O   1 
ATOM   16162 C  CB  . ASP   E 2 658 ? 15.941  -1.711  -10.133 1.00 115.01 ? 962  ASP   E CB  1 
ATOM   16163 C  CG  . ASP   E 2 658 ? 16.624  -0.371  -10.076 1.00 121.94 ? 962  ASP   E CG  1 
ATOM   16164 O  OD1 . ASP   E 2 658 ? 17.774  -0.309  -9.594  1.00 126.24 ? 962  ASP   E OD1 1 
ATOM   16165 O  OD2 . ASP   E 2 658 ? 16.004  0.623   -10.511 1.00 125.98 ? 962  ASP   E OD2 1 
ATOM   16166 N  N   . ASP   E 2 659 ? 15.186  -4.609  -11.540 1.00 114.04 ? 963  ASP   E N   1 
ATOM   16167 C  CA  . ASP   E 2 659 ? 14.550  -5.883  -11.239 1.00 114.97 ? 963  ASP   E CA  1 
ATOM   16168 C  C   . ASP   E 2 659 ? 14.811  -6.977  -12.264 1.00 112.47 ? 963  ASP   E C   1 
ATOM   16169 O  O   . ASP   E 2 659 ? 14.857  -8.148  -11.892 1.00 115.45 ? 963  ASP   E O   1 
ATOM   16170 C  CB  . ASP   E 2 659 ? 13.035  -5.696  -11.079 1.00 116.61 ? 963  ASP   E CB  1 
ATOM   16171 C  CG  . ASP   E 2 659 ? 12.696  -4.667  -10.032 1.00 119.30 ? 963  ASP   E CG  1 
ATOM   16172 O  OD1 . ASP   E 2 659 ? 12.378  -3.527  -10.429 1.00 118.77 ? 963  ASP   E OD1 1 
ATOM   16173 O  OD2 . ASP   E 2 659 ? 12.787  -4.991  -8.822  1.00 118.44 ? 963  ASP   E OD2 1 
ATOM   16174 N  N   . ASN   E 2 660 ? 14.984  -6.648  -13.534 1.00 104.20 ? 964  ASN   E N   1 
ATOM   16175 C  CA  . ASN   E 2 660 ? 15.162  -7.662  -14.559 1.00 97.60  ? 964  ASN   E CA  1 
ATOM   16176 C  C   . ASN   E 2 660 ? 16.592  -7.624  -15.080 1.00 95.83  ? 964  ASN   E C   1 
ATOM   16177 O  O   . ASN   E 2 660 ? 17.168  -6.546  -15.268 1.00 96.66  ? 964  ASN   E O   1 
ATOM   16178 C  CB  . ASN   E 2 660 ? 14.159  -7.459  -15.692 1.00 95.95  ? 964  ASN   E CB  1 
ATOM   16179 C  CG  . ASN   E 2 660 ? 12.753  -7.276  -15.178 1.00 100.99 ? 964  ASN   E CG  1 
ATOM   16180 O  OD1 . ASN   E 2 660 ? 12.092  -8.231  -14.797 1.00 104.42 ? 964  ASN   E OD1 1 
ATOM   16181 N  ND2 . ASN   E 2 660 ? 12.291  -6.045  -15.150 1.00 107.70 ? 964  ASN   E ND2 1 
ATOM   16182 N  N   . PHE   E 2 661 ? 17.167  -8.810  -15.292 1.00 92.56  ? 965  PHE   E N   1 
ATOM   16183 C  CA  . PHE   E 2 661 ? 18.531  -8.967  -15.786 1.00 88.98  ? 965  PHE   E CA  1 
ATOM   16184 C  C   . PHE   E 2 661 ? 18.524  -9.896  -16.990 1.00 86.57  ? 965  PHE   E C   1 
ATOM   16185 O  O   . PHE   E 2 661 ? 17.864  -10.937 -16.961 1.00 90.12  ? 965  PHE   E O   1 
ATOM   16186 C  CB  . PHE   E 2 661 ? 19.454  -9.540  -14.708 1.00 88.44  ? 965  PHE   E CB  1 
ATOM   16187 C  CG  . PHE   E 2 661 ? 19.241  -8.939  -13.373 1.00 90.93  ? 965  PHE   E CG  1 
ATOM   16188 C  CD1 . PHE   E 2 661 ? 19.928  -7.804  -13.000 1.00 88.51  ? 965  PHE   E CD1 1 
ATOM   16189 C  CD2 . PHE   E 2 661 ? 18.323  -9.485  -12.499 1.00 94.02  ? 965  PHE   E CD2 1 
ATOM   16190 C  CE1 . PHE   E 2 661 ? 19.720  -7.239  -11.772 1.00 90.84  ? 965  PHE   E CE1 1 
ATOM   16191 C  CE2 . PHE   E 2 661 ? 18.110  -8.918  -11.271 1.00 95.53  ? 965  PHE   E CE2 1 
ATOM   16192 C  CZ  . PHE   E 2 661 ? 18.808  -7.796  -10.910 1.00 93.43  ? 965  PHE   E CZ  1 
ATOM   16193 N  N   . LEU   E 2 662 ? 19.250  -9.519  -18.050 1.00 82.79  ? 966  LEU   E N   1 
ATOM   16194 C  CA  . LEU   E 2 662 ? 19.271  -10.256 -19.309 1.00 80.14  ? 966  LEU   E CA  1 
ATOM   16195 C  C   . LEU   E 2 662 ? 20.623  -10.935 -19.488 1.00 80.96  ? 966  LEU   E C   1 
ATOM   16196 O  O   . LEU   E 2 662 ? 21.668  -10.328 -19.225 1.00 80.98  ? 966  LEU   E O   1 
ATOM   16197 C  CB  . LEU   E 2 662 ? 18.989  -9.343  -20.514 1.00 80.45  ? 966  LEU   E CB  1 
ATOM   16198 C  CG  . LEU   E 2 662 ? 19.065  -9.921  -21.942 1.00 76.28  ? 966  LEU   E CG  1 
ATOM   16199 C  CD1 . LEU   E 2 662 ? 17.987  -10.964 -22.186 1.00 81.07  ? 966  LEU   E CD1 1 
ATOM   16200 C  CD2 . LEU   E 2 662 ? 19.004  -8.846  -23.014 1.00 72.40  ? 966  LEU   E CD2 1 
ATOM   16201 N  N   . GLY   E 2 663 ? 20.587  -12.184 -19.968 1.00 80.82  ? 967  GLY   E N   1 
ATOM   16202 C  CA  . GLY   E 2 663 ? 21.794  -12.965 -20.177 1.00 78.49  ? 967  GLY   E CA  1 
ATOM   16203 C  C   . GLY   E 2 663 ? 21.642  -13.920 -21.343 1.00 80.15  ? 967  GLY   E C   1 
ATOM   16204 O  O   . GLY   E 2 663 ? 20.532  -14.168 -21.834 1.00 80.55  ? 967  GLY   E O   1 
ATOM   16205 N  N   . ALA   E 2 664 ? 22.785  -14.464 -21.778 1.00 79.36  ? 968  ALA   E N   1 
ATOM   16206 C  CA  . ALA   E 2 664 ? 22.880  -15.333 -22.949 1.00 76.09  ? 968  ALA   E CA  1 
ATOM   16207 C  C   . ALA   E 2 664 ? 23.433  -16.679 -22.515 1.00 80.37  ? 968  ALA   E C   1 
ATOM   16208 O  O   . ALA   E 2 664 ? 24.539  -16.742 -21.965 1.00 80.82  ? 968  ALA   E O   1 
ATOM   16209 C  CB  . ALA   E 2 664 ? 23.786  -14.717 -24.018 1.00 73.61  ? 968  ALA   E CB  1 
ATOM   16210 N  N   . GLU   E 2 665 ? 22.678  -17.746 -22.805 1.00 80.21  ? 969  GLU   E N   1 
ATOM   16211 C  CA  . GLU   E 2 665 ? 23.095  -19.076 -22.292 1.00 81.74  ? 969  GLU   E CA  1 
ATOM   16212 C  C   . GLU   E 2 665 ? 23.048  -20.188 -23.358 1.00 84.52  ? 969  GLU   E C   1 
ATOM   16213 O  O   . GLU   E 2 665 ? 22.104  -20.187 -24.178 1.00 86.04  ? 969  GLU   E O   1 
ATOM   16214 C  CB  . GLU   E 2 665 ? 22.227  -19.424 -21.080 1.00 84.85  ? 969  GLU   E CB  1 
ATOM   16215 C  CG  . GLU   E 2 665 ? 20.733  -19.485 -21.386 1.00 88.10  ? 969  GLU   E CG  1 
ATOM   16216 C  CD  . GLU   E 2 665 ? 19.899  -20.019 -20.236 1.00 95.50  ? 969  GLU   E CD  1 
ATOM   16217 O  OE1 . GLU   E 2 665 ? 20.331  -20.993 -19.590 1.00 95.50  ? 969  GLU   E OE1 1 
ATOM   16218 O  OE2 . GLU   E 2 665 ? 18.810  -19.467 -19.984 1.00 96.14  ? 969  GLU   E OE2 1 
ATOM   16219 N  N   . ASN   E 2 666 ? 24.046  -21.080 -23.358 1.00 86.07  ? 970  ASN   E N   1 
ATOM   16220 C  CA  . ASN   E 2 666 ? 24.091  -22.274 -24.256 1.00 87.00  ? 970  ASN   E CA  1 
ATOM   16221 C  C   . ASN   E 2 666 ? 23.753  -22.141 -25.743 1.00 87.23  ? 970  ASN   E C   1 
ATOM   16222 O  O   . ASN   E 2 666 ? 24.442  -21.373 -26.451 1.00 90.14  ? 970  ASN   E O   1 
ATOM   16223 C  CB  . ASN   E 2 666 ? 23.260  -23.428 -23.709 1.00 88.21  ? 970  ASN   E CB  1 
ATOM   16224 C  CG  . ASN   E 2 666 ? 23.943  -24.760 -23.906 1.00 91.41  ? 970  ASN   E CG  1 
ATOM   16225 O  OD1 . ASN   E 2 666 ? 23.331  -25.705 -24.417 1.00 92.18  ? 970  ASN   E OD1 1 
ATOM   16226 N  ND2 . ASN   E 2 666 ? 25.204  -24.854 -23.513 1.00 96.74  ? 970  ASN   E ND2 1 
ATOM   16227 N  N   . ALA   E 2 667 ? 22.743  -22.894 -26.194 1.00 85.95  ? 971  ALA   E N   1 
ATOM   16228 C  CA  . ALA   E 2 667 ? 22.403  -22.966 -27.636 1.00 85.76  ? 971  ALA   E CA  1 
ATOM   16229 C  C   . ALA   E 2 667 ? 21.663  -21.691 -28.033 1.00 88.13  ? 971  ALA   E C   1 
ATOM   16230 O  O   . ALA   E 2 667 ? 20.417  -21.719 -28.026 1.00 87.00  ? 971  ALA   E O   1 
ATOM   16231 C  CB  . ALA   E 2 667 ? 21.558  -24.190 -27.928 1.00 82.15  ? 971  ALA   E CB  1 
ATOM   16232 N  N   . PHE   E 2 668 ? 22.396  -20.633 -28.389 1.00 86.72  ? 972  PHE   E N   1 
ATOM   16233 C  CA  . PHE   E 2 668 ? 21.743  -19.418 -28.942 1.00 78.88  ? 972  PHE   E CA  1 
ATOM   16234 C  C   . PHE   E 2 668 ? 20.438  -19.135 -28.224 1.00 79.03  ? 972  PHE   E C   1 
ATOM   16235 O  O   . PHE   E 2 668 ? 19.379  -19.090 -28.888 1.00 80.90  ? 972  PHE   E O   1 
ATOM   16236 C  CB  . PHE   E 2 668 ? 21.601  -19.835 -30.405 1.00 78.82  ? 972  PHE   E CB  1 
ATOM   16237 C  CG  . PHE   E 2 668 ? 22.805  -20.588 -30.957 1.00 83.52  ? 972  PHE   E CG  1 
ATOM   16238 C  CD1 . PHE   E 2 668 ? 24.022  -19.945 -31.148 1.00 85.30  ? 972  PHE   E CD1 1 
ATOM   16239 C  CD2 . PHE   E 2 668 ? 22.721  -21.941 -31.267 1.00 79.85  ? 972  PHE   E CD2 1 
ATOM   16240 C  CE1 . PHE   E 2 668 ? 25.119  -20.634 -31.638 1.00 82.60  ? 972  PHE   E CE1 1 
ATOM   16241 C  CE2 . PHE   E 2 668 ? 23.824  -22.627 -31.749 1.00 80.63  ? 972  PHE   E CE2 1 
ATOM   16242 C  CZ  . PHE   E 2 668 ? 25.018  -21.971 -31.938 1.00 80.00  ? 972  PHE   E CZ  1 
ATOM   16243 N  N   . ASN   E 2 669 ? 20.508  -18.918 -26.911 1.00 82.56  ? 973  ASN   E N   1 
ATOM   16244 C  CA  . ASN   E 2 669 ? 19.321  -18.679 -26.097 1.00 80.70  ? 973  ASN   E CA  1 
ATOM   16245 C  C   . ASN   E 2 669 ? 19.504  -17.450 -25.217 1.00 81.24  ? 973  ASN   E C   1 
ATOM   16246 O  O   . ASN   E 2 669 ? 20.595  -17.204 -24.694 1.00 81.90  ? 973  ASN   E O   1 
ATOM   16247 C  CB  . ASN   E 2 669 ? 19.012  -19.885 -25.202 1.00 81.21  ? 973  ASN   E CB  1 
ATOM   16248 C  CG  . ASN   E 2 669 ? 18.363  -21.008 -25.951 1.00 84.27  ? 973  ASN   E CG  1 
ATOM   16249 O  OD1 . ASN   E 2 669 ? 17.703  -20.777 -26.951 1.00 83.65  ? 973  ASN   E OD1 1 
ATOM   16250 N  ND2 . ASN   E 2 669 ? 18.547  -22.231 -25.481 1.00 89.11  ? 973  ASN   E ND2 1 
ATOM   16251 N  N   . LEU   E 2 670 ? 18.435  -16.683 -25.046 1.00 80.35  ? 974  LEU   E N   1 
ATOM   16252 C  CA  . LEU   E 2 670 ? 18.420  -15.563 -24.120 1.00 79.66  ? 974  LEU   E CA  1 
ATOM   16253 C  C   . LEU   E 2 670 ? 17.538  -15.901 -22.932 1.00 83.48  ? 974  LEU   E C   1 
ATOM   16254 O  O   . LEU   E 2 670 ? 16.630  -16.735 -23.022 1.00 82.88  ? 974  LEU   E O   1 
ATOM   16255 C  CB  . LEU   E 2 670 ? 17.882  -14.284 -24.759 1.00 77.00  ? 974  LEU   E CB  1 
ATOM   16256 C  CG  . LEU   E 2 670 ? 18.587  -13.577 -25.888 1.00 73.44  ? 974  LEU   E CG  1 
ATOM   16257 C  CD1 . LEU   E 2 670 ? 17.779  -12.333 -26.178 1.00 73.41  ? 974  LEU   E CD1 1 
ATOM   16258 C  CD2 . LEU   E 2 670 ? 19.972  -13.244 -25.441 1.00 73.12  ? 974  LEU   E CD2 1 
ATOM   16259 N  N   . PHE   E 2 671 ? 17.790  -15.208 -21.822 1.00 86.68  ? 975  PHE   E N   1 
ATOM   16260 C  CA  . PHE   E 2 671 ? 16.980  -15.383 -20.628 1.00 85.14  ? 975  PHE   E CA  1 
ATOM   16261 C  C   . PHE   E 2 671 ? 16.971  -14.088 -19.844 1.00 80.40  ? 975  PHE   E C   1 
ATOM   16262 O  O   . PHE   E 2 671 ? 17.947  -13.337 -19.856 1.00 79.37  ? 975  PHE   E O   1 
ATOM   16263 C  CB  . PHE   E 2 671 ? 17.496  -16.521 -19.739 1.00 85.68  ? 975  PHE   E CB  1 
ATOM   16264 C  CG  . PHE   E 2 671 ? 18.798  -16.211 -19.060 1.00 85.91  ? 975  PHE   E CG  1 
ATOM   16265 C  CD1 . PHE   E 2 671 ? 18.822  -15.585 -17.830 1.00 89.01  ? 975  PHE   E CD1 1 
ATOM   16266 C  CD2 . PHE   E 2 671 ? 20.005  -16.536 -19.659 1.00 87.28  ? 975  PHE   E CD2 1 
ATOM   16267 C  CE1 . PHE   E 2 671 ? 20.020  -15.294 -17.205 1.00 90.18  ? 975  PHE   E CE1 1 
ATOM   16268 C  CE2 . PHE   E 2 671 ? 21.207  -16.251 -19.043 1.00 87.68  ? 975  PHE   E CE2 1 
ATOM   16269 C  CZ  . PHE   E 2 671 ? 21.214  -15.628 -17.811 1.00 89.59  ? 975  PHE   E CZ  1 
ATOM   16270 N  N   . VAL   E 2 672 ? 15.863  -13.848 -19.155 1.00 82.50  ? 976  VAL   E N   1 
ATOM   16271 C  CA  . VAL   E 2 672 ? 15.719  -12.742 -18.215 1.00 86.51  ? 976  VAL   E CA  1 
ATOM   16272 C  C   . VAL   E 2 672 ? 15.204  -13.310 -16.908 1.00 91.39  ? 976  VAL   E C   1 
ATOM   16273 O  O   . VAL   E 2 672 ? 14.321  -14.175 -16.910 1.00 96.74  ? 976  VAL   E O   1 
ATOM   16274 C  CB  . VAL   E 2 672 ? 14.752  -11.651 -18.725 1.00 88.03  ? 976  VAL   E CB  1 
ATOM   16275 C  CG1 . VAL   E 2 672 ? 14.556  -10.579 -17.661 1.00 90.25  ? 976  VAL   E CG1 1 
ATOM   16276 C  CG2 . VAL   E 2 672 ? 15.234  -11.042 -20.048 1.00 87.29  ? 976  VAL   E CG2 1 
ATOM   16277 N  N   . CYS   E 2 673 ? 15.750  -12.823 -15.791 1.00 91.85  ? 977  CYS   E N   1 
ATOM   16278 C  CA  . CYS   E 2 673 ? 15.312  -13.225 -14.464 1.00 97.83  ? 977  CYS   E CA  1 
ATOM   16279 C  C   . CYS   E 2 673 ? 15.143  -11.987 -13.598 1.00 98.45  ? 977  CYS   E C   1 
ATOM   16280 O  O   . CYS   E 2 673 ? 15.835  -10.980 -13.781 1.00 98.34  ? 977  CYS   E O   1 
ATOM   16281 C  CB  . CYS   E 2 673 ? 16.292  -14.192 -13.816 1.00 100.11 ? 977  CYS   E CB  1 
ATOM   16282 S  SG  . CYS   E 2 673 ? 17.948  -13.528 -13.818 1.00 99.94  ? 977  CYS   E SG  1 
ATOM   16283 N  N   . GLN   E 2 674 ? 14.220  -12.081 -12.649 1.00 102.69 ? 978  GLN   E N   1 
ATOM   16284 C  CA  . GLN   E 2 674 ? 13.662  -10.910 -12.010 1.00 106.96 ? 978  GLN   E CA  1 
ATOM   16285 C  C   . GLN   E 2 674 ? 13.760  -11.025 -10.497 1.00 115.12 ? 978  GLN   E C   1 
ATOM   16286 O  O   . GLN   E 2 674 ? 13.751  -12.121 -9.939  1.00 117.53 ? 978  GLN   E O   1 
ATOM   16287 C  CB  . GLN   E 2 674 ? 12.223  -10.724 -12.452 1.00 105.24 ? 978  GLN   E CB  1 
ATOM   16288 C  CG  . GLN   E 2 674 ? 11.571  -9.516  -11.902 1.00 109.93 ? 978  GLN   E CG  1 
ATOM   16289 C  CD  . GLN   E 2 674 ? 10.199  -9.852  -11.420 1.00 117.05 ? 978  GLN   E CD  1 
ATOM   16290 O  OE1 . GLN   E 2 674 ? 9.583   -10.791 -11.916 1.00 106.86 ? 978  GLN   E OE1 1 
ATOM   16291 N  NE2 . GLN   E 2 674 ? 9.708   -9.107  -10.434 1.00 130.94 ? 978  GLN   E NE2 1 
ATOM   16292 N  N   . LYS   E 2 675 ? 13.867  -9.873  -9.837  1.00 119.86 ? 979  LYS   E N   1 
ATOM   16293 C  CA  . LYS   E 2 675 ? 13.991  -9.820  -8.387  1.00 126.93 ? 979  LYS   E CA  1 
ATOM   16294 C  C   . LYS   E 2 675 ? 12.595  -9.951  -7.780  1.00 140.18 ? 979  LYS   E C   1 
ATOM   16295 O  O   . LYS   E 2 675 ? 11.811  -8.998  -7.812  1.00 142.27 ? 979  LYS   E O   1 
ATOM   16296 C  CB  . LYS   E 2 675 ? 14.659  -8.514  -7.961  1.00 123.03 ? 979  LYS   E CB  1 
ATOM   16297 N  N   . ASP   E 2 676 ? 12.274  -11.128 -7.232  1.00 162.51 ? 980  ASP   E N   1 
ATOM   16298 C  CA  . ASP   E 2 676 ? 10.971  -11.366 -6.615  1.00 167.62 ? 980  ASP   E CA  1 
ATOM   16299 C  C   . ASP   E 2 676 ? 11.080  -10.381 -5.455  1.00 175.93 ? 980  ASP   E C   1 
ATOM   16300 O  O   . ASP   E 2 676 ? 11.787  -10.612 -4.474  1.00 181.49 ? 980  ASP   E O   1 
ATOM   16301 C  CB  . ASP   E 2 676 ? 10.803  -12.837 -6.226  1.00 168.52 ? 980  ASP   E CB  1 
ATOM   16302 N  N   . SER   E 2 677 ? 10.360  -9.247  -5.573  1.00 161.38 ? 981  SER   E N   1 
ATOM   16303 C  CA  . SER   E 2 677 ? 10.470  -8.143  -4.612  1.00 167.76 ? 981  SER   E CA  1 
ATOM   16304 C  C   . SER   E 2 677 ? 9.529   -8.516  -3.465  1.00 172.33 ? 981  SER   E C   1 
ATOM   16305 O  O   . SER   E 2 677 ? 9.730   -8.080  -2.318  1.00 169.22 ? 981  SER   E O   1 
ATOM   16306 C  CB  . SER   E 2 677 ? 10.065  -6.792  -5.206  1.00 166.32 ? 981  SER   E CB  1 
ATOM   16307 O  OG  . SER   E 2 677 ? 8.687   -6.787  -5.560  1.00 171.38 ? 981  SER   E OG  1 
ATOM   16308 N  N   . ALA   E 2 678 ? 8.487   -9.303  -3.756  1.00 173.80 ? 982  ALA   E N   1 
ATOM   16309 C  CA  . ALA   E 2 678 ? 7.579   -9.803  -2.730  1.00 169.15 ? 982  ALA   E CA  1 
ATOM   16310 C  C   . ALA   E 2 678 ? 8.463   -10.519 -1.718  1.00 169.43 ? 982  ALA   E C   1 
ATOM   16311 O  O   . ALA   E 2 678 ? 9.071   -11.544 -2.040  1.00 169.76 ? 982  ALA   E O   1 
ATOM   16312 C  CB  . ALA   E 2 678 ? 6.495   -10.697 -3.343  1.00 164.68 ? 982  ALA   E CB  1 
ATOM   16313 N  N   . ALA   E 2 679 ? 8.561   -9.972  -0.491  1.00 172.60 ? 983  ALA   E N   1 
ATOM   16314 C  CA  . ALA   E 2 679 ? 9.397   -10.589 0.546   1.00 172.14 ? 983  ALA   E CA  1 
ATOM   16315 C  C   . ALA   E 2 679 ? 8.436   -11.469 1.370   1.00 172.13 ? 983  ALA   E C   1 
ATOM   16316 O  O   . ALA   E 2 679 ? 8.681   -11.554 2.577   1.00 169.80 ? 983  ALA   E O   1 
ATOM   16317 C  CB  . ALA   E 2 679 ? 9.965   -9.551  1.520   1.00 163.26 ? 983  ALA   E CB  1 
ATOM   16318 N  N   . THR   E 2 680 ? 7.405   -12.005 0.694   1.00 170.70 ? 984  THR   E N   1 
ATOM   16319 C  CA  . THR   E 2 680 ? 6.493   -13.032 1.237   1.00 171.83 ? 984  THR   E CA  1 
ATOM   16320 C  C   . THR   E 2 680 ? 7.075   -14.191 1.911   1.00 176.35 ? 984  THR   E C   1 
ATOM   16321 O  O   . THR   E 2 680 ? 6.748   -14.501 3.061   1.00 178.62 ? 984  THR   E O   1 
ATOM   16322 C  CB  . THR   E 2 680 ? 5.743   -13.606 0.012   1.00 168.87 ? 984  THR   E CB  1 
ATOM   16323 O  OG1 . THR   E 2 680 ? 5.043   -12.590 -0.710  1.00 165.12 ? 984  THR   E OG1 1 
ATOM   16324 C  CG2 . THR   E 2 680 ? 4.765   -14.692 0.448   1.00 167.09 ? 984  THR   E CG2 1 
ATOM   16325 N  N   . THR   E 2 681 ? 8.076   -14.774 1.202   1.00 177.81 ? 985  THR   E N   1 
ATOM   16326 C  CA  . THR   E 2 681 ? 9.132   -15.683 1.782   1.00 179.60 ? 985  THR   E CA  1 
ATOM   16327 C  C   . THR   E 2 681 ? 10.427  -14.950 1.527   1.00 179.37 ? 985  THR   E C   1 
ATOM   16328 O  O   . THR   E 2 681 ? 10.749  -14.606 0.387   1.00 175.57 ? 985  THR   E O   1 
ATOM   16329 C  CB  . THR   E 2 681 ? 9.094   -17.022 1.116   1.00 178.60 ? 985  THR   E CB  1 
ATOM   16330 O  OG1 . THR   E 2 681 ? 7.743   -17.410 0.838   1.00 179.89 ? 985  THR   E OG1 1 
ATOM   16331 C  CG2 . THR   E 2 681 ? 9.720   -18.047 2.046   1.00 175.91 ? 985  THR   E CG2 1 
ATOM   16332 N  N   . ASP   E 2 682 ? 11.182  -14.719 2.605   1.00 189.90 ? 986  ASP   E N   1 
ATOM   16333 C  CA  . ASP   E 2 682 ? 12.567  -14.288 2.445   1.00 187.53 ? 986  ASP   E CA  1 
ATOM   16334 C  C   . ASP   E 2 682 ? 13.300  -15.203 1.461   1.00 186.50 ? 986  ASP   E C   1 
ATOM   16335 O  O   . ASP   E 2 682 ? 14.194  -14.746 0.735   1.00 185.03 ? 986  ASP   E O   1 
ATOM   16336 C  CB  . ASP   E 2 682 ? 13.267  -14.253 3.797   1.00 186.56 ? 986  ASP   E CB  1 
ATOM   16337 C  CG  . ASP   E 2 682 ? 14.621  -13.579 3.735   1.00 188.91 ? 986  ASP   E CG  1 
ATOM   16338 O  OD1 . ASP   E 2 682 ? 15.604  -14.240 3.318   1.00 190.23 ? 986  ASP   E OD1 1 
ATOM   16339 O  OD2 . ASP   E 2 682 ? 14.689  -12.382 4.094   1.00 187.17 ? 986  ASP   E OD2 1 
ATOM   16340 N  N   . GLU   E 2 683 ? 12.897  -16.476 1.393   1.00 187.41 ? 987  GLU   E N   1 
ATOM   16341 C  CA  . GLU   E 2 683 ? 13.410  -17.379 0.372   1.00 175.75 ? 987  GLU   E CA  1 
ATOM   16342 C  C   . GLU   E 2 683 ? 13.151  -16.831 -1.025  1.00 172.49 ? 987  GLU   E C   1 
ATOM   16343 O  O   . GLU   E 2 683 ? 14.041  -16.849 -1.883  1.00 165.42 ? 987  GLU   E O   1 
ATOM   16344 C  CB  . GLU   E 2 683 ? 12.768  -18.759 0.546   1.00 166.45 ? 987  GLU   E CB  1 
ATOM   16345 N  N   . GLU   E 2 684 ? 11.941  -16.319 -1.267  1.00 184.67 ? 988  GLU   E N   1 
ATOM   16346 C  CA  . GLU   E 2 684 ? 11.621  -15.761 -2.583  1.00 181.43 ? 988  GLU   E CA  1 
ATOM   16347 C  C   . GLU   E 2 684 ? 12.415  -14.480 -2.860  1.00 177.91 ? 988  GLU   E C   1 
ATOM   16348 O  O   . GLU   E 2 684 ? 12.884  -14.266 -3.988  1.00 173.07 ? 988  GLU   E O   1 
ATOM   16349 C  CB  . GLU   E 2 684 ? 10.116  -15.499 -2.698  1.00 181.63 ? 988  GLU   E CB  1 
ATOM   16350 N  N   . ARG   E 2 685 ? 12.566  -13.613 -1.847  1.00 169.09 ? 989  ARG   E N   1 
ATOM   16351 C  CA  . ARG   E 2 685 ? 13.321  -12.374 -2.030  1.00 158.68 ? 989  ARG   E CA  1 
ATOM   16352 C  C   . ARG   E 2 685 ? 14.763  -12.657 -2.459  1.00 147.91 ? 989  ARG   E C   1 
ATOM   16353 O  O   . ARG   E 2 685 ? 15.287  -11.995 -3.361  1.00 142.83 ? 989  ARG   E O   1 
ATOM   16354 C  CB  . ARG   E 2 685 ? 13.273  -11.547 -0.740  1.00 154.61 ? 989  ARG   E CB  1 
ATOM   16355 N  N   . GLN   E 2 686 ? 15.414  -13.649 -1.847  1.00 141.11 ? 990  GLN   E N   1 
ATOM   16356 C  CA  . GLN   E 2 686 ? 16.782  -14.022 -2.195  1.00 132.28 ? 990  GLN   E CA  1 
ATOM   16357 C  C   . GLN   E 2 686 ? 16.847  -15.067 -3.311  1.00 129.69 ? 990  GLN   E C   1 
ATOM   16358 O  O   . GLN   E 2 686 ? 17.744  -15.925 -3.312  1.00 124.72 ? 990  GLN   E O   1 
ATOM   16359 C  CB  . GLN   E 2 686 ? 17.535  -14.521 -0.958  1.00 138.06 ? 990  GLN   E CB  1 
ATOM   16360 N  N   . HIS   E 2 687 ? 15.905  -15.037 -4.244  1.00 129.51 ? 991  HIS   E N   1 
ATOM   16361 C  CA  . HIS   E 2 687 ? 15.961  -15.886 -5.428  1.00 122.76 ? 991  HIS   E CA  1 
ATOM   16362 C  C   . HIS   E 2 687 ? 15.489  -15.075 -6.622  1.00 118.24 ? 991  HIS   E C   1 
ATOM   16363 O  O   . HIS   E 2 687 ? 14.469  -14.376 -6.548  1.00 119.87 ? 991  HIS   E O   1 
ATOM   16364 C  CB  . HIS   E 2 687 ? 15.112  -17.157 -5.284  1.00 125.81 ? 991  HIS   E CB  1 
ATOM   16365 C  CG  . HIS   E 2 687 ? 14.763  -17.807 -6.596  1.00 123.73 ? 991  HIS   E CG  1 
ATOM   16366 N  ND1 . HIS   E 2 687 ? 15.656  -18.570 -7.319  1.00 119.82 ? 991  HIS   E ND1 1 
ATOM   16367 C  CD2 . HIS   E 2 687 ? 13.612  -17.800 -7.316  1.00 121.57 ? 991  HIS   E CD2 1 
ATOM   16368 C  CE1 . HIS   E 2 687 ? 15.070  -19.010 -8.421  1.00 116.20 ? 991  HIS   E CE1 1 
ATOM   16369 N  NE2 . HIS   E 2 687 ? 13.830  -18.555 -8.445  1.00 116.70 ? 991  HIS   E NE2 1 
ATOM   16370 N  N   . LEU   E 2 688 ? 16.248  -15.167 -7.703  1.00 114.28 ? 992  LEU   E N   1 
ATOM   16371 C  CA  . LEU   E 2 688 ? 15.928  -14.505 -8.958  1.00 114.15 ? 992  LEU   E CA  1 
ATOM   16372 C  C   . LEU   E 2 688 ? 15.102  -15.465 -9.810  1.00 115.51 ? 992  LEU   E C   1 
ATOM   16373 O  O   . LEU   E 2 688 ? 15.627  -16.449 -10.342 1.00 116.08 ? 992  LEU   E O   1 
ATOM   16374 C  CB  . LEU   E 2 688 ? 17.214  -14.084 -9.655  1.00 110.13 ? 992  LEU   E CB  1 
ATOM   16375 C  CG  . LEU   E 2 688 ? 18.046  -13.148 -8.797  1.00 108.94 ? 992  LEU   E CG  1 
ATOM   16376 C  CD1 . LEU   E 2 688 ? 19.493  -13.153 -9.244  1.00 105.88 ? 992  LEU   E CD1 1 
ATOM   16377 C  CD2 . LEU   E 2 688 ? 17.425  -11.777 -8.931  1.00 107.54 ? 992  LEU   E CD2 1 
ATOM   16378 N  N   . GLN   E 2 689 ? 13.799  -15.198 -9.919  1.00 115.34 ? 993  GLN   E N   1 
ATOM   16379 C  CA  . GLN   E 2 689 ? 12.911  -16.041 -10.706 1.00 113.42 ? 993  GLN   E CA  1 
ATOM   16380 C  C   . GLN   E 2 689 ? 13.087  -15.712 -12.180 1.00 109.78 ? 993  GLN   E C   1 
ATOM   16381 O  O   . GLN   E 2 689 ? 13.024  -14.545 -12.573 1.00 107.11 ? 993  GLN   E O   1 
ATOM   16382 C  CB  . GLN   E 2 689 ? 11.454  -15.837 -10.277 1.00 108.32 ? 993  GLN   E CB  1 
ATOM   16383 N  N   . GLU   E 2 690 ? 13.334  -16.734 -12.995 1.00 114.36 ? 994  GLU   E N   1 
ATOM   16384 C  CA  . GLU   E 2 690 ? 13.360  -16.549 -14.437 1.00 111.58 ? 994  GLU   E CA  1 
ATOM   16385 C  C   . GLU   E 2 690 ? 11.968  -16.167 -14.913 1.00 112.75 ? 994  GLU   E C   1 
ATOM   16386 O  O   . GLU   E 2 690 ? 10.968  -16.660 -14.391 1.00 114.87 ? 994  GLU   E O   1 
ATOM   16387 C  CB  . GLU   E 2 690 ? 13.822  -17.829 -15.120 1.00 116.48 ? 994  GLU   E CB  1 
ATOM   16388 C  CG  . GLU   E 2 690 ? 14.662  -18.710 -14.208 1.00 121.93 ? 994  GLU   E CG  1 
ATOM   16389 C  CD  . GLU   E 2 690 ? 15.045  -20.042 -14.851 1.00 126.29 ? 994  GLU   E CD  1 
ATOM   16390 O  OE1 . GLU   E 2 690 ? 14.310  -20.522 -15.756 1.00 123.93 ? 994  GLU   E OE1 1 
ATOM   16391 O  OE2 . GLU   E 2 690 ? 16.097  -20.601 -14.448 1.00 125.04 ? 994  GLU   E OE2 1 
ATOM   16392 N  N   . VAL   E 2 691 ? 11.902  -15.268 -15.897 1.00 102.61 ? 995  VAL   E N   1 
ATOM   16393 C  CA  . VAL   E 2 691 ? 10.627  -14.765 -16.398 1.00 104.67 ? 995  VAL   E CA  1 
ATOM   16394 C  C   . VAL   E 2 691 ? 10.716  -14.548 -17.907 1.00 97.21  ? 995  VAL   E C   1 
ATOM   16395 O  O   . VAL   E 2 691 ? 9.847   -13.899 -18.505 1.00 100.55 ? 995  VAL   E O   1 
ATOM   16396 C  CB  . VAL   E 2 691 ? 10.188  -13.472 -15.671 1.00 106.88 ? 995  VAL   E CB  1 
ATOM   16397 C  CG1 . VAL   E 2 691 ? 9.669   -13.779 -14.269 1.00 103.92 ? 995  VAL   E CG1 1 
ATOM   16398 C  CG2 . VAL   E 2 691 ? 11.308  -12.418 -15.617 1.00 97.52  ? 995  VAL   E CG2 1 
ATOM   16399 N  N   . GLY   E 2 692 ? 11.754  -15.094 -18.541 1.00 90.53  ? 996  GLY   E N   1 
ATOM   16400 C  CA  . GLY   E 2 692 ? 11.881  -14.931 -19.980 1.00 91.44  ? 996  GLY   E CA  1 
ATOM   16401 C  C   . GLY   E 2 692 ? 12.846  -15.874 -20.677 1.00 90.02  ? 996  GLY   E C   1 
ATOM   16402 O  O   . GLY   E 2 692 ? 14.044  -15.873 -20.389 1.00 87.13  ? 996  GLY   E O   1 
ATOM   16403 N  N   . LEU   E 2 693 ? 12.333  -16.667 -21.612 1.00 89.44  ? 997  LEU   E N   1 
ATOM   16404 C  CA  . LEU   E 2 693 ? 13.133  -17.586 -22.397 1.00 86.58  ? 997  LEU   E CA  1 
ATOM   16405 C  C   . LEU   E 2 693 ? 12.921  -17.314 -23.877 1.00 86.14  ? 997  LEU   E C   1 
ATOM   16406 O  O   . LEU   E 2 693 ? 11.816  -16.968 -24.302 1.00 89.21  ? 997  LEU   E O   1 
ATOM   16407 C  CB  . LEU   E 2 693 ? 12.780  -19.021 -22.068 1.00 85.80  ? 997  LEU   E CB  1 
ATOM   16408 C  CG  . LEU   E 2 693 ? 13.403  -19.484 -20.760 1.00 84.58  ? 997  LEU   E CG  1 
ATOM   16409 C  CD1 . LEU   E 2 693 ? 13.476  -20.998 -20.726 1.00 89.87  ? 997  LEU   E CD1 1 
ATOM   16410 C  CD2 . LEU   E 2 693 ? 14.784  -18.896 -20.596 1.00 83.80  ? 997  LEU   E CD2 1 
ATOM   16411 N  N   . PHE   E 2 694 ? 13.986  -17.475 -24.656 1.00 82.37  ? 998  PHE   E N   1 
ATOM   16412 C  CA  . PHE   E 2 694 ? 13.930  -17.161 -26.076 1.00 82.08  ? 998  PHE   E CA  1 
ATOM   16413 C  C   . PHE   E 2 694 ? 15.168  -17.723 -26.762 1.00 80.72  ? 998  PHE   E C   1 
ATOM   16414 O  O   . PHE   E 2 694 ? 16.287  -17.545 -26.276 1.00 78.82  ? 998  PHE   E O   1 
ATOM   16415 C  CB  . PHE   E 2 694 ? 13.843  -15.650 -26.285 1.00 84.11  ? 998  PHE   E CB  1 
ATOM   16416 C  CG  . PHE   E 2 694 ? 13.688  -15.229 -27.712 1.00 78.36  ? 998  PHE   E CG  1 
ATOM   16417 C  CD1 . PHE   E 2 694 ? 12.453  -15.248 -28.308 1.00 83.44  ? 998  PHE   E CD1 1 
ATOM   16418 C  CD2 . PHE   E 2 694 ? 14.766  -14.772 -28.436 1.00 77.99  ? 998  PHE   E CD2 1 
ATOM   16419 C  CE1 . PHE   E 2 694 ? 12.282  -14.840 -29.616 1.00 86.09  ? 998  PHE   E CE1 1 
ATOM   16420 C  CE2 . PHE   E 2 694 ? 14.609  -14.367 -29.743 1.00 83.15  ? 998  PHE   E CE2 1 
ATOM   16421 C  CZ  . PHE   E 2 694 ? 13.357  -14.398 -30.336 1.00 86.04  ? 998  PHE   E CZ  1 
ATOM   16422 N  N   . HIS   E 2 695 ? 14.941  -18.417 -27.867 1.00 80.27  ? 999  HIS   E N   1 
ATOM   16423 C  CA  . HIS   E 2 695 ? 16.014  -18.933 -28.698 1.00 75.84  ? 999  HIS   E CA  1 
ATOM   16424 C  C   . HIS   E 2 695 ? 16.311  -17.828 -29.702 1.00 79.91  ? 999  HIS   E C   1 
ATOM   16425 O  O   . HIS   E 2 695 ? 15.550  -17.605 -30.642 1.00 79.21  ? 999  HIS   E O   1 
ATOM   16426 C  CB  . HIS   E 2 695 ? 15.574  -20.241 -29.343 1.00 79.08  ? 999  HIS   E CB  1 
ATOM   16427 C  CG  . HIS   E 2 695 ? 16.649  -20.930 -30.119 1.00 82.41  ? 999  HIS   E CG  1 
ATOM   16428 N  ND1 . HIS   E 2 695 ? 17.576  -21.757 -29.530 1.00 83.64  ? 999  HIS   E ND1 1 
ATOM   16429 C  CD2 . HIS   E 2 695 ? 16.945  -20.913 -31.442 1.00 83.13  ? 999  HIS   E CD2 1 
ATOM   16430 C  CE1 . HIS   E 2 695 ? 18.399  -22.218 -30.454 1.00 82.80  ? 999  HIS   E CE1 1 
ATOM   16431 N  NE2 . HIS   E 2 695 ? 18.041  -21.719 -31.623 1.00 78.96  ? 999  HIS   E NE2 1 
ATOM   16432 N  N   . LEU   E 2 696 ? 17.390  -17.078 -29.469 1.00 80.47  ? 1000 LEU   E N   1 
ATOM   16433 C  CA  . LEU   E 2 696 ? 17.784  -16.050 -30.429 1.00 76.16  ? 1000 LEU   E CA  1 
ATOM   16434 C  C   . LEU   E 2 696 ? 18.248  -16.682 -31.731 1.00 74.85  ? 1000 LEU   E C   1 
ATOM   16435 O  O   . LEU   E 2 696 ? 17.918  -16.195 -32.815 1.00 78.56  ? 1000 LEU   E O   1 
ATOM   16436 C  CB  . LEU   E 2 696 ? 18.872  -15.153 -29.838 1.00 74.22  ? 1000 LEU   E CB  1 
ATOM   16437 C  CG  . LEU   E 2 696 ? 19.299  -13.893 -30.604 1.00 73.98  ? 1000 LEU   E CG  1 
ATOM   16438 C  CD1 . LEU   E 2 696 ? 18.278  -12.816 -30.403 1.00 73.94  ? 1000 LEU   E CD1 1 
ATOM   16439 C  CD2 . LEU   E 2 696 ? 20.671  -13.390 -30.213 1.00 73.63  ? 1000 LEU   E CD2 1 
ATOM   16440 N  N   . GLY   E 2 697 ? 18.963  -17.799 -31.640 1.00 77.83  ? 1001 GLY   E N   1 
ATOM   16441 C  CA  . GLY   E 2 697 ? 19.592  -18.444 -32.773 1.00 79.62  ? 1001 GLY   E CA  1 
ATOM   16442 C  C   . GLY   E 2 697 ? 21.044  -18.055 -32.963 1.00 82.69  ? 1001 GLY   E C   1 
ATOM   16443 O  O   . GLY   E 2 697 ? 21.716  -18.627 -33.829 1.00 85.79  ? 1001 GLY   E O   1 
ATOM   16444 N  N   . GLU   E 2 698 ? 21.552  -17.120 -32.157 1.00 78.40  ? 1002 GLU   E N   1 
ATOM   16445 C  CA  . GLU   E 2 698 ? 22.851  -16.505 -32.351 1.00 78.06  ? 1002 GLU   E CA  1 
ATOM   16446 C  C   . GLU   E 2 698 ? 23.591  -16.512 -31.023 1.00 76.96  ? 1002 GLU   E C   1 
ATOM   16447 O  O   . GLU   E 2 698 ? 22.972  -16.495 -29.960 1.00 75.76  ? 1002 GLU   E O   1 
ATOM   16448 C  CB  . GLU   E 2 698 ? 22.673  -15.073 -32.875 1.00 79.65  ? 1002 GLU   E CB  1 
ATOM   16449 C  CG  . GLU   E 2 698 ? 23.764  -14.566 -33.758 1.00 84.72  ? 1002 GLU   E CG  1 
ATOM   16450 C  CD  . GLU   E 2 698 ? 23.936  -15.387 -35.000 1.00 87.28  ? 1002 GLU   E CD  1 
ATOM   16451 O  OE1 . GLU   E 2 698 ? 23.030  -15.356 -35.875 1.00 79.50  ? 1002 GLU   E OE1 1 
ATOM   16452 O  OE2 . GLU   E 2 698 ? 24.986  -16.071 -35.081 1.00 91.44  ? 1002 GLU   E OE2 1 
ATOM   16453 N  N   . PHE   E 2 699 ? 24.917  -16.534 -31.075 1.00 75.89  ? 1003 PHE   E N   1 
ATOM   16454 C  CA  . PHE   E 2 699 ? 25.730  -16.696 -29.870 1.00 77.04  ? 1003 PHE   E CA  1 
ATOM   16455 C  C   . PHE   E 2 699 ? 26.225  -15.318 -29.445 1.00 77.07  ? 1003 PHE   E C   1 
ATOM   16456 O  O   . PHE   E 2 699 ? 27.093  -14.739 -30.111 1.00 76.47  ? 1003 PHE   E O   1 
ATOM   16457 C  CB  . PHE   E 2 699 ? 26.874  -17.669 -30.146 1.00 80.87  ? 1003 PHE   E CB  1 
ATOM   16458 C  CG  . PHE   E 2 699 ? 27.832  -17.862 -28.996 1.00 79.75  ? 1003 PHE   E CG  1 
ATOM   16459 C  CD1 . PHE   E 2 699 ? 28.890  -16.975 -28.792 1.00 79.28  ? 1003 PHE   E CD1 1 
ATOM   16460 C  CD2 . PHE   E 2 699 ? 27.713  -18.954 -28.162 1.00 79.76  ? 1003 PHE   E CD2 1 
ATOM   16461 C  CE1 . PHE   E 2 699 ? 29.782  -17.156 -27.763 1.00 75.07  ? 1003 PHE   E CE1 1 
ATOM   16462 C  CE2 . PHE   E 2 699 ? 28.597  -19.136 -27.134 1.00 81.17  ? 1003 PHE   E CE2 1 
ATOM   16463 C  CZ  . PHE   E 2 699 ? 29.634  -18.234 -26.934 1.00 77.08  ? 1003 PHE   E CZ  1 
ATOM   16464 N  N   . VAL   E 2 700 ? 25.673  -14.792 -28.340 1.00 75.93  ? 1004 VAL   E N   1 
ATOM   16465 C  CA  . VAL   E 2 700 ? 25.974  -13.422 -27.917 1.00 74.27  ? 1004 VAL   E CA  1 
ATOM   16466 C  C   . VAL   E 2 700 ? 27.291  -13.393 -27.156 1.00 72.72  ? 1004 VAL   E C   1 
ATOM   16467 O  O   . VAL   E 2 700 ? 27.528  -14.204 -26.253 1.00 73.67  ? 1004 VAL   E O   1 
ATOM   16468 C  CB  . VAL   E 2 700 ? 24.839  -12.831 -27.059 1.00 72.67  ? 1004 VAL   E CB  1 
ATOM   16469 C  CG1 . VAL   E 2 700 ? 25.110  -11.361 -26.807 1.00 73.62  ? 1004 VAL   E CG1 1 
ATOM   16470 C  CG2 . VAL   E 2 700 ? 23.500  -12.971 -27.731 1.00 72.89  ? 1004 VAL   E CG2 1 
ATOM   16471 N  N   . ASN   E 2 701 ? 28.150  -12.438 -27.508 1.00 73.19  ? 1005 ASN   E N   1 
ATOM   16472 C  CA  . ASN   E 2 701 ? 29.391  -12.240 -26.786 1.00 72.37  ? 1005 ASN   E CA  1 
ATOM   16473 C  C   . ASN   E 2 701 ? 29.429  -10.962 -25.977 1.00 75.21  ? 1005 ASN   E C   1 
ATOM   16474 O  O   . ASN   E 2 701 ? 30.189  -10.892 -25.007 1.00 73.18  ? 1005 ASN   E O   1 
ATOM   16475 C  CB  . ASN   E 2 701 ? 30.579  -12.239 -27.745 1.00 72.49  ? 1005 ASN   E CB  1 
ATOM   16476 C  CG  . ASN   E 2 701 ? 31.217  -13.576 -27.840 1.00 76.99  ? 1005 ASN   E CG  1 
ATOM   16477 O  OD1 . ASN   E 2 701 ? 31.545  -14.031 -28.924 1.00 80.80  ? 1005 ASN   E OD1 1 
ATOM   16478 N  ND2 . ASN   E 2 701 ? 31.379  -14.241 -26.701 1.00 78.86  ? 1005 ASN   E ND2 1 
ATOM   16479 N  N   . VAL   E 2 702 ? 28.617  -9.966  -26.337 1.00 75.60  ? 1006 VAL   E N   1 
ATOM   16480 C  CA  . VAL   E 2 702 ? 28.698  -8.635  -25.753 1.00 75.09  ? 1006 VAL   E CA  1 
ATOM   16481 C  C   . VAL   E 2 702 ? 27.312  -8.009  -25.750 1.00 75.56  ? 1006 VAL   E C   1 
ATOM   16482 O  O   . VAL   E 2 702 ? 26.679  -7.902  -26.800 1.00 77.83  ? 1006 VAL   E O   1 
ATOM   16483 C  CB  . VAL   E 2 702 ? 29.726  -7.774  -26.522 1.00 74.86  ? 1006 VAL   E CB  1 
ATOM   16484 C  CG1 . VAL   E 2 702 ? 29.363  -7.624  -27.992 1.00 76.23  ? 1006 VAL   E CG1 1 
ATOM   16485 C  CG2 . VAL   E 2 702 ? 29.914  -6.432  -25.881 1.00 79.49  ? 1006 VAL   E CG2 1 
ATOM   16486 N  N   . PHE   E 2 703 ? 26.806  -7.641  -24.569 1.00 78.55  ? 1007 PHE   E N   1 
ATOM   16487 C  CA  . PHE   E 2 703 ? 25.677  -6.721  -24.436 1.00 79.64  ? 1007 PHE   E CA  1 
ATOM   16488 C  C   . PHE   E 2 703 ? 26.199  -5.343  -24.073 1.00 85.73  ? 1007 PHE   E C   1 
ATOM   16489 O  O   . PHE   E 2 703 ? 27.110  -5.220  -23.241 1.00 90.56  ? 1007 PHE   E O   1 
ATOM   16490 C  CB  . PHE   E 2 703 ? 24.706  -7.113  -23.324 1.00 78.28  ? 1007 PHE   E CB  1 
ATOM   16491 C  CG  . PHE   E 2 703 ? 23.949  -8.361  -23.569 1.00 77.01  ? 1007 PHE   E CG  1 
ATOM   16492 C  CD1 . PHE   E 2 703 ? 22.768  -8.336  -24.284 1.00 76.46  ? 1007 PHE   E CD1 1 
ATOM   16493 C  CD2 . PHE   E 2 703 ? 24.384  -9.564  -23.031 1.00 78.27  ? 1007 PHE   E CD2 1 
ATOM   16494 C  CE1 . PHE   E 2 703 ? 22.046  -9.502  -24.483 1.00 78.95  ? 1007 PHE   E CE1 1 
ATOM   16495 C  CE2 . PHE   E 2 703 ? 23.677  -10.727 -23.228 1.00 76.93  ? 1007 PHE   E CE2 1 
ATOM   16496 C  CZ  . PHE   E 2 703 ? 22.505  -10.700 -23.952 1.00 78.08  ? 1007 PHE   E CZ  1 
ATOM   16497 N  N   . CYS   E 2 704 ? 25.577  -4.308  -24.632 1.00 88.06  ? 1008 CYS   E N   1 
ATOM   16498 C  CA  . CYS   E 2 704 ? 25.834  -2.958  -24.146 1.00 90.56  ? 1008 CYS   E CA  1 
ATOM   16499 C  C   . CYS   E 2 704 ? 24.615  -2.069  -24.391 1.00 87.69  ? 1008 CYS   E C   1 
ATOM   16500 O  O   . CYS   E 2 704 ? 23.938  -2.194  -25.418 1.00 86.37  ? 1008 CYS   E O   1 
ATOM   16501 C  CB  . CYS   E 2 704 ? 27.097  -2.365  -24.791 1.00 87.84  ? 1008 CYS   E CB  1 
ATOM   16502 S  SG  . CYS   E 2 704 ? 26.841  -1.548  -26.350 1.00 87.79  ? 1008 CYS   E SG  1 
ATOM   16503 N  N   . HIS   E 2 705 ? 24.317  -1.207  -23.417 1.00 81.94  ? 1009 HIS   E N   1 
ATOM   16504 C  CA  . HIS   E 2 705 ? 23.245  -0.245  -23.597 1.00 80.99  ? 1009 HIS   E CA  1 
ATOM   16505 C  C   . HIS   E 2 705 ? 23.655  0.814   -24.614 1.00 84.27  ? 1009 HIS   E C   1 
ATOM   16506 O  O   . HIS   E 2 705 ? 24.837  1.134   -24.765 1.00 87.37  ? 1009 HIS   E O   1 
ATOM   16507 C  CB  . HIS   E 2 705 ? 22.896  0.404   -22.269 1.00 81.28  ? 1009 HIS   E CB  1 
ATOM   16508 C  CG  . HIS   E 2 705 ? 22.199  -0.516  -21.324 1.00 83.75  ? 1009 HIS   E CG  1 
ATOM   16509 N  ND1 . HIS   E 2 705 ? 20.823  -0.556  -21.203 1.00 87.88  ? 1009 HIS   E ND1 1 
ATOM   16510 C  CD2 . HIS   E 2 705 ? 22.681  -1.435  -20.455 1.00 84.04  ? 1009 HIS   E CD2 1 
ATOM   16511 C  CE1 . HIS   E 2 705 ? 20.488  -1.463  -20.300 1.00 83.90  ? 1009 HIS   E CE1 1 
ATOM   16512 N  NE2 . HIS   E 2 705 ? 21.597  -2.002  -19.823 1.00 85.67  ? 1009 HIS   E NE2 1 
ATOM   16513 N  N   . GLY   E 2 706 ? 22.673  1.353   -25.314 1.00 86.24  ? 1010 GLY   E N   1 
ATOM   16514 C  CA  . GLY   E 2 706 ? 22.910  2.309   -26.382 1.00 85.33  ? 1010 GLY   E CA  1 
ATOM   16515 C  C   . GLY   E 2 706 ? 21.935  2.090   -27.515 1.00 81.91  ? 1010 GLY   E C   1 
ATOM   16516 O  O   . GLY   E 2 706 ? 21.269  1.061   -27.614 1.00 82.82  ? 1010 GLY   E O   1 
ATOM   16517 N  N   . SER   E 2 707 ? 21.829  3.089   -28.385 1.00 84.44  ? 1011 SER   E N   1 
ATOM   16518 C  CA  . SER   E 2 707 ? 20.983  3.023   -29.565 1.00 92.33  ? 1011 SER   E CA  1 
ATOM   16519 C  C   . SER   E 2 707 ? 21.713  3.725   -30.690 1.00 97.09  ? 1011 SER   E C   1 
ATOM   16520 O  O   . SER   E 2 707 ? 22.524  4.619   -30.453 1.00 103.16 ? 1011 SER   E O   1 
ATOM   16521 C  CB  . SER   E 2 707 ? 19.593  3.673   -29.354 1.00 96.58  ? 1011 SER   E CB  1 
ATOM   16522 O  OG  . SER   E 2 707 ? 18.607  3.206   -30.277 1.00 95.75  ? 1011 SER   E OG  1 
ATOM   16523 N  N   . LEU   E 2 708 ? 21.433  3.308   -31.919 1.00 101.14 ? 1012 LEU   E N   1 
ATOM   16524 C  CA  . LEU   E 2 708 ? 22.038  3.945   -33.080 1.00 108.33 ? 1012 LEU   E CA  1 
ATOM   16525 C  C   . LEU   E 2 708 ? 21.091  4.949   -33.744 1.00 110.89 ? 1012 LEU   E C   1 
ATOM   16526 O  O   . LEU   E 2 708 ? 21.340  5.364   -34.880 1.00 112.99 ? 1012 LEU   E O   1 
ATOM   16527 C  CB  . LEU   E 2 708 ? 22.523  2.881   -34.076 1.00 109.75 ? 1012 LEU   E CB  1 
ATOM   16528 C  CG  . LEU   E 2 708 ? 23.398  1.746   -33.495 1.00 99.99  ? 1012 LEU   E CG  1 
ATOM   16529 C  CD1 . LEU   E 2 708 ? 23.965  0.870   -34.597 1.00 93.60  ? 1012 LEU   E CD1 1 
ATOM   16530 C  CD2 . LEU   E 2 708 ? 24.525  2.289   -32.615 1.00 96.07  ? 1012 LEU   E CD2 1 
ATOM   16531 N  N   . VAL   E 2 709 ? 20.019  5.339   -33.048 1.00 110.32 ? 1013 VAL   E N   1 
ATOM   16532 C  CA  . VAL   E 2 709 ? 19.058  6.335   -33.505 1.00 112.78 ? 1013 VAL   E CA  1 
ATOM   16533 C  C   . VAL   E 2 709 ? 19.018  7.463   -32.474 1.00 118.26 ? 1013 VAL   E C   1 
ATOM   16534 O  O   . VAL   E 2 709 ? 19.546  7.342   -31.370 1.00 120.55 ? 1013 VAL   E O   1 
ATOM   16535 C  CB  . VAL   E 2 709 ? 17.651  5.748   -33.715 1.00 105.97 ? 1013 VAL   E CB  1 
ATOM   16536 C  CG1 . VAL   E 2 709 ? 17.600  4.804   -34.913 1.00 103.98 ? 1013 VAL   E CG1 1 
ATOM   16537 C  CG2 . VAL   E 2 709 ? 17.214  5.022   -32.462 1.00 107.10 ? 1013 VAL   E CG2 1 
ATOM   16538 N  N   . MET   E 2 710 ? 18.341  8.554   -32.835 1.00 117.31 ? 1014 MET   E N   1 
ATOM   16539 C  CA  . MET   E 2 710 ? 18.255  9.731   -31.958 1.00 116.77 ? 1014 MET   E CA  1 
ATOM   16540 C  C   . MET   E 2 710 ? 17.076  9.771   -30.977 1.00 107.54 ? 1014 MET   E C   1 
ATOM   16541 O  O   . MET   E 2 710 ? 17.032  10.624  -30.076 1.00 98.65  ? 1014 MET   E O   1 
ATOM   16542 C  CB  . MET   E 2 710 ? 18.223  10.991  -32.808 1.00 123.42 ? 1014 MET   E CB  1 
ATOM   16543 C  CG  . MET   E 2 710 ? 19.554  11.268  -33.439 1.00 133.33 ? 1014 MET   E CG  1 
ATOM   16544 S  SD  . MET   E 2 710 ? 19.587  12.759  -34.434 1.00 144.00 ? 1014 MET   E SD  1 
ATOM   16545 C  CE  . MET   E 2 710 ? 20.578  12.172  -35.808 1.00 144.16 ? 1014 MET   E CE  1 
ATOM   16546 N  N   . PRO   E 2 719 ? 6.279   3.866   -25.699 1.00 133.96 ? 1023 PRO   E N   1 
ATOM   16547 C  CA  . PRO   E 2 719 ? 6.088   2.564   -26.363 1.00 128.69 ? 1023 PRO   E CA  1 
ATOM   16548 C  C   . PRO   E 2 719 ? 7.087   1.541   -25.833 1.00 125.63 ? 1023 PRO   E C   1 
ATOM   16549 O  O   . PRO   E 2 719 ? 6.807   0.780   -24.896 1.00 119.96 ? 1023 PRO   E O   1 
ATOM   16550 C  CB  . PRO   E 2 719 ? 6.337   2.875   -27.848 1.00 125.65 ? 1023 PRO   E CB  1 
ATOM   16551 C  CG  . PRO   E 2 719 ? 7.203   4.131   -27.844 1.00 129.42 ? 1023 PRO   E CG  1 
ATOM   16552 C  CD  . PRO   E 2 719 ? 6.888   4.890   -26.574 1.00 133.56 ? 1023 PRO   E CD  1 
ATOM   16553 N  N   . THR   E 2 720 ? 8.264   1.550   -26.449 1.00 125.52 ? 1024 THR   E N   1 
ATOM   16554 C  CA  . THR   E 2 720 ? 9.408   0.833   -25.914 1.00 125.16 ? 1024 THR   E CA  1 
ATOM   16555 C  C   . THR   E 2 720 ? 10.026  1.631   -24.776 1.00 123.98 ? 1024 THR   E C   1 
ATOM   16556 O  O   . THR   E 2 720 ? 9.906   2.858   -24.708 1.00 126.07 ? 1024 THR   E O   1 
ATOM   16557 C  CB  . THR   E 2 720 ? 10.471  0.602   -26.995 1.00 126.20 ? 1024 THR   E CB  1 
ATOM   16558 O  OG1 . THR   E 2 720 ? 10.893  1.863   -27.534 1.00 128.89 ? 1024 THR   E OG1 1 
ATOM   16559 C  CG2 . THR   E 2 720 ? 9.948   -0.302  -28.112 1.00 122.39 ? 1024 THR   E CG2 1 
ATOM   16560 N  N   . GLN   E 2 721 ? 10.696  0.915   -23.877 1.00 125.52 ? 1025 GLN   E N   1 
ATOM   16561 C  CA  . GLN   E 2 721 ? 11.505  1.506   -22.817 1.00 125.71 ? 1025 GLN   E CA  1 
ATOM   16562 C  C   . GLN   E 2 721 ? 12.827  0.763   -22.798 1.00 124.40 ? 1025 GLN   E C   1 
ATOM   16563 O  O   . GLN   E 2 721 ? 12.844  -0.463  -22.656 1.00 123.38 ? 1025 GLN   E O   1 
ATOM   16564 C  CB  . GLN   E 2 721 ? 10.819  1.399   -21.452 1.00 129.66 ? 1025 GLN   E CB  1 
ATOM   16565 C  CG  . GLN   E 2 721 ? 9.386   1.909   -21.426 1.00 141.95 ? 1025 GLN   E CG  1 
ATOM   16566 C  CD  . GLN   E 2 721 ? 8.637   1.520   -20.159 1.00 146.25 ? 1025 GLN   E CD  1 
ATOM   16567 O  OE1 . GLN   E 2 721 ? 8.698   0.364   -19.704 1.00 140.82 ? 1025 GLN   E OE1 1 
ATOM   16568 N  NE2 . GLN   E 2 721 ? 7.924   2.489   -19.579 1.00 151.40 ? 1025 GLN   E NE2 1 
ATOM   16569 N  N   . GLY   E 2 722 ? 13.928  1.486   -22.982 1.00 113.86 ? 1026 GLY   E N   1 
ATOM   16570 C  CA  . GLY   E 2 722 ? 15.242  0.875   -22.922 1.00 106.29 ? 1026 GLY   E CA  1 
ATOM   16571 C  C   . GLY   E 2 722 ? 15.804  0.488   -24.285 1.00 98.32  ? 1026 GLY   E C   1 
ATOM   16572 O  O   . GLY   E 2 722 ? 15.116  0.471   -25.308 1.00 100.45 ? 1026 GLY   E O   1 
ATOM   16573 N  N   . SER   E 2 723 ? 17.085  0.140   -24.280 1.00 92.87  ? 1027 SER   E N   1 
ATOM   16574 C  CA  . SER   E 2 723 ? 17.817  -0.090  -25.506 1.00 86.71  ? 1027 SER   E CA  1 
ATOM   16575 C  C   . SER   E 2 723 ? 19.121  -0.812  -25.197 1.00 85.75  ? 1027 SER   E C   1 
ATOM   16576 O  O   . SER   E 2 723 ? 20.118  -0.163  -24.850 1.00 87.07  ? 1027 SER   E O   1 
ATOM   16577 C  CB  . SER   E 2 723 ? 18.082  1.260   -26.194 1.00 86.48  ? 1027 SER   E CB  1 
ATOM   16578 O  OG  . SER   E 2 723 ? 18.585  1.117   -27.501 1.00 83.29  ? 1027 SER   E OG  1 
ATOM   16579 N  N   . VAL   E 2 724 ? 19.154  -2.141  -25.297 1.00 82.50  ? 1028 VAL   E N   1 
ATOM   16580 C  CA  . VAL   E 2 724 ? 20.397  -2.879  -25.117 1.00 78.87  ? 1028 VAL   E CA  1 
ATOM   16581 C  C   . VAL   E 2 724 ? 20.799  -3.478  -26.449 1.00 80.09  ? 1028 VAL   E C   1 
ATOM   16582 O  O   . VAL   E 2 724 ? 20.001  -4.174  -27.095 1.00 81.51  ? 1028 VAL   E O   1 
ATOM   16583 C  CB  . VAL   E 2 724 ? 20.290  -3.979  -24.056 1.00 80.49  ? 1028 VAL   E CB  1 
ATOM   16584 C  CG1 . VAL   E 2 724 ? 21.686  -4.451  -23.694 1.00 82.49  ? 1028 VAL   E CG1 1 
ATOM   16585 C  CG2 . VAL   E 2 724 ? 19.607  -3.460  -22.840 1.00 89.60  ? 1028 VAL   E CG2 1 
ATOM   16586 N  N   . LEU   E 2 725 ? 22.029  -3.220  -26.846 1.00 79.29  ? 1029 LEU   E N   1 
ATOM   16587 C  CA  . LEU   E 2 725 ? 22.570  -3.767  -28.075 1.00 79.89  ? 1029 LEU   E CA  1 
ATOM   16588 C  C   . LEU   E 2 725 ? 23.418  -4.997  -27.768 1.00 80.91  ? 1029 LEU   E C   1 
ATOM   16589 O  O   . LEU   E 2 725 ? 23.977  -5.141  -26.674 1.00 81.18  ? 1029 LEU   E O   1 
ATOM   16590 C  CB  . LEU   E 2 725 ? 23.406  -2.718  -28.823 1.00 77.34  ? 1029 LEU   E CB  1 
ATOM   16591 C  CG  . LEU   E 2 725 ? 22.671  -1.535  -29.462 1.00 73.02  ? 1029 LEU   E CG  1 
ATOM   16592 C  CD1 . LEU   E 2 725 ? 23.679  -0.526  -29.972 1.00 79.54  ? 1029 LEU   E CD1 1 
ATOM   16593 C  CD2 . LEU   E 2 725 ? 21.762  -1.983  -30.569 1.00 73.04  ? 1029 LEU   E CD2 1 
ATOM   16594 N  N   . PHE   E 2 726 ? 23.501  -5.896  -28.752 1.00 78.22  ? 1030 PHE   E N   1 
ATOM   16595 C  CA  . PHE   E 2 726 ? 24.381  -7.038  -28.591 1.00 76.66  ? 1030 PHE   E CA  1 
ATOM   16596 C  C   . PHE   E 2 726 ? 25.020  -7.433  -29.912 1.00 73.68  ? 1030 PHE   E C   1 
ATOM   16597 O  O   . PHE   E 2 726 ? 24.341  -7.515  -30.938 1.00 74.90  ? 1030 PHE   E O   1 
ATOM   16598 C  CB  . PHE   E 2 726 ? 23.646  -8.236  -27.960 1.00 75.36  ? 1030 PHE   E CB  1 
ATOM   16599 C  CG  . PHE   E 2 726 ? 22.441  -8.717  -28.718 1.00 72.64  ? 1030 PHE   E CG  1 
ATOM   16600 C  CD1 . PHE   E 2 726 ? 22.575  -9.558  -29.810 1.00 75.42  ? 1030 PHE   E CD1 1 
ATOM   16601 C  CD2 . PHE   E 2 726 ? 21.168  -8.392  -28.289 1.00 75.15  ? 1030 PHE   E CD2 1 
ATOM   16602 C  CE1 . PHE   E 2 726 ? 21.464  -10.018 -30.495 1.00 76.07  ? 1030 PHE   E CE1 1 
ATOM   16603 C  CE2 . PHE   E 2 726 ? 20.040  -8.860  -28.969 1.00 76.22  ? 1030 PHE   E CE2 1 
ATOM   16604 C  CZ  . PHE   E 2 726 ? 20.192  -9.673  -30.071 1.00 73.58  ? 1030 PHE   E CZ  1 
ATOM   16605 N  N   . GLY   E 2 727 ? 26.345  -7.672  -29.857 1.00 73.33  ? 1031 GLY   E N   1 
ATOM   16606 C  CA  . GLY   E 2 727 ? 27.049  -8.353  -30.924 1.00 74.42  ? 1031 GLY   E CA  1 
ATOM   16607 C  C   . GLY   E 2 727 ? 27.144  -9.858  -30.697 1.00 75.44  ? 1031 GLY   E C   1 
ATOM   16608 O  O   . GLY   E 2 727 ? 26.978  -10.353 -29.581 1.00 74.82  ? 1031 GLY   E O   1 
ATOM   16609 N  N   . THR   E 2 728 ? 27.404  -10.596 -31.780 1.00 77.19  ? 1032 THR   E N   1 
ATOM   16610 C  CA  . THR   E 2 728 ? 27.367  -12.053 -31.754 1.00 77.55  ? 1032 THR   E CA  1 
ATOM   16611 C  C   . THR   E 2 728 ? 28.502  -12.625 -32.604 1.00 82.48  ? 1032 THR   E C   1 
ATOM   16612 O  O   . THR   E 2 728 ? 29.323  -11.901 -33.179 1.00 81.93  ? 1032 THR   E O   1 
ATOM   16613 C  CB  . THR   E 2 728 ? 26.025  -12.597 -32.253 1.00 77.03  ? 1032 THR   E CB  1 
ATOM   16614 O  OG1 . THR   E 2 728 ? 25.913  -12.357 -33.658 1.00 80.98  ? 1032 THR   E OG1 1 
ATOM   16615 C  CG2 . THR   E 2 728 ? 24.833  -11.963 -31.528 1.00 73.19  ? 1032 THR   E CG2 1 
ATOM   16616 N  N   . VAL   E 2 729 ? 28.536  -13.954 -32.700 1.00 84.29  ? 1033 VAL   E N   1 
ATOM   16617 C  CA  . VAL   E 2 729 ? 29.705  -14.582 -33.292 1.00 85.39  ? 1033 VAL   E CA  1 
ATOM   16618 C  C   . VAL   E 2 729 ? 29.592  -14.660 -34.803 1.00 89.97  ? 1033 VAL   E C   1 
ATOM   16619 O  O   . VAL   E 2 729 ? 30.615  -14.633 -35.507 1.00 91.32  ? 1033 VAL   E O   1 
ATOM   16620 C  CB  . VAL   E 2 729 ? 29.923  -15.957 -32.654 1.00 87.31  ? 1033 VAL   E CB  1 
ATOM   16621 C  CG1 . VAL   E 2 729 ? 30.648  -16.898 -33.602 1.00 94.01  ? 1033 VAL   E CG1 1 
ATOM   16622 C  CG2 . VAL   E 2 729 ? 30.739  -15.774 -31.410 1.00 87.97  ? 1033 VAL   E CG2 1 
ATOM   16623 N  N   . ASN   E 2 730 ? 28.371  -14.762 -35.336 1.00 93.78  ? 1034 ASN   E N   1 
ATOM   16624 C  CA  . ASN   E 2 730 ? 28.146  -14.652 -36.769 1.00 94.69  ? 1034 ASN   E CA  1 
ATOM   16625 C  C   . ASN   E 2 730 ? 27.959  -13.210 -37.229 1.00 94.19  ? 1034 ASN   E C   1 
ATOM   16626 O  O   . ASN   E 2 730 ? 27.431  -12.987 -38.327 1.00 94.24  ? 1034 ASN   E O   1 
ATOM   16627 C  CB  . ASN   E 2 730 ? 26.936  -15.485 -37.192 1.00 94.11  ? 1034 ASN   E CB  1 
ATOM   16628 C  CG  . ASN   E 2 730 ? 27.163  -16.979 -37.042 1.00 96.46  ? 1034 ASN   E CG  1 
ATOM   16629 O  OD1 . ASN   E 2 730 ? 27.611  -17.646 -37.982 1.00 99.57  ? 1034 ASN   E OD1 1 
ATOM   16630 N  ND2 . ASN   E 2 730 ? 26.846  -17.519 -35.860 1.00 95.51  ? 1034 ASN   E ND2 1 
ATOM   16631 N  N   . GLY   E 2 731 ? 28.348  -12.223 -36.427 1.00 87.86  ? 1035 GLY   E N   1 
ATOM   16632 C  CA  . GLY   E 2 731 ? 28.257  -10.842 -36.841 1.00 88.49  ? 1035 GLY   E CA  1 
ATOM   16633 C  C   . GLY   E 2 731 ? 26.882  -10.202 -36.757 1.00 89.88  ? 1035 GLY   E C   1 
ATOM   16634 O  O   . GLY   E 2 731 ? 26.782  -8.984  -36.947 1.00 88.22  ? 1035 GLY   E O   1 
ATOM   16635 N  N   . MET   E 2 732 ? 25.819  -10.970 -36.487 1.00 83.87  ? 1036 MET   E N   1 
ATOM   16636 C  CA  . MET   E 2 732 ? 24.490  -10.406 -36.250 1.00 79.04  ? 1036 MET   E CA  1 
ATOM   16637 C  C   . MET   E 2 732 ? 24.509  -9.440  -35.062 1.00 77.85  ? 1036 MET   E C   1 
ATOM   16638 O  O   . MET   E 2 732 ? 25.123  -9.715  -34.031 1.00 80.37  ? 1036 MET   E O   1 
ATOM   16639 C  CB  . MET   E 2 732 ? 23.500  -11.553 -35.996 1.00 80.14  ? 1036 MET   E CB  1 
ATOM   16640 C  CG  . MET   E 2 732 ? 22.024  -11.179 -35.736 1.00 81.43  ? 1036 MET   E CG  1 
ATOM   16641 S  SD  . MET   E 2 732 ? 21.610  -10.668 -34.045 1.00 83.28  ? 1036 MET   E SD  1 
ATOM   16642 C  CE  . MET   E 2 732 ? 19.870  -10.224 -34.163 1.00 79.49  ? 1036 MET   E CE  1 
ATOM   16643 N  N   . ILE   E 2 733 ? 23.845  -8.297  -35.209 1.00 76.68  ? 1037 ILE   E N   1 
ATOM   16644 C  CA  . ILE   E 2 733 ? 23.702  -7.306  -34.145 1.00 73.60  ? 1037 ILE   E CA  1 
ATOM   16645 C  C   . ILE   E 2 733 ? 22.221  -7.178  -33.845 1.00 79.02  ? 1037 ILE   E C   1 
ATOM   16646 O  O   . ILE   E 2 733 ? 21.410  -7.018  -34.763 1.00 84.35  ? 1037 ILE   E O   1 
ATOM   16647 C  CB  . ILE   E 2 733 ? 24.277  -5.938  -34.553 1.00 76.03  ? 1037 ILE   E CB  1 
ATOM   16648 C  CG1 . ILE   E 2 733 ? 25.760  -6.082  -34.929 1.00 79.36  ? 1037 ILE   E CG1 1 
ATOM   16649 C  CG2 . ILE   E 2 733 ? 24.014  -4.908  -33.463 1.00 72.78  ? 1037 ILE   E CG2 1 
ATOM   16650 C  CD1 . ILE   E 2 733 ? 26.352  -4.934  -35.705 1.00 73.18  ? 1037 ILE   E CD1 1 
ATOM   16651 N  N   . GLY   E 2 734 ? 21.855  -7.243  -32.567 1.00 78.83  ? 1038 GLY   E N   1 
ATOM   16652 C  CA  . GLY   E 2 734 ? 20.462  -7.208  -32.182 1.00 79.84  ? 1038 GLY   E CA  1 
ATOM   16653 C  C   . GLY   E 2 734 ? 20.177  -6.122  -31.159 1.00 78.22  ? 1038 GLY   E C   1 
ATOM   16654 O  O   . GLY   E 2 734 ? 21.083  -5.478  -30.624 1.00 75.99  ? 1038 GLY   E O   1 
ATOM   16655 N  N   . LEU   E 2 735 ? 18.891  -5.944  -30.884 1.00 79.15  ? 1039 LEU   E N   1 
ATOM   16656 C  CA  . LEU   E 2 735 ? 18.443  -4.945  -29.931 1.00 79.41  ? 1039 LEU   E CA  1 
ATOM   16657 C  C   . LEU   E 2 735 ? 17.436  -5.572  -28.978 1.00 81.37  ? 1039 LEU   E C   1 
ATOM   16658 O  O   . LEU   E 2 735 ? 16.589  -6.370  -29.398 1.00 83.14  ? 1039 LEU   E O   1 
ATOM   16659 C  CB  . LEU   E 2 735 ? 17.830  -3.749  -30.668 1.00 79.70  ? 1039 LEU   E CB  1 
ATOM   16660 C  CG  . LEU   E 2 735 ? 17.513  -2.464  -29.909 1.00 80.16  ? 1039 LEU   E CG  1 
ATOM   16661 C  CD1 . LEU   E 2 735 ? 18.725  -1.864  -29.227 1.00 79.63  ? 1039 LEU   E CD1 1 
ATOM   16662 C  CD2 . LEU   E 2 735 ? 16.920  -1.463  -30.862 1.00 87.90  ? 1039 LEU   E CD2 1 
ATOM   16663 N  N   . VAL   E 2 736 ? 17.555  -5.248  -27.689 1.00 82.03  ? 1040 VAL   E N   1 
ATOM   16664 C  CA  . VAL   E 2 736 ? 16.537  -5.600  -26.705 1.00 85.83  ? 1040 VAL   E CA  1 
ATOM   16665 C  C   . VAL   E 2 736 ? 16.041  -4.336  -26.025 1.00 93.49  ? 1040 VAL   E C   1 
ATOM   16666 O  O   . VAL   E 2 736 ? 16.839  -3.551  -25.492 1.00 89.60  ? 1040 VAL   E O   1 
ATOM   16667 C  CB  . VAL   E 2 736 ? 17.037  -6.589  -25.646 1.00 80.41  ? 1040 VAL   E CB  1 
ATOM   16668 C  CG1 . VAL   E 2 736 ? 15.859  -7.007  -24.806 1.00 84.12  ? 1040 VAL   E CG1 1 
ATOM   16669 C  CG2 . VAL   E 2 736 ? 17.659  -7.790  -26.298 1.00 84.11  ? 1040 VAL   E CG2 1 
ATOM   16670 N  N   . THR   E 2 737 ? 14.716  -4.162  -26.030 1.00 100.96 ? 1041 THR   E N   1 
ATOM   16671 C  CA  . THR   E 2 737 ? 14.018  -3.103  -25.315 1.00 105.22 ? 1041 THR   E CA  1 
ATOM   16672 C  C   . THR   E 2 737 ? 12.840  -3.709  -24.561 1.00 106.97 ? 1041 THR   E C   1 
ATOM   16673 O  O   . THR   E 2 737 ? 12.310  -4.760  -24.945 1.00 105.26 ? 1041 THR   E O   1 
ATOM   16674 C  CB  . THR   E 2 737 ? 13.509  -2.008  -26.256 1.00 106.87 ? 1041 THR   E CB  1 
ATOM   16675 O  OG1 . THR   E 2 737 ? 12.866  -0.992  -25.482 1.00 110.94 ? 1041 THR   E OG1 1 
ATOM   16676 C  CG2 . THR   E 2 737 ? 12.521  -2.583  -27.272 1.00 105.12 ? 1041 THR   E CG2 1 
ATOM   16677 N  N   . SER   E 2 738 ? 12.435  -3.041  -23.482 1.00 107.07 ? 1042 SER   E N   1 
ATOM   16678 C  CA  . SER   E 2 738 ? 11.390  -3.571  -22.617 1.00 107.25 ? 1042 SER   E CA  1 
ATOM   16679 C  C   . SER   E 2 738 ? 10.037  -3.038  -23.033 1.00 107.83 ? 1042 SER   E C   1 
ATOM   16680 O  O   . SER   E 2 738 ? 9.924   -2.025  -23.719 1.00 112.31 ? 1042 SER   E O   1 
ATOM   16681 C  CB  . SER   E 2 738 ? 11.634  -3.219  -21.151 1.00 111.61 ? 1042 SER   E CB  1 
ATOM   16682 O  OG  . SER   E 2 738 ? 12.802  -3.853  -20.658 1.00 109.92 ? 1042 SER   E OG  1 
ATOM   16683 N  N   . LEU   E 2 739 ? 9.000   -3.739  -22.601 1.00 108.66 ? 1043 LEU   E N   1 
ATOM   16684 C  CA  . LEU   E 2 739 ? 7.626   -3.395  -22.927 1.00 111.09 ? 1043 LEU   E CA  1 
ATOM   16685 C  C   . LEU   E 2 739 ? 6.789   -3.471  -21.659 1.00 112.93 ? 1043 LEU   E C   1 
ATOM   16686 O  O   . LEU   E 2 739 ? 7.271   -3.854  -20.584 1.00 111.97 ? 1043 LEU   E O   1 
ATOM   16687 C  CB  . LEU   E 2 739 ? 7.058   -4.325  -24.003 1.00 105.14 ? 1043 LEU   E CB  1 
ATOM   16688 C  CG  . LEU   E 2 739 ? 8.000   -4.609  -25.166 1.00 105.38 ? 1043 LEU   E CG  1 
ATOM   16689 C  CD1 . LEU   E 2 739 ? 7.413   -5.688  -26.013 1.00 103.75 ? 1043 LEU   E CD1 1 
ATOM   16690 C  CD2 . LEU   E 2 739 ? 8.175   -3.352  -25.985 1.00 110.60 ? 1043 LEU   E CD2 1 
ATOM   16691 N  N   . SER   E 2 740 ? 5.517   -3.125  -21.796 1.00 114.35 ? 1044 SER   E N   1 
ATOM   16692 C  CA  . SER   E 2 740 ? 4.560   -3.219  -20.706 1.00 118.49 ? 1044 SER   E CA  1 
ATOM   16693 C  C   . SER   E 2 740 ? 3.768   -4.523  -20.804 1.00 119.90 ? 1044 SER   E C   1 
ATOM   16694 O  O   . SER   E 2 740 ? 3.795   -5.214  -21.828 1.00 121.30 ? 1044 SER   E O   1 
ATOM   16695 C  CB  . SER   E 2 740 ? 3.609   -2.022  -20.739 1.00 117.26 ? 1044 SER   E CB  1 
ATOM   16696 O  OG  . SER   E 2 740 ? 3.050   -1.908  -22.033 1.00 118.01 ? 1044 SER   E OG  1 
ATOM   16697 N  N   . GLU   E 2 741 ? 3.062   -4.859  -19.715 1.00 117.41 ? 1045 GLU   E N   1 
ATOM   16698 C  CA  . GLU   E 2 741 ? 2.099   -5.956  -19.765 1.00 109.26 ? 1045 GLU   E CA  1 
ATOM   16699 C  C   . GLU   E 2 741 ? 1.113   -5.736  -20.903 1.00 107.95 ? 1045 GLU   E C   1 
ATOM   16700 O  O   . GLU   E 2 741 ? 0.868   -6.636  -21.710 1.00 109.50 ? 1045 GLU   E O   1 
ATOM   16701 C  CB  . GLU   E 2 741 ? 1.365   -6.086  -18.425 1.00 109.42 ? 1045 GLU   E CB  1 
ATOM   16702 C  CG  . GLU   E 2 741 ? 0.322   -7.229  -18.368 1.00 114.09 ? 1045 GLU   E CG  1 
ATOM   16703 C  CD  . GLU   E 2 741 ? 0.892   -8.554  -17.848 1.00 117.41 ? 1045 GLU   E CD  1 
ATOM   16704 O  OE1 . GLU   E 2 741 ? 1.443   -8.564  -16.718 1.00 117.09 ? 1045 GLU   E OE1 1 
ATOM   16705 O  OE2 . GLU   E 2 741 ? 0.794   -9.584  -18.565 1.00 113.30 ? 1045 GLU   E OE2 1 
ATOM   16706 N  N   . SER   E 2 742 ? 0.568   -4.522  -20.999 1.00 109.45 ? 1046 SER   E N   1 
ATOM   16707 C  CA  . SER   E 2 742 ? -0.345  -4.181  -22.086 1.00 113.18 ? 1046 SER   E CA  1 
ATOM   16708 C  C   . SER   E 2 742 ? 0.295   -4.403  -23.451 1.00 112.78 ? 1046 SER   E C   1 
ATOM   16709 O  O   . SER   E 2 742 ? -0.305  -5.025  -24.334 1.00 110.56 ? 1046 SER   E O   1 
ATOM   16710 C  CB  . SER   E 2 742 ? -0.793  -2.727  -21.948 1.00 117.56 ? 1046 SER   E CB  1 
ATOM   16711 O  OG  . SER   E 2 742 ? -1.259  -2.213  -23.192 1.00 119.62 ? 1046 SER   E OG  1 
ATOM   16712 N  N   . TRP   E 2 743 ? 1.514   -3.890  -23.651 1.00 113.59 ? 1047 TRP   E N   1 
ATOM   16713 C  CA  . TRP   E 2 743 ? 2.135   -3.979  -24.974 1.00 114.83 ? 1047 TRP   E CA  1 
ATOM   16714 C  C   . TRP   E 2 743 ? 2.668   -5.377  -25.274 1.00 114.29 ? 1047 TRP   E C   1 
ATOM   16715 O  O   . TRP   E 2 743 ? 2.784   -5.756  -26.447 1.00 115.53 ? 1047 TRP   E O   1 
ATOM   16716 C  CB  . TRP   E 2 743 ? 3.249   -2.939  -25.105 1.00 116.67 ? 1047 TRP   E CB  1 
ATOM   16717 C  CG  . TRP   E 2 743 ? 2.718   -1.619  -25.553 1.00 121.41 ? 1047 TRP   E CG  1 
ATOM   16718 C  CD1 . TRP   E 2 743 ? 1.805   -0.847  -24.903 1.00 124.54 ? 1047 TRP   E CD1 1 
ATOM   16719 C  CD2 . TRP   E 2 743 ? 3.042   -0.922  -26.764 1.00 122.37 ? 1047 TRP   E CD2 1 
ATOM   16720 N  NE1 . TRP   E 2 743 ? 1.544   0.290   -25.627 1.00 126.99 ? 1047 TRP   E NE1 1 
ATOM   16721 C  CE2 . TRP   E 2 743 ? 2.292   0.266   -26.774 1.00 122.99 ? 1047 TRP   E CE2 1 
ATOM   16722 C  CE3 . TRP   E 2 743 ? 3.897   -1.186  -27.836 1.00 127.47 ? 1047 TRP   E CE3 1 
ATOM   16723 C  CZ2 . TRP   E 2 743 ? 2.372   1.187   -27.809 1.00 126.64 ? 1047 TRP   E CZ2 1 
ATOM   16724 C  CZ3 . TRP   E 2 743 ? 3.975   -0.267  -28.869 1.00 123.56 ? 1047 TRP   E CZ3 1 
ATOM   16725 C  CH2 . TRP   E 2 743 ? 3.219   0.902   -28.845 1.00 125.26 ? 1047 TRP   E CH2 1 
ATOM   16726 N  N   . TYR   E 2 744 ? 3.007   -6.151  -24.241 1.00 112.15 ? 1048 TYR   E N   1 
ATOM   16727 C  CA  . TYR   E 2 744 ? 3.450   -7.520  -24.464 1.00 105.74 ? 1048 TYR   E CA  1 
ATOM   16728 C  C   . TYR   E 2 744 ? 2.294   -8.386  -24.915 1.00 104.44 ? 1048 TYR   E C   1 
ATOM   16729 O  O   . TYR   E 2 744 ? 2.423   -9.153  -25.872 1.00 107.68 ? 1048 TYR   E O   1 
ATOM   16730 C  CB  . TYR   E 2 744 ? 4.087   -8.086  -23.200 1.00 104.96 ? 1048 TYR   E CB  1 
ATOM   16731 C  CG  . TYR   E 2 744 ? 4.377   -9.565  -23.240 1.00 102.38 ? 1048 TYR   E CG  1 
ATOM   16732 C  CD1 . TYR   E 2 744 ? 5.460   -10.059 -23.947 1.00 101.45 ? 1048 TYR   E CD1 1 
ATOM   16733 C  CD2 . TYR   E 2 744 ? 3.580   -10.469 -22.540 1.00 105.87 ? 1048 TYR   E CD2 1 
ATOM   16734 C  CE1 . TYR   E 2 744 ? 5.740   -11.427 -23.977 1.00 107.69 ? 1048 TYR   E CE1 1 
ATOM   16735 C  CE2 . TYR   E 2 744 ? 3.848   -11.840 -22.555 1.00 102.56 ? 1048 TYR   E CE2 1 
ATOM   16736 C  CZ  . TYR   E 2 744 ? 4.931   -12.316 -23.275 1.00 106.89 ? 1048 TYR   E CZ  1 
ATOM   16737 O  OH  . TYR   E 2 744 ? 5.212   -13.673 -23.298 1.00 106.18 ? 1048 TYR   E OH  1 
ATOM   16738 N  N   . ASN   E 2 745 ? 1.153   -8.281  -24.224 1.00 105.04 ? 1049 ASN   E N   1 
ATOM   16739 C  CA  . ASN   E 2 745 ? -0.026  -9.065  -24.589 1.00 106.07 ? 1049 ASN   E CA  1 
ATOM   16740 C  C   . ASN   E 2 745 ? -0.499  -8.735  -26.002 1.00 107.39 ? 1049 ASN   E C   1 
ATOM   16741 O  O   . ASN   E 2 745 ? -0.859  -9.638  -26.773 1.00 108.50 ? 1049 ASN   E O   1 
ATOM   16742 C  CB  . ASN   E 2 745 ? -1.158  -8.828  -23.581 1.00 105.37 ? 1049 ASN   E CB  1 
ATOM   16743 C  CG  . ASN   E 2 745 ? -0.844  -9.376  -22.174 1.00 108.29 ? 1049 ASN   E CG  1 
ATOM   16744 O  OD1 . ASN   E 2 745 ? 0.132   -10.113 -21.963 1.00 103.61 ? 1049 ASN   E OD1 1 
ATOM   16745 N  ND2 . ASN   E 2 745 ? -1.696  -9.022  -21.206 1.00 111.91 ? 1049 ASN   E ND2 1 
ATOM   16746 N  N   . LEU   E 2 746 ? -0.518  -7.444  -26.354 1.00 106.00 ? 1050 LEU   E N   1 
ATOM   16747 C  CA  . LEU   E 2 746 ? -0.948  -7.025  -27.685 1.00 103.47 ? 1050 LEU   E CA  1 
ATOM   16748 C  C   . LEU   E 2 746 ? -0.093  -7.667  -28.767 1.00 107.81 ? 1050 LEU   E C   1 
ATOM   16749 O  O   . LEU   E 2 746 ? -0.616  -8.191  -29.757 1.00 113.02 ? 1050 LEU   E O   1 
ATOM   16750 C  CB  . LEU   E 2 746 ? -0.881  -5.506  -27.788 1.00 102.97 ? 1050 LEU   E CB  1 
ATOM   16751 C  CG  . LEU   E 2 746 ? -1.706  -4.836  -28.884 1.00 103.55 ? 1050 LEU   E CG  1 
ATOM   16752 C  CD1 . LEU   E 2 746 ? -0.994  -4.893  -30.224 1.00 99.92  ? 1050 LEU   E CD1 1 
ATOM   16753 C  CD2 . LEU   E 2 746 ? -3.086  -5.486  -28.962 1.00 111.34 ? 1050 LEU   E CD2 1 
ATOM   16754 N  N   . LEU   E 2 747 ? 1.235   -7.616  -28.597 1.00 108.59 ? 1051 LEU   E N   1 
ATOM   16755 C  CA  . LEU   E 2 747 ? 2.156   -8.183  -29.582 1.00 108.51 ? 1051 LEU   E CA  1 
ATOM   16756 C  C   . LEU   E 2 747 ? 2.253   -9.699  -29.462 1.00 108.41 ? 1051 LEU   E C   1 
ATOM   16757 O  O   . LEU   E 2 747 ? 2.625   -10.373 -30.433 1.00 109.92 ? 1051 LEU   E O   1 
ATOM   16758 C  CB  . LEU   E 2 747 ? 3.543   -7.556  -29.435 1.00 105.01 ? 1051 LEU   E CB  1 
ATOM   16759 C  CG  . LEU   E 2 747 ? 3.680   -6.109  -29.897 1.00 98.93  ? 1051 LEU   E CG  1 
ATOM   16760 C  CD1 . LEU   E 2 747 ? 5.101   -5.579  -29.732 1.00 100.32 ? 1051 LEU   E CD1 1 
ATOM   16761 C  CD2 . LEU   E 2 747 ? 3.244   -6.051  -31.336 1.00 99.19  ? 1051 LEU   E CD2 1 
ATOM   16762 N  N   . LEU   E 2 748 ? 1.947   -10.251 -28.287 1.00 107.45 ? 1052 LEU   E N   1 
ATOM   16763 C  CA  . LEU   E 2 748 ? 1.822   -11.698 -28.176 1.00 107.77 ? 1052 LEU   E CA  1 
ATOM   16764 C  C   . LEU   E 2 748 ? 0.642   -12.193 -28.999 1.00 114.65 ? 1052 LEU   E C   1 
ATOM   16765 O  O   . LEU   E 2 748 ? 0.769   -13.157 -29.762 1.00 120.25 ? 1052 LEU   E O   1 
ATOM   16766 C  CB  . LEU   E 2 748 ? 1.678   -12.111 -26.714 1.00 105.83 ? 1052 LEU   E CB  1 
ATOM   16767 C  CG  . LEU   E 2 748 ? 2.488   -13.339 -26.312 1.00 103.55 ? 1052 LEU   E CG  1 
ATOM   16768 C  CD1 . LEU   E 2 748 ? 3.962   -13.095 -26.593 1.00 108.52 ? 1052 LEU   E CD1 1 
ATOM   16769 C  CD2 . LEU   E 2 748 ? 2.252   -13.682 -24.848 1.00 101.66 ? 1052 LEU   E CD2 1 
ATOM   16770 N  N   . ASP   E 2 749 ? -0.517  -11.535 -28.861 1.00 112.16 ? 1053 ASP   E N   1 
ATOM   16771 C  CA  . ASP   E 2 749 ? -1.660  -11.829 -29.725 1.00 114.91 ? 1053 ASP   E CA  1 
ATOM   16772 C  C   . ASP   E 2 749 ? -1.303  -11.601 -31.188 1.00 118.10 ? 1053 ASP   E C   1 
ATOM   16773 O  O   . ASP   E 2 749 ? -1.533  -12.463 -32.046 1.00 122.82 ? 1053 ASP   E O   1 
ATOM   16774 C  CB  . ASP   E 2 749 ? -2.856  -10.960 -29.325 1.00 110.34 ? 1053 ASP   E CB  1 
ATOM   16775 N  N   . MET   E 2 750 ? -0.710  -10.443 -31.478 1.00 116.64 ? 1054 MET   E N   1 
ATOM   16776 C  CA  . MET   E 2 750 ? -0.332  -10.079 -32.840 1.00 114.25 ? 1054 MET   E CA  1 
ATOM   16777 C  C   . MET   E 2 750 ? 0.669   -11.071 -33.451 1.00 118.27 ? 1054 MET   E C   1 
ATOM   16778 O  O   . MET   E 2 750 ? 0.639   -11.322 -34.665 1.00 116.76 ? 1054 MET   E O   1 
ATOM   16779 C  CB  . MET   E 2 750 ? 0.222   -8.655  -32.808 1.00 107.73 ? 1054 MET   E CB  1 
ATOM   16780 C  CG  . MET   E 2 750 ? 0.766   -8.158  -34.094 1.00 116.51 ? 1054 MET   E CG  1 
ATOM   16781 S  SD  . MET   E 2 750 ? -0.502  -7.321  -35.045 1.00 126.30 ? 1054 MET   E SD  1 
ATOM   16782 C  CE  . MET   E 2 750 ? -1.066  -8.612  -36.160 1.00 129.18 ? 1054 MET   E CE  1 
ATOM   16783 N  N   . GLN   E 2 751 ? 1.562   -11.645 -32.633 1.00 122.36 ? 1055 GLN   E N   1 
ATOM   16784 C  CA  . GLN   E 2 751 ? 2.535   -12.608 -33.152 1.00 119.01 ? 1055 GLN   E CA  1 
ATOM   16785 C  C   . GLN   E 2 751 ? 1.848   -13.874 -33.649 1.00 123.31 ? 1055 GLN   E C   1 
ATOM   16786 O  O   . GLN   E 2 751 ? 2.207   -14.405 -34.707 1.00 124.26 ? 1055 GLN   E O   1 
ATOM   16787 C  CB  . GLN   E 2 751 ? 3.572   -12.961 -32.089 1.00 113.10 ? 1055 GLN   E CB  1 
ATOM   16788 C  CG  . GLN   E 2 751 ? 4.913   -12.275 -32.270 1.00 112.93 ? 1055 GLN   E CG  1 
ATOM   16789 C  CD  . GLN   E 2 751 ? 5.939   -12.692 -31.215 1.00 111.75 ? 1055 GLN   E CD  1 
ATOM   16790 O  OE1 . GLN   E 2 751 ? 6.846   -13.466 -31.497 1.00 109.14 ? 1055 GLN   E OE1 1 
ATOM   16791 N  NE2 . GLN   E 2 751 ? 5.802   -12.166 -29.999 1.00 113.20 ? 1055 GLN   E NE2 1 
ATOM   16792 N  N   . ASN   E 2 752 ? 0.870   -14.388 -32.888 1.00 134.14 ? 1056 ASN   E N   1 
ATOM   16793 C  CA  . ASN   E 2 752 ? 0.151   -15.585 -33.321 1.00 134.63 ? 1056 ASN   E CA  1 
ATOM   16794 C  C   . ASN   E 2 752 ? -0.544  -15.343 -34.648 1.00 134.52 ? 1056 ASN   E C   1 
ATOM   16795 O  O   . ASN   E 2 752 ? -0.460  -16.170 -35.564 1.00 134.30 ? 1056 ASN   E O   1 
ATOM   16796 C  CB  . ASN   E 2 752 ? -0.881  -16.019 -32.282 1.00 135.52 ? 1056 ASN   E CB  1 
ATOM   16797 C  CG  . ASN   E 2 752 ? -0.306  -16.122 -30.889 1.00 142.62 ? 1056 ASN   E CG  1 
ATOM   16798 O  OD1 . ASN   E 2 752 ? -0.873  -15.582 -29.933 1.00 146.68 ? 1056 ASN   E OD1 1 
ATOM   16799 N  ND2 . ASN   E 2 752 ? 0.818   -16.823 -30.757 1.00 144.37 ? 1056 ASN   E ND2 1 
ATOM   16800 N  N   . ARG   E 2 753 ? -1.252  -14.212 -34.760 1.00 126.19 ? 1057 ARG   E N   1 
ATOM   16801 C  CA  . ARG   E 2 753 ? -1.953  -13.888 -35.996 1.00 123.97 ? 1057 ARG   E CA  1 
ATOM   16802 C  C   . ARG   E 2 753 ? -0.997  -13.895 -37.181 1.00 124.53 ? 1057 ARG   E C   1 
ATOM   16803 O  O   . ARG   E 2 753 ? -1.302  -14.465 -38.236 1.00 125.43 ? 1057 ARG   E O   1 
ATOM   16804 C  CB  . ARG   E 2 753 ? -2.648  -12.534 -35.863 1.00 123.17 ? 1057 ARG   E CB  1 
ATOM   16805 N  N   . LEU   E 2 754 ? 0.189   -13.310 -37.002 1.00 120.13 ? 1058 LEU   E N   1 
ATOM   16806 C  CA  . LEU   E 2 754 ? 1.173   -13.260 -38.077 1.00 117.44 ? 1058 LEU   E CA  1 
ATOM   16807 C  C   . LEU   E 2 754 ? 1.678   -14.650 -38.454 1.00 119.46 ? 1058 LEU   E C   1 
ATOM   16808 O  O   . LEU   E 2 754 ? 1.798   -14.967 -39.642 1.00 120.39 ? 1058 LEU   E O   1 
ATOM   16809 C  CB  . LEU   E 2 754 ? 2.337   -12.365 -37.676 1.00 114.79 ? 1058 LEU   E CB  1 
ATOM   16810 C  CG  . LEU   E 2 754 ? 2.058   -10.876 -37.725 1.00 116.55 ? 1058 LEU   E CG  1 
ATOM   16811 C  CD1 . LEU   E 2 754 ? 3.321   -10.145 -37.358 1.00 112.54 ? 1058 LEU   E CD1 1 
ATOM   16812 C  CD2 . LEU   E 2 754 ? 1.619   -10.507 -39.128 1.00 122.54 ? 1058 LEU   E CD2 1 
ATOM   16813 N  N   . ASN   E 2 755 ? 2.002   -15.492 -37.457 1.00 121.03 ? 1059 ASN   E N   1 
ATOM   16814 C  CA  . ASN   E 2 755 ? 2.500   -16.839 -37.752 1.00 116.67 ? 1059 ASN   E CA  1 
ATOM   16815 C  C   . ASN   E 2 755 ? 1.541   -17.618 -38.635 1.00 121.77 ? 1059 ASN   E C   1 
ATOM   16816 O  O   . ASN   E 2 755 ? 1.969   -18.410 -39.490 1.00 118.41 ? 1059 ASN   E O   1 
ATOM   16817 C  CB  . ASN   E 2 755 ? 2.735   -17.620 -36.465 1.00 115.91 ? 1059 ASN   E CB  1 
ATOM   16818 C  CG  . ASN   E 2 755 ? 4.093   -17.357 -35.883 1.00 118.54 ? 1059 ASN   E CG  1 
ATOM   16819 O  OD1 . ASN   E 2 755 ? 4.971   -16.830 -36.568 1.00 118.05 ? 1059 ASN   E OD1 1 
ATOM   16820 N  ND2 . ASN   E 2 755 ? 4.286   -17.721 -34.610 1.00 117.06 ? 1059 ASN   E ND2 1 
ATOM   16821 N  N   . LYS   E 2 756 ? 0.241   -17.400 -38.438 1.00 120.72 ? 1060 LYS   E N   1 
ATOM   16822 C  CA  . LYS   E 2 756 ? -0.767  -18.066 -39.240 1.00 116.00 ? 1060 LYS   E CA  1 
ATOM   16823 C  C   . LYS   E 2 756 ? -0.646  -17.708 -40.713 1.00 117.05 ? 1060 LYS   E C   1 
ATOM   16824 O  O   . LYS   E 2 756 ? -0.975  -18.535 -41.572 1.00 118.26 ? 1060 LYS   E O   1 
ATOM   16825 C  CB  . LYS   E 2 756 ? -2.148  -17.708 -38.707 1.00 115.04 ? 1060 LYS   E CB  1 
ATOM   16826 N  N   . VAL   E 2 757 ? -0.132  -16.517 -41.028 1.00 119.13 ? 1061 VAL   E N   1 
ATOM   16827 C  CA  . VAL   E 2 757 ? -0.215  -15.971 -42.376 1.00 117.35 ? 1061 VAL   E CA  1 
ATOM   16828 C  C   . VAL   E 2 757 ? 1.133   -15.889 -43.093 1.00 121.15 ? 1061 VAL   E C   1 
ATOM   16829 O  O   . VAL   E 2 757 ? 1.147   -15.845 -44.335 1.00 120.09 ? 1061 VAL   E O   1 
ATOM   16830 C  CB  . VAL   E 2 757 ? -0.895  -14.587 -42.356 1.00 113.05 ? 1061 VAL   E CB  1 
ATOM   16831 C  CG1 . VAL   E 2 757 ? -2.247  -14.700 -41.681 1.00 120.14 ? 1061 VAL   E CG1 1 
ATOM   16832 C  CG2 . VAL   E 2 757 ? -0.034  -13.562 -41.637 1.00 122.16 ? 1061 VAL   E CG2 1 
ATOM   16833 N  N   . ILE   E 2 758 ? 2.263   -15.879 -42.365 1.00 126.81 ? 1062 ILE   E N   1 
ATOM   16834 C  CA  . ILE   E 2 758 ? 3.599   -15.775 -42.954 1.00 127.33 ? 1062 ILE   E CA  1 
ATOM   16835 C  C   . ILE   E 2 758 ? 4.107   -17.172 -43.283 1.00 126.60 ? 1062 ILE   E C   1 
ATOM   16836 O  O   . ILE   E 2 758 ? 3.903   -18.116 -42.508 1.00 126.16 ? 1062 ILE   E O   1 
ATOM   16837 C  CB  . ILE   E 2 758 ? 4.551   -15.025 -41.997 1.00 127.58 ? 1062 ILE   E CB  1 
ATOM   16838 C  CG1 . ILE   E 2 758 ? 4.174   -13.538 -41.949 1.00 125.76 ? 1062 ILE   E CG1 1 
ATOM   16839 C  CG2 . ILE   E 2 758 ? 6.034   -15.235 -42.372 1.00 128.71 ? 1062 ILE   E CG2 1 
ATOM   16840 C  CD1 . ILE   E 2 758 ? 4.757   -12.791 -40.764 1.00 119.00 ? 1062 ILE   E CD1 1 
ATOM   16841 N  N   . LYS   E 2 759 ? 4.743   -17.319 -44.448 1.00 116.72 ? 1063 LYS   E N   1 
ATOM   16842 C  CA  . LYS   E 2 759 ? 5.254   -18.615 -44.874 1.00 113.97 ? 1063 LYS   E CA  1 
ATOM   16843 C  C   . LYS   E 2 759 ? 6.662   -18.834 -44.326 1.00 117.47 ? 1063 LYS   E C   1 
ATOM   16844 O  O   . LYS   E 2 759 ? 7.460   -17.897 -44.239 1.00 121.99 ? 1063 LYS   E O   1 
ATOM   16845 C  CB  . LYS   E 2 759 ? 5.243   -18.716 -46.400 1.00 104.28 ? 1063 LYS   E CB  1 
ATOM   16846 N  N   . SER   E 2 760 ? 6.947   -20.069 -43.914 1.00 112.25 ? 1064 SER   E N   1 
ATOM   16847 C  CA  . SER   E 2 760 ? 8.256   -20.458 -43.412 1.00 107.45 ? 1064 SER   E CA  1 
ATOM   16848 C  C   . SER   E 2 760 ? 8.920   -21.355 -44.439 1.00 106.57 ? 1064 SER   E C   1 
ATOM   16849 O  O   . SER   E 2 760 ? 8.273   -22.247 -44.997 1.00 107.25 ? 1064 SER   E O   1 
ATOM   16850 C  CB  . SER   E 2 760 ? 8.147   -21.198 -42.077 1.00 107.13 ? 1064 SER   E CB  1 
ATOM   16851 O  OG  . SER   E 2 760 ? 9.388   -21.790 -41.716 1.00 106.15 ? 1064 SER   E OG  1 
ATOM   16852 N  N   . VAL   E 2 761 ? 10.219  -21.131 -44.662 1.00 103.00 ? 1065 VAL   E N   1 
ATOM   16853 C  CA  . VAL   E 2 761 ? 10.901  -21.777 -45.784 1.00 102.37 ? 1065 VAL   E CA  1 
ATOM   16854 C  C   . VAL   E 2 761 ? 10.952  -23.294 -45.606 1.00 102.04 ? 1065 VAL   E C   1 
ATOM   16855 O  O   . VAL   E 2 761 ? 10.835  -24.049 -46.579 1.00 103.53 ? 1065 VAL   E O   1 
ATOM   16856 C  CB  . VAL   E 2 761 ? 12.303  -21.177 -45.980 1.00 98.04  ? 1065 VAL   E CB  1 
ATOM   16857 C  CG1 . VAL   E 2 761 ? 12.970  -21.781 -47.199 1.00 90.29  ? 1065 VAL   E CG1 1 
ATOM   16858 C  CG2 . VAL   E 2 761 ? 12.203  -19.677 -46.117 1.00 100.96 ? 1065 VAL   E CG2 1 
ATOM   16859 N  N   . GLY   E 2 762 ? 11.108  -23.770 -44.382 1.00 98.60  ? 1066 GLY   E N   1 
ATOM   16860 C  CA  . GLY   E 2 762 ? 11.084  -25.215 -44.339 1.00 98.16  ? 1066 GLY   E CA  1 
ATOM   16861 C  C   . GLY   E 2 762 ? 9.802   -25.804 -43.832 1.00 95.01  ? 1066 GLY   E C   1 
ATOM   16862 O  O   . GLY   E 2 762 ? 9.739   -27.018 -43.604 1.00 93.66  ? 1066 GLY   E O   1 
ATOM   16863 N  N   . LYS   E 2 763 ? 8.772   -24.969 -43.665 1.00 95.69  ? 1067 LYS   E N   1 
ATOM   16864 C  CA  . LYS   E 2 763 ? 7.577   -25.310 -42.892 1.00 97.34  ? 1067 LYS   E CA  1 
ATOM   16865 C  C   . LYS   E 2 763 ? 7.973   -25.625 -41.448 1.00 99.15  ? 1067 LYS   E C   1 
ATOM   16866 O  O   . LYS   E 2 763 ? 7.598   -26.659 -40.881 1.00 97.30  ? 1067 LYS   E O   1 
ATOM   16867 C  CB  . LYS   E 2 763 ? 6.783   -26.462 -43.531 1.00 94.60  ? 1067 LYS   E CB  1 
ATOM   16868 C  CG  . LYS   E 2 763 ? 6.118   -26.142 -44.884 1.00 93.65  ? 1067 LYS   E CG  1 
ATOM   16869 C  CD  . LYS   E 2 763 ? 5.402   -27.376 -45.428 1.00 97.89  ? 1067 LYS   E CD  1 
ATOM   16870 C  CE  . LYS   E 2 763 ? 4.677   -27.145 -46.762 1.00 100.99 ? 1067 LYS   E CE  1 
ATOM   16871 N  NZ  . LYS   E 2 763 ? 4.068   -28.412 -47.335 1.00 102.65 ? 1067 LYS   E NZ  1 
ATOM   16872 N  N   . ILE   E 2 764 ? 8.771   -24.725 -40.864 1.00 99.25  ? 1068 ILE   E N   1 
ATOM   16873 C  CA  . ILE   E 2 764 ? 9.181   -24.799 -39.465 1.00 96.22  ? 1068 ILE   E CA  1 
ATOM   16874 C  C   . ILE   E 2 764 ? 8.275   -23.867 -38.683 1.00 97.79  ? 1068 ILE   E C   1 
ATOM   16875 O  O   . ILE   E 2 764 ? 8.223   -22.662 -38.966 1.00 98.67  ? 1068 ILE   E O   1 
ATOM   16876 C  CB  . ILE   E 2 764 ? 10.657  -24.406 -39.278 1.00 92.63  ? 1068 ILE   E CB  1 
ATOM   16877 C  CG1 . ILE   E 2 764 ? 11.511  -24.935 -40.434 1.00 92.54  ? 1068 ILE   E CG1 1 
ATOM   16878 C  CG2 . ILE   E 2 764 ? 11.188  -24.890 -37.924 1.00 89.03  ? 1068 ILE   E CG2 1 
ATOM   16879 C  CD1 . ILE   E 2 764 ? 12.883  -24.270 -40.574 1.00 93.50  ? 1068 ILE   E CD1 1 
ATOM   16880 N  N   . GLU   E 2 765 ? 7.546   -24.410 -37.713 1.00 94.71  ? 1069 GLU   E N   1 
ATOM   16881 C  CA  . GLU   E 2 765 ? 6.703   -23.542 -36.914 1.00 98.18  ? 1069 GLU   E CA  1 
ATOM   16882 C  C   . GLU   E 2 765 ? 7.575   -22.548 -36.171 1.00 100.73 ? 1069 GLU   E C   1 
ATOM   16883 O  O   . GLU   E 2 765 ? 8.612   -22.913 -35.606 1.00 99.33  ? 1069 GLU   E O   1 
ATOM   16884 C  CB  . GLU   E 2 765 ? 5.868   -24.340 -35.937 1.00 99.25  ? 1069 GLU   E CB  1 
ATOM   16885 C  CG  . GLU   E 2 765 ? 5.095   -25.419 -36.590 1.00 102.26 ? 1069 GLU   E CG  1 
ATOM   16886 C  CD  . GLU   E 2 765 ? 4.617   -26.412 -35.569 1.00 118.14 ? 1069 GLU   E CD  1 
ATOM   16887 O  OE1 . GLU   E 2 765 ? 5.401   -26.711 -34.630 1.00 119.52 ? 1069 GLU   E OE1 1 
ATOM   16888 O  OE2 . GLU   E 2 765 ? 3.455   -26.870 -35.680 1.00 125.30 ? 1069 GLU   E OE2 1 
ATOM   16889 N  N   . HIS   E 2 766 ? 7.173   -21.276 -36.222 1.00 102.25 ? 1070 HIS   E N   1 
ATOM   16890 C  CA  . HIS   E 2 766 ? 7.887   -20.238 -35.487 1.00 101.58 ? 1070 HIS   E CA  1 
ATOM   16891 C  C   . HIS   E 2 766 ? 8.029   -20.630 -34.025 1.00 98.91  ? 1070 HIS   E C   1 
ATOM   16892 O  O   . HIS   E 2 766 ? 9.110   -20.531 -33.439 1.00 99.14  ? 1070 HIS   E O   1 
ATOM   16893 C  CB  . HIS   E 2 766 ? 7.141   -18.911 -35.634 1.00 105.91 ? 1070 HIS   E CB  1 
ATOM   16894 C  CG  . HIS   E 2 766 ? 7.698   -17.776 -34.823 1.00 104.33 ? 1070 HIS   E CG  1 
ATOM   16895 N  ND1 . HIS   E 2 766 ? 7.393   -17.590 -33.491 1.00 103.80 ? 1070 HIS   E ND1 1 
ATOM   16896 C  CD2 . HIS   E 2 766 ? 8.483   -16.730 -35.180 1.00 100.05 ? 1070 HIS   E CD2 1 
ATOM   16897 C  CE1 . HIS   E 2 766 ? 7.997   -16.499 -33.055 1.00 101.06 ? 1070 HIS   E CE1 1 
ATOM   16898 N  NE2 . HIS   E 2 766 ? 8.665   -15.959 -34.061 1.00 98.50  ? 1070 HIS   E NE2 1 
ATOM   16899 N  N   . SER   E 2 767 ? 6.945   -21.137 -33.443 1.00 96.61  ? 1071 SER   E N   1 
ATOM   16900 C  CA  . SER   E 2 767 ? 6.947   -21.497 -32.033 1.00 97.75  ? 1071 SER   E CA  1 
ATOM   16901 C  C   . SER   E 2 767 ? 8.017   -22.540 -31.718 1.00 93.69  ? 1071 SER   E C   1 
ATOM   16902 O  O   . SER   E 2 767 ? 8.752   -22.409 -30.733 1.00 90.95  ? 1071 SER   E O   1 
ATOM   16903 C  CB  . SER   E 2 767 ? 5.556   -21.992 -31.665 1.00 105.09 ? 1071 SER   E CB  1 
ATOM   16904 O  OG  . SER   E 2 767 ? 4.600   -21.007 -32.034 1.00 115.09 ? 1071 SER   E OG  1 
ATOM   16905 N  N   . PHE   E 2 768 ? 8.127   -23.574 -32.555 1.00 96.30  ? 1072 PHE   E N   1 
ATOM   16906 C  CA  . PHE   E 2 768 ? 9.196   -24.557 -32.401 1.00 93.35  ? 1072 PHE   E CA  1 
ATOM   16907 C  C   . PHE   E 2 768 ? 10.558  -23.877 -32.420 1.00 89.01  ? 1072 PHE   E C   1 
ATOM   16908 O  O   . PHE   E 2 768 ? 11.434  -24.202 -31.609 1.00 87.41  ? 1072 PHE   E O   1 
ATOM   16909 C  CB  . PHE   E 2 768 ? 9.086   -25.615 -33.511 1.00 92.69  ? 1072 PHE   E CB  1 
ATOM   16910 C  CG  . PHE   E 2 768 ? 10.196  -26.630 -33.513 1.00 86.62  ? 1072 PHE   E CG  1 
ATOM   16911 C  CD1 . PHE   E 2 768 ? 10.054  -27.831 -32.841 1.00 83.32  ? 1072 PHE   E CD1 1 
ATOM   16912 C  CD2 . PHE   E 2 768 ? 11.371  -26.386 -34.201 1.00 86.57  ? 1072 PHE   E CD2 1 
ATOM   16913 C  CE1 . PHE   E 2 768 ? 11.066  -28.762 -32.841 1.00 80.95  ? 1072 PHE   E CE1 1 
ATOM   16914 C  CE2 . PHE   E 2 768 ? 12.384  -27.309 -34.207 1.00 85.12  ? 1072 PHE   E CE2 1 
ATOM   16915 C  CZ  . PHE   E 2 768 ? 12.233  -28.500 -33.525 1.00 84.19  ? 1072 PHE   E CZ  1 
ATOM   16916 N  N   . TRP   E 2 769 ? 10.730  -22.896 -33.316 1.00 91.17  ? 1073 TRP   E N   1 
ATOM   16917 C  CA  . TRP   E 2 769 ? 12.044  -22.298 -33.575 1.00 92.43  ? 1073 TRP   E CA  1 
ATOM   16918 C  C   . TRP   E 2 769 ? 12.524  -21.445 -32.408 1.00 86.97  ? 1073 TRP   E C   1 
ATOM   16919 O  O   . TRP   E 2 769 ? 13.649  -21.624 -31.919 1.00 85.95  ? 1073 TRP   E O   1 
ATOM   16920 C  CB  . TRP   E 2 769 ? 11.980  -21.473 -34.864 1.00 90.85  ? 1073 TRP   E CB  1 
ATOM   16921 C  CG  . TRP   E 2 769 ? 13.008  -20.381 -35.054 1.00 84.71  ? 1073 TRP   E CG  1 
ATOM   16922 C  CD1 . TRP   E 2 769 ? 12.747  -19.082 -35.340 1.00 84.01  ? 1073 TRP   E CD1 1 
ATOM   16923 C  CD2 . TRP   E 2 769 ? 14.444  -20.503 -35.032 1.00 86.35  ? 1073 TRP   E CD2 1 
ATOM   16924 N  NE1 . TRP   E 2 769 ? 13.909  -18.383 -35.485 1.00 85.25  ? 1073 TRP   E NE1 1 
ATOM   16925 C  CE2 . TRP   E 2 769 ? 14.969  -19.227 -35.302 1.00 83.49  ? 1073 TRP   E CE2 1 
ATOM   16926 C  CE3 . TRP   E 2 769 ? 15.335  -21.560 -34.799 1.00 88.40  ? 1073 TRP   E CE3 1 
ATOM   16927 C  CZ2 . TRP   E 2 769 ? 16.346  -18.965 -35.346 1.00 79.92  ? 1073 TRP   E CZ2 1 
ATOM   16928 C  CZ3 . TRP   E 2 769 ? 16.718  -21.290 -34.843 1.00 88.53  ? 1073 TRP   E CZ3 1 
ATOM   16929 C  CH2 . TRP   E 2 769 ? 17.199  -20.002 -35.113 1.00 81.38  ? 1073 TRP   E CH2 1 
ATOM   16930 N  N   . ARG   E 2 770 ? 11.690  -20.510 -31.960 1.00 86.11  ? 1074 ARG   E N   1 
ATOM   16931 C  CA  . ARG   E 2 770 ? 12.027  -19.572 -30.899 1.00 86.50  ? 1074 ARG   E CA  1 
ATOM   16932 C  C   . ARG   E 2 770 ? 11.886  -20.166 -29.497 1.00 87.83  ? 1074 ARG   E C   1 
ATOM   16933 O  O   . ARG   E 2 770 ? 12.210  -19.485 -28.515 1.00 84.45  ? 1074 ARG   E O   1 
ATOM   16934 C  CB  . ARG   E 2 770 ? 11.156  -18.324 -31.033 1.00 88.76  ? 1074 ARG   E CB  1 
ATOM   16935 C  CG  . ARG   E 2 770 ? 11.404  -17.530 -32.298 1.00 88.99  ? 1074 ARG   E CG  1 
ATOM   16936 C  CD  . ARG   E 2 770 ? 12.800  -17.013 -32.293 1.00 85.95  ? 1074 ARG   E CD  1 
ATOM   16937 N  NE  . ARG   E 2 770 ? 13.063  -16.110 -33.399 1.00 87.64  ? 1074 ARG   E NE  1 
ATOM   16938 C  CZ  . ARG   E 2 770 ? 14.252  -15.581 -33.644 1.00 86.57  ? 1074 ARG   E CZ  1 
ATOM   16939 N  NH1 . ARG   E 2 770 ? 15.284  -15.812 -32.850 1.00 80.84  ? 1074 ARG   E NH1 1 
ATOM   16940 N  NH2 . ARG   E 2 770 ? 14.415  -14.816 -34.723 1.00 89.89  ? 1074 ARG   E NH2 1 
ATOM   16941 N  N   . SER   E 2 771 ? 11.409  -21.403 -29.386 1.00 92.69  ? 1075 SER   E N   1 
ATOM   16942 C  CA  . SER   E 2 771 ? 11.356  -22.080 -28.102 1.00 92.93  ? 1075 SER   E CA  1 
ATOM   16943 C  C   . SER   E 2 771 ? 12.764  -22.378 -27.605 1.00 91.29  ? 1075 SER   E C   1 
ATOM   16944 O  O   . SER   E 2 771 ? 13.670  -22.667 -28.387 1.00 90.33  ? 1075 SER   E O   1 
ATOM   16945 C  CB  . SER   E 2 771 ? 10.550  -23.374 -28.208 1.00 97.84  ? 1075 SER   E CB  1 
ATOM   16946 O  OG  . SER   E 2 771 ? 9.217   -23.103 -28.630 1.00 101.07 ? 1075 SER   E OG  1 
ATOM   16947 N  N   . PHE   E 2 772 ? 12.932  -22.310 -26.291 1.00 91.94  ? 1076 PHE   E N   1 
ATOM   16948 C  CA  . PHE   E 2 772 ? 14.246  -22.344 -25.660 1.00 94.84  ? 1076 PHE   E CA  1 
ATOM   16949 C  C   . PHE   E 2 772 ? 14.851  -23.741 -25.758 1.00 100.81 ? 1076 PHE   E C   1 
ATOM   16950 O  O   . PHE   E 2 772 ? 14.421  -24.655 -25.056 1.00 107.10 ? 1076 PHE   E O   1 
ATOM   16951 C  CB  . PHE   E 2 772 ? 14.096  -21.907 -24.203 1.00 93.57  ? 1076 PHE   E CB  1 
ATOM   16952 C  CG  . PHE   E 2 772 ? 15.357  -21.978 -23.401 1.00 92.65  ? 1076 PHE   E CG  1 
ATOM   16953 C  CD1 . PHE   E 2 772 ? 15.793  -23.174 -22.871 1.00 96.33  ? 1076 PHE   E CD1 1 
ATOM   16954 C  CD2 . PHE   E 2 772 ? 16.079  -20.838 -23.134 1.00 90.26  ? 1076 PHE   E CD2 1 
ATOM   16955 C  CE1 . PHE   E 2 772 ? 16.928  -23.230 -22.130 1.00 94.21  ? 1076 PHE   E CE1 1 
ATOM   16956 C  CE2 . PHE   E 2 772 ? 17.218  -20.893 -22.379 1.00 87.74  ? 1076 PHE   E CE2 1 
ATOM   16957 C  CZ  . PHE   E 2 772 ? 17.642  -22.085 -21.881 1.00 87.83  ? 1076 PHE   E CZ  1 
ATOM   16958 N  N   . HIS   E 2 773 ? 15.869  -23.905 -26.595 1.00 104.55 ? 1077 HIS   E N   1 
ATOM   16959 C  CA  . HIS   E 2 773 ? 16.363  -25.230 -26.943 1.00 108.52 ? 1077 HIS   E CA  1 
ATOM   16960 C  C   . HIS   E 2 773 ? 17.715  -25.531 -26.308 1.00 114.61 ? 1077 HIS   E C   1 
ATOM   16961 O  O   . HIS   E 2 773 ? 18.610  -24.677 -26.260 1.00 107.69 ? 1077 HIS   E O   1 
ATOM   16962 C  CB  . HIS   E 2 773 ? 16.476  -25.398 -28.454 1.00 109.08 ? 1077 HIS   E CB  1 
ATOM   16963 C  CG  . HIS   E 2 773 ? 17.251  -26.609 -28.871 1.00 112.75 ? 1077 HIS   E CG  1 
ATOM   16964 N  ND1 . HIS   E 2 773 ? 16.839  -27.891 -28.580 1.00 116.24 ? 1077 HIS   E ND1 1 
ATOM   16965 C  CD2 . HIS   E 2 773 ? 18.408  -26.730 -29.565 1.00 112.76 ? 1077 HIS   E CD2 1 
ATOM   16966 C  CE1 . HIS   E 2 773 ? 17.706  -28.751 -29.082 1.00 122.95 ? 1077 HIS   E CE1 1 
ATOM   16967 N  NE2 . HIS   E 2 773 ? 18.667  -28.073 -29.687 1.00 121.25 ? 1077 HIS   E NE2 1 
ATOM   16968 N  N   . THR   E 2 774 ? 17.831  -26.775 -25.837 1.00 127.88 ? 1078 THR   E N   1 
ATOM   16969 C  CA  . THR   E 2 774 ? 19.053  -27.416 -25.369 1.00 133.27 ? 1078 THR   E CA  1 
ATOM   16970 C  C   . THR   E 2 774 ? 18.899  -28.909 -25.673 1.00 139.20 ? 1078 THR   E C   1 
ATOM   16971 O  O   . THR   E 2 774 ? 17.773  -29.420 -25.765 1.00 138.36 ? 1078 THR   E O   1 
ATOM   16972 C  CB  . THR   E 2 774 ? 19.287  -27.122 -23.869 1.00 129.16 ? 1078 THR   E CB  1 
ATOM   16973 O  OG1 . THR   E 2 774 ? 19.356  -25.710 -23.675 1.00 121.20 ? 1078 THR   E OG1 1 
ATOM   16974 C  CG2 . THR   E 2 774 ? 20.587  -27.704 -23.366 1.00 129.66 ? 1078 THR   E CG2 1 
ATOM   16975 N  N   . GLU   E 2 775 ? 20.033  -29.597 -25.885 1.00 135.44 ? 1079 GLU   E N   1 
ATOM   16976 C  CA  . GLU   E 2 775 ? 20.007  -31.038 -26.141 1.00 134.08 ? 1079 GLU   E CA  1 
ATOM   16977 C  C   . GLU   E 2 775 ? 19.320  -31.812 -25.015 1.00 139.48 ? 1079 GLU   E C   1 
ATOM   16978 O  O   . GLU   E 2 775 ? 18.843  -32.934 -25.242 1.00 136.26 ? 1079 GLU   E O   1 
ATOM   16979 C  CB  . GLU   E 2 775 ? 21.438  -31.556 -26.363 1.00 130.72 ? 1079 GLU   E CB  1 
ATOM   16980 C  CG  . GLU   E 2 775 ? 22.331  -31.635 -25.105 1.00 134.79 ? 1079 GLU   E CG  1 
ATOM   16981 C  CD  . GLU   E 2 775 ? 22.629  -30.273 -24.465 1.00 130.63 ? 1079 GLU   E CD  1 
ATOM   16982 O  OE1 . GLU   E 2 775 ? 22.715  -29.259 -25.203 1.00 126.55 ? 1079 GLU   E OE1 1 
ATOM   16983 O  OE2 . GLU   E 2 775 ? 22.777  -30.220 -23.217 1.00 126.92 ? 1079 GLU   E OE2 1 
ATOM   16984 N  N   . ARG   E 2 776 ? 19.247  -31.226 -23.812 1.00 149.80 ? 1080 ARG   E N   1 
ATOM   16985 C  CA  . ARG   E 2 776 ? 18.599  -31.805 -22.642 1.00 148.69 ? 1080 ARG   E CA  1 
ATOM   16986 C  C   . ARG   E 2 776 ? 17.155  -31.325 -22.479 1.00 152.36 ? 1080 ARG   E C   1 
ATOM   16987 O  O   . ARG   E 2 776 ? 16.264  -32.138 -22.223 1.00 154.59 ? 1080 ARG   E O   1 
ATOM   16988 C  CB  . ARG   E 2 776 ? 19.412  -31.488 -21.378 1.00 143.79 ? 1080 ARG   E CB  1 
ATOM   16989 N  N   . LYS   E 2 777 ? 16.900  -30.022 -22.623 1.00 154.92 ? 1081 LYS   E N   1 
ATOM   16990 C  CA  . LYS   E 2 777 ? 15.557  -29.462 -22.466 1.00 154.24 ? 1081 LYS   E CA  1 
ATOM   16991 C  C   . LYS   E 2 777 ? 15.216  -28.550 -23.638 1.00 150.38 ? 1081 LYS   E C   1 
ATOM   16992 O  O   . LYS   E 2 777 ? 16.068  -27.794 -24.115 1.00 149.78 ? 1081 LYS   E O   1 
ATOM   16993 C  CB  . LYS   E 2 777 ? 15.434  -28.673 -21.138 1.00 153.80 ? 1081 LYS   E CB  1 
ATOM   16994 C  CG  . LYS   E 2 777 ? 15.717  -29.506 -19.907 1.00 158.51 ? 1081 LYS   E CG  1 
ATOM   16995 C  CD  . LYS   E 2 777 ? 15.747  -28.688 -18.621 1.00 158.67 ? 1081 LYS   E CD  1 
ATOM   16996 C  CE  . LYS   E 2 777 ? 16.078  -29.619 -17.453 1.00 159.44 ? 1081 LYS   E CE  1 
ATOM   16997 N  NZ  . LYS   E 2 777 ? 15.935  -28.970 -16.135 1.00 160.11 ? 1081 LYS   E NZ  1 
ATOM   16998 N  N   . THR   E 2 778 ? 13.967  -28.619 -24.103 1.00 133.05 ? 1082 THR   E N   1 
ATOM   16999 C  CA  . THR   E 2 778 ? 13.412  -27.610 -24.997 1.00 121.16 ? 1082 THR   E CA  1 
ATOM   17000 C  C   . THR   E 2 778 ? 12.069  -27.186 -24.424 1.00 117.68 ? 1082 THR   E C   1 
ATOM   17001 O  O   . THR   E 2 778 ? 11.158  -28.014 -24.312 1.00 115.32 ? 1082 THR   E O   1 
ATOM   17002 C  CB  . THR   E 2 778 ? 13.257  -28.114 -26.436 1.00 119.10 ? 1082 THR   E CB  1 
ATOM   17003 O  OG1 . THR   E 2 778 ? 12.043  -28.857 -26.544 1.00 119.80 ? 1082 THR   E OG1 1 
ATOM   17004 C  CG2 . THR   E 2 778 ? 14.442  -28.986 -26.858 1.00 122.83 ? 1082 THR   E CG2 1 
ATOM   17005 N  N   . GLU   E 2 779 ? 11.967  -25.908 -24.041 1.00 111.20 ? 1083 GLU   E N   1 
ATOM   17006 C  CA  . GLU   E 2 779 ? 10.850  -25.210 -23.414 1.00 107.47 ? 1083 GLU   E CA  1 
ATOM   17007 C  C   . GLU   E 2 779 ? 10.423  -24.014 -24.264 1.00 104.57 ? 1083 GLU   E C   1 
ATOM   17008 O  O   . GLU   E 2 779 ? 11.261  -23.387 -24.918 1.00 105.48 ? 1083 GLU   E O   1 
ATOM   17009 C  CB  . GLU   E 2 779 ? 11.239  -24.745 -22.000 1.00 108.67 ? 1083 GLU   E CB  1 
ATOM   17010 C  CG  . GLU   E 2 779 ? 11.558  -25.935 -21.045 1.00 124.49 ? 1083 GLU   E CG  1 
ATOM   17011 C  CD  . GLU   E 2 779 ? 12.382  -25.567 -19.792 1.00 131.77 ? 1083 GLU   E CD  1 
ATOM   17012 O  OE1 . GLU   E 2 779 ? 12.055  -24.555 -19.119 1.00 130.25 ? 1083 GLU   E OE1 1 
ATOM   17013 O  OE2 . GLU   E 2 779 ? 13.353  -26.308 -19.476 1.00 135.15 ? 1083 GLU   E OE2 1 
ATOM   17014 N  N   . PRO   E 2 780 ? 9.128   -23.675 -24.278 1.00 105.68 ? 1084 PRO   E N   1 
ATOM   17015 C  CA  . PRO   E 2 780 ? 8.645   -22.600 -25.160 1.00 102.50 ? 1084 PRO   E CA  1 
ATOM   17016 C  C   . PRO   E 2 780 ? 9.234   -21.254 -24.783 1.00 99.53  ? 1084 PRO   E C   1 
ATOM   17017 O  O   . PRO   E 2 780 ? 9.801   -21.073 -23.705 1.00 101.73 ? 1084 PRO   E O   1 
ATOM   17018 C  CB  . PRO   E 2 780 ? 7.137   -22.597 -24.918 1.00 104.01 ? 1084 PRO   E CB  1 
ATOM   17019 C  CG  . PRO   E 2 780 ? 7.053   -22.988 -23.468 1.00 105.26 ? 1084 PRO   E CG  1 
ATOM   17020 C  CD  . PRO   E 2 780 ? 8.086   -24.086 -23.321 1.00 106.82 ? 1084 PRO   E CD  1 
ATOM   17021 N  N   . ALA   E 2 781 ? 9.050   -20.280 -25.653 1.00 94.30  ? 1085 ALA   E N   1 
ATOM   17022 C  CA  . ALA   E 2 781 ? 9.538   -18.959 -25.299 1.00 92.34  ? 1085 ALA   E CA  1 
ATOM   17023 C  C   . ALA   E 2 781 ? 8.533   -18.248 -24.401 1.00 93.16  ? 1085 ALA   E C   1 
ATOM   17024 O  O   . ALA   E 2 781 ? 7.391   -18.683 -24.227 1.00 95.75  ? 1085 ALA   E O   1 
ATOM   17025 C  CB  . ALA   E 2 781 ? 9.829   -18.122 -26.543 1.00 89.22  ? 1085 ALA   E CB  1 
ATOM   17026 N  N   . THR   E 2 782 ? 8.967   -17.120 -23.853 1.00 93.19  ? 1086 THR   E N   1 
ATOM   17027 C  CA  . THR   E 2 782 ? 8.164   -16.339 -22.929 1.00 96.78  ? 1086 THR   E CA  1 
ATOM   17028 C  C   . THR   E 2 782 ? 8.841   -14.996 -22.710 1.00 96.93  ? 1086 THR   E C   1 
ATOM   17029 O  O   . THR   E 2 782 ? 10.070  -14.903 -22.746 1.00 97.43  ? 1086 THR   E O   1 
ATOM   17030 C  CB  . THR   E 2 782 ? 8.007   -17.077 -21.600 1.00 95.61  ? 1086 THR   E CB  1 
ATOM   17031 O  OG1 . THR   E 2 782 ? 7.344   -16.214 -20.677 1.00 99.30  ? 1086 THR   E OG1 1 
ATOM   17032 C  CG2 . THR   E 2 782 ? 9.375   -17.484 -21.049 1.00 86.47  ? 1086 THR   E CG2 1 
ATOM   17033 N  N   . GLY   E 2 783 ? 8.039   -13.957 -22.491 1.00 102.73 ? 1087 GLY   E N   1 
ATOM   17034 C  CA  . GLY   E 2 783 ? 8.608   -12.683 -22.097 1.00 106.29 ? 1087 GLY   E CA  1 
ATOM   17035 C  C   . GLY   E 2 783 ? 9.404   -12.009 -23.194 1.00 108.49 ? 1087 GLY   E C   1 
ATOM   17036 O  O   . GLY   E 2 783 ? 10.049  -10.979 -22.947 1.00 107.67 ? 1087 GLY   E O   1 
ATOM   17037 N  N   . PHE   E 2 784 ? 9.366   -12.571 -24.412 1.00 103.12 ? 1088 PHE   E N   1 
ATOM   17038 C  CA  . PHE   E 2 784 ? 10.087  -12.041 -25.562 1.00 99.22  ? 1088 PHE   E CA  1 
ATOM   17039 C  C   . PHE   E 2 784 ? 9.148   -11.975 -26.758 1.00 101.30 ? 1088 PHE   E C   1 
ATOM   17040 O  O   . PHE   E 2 784 ? 8.224   -12.782 -26.887 1.00 103.13 ? 1088 PHE   E O   1 
ATOM   17041 C  CB  . PHE   E 2 784 ? 11.316  -12.901 -25.887 1.00 93.12  ? 1088 PHE   E CB  1 
ATOM   17042 C  CG  . PHE   E 2 784 ? 12.522  -12.603 -25.026 1.00 92.12  ? 1088 PHE   E CG  1 
ATOM   17043 C  CD1 . PHE   E 2 784 ? 13.472  -11.665 -25.434 1.00 89.93  ? 1088 PHE   E CD1 1 
ATOM   17044 C  CD2 . PHE   E 2 784 ? 12.721  -13.272 -23.828 1.00 89.50  ? 1088 PHE   E CD2 1 
ATOM   17045 C  CE1 . PHE   E 2 784 ? 14.589  -11.399 -24.661 1.00 88.16  ? 1088 PHE   E CE1 1 
ATOM   17046 C  CE2 . PHE   E 2 784 ? 13.837  -13.006 -23.042 1.00 88.02  ? 1088 PHE   E CE2 1 
ATOM   17047 C  CZ  . PHE   E 2 784 ? 14.771  -12.068 -23.458 1.00 86.48  ? 1088 PHE   E CZ  1 
ATOM   17048 N  N   . ILE   E 2 785 ? 9.398   -11.001 -27.635 1.00 106.90 ? 1089 ILE   E N   1 
ATOM   17049 C  CA  . ILE   E 2 785 ? 8.568   -10.755 -28.813 1.00 106.25 ? 1089 ILE   E CA  1 
ATOM   17050 C  C   . ILE   E 2 785 ? 9.456   -10.639 -30.036 1.00 107.03 ? 1089 ILE   E C   1 
ATOM   17051 O  O   . ILE   E 2 785 ? 10.204  -9.660  -30.177 1.00 105.56 ? 1089 ILE   E O   1 
ATOM   17052 C  CB  . ILE   E 2 785 ? 7.705   -9.504  -28.655 1.00 105.77 ? 1089 ILE   E CB  1 
ATOM   17053 C  CG1 . ILE   E 2 785 ? 6.585   -9.842  -27.684 1.00 107.57 ? 1089 ILE   E CG1 1 
ATOM   17054 C  CG2 . ILE   E 2 785 ? 7.186   -9.044  -30.021 1.00 104.89 ? 1089 ILE   E CG2 1 
ATOM   17055 C  CD1 . ILE   E 2 785 ? 5.969   -8.669  -27.060 1.00 112.29 ? 1089 ILE   E CD1 1 
ATOM   17056 N  N   . ASP   E 2 786 ? 9.356   -11.625 -30.931 1.00 101.41 ? 1090 ASP   E N   1 
ATOM   17057 C  CA  . ASP   E 2 786 ? 10.186  -11.684 -32.132 1.00 102.57 ? 1090 ASP   E CA  1 
ATOM   17058 C  C   . ASP   E 2 786 ? 9.764   -10.363 -32.761 1.00 101.84 ? 1090 ASP   E C   1 
ATOM   17059 O  O   . ASP   E 2 786 ? 8.621   -10.206 -33.199 1.00 103.62 ? 1090 ASP   E O   1 
ATOM   17060 C  CB  . ASP   E 2 786 ? 9.904   -12.976 -32.911 1.00 101.50 ? 1090 ASP   E CB  1 
ATOM   17061 C  CG  . ASP   E 2 786 ? 10.903  -13.237 -34.026 1.00 99.99  ? 1090 ASP   E CG  1 
ATOM   17062 O  OD1 . ASP   E 2 786 ? 11.761  -12.363 -34.306 1.00 99.51  ? 1090 ASP   E OD1 1 
ATOM   17063 O  OD2 . ASP   E 2 786 ? 10.817  -14.327 -34.630 1.00 96.65  ? 1090 ASP   E OD2 1 
ATOM   17064 N  N   . GLY   E 2 787 ? 10.692  -9.392  -32.788 1.00 94.78  ? 1091 GLY   E N   1 
ATOM   17065 C  CA  . GLY   E 2 787 ? 10.360  -8.063  -33.288 1.00 94.93  ? 1091 GLY   E CA  1 
ATOM   17066 C  C   . GLY   E 2 787 ? 10.553  -8.125  -34.784 1.00 93.26  ? 1091 GLY   E C   1 
ATOM   17067 O  O   . GLY   E 2 787 ? 9.979   -7.310  -35.519 1.00 93.41  ? 1091 GLY   E O   1 
ATOM   17068 N  N   . ASP   E 2 788 ? 11.363  -9.067  -35.256 1.00 93.05  ? 1092 ASP   E N   1 
ATOM   17069 C  CA  . ASP   E 2 788 ? 11.463  -9.322  -36.684 1.00 89.06  ? 1092 ASP   E CA  1 
ATOM   17070 C  C   . ASP   E 2 788 ? 10.154  -9.858  -37.215 1.00 93.06  ? 1092 ASP   E C   1 
ATOM   17071 O  O   . ASP   E 2 788 ? 9.694   -9.436  -38.277 1.00 98.41  ? 1092 ASP   E O   1 
ATOM   17072 C  CB  . ASP   E 2 788 ? 12.584  -10.318 -36.975 1.00 89.49  ? 1092 ASP   E CB  1 
ATOM   17073 C  CG  . ASP   E 2 788 ? 13.960  -9.776  -36.638 1.00 91.94  ? 1092 ASP   E CG  1 
ATOM   17074 O  OD1 . ASP   E 2 788 ? 14.297  -8.662  -37.110 1.00 90.95  ? 1092 ASP   E OD1 1 
ATOM   17075 O  OD2 . ASP   E 2 788 ? 14.705  -10.453 -35.885 1.00 91.82  ? 1092 ASP   E OD2 1 
ATOM   17076 N  N   . LEU   E 2 789 ? 9.546   -10.799 -36.496 1.00 94.93  ? 1093 LEU   E N   1 
ATOM   17077 C  CA  . LEU   E 2 789 ? 8.232   -11.281 -36.890 1.00 97.87  ? 1093 LEU   E CA  1 
ATOM   17078 C  C   . LEU   E 2 789 ? 7.230   -10.137 -36.961 1.00 98.22  ? 1093 LEU   E C   1 
ATOM   17079 O  O   . LEU   E 2 789 ? 6.429   -10.049 -37.897 1.00 100.63 ? 1093 LEU   E O   1 
ATOM   17080 C  CB  . LEU   E 2 789 ? 7.768   -12.347 -35.904 1.00 101.09 ? 1093 LEU   E CB  1 
ATOM   17081 C  CG  . LEU   E 2 789 ? 6.485   -13.047 -36.297 1.00 105.01 ? 1093 LEU   E CG  1 
ATOM   17082 C  CD1 . LEU   E 2 789 ? 6.696   -13.832 -37.587 1.00 105.68 ? 1093 LEU   E CD1 1 
ATOM   17083 C  CD2 . LEU   E 2 789 ? 6.083   -13.949 -35.167 1.00 107.45 ? 1093 LEU   E CD2 1 
ATOM   17084 N  N   . ILE   E 2 790 ? 7.298   -9.226  -35.993 1.00 99.30  ? 1094 ILE   E N   1 
ATOM   17085 C  CA  . ILE   E 2 790 ? 6.357   -8.117  -35.913 1.00 99.96  ? 1094 ILE   E CA  1 
ATOM   17086 C  C   . ILE   E 2 790 ? 6.559   -7.147  -37.068 1.00 102.92 ? 1094 ILE   E C   1 
ATOM   17087 O  O   . ILE   E 2 790 ? 5.589   -6.664  -37.658 1.00 106.78 ? 1094 ILE   E O   1 
ATOM   17088 C  CB  . ILE   E 2 790 ? 6.501   -7.398  -34.563 1.00 98.99  ? 1094 ILE   E CB  1 
ATOM   17089 C  CG1 . ILE   E 2 790 ? 6.355   -8.383  -33.409 1.00 96.25  ? 1094 ILE   E CG1 1 
ATOM   17090 C  CG2 . ILE   E 2 790 ? 5.485   -6.270  -34.464 1.00 101.57 ? 1094 ILE   E CG2 1 
ATOM   17091 C  CD1 . ILE   E 2 790 ? 4.948   -8.756  -33.125 1.00 100.99 ? 1094 ILE   E CD1 1 
ATOM   17092 N  N   . GLU   E 2 791 ? 7.817   -6.808  -37.380 1.00 105.90 ? 1095 GLU   E N   1 
ATOM   17093 C  CA  . GLU   E 2 791 ? 8.101   -5.868  -38.464 1.00 106.09 ? 1095 GLU   E CA  1 
ATOM   17094 C  C   . GLU   E 2 791 ? 7.765   -6.450  -39.828 1.00 108.93 ? 1095 GLU   E C   1 
ATOM   17095 O  O   . GLU   E 2 791 ? 7.591   -5.689  -40.786 1.00 113.44 ? 1095 GLU   E O   1 
ATOM   17096 C  CB  . GLU   E 2 791 ? 9.571   -5.428  -38.451 1.00 103.85 ? 1095 GLU   E CB  1 
ATOM   17097 C  CG  . GLU   E 2 791 ? 9.915   -4.404  -37.372 1.00 108.15 ? 1095 GLU   E CG  1 
ATOM   17098 C  CD  . GLU   E 2 791 ? 11.394  -3.989  -37.371 1.00 110.57 ? 1095 GLU   E CD  1 
ATOM   17099 O  OE1 . GLU   E 2 791 ? 12.096  -4.232  -38.388 1.00 108.98 ? 1095 GLU   E OE1 1 
ATOM   17100 O  OE2 . GLU   E 2 791 ? 11.853  -3.423  -36.341 1.00 110.17 ? 1095 GLU   E OE2 1 
ATOM   17101 N  N   . SER   E 2 792 ? 7.676   -7.774  -39.945 1.00 107.67 ? 1096 SER   E N   1 
ATOM   17102 C  CA  . SER   E 2 792 ? 7.258   -8.359  -41.210 1.00 107.21 ? 1096 SER   E CA  1 
ATOM   17103 C  C   . SER   E 2 792 ? 5.775   -8.146  -41.473 1.00 112.36 ? 1096 SER   E C   1 
ATOM   17104 O  O   . SER   E 2 792 ? 5.340   -8.297  -42.615 1.00 119.09 ? 1096 SER   E O   1 
ATOM   17105 C  CB  . SER   E 2 792 ? 7.583   -9.844  -41.222 1.00 103.79 ? 1096 SER   E CB  1 
ATOM   17106 O  OG  . SER   E 2 792 ? 7.043   -10.451 -40.064 1.00 106.95 ? 1096 SER   E OG  1 
ATOM   17107 N  N   . PHE   E 2 793 ? 4.991   -7.815  -40.443 1.00 114.85 ? 1097 PHE   E N   1 
ATOM   17108 C  CA  . PHE   E 2 793 ? 3.592   -7.445  -40.646 1.00 119.08 ? 1097 PHE   E CA  1 
ATOM   17109 C  C   . PHE   E 2 793 ? 3.466   -6.282  -41.621 1.00 124.94 ? 1097 PHE   E C   1 
ATOM   17110 O  O   . PHE   E 2 793 ? 2.558   -6.267  -42.460 1.00 129.78 ? 1097 PHE   E O   1 
ATOM   17111 C  CB  . PHE   E 2 793 ? 2.946   -7.098  -39.295 1.00 121.51 ? 1097 PHE   E CB  1 
ATOM   17112 C  CG  . PHE   E 2 793 ? 1.733   -6.168  -39.384 1.00 127.48 ? 1097 PHE   E CG  1 
ATOM   17113 C  CD1 . PHE   E 2 793 ? 1.888   -4.779  -39.320 1.00 128.10 ? 1097 PHE   E CD1 1 
ATOM   17114 C  CD2 . PHE   E 2 793 ? 0.436   -6.683  -39.488 1.00 131.00 ? 1097 PHE   E CD2 1 
ATOM   17115 C  CE1 . PHE   E 2 793 ? 0.782   -3.933  -39.390 1.00 129.85 ? 1097 PHE   E CE1 1 
ATOM   17116 C  CE2 . PHE   E 2 793 ? -0.675  -5.827  -39.559 1.00 131.65 ? 1097 PHE   E CE2 1 
ATOM   17117 C  CZ  . PHE   E 2 793 ? -0.495  -4.459  -39.502 1.00 130.30 ? 1097 PHE   E CZ  1 
ATOM   17118 N  N   . LEU   E 2 794 ? 4.364   -5.294  -41.526 1.00 119.08 ? 1098 LEU   E N   1 
ATOM   17119 C  CA  . LEU   E 2 794 ? 4.299   -4.131  -42.406 1.00 120.24 ? 1098 LEU   E CA  1 
ATOM   17120 C  C   . LEU   E 2 794 ? 4.320   -4.515  -43.878 1.00 124.79 ? 1098 LEU   E C   1 
ATOM   17121 O  O   . LEU   E 2 794 ? 3.720   -3.829  -44.711 1.00 131.41 ? 1098 LEU   E O   1 
ATOM   17122 C  CB  . LEU   E 2 794 ? 5.455   -3.176  -42.115 1.00 116.95 ? 1098 LEU   E CB  1 
ATOM   17123 C  CG  . LEU   E 2 794 ? 5.347   -2.481  -40.765 1.00 117.34 ? 1098 LEU   E CG  1 
ATOM   17124 C  CD1 . LEU   E 2 794 ? 6.469   -1.459  -40.555 1.00 114.19 ? 1098 LEU   E CD1 1 
ATOM   17125 C  CD2 . LEU   E 2 794 ? 3.980   -1.828  -40.683 1.00 118.89 ? 1098 LEU   E CD2 1 
ATOM   17126 N  N   . ASP   E 2 795 ? 4.982   -5.608  -44.221 1.00 123.09 ? 1099 ASP   E N   1 
ATOM   17127 C  CA  . ASP   E 2 795 ? 5.151   -5.966  -45.625 1.00 126.55 ? 1099 ASP   E CA  1 
ATOM   17128 C  C   . ASP   E 2 795 ? 4.261   -7.137  -46.040 1.00 131.24 ? 1099 ASP   E C   1 
ATOM   17129 O  O   . ASP   E 2 795 ? 4.743   -8.090  -46.656 1.00 135.35 ? 1099 ASP   E O   1 
ATOM   17130 C  CB  . ASP   E 2 795 ? 6.618   -6.267  -45.892 1.00 127.73 ? 1099 ASP   E CB  1 
ATOM   17131 C  CG  . ASP   E 2 795 ? 7.040   -5.910  -47.307 1.00 134.48 ? 1099 ASP   E CG  1 
ATOM   17132 O  OD1 . ASP   E 2 795 ? 6.594   -6.614  -48.248 1.00 128.82 ? 1099 ASP   E OD1 1 
ATOM   17133 O  OD2 . ASP   E 2 795 ? 7.802   -4.919  -47.477 1.00 139.47 ? 1099 ASP   E OD2 1 
ATOM   17134 N  N   . ILE   E 2 796 ? 2.962   -7.092  -45.735 1.00 132.78 ? 1100 ILE   E N   1 
ATOM   17135 C  CA  . ILE   E 2 796 ? 2.050   -8.122  -46.240 1.00 140.19 ? 1100 ILE   E CA  1 
ATOM   17136 C  C   . ILE   E 2 796 ? 0.947   -7.466  -47.067 1.00 149.09 ? 1100 ILE   E C   1 
ATOM   17137 O  O   . ILE   E 2 796 ? 0.908   -6.237  -47.198 1.00 149.94 ? 1100 ILE   E O   1 
ATOM   17138 C  CB  . ILE   E 2 796 ? 1.466   -8.983  -45.104 1.00 138.88 ? 1100 ILE   E CB  1 
ATOM   17139 C  CG1 . ILE   E 2 796 ? 0.671   -8.134  -44.117 1.00 142.85 ? 1100 ILE   E CG1 1 
ATOM   17140 C  CG2 . ILE   E 2 796 ? 2.563   -9.697  -44.358 1.00 132.20 ? 1100 ILE   E CG2 1 
ATOM   17141 C  CD1 . ILE   E 2 796 ? 0.177   -8.900  -42.883 1.00 140.78 ? 1100 ILE   E CD1 1 
ATOM   17142 N  N   . SER   E 2 797 ? 0.047   -8.274  -47.632 1.00 164.68 ? 1101 SER   E N   1 
ATOM   17143 C  CA  . SER   E 2 797 ? -1.008  -7.759  -48.501 1.00 163.97 ? 1101 SER   E CA  1 
ATOM   17144 C  C   . SER   E 2 797 ? -2.121  -7.124  -47.675 1.00 164.35 ? 1101 SER   E C   1 
ATOM   17145 O  O   . SER   E 2 797 ? -2.475  -7.619  -46.604 1.00 166.84 ? 1101 SER   E O   1 
ATOM   17146 C  CB  . SER   E 2 797 ? -1.581  -8.874  -49.381 1.00 164.20 ? 1101 SER   E CB  1 
ATOM   17147 O  OG  . SER   E 2 797 ? -2.558  -9.642  -48.692 1.00 166.28 ? 1101 SER   E OG  1 
ATOM   17148 N  N   . ARG   E 2 798 ? -2.690  -6.028  -48.197 1.00 155.90 ? 1102 ARG   E N   1 
ATOM   17149 C  CA  . ARG   E 2 798 ? -3.701  -5.277  -47.447 1.00 154.40 ? 1102 ARG   E CA  1 
ATOM   17150 C  C   . ARG   E 2 798 ? -4.899  -6.125  -47.015 1.00 155.85 ? 1102 ARG   E C   1 
ATOM   17151 O  O   . ARG   E 2 798 ? -5.438  -5.854  -45.925 1.00 156.43 ? 1102 ARG   E O   1 
ATOM   17152 C  CB  . ARG   E 2 798 ? -4.151  -4.058  -48.261 1.00 150.79 ? 1102 ARG   E CB  1 
ATOM   17153 N  N   . PRO   E 2 799 ? -5.360  -7.129  -47.771 1.00 152.16 ? 1103 PRO   E N   1 
ATOM   17154 C  CA  . PRO   E 2 799 ? -6.336  -8.072  -47.179 1.00 151.93 ? 1103 PRO   E CA  1 
ATOM   17155 C  C   . PRO   E 2 799 ? -5.767  -8.835  -46.003 1.00 152.38 ? 1103 PRO   E C   1 
ATOM   17156 O  O   . PRO   E 2 799 ? -6.417  -8.899  -44.948 1.00 152.34 ? 1103 PRO   E O   1 
ATOM   17157 C  CB  . PRO   E 2 799 ? -6.697  -8.998  -48.350 1.00 153.39 ? 1103 PRO   E CB  1 
ATOM   17158 C  CG  . PRO   E 2 799 ? -6.421  -8.188  -49.570 1.00 157.08 ? 1103 PRO   E CG  1 
ATOM   17159 C  CD  . PRO   E 2 799 ? -5.243  -7.303  -49.229 1.00 153.96 ? 1103 PRO   E CD  1 
ATOM   17160 N  N   . LYS   E 2 800 ? -4.560  -9.413  -46.133 1.00 157.68 ? 1104 LYS   E N   1 
ATOM   17161 C  CA  . LYS   E 2 800 ? -3.940  -10.125 -45.019 1.00 152.84 ? 1104 LYS   E CA  1 
ATOM   17162 C  C   . LYS   E 2 800 ? -3.796  -9.223  -43.794 1.00 151.92 ? 1104 LYS   E C   1 
ATOM   17163 O  O   . LYS   E 2 800 ? -4.087  -9.650  -42.670 1.00 152.73 ? 1104 LYS   E O   1 
ATOM   17164 C  CB  . LYS   E 2 800 ? -2.581  -10.700 -45.439 1.00 148.59 ? 1104 LYS   E CB  1 
ATOM   17165 N  N   . MET   E 2 801 ? -3.369  -7.969  -43.990 1.00 151.06 ? 1105 MET   E N   1 
ATOM   17166 C  CA  . MET   E 2 801 ? -3.355  -6.995  -42.896 1.00 150.67 ? 1105 MET   E CA  1 
ATOM   17167 C  C   . MET   E 2 801 ? -4.752  -6.821  -42.297 1.00 155.71 ? 1105 MET   E C   1 
ATOM   17168 O  O   . MET   E 2 801 ? -4.937  -6.944  -41.077 1.00 155.58 ? 1105 MET   E O   1 
ATOM   17169 C  CB  . MET   E 2 801 ? -2.823  -5.642  -43.391 1.00 145.42 ? 1105 MET   E CB  1 
ATOM   17170 C  CG  . MET   E 2 801 ? -1.586  -5.686  -44.279 1.00 145.42 ? 1105 MET   E CG  1 
ATOM   17171 S  SD  . MET   E 2 801 ? -0.639  -4.142  -44.328 1.00 140.61 ? 1105 MET   E SD  1 
ATOM   17172 C  CE  . MET   E 2 801 ? -0.934  -3.607  -42.665 1.00 133.56 ? 1105 MET   E CE  1 
ATOM   17173 N  N   . GLN   E 2 802 ? -5.753  -6.527  -43.143 1.00 153.31 ? 1106 GLN   E N   1 
ATOM   17174 C  CA  . GLN   E 2 802 ? -7.127  -6.376  -42.670 1.00 153.39 ? 1106 GLN   E CA  1 
ATOM   17175 C  C   . GLN   E 2 802 ? -7.636  -7.639  -41.970 1.00 152.75 ? 1106 GLN   E C   1 
ATOM   17176 O  O   . GLN   E 2 802 ? -8.513  -7.542  -41.103 1.00 153.60 ? 1106 GLN   E O   1 
ATOM   17177 C  CB  . GLN   E 2 802 ? -8.051  -5.988  -43.845 1.00 150.14 ? 1106 GLN   E CB  1 
ATOM   17178 N  N   . GLU   E 2 803 ? -7.101  -8.819  -42.317 1.00 158.36 ? 1107 GLU   E N   1 
ATOM   17179 C  CA  . GLU   E 2 803 ? -7.510  -10.089 -41.713 1.00 158.65 ? 1107 GLU   E CA  1 
ATOM   17180 C  C   . GLU   E 2 803 ? -6.793  -10.376 -40.403 1.00 159.96 ? 1107 GLU   E C   1 
ATOM   17181 O  O   . GLU   E 2 803 ? -7.419  -10.825 -39.435 1.00 157.39 ? 1107 GLU   E O   1 
ATOM   17182 C  CB  . GLU   E 2 803 ? -7.254  -11.260 -42.678 1.00 156.62 ? 1107 GLU   E CB  1 
ATOM   17183 N  N   . VAL   E 2 804 ? -5.478  -10.156 -40.365 1.00 157.88 ? 1108 VAL   E N   1 
ATOM   17184 C  CA  . VAL   E 2 804 ? -4.705  -10.386 -39.151 1.00 157.85 ? 1108 VAL   E CA  1 
ATOM   17185 C  C   . VAL   E 2 804 ? -5.042  -9.405  -38.043 1.00 160.29 ? 1108 VAL   E C   1 
ATOM   17186 O  O   . VAL   E 2 804 ? -4.559  -9.574  -36.917 1.00 158.03 ? 1108 VAL   E O   1 
ATOM   17187 C  CB  . VAL   E 2 804 ? -3.187  -10.308 -39.423 1.00 156.36 ? 1108 VAL   E CB  1 
ATOM   17188 C  CG1 . VAL   E 2 804 ? -2.791  -11.294 -40.498 1.00 152.41 ? 1108 VAL   E CG1 1 
ATOM   17189 C  CG2 . VAL   E 2 804 ? -2.786  -8.891  -39.811 1.00 154.41 ? 1108 VAL   E CG2 1 
ATOM   17190 N  N   . VAL   E 2 805 ? -5.854  -8.384  -38.327 1.00 177.70 ? 1109 VAL   E N   1 
ATOM   17191 C  CA  . VAL   E 2 805 ? -6.244  -7.405  -37.312 1.00 178.04 ? 1109 VAL   E CA  1 
ATOM   17192 C  C   . VAL   E 2 805 ? -7.681  -7.595  -36.831 1.00 179.28 ? 1109 VAL   E C   1 
ATOM   17193 O  O   . VAL   E 2 805 ? -8.095  -6.914  -35.875 1.00 179.30 ? 1109 VAL   E O   1 
ATOM   17194 C  CB  . VAL   E 2 805 ? -6.041  -5.964  -37.826 1.00 177.63 ? 1109 VAL   E CB  1 
ATOM   17195 C  CG1 . VAL   E 2 805 ? -4.603  -5.758  -38.244 1.00 175.61 ? 1109 VAL   E CG1 1 
ATOM   17196 C  CG2 . VAL   E 2 805 ? -6.997  -5.668  -38.980 1.00 177.80 ? 1109 VAL   E CG2 1 
ATOM   17197 N  N   . ALA   E 2 806 ? -8.442  -8.501  -37.441 1.00 161.55 ? 1110 ALA   E N   1 
ATOM   17198 C  CA  . ALA   E 2 806 ? -9.816  -8.736  -37.026 1.00 152.59 ? 1110 ALA   E CA  1 
ATOM   17199 C  C   . ALA   E 2 806 ? -9.876  -9.173  -35.567 1.00 150.69 ? 1110 ALA   E C   1 
ATOM   17200 O  O   . ALA   E 2 806 ? -8.913  -9.718  -35.020 1.00 154.85 ? 1110 ALA   E O   1 
ATOM   17201 C  CB  . ALA   E 2 806 ? -10.463 -9.797  -37.913 1.00 145.90 ? 1110 ALA   E CB  1 
ATOM   17202 N  N   . ASN   E 2 807 ? -11.020 -8.907  -34.935 1.00 145.52 ? 1111 ASN   E N   1 
ATOM   17203 C  CA  . ASN   E 2 807 ? -11.303 -9.311  -33.550 1.00 142.62 ? 1111 ASN   E CA  1 
ATOM   17204 C  C   . ASN   E 2 807 ? -10.225 -8.829  -32.568 1.00 142.67 ? 1111 ASN   E C   1 
ATOM   17205 O  O   . ASN   E 2 807 ? -9.709  -9.579  -31.735 1.00 139.16 ? 1111 ASN   E O   1 
ATOM   17206 C  CB  . ASN   E 2 807 ? -11.502 -10.827 -33.461 1.00 136.36 ? 1111 ASN   E CB  1 
ATOM   17207 C  CG  . ASN   E 2 807 ? -12.861 -11.269 -33.982 1.00 134.66 ? 1111 ASN   E CG  1 
ATOM   17208 O  OD1 . ASN   E 2 807 ? -13.486 -10.569 -34.778 1.00 137.20 ? 1111 ASN   E OD1 1 
ATOM   17209 N  ND2 . ASN   E 2 807 ? -13.330 -12.431 -33.523 1.00 130.28 ? 1111 ASN   E ND2 1 
ATOM   17210 N  N   . LEU   E 2 808 ? -9.906  -7.543  -32.647 1.00 143.13 ? 1112 LEU   E N   1 
ATOM   17211 C  CA  . LEU   E 2 808 ? -8.911  -6.980  -31.753 1.00 142.90 ? 1112 LEU   E CA  1 
ATOM   17212 C  C   . LEU   E 2 808 ? -9.083  -5.467  -31.741 1.00 151.01 ? 1112 LEU   E C   1 
ATOM   17213 O  O   . LEU   E 2 808 ? -9.436  -4.861  -32.761 1.00 151.13 ? 1112 LEU   E O   1 
ATOM   17214 C  CB  . LEU   E 2 808 ? -7.496  -7.377  -32.187 1.00 140.15 ? 1112 LEU   E CB  1 
ATOM   17215 C  CG  . LEU   E 2 808 ? -6.439  -7.278  -31.093 1.00 137.21 ? 1112 LEU   E CG  1 
ATOM   17216 C  CD1 . LEU   E 2 808 ? -6.809  -8.201  -29.952 1.00 137.96 ? 1112 LEU   E CD1 1 
ATOM   17217 C  CD2 . LEU   E 2 808 ? -5.058  -7.612  -31.627 1.00 128.04 ? 1112 LEU   E CD2 1 
ATOM   17218 N  N   . GLN   E 2 809 ? -8.841  -4.864  -30.575 1.00 152.04 ? 1113 GLN   E N   1 
ATOM   17219 C  CA  . GLN   E 2 809 ? -9.021  -3.416  -30.414 1.00 151.59 ? 1113 GLN   E CA  1 
ATOM   17220 C  C   . GLN   E 2 809 ? -8.235  -2.865  -29.212 1.00 153.76 ? 1113 GLN   E C   1 
ATOM   17221 O  O   . GLN   E 2 809 ? -7.777  -3.619  -28.341 1.00 149.19 ? 1113 GLN   E O   1 
ATOM   17222 C  CB  . GLN   E 2 809 ? -10.517 -3.091  -30.277 1.00 151.89 ? 1113 GLN   E CB  1 
ATOM   17223 C  CG  . GLN   E 2 809 ? -10.999 -1.927  -31.124 1.00 151.26 ? 1113 GLN   E CG  1 
ATOM   17224 C  CD  . GLN   E 2 809 ? -10.981 -0.616  -30.364 1.00 154.62 ? 1113 GLN   E CD  1 
ATOM   17225 O  OE1 . GLN   E 2 809 ? -10.827 -0.595  -29.137 1.00 156.28 ? 1113 GLN   E OE1 1 
ATOM   17226 N  NE2 . GLN   E 2 809 ? -11.140 0.491   -31.090 1.00 156.58 ? 1113 GLN   E NE2 1 
ATOM   17227 N  N   . ALA   E 2 820 ? -9.714  -2.878  -34.147 1.00 152.91 ? 1124 ALA   E N   1 
ATOM   17228 C  CA  . ALA   E 2 820 ? -8.574  -2.101  -34.631 1.00 156.12 ? 1124 ALA   E CA  1 
ATOM   17229 C  C   . ALA   E 2 820 ? -8.280  -2.403  -36.105 1.00 161.74 ? 1124 ALA   E C   1 
ATOM   17230 O  O   . ALA   E 2 820 ? -8.147  -3.563  -36.488 1.00 164.88 ? 1124 ALA   E O   1 
ATOM   17231 C  CB  . ALA   E 2 820 ? -7.359  -2.375  -33.781 1.00 149.09 ? 1124 ALA   E CB  1 
ATOM   17232 N  N   . THR   E 2 821 ? -8.189  -1.360  -36.928 1.00 162.15 ? 1125 THR   E N   1 
ATOM   17233 C  CA  . THR   E 2 821 ? -7.992  -1.516  -38.364 1.00 162.57 ? 1125 THR   E CA  1 
ATOM   17234 C  C   . THR   E 2 821 ? -6.513  -1.654  -38.699 1.00 164.37 ? 1125 THR   E C   1 
ATOM   17235 O  O   . THR   E 2 821 ? -5.635  -1.264  -37.927 1.00 163.28 ? 1125 THR   E O   1 
ATOM   17236 C  CB  . THR   E 2 821 ? -8.567  -0.331  -39.145 1.00 165.29 ? 1125 THR   E CB  1 
ATOM   17237 O  OG1 . THR   E 2 821 ? -8.353  -0.541  -40.549 1.00 166.94 ? 1125 THR   E OG1 1 
ATOM   17238 C  CG2 . THR   E 2 821 ? -7.870  0.970   -38.736 1.00 164.39 ? 1125 THR   E CG2 1 
ATOM   17239 N  N   . ALA   E 2 822 ? -6.247  -2.203  -39.889 1.00 170.07 ? 1126 ALA   E N   1 
ATOM   17240 C  CA  . ALA   E 2 822 ? -4.867  -2.362  -40.335 1.00 166.26 ? 1126 ALA   E CA  1 
ATOM   17241 C  C   . ALA   E 2 822 ? -4.100  -1.049  -40.272 1.00 165.49 ? 1126 ALA   E C   1 
ATOM   17242 O  O   . ALA   E 2 822 ? -2.893  -1.043  -40.007 1.00 158.53 ? 1126 ALA   E O   1 
ATOM   17243 C  CB  . ALA   E 2 822 ? -4.839  -2.926  -41.753 1.00 162.70 ? 1126 ALA   E CB  1 
ATOM   17244 N  N   . ASP   E 2 823 ? -4.786  0.072   -40.473 1.00 183.69 ? 1127 ASP   E N   1 
ATOM   17245 C  CA  . ASP   E 2 823 ? -4.091  1.345   -40.568 1.00 183.67 ? 1127 ASP   E CA  1 
ATOM   17246 C  C   . ASP   E 2 823 ? -3.568  1.804   -39.217 1.00 180.32 ? 1127 ASP   E C   1 
ATOM   17247 O  O   . ASP   E 2 823 ? -2.558  2.508   -39.164 1.00 182.23 ? 1127 ASP   E O   1 
ATOM   17248 C  CB  . ASP   E 2 823 ? -5.016  2.388   -41.185 1.00 187.57 ? 1127 ASP   E CB  1 
ATOM   17249 C  CG  . ASP   E 2 823 ? -5.565  1.946   -42.540 1.00 193.12 ? 1127 ASP   E CG  1 
ATOM   17250 O  OD1 . ASP   E 2 823 ? -6.537  1.146   -42.554 1.00 194.41 ? 1127 ASP   E OD1 1 
ATOM   17251 O  OD2 . ASP   E 2 823 ? -5.009  2.373   -43.585 1.00 191.38 ? 1127 ASP   E OD2 1 
ATOM   17252 N  N   . ASP   E 2 824 ? -4.218  1.418   -38.118 1.00 157.04 ? 1128 ASP   E N   1 
ATOM   17253 C  CA  . ASP   E 2 824 ? -3.701  1.813   -36.810 1.00 150.88 ? 1128 ASP   E CA  1 
ATOM   17254 C  C   . ASP   E 2 824 ? -2.602  0.880   -36.300 1.00 146.12 ? 1128 ASP   E C   1 
ATOM   17255 O  O   . ASP   E 2 824 ? -1.833  1.272   -35.409 1.00 138.89 ? 1128 ASP   E O   1 
ATOM   17256 C  CB  . ASP   E 2 824 ? -4.839  1.906   -35.786 1.00 152.41 ? 1128 ASP   E CB  1 
ATOM   17257 C  CG  . ASP   E 2 824 ? -5.507  0.571   -35.525 1.00 152.40 ? 1128 ASP   E CG  1 
ATOM   17258 O  OD1 . ASP   E 2 824 ? -4.867  -0.309  -34.907 1.00 149.90 ? 1128 ASP   E OD1 1 
ATOM   17259 O  OD2 . ASP   E 2 824 ? -6.680  0.411   -35.931 1.00 153.97 ? 1128 ASP   E OD2 1 
ATOM   17260 N  N   . LEU   E 2 825 ? -2.508  -0.342  -36.846 1.00 149.08 ? 1129 LEU   E N   1 
ATOM   17261 C  CA  . LEU   E 2 825 ? -1.395  -1.235  -36.530 1.00 138.88 ? 1129 LEU   E CA  1 
ATOM   17262 C  C   . LEU   E 2 825 ? -0.181  -0.972  -37.409 1.00 129.99 ? 1129 LEU   E C   1 
ATOM   17263 O  O   . LEU   E 2 825 ? 0.948   -1.201  -36.968 1.00 124.09 ? 1129 LEU   E O   1 
ATOM   17264 C  CB  . LEU   E 2 825 ? -1.813  -2.696  -36.666 1.00 139.33 ? 1129 LEU   E CB  1 
ATOM   17265 C  CG  . LEU   E 2 825 ? -2.692  -3.254  -35.549 1.00 139.20 ? 1129 LEU   E CG  1 
ATOM   17266 C  CD1 . LEU   E 2 825 ? -4.173  -3.128  -35.854 1.00 151.48 ? 1129 LEU   E CD1 1 
ATOM   17267 C  CD2 . LEU   E 2 825 ? -2.360  -4.680  -35.368 1.00 134.85 ? 1129 LEU   E CD2 1 
ATOM   17268 N  N   . ILE   E 2 826 ? -0.395  -0.519  -38.651 1.00 136.96 ? 1130 ILE   E N   1 
ATOM   17269 C  CA  . ILE   E 2 826 ? 0.701   0.030   -39.449 1.00 134.62 ? 1130 ILE   E CA  1 
ATOM   17270 C  C   . ILE   E 2 826 ? 1.426   1.107   -38.669 1.00 130.14 ? 1130 ILE   E C   1 
ATOM   17271 O  O   . ILE   E 2 826 ? 2.646   1.266   -38.776 1.00 125.71 ? 1130 ILE   E O   1 
ATOM   17272 C  CB  . ILE   E 2 826 ? 0.178   0.608   -40.775 1.00 136.03 ? 1130 ILE   E CB  1 
ATOM   17273 C  CG1 . ILE   E 2 826 ? -0.409  -0.476  -41.660 1.00 137.70 ? 1130 ILE   E CG1 1 
ATOM   17274 C  CG2 . ILE   E 2 826 ? 1.297   1.350   -41.500 1.00 126.66 ? 1130 ILE   E CG2 1 
ATOM   17275 C  CD1 . ILE   E 2 826 ? -1.357  0.043   -42.700 1.00 147.53 ? 1130 ILE   E CD1 1 
ATOM   17276 N  N   . LYS   E 2 827 ? 0.670   1.897   -37.909 1.00 129.47 ? 1131 LYS   E N   1 
ATOM   17277 C  CA  . LYS   E 2 827 ? 1.255   2.971   -37.125 1.00 124.18 ? 1131 LYS   E CA  1 
ATOM   17278 C  C   . LYS   E 2 827 ? 2.173   2.412   -36.043 1.00 125.92 ? 1131 LYS   E C   1 
ATOM   17279 O  O   . LYS   E 2 827 ? 3.354   2.776   -35.964 1.00 125.72 ? 1131 LYS   E O   1 
ATOM   17280 C  CB  . LYS   E 2 827 ? 0.141   3.826   -36.522 1.00 122.76 ? 1131 LYS   E CB  1 
ATOM   17281 N  N   . VAL   E 2 828 ? 1.653   1.508   -35.205 1.00 124.86 ? 1132 VAL   E N   1 
ATOM   17282 C  CA  . VAL   E 2 828 ? 2.443   1.028   -34.072 1.00 122.67 ? 1132 VAL   E CA  1 
ATOM   17283 C  C   . VAL   E 2 828 ? 3.652   0.228   -34.552 1.00 120.90 ? 1132 VAL   E C   1 
ATOM   17284 O  O   . VAL   E 2 828 ? 4.772   0.421   -34.065 1.00 121.79 ? 1132 VAL   E O   1 
ATOM   17285 C  CB  . VAL   E 2 828 ? 1.573   0.213   -33.099 1.00 121.58 ? 1132 VAL   E CB  1 
ATOM   17286 C  CG1 . VAL   E 2 828 ? 0.748   -0.785  -33.851 1.00 122.00 ? 1132 VAL   E CG1 1 
ATOM   17287 C  CG2 . VAL   E 2 828 ? 2.454   -0.500  -32.083 1.00 117.59 ? 1132 VAL   E CG2 1 
ATOM   17288 N  N   . VAL   E 2 829 ? 3.452   -0.675  -35.522 1.00 120.24 ? 1133 VAL   E N   1 
ATOM   17289 C  CA  . VAL   E 2 829 ? 4.582   -1.475  -35.988 1.00 117.89 ? 1133 VAL   E CA  1 
ATOM   17290 C  C   . VAL   E 2 829 ? 5.621   -0.606  -36.681 1.00 120.72 ? 1133 VAL   E C   1 
ATOM   17291 O  O   . VAL   E 2 829 ? 6.821   -0.891  -36.607 1.00 123.11 ? 1133 VAL   E O   1 
ATOM   17292 C  CB  . VAL   E 2 829 ? 4.115   -2.622  -36.900 1.00 115.35 ? 1133 VAL   E CB  1 
ATOM   17293 C  CG1 . VAL   E 2 829 ? 5.287   -3.498  -37.265 1.00 110.40 ? 1133 VAL   E CG1 1 
ATOM   17294 C  CG2 . VAL   E 2 829 ? 3.093   -3.444  -36.186 1.00 117.07 ? 1133 VAL   E CG2 1 
ATOM   17295 N  N   . GLU   E 2 830 ? 5.193   0.465   -37.358 1.00 125.31 ? 1134 GLU   E N   1 
ATOM   17296 C  CA  . GLU   E 2 830 ? 6.158   1.418   -37.903 1.00 124.65 ? 1134 GLU   E CA  1 
ATOM   17297 C  C   . GLU   E 2 830 ? 7.009   2.015   -36.795 1.00 125.99 ? 1134 GLU   E C   1 
ATOM   17298 O  O   . GLU   E 2 830 ? 8.238   2.095   -36.916 1.00 126.43 ? 1134 GLU   E O   1 
ATOM   17299 C  CB  . GLU   E 2 830 ? 5.446   2.529   -38.668 1.00 126.06 ? 1134 GLU   E CB  1 
ATOM   17300 C  CG  . GLU   E 2 830 ? 5.550   2.430   -40.172 1.00 126.03 ? 1134 GLU   E CG  1 
ATOM   17301 C  CD  . GLU   E 2 830 ? 4.561   3.343   -40.865 1.00 130.99 ? 1134 GLU   E CD  1 
ATOM   17302 O  OE1 . GLU   E 2 830 ? 4.194   4.373   -40.253 1.00 133.66 ? 1134 GLU   E OE1 1 
ATOM   17303 O  OE2 . GLU   E 2 830 ? 4.143   3.028   -42.006 1.00 133.03 ? 1134 GLU   E OE2 1 
ATOM   17304 N  N   . GLU   E 2 831 ? 6.364   2.436   -35.700 1.00 118.15 ? 1135 GLU   E N   1 
ATOM   17305 C  CA  . GLU   E 2 831 ? 7.084   3.013   -34.568 1.00 117.28 ? 1135 GLU   E CA  1 
ATOM   17306 C  C   . GLU   E 2 831 ? 8.114   2.049   -34.003 1.00 117.32 ? 1135 GLU   E C   1 
ATOM   17307 O  O   . GLU   E 2 831 ? 9.174   2.476   -33.520 1.00 114.76 ? 1135 GLU   E O   1 
ATOM   17308 C  CB  . GLU   E 2 831 ? 6.099   3.429   -33.474 1.00 116.74 ? 1135 GLU   E CB  1 
ATOM   17309 C  CG  . GLU   E 2 831 ? 6.712   4.291   -32.375 1.00 121.62 ? 1135 GLU   E CG  1 
ATOM   17310 C  CD  . GLU   E 2 831 ? 7.363   5.573   -32.911 1.00 131.54 ? 1135 GLU   E CD  1 
ATOM   17311 O  OE1 . GLU   E 2 831 ? 7.194   5.905   -34.112 1.00 125.79 ? 1135 GLU   E OE1 1 
ATOM   17312 O  OE2 . GLU   E 2 831 ? 8.052   6.258   -32.118 1.00 138.91 ? 1135 GLU   E OE2 1 
ATOM   17313 N  N   . LEU   E 2 832 ? 7.825   0.748   -34.051 1.00 115.39 ? 1136 LEU   E N   1 
ATOM   17314 C  CA  . LEU   E 2 832 ? 8.811   -0.224  -33.613 1.00 112.82 ? 1136 LEU   E CA  1 
ATOM   17315 C  C   . LEU   E 2 832 ? 10.045  -0.206  -34.528 1.00 115.45 ? 1136 LEU   E C   1 
ATOM   17316 O  O   . LEU   E 2 832 ? 11.180  -0.299  -34.038 1.00 116.06 ? 1136 LEU   E O   1 
ATOM   17317 C  CB  . LEU   E 2 832 ? 8.155   -1.608  -33.498 1.00 106.56 ? 1136 LEU   E CB  1 
ATOM   17318 C  CG  . LEU   E 2 832 ? 6.901   -1.673  -32.583 1.00 102.83 ? 1136 LEU   E CG  1 
ATOM   17319 C  CD1 . LEU   E 2 832 ? 6.282   -3.064  -32.498 1.00 102.80 ? 1136 LEU   E CD1 1 
ATOM   17320 C  CD2 . LEU   E 2 832 ? 7.172   -1.183  -31.181 1.00 101.20 ? 1136 LEU   E CD2 1 
ATOM   17321 N  N   . THR   E 2 833 ? 9.856   -0.011  -35.853 1.00 114.16 ? 1137 THR   E N   1 
ATOM   17322 C  CA  . THR   E 2 833 ? 10.990  0.077   -36.782 1.00 113.85 ? 1137 THR   E CA  1 
ATOM   17323 C  C   . THR   E 2 833 ? 11.873  1.309   -36.542 1.00 114.57 ? 1137 THR   E C   1 
ATOM   17324 O  O   . THR   E 2 833 ? 12.891  1.475   -37.231 1.00 110.16 ? 1137 THR   E O   1 
ATOM   17325 C  CB  . THR   E 2 833 ? 10.513  0.069   -38.243 1.00 110.95 ? 1137 THR   E CB  1 
ATOM   17326 O  OG1 . THR   E 2 833 ? 9.994   1.356   -38.596 1.00 115.96 ? 1137 THR   E OG1 1 
ATOM   17327 C  CG2 . THR   E 2 833 ? 9.437   -0.967  -38.454 1.00 113.18 ? 1137 THR   E CG2 1 
ATOM   17328 N  N   . ARG   E 2 834 ? 11.539  2.165   -35.578 1.00 110.02 ? 1138 ARG   E N   1 
ATOM   17329 C  CA  . ARG   E 2 834 ? 12.306  3.372   -35.330 1.00 107.09 ? 1138 ARG   E CA  1 
ATOM   17330 C  C   . ARG   E 2 834 ? 13.219  3.244   -34.116 1.00 107.72 ? 1138 ARG   E C   1 
ATOM   17331 O  O   . ARG   E 2 834 ? 13.855  4.228   -33.721 1.00 109.15 ? 1138 ARG   E O   1 
ATOM   17332 C  CB  . ARG   E 2 834 ? 11.357  4.569   -35.191 1.00 114.64 ? 1138 ARG   E CB  1 
ATOM   17333 C  CG  . ARG   E 2 834 ? 10.889  5.153   -36.557 1.00 115.75 ? 1138 ARG   E CG  1 
ATOM   17334 C  CD  . ARG   E 2 834 ? 9.378   5.356   -36.642 1.00 116.28 ? 1138 ARG   E CD  1 
ATOM   17335 N  NE  . ARG   E 2 834 ? 8.927   5.807   -37.960 1.00 121.65 ? 1138 ARG   E NE  1 
ATOM   17336 C  CZ  . ARG   E 2 834 ? 8.762   5.023   -39.022 1.00 125.77 ? 1138 ARG   E CZ  1 
ATOM   17337 N  NH1 . ARG   E 2 834 ? 9.114   3.745   -39.006 1.00 123.94 ? 1138 ARG   E NH1 1 
ATOM   17338 N  NH2 . ARG   E 2 834 ? 8.227   5.534   -40.130 1.00 123.31 ? 1138 ARG   E NH2 1 
ATOM   17339 N  N   . ILE   E 2 835 ? 13.315  2.047   -33.520 1.00 107.16 ? 1139 ILE   E N   1 
ATOM   17340 C  CA  . ILE   E 2 835 ? 14.338  1.811   -32.501 1.00 103.77 ? 1139 ILE   E CA  1 
ATOM   17341 C  C   . ILE   E 2 835 ? 15.656  1.357   -33.123 1.00 100.27 ? 1139 ILE   E C   1 
ATOM   17342 O  O   . ILE   E 2 835 ? 16.694  1.372   -32.445 1.00 98.80  ? 1139 ILE   E O   1 
ATOM   17343 C  CB  . ILE   E 2 835 ? 13.859  0.801   -31.438 1.00 101.18 ? 1139 ILE   E CB  1 
ATOM   17344 C  CG1 . ILE   E 2 835 ? 13.506  -0.527  -32.068 1.00 98.60  ? 1139 ILE   E CG1 1 
ATOM   17345 C  CG2 . ILE   E 2 835 ? 12.628  1.301   -30.721 1.00 103.96 ? 1139 ILE   E CG2 1 
ATOM   17346 C  CD1 . ILE   E 2 835 ? 12.994  -1.505  -31.050 1.00 101.12 ? 1139 ILE   E CD1 1 
ATOM   17347 N  N   . HIS   E 2 836 ? 15.652  0.970   -34.393 1.00 100.57 ? 1140 HIS   E N   1 
ATOM   17348 C  CA  . HIS   E 2 836 ? 16.884  0.695   -35.115 1.00 98.13  ? 1140 HIS   E CA  1 
ATOM   17349 C  C   . HIS   E 2 836 ? 16.822  1.275   -36.532 1.00 104.80 ? 1140 HIS   E C   1 
ATOM   17350 O  O   . HIS   E 2 836 ? 17.368  0.705   -37.485 1.00 108.74 ? 1140 HIS   E O   1 
ATOM   17351 C  CB  . HIS   E 2 836 ? 17.148  -0.805  -35.167 1.00 95.19  ? 1140 HIS   E CB  1 
ATOM   17352 C  CG  . HIS   E 2 836 ? 16.167  -1.579  -36.003 1.00 96.34  ? 1140 HIS   E CG  1 
ATOM   17353 N  ND1 . HIS   E 2 836 ? 16.500  -2.137  -37.222 1.00 94.36  ? 1140 HIS   E ND1 1 
ATOM   17354 C  CD2 . HIS   E 2 836 ? 14.870  -1.904  -35.785 1.00 97.13  ? 1140 HIS   E CD2 1 
ATOM   17355 C  CE1 . HIS   E 2 836 ? 15.450  -2.770  -37.716 1.00 95.70  ? 1140 HIS   E CE1 1 
ATOM   17356 N  NE2 . HIS   E 2 836 ? 14.448  -2.643  -36.864 1.00 96.63  ? 1140 HIS   E NE2 1 
ATOM   17357 N  N   . SER   F 3 3   ? 37.236  -57.301 29.091  1.00 114.65 ? 868  SER   F N   1 
ATOM   17358 C  CA  . SER   F 3 3   ? 36.079  -58.144 28.781  1.00 121.21 ? 868  SER   F CA  1 
ATOM   17359 C  C   . SER   F 3 3   ? 34.763  -57.353 28.780  1.00 122.47 ? 868  SER   F C   1 
ATOM   17360 O  O   . SER   F 3 3   ? 34.212  -57.055 27.723  1.00 116.60 ? 868  SER   F O   1 
ATOM   17361 C  CB  . SER   F 3 3   ? 35.988  -59.308 29.776  1.00 126.76 ? 868  SER   F CB  1 
ATOM   17362 O  OG  . SER   F 3 3   ? 37.234  -59.988 29.899  1.00 129.82 ? 868  SER   F OG  1 
ATOM   17363 N  N   . LEU   F 3 4   ? 34.250  -57.026 29.968  1.00 132.14 ? 869  LEU   F N   1 
ATOM   17364 C  CA  . LEU   F 3 4   ? 33.037  -56.221 30.109  1.00 129.95 ? 869  LEU   F CA  1 
ATOM   17365 C  C   . LEU   F 3 4   ? 33.313  -54.722 30.146  1.00 130.42 ? 869  LEU   F C   1 
ATOM   17366 O  O   . LEU   F 3 4   ? 32.391  -53.939 30.393  1.00 131.14 ? 869  LEU   F O   1 
ATOM   17367 C  CB  . LEU   F 3 4   ? 32.263  -56.625 31.368  1.00 130.52 ? 869  LEU   F CB  1 
ATOM   17368 C  CG  . LEU   F 3 4   ? 31.284  -57.777 31.157  1.00 135.00 ? 869  LEU   F CG  1 
ATOM   17369 C  CD1 . LEU   F 3 4   ? 30.276  -57.807 32.288  1.00 135.21 ? 869  LEU   F CD1 1 
ATOM   17370 C  CD2 . LEU   F 3 4   ? 30.594  -57.647 29.797  1.00 135.44 ? 869  LEU   F CD2 1 
ATOM   17371 N  N   . THR   F 3 5   ? 34.558  -54.307 29.908  1.00 122.15 ? 870  THR   F N   1 
ATOM   17372 C  CA  . THR   F 3 5   ? 34.935  -52.899 29.930  1.00 113.65 ? 870  THR   F CA  1 
ATOM   17373 C  C   . THR   F 3 5   ? 35.733  -52.494 28.703  1.00 114.36 ? 870  THR   F C   1 
ATOM   17374 O  O   . THR   F 3 5   ? 36.480  -51.514 28.770  1.00 109.80 ? 870  THR   F O   1 
ATOM   17375 C  CB  . THR   F 3 5   ? 35.762  -52.570 31.163  1.00 118.21 ? 870  THR   F CB  1 
ATOM   17376 O  OG1 . THR   F 3 5   ? 36.866  -53.485 31.242  1.00 121.50 ? 870  THR   F OG1 1 
ATOM   17377 C  CG2 . THR   F 3 5   ? 34.916  -52.666 32.419  1.00 124.18 ? 870  THR   F CG2 1 
ATOM   17378 N  N   . THR   F 3 6   ? 35.640  -53.257 27.611  1.00 117.40 ? 871  THR   F N   1 
ATOM   17379 C  CA  . THR   F 3 6   ? 36.179  -52.861 26.317  1.00 108.70 ? 871  THR   F CA  1 
ATOM   17380 C  C   . THR   F 3 6   ? 35.062  -52.263 25.471  1.00 106.33 ? 871  THR   F C   1 
ATOM   17381 O  O   . THR   F 3 6   ? 33.889  -52.626 25.594  1.00 105.97 ? 871  THR   F O   1 
ATOM   17382 C  CB  . THR   F 3 6   ? 36.835  -54.037 25.568  1.00 109.40 ? 871  THR   F CB  1 
ATOM   17383 O  OG1 . THR   F 3 6   ? 35.838  -54.849 24.934  1.00 109.69 ? 871  THR   F OG1 1 
ATOM   17384 C  CG2 . THR   F 3 6   ? 37.649  -54.898 26.517  1.00 110.93 ? 871  THR   F CG2 1 
ATOM   17385 N  N   . CYS   F 3 7   ? 35.443  -51.340 24.605  1.00 107.61 ? 872  CYS   F N   1 
ATOM   17386 C  CA  . CYS   F 3 7   ? 34.484  -50.550 23.847  1.00 103.20 ? 872  CYS   F CA  1 
ATOM   17387 C  C   . CYS   F 3 7   ? 34.232  -51.172 22.481  1.00 104.73 ? 872  CYS   F C   1 
ATOM   17388 O  O   . CYS   F 3 7   ? 35.166  -51.570 21.774  1.00 103.09 ? 872  CYS   F O   1 
ATOM   17389 C  CB  . CYS   F 3 7   ? 34.991  -49.120 23.675  1.00 99.68  ? 872  CYS   F CB  1 
ATOM   17390 S  SG  . CYS   F 3 7   ? 33.938  -48.063 22.650  1.00 96.02  ? 872  CYS   F SG  1 
ATOM   17391 N  N   . GLU   F 3 8   ? 32.959  -51.234 22.103  1.00 110.30 ? 873  GLU   F N   1 
ATOM   17392 C  CA  . GLU   F 3 8   ? 32.604  -51.917 20.870  1.00 108.14 ? 873  GLU   F CA  1 
ATOM   17393 C  C   . GLU   F 3 8   ? 32.965  -51.117 19.636  1.00 105.91 ? 873  GLU   F C   1 
ATOM   17394 O  O   . GLU   F 3 8   ? 33.133  -51.704 18.565  1.00 106.19 ? 873  GLU   F O   1 
ATOM   17395 C  CB  . GLU   F 3 8   ? 31.114  -52.230 20.867  1.00 111.22 ? 873  GLU   F CB  1 
ATOM   17396 C  CG  . GLU   F 3 8   ? 30.666  -52.772 22.204  1.00 117.15 ? 873  GLU   F CG  1 
ATOM   17397 C  CD  . GLU   F 3 8   ? 29.693  -53.911 22.055  1.00 120.71 ? 873  GLU   F CD  1 
ATOM   17398 O  OE1 . GLU   F 3 8   ? 28.800  -53.796 21.175  1.00 124.77 ? 873  GLU   F OE1 1 
ATOM   17399 O  OE2 . GLU   F 3 8   ? 29.831  -54.910 22.809  1.00 117.37 ? 873  GLU   F OE2 1 
ATOM   17400 N  N   . VAL   F 3 9   ? 33.099  -49.801 19.751  1.00 99.64  ? 874  VAL   F N   1 
ATOM   17401 C  CA  . VAL   F 3 9   ? 33.282  -48.979 18.561  1.00 97.51  ? 874  VAL   F CA  1 
ATOM   17402 C  C   . VAL   F 3 9   ? 34.751  -48.832 18.196  1.00 98.20  ? 874  VAL   F C   1 
ATOM   17403 O  O   . VAL   F 3 9   ? 35.130  -48.981 17.035  1.00 97.90  ? 874  VAL   F O   1 
ATOM   17404 C  CB  . VAL   F 3 9   ? 32.614  -47.608 18.753  1.00 94.75  ? 874  VAL   F CB  1 
ATOM   17405 C  CG1 . VAL   F 3 9   ? 32.844  -46.741 17.513  1.00 93.00  ? 874  VAL   F CG1 1 
ATOM   17406 C  CG2 . VAL   F 3 9   ? 31.144  -47.787 19.040  1.00 95.06  ? 874  VAL   F CG2 1 
ATOM   17407 N  N   . CYS   F 3 10  ? 35.618  -48.541 19.158  1.00 99.72  ? 875  CYS   F N   1 
ATOM   17408 C  CA  . CYS   F 3 10  ? 37.016  -48.327 18.836  1.00 93.17  ? 875  CYS   F CA  1 
ATOM   17409 C  C   . CYS   F 3 10  ? 37.954  -49.327 19.481  1.00 97.23  ? 875  CYS   F C   1 
ATOM   17410 O  O   . CYS   F 3 10  ? 39.098  -49.429 19.045  1.00 100.42 ? 875  CYS   F O   1 
ATOM   17411 C  CB  . CYS   F 3 10  ? 37.446  -46.923 19.268  1.00 94.74  ? 875  CYS   F CB  1 
ATOM   17412 S  SG  . CYS   F 3 10  ? 37.444  -46.769 21.093  1.00 92.10  ? 875  CYS   F SG  1 
ATOM   17413 N  N   . GLY   F 3 11  ? 37.517  -50.045 20.513  1.00 103.97 ? 876  GLY   F N   1 
ATOM   17414 C  CA  . GLY   F 3 11  ? 38.352  -51.058 21.139  1.00 107.45 ? 876  GLY   F CA  1 
ATOM   17415 C  C   . GLY   F 3 11  ? 39.080  -50.629 22.396  1.00 108.40 ? 876  GLY   F C   1 
ATOM   17416 O  O   . GLY   F 3 11  ? 39.863  -51.422 22.941  1.00 109.14 ? 876  GLY   F O   1 
ATOM   17417 N  N   . ALA   F 3 12  ? 38.845  -49.404 22.869  1.00 102.54 ? 877  ALA   F N   1 
ATOM   17418 C  CA  . ALA   F 3 12  ? 39.469  -48.918 24.092  1.00 102.55 ? 877  ALA   F CA  1 
ATOM   17419 C  C   . ALA   F 3 12  ? 39.049  -49.756 25.291  1.00 104.44 ? 877  ALA   F C   1 
ATOM   17420 O  O   . ALA   F 3 12  ? 37.859  -49.993 25.513  1.00 106.13 ? 877  ALA   F O   1 
ATOM   17421 C  CB  . ALA   F 3 12  ? 39.088  -47.459 24.313  1.00 101.54 ? 877  ALA   F CB  1 
ATOM   17422 N  N   . CYS   F 3 13  ? 40.028  -50.208 26.062  1.00 105.43 ? 878  CYS   F N   1 
ATOM   17423 C  CA  . CYS   F 3 13  ? 39.784  -51.101 27.184  1.00 108.73 ? 878  CYS   F CA  1 
ATOM   17424 C  C   . CYS   F 3 13  ? 39.923  -50.320 28.482  1.00 110.68 ? 878  CYS   F C   1 
ATOM   17425 O  O   . CYS   F 3 13  ? 40.995  -49.785 28.777  1.00 112.91 ? 878  CYS   F O   1 
ATOM   17426 C  CB  . CYS   F 3 13  ? 40.746  -52.286 27.161  1.00 109.19 ? 878  CYS   F CB  1 
ATOM   17427 S  SG  . CYS   F 3 13  ? 40.300  -53.574 28.325  1.00 123.54 ? 878  CYS   F SG  1 
ATOM   17428 N  N   . PHE   F 3 14  ? 38.847  -50.254 29.254  1.00 112.92 ? 879  PHE   F N   1 
ATOM   17429 C  CA  . PHE   F 3 14  ? 38.848  -49.486 30.488  1.00 116.38 ? 879  PHE   F CA  1 
ATOM   17430 C  C   . PHE   F 3 14  ? 38.980  -50.400 31.698  1.00 122.57 ? 879  PHE   F C   1 
ATOM   17431 O  O   . PHE   F 3 14  ? 38.718  -51.604 31.629  1.00 122.35 ? 879  PHE   F O   1 
ATOM   17432 C  CB  . PHE   F 3 14  ? 37.584  -48.640 30.591  1.00 113.53 ? 879  PHE   F CB  1 
ATOM   17433 C  CG  . PHE   F 3 14  ? 37.567  -47.525 29.625  1.00 109.44 ? 879  PHE   F CG  1 
ATOM   17434 C  CD1 . PHE   F 3 14  ? 38.090  -46.304 29.967  1.00 108.68 ? 879  PHE   F CD1 1 
ATOM   17435 C  CD2 . PHE   F 3 14  ? 37.100  -47.718 28.344  1.00 111.09 ? 879  PHE   F CD2 1 
ATOM   17436 C  CE1 . PHE   F 3 14  ? 38.107  -45.276 29.070  1.00 111.82 ? 879  PHE   F CE1 1 
ATOM   17437 C  CE2 . PHE   F 3 14  ? 37.115  -46.691 27.427  1.00 111.47 ? 879  PHE   F CE2 1 
ATOM   17438 C  CZ  . PHE   F 3 14  ? 37.622  -45.468 27.791  1.00 112.61 ? 879  PHE   F CZ  1 
ATOM   17439 N  N   . GLU   F 3 15  ? 39.425  -49.810 32.811  1.00 121.15 ? 880  GLU   F N   1 
ATOM   17440 C  CA  . GLU   F 3 15  ? 39.566  -50.582 34.034  1.00 115.90 ? 880  GLU   F CA  1 
ATOM   17441 C  C   . GLU   F 3 15  ? 38.263  -50.641 34.802  1.00 117.62 ? 880  GLU   F C   1 
ATOM   17442 O  O   . GLU   F 3 15  ? 38.023  -51.597 35.545  1.00 129.38 ? 880  GLU   F O   1 
ATOM   17443 C  CB  . GLU   F 3 15  ? 40.648  -49.973 34.922  1.00 120.42 ? 880  GLU   F CB  1 
ATOM   17444 C  CG  . GLU   F 3 15  ? 42.045  -50.014 34.362  1.00 124.43 ? 880  GLU   F CG  1 
ATOM   17445 C  CD  . GLU   F 3 15  ? 43.050  -49.330 35.280  1.00 131.79 ? 880  GLU   F CD  1 
ATOM   17446 O  OE1 . GLU   F 3 15  ? 42.936  -49.483 36.520  1.00 135.81 ? 880  GLU   F OE1 1 
ATOM   17447 O  OE2 . GLU   F 3 15  ? 43.949  -48.628 34.762  1.00 134.42 ? 880  GLU   F OE2 1 
ATOM   17448 N  N   . THR   F 3 16  ? 37.432  -49.620 34.675  1.00 123.38 ? 881  THR   F N   1 
ATOM   17449 C  CA  . THR   F 3 16  ? 36.179  -49.563 35.407  1.00 124.85 ? 881  THR   F CA  1 
ATOM   17450 C  C   . THR   F 3 16  ? 35.019  -49.484 34.432  1.00 121.12 ? 881  THR   F C   1 
ATOM   17451 O  O   . THR   F 3 16  ? 35.150  -48.938 33.341  1.00 120.42 ? 881  THR   F O   1 
ATOM   17452 C  CB  . THR   F 3 16  ? 36.117  -48.359 36.327  1.00 124.24 ? 881  THR   F CB  1 
ATOM   17453 O  OG1 . THR   F 3 16  ? 34.801  -48.275 36.894  1.00 126.92 ? 881  THR   F OG1 1 
ATOM   17454 C  CG2 . THR   F 3 16  ? 36.397  -47.099 35.515  1.00 119.35 ? 881  THR   F CG2 1 
ATOM   17455 N  N   . ARG   F 3 17  ? 33.874  -50.011 34.840  1.00 115.28 ? 882  ARG   F N   1 
ATOM   17456 C  CA  . ARG   F 3 17  ? 32.704  -49.857 34.001  1.00 108.86 ? 882  ARG   F CA  1 
ATOM   17457 C  C   . ARG   F 3 17  ? 32.302  -48.384 33.837  1.00 115.21 ? 882  ARG   F C   1 
ATOM   17458 O  O   . ARG   F 3 17  ? 31.592  -48.062 32.877  1.00 113.62 ? 882  ARG   F O   1 
ATOM   17459 C  CB  . ARG   F 3 17  ? 31.556  -50.701 34.568  1.00 104.20 ? 882  ARG   F CB  1 
ATOM   17460 N  N   . LYS   F 3 18  ? 32.750  -47.473 34.722  1.00 114.42 ? 883  LYS   F N   1 
ATOM   17461 C  CA  . LYS   F 3 18  ? 32.486  -46.047 34.481  1.00 114.51 ? 883  LYS   F CA  1 
ATOM   17462 C  C   . LYS   F 3 18  ? 33.369  -45.507 33.363  1.00 116.30 ? 883  LYS   F C   1 
ATOM   17463 O  O   . LYS   F 3 18  ? 32.950  -44.620 32.603  1.00 113.78 ? 883  LYS   F O   1 
ATOM   17464 C  CB  . LYS   F 3 18  ? 32.694  -45.206 35.744  1.00 120.04 ? 883  LYS   F CB  1 
ATOM   17465 N  N   . GLY   F 3 19  ? 34.606  -46.004 33.272  1.00 121.92 ? 884  GLY   F N   1 
ATOM   17466 C  CA  . GLY   F 3 19  ? 35.461  -45.655 32.146  1.00 118.81 ? 884  GLY   F CA  1 
ATOM   17467 C  C   . GLY   F 3 19  ? 34.786  -45.918 30.820  1.00 113.60 ? 884  GLY   F C   1 
ATOM   17468 O  O   . GLY   F 3 19  ? 34.806  -45.078 29.924  1.00 116.97 ? 884  GLY   F O   1 
ATOM   17469 N  N   . LEU   F 3 20  ? 34.098  -47.052 30.714  1.00 106.02 ? 885  LEU   F N   1 
ATOM   17470 C  CA  . LEU   F 3 20  ? 33.327  -47.325 29.519  1.00 101.57 ? 885  LEU   F CA  1 
ATOM   17471 C  C   . LEU   F 3 20  ? 32.167  -46.365 29.380  1.00 106.01 ? 885  LEU   F C   1 
ATOM   17472 O  O   . LEU   F 3 20  ? 31.955  -45.798 28.308  1.00 111.78 ? 885  LEU   F O   1 
ATOM   17473 C  CB  . LEU   F 3 20  ? 32.801  -48.744 29.525  1.00 102.63 ? 885  LEU   F CB  1 
ATOM   17474 C  CG  . LEU   F 3 20  ? 33.500  -49.641 28.526  1.00 108.27 ? 885  LEU   F CG  1 
ATOM   17475 C  CD1 . LEU   F 3 20  ? 32.614  -50.813 28.259  1.00 118.07 ? 885  LEU   F CD1 1 
ATOM   17476 C  CD2 . LEU   F 3 20  ? 33.770  -48.895 27.255  1.00 101.54 ? 885  LEU   F CD2 1 
ATOM   17477 N  N   . SER   F 3 21  ? 31.392  -46.172 30.445  1.00 103.58 ? 886  SER   F N   1 
ATOM   17478 C  CA  . SER   F 3 21  ? 30.239  -45.288 30.332  1.00 103.27 ? 886  SER   F CA  1 
ATOM   17479 C  C   . SER   F 3 21  ? 30.642  -43.913 29.802  1.00 102.00 ? 886  SER   F C   1 
ATOM   17480 O  O   . SER   F 3 21  ? 30.020  -43.391 28.870  1.00 103.44 ? 886  SER   F O   1 
ATOM   17481 C  CB  . SER   F 3 21  ? 29.546  -45.145 31.677  1.00 107.96 ? 886  SER   F CB  1 
ATOM   17482 O  OG  . SER   F 3 21  ? 30.179  -44.110 32.411  1.00 113.54 ? 886  SER   F OG  1 
ATOM   17483 N  N   . SER   F 3 22  ? 31.696  -43.317 30.371  1.00 101.31 ? 887  SER   F N   1 
ATOM   17484 C  CA  . SER   F 3 22  ? 32.139  -42.005 29.902  1.00 100.60 ? 887  SER   F CA  1 
ATOM   17485 C  C   . SER   F 3 22  ? 32.536  -42.046 28.425  1.00 105.31 ? 887  SER   F C   1 
ATOM   17486 O  O   . SER   F 3 22  ? 32.082  -41.214 27.626  1.00 106.38 ? 887  SER   F O   1 
ATOM   17487 C  CB  . SER   F 3 22  ? 33.299  -41.500 30.751  1.00 96.78  ? 887  SER   F CB  1 
ATOM   17488 O  OG  . SER   F 3 22  ? 34.481  -42.207 30.445  1.00 100.70 ? 887  SER   F OG  1 
ATOM   17489 N  N   . HIS   F 3 23  ? 33.383  -43.015 28.043  1.00 103.33 ? 888  HIS   F N   1 
ATOM   17490 C  CA  . HIS   F 3 23  ? 33.837  -43.135 26.655  1.00 101.29 ? 888  HIS   F CA  1 
ATOM   17491 C  C   . HIS   F 3 23  ? 32.683  -43.284 25.671  1.00 101.60 ? 888  HIS   F C   1 
ATOM   17492 O  O   . HIS   F 3 23  ? 32.806  -42.906 24.498  1.00 101.72 ? 888  HIS   F O   1 
ATOM   17493 C  CB  . HIS   F 3 23  ? 34.779  -44.334 26.518  1.00 99.71  ? 888  HIS   F CB  1 
ATOM   17494 C  CG  . HIS   F 3 23  ? 35.350  -44.515 25.141  1.00 99.78  ? 888  HIS   F CG  1 
ATOM   17495 N  ND1 . HIS   F 3 23  ? 35.748  -43.454 24.352  1.00 100.68 ? 888  HIS   F ND1 1 
ATOM   17496 C  CD2 . HIS   F 3 23  ? 35.601  -45.633 24.420  1.00 98.91  ? 888  HIS   F CD2 1 
ATOM   17497 C  CE1 . HIS   F 3 23  ? 36.214  -43.911 23.205  1.00 96.87  ? 888  HIS   F CE1 1 
ATOM   17498 N  NE2 . HIS   F 3 23  ? 36.139  -45.229 23.223  1.00 95.55  ? 888  HIS   F NE2 1 
ATOM   17499 N  N   . ALA   F 3 24  ? 31.568  -43.857 26.120  1.00 100.56 ? 889  ALA   F N   1 
ATOM   17500 C  CA  . ALA   F 3 24  ? 30.402  -43.962 25.261  1.00 102.00 ? 889  ALA   F CA  1 
ATOM   17501 C  C   . ALA   F 3 24  ? 29.875  -42.586 24.855  1.00 105.16 ? 889  ALA   F C   1 
ATOM   17502 O  O   . ALA   F 3 24  ? 29.241  -42.459 23.804  1.00 111.65 ? 889  ALA   F O   1 
ATOM   17503 C  CB  . ALA   F 3 24  ? 29.325  -44.784 25.966  1.00 101.36 ? 889  ALA   F CB  1 
ATOM   17504 N  N   . ARG   F 3 25  ? 30.139  -41.541 25.645  1.00 100.87 ? 890  ARG   F N   1 
ATOM   17505 C  CA  . ARG   F 3 25  ? 29.815  -40.201 25.168  1.00 101.09 ? 890  ARG   F CA  1 
ATOM   17506 C  C   . ARG   F 3 25  ? 30.739  -39.783 24.028  1.00 105.20 ? 890  ARG   F C   1 
ATOM   17507 O  O   . ARG   F 3 25  ? 30.275  -39.255 23.014  1.00 111.33 ? 890  ARG   F O   1 
ATOM   17508 C  CB  . ARG   F 3 25  ? 29.889  -39.190 26.308  1.00 104.24 ? 890  ARG   F CB  1 
ATOM   17509 N  N   . SER   F 3 26  ? 32.048  -40.023 24.172  1.00 103.00 ? 891  SER   F N   1 
ATOM   17510 C  CA  . SER   F 3 26  ? 33.020  -39.668 23.134  1.00 105.85 ? 891  SER   F CA  1 
ATOM   17511 C  C   . SER   F 3 26  ? 32.553  -40.086 21.739  1.00 110.64 ? 891  SER   F C   1 
ATOM   17512 O  O   . SER   F 3 26  ? 32.760  -39.365 20.753  1.00 113.68 ? 891  SER   F O   1 
ATOM   17513 C  CB  . SER   F 3 26  ? 34.380  -40.305 23.456  1.00 99.56  ? 891  SER   F CB  1 
ATOM   17514 O  OG  . SER   F 3 26  ? 35.174  -40.465 22.286  1.00 94.92  ? 891  SER   F OG  1 
ATOM   17515 N  N   . HIS   F 3 27  ? 31.892  -41.238 21.649  1.00 112.08 ? 892  HIS   F N   1 
ATOM   17516 C  CA  . HIS   F 3 27  ? 31.518  -41.829 20.373  1.00 113.11 ? 892  HIS   F CA  1 
ATOM   17517 C  C   . HIS   F 3 27  ? 30.158  -41.383 19.883  1.00 115.55 ? 892  HIS   F C   1 
ATOM   17518 O  O   . HIS   F 3 27  ? 29.775  -41.748 18.771  1.00 125.88 ? 892  HIS   F O   1 
ATOM   17519 C  CB  . HIS   F 3 27  ? 31.522  -43.352 20.477  1.00 104.99 ? 892  HIS   F CB  1 
ATOM   17520 C  CG  . HIS   F 3 27  ? 32.868  -43.958 20.309  1.00 98.52  ? 892  HIS   F CG  1 
ATOM   17521 N  ND1 . HIS   F 3 27  ? 33.675  -43.670 19.230  1.00 104.47 ? 892  HIS   F ND1 1 
ATOM   17522 C  CD2 . HIS   F 3 27  ? 33.552  -44.838 21.072  1.00 96.79  ? 892  HIS   F CD2 1 
ATOM   17523 C  CE1 . HIS   F 3 27  ? 34.803  -44.348 19.338  1.00 104.52 ? 892  HIS   F CE1 1 
ATOM   17524 N  NE2 . HIS   F 3 27  ? 34.755  -45.063 20.447  1.00 100.01 ? 892  HIS   F NE2 1 
ATOM   17525 N  N   . LEU   F 3 28  ? 29.408  -40.634 20.674  1.00 111.18 ? 893  LEU   F N   1 
ATOM   17526 C  CA  . LEU   F 3 28  ? 28.142  -40.149 20.156  1.00 121.65 ? 893  LEU   F CA  1 
ATOM   17527 C  C   . LEU   F 3 28  ? 28.417  -38.928 19.275  1.00 138.38 ? 893  LEU   F C   1 
ATOM   17528 O  O   . LEU   F 3 28  ? 28.140  -37.782 19.662  1.00 132.93 ? 893  LEU   F O   1 
ATOM   17529 C  CB  . LEU   F 3 28  ? 27.172  -39.866 21.305  1.00 118.63 ? 893  LEU   F CB  1 
ATOM   17530 C  CG  . LEU   F 3 28  ? 26.937  -41.106 22.201  1.00 114.97 ? 893  LEU   F CG  1 
ATOM   17531 C  CD1 . LEU   F 3 28  ? 25.957  -40.856 23.374  1.00 107.93 ? 893  LEU   F CD1 1 
ATOM   17532 C  CD2 . LEU   F 3 28  ? 26.550  -42.362 21.396  1.00 105.49 ? 893  LEU   F CD2 1 
ATOM   17533 N  N   . ARG   F 3 29  ? 29.024  -39.194 18.105  1.00 164.67 ? 894  ARG   F N   1 
ATOM   17534 C  CA  . ARG   F 3 29  ? 29.181  -38.262 16.971  1.00 162.91 ? 894  ARG   F CA  1 
ATOM   17535 C  C   . ARG   F 3 29  ? 28.218  -38.693 15.872  1.00 163.84 ? 894  ARG   F C   1 
ATOM   17536 O  O   . ARG   F 3 29  ? 28.397  -39.761 15.273  1.00 161.11 ? 894  ARG   F O   1 
ATOM   17537 C  CB  . ARG   F 3 29  ? 30.613  -38.259 16.405  1.00 157.76 ? 894  ARG   F CB  1 
ATOM   17538 C  CG  . ARG   F 3 29  ? 31.707  -37.890 17.380  1.00 158.16 ? 894  ARG   F CG  1 
ATOM   17539 C  CD  . ARG   F 3 29  ? 33.060  -38.166 16.773  1.00 158.21 ? 894  ARG   F CD  1 
ATOM   17540 N  NE  . ARG   F 3 29  ? 33.153  -39.541 16.290  1.00 159.12 ? 894  ARG   F NE  1 
ATOM   17541 C  CZ  . ARG   F 3 29  ? 33.711  -40.542 16.966  1.00 159.63 ? 894  ARG   F CZ  1 
ATOM   17542 N  NH1 . ARG   F 3 29  ? 34.240  -40.353 18.166  1.00 159.27 ? 894  ARG   F NH1 1 
ATOM   17543 N  NH2 . ARG   F 3 29  ? 33.749  -41.761 16.420  1.00 159.78 ? 894  ARG   F NH2 1 
HETATM 17544 ZN ZN  . ZN    G 4 .   ? 16.400  38.781  -61.914 1.00 88.54  2 501  ZN    A ZN  1 
HETATM 17545 S  S   . SO4   H 5 .   ? 10.118  42.131  -32.154 1.00 131.82 ? 502  SO4   A S   1 
HETATM 17546 O  O1  . SO4   H 5 .   ? 10.660  41.658  -33.487 1.00 106.80 ? 502  SO4   A O1  1 
HETATM 17547 O  O2  . SO4   H 5 .   ? 11.295  42.558  -31.304 1.00 111.79 ? 502  SO4   A O2  1 
HETATM 17548 O  O3  . SO4   H 5 .   ? 9.152   43.295  -32.301 1.00 120.01 ? 502  SO4   A O3  1 
HETATM 17549 O  O4  . SO4   H 5 .   ? 9.399   40.972  -31.497 1.00 121.54 ? 502  SO4   A O4  1 
HETATM 17550 C  C1  . A1A5I I 6 .   ? 19.531  16.824  -62.019 1.00 97.27  ? 503  A1A5I A C1  1 
HETATM 17551 C  C2  . A1A5I I 6 .   ? 18.547  15.890  -62.315 1.00 102.63 ? 503  A1A5I A C2  1 
HETATM 17552 C  C3  . A1A5I I 6 .   ? 17.367  15.856  -61.590 1.00 102.17 ? 503  A1A5I A C3  1 
HETATM 17553 C  C12 . A1A5I I 6 .   ? 15.691  18.582  -57.673 1.00 92.59  ? 503  A1A5I A C12 1 
HETATM 17554 C  C13 . A1A5I I 6 .   ? 14.337  19.134  -58.072 1.00 92.80  ? 503  A1A5I A C13 1 
HETATM 17555 C  C14 . A1A5I I 6 .   ? 13.566  19.564  -56.836 1.00 98.24  ? 503  A1A5I A C14 1 
HETATM 17556 C  C15 . A1A5I I 6 .   ? 13.446  18.458  -55.837 1.00 100.15 ? 503  A1A5I A C15 1 
HETATM 17557 C  C17 . A1A5I I 6 .   ? 15.591  17.541  -56.574 1.00 105.06 ? 503  A1A5I A C17 1 
HETATM 17558 C  C20 . A1A5I I 6 .   ? 18.354  13.584  -63.035 1.00 104.98 ? 503  A1A5I A C20 1 
HETATM 17559 C  C21 . A1A5I I 6 .   ? 19.627  12.820  -62.755 1.00 104.59 ? 503  A1A5I A C21 1 
HETATM 17560 C  C22 . A1A5I I 6 .   ? 20.497  12.739  -64.004 1.00 110.52 ? 503  A1A5I A C22 1 
HETATM 17561 C  C23 . A1A5I I 6 .   ? 19.720  12.252  -65.218 1.00 112.82 ? 503  A1A5I A C23 1 
HETATM 17562 C  C25 . A1A5I I 6 .   ? 17.627  13.015  -64.233 1.00 108.91 ? 503  A1A5I A C25 1 
HETATM 17563 C  C26 . A1A5I I 6 .   ? 17.766  12.697  -66.629 1.00 120.29 ? 503  A1A5I A C26 1 
HETATM 17564 C  C27 . A1A5I I 6 .   ? 16.323  13.121  -66.601 1.00 118.78 ? 503  A1A5I A C27 1 
HETATM 17565 C  C28 . A1A5I I 6 .   ? 20.573  12.192  -66.470 1.00 115.96 ? 503  A1A5I A C28 1 
HETATM 17566 C  C4  . A1A5I I 6 .   ? 17.178  16.763  -60.558 1.00 95.67  ? 503  A1A5I A C4  1 
HETATM 17567 C  C5  . A1A5I I 6 .   ? 18.147  17.705  -60.267 1.00 97.79  ? 503  A1A5I A C5  1 
HETATM 17568 C  C6  . A1A5I I 6 .   ? 19.334  17.732  -60.993 1.00 93.79  ? 503  A1A5I A C6  1 
HETATM 17569 C  C7  . A1A5I I 6 .   ? 16.042  16.895  -59.589 1.00 94.71  ? 503  A1A5I A C7  1 
HETATM 17570 C  C9  . A1A5I I 6 .   ? 17.655  18.566  -59.169 1.00 102.06 ? 503  A1A5I A C9  1 
HETATM 17571 N  N16 . A1A5I I 6 .   ? 14.471  17.558  -55.786 1.00 105.47 ? 503  A1A5I A N16 1 
HETATM 17572 N  N24 . A1A5I I 6 .   ? 18.501  13.047  -65.409 1.00 113.73 ? 503  A1A5I A N24 1 
HETATM 17573 N  N8  . A1A5I I 6 .   ? 16.457  18.048  -58.786 1.00 96.37  ? 503  A1A5I A N8  1 
HETATM 17574 O  O10 . A1A5I I 6 .   ? 18.713  14.959  -63.312 1.00 104.05 ? 503  A1A5I A O10 1 
HETATM 17575 O  O11 . A1A5I I 6 .   ? 18.161  19.568  -58.705 1.00 101.11 ? 503  A1A5I A O11 1 
HETATM 17576 O  O18 . A1A5I I 6 .   ? 16.496  16.739  -56.370 1.00 109.70 ? 503  A1A5I A O18 1 
HETATM 17577 O  O19 . A1A5I I 6 .   ? 12.482  18.345  -55.089 1.00 94.91  ? 503  A1A5I A O19 1 
HETATM 17578 ZN ZN  . ZN    J 4 .   ? 20.038  24.670  -63.511 1.00 86.41  2 900  ZN    C ZN  1 
HETATM 17579 ZN ZN  . ZN    K 4 .   ? 38.464  -31.897 20.008  1.00 89.15  2 501  ZN    D ZN  1 
HETATM 17580 S  S   . SO4   L 5 .   ? 45.811  -28.327 -9.444  1.00 160.05 ? 502  SO4   D S   1 
HETATM 17581 O  O1  . SO4   L 5 .   ? 44.849  -27.984 -10.563 1.00 146.85 ? 502  SO4   D O1  1 
HETATM 17582 O  O2  . SO4   L 5 .   ? 46.841  -27.227 -9.263  1.00 157.06 ? 502  SO4   D O2  1 
HETATM 17583 O  O3  . SO4   L 5 .   ? 44.973  -28.484 -8.192  1.00 147.65 ? 502  SO4   D O3  1 
HETATM 17584 O  O4  . SO4   L 5 .   ? 46.540  -29.625 -9.752  1.00 148.19 ? 502  SO4   D O4  1 
HETATM 17585 C  C1  . A1A5I M 6 .   ? 36.240  -53.948 20.003  0.96 104.86 ? 503  A1A5I D C1  1 
HETATM 17586 C  C2  . A1A5I M 6 .   ? 37.281  -54.810 20.320  0.96 106.89 ? 503  A1A5I D C2  1 
HETATM 17587 C  C3  . A1A5I M 6 .   ? 38.483  -54.746 19.634  0.96 108.47 ? 503  A1A5I D C3  1 
HETATM 17588 C  C12 . A1A5I M 6 .   ? 40.056  -51.882 15.776  0.96 99.85  ? 503  A1A5I D C12 1 
HETATM 17589 C  C13 . A1A5I M 6 .   ? 41.366  -51.242 16.198  0.96 100.64 ? 503  A1A5I D C13 1 
HETATM 17590 C  C14 . A1A5I M 6 .   ? 42.122  -50.753 14.973  0.96 100.31 ? 503  A1A5I D C14 1 
HETATM 17591 C  C15 . A1A5I M 6 .   ? 42.324  -51.838 13.964  0.96 102.93 ? 503  A1A5I D C15 1 
HETATM 17592 C  C17 . A1A5I M 6 .   ? 40.248  -52.916 14.685  0.96 105.48 ? 503  A1A5I D C17 1 
HETATM 17593 C  C20 . A1A5I M 6 .   ? 37.447  -57.132 20.992  0.96 106.80 ? 503  A1A5I D C20 1 
HETATM 17594 C  C21 . A1A5I M 6 .   ? 36.137  -57.859 20.800  0.96 108.16 ? 503  A1A5I D C21 1 
HETATM 17595 C  C22 . A1A5I M 6 .   ? 35.353  -57.915 22.105  0.96 108.68 ? 503  A1A5I D C22 1 
HETATM 17596 C  C23 . A1A5I M 6 .   ? 36.196  -58.435 23.260  0.96 113.98 ? 503  A1A5I D C23 1 
HETATM 17597 C  C25 . A1A5I M 6 .   ? 38.245  -57.731 22.129  0.96 112.96 ? 503  A1A5I D C25 1 
HETATM 17598 C  C26 . A1A5I M 6 .   ? 38.264  -58.065 24.527  0.96 125.56 ? 503  A1A5I D C26 1 
HETATM 17599 C  C27 . A1A5I M 6 .   ? 39.625  -57.427 24.540  0.96 120.82 ? 503  A1A5I D C27 1 
HETATM 17600 C  C28 . A1A5I M 6 .   ? 35.432  -58.471 24.570  0.96 109.95 ? 503  A1A5I D C28 1 
HETATM 17601 C  C4  . A1A5I M 6 .   ? 38.635  -53.812 18.619  0.96 103.88 ? 503  A1A5I D C4  1 
HETATM 17602 C  C5  . A1A5I M 6 .   ? 37.606  -52.946 18.304  0.96 103.71 ? 503  A1A5I D C5  1 
HETATM 17603 C  C6  . A1A5I M 6 .   ? 36.400  -53.014 18.993  0.96 104.87 ? 503  A1A5I D C6  1 
HETATM 17604 C  C7  . A1A5I M 6 .   ? 39.794  -53.574 17.700  0.96 102.86 ? 503  A1A5I D C7  1 
HETATM 17605 C  C9  . A1A5I M 6 .   ? 38.055  -52.055 17.211  0.96 101.62 ? 503  A1A5I D C9  1 
HETATM 17606 N  N16 . A1A5I M 6 .   ? 41.370  -52.813 13.906  0.96 106.19 ? 503  A1A5I D N16 1 
HETATM 17607 N  N24 . A1A5I M 6 .   ? 37.455  -57.686 23.364  0.96 119.74 ? 503  A1A5I D N24 1 
HETATM 17608 N  N8  . A1A5I M 6 .   ? 39.306  -52.467 16.873  0.96 100.93 ? 503  A1A5I D N8  1 
HETATM 17609 O  O10 . A1A5I M 6 .   ? 37.141  -55.755 21.309  0.96 108.36 ? 503  A1A5I D O10 1 
HETATM 17610 O  O11 . A1A5I M 6 .   ? 37.473  -51.113 16.713  0.96 102.23 ? 503  A1A5I D O11 1 
HETATM 17611 O  O18 . A1A5I M 6 .   ? 39.413  -53.789 14.482  0.96 107.68 ? 503  A1A5I D O18 1 
HETATM 17612 O  O19 . A1A5I M 6 .   ? 43.288  -51.866 13.207  0.96 103.44 ? 503  A1A5I D O19 1 
HETATM 17613 S  S   . SO4   N 5 .   ? 45.169  -1.997  -0.635  1.00 145.75 ? 1201 SO4   E S   1 
HETATM 17614 O  O1  . SO4   N 5 .   ? 45.424  -3.429  -0.237  1.00 137.61 ? 1201 SO4   E O1  1 
HETATM 17615 O  O2  . SO4   N 5 .   ? 46.499  -1.328  -0.872  1.00 135.38 ? 1201 SO4   E O2  1 
HETATM 17616 O  O3  . SO4   N 5 .   ? 44.330  -1.997  -1.893  1.00 130.57 ? 1201 SO4   E O3  1 
HETATM 17617 O  O4  . SO4   N 5 .   ? 44.426  -1.250  0.450   1.00 133.05 ? 1201 SO4   E O4  1 
HETATM 17618 ZN ZN  . ZN    O 4 .   ? 35.318  -46.379 21.875  1.00 90.51  2 900  ZN    F ZN  1 
HETATM 17619 O  O   . HOH   P 7 .   ? 39.968  26.442  -29.865 1.00 114.17 ? 601  HOH   A O   1 
HETATM 17620 O  O   . HOH   P 7 .   ? 15.115  38.112  -44.036 1.00 76.87  ? 602  HOH   A O   1 
HETATM 17621 O  O   . HOH   P 7 .   ? 10.058  38.928  -25.174 1.00 72.79  ? 603  HOH   A O   1 
HETATM 17622 O  O   . HOH   P 7 .   ? 31.097  20.724  -30.393 1.00 72.17  ? 604  HOH   A O   1 
HETATM 17623 O  O   . HOH   Q 7 .   ? 43.601  31.788  -0.114  1.00 80.40  ? 1201 HOH   B O   1 
HETATM 17624 O  O   . HOH   Q 7 .   ? 20.440  42.772  6.878   1.00 92.39  ? 1202 HOH   B O   1 
HETATM 17625 O  O   . HOH   Q 7 .   ? -0.560  42.319  -17.593 1.00 124.71 ? 1203 HOH   B O   1 
HETATM 17626 O  O   . HOH   Q 7 .   ? 20.117  23.162  14.044  1.00 77.47  ? 1204 HOH   B O   1 
HETATM 17627 O  O   . HOH   Q 7 .   ? 16.637  45.144  -31.475 1.00 74.28  ? 1205 HOH   B O   1 
HETATM 17628 O  O   . HOH   R 7 .   ? 15.717  23.551  -75.208 1.00 30.00  ? 1001 HOH   C O   1 
HETATM 17629 O  O   . HOH   R 7 .   ? 18.044  16.283  -78.796 1.00 95.33  ? 1002 HOH   C O   1 
HETATM 17630 O  O   . HOH   R 7 .   ? 12.427  23.608  -72.409 1.00 30.00  ? 1003 HOH   C O   1 
HETATM 17631 O  O   . HOH   S 7 .   ? 46.419  -31.507 -16.032 1.00 30.00  ? 601  HOH   D O   1 
HETATM 17632 O  O   . HOH   S 7 .   ? 32.867  -45.649 -16.469 1.00 90.17  ? 602  HOH   D O   1 
HETATM 17633 O  O   . HOH   S 7 .   ? 40.835  -32.452 2.490   1.00 78.82  ? 603  HOH   D O   1 
HETATM 17634 O  O   . HOH   S 7 .   ? 25.946  -42.439 -15.613 1.00 81.53  ? 604  HOH   D O   1 
HETATM 17635 O  O   . HOH   T 7 .   ? 10.930  -17.460 -43.128 1.00 79.57  ? 1301 HOH   E O   1 
HETATM 17636 O  O   . HOH   T 7 .   ? 17.502  -16.010 -63.229 1.00 101.10 ? 1302 HOH   E O   1 
HETATM 17637 O  O   . HOH   T 7 .   ? 58.340  -10.273 -28.445 1.00 91.59  ? 1303 HOH   E O   1 
HETATM 17638 O  O   . HOH   T 7 .   ? 24.602  -29.568 -59.033 1.00 92.25  ? 1304 HOH   E O   1 
HETATM 17639 O  O   . HOH   T 7 .   ? 27.686  3.141   -11.827 1.00 96.64  ? 1305 HOH   E O   1 
HETATM 17640 O  O   . HOH   T 7 .   ? 50.858  -14.673 -22.933 1.00 75.51  ? 1306 HOH   E 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   . HIS   A 4   ? 1.8957 2.0452 2.2044 -0.0582 -0.0103 -0.0192 73   HIS   A N   
2     C  CA  . HIS   A 4   ? 1.9237 2.0751 2.2275 -0.0573 -0.0075 -0.0188 73   HIS   A CA  
3     C  C   . HIS   A 4   ? 1.9909 2.1367 2.2800 -0.0582 -0.0003 -0.0146 73   HIS   A C   
4     O  O   . HIS   A 4   ? 1.9400 2.0843 2.2328 -0.0599 0.0077  -0.0133 73   HIS   A O   
5     C  CB  . HIS   A 4   ? 1.7903 1.9450 2.0870 -0.0541 -0.0154 -0.0206 73   HIS   A CB  
6     N  N   . ASP   A 5   ? 2.1624 2.3049 2.4352 -0.0568 -0.0030 -0.0123 74   ASP   A N   
7     C  CA  . ASP   A 5   ? 2.1333 2.2701 2.3909 -0.0571 0.0025  -0.0086 74   ASP   A CA  
8     C  C   . ASP   A 5   ? 2.0787 2.2093 2.3286 -0.0579 0.0038  -0.0058 74   ASP   A C   
9     O  O   . ASP   A 5   ? 2.0526 2.1776 2.2995 -0.0596 0.0112  -0.0032 74   ASP   A O   
10    C  CB  . ASP   A 5   ? 2.1337 2.2716 2.3780 -0.0548 -0.0013 -0.0081 74   ASP   A CB  
11    C  CG  . ASP   A 5   ? 2.0945 2.2290 2.3296 -0.0551 0.0051  -0.0060 74   ASP   A CG  
12    O  OD1 . ASP   A 5   ? 2.0490 2.1800 2.2872 -0.0568 0.0128  -0.0047 74   ASP   A OD1 
13    O  OD2 . ASP   A 5   ? 2.0487 2.1838 2.2734 -0.0535 0.0024  -0.0057 74   ASP   A OD2 
14    N  N   . ASP   A 6   ? 1.8751 2.0059 2.1208 -0.0566 -0.0029 -0.0060 75   ASP   A N   
15    C  CA  . ASP   A 6   ? 1.8213 1.9462 2.0599 -0.0572 -0.0019 -0.0035 75   ASP   A CA  
16    C  C   . ASP   A 6   ? 1.7991 1.9218 2.0503 -0.0598 0.0023  -0.0037 75   ASP   A C   
17    O  O   . ASP   A 6   ? 1.7980 1.9253 2.0650 -0.0606 0.0009  -0.0067 75   ASP   A O   
18    C  CB  . ASP   A 6   ? 1.7658 1.8918 1.9985 -0.0550 -0.0101 -0.0040 75   ASP   A CB  
19    C  CG  . ASP   A 6   ? 1.7302 1.8499 1.9491 -0.0546 -0.0094 -0.0006 75   ASP   A CG  
20    O  OD1 . ASP   A 6   ? 1.7025 1.8183 1.9239 -0.0556 -0.0085 0.0001  75   ASP   A OD1 
21    O  OD2 . ASP   A 6   ? 1.7068 1.8252 1.9125 -0.0532 -0.0101 0.0012  75   ASP   A OD2 
22    N  N   . ASP   A 7   ? 1.6964 1.8119 1.9404 -0.0610 0.0075  -0.0006 76   ASP   A N   
23    C  CA  . ASP   A 7   ? 1.6250 1.7367 1.8786 -0.0637 0.0129  0.0001  76   ASP   A CA  
24    C  C   . ASP   A 7   ? 1.5719 1.6875 1.8431 -0.0657 0.0176  -0.0019 76   ASP   A C   
25    O  O   . ASP   A 7   ? 1.5738 1.6909 1.8604 -0.0676 0.0175  -0.0038 76   ASP   A O   
26    C  CB  . ASP   A 7   ? 1.6733 1.7846 1.9314 -0.0637 0.0073  -0.0010 76   ASP   A CB  
27    C  CG  . ASP   A 7   ? 1.6779 1.7827 1.9197 -0.0624 0.0059  0.0020  76   ASP   A CG  
28    O  OD1 . ASP   A 7   ? 1.6363 1.7383 1.8631 -0.0610 0.0071  0.0043  76   ASP   A OD1 
29    O  OD2 . ASP   A 7   ? 1.7104 1.8128 1.9547 -0.0627 0.0032  0.0018  76   ASP   A OD2 
30    N  N   . SER   A 8   ? 1.5352 1.6521 1.8041 -0.0654 0.0217  -0.0016 77   SER   A N   
31    C  CA  . SER   A 8   ? 1.5304 1.6512 1.8152 -0.0670 0.0264  -0.0034 77   SER   A CA  
32    C  C   . SER   A 8   ? 1.4285 1.5435 1.7073 -0.0680 0.0370  -0.0002 77   SER   A C   
33    O  O   . SER   A 8   ? 1.3820 1.4914 1.6428 -0.0667 0.0388  0.0026  77   SER   A O   
34    C  CB  . SER   A 8   ? 1.6609 1.7898 1.9508 -0.0652 0.0209  -0.0067 77   SER   A CB  
35    O  OG  . SER   A 8   ? 1.6649 1.7925 1.9419 -0.0637 0.0233  -0.0052 77   SER   A OG  
36    N  N   . CYS   A 9   ? 1.3972 1.5130 1.6912 -0.0703 0.0440  -0.0007 78   CYS   A N   
37    C  CA  . CYS   A 9   ? 1.3577 1.4672 1.6475 -0.0713 0.0552  0.0023  78   CYS   A CA  
38    C  C   . CYS   A 9   ? 1.3507 1.4645 1.6440 -0.0704 0.0580  0.0011  78   CYS   A C   
39    O  O   . CYS   A 9   ? 1.3385 1.4586 1.6506 -0.0716 0.0594  -0.0015 78   CYS   A O   
40    C  CB  . CYS   A 9   ? 1.3763 1.4831 1.6805 -0.0745 0.0627  0.0031  78   CYS   A CB  
41    S  SG  . CYS   A 9   ? 1.5959 1.7005 1.9041 -0.0760 0.0575  0.0029  78   CYS   A SG  
42    N  N   . GLN   A 10  ? 1.3115 1.4216 1.5870 -0.0684 0.0589  0.0029  79   GLN   A N   
43    C  CA  . GLN   A 10  ? 1.2783 1.3909 1.5535 -0.0672 0.0618  0.0021  79   GLN   A CA  
44    C  C   . GLN   A 10  ? 1.2004 1.3038 1.4646 -0.0673 0.0727  0.0057  79   GLN   A C   
45    O  O   . GLN   A 10  ? 1.1543 1.2489 1.4064 -0.0675 0.0764  0.0090  79   GLN   A O   
46    C  CB  . GLN   A 10  ? 1.3040 1.4195 1.5669 -0.0645 0.0535  0.0010  79   GLN   A CB  
47    C  CG  . GLN   A 10  ? 1.3851 1.5062 1.6511 -0.0639 0.0428  -0.0013 79   GLN   A CG  
48    C  CD  . GLN   A 10  ? 1.4845 1.6148 1.7704 -0.0642 0.0387  -0.0055 79   GLN   A CD  
49    O  OE1 . GLN   A 10  ? 1.4672 1.6010 1.7618 -0.0641 0.0421  -0.0069 79   GLN   A OE1 
50    N  NE2 . GLN   A 10  ? 1.5475 1.6813 1.8405 -0.0642 0.0312  -0.0075 79   GLN   A NE2 
51    N  N   . VAL   A 11  ? 1.2354 1.3405 1.5031 -0.0667 0.0777  0.0051  80   VAL   A N   
52    C  CA  . VAL   A 11  ? 1.2655 1.3615 1.5194 -0.0658 0.0870  0.0084  80   VAL   A CA  
53    C  C   . VAL   A 11  ? 1.2848 1.3811 1.5244 -0.0631 0.0828  0.0078  80   VAL   A C   
54    O  O   . VAL   A 11  ? 1.2667 1.3715 1.5145 -0.0623 0.0774  0.0047  80   VAL   A O   
55    C  CB  . VAL   A 11  ? 1.2116 1.3075 1.4800 -0.0672 0.0980  0.0086  80   VAL   A CB  
56    C  CG1 . VAL   A 11  ? 1.2248 1.3320 1.5127 -0.0673 0.0953  0.0046  80   VAL   A CG1 
57    C  CG2 . VAL   A 11  ? 1.2712 1.3567 1.5232 -0.0658 0.1077  0.0120  80   VAL   A CG2 
58    N  N   . ILE   A 12  ? 1.2963 1.3830 1.5142 -0.0615 0.0846  0.0108  81   ILE   A N   
59    C  CA  . ILE   A 12  ? 1.3043 1.3896 1.5072 -0.0591 0.0814  0.0107  81   ILE   A CA  
60    C  C   . ILE   A 12  ? 1.4040 1.4775 1.5911 -0.0579 0.0907  0.0140  81   ILE   A C   
61    O  O   . ILE   A 12  ? 1.4224 1.4875 1.6039 -0.0586 0.0965  0.0168  81   ILE   A O   
62    C  CB  . ILE   A 12  ? 1.3037 1.3898 1.4944 -0.0579 0.0710  0.0105  81   ILE   A CB  
63    C  CG1 . ILE   A 12  ? 1.2742 1.3527 1.4555 -0.0584 0.0717  0.0133  81   ILE   A CG1 
64    C  CG2 . ILE   A 12  ? 1.2923 1.3899 1.4968 -0.0583 0.0617  0.0069  81   ILE   A CG2 
65    C  CD1 . ILE   A 12  ? 1.2275 1.3079 1.4009 -0.0576 0.0617  0.0129  81   ILE   A CD1 
66    N  N   . PRO   A 13  ? 1.4632 1.5350 1.6424 -0.0560 0.0924  0.0137  82   PRO   A N   
67    C  CA  . PRO   A 13  ? 1.4858 1.5451 1.6479 -0.0544 0.1009  0.0168  82   PRO   A CA  
68    C  C   . PRO   A 13  ? 1.4776 1.5281 1.6175 -0.0529 0.0966  0.0190  82   PRO   A C   
69    O  O   . PRO   A 13  ? 1.4599 1.5147 1.5966 -0.0528 0.0867  0.0179  82   PRO   A O   
70    C  CB  . PRO   A 13  ? 1.5176 1.5789 1.6783 -0.0527 0.1019  0.0152  82   PRO   A CB  
71    C  CG  . PRO   A 13  ? 1.4994 1.5718 1.6672 -0.0527 0.0907  0.0119  82   PRO   A CG  
72    C  CD  . PRO   A 13  ? 1.4460 1.5265 1.6309 -0.0550 0.0868  0.0105  82   PRO   A CD  
73    N  N   . VAL   A 14  ? 1.5476 1.5853 1.6721 -0.0516 0.1044  0.0221  83   VAL   A N   
74    C  CA  . VAL   A 14  ? 1.5830 1.6105 1.6858 -0.0500 0.1013  0.0244  83   VAL   A CA  
75    C  C   . VAL   A 14  ? 1.7314 1.7503 1.8154 -0.0470 0.1029  0.0251  83   VAL   A C   
76    O  O   . VAL   A 14  ? 1.8231 1.8362 1.9051 -0.0461 0.1123  0.0262  83   VAL   A O   
77    C  CB  . VAL   A 14  ? 1.5494 1.5669 1.6473 -0.0505 0.1086  0.0277  83   VAL   A CB  
78    C  CG1 . VAL   A 14  ? 1.5704 1.5771 1.6450 -0.0483 0.1047  0.0298  83   VAL   A CG1 
79    C  CG2 . VAL   A 14  ? 1.5565 1.5818 1.6729 -0.0535 0.1070  0.0269  83   VAL   A CG2 
80    N  N   . LEU   A 15  ? 1.6491 1.6669 1.7193 -0.0455 0.0938  0.0246  84   LEU   A N   
81    C  CA  . LEU   A 15  ? 1.7482 1.7554 1.7978 -0.0425 0.0949  0.0256  84   LEU   A CA  
82    C  C   . LEU   A 15  ? 1.8847 1.8763 1.9178 -0.0410 0.1024  0.0292  84   LEU   A C   
83    O  O   . LEU   A 15  ? 1.9033 1.8909 1.9291 -0.0410 0.0988  0.0306  84   LEU   A O   
84    C  CB  . LEU   A 15  ? 1.7310 1.7402 1.7704 -0.0414 0.0832  0.0243  84   LEU   A CB  
85    C  CG  . LEU   A 15  ? 1.8538 1.8497 1.8693 -0.0383 0.0833  0.0257  84   LEU   A CG  
86    C  CD1 . LEU   A 15  ? 1.8418 1.8359 1.8554 -0.0369 0.0881  0.0247  84   LEU   A CD1 
87    C  CD2 . LEU   A 15  ? 1.7523 1.7498 1.7588 -0.0375 0.0716  0.0248  84   LEU   A CD2 
88    N  N   . PRO   A 16  ? 2.0045 1.9869 2.0314 -0.0396 0.1129  0.0308  85   PRO   A N   
89    C  CA  . PRO   A 16  ? 2.0445 2.0120 2.0578 -0.0383 0.1215  0.0345  85   PRO   A CA  
90    C  C   . PRO   A 16  ? 2.0770 2.0329 2.0662 -0.0356 0.1158  0.0359  85   PRO   A C   
91    O  O   . PRO   A 16  ? 2.0874 2.0375 2.0709 -0.0357 0.1159  0.0380  85   PRO   A O   
92    C  CB  . PRO   A 16  ? 2.0494 2.0097 2.0596 -0.0368 0.1331  0.0355  85   PRO   A CB  
93    C  CG  . PRO   A 16  ? 1.9962 1.9712 2.0273 -0.0385 0.1319  0.0323  85   PRO   A CG  
94    C  CD  . PRO   A 16  ? 1.9849 1.9696 2.0171 -0.0389 0.1181  0.0295  85   PRO   A CD  
95    N  N   . GLN   A 17  ? 2.0138 1.9663 1.9890 -0.0332 0.1104  0.0348  86   GLN   A N   
96    C  CA  . GLN   A 17  ? 2.0673 2.0093 2.0202 -0.0305 0.1038  0.0358  86   GLN   A CA  
97    C  C   . GLN   A 17  ? 2.0892 2.0425 2.0490 -0.0320 0.0911  0.0339  86   GLN   A C   
98    O  O   . GLN   A 17  ? 2.0389 2.0003 2.0019 -0.0322 0.0830  0.0313  86   GLN   A O   
99    C  CB  . GLN   A 17  ? 2.0653 1.9984 2.0006 -0.0272 0.1032  0.0353  86   GLN   A CB  
100   N  N   . VAL   A 18  ? 2.1323 2.0856 2.0945 -0.0331 0.0896  0.0352  87   VAL   A N   
101   C  CA  . VAL   A 18  ? 2.1316 2.0951 2.1007 -0.0344 0.0786  0.0337  87   VAL   A CA  
102   C  C   . VAL   A 18  ? 2.1350 2.0921 2.0986 -0.0343 0.0789  0.0360  87   VAL   A C   
103   O  O   . VAL   A 18  ? 2.1325 2.0803 2.0926 -0.0341 0.0883  0.0385  87   VAL   A O   
104   C  CB  . VAL   A 18  ? 2.1107 2.0914 2.1046 -0.0377 0.0763  0.0311  87   VAL   A CB  
105   C  CG1 . VAL   A 18  ? 2.0814 2.0650 2.0897 -0.0402 0.0822  0.0322  87   VAL   A CG1 
106   C  CG2 . VAL   A 18  ? 2.0896 2.0804 2.0874 -0.0382 0.0640  0.0291  87   VAL   A CG2 
107   N  N   . MET   A 19  ? 1.9867 1.9484 1.9498 -0.0343 0.0690  0.0353  88   MET   A N   
108   C  CA  . MET   A 19  ? 1.9566 1.9124 1.9146 -0.0340 0.0689  0.0374  88   MET   A CA  
109   C  C   . MET   A 19  ? 1.9223 1.8878 1.8867 -0.0348 0.0580  0.0361  88   MET   A C   
110   O  O   . MET   A 19  ? 1.9123 1.8790 1.8819 -0.0358 0.0579  0.0371  88   MET   A O   
111   C  CB  . MET   A 19  ? 2.0510 1.9888 1.9840 -0.0304 0.0710  0.0399  88   MET   A CB  
112   C  CG  . MET   A 19  ? 2.1232 2.0577 2.0413 -0.0277 0.0623  0.0386  88   MET   A CG  
113   S  SD  . MET   A 19  ? 2.3008 2.2210 2.1952 -0.0238 0.0563  0.0405  88   MET   A SD  
114   C  CE  . MET   A 19  ? 2.0372 1.9712 1.9456 -0.0258 0.0461  0.0393  88   MET   A CE  
115   N  N   . MET   A 20  ? 1.8406 1.8126 1.8042 -0.0343 0.0492  0.0339  89   MET   A N   
116   C  CA  . MET   A 20  ? 1.6947 1.6737 1.6604 -0.0342 0.0386  0.0330  89   MET   A CA  
117   C  C   . MET   A 20  ? 1.5732 1.5624 1.5562 -0.0367 0.0378  0.0326  89   MET   A C   
118   O  O   . MET   A 20  ? 1.6032 1.5981 1.6010 -0.0390 0.0434  0.0321  89   MET   A O   
119   C  CB  . MET   A 20  ? 1.7090 1.6966 1.6775 -0.0342 0.0310  0.0304  89   MET   A CB  
120   C  CG  . MET   A 20  ? 1.6368 1.6335 1.6196 -0.0362 0.0345  0.0285  89   MET   A CG  
121   S  SD  . MET   A 20  ? 1.8240 1.8325 1.8131 -0.0367 0.0248  0.0255  89   MET   A SD  
122   C  CE  . MET   A 20  ? 1.4971 1.5144 1.4931 -0.0372 0.0154  0.0251  89   MET   A CE  
123   N  N   . ILE   A 21  ? 1.4803 1.4717 1.4617 -0.0361 0.0304  0.0327  90   ILE   A N   
124   C  CA  . ILE   A 21  ? 1.4033 1.4058 1.4007 -0.0380 0.0269  0.0317  90   ILE   A CA  
125   C  C   . ILE   A 21  ? 1.4338 1.4491 1.4409 -0.0388 0.0197  0.0290  90   ILE   A C   
126   O  O   . ILE   A 21  ? 1.4275 1.4445 1.4287 -0.0374 0.0118  0.0284  90   ILE   A O   
127   C  CB  . ILE   A 21  ? 1.2442 1.2427 1.2351 -0.0368 0.0229  0.0332  90   ILE   A CB  
128   C  CG1 . ILE   A 21  ? 1.3069 1.2944 1.2924 -0.0367 0.0312  0.0358  90   ILE   A CG1 
129   C  CG2 . ILE   A 21  ? 1.1292 1.1396 1.1352 -0.0383 0.0176  0.0319  90   ILE   A CG2 
130   C  CD1 . ILE   A 21  ? 1.4212 1.3931 1.3862 -0.0341 0.0351  0.0379  90   ILE   A CD1 
131   N  N   . LEU   A 22  ? 1.4220 1.4457 1.4436 -0.0409 0.0225  0.0273  91   LEU   A N   
132   C  CA  . LEU   A 22  ? 1.2856 1.3209 1.3168 -0.0416 0.0167  0.0247  91   LEU   A CA  
133   C  C   . LEU   A 22  ? 1.2639 1.3088 1.3070 -0.0425 0.0113  0.0238  91   LEU   A C   
134   O  O   . LEU   A 22  ? 1.2679 1.3168 1.3233 -0.0442 0.0144  0.0234  91   LEU   A O   
135   C  CB  . LEU   A 22  ? 1.2311 1.2702 1.2719 -0.0430 0.0222  0.0233  91   LEU   A CB  
136   C  CG  . LEU   A 22  ? 1.1625 1.2135 1.2144 -0.0438 0.0169  0.0207  91   LEU   A CG  
137   C  CD1 . LEU   A 22  ? 1.2389 1.2887 1.2799 -0.0423 0.0108  0.0203  91   LEU   A CD1 
138   C  CD2 . LEU   A 22  ? 1.1387 1.1930 1.2005 -0.0450 0.0226  0.0193  91   LEU   A CD2 
139   N  N   . ILE   A 23  ? 1.2496 1.2979 1.2893 -0.0413 0.0033  0.0234  92   ILE   A N   
140   C  CA  . ILE   A 23  ? 1.2126 1.2704 1.2635 -0.0419 -0.0020 0.0224  92   ILE   A CA  
141   C  C   . ILE   A 23  ? 1.1642 1.2327 1.2278 -0.0431 -0.0039 0.0199  92   ILE   A C   
142   O  O   . ILE   A 23  ? 1.1933 1.2627 1.2535 -0.0428 -0.0051 0.0190  92   ILE   A O   
143   C  CB  . ILE   A 23  ? 1.1403 1.1981 1.1837 -0.0401 -0.0095 0.0230  92   ILE   A CB  
144   C  CG1 . ILE   A 23  ? 1.1228 1.1686 1.1511 -0.0384 -0.0080 0.0254  92   ILE   A CG1 
145   C  CG2 . ILE   A 23  ? 1.0121 1.0779 1.0658 -0.0403 -0.0137 0.0224  92   ILE   A CG2 
146   C  CD1 . ILE   A 23  ? 1.1299 1.1757 1.1520 -0.0365 -0.0152 0.0260  92   ILE   A CD1 
147   N  N   . PRO   A 24  ? 1.0642 1.1401 1.1417 -0.0443 -0.0041 0.0186  93   PRO   A N   
148   C  CA  . PRO   A 24  ? 1.1219 1.2072 1.2106 -0.0450 -0.0063 0.0162  93   PRO   A CA  
149   C  C   . PRO   A 24  ? 1.1211 1.2109 1.2061 -0.0439 -0.0131 0.0155  93   PRO   A C   
150   O  O   . PRO   A 24  ? 1.0979 1.1877 1.1781 -0.0428 -0.0179 0.0164  93   PRO   A O   
151   C  CB  . PRO   A 24  ? 1.0559 1.1469 1.1572 -0.0458 -0.0074 0.0152  93   PRO   A CB  
152   C  CG  . PRO   A 24  ? 1.0868 1.1717 1.1830 -0.0454 -0.0064 0.0172  93   PRO   A CG  
153   C  CD  . PRO   A 24  ? 1.0908 1.1655 1.1741 -0.0450 -0.0017 0.0193  93   PRO   A CD  
154   N  N   . GLY   A 25  ? 1.0879 1.1812 1.1755 -0.0443 -0.0132 0.0140  94   GLY   A N   
155   C  CA  . GLY   A 25  ? 1.1287 1.2257 1.2132 -0.0435 -0.0188 0.0133  94   GLY   A CA  
156   C  C   . GLY   A 25  ? 1.2096 1.2997 1.2808 -0.0428 -0.0190 0.0143  94   GLY   A C   
157   O  O   . GLY   A 25  ? 1.1762 1.2689 1.2460 -0.0426 -0.0222 0.0134  94   GLY   A O   
158   N  N   . GLN   A 26  ? 1.3242 1.4050 1.3854 -0.0422 -0.0157 0.0161  95   GLN   A N   
159   C  CA  . GLN   A 26  ? 1.3544 1.4272 1.4023 -0.0413 -0.0151 0.0167  95   GLN   A CA  
160   C  C   . GLN   A 26  ? 1.3444 1.4170 1.3942 -0.0420 -0.0107 0.0155  95   GLN   A C   
161   O  O   . GLN   A 26  ? 1.3273 1.4039 1.3877 -0.0432 -0.0066 0.0146  95   GLN   A O   
162   C  CB  . GLN   A 26  ? 1.4062 1.4678 1.4424 -0.0403 -0.0113 0.0189  95   GLN   A CB  
163   C  CG  . GLN   A 26  ? 1.4613 1.5196 1.4897 -0.0388 -0.0164 0.0203  95   GLN   A CG  
164   C  CD  . GLN   A 26  ? 1.5036 1.5498 1.5198 -0.0376 -0.0121 0.0224  95   GLN   A CD  
165   O  OE1 . GLN   A 26  ? 1.5045 1.5458 1.5206 -0.0383 -0.0046 0.0231  95   GLN   A OE1 
166   N  NE2 . GLN   A 26  ? 1.4848 1.5258 1.4905 -0.0358 -0.0167 0.0236  95   GLN   A NE2 
167   N  N   . THR   A 27  ? 1.2688 1.3363 1.3082 -0.0412 -0.0118 0.0154  96   THR   A N   
168   C  CA  . THR   A 27  ? 1.2363 1.3019 1.2748 -0.0414 -0.0078 0.0144  96   THR   A CA  
169   C  C   . THR   A 27  ? 1.2672 1.3202 1.2904 -0.0400 -0.0035 0.0159  96   THR   A C   
170   O  O   . THR   A 27  ? 1.2909 1.3370 1.3024 -0.0387 -0.0064 0.0172  96   THR   A O   
171   C  CB  . THR   A 27  ? 1.1785 1.2492 1.2180 -0.0415 -0.0131 0.0127  96   THR   A CB  
172   O  OG1 . THR   A 27  ? 1.2629 1.3326 1.2953 -0.0407 -0.0199 0.0132  96   THR   A OG1 
173   C  CG2 . THR   A 27  ? 1.1335 1.2155 1.1879 -0.0427 -0.0148 0.0111  96   THR   A CG2 
174   N  N   . LEU   A 28  ? 1.2473 1.2967 1.2705 -0.0402 0.0035  0.0157  97   LEU   A N   
175   C  CA  . LEU   A 28  ? 1.2666 1.3032 1.2745 -0.0385 0.0081  0.0171  97   LEU   A CA  
176   C  C   . LEU   A 28  ? 1.3303 1.3654 1.3353 -0.0381 0.0100  0.0158  97   LEU   A C   
177   O  O   . LEU   A 28  ? 1.3460 1.3878 1.3628 -0.0393 0.0132  0.0144  97   LEU   A O   
178   C  CB  . LEU   A 28  ? 1.2601 1.2912 1.2685 -0.0386 0.0167  0.0188  97   LEU   A CB  
179   C  CG  . LEU   A 28  ? 1.2317 1.2688 1.2555 -0.0404 0.0233  0.0181  97   LEU   A CG  
180   C  CD1 . LEU   A 28  ? 1.2557 1.2862 1.2750 -0.0396 0.0313  0.0183  97   LEU   A CD1 
181   C  CD2 . LEU   A 28  ? 1.2427 1.2799 1.2730 -0.0413 0.0268  0.0195  97   LEU   A CD2 
182   N  N   . PRO   A 29  ? 1.3651 1.3912 1.3546 -0.0364 0.0078  0.0160  98   PRO   A N   
183   C  CA  . PRO   A 29  ? 1.3805 1.4028 1.3651 -0.0356 0.0107  0.0149  98   PRO   A CA  
184   C  C   . PRO   A 29  ? 1.3920 1.4054 1.3715 -0.0346 0.0209  0.0163  98   PRO   A C   
185   O  O   . PRO   A 29  ? 1.3884 1.3950 1.3625 -0.0340 0.0248  0.0183  98   PRO   A O   
186   C  CB  . PRO   A 29  ? 1.4550 1.4695 1.4237 -0.0339 0.0043  0.0148  98   PRO   A CB  
187   C  CG  . PRO   A 29  ? 1.4843 1.4923 1.4443 -0.0328 0.0027  0.0168  98   PRO   A CG  
188   C  CD  . PRO   A 29  ? 1.4463 1.4649 1.4219 -0.0348 0.0024  0.0171  98   PRO   A CD  
189   N  N   . LEU   A 30  ? 1.4500 1.4630 1.4311 -0.0344 0.0254  0.0152  99   LEU   A N   
190   C  CA  . LEU   A 30  ? 1.5089 1.5148 1.4878 -0.0336 0.0360  0.0165  99   LEU   A CA  
191   C  C   . LEU   A 30  ? 1.6294 1.6295 1.6006 -0.0320 0.0393  0.0157  99   LEU   A C   
192   O  O   . LEU   A 30  ? 1.6416 1.6484 1.6183 -0.0326 0.0354  0.0135  99   LEU   A O   
193   C  CB  . LEU   A 30  ? 1.4657 1.4816 1.4643 -0.0358 0.0409  0.0162  99   LEU   A CB  
194   C  CG  . LEU   A 30  ? 1.4880 1.4980 1.4875 -0.0358 0.0507  0.0184  99   LEU   A CG  
195   C  CD1 . LEU   A 30  ? 1.4991 1.4969 1.4814 -0.0341 0.0508  0.0208  99   LEU   A CD1 
196   C  CD2 . LEU   A 30  ? 1.4207 1.4416 1.4398 -0.0383 0.0515  0.0179  99   LEU   A CD2 
197   N  N   . GLN   A 31  ? 1.8282 1.8153 1.7859 -0.0299 0.0468  0.0174  100  GLN   A N   
198   C  CA  . GLN   A 31  ? 1.8462 1.8255 1.7938 -0.0278 0.0507  0.0168  100  GLN   A CA  
199   C  C   . GLN   A 31  ? 1.8531 1.8262 1.8011 -0.0269 0.0631  0.0186  100  GLN   A C   
200   O  O   . GLN   A 31  ? 1.8694 1.8311 1.8053 -0.0254 0.0679  0.0210  100  GLN   A O   
201   C  CB  . GLN   A 31  ? 1.8909 1.8574 1.8164 -0.0251 0.0457  0.0172  100  GLN   A CB  
202   C  CG  . GLN   A 31  ? 1.9454 1.9040 1.8600 -0.0229 0.0484  0.0163  100  GLN   A CG  
203   C  CD  . GLN   A 31  ? 2.0716 2.0318 1.9814 -0.0228 0.0382  0.0141  100  GLN   A CD  
204   O  OE1 . GLN   A 31  ? 2.0531 2.0249 1.9743 -0.0251 0.0304  0.0128  100  GLN   A OE1 
205   N  NE2 . GLN   A 31  ? 2.1235 2.0716 2.0160 -0.0200 0.0383  0.0137  100  GLN   A NE2 
206   N  N   . LEU   A 32  ? 1.7932 1.7734 1.7548 -0.0278 0.0683  0.0174  101  LEU   A N   
207   C  CA  . LEU   A 32  ? 1.8378 1.8154 1.8055 -0.0276 0.0803  0.0187  101  LEU   A CA  
208   C  C   . LEU   A 32  ? 1.9146 1.8827 1.8712 -0.0248 0.0869  0.0188  101  LEU   A C   
209   O  O   . LEU   A 32  ? 1.9136 1.8871 1.8756 -0.0247 0.0853  0.0166  101  LEU   A O   
210   C  CB  . LEU   A 32  ? 1.8049 1.7980 1.7979 -0.0305 0.0816  0.0173  101  LEU   A CB  
211   C  CG  . LEU   A 32  ? 1.7685 1.7712 1.7732 -0.0332 0.0753  0.0171  101  LEU   A CG  
212   C  CD1 . LEU   A 32  ? 1.6919 1.7085 1.7103 -0.0348 0.0669  0.0142  101  LEU   A CD1 
213   C  CD2 . LEU   A 32  ? 1.7360 1.7416 1.7543 -0.0349 0.0828  0.0184  101  LEU   A CD2 
214   N  N   . PHE   A 33  ? 2.0418 1.9950 1.9824 -0.0223 0.0946  0.0213  102  PHE   A N   
215   C  CA  . PHE   A 33  ? 2.0636 2.0050 1.9906 -0.0191 0.1019  0.0219  102  PHE   A CA  
216   C  C   . PHE   A 33  ? 2.0604 2.0020 1.9982 -0.0191 0.1152  0.0231  102  PHE   A C   
217   O  O   . PHE   A 33  ? 2.0521 1.9979 1.9979 -0.0188 0.1191  0.0217  102  PHE   A O   
218   C  CB  . PHE   A 33  ? 2.0789 2.0017 1.9789 -0.0157 0.1019  0.0239  102  PHE   A CB  
219   C  CG  . PHE   A 33  ? 2.1593 2.0783 2.0448 -0.0143 0.0906  0.0222  102  PHE   A CG  
220   C  CD1 . PHE   A 33  ? 2.1542 2.0813 2.0440 -0.0164 0.0790  0.0211  102  PHE   A CD1 
221   C  CD2 . PHE   A 33  ? 2.2668 2.1737 2.1343 -0.0108 0.0915  0.0217  102  PHE   A CD2 
222   C  CE1 . PHE   A 33  ? 2.1742 2.0981 2.0520 -0.0153 0.0686  0.0195  102  PHE   A CE1 
223   C  CE2 . PHE   A 33  ? 2.2408 2.1439 2.0954 -0.0097 0.0807  0.0200  102  PHE   A CE2 
224   C  CZ  . PHE   A 33  ? 2.2318 2.1437 2.0922 -0.0120 0.0692  0.0189  102  PHE   A CZ  
225   N  N   . HIS   A 34  ? 2.0205 1.9574 1.9589 -0.0196 0.1223  0.0258  103  HIS   A N   
226   C  CA  . HIS   A 34  ? 1.9864 1.9208 1.9325 -0.0193 0.1361  0.0275  103  HIS   A CA  
227   C  C   . HIS   A 34  ? 1.9220 1.8734 1.8956 -0.0222 0.1375  0.0253  103  HIS   A C   
228   O  O   . HIS   A 34  ? 1.9308 1.8958 1.9197 -0.0252 0.1292  0.0234  103  HIS   A O   
229   C  CB  . HIS   A 34  ? 1.9870 1.9152 1.9314 -0.0200 0.1420  0.0307  103  HIS   A CB  
230   C  CG  . HIS   A 34  ? 2.0456 1.9598 1.9658 -0.0178 0.1375  0.0324  103  HIS   A CG  
231   N  ND1 . HIS   A 34  ? 2.0616 1.9801 1.9823 -0.0195 0.1277  0.0322  103  HIS   A ND1 
232   C  CD2 . HIS   A 34  ? 2.0707 1.9664 1.9652 -0.0137 0.1413  0.0344  103  HIS   A CD2 
233   C  CE1 . HIS   A 34  ? 2.0811 1.9849 1.9782 -0.0166 0.1254  0.0339  103  HIS   A CE1 
234   N  NE2 . HIS   A 34  ? 2.1079 1.9973 1.9884 -0.0130 0.1333  0.0352  103  HIS   A NE2 
235   N  N   . PRO   A 35  ? 1.8931 1.8441 1.8735 -0.0212 0.1477  0.0254  104  PRO   A N   
236   C  CA  . PRO   A 35  ? 1.8698 1.8371 1.8761 -0.0235 0.1479  0.0228  104  PRO   A CA  
237   C  C   . PRO   A 35  ? 1.8310 1.8095 1.8598 -0.0272 0.1489  0.0229  104  PRO   A C   
238   O  O   . PRO   A 35  ? 1.8426 1.8361 1.8920 -0.0295 0.1441  0.0202  104  PRO   A O   
239   C  CB  . PRO   A 35  ? 1.9121 1.8735 1.9178 -0.0210 0.1599  0.0234  104  PRO   A CB  
240   C  CG  . PRO   A 35  ? 1.9683 1.9117 1.9532 -0.0183 0.1687  0.0271  104  PRO   A CG  
241   C  CD  . PRO   A 35  ? 1.9857 1.9211 1.9498 -0.0175 0.1588  0.0276  104  PRO   A CD  
242   N  N   . GLN   A 36  ? 1.8860 1.8573 1.9112 -0.0278 0.1549  0.0258  105  GLN   A N   
243   C  CA  . GLN   A 36  ? 1.8826 1.8639 1.9281 -0.0314 0.1548  0.0259  105  GLN   A CA  
244   C  C   . GLN   A 36  ? 1.8905 1.8833 1.9427 -0.0336 0.1408  0.0234  105  GLN   A C   
245   O  O   . GLN   A 36  ? 1.8515 1.8586 1.9256 -0.0361 0.1371  0.0210  105  GLN   A O   
246   C  CB  . GLN   A 36  ? 1.8339 1.8036 1.8703 -0.0314 0.1624  0.0296  105  GLN   A CB  
247   N  N   . GLU   A 37  ? 1.9134 1.8997 1.9468 -0.0325 0.1327  0.0240  106  GLU   A N   
248   C  CA  . GLU   A 37  ? 1.8739 1.8703 1.9129 -0.0344 0.1200  0.0220  106  GLU   A CA  
249   C  C   . GLU   A 37  ? 1.8598 1.8661 1.9051 -0.0343 0.1124  0.0186  106  GLU   A C   
250   O  O   . GLU   A 37  ? 1.8426 1.8606 1.8999 -0.0363 0.1037  0.0165  106  GLU   A O   
251   C  CB  . GLU   A 37  ? 1.8640 1.8506 1.8818 -0.0331 0.1139  0.0236  106  GLU   A CB  
252   C  CG  . GLU   A 37  ? 1.9065 1.8787 1.9000 -0.0295 0.1152  0.0246  106  GLU   A CG  
253   C  CD  . GLU   A 37  ? 1.9711 1.9321 1.9444 -0.0281 0.1108  0.0266  106  GLU   A CD  
254   O  OE1 . GLU   A 37  ? 2.0222 1.9750 1.9769 -0.0256 0.1058  0.0263  106  GLU   A OE1 
255   O  OE2 . GLU   A 37  ? 1.9611 1.9215 1.9373 -0.0294 0.1119  0.0283  106  GLU   A OE2 
256   N  N   . VAL   A 38  ? 1.8030 1.8041 1.8397 -0.0319 0.1155  0.0181  107  VAL   A N   
257   C  CA  . VAL   A 38  ? 1.7703 1.7802 1.8131 -0.0318 0.1089  0.0149  107  VAL   A CA  
258   C  C   . VAL   A 38  ? 1.7209 1.7446 1.7894 -0.0337 0.1109  0.0128  107  VAL   A C   
259   O  O   . VAL   A 38  ? 1.7092 1.7440 1.7885 -0.0348 0.1028  0.0100  107  VAL   A O   
260   C  CB  . VAL   A 38  ? 1.7972 1.7971 1.8235 -0.0285 0.1117  0.0148  107  VAL   A CB  
261   C  CG1 . VAL   A 38  ? 1.7426 1.7521 1.7799 -0.0284 0.1087  0.0117  107  VAL   A CG1 
262   C  CG2 . VAL   A 38  ? 1.8156 1.8052 1.8185 -0.0268 0.1048  0.0156  107  VAL   A CG2 
263   N  N   . SER   A 39  ? 1.7443 1.7673 1.8231 -0.0340 0.1217  0.0139  108  SER   A N   
264   C  CA  . SER   A 39  ? 1.7161 1.7522 1.8205 -0.0359 0.1234  0.0117  108  SER   A CA  
265   C  C   . SER   A 39  ? 1.7190 1.7648 1.8379 -0.0389 0.1171  0.0110  108  SER   A C   
266   O  O   . SER   A 39  ? 1.6751 1.7335 1.8126 -0.0403 0.1124  0.0082  108  SER   A O   
267   C  CB  . SER   A 39  ? 1.7403 1.7731 1.8528 -0.0355 0.1369  0.0132  108  SER   A CB  
268   O  OG  . SER   A 39  ? 1.7306 1.7549 1.8310 -0.0323 0.1431  0.0137  108  SER   A OG  
269   N  N   . MET   A 40  ? 1.7776 1.8173 1.8878 -0.0398 0.1168  0.0134  109  MET   A N   
270   C  CA  . MET   A 40  ? 1.7689 1.8163 1.8894 -0.0423 0.1101  0.0128  109  MET   A CA  
271   C  C   . MET   A 40  ? 1.7478 1.8041 1.8701 -0.0426 0.0976  0.0101  109  MET   A C   
272   O  O   . MET   A 40  ? 1.7227 1.7908 1.8634 -0.0440 0.0935  0.0075  109  MET   A O   
273   C  CB  . MET   A 40  ? 1.7986 1.8359 1.9047 -0.0425 0.1111  0.0160  109  MET   A CB  
274   C  CG  . MET   A 40  ? 1.7726 1.8168 1.8874 -0.0449 0.1039  0.0156  109  MET   A CG  
275   S  SD  . MET   A 40  ? 1.9440 1.9775 2.0362 -0.0440 0.0993  0.0183  109  MET   A SD  
276   C  CE  . MET   A 40  ? 1.6927 1.7353 1.7996 -0.0469 0.0932  0.0177  109  MET   A CE  
277   N  N   . VAL   A 41  ? 1.6833 1.7339 1.7868 -0.0412 0.0914  0.0106  110  VAL   A N   
278   C  CA  . VAL   A 41  ? 1.5815 1.6399 1.6862 -0.0415 0.0799  0.0083  110  VAL   A CA  
279   C  C   . VAL   A 41  ? 1.5381 1.6055 1.6554 -0.0412 0.0783  0.0053  110  VAL   A C   
280   O  O   . VAL   A 41  ? 1.5218 1.5990 1.6492 -0.0421 0.0706  0.0030  110  VAL   A O   
281   C  CB  . VAL   A 41  ? 1.5108 1.5610 1.5936 -0.0399 0.0745  0.0093  110  VAL   A CB  
282   C  CG1 . VAL   A 41  ? 1.5417 1.5836 1.6129 -0.0400 0.0750  0.0120  110  VAL   A CG1 
283   C  CG2 . VAL   A 41  ? 1.5682 1.6098 1.6384 -0.0375 0.0793  0.0095  110  VAL   A CG2 
284   N  N   . ARG   A 42  ? 1.5605 1.6245 1.6775 -0.0397 0.0857  0.0051  111  ARG   A N   
285   C  CA  . ARG   A 42  ? 1.5622 1.6348 1.6926 -0.0393 0.0849  0.0022  111  ARG   A CA  
286   C  C   . ARG   A 42  ? 1.5963 1.6804 1.7501 -0.0413 0.0840  0.0004  111  ARG   A C   
287   O  O   . ARG   A 42  ? 1.5662 1.6597 1.7299 -0.0416 0.0766  -0.0023 111  ARG   A O   
288   C  CB  . ARG   A 42  ? 1.5771 1.6435 1.7041 -0.0373 0.0945  0.0027  111  ARG   A CB  
289   N  N   . ASN   A 43  ? 1.5942 1.6774 1.7570 -0.0426 0.0914  0.0018  112  ASN   A N   
290   C  CA  . ASN   A 43  ? 1.5905 1.6841 1.7755 -0.0447 0.0898  0.0001  112  ASN   A CA  
291   C  C   . ASN   A 43  ? 1.5237 1.6221 1.7090 -0.0459 0.0796  -0.0007 112  ASN   A C   
292   O  O   . ASN   A 43  ? 1.5097 1.6180 1.7101 -0.0467 0.0738  -0.0033 112  ASN   A O   
293   C  CB  . ASN   A 43  ? 1.6279 1.7186 1.8214 -0.0461 0.0996  0.0020  112  ASN   A CB  
294   C  CG  . ASN   A 43  ? 1.7459 1.8354 1.9468 -0.0451 0.1098  0.0020  112  ASN   A CG  
295   O  OD1 . ASN   A 43  ? 1.8129 1.9074 2.0197 -0.0437 0.1087  -0.0004 112  ASN   A OD1 
296   N  ND2 . ASN   A 43  ? 1.7754 1.8580 1.9760 -0.0457 0.1202  0.0048  112  ASN   A ND2 
297   N  N   . LEU   A 44  ? 1.5186 1.6099 1.6872 -0.0460 0.0772  0.0017  113  LEU   A N   
298   C  CA  . LEU   A 44  ? 1.4811 1.5764 1.6500 -0.0471 0.0684  0.0013  113  LEU   A CA  
299   C  C   . LEU   A 44  ? 1.5040 1.6069 1.6752 -0.0464 0.0589  -0.0014 113  LEU   A C   
300   O  O   . LEU   A 44  ? 1.5010 1.6122 1.6846 -0.0472 0.0532  -0.0034 113  LEU   A O   
301   C  CB  . LEU   A 44  ? 1.4846 1.5703 1.6340 -0.0468 0.0677  0.0043  113  LEU   A CB  
302   C  CG  . LEU   A 44  ? 1.4917 1.5728 1.6416 -0.0482 0.0723  0.0067  113  LEU   A CG  
303   C  CD1 . LEU   A 44  ? 1.5131 1.5833 1.6413 -0.0471 0.0717  0.0095  113  LEU   A CD1 
304   C  CD2 . LEU   A 44  ? 1.4944 1.5839 1.6581 -0.0500 0.0664  0.0054  113  LEU   A CD2 
305   N  N   . ILE   A 45  ? 1.4858 1.5853 1.6446 -0.0447 0.0572  -0.0016 114  ILE   A N   
306   C  CA  . ILE   A 45  ? 1.4520 1.5575 1.6107 -0.0441 0.0482  -0.0038 114  ILE   A CA  
307   C  C   . ILE   A 45  ? 1.4036 1.5178 1.5790 -0.0437 0.0473  -0.0069 114  ILE   A C   
308   O  O   . ILE   A 45  ? 1.3444 1.4651 1.5245 -0.0435 0.0397  -0.0090 114  ILE   A O   
309   C  CB  . ILE   A 45  ? 1.3814 1.4800 1.5221 -0.0426 0.0469  -0.0030 114  ILE   A CB  
310   C  CG1 . ILE   A 45  ? 1.4093 1.5020 1.5470 -0.0414 0.0558  -0.0025 114  ILE   A CG1 
311   C  CG2 . ILE   A 45  ? 1.3406 1.4322 1.4654 -0.0428 0.0443  -0.0006 114  ILE   A CG2 
312   C  CD1 . ILE   A 45  ? 1.4480 1.5366 1.5732 -0.0395 0.0541  -0.0031 114  ILE   A CD1 
313   N  N   . GLN   A 46  ? 1.4040 1.5182 1.5884 -0.0435 0.0551  -0.0073 115  GLN   A N   
314   C  CA  . GLN   A 46  ? 1.4026 1.5257 1.6060 -0.0433 0.0545  -0.0104 115  GLN   A CA  
315   C  C   . GLN   A 46  ? 1.4040 1.5340 1.6224 -0.0450 0.0509  -0.0115 115  GLN   A C   
316   O  O   . GLN   A 46  ? 1.3528 1.4906 1.5824 -0.0446 0.0448  -0.0143 115  GLN   A O   
317   C  CB  . GLN   A 46  ? 1.3928 1.5143 1.6032 -0.0428 0.0644  -0.0103 115  GLN   A CB  
318   C  CG  . GLN   A 46  ? 1.4384 1.5536 1.6353 -0.0407 0.0676  -0.0098 115  GLN   A CG  
319   C  CD  . GLN   A 46  ? 1.5085 1.6296 1.7109 -0.0390 0.0630  -0.0129 115  GLN   A CD  
320   O  OE1 . GLN   A 46  ? 1.4675 1.5911 1.6650 -0.0386 0.0544  -0.0141 115  GLN   A OE1 
321   N  NE2 . GLN   A 46  ? 1.5055 1.6288 1.7184 -0.0379 0.0689  -0.0142 115  GLN   A NE2 
322   N  N   . LYS   A 47  ? 1.4545 1.5810 1.6725 -0.0466 0.0545  -0.0092 116  LYS   A N   
323   C  CA  . LYS   A 47  ? 1.4423 1.5739 1.6731 -0.0483 0.0514  -0.0100 116  LYS   A CA  
324   C  C   . LYS   A 47  ? 1.5123 1.6435 1.7332 -0.0485 0.0432  -0.0093 116  LYS   A C   
325   O  O   . LYS   A 47  ? 1.5354 1.6689 1.7505 -0.0473 0.0363  -0.0105 116  LYS   A O   
326   C  CB  . LYS   A 47  ? 1.3841 1.5119 1.6205 -0.0501 0.0600  -0.0079 116  LYS   A CB  
327   N  N   . ASP   A 48  ? 1.6542 1.7823 1.8730 -0.0500 0.0441  -0.0073 117  ASP   A N   
328   C  CA  . ASP   A 48  ? 1.6543 1.7827 1.8661 -0.0501 0.0366  -0.0067 117  ASP   A CA  
329   C  C   . ASP   A 48  ? 1.6440 1.7648 1.8352 -0.0495 0.0359  -0.0040 117  ASP   A C   
330   O  O   . ASP   A 48  ? 1.6259 1.7470 1.8108 -0.0494 0.0297  -0.0035 117  ASP   A O   
331   C  CB  . ASP   A 48  ? 1.6824 1.8112 1.9025 -0.0519 0.0374  -0.0061 117  ASP   A CB  
332   C  CG  . ASP   A 48  ? 1.7081 1.8285 1.9218 -0.0530 0.0460  -0.0028 117  ASP   A CG  
333   O  OD1 . ASP   A 48  ? 1.7001 1.8162 1.9107 -0.0526 0.0535  -0.0018 117  ASP   A OD1 
334   O  OD2 . ASP   A 48  ? 1.6772 1.7946 1.8883 -0.0541 0.0456  -0.0011 117  ASP   A OD2 
335   N  N   . ARG   A 49  ? 1.4799 1.5937 1.6608 -0.0489 0.0421  -0.0024 118  ARG   A N   
336   C  CA  . ARG   A 49  ? 1.4299 1.5351 1.5909 -0.0481 0.0423  0.0001  118  ARG   A CA  
337   C  C   . ARG   A 49  ? 1.3721 1.4734 1.5259 -0.0488 0.0402  0.0023  118  ARG   A C   
338   O  O   . ARG   A 49  ? 1.3236 1.4198 1.4621 -0.0480 0.0371  0.0038  118  ARG   A O   
339   C  CB  . ARG   A 49  ? 1.4550 1.5615 1.6074 -0.0467 0.0359  -0.0010 118  ARG   A CB  
340   N  N   . THR   A 50  ? 1.4370 1.5403 1.6015 -0.0503 0.0420  0.0025  119  THR   A N   
341   C  CA  . THR   A 50  ? 1.3483 1.4472 1.5064 -0.0509 0.0412  0.0048  119  THR   A CA  
342   C  C   . THR   A 50  ? 1.3775 1.4683 1.5333 -0.0516 0.0510  0.0072  119  THR   A C   
343   O  O   . THR   A 50  ? 1.3815 1.4746 1.5512 -0.0528 0.0566  0.0065  119  THR   A O   
344   C  CB  . THR   A 50  ? 1.3034 1.4094 1.4741 -0.0520 0.0359  0.0034  119  THR   A CB  
345   O  OG1 . THR   A 50  ? 1.3501 1.4632 1.5229 -0.0511 0.0276  0.0011  119  THR   A OG1 
346   C  CG2 . THR   A 50  ? 1.2273 1.3283 1.3894 -0.0523 0.0346  0.0057  119  THR   A CG2 
347   N  N   . PHE   A 51  ? 1.3492 1.4302 1.4875 -0.0507 0.0529  0.0099  120  PHE   A N   
348   C  CA  . PHE   A 51  ? 1.3263 1.3977 1.4590 -0.0510 0.0619  0.0126  120  PHE   A CA  
349   C  C   . PHE   A 51  ? 1.2791 1.3460 1.4052 -0.0514 0.0598  0.0147  120  PHE   A C   
350   O  O   . PHE   A 51  ? 1.2264 1.2981 1.3529 -0.0514 0.0515  0.0139  120  PHE   A O   
351   C  CB  . PHE   A 51  ? 1.3201 1.3820 1.4366 -0.0490 0.0669  0.0141  120  PHE   A CB  
352   C  CG  . PHE   A 51  ? 1.2496 1.3054 1.3467 -0.0473 0.0610  0.0152  120  PHE   A CG  
353   C  CD1 . PHE   A 51  ? 1.2020 1.2635 1.2972 -0.0466 0.0525  0.0133  120  PHE   A CD1 
354   C  CD2 . PHE   A 51  ? 1.3155 1.3596 1.3964 -0.0462 0.0640  0.0181  120  PHE   A CD2 
355   C  CE1 . PHE   A 51  ? 1.2115 1.2678 1.2904 -0.0452 0.0471  0.0142  120  PHE   A CE1 
356   C  CE2 . PHE   A 51  ? 1.3095 1.3481 1.3733 -0.0445 0.0581  0.0189  120  PHE   A CE2 
357   C  CZ  . PHE   A 51  ? 1.2297 1.2747 1.2931 -0.0442 0.0496  0.0169  120  PHE   A CZ  
358   N  N   . ALA   A 52  ? 1.2914 1.3487 1.4113 -0.0515 0.0677  0.0174  121  ALA   A N   
359   C  CA  . ALA   A 52  ? 1.2846 1.3365 1.3986 -0.0519 0.0672  0.0196  121  ALA   A CA  
360   C  C   . ALA   A 52  ? 1.3483 1.3879 1.4395 -0.0497 0.0679  0.0222  121  ALA   A C   
361   O  O   . ALA   A 52  ? 1.4488 1.4800 1.5302 -0.0484 0.0747  0.0236  121  ALA   A O   
362   C  CB  . ALA   A 52  ? 1.2586 1.3083 1.3836 -0.0538 0.0756  0.0208  121  ALA   A CB  
363   N  N   . VAL   A 53  ? 1.3297 1.3680 1.4122 -0.0490 0.0609  0.0229  122  VAL   A N   
364   C  CA  . VAL   A 53  ? 1.4200 1.4465 1.4812 -0.0468 0.0605  0.0253  122  VAL   A CA  
365   C  C   . VAL   A 53  ? 1.5125 1.5323 1.5712 -0.0472 0.0639  0.0277  122  VAL   A C   
366   O  O   . VAL   A 53  ? 1.5041 1.5278 1.5663 -0.0478 0.0580  0.0275  122  VAL   A O   
367   C  CB  . VAL   A 53  ? 1.3534 1.3827 1.4060 -0.0454 0.0500  0.0243  122  VAL   A CB  
368   C  CG1 . VAL   A 53  ? 1.5024 1.5190 1.5339 -0.0430 0.0495  0.0267  122  VAL   A CG1 
369   C  CG2 . VAL   A 53  ? 1.2936 1.3281 1.3477 -0.0449 0.0475  0.0222  122  VAL   A CG2 
370   N  N   . LEU   A 54  ? 1.5669 1.5758 1.6186 -0.0468 0.0736  0.0301  123  LEU   A N   
371   C  CA  . LEU   A 54  ? 1.6500 1.6513 1.6996 -0.0474 0.0786  0.0326  123  LEU   A CA  
372   C  C   . LEU   A 54  ? 1.8150 1.8076 1.8457 -0.0451 0.0734  0.0344  123  LEU   A C   
373   O  O   . LEU   A 54  ? 1.8641 1.8469 1.8764 -0.0425 0.0736  0.0356  123  LEU   A O   
374   C  CB  . LEU   A 54  ? 1.6134 1.6048 1.6600 -0.0474 0.0912  0.0348  123  LEU   A CB  
375   C  CG  . LEU   A 54  ? 1.4958 1.4932 1.5636 -0.0504 0.0988  0.0343  123  LEU   A CG  
376   C  CD1 . LEU   A 54  ? 1.5347 1.5328 1.6114 -0.0524 0.0991  0.0352  123  LEU   A CD1 
377   C  CD2 . LEU   A 54  ? 1.4845 1.4965 1.5695 -0.0517 0.0939  0.0307  123  LEU   A CD2 
378   N  N   . ALA   A 55  ? 2.2792 2.2749 2.3144 -0.0459 0.0686  0.0345  124  ALA   A N   
379   C  CA  . ALA   A 55  ? 2.2950 2.2834 2.3142 -0.0437 0.0630  0.0361  124  ALA   A CA  
380   C  C   . ALA   A 55  ? 2.3172 2.2936 2.3294 -0.0436 0.0704  0.0392  124  ALA   A C   
381   O  O   . ALA   A 55  ? 2.3182 2.2971 2.3391 -0.0452 0.0700  0.0395  124  ALA   A O   
382   C  CB  . ALA   A 55  ? 2.2737 2.2731 2.3012 -0.0443 0.0526  0.0342  124  ALA   A CB  
383   N  N   . TYR   A 56  ? 1.9964 1.9589 1.9918 -0.0415 0.0770  0.0415  125  TYR   A N   
384   C  CA  . TYR   A 56  ? 1.8938 1.8432 1.8808 -0.0411 0.0853  0.0447  125  TYR   A CA  
385   C  C   . TYR   A 56  ? 1.8756 1.8186 1.8498 -0.0391 0.0792  0.0461  125  TYR   A C   
386   O  O   . TYR   A 56  ? 1.8083 1.7528 1.7736 -0.0370 0.0698  0.0451  125  TYR   A O   
387   C  CB  . TYR   A 56  ? 1.8517 1.7873 1.8230 -0.0389 0.0942  0.0468  125  TYR   A CB  
388   C  CG  . TYR   A 56  ? 1.8529 1.7940 1.8309 -0.0394 0.0974  0.0451  125  TYR   A CG  
389   C  CD1 . TYR   A 56  ? 1.8115 1.7576 1.8067 -0.0421 0.1061  0.0449  125  TYR   A CD1 
390   C  CD2 . TYR   A 56  ? 1.8646 1.8053 1.8315 -0.0370 0.0917  0.0438  125  TYR   A CD2 
391   C  CE1 . TYR   A 56  ? 1.7642 1.7149 1.7652 -0.0423 0.1092  0.0433  125  TYR   A CE1 
392   C  CE2 . TYR   A 56  ? 1.8330 1.7780 1.8052 -0.0373 0.0947  0.0422  125  TYR   A CE2 
393   C  CZ  . TYR   A 56  ? 1.7932 1.7433 1.7822 -0.0398 0.1034  0.0420  125  TYR   A CZ  
394   O  OH  . TYR   A 56  ? 1.8080 1.7623 1.8020 -0.0398 0.1061  0.0404  125  TYR   A OH  
395   N  N   . ALA   A 64  ? 1.8840 1.8251 1.8919 -0.0461 0.1097  0.0486  133  ALA   A N   
396   C  CA  . ALA   A 64  ? 1.9072 1.8568 1.9307 -0.0488 0.1055  0.0476  133  ALA   A CA  
397   C  C   . ALA   A 64  ? 1.8276 1.7936 1.8769 -0.0522 0.1039  0.0444  133  ALA   A C   
398   O  O   . ALA   A 64  ? 1.7809 1.7509 1.8374 -0.0528 0.1083  0.0433  133  ALA   A O   
399   C  CB  . ALA   A 64  ? 1.9111 1.8624 1.9256 -0.0469 0.0936  0.0469  133  ALA   A CB  
400   N  N   . GLN   A 65  ? 1.6714 1.6463 1.7338 -0.0540 0.0975  0.0427  134  GLN   A N   
401   C  CA  . GLN   A 65  ? 1.5747 1.5634 1.6620 -0.0573 0.0967  0.0399  134  GLN   A CA  
402   C  C   . GLN   A 65  ? 1.5504 1.5524 1.6448 -0.0571 0.0846  0.0364  134  GLN   A C   
403   O  O   . GLN   A 65  ? 1.4729 1.4845 1.5846 -0.0592 0.0808  0.0343  134  GLN   A O   
404   C  CB  . GLN   A 65  ? 1.5092 1.4966 1.6087 -0.0601 0.1008  0.0407  134  GLN   A CB  
405   C  CG  . GLN   A 65  ? 1.5838 1.5626 1.6706 -0.0589 0.0979  0.0429  134  GLN   A CG  
406   C  CD  . GLN   A 65  ? 1.6603 1.6232 1.7351 -0.0585 0.1088  0.0469  134  GLN   A CD  
407   O  OE1 . GLN   A 65  ? 1.6479 1.6043 1.7173 -0.0580 0.1175  0.0484  134  GLN   A OE1 
408   N  NE2 . GLN   A 65  ? 1.6683 1.6244 1.7385 -0.0586 0.1085  0.0487  134  GLN   A NE2 
409   N  N   . PHE   A 66  ? 1.5913 1.5934 1.6723 -0.0544 0.0783  0.0360  135  PHE   A N   
410   C  CA  . PHE   A 66  ? 1.5145 1.5284 1.6010 -0.0540 0.0674  0.0330  135  PHE   A CA  
411   C  C   . PHE   A 66  ? 1.5436 1.5595 1.6224 -0.0522 0.0648  0.0320  135  PHE   A C   
412   O  O   . PHE   A 66  ? 1.5715 1.5784 1.6375 -0.0508 0.0703  0.0336  135  PHE   A O   
413   C  CB  . PHE   A 66  ? 1.5129 1.5254 1.5905 -0.0525 0.0593  0.0336  135  PHE   A CB  
414   C  CG  . PHE   A 66  ? 1.4369 1.4494 1.5234 -0.0542 0.0597  0.0340  135  PHE   A CG  
415   C  CD1 . PHE   A 66  ? 1.4880 1.4889 1.5683 -0.0546 0.0672  0.0370  135  PHE   A CD1 
416   C  CD2 . PHE   A 66  ? 1.3959 1.4191 1.4957 -0.0552 0.0523  0.0316  135  PHE   A CD2 
417   C  CE1 . PHE   A 66  ? 1.4367 1.4371 1.5249 -0.0562 0.0673  0.0374  135  PHE   A CE1 
418   C  CE2 . PHE   A 66  ? 1.3919 1.4145 1.4992 -0.0566 0.0521  0.0318  135  PHE   A CE2 
419   C  CZ  . PHE   A 66  ? 1.4295 1.4409 1.5313 -0.0572 0.0596  0.0347  135  PHE   A CZ  
420   N  N   . GLY   A 67  ? 1.5209 1.5480 1.6068 -0.0522 0.0562  0.0292  136  GLY   A N   
421   C  CA  . GLY   A 67  ? 1.4755 1.5057 1.5560 -0.0507 0.0530  0.0279  136  GLY   A CA  
422   C  C   . GLY   A 67  ? 1.3001 1.3437 1.3930 -0.0513 0.0447  0.0247  136  GLY   A C   
423   O  O   . GLY   A 67  ? 1.2669 1.3169 1.3707 -0.0524 0.0407  0.0236  136  GLY   A O   
424   N  N   . THR   A 68  ? 1.2536 1.3009 1.3443 -0.0504 0.0423  0.0233  137  THR   A N   
425   C  CA  . THR   A 68  ? 1.2097 1.2687 1.3102 -0.0506 0.0348  0.0204  137  THR   A CA  
426   C  C   . THR   A 68  ? 1.2031 1.2660 1.3096 -0.0510 0.0376  0.0187  137  THR   A C   
427   O  O   . THR   A 68  ? 1.2466 1.3028 1.3430 -0.0500 0.0422  0.0198  137  THR   A O   
428   C  CB  . THR   A 68  ? 1.1924 1.2521 1.2817 -0.0487 0.0263  0.0205  137  THR   A CB  
429   O  OG1 . THR   A 68  ? 1.2233 1.2809 1.3095 -0.0484 0.0231  0.0218  137  THR   A OG1 
430   C  CG2 . THR   A 68  ? 1.1318 1.2026 1.2302 -0.0488 0.0197  0.0178  137  THR   A CG2 
431   N  N   . THR   A 69  ? 1.1771 1.2504 1.2999 -0.0521 0.0351  0.0160  138  THR   A N   
432   C  CA  . THR   A 69  ? 1.1369 1.2150 1.2659 -0.0521 0.0364  0.0140  138  THR   A CA  
433   C  C   . THR   A 69  ? 1.1502 1.2299 1.2693 -0.0505 0.0302  0.0134  138  THR   A C   
434   O  O   . THR   A 69  ? 1.1684 1.2514 1.2847 -0.0498 0.0227  0.0131  138  THR   A O   
435   C  CB  . THR   A 69  ? 1.1017 1.1902 1.2504 -0.0535 0.0344  0.0112  138  THR   A CB  
436   O  OG1 . THR   A 69  ? 1.0914 1.1865 1.2420 -0.0529 0.0253  0.0097  138  THR   A OG1 
437   C  CG2 . THR   A 69  ? 1.1019 1.1891 1.2608 -0.0553 0.0390  0.0117  138  THR   A CG2 
438   N  N   . ALA   A 70  ? 1.1422 1.2195 1.2564 -0.0498 0.0333  0.0131  139  ALA   A N   
439   C  CA  . ALA   A 70  ? 1.1036 1.1818 1.2087 -0.0484 0.0279  0.0124  139  ALA   A CA  
440   C  C   . ALA   A 70  ? 1.1975 1.2826 1.3124 -0.0486 0.0279  0.0099  139  ALA   A C   
441   O  O   . ALA   A 70  ? 1.2348 1.3189 1.3554 -0.0490 0.0347  0.0096  139  ALA   A O   
442   C  CB  . ALA   A 70  ? 1.0892 1.1565 1.1759 -0.0469 0.0304  0.0145  139  ALA   A CB  
443   N  N   . GLU   A 71  ? 1.1671 1.2592 1.2843 -0.0481 0.0205  0.0081  140  GLU   A N   
444   C  CA  . GLU   A 71  ? 1.1378 1.2370 1.2645 -0.0481 0.0192  0.0055  140  GLU   A CA  
445   C  C   . GLU   A 71  ? 1.1678 1.2638 1.2830 -0.0469 0.0181  0.0054  140  GLU   A C   
446   O  O   . GLU   A 71  ? 1.2030 1.2978 1.3086 -0.0462 0.0125  0.0060  140  GLU   A O   
447   C  CB  . GLU   A 71  ? 1.0935 1.2020 1.2301 -0.0482 0.0120  0.0035  140  GLU   A CB  
448   C  CG  . GLU   A 71  ? 1.1289 1.2442 1.2758 -0.0479 0.0108  0.0007  140  GLU   A CG  
449   C  CD  . GLU   A 71  ? 1.1942 1.3168 1.3458 -0.0473 0.0029  -0.0011 140  GLU   A CD  
450   O  OE1 . GLU   A 71  ? 1.1277 1.2525 1.2819 -0.0474 -0.0008 -0.0009 140  GLU   A OE1 
451   O  OE2 . GLU   A 71  ? 1.2773 1.4030 1.4295 -0.0465 0.0005  -0.0027 140  GLU   A OE2 
452   N  N   . ILE   A 72  ? 1.2365 1.3310 1.3530 -0.0466 0.0232  0.0047  141  ILE   A N   
453   C  CA  . ILE   A 72  ? 1.2700 1.3613 1.3761 -0.0454 0.0222  0.0044  141  ILE   A CA  
454   C  C   . ILE   A 72  ? 1.2456 1.3447 1.3562 -0.0452 0.0148  0.0023  141  ILE   A C   
455   O  O   . ILE   A 72  ? 1.2405 1.3473 1.3645 -0.0456 0.0135  0.0003  141  ILE   A O   
456   C  CB  . ILE   A 72  ? 1.3067 1.3946 1.4140 -0.0450 0.0299  0.0041  141  ILE   A CB  
457   C  CG1 . ILE   A 72  ? 1.3032 1.3825 1.4055 -0.0450 0.0381  0.0064  141  ILE   A CG1 
458   C  CG2 . ILE   A 72  ? 1.3107 1.3946 1.4067 -0.0436 0.0288  0.0036  141  ILE   A CG2 
459   C  CD1 . ILE   A 72  ? 1.3517 1.4278 1.4567 -0.0445 0.0469  0.0063  141  ILE   A CD1 
460   N  N   . TYR   A 73  ? 1.1865 1.2833 1.2860 -0.0446 0.0096  0.0028  142  TYR   A N   
461   C  CA  . TYR   A 73  ? 1.2212 1.3243 1.3236 -0.0444 0.0031  0.0011  142  TYR   A CA  
462   C  C   . TYR   A 73  ? 1.2414 1.3406 1.3342 -0.0437 0.0023  0.0007  142  TYR   A C   
463   O  O   . TYR   A 73  ? 1.2837 1.3876 1.3788 -0.0435 -0.0023 -0.0007 142  TYR   A O   
464   C  CB  . TYR   A 73  ? 1.2428 1.3488 1.3437 -0.0447 -0.0035 0.0018  142  TYR   A CB  
465   C  CG  . TYR   A 73  ? 1.2195 1.3189 1.3063 -0.0443 -0.0058 0.0038  142  TYR   A CG  
466   C  CD1 . TYR   A 73  ? 1.1972 1.2945 1.2755 -0.0439 -0.0097 0.0036  142  TYR   A CD1 
467   C  CD2 . TYR   A 73  ? 1.2136 1.3086 1.2960 -0.0444 -0.0045 0.0057  142  TYR   A CD2 
468   C  CE1 . TYR   A 73  ? 1.2187 1.3101 1.2849 -0.0435 -0.0124 0.0051  142  TYR   A CE1 
469   C  CE2 . TYR   A 73  ? 1.2200 1.3087 1.2896 -0.0438 -0.0071 0.0073  142  TYR   A CE2 
470   C  CZ  . TYR   A 73  ? 1.2318 1.3189 1.2936 -0.0433 -0.0113 0.0069  142  TYR   A CZ  
471   O  OH  . TYR   A 73  ? 1.3482 1.4291 1.3978 -0.0426 -0.0145 0.0082  142  TYR   A OH  
472   N  N   . ALA   A 74  ? 1.2524 1.3429 1.3342 -0.0430 0.0068  0.0019  143  ALA   A N   
473   C  CA  . ALA   A 74  ? 1.2681 1.3536 1.3397 -0.0421 0.0062  0.0014  143  ALA   A CA  
474   C  C   . ALA   A 74  ? 1.3362 1.4144 1.4031 -0.0412 0.0142  0.0019  143  ALA   A C   
475   O  O   . ALA   A 74  ? 1.3851 1.4565 1.4459 -0.0409 0.0187  0.0037  143  ALA   A O   
476   C  CB  . ALA   A 74  ? 1.3116 1.3915 1.3696 -0.0418 0.0012  0.0027  143  ALA   A CB  
477   N  N   . TYR   A 75  ? 1.3399 1.4189 1.4090 -0.0405 0.0163  0.0003  144  TYR   A N   
478   C  CA  . TYR   A 75  ? 1.3443 1.4175 1.4112 -0.0395 0.0246  0.0005  144  TYR   A CA  
479   C  C   . TYR   A 75  ? 1.3436 1.4119 1.4011 -0.0381 0.0245  -0.0004 144  TYR   A C   
480   O  O   . TYR   A 75  ? 1.2964 1.3703 1.3597 -0.0381 0.0213  -0.0024 144  TYR   A O   
481   C  CB  . TYR   A 75  ? 1.3395 1.4200 1.4237 -0.0400 0.0293  -0.0007 144  TYR   A CB  
482   C  CG  . TYR   A 75  ? 1.3649 1.4402 1.4490 -0.0390 0.0387  -0.0003 144  TYR   A CG  
483   C  CD1 . TYR   A 75  ? 1.3908 1.4610 1.4741 -0.0392 0.0456  0.0017  144  TYR   A CD1 
484   C  CD2 . TYR   A 75  ? 1.3524 1.4273 1.4367 -0.0377 0.0409  -0.0018 144  TYR   A CD2 
485   C  CE1 . TYR   A 75  ? 1.3998 1.4648 1.4828 -0.0381 0.0549  0.0023  144  TYR   A CE1 
486   C  CE2 . TYR   A 75  ? 1.4174 1.4875 1.5017 -0.0365 0.0499  -0.0014 144  TYR   A CE2 
487   C  CZ  . TYR   A 75  ? 1.3870 1.4522 1.4709 -0.0368 0.0570  0.0007  144  TYR   A CZ  
488   O  OH  . TYR   A 75  ? 1.3179 1.3781 1.4019 -0.0356 0.0666  0.0013  144  TYR   A OH  
489   N  N   . ARG   A 76  ? 1.3707 1.4279 1.4136 -0.0367 0.0285  0.0010  145  ARG   A N   
490   C  CA  . ARG   A 76  ? 1.4267 1.4768 1.4570 -0.0352 0.0277  0.0004  145  ARG   A CA  
491   C  C   . ARG   A 76  ? 1.4963 1.5357 1.5169 -0.0333 0.0364  0.0016  145  ARG   A C   
492   O  O   . ARG   A 76  ? 1.5422 1.5740 1.5541 -0.0328 0.0394  0.0037  145  ARG   A O   
493   C  CB  . ARG   A 76  ? 1.4344 1.4803 1.4522 -0.0353 0.0198  0.0008  145  ARG   A CB  
494   C  CG  . ARG   A 76  ? 1.4151 1.4558 1.4221 -0.0342 0.0162  -0.0003 145  ARG   A CG  
495   C  CD  . ARG   A 76  ? 1.4435 1.4867 1.4478 -0.0354 0.0066  -0.0007 145  ARG   A CD  
496   N  NE  . ARG   A 76  ? 1.6018 1.6365 1.5922 -0.0349 0.0035  0.0008  145  ARG   A NE  
497   C  CZ  . ARG   A 76  ? 1.6181 1.6557 1.6101 -0.0359 -0.0011 0.0018  145  ARG   A CZ  
498   N  NH1 . ARG   A 76  ? 1.5456 1.5940 1.5519 -0.0376 -0.0026 0.0017  145  ARG   A NH1 
499   N  NH2 . ARG   A 76  ? 1.5611 1.5904 1.5396 -0.0351 -0.0047 0.0028  145  ARG   A NH2 
500   N  N   . GLU   A 77  ? 1.5438 1.5822 1.5656 -0.0320 0.0408  0.0004  146  GLU   A N   
501   C  CA  . GLU   A 77  ? 1.5827 1.6100 1.5935 -0.0297 0.0491  0.0015  146  GLU   A CA  
502   C  C   . GLU   A 77  ? 1.6988 1.7175 1.6934 -0.0279 0.0457  0.0007  146  GLU   A C   
503   O  O   . GLU   A 77  ? 1.7124 1.7347 1.7106 -0.0275 0.0440  -0.0013 146  GLU   A O   
504   C  CB  . GLU   A 77  ? 1.4908 1.5224 1.5147 -0.0292 0.0573  0.0007  146  GLU   A CB  
505   C  CG  . GLU   A 77  ? 1.4773 1.5202 1.5214 -0.0313 0.0587  0.0004  146  GLU   A CG  
506   C  CD  . GLU   A 77  ? 1.4422 1.4883 1.4992 -0.0307 0.0675  -0.0002 146  GLU   A CD  
507   O  OE1 . GLU   A 77  ? 1.3759 1.4152 1.4298 -0.0298 0.0764  0.0017  146  GLU   A OE1 
508   O  OE2 . GLU   A 77  ? 1.4715 1.5266 1.5417 -0.0309 0.0657  -0.0026 146  GLU   A OE2 
509   N  N   . GLU   A 78  ? 1.7575 1.7646 1.7339 -0.0266 0.0445  0.0022  147  GLU   A N   
510   C  CA  . GLU   A 78  ? 1.8626 1.8602 1.8224 -0.0248 0.0408  0.0014  147  GLU   A CA  
511   C  C   . GLU   A 78  ? 1.9949 1.9779 1.9388 -0.0217 0.0490  0.0029  147  GLU   A C   
512   O  O   . GLU   A 78  ? 2.0640 2.0371 1.9941 -0.0206 0.0490  0.0047  147  GLU   A O   
513   C  CB  . GLU   A 78  ? 1.8131 1.8092 1.7646 -0.0258 0.0307  0.0015  147  GLU   A CB  
514   N  N   . GLN   A 79  ? 2.0622 2.0437 2.0081 -0.0201 0.0560  0.0022  148  GLN   A N   
515   C  CA  . GLN   A 79  ? 2.1436 2.1110 2.0741 -0.0168 0.0643  0.0035  148  GLN   A CA  
516   C  C   . GLN   A 79  ? 2.2756 2.2294 2.1832 -0.0147 0.0587  0.0035  148  GLN   A C   
517   O  O   . GLN   A 79  ? 2.2519 2.2051 2.1550 -0.0144 0.0526  0.0015  148  GLN   A O   
518   C  CB  . GLN   A 79  ? 2.0580 2.0271 1.9947 -0.0153 0.0710  0.0022  148  GLN   A CB  
519   N  N   . ASP   A 80  ? 2.3886 2.3312 2.2818 -0.0133 0.0603  0.0056  149  ASP   A N   
520   C  CA  . ASP   A 80  ? 2.4155 2.3444 2.2864 -0.0111 0.0544  0.0056  149  ASP   A CA  
521   C  C   . ASP   A 80  ? 2.4629 2.3759 2.3165 -0.0077 0.0626  0.0081  149  ASP   A C   
522   O  O   . ASP   A 80  ? 2.4148 2.3291 2.2743 -0.0082 0.0695  0.0102  149  ASP   A O   
523   C  CB  . ASP   A 80  ? 2.4066 2.3399 2.2781 -0.0133 0.0432  0.0053  149  ASP   A CB  
524   N  N   . PHE   A 81  ? 2.5769 2.4745 2.4088 -0.0042 0.0616  0.0078  150  PHE   A N   
525   C  CA  . PHE   A 81  ? 2.6016 2.4818 2.4139 -0.0002 0.0697  0.0100  150  PHE   A CA  
526   C  C   . PHE   A 81  ? 2.5938 2.4744 2.4137 0.0008  0.0837  0.0114  150  PHE   A C   
527   O  O   . PHE   A 81  ? 2.5909 2.4635 2.4049 0.0024  0.0924  0.0141  150  PHE   A O   
528   C  CB  . PHE   A 81  ? 2.6209 2.4959 2.4260 -0.0002 0.0677  0.0121  150  PHE   A CB  
529   C  CG  . PHE   A 81  ? 2.6367 2.5181 2.4442 -0.0027 0.0543  0.0108  150  PHE   A CG  
530   C  CD1 . PHE   A 81  ? 2.6288 2.5038 2.4233 -0.0015 0.0443  0.0089  150  PHE   A CD1 
531   C  CD2 . PHE   A 81  ? 2.6273 2.5207 2.4502 -0.0060 0.0518  0.0116  150  PHE   A CD2 
532   C  CE1 . PHE   A 81  ? 2.6124 2.4937 2.4105 -0.0038 0.0324  0.0078  150  PHE   A CE1 
533   C  CE2 . PHE   A 81  ? 2.6219 2.5213 2.4475 -0.0080 0.0401  0.0106  150  PHE   A CE2 
534   C  CZ  . PHE   A 81  ? 2.6203 2.5138 2.4339 -0.0070 0.0306  0.0087  150  PHE   A CZ  
535   N  N   . GLY   A 82  ? 2.4909 2.3812 2.3248 -0.0001 0.0859  0.0097  151  GLY   A N   
536   C  CA  . GLY   A 82  ? 2.3971 2.2869 2.2373 0.0014  0.0988  0.0106  151  GLY   A CA  
537   C  C   . GLY   A 82  ? 2.3694 2.2674 2.2267 -0.0007 0.1070  0.0126  151  GLY   A C   
538   O  O   . GLY   A 82  ? 2.2661 2.1602 2.1252 0.0010  0.1190  0.0141  151  GLY   A O   
539   N  N   . ILE   A 83  ? 2.3486 2.2577 2.2187 -0.0043 0.1009  0.0126  152  ILE   A N   
540   C  CA  . ILE   A 83  ? 2.3030 2.2211 2.1910 -0.0068 0.1072  0.0142  152  ILE   A CA  
541   C  C   . ILE   A 83  ? 2.2505 2.1876 2.1609 -0.0110 0.0991  0.0122  152  ILE   A C   
542   O  O   . ILE   A 83  ? 2.2339 2.1747 2.1422 -0.0122 0.0879  0.0105  152  ILE   A O   
543   C  CB  . ILE   A 83  ? 2.2946 2.2028 2.1708 -0.0062 0.1093  0.0171  152  ILE   A CB  
544   C  CG1 . ILE   A 83  ? 2.2626 2.1815 2.1589 -0.0094 0.1140  0.0185  152  ILE   A CG1 
545   C  CG2 . ILE   A 83  ? 2.3232 2.2275 2.1860 -0.0063 0.0968  0.0165  152  ILE   A CG2 
546   C  CD1 . ILE   A 83  ? 2.2655 2.1868 2.1745 -0.0091 0.1271  0.0194  152  ILE   A CD1 
547   N  N   . GLU   A 84  ? 2.1845 2.1331 2.1165 -0.0132 0.1049  0.0122  153  GLU   A N   
548   C  CA  . GLU   A 84  ? 2.1802 2.1463 2.1338 -0.0168 0.0981  0.0102  153  GLU   A CA  
549   C  C   . GLU   A 84  ? 2.1594 2.1286 2.1148 -0.0191 0.0923  0.0114  153  GLU   A C   
550   O  O   . GLU   A 84  ? 2.1413 2.1156 2.1089 -0.0209 0.0966  0.0126  153  GLU   A O   
551   C  CB  . GLU   A 84  ? 2.1669 2.1435 2.1426 -0.0179 0.1058  0.0097  153  GLU   A CB  
552   N  N   . ILE   A 85  ? 2.1100 2.0761 2.0533 -0.0191 0.0823  0.0109  154  ILE   A N   
553   C  CA  . ILE   A 85  ? 1.9452 1.9152 1.8906 -0.0212 0.0755  0.0116  154  ILE   A CA  
554   C  C   . ILE   A 85  ? 1.8735 1.8608 1.8404 -0.0245 0.0694  0.0096  154  ILE   A C   
555   O  O   . ILE   A 85  ? 1.8706 1.8640 1.8417 -0.0249 0.0638  0.0073  154  ILE   A O   
556   C  CB  . ILE   A 85  ? 1.9823 1.9431 1.9081 -0.0199 0.0667  0.0117  154  ILE   A CB  
557   C  CG1 . ILE   A 85  ? 2.1426 2.0849 2.0451 -0.0161 0.0720  0.0132  154  ILE   A CG1 
558   C  CG2 . ILE   A 85  ? 1.9294 1.8938 1.8574 -0.0218 0.0607  0.0126  154  ILE   A CG2 
559   C  CD1 . ILE   A 85  ? 2.2037 2.1362 2.0864 -0.0144 0.0626  0.0126  154  ILE   A CD1 
560   N  N   . VAL   A 86  ? 1.8578 1.8525 1.8379 -0.0267 0.0705  0.0105  155  VAL   A N   
561   C  CA  . VAL   A 86  ? 1.7052 1.7146 1.7028 -0.0295 0.0635  0.0089  155  VAL   A CA  
562   C  C   . VAL   A 86  ? 1.6628 1.6715 1.6542 -0.0305 0.0558  0.0098  155  VAL   A C   
563   O  O   . VAL   A 86  ? 1.7052 1.7065 1.6888 -0.0300 0.0589  0.0121  155  VAL   A O   
564   C  CB  . VAL   A 86  ? 1.6069 1.6257 1.6249 -0.0313 0.0696  0.0088  155  VAL   A CB  
565   C  CG1 . VAL   A 86  ? 1.5394 1.5722 1.5737 -0.0337 0.0619  0.0070  155  VAL   A CG1 
566   C  CG2 . VAL   A 86  ? 1.6500 1.6694 1.6745 -0.0301 0.0773  0.0078  155  VAL   A CG2 
567   N  N   . LYS   A 87  ? 1.5546 1.5705 1.5490 -0.0316 0.0461  0.0082  156  LYS   A N   
568   C  CA  . LYS   A 87  ? 1.5501 1.5663 1.5396 -0.0324 0.0383  0.0089  156  LYS   A CA  
569   C  C   . LYS   A 87  ? 1.4740 1.5043 1.4817 -0.0349 0.0336  0.0078  156  LYS   A C   
570   O  O   . LYS   A 87  ? 1.4616 1.5005 1.4784 -0.0357 0.0296  0.0058  156  LYS   A O   
571   C  CB  . LYS   A 87  ? 1.5211 1.5321 1.4968 -0.0313 0.0305  0.0080  156  LYS   A CB  
572   N  N   . VAL   A 88  ? 1.4569 1.4889 1.4691 -0.0359 0.0343  0.0093  157  VAL   A N   
573   C  CA  . VAL   A 88  ? 1.4187 1.4631 1.4479 -0.0380 0.0308  0.0084  157  VAL   A CA  
574   C  C   . VAL   A 88  ? 1.3669 1.4116 1.3925 -0.0386 0.0246  0.0095  157  VAL   A C   
575   O  O   . VAL   A 88  ? 1.4069 1.4421 1.4182 -0.0374 0.0243  0.0112  157  VAL   A O   
576   C  CB  . VAL   A 88  ? 1.4001 1.4484 1.4433 -0.0390 0.0385  0.0087  157  VAL   A CB  
577   C  CG1 . VAL   A 88  ? 1.4265 1.4726 1.4718 -0.0380 0.0460  0.0079  157  VAL   A CG1 
578   C  CG2 . VAL   A 88  ? 1.3734 1.4151 1.4119 -0.0390 0.0429  0.0112  157  VAL   A CG2 
579   N  N   . LYS   A 89  ? 1.3236 1.3792 1.3621 -0.0402 0.0195  0.0085  158  LYS   A N   
580   C  CA  . LYS   A 89  ? 1.3047 1.3625 1.3426 -0.0407 0.0135  0.0094  158  LYS   A CA  
581   C  C   . LYS   A 89  ? 1.3117 1.3787 1.3659 -0.0422 0.0141  0.0089  158  LYS   A C   
582   O  O   . LYS   A 89  ? 1.3215 1.3968 1.3882 -0.0430 0.0137  0.0070  158  LYS   A O   
583   C  CB  . LYS   A 89  ? 1.3144 1.3760 1.3497 -0.0408 0.0047  0.0083  158  LYS   A CB  
584   C  CG  . LYS   A 89  ? 1.4104 1.4627 1.4289 -0.0394 0.0015  0.0090  158  LYS   A CG  
585   C  CD  . LYS   A 89  ? 1.4968 1.5534 1.5152 -0.0397 -0.0060 0.0075  158  LYS   A CD  
586   C  CE  . LYS   A 89  ? 1.5569 1.6143 1.5770 -0.0396 -0.0038 0.0058  158  LYS   A CE  
587   N  NZ  . LYS   A 89  ? 1.5965 1.6506 1.6077 -0.0391 -0.0092 0.0049  158  LYS   A NZ  
588   N  N   . ALA   A 90  ? 1.2688 1.3339 1.3227 -0.0425 0.0148  0.0106  159  ALA   A N   
589   C  CA  . ALA   A 90  ? 1.1730 1.2459 1.2418 -0.0439 0.0151  0.0101  159  ALA   A CA  
590   C  C   . ALA   A 90  ? 1.2005 1.2761 1.2686 -0.0441 0.0087  0.0108  159  ALA   A C   
591   O  O   . ALA   A 90  ? 1.2221 1.2923 1.2780 -0.0431 0.0052  0.0120  159  ALA   A O   
592   C  CB  . ALA   A 90  ? 1.0917 1.1606 1.1644 -0.0444 0.0236  0.0113  159  ALA   A CB  
593   N  N   . ILE   A 91  ? 1.1673 1.2511 1.2487 -0.0451 0.0068  0.0099  160  ILE   A N   
594   C  CA  . ILE   A 91  ? 1.1159 1.2024 1.1982 -0.0451 0.0016  0.0106  160  ILE   A CA  
595   C  C   . ILE   A 91  ? 1.1783 1.2654 1.2690 -0.0460 0.0052  0.0112  160  ILE   A C   
596   O  O   . ILE   A 91  ? 1.1726 1.2628 1.2743 -0.0470 0.0095  0.0101  160  ILE   A O   
597   C  CB  . ILE   A 91  ? 1.0375 1.1332 1.1267 -0.0452 -0.0054 0.0089  160  ILE   A CB  
598   C  CG1 . ILE   A 91  ? 1.0404 1.1380 1.1292 -0.0449 -0.0104 0.0099  160  ILE   A CG1 
599   C  CG2 . ILE   A 91  ? 1.0565 1.1596 1.1601 -0.0459 -0.0041 0.0068  160  ILE   A CG2 
600   C  CD1 . ILE   A 91  ? 1.0457 1.1517 1.1411 -0.0447 -0.0166 0.0086  160  ILE   A CD1 
601   N  N   . GLY   A 92  ? 1.1931 1.2775 1.2792 -0.0457 0.0032  0.0128  161  GLY   A N   
602   C  CA  . GLY   A 92  ? 1.1200 1.2033 1.2121 -0.0466 0.0066  0.0136  161  GLY   A CA  
603   C  C   . GLY   A 92  ? 1.0143 1.1070 1.1201 -0.0472 0.0025  0.0119  161  GLY   A C   
604   O  O   . GLY   A 92  ? 1.0091 1.1063 1.1145 -0.0465 -0.0041 0.0115  161  GLY   A O   
605   N  N   . ARG   A 93  ? 1.0148 1.1100 1.1327 -0.0485 0.0064  0.0110  162  ARG   A N   
606   C  CA  . ARG   A 93  ? 1.0871 1.1907 1.2185 -0.0489 0.0026  0.0089  162  ARG   A CA  
607   C  C   . ARG   A 93  ? 1.1060 1.2082 1.2417 -0.0495 0.0032  0.0098  162  ARG   A C   
608   O  O   . ARG   A 93  ? 1.1157 1.2201 1.2505 -0.0488 -0.0022 0.0099  162  ARG   A O   
609   C  CB  . ARG   A 93  ? 1.1086 1.2172 1.2521 -0.0496 0.0052  0.0066  162  ARG   A CB  
610   C  CG  . ARG   A 93  ? 1.0441 1.1540 1.1835 -0.0489 0.0045  0.0056  162  ARG   A CG  
611   C  CD  . ARG   A 93  ? 1.0139 1.1270 1.1474 -0.0477 -0.0029 0.0054  162  ARG   A CD  
612   N  NE  . ARG   A 93  ? 1.0218 1.1399 1.1592 -0.0472 -0.0049 0.0033  162  ARG   A NE  
613   C  CZ  . ARG   A 93  ? 0.9865 1.1083 1.1213 -0.0463 -0.0106 0.0026  162  ARG   A CZ  
614   N  NH1 . ARG   A 93  ? 0.9507 1.0720 1.0789 -0.0457 -0.0150 0.0039  162  ARG   A NH1 
615   N  NH2 . ARG   A 93  ? 0.9432 1.0693 1.0827 -0.0459 -0.0120 0.0006  162  ARG   A NH2 
616   N  N   . GLN   A 94  ? 1.0940 1.1924 1.2345 -0.0509 0.0098  0.0104  163  GLN   A N   
617   C  CA  . GLN   A 94  ? 1.1338 1.2317 1.2814 -0.0519 0.0107  0.0107  163  GLN   A CA  
618   C  C   . GLN   A 94  ? 1.1643 1.2524 1.3044 -0.0525 0.0176  0.0135  163  GLN   A C   
619   O  O   . GLN   A 94  ? 1.1858 1.2697 1.3243 -0.0531 0.0243  0.0142  163  GLN   A O   
620   C  CB  . GLN   A 94  ? 1.1692 1.2732 1.3344 -0.0533 0.0118  0.0082  163  GLN   A CB  
621   C  CG  . GLN   A 94  ? 1.1777 1.2903 1.3502 -0.0525 0.0062  0.0052  163  GLN   A CG  
622   C  CD  . GLN   A 94  ? 1.3115 1.4290 1.5007 -0.0537 0.0081  0.0027  163  GLN   A CD  
623   O  OE1 . GLN   A 94  ? 1.4602 1.5813 1.6598 -0.0540 0.0051  0.0011  163  GLN   A OE1 
624   N  NE2 . GLN   A 94  ? 1.2880 1.4055 1.4800 -0.0542 0.0132  0.0022  163  GLN   A NE2 
625   N  N   . ARG   A 95  ? 1.1834 1.2675 1.3188 -0.0523 0.0161  0.0151  164  ARG   A N   
626   C  CA  . ARG   A 95  ? 1.1863 1.2607 1.3150 -0.0528 0.0227  0.0178  164  ARG   A CA  
627   C  C   . ARG   A 95  ? 1.2174 1.2924 1.3606 -0.0552 0.0287  0.0172  164  ARG   A C   
628   O  O   . ARG   A 95  ? 1.2186 1.3016 1.3768 -0.0562 0.0262  0.0146  164  ARG   A O   
629   C  CB  . ARG   A 95  ? 1.1654 1.2354 1.2857 -0.0518 0.0192  0.0195  164  ARG   A CB  
630   N  N   . PHE   A 96  ? 1.2965 1.3625 1.4350 -0.0559 0.0368  0.0196  165  PHE   A N   
631   C  CA  . PHE   A 96  ? 1.2892 1.3552 1.4417 -0.0583 0.0436  0.0193  165  PHE   A CA  
632   C  C   . PHE   A 96  ? 1.3008 1.3553 1.4454 -0.0589 0.0511  0.0226  165  PHE   A C   
633   O  O   . PHE   A 96  ? 1.3234 1.3691 1.4504 -0.0571 0.0526  0.0251  165  PHE   A O   
634   C  CB  . PHE   A 96  ? 1.2807 1.3506 1.4416 -0.0590 0.0481  0.0178  165  PHE   A CB  
635   C  CG  . PHE   A 96  ? 1.2834 1.3453 1.4305 -0.0578 0.0545  0.0199  165  PHE   A CG  
636   C  CD1 . PHE   A 96  ? 1.3037 1.3548 1.4433 -0.0582 0.0633  0.0229  165  PHE   A CD1 
637   C  CD2 . PHE   A 96  ? 1.2787 1.3436 1.4207 -0.0564 0.0520  0.0187  165  PHE   A CD2 
638   C  CE1 . PHE   A 96  ? 1.3493 1.3923 1.4756 -0.0567 0.0692  0.0247  165  PHE   A CE1 
639   C  CE2 . PHE   A 96  ? 1.3179 1.3749 1.4470 -0.0552 0.0576  0.0204  165  PHE   A CE2 
640   C  CZ  . PHE   A 96  ? 1.3708 1.4167 1.4918 -0.0552 0.0662  0.0234  165  PHE   A CZ  
641   N  N   . LYS   A 97  ? 1.2595 1.3139 1.4174 -0.0612 0.0558  0.0225  166  LYS   A N   
642   C  CA  . LYS   A 97  ? 1.2862 1.3298 1.4395 -0.0622 0.0647  0.0256  166  LYS   A CA  
643   C  C   . LYS   A 97  ? 1.2276 1.2710 1.3922 -0.0642 0.0744  0.0256  166  LYS   A C   
644   O  O   . LYS   A 97  ? 1.2022 1.2540 1.3865 -0.0662 0.0741  0.0231  166  LYS   A O   
645   C  CB  . LYS   A 97  ? 1.2741 1.3168 1.4336 -0.0636 0.0627  0.0259  166  LYS   A CB  
646   N  N   . VAL   A 98  ? 1.2518 1.2852 1.4043 -0.0633 0.0829  0.0284  167  VAL   A N   
647   C  CA  . VAL   A 98  ? 1.2474 1.2811 1.4106 -0.0648 0.0925  0.0284  167  VAL   A CA  
648   C  C   . VAL   A 98  ? 1.2283 1.2617 1.4080 -0.0680 0.0984  0.0288  167  VAL   A C   
649   O  O   . VAL   A 98  ? 1.2627 1.2914 1.4400 -0.0687 0.0975  0.0301  167  VAL   A O   
650   C  CB  . VAL   A 98  ? 1.2471 1.2691 1.3927 -0.0630 0.1009  0.0314  167  VAL   A CB  
651   C  CG1 . VAL   A 98  ? 1.2997 1.3200 1.4267 -0.0598 0.0943  0.0314  167  VAL   A CG1 
652   C  CG2 . VAL   A 98  ? 1.3573 1.3658 1.4919 -0.0630 0.1081  0.0353  167  VAL   A CG2 
653   N  N   . LEU   A 99  ? 1.2022 1.2402 1.3990 -0.0699 0.1047  0.0276  168  LEU   A N   
654   C  CA  . LEU   A 99  ? 1.2060 1.2440 1.4205 -0.0732 0.1113  0.0278  168  LEU   A CA  
655   C  C   . LEU   A 99  ? 1.2369 1.2677 1.4525 -0.0740 0.1250  0.0304  168  LEU   A C   
656   O  O   . LEU   A 99  ? 1.3103 1.3329 1.5270 -0.0756 0.1331  0.0330  168  LEU   A O   
657   C  CB  . LEU   A 99  ? 1.1534 1.2054 1.3925 -0.0752 0.1054  0.0235  168  LEU   A CB  
658   C  CG  . LEU   A 99  ? 1.0873 1.1470 1.3269 -0.0743 0.0921  0.0206  168  LEU   A CG  
659   C  CD1 . LEU   A 99  ? 1.1049 1.1771 1.3678 -0.0758 0.0874  0.0163  168  LEU   A CD1 
660   C  CD2 . LEU   A 99  ? 1.0967 1.1506 1.3310 -0.0749 0.0898  0.0222  168  LEU   A CD2 
661   N  N   . GLU   A 100 ? 1.1855 1.2191 1.4015 -0.0728 0.1282  0.0296  169  GLU   A N   
662   C  CA  . GLU   A 100 ? 1.2074 1.2349 1.4248 -0.0730 0.1413  0.0317  169  GLU   A CA  
663   C  C   . GLU   A 100 ? 1.3730 1.3982 1.5750 -0.0698 0.1418  0.0320  169  GLU   A C   
664   O  O   . GLU   A 100 ? 1.4300 1.4650 1.6367 -0.0689 0.1343  0.0288  169  GLU   A O   
665   C  CB  . GLU   A 100 ? 1.2616 1.2989 1.5073 -0.0761 0.1456  0.0294  169  GLU   A CB  
666   C  CG  . GLU   A 100 ? 1.3013 1.3440 1.5658 -0.0793 0.1422  0.0278  169  GLU   A CG  
667   C  CD  . GLU   A 100 ? 1.4189 1.4713 1.7123 -0.0822 0.1461  0.0253  169  GLU   A CD  
668   O  OE1 . GLU   A 100 ? 1.3867 1.4426 1.6863 -0.0815 0.1512  0.0245  169  GLU   A OE1 
669   O  OE2 . GLU   A 100 ? 1.5236 1.5799 1.8341 -0.0851 0.1441  0.0239  169  GLU   A OE2 
670   N  N   . LEU   A 101 ? 1.4718 1.4835 1.6551 -0.0679 0.1506  0.0357  170  LEU   A N   
671   C  CA  . LEU   A 101 ? 1.5124 1.5200 1.6807 -0.0648 0.1527  0.0361  170  LEU   A CA  
672   C  C   . LEU   A 101 ? 1.5951 1.6002 1.7722 -0.0653 0.1659  0.0372  170  LEU   A C   
673   O  O   . LEU   A 101 ? 1.6204 1.6149 1.7939 -0.0657 0.1771  0.0406  170  LEU   A O   
674   C  CB  . LEU   A 101 ? 1.4541 1.4474 1.5931 -0.0616 0.1524  0.0392  170  LEU   A CB  
675   C  CG  . LEU   A 101 ? 1.4237 1.4193 1.5500 -0.0599 0.1392  0.0379  170  LEU   A CG  
676   C  CD1 . LEU   A 101 ? 1.3040 1.2843 1.4021 -0.0565 0.1406  0.0411  170  LEU   A CD1 
677   C  CD2 . LEU   A 101 ? 1.5456 1.5521 1.6771 -0.0590 0.1325  0.0345  170  LEU   A CD2 
678   N  N   . ARG   A 102 ? 1.6772 1.6918 1.8654 -0.0650 0.1650  0.0344  171  ARG   A N   
679   C  CA  . ARG   A 102 ? 1.6969 1.7104 1.8940 -0.0650 0.1769  0.0351  171  ARG   A CA  
680   C  C   . ARG   A 102 ? 1.7907 1.7985 1.9687 -0.0612 0.1780  0.0356  171  ARG   A C   
681   O  O   . ARG   A 102 ? 1.8512 1.8668 2.0281 -0.0600 0.1686  0.0327  171  ARG   A O   
682   C  CB  . ARG   A 102 ? 1.6767 1.7059 1.9037 -0.0676 0.1752  0.0313  171  ARG   A CB  
683   C  CG  . ARG   A 102 ? 1.6802 1.7225 1.9157 -0.0681 0.1604  0.0271  171  ARG   A CG  
684   C  CD  . ARG   A 102 ? 1.6867 1.7416 1.9527 -0.0711 0.1604  0.0240  171  ARG   A CD  
685   N  NE  . ARG   A 102 ? 1.7675 1.8357 2.0455 -0.0715 0.1474  0.0196  171  ARG   A NE  
686   C  CZ  . ARG   A 102 ? 1.6633 1.7373 1.9528 -0.0736 0.1400  0.0178  171  ARG   A CZ  
687   N  NH1 . ARG   A 102 ? 1.5991 1.6671 1.8890 -0.0757 0.1434  0.0201  171  ARG   A NH1 
688   N  NH2 . ARG   A 102 ? 1.6079 1.6936 1.9083 -0.0736 0.1289  0.0136  171  ARG   A NH2 
689   N  N   . THR   A 103 ? 1.8472 1.8408 2.0096 -0.0593 0.1894  0.0393  172  THR   A N   
690   C  CA  . THR   A 103 ? 1.8969 1.8826 2.0387 -0.0553 0.1912  0.0401  172  THR   A CA  
691   C  C   . THR   A 103 ? 1.9549 1.9459 2.1109 -0.0551 0.1991  0.0388  172  THR   A C   
692   O  O   . THR   A 103 ? 1.9810 1.9689 2.1475 -0.0563 0.2115  0.0407  172  THR   A O   
693   C  CB  . THR   A 103 ? 1.8773 1.8435 1.9928 -0.0527 0.1991  0.0446  172  THR   A CB  
694   O  OG1 . THR   A 103 ? 1.7845 1.7463 1.8882 -0.0529 0.1916  0.0456  172  THR   A OG1 
695   C  CG2 . THR   A 103 ? 1.9040 1.8615 1.9966 -0.0483 0.1993  0.0450  172  THR   A CG2 
696   N  N   . GLN   A 104 ? 2.1404 2.1396 2.2976 -0.0537 0.1919  0.0357  173  GLN   A N   
697   C  CA  . GLN   A 104 ? 2.1520 2.1576 2.3239 -0.0534 0.1981  0.0341  173  GLN   A CA  
698   C  C   . GLN   A 104 ? 2.2389 2.2302 2.3932 -0.0501 0.2102  0.0372  173  GLN   A C   
699   O  O   . GLN   A 104 ? 2.2768 2.2531 2.4064 -0.0478 0.2128  0.0404  173  GLN   A O   
700   C  CB  . GLN   A 104 ? 2.1482 2.1656 2.3247 -0.0526 0.1867  0.0299  173  GLN   A CB  
701   C  CG  . GLN   A 104 ? 2.1345 2.1677 2.3338 -0.0557 0.1767  0.0263  173  GLN   A CG  
702   C  CD  . GLN   A 104 ? 2.1537 2.1970 2.3553 -0.0545 0.1659  0.0224  173  GLN   A CD  
703   O  OE1 . GLN   A 104 ? 2.1561 2.1942 2.3382 -0.0517 0.1625  0.0226  173  GLN   A OE1 
704   N  NE2 . GLN   A 104 ? 2.1097 2.1674 2.3353 -0.0566 0.1605  0.0189  173  GLN   A NE2 
705   N  N   . SER   A 105 ? 2.1190 2.1148 2.2860 -0.0496 0.2175  0.0362  174  SER   A N   
706   C  CA  . SER   A 105 ? 2.0575 2.0401 2.2083 -0.0460 0.2292  0.0389  174  SER   A CA  
707   C  C   . SER   A 105 ? 2.0511 2.0261 2.1749 -0.0421 0.2222  0.0385  174  SER   A C   
708   O  O   . SER   A 105 ? 2.0443 2.0030 2.1437 -0.0388 0.2285  0.0416  174  SER   A O   
709   C  CB  . SER   A 105 ? 1.9898 1.9798 2.1617 -0.0463 0.2382  0.0377  174  SER   A CB  
710   O  OG  . SER   A 105 ? 2.0589 2.0649 2.2474 -0.0471 0.2283  0.0331  174  SER   A OG  
711   N  N   . ASP   A 106 ? 2.0384 2.0244 2.1655 -0.0423 0.2088  0.0348  175  ASP   A N   
712   C  CA  . ASP   A 106 ? 2.0274 2.0076 2.1311 -0.0390 0.2009  0.0341  175  ASP   A CA  
713   C  C   . ASP   A 106 ? 2.0057 1.9738 2.0849 -0.0379 0.1961  0.0364  175  ASP   A C   
714   O  O   . ASP   A 106 ? 1.9363 1.8948 1.9921 -0.0346 0.1927  0.0368  175  ASP   A O   
715   C  CB  . ASP   A 106 ? 1.9537 1.9492 2.0690 -0.0400 0.1878  0.0297  175  ASP   A CB  
716   N  N   . GLY   A 107 ? 1.9838 1.9521 2.0683 -0.0404 0.1954  0.0378  176  GLY   A N   
717   C  CA  . GLY   A 107 ? 1.9619 1.9217 2.0272 -0.0397 0.1890  0.0394  176  GLY   A CA  
718   C  C   . GLY   A 107 ? 1.9781 1.9503 2.0518 -0.0420 0.1745  0.0366  176  GLY   A C   
719   O  O   . GLY   A 107 ? 1.9537 1.9220 2.0199 -0.0426 0.1702  0.0380  176  GLY   A O   
720   N  N   . ILE   A 108 ? 2.0114 1.9978 2.0999 -0.0430 0.1671  0.0329  177  ILE   A N   
721   C  CA  . ILE   A 108 ? 1.9211 1.9198 2.0192 -0.0451 0.1540  0.0302  177  ILE   A CA  
722   C  C   . ILE   A 108 ? 1.8910 1.8955 2.0073 -0.0486 0.1554  0.0305  177  ILE   A C   
723   O  O   . ILE   A 108 ? 1.8987 1.9097 2.0359 -0.0506 0.1620  0.0298  177  ILE   A O   
724   C  CB  . ILE   A 108 ? 1.8711 1.8832 1.9829 -0.0453 0.1478  0.0262  177  ILE   A CB  
725   C  CG1 . ILE   A 108 ? 1.8445 1.8506 1.9435 -0.0421 0.1513  0.0261  177  ILE   A CG1 
726   C  CG2 . ILE   A 108 ? 1.8336 1.8541 1.9451 -0.0460 0.1335  0.0238  177  ILE   A CG2 
727   C  CD1 . ILE   A 108 ? 1.7980 1.8164 1.9134 -0.0424 0.1487  0.0226  177  ILE   A CD1 
728   N  N   . GLN   A 109 ? 1.8285 1.8308 1.9375 -0.0492 0.1489  0.0314  178  GLN   A N   
729   C  CA  . GLN   A 109 ? 1.8011 1.8070 1.9245 -0.0523 0.1498  0.0319  178  GLN   A CA  
730   C  C   . GLN   A 109 ? 1.8102 1.8318 1.9524 -0.0546 0.1390  0.0282  178  GLN   A C   
731   O  O   . GLN   A 109 ? 1.7749 1.8008 1.9104 -0.0536 0.1281  0.0265  178  GLN   A O   
732   C  CB  . GLN   A 109 ? 1.7705 1.7643 1.8752 -0.0515 0.1494  0.0350  178  GLN   A CB  
733   C  CG  . GLN   A 109 ? 1.8047 1.7829 1.8970 -0.0502 0.1626  0.0390  178  GLN   A CG  
734   C  CD  . GLN   A 109 ? 1.7364 1.7014 1.8079 -0.0488 0.1618  0.0421  178  GLN   A CD  
735   O  OE1 . GLN   A 109 ? 1.6122 1.5792 1.6762 -0.0484 0.1508  0.0412  178  GLN   A OE1 
736   N  NE2 . GLN   A 109 ? 1.6860 1.6371 1.7479 -0.0479 0.1737  0.0458  178  GLN   A NE2 
737   N  N   . GLN   A 110 ? 1.9041 1.9340 2.0699 -0.0576 0.1419  0.0271  179  GLN   A N   
738   C  CA  . GLN   A 110 ? 1.8438 1.8876 2.0286 -0.0597 0.1324  0.0236  179  GLN   A CA  
739   C  C   . GLN   A 110 ? 1.8225 1.8649 2.0101 -0.0618 0.1303  0.0248  179  GLN   A C   
740   O  O   . GLN   A 110 ? 1.8598 1.8928 2.0437 -0.0625 0.1389  0.0279  179  GLN   A O   
741   C  CB  . GLN   A 110 ? 1.8407 1.8951 2.0511 -0.0615 0.1360  0.0211  179  GLN   A CB  
742   C  CG  . GLN   A 110 ? 1.9237 1.9768 2.1327 -0.0596 0.1429  0.0209  179  GLN   A CG  
743   C  CD  . GLN   A 110 ? 1.9401 1.9980 2.1414 -0.0574 0.1341  0.0184  179  GLN   A CD  
744   O  OE1 . GLN   A 110 ? 1.9540 2.0054 2.1404 -0.0548 0.1374  0.0194  179  GLN   A OE1 
745   N  NE2 . GLN   A 110 ? 1.9795 2.0484 2.1904 -0.0582 0.1229  0.0152  179  GLN   A NE2 
746   N  N   . ALA   A 111 ? 1.5745 1.6257 1.7685 -0.0626 0.1190  0.0223  180  ALA   A N   
747   C  CA  . ALA   A 111 ? 1.4294 1.4782 1.6217 -0.0638 0.1153  0.0234  180  ALA   A CA  
748   C  C   . ALA   A 111 ? 1.3067 1.3678 1.5201 -0.0660 0.1078  0.0200  180  ALA   A C   
749   O  O   . ALA   A 111 ? 1.2976 1.3674 1.5137 -0.0652 0.0981  0.0171  180  ALA   A O   
750   C  CB  . ALA   A 111 ? 1.3534 1.3964 1.5229 -0.0615 0.1081  0.0246  180  ALA   A CB  
751   N  N   . LYS   A 112 ? 1.2658 1.3270 1.4935 -0.0687 0.1123  0.0205  181  LYS   A N   
752   C  CA  . LYS   A 112 ? 1.1722 1.2422 1.4158 -0.0706 0.1043  0.0178  181  LYS   A CA  
753   C  C   . LYS   A 112 ? 1.2004 1.2669 1.4289 -0.0695 0.0962  0.0187  181  LYS   A C   
754   O  O   . LYS   A 112 ? 1.2290 1.2848 1.4420 -0.0690 0.0999  0.0221  181  LYS   A O   
755   C  CB  . LYS   A 112 ? 1.2031 1.2728 1.4649 -0.0738 0.1114  0.0182  181  LYS   A CB  
756   C  CG  . LYS   A 112 ? 1.1992 1.2792 1.4819 -0.0759 0.1036  0.0146  181  LYS   A CG  
757   C  CD  . LYS   A 112 ? 1.2280 1.3107 1.5341 -0.0790 0.1113  0.0140  181  LYS   A CD  
758   C  CE  . LYS   A 112 ? 1.1994 1.2946 1.5286 -0.0803 0.1032  0.0092  181  LYS   A CE  
759   N  NZ  . LYS   A 112 ? 1.1690 1.2657 1.4986 -0.0808 0.0936  0.0079  181  LYS   A NZ  
760   N  N   . VAL   A 113 ? 1.2259 1.3012 1.4590 -0.0690 0.0852  0.0157  182  VAL   A N   
761   C  CA  . VAL   A 113 ? 1.1633 1.2366 1.3801 -0.0671 0.0767  0.0163  182  VAL   A CA  
762   C  C   . VAL   A 113 ? 1.1541 1.2349 1.3823 -0.0679 0.0676  0.0137  182  VAL   A C   
763   O  O   . VAL   A 113 ? 1.2257 1.3161 1.4700 -0.0685 0.0635  0.0102  182  VAL   A O   
764   C  CB  . VAL   A 113 ? 1.1598 1.2354 1.3650 -0.0645 0.0722  0.0154  182  VAL   A CB  
765   C  CG1 . VAL   A 113 ? 1.1991 1.2776 1.3959 -0.0630 0.0615  0.0146  182  VAL   A CG1 
766   C  CG2 . VAL   A 113 ? 1.1846 1.2499 1.3720 -0.0630 0.0793  0.0185  182  VAL   A CG2 
767   N  N   . GLN   A 114 ? 1.1396 1.2158 1.3591 -0.0677 0.0642  0.0152  183  GLN   A N   
768   C  CA  . GLN   A 114 ? 1.1774 1.2597 1.4048 -0.0679 0.0551  0.0128  183  GLN   A CA  
769   C  C   . GLN   A 114 ? 1.2685 1.3523 1.4815 -0.0651 0.0463  0.0126  183  GLN   A C   
770   O  O   . GLN   A 114 ? 1.2644 1.3409 1.4599 -0.0637 0.0466  0.0154  183  GLN   A O   
771   C  CB  . GLN   A 114 ? 1.2179 1.2947 1.4479 -0.0696 0.0570  0.0144  183  GLN   A CB  
772   C  CG  . GLN   A 114 ? 1.2736 1.3549 1.5082 -0.0693 0.0474  0.0123  183  GLN   A CG  
773   C  CD  . GLN   A 114 ? 1.3014 1.3899 1.5587 -0.0714 0.0455  0.0090  183  GLN   A CD  
774   O  OE1 . GLN   A 114 ? 1.2742 1.3624 1.5445 -0.0738 0.0526  0.0089  183  GLN   A OE1 
775   N  NE2 . GLN   A 114 ? 1.3458 1.4403 1.6078 -0.0704 0.0358  0.0061  183  GLN   A NE2 
776   N  N   . ILE   A 115 ? 1.3601 1.4532 1.5806 -0.0642 0.0384  0.0094  184  ILE   A N   
777   C  CA  . ILE   A 115 ? 1.3984 1.4938 1.6069 -0.0617 0.0304  0.0090  184  ILE   A CA  
778   C  C   . ILE   A 115 ? 1.3680 1.4605 1.5703 -0.0611 0.0256  0.0101  184  ILE   A C   
779   O  O   . ILE   A 115 ? 1.4287 1.5241 1.6417 -0.0619 0.0222  0.0084  184  ILE   A O   
780   C  CB  . ILE   A 115 ? 1.4203 1.5256 1.6385 -0.0608 0.0239  0.0054  184  ILE   A CB  
781   C  CG1 . ILE   A 115 ? 1.3849 1.4926 1.6076 -0.0611 0.0286  0.0045  184  ILE   A CG1 
782   C  CG2 . ILE   A 115 ? 1.4409 1.5483 1.6473 -0.0584 0.0161  0.0053  184  ILE   A CG2 
783   C  CD1 . ILE   A 115 ? 1.3100 1.4117 1.5163 -0.0600 0.0326  0.0071  184  ILE   A CD1 
784   N  N   . LEU   A 116 ? 1.3285 1.4149 1.5133 -0.0595 0.0251  0.0127  185  LEU   A N   
785   C  CA  . LEU   A 116 ? 1.3063 1.3898 1.4838 -0.0585 0.0205  0.0139  185  LEU   A CA  
786   C  C   . LEU   A 116 ? 1.4475 1.5391 1.6298 -0.0571 0.0111  0.0112  185  LEU   A C   
787   O  O   . LEU   A 116 ? 1.4583 1.5570 1.6468 -0.0566 0.0082  0.0088  185  LEU   A O   
788   C  CB  . LEU   A 116 ? 1.2931 1.3690 1.4510 -0.0567 0.0213  0.0169  185  LEU   A CB  
789   C  CG  . LEU   A 116 ? 1.3008 1.3665 1.4524 -0.0577 0.0305  0.0198  185  LEU   A CG  
790   C  CD1 . LEU   A 116 ? 1.2101 1.2670 1.3423 -0.0557 0.0300  0.0228  185  LEU   A CD1 
791   C  CD2 . LEU   A 116 ? 1.3405 1.4041 1.5042 -0.0602 0.0350  0.0199  185  LEU   A CD2 
792   N  N   . PRO   A 117 ? 1.5176 1.6080 1.6968 -0.0561 0.0064  0.0116  186  PRO   A N   
793   C  CA  . PRO   A 117 ? 1.5426 1.6400 1.7266 -0.0546 -0.0020 0.0092  186  PRO   A CA  
794   C  C   . PRO   A 117 ? 1.4778 1.5770 1.6497 -0.0519 -0.0074 0.0098  186  PRO   A C   
795   O  O   . PRO   A 117 ? 1.4424 1.5364 1.6011 -0.0510 -0.0064 0.0124  186  PRO   A O   
796   C  CB  . PRO   A 117 ? 1.5580 1.6523 1.7453 -0.0549 -0.0035 0.0094  186  PRO   A CB  
797   C  CG  . PRO   A 117 ? 1.5020 1.5870 1.6777 -0.0553 0.0017  0.0129  186  PRO   A CG  
798   C  CD  . PRO   A 117 ? 1.4800 1.5624 1.6543 -0.0567 0.0092  0.0140  186  PRO   A CD  
799   N  N   . GLU   A 118 ? 1.3772 1.4838 1.5542 -0.0506 -0.0133 0.0073  187  GLU   A N   
800   C  CA  . GLU   A 118 ? 1.2814 1.3907 1.4498 -0.0480 -0.0193 0.0076  187  GLU   A CA  
801   C  C   . GLU   A 118 ? 1.2376 1.3507 1.4124 -0.0466 -0.0253 0.0056  187  GLU   A C   
802   O  O   . GLU   A 118 ? 1.2464 1.3651 1.4287 -0.0460 -0.0285 0.0030  187  GLU   A O   
803   C  CB  . GLU   A 118 ? 1.2202 1.3339 1.3868 -0.0474 -0.0200 0.0068  187  GLU   A CB  
804   C  CG  . GLU   A 118 ? 1.2271 1.3431 1.3845 -0.0451 -0.0253 0.0074  187  GLU   A CG  
805   C  CD  . GLU   A 118 ? 1.2058 1.3160 1.3500 -0.0444 -0.0244 0.0105  187  GLU   A CD  
806   O  OE1 . GLU   A 118 ? 1.1331 1.2380 1.2720 -0.0456 -0.0193 0.0120  187  GLU   A OE1 
807   O  OE2 . GLU   A 118 ? 1.1829 1.2937 1.3216 -0.0425 -0.0288 0.0113  187  GLU   A OE2 
808   N  N   . CYS   A 119 ? 1.1850 1.2943 1.3562 -0.0460 -0.0267 0.0068  188  CYS   A N   
809   C  CA  . CYS   A 119 ? 1.1407 1.2519 1.3174 -0.0446 -0.0319 0.0050  188  CYS   A CA  
810   C  C   . CYS   A 119 ? 1.1408 1.2564 1.3127 -0.0416 -0.0378 0.0045  188  CYS   A C   
811   O  O   . CYS   A 119 ? 1.1843 1.2984 1.3463 -0.0400 -0.0393 0.0065  188  CYS   A O   
812   C  CB  . CYS   A 119 ? 1.1527 1.2577 1.3259 -0.0447 -0.0313 0.0067  188  CYS   A CB  
813   S  SG  . CYS   A 119 ? 1.2770 1.3764 1.4578 -0.0482 -0.0246 0.0071  188  CYS   A SG  
814   N  N   . VAL   A 120 ? 1.0408 1.1616 1.2199 -0.0408 -0.0411 0.0017  189  VAL   A N   
815   C  CA  . VAL   A 120 ? 0.9888 1.1133 1.1642 -0.0377 -0.0465 0.0010  189  VAL   A CA  
816   C  C   . VAL   A 120 ? 1.0187 1.1416 1.1954 -0.0359 -0.0505 0.0002  189  VAL   A C   
817   O  O   . VAL   A 120 ? 1.0699 1.1919 1.2554 -0.0367 -0.0513 -0.0019 189  VAL   A O   
818   C  CB  . VAL   A 120 ? 1.0009 1.1306 1.1822 -0.0373 -0.0482 -0.0015 189  VAL   A CB  
819   C  CG1 . VAL   A 120 ? 1.0372 1.1700 1.2124 -0.0344 -0.0523 -0.0014 189  VAL   A CG1 
820   C  CG2 . VAL   A 120 ? 1.1142 1.2447 1.2968 -0.0396 -0.0435 -0.0012 189  VAL   A CG2 
821   N  N   . LEU   A 121 ? 1.0081 1.1304 1.1764 -0.0334 -0.0532 0.0018  190  LEU   A N   
822   C  CA  . LEU   A 121 ? 1.0039 1.1238 1.1719 -0.0314 -0.0567 0.0014  190  LEU   A CA  
823   C  C   . LEU   A 121 ? 0.9866 1.1095 1.1508 -0.0277 -0.0614 0.0009  190  LEU   A C   
824   O  O   . LEU   A 121 ? 0.9806 1.1062 1.1388 -0.0267 -0.0614 0.0024  190  LEU   A O   
825   C  CB  . LEU   A 121 ? 0.9981 1.1127 1.1594 -0.0317 -0.0549 0.0041  190  LEU   A CB  
826   C  CG  . LEU   A 121 ? 0.9539 1.0637 1.1210 -0.0342 -0.0523 0.0037  190  LEU   A CG  
827   C  CD1 . LEU   A 121 ? 1.0620 1.1712 1.2323 -0.0376 -0.0466 0.0043  190  LEU   A CD1 
828   C  CD2 . LEU   A 121 ? 0.9345 1.0387 1.0947 -0.0334 -0.0522 0.0059  190  LEU   A CD2 
829   N  N   . PRO   A 122 ? 0.9944 1.1165 1.1618 -0.0256 -0.0653 -0.0012 191  PRO   A N   
830   C  CA  . PRO   A 122 ? 1.0044 1.1284 1.1676 -0.0217 -0.0694 -0.0016 191  PRO   A CA  
831   C  C   . PRO   A 122 ? 1.0735 1.1961 1.2281 -0.0195 -0.0699 0.0010  191  PRO   A C   
832   O  O   . PRO   A 122 ? 1.1122 1.2317 1.2639 -0.0209 -0.0678 0.0030  191  PRO   A O   
833   C  CB  . PRO   A 122 ? 1.1202 1.2420 1.2890 -0.0202 -0.0732 -0.0047 191  PRO   A CB  
834   C  CG  . PRO   A 122 ? 1.1700 1.2876 1.3429 -0.0229 -0.0715 -0.0046 191  PRO   A CG  
835   C  CD  . PRO   A 122 ? 1.0622 1.1809 1.2369 -0.0267 -0.0662 -0.0031 191  PRO   A CD  
836   N  N   . SER   A 123 ? 1.1190 1.2434 1.2695 -0.0160 -0.0727 0.0011  192  SER   A N   
837   C  CA  . SER   A 123 ? 1.1380 1.2613 1.2814 -0.0135 -0.0734 0.0035  192  SER   A CA  
838   C  C   . SER   A 123 ? 1.1645 1.2823 1.3074 -0.0130 -0.0744 0.0034  192  SER   A C   
839   O  O   . SER   A 123 ? 1.1779 1.2930 1.3258 -0.0132 -0.0761 0.0010  192  SER   A O   
840   C  CB  . SER   A 123 ? 1.1707 1.2962 1.3108 -0.0094 -0.0760 0.0033  192  SER   A CB  
841   O  OG  . SER   A 123 ? 1.1919 1.3158 1.3264 -0.0066 -0.0769 0.0051  192  SER   A OG  
842   N  N   . THR   A 124 ? 1.1370 1.2530 1.2741 -0.0124 -0.0736 0.0060  193  THR   A N   
843   C  CA  . THR   A 124 ? 1.0674 1.1778 1.2029 -0.0117 -0.0744 0.0063  193  THR   A CA  
844   C  C   . THR   A 124 ? 1.0936 1.2021 1.2288 -0.0080 -0.0784 0.0045  193  THR   A C   
845   O  O   . THR   A 124 ? 1.0172 1.1207 1.1544 -0.0080 -0.0798 0.0032  193  THR   A O   
846   C  CB  . THR   A 124 ? 0.9894 1.0986 1.1178 -0.0111 -0.0731 0.0095  193  THR   A CB  
847   O  OG1 . THR   A 124 ? 1.0775 1.1893 1.2015 -0.0072 -0.0752 0.0105  193  THR   A OG1 
848   C  CG2 . THR   A 124 ? 0.9928 1.1043 1.1202 -0.0140 -0.0699 0.0110  193  THR   A CG2 
849   N  N   . MET   A 125 ? 1.1143 1.2261 1.2474 -0.0048 -0.0801 0.0042  194  MET   A N   
850   C  CA  . MET   A 125 ? 1.1164 1.2261 1.2473 -0.0005 -0.0836 0.0028  194  MET   A CA  
851   C  C   . MET   A 125 ? 1.1771 1.2870 1.3127 -0.0001 -0.0859 -0.0005 194  MET   A C   
852   O  O   . MET   A 125 ? 1.1753 1.2835 1.3081 0.0040  -0.0888 -0.0018 194  MET   A O   
853   C  CB  . MET   A 125 ? 1.0890 1.2016 1.2139 0.0032  -0.0836 0.0048  194  MET   A CB  
854   C  CG  . MET   A 125 ? 1.0095 1.1217 1.1301 0.0033  -0.0821 0.0078  194  MET   A CG  
855   S  SD  . MET   A 125 ? 1.0913 1.1965 1.2084 0.0063  -0.0846 0.0074  194  MET   A SD  
856   C  CE  . MET   A 125 ? 1.0173 1.1172 1.1380 0.0019  -0.0838 0.0067  194  MET   A CE  
857   N  N   . SER   A 126 ? 1.2316 1.3432 1.3740 -0.0039 -0.0846 -0.0019 195  SER   A N   
858   C  CA  . SER   A 126 ? 1.2540 1.3664 1.4012 -0.0034 -0.0869 -0.0050 195  SER   A CA  
859   C  C   . SER   A 126 ? 1.2811 1.3880 1.4300 -0.0013 -0.0912 -0.0079 195  SER   A C   
860   O  O   . SER   A 126 ? 1.3015 1.4075 1.4502 0.0016  -0.0946 -0.0103 195  SER   A O   
861   C  CB  . SER   A 126 ? 1.2416 1.3569 1.3964 -0.0080 -0.0844 -0.0059 195  SER   A CB  
862   O  OG  . SER   A 126 ? 1.2510 1.3630 1.4117 -0.0110 -0.0839 -0.0068 195  SER   A OG  
863   N  N   . ALA   A 127 ? 1.2724 1.3750 1.4226 -0.0026 -0.0914 -0.0077 196  ALA   A N   
864   C  CA  . ALA   A 127 ? 1.2683 1.3652 1.4208 -0.0011 -0.0957 -0.0106 196  ALA   A CA  
865   C  C   . ALA   A 127 ? 1.3002 1.3927 1.4440 0.0038  -0.0983 -0.0099 196  ALA   A C   
866   O  O   . ALA   A 127 ? 1.3347 1.4224 1.4779 0.0068  -0.1029 -0.0126 196  ALA   A O   
867   C  CB  . ALA   A 127 ? 1.2375 1.3315 1.3968 -0.0053 -0.0943 -0.0109 196  ALA   A CB  
868   N  N   . VAL   A 128 ? 1.3148 1.4084 1.4517 0.0049  -0.0958 -0.0065 197  VAL   A N   
869   C  CA  . VAL   A 128 ? 1.3260 1.4155 1.4550 0.0097  -0.0979 -0.0058 197  VAL   A CA  
870   C  C   . VAL   A 128 ? 1.3428 1.4344 1.4657 0.0143  -0.0985 -0.0054 197  VAL   A C   
871   O  O   . VAL   A 128 ? 1.3598 1.4473 1.4762 0.0191  -0.1007 -0.0055 197  VAL   A O   
872   C  CB  . VAL   A 128 ? 1.3130 1.4020 1.4381 0.0089  -0.0951 -0.0025 197  VAL   A CB  
873   C  CG1 . VAL   A 128 ? 1.3549 1.4380 1.4734 0.0134  -0.0977 -0.0023 197  VAL   A CG1 
874   C  CG2 . VAL   A 128 ? 1.2877 1.3754 1.4187 0.0037  -0.0930 -0.0023 197  VAL   A CG2 
875   N  N   . GLN   A 129 ? 1.2675 1.3649 1.3922 0.0131  -0.0965 -0.0049 198  GLN   A N   
876   C  CA  . GLN   A 129 ? 1.2453 1.3447 1.3645 0.0171  -0.0963 -0.0042 198  GLN   A CA  
877   C  C   . GLN   A 129 ? 1.2735 1.3671 1.3888 0.0220  -0.1006 -0.0069 198  GLN   A C   
878   O  O   . GLN   A 129 ? 1.3155 1.4069 1.4349 0.0214  -0.1037 -0.0102 198  GLN   A O   
879   C  CB  . GLN   A 129 ? 1.2485 1.3540 1.3714 0.0146  -0.0941 -0.0041 198  GLN   A CB  
880   C  CG  . GLN   A 129 ? 1.2659 1.3745 1.3837 0.0177  -0.0924 -0.0023 198  GLN   A CG  
881   C  CD  . GLN   A 129 ? 1.3091 1.4210 1.4238 0.0178  -0.0893 0.0014  198  GLN   A CD  
882   O  OE1 . GLN   A 129 ? 1.3121 1.4220 1.4214 0.0219  -0.0895 0.0027  198  GLN   A OE1 
883   N  NE2 . GLN   A 129 ? 1.3532 1.4700 1.4716 0.0135  -0.0866 0.0030  198  GLN   A NE2 
884   N  N   . LEU   A 130 ? 1.2652 1.3559 1.3725 0.0270  -0.1009 -0.0056 199  LEU   A N   
885   C  CA  . LEU   A 130 ? 1.2284 1.3126 1.3299 0.0324  -0.1047 -0.0079 199  LEU   A CA  
886   C  C   . LEU   A 130 ? 1.2457 1.3313 1.3464 0.0339  -0.1051 -0.0093 199  LEU   A C   
887   O  O   . LEU   A 130 ? 1.2752 1.3668 1.3764 0.0328  -0.1014 -0.0072 199  LEU   A O   
888   C  CB  . LEU   A 130 ? 1.1790 1.2604 1.2716 0.0375  -0.1038 -0.0056 199  LEU   A CB  
889   C  CG  . LEU   A 130 ? 1.1359 1.2095 1.2248 0.0401  -0.1072 -0.0069 199  LEU   A CG  
890   C  CD1 . LEU   A 130 ? 1.1181 1.1928 1.2122 0.0355  -0.1063 -0.0059 199  LEU   A CD1 
891   C  CD2 . LEU   A 130 ? 1.1589 1.2291 1.2382 0.0462  -0.1063 -0.0050 199  LEU   A CD2 
892   N  N   . GLU   A 131 ? 1.2315 1.3111 1.3310 0.0365  -0.1098 -0.0129 200  GLU   A N   
893   C  CA  . GLU   A 131 ? 1.2536 1.3334 1.3520 0.0382  -0.1108 -0.0146 200  GLU   A CA  
894   C  C   . GLU   A 131 ? 1.2223 1.3030 1.3124 0.0424  -0.1075 -0.0119 200  GLU   A C   
895   O  O   . GLU   A 131 ? 1.2394 1.3245 1.3305 0.0414  -0.1050 -0.0112 200  GLU   A O   
896   C  CB  . GLU   A 131 ? 1.2940 1.3658 1.3908 0.0414  -0.1172 -0.0189 200  GLU   A CB  
897   C  CG  . GLU   A 131 ? 1.3121 1.3849 1.4197 0.0369  -0.1203 -0.0222 200  GLU   A CG  
898   C  CD  . GLU   A 131 ? 1.3339 1.4094 1.4492 0.0316  -0.1186 -0.0212 200  GLU   A CD  
899   O  OE1 . GLU   A 131 ? 1.2681 1.3397 1.3794 0.0331  -0.1191 -0.0202 200  GLU   A OE1 
900   O  OE2 . GLU   A 131 ? 1.3384 1.4196 1.4631 0.0262  -0.1166 -0.0212 200  GLU   A OE2 
901   N  N   . SER   A 132 ? 1.2474 1.3237 1.3294 0.0471  -0.1071 -0.0105 201  SER   A N   
902   C  CA  . SER   A 132 ? 1.2391 1.3164 1.3139 0.0511  -0.1032 -0.0076 201  SER   A CA  
903   C  C   . SER   A 132 ? 1.2499 1.3367 1.3298 0.0470  -0.0978 -0.0040 201  SER   A C   
904   O  O   . SER   A 132 ? 1.2831 1.3732 1.3613 0.0479  -0.0944 -0.0022 201  SER   A O   
905   C  CB  . SER   A 132 ? 1.2166 1.2876 1.2828 0.0566  -0.1035 -0.0066 201  SER   A CB  
906   O  OG  . SER   A 132 ? 1.1375 1.2093 1.2070 0.0541  -0.1038 -0.0058 201  SER   A OG  
907   N  N   . LEU   A 133 ? 1.2653 1.3559 1.3510 0.0426  -0.0970 -0.0029 202  LEU   A N   
908   C  CA  . LEU   A 133 ? 1.2956 1.3945 1.3860 0.0387  -0.0927 0.0003  202  LEU   A CA  
909   C  C   . LEU   A 133 ? 1.3576 1.4620 1.4547 0.0338  -0.0917 -0.0004 202  LEU   A C   
910   O  O   . LEU   A 133 ? 1.3901 1.5010 1.4904 0.0308  -0.0882 0.0020  202  LEU   A O   
911   C  CB  . LEU   A 133 ? 1.2636 1.3631 1.3565 0.0363  -0.0926 0.0014  202  LEU   A CB  
912   C  CG  . LEU   A 133 ? 1.1677 1.2659 1.2551 0.0402  -0.0911 0.0040  202  LEU   A CG  
913   C  CD1 . LEU   A 133 ? 1.2905 1.3959 1.3792 0.0398  -0.0868 0.0072  202  LEU   A CD1 
914   C  CD2 . LEU   A 133 ? 1.1513 1.2424 1.2307 0.0467  -0.0929 0.0029  202  LEU   A CD2 
915   N  N   . ASN   A 134 ? 1.3765 1.4781 1.4760 0.0330  -0.0948 -0.0038 203  ASN   A N   
916   C  CA  . ASN   A 134 ? 1.3722 1.4786 1.4780 0.0287  -0.0940 -0.0046 203  ASN   A CA  
917   C  C   . ASN   A 134 ? 1.3639 1.4737 1.4670 0.0300  -0.0909 -0.0029 203  ASN   A C   
918   O  O   . ASN   A 134 ? 1.3662 1.4820 1.4737 0.0261  -0.0883 -0.0018 203  ASN   A O   
919   C  CB  . ASN   A 134 ? 1.3535 1.4558 1.4623 0.0285  -0.0984 -0.0088 203  ASN   A CB  
920   C  CG  . ASN   A 134 ? 1.3744 1.4774 1.4915 0.0236  -0.0997 -0.0102 203  ASN   A CG  
921   O  OD1 . ASN   A 134 ? 1.3462 1.4441 1.4650 0.0244  -0.1039 -0.0132 203  ASN   A OD1 
922   N  ND2 . ASN   A 134 ? 1.3697 1.4785 1.4918 0.0187  -0.0962 -0.0082 203  ASN   A ND2 
923   N  N   . LYS   A 135 ? 1.4445 1.5501 1.5399 0.0355  -0.0910 -0.0027 204  LYS   A N   
924   C  CA  . LYS   A 135 ? 1.4352 1.5430 1.5277 0.0370  -0.0879 -0.0011 204  LYS   A CA  
925   C  C   . LYS   A 135 ? 1.4701 1.5844 1.5642 0.0354  -0.0832 0.0028  204  LYS   A C   
926   O  O   . LYS   A 135 ? 1.4690 1.5882 1.5656 0.0334  -0.0803 0.0042  204  LYS   A O   
927   C  CB  . LYS   A 135 ? 1.4326 1.5331 1.5157 0.0438  -0.0888 -0.0018 204  LYS   A CB  
928   C  CG  . LYS   A 135 ? 1.4357 1.5288 1.5161 0.0462  -0.0942 -0.0059 204  LYS   A CG  
929   C  CD  . LYS   A 135 ? 1.4333 1.5284 1.5182 0.0434  -0.0953 -0.0080 204  LYS   A CD  
930   C  CE  . LYS   A 135 ? 1.4272 1.5162 1.5124 0.0448  -0.1014 -0.0125 204  LYS   A CE  
931   N  NZ  . LYS   A 135 ? 1.4567 1.5454 1.5474 0.0422  -0.1042 -0.0138 204  LYS   A NZ  
932   N  N   . CYS   A 136 ? 1.5422 1.6565 1.6353 0.0365  -0.0825 0.0046  205  CYS   A N   
933   C  CA  . CYS   A 136 ? 1.5407 1.6611 1.6357 0.0356  -0.0786 0.0082  205  CYS   A CA  
934   C  C   . CYS   A 136 ? 1.5727 1.6989 1.6747 0.0297  -0.0781 0.0090  205  CYS   A C   
935   O  O   . CYS   A 136 ? 1.5918 1.7209 1.6951 0.0290  -0.0769 0.0112  205  CYS   A O   
936   C  CB  . CYS   A 136 ? 1.4987 1.6160 1.5891 0.0399  -0.0783 0.0097  205  CYS   A CB  
937   S  SG  . CYS   A 136 ? 1.5897 1.6968 1.6704 0.0469  -0.0808 0.0076  205  CYS   A SG  
938   N  N   . GLN   A 137 ? 1.4922 1.6198 1.5985 0.0256  -0.0791 0.0072  206  GLN   A N   
939   C  CA  . GLN   A 137 ? 1.4555 1.5873 1.5673 0.0203  -0.0787 0.0077  206  GLN   A CA  
940   C  C   . GLN   A 137 ? 1.4201 1.5580 1.5353 0.0171  -0.0760 0.0091  206  GLN   A C   
941   O  O   . GLN   A 137 ? 1.4187 1.5608 1.5359 0.0151  -0.0744 0.0114  206  GLN   A O   
942   C  CB  . GLN   A 137 ? 1.4467 1.5757 1.5617 0.0177  -0.0813 0.0047  206  GLN   A CB  
943   C  CG  . GLN   A 137 ? 1.4191 1.5438 1.5333 0.0183  -0.0834 0.0041  206  GLN   A CG  
944   C  CD  . GLN   A 137 ? 1.4430 1.5695 1.5554 0.0189  -0.0818 0.0071  206  GLN   A CD  
945   O  OE1 . GLN   A 137 ? 1.4395 1.5628 1.5474 0.0230  -0.0825 0.0078  206  GLN   A OE1 
946   N  NE2 . GLN   A 137 ? 1.3687 1.4999 1.4843 0.0151  -0.0798 0.0089  206  GLN   A NE2 
947   N  N   . ILE   A 138 ? 1.3581 1.4963 1.4739 0.0167  -0.0758 0.0078  207  ILE   A N   
948   C  CA  . ILE   A 138 ? 1.3224 1.4658 1.4412 0.0135  -0.0735 0.0089  207  ILE   A CA  
949   C  C   . ILE   A 138 ? 1.3351 1.4826 1.4540 0.0141  -0.0709 0.0121  207  ILE   A C   
950   O  O   . ILE   A 138 ? 1.3427 1.4897 1.4588 0.0178  -0.0695 0.0133  207  ILE   A O   
951   C  CB  . ILE   A 138 ? 1.3133 1.4555 1.4308 0.0146  -0.0733 0.0074  207  ILE   A CB  
952   C  CG1 . ILE   A 138 ? 1.3560 1.4958 1.4759 0.0128  -0.0759 0.0042  207  ILE   A CG1 
953   C  CG2 . ILE   A 138 ? 1.2832 1.4304 1.4030 0.0121  -0.0706 0.0091  207  ILE   A CG2 
954   C  CD1 . ILE   A 138 ? 1.2985 1.4425 1.4236 0.0075  -0.0748 0.0040  207  ILE   A CD1 
955   N  N   . PHE   A 139 ? 1.3780 1.5296 1.5003 0.0105  -0.0703 0.0135  208  PHE   A N   
956   C  CA  . PHE   A 139 ? 1.3590 1.5148 1.4826 0.0108  -0.0686 0.0163  208  PHE   A CA  
957   C  C   . PHE   A 139 ? 1.3669 1.5264 1.4921 0.0104  -0.0662 0.0174  208  PHE   A C   
958   O  O   . PHE   A 139 ? 1.3875 1.5479 1.5142 0.0076  -0.0660 0.0164  208  PHE   A O   
959   C  CB  . PHE   A 139 ? 1.3678 1.5260 1.4938 0.0072  -0.0692 0.0172  208  PHE   A CB  
960   C  CG  . PHE   A 139 ? 1.3222 1.4773 1.4464 0.0082  -0.0708 0.0171  208  PHE   A CG  
961   C  CD1 . PHE   A 139 ? 1.3230 1.4737 1.4463 0.0072  -0.0724 0.0150  208  PHE   A CD1 
962   C  CD2 . PHE   A 139 ? 1.3083 1.4647 1.4321 0.0102  -0.0707 0.0192  208  PHE   A CD2 
963   C  CE1 . PHE   A 139 ? 1.2821 1.4293 1.4037 0.0080  -0.0737 0.0150  208  PHE   A CE1 
964   C  CE2 . PHE   A 139 ? 1.2770 1.4300 1.3986 0.0112  -0.0722 0.0192  208  PHE   A CE2 
965   C  CZ  . PHE   A 139 ? 1.2737 1.4219 1.3939 0.0101  -0.0737 0.0171  208  PHE   A CZ  
966   N  N   . PRO   A 140 ? 1.3487 1.5100 1.4739 0.0132  -0.0642 0.0196  209  PRO   A N   
967   C  CA  . PRO   A 140 ? 1.4043 1.5695 1.5322 0.0123  -0.0617 0.0209  209  PRO   A CA  
968   C  C   . PRO   A 140 ? 1.5012 1.6712 1.6339 0.0075  -0.0621 0.0215  209  PRO   A C   
969   O  O   . PRO   A 140 ? 1.4825 1.6539 1.6166 0.0062  -0.0636 0.0221  209  PRO   A O   
970   C  CB  . PRO   A 140 ? 1.3633 1.5299 1.4914 0.0162  -0.0593 0.0233  209  PRO   A CB  
971   C  CG  . PRO   A 140 ? 1.3438 1.5086 1.4702 0.0183  -0.0610 0.0235  209  PRO   A CG  
972   C  CD  . PRO   A 140 ? 1.3324 1.4925 1.4556 0.0174  -0.0639 0.0209  209  PRO   A CD  
973   N  N   . SER   A 141 ? 1.5826 1.7542 1.7170 0.0051  -0.0611 0.0212  210  SER   A N   
974   C  CA  . SER   A 141 ? 1.5934 1.7681 1.7310 0.0004  -0.0619 0.0211  210  SER   A CA  
975   C  C   . SER   A 141 ? 1.5837 1.7625 1.7249 -0.0010 -0.0627 0.0229  210  SER   A C   
976   O  O   . SER   A 141 ? 1.5454 1.7263 1.6884 0.0014  -0.0620 0.0248  210  SER   A O   
977   C  CB  . SER   A 141 ? 1.5637 1.7401 1.7029 -0.0011 -0.0601 0.0212  210  SER   A CB  
978   O  OG  . SER   A 141 ? 1.5211 1.6935 1.6567 0.0008  -0.0595 0.0196  210  SER   A OG  
979   N  N   . SER   A 151 ? 1.8061 2.0040 1.9668 0.0013  -0.0778 0.0324  220  SER   A N   
980   C  CA  . SER   A 151 ? 1.9604 2.1571 2.1194 0.0005  -0.0818 0.0324  220  SER   A CA  
981   C  C   . SER   A 151 ? 2.0219 2.2118 2.1721 0.0014  -0.0827 0.0317  220  SER   A C   
982   O  O   . SER   A 151 ? 1.9144 2.0994 2.0587 -0.0008 -0.0821 0.0305  220  SER   A O   
983   C  CB  . SER   A 151 ? 1.9741 2.1762 2.1403 0.0029  -0.0836 0.0338  220  SER   A CB  
984   O  OG  . SER   A 151 ? 1.9163 2.1205 2.0852 0.0066  -0.0807 0.0349  220  SER   A OG  
985   N  N   . TYR   A 152 ? 2.1344 2.3238 2.2840 0.0047  -0.0838 0.0327  221  TYR   A N   
986   C  CA  . TYR   A 152 ? 2.1048 2.2875 2.2466 0.0059  -0.0846 0.0323  221  TYR   A CA  
987   C  C   . TYR   A 152 ? 2.0806 2.2619 2.2211 0.0094  -0.0824 0.0326  221  TYR   A C   
988   O  O   . TYR   A 152 ? 2.0605 2.2358 2.1946 0.0096  -0.0820 0.0319  221  TYR   A O   
989   C  CB  . TYR   A 152 ? 2.1324 2.3141 2.2727 0.0071  -0.0885 0.0330  221  TYR   A CB  
990   C  CG  . TYR   A 152 ? 2.2336 2.4184 2.3773 0.0049  -0.0915 0.0330  221  TYR   A CG  
991   C  CD1 . TYR   A 152 ? 2.2926 2.4754 2.4338 0.0011  -0.0915 0.0319  221  TYR   A CD1 
992   C  CD2 . TYR   A 152 ? 2.2408 2.4303 2.3906 0.0067  -0.0945 0.0339  221  TYR   A CD2 
993   C  CE1 . TYR   A 152 ? 2.3199 2.5047 2.4636 -0.0008 -0.0946 0.0317  221  TYR   A CE1 
994   C  CE2 . TYR   A 152 ? 2.3011 2.4931 2.4543 0.0047  -0.0979 0.0336  221  TYR   A CE2 
995   C  CZ  . TYR   A 152 ? 2.3461 2.5354 2.4957 0.0009  -0.0980 0.0324  221  TYR   A CZ  
996   O  OH  . TYR   A 152 ? 2.3974 2.5885 2.5498 -0.0009 -0.1017 0.0320  221  TYR   A OH  
997   N  N   . LYS   A 153 ? 1.8835 2.0699 2.0300 0.0122  -0.0809 0.0337  222  LYS   A N   
998   C  CA  . LYS   A 153 ? 1.7837 1.9682 1.9283 0.0157  -0.0784 0.0339  222  LYS   A CA  
999   C  C   . LYS   A 153 ? 1.7039 1.8846 1.8446 0.0144  -0.0762 0.0325  222  LYS   A C   
1000  O  O   . LYS   A 153 ? 1.6601 1.8365 1.7964 0.0167  -0.0753 0.0319  222  LYS   A O   
1001  C  CB  . LYS   A 153 ? 1.7755 1.9660 1.9273 0.0187  -0.0763 0.0354  222  LYS   A CB  
1002  C  CG  . LYS   A 153 ? 1.7827 1.9770 1.9390 0.0211  -0.0784 0.0368  222  LYS   A CG  
1003  C  CD  . LYS   A 153 ? 1.8894 2.0898 2.0537 0.0240  -0.0754 0.0384  222  LYS   A CD  
1004  C  CE  . LYS   A 153 ? 1.8777 2.0820 2.0473 0.0270  -0.0774 0.0398  222  LYS   A CE  
1005  N  NZ  . LYS   A 153 ? 1.8884 2.0990 2.0667 0.0299  -0.0738 0.0415  222  LYS   A NZ  
1006  N  N   . TRP   A 154 ? 1.5590 1.7413 1.7014 0.0108  -0.0756 0.0317  223  TRP   A N   
1007  C  CA  . TRP   A 154 ? 1.3826 1.5614 1.5217 0.0095  -0.0739 0.0301  223  TRP   A CA  
1008  C  C   . TRP   A 154 ? 1.3726 1.5447 1.5052 0.0086  -0.0751 0.0288  223  TRP   A C   
1009  O  O   . TRP   A 154 ? 1.3667 1.5351 1.4965 0.0094  -0.0741 0.0276  223  TRP   A O   
1010  C  CB  . TRP   A 154 ? 1.3382 1.5196 1.4800 0.0057  -0.0733 0.0295  223  TRP   A CB  
1011  C  CG  . TRP   A 154 ? 1.2087 1.3865 1.3472 0.0040  -0.0721 0.0277  223  TRP   A CG  
1012  C  CD1 . TRP   A 154 ? 1.1918 1.3653 1.3264 0.0014  -0.0730 0.0262  223  TRP   A CD1 
1013  C  CD2 . TRP   A 154 ? 1.2709 1.4486 1.4098 0.0052  -0.0698 0.0271  223  TRP   A CD2 
1014  N  NE1 . TRP   A 154 ? 1.1182 1.2897 1.2517 0.0007  -0.0716 0.0247  223  TRP   A NE1 
1015  C  CE2 . TRP   A 154 ? 1.3029 1.4767 1.4385 0.0030  -0.0698 0.0251  223  TRP   A CE2 
1016  C  CE3 . TRP   A 154 ? 1.3733 1.5538 1.5149 0.0079  -0.0675 0.0281  223  TRP   A CE3 
1017  C  CZ2 . TRP   A 154 ? 1.4346 1.6070 1.5694 0.0037  -0.0683 0.0239  223  TRP   A CZ2 
1018  C  CZ3 . TRP   A 154 ? 1.4875 1.6659 1.6272 0.0087  -0.0656 0.0270  223  TRP   A CZ3 
1019  C  CH2 . TRP   A 154 ? 1.4757 1.6501 1.6120 0.0067  -0.0663 0.0248  223  TRP   A CH2 
1020  N  N   . TRP   A 155 ? 1.3836 1.5539 1.5141 0.0070  -0.0773 0.0290  224  TRP   A N   
1021  C  CA  . TRP   A 155 ? 1.2696 1.4332 1.3942 0.0058  -0.0778 0.0279  224  TRP   A CA  
1022  C  C   . TRP   A 155 ? 1.2492 1.4091 1.3707 0.0093  -0.0784 0.0283  224  TRP   A C   
1023  O  O   . TRP   A 155 ? 1.2329 1.3874 1.3508 0.0091  -0.0781 0.0271  224  TRP   A O   
1024  C  CB  . TRP   A 155 ? 1.2222 1.3838 1.3442 0.0029  -0.0794 0.0281  224  TRP   A CB  
1025  C  CG  . TRP   A 155 ? 1.0945 1.2572 1.2176 -0.0009 -0.0785 0.0271  224  TRP   A CG  
1026  C  CD1 . TRP   A 155 ? 1.0903 1.2578 1.2171 -0.0024 -0.0790 0.0275  224  TRP   A CD1 
1027  C  CD2 . TRP   A 155 ? 1.0247 1.1837 1.1456 -0.0035 -0.0769 0.0255  224  TRP   A CD2 
1028  N  NE1 . TRP   A 155 ? 1.0261 1.1926 1.1523 -0.0056 -0.0779 0.0263  224  TRP   A NE1 
1029  C  CE2 . TRP   A 155 ? 0.9527 1.1144 1.0756 -0.0063 -0.0765 0.0251  224  TRP   A CE2 
1030  C  CE3 . TRP   A 155 ? 1.0864 1.2402 1.2045 -0.0038 -0.0759 0.0244  224  TRP   A CE3 
1031  C  CZ2 . TRP   A 155 ? 0.9823 1.1417 1.1041 -0.0091 -0.0749 0.0236  224  TRP   A CZ2 
1032  C  CZ3 . TRP   A 155 ? 1.0299 1.1817 1.1478 -0.0068 -0.0744 0.0229  224  TRP   A CZ3 
1033  C  CH2 . TRP   A 155 ? 0.9977 1.1524 1.1174 -0.0093 -0.0738 0.0225  224  TRP   A CH2 
1034  N  N   . GLN   A 156 ? 1.2945 1.4571 1.4177 0.0126  -0.0791 0.0298  225  GLN   A N   
1035  C  CA  . GLN   A 156 ? 1.2886 1.4477 1.4089 0.0165  -0.0793 0.0300  225  GLN   A CA  
1036  C  C   . GLN   A 156 ? 1.2376 1.3956 1.3576 0.0183  -0.0774 0.0290  225  GLN   A C   
1037  O  O   . GLN   A 156 ? 1.2023 1.3547 1.3181 0.0197  -0.0777 0.0281  225  GLN   A O   
1038  C  CB  . GLN   A 156 ? 1.3696 1.5323 1.4924 0.0200  -0.0802 0.0318  225  GLN   A CB  
1039  C  CG  . GLN   A 156 ? 1.4610 1.6232 1.5826 0.0192  -0.0830 0.0327  225  GLN   A CG  
1040  C  CD  . GLN   A 156 ? 1.6392 1.8087 1.7674 0.0204  -0.0841 0.0341  225  GLN   A CD  
1041  O  OE1 . GLN   A 156 ? 1.6469 1.8205 1.7796 0.0236  -0.0828 0.0350  225  GLN   A OE1 
1042  N  NE2 . GLN   A 156 ? 1.6826 1.8533 1.8116 0.0178  -0.0864 0.0342  225  GLN   A NE2 
1043  N  N   . LYS   A 157 ? 1.2783 1.4410 1.4024 0.0184  -0.0755 0.0292  226  LYS   A N   
1044  C  CA  . LYS   A 157 ? 1.1503 1.3113 1.2733 0.0202  -0.0738 0.0281  226  LYS   A CA  
1045  C  C   . LYS   A 157 ? 1.1271 1.2838 1.2476 0.0173  -0.0741 0.0259  226  LYS   A C   
1046  O  O   . LYS   A 157 ? 1.1486 1.3007 1.2660 0.0191  -0.0743 0.0245  226  LYS   A O   
1047  C  CB  . LYS   A 157 ? 1.2116 1.3781 1.3392 0.0207  -0.0715 0.0290  226  LYS   A CB  
1048  C  CG  . LYS   A 157 ? 1.3093 1.4805 1.4408 0.0239  -0.0705 0.0312  226  LYS   A CG  
1049  C  CD  . LYS   A 157 ? 1.3382 1.5154 1.4757 0.0232  -0.0680 0.0322  226  LYS   A CD  
1050  C  CE  . LYS   A 157 ? 1.2804 1.4630 1.4236 0.0261  -0.0668 0.0344  226  LYS   A CE  
1051  N  NZ  . LYS   A 157 ? 1.2541 1.4374 1.3982 0.0298  -0.0629 0.0354  226  LYS   A NZ  
1052  N  N   . TYR   A 158 ? 1.1850 1.3431 1.3071 0.0129  -0.0743 0.0254  227  TYR   A N   
1053  C  CA  . TYR   A 158 ? 1.1151 1.2697 1.2359 0.0099  -0.0744 0.0234  227  TYR   A CA  
1054  C  C   . TYR   A 158 ? 1.1017 1.2500 1.2187 0.0105  -0.0757 0.0225  227  TYR   A C   
1055  O  O   . TYR   A 158 ? 1.0567 1.2013 1.1729 0.0103  -0.0758 0.0205  227  TYR   A O   
1056  C  CB  . TYR   A 158 ? 1.1014 1.2578 1.2237 0.0055  -0.0744 0.0234  227  TYR   A CB  
1057  C  CG  . TYR   A 158 ? 1.1019 1.2548 1.2233 0.0021  -0.0741 0.0215  227  TYR   A CG  
1058  C  CD1 . TYR   A 158 ? 1.1234 1.2716 1.2420 0.0005  -0.0746 0.0213  227  TYR   A CD1 
1059  C  CD2 . TYR   A 158 ? 1.1062 1.2600 1.2295 0.0007  -0.0731 0.0199  227  TYR   A CD2 
1060  C  CE1 . TYR   A 158 ? 1.0841 1.2293 1.2028 -0.0025 -0.0738 0.0197  227  TYR   A CE1 
1061  C  CE2 . TYR   A 158 ? 1.0408 1.1918 1.1642 -0.0022 -0.0727 0.0182  227  TYR   A CE2 
1062  C  CZ  . TYR   A 158 ? 1.0923 1.2392 1.2139 -0.0039 -0.0729 0.0181  227  TYR   A CZ  
1063  O  OH  . TYR   A 158 ? 1.1857 1.3299 1.3082 -0.0068 -0.0720 0.0165  227  TYR   A OH  
1064  N  N   . GLN   A 159 ? 1.1269 1.2737 1.2419 0.0113  -0.0767 0.0238  228  GLN   A N   
1065  C  CA  . GLN   A 159 ? 1.0906 1.2309 1.2019 0.0114  -0.0777 0.0231  228  GLN   A CA  
1066  C  C   . GLN   A 159 ? 1.0980 1.2351 1.2072 0.0156  -0.0784 0.0226  228  GLN   A C   
1067  O  O   . GLN   A 159 ? 1.0815 1.2133 1.1890 0.0154  -0.0791 0.0209  228  GLN   A O   
1068  C  CB  . GLN   A 159 ? 1.0708 1.2102 1.1798 0.0110  -0.0787 0.0248  228  GLN   A CB  
1069  C  CG  . GLN   A 159 ? 1.0377 1.1699 1.1425 0.0106  -0.0794 0.0245  228  GLN   A CG  
1070  C  CD  . GLN   A 159 ? 0.9876 1.1184 1.0891 0.0120  -0.0807 0.0264  228  GLN   A CD  
1071  O  OE1 . GLN   A 159 ? 0.9952 1.1267 1.0959 0.0159  -0.0816 0.0273  228  GLN   A OE1 
1072  N  NE2 . GLN   A 159 ? 0.9945 1.1230 1.0936 0.0091  -0.0806 0.0269  228  GLN   A NE2 
1073  N  N   . LYS   A 160 ? 1.0960 1.2361 1.2054 0.0196  -0.0781 0.0239  229  LYS   A N   
1074  C  CA  . LYS   A 160 ? 1.0685 1.2052 1.1751 0.0240  -0.0784 0.0234  229  LYS   A CA  
1075  C  C   . LYS   A 160 ? 1.0599 1.1941 1.1662 0.0238  -0.0783 0.0210  229  LYS   A C   
1076  O  O   . LYS   A 160 ? 1.0507 1.1791 1.1541 0.0254  -0.0798 0.0194  229  LYS   A O   
1077  C  CB  . LYS   A 160 ? 1.0499 1.1908 1.1575 0.0281  -0.0771 0.0252  229  LYS   A CB  
1078  C  CG  . LYS   A 160 ? 1.1335 1.2757 1.2409 0.0302  -0.0777 0.0272  229  LYS   A CG  
1079  C  CD  . LYS   A 160 ? 1.2613 1.4104 1.3731 0.0325  -0.0759 0.0292  229  LYS   A CD  
1080  C  CE  . LYS   A 160 ? 1.2756 1.4297 1.3912 0.0308  -0.0768 0.0309  229  LYS   A CE  
1081  N  NZ  . LYS   A 160 ? 1.1592 1.3211 1.2814 0.0314  -0.0752 0.0325  229  LYS   A NZ  
1082  N  N   . ARG   A 161 ? 1.0935 1.2318 1.2030 0.0217  -0.0770 0.0207  230  ARG   A N   
1083  C  CA  . ARG   A 161 ? 1.1062 1.2423 1.2153 0.0222  -0.0771 0.0185  230  ARG   A CA  
1084  C  C   . ARG   A 161 ? 1.1178 1.2502 1.2277 0.0187  -0.0786 0.0161  230  ARG   A C   
1085  O  O   . ARG   A 161 ? 1.1980 1.3252 1.3061 0.0202  -0.0803 0.0141  230  ARG   A O   
1086  C  CB  . ARG   A 161 ? 1.1321 1.2732 1.2438 0.0216  -0.0752 0.0189  230  ARG   A CB  
1087  C  CG  . ARG   A 161 ? 1.3174 1.4553 1.4275 0.0229  -0.0756 0.0166  230  ARG   A CG  
1088  C  CD  . ARG   A 161 ? 1.3602 1.5019 1.4729 0.0211  -0.0740 0.0165  230  ARG   A CD  
1089  N  NE  . ARG   A 161 ? 1.3969 1.5432 1.5106 0.0229  -0.0714 0.0189  230  ARG   A NE  
1090  C  CZ  . ARG   A 161 ? 1.4243 1.5735 1.5395 0.0224  -0.0695 0.0192  230  ARG   A CZ  
1091  N  NH1 . ARG   A 161 ? 1.4256 1.5734 1.5409 0.0207  -0.0700 0.0171  230  ARG   A NH1 
1092  N  NH2 . ARG   A 161 ? 1.4208 1.5744 1.5381 0.0237  -0.0670 0.0215  230  ARG   A NH2 
1093  N  N   . LYS   A 162 ? 1.0855 1.2205 1.1986 0.0141  -0.0778 0.0163  231  LYS   A N   
1094  C  CA  . LYS   A 162 ? 1.0509 1.1832 1.1660 0.0107  -0.0784 0.0141  231  LYS   A CA  
1095  C  C   . LYS   A 162 ? 1.0635 1.1895 1.1769 0.0111  -0.0801 0.0131  231  LYS   A C   
1096  O  O   . LYS   A 162 ? 1.0984 1.2209 1.2133 0.0105  -0.0814 0.0107  231  LYS   A O   
1097  C  CB  . LYS   A 162 ? 1.0669 1.2023 1.1847 0.0060  -0.0769 0.0147  231  LYS   A CB  
1098  C  CG  . LYS   A 162 ? 1.0673 1.2006 1.1880 0.0023  -0.0767 0.0127  231  LYS   A CG  
1099  C  CD  . LYS   A 162 ? 1.0340 1.1705 1.1567 -0.0017 -0.0748 0.0133  231  LYS   A CD  
1100  C  CE  . LYS   A 162 ? 1.1293 1.2639 1.2556 -0.0050 -0.0741 0.0111  231  LYS   A CE  
1101  N  NZ  . LYS   A 162 ? 1.1040 1.2421 1.2326 -0.0080 -0.0724 0.0109  231  LYS   A NZ  
1102  N  N   . PHE   A 163 ? 1.0361 1.1607 1.1467 0.0123  -0.0803 0.0149  232  PHE   A N   
1103  C  CA  . PHE   A 163 ? 1.0155 1.1340 1.1242 0.0123  -0.0815 0.0144  232  PHE   A CA  
1104  C  C   . PHE   A 163 ? 1.0863 1.2012 1.1909 0.0172  -0.0833 0.0144  232  PHE   A C   
1105  O  O   . PHE   A 163 ? 1.1192 1.2296 1.2211 0.0181  -0.0841 0.0149  232  PHE   A O   
1106  C  CB  . PHE   A 163 ? 1.0101 1.1284 1.1178 0.0098  -0.0805 0.0163  232  PHE   A CB  
1107  C  CG  . PHE   A 163 ? 0.9994 1.1205 1.1100 0.0054  -0.0786 0.0164  232  PHE   A CG  
1108  C  CD1 . PHE   A 163 ? 0.9771 1.0960 1.0909 0.0019  -0.0780 0.0145  232  PHE   A CD1 
1109  C  CD2 . PHE   A 163 ? 0.9721 1.0980 1.0823 0.0046  -0.0776 0.0183  232  PHE   A CD2 
1110  C  CE1 . PHE   A 163 ? 0.9688 1.0899 1.0848 -0.0019 -0.0759 0.0147  232  PHE   A CE1 
1111  C  CE2 . PHE   A 163 ? 0.9734 1.1011 1.0854 0.0007  -0.0761 0.0183  232  PHE   A CE2 
1112  C  CZ  . PHE   A 163 ? 1.0016 1.1268 1.1161 -0.0025 -0.0750 0.0166  232  PHE   A CZ  
1113  N  N   . HIS   A 164 ? 1.0729 1.1891 1.1764 0.0208  -0.0835 0.0140  233  HIS   A N   
1114  C  CA  . HIS   A 164 ? 1.0539 1.1659 1.1527 0.0260  -0.0849 0.0139  233  HIS   A CA  
1115  C  C   . HIS   A 164 ? 1.0738 1.1783 1.1713 0.0262  -0.0876 0.0115  233  HIS   A C   
1116  O  O   . HIS   A 164 ? 1.1190 1.2188 1.2127 0.0287  -0.0889 0.0119  233  HIS   A O   
1117  C  CB  . HIS   A 164 ? 1.0572 1.1710 1.1548 0.0294  -0.0843 0.0136  233  HIS   A CB  
1118  C  CG  . HIS   A 164 ? 1.0384 1.1475 1.1304 0.0352  -0.0854 0.0134  233  HIS   A CG  
1119  N  ND1 . HIS   A 164 ? 1.0518 1.1555 1.1408 0.0378  -0.0875 0.0109  233  HIS   A ND1 
1120  C  CD2 . HIS   A 164 ? 1.0618 1.1705 1.1502 0.0392  -0.0847 0.0154  233  HIS   A CD2 
1121  C  CE1 . HIS   A 164 ? 1.0708 1.1704 1.1540 0.0432  -0.0879 0.0113  233  HIS   A CE1 
1122  N  NE2 . HIS   A 164 ? 1.0875 1.1902 1.1704 0.0442  -0.0860 0.0141  233  HIS   A NE2 
1123  N  N   . CYS   A 165 ? 1.0404 1.1437 1.1416 0.0234  -0.0887 0.0090  234  CYS   A N   
1124  C  CA  . CYS   A 165 ? 1.0310 1.1275 1.1327 0.0231  -0.0915 0.0064  234  CYS   A CA  
1125  C  C   . CYS   A 165 ? 1.0729 1.1666 1.1758 0.0199  -0.0911 0.0071  234  CYS   A C   
1126  O  O   . CYS   A 165 ? 1.1020 1.1905 1.2068 0.0186  -0.0930 0.0051  234  CYS   A O   
1127  C  CB  . CYS   A 165 ? 1.0973 1.1943 1.2040 0.0207  -0.0926 0.0035  234  CYS   A CB  
1128  S  SG  . CYS   A 165 ? 1.2759 1.3718 1.3789 0.0259  -0.0945 0.0019  234  CYS   A SG  
1129  N  N   . ALA   A 166 ? 1.0596 1.1564 1.1615 0.0185  -0.0887 0.0099  235  ALA   A N   
1130  C  CA  . ALA   A 166 ? 1.0547 1.1476 1.1562 0.0161  -0.0882 0.0108  235  ALA   A CA  
1131  C  C   . ALA   A 166 ? 1.0938 1.1805 1.1903 0.0199  -0.0903 0.0109  235  ALA   A C   
1132  O  O   . ALA   A 166 ? 1.0400 1.1213 1.1359 0.0182  -0.0906 0.0109  235  ALA   A O   
1133  C  CB  . ALA   A 166 ? 1.0416 1.1390 1.1425 0.0142  -0.0856 0.0136  235  ALA   A CB  
1134  N  N   . ASN   A 167 ? 1.1988 1.2855 1.2912 0.0249  -0.0915 0.0111  236  ASN   A N   
1135  C  CA  . ASN   A 167 ? 1.2175 1.2979 1.3044 0.0290  -0.0935 0.0111  236  ASN   A CA  
1136  C  C   . ASN   A 167 ? 1.2163 1.2894 1.3041 0.0285  -0.0964 0.0081  236  ASN   A C   
1137  O  O   . ASN   A 167 ? 1.2293 1.2960 1.3135 0.0302  -0.0980 0.0081  236  ASN   A O   
1138  C  CB  . ASN   A 167 ? 1.2500 1.3320 1.3325 0.0347  -0.0936 0.0119  236  ASN   A CB  
1139  C  CG  . ASN   A 167 ? 1.2962 1.3850 1.3785 0.0354  -0.0909 0.0151  236  ASN   A CG  
1140  O  OD1 . ASN   A 167 ? 1.3217 1.4093 1.4007 0.0376  -0.0908 0.0170  236  ASN   A OD1 
1141  N  ND2 . ASN   A 167 ? 1.2639 1.3596 1.3501 0.0334  -0.0890 0.0156  236  ASN   A ND2 
1142  N  N   . LEU   A 168 ? 1.0478 1.1218 1.1406 0.0262  -0.0973 0.0056  237  LEU   A N   
1143  C  CA  . LEU   A 168 ? 1.0857 1.1534 1.1813 0.0252  -0.1005 0.0024  237  LEU   A CA  
1144  C  C   . LEU   A 168 ? 1.0616 1.1272 1.1625 0.0198  -0.0994 0.0023  237  LEU   A C   
1145  O  O   . LEU   A 168 ? 1.0196 1.0796 1.1238 0.0185  -0.1019 -0.0002 237  LEU   A O   
1146  C  CB  . LEU   A 168 ? 1.0106 1.0801 1.1101 0.0251  -0.1022 -0.0004 237  LEU   A CB  
1147  C  CG  . LEU   A 168 ? 0.9340 1.0036 1.0282 0.0305  -0.1037 -0.0011 237  LEU   A CG  
1148  C  CD1 . LEU   A 168 ? 1.0387 1.1161 1.1329 0.0306  -0.1004 0.0010  237  LEU   A CD1 
1149  C  CD2 . LEU   A 168 ? 1.0005 1.0672 1.0979 0.0305  -0.1072 -0.0048 237  LEU   A CD2 
1150  N  N   . THR   A 169 ? 1.0588 1.1284 1.1608 0.0165  -0.0957 0.0049  238  THR   A N   
1151  C  CA  . THR   A 169 ? 1.0003 1.0675 1.1063 0.0115  -0.0937 0.0052  238  THR   A CA  
1152  C  C   . THR   A 169 ? 0.9879 1.0507 1.0878 0.0126  -0.0928 0.0077  238  THR   A C   
1153  O  O   . THR   A 169 ? 1.0073 1.0688 1.1008 0.0172  -0.0943 0.0088  238  THR   A O   
1154  C  CB  . THR   A 169 ? 0.9355 1.0088 1.0461 0.0072  -0.0902 0.0061  238  THR   A CB  
1155  O  OG1 . THR   A 169 ? 0.9931 1.0705 1.0989 0.0083  -0.0880 0.0092  238  THR   A OG1 
1156  C  CG2 . THR   A 169 ? 0.9403 1.0185 1.0559 0.0070  -0.0912 0.0039  238  THR   A CG2 
1157  N  N   . SER   A 170 ? 0.9387 0.9987 1.0404 0.0085  -0.0904 0.0087  239  SER   A N   
1158  C  CA  . SER   A 170 ? 0.9655 1.0202 1.0613 0.0091  -0.0895 0.0110  239  SER   A CA  
1159  C  C   . SER   A 170 ? 0.9463 1.0046 1.0386 0.0082  -0.0863 0.0141  239  SER   A C   
1160  O  O   . SER   A 170 ? 0.9600 1.0137 1.0471 0.0084  -0.0853 0.0162  239  SER   A O   
1161  C  CB  . SER   A 170 ? 0.9539 1.0011 1.0531 0.0055  -0.0888 0.0101  239  SER   A CB  
1162  O  OG  . SER   A 170 ? 0.9776 1.0275 1.0854 0.0008  -0.0869 0.0087  239  SER   A OG  
1163  N  N   . TRP   A 171 ? 0.9247 0.9905 1.0193 0.0074  -0.0851 0.0144  240  TRP   A N   
1164  C  CA  . TRP   A 171 ? 0.9039 0.9735 0.9958 0.0064  -0.0826 0.0170  240  TRP   A CA  
1165  C  C   . TRP   A 171 ? 0.9485 1.0252 1.0388 0.0100  -0.0838 0.0177  240  TRP   A C   
1166  O  O   . TRP   A 171 ? 1.0224 1.1019 1.1150 0.0120  -0.0855 0.0161  240  TRP   A O   
1167  C  CB  . TRP   A 171 ? 0.9148 0.9868 1.0118 0.0014  -0.0796 0.0167  240  TRP   A CB  
1168  C  CG  . TRP   A 171 ? 0.9575 1.0226 1.0558 -0.0024 -0.0772 0.0167  240  TRP   A CG  
1169  C  CD1 . TRP   A 171 ? 0.9255 0.9897 1.0312 -0.0064 -0.0756 0.0149  240  TRP   A CD1 
1170  C  CD2 . TRP   A 171 ? 0.9913 1.0493 1.0836 -0.0026 -0.0758 0.0188  240  TRP   A CD2 
1171  N  NE1 . TRP   A 171 ? 0.9338 0.9910 1.0389 -0.0091 -0.0729 0.0158  240  TRP   A NE1 
1172  C  CE2 . TRP   A 171 ? 1.0266 1.0795 1.1229 -0.0068 -0.0730 0.0182  240  TRP   A CE2 
1173  C  CE3 . TRP   A 171 ? 0.9910 1.0464 1.0750 0.0006  -0.0767 0.0211  240  TRP   A CE3 
1174  C  CZ2 . TRP   A 171 ? 1.1213 1.1660 1.2129 -0.0079 -0.0707 0.0200  240  TRP   A CZ2 
1175  C  CZ3 . TRP   A 171 ? 1.0305 1.0777 1.1095 -0.0003 -0.0750 0.0227  240  TRP   A CZ3 
1176  C  CH2 . TRP   A 171 ? 1.1292 1.1709 1.2116 -0.0046 -0.0719 0.0222  240  TRP   A CH2 
1177  N  N   . PRO   A 172 ? 0.9511 1.0305 1.0375 0.0110  -0.0830 0.0202  241  PRO   A N   
1178  C  CA  . PRO   A 172 ? 0.9589 1.0452 1.0449 0.0142  -0.0839 0.0210  241  PRO   A CA  
1179  C  C   . PRO   A 172 ? 0.9148 1.0081 1.0052 0.0116  -0.0824 0.0208  241  PRO   A C   
1180  O  O   . PRO   A 172 ? 0.9151 1.0080 1.0081 0.0074  -0.0806 0.0202  241  PRO   A O   
1181  C  CB  . PRO   A 172 ? 0.9631 1.0485 1.0437 0.0161  -0.0840 0.0236  241  PRO   A CB  
1182  C  CG  . PRO   A 172 ? 0.9679 1.0490 1.0470 0.0121  -0.0821 0.0243  241  PRO   A CG  
1183  C  CD  . PRO   A 172 ? 1.0034 1.0792 1.0856 0.0092  -0.0813 0.0223  241  PRO   A CD  
1184  N  N   . ARG   A 173 ? 0.9462 1.0459 1.0375 0.0143  -0.0829 0.0213  242  ARG   A N   
1185  C  CA  . ARG   A 173 ? 0.9645 1.0709 1.0599 0.0122  -0.0817 0.0211  242  ARG   A CA  
1186  C  C   . ARG   A 173 ? 0.9692 1.0770 1.0639 0.0090  -0.0802 0.0226  242  ARG   A C   
1187  O  O   . ARG   A 173 ? 0.9465 1.0561 1.0441 0.0054  -0.0787 0.0218  242  ARG   A O   
1188  C  CB  . ARG   A 173 ? 0.9660 1.0783 1.0622 0.0159  -0.0822 0.0217  242  ARG   A CB  
1189  C  CG  . ARG   A 173 ? 1.0070 1.1178 1.1031 0.0193  -0.0833 0.0202  242  ARG   A CG  
1190  C  CD  . ARG   A 173 ? 1.0033 1.1201 1.1005 0.0224  -0.0828 0.0210  242  ARG   A CD  
1191  N  NE  . ARG   A 173 ? 1.1145 1.2365 1.2127 0.0220  -0.0820 0.0233  242  ARG   A NE  
1192  C  CZ  . ARG   A 173 ? 1.1696 1.2943 1.2670 0.0258  -0.0822 0.0251  242  ARG   A CZ  
1193  N  NH1 . ARG   A 173 ? 1.1907 1.3129 1.2855 0.0304  -0.0827 0.0251  242  ARG   A NH1 
1194  N  NH2 . ARG   A 173 ? 1.0536 1.1834 1.1531 0.0250  -0.0819 0.0268  242  ARG   A NH2 
1195  N  N   . TRP   A 174 ? 0.9572 1.0638 1.0477 0.0105  -0.0809 0.0246  243  TRP   A N   
1196  C  CA  . TRP   A 174 ? 0.9083 1.0155 0.9970 0.0080  -0.0801 0.0259  243  TRP   A CA  
1197  C  C   . TRP   A 174 ? 0.9322 1.0336 1.0195 0.0040  -0.0780 0.0255  243  TRP   A C   
1198  O  O   . TRP   A 174 ? 0.9744 1.0765 1.0608 0.0014  -0.0767 0.0261  243  TRP   A O   
1199  C  CB  . TRP   A 174 ? 0.9278 1.0343 1.0120 0.0109  -0.0818 0.0280  243  TRP   A CB  
1200  C  CG  . TRP   A 174 ? 0.9803 1.0796 1.0596 0.0132  -0.0827 0.0285  243  TRP   A CG  
1201  C  CD1 . TRP   A 174 ? 0.9788 1.0778 1.0574 0.0174  -0.0842 0.0286  243  TRP   A CD1 
1202  C  CD2 . TRP   A 174 ? 1.0154 1.1063 1.0895 0.0115  -0.0818 0.0290  243  TRP   A CD2 
1203  N  NE1 . TRP   A 174 ? 0.9802 1.0712 1.0535 0.0184  -0.0848 0.0290  243  TRP   A NE1 
1204  C  CE2 . TRP   A 174 ? 0.9806 1.0666 1.0512 0.0147  -0.0832 0.0293  243  TRP   A CE2 
1205  C  CE3 . TRP   A 174 ? 1.0061 1.0928 1.0778 0.0077  -0.0797 0.0293  243  TRP   A CE3 
1206  C  CZ2 . TRP   A 174 ? 1.0125 1.0895 1.0775 0.0141  -0.0826 0.0300  243  TRP   A CZ2 
1207  C  CZ3 . TRP   A 174 ? 0.9788 1.0564 1.0448 0.0071  -0.0787 0.0300  243  TRP   A CZ3 
1208  C  CH2 . TRP   A 174 ? 1.0257 1.0986 1.0886 0.0102  -0.0803 0.0304  243  TRP   A CH2 
1209  N  N   . LEU   A 175 ? 0.9312 1.0267 1.0184 0.0034  -0.0775 0.0245  244  LEU   A N   
1210  C  CA  . LEU   A 175 ? 0.9048 0.9956 0.9925 -0.0008 -0.0748 0.0239  244  LEU   A CA  
1211  C  C   . LEU   A 175 ? 0.9428 1.0382 1.0370 -0.0035 -0.0735 0.0221  244  LEU   A C   
1212  O  O   . LEU   A 175 ? 0.9813 1.0767 1.0759 -0.0067 -0.0711 0.0223  244  LEU   A O   
1213  C  CB  . LEU   A 175 ? 0.9061 0.9894 0.9932 -0.0009 -0.0746 0.0233  244  LEU   A CB  
1214  C  CG  . LEU   A 175 ? 0.9301 1.0082 1.0188 -0.0053 -0.0713 0.0228  244  LEU   A CG  
1215  C  CD1 . LEU   A 175 ? 0.9771 1.0527 1.0606 -0.0072 -0.0687 0.0248  244  LEU   A CD1 
1216  C  CD2 . LEU   A 175 ? 1.0065 1.0767 1.0943 -0.0051 -0.0713 0.0225  244  LEU   A CD2 
1217  N  N   . TYR   A 176 ? 0.9383 1.0374 1.0370 -0.0020 -0.0750 0.0204  245  TYR   A N   
1218  C  CA  . TYR   A 176 ? 0.9529 1.0561 1.0576 -0.0042 -0.0741 0.0185  245  TYR   A CA  
1219  C  C   . TYR   A 176 ? 0.9470 1.0559 1.0520 -0.0054 -0.0731 0.0193  245  TYR   A C   
1220  O  O   . TYR   A 176 ? 0.9586 1.0696 1.0675 -0.0083 -0.0715 0.0182  245  TYR   A O   
1221  C  CB  . TYR   A 176 ? 0.9274 1.0328 1.0352 -0.0015 -0.0764 0.0166  245  TYR   A CB  
1222  C  CG  . TYR   A 176 ? 0.8994 0.9989 1.0087 -0.0013 -0.0775 0.0149  245  TYR   A CG  
1223  C  CD1 . TYR   A 176 ? 0.8789 0.9759 0.9931 -0.0049 -0.0761 0.0133  245  TYR   A CD1 
1224  C  CD2 . TYR   A 176 ? 0.9318 1.0282 1.0378 0.0025  -0.0799 0.0149  245  TYR   A CD2 
1225  C  CE1 . TYR   A 176 ? 0.8946 0.9861 1.0110 -0.0050 -0.0774 0.0116  245  TYR   A CE1 
1226  C  CE2 . TYR   A 176 ? 0.9181 1.0086 1.0253 0.0027  -0.0813 0.0133  245  TYR   A CE2 
1227  C  CZ  . TYR   A 176 ? 0.9146 1.0027 1.0273 -0.0012 -0.0802 0.0116  245  TYR   A CZ  
1228  O  OH  . TYR   A 176 ? 0.9289 1.0112 1.0438 -0.0013 -0.0818 0.0098  245  TYR   A OH  
1229  N  N   . SER   A 177 ? 0.9123 1.0236 1.0135 -0.0034 -0.0742 0.0212  246  SER   A N   
1230  C  CA  . SER   A 177 ? 0.9371 1.0534 1.0386 -0.0046 -0.0737 0.0220  246  SER   A CA  
1231  C  C   . SER   A 177 ? 0.9595 1.0719 1.0576 -0.0078 -0.0716 0.0229  246  SER   A C   
1232  O  O   . SER   A 177 ? 0.9126 1.0277 1.0119 -0.0100 -0.0704 0.0227  246  SER   A O   
1233  C  CB  . SER   A 177 ? 0.9536 1.0738 1.0534 -0.0013 -0.0758 0.0236  246  SER   A CB  
1234  O  OG  . SER   A 177 ? 1.1665 1.2926 1.2683 -0.0022 -0.0758 0.0240  246  SER   A OG  
1235  N  N   . LEU   A 178 ? 0.9613 1.0669 1.0549 -0.0079 -0.0710 0.0238  247  LEU   A N   
1236  C  CA  . LEU   A 178 ? 0.9093 1.0101 0.9986 -0.0106 -0.0685 0.0247  247  LEU   A CA  
1237  C  C   . LEU   A 178 ? 0.9146 1.0140 1.0082 -0.0142 -0.0652 0.0232  247  LEU   A C   
1238  O  O   . LEU   A 178 ? 0.9907 1.0855 1.0808 -0.0165 -0.0624 0.0240  247  LEU   A O   
1239  C  CB  . LEU   A 178 ? 0.9020 0.9950 0.9845 -0.0096 -0.0684 0.0262  247  LEU   A CB  
1240  C  CG  . LEU   A 178 ? 0.9136 1.0066 0.9917 -0.0056 -0.0717 0.0277  247  LEU   A CG  
1241  C  CD1 . LEU   A 178 ? 1.0081 1.0920 1.0799 -0.0050 -0.0710 0.0288  247  LEU   A CD1 
1242  C  CD2 . LEU   A 178 ? 0.9534 1.0498 1.0286 -0.0048 -0.0734 0.0288  247  LEU   A CD2 
1243  N  N   . TYR   A 179 ? 0.9128 1.0157 1.0135 -0.0146 -0.0654 0.0212  248  TYR   A N   
1244  C  CA  . TYR   A 179 ? 0.8999 1.0027 1.0060 -0.0179 -0.0626 0.0196  248  TYR   A CA  
1245  C  C   . TYR   A 179 ? 0.9939 1.1038 1.1056 -0.0180 -0.0636 0.0179  248  TYR   A C   
1246  O  O   . TYR   A 179 ? 1.0400 1.1508 1.1576 -0.0201 -0.0622 0.0161  248  TYR   A O   
1247  C  CB  . TYR   A 179 ? 0.8950 0.9933 1.0051 -0.0188 -0.0618 0.0183  248  TYR   A CB  
1248  C  CG  . TYR   A 179 ? 0.9142 1.0044 1.0192 -0.0195 -0.0599 0.0199  248  TYR   A CG  
1249  C  CD1 . TYR   A 179 ? 0.9285 1.0155 1.0286 -0.0166 -0.0622 0.0211  248  TYR   A CD1 
1250  C  CD2 . TYR   A 179 ? 0.9256 1.0111 1.0305 -0.0227 -0.0555 0.0204  248  TYR   A CD2 
1251  C  CE1 . TYR   A 179 ? 1.0090 1.0881 1.1038 -0.0170 -0.0604 0.0226  248  TYR   A CE1 
1252  C  CE2 . TYR   A 179 ? 0.9903 1.0676 1.0899 -0.0232 -0.0533 0.0221  248  TYR   A CE2 
1253  C  CZ  . TYR   A 179 ? 1.0451 1.1191 1.1394 -0.0204 -0.0559 0.0232  248  TYR   A CZ  
1254  O  OH  . TYR   A 179 ? 1.1464 1.2116 1.2347 -0.0206 -0.0537 0.0249  248  TYR   A OH  
1255  N  N   . ASP   A 180 ? 1.0795 1.1945 1.1901 -0.0156 -0.0661 0.0184  249  ASP   A N   
1256  C  CA  . ASP   A 180 ? 1.0636 1.1848 1.1789 -0.0153 -0.0669 0.0170  249  ASP   A CA  
1257  C  C   . ASP   A 180 ? 1.0633 1.1872 1.1778 -0.0174 -0.0655 0.0175  249  ASP   A C   
1258  O  O   . ASP   A 180 ? 1.0874 1.2122 1.1976 -0.0167 -0.0663 0.0192  249  ASP   A O   
1259  C  CB  . ASP   A 180 ? 1.0524 1.1772 1.1673 -0.0116 -0.0698 0.0173  249  ASP   A CB  
1260  C  CG  . ASP   A 180 ? 1.1050 1.2356 1.2233 -0.0111 -0.0703 0.0164  249  ASP   A CG  
1261  O  OD1 . ASP   A 180 ? 1.1617 1.2929 1.2844 -0.0121 -0.0699 0.0143  249  ASP   A OD1 
1262  O  OD2 . ASP   A 180 ? 1.1324 1.2670 1.2495 -0.0099 -0.0711 0.0177  249  ASP   A OD2 
1263  N  N   . ALA   A 181 ? 1.0608 1.1856 1.1793 -0.0199 -0.0635 0.0160  250  ALA   A N   
1264  C  CA  . ALA   A 181 ? 1.0273 1.1537 1.1447 -0.0221 -0.0618 0.0163  250  ALA   A CA  
1265  C  C   . ALA   A 181 ? 1.1181 1.2493 1.2337 -0.0206 -0.0640 0.0172  250  ALA   A C   
1266  O  O   . ALA   A 181 ? 1.1376 1.2684 1.2490 -0.0213 -0.0639 0.0185  250  ALA   A O   
1267  C  CB  . ALA   A 181 ? 1.0895 1.2175 1.2128 -0.0241 -0.0600 0.0142  250  ALA   A CB  
1268  N  N   . GLU   A 182 ? 1.4235 1.5592 1.5424 -0.0184 -0.0659 0.0166  251  GLU   A N   
1269  C  CA  . GLU   A 182 ? 1.4366 1.5772 1.5552 -0.0173 -0.0674 0.0174  251  GLU   A CA  
1270  C  C   . GLU   A 182 ? 1.4202 1.5603 1.5346 -0.0158 -0.0690 0.0195  251  GLU   A C   
1271  O  O   . GLU   A 182 ? 1.4475 1.5902 1.5607 -0.0162 -0.0698 0.0204  251  GLU   A O   
1272  C  CB  . GLU   A 182 ? 1.4622 1.6068 1.5846 -0.0150 -0.0686 0.0165  251  GLU   A CB  
1273  C  CG  . GLU   A 182 ? 1.5396 1.6835 1.6660 -0.0157 -0.0678 0.0141  251  GLU   A CG  
1274  C  CD  . GLU   A 182 ? 1.7164 1.8623 1.8449 -0.0182 -0.0663 0.0131  251  GLU   A CD  
1275  O  OE1 . GLU   A 182 ? 1.7102 1.8597 1.8382 -0.0184 -0.0665 0.0139  251  GLU   A OE1 
1276  O  OE2 . GLU   A 182 ? 1.7271 1.8712 1.8584 -0.0200 -0.0650 0.0114  251  GLU   A OE2 
1277  N  N   . THR   A 183 ? 1.1471 1.2839 1.2593 -0.0140 -0.0698 0.0202  252  THR   A N   
1278  C  CA  . THR   A 183 ? 1.0390 1.1751 1.1471 -0.0123 -0.0716 0.0221  252  THR   A CA  
1279  C  C   . THR   A 183 ? 1.0459 1.1778 1.1488 -0.0143 -0.0709 0.0230  252  THR   A C   
1280  O  O   . THR   A 183 ? 1.0469 1.1801 1.1474 -0.0138 -0.0727 0.0241  252  THR   A O   
1281  C  CB  . THR   A 183 ? 1.0242 1.1569 1.1306 -0.0097 -0.0725 0.0225  252  THR   A CB  
1282  O  OG1 . THR   A 183 ? 1.0658 1.2016 1.1761 -0.0073 -0.0732 0.0217  252  THR   A OG1 
1283  C  CG2 . THR   A 183 ? 1.0304 1.1624 1.1327 -0.0077 -0.0746 0.0245  252  THR   A CG2 
1284  N  N   . LEU   A 184 ? 1.0411 1.1675 1.1421 -0.0164 -0.0684 0.0224  253  LEU   A N   
1285  C  CA  . LEU   A 184 ? 0.9990 1.1202 1.0940 -0.0181 -0.0670 0.0233  253  LEU   A CA  
1286  C  C   . LEU   A 184 ? 0.9594 1.0836 1.0540 -0.0196 -0.0673 0.0232  253  LEU   A C   
1287  O  O   . LEU   A 184 ? 0.9910 1.1140 1.0807 -0.0190 -0.0691 0.0243  253  LEU   A O   
1288  C  CB  . LEU   A 184 ? 0.9285 1.0440 1.0232 -0.0204 -0.0633 0.0226  253  LEU   A CB  
1289  C  CG  . LEU   A 184 ? 0.8898 1.0008 0.9840 -0.0194 -0.0629 0.0229  253  LEU   A CG  
1290  C  CD1 . LEU   A 184 ? 0.8929 0.9991 0.9887 -0.0221 -0.0590 0.0222  253  LEU   A CD1 
1291  C  CD2 . LEU   A 184 ? 0.8632 0.9693 0.9498 -0.0174 -0.0645 0.0249  253  LEU   A CD2 
1292  N  N   . MET   A 185 ? 0.9529 1.0810 1.0527 -0.0212 -0.0659 0.0217  254  MET   A N   
1293  C  CA  . MET   A 185 ? 0.9124 1.0428 1.0117 -0.0227 -0.0661 0.0215  254  MET   A CA  
1294  C  C   . MET   A 185 ? 0.9348 1.0693 1.0338 -0.0211 -0.0696 0.0224  254  MET   A C   
1295  O  O   . MET   A 185 ? 0.9362 1.0701 1.0320 -0.0220 -0.0706 0.0227  254  MET   A O   
1296  C  CB  . MET   A 185 ? 0.9429 1.0775 1.0484 -0.0240 -0.0646 0.0197  254  MET   A CB  
1297  C  CG  . MET   A 185 ? 0.9500 1.0809 1.0564 -0.0261 -0.0610 0.0186  254  MET   A CG  
1298  S  SD  . MET   A 185 ? 0.9537 1.0892 1.0683 -0.0271 -0.0597 0.0162  254  MET   A SD  
1299  C  CE  . MET   A 185 ? 1.0452 1.1862 1.1600 -0.0271 -0.0616 0.0163  254  MET   A CE  
1300  N  N   . ASP   A 186 ? 0.9680 1.1064 1.0704 -0.0186 -0.0716 0.0229  255  ASP   A N   
1301  C  CA  . ASP   A 186 ? 0.9404 1.0831 1.0439 -0.0172 -0.0748 0.0238  255  ASP   A CA  
1302  C  C   . ASP   A 186 ? 0.9199 1.0584 1.0173 -0.0160 -0.0770 0.0252  255  ASP   A C   
1303  O  O   . ASP   A 186 ? 0.9358 1.0755 1.0320 -0.0160 -0.0796 0.0256  255  ASP   A O   
1304  C  CB  . ASP   A 186 ? 0.9672 1.1155 1.0764 -0.0146 -0.0758 0.0241  255  ASP   A CB  
1305  C  CG  . ASP   A 186 ? 0.9524 1.1057 1.0642 -0.0133 -0.0787 0.0251  255  ASP   A CG  
1306  O  OD1 . ASP   A 186 ? 0.9289 1.0861 1.0438 -0.0148 -0.0790 0.0248  255  ASP   A OD1 
1307  O  OD2 . ASP   A 186 ? 0.9143 1.0676 1.0254 -0.0109 -0.0807 0.0263  255  ASP   A OD2 
1308  N  N   . ARG   A 187 ? 0.9552 1.0884 1.0486 -0.0149 -0.0764 0.0257  256  ARG   A N   
1309  C  CA  . ARG   A 187 ? 0.9848 1.1127 1.0711 -0.0137 -0.0784 0.0270  256  ARG   A CA  
1310  C  C   . ARG   A 187 ? 0.9651 1.0879 1.0448 -0.0157 -0.0780 0.0269  256  ARG   A C   
1311  O  O   . ARG   A 187 ? 0.9861 1.1074 1.0615 -0.0148 -0.0812 0.0276  256  ARG   A O   
1312  C  CB  . ARG   A 187 ? 0.9817 1.1036 1.0643 -0.0125 -0.0770 0.0275  256  ARG   A CB  
1313  C  CG  . ARG   A 187 ? 0.9547 1.0802 1.0416 -0.0098 -0.0784 0.0278  256  ARG   A CG  
1314  C  CD  . ARG   A 187 ? 1.0386 1.1584 1.1232 -0.0094 -0.0763 0.0278  256  ARG   A CD  
1315  N  NE  . ARG   A 187 ? 1.0061 1.1177 1.0823 -0.0089 -0.0765 0.0290  256  ARG   A NE  
1316  C  CZ  . ARG   A 187 ? 0.9384 1.0435 1.0116 -0.0092 -0.0742 0.0291  256  ARG   A CZ  
1317  N  NH1 . ARG   A 187 ? 1.0128 1.1187 1.0910 -0.0103 -0.0720 0.0279  256  ARG   A NH1 
1318  N  NH2 . ARG   A 187 ? 0.9467 1.0438 1.0114 -0.0085 -0.0742 0.0304  256  ARG   A NH2 
1319  N  N   . ILE   A 188 ? 0.9041 1.0240 0.9828 -0.0182 -0.0742 0.0261  257  ILE   A N   
1320  C  CA  . ILE   A 188 ? 0.8795 0.9945 0.9519 -0.0200 -0.0733 0.0260  257  ILE   A CA  
1321  C  C   . ILE   A 188 ? 0.9618 1.0820 1.0367 -0.0204 -0.0763 0.0255  257  ILE   A C   
1322  O  O   . ILE   A 188 ? 0.9899 1.1069 1.0589 -0.0200 -0.0790 0.0259  257  ILE   A O   
1323  C  CB  . ILE   A 188 ? 0.8654 0.9778 0.9385 -0.0226 -0.0683 0.0251  257  ILE   A CB  
1324  C  CG1 . ILE   A 188 ? 0.9052 1.0114 0.9756 -0.0224 -0.0653 0.0257  257  ILE   A CG1 
1325  C  CG2 . ILE   A 188 ? 0.8788 0.9874 0.9464 -0.0243 -0.0671 0.0248  257  ILE   A CG2 
1326  C  CD1 . ILE   A 188 ? 0.9533 1.0580 1.0268 -0.0249 -0.0604 0.0246  257  ILE   A CD1 
1327  N  N   . LYS   A 189 ? 0.9624 1.0903 1.0458 -0.0212 -0.0760 0.0246  258  LYS   A N   
1328  C  CA  . LYS   A 189 ? 0.9197 1.0527 1.0065 -0.0219 -0.0784 0.0241  258  LYS   A CA  
1329  C  C   . LYS   A 189 ? 0.9249 1.0607 1.0125 -0.0199 -0.0832 0.0250  258  LYS   A C   
1330  O  O   . LYS   A 189 ? 0.9859 1.1237 1.0744 -0.0206 -0.0858 0.0247  258  LYS   A O   
1331  C  CB  . LYS   A 189 ? 0.8734 1.0135 0.9689 -0.0228 -0.0767 0.0231  258  LYS   A CB  
1332  N  N   . LYS   A 190 ? 0.9293 1.0655 1.0175 -0.0174 -0.0846 0.0259  259  LYS   A N   
1333  C  CA  . LYS   A 190 ? 0.9629 1.1020 1.0528 -0.0154 -0.0893 0.0266  259  LYS   A CA  
1334  C  C   . LYS   A 190 ? 1.0109 1.1428 1.0915 -0.0149 -0.0922 0.0269  259  LYS   A C   
1335  O  O   . LYS   A 190 ? 1.0405 1.1740 1.1217 -0.0147 -0.0964 0.0268  259  LYS   A O   
1336  C  CB  . LYS   A 190 ? 0.9530 1.0948 1.0464 -0.0125 -0.0901 0.0276  259  LYS   A CB  
1337  C  CG  . LYS   A 190 ? 0.9349 1.0847 1.0379 -0.0120 -0.0884 0.0274  259  LYS   A CG  
1338  C  CD  . LYS   A 190 ? 0.9666 1.1234 1.0768 -0.0132 -0.0896 0.0271  259  LYS   A CD  
1339  C  CE  . LYS   A 190 ? 1.0079 1.1698 1.1246 -0.0137 -0.0863 0.0266  259  LYS   A CE  
1340  N  NZ  . LYS   A 190 ? 1.1321 1.3002 1.2556 -0.0150 -0.0869 0.0263  259  LYS   A NZ  
1341  N  N   . GLN   A 191 ? 1.0209 1.1442 1.0926 -0.0147 -0.0901 0.0274  260  GLN   A N   
1342  C  CA  . GLN   A 191 ? 1.0349 1.1494 1.0956 -0.0140 -0.0923 0.0277  260  GLN   A CA  
1343  C  C   . GLN   A 191 ? 1.0523 1.1647 1.1097 -0.0162 -0.0925 0.0268  260  GLN   A C   
1344  O  O   . GLN   A 191 ? 1.0898 1.1991 1.1422 -0.0154 -0.0968 0.0266  260  GLN   A O   
1345  C  CB  . GLN   A 191 ? 1.0469 1.1523 1.0990 -0.0136 -0.0888 0.0285  260  GLN   A CB  
1346  C  CG  . GLN   A 191 ? 1.0552 1.1622 1.1106 -0.0117 -0.0881 0.0293  260  GLN   A CG  
1347  C  CD  . GLN   A 191 ? 1.1120 1.2086 1.1575 -0.0109 -0.0859 0.0303  260  GLN   A CD  
1348  O  OE1 . GLN   A 191 ? 1.1384 1.2265 1.1735 -0.0107 -0.0862 0.0307  260  GLN   A OE1 
1349  N  NE2 . GLN   A 191 ? 1.0992 1.1958 1.1472 -0.0103 -0.0835 0.0307  260  GLN   A NE2 
1350  N  N   . LEU   A 192 ? 1.0345 1.1483 1.0946 -0.0188 -0.0880 0.0260  261  LEU   A N   
1351  C  CA  . LEU   A 192 ? 1.0051 1.1179 1.0632 -0.0208 -0.0880 0.0250  261  LEU   A CA  
1352  C  C   . LEU   A 192 ? 1.0795 1.1988 1.1436 -0.0207 -0.0932 0.0244  261  LEU   A C   
1353  O  O   . LEU   A 192 ? 1.1563 1.2726 1.2159 -0.0214 -0.0956 0.0238  261  LEU   A O   
1354  C  CB  . LEU   A 192 ? 0.9109 1.0262 0.9735 -0.0233 -0.0828 0.0242  261  LEU   A CB  
1355  C  CG  . LEU   A 192 ? 0.9167 1.0237 0.9720 -0.0240 -0.0777 0.0245  261  LEU   A CG  
1356  C  CD1 . LEU   A 192 ? 0.8940 1.0041 0.9551 -0.0263 -0.0729 0.0235  261  LEU   A CD1 
1357  C  CD2 . LEU   A 192 ? 1.0023 1.1001 1.0459 -0.0239 -0.0784 0.0246  261  LEU   A CD2 
1358  N  N   . ARG   A 193 ? 1.0949 1.2229 1.1691 -0.0198 -0.0949 0.0247  262  ARG   A N   
1359  C  CA  . ARG   A 193 ? 1.1308 1.2657 1.2125 -0.0199 -0.0991 0.0243  262  ARG   A CA  
1360  C  C   . ARG   A 193 ? 1.1711 1.3028 1.2484 -0.0180 -0.1052 0.0245  262  ARG   A C   
1361  O  O   . ARG   A 193 ? 1.2351 1.3693 1.3155 -0.0186 -0.1093 0.0238  262  ARG   A O   
1362  C  CB  . ARG   A 193 ? 1.1505 1.2950 1.2440 -0.0192 -0.0983 0.0248  262  ARG   A CB  
1363  N  N   . GLU   A 194 ? 1.1059 1.2316 1.1761 -0.0156 -0.1062 0.0254  263  GLU   A N   
1364  C  CA  . GLU   A 194 ? 1.0981 1.2193 1.1624 -0.0135 -0.1122 0.0253  263  GLU   A CA  
1365  C  C   . GLU   A 194 ? 1.1391 1.2515 1.1926 -0.0144 -0.1137 0.0244  263  GLU   A C   
1366  O  O   . GLU   A 194 ? 1.2123 1.3220 1.2624 -0.0131 -0.1198 0.0239  263  GLU   A O   
1367  C  CB  . GLU   A 194 ? 1.0998 1.2152 1.1572 -0.0105 -0.1126 0.0265  263  GLU   A CB  
1368  C  CG  . GLU   A 194 ? 1.1265 1.2483 1.1921 -0.0092 -0.1106 0.0274  263  GLU   A CG  
1369  C  CD  . GLU   A 194 ? 1.1931 1.3072 1.2500 -0.0075 -0.1082 0.0285  263  GLU   A CD  
1370  O  OE1 . GLU   A 194 ? 1.2009 1.3046 1.2456 -0.0076 -0.1072 0.0286  263  GLU   A OE1 
1371  O  OE2 . GLU   A 194 ? 1.2290 1.3468 1.2909 -0.0060 -0.1069 0.0292  263  GLU   A OE2 
1372  N  N   . TRP   A 195 ? 1.1032 1.2109 1.1512 -0.0165 -0.1084 0.0242  264  TRP   A N   
1373  C  CA  . TRP   A 195 ? 1.1071 1.2061 1.1443 -0.0171 -0.1093 0.0234  264  TRP   A CA  
1374  C  C   . TRP   A 195 ? 1.2075 1.3119 1.2511 -0.0195 -0.1108 0.0220  264  TRP   A C   
1375  O  O   . TRP   A 195 ? 1.2492 1.3501 1.2885 -0.0193 -0.1159 0.0211  264  TRP   A O   
1376  C  CB  . TRP   A 195 ? 1.0771 1.1678 1.1049 -0.0180 -0.1026 0.0238  264  TRP   A CB  
1377  C  CG  . TRP   A 195 ? 1.0528 1.1368 1.0733 -0.0159 -0.1008 0.0252  264  TRP   A CG  
1378  C  CD1 . TRP   A 195 ? 1.0582 1.1414 1.0774 -0.0130 -0.1049 0.0260  264  TRP   A CD1 
1379  C  CD2 . TRP   A 195 ? 1.0151 1.0921 1.0289 -0.0165 -0.0941 0.0261  264  TRP   A CD2 
1380  N  NE1 . TRP   A 195 ? 1.0627 1.1385 1.0743 -0.0118 -0.1013 0.0273  264  TRP   A NE1 
1381  C  CE2 . TRP   A 195 ? 1.0474 1.1193 1.0558 -0.0140 -0.0945 0.0274  264  TRP   A CE2 
1382  C  CE3 . TRP   A 195 ? 1.0423 1.1170 1.0548 -0.0188 -0.0878 0.0258  264  TRP   A CE3 
1383  C  CZ2 . TRP   A 195 ? 1.0800 1.1443 1.0818 -0.0140 -0.0886 0.0285  264  TRP   A CZ2 
1384  C  CZ3 . TRP   A 195 ? 1.0265 1.0941 1.0331 -0.0188 -0.0820 0.0269  264  TRP   A CZ3 
1385  C  CH2 . TRP   A 195 ? 0.9951 1.0576 0.9965 -0.0166 -0.0824 0.0282  264  TRP   A CH2 
1386  N  N   . ASP   A 196 ? 1.2871 1.3993 1.3404 -0.0218 -0.1067 0.0218  265  ASP   A N   
1387  C  CA  . ASP   A 196 ? 1.3573 1.4743 1.4167 -0.0243 -0.1071 0.0207  265  ASP   A CA  
1388  C  C   . ASP   A 196 ? 1.4171 1.5461 1.4914 -0.0247 -0.1079 0.0209  265  ASP   A C   
1389  O  O   . ASP   A 196 ? 1.4509 1.5850 1.5314 -0.0255 -0.1033 0.0212  265  ASP   A O   
1390  C  CB  . ASP   A 196 ? 1.3653 1.4797 1.4216 -0.0264 -0.1009 0.0202  265  ASP   A CB  
1391  C  CG  . ASP   A 196 ? 1.4148 1.5301 1.4723 -0.0286 -0.1019 0.0189  265  ASP   A CG  
1392  O  OD1 . ASP   A 196 ? 1.4368 1.5546 1.4976 -0.0286 -0.1074 0.0183  265  ASP   A OD1 
1393  O  OD2 . ASP   A 196 ? 1.4426 1.5562 1.4982 -0.0302 -0.0971 0.0184  265  ASP   A OD2 
1394  N  N   . GLU   A 197 ? 1.4526 1.5857 1.5325 -0.0239 -0.1138 0.0207  266  GLU   A N   
1395  C  CA  . GLU   A 197 ? 1.5399 1.6842 1.6344 -0.0243 -0.1142 0.0210  266  GLU   A CA  
1396  C  C   . GLU   A 197 ? 1.5902 1.7391 1.6908 -0.0271 -0.1109 0.0204  266  GLU   A C   
1397  O  O   . GLU   A 197 ? 1.5534 1.7060 1.6600 -0.0286 -0.1139 0.0197  266  GLU   A O   
1398  C  CB  . GLU   A 197 ? 1.5517 1.6993 1.6519 -0.0232 -0.1213 0.0207  266  GLU   A CB  
1399  C  CG  . GLU   A 197 ? 1.5255 1.6681 1.6193 -0.0201 -0.1257 0.0211  266  GLU   A CG  
1400  C  CD  . GLU   A 197 ? 1.5454 1.6919 1.6433 -0.0178 -0.1235 0.0226  266  GLU   A CD  
1401  O  OE1 . GLU   A 197 ? 1.5986 1.7523 1.7053 -0.0186 -0.1190 0.0233  266  GLU   A OE1 
1402  O  OE2 . GLU   A 197 ? 1.5220 1.6637 1.6137 -0.0151 -0.1263 0.0231  266  GLU   A OE2 
1403  N  N   . ASN   A 198 ? 1.7782 1.9270 1.8779 -0.0279 -0.1049 0.0206  267  ASN   A N   
1404  C  CA  . ASN   A 198 ? 1.8301 1.9816 1.9334 -0.0304 -0.1015 0.0199  267  ASN   A CA  
1405  C  C   . ASN   A 198 ? 1.8317 1.9875 1.9401 -0.0304 -0.0961 0.0203  267  ASN   A C   
1406  O  O   . ASN   A 198 ? 1.8448 2.0052 1.9588 -0.0287 -0.0956 0.0213  267  ASN   A O   
1407  C  CB  . ASN   A 198 ? 1.8214 1.9645 1.9141 -0.0318 -0.1004 0.0188  267  ASN   A CB  
1408  C  CG  . ASN   A 198 ? 1.8821 2.0226 1.9723 -0.0327 -0.1054 0.0178  267  ASN   A CG  
1409  O  OD1 . ASN   A 198 ? 1.9069 2.0521 2.0041 -0.0325 -0.1101 0.0178  267  ASN   A OD1 
1410  N  ND2 . ASN   A 198 ? 1.8912 2.0238 1.9715 -0.0336 -0.1045 0.0169  267  ASN   A ND2 
1411  N  N   . LEU   A 199 ? 1.7046 1.8587 1.8109 -0.0321 -0.0922 0.0195  268  LEU   A N   
1412  C  CA  . LEU   A 199 ? 1.6602 1.8194 1.7729 -0.0324 -0.0881 0.0196  268  LEU   A CA  
1413  C  C   . LEU   A 199 ? 1.6459 1.8049 1.7584 -0.0306 -0.0854 0.0202  268  LEU   A C   
1414  O  O   . LEU   A 199 ? 1.6978 1.8511 1.8033 -0.0299 -0.0849 0.0204  268  LEU   A O   
1415  C  CB  . LEU   A 199 ? 1.6198 1.7766 1.7300 -0.0345 -0.0850 0.0183  268  LEU   A CB  
1416  C  CG  . LEU   A 199 ? 1.7191 1.8761 1.8299 -0.0364 -0.0872 0.0175  268  LEU   A CG  
1417  C  CD1 . LEU   A 199 ? 1.7453 1.8998 1.8534 -0.0381 -0.0839 0.0163  268  LEU   A CD1 
1418  C  CD2 . LEU   A 199 ? 1.6225 1.7871 1.7435 -0.0366 -0.0891 0.0181  268  LEU   A CD2 
1419  N  N   . LYS   A 200 ? 1.6237 1.7886 1.7436 -0.0297 -0.0837 0.0207  269  LYS   A N   
1420  C  CA  . LYS   A 200 ? 1.6099 1.7753 1.7307 -0.0279 -0.0814 0.0211  269  LYS   A CA  
1421  C  C   . LYS   A 200 ? 1.5355 1.7013 1.6576 -0.0285 -0.0775 0.0202  269  LYS   A C   
1422  O  O   . LYS   A 200 ? 1.4748 1.6418 1.5991 -0.0269 -0.0757 0.0203  269  LYS   A O   
1423  C  CB  . LYS   A 200 ? 1.6406 1.8119 1.7683 -0.0257 -0.0826 0.0223  269  LYS   A CB  
1424  N  N   . ASP   A 201 ? 1.5548 1.7191 1.6754 -0.0306 -0.0764 0.0191  270  ASP   A N   
1425  C  CA  . ASP   A 201 ? 1.5771 1.7431 1.7007 -0.0311 -0.0734 0.0181  270  ASP   A CA  
1426  C  C   . ASP   A 201 ? 1.5069 1.6680 1.6257 -0.0326 -0.0711 0.0169  270  ASP   A C   
1427  O  O   . ASP   A 201 ? 1.4293 1.5861 1.5438 -0.0323 -0.0703 0.0169  270  ASP   A O   
1428  C  CB  . ASP   A 201 ? 1.5378 1.7081 1.6661 -0.0321 -0.0741 0.0181  270  ASP   A CB  
1429  N  N   . ASP   A 202 ? 1.5487 1.7102 1.6683 -0.0341 -0.0699 0.0158  271  ASP   A N   
1430  C  CA  . ASP   A 202 ? 1.5594 1.7166 1.6751 -0.0354 -0.0674 0.0145  271  ASP   A CA  
1431  C  C   . ASP   A 202 ? 1.5609 1.7122 1.6694 -0.0360 -0.0678 0.0149  271  ASP   A C   
1432  O  O   . ASP   A 202 ? 1.5687 1.7157 1.6738 -0.0367 -0.0651 0.0142  271  ASP   A O   
1433  C  CB  . ASP   A 202 ? 1.6035 1.7617 1.7204 -0.0368 -0.0669 0.0135  271  ASP   A CB  
1434  N  N   . SER   A 203 ? 1.4780 1.6285 1.5839 -0.0357 -0.0711 0.0159  272  SER   A N   
1435  C  CA  . SER   A 203 ? 1.4405 1.5847 1.5385 -0.0356 -0.0721 0.0164  272  SER   A CA  
1436  C  C   . SER   A 203 ? 1.3774 1.5165 1.4712 -0.0353 -0.0687 0.0164  272  SER   A C   
1437  O  O   . SER   A 203 ? 1.3211 1.4537 1.4078 -0.0360 -0.0671 0.0162  272  SER   A O   
1438  C  CB  . SER   A 203 ? 1.5183 1.6642 1.6170 -0.0341 -0.0760 0.0177  272  SER   A CB  
1439  O  OG  . SER   A 203 ? 1.5139 1.6648 1.6189 -0.0326 -0.0754 0.0182  272  SER   A OG  
1440  N  N   . LEU   A 204 ? 1.3818 1.5233 1.4799 -0.0343 -0.0674 0.0167  273  LEU   A N   
1441  C  CA  . LEU   A 204 ? 1.2502 1.3879 1.3467 -0.0341 -0.0642 0.0166  273  LEU   A CA  
1442  C  C   . LEU   A 204 ? 1.2008 1.3424 1.3045 -0.0342 -0.0619 0.0155  273  LEU   A C   
1443  O  O   . LEU   A 204 ? 1.2812 1.4282 1.3903 -0.0338 -0.0631 0.0150  273  LEU   A O   
1444  C  CB  . LEU   A 204 ? 1.1815 1.3180 1.2765 -0.0323 -0.0658 0.0180  273  LEU   A CB  
1445  C  CG  . LEU   A 204 ? 1.1053 1.2358 1.1918 -0.0317 -0.0675 0.0191  273  LEU   A CG  
1446  C  CD1 . LEU   A 204 ? 0.9965 1.1287 1.0843 -0.0296 -0.0702 0.0203  273  LEU   A CD1 
1447  C  CD2 . LEU   A 204 ? 1.1469 1.2696 1.2270 -0.0324 -0.0636 0.0192  273  LEU   A CD2 
1448  N  N   . PRO   A 205 ? 1.1012 1.2398 1.2051 -0.0346 -0.0586 0.0149  274  PRO   A N   
1449  C  CA  . PRO   A 205 ? 1.1073 1.2492 1.2183 -0.0345 -0.0571 0.0135  274  PRO   A CA  
1450  C  C   . PRO   A 205 ? 1.1530 1.2980 1.2681 -0.0325 -0.0588 0.0138  274  PRO   A C   
1451  O  O   . PRO   A 205 ? 1.1511 1.2957 1.2641 -0.0312 -0.0607 0.0152  274  PRO   A O   
1452  C  CB  . PRO   A 205 ? 1.1186 1.2559 1.2290 -0.0356 -0.0532 0.0129  274  PRO   A CB  
1453  C  CG  . PRO   A 205 ? 1.1582 1.2897 1.2604 -0.0366 -0.0521 0.0139  274  PRO   A CG  
1454  C  CD  . PRO   A 205 ? 1.1310 1.2626 1.2288 -0.0354 -0.0559 0.0154  274  PRO   A CD  
1455  N  N   . SER   A 206 ? 1.0772 1.2249 1.1981 -0.0320 -0.0582 0.0123  275  SER   A N   
1456  C  CA  . SER   A 206 ? 1.0142 1.1640 1.1385 -0.0299 -0.0597 0.0123  275  SER   A CA  
1457  C  C   . SER   A 206 ? 1.0127 1.1599 1.1395 -0.0299 -0.0582 0.0113  275  SER   A C   
1458  O  O   . SER   A 206 ? 1.0449 1.1919 1.1725 -0.0281 -0.0595 0.0117  275  SER   A O   
1459  C  CB  . SER   A 206 ? 1.0172 1.1717 1.1456 -0.0287 -0.0608 0.0114  275  SER   A CB  
1460  O  OG  . SER   A 206 ? 1.0652 1.2200 1.1957 -0.0300 -0.0593 0.0097  275  SER   A OG  
1461  N  N   . ASN   A 207 ? 0.9713 1.1165 1.0999 -0.0317 -0.0555 0.0101  276  ASN   A N   
1462  C  CA  . ASN   A 207 ? 1.0147 1.1573 1.1466 -0.0319 -0.0541 0.0093  276  ASN   A CA  
1463  C  C   . ASN   A 207 ? 1.1103 1.2479 1.2372 -0.0325 -0.0527 0.0110  276  ASN   A C   
1464  O  O   . ASN   A 207 ? 1.1821 1.3168 1.3038 -0.0338 -0.0511 0.0120  276  ASN   A O   
1465  C  CB  . ASN   A 207 ? 1.0759 1.2182 1.2126 -0.0336 -0.0515 0.0074  276  ASN   A CB  
1466  C  CG  . ASN   A 207 ? 1.1051 1.2452 1.2471 -0.0340 -0.0502 0.0062  276  ASN   A CG  
1467  O  OD1 . ASN   A 207 ? 1.0511 1.1879 1.1913 -0.0340 -0.0497 0.0074  276  ASN   A OD1 
1468  N  ND2 . ASN   A 207 ? 1.1829 1.3248 1.3320 -0.0343 -0.0498 0.0039  276  ASN   A ND2 
1469  N  N   . PRO   A 208 ? 1.0527 1.1884 1.1804 -0.0314 -0.0534 0.0113  277  PRO   A N   
1470  C  CA  . PRO   A 208 ? 1.0148 1.1448 1.1380 -0.0321 -0.0516 0.0128  277  PRO   A CA  
1471  C  C   . PRO   A 208 ? 1.0594 1.1853 1.1819 -0.0346 -0.0471 0.0127  277  PRO   A C   
1472  O  O   . PRO   A 208 ? 1.0798 1.2010 1.1950 -0.0351 -0.0456 0.0144  277  PRO   A O   
1473  C  CB  . PRO   A 208 ? 1.0035 1.1326 1.1304 -0.0310 -0.0526 0.0123  277  PRO   A CB  
1474  C  CG  . PRO   A 208 ? 1.0194 1.1534 1.1480 -0.0286 -0.0563 0.0118  277  PRO   A CG  
1475  C  CD  . PRO   A 208 ? 1.0983 1.2366 1.2293 -0.0291 -0.0564 0.0107  277  PRO   A CD  
1476  N  N   . ILE   A 209 ? 1.1031 1.2303 1.2327 -0.0359 -0.0450 0.0108  278  ILE   A N   
1477  C  CA  . ILE   A 209 ? 1.1613 1.2842 1.2908 -0.0382 -0.0401 0.0110  278  ILE   A CA  
1478  C  C   . ILE   A 209 ? 1.1469 1.2681 1.2690 -0.0388 -0.0386 0.0120  278  ILE   A C   
1479  O  O   . ILE   A 209 ? 1.1050 1.2202 1.2214 -0.0398 -0.0350 0.0133  278  ILE   A O   
1480  C  CB  . ILE   A 209 ? 1.1730 1.2982 1.3128 -0.0395 -0.0381 0.0086  278  ILE   A CB  
1481  C  CG1 . ILE   A 209 ? 1.2555 1.3865 1.3990 -0.0389 -0.0403 0.0067  278  ILE   A CG1 
1482  C  CG2 . ILE   A 209 ? 1.0748 1.1998 1.2216 -0.0392 -0.0391 0.0075  278  ILE   A CG2 
1483  C  CD1 . ILE   A 209 ? 1.2923 1.4258 1.4462 -0.0398 -0.0390 0.0041  278  ILE   A CD1 
1484  N  N   . ASP   A 210 ? 1.3240 1.4496 1.4453 -0.0381 -0.0414 0.0115  279  ASP   A N   
1485  C  CA  . ASP   A 210 ? 1.3304 1.4540 1.4446 -0.0387 -0.0407 0.0123  279  ASP   A CA  
1486  C  C   . ASP   A 210 ? 1.3386 1.4592 1.4438 -0.0375 -0.0431 0.0144  279  ASP   A C   
1487  O  O   . ASP   A 210 ? 1.3703 1.4855 1.4676 -0.0380 -0.0415 0.0155  279  ASP   A O   
1488  C  CB  . ASP   A 210 ? 1.3980 1.5270 1.5151 -0.0386 -0.0426 0.0110  279  ASP   A CB  
1489  C  CG  . ASP   A 210 ? 1.4362 1.5685 1.5623 -0.0392 -0.0411 0.0087  279  ASP   A CG  
1490  O  OD1 . ASP   A 210 ? 1.4730 1.6026 1.6022 -0.0405 -0.0372 0.0082  279  ASP   A OD1 
1491  O  OD2 . ASP   A 210 ? 1.3946 1.5320 1.5248 -0.0383 -0.0438 0.0075  279  ASP   A OD2 
1492  N  N   . PHE   A 211 ? 1.1520 1.2758 1.2583 -0.0359 -0.0470 0.0148  280  PHE   A N   
1493  C  CA  . PHE   A 211 ? 1.0799 1.2020 1.1792 -0.0345 -0.0500 0.0166  280  PHE   A CA  
1494  C  C   . PHE   A 211 ? 1.0418 1.1559 1.1338 -0.0345 -0.0478 0.0181  280  PHE   A C   
1495  O  O   . PHE   A 211 ? 1.0356 1.1458 1.1193 -0.0339 -0.0491 0.0194  280  PHE   A O   
1496  C  CB  . PHE   A 211 ? 1.0304 1.1573 1.1337 -0.0326 -0.0536 0.0167  280  PHE   A CB  
1497  C  CG  . PHE   A 211 ? 1.0029 1.1299 1.1012 -0.0310 -0.0573 0.0182  280  PHE   A CG  
1498  C  CD1 . PHE   A 211 ? 0.9893 1.1113 1.0818 -0.0299 -0.0578 0.0197  280  PHE   A CD1 
1499  C  CD2 . PHE   A 211 ? 1.0076 1.1400 1.1078 -0.0304 -0.0603 0.0181  280  PHE   A CD2 
1500  C  CE1 . PHE   A 211 ? 0.9747 1.0973 1.0636 -0.0282 -0.0616 0.0209  280  PHE   A CE1 
1501  C  CE2 . PHE   A 211 ? 1.0121 1.1453 1.1094 -0.0290 -0.0638 0.0193  280  PHE   A CE2 
1502  C  CZ  . PHE   A 211 ? 0.9837 1.1122 1.0755 -0.0278 -0.0646 0.0207  280  PHE   A CZ  
1503  N  N   . SER   A 212 ? 1.0348 1.1463 1.1298 -0.0351 -0.0447 0.0180  281  SER   A N   
1504  C  CA  . SER   A 212 ? 1.0052 1.1083 1.0932 -0.0353 -0.0417 0.0195  281  SER   A CA  
1505  C  C   . SER   A 212 ? 1.0180 1.1155 1.0993 -0.0365 -0.0381 0.0200  281  SER   A C   
1506  O  O   . SER   A 212 ? 1.0358 1.1270 1.1067 -0.0356 -0.0384 0.0215  281  SER   A O   
1507  C  CB  . SER   A 212 ? 1.0289 1.1305 1.1230 -0.0361 -0.0388 0.0191  281  SER   A CB  
1508  O  OG  . SER   A 212 ? 1.0596 1.1620 1.1601 -0.0382 -0.0347 0.0177  281  SER   A OG  
1509  N  N   . TYR   A 213 ? 1.0525 1.1518 1.1391 -0.0382 -0.0347 0.0186  282  TYR   A N   
1510  C  CA  . TYR   A 213 ? 1.0395 1.1329 1.1195 -0.0391 -0.0306 0.0191  282  TYR   A CA  
1511  C  C   . TYR   A 213 ? 1.0557 1.1483 1.1275 -0.0382 -0.0339 0.0194  282  TYR   A C   
1512  O  O   . TYR   A 213 ? 1.0891 1.1744 1.1512 -0.0381 -0.0317 0.0203  282  TYR   A O   
1513  C  CB  . TYR   A 213 ? 1.0141 1.1106 1.1024 -0.0409 -0.0267 0.0173  282  TYR   A CB  
1514  C  CG  . TYR   A 213 ? 1.0181 1.1140 1.1146 -0.0421 -0.0226 0.0169  282  TYR   A CG  
1515  C  CD1 . TYR   A 213 ? 0.9919 1.0806 1.0844 -0.0423 -0.0193 0.0186  282  TYR   A CD1 
1516  C  CD2 . TYR   A 213 ? 1.0974 1.1997 1.2059 -0.0431 -0.0222 0.0147  282  TYR   A CD2 
1517  C  CE1 . TYR   A 213 ? 1.0159 1.1043 1.1171 -0.0437 -0.0156 0.0181  282  TYR   A CE1 
1518  C  CE2 . TYR   A 213 ? 1.0995 1.2017 1.2168 -0.0444 -0.0190 0.0140  282  TYR   A CE2 
1519  C  CZ  . TYR   A 213 ? 1.0526 1.1480 1.1666 -0.0448 -0.0156 0.0157  282  TYR   A CZ  
1520  O  OH  . TYR   A 213 ? 1.0956 1.1914 1.2199 -0.0462 -0.0125 0.0149  282  TYR   A OH  
1521  N  N   . ARG   A 214 ? 1.0678 1.1675 1.1432 -0.0376 -0.0391 0.0186  283  ARG   A N   
1522  C  CA  . ARG   A 214 ? 1.0793 1.1785 1.1479 -0.0368 -0.0428 0.0189  283  ARG   A CA  
1523  C  C   . ARG   A 214 ? 1.1133 1.2068 1.1725 -0.0351 -0.0455 0.0207  283  ARG   A C   
1524  O  O   . ARG   A 214 ? 1.1203 1.2074 1.1694 -0.0345 -0.0460 0.0213  283  ARG   A O   
1525  C  CB  . ARG   A 214 ? 1.1300 1.2384 1.2061 -0.0366 -0.0471 0.0178  283  ARG   A CB  
1526  C  CG  . ARG   A 214 ? 1.1663 1.2749 1.2374 -0.0363 -0.0508 0.0178  283  ARG   A CG  
1527  C  CD  . ARG   A 214 ? 1.1882 1.2947 1.2568 -0.0376 -0.0485 0.0169  283  ARG   A CD  
1528  N  NE  . ARG   A 214 ? 1.3124 1.4184 1.3757 -0.0372 -0.0527 0.0169  283  ARG   A NE  
1529  C  CZ  . ARG   A 214 ? 1.3703 1.4833 1.4391 -0.0372 -0.0568 0.0164  283  ARG   A CZ  
1530  N  NH1 . ARG   A 214 ? 1.3003 1.4207 1.3789 -0.0373 -0.0570 0.0157  283  ARG   A NH1 
1531  N  NH2 . ARG   A 214 ? 1.4103 1.5221 1.4745 -0.0369 -0.0609 0.0165  283  ARG   A NH2 
1532  N  N   . VAL   A 215 ? 1.0739 1.1692 1.1357 -0.0339 -0.0475 0.0213  284  VAL   A N   
1533  C  CA  . VAL   A 215 ? 1.0132 1.1031 1.0663 -0.0320 -0.0503 0.0229  284  VAL   A CA  
1534  C  C   . VAL   A 215 ? 1.0046 1.0833 1.0467 -0.0319 -0.0463 0.0242  284  VAL   A C   
1535  O  O   . VAL   A 215 ? 1.0125 1.0848 1.0440 -0.0304 -0.0486 0.0251  284  VAL   A O   
1536  C  CB  . VAL   A 215 ? 0.9670 1.0601 1.0250 -0.0308 -0.0522 0.0235  284  VAL   A CB  
1537  C  CG1 . VAL   A 215 ? 1.0108 1.0974 1.0594 -0.0287 -0.0545 0.0251  284  VAL   A CG1 
1538  C  CG2 . VAL   A 215 ? 1.0249 1.1280 1.0918 -0.0303 -0.0563 0.0225  284  VAL   A CG2 
1539  N  N   . ALA   A 216 ? 0.9980 1.0737 1.0424 -0.0333 -0.0403 0.0242  285  ALA   A N   
1540  C  CA  . ALA   A 216 ? 0.9940 1.0586 1.0282 -0.0332 -0.0354 0.0257  285  ALA   A CA  
1541  C  C   . ALA   A 216 ? 1.0424 1.1013 1.0673 -0.0331 -0.0343 0.0256  285  ALA   A C   
1542  O  O   . ALA   A 216 ? 1.0747 1.1230 1.0871 -0.0319 -0.0322 0.0270  285  ALA   A O   
1543  C  CB  . ALA   A 216 ? 0.9408 1.0043 0.9817 -0.0350 -0.0288 0.0256  285  ALA   A CB  
1544  N  N   . ALA   A 217 ? 1.0290 1.0943 1.0592 -0.0342 -0.0355 0.0240  286  ALA   A N   
1545  C  CA  . ALA   A 217 ? 1.0470 1.1069 1.0685 -0.0341 -0.0345 0.0238  286  ALA   A CA  
1546  C  C   . ALA   A 217 ? 1.0990 1.1581 1.1132 -0.0325 -0.0415 0.0237  286  ALA   A C   
1547  O  O   . ALA   A 217 ? 1.1368 1.1897 1.1416 -0.0319 -0.0415 0.0236  286  ALA   A O   
1548  C  CB  . ALA   A 217 ? 1.1102 1.1759 1.1401 -0.0360 -0.0318 0.0221  286  ALA   A CB  
1549  N  N   . CYS   A 218 ? 1.1450 1.2101 1.1636 -0.0315 -0.0473 0.0237  287  CYS   A N   
1550  C  CA  . CYS   A 218 ? 1.1501 1.2150 1.1634 -0.0300 -0.0542 0.0236  287  CYS   A CA  
1551  C  C   . CYS   A 218 ? 1.1440 1.2050 1.1517 -0.0277 -0.0577 0.0250  287  CYS   A C   
1552  O  O   . CYS   A 218 ? 1.1322 1.1947 1.1380 -0.0262 -0.0641 0.0248  287  CYS   A O   
1553  C  CB  . CYS   A 218 ? 1.1906 1.2670 1.2150 -0.0309 -0.0586 0.0223  287  CYS   A CB  
1554  S  SG  . CYS   A 218 ? 1.3367 1.4226 1.3727 -0.0303 -0.0611 0.0226  287  CYS   A SG  
1555  N  N   . LEU   A 219 ? 1.0468 1.1030 1.0524 -0.0273 -0.0536 0.0263  288  LEU   A N   
1556  C  CA  . LEU   A 219 ? 1.0447 1.0942 1.0416 -0.0248 -0.0563 0.0277  288  LEU   A CA  
1557  C  C   . LEU   A 219 ? 1.0767 1.1128 1.0571 -0.0233 -0.0549 0.0286  288  LEU   A C   
1558  O  O   . LEU   A 219 ? 1.0380 1.0686 1.0145 -0.0244 -0.0490 0.0287  288  LEU   A O   
1559  C  CB  . LEU   A 219 ? 1.0095 1.0582 1.0099 -0.0249 -0.0525 0.0288  288  LEU   A CB  
1560  C  CG  . LEU   A 219 ? 0.9521 1.0100 0.9624 -0.0242 -0.0567 0.0286  288  LEU   A CG  
1561  C  CD1 . LEU   A 219 ? 0.9263 0.9843 0.9419 -0.0250 -0.0523 0.0292  288  LEU   A CD1 
1562  C  CD2 . LEU   A 219 ? 1.0324 1.0873 1.0354 -0.0213 -0.0630 0.0294  288  LEU   A CD2 
1563  N  N   . PRO   A 220 ? 1.0780 1.1082 1.0484 -0.0205 -0.0605 0.0292  289  PRO   A N   
1564  C  CA  . PRO   A 220 ? 1.0913 1.1065 1.0441 -0.0183 -0.0590 0.0303  289  PRO   A CA  
1565  C  C   . PRO   A 220 ? 1.1409 1.1485 1.0890 -0.0178 -0.0530 0.0322  289  PRO   A C   
1566  O  O   . PRO   A 220 ? 1.1843 1.1880 1.1276 -0.0156 -0.0558 0.0333  289  PRO   A O   
1567  C  CB  . PRO   A 220 ? 1.0334 1.0468 0.9798 -0.0154 -0.0680 0.0300  289  PRO   A CB  
1568  C  CG  . PRO   A 220 ? 1.0546 1.0798 1.0143 -0.0156 -0.0720 0.0297  289  PRO   A CG  
1569  C  CD  . PRO   A 220 ? 1.0435 1.0803 1.0188 -0.0189 -0.0681 0.0289  289  PRO   A CD  
1570  N  N   . ILE   A 221 ? 1.0402 1.0463 0.9912 -0.0200 -0.0449 0.0326  290  ILE   A N   
1571  C  CA  . ILE   A 221 ? 1.0533 1.0522 1.0013 -0.0201 -0.0384 0.0344  290  ILE   A CA  
1572  C  C   . ILE   A 221 ? 1.1027 1.0903 1.0399 -0.0202 -0.0312 0.0353  290  ILE   A C   
1573  O  O   . ILE   A 221 ? 1.0464 1.0343 0.9819 -0.0208 -0.0309 0.0342  290  ILE   A O   
1574  C  CB  . ILE   A 221 ? 1.1066 1.1156 1.0712 -0.0228 -0.0350 0.0341  290  ILE   A CB  
1575  C  CG1 . ILE   A 221 ? 1.0824 1.1002 1.0583 -0.0257 -0.0325 0.0323  290  ILE   A CG1 
1576  C  CG2 . ILE   A 221 ? 1.0649 1.0829 1.0378 -0.0220 -0.0416 0.0336  290  ILE   A CG2 
1577  C  CD1 . ILE   A 221 ? 1.0047 1.0311 0.9961 -0.0282 -0.0291 0.0317  290  ILE   A CD1 
1578  N  N   . ASP   A 222 ? 1.3056 1.2826 1.2350 -0.0196 -0.0251 0.0374  291  ASP   A N   
1579  C  CA  . ASP   A 222 ? 1.3102 1.2753 1.2288 -0.0195 -0.0171 0.0386  291  ASP   A CA  
1580  C  C   . ASP   A 222 ? 1.3133 1.2839 1.2454 -0.0230 -0.0089 0.0384  291  ASP   A C   
1581  O  O   . ASP   A 222 ? 1.3296 1.3123 1.2780 -0.0253 -0.0100 0.0373  291  ASP   A O   
1582  C  CB  . ASP   A 222 ? 1.3248 1.2739 1.2264 -0.0166 -0.0144 0.0410  291  ASP   A CB  
1583  C  CG  . ASP   A 222 ? 1.3589 1.3086 1.2661 -0.0171 -0.0126 0.0424  291  ASP   A CG  
1584  O  OD1 . ASP   A 222 ? 1.3576 1.3205 1.2814 -0.0193 -0.0149 0.0412  291  ASP   A OD1 
1585  O  OD2 . ASP   A 222 ? 1.3777 1.3141 1.2720 -0.0152 -0.0089 0.0446  291  ASP   A OD2 
1586  N  N   . ASP   A 223 ? 1.1907 1.1525 1.1163 -0.0234 -0.0006 0.0394  292  ASP   A N   
1587  C  CA  . ASP   A 223 ? 1.1888 1.1567 1.1286 -0.0268 0.0068  0.0389  292  ASP   A CA  
1588  C  C   . ASP   A 223 ? 1.1295 1.0990 1.0788 -0.0284 0.0107  0.0400  292  ASP   A C   
1589  O  O   . ASP   A 223 ? 1.0830 1.0622 1.0489 -0.0314 0.0135  0.0388  292  ASP   A O   
1590  C  CB  . ASP   A 223 ? 1.1742 1.1322 1.1053 -0.0266 0.0153  0.0398  292  ASP   A CB  
1591  C  CG  . ASP   A 223 ? 1.1617 1.1256 1.0956 -0.0272 0.0135  0.0378  292  ASP   A CG  
1592  O  OD1 . ASP   A 223 ? 1.1497 1.1249 1.0919 -0.0278 0.0057  0.0357  292  ASP   A OD1 
1593  O  OD2 . ASP   A 223 ? 1.2438 1.2006 1.1714 -0.0270 0.0201  0.0383  292  ASP   A OD2 
1594  N  N   . VAL   A 224 ? 1.1392 1.0999 1.0790 -0.0266 0.0103  0.0419  293  VAL   A N   
1595  C  CA  . VAL   A 224 ? 1.1073 1.0690 1.0563 -0.0284 0.0145  0.0429  293  VAL   A CA  
1596  C  C   . VAL   A 224 ? 1.1459 1.1213 1.1095 -0.0294 0.0074  0.0411  293  VAL   A C   
1597  O  O   . VAL   A 224 ? 1.1816 1.1632 1.1594 -0.0320 0.0101  0.0406  293  VAL   A O   
1598  C  CB  . VAL   A 224 ? 1.0691 1.0155 1.0027 -0.0261 0.0177  0.0457  293  VAL   A CB  
1599  C  CG1 . VAL   A 224 ? 1.0665 1.0085 0.9866 -0.0224 0.0091  0.0460  293  VAL   A CG1 
1600  C  CG2 . VAL   A 224 ? 1.1525 1.1003 1.0968 -0.0283 0.0218  0.0466  293  VAL   A CG2 
1601  N  N   . LEU   A 225 ? 1.1496 1.1300 1.1107 -0.0275 -0.0017 0.0400  294  LEU   A N   
1602  C  CA  . LEU   A 225 ? 1.0876 1.0815 1.0628 -0.0284 -0.0080 0.0383  294  LEU   A CA  
1603  C  C   . LEU   A 225 ? 1.0662 1.0722 1.0569 -0.0311 -0.0073 0.0360  294  LEU   A C   
1604  O  O   . LEU   A 225 ? 1.0859 1.1006 1.0907 -0.0329 -0.0076 0.0350  294  LEU   A O   
1605  C  CB  . LEU   A 225 ? 1.1108 1.1072 1.0801 -0.0256 -0.0173 0.0378  294  LEU   A CB  
1606  C  CG  . LEU   A 225 ? 1.0297 1.0223 0.9938 -0.0233 -0.0211 0.0390  294  LEU   A CG  
1607  C  CD1 . LEU   A 225 ? 1.1030 1.0801 1.0532 -0.0222 -0.0151 0.0415  294  LEU   A CD1 
1608  C  CD2 . LEU   A 225 ? 1.1014 1.0962 1.0597 -0.0206 -0.0299 0.0384  294  LEU   A CD2 
1609  N  N   . ARG   A 226 ? 1.0591 1.0657 1.0469 -0.0313 -0.0071 0.0352  295  ARG   A N   
1610  C  CA  . ARG   A 226 ? 1.0282 1.0445 1.0295 -0.0338 -0.0051 0.0332  295  ARG   A CA  
1611  C  C   . ARG   A 226 ? 1.0373 1.0543 1.0495 -0.0364 0.0020  0.0333  295  ARG   A C   
1612  O  O   . ARG   A 226 ? 1.0000 1.0272 1.0273 -0.0382 0.0009  0.0316  295  ARG   A O   
1613  C  CB  . ARG   A 226 ? 1.0559 1.0687 1.0502 -0.0336 -0.0030 0.0328  295  ARG   A CB  
1614  C  CG  . ARG   A 226 ? 1.0462 1.0569 1.0292 -0.0312 -0.0099 0.0325  295  ARG   A CG  
1615  C  CD  . ARG   A 226 ? 1.0336 1.0458 1.0154 -0.0317 -0.0094 0.0312  295  ARG   A CD  
1616  N  NE  . ARG   A 226 ? 1.0790 1.0971 1.0603 -0.0306 -0.0182 0.0299  295  ARG   A NE  
1617  C  CZ  . ARG   A 226 ? 1.0475 1.0644 1.0227 -0.0300 -0.0208 0.0290  295  ARG   A CZ  
1618  N  NH1 . ARG   A 226 ? 1.0087 1.0189 0.9774 -0.0301 -0.0153 0.0291  295  ARG   A NH1 
1619  N  NH2 . ARG   A 226 ? 1.0331 1.0555 1.0089 -0.0291 -0.0290 0.0279  295  ARG   A NH2 
1620  N  N   . ILE   A 227 ? 1.0829 1.0885 1.0873 -0.0364 0.0094  0.0354  296  ILE   A N   
1621  C  CA  . ILE   A 227 ? 1.0668 1.0724 1.0820 -0.0391 0.0173  0.0356  296  ILE   A CA  
1622  C  C   . ILE   A 227 ? 1.0491 1.0600 1.0757 -0.0402 0.0153  0.0352  296  ILE   A C   
1623  O  O   . ILE   A 227 ? 1.0439 1.0616 1.0859 -0.0427 0.0178  0.0338  296  ILE   A O   
1624  C  CB  . ILE   A 227 ? 1.0323 1.0235 1.0354 -0.0386 0.0261  0.0382  296  ILE   A CB  
1625  C  CG1 . ILE   A 227 ? 1.0012 0.9890 0.9967 -0.0379 0.0290  0.0380  296  ILE   A CG1 
1626  C  CG2 . ILE   A 227 ? 1.0711 1.0614 1.0853 -0.0413 0.0343  0.0388  296  ILE   A CG2 
1627  C  CD1 . ILE   A 227 ? 1.0746 1.0492 1.0604 -0.0376 0.0389  0.0403  296  ILE   A CD1 
1628  N  N   . GLN   A 228 ? 1.1351 1.1435 1.1549 -0.0382 0.0102  0.0361  297  GLN   A N   
1629  C  CA  . GLN   A 228 ? 1.1351 1.1481 1.1646 -0.0390 0.0077  0.0356  297  GLN   A CA  
1630  C  C   . GLN   A 228 ? 1.1070 1.1340 1.1495 -0.0394 0.0009  0.0329  297  GLN   A C   
1631  O  O   . GLN   A 228 ? 1.1161 1.1493 1.1721 -0.0412 0.0010  0.0316  297  GLN   A O   
1632  C  CB  . GLN   A 228 ? 1.2226 1.2277 1.2397 -0.0363 0.0046  0.0376  297  GLN   A CB  
1633  C  CG  . GLN   A 228 ? 1.2973 1.2872 1.3001 -0.0355 0.0113  0.0404  297  GLN   A CG  
1634  C  CD  . GLN   A 228 ? 1.4228 1.4039 1.4085 -0.0318 0.0068  0.0422  297  GLN   A CD  
1635  O  OE1 . GLN   A 228 ? 1.4572 1.4441 1.4419 -0.0299 -0.0014 0.0412  297  GLN   A OE1 
1636  N  NE2 . GLN   A 228 ? 1.4042 1.3710 1.3764 -0.0307 0.0124  0.0448  297  GLN   A NE2 
1637  N  N   . LEU   A 229 ? 1.0318 1.0635 1.0702 -0.0378 -0.0050 0.0321  298  LEU   A N   
1638  C  CA  . LEU   A 229 ? 0.9509 0.9952 1.0010 -0.0382 -0.0104 0.0297  298  LEU   A CA  
1639  C  C   . LEU   A 229 ? 0.9815 1.0315 1.0441 -0.0409 -0.0064 0.0278  298  LEU   A C   
1640  O  O   . LEU   A 229 ? 1.0040 1.0629 1.0793 -0.0418 -0.0090 0.0259  298  LEU   A O   
1641  C  CB  . LEU   A 229 ? 0.9768 1.0243 1.0205 -0.0364 -0.0163 0.0292  298  LEU   A CB  
1642  C  CG  . LEU   A 229 ? 0.9697 1.0172 1.0060 -0.0337 -0.0232 0.0299  298  LEU   A CG  
1643  C  CD1 . LEU   A 229 ? 1.0078 1.0638 1.0539 -0.0332 -0.0280 0.0289  298  LEU   A CD1 
1644  C  CD2 . LEU   A 229 ? 1.0728 1.1081 1.0952 -0.0319 -0.0215 0.0323  298  LEU   A CD2 
1645  N  N   . LEU   A 230 ? 0.9907 1.0355 1.0498 -0.0418 -0.0002 0.0284  299  LEU   A N   
1646  C  CA  . LEU   A 230 ? 0.9838 1.0341 1.0549 -0.0441 0.0037  0.0267  299  LEU   A CA  
1647  C  C   . LEU   A 230 ? 0.9904 1.0415 1.0738 -0.0462 0.0076  0.0262  299  LEU   A C   
1648  O  O   . LEU   A 230 ? 1.0681 1.1273 1.1654 -0.0478 0.0073  0.0240  299  LEU   A O   
1649  C  CB  . LEU   A 230 ? 0.9822 1.0262 1.0460 -0.0444 0.0097  0.0275  299  LEU   A CB  
1650  C  CG  . LEU   A 230 ? 0.9939 1.0389 1.0493 -0.0429 0.0061  0.0270  299  LEU   A CG  
1651  C  CD1 . LEU   A 230 ? 1.0287 1.0683 1.0797 -0.0434 0.0128  0.0274  299  LEU   A CD1 
1652  C  CD2 . LEU   A 230 ? 1.0166 1.0737 1.0818 -0.0431 -0.0003 0.0245  299  LEU   A CD2 
1653  N  N   . LYS   A 231 ? 0.9898 1.0323 1.0682 -0.0463 0.0111  0.0283  300  LYS   A N   
1654  C  CA  . LYS   A 231 ? 0.9753 1.0178 1.0653 -0.0484 0.0147  0.0281  300  LYS   A CA  
1655  C  C   . LYS   A 231 ? 1.0174 1.0667 1.1158 -0.0481 0.0080  0.0265  300  LYS   A C   
1656  O  O   . LYS   A 231 ? 1.0337 1.0858 1.1450 -0.0500 0.0093  0.0253  300  LYS   A O   
1657  C  CB  . LYS   A 231 ? 0.9785 1.0085 1.0594 -0.0485 0.0212  0.0310  300  LYS   A CB  
1658  C  CG  . LYS   A 231 ? 0.9700 0.9921 1.0434 -0.0489 0.0292  0.0326  300  LYS   A CG  
1659  C  CD  . LYS   A 231 ? 1.0837 1.0942 1.1524 -0.0497 0.0371  0.0353  300  LYS   A CD  
1660  C  CE  . LYS   A 231 ? 1.1334 1.1321 1.1847 -0.0480 0.0425  0.0379  300  LYS   A CE  
1661  N  NZ  . LYS   A 231 ? 0.9993 0.9854 1.0358 -0.0462 0.0440  0.0408  300  LYS   A NZ  
1662  N  N   . ILE   A 232 ? 1.0233 1.0755 1.1153 -0.0457 0.0009  0.0264  301  ILE   A N   
1663  C  CA  . ILE   A 232 ? 0.9809 1.0393 1.0797 -0.0449 -0.0054 0.0250  301  ILE   A CA  
1664  C  C   . ILE   A 232 ? 1.0813 1.1500 1.1946 -0.0461 -0.0077 0.0219  301  ILE   A C   
1665  O  O   . ILE   A 232 ? 1.0860 1.1600 1.2001 -0.0458 -0.0091 0.0208  301  ILE   A O   
1666  C  CB  . ILE   A 232 ? 0.9540 1.0129 1.0424 -0.0419 -0.0119 0.0258  301  ILE   A CB  
1667  C  CG1 . ILE   A 232 ? 0.9783 1.0273 1.0552 -0.0406 -0.0108 0.0284  301  ILE   A CG1 
1668  C  CG2 . ILE   A 232 ? 1.0167 1.0846 1.1127 -0.0408 -0.0186 0.0239  301  ILE   A CG2 
1669  C  CD1 . ILE   A 232 ? 1.0388 1.0870 1.1045 -0.0375 -0.0165 0.0295  301  ILE   A CD1 
1670  N  N   . GLY   A 233 ? 1.2173 1.2884 1.3418 -0.0471 -0.0084 0.0205  302  GLY   A N   
1671  C  CA  . GLY   A 233 ? 1.2206 1.3002 1.3593 -0.0481 -0.0105 0.0174  302  GLY   A CA  
1672  C  C   . GLY   A 233 ? 1.1918 1.2793 1.3312 -0.0460 -0.0177 0.0157  302  GLY   A C   
1673  O  O   . GLY   A 233 ? 1.2115 1.3044 1.3539 -0.0461 -0.0184 0.0143  302  GLY   A O   
1674  N  N   . SER   A 234 ? 1.2212 1.3090 1.3574 -0.0440 -0.0227 0.0159  303  SER   A N   
1675  C  CA  . SER   A 234 ? 1.1894 1.2845 1.3275 -0.0418 -0.0291 0.0143  303  SER   A CA  
1676  C  C   . SER   A 234 ? 1.1622 1.2584 1.2898 -0.0399 -0.0315 0.0158  303  SER   A C   
1677  O  O   . SER   A 234 ? 1.1680 1.2586 1.2854 -0.0392 -0.0305 0.0181  303  SER   A O   
1678  C  CB  . SER   A 234 ? 1.1745 1.2692 1.3144 -0.0403 -0.0332 0.0139  303  SER   A CB  
1679  O  OG  . SER   A 234 ? 1.1727 1.2616 1.3022 -0.0390 -0.0333 0.0164  303  SER   A OG  
1680  N  N   . ALA   A 235 ? 1.0079 1.1111 1.1382 -0.0389 -0.0350 0.0143  304  ALA   A N   
1681  C  CA  . ALA   A 235 ? 0.9449 1.0499 1.0669 -0.0374 -0.0375 0.0154  304  ALA   A CA  
1682  C  C   . ALA   A 235 ? 0.9238 1.0274 1.0393 -0.0349 -0.0413 0.0169  304  ALA   A C   
1683  O  O   . ALA   A 235 ? 0.9756 1.0780 1.0827 -0.0338 -0.0425 0.0185  304  ALA   A O   
1684  C  CB  . ALA   A 235 ? 1.0112 1.1238 1.1383 -0.0369 -0.0403 0.0135  304  ALA   A CB  
1685  N  N   . ILE   A 236 ? 0.9711 1.0748 1.0903 -0.0338 -0.0434 0.0164  305  ILE   A N   
1686  C  CA  . ILE   A 236 ? 0.9206 1.0229 1.0337 -0.0312 -0.0468 0.0178  305  ILE   A CA  
1687  C  C   . ILE   A 236 ? 0.9363 1.0303 1.0411 -0.0315 -0.0443 0.0201  305  ILE   A C   
1688  O  O   . ILE   A 236 ? 0.9420 1.0342 1.0385 -0.0297 -0.0461 0.0218  305  ILE   A O   
1689  C  CB  . ILE   A 236 ? 0.8920 0.9961 1.0109 -0.0297 -0.0498 0.0165  305  ILE   A CB  
1690  C  CG1 . ILE   A 236 ? 0.8980 1.0095 1.0208 -0.0280 -0.0536 0.0149  305  ILE   A CG1 
1691  C  CG2 . ILE   A 236 ? 0.8749 0.9747 0.9878 -0.0277 -0.0515 0.0181  305  ILE   A CG2 
1692  C  CD1 . ILE   A 236 ? 0.9671 1.0801 1.0972 -0.0271 -0.0556 0.0128  305  ILE   A CD1 
1693  N  N   . GLN   A 237 ? 0.9567 1.0454 1.0639 -0.0335 -0.0400 0.0202  306  GLN   A N   
1694  C  CA  . GLN   A 237 ? 1.0099 1.0897 1.1084 -0.0338 -0.0368 0.0225  306  GLN   A CA  
1695  C  C   . GLN   A 237 ? 1.0345 1.1117 1.1238 -0.0338 -0.0353 0.0239  306  GLN   A C   
1696  O  O   . GLN   A 237 ? 1.0286 1.0995 1.1074 -0.0324 -0.0354 0.0260  306  GLN   A O   
1697  C  CB  . GLN   A 237 ? 1.0145 1.0895 1.1184 -0.0366 -0.0314 0.0223  306  GLN   A CB  
1698  C  CG  . GLN   A 237 ? 1.0078 1.0811 1.1169 -0.0364 -0.0326 0.0216  306  GLN   A CG  
1699  C  CD  . GLN   A 237 ? 1.0338 1.1053 1.1525 -0.0395 -0.0280 0.0206  306  GLN   A CD  
1700  O  OE1 . GLN   A 237 ? 1.0190 1.0921 1.1420 -0.0416 -0.0244 0.0199  306  GLN   A OE1 
1701  N  NE2 . GLN   A 237 ? 1.0458 1.1138 1.1683 -0.0399 -0.0282 0.0203  306  GLN   A NE2 
1702  N  N   . ARG   A 238 ? 1.0097 1.0913 1.1024 -0.0351 -0.0341 0.0228  307  ARG   A N   
1703  C  CA  . ARG   A 238 ? 0.9452 1.0242 1.0293 -0.0351 -0.0329 0.0238  307  ARG   A CA  
1704  C  C   . ARG   A 238 ? 0.9477 1.0295 1.0257 -0.0326 -0.0384 0.0244  307  ARG   A C   
1705  O  O   . ARG   A 238 ? 0.9582 1.0346 1.0258 -0.0316 -0.0387 0.0260  307  ARG   A O   
1706  C  CB  . ARG   A 238 ? 0.9631 1.0464 1.0535 -0.0371 -0.0304 0.0222  307  ARG   A CB  
1707  C  CG  . ARG   A 238 ? 0.9653 1.0446 1.0472 -0.0375 -0.0279 0.0231  307  ARG   A CG  
1708  C  CD  . ARG   A 238 ? 0.9085 0.9919 0.9970 -0.0394 -0.0251 0.0214  307  ARG   A CD  
1709  N  NE  . ARG   A 238 ? 0.9772 1.0594 1.0741 -0.0415 -0.0199 0.0207  307  ARG   A NE  
1710  C  CZ  . ARG   A 238 ? 1.0615 1.1503 1.1711 -0.0425 -0.0206 0.0185  307  ARG   A CZ  
1711  N  NH1 . ARG   A 238 ? 1.0416 1.1381 1.1560 -0.0414 -0.0260 0.0169  307  ARG   A NH1 
1712  N  NH2 . ARG   A 238 ? 1.0640 1.1511 1.1815 -0.0445 -0.0159 0.0179  307  ARG   A NH2 
1713  N  N   . LEU   A 239 ? 0.9250 1.0150 1.0095 -0.0315 -0.0429 0.0232  308  LEU   A N   
1714  C  CA  . LEU   A 239 ? 0.9368 1.0299 1.0172 -0.0291 -0.0481 0.0238  308  LEU   A CA  
1715  C  C   . LEU   A 239 ? 0.9789 1.0666 1.0523 -0.0269 -0.0497 0.0256  308  LEU   A C   
1716  O  O   . LEU   A 239 ? 0.9320 1.0173 0.9974 -0.0253 -0.0522 0.0268  308  LEU   A O   
1717  C  CB  . LEU   A 239 ? 0.8728 0.9750 0.9619 -0.0282 -0.0515 0.0223  308  LEU   A CB  
1718  C  CG  . LEU   A 239 ? 0.8743 0.9820 0.9700 -0.0298 -0.0505 0.0204  308  LEU   A CG  
1719  C  CD1 . LEU   A 239 ? 0.8486 0.9630 0.9523 -0.0287 -0.0532 0.0190  308  LEU   A CD1 
1720  C  CD2 . LEU   A 239 ? 0.9318 1.0409 1.0230 -0.0300 -0.0516 0.0208  308  LEU   A CD2 
1721  N  N   . ARG   A 240 ? 0.9906 1.0761 1.0670 -0.0268 -0.0488 0.0256  309  ARG   A N   
1722  C  CA  . ARG   A 240 ? 0.9694 1.0498 1.0397 -0.0246 -0.0505 0.0271  309  ARG   A CA  
1723  C  C   . ARG   A 240 ? 0.9769 1.0477 1.0357 -0.0244 -0.0484 0.0291  309  ARG   A C   
1724  O  O   . ARG   A 240 ? 0.9499 1.0170 1.0011 -0.0220 -0.0511 0.0305  309  ARG   A O   
1725  C  CB  . ARG   A 240 ? 0.9700 1.0485 1.0456 -0.0250 -0.0491 0.0266  309  ARG   A CB  
1726  C  CG  . ARG   A 240 ? 0.9073 0.9929 0.9905 -0.0236 -0.0528 0.0252  309  ARG   A CG  
1727  C  CD  . ARG   A 240 ? 0.9320 1.0149 1.0200 -0.0241 -0.0515 0.0244  309  ARG   A CD  
1728  N  NE  . ARG   A 240 ? 0.9034 0.9776 0.9845 -0.0235 -0.0502 0.0262  309  ARG   A NE  
1729  C  CZ  . ARG   A 240 ? 0.9939 1.0661 1.0693 -0.0206 -0.0534 0.0274  309  ARG   A CZ  
1730  N  NH1 . ARG   A 240 ? 0.9695 1.0479 1.0452 -0.0179 -0.0579 0.0273  309  ARG   A NH1 
1731  N  NH2 . ARG   A 240 ? 1.1803 1.2439 1.2498 -0.0202 -0.0519 0.0289  309  ARG   A NH2 
1732  N  N   . CYS   A 241 ? 0.9857 1.0522 1.0430 -0.0268 -0.0433 0.0292  310  CYS   A N   
1733  C  CA  . CYS   A 241 ? 1.0098 1.0663 1.0553 -0.0267 -0.0404 0.0310  310  CYS   A CA  
1734  C  C   . CYS   A 241 ? 0.9946 1.0520 1.0333 -0.0255 -0.0435 0.0311  310  CYS   A C   
1735  O  O   . CYS   A 241 ? 0.9744 1.0254 1.0022 -0.0234 -0.0455 0.0326  310  CYS   A O   
1736  C  CB  . CYS   A 241 ? 1.0712 1.1231 1.1186 -0.0296 -0.0334 0.0309  310  CYS   A CB  
1737  S  SG  . CYS   A 241 ? 1.0622 1.1003 1.0946 -0.0295 -0.0281 0.0333  310  CYS   A SG  
1738  N  N   . GLU   A 242 ? 1.0032 1.0681 1.0483 -0.0268 -0.0442 0.0296  311  GLU   A N   
1739  C  CA  . GLU   A 242 ? 1.0237 1.0904 1.0638 -0.0258 -0.0478 0.0295  311  GLU   A CA  
1740  C  C   . GLU   A 242 ? 1.0157 1.0848 1.0534 -0.0229 -0.0540 0.0300  311  GLU   A C   
1741  O  O   . GLU   A 242 ? 0.9972 1.0638 1.0273 -0.0214 -0.0573 0.0306  311  GLU   A O   
1742  C  CB  . GLU   A 242 ? 1.0021 1.0779 1.0512 -0.0275 -0.0482 0.0276  311  GLU   A CB  
1743  C  CG  . GLU   A 242 ? 0.9861 1.0590 1.0340 -0.0297 -0.0435 0.0271  311  GLU   A CG  
1744  C  CD  . GLU   A 242 ? 1.0098 1.0916 1.0689 -0.0314 -0.0431 0.0252  311  GLU   A CD  
1745  O  OE1 . GLU   A 242 ? 1.0219 1.1117 1.0871 -0.0306 -0.0474 0.0243  311  GLU   A OE1 
1746  O  OE2 . GLU   A 242 ? 1.0457 1.1262 1.1076 -0.0334 -0.0383 0.0245  311  GLU   A OE2 
1747  N  N   . LEU   A 243 ? 0.9627 1.0369 1.0074 -0.0220 -0.0560 0.0297  312  LEU   A N   
1748  C  CA  . LEU   A 243 ? 0.9170 0.9934 0.9599 -0.0190 -0.0615 0.0304  312  LEU   A CA  
1749  C  C   . LEU   A 243 ? 0.9747 1.0409 1.0065 -0.0171 -0.0616 0.0321  312  LEU   A C   
1750  O  O   . LEU   A 243 ? 1.0385 1.1036 1.0646 -0.0146 -0.0661 0.0328  312  LEU   A O   
1751  C  CB  . LEU   A 243 ? 0.9678 1.0518 1.0207 -0.0183 -0.0630 0.0296  312  LEU   A CB  
1752  C  CG  . LEU   A 243 ? 0.9733 1.0641 1.0292 -0.0157 -0.0685 0.0297  312  LEU   A CG  
1753  C  CD1 . LEU   A 243 ? 0.9885 1.0841 1.0451 -0.0160 -0.0711 0.0292  312  LEU   A CD1 
1754  C  CD2 . LEU   A 243 ? 1.0339 1.1315 1.0994 -0.0155 -0.0685 0.0286  312  LEU   A CD2 
1755  N  N   . ASP   A 244 ? 0.9916 1.0501 1.0202 -0.0182 -0.0567 0.0329  313  ASP   A N   
1756  C  CA  . ASP   A 244 ? 0.9973 1.0451 1.0147 -0.0163 -0.0562 0.0347  313  ASP   A CA  
1757  C  C   . ASP   A 244 ? 1.0205 1.0606 1.0256 -0.0154 -0.0566 0.0356  313  ASP   A C   
1758  O  O   . ASP   A 244 ? 0.9966 1.0318 0.9927 -0.0125 -0.0605 0.0366  313  ASP   A O   
1759  C  CB  . ASP   A 244 ? 1.0428 1.0842 1.0607 -0.0181 -0.0501 0.0353  313  ASP   A CB  
1760  C  CG  . ASP   A 244 ? 1.1135 1.1498 1.1281 -0.0161 -0.0511 0.0365  313  ASP   A CG  
1761  O  OD1 . ASP   A 244 ? 1.1360 1.1727 1.1463 -0.0129 -0.0564 0.0371  313  ASP   A OD1 
1762  O  OD2 . ASP   A 244 ? 1.1589 1.1906 1.1753 -0.0176 -0.0467 0.0369  313  ASP   A OD2 
1763  N  N   . ILE   A 245 ? 1.0457 1.0844 1.0500 -0.0177 -0.0528 0.0351  314  ILE   A N   
1764  C  CA  . ILE   A 245 ? 0.9920 1.0232 0.9842 -0.0169 -0.0531 0.0357  314  ILE   A CA  
1765  C  C   . ILE   A 245 ? 1.0097 1.0455 1.0004 -0.0146 -0.0607 0.0351  314  ILE   A C   
1766  O  O   . ILE   A 245 ? 1.0465 1.0745 1.0254 -0.0122 -0.0636 0.0359  314  ILE   A O   
1767  C  CB  . ILE   A 245 ? 0.9552 0.9868 0.9496 -0.0198 -0.0481 0.0349  314  ILE   A CB  
1768  C  CG1 . ILE   A 245 ? 0.9592 0.9849 0.9544 -0.0219 -0.0403 0.0356  314  ILE   A CG1 
1769  C  CG2 . ILE   A 245 ? 0.9756 1.0010 0.9585 -0.0187 -0.0496 0.0350  314  ILE   A CG2 
1770  C  CD1 . ILE   A 245 ? 0.9557 0.9836 0.9555 -0.0246 -0.0356 0.0346  314  ILE   A CD1 
1771  N  N   . MET   A 246 ? 1.0098 1.0579 1.0125 -0.0153 -0.0641 0.0336  315  MET   A N   
1772  C  CA  . MET   A 246 ? 0.9767 1.0302 0.9802 -0.0135 -0.0710 0.0330  315  MET   A CA  
1773  C  C   . MET   A 246 ? 1.0037 1.0565 1.0049 -0.0101 -0.0758 0.0339  315  MET   A C   
1774  O  O   . MET   A 246 ? 1.0586 1.1135 1.0583 -0.0081 -0.0818 0.0336  315  MET   A O   
1775  C  CB  . MET   A 246 ? 0.9244 0.9909 0.9416 -0.0151 -0.0725 0.0315  315  MET   A CB  
1776  C  CG  . MET   A 246 ? 0.9199 0.9883 0.9408 -0.0182 -0.0681 0.0304  315  MET   A CG  
1777  S  SD  . MET   A 246 ? 0.9138 0.9966 0.9494 -0.0192 -0.0708 0.0289  315  MET   A SD  
1778  C  CE  . MET   A 246 ? 0.9825 1.0666 1.0145 -0.0179 -0.0772 0.0286  315  MET   A CE  
1779  N  N   . ASN   A 247 ? 1.0019 1.0520 1.0034 -0.0095 -0.0736 0.0348  316  ASN   A N   
1780  C  CA  . ASN   A 247 ? 1.0227 1.0713 1.0215 -0.0062 -0.0777 0.0357  316  ASN   A CA  
1781  C  C   . ASN   A 247 ? 1.0048 1.0395 0.9888 -0.0042 -0.0767 0.0373  316  ASN   A C   
1782  O  O   . ASN   A 247 ? 1.0076 1.0390 0.9854 -0.0008 -0.0817 0.0379  316  ASN   A O   
1783  C  CB  . ASN   A 247 ? 1.0501 1.1048 1.0587 -0.0062 -0.0766 0.0356  316  ASN   A CB  
1784  C  CG  . ASN   A 247 ? 1.0601 1.1279 1.0825 -0.0076 -0.0777 0.0341  316  ASN   A CG  
1785  O  OD1 . ASN   A 247 ? 1.0361 1.1104 1.0621 -0.0073 -0.0814 0.0334  316  ASN   A OD1 
1786  N  ND2 . ASN   A 247 ? 1.1300 1.2013 1.1601 -0.0089 -0.0745 0.0337  316  ASN   A ND2 
1787  N  N   . LYS   A 248 ? 1.0322 1.0583 1.0104 -0.0061 -0.0702 0.0381  317  LYS   A N   
1788  C  CA  . LYS   A 248 ? 1.0541 1.0659 1.0178 -0.0043 -0.0680 0.0399  317  LYS   A CA  
1789  C  C   . LYS   A 248 ? 1.0785 1.0808 1.0287 -0.0034 -0.0682 0.0402  317  LYS   A C   
1790  O  O   . LYS   A 248 ? 1.0703 1.0639 1.0083 0.0000  -0.0718 0.0411  317  LYS   A O   
1791  C  CB  . LYS   A 248 ? 1.0679 1.0748 1.0330 -0.0067 -0.0603 0.0407  317  LYS   A CB  
1792  N  N   . CYS   A 249 ? 1.0641 1.0675 1.0158 -0.0061 -0.0646 0.0395  318  CYS   A N   
1793  C  CA  . CYS   A 249 ? 1.0089 1.0022 0.9472 -0.0055 -0.0636 0.0398  318  CYS   A CA  
1794  C  C   . CYS   A 249 ? 1.0060 1.0048 0.9450 -0.0044 -0.0708 0.0382  318  CYS   A C   
1795  O  O   . CYS   A 249 ? 1.0037 1.0065 0.9460 -0.0064 -0.0701 0.0370  318  CYS   A O   
1796  C  CB  . CYS   A 249 ? 1.0086 0.9996 0.9483 -0.0089 -0.0554 0.0399  318  CYS   A CB  
1797  S  SG  . CYS   A 249 ? 1.0306 1.0164 0.9722 -0.0105 -0.0474 0.0415  318  CYS   A SG  
1798  N  N   . THR   A 250 ? 1.0098 1.0082 0.9452 -0.0010 -0.0779 0.0383  319  THR   A N   
1799  C  CA  . THR   A 250 ? 1.0743 1.0790 1.0124 0.0003  -0.0859 0.0368  319  THR   A CA  
1800  C  C   . THR   A 250 ? 1.1204 1.1133 1.0423 0.0030  -0.0896 0.0369  319  THR   A C   
1801  O  O   . THR   A 250 ? 1.0995 1.0963 1.0229 0.0039  -0.0963 0.0354  319  THR   A O   
1802  C  CB  . THR   A 250 ? 1.0897 1.1017 1.0352 0.0026  -0.0918 0.0368  319  THR   A CB  
1803  O  OG1 . THR   A 250 ? 1.0379 1.0386 0.9712 0.0059  -0.0923 0.0383  319  THR   A OG1 
1804  C  CG2 . THR   A 250 ? 1.1206 1.1439 1.0815 0.0002  -0.0883 0.0366  319  THR   A CG2 
1805  N  N   . SER   A 251 ? 1.1703 1.1482 1.0767 0.0045  -0.0854 0.0384  320  SER   A N   
1806  C  CA  . SER   A 251 ? 1.2100 1.1744 1.0986 0.0072  -0.0876 0.0386  320  SER   A CA  
1807  C  C   . SER   A 251 ? 1.2154 1.1734 1.0983 0.0047  -0.0800 0.0388  320  SER   A C   
1808  O  O   . SER   A 251 ? 1.1997 1.1558 1.0844 0.0025  -0.0715 0.0401  320  SER   A O   
1809  C  CB  . SER   A 251 ? 1.2172 1.1676 1.0903 0.0112  -0.0884 0.0403  320  SER   A CB  
1810  O  OG  . SER   A 251 ? 1.2482 1.1855 1.1036 0.0146  -0.0924 0.0402  320  SER   A OG  
1811  N  N   . LEU   A 252 ? 1.1912 1.1466 1.0682 0.0052  -0.0832 0.0375  321  LEU   A N   
1812  C  CA  . LEU   A 252 ? 1.1429 1.0912 1.0125 0.0036  -0.0768 0.0376  321  LEU   A CA  
1813  C  C   . LEU   A 252 ? 1.2195 1.1487 1.0660 0.0075  -0.0770 0.0386  321  LEU   A C   
1814  O  O   . LEU   A 252 ? 1.2126 1.1374 1.0507 0.0109  -0.0856 0.0378  321  LEU   A O   
1815  C  CB  . LEU   A 252 ? 1.0950 1.0529 0.9733 0.0014  -0.0801 0.0354  321  LEU   A CB  
1816  C  CG  . LEU   A 252 ? 1.0772 1.0528 0.9769 -0.0024 -0.0791 0.0344  321  LEU   A CG  
1817  C  CD1 . LEU   A 252 ? 1.0439 1.0268 0.9499 -0.0042 -0.0819 0.0323  321  LEU   A CD1 
1818  C  CD2 . LEU   A 252 ? 1.1188 1.0955 1.0244 -0.0052 -0.0693 0.0356  321  LEU   A CD2 
1819  N  N   . CYS   A 253 ? 1.2219 1.1397 1.0584 0.0071  -0.0676 0.0405  322  CYS   A N   
1820  C  CA  . CYS   A 253 ? 1.2470 1.1447 1.0601 0.0110  -0.0659 0.0420  322  CYS   A CA  
1821  C  C   . CYS   A 253 ? 1.2401 1.1292 1.0438 0.0102  -0.0593 0.0421  322  CYS   A C   
1822  O  O   . CYS   A 253 ? 1.2289 1.1276 1.0448 0.0064  -0.0552 0.0412  322  CYS   A O   
1823  C  CB  . CYS   A 253 ? 1.1796 1.0684 0.9864 0.0120  -0.0600 0.0446  322  CYS   A CB  
1824  S  SG  . CYS   A 253 ? 1.2337 1.1296 1.0474 0.0141  -0.0686 0.0444  322  CYS   A SG  
1825  N  N   . CYS   A 254 ? 1.2424 1.1126 1.0235 0.0141  -0.0581 0.0433  323  CYS   A N   
1826  C  CA  . CYS   A 254 ? 1.2897 1.1487 1.0588 0.0142  -0.0508 0.0439  323  CYS   A CA  
1827  C  C   . CYS   A 254 ? 1.3101 1.1677 1.0838 0.0111  -0.0377 0.0462  323  CYS   A C   
1828  O  O   . CYS   A 254 ? 1.3468 1.1968 1.1153 0.0121  -0.0332 0.0485  323  CYS   A O   
1829  C  CB  . CYS   A 254 ? 1.3298 1.1676 1.0721 0.0198  -0.0531 0.0448  323  CYS   A CB  
1830  S  SG  . CYS   A 254 ? 1.4810 1.3024 1.2051 0.0208  -0.0441 0.0457  323  CYS   A SG  
1831  N  N   . LYS   A 255 ? 1.2746 1.1390 1.0581 0.0075  -0.0316 0.0455  324  LYS   A N   
1832  C  CA  . LYS   A 255 ? 1.2513 1.1165 1.0425 0.0042  -0.0196 0.0473  324  LYS   A CA  
1833  C  C   . LYS   A 255 ? 1.2428 1.0877 1.0141 0.0068  -0.0107 0.0502  324  LYS   A C   
1834  O  O   . LYS   A 255 ? 1.2567 1.0997 1.0322 0.0051  -0.0022 0.0523  324  LYS   A O   
1835  C  CB  . LYS   A 255 ? 1.2738 1.1497 1.0785 0.0004  -0.0155 0.0458  324  LYS   A CB  
1836  C  CG  . LYS   A 255 ? 1.2615 1.1394 1.0763 -0.0033 -0.0032 0.0473  324  LYS   A CG  
1837  C  CD  . LYS   A 255 ? 1.2151 1.1094 1.0527 -0.0072 -0.0032 0.0468  324  LYS   A CD  
1838  C  CE  . LYS   A 255 ? 1.1661 1.0580 1.0101 -0.0097 0.0083  0.0488  324  LYS   A CE  
1839  N  NZ  . LYS   A 255 ? 1.1394 1.0149 0.9677 -0.0071 0.0127  0.0517  324  LYS   A NZ  
1840  N  N   . GLN   A 256 ? 1.3093 1.1385 1.0587 0.0111  -0.0126 0.0504  325  GLN   A N   
1841  C  CA  . GLN   A 256 ? 1.3725 1.1812 1.1014 0.0138  -0.0031 0.0533  325  GLN   A CA  
1842  C  C   . GLN   A 256 ? 1.4062 1.2017 1.1205 0.0176  -0.0044 0.0554  325  GLN   A C   
1843  O  O   . GLN   A 256 ? 1.4887 1.2808 1.2054 0.0163  0.0037  0.0579  325  GLN   A O   
1844  C  CB  . GLN   A 256 ? 1.3595 1.1558 1.0701 0.0170  -0.0039 0.0526  325  GLN   A CB  
1845  C  CG  . GLN   A 256 ? 1.3865 1.1960 1.1099 0.0141  -0.0061 0.0499  325  GLN   A CG  
1846  C  CD  . GLN   A 256 ? 1.4072 1.2225 1.1432 0.0099  0.0059  0.0506  325  GLN   A CD  
1847  O  OE1 . GLN   A 256 ? 1.3963 1.2147 1.1423 0.0073  0.0137  0.0524  325  GLN   A OE1 
1848  N  NE2 . GLN   A 256 ? 1.4551 1.2717 1.1909 0.0093  0.0071  0.0491  325  GLN   A NE2 
1849  N  N   . CYS   A 257 ? 1.3687 1.1562 1.0679 0.0223  -0.0147 0.0545  326  CYS   A N   
1850  C  CA  . CYS   A 257 ? 1.4186 1.1929 1.1026 0.0264  -0.0169 0.0563  326  CYS   A CA  
1851  C  C   . CYS   A 257 ? 1.4491 1.2362 1.1501 0.0242  -0.0197 0.0565  326  CYS   A C   
1852  O  O   . CYS   A 257 ? 1.5420 1.3192 1.2338 0.0265  -0.0183 0.0586  326  CYS   A O   
1853  C  CB  . CYS   A 257 ? 1.3946 1.1588 1.0602 0.0321  -0.0285 0.0548  326  CYS   A CB  
1854  S  SG  . CYS   A 257 ? 1.3865 1.1709 1.0703 0.0312  -0.0441 0.0512  326  CYS   A SG  
1855  N  N   . GLN   A 258 ? 1.3916 1.1999 1.1165 0.0200  -0.0236 0.0543  327  GLN   A N   
1856  C  CA  . GLN   A 258 ? 1.3762 1.1989 1.1199 0.0173  -0.0257 0.0541  327  GLN   A CA  
1857  C  C   . GLN   A 258 ? 1.4171 1.2386 1.1557 0.0211  -0.0362 0.0537  327  GLN   A C   
1858  O  O   . GLN   A 258 ? 1.4828 1.3149 1.2353 0.0195  -0.0382 0.0536  327  GLN   A O   
1859  C  CB  . GLN   A 258 ? 1.4115 1.2312 1.1598 0.0147  -0.0143 0.0568  327  GLN   A CB  
1860  C  CG  . GLN   A 258 ? 1.4041 1.2393 1.1748 0.0089  -0.0082 0.0560  327  GLN   A CG  
1861  C  CD  . GLN   A 258 ? 1.5620 1.3927 1.3365 0.0066  0.0028  0.0586  327  GLN   A CD  
1862  O  OE1 . GLN   A 258 ? 1.5248 1.3512 1.2968 0.0077  0.0024  0.0601  327  GLN   A OE1 
1863  N  NE2 . GLN   A 258 ? 1.5811 1.4125 1.3617 0.0034  0.0128  0.0592  327  GLN   A NE2 
1864  N  N   . GLU   A 259 ? 1.4257 1.2342 1.1447 0.0262  -0.0429 0.0533  328  GLU   A N   
1865  C  CA  . GLU   A 259 ? 1.4348 1.2417 1.1488 0.0302  -0.0533 0.0528  328  GLU   A CA  
1866  C  C   . GLU   A 259 ? 1.4646 1.2723 1.1733 0.0331  -0.0648 0.0500  328  GLU   A C   
1867  O  O   . GLU   A 259 ? 1.4827 1.2736 1.1695 0.0379  -0.0678 0.0502  328  GLU   A O   
1868  C  CB  . GLU   A 259 ? 1.5474 1.3339 1.2401 0.0345  -0.0495 0.0557  328  GLU   A CB  
1869  N  N   . THR   A 260 ? 1.5872 1.4143 1.3160 0.0302  -0.0714 0.0474  329  THR   A N   
1870  C  CA  . THR   A 260 ? 1.5666 1.3986 1.2962 0.0318  -0.0826 0.0445  329  THR   A CA  
1871  C  C   . THR   A 260 ? 1.4741 1.3294 1.2302 0.0272  -0.0859 0.0425  329  THR   A C   
1872  O  O   . THR   A 260 ? 1.4423 1.3057 1.2082 0.0233  -0.0818 0.0416  329  THR   A O   
1873  C  CB  . THR   A 260 ? 1.5690 1.3899 1.2840 0.0328  -0.0810 0.0438  329  THR   A CB  
1874  O  OG1 . THR   A 260 ? 1.5710 1.3689 1.2599 0.0376  -0.0778 0.0458  329  THR   A OG1 
1875  C  CG2 . THR   A 260 ? 1.5373 1.3633 1.2539 0.0343  -0.0932 0.0405  329  THR   A CG2 
1876  N  N   . GLU   A 261 ? 1.3393 1.2049 1.1066 0.0277  -0.0929 0.0418  330  GLU   A N   
1877  C  CA  . GLU   A 261 ? 1.2823 1.1693 1.0741 0.0238  -0.0959 0.0401  330  GLU   A CA  
1878  C  C   . GLU   A 261 ? 1.3205 1.2136 1.1160 0.0239  -0.1044 0.0373  330  GLU   A C   
1879  O  O   . GLU   A 261 ? 1.3482 1.2376 1.1370 0.0276  -0.1143 0.0360  330  GLU   A O   
1880  C  CB  . GLU   A 261 ? 1.2870 1.1812 1.0875 0.0251  -0.1006 0.0405  330  GLU   A CB  
1881  C  CG  . GLU   A 261 ? 1.2847 1.1990 1.1072 0.0229  -0.1069 0.0385  330  GLU   A CG  
1882  C  CD  . GLU   A 261 ? 1.2888 1.2079 1.1171 0.0252  -0.1120 0.0389  330  GLU   A CD  
1883  O  OE1 . GLU   A 261 ? 1.2787 1.1935 1.1046 0.0254  -0.1065 0.0409  330  GLU   A OE1 
1884  O  OE2 . GLU   A 261 ? 1.2710 1.1979 1.1062 0.0269  -0.1215 0.0371  330  GLU   A OE2 
1885  N  N   . ILE   A 262 ? 1.3017 1.2035 1.1074 0.0197  -0.1005 0.0364  331  ILE   A N   
1886  C  CA  . ILE   A 262 ? 1.2821 1.1875 1.0896 0.0194  -0.1070 0.0338  331  ILE   A CA  
1887  C  C   . ILE   A 262 ? 1.3030 1.2266 1.1307 0.0179  -0.1150 0.0320  331  ILE   A C   
1888  O  O   . ILE   A 262 ? 1.3175 1.2419 1.1443 0.0202  -0.1251 0.0301  331  ILE   A O   
1889  C  CB  . ILE   A 262 ? 1.2740 1.1803 1.0833 0.0158  -0.0991 0.0337  331  ILE   A CB  
1890  C  CG1 . ILE   A 262 ? 1.2855 1.1748 1.0768 0.0171  -0.0895 0.0359  331  ILE   A CG1 
1891  C  CG2 . ILE   A 262 ? 1.3116 1.2190 1.1196 0.0159  -0.1058 0.0312  331  ILE   A CG2 
1892  C  CD1 . ILE   A 262 ? 1.3490 1.2204 1.1174 0.0215  -0.0931 0.0356  331  ILE   A CD1 
1893  N  N   . THR   A 263 ? 1.2574 1.1957 1.1037 0.0141  -0.1106 0.0324  332  THR   A N   
1894  C  CA  . THR   A 263 ? 1.2446 1.2008 1.1111 0.0122  -0.1164 0.0308  332  THR   A CA  
1895  C  C   . THR   A 263 ? 1.2048 1.1709 1.0847 0.0104  -0.1118 0.0322  332  THR   A C   
1896  O  O   . THR   A 263 ? 1.1361 1.0957 1.0107 0.0101  -0.1041 0.0341  332  THR   A O   
1897  C  CB  . THR   A 263 ? 1.1627 1.1274 1.0385 0.0087  -0.1162 0.0290  332  THR   A CB  
1898  O  OG1 . THR   A 263 ? 1.1531 1.1330 1.0461 0.0075  -0.1231 0.0274  332  THR   A OG1 
1899  C  CG2 . THR   A 263 ? 1.1768 1.1460 1.0597 0.0046  -0.1057 0.0299  332  THR   A CG2 
1900  N  N   . THR   A 264 ? 1.2027 1.1841 1.1002 0.0094  -0.1165 0.0311  333  THR   A N   
1901  C  CA  . THR   A 264 ? 1.1746 1.1656 1.0846 0.0085  -0.1142 0.0321  333  THR   A CA  
1902  C  C   . THR   A 264 ? 1.1761 1.1847 1.1067 0.0050  -0.1144 0.0309  333  THR   A C   
1903  O  O   . THR   A 264 ? 1.1681 1.1826 1.1043 0.0042  -0.1193 0.0292  333  THR   A O   
1904  C  CB  . THR   A 264 ? 1.1854 1.1743 1.0925 0.0127  -0.1211 0.0325  333  THR   A CB  
1905  O  OG1 . THR   A 264 ? 1.2964 1.2964 1.2177 0.0119  -0.1196 0.0331  333  THR   A OG1 
1906  C  CG2 . THR   A 264 ? 1.1962 1.1883 1.1053 0.0147  -0.1316 0.0305  333  THR   A CG2 
1907  N  N   . LYS   A 265 ? 1.1351 1.1515 1.0765 0.0031  -0.1092 0.0318  334  LYS   A N   
1908  C  CA  . LYS   A 265 ? 1.1199 1.1507 1.0784 -0.0005 -0.1071 0.0309  334  LYS   A CA  
1909  C  C   . LYS   A 265 ? 1.1594 1.2012 1.1291 -0.0002 -0.1146 0.0294  334  LYS   A C   
1910  O  O   . LYS   A 265 ? 1.2191 1.2696 1.1988 -0.0031 -0.1141 0.0283  334  LYS   A O   
1911  C  CB  . LYS   A 265 ? 1.0923 1.1294 1.0603 -0.0017 -0.1021 0.0319  334  LYS   A CB  
1912  N  N   . ASN   A 266 ? 1.1665 1.2079 1.1352 0.0031  -0.1216 0.0294  335  ASN   A N   
1913  C  CA  . ASN   A 266 ? 1.1745 1.2275 1.1562 0.0033  -0.1283 0.0281  335  ASN   A CA  
1914  C  C   . ASN   A 266 ? 1.1966 1.2472 1.1748 0.0031  -0.1339 0.0264  335  ASN   A C   
1915  O  O   . ASN   A 266 ? 1.2205 1.2803 1.2099 0.0030  -0.1397 0.0252  335  ASN   A O   
1916  C  CB  . ASN   A 266 ? 1.1992 1.2538 1.1831 0.0069  -0.1336 0.0286  335  ASN   A CB  
1917  C  CG  . ASN   A 266 ? 1.2649 1.3048 1.2312 0.0107  -0.1359 0.0293  335  ASN   A CG  
1918  O  OD1 . ASN   A 266 ? 1.4152 1.4469 1.3711 0.0123  -0.1409 0.0284  335  ASN   A OD1 
1919  N  ND2 . ASN   A 266 ? 1.2474 1.2830 1.2093 0.0122  -0.1324 0.0309  335  ASN   A ND2 
1920  N  N   . GLU   A 267 ? 1.2067 1.2448 1.1697 0.0033  -0.1324 0.0263  336  GLU   A N   
1921  C  CA  . GLU   A 267 ? 1.2140 1.2488 1.1726 0.0031  -0.1375 0.0245  336  GLU   A CA  
1922  C  C   . GLU   A 267 ? 1.1650 1.2031 1.1274 -0.0009 -0.1324 0.0238  336  GLU   A C   
1923  O  O   . GLU   A 267 ? 1.1581 1.1933 1.1168 -0.0014 -0.1359 0.0223  336  GLU   A O   
1924  C  CB  . GLU   A 267 ? 1.2482 1.2658 1.1858 0.0065  -0.1402 0.0245  336  GLU   A CB  
1925  C  CG  . GLU   A 267 ? 1.2818 1.2940 1.2131 0.0111  -0.1465 0.0250  336  GLU   A CG  
1926  C  CD  . GLU   A 267 ? 1.3262 1.3483 1.2698 0.0123  -0.1563 0.0234  336  GLU   A CD  
1927  O  OE1 . GLU   A 267 ? 1.3248 1.3536 1.2771 0.0103  -0.1600 0.0216  336  GLU   A OE1 
1928  O  OE2 . GLU   A 267 ? 1.3309 1.3537 1.2758 0.0155  -0.1603 0.0239  336  GLU   A OE2 
1929  N  N   . ILE   A 268 ? 1.1218 1.1650 1.0907 -0.0036 -0.1244 0.0248  337  ILE   A N   
1930  C  CA  . ILE   A 268 ? 1.0909 1.1380 1.0645 -0.0072 -0.1196 0.0241  337  ILE   A CA  
1931  C  C   . ILE   A 268 ? 1.1235 1.1845 1.1138 -0.0092 -0.1234 0.0228  337  ILE   A C   
1932  O  O   . ILE   A 268 ? 1.1643 1.2352 1.1667 -0.0089 -0.1250 0.0232  337  ILE   A O   
1933  C  CB  . ILE   A 268 ? 1.0772 1.1255 1.0533 -0.0092 -0.1103 0.0254  337  ILE   A CB  
1934  C  CG1 . ILE   A 268 ? 1.0531 1.0872 1.0132 -0.0076 -0.1057 0.0268  337  ILE   A CG1 
1935  C  CG2 . ILE   A 268 ? 1.0967 1.1505 1.0797 -0.0128 -0.1059 0.0245  337  ILE   A CG2 
1936  C  CD1 . ILE   A 268 ? 0.9949 1.0300 0.9583 -0.0097 -0.0967 0.0279  337  ILE   A CD1 
1937  N  N   . PHE   A 269 ? 1.0887 1.1501 1.0794 -0.0111 -0.1247 0.0214  338  PHE   A N   
1938  C  CA  . PHE   A 269 ? 1.1141 1.1884 1.1207 -0.0135 -0.1266 0.0204  338  PHE   A CA  
1939  C  C   . PHE   A 269 ? 1.1446 1.2185 1.1507 -0.0166 -0.1215 0.0197  338  PHE   A C   
1940  O  O   . PHE   A 269 ? 1.1346 1.2015 1.1321 -0.0170 -0.1152 0.0203  338  PHE   A O   
1941  C  CB  . PHE   A 269 ? 1.1063 1.1827 1.1163 -0.0122 -0.1360 0.0191  338  PHE   A CB  
1942  C  CG  . PHE   A 269 ? 1.1282 1.1951 1.1269 -0.0119 -0.1402 0.0175  338  PHE   A CG  
1943  C  CD1 . PHE   A 269 ? 1.1663 1.2185 1.1465 -0.0094 -0.1404 0.0178  338  PHE   A CD1 
1944  C  CD2 . PHE   A 269 ? 1.1935 1.2656 1.1998 -0.0141 -0.1440 0.0159  338  PHE   A CD2 
1945  C  CE1 . PHE   A 269 ? 1.1752 1.2179 1.1441 -0.0088 -0.1443 0.0163  338  PHE   A CE1 
1946  C  CE2 . PHE   A 269 ? 1.1941 1.2571 1.1898 -0.0137 -0.1483 0.0143  338  PHE   A CE2 
1947  C  CZ  . PHE   A 269 ? 1.1709 1.2191 1.1477 -0.0109 -0.1485 0.0145  338  PHE   A CZ  
1948  N  N   . SER   A 270 ? 1.1659 1.2477 1.1820 -0.0188 -0.1240 0.0184  339  SER   A N   
1949  C  CA  . SER   A 270 ? 1.2120 1.2940 1.2284 -0.0217 -0.1196 0.0177  339  SER   A CA  
1950  C  C   . SER   A 270 ? 1.2680 1.3518 1.2875 -0.0227 -0.1257 0.0159  339  SER   A C   
1951  O  O   . SER   A 270 ? 1.3345 1.4290 1.3681 -0.0244 -0.1276 0.0155  339  SER   A O   
1952  C  CB  . SER   A 270 ? 1.2270 1.3192 1.2559 -0.0239 -0.1135 0.0183  339  SER   A CB  
1953  O  OG  . SER   A 270 ? 1.1955 1.2849 1.2208 -0.0232 -0.1077 0.0196  339  SER   A OG  
1954  N  N   . LEU   A 271 ? 1.3158 1.3884 1.3217 -0.0217 -0.1285 0.0150  340  LEU   A N   
1955  C  CA  . LEU   A 271 ? 1.3415 1.4139 1.3486 -0.0223 -0.1356 0.0131  340  LEU   A CA  
1956  C  C   . LEU   A 271 ? 1.4660 1.5472 1.4847 -0.0259 -0.1333 0.0123  340  LEU   A C   
1957  O  O   . LEU   A 271 ? 1.4987 1.5874 1.5286 -0.0271 -0.1384 0.0114  340  LEU   A O   
1958  C  CB  . LEU   A 271 ? 1.2486 1.3061 1.2373 -0.0206 -0.1378 0.0122  340  LEU   A CB  
1959  C  CG  . LEU   A 271 ? 1.2676 1.3248 1.2580 -0.0212 -0.1457 0.0100  340  LEU   A CG  
1960  C  CD1 . LEU   A 271 ? 1.3034 1.3645 1.3004 -0.0194 -0.1548 0.0094  340  LEU   A CD1 
1961  C  CD2 . LEU   A 271 ? 1.2905 1.3328 1.2622 -0.0198 -0.1465 0.0090  340  LEU   A CD2 
1962  N  N   . SER   A 272 ? 1.6592 1.7396 1.6759 -0.0275 -0.1257 0.0128  341  SER   A N   
1963  C  CA  . SER   A 272 ? 1.6961 1.7841 1.7228 -0.0306 -0.1227 0.0122  341  SER   A CA  
1964  C  C   . SER   A 272 ? 1.6497 1.7465 1.6862 -0.0317 -0.1161 0.0135  341  SER   A C   
1965  O  O   . SER   A 272 ? 1.6373 1.7331 1.6717 -0.0302 -0.1131 0.0148  341  SER   A O   
1966  C  CB  . SER   A 272 ? 1.7539 1.8336 1.7701 -0.0315 -0.1199 0.0112  341  SER   A CB  
1967  O  OG  . SER   A 272 ? 1.7597 1.8337 1.7703 -0.0312 -0.1268 0.0095  341  SER   A OG  
1968  N  N   . LEU   A 273 ? 1.6055 1.7102 1.6525 -0.0342 -0.1139 0.0131  342  LEU   A N   
1969  C  CA  . LEU   A 273 ? 1.6115 1.7247 1.6684 -0.0351 -0.1083 0.0140  342  LEU   A CA  
1970  C  C   . LEU   A 273 ? 1.5753 1.6841 1.6260 -0.0351 -0.1011 0.0145  342  LEU   A C   
1971  O  O   . LEU   A 273 ? 1.5851 1.7001 1.6433 -0.0357 -0.0967 0.0150  342  LEU   A O   
1972  C  CB  . LEU   A 273 ? 1.6611 1.7825 1.7293 -0.0375 -0.1082 0.0134  342  LEU   A CB  
1973  C  CG  . LEU   A 273 ? 1.6764 1.7933 1.7396 -0.0393 -0.1073 0.0120  342  LEU   A CG  
1974  C  CD1 . LEU   A 273 ? 1.6711 1.7896 1.7357 -0.0404 -0.1001 0.0121  342  LEU   A CD1 
1975  C  CD2 . LEU   A 273 ? 1.5981 1.7194 1.6691 -0.0411 -0.1121 0.0110  342  LEU   A CD2 
1976  N  N   . CYS   A 274 ? 1.5758 1.6739 1.6131 -0.0343 -0.0999 0.0142  343  CYS   A N   
1977  C  CA  . CYS   A 274 ? 1.5568 1.6507 1.5890 -0.0346 -0.0927 0.0145  343  CYS   A CA  
1978  C  C   . CYS   A 274 ? 1.4987 1.5900 1.5278 -0.0330 -0.0895 0.0160  343  CYS   A C   
1979  O  O   . CYS   A 274 ? 1.4447 1.5333 1.4715 -0.0334 -0.0833 0.0163  343  CYS   A O   
1980  C  CB  . CYS   A 274 ? 1.6244 1.7077 1.6437 -0.0345 -0.0919 0.0137  343  CYS   A CB  
1981  S  SG  . CYS   A 274 ? 1.7189 1.8017 1.7378 -0.0355 -0.0985 0.0119  343  CYS   A SG  
1982  N  N   . GLY   A 275 ? 1.4367 1.5287 1.4661 -0.0312 -0.0937 0.0168  344  GLY   A N   
1983  C  CA  . GLY   A 275 ? 1.3428 1.4314 1.3684 -0.0295 -0.0913 0.0182  344  GLY   A CA  
1984  C  C   . GLY   A 275 ? 1.2210 1.3013 1.2359 -0.0269 -0.0962 0.0186  344  GLY   A C   
1985  O  O   . GLY   A 275 ? 1.2427 1.3199 1.2534 -0.0264 -0.1018 0.0177  344  GLY   A O   
1986  N  N   . PRO   A 276 ? 1.1249 1.2009 1.1350 -0.0251 -0.0944 0.0200  345  PRO   A N   
1987  C  CA  . PRO   A 276 ? 1.0722 1.1375 1.0689 -0.0223 -0.0979 0.0204  345  PRO   A CA  
1988  C  C   . PRO   A 276 ? 1.1190 1.1720 1.1013 -0.0220 -0.0934 0.0206  345  PRO   A C   
1989  O  O   . PRO   A 276 ? 1.2128 1.2581 1.1851 -0.0212 -0.0966 0.0197  345  PRO   A O   
1990  C  CB  . PRO   A 276 ? 1.0407 1.1070 1.0391 -0.0207 -0.0971 0.0219  345  PRO   A CB  
1991  C  CG  . PRO   A 276 ? 1.1377 1.2157 1.1509 -0.0226 -0.0938 0.0221  345  PRO   A CG  
1992  C  CD  . PRO   A 276 ? 1.1857 1.2664 1.2025 -0.0253 -0.0899 0.0211  345  PRO   A CD  
1993  N  N   . MET   A 277 ? 1.0904 1.1415 1.0721 -0.0228 -0.0858 0.0216  346  MET   A N   
1994  C  CA  . MET   A 277 ? 1.0210 1.0607 0.9903 -0.0226 -0.0800 0.0220  346  MET   A CA  
1995  C  C   . MET   A 277 ? 1.0094 1.0536 0.9848 -0.0253 -0.0755 0.0210  346  MET   A C   
1996  O  O   . MET   A 277 ? 1.0624 1.1095 1.0436 -0.0269 -0.0690 0.0213  346  MET   A O   
1997  C  CB  . MET   A 277 ? 1.0246 1.0593 0.9902 -0.0218 -0.0742 0.0238  346  MET   A CB  
1998  C  CG  . MET   A 277 ? 1.0544 1.0756 1.0054 -0.0209 -0.0686 0.0247  346  MET   A CG  
1999  S  SD  . MET   A 277 ? 1.1301 1.1489 1.0830 -0.0216 -0.0595 0.0265  346  MET   A SD  
2000  C  CE  . MET   A 277 ? 1.0928 1.1242 1.0629 -0.0253 -0.0546 0.0253  346  MET   A CE  
2001  N  N   . ALA   A 278 ? 0.9675 1.0121 0.9418 -0.0258 -0.0795 0.0195  347  ALA   A N   
2002  C  CA  . ALA   A 278 ? 1.0154 1.0621 0.9929 -0.0279 -0.0755 0.0184  347  ALA   A CA  
2003  C  C   . ALA   A 278 ? 1.0513 1.0851 1.0143 -0.0270 -0.0703 0.0188  347  ALA   A C   
2004  O  O   . ALA   A 278 ? 1.0908 1.1138 1.0408 -0.0246 -0.0704 0.0199  347  ALA   A O   
2005  C  CB  . ALA   A 278 ? 1.1305 1.1822 1.1124 -0.0289 -0.0816 0.0168  347  ALA   A CB  
2006  N  N   . ALA   A 279 ? 1.0476 1.0821 1.0125 -0.0286 -0.0654 0.0181  348  ALA   A N   
2007  C  CA  . ALA   A 279 ? 1.0635 1.0861 1.0152 -0.0277 -0.0601 0.0183  348  ALA   A CA  
2008  C  C   . ALA   A 279 ? 1.1037 1.1228 1.0493 -0.0276 -0.0638 0.0167  348  ALA   A C   
2009  O  O   . ALA   A 279 ? 1.1837 1.2116 1.1395 -0.0296 -0.0652 0.0153  348  ALA   A O   
2010  C  CB  . ALA   A 279 ? 1.0761 1.1013 1.0343 -0.0294 -0.0511 0.0187  348  ALA   A CB  
2011  N  N   . TYR   A 280 ? 1.0880 1.0937 1.0165 -0.0250 -0.0654 0.0168  349  TYR   A N   
2012  C  CA  . TYR   A 280 ? 1.1055 1.1057 1.0259 -0.0244 -0.0698 0.0151  349  TYR   A CA  
2013  C  C   . TYR   A 280 ? 1.1729 1.1602 1.0788 -0.0230 -0.0630 0.0155  349  TYR   A C   
2014  O  O   . TYR   A 280 ? 1.2000 1.1810 1.1002 -0.0220 -0.0561 0.0172  349  TYR   A O   
2015  C  CB  . TYR   A 280 ? 1.1342 1.1289 1.0461 -0.0222 -0.0794 0.0145  349  TYR   A CB  
2016  C  CG  . TYR   A 280 ? 1.1292 1.1358 1.0548 -0.0232 -0.0861 0.0143  349  TYR   A CG  
2017  C  CD1 . TYR   A 280 ? 1.1354 1.1464 1.0668 -0.0230 -0.0844 0.0159  349  TYR   A CD1 
2018  C  CD2 . TYR   A 280 ? 1.1504 1.1635 1.0833 -0.0243 -0.0939 0.0126  349  TYR   A CD2 
2019  C  CE1 . TYR   A 280 ? 1.1620 1.1835 1.1055 -0.0236 -0.0899 0.0158  349  TYR   A CE1 
2020  C  CE2 . TYR   A 280 ? 1.1493 1.1734 1.0953 -0.0251 -0.0992 0.0126  349  TYR   A CE2 
2021  C  CZ  . TYR   A 280 ? 1.1991 1.2272 1.1500 -0.0246 -0.0971 0.0142  349  TYR   A CZ  
2022  O  OH  . TYR   A 280 ? 1.3180 1.3567 1.2816 -0.0251 -0.1017 0.0144  349  TYR   A OH  
2023  N  N   . VAL   A 281 ? 1.2036 1.1868 1.1037 -0.0229 -0.0648 0.0139  350  VAL   A N   
2024  C  CA  . VAL   A 281 ? 1.2447 1.2160 1.1316 -0.0215 -0.0581 0.0141  350  VAL   A CA  
2025  C  C   . VAL   A 281 ? 1.3544 1.3122 1.2232 -0.0185 -0.0639 0.0131  350  VAL   A C   
2026  O  O   . VAL   A 281 ? 1.3741 1.3346 1.2449 -0.0191 -0.0719 0.0112  350  VAL   A O   
2027  C  CB  . VAL   A 281 ? 1.2649 1.2428 1.1609 -0.0238 -0.0531 0.0131  350  VAL   A CB  
2028  C  CG1 . VAL   A 281 ? 1.2949 1.2611 1.1785 -0.0221 -0.0445 0.0139  350  VAL   A CG1 
2029  C  CG2 . VAL   A 281 ? 1.3220 1.3152 1.2380 -0.0268 -0.0498 0.0135  350  VAL   A CG2 
2030  N  N   . ASN   A 282 ? 1.4464 1.3889 1.2973 -0.0154 -0.0596 0.0144  351  ASN   A N   
2031  C  CA  . ASN   A 282 ? 1.4621 1.3891 1.2928 -0.0119 -0.0643 0.0135  351  ASN   A CA  
2032  C  C   . ASN   A 282 ? 1.4813 1.4033 1.3064 -0.0119 -0.0606 0.0123  351  ASN   A C   
2033  O  O   . ASN   A 282 ? 1.4833 1.4125 1.3186 -0.0142 -0.0531 0.0126  351  ASN   A O   
2034  C  CB  . ASN   A 282 ? 1.4384 1.3502 1.2513 -0.0081 -0.0611 0.0155  351  ASN   A CB  
2035  C  CG  . ASN   A 282 ? 1.4818 1.3841 1.2855 -0.0070 -0.0490 0.0173  351  ASN   A CG  
2036  O  OD1 . ASN   A 282 ? 1.4999 1.4099 1.3148 -0.0095 -0.0416 0.0174  351  ASN   A OD1 
2037  N  ND2 . ASN   A 282 ? 1.4982 1.3834 1.2815 -0.0030 -0.0467 0.0187  351  ASN   A ND2 
2038  N  N   . PRO   A 283 ? 1.4665 1.3761 1.2754 -0.0093 -0.0659 0.0109  352  PRO   A N   
2039  C  CA  . PRO   A 283 ? 1.4488 1.3545 1.2532 -0.0094 -0.0633 0.0095  352  PRO   A CA  
2040  C  C   . PRO   A 283 ? 1.3854 1.2826 1.1814 -0.0079 -0.0510 0.0112  352  PRO   A C   
2041  O  O   . PRO   A 283 ? 1.4514 1.3431 1.2410 -0.0073 -0.0480 0.0102  352  PRO   A O   
2042  C  CB  . PRO   A 283 ? 1.4528 1.3454 1.2400 -0.0063 -0.0726 0.0077  352  PRO   A CB  
2043  C  CG  . PRO   A 283 ? 1.4333 1.3185 1.2108 -0.0035 -0.0767 0.0087  352  PRO   A CG  
2044  C  CD  . PRO   A 283 ? 1.4541 1.3542 1.2500 -0.0063 -0.0759 0.0100  352  PRO   A CD  
2045  N  N   . HIS   A 284 ? 1.3572 1.2532 1.1533 -0.0075 -0.0436 0.0136  353  HIS   A N   
2046  C  CA  . HIS   A 284 ? 1.3755 1.2653 1.1669 -0.0066 -0.0311 0.0154  353  HIS   A CA  
2047  C  C   . HIS   A 284 ? 1.3685 1.2723 1.1798 -0.0101 -0.0237 0.0167  353  HIS   A C   
2048  O  O   . HIS   A 284 ? 1.3804 1.2797 1.1897 -0.0095 -0.0131 0.0186  353  HIS   A O   
2049  C  CB  . HIS   A 284 ? 1.4315 1.3023 1.2006 -0.0022 -0.0272 0.0174  353  HIS   A CB  
2050  C  CG  . HIS   A 284 ? 1.4495 1.3038 1.1962 0.0019  -0.0331 0.0160  353  HIS   A CG  
2051  N  ND1 . HIS   A 284 ? 1.4120 1.2574 1.1482 0.0035  -0.0295 0.0151  353  HIS   A ND1 
2052  C  CD2 . HIS   A 284 ? 1.4710 1.3154 1.2036 0.0049  -0.0426 0.0154  353  HIS   A CD2 
2053  C  CE1 . HIS   A 284 ? 1.4837 1.3142 1.1998 0.0073  -0.0367 0.0139  353  HIS   A CE1 
2054  N  NE2 . HIS   A 284 ? 1.4595 1.2892 1.1732 0.0082  -0.0449 0.0140  353  HIS   A NE2 
2055  N  N   . GLY   A 285 ? 1.3426 1.2631 1.1734 -0.0135 -0.0288 0.0158  354  GLY   A N   
2056  C  CA  . GLY   A 285 ? 1.3761 1.3102 1.2262 -0.0167 -0.0227 0.0166  354  GLY   A CA  
2057  C  C   . GLY   A 285 ? 1.3300 1.2653 1.1832 -0.0167 -0.0205 0.0187  354  GLY   A C   
2058  O  O   . GLY   A 285 ? 1.3135 1.2602 1.1832 -0.0194 -0.0161 0.0193  354  GLY   A O   
2059  N  N   . TYR   A 286 ? 1.3247 1.2483 1.1625 -0.0138 -0.0234 0.0198  355  TYR   A N   
2060  C  CA  . TYR   A 286 ? 1.3029 1.2281 1.1440 -0.0138 -0.0225 0.0217  355  TYR   A CA  
2061  C  C   . TYR   A 286 ? 1.3026 1.2436 1.1609 -0.0164 -0.0305 0.0206  355  TYR   A C   
2062  O  O   . TYR   A 286 ? 1.3055 1.2499 1.1646 -0.0165 -0.0397 0.0188  355  TYR   A O   
2063  C  CB  . TYR   A 286 ? 1.3374 1.2455 1.1568 -0.0097 -0.0244 0.0229  355  TYR   A CB  
2064  C  CG  . TYR   A 286 ? 1.3561 1.2483 1.1590 -0.0070 -0.0145 0.0246  355  TYR   A CG  
2065  C  CD1 . TYR   A 286 ? 1.3436 1.2350 1.1505 -0.0078 -0.0035 0.0269  355  TYR   A CD1 
2066  C  CD2 . TYR   A 286 ? 1.3437 1.2217 1.1275 -0.0037 -0.0158 0.0238  355  TYR   A CD2 
2067  C  CE1 . TYR   A 286 ? 1.2793 1.1564 1.0720 -0.0054 0.0064  0.0286  355  TYR   A CE1 
2068  C  CE2 . TYR   A 286 ? 1.3830 1.2461 1.1514 -0.0010 -0.0060 0.0255  355  TYR   A CE2 
2069  C  CZ  . TYR   A 286 ? 1.3330 1.1958 1.1062 -0.0019 0.0053  0.0280  355  TYR   A CZ  
2070  O  OH  . TYR   A 286 ? 1.3585 1.2066 1.1171 0.0007  0.0158  0.0299  355  TYR   A OH  
2071  N  N   . VAL   A 287 ? 1.2824 1.2330 1.1549 -0.0186 -0.0268 0.0217  356  VAL   A N   
2072  C  CA  . VAL   A 287 ? 1.1859 1.1510 1.0746 -0.0208 -0.0332 0.0210  356  VAL   A CA  
2073  C  C   . VAL   A 287 ? 1.1379 1.0990 1.0212 -0.0190 -0.0365 0.0225  356  VAL   A C   
2074  O  O   . VAL   A 287 ? 1.2170 1.1685 1.0913 -0.0175 -0.0305 0.0245  356  VAL   A O   
2075  C  CB  . VAL   A 287 ? 1.1630 1.1417 1.0712 -0.0241 -0.0278 0.0210  356  VAL   A CB  
2076  C  CG1 . VAL   A 287 ? 1.2008 1.1944 1.1248 -0.0262 -0.0350 0.0198  356  VAL   A CG1 
2077  C  CG2 . VAL   A 287 ? 1.1729 1.1522 1.0836 -0.0251 -0.0219 0.0200  356  VAL   A CG2 
2078  N  N   . HIS   A 288 ? 1.1084 1.0765 0.9972 -0.0192 -0.0457 0.0216  357  HIS   A N   
2079  C  CA  . HIS   A 288 ? 1.1275 1.0912 1.0100 -0.0170 -0.0504 0.0227  357  HIS   A CA  
2080  C  C   . HIS   A 288 ? 1.1111 1.0899 1.0110 -0.0190 -0.0555 0.0222  357  HIS   A C   
2081  O  O   . HIS   A 288 ? 1.0911 1.0758 0.9954 -0.0191 -0.0640 0.0207  357  HIS   A O   
2082  C  CB  . HIS   A 288 ? 1.1759 1.1283 1.0418 -0.0138 -0.0580 0.0218  357  HIS   A CB  
2083  C  CG  . HIS   A 288 ? 1.2097 1.1437 1.0543 -0.0105 -0.0532 0.0230  357  HIS   A CG  
2084  N  ND1 . HIS   A 288 ? 1.1673 1.0912 1.0015 -0.0083 -0.0487 0.0252  357  HIS   A ND1 
2085  C  CD2 . HIS   A 288 ? 1.2365 1.1598 1.0676 -0.0089 -0.0520 0.0222  357  HIS   A CD2 
2086  C  CE1 . HIS   A 288 ? 1.2331 1.1407 1.0482 -0.0055 -0.0446 0.0259  357  HIS   A CE1 
2087  N  NE2 . HIS   A 288 ? 1.2578 1.1646 1.0704 -0.0057 -0.0466 0.0241  357  HIS   A NE2 
2088  N  N   . GLU   A 289 ? 1.0921 1.0768 1.0018 -0.0203 -0.0505 0.0235  358  GLU   A N   
2089  C  CA  . GLU   A 289 ? 1.0387 1.0354 0.9620 -0.0214 -0.0554 0.0234  358  GLU   A CA  
2090  C  C   . GLU   A 289 ? 1.0548 1.0456 0.9686 -0.0184 -0.0631 0.0237  358  GLU   A C   
2091  O  O   . GLU   A 289 ? 1.0751 1.0570 0.9793 -0.0163 -0.0612 0.0254  358  GLU   A O   
2092  C  CB  . GLU   A 289 ? 1.0517 1.0533 0.9847 -0.0229 -0.0488 0.0247  358  GLU   A CB  
2093  C  CG  . GLU   A 289 ? 1.0519 1.0524 0.9876 -0.0246 -0.0391 0.0250  358  GLU   A CG  
2094  C  CD  . GLU   A 289 ? 1.0569 1.0634 1.0045 -0.0264 -0.0333 0.0260  358  GLU   A CD  
2095  O  OE1 . GLU   A 289 ? 1.0777 1.0964 1.0398 -0.0280 -0.0361 0.0253  358  GLU   A OE1 
2096  O  OE2 . GLU   A 289 ? 1.0384 1.0368 0.9807 -0.0262 -0.0257 0.0275  358  GLU   A OE2 
2097  N  N   . THR   A 290 ? 1.0166 1.0117 0.9326 -0.0181 -0.0718 0.0221  359  THR   A N   
2098  C  CA  . THR   A 290 ? 1.0503 1.0395 0.9574 -0.0152 -0.0799 0.0221  359  THR   A CA  
2099  C  C   . THR   A 290 ? 1.0322 1.0340 0.9537 -0.0158 -0.0857 0.0219  359  THR   A C   
2100  O  O   . THR   A 290 ? 1.0282 1.0416 0.9628 -0.0178 -0.0895 0.0205  359  THR   A O   
2101  C  CB  . THR   A 290 ? 1.0972 1.0802 0.9949 -0.0140 -0.0860 0.0203  359  THR   A CB  
2102  O  OG1 . THR   A 290 ? 1.1729 1.1671 1.0837 -0.0170 -0.0875 0.0186  359  THR   A OG1 
2103  C  CG2 . THR   A 290 ? 1.1292 1.0974 1.0098 -0.0124 -0.0806 0.0207  359  THR   A CG2 
2104  N  N   . LEU   A 291 ? 1.0148 1.0138 0.9333 -0.0139 -0.0862 0.0233  360  LEU   A N   
2105  C  CA  . LEU   A 291 ? 1.0040 1.0137 0.9348 -0.0139 -0.0910 0.0234  360  LEU   A CA  
2106  C  C   . LEU   A 291 ? 1.0516 1.0601 0.9791 -0.0116 -0.1013 0.0222  360  LEU   A C   
2107  O  O   . LEU   A 291 ? 1.1111 1.1082 1.0245 -0.0083 -0.1045 0.0227  360  LEU   A O   
2108  C  CB  . LEU   A 291 ? 1.0112 1.0173 0.9394 -0.0126 -0.0869 0.0254  360  LEU   A CB  
2109  C  CG  . LEU   A 291 ? 1.0303 1.0436 0.9666 -0.0115 -0.0920 0.0258  360  LEU   A CG  
2110  C  CD1 . LEU   A 291 ? 1.1012 1.1306 1.0569 -0.0145 -0.0914 0.0251  360  LEU   A CD1 
2111  C  CD2 . LEU   A 291 ? 1.0074 1.0134 0.9368 -0.0097 -0.0881 0.0278  360  LEU   A CD2 
2112  N  N   . THR   A 292 ? 1.0777 1.0974 1.0180 -0.0133 -0.1065 0.0207  361  THR   A N   
2113  C  CA  . THR   A 292 ? 1.0753 1.0949 1.0147 -0.0114 -0.1165 0.0195  361  THR   A CA  
2114  C  C   . THR   A 292 ? 1.0561 1.0783 0.9987 -0.0091 -0.1205 0.0204  361  THR   A C   
2115  O  O   . THR   A 292 ? 1.1012 1.1347 1.0578 -0.0104 -0.1188 0.0210  361  THR   A O   
2116  C  CB  . THR   A 292 ? 1.1105 1.1420 1.0644 -0.0142 -0.1203 0.0177  361  THR   A CB  
2117  O  OG1 . THR   A 292 ? 1.0980 1.1431 1.0686 -0.0167 -0.1163 0.0184  361  THR   A OG1 
2118  C  CG2 . THR   A 292 ? 1.1354 1.1621 1.0835 -0.0158 -0.1181 0.0166  361  THR   A CG2 
2119  N  N   . VAL   A 293 ? 1.0947 1.1060 1.0238 -0.0054 -0.1257 0.0204  362  VAL   A N   
2120  C  CA  . VAL   A 293 ? 1.1409 1.1541 1.0724 -0.0028 -0.1306 0.0210  362  VAL   A CA  
2121  C  C   . VAL   A 293 ? 1.1799 1.1921 1.1103 -0.0006 -0.1417 0.0192  362  VAL   A C   
2122  O  O   . VAL   A 293 ? 1.1740 1.1800 1.0970 -0.0004 -0.1454 0.0176  362  VAL   A O   
2123  C  CB  . VAL   A 293 ? 1.1284 1.1291 1.0450 0.0001  -0.1268 0.0230  362  VAL   A CB  
2124  C  CG1 . VAL   A 293 ? 1.1112 1.1121 1.0290 -0.0024 -0.1159 0.0245  362  VAL   A CG1 
2125  C  CG2 . VAL   A 293 ? 1.1056 1.0892 1.0012 0.0034  -0.1299 0.0225  362  VAL   A CG2 
2126  N  N   . TYR   A 294 ? 1.2072 1.2256 1.1456 0.0012  -0.1472 0.0193  363  TYR   A N   
2127  C  CA  . TYR   A 294 ? 1.2012 1.2206 1.1418 0.0032  -0.1582 0.0175  363  TYR   A CA  
2128  C  C   . TYR   A 294 ? 1.1931 1.1959 1.1135 0.0079  -0.1634 0.0173  363  TYR   A C   
2129  O  O   . TYR   A 294 ? 1.1855 1.1823 1.0995 0.0094  -0.1712 0.0153  363  TYR   A O   
2130  C  CB  . TYR   A 294 ? 1.1672 1.2005 1.1256 0.0034  -0.1617 0.0178  363  TYR   A CB  
2131  C  CG  . TYR   A 294 ? 1.1721 1.2214 1.1509 -0.0005 -0.1616 0.0169  363  TYR   A CG  
2132  C  CD1 . TYR   A 294 ? 1.2091 1.2602 1.1915 -0.0022 -0.1664 0.0149  363  TYR   A CD1 
2133  C  CD2 . TYR   A 294 ? 1.1996 1.2615 1.1935 -0.0023 -0.1565 0.0182  363  TYR   A CD2 
2134  C  CE1 . TYR   A 294 ? 1.2249 1.2899 1.2257 -0.0058 -0.1659 0.0143  363  TYR   A CE1 
2135  C  CE2 . TYR   A 294 ? 1.2006 1.2763 1.2123 -0.0056 -0.1560 0.0176  363  TYR   A CE2 
2136  C  CZ  . TYR   A 294 ? 1.2029 1.2801 1.2180 -0.0074 -0.1606 0.0157  363  TYR   A CZ  
2137  O  OH  . TYR   A 294 ? 1.1380 1.2279 1.1700 -0.0106 -0.1598 0.0153  363  TYR   A OH  
2138  N  N   . LYS   A 295 ? 1.2194 1.2141 1.1293 0.0104  -0.1593 0.0192  364  LYS   A N   
2139  C  CA  . LYS   A 295 ? 1.1371 1.1153 1.0269 0.0152  -0.1634 0.0194  364  LYS   A CA  
2140  C  C   . LYS   A 295 ? 1.2166 1.1824 1.0907 0.0157  -0.1536 0.0216  364  LYS   A C   
2141  O  O   . LYS   A 295 ? 1.2548 1.2264 1.1361 0.0134  -0.1454 0.0234  364  LYS   A O   
2142  C  CB  . LYS   A 295 ? 1.0780 1.0597 0.9727 0.0184  -0.1698 0.0196  364  LYS   A CB  
2143  N  N   . ALA   A 296 ? 1.3026 1.2510 1.1555 0.0185  -0.1542 0.0214  365  ALA   A N   
2144  C  CA  . ALA   A 296 ? 1.3084 1.2426 1.1441 0.0198  -0.1454 0.0237  365  ALA   A CA  
2145  C  C   . ALA   A 296 ? 1.3739 1.2911 1.1892 0.0256  -0.1507 0.0240  365  ALA   A C   
2146  O  O   . ALA   A 296 ? 1.3664 1.2801 1.1773 0.0286  -0.1613 0.0220  365  ALA   A O   
2147  C  CB  . ALA   A 296 ? 1.2512 1.1784 1.0783 0.0179  -0.1385 0.0237  365  ALA   A CB  
2148  N  N   . CYS   A 297 ? 1.4607 1.3671 1.2636 0.0273  -0.1435 0.0266  366  CYS   A N   
2149  C  CA  . CYS   A 297 ? 1.4951 1.3845 1.2776 0.0330  -0.1473 0.0273  366  CYS   A CA  
2150  C  C   . CYS   A 297 ? 1.5092 1.3798 1.2698 0.0345  -0.1383 0.0293  366  CYS   A C   
2151  O  O   . CYS   A 297 ? 1.5239 1.3966 1.2881 0.0309  -0.1274 0.0309  366  CYS   A O   
2152  C  CB  . CYS   A 297 ? 1.5068 1.4004 1.2950 0.0345  -0.1482 0.0287  366  CYS   A CB  
2153  S  SG  . CYS   A 297 ? 1.6353 1.5397 1.4361 0.0370  -0.1626 0.0263  366  CYS   A SG  
2154  N  N   . ASN   A 298 ? 1.4126 1.2648 1.1506 0.0399  -0.1431 0.0292  367  ASN   A N   
2155  C  CA  . ASN   A 298 ? 1.3738 1.2054 1.0880 0.0425  -0.1351 0.0314  367  ASN   A CA  
2156  C  C   . ASN   A 298 ? 1.3502 1.1780 1.0597 0.0401  -0.1284 0.0311  367  ASN   A C   
2157  O  O   . ASN   A 298 ? 1.3479 1.1682 1.0501 0.0390  -0.1168 0.0334  367  ASN   A O   
2158  C  CB  . ASN   A 298 ? 1.3725 1.2028 1.0874 0.0417  -0.1252 0.0346  367  ASN   A CB  
2159  C  CG  . ASN   A 298 ? 1.4398 1.2732 1.1585 0.0443  -0.1314 0.0350  367  ASN   A CG  
2160  O  OD1 . ASN   A 298 ? 1.4307 1.2524 1.1347 0.0497  -0.1397 0.0344  367  ASN   A OD1 
2161  N  ND2 . ASN   A 298 ? 1.4601 1.3087 1.1982 0.0407  -0.1275 0.0359  367  ASN   A ND2 
2162  N  N   . LEU   A 299 ? 1.3736 1.2060 1.0872 0.0395  -0.1358 0.0282  368  LEU   A N   
2163  C  CA  . LEU   A 299 ? 1.3287 1.1581 1.0383 0.0374  -0.1311 0.0275  368  LEU   A CA  
2164  C  C   . LEU   A 299 ? 1.2983 1.1125 0.9885 0.0420  -0.1400 0.0253  368  LEU   A C   
2165  O  O   . LEU   A 299 ? 1.3683 1.1864 1.0624 0.0438  -0.1524 0.0228  368  LEU   A O   
2166  C  CB  . LEU   A 299 ? 1.2567 1.1075 0.9917 0.0316  -0.1313 0.0259  368  LEU   A CB  
2167  C  CG  . LEU   A 299 ? 1.2183 1.0822 0.9705 0.0267  -0.1206 0.0279  368  LEU   A CG  
2168  C  CD1 . LEU   A 299 ? 1.2524 1.1347 1.0262 0.0217  -0.1211 0.0262  368  LEU   A CD1 
2169  C  CD2 . LEU   A 299 ? 1.2111 1.0629 0.9505 0.0266  -0.1079 0.0304  368  LEU   A CD2 
2170  N  N   . ASN   A 300 ? 1.2978 1.0952 0.9678 0.0439  -0.1338 0.0261  369  ASN   A N   
2171  C  CA  . ASN   A 300 ? 1.3303 1.1117 0.9800 0.0484  -0.1414 0.0240  369  ASN   A CA  
2172  C  C   . ASN   A 300 ? 1.3308 1.1188 0.9879 0.0449  -0.1410 0.0220  369  ASN   A C   
2173  O  O   . ASN   A 300 ? 1.3223 1.1145 0.9850 0.0412  -0.1298 0.0234  369  ASN   A O   
2174  C  CB  . ASN   A 300 ? 1.4061 1.1622 1.0259 0.0535  -0.1349 0.0263  369  ASN   A CB  
2175  C  CG  . ASN   A 300 ? 1.4355 1.1789 1.0401 0.0593  -0.1406 0.0271  369  ASN   A CG  
2176  O  OD1 . ASN   A 300 ? 1.4774 1.2217 1.0823 0.0622  -0.1539 0.0247  369  ASN   A OD1 
2177  N  ND2 . ASN   A 300 ? 1.4315 1.1623 1.0224 0.0611  -0.1304 0.0306  369  ASN   A ND2 
2178  N  N   . LEU   A 301 ? 1.2908 1.0792 0.9478 0.0462  -0.1532 0.0186  370  LEU   A N   
2179  C  CA  . LEU   A 301 ? 1.2822 1.0778 0.9477 0.0428  -0.1544 0.0164  370  LEU   A CA  
2180  C  C   . LEU   A 301 ? 1.3062 1.0812 0.9464 0.0463  -0.1524 0.0159  370  LEU   A C   
2181  O  O   . LEU   A 301 ? 1.4682 1.2272 1.0889 0.0517  -0.1613 0.0143  370  LEU   A O   
2182  C  CB  . LEU   A 301 ? 1.3359 1.1437 1.0165 0.0419  -0.1685 0.0129  370  LEU   A CB  
2183  C  CG  . LEU   A 301 ? 1.2807 1.1140 0.9926 0.0357  -0.1687 0.0123  370  LEU   A CG  
2184  C  CD1 . LEU   A 301 ? 1.2562 1.0983 0.9786 0.0340  -0.1612 0.0152  370  LEU   A CD1 
2185  C  CD2 . LEU   A 301 ? 1.2442 1.0859 0.9675 0.0361  -0.1833 0.0092  370  LEU   A CD2 
2186  N  N   . ILE   A 302 ? 1.3009 1.0768 0.9422 0.0433  -0.1416 0.0169  371  ILE   A N   
2187  C  CA  . ILE   A 302 ? 1.3292 1.0853 0.9464 0.0465  -0.1366 0.0171  371  ILE   A CA  
2188  C  C   . ILE   A 302 ? 1.3611 1.1206 0.9822 0.0448  -0.1424 0.0139  371  ILE   A C   
2189  O  O   . ILE   A 302 ? 1.4023 1.1772 1.0420 0.0395  -0.1377 0.0136  371  ILE   A O   
2190  C  CB  . ILE   A 302 ? 1.3210 1.0747 0.9362 0.0446  -0.1197 0.0206  371  ILE   A CB  
2191  C  CG1 . ILE   A 302 ? 1.3289 1.0749 0.9359 0.0469  -0.1135 0.0239  371  ILE   A CG1 
2192  C  CG2 . ILE   A 302 ? 1.3390 1.0763 0.9344 0.0468  -0.1136 0.0207  371  ILE   A CG2 
2193  C  CD1 . ILE   A 302 ? 1.3713 1.0987 0.9553 0.0537  -0.1219 0.0237  371  ILE   A CD1 
2194  N  N   . GLY   A 303 ? 1.4115 1.1564 1.0146 0.0495  -0.1528 0.0114  372  GLY   A N   
2195  C  CA  . GLY   A 303 ? 1.4363 1.1815 1.0400 0.0484  -0.1582 0.0083  372  GLY   A CA  
2196  C  C   . GLY   A 303 ? 1.5235 1.2802 1.1422 0.0472  -0.1736 0.0047  372  GLY   A C   
2197  O  O   . GLY   A 303 ? 1.5181 1.2793 1.1428 0.0484  -0.1817 0.0042  372  GLY   A O   
2198  N  N   . ARG   A 304 ? 1.5576 1.3184 1.1821 0.0448  -0.1776 0.0020  373  ARG   A N   
2199  C  CA  . ARG   A 304 ? 1.5580 1.3313 1.1995 0.0428  -0.1913 -0.0014 373  ARG   A CA  
2200  C  C   . ARG   A 304 ? 1.5980 1.3949 1.2686 0.0355  -0.1870 -0.0014 373  ARG   A C   
2201  O  O   . ARG   A 304 ? 1.6007 1.3998 1.2729 0.0327  -0.1764 -0.0001 373  ARG   A O   
2202  C  CB  . ARG   A 304 ? 1.4622 1.2212 1.0880 0.0461  -0.2020 -0.0050 373  ARG   A CB  
2203  N  N   . PRO   A 305 ? 1.6774 1.4920 1.3711 0.0325  -0.1946 -0.0025 374  PRO   A N   
2204  C  CA  . PRO   A 305 ? 1.6127 1.4497 1.3340 0.0258  -0.1906 -0.0023 374  PRO   A CA  
2205  C  C   . PRO   A 305 ? 1.5734 1.4109 1.2959 0.0231  -0.1890 -0.0040 374  PRO   A C   
2206  O  O   . PRO   A 305 ? 1.5717 1.3968 1.2805 0.0257  -0.1965 -0.0066 374  PRO   A O   
2207  C  CB  . PRO   A 305 ? 1.6287 1.4793 1.3690 0.0246  -0.2026 -0.0043 374  PRO   A CB  
2208  C  CG  . PRO   A 305 ? 1.6454 1.4851 1.3722 0.0300  -0.2078 -0.0037 374  PRO   A CG  
2209  C  CD  . PRO   A 305 ? 1.6810 1.4960 1.3764 0.0354  -0.2057 -0.0035 374  PRO   A CD  
2210  N  N   . SER   A 306 ? 1.4809 1.3325 1.2197 0.0181  -0.1793 -0.0026 375  SER   A N   
2211  C  CA  . SER   A 306 ? 1.4769 1.3313 1.2197 0.0150  -0.1766 -0.0039 375  SER   A CA  
2212  C  C   . SER   A 306 ? 1.4833 1.3609 1.2549 0.0088  -0.1739 -0.0036 375  SER   A C   
2213  O  O   . SER   A 306 ? 1.4565 1.3465 1.2426 0.0071  -0.1712 -0.0018 375  SER   A O   
2214  C  CB  . SER   A 306 ? 1.4218 1.2642 1.1479 0.0163  -0.1642 -0.0020 375  SER   A CB  
2215  O  OG  . SER   A 306 ? 1.4314 1.2776 1.1627 0.0132  -0.1609 -0.0031 375  SER   A OG  
2216  N  N   . THR   A 307 ? 1.5185 1.4013 1.2979 0.0056  -0.1748 -0.0053 376  THR   A N   
2217  C  CA  . THR   A 307 ? 1.4542 1.3573 1.2589 -0.0001 -0.1712 -0.0049 376  THR   A CA  
2218  C  C   . THR   A 307 ? 1.5109 1.4151 1.3159 -0.0025 -0.1613 -0.0044 376  THR   A C   
2219  O  O   . THR   A 307 ? 1.5278 1.4478 1.3523 -0.0070 -0.1577 -0.0041 376  THR   A O   
2220  C  CB  . THR   A 307 ? 1.4090 1.3221 1.2295 -0.0025 -0.1825 -0.0076 376  THR   A CB  
2221  O  OG1 . THR   A 307 ? 1.4255 1.3285 1.2357 -0.0020 -0.1875 -0.0103 376  THR   A OG1 
2222  C  CG2 . THR   A 307 ? 1.3951 1.3083 1.2174 -0.0001 -0.1929 -0.0084 376  THR   A CG2 
2223  N  N   . GLU   A 308 ? 1.6536 1.5413 1.4374 0.0004  -0.1569 -0.0043 377  GLU   A N   
2224  C  CA  . GLU   A 308 ? 1.6863 1.5748 1.4702 -0.0016 -0.1469 -0.0037 377  GLU   A CA  
2225  C  C   . GLU   A 308 ? 1.6774 1.5783 1.4749 -0.0042 -0.1358 -0.0008 377  GLU   A C   
2226  O  O   . GLU   A 308 ? 1.6512 1.5510 1.4463 -0.0027 -0.1326 0.0012  377  GLU   A O   
2227  C  CB  . GLU   A 308 ? 1.7127 1.5803 1.4702 0.0028  -0.1429 -0.0036 377  GLU   A CB  
2228  C  CG  . GLU   A 308 ? 1.7442 1.6042 1.4907 0.0051  -0.1316 -0.0005 377  GLU   A CG  
2229  C  CD  . GLU   A 308 ? 1.7936 1.6318 1.5129 0.0099  -0.1276 -0.0003 377  GLU   A CD  
2230  O  OE1 . GLU   A 308 ? 1.8234 1.6561 1.5365 0.0099  -0.1270 -0.0018 377  GLU   A OE1 
2231  O  OE2 . GLU   A 308 ? 1.8013 1.6274 1.5051 0.0138  -0.1248 0.0015  377  GLU   A OE2 
2232  N  N   . HIS   A 309 ? 1.7256 1.6386 1.5381 -0.0083 -0.1307 -0.0009 378  HIS   A N   
2233  C  CA  . HIS   A 309 ? 1.7372 1.6627 1.5641 -0.0111 -0.1209 0.0013  378  HIS   A CA  
2234  C  C   . HIS   A 309 ? 1.6735 1.6099 1.5135 -0.0120 -0.1230 0.0027  378  HIS   A C   
2235  O  O   . HIS   A 309 ? 1.6722 1.6142 1.5183 -0.0128 -0.1150 0.0048  378  HIS   A O   
2236  C  CB  . HIS   A 309 ? 1.7701 1.6855 1.5837 -0.0091 -0.1094 0.0034  378  HIS   A CB  
2237  C  CG  . HIS   A 309 ? 1.8337 1.7600 1.6608 -0.0124 -0.0993 0.0045  378  HIS   A CG  
2238  N  ND1 . HIS   A 309 ? 1.7815 1.7164 1.6191 -0.0138 -0.0924 0.0067  378  HIS   A ND1 
2239  C  CD2 . HIS   A 309 ? 1.8474 1.7769 1.6789 -0.0144 -0.0951 0.0036  378  HIS   A CD2 
2240  C  CE1 . HIS   A 309 ? 1.7632 1.7062 1.6113 -0.0164 -0.0848 0.0070  378  HIS   A CE1 
2241  N  NE2 . HIS   A 309 ? 1.7919 1.7319 1.6365 -0.0168 -0.0862 0.0052  378  HIS   A NE2 
2242  N  N   . SER   A 310 ? 1.5023 1.4418 1.3469 -0.0117 -0.1336 0.0013  379  SER   A N   
2243  C  CA  . SER   A 310 ? 1.4097 1.3586 1.2656 -0.0120 -0.1359 0.0025  379  SER   A CA  
2244  C  C   . SER   A 310 ? 1.3801 1.3470 1.2578 -0.0162 -0.1303 0.0036  379  SER   A C   
2245  O  O   . SER   A 310 ? 1.3847 1.3611 1.2751 -0.0194 -0.1317 0.0024  379  SER   A O   
2246  C  CB  . SER   A 310 ? 1.3955 1.3458 1.2549 -0.0112 -0.1486 0.0006  379  SER   A CB  
2247  O  OG  . SER   A 310 ? 1.3388 1.2966 1.2071 -0.0107 -0.1504 0.0019  379  SER   A OG  
2248  N  N   . TRP   A 311 ? 1.3473 1.3182 1.2289 -0.0161 -0.1242 0.0059  380  TRP   A N   
2249  C  CA  . TRP   A 311 ? 1.2421 1.2287 1.1427 -0.0196 -0.1184 0.0069  380  TRP   A CA  
2250  C  C   . TRP   A 311 ? 1.2028 1.2033 1.1213 -0.0216 -0.1253 0.0063  380  TRP   A C   
2251  O  O   . TRP   A 311 ? 1.2577 1.2710 1.1921 -0.0248 -0.1228 0.0063  380  TRP   A O   
2252  C  CB  . TRP   A 311 ? 1.2172 1.2033 1.1165 -0.0187 -0.1105 0.0094  380  TRP   A CB  
2253  C  CG  . TRP   A 311 ? 1.2514 1.2273 1.1382 -0.0178 -0.1011 0.0104  380  TRP   A CG  
2254  C  CD1 . TRP   A 311 ? 1.2844 1.2588 1.1698 -0.0191 -0.0963 0.0096  380  TRP   A CD1 
2255  C  CD2 . TRP   A 311 ? 1.2673 1.2332 1.1421 -0.0153 -0.0951 0.0124  380  TRP   A CD2 
2256  N  NE1 . TRP   A 311 ? 1.2887 1.2532 1.1625 -0.0176 -0.0875 0.0110  380  TRP   A NE1 
2257  C  CE2 . TRP   A 311 ? 1.2957 1.2548 1.1629 -0.0154 -0.0865 0.0128  380  TRP   A CE2 
2258  C  CE3 . TRP   A 311 ? 1.2731 1.2350 1.1429 -0.0130 -0.0960 0.0139  380  TRP   A CE3 
2259  C  CZ2 . TRP   A 311 ? 1.3279 1.2764 1.1833 -0.0133 -0.0784 0.0148  380  TRP   A CZ2 
2260  C  CZ3 . TRP   A 311 ? 1.2544 1.2053 1.1116 -0.0110 -0.0881 0.0159  380  TRP   A CZ3 
2261  C  CH2 . TRP   A 311 ? 1.2764 1.2209 1.1269 -0.0113 -0.0793 0.0164  380  TRP   A CH2 
2262  N  N   . PHE   A 312 ? 1.2251 1.2231 1.1411 -0.0195 -0.1338 0.0057  381  PHE   A N   
2263  C  CA  . PHE   A 312 ? 1.2428 1.2533 1.1755 -0.0209 -0.1409 0.0051  381  PHE   A CA  
2264  C  C   . PHE   A 312 ? 1.2626 1.2692 1.1930 -0.0207 -0.1507 0.0026  381  PHE   A C   
2265  O  O   . PHE   A 312 ? 1.2610 1.2602 1.1832 -0.0177 -0.1585 0.0017  381  PHE   A O   
2266  C  CB  . PHE   A 312 ? 1.2178 1.2295 1.1515 -0.0186 -0.1432 0.0064  381  PHE   A CB  
2267  C  CG  . PHE   A 312 ? 1.1869 1.1977 1.1176 -0.0181 -0.1342 0.0088  381  PHE   A CG  
2268  C  CD1 . PHE   A 312 ? 1.1684 1.1907 1.1128 -0.0210 -0.1270 0.0099  381  PHE   A CD1 
2269  C  CD2 . PHE   A 312 ? 1.2175 1.2152 1.1313 -0.0146 -0.1327 0.0098  381  PHE   A CD2 
2270  C  CE1 . PHE   A 312 ? 1.1737 1.1951 1.1160 -0.0206 -0.1190 0.0118  381  PHE   A CE1 
2271  C  CE2 . PHE   A 312 ? 1.1919 1.1886 1.1036 -0.0143 -0.1241 0.0120  381  PHE   A CE2 
2272  C  CZ  . PHE   A 312 ? 1.1419 1.1508 1.0685 -0.0174 -0.1174 0.0129  381  PHE   A CZ  
2273  N  N   . PRO   A 313 ? 1.2578 1.2688 1.1951 -0.0236 -0.1509 0.0012  382  PRO   A N   
2274  C  CA  . PRO   A 313 ? 1.2561 1.2626 1.1909 -0.0236 -0.1602 -0.0013 382  PRO   A CA  
2275  C  C   . PRO   A 313 ? 1.2625 1.2738 1.2058 -0.0228 -0.1702 -0.0022 382  PRO   A C   
2276  O  O   . PRO   A 313 ? 1.2900 1.3137 1.2488 -0.0240 -0.1697 -0.0010 382  PRO   A O   
2277  C  CB  . PRO   A 313 ? 1.1838 1.1993 1.1310 -0.0277 -0.1575 -0.0020 382  PRO   A CB  
2278  C  CG  . PRO   A 313 ? 1.1953 1.2113 1.1401 -0.0284 -0.1462 -0.0003 382  PRO   A CG  
2279  C  CD  . PRO   A 313 ? 1.2617 1.2805 1.2078 -0.0268 -0.1425 0.0019  382  PRO   A CD  
2280  N  N   . GLY   A 314 ? 1.2023 1.2029 1.1348 -0.0204 -0.1793 -0.0043 383  GLY   A N   
2281  C  CA  . GLY   A 314 ? 1.2625 1.2657 1.2011 -0.0190 -0.1893 -0.0053 383  GLY   A CA  
2282  C  C   . GLY   A 314 ? 1.3914 1.3857 1.3169 -0.0145 -0.1911 -0.0044 383  GLY   A C   
2283  O  O   . GLY   A 314 ? 1.4470 1.4400 1.3735 -0.0123 -0.2007 -0.0057 383  GLY   A O   
2284  N  N   . TYR   A 315 ? 1.4308 1.4185 1.3442 -0.0129 -0.1822 -0.0023 384  TYR   A N   
2285  C  CA  . TYR   A 315 ? 1.4106 1.3867 1.3081 -0.0083 -0.1834 -0.0014 384  TYR   A CA  
2286  C  C   . TYR   A 315 ? 1.4252 1.3826 1.2981 -0.0054 -0.1805 -0.0016 384  TYR   A C   
2287  O  O   . TYR   A 315 ? 1.4236 1.3788 1.2931 -0.0072 -0.1746 -0.0018 384  TYR   A O   
2288  C  CB  . TYR   A 315 ? 1.3680 1.3512 1.2716 -0.0084 -0.1756 0.0015  384  TYR   A CB  
2289  C  CG  . TYR   A 315 ? 1.3641 1.3640 1.2895 -0.0102 -0.1786 0.0018  384  TYR   A CG  
2290  C  CD1 . TYR   A 315 ? 1.3814 1.3966 1.3259 -0.0145 -0.1741 0.0024  384  TYR   A CD1 
2291  C  CD2 . TYR   A 315 ? 1.3729 1.3729 1.2994 -0.0074 -0.1857 0.0018  384  TYR   A CD2 
2292  C  CE1 . TYR   A 315 ? 1.3930 1.4228 1.3569 -0.0160 -0.1761 0.0029  384  TYR   A CE1 
2293  C  CE2 . TYR   A 315 ? 1.3617 1.3769 1.3083 -0.0088 -0.1878 0.0022  384  TYR   A CE2 
2294  C  CZ  . TYR   A 315 ? 1.3479 1.3779 1.3130 -0.0131 -0.1828 0.0029  384  TYR   A CZ  
2295  O  OH  . TYR   A 315 ? 1.4353 1.4798 1.4198 -0.0143 -0.1844 0.0035  384  TYR   A OH  
2296  N  N   . ALA   A 316 ? 1.4124 1.3557 1.2677 -0.0006 -0.1849 -0.0017 385  ALA   A N   
2297  C  CA  . ALA   A 316 ? 1.4023 1.3258 1.2320 0.0031  -0.1833 -0.0020 385  ALA   A CA  
2298  C  C   . ALA   A 316 ? 1.4087 1.3231 1.2246 0.0063  -0.1761 0.0008  385  ALA   A C   
2299  O  O   . ALA   A 316 ? 1.4003 1.3135 1.2148 0.0089  -0.1804 0.0013  385  ALA   A O   
2300  C  CB  . ALA   A 316 ? 1.4243 1.3362 1.2425 0.0065  -0.1962 -0.0049 385  ALA   A CB  
2301  N  N   . TRP   A 317 ? 1.3591 1.2664 1.1645 0.0062  -0.1652 0.0024  386  TRP   A N   
2302  C  CA  . TRP   A 317 ? 1.3020 1.2029 1.0978 0.0081  -0.1560 0.0054  386  TRP   A CA  
2303  C  C   . TRP   A 317 ? 1.3400 1.2188 1.1083 0.0138  -0.1573 0.0056  386  TRP   A C   
2304  O  O   . TRP   A 317 ? 1.4094 1.2751 1.1620 0.0159  -0.1598 0.0041  386  TRP   A O   
2305  C  CB  . TRP   A 317 ? 1.2863 1.1912 1.0860 0.0050  -0.1431 0.0071  386  TRP   A CB  
2306  C  CG  . TRP   A 317 ? 1.3372 1.2326 1.1255 0.0051  -0.1403 0.0060  386  TRP   A CG  
2307  C  CD1 . TRP   A 317 ? 1.3774 1.2808 1.1761 0.0018  -0.1415 0.0042  386  TRP   A CD1 
2308  C  CD2 . TRP   A 317 ? 1.3582 1.2344 1.1225 0.0088  -0.1350 0.0068  386  TRP   A CD2 
2309  N  NE1 . TRP   A 317 ? 1.3888 1.2794 1.1717 0.0032  -0.1376 0.0037  386  TRP   A NE1 
2310  C  CE2 . TRP   A 317 ? 1.3858 1.2596 1.1474 0.0075  -0.1335 0.0053  386  TRP   A CE2 
2311  C  CE3 . TRP   A 317 ? 1.3101 1.1706 1.0547 0.0131  -0.1309 0.0087  386  TRP   A CE3 
2312  C  CZ2 . TRP   A 317 ? 1.4189 1.2753 1.1590 0.0106  -0.1282 0.0056  386  TRP   A CZ2 
2313  C  CZ3 . TRP   A 317 ? 1.3331 1.1762 1.0563 0.0161  -0.1254 0.0091  386  TRP   A CZ3 
2314  C  CH2 . TRP   A 317 ? 1.3839 1.2251 1.1050 0.0149  -0.1240 0.0076  386  TRP   A CH2 
2315  N  N   . THR   A 318 ? 1.3050 1.1791 1.0669 0.0164  -0.1551 0.0077  387  THR   A N   
2316  C  CA  . THR   A 318 ? 1.3326 1.1853 1.0681 0.0222  -0.1551 0.0086  387  THR   A CA  
2317  C  C   . THR   A 318 ? 1.2812 1.1316 1.0132 0.0222  -0.1428 0.0121  387  THR   A C   
2318  O  O   . THR   A 318 ? 1.2544 1.1168 1.0011 0.0204  -0.1411 0.0135  387  THR   A O   
2319  C  CB  . THR   A 318 ? 1.3495 1.1977 1.0802 0.0261  -0.1677 0.0071  387  THR   A CB  
2320  O  OG1 . THR   A 318 ? 1.4131 1.2694 1.1554 0.0246  -0.1793 0.0038  387  THR   A OG1 
2321  C  CG2 . THR   A 318 ? 1.3301 1.1541 1.0310 0.0325  -0.1696 0.0073  387  THR   A CG2 
2322  N  N   . VAL   A 319 ? 1.2718 1.1067 0.9848 0.0243  -0.1340 0.0136  388  VAL   A N   
2323  C  CA  . VAL   A 319 ? 1.2374 1.0705 0.9487 0.0238  -0.1213 0.0170  388  VAL   A CA  
2324  C  C   . VAL   A 319 ? 1.2763 1.1053 0.9828 0.0268  -0.1237 0.0186  388  VAL   A C   
2325  O  O   . VAL   A 319 ? 1.3331 1.1516 1.0265 0.0312  -0.1334 0.0174  388  VAL   A O   
2326  C  CB  . VAL   A 319 ? 1.2438 1.0594 0.9343 0.0261  -0.1119 0.0183  388  VAL   A CB  
2327  C  CG1 . VAL   A 319 ? 1.2435 1.0566 0.9324 0.0256  -0.0987 0.0218  388  VAL   A CG1 
2328  C  CG2 . VAL   A 319 ? 1.3016 1.1238 1.0000 0.0227  -0.1092 0.0168  388  VAL   A CG2 
2329  N  N   . ALA   A 320 ? 1.2478 1.0856 0.9659 0.0244  -0.1157 0.0210  389  ALA   A N   
2330  C  CA  . ALA   A 320 ? 1.2211 1.0577 0.9380 0.0265  -0.1174 0.0226  389  ALA   A CA  
2331  C  C   . ALA   A 320 ? 1.2255 1.0552 0.9359 0.0265  -0.1043 0.0261  389  ALA   A C   
2332  O  O   . ALA   A 320 ? 1.2109 1.0504 0.9345 0.0223  -0.0948 0.0272  389  ALA   A O   
2333  C  CB  . ALA   A 320 ? 1.1978 1.0555 0.9400 0.0232  -0.1230 0.0218  389  ALA   A CB  
2334  N  N   . GLN   A 321 ? 1.2460 1.0587 0.9364 0.0313  -0.1040 0.0277  390  GLN   A N   
2335  C  CA  . GLN   A 321 ? 1.2656 1.0695 0.9479 0.0318  -0.0917 0.0311  390  GLN   A CA  
2336  C  C   . GLN   A 321 ? 1.2619 1.0626 0.9409 0.0344  -0.0947 0.0326  390  GLN   A C   
2337  O  O   . GLN   A 321 ? 1.2709 1.0733 0.9502 0.0368  -0.1063 0.0309  390  GLN   A O   
2338  C  CB  . GLN   A 321 ? 1.2963 1.0781 0.9526 0.0355  -0.0854 0.0322  390  GLN   A CB  
2339  C  CG  . GLN   A 321 ? 1.3476 1.1105 0.9794 0.0421  -0.0949 0.0312  390  GLN   A CG  
2340  C  CD  . GLN   A 321 ? 1.4086 1.1475 1.0124 0.0465  -0.0872 0.0329  390  GLN   A CD  
2341  O  OE1 . GLN   A 321 ? 1.4390 1.1757 1.0413 0.0447  -0.0779 0.0336  390  GLN   A OE1 
2342  N  NE2 . GLN   A 321 ? 1.3766 1.0968 0.9578 0.0525  -0.0909 0.0338  390  GLN   A NE2 
2343  N  N   . CYS   A 322 ? 1.2604 1.0564 0.9368 0.0339  -0.0839 0.0357  391  CYS   A N   
2344  C  CA  . CYS   A 322 ? 1.2768 1.0693 0.9500 0.0361  -0.0847 0.0375  391  CYS   A CA  
2345  C  C   . CYS   A 322 ? 1.3452 1.1167 0.9920 0.0430  -0.0914 0.0375  391  CYS   A C   
2346  O  O   . CYS   A 322 ? 1.4156 1.1698 1.0413 0.0463  -0.0892 0.0377  391  CYS   A O   
2347  C  CB  . CYS   A 322 ? 1.2883 1.0785 0.9632 0.0339  -0.0705 0.0409  391  CYS   A CB  
2348  S  SG  . CYS   A 322 ? 1.2681 1.0539 0.9403 0.0357  -0.0689 0.0435  391  CYS   A SG  
2349  N  N   . LYS   A 323 ? 1.3231 1.0959 0.9706 0.0455  -0.1001 0.0371  392  LYS   A N   
2350  C  CA  . LYS   A 323 ? 1.3194 1.0719 0.9415 0.0524  -0.1065 0.0372  392  LYS   A CA  
2351  C  C   . LYS   A 323 ? 1.3593 1.0931 0.9619 0.0552  -0.0959 0.0409  392  LYS   A C   
2352  O  O   . LYS   A 323 ? 1.4316 1.1454 1.0098 0.0613  -0.0996 0.0413  392  LYS   A O   
2353  C  CB  . LYS   A 323 ? 1.3245 1.0843 0.9539 0.0545  -0.1194 0.0355  392  LYS   A CB  
2354  C  CG  . LYS   A 323 ? 1.4235 1.1803 1.0513 0.0560  -0.1164 0.0381  392  LYS   A CG  
2355  C  CD  . LYS   A 323 ? 1.4255 1.1989 1.0724 0.0553  -0.1258 0.0368  392  LYS   A CD  
2356  C  CE  . LYS   A 323 ? 1.4364 1.2024 1.0725 0.0610  -0.1403 0.0345  392  LYS   A CE  
2357  N  NZ  . LYS   A 323 ? 1.3899 1.1698 1.0426 0.0611  -0.1481 0.0337  392  LYS   A NZ  
2358  N  N   . ILE   A 324 ? 1.3615 1.1007 0.9741 0.0510  -0.0831 0.0435  393  ILE   A N   
2359  C  CA  . ILE   A 324 ? 1.4090 1.1325 1.0067 0.0529  -0.0722 0.0473  393  ILE   A CA  
2360  C  C   . ILE   A 324 ? 1.4282 1.1415 1.0165 0.0518  -0.0588 0.0492  393  ILE   A C   
2361  O  O   . ILE   A 324 ? 1.4483 1.1395 1.0114 0.0563  -0.0538 0.0512  393  ILE   A O   
2362  C  CB  . ILE   A 324 ? 1.3798 1.1161 0.9959 0.0494  -0.0680 0.0490  393  ILE   A CB  
2363  C  CG1 . ILE   A 324 ? 1.3412 1.0858 0.9647 0.0512  -0.0807 0.0474  393  ILE   A CG1 
2364  C  CG2 . ILE   A 324 ? 1.3799 1.1003 0.9821 0.0506  -0.0556 0.0530  393  ILE   A CG2 
2365  C  CD1 . ILE   A 324 ? 1.3461 1.0726 0.9486 0.0572  -0.0834 0.0491  393  ILE   A CD1 
2366  N  N   . CYS   A 325 ? 1.3723 1.1013 0.9807 0.0459  -0.0524 0.0488  394  CYS   A N   
2367  C  CA  . CYS   A 325 ? 1.3415 1.0635 0.9450 0.0442  -0.0388 0.0506  394  CYS   A CA  
2368  C  C   . CYS   A 325 ? 1.3480 1.0723 0.9515 0.0435  -0.0406 0.0482  394  CYS   A C   
2369  O  O   . CYS   A 325 ? 1.3919 1.1121 0.9931 0.0419  -0.0297 0.0495  394  CYS   A O   
2370  C  CB  . CYS   A 325 ? 1.3427 1.0794 0.9688 0.0381  -0.0282 0.0523  394  CYS   A CB  
2371  S  SG  . CYS   A 325 ? 1.3597 1.1263 1.0196 0.0316  -0.0338 0.0493  394  CYS   A SG  
2372  N  N   . ALA   A 326 ? 1.3332 1.0642 0.9398 0.0444  -0.0541 0.0449  395  ALA   A N   
2373  C  CA  . ALA   A 326 ? 1.3492 1.0818 0.9549 0.0441  -0.0577 0.0422  395  ALA   A CA  
2374  C  C   . ALA   A 326 ? 1.3604 1.1087 0.9868 0.0379  -0.0492 0.0421  395  ALA   A C   
2375  O  O   . ALA   A 326 ? 1.3974 1.1407 1.0177 0.0378  -0.0447 0.0416  395  ALA   A O   
2376  C  CB  . ALA   A 326 ? 1.3617 1.0693 0.9369 0.0498  -0.0559 0.0428  395  ALA   A CB  
2377  N  N   . SER   A 327 ? 1.3037 1.0707 0.9543 0.0330  -0.0469 0.0425  396  SER   A N   
2378  C  CA  . SER   A 327 ? 1.2882 1.0707 0.9594 0.0273  -0.0396 0.0422  396  SER   A CA  
2379  C  C   . SER   A 327 ? 1.2625 1.0645 0.9534 0.0243  -0.0498 0.0389  396  SER   A C   
2380  O  O   . SER   A 327 ? 1.2710 1.0808 0.9693 0.0246  -0.0594 0.0378  396  SER   A O   
2381  C  CB  . SER   A 327 ? 1.3009 1.0905 0.9858 0.0238  -0.0296 0.0448  396  SER   A CB  
2382  O  OG  . SER   A 327 ? 1.3109 1.0842 0.9808 0.0254  -0.0173 0.0477  396  SER   A OG  
2383  N  N   . HIS   A 328 ? 1.2368 1.0455 0.9352 0.0216  -0.0476 0.0374  397  HIS   A N   
2384  C  CA  . HIS   A 328 ? 1.2198 1.0441 0.9337 0.0191  -0.0571 0.0343  397  HIS   A CA  
2385  C  C   . HIS   A 328 ? 1.1956 1.0399 0.9340 0.0151  -0.0593 0.0341  397  HIS   A C   
2386  O  O   . HIS   A 328 ? 1.1859 1.0364 0.9352 0.0123  -0.0505 0.0359  397  HIS   A O   
2387  C  CB  . HIS   A 328 ? 1.2148 1.0425 0.9329 0.0167  -0.0520 0.0332  397  HIS   A CB  
2388  C  CG  . HIS   A 328 ? 1.1978 1.0409 0.9316 0.0139  -0.0606 0.0302  397  HIS   A CG  
2389  N  ND1 . HIS   A 328 ? 1.1765 1.0362 0.9313 0.0089  -0.0566 0.0294  397  HIS   A ND1 
2390  C  CD2 . HIS   A 328 ? 1.1997 1.0435 0.9312 0.0154  -0.0728 0.0276  397  HIS   A CD2 
2391  C  CE1 . HIS   A 328 ? 1.1663 1.0360 0.9304 0.0075  -0.0656 0.0267  397  HIS   A CE1 
2392  N  NE2 . HIS   A 328 ? 1.1797 1.0404 0.9307 0.0112  -0.0755 0.0256  397  HIS   A NE2 
2393  N  N   . ILE   A 329 ? 1.1868 1.0407 0.9336 0.0152  -0.0710 0.0319  398  ILE   A N   
2394  C  CA  . ILE   A 329 ? 1.1648 1.0373 0.9341 0.0119  -0.0740 0.0316  398  ILE   A CA  
2395  C  C   . ILE   A 329 ? 1.1468 1.0355 0.9335 0.0086  -0.0799 0.0289  398  ILE   A C   
2396  O  O   . ILE   A 329 ? 1.1263 1.0313 0.9333 0.0046  -0.0778 0.0288  398  ILE   A O   
2397  C  CB  . ILE   A 329 ? 1.1707 1.0402 0.9353 0.0152  -0.0819 0.0319  398  ILE   A CB  
2398  C  CG1 . ILE   A 329 ? 1.1870 1.0413 0.9360 0.0180  -0.0749 0.0348  398  ILE   A CG1 
2399  C  CG2 . ILE   A 329 ? 1.1534 1.0418 0.9405 0.0124  -0.0862 0.0314  398  ILE   A CG2 
2400  C  CD1 . ILE   A 329 ? 1.1750 1.0367 0.9368 0.0144  -0.0645 0.0370  398  ILE   A CD1 
2401  N  N   . GLY   A 330 ? 1.1549 1.0386 0.9334 0.0103  -0.0869 0.0268  399  GLY   A N   
2402  C  CA  . GLY   A 330 ? 1.1400 1.0373 0.9334 0.0073  -0.0924 0.0243  399  GLY   A CA  
2403  C  C   . GLY   A 330 ? 1.1645 1.0544 0.9470 0.0099  -0.1027 0.0218  399  GLY   A C   
2404  O  O   . GLY   A 330 ? 1.2052 1.0777 0.9666 0.0135  -0.1023 0.0219  399  GLY   A O   
2405  N  N   . TRP   A 331 ? 1.1902 1.0930 0.9873 0.0083  -0.1119 0.0197  400  TRP   A N   
2406  C  CA  . TRP   A 331 ? 1.1981 1.0963 0.9888 0.0102  -0.1228 0.0170  400  TRP   A CA  
2407  C  C   . TRP   A 331 ? 1.2013 1.1090 1.0034 0.0107  -0.1335 0.0159  400  TRP   A C   
2408  O  O   . TRP   A 331 ? 1.2257 1.1470 1.0445 0.0084  -0.1321 0.0168  400  TRP   A O   
2409  C  CB  . TRP   A 331 ? 1.2314 1.1367 1.0306 0.0068  -0.1227 0.0151  400  TRP   A CB  
2410  C  CG  . TRP   A 331 ? 1.2412 1.1391 1.0318 0.0061  -0.1121 0.0160  400  TRP   A CG  
2411  C  CD1 . TRP   A 331 ? 1.2585 1.1418 1.0312 0.0084  -0.1118 0.0151  400  TRP   A CD1 
2412  C  CD2 . TRP   A 331 ? 1.2275 1.1321 1.0273 0.0031  -0.1004 0.0179  400  TRP   A CD2 
2413  N  NE1 . TRP   A 331 ? 1.2596 1.1406 1.0303 0.0069  -0.1002 0.0165  400  TRP   A NE1 
2414  C  CE2 . TRP   A 331 ? 1.2688 1.1629 1.0564 0.0036  -0.0932 0.0182  400  TRP   A CE2 
2415  C  CE3 . TRP   A 331 ? 1.2233 1.1415 1.0403 0.0001  -0.0955 0.0194  400  TRP   A CE3 
2416  C  CZ2 . TRP   A 331 ? 1.2873 1.1848 1.0806 0.0012  -0.0814 0.0198  400  TRP   A CZ2 
2417  C  CZ3 . TRP   A 331 ? 1.2482 1.1692 1.0703 -0.0023 -0.0842 0.0208  400  TRP   A CZ3 
2418  C  CH2 . TRP   A 331 ? 1.2454 1.1565 1.0563 -0.0019 -0.0773 0.0210  400  TRP   A CH2 
2419  N  N   . LYS   A 332 ? 1.2052 1.1053 0.9982 0.0138  -0.1444 0.0138  401  LYS   A N   
2420  C  CA  . LYS   A 332 ? 1.2271 1.1371 1.0326 0.0141  -0.1555 0.0122  401  LYS   A CA  
2421  C  C   . LYS   A 332 ? 1.2198 1.1375 1.0357 0.0116  -0.1624 0.0094  401  LYS   A C   
2422  O  O   . LYS   A 332 ? 1.2681 1.1740 1.0703 0.0139  -0.1683 0.0075  401  LYS   A O   
2423  C  CB  . LYS   A 332 ? 1.1673 1.0636 0.9565 0.0197  -0.1638 0.0119  401  LYS   A CB  
2424  N  N   . PHE   A 333 ? 1.1961 1.1326 1.0354 0.0071  -0.1617 0.0091  402  PHE   A N   
2425  C  CA  . PHE   A 333 ? 1.2011 1.1460 1.0521 0.0042  -0.1670 0.0067  402  PHE   A CA  
2426  C  C   . PHE   A 333 ? 1.2477 1.1977 1.1072 0.0052  -0.1798 0.0046  402  PHE   A C   
2427  O  O   . PHE   A 333 ? 1.2222 1.1815 1.0934 0.0054  -0.1823 0.0053  402  PHE   A O   
2428  C  CB  . PHE   A 333 ? 1.2010 1.1629 1.0724 -0.0010 -0.1598 0.0075  402  PHE   A CB  
2429  C  CG  . PHE   A 333 ? 1.1920 1.1502 1.0575 -0.0026 -0.1482 0.0090  402  PHE   A CG  
2430  C  CD1 . PHE   A 333 ? 1.1693 1.1262 1.0322 -0.0022 -0.1392 0.0116  402  PHE   A CD1 
2431  C  CD2 . PHE   A 333 ? 1.2483 1.2045 1.1117 -0.0044 -0.1462 0.0077  402  PHE   A CD2 
2432  C  CE1 . PHE   A 333 ? 1.1804 1.1344 1.0393 -0.0037 -0.1286 0.0128  402  PHE   A CE1 
2433  C  CE2 . PHE   A 333 ? 1.2520 1.2053 1.1109 -0.0057 -0.1354 0.0090  402  PHE   A CE2 
2434  C  CZ  . PHE   A 333 ? 1.1616 1.1139 1.0187 -0.0053 -0.1266 0.0115  402  PHE   A CZ  
2435  N  N   . THR   A 334 ? 1.3036 1.2476 1.1578 0.0059  -0.1880 0.0019  403  THR   A N   
2436  C  CA  . THR   A 334 ? 1.2884 1.2340 1.1477 0.0075  -0.2012 -0.0006 403  THR   A CA  
2437  C  C   . THR   A 334 ? 1.3575 1.3160 1.2357 0.0031  -0.2055 -0.0027 403  THR   A C   
2438  O  O   . THR   A 334 ? 1.3696 1.3254 1.2446 0.0011  -0.2028 -0.0036 403  THR   A O   
2439  C  CB  . THR   A 334 ? 1.2994 1.2251 1.1352 0.0124  -0.2089 -0.0025 403  THR   A CB  
2440  O  OG1 . THR   A 334 ? 1.2519 1.1623 1.0661 0.0162  -0.2026 -0.0004 403  THR   A OG1 
2441  C  CG2 . THR   A 334 ? 1.3738 1.3005 1.2144 0.0149  -0.2229 -0.0049 403  THR   A CG2 
2442  N  N   . ALA   A 335 ? 1.3439 1.3153 1.2408 0.0021  -0.2125 -0.0035 404  ALA   A N   
2443  C  CA  . ALA   A 335 ? 1.3576 1.3410 1.2731 -0.0020 -0.2169 -0.0054 404  ALA   A CA  
2444  C  C   . ALA   A 335 ? 1.3535 1.3254 1.2580 -0.0007 -0.2258 -0.0085 404  ALA   A C   
2445  O  O   . ALA   A 335 ? 1.3919 1.3537 1.2860 0.0033  -0.2355 -0.0102 404  ALA   A O   
2446  C  CB  . ALA   A 335 ? 1.4340 1.4321 1.3708 -0.0027 -0.2231 -0.0056 404  ALA   A CB  
2447  N  N   . THR   A 336 ? 1.3706 1.3432 1.2767 -0.0040 -0.2229 -0.0094 405  THR   A N   
2448  C  CA  . THR   A 336 ? 1.4352 1.3985 1.3339 -0.0032 -0.2324 -0.0127 405  THR   A CA  
2449  C  C   . THR   A 336 ? 1.4784 1.4527 1.3970 -0.0048 -0.2435 -0.0149 405  THR   A C   
2450  O  O   . THR   A 336 ? 1.4127 1.3794 1.3254 -0.0015 -0.2549 -0.0172 405  THR   A O   
2451  C  CB  . THR   A 336 ? 1.3423 1.3034 1.2378 -0.0062 -0.2267 -0.0131 405  THR   A CB  
2452  O  OG1 . THR   A 336 ? 1.3338 1.3126 1.2523 -0.0116 -0.2221 -0.0124 405  THR   A OG1 
2453  C  CG2 . THR   A 336 ? 1.3672 1.3171 1.2435 -0.0045 -0.2159 -0.0110 405  THR   A CG2 
2454  N  N   . LYS   A 337 ? 1.4943 1.4868 1.4370 -0.0095 -0.2401 -0.0140 406  LYS   A N   
2455  C  CA  . LYS   A 337 ? 1.4935 1.4979 1.4576 -0.0118 -0.2490 -0.0159 406  LYS   A CA  
2456  C  C   . LYS   A 337 ? 1.5958 1.6058 1.5684 -0.0092 -0.2548 -0.0156 406  LYS   A C   
2457  O  O   . LYS   A 337 ? 1.5612 1.5620 1.5189 -0.0047 -0.2551 -0.0147 406  LYS   A O   
2458  C  CB  . LYS   A 337 ? 1.4279 1.4490 1.4139 -0.0174 -0.2422 -0.0147 406  LYS   A CB  
2459  N  N   . LYS   A 338 ? 1.8438 1.8689 1.8405 -0.0119 -0.2593 -0.0162 407  LYS   A N   
2460  C  CA  . LYS   A 338 ? 1.8562 1.8894 1.8645 -0.0099 -0.2635 -0.0157 407  LYS   A CA  
2461  C  C   . LYS   A 338 ? 1.8515 1.9037 1.8831 -0.0135 -0.2559 -0.0132 407  LYS   A C   
2462  O  O   . LYS   A 338 ? 1.8789 1.9377 1.9176 -0.0117 -0.2554 -0.0117 407  LYS   A O   
2463  C  CB  . LYS   A 338 ? 1.8482 1.8808 1.8639 -0.0085 -0.2781 -0.0191 407  LYS   A CB  
2464  N  N   . ASP   A 339 ? 1.7043 1.7647 1.7469 -0.0183 -0.2498 -0.0127 408  ASP   A N   
2465  C  CA  . ASP   A 339 ? 1.7232 1.8005 1.7865 -0.0216 -0.2421 -0.0103 408  ASP   A CA  
2466  C  C   . ASP   A 339 ? 1.7175 1.7949 1.7731 -0.0203 -0.2314 -0.0072 408  ASP   A C   
2467  O  O   . ASP   A 339 ? 1.6857 1.7742 1.7542 -0.0203 -0.2280 -0.0053 408  ASP   A O   
2468  C  CB  . ASP   A 339 ? 1.6719 1.7559 1.7462 -0.0268 -0.2381 -0.0106 408  ASP   A CB  
2469  N  N   . MET   A 340 ? 1.6964 1.7612 1.7309 -0.0189 -0.2263 -0.0067 409  MET   A N   
2470  C  CA  . MET   A 340 ? 1.6405 1.7053 1.6685 -0.0185 -0.2153 -0.0038 409  MET   A CA  
2471  C  C   . MET   A 340 ? 1.6454 1.7131 1.6752 -0.0154 -0.2156 -0.0022 409  MET   A C   
2472  O  O   . MET   A 340 ? 1.6387 1.7007 1.6634 -0.0118 -0.2241 -0.0034 409  MET   A O   
2473  C  CB  . MET   A 340 ? 1.5717 1.6203 1.5754 -0.0167 -0.2116 -0.0038 409  MET   A CB  
2474  C  CG  . MET   A 340 ? 1.5386 1.5776 1.5332 -0.0173 -0.2170 -0.0065 409  MET   A CG  
2475  S  SD  . MET   A 340 ? 1.4833 1.5080 1.4549 -0.0166 -0.2079 -0.0056 409  MET   A SD  
2476  C  CE  . MET   A 340 ? 1.2635 1.3015 1.2492 -0.0215 -0.1956 -0.0035 409  MET   A CE  
2477  N  N   . SER   A 341 ? 1.6314 1.7072 1.6676 -0.0164 -0.2063 0.0004  410  SER   A N   
2478  C  CA  . SER   A 341 ? 1.6376 1.7157 1.6744 -0.0135 -0.2050 0.0021  410  SER   A CA  
2479  C  C   . SER   A 341 ? 1.6323 1.7112 1.6649 -0.0144 -0.1933 0.0047  410  SER   A C   
2480  O  O   . SER   A 341 ? 1.6203 1.7095 1.6653 -0.0178 -0.1869 0.0056  410  SER   A O   
2481  C  CB  . SER   A 341 ? 1.6982 1.7913 1.7573 -0.0141 -0.2085 0.0023  410  SER   A CB  
2482  O  OG  . SER   A 341 ? 1.7674 1.8625 1.8264 -0.0113 -0.2063 0.0042  410  SER   A OG  
2483  N  N   . PRO   A 342 ? 1.5686 1.6366 1.5841 -0.0114 -0.1903 0.0058  411  PRO   A N   
2484  C  CA  . PRO   A 342 ? 1.5197 1.5750 1.5193 -0.0068 -0.1966 0.0052  411  PRO   A CA  
2485  C  C   . PRO   A 342 ? 1.5208 1.5619 1.5039 -0.0056 -0.2019 0.0030  411  PRO   A C   
2486  O  O   . PRO   A 342 ? 1.5166 1.5567 1.4989 -0.0084 -0.1997 0.0022  411  PRO   A O   
2487  C  CB  . PRO   A 342 ? 1.4226 1.4724 1.4111 -0.0051 -0.1882 0.0077  411  PRO   A CB  
2488  C  CG  . PRO   A 342 ? 1.3737 1.4249 1.3619 -0.0086 -0.1787 0.0085  411  PRO   A CG  
2489  C  CD  . PRO   A 342 ? 1.5382 1.6037 1.5465 -0.0126 -0.1793 0.0077  411  PRO   A CD  
2490  N  N   . GLN   A 343 ? 1.4935 1.5227 1.4625 -0.0012 -0.2091 0.0021  412  GLN   A N   
2491  C  CA  . GLN   A 343 ? 1.4304 1.4442 1.3812 0.0008  -0.2146 0.0000  412  GLN   A CA  
2492  C  C   . GLN   A 343 ? 1.3967 1.3936 1.3229 0.0039  -0.2091 0.0014  412  GLN   A C   
2493  O  O   . GLN   A 343 ? 1.3758 1.3619 1.2879 0.0038  -0.2068 0.0008  412  GLN   A O   
2494  C  CB  . GLN   A 343 ? 1.4826 1.4934 1.4341 0.0038  -0.2281 -0.0025 412  GLN   A CB  
2495  C  CG  . GLN   A 343 ? 1.5166 1.5429 1.4925 0.0008  -0.2343 -0.0041 412  GLN   A CG  
2496  C  CD  . GLN   A 343 ? 1.5307 1.5523 1.5052 -0.0003 -0.2425 -0.0072 412  GLN   A CD  
2497  O  OE1 . GLN   A 343 ? 1.4935 1.5040 1.4569 0.0033  -0.2525 -0.0095 412  GLN   A OE1 
2498  N  NE2 . GLN   A 343 ? 1.5729 1.6023 1.5584 -0.0051 -0.2384 -0.0074 412  GLN   A NE2 
2499  N  N   . LYS   A 344 ? 1.3340 1.3280 1.2546 0.0068  -0.2068 0.0033  413  LYS   A N   
2500  C  CA  . LYS   A 344 ? 1.2599 1.2396 1.1596 0.0092  -0.1995 0.0051  413  LYS   A CA  
2501  C  C   . LYS   A 344 ? 1.2874 1.2766 1.1964 0.0067  -0.1883 0.0079  413  LYS   A C   
2502  O  O   . LYS   A 344 ? 1.3187 1.3171 1.2390 0.0071  -0.1888 0.0090  413  LYS   A O   
2503  C  CB  . LYS   A 344 ? 1.1912 1.1575 1.0745 0.0149  -0.2058 0.0050  413  LYS   A CB  
2504  N  N   . PHE   A 345 ? 1.2360 1.2233 1.1408 0.0042  -0.1787 0.0090  414  PHE   A N   
2505  C  CA  . PHE   A 345 ? 1.2157 1.2060 1.1221 0.0030  -0.1679 0.0117  414  PHE   A CA  
2506  C  C   . PHE   A 345 ? 1.2146 1.1887 1.0998 0.0045  -0.1610 0.0128  414  PHE   A C   
2507  O  O   . PHE   A 345 ? 1.2256 1.1861 1.0944 0.0069  -0.1648 0.0115  414  PHE   A O   
2508  C  CB  . PHE   A 345 ? 1.1973 1.2041 1.1238 -0.0019 -0.1620 0.0121  414  PHE   A CB  
2509  C  CG  . PHE   A 345 ? 1.2088 1.2153 1.1350 -0.0050 -0.1582 0.0112  414  PHE   A CG  
2510  C  CD1 . PHE   A 345 ? 1.2182 1.2288 1.1512 -0.0066 -0.1649 0.0089  414  PHE   A CD1 
2511  C  CD2 . PHE   A 345 ? 1.1857 1.1890 1.1064 -0.0065 -0.1479 0.0126  414  PHE   A CD2 
2512  C  CE1 . PHE   A 345 ? 1.2190 1.2292 1.1515 -0.0094 -0.1613 0.0080  414  PHE   A CE1 
2513  C  CE2 . PHE   A 345 ? 1.1540 1.1573 1.0748 -0.0092 -0.1443 0.0117  414  PHE   A CE2 
2514  C  CZ  . PHE   A 345 ? 1.1960 1.2025 1.1222 -0.0105 -0.1510 0.0094  414  PHE   A CZ  
2515  N  N   . TRP   A 346 ? 1.2759 1.2509 1.1611 0.0033  -0.1507 0.0151  415  TRP   A N   
2516  C  CA  . TRP   A 346 ? 1.2660 1.2266 1.1330 0.0045  -0.1428 0.0164  415  TRP   A CA  
2517  C  C   . TRP   A 346 ? 1.2536 1.2214 1.1293 0.0006  -0.1318 0.0177  415  TRP   A C   
2518  O  O   . TRP   A 346 ? 1.2659 1.2466 1.1575 -0.0017 -0.1287 0.0186  415  TRP   A O   
2519  C  CB  . TRP   A 346 ? 1.3118 1.2614 1.1654 0.0084  -0.1412 0.0183  415  TRP   A CB  
2520  C  CG  . TRP   A 346 ? 1.3287 1.2708 1.1733 0.0128  -0.1516 0.0173  415  TRP   A CG  
2521  C  CD1 . TRP   A 346 ? 1.3378 1.2897 1.1949 0.0134  -0.1602 0.0163  415  TRP   A CD1 
2522  C  CD2 . TRP   A 346 ? 1.3523 1.2748 1.1730 0.0175  -0.1543 0.0173  415  TRP   A CD2 
2523  N  NE1 . TRP   A 346 ? 1.3715 1.3115 1.2145 0.0183  -0.1688 0.0155  415  TRP   A NE1 
2524  C  CE2 . TRP   A 346 ? 1.3871 1.3084 1.2069 0.0210  -0.1654 0.0160  415  TRP   A CE2 
2525  C  CE3 . TRP   A 346 ? 1.3409 1.2463 1.1406 0.0194  -0.1482 0.0182  415  TRP   A CE3 
2526  C  CZ2 . TRP   A 346 ? 1.4310 1.3343 1.2290 0.0263  -0.1713 0.0155  415  TRP   A CZ2 
2527  C  CZ3 . TRP   A 346 ? 1.3766 1.2638 1.1542 0.0247  -0.1534 0.0179  415  TRP   A CZ3 
2528  C  CH2 . TRP   A 346 ? 1.4123 1.2983 1.1887 0.0282  -0.1651 0.0165  415  TRP   A CH2 
2529  N  N   . GLY   A 347 ? 1.1269 1.0858 0.9918 0.0001  -0.1258 0.0178  416  GLY   A N   
2530  C  CA  . GLY   A 347 ? 1.1570 1.1215 1.0291 -0.0033 -0.1153 0.0189  416  GLY   A CA  
2531  C  C   . GLY   A 347 ? 1.1673 1.1198 1.0258 -0.0018 -0.1061 0.0212  416  GLY   A C   
2532  O  O   . GLY   A 347 ? 1.2299 1.1669 1.0696 0.0008  -0.1050 0.0213  416  GLY   A O   
2533  N  N   . LEU   A 348 ? 1.1432 1.1019 1.0104 -0.0033 -0.0995 0.0230  417  LEU   A N   
2534  C  CA  . LEU   A 348 ? 1.0841 1.0317 0.9398 -0.0020 -0.0910 0.0253  417  LEU   A CA  
2535  C  C   . LEU   A 348 ? 1.0685 1.0216 0.9330 -0.0055 -0.0806 0.0261  417  LEU   A C   
2536  O  O   . LEU   A 348 ? 1.0677 1.0354 0.9503 -0.0086 -0.0792 0.0259  417  LEU   A O   
2537  C  CB  . LEU   A 348 ? 1.0783 1.0268 0.9357 -0.0004 -0.0923 0.0268  417  LEU   A CB  
2538  C  CG  . LEU   A 348 ? 1.1046 1.0531 0.9601 0.0026  -0.1035 0.0258  417  LEU   A CG  
2539  C  CD1 . LEU   A 348 ? 1.1153 1.0653 0.9735 0.0039  -0.1032 0.0275  417  LEU   A CD1 
2540  C  CD2 . LEU   A 348 ? 1.1046 1.0363 0.9389 0.0066  -0.1084 0.0251  417  LEU   A CD2 
2541  N  N   . THR   A 349 ? 1.0948 1.0361 0.9465 -0.0049 -0.0733 0.0269  418  THR   A N   
2542  C  CA  . THR   A 349 ? 1.1335 1.0795 0.9934 -0.0081 -0.0635 0.0274  418  THR   A CA  
2543  C  C   . THR   A 349 ? 1.1269 1.0738 0.9917 -0.0090 -0.0559 0.0296  418  THR   A C   
2544  O  O   . THR   A 349 ? 1.1581 1.0924 1.0094 -0.0065 -0.0526 0.0315  418  THR   A O   
2545  C  CB  . THR   A 349 ? 1.1489 1.0821 0.9939 -0.0069 -0.0585 0.0274  418  THR   A CB  
2546  O  OG1 . THR   A 349 ? 1.1444 1.0818 0.9977 -0.0099 -0.0486 0.0279  418  THR   A OG1 
2547  C  CG2 . THR   A 349 ? 1.1952 1.1090 1.0174 -0.0026 -0.0570 0.0290  418  THR   A CG2 
2548  N  N   . ARG   A 350 ? 1.0500 1.0114 0.9337 -0.0124 -0.0533 0.0293  419  ARG   A N   
2549  C  CA  . ARG   A 350 ? 1.0438 1.0087 0.9357 -0.0138 -0.0472 0.0309  419  ARG   A CA  
2550  C  C   . ARG   A 350 ? 1.0689 1.0196 0.9480 -0.0126 -0.0382 0.0332  419  ARG   A C   
2551  O  O   . ARG   A 350 ? 1.0615 1.0094 0.9401 -0.0121 -0.0353 0.0349  419  ARG   A O   
2552  C  CB  . ARG   A 350 ? 1.0252 1.0043 0.9361 -0.0178 -0.0435 0.0300  419  ARG   A CB  
2553  C  CG  . ARG   A 350 ? 1.0162 1.0015 0.9382 -0.0193 -0.0398 0.0310  419  ARG   A CG  
2554  C  CD  . ARG   A 350 ? 1.0179 1.0135 0.9553 -0.0227 -0.0346 0.0301  419  ARG   A CD  
2555  N  NE  . ARG   A 350 ? 1.0367 1.0253 0.9697 -0.0235 -0.0258 0.0307  419  ARG   A NE  
2556  C  CZ  . ARG   A 350 ? 1.1206 1.1004 1.0483 -0.0232 -0.0181 0.0326  419  ARG   A CZ  
2557  N  NH1 . ARG   A 350 ? 1.1445 1.1192 1.0677 -0.0219 -0.0184 0.0342  419  ARG   A NH1 
2558  N  NH2 . ARG   A 350 ? 1.1402 1.1162 1.0675 -0.0244 -0.0098 0.0329  419  ARG   A NH2 
2559  N  N   . SER   A 351 ? 1.0848 1.0268 0.9540 -0.0122 -0.0334 0.0332  420  SER   A N   
2560  C  CA  . SER   A 351 ? 1.0833 1.0122 0.9416 -0.0113 -0.0234 0.0354  420  SER   A CA  
2561  C  C   . SER   A 351 ? 1.1377 1.0524 0.9789 -0.0076 -0.0247 0.0373  420  SER   A C   
2562  O  O   . SER   A 351 ? 1.1905 1.0962 1.0256 -0.0071 -0.0166 0.0395  420  SER   A O   
2563  C  CB  . SER   A 351 ? 1.1373 1.0581 0.9856 -0.0107 -0.0192 0.0350  420  SER   A CB  
2564  O  OG  . SER   A 351 ? 1.1870 1.1203 1.0489 -0.0134 -0.0207 0.0328  420  SER   A OG  
2565  N  N   . ALA   A 352 ? 1.1648 1.0770 0.9980 -0.0048 -0.0347 0.0363  421  ALA   A N   
2566  C  CA  . ALA   A 352 ? 1.1855 1.0826 0.9999 -0.0005 -0.0370 0.0378  421  ALA   A CA  
2567  C  C   . ALA   A 352 ? 1.2013 1.1029 1.0218 -0.0002 -0.0403 0.0387  421  ALA   A C   
2568  O  O   . ALA   A 352 ? 1.2758 1.1645 1.0820 0.0030  -0.0395 0.0405  421  ALA   A O   
2569  C  CB  . ALA   A 352 ? 1.1783 1.0685 0.9793 0.0028  -0.0466 0.0361  421  ALA   A CB  
2570  N  N   . LEU   A 353 ? 1.1940 1.1129 1.0346 -0.0031 -0.0437 0.0375  422  LEU   A N   
2571  C  CA  . LEU   A 353 ? 1.1697 1.0936 1.0162 -0.0024 -0.0484 0.0380  422  LEU   A CA  
2572  C  C   . LEU   A 353 ? 1.1679 1.0927 1.0212 -0.0043 -0.0400 0.0400  422  LEU   A C   
2573  O  O   . LEU   A 353 ? 1.1758 1.1005 1.0335 -0.0068 -0.0310 0.0406  422  LEU   A O   
2574  C  CB  . LEU   A 353 ? 1.0868 1.0281 0.9507 -0.0041 -0.0565 0.0358  422  LEU   A CB  
2575  C  CG  . LEU   A 353 ? 1.0776 1.0186 0.9365 -0.0028 -0.0644 0.0338  422  LEU   A CG  
2576  C  CD1 . LEU   A 353 ? 1.0578 1.0164 0.9356 -0.0057 -0.0694 0.0316  422  LEU   A CD1 
2577  C  CD2 . LEU   A 353 ? 1.1193 1.0501 0.9634 0.0017  -0.0726 0.0338  422  LEU   A CD2 
2578  N  N   . LEU   A 354 ? 1.1843 1.1094 1.0383 -0.0029 -0.0433 0.0408  423  LEU   A N   
2579  C  CA  . LEU   A 354 ? 1.1988 1.1252 1.0600 -0.0045 -0.0369 0.0425  423  LEU   A CA  
2580  C  C   . LEU   A 354 ? 1.1789 1.1134 1.0483 -0.0037 -0.0437 0.0423  423  LEU   A C   
2581  O  O   . LEU   A 354 ? 1.1457 1.0725 1.0036 0.0000  -0.0491 0.0429  423  LEU   A O   
2582  C  CB  . LEU   A 354 ? 1.1721 1.0805 1.0161 -0.0026 -0.0294 0.0451  423  LEU   A CB  
2583  C  CG  . LEU   A 354 ? 1.1060 1.0125 0.9539 -0.0036 -0.0237 0.0471  423  LEU   A CG  
2584  C  CD1 . LEU   A 354 ? 1.1975 1.0935 1.0397 -0.0048 -0.0119 0.0491  423  LEU   A CD1 
2585  C  CD2 . LEU   A 354 ? 1.1184 1.0155 0.9532 0.0006  -0.0290 0.0482  423  LEU   A CD2 
2586  N  N   . PRO   A 355 ? 1.1701 1.1195 1.0587 -0.0069 -0.0434 0.0414  424  PRO   A N   
2587  C  CA  . PRO   A 355 ? 1.1394 1.0971 1.0367 -0.0061 -0.0493 0.0411  424  PRO   A CA  
2588  C  C   . PRO   A 355 ? 1.1463 1.0943 1.0357 -0.0042 -0.0469 0.0433  424  PRO   A C   
2589  O  O   . PRO   A 355 ? 1.1729 1.1129 1.0586 -0.0053 -0.0385 0.0449  424  PRO   A O   
2590  C  CB  . PRO   A 355 ? 1.1174 1.0906 1.0352 -0.0100 -0.0471 0.0399  424  PRO   A CB  
2591  C  CG  . PRO   A 355 ? 1.1405 1.1163 1.0611 -0.0124 -0.0438 0.0388  424  PRO   A CG  
2592  C  CD  . PRO   A 355 ? 1.2069 1.1667 1.1101 -0.0110 -0.0385 0.0402  424  PRO   A CD  
2593  N  N   . THR   A 356 ? 1.0603 1.0095 0.9483 -0.0014 -0.0542 0.0433  425  THR   A N   
2594  C  CA  . THR   A 356 ? 1.0717 1.0108 0.9504 0.0011  -0.0531 0.0453  425  THR   A CA  
2595  C  C   . THR   A 356 ? 1.0926 1.0414 0.9811 0.0023  -0.0598 0.0447  425  THR   A C   
2596  O  O   . THR   A 356 ? 1.1304 1.0898 1.0267 0.0028  -0.0671 0.0429  425  THR   A O   
2597  C  CB  . THR   A 356 ? 1.1985 1.1210 1.0554 0.0054  -0.0554 0.0463  425  THR   A CB  
2598  O  OG1 . THR   A 356 ? 1.1990 1.1255 1.0543 0.0077  -0.0651 0.0445  425  THR   A OG1 
2599  C  CG2 . THR   A 356 ? 1.2185 1.1287 1.0635 0.0047  -0.0473 0.0474  425  THR   A CG2 
2600  N  N   . ILE   A 357 ? 1.1095 1.0543 0.9974 0.0028  -0.0571 0.0462  426  ILE   A N   
2601  C  CA  . ILE   A 357 ? 1.1329 1.0856 1.0292 0.0041  -0.0623 0.0459  426  ILE   A CA  
2602  C  C   . ILE   A 357 ? 1.1369 1.0793 1.0188 0.0091  -0.0680 0.0469  426  ILE   A C   
2603  O  O   . ILE   A 357 ? 1.1674 1.0975 1.0384 0.0106  -0.0642 0.0489  426  ILE   A O   
2604  C  CB  . ILE   A 357 ? 1.1307 1.0857 1.0362 0.0016  -0.0562 0.0467  426  ILE   A CB  
2605  C  CG1 . ILE   A 357 ? 1.0695 1.0330 0.9883 -0.0031 -0.0504 0.0457  426  ILE   A CG1 
2606  C  CG2 . ILE   A 357 ? 1.1363 1.1002 1.0513 0.0029  -0.0615 0.0462  426  ILE   A CG2 
2607  C  CD1 . ILE   A 357 ? 1.1121 1.0728 1.0358 -0.0058 -0.0426 0.0467  426  ILE   A CD1 
2608  N  N   . PRO   A 358 ? 1.0734 1.0203 0.9548 0.0119  -0.0771 0.0456  427  PRO   A N   
2609  C  CA  . PRO   A 358 ? 1.1145 1.0528 0.9833 0.0171  -0.0840 0.0461  427  PRO   A CA  
2610  C  C   . PRO   A 358 ? 1.1700 1.1042 1.0366 0.0194  -0.0841 0.0476  427  PRO   A C   
2611  O  O   . PRO   A 358 ? 1.1242 1.0480 0.9774 0.0239  -0.0884 0.0484  427  PRO   A O   
2612  C  CB  . PRO   A 358 ? 1.0729 1.0241 0.9517 0.0180  -0.0932 0.0439  427  PRO   A CB  
2613  C  CG  . PRO   A 358 ? 1.0656 1.0237 0.9516 0.0143  -0.0908 0.0425  427  PRO   A CG  
2614  C  CD  . PRO   A 358 ? 1.0570 1.0168 0.9497 0.0102  -0.0812 0.0434  427  PRO   A CD  
2615  N  N   . VAL   A 369 ? 1.7678 1.7055 1.6881 -0.0040 -0.0341 0.0522  438  VAL   A N   
2616  C  CA  . VAL   A 369 ? 1.7408 1.6925 1.6717 -0.0052 -0.0379 0.0499  438  VAL   A CA  
2617  C  C   . VAL   A 369 ? 1.7005 1.6556 1.6396 -0.0096 -0.0313 0.0491  438  VAL   A C   
2618  O  O   . VAL   A 369 ? 1.7324 1.6798 1.6628 -0.0101 -0.0269 0.0500  438  VAL   A O   
2619  C  CB  . VAL   A 369 ? 1.7406 1.6913 1.6613 -0.0017 -0.0442 0.0497  438  VAL   A CB  
2620  C  CG1 . VAL   A 369 ? 1.7731 1.7280 1.6937 0.0021  -0.0525 0.0493  438  VAL   A CG1 
2621  C  CG2 . VAL   A 369 ? 1.7377 1.6716 1.6392 0.0001  -0.0408 0.0517  438  VAL   A CG2 
2622  N  N   . ILE   A 370 ? 1.5235 1.4899 1.4791 -0.0125 -0.0307 0.0475  439  ILE   A N   
2623  C  CA  . ILE   A 370 ? 1.3988 1.3699 1.3648 -0.0167 -0.0250 0.0464  439  ILE   A CA  
2624  C  C   . ILE   A 370 ? 1.3288 1.3152 1.3076 -0.0176 -0.0297 0.0439  439  ILE   A C   
2625  O  O   . ILE   A 370 ? 1.3248 1.3192 1.3098 -0.0162 -0.0356 0.0428  439  ILE   A O   
2626  C  CB  . ILE   A 370 ? 1.3651 1.3342 1.3396 -0.0196 -0.0193 0.0467  439  ILE   A CB  
2627  C  CG1 . ILE   A 370 ? 1.3586 1.3130 1.3209 -0.0182 -0.0158 0.0493  439  ILE   A CG1 
2628  C  CG2 . ILE   A 370 ? 1.3379 1.3097 1.3216 -0.0237 -0.0126 0.0459  439  ILE   A CG2 
2629  C  CD1 . ILE   A 370 ? 1.3038 1.2568 1.2749 -0.0206 -0.0121 0.0494  439  ILE   A CD1 
2630  N  N   . LEU   A 371 ? 1.2650 1.2552 1.2478 -0.0199 -0.0269 0.0429  440  LEU   A N   
2631  C  CA  . LEU   A 371 ? 1.2237 1.2278 1.2195 -0.0212 -0.0303 0.0405  440  LEU   A CA  
2632  C  C   . LEU   A 371 ? 1.2381 1.2486 1.2486 -0.0239 -0.0282 0.0392  440  LEU   A C   
2633  O  O   . LEU   A 371 ? 1.2379 1.2433 1.2512 -0.0263 -0.0219 0.0397  440  LEU   A O   
2634  C  CB  . LEU   A 371 ? 1.1922 1.1976 1.1869 -0.0227 -0.0280 0.0399  440  LEU   A CB  
2635  C  CG  . LEU   A 371 ? 1.1269 1.1293 1.1097 -0.0202 -0.0318 0.0403  440  LEU   A CG  
2636  C  CD1 . LEU   A 371 ? 1.0947 1.1065 1.0809 -0.0181 -0.0402 0.0391  440  LEU   A CD1 
2637  C  CD2 . LEU   A 371 ? 1.1924 1.1802 1.1581 -0.0177 -0.0304 0.0426  440  LEU   A CD2 
2638  N  N   . CYS   A 372 ? 1.2809 1.3022 1.3010 -0.0232 -0.0336 0.0375  441  CYS   A N   
2639  C  CA  . CYS   A 372 ? 1.2478 1.2748 1.2806 -0.0248 -0.0334 0.0360  441  CYS   A CA  
2640  C  C   . CYS   A 372 ? 1.2048 1.2422 1.2499 -0.0270 -0.0335 0.0337  441  CYS   A C   
2641  O  O   . CYS   A 372 ? 1.2121 1.2536 1.2565 -0.0272 -0.0343 0.0331  441  CYS   A O   
2642  C  CB  . CYS   A 372 ? 1.2467 1.2771 1.2804 -0.0219 -0.0394 0.0358  441  CYS   A CB  
2643  S  SG  . CYS   A 372 ? 1.4214 1.4402 1.4463 -0.0201 -0.0384 0.0379  441  CYS   A SG  
2644  N  N   . LEU   A 373 ? 1.1624 1.2041 1.2188 -0.0284 -0.0332 0.0322  442  LEU   A N   
2645  C  CA  . LEU   A 373 ? 1.2032 1.2546 1.2716 -0.0300 -0.0340 0.0297  442  LEU   A CA  
2646  C  C   . LEU   A 373 ? 1.2065 1.2631 1.2842 -0.0294 -0.0375 0.0280  442  LEU   A C   
2647  O  O   . LEU   A 373 ? 1.1545 1.2176 1.2429 -0.0308 -0.0380 0.0258  442  LEU   A O   
2648  C  CB  . LEU   A 373 ? 1.1706 1.2201 1.2439 -0.0335 -0.0275 0.0293  442  LEU   A CB  
2649  C  CG  . LEU   A 373 ? 1.1702 1.2121 1.2461 -0.0360 -0.0213 0.0300  442  LEU   A CG  
2650  C  CD1 . LEU   A 373 ? 1.2417 1.2890 1.3322 -0.0378 -0.0218 0.0276  442  LEU   A CD1 
2651  C  CD2 . LEU   A 373 ? 1.0357 1.0731 1.1093 -0.0381 -0.0147 0.0309  442  LEU   A CD2 
2652  O  OXT . LEU   A 373 ? 1.1898 1.2440 1.2640 -0.0271 -0.0404 0.0288  442  LEU   A OXT 
2653  N  N   . SER   B 2   ? 1.3638 1.3926 1.7302 -0.0901 -0.0197 -0.0112 2    SER   B N   
2654  C  CA  . SER   B 2   ? 1.3717 1.3972 1.7351 -0.0875 -0.0302 -0.0141 2    SER   B CA  
2655  C  C   . SER   B 2   ? 1.3408 1.3741 1.7169 -0.0860 -0.0404 -0.0199 2    SER   B C   
2656  O  O   . SER   B 2   ? 1.3386 1.3805 1.7208 -0.0856 -0.0405 -0.0214 2    SER   B O   
2657  C  CB  . SER   B 2   ? 1.3639 1.3858 1.7025 -0.0824 -0.0334 -0.0116 2    SER   B CB  
2658  O  OG  . SER   B 2   ? 1.3319 1.3475 1.6663 -0.0805 -0.0408 -0.0132 2    SER   B OG  
2659  N  N   . TYR   B 3   ? 1.3990 1.4286 1.7779 -0.0848 -0.0492 -0.0231 3    TYR   B N   
2660  C  CA  . TYR   B 3   ? 1.4107 1.4455 1.7993 -0.0827 -0.0601 -0.0289 3    TYR   B CA  
2661  C  C   . TYR   B 3   ? 1.4388 1.4674 1.8140 -0.0782 -0.0693 -0.0302 3    TYR   B C   
2662  O  O   . TYR   B 3   ? 1.4186 1.4386 1.7920 -0.0795 -0.0690 -0.0292 3    TYR   B O   
2663  C  CB  . TYR   B 3   ? 1.4566 1.4931 1.8716 -0.0873 -0.0612 -0.0327 3    TYR   B CB  
2664  C  CG  . TYR   B 3   ? 1.4901 1.5303 1.9195 -0.0925 -0.0501 -0.0306 3    TYR   B CG  
2665  C  CD1 . TYR   B 3   ? 1.4822 1.5312 1.9141 -0.0922 -0.0468 -0.0304 3    TYR   B CD1 
2666  C  CD2 . TYR   B 3   ? 1.5150 1.5492 1.9553 -0.0978 -0.0426 -0.0287 3    TYR   B CD2 
2667  C  CE1 . TYR   B 3   ? 1.5126 1.5645 1.9572 -0.0966 -0.0362 -0.0284 3    TYR   B CE1 
2668  C  CE2 . TYR   B 3   ? 1.5002 1.5373 1.9535 -0.1024 -0.0317 -0.0265 3    TYR   B CE2 
2669  C  CZ  . TYR   B 3   ? 1.5015 1.5475 1.9568 -0.1017 -0.0285 -0.0265 3    TYR   B CZ  
2670  O  OH  . TYR   B 3   ? 1.4903 1.5390 1.9582 -0.1059 -0.0175 -0.0244 3    TYR   B OH  
2671  N  N   . ASN   B 4   ? 1.2821 1.3147 1.6477 -0.0730 -0.0772 -0.0323 4    ASN   B N   
2672  C  CA  . ASN   B 4   ? 1.2422 1.2690 1.5919 -0.0680 -0.0847 -0.0329 4    ASN   B CA  
2673  C  C   . ASN   B 4   ? 1.1747 1.2038 1.5286 -0.0643 -0.0965 -0.0385 4    ASN   B C   
2674  O  O   . ASN   B 4   ? 1.1517 1.1882 1.5172 -0.0646 -0.0990 -0.0416 4    ASN   B O   
2675  C  CB  . ASN   B 4   ? 1.1916 1.2186 1.5189 -0.0643 -0.0813 -0.0285 4    ASN   B CB  
2676  C  CG  . ASN   B 4   ? 1.3120 1.3342 1.6328 -0.0673 -0.0707 -0.0230 4    ASN   B CG  
2677  O  OD1 . ASN   B 4   ? 1.2830 1.2964 1.5978 -0.0677 -0.0699 -0.0213 4    ASN   B OD1 
2678  N  ND2 . ASN   B 4   ? 1.3133 1.3406 1.6349 -0.0694 -0.0626 -0.0203 4    ASN   B ND2 
2679  N  N   . TYR   B 5   ? 1.1692 1.1913 1.5135 -0.0608 -0.1036 -0.0398 5    TYR   B N   
2680  C  CA  . TYR   B 5   ? 1.1287 1.1500 1.4736 -0.0565 -0.1153 -0.0450 5    TYR   B CA  
2681  C  C   . TYR   B 5   ? 1.1460 1.1649 1.4677 -0.0500 -0.1186 -0.0433 5    TYR   B C   
2682  O  O   . TYR   B 5   ? 1.1546 1.1668 1.4635 -0.0490 -0.1163 -0.0402 5    TYR   B O   
2683  C  CB  . TYR   B 5   ? 1.1405 1.1542 1.4967 -0.0585 -0.1208 -0.0483 5    TYR   B CB  
2684  C  CG  . TYR   B 5   ? 1.1385 1.1492 1.4971 -0.0545 -0.1336 -0.0543 5    TYR   B CG  
2685  C  CD1 . TYR   B 5   ? 1.1170 1.1195 1.4594 -0.0494 -0.1401 -0.0548 5    TYR   B CD1 
2686  C  CD2 . TYR   B 5   ? 1.1459 1.1610 1.5233 -0.0559 -0.1394 -0.0595 5    TYR   B CD2 
2687  C  CE1 . TYR   B 5   ? 1.1254 1.1238 1.4688 -0.0455 -0.1519 -0.0603 5    TYR   B CE1 
2688  C  CE2 . TYR   B 5   ? 1.1776 1.1887 1.5564 -0.0520 -0.1517 -0.0651 5    TYR   B CE2 
2689  C  CZ  . TYR   B 5   ? 1.1490 1.1514 1.5102 -0.0467 -0.1579 -0.0654 5    TYR   B CZ  
2690  O  OH  . TYR   B 5   ? 1.0802 1.0774 1.4410 -0.0424 -0.1700 -0.0709 5    TYR   B OH  
2691  N  N   . VAL   B 6   ? 1.1251 1.1494 1.4412 -0.0457 -0.1231 -0.0451 6    VAL   B N   
2692  C  CA  . VAL   B 6   ? 1.0609 1.0836 1.3562 -0.0393 -0.1262 -0.0438 6    VAL   B CA  
2693  C  C   . VAL   B 6   ? 1.0731 1.0919 1.3672 -0.0345 -0.1376 -0.0489 6    VAL   B C   
2694  O  O   . VAL   B 6   ? 1.0932 1.1155 1.3988 -0.0345 -0.1428 -0.0532 6    VAL   B O   
2695  C  CB  . VAL   B 6   ? 1.0637 1.0950 1.3519 -0.0377 -0.1220 -0.0414 6    VAL   B CB  
2696  C  CG1 . VAL   B 6   ? 1.0831 1.1160 1.3664 -0.0409 -0.1115 -0.0359 6    VAL   B CG1 
2697  C  CG2 . VAL   B 6   ? 1.0562 1.0953 1.3594 -0.0395 -0.1234 -0.0447 6    VAL   B CG2 
2698  N  N   . VAL   B 7   ? 1.1010 1.1120 1.3810 -0.0302 -0.1416 -0.0485 7    VAL   B N   
2699  C  CA  . VAL   B 7   ? 1.1059 1.1118 1.3818 -0.0249 -0.1524 -0.0532 7    VAL   B CA  
2700  C  C   . VAL   B 7   ? 1.0646 1.0672 1.3186 -0.0183 -0.1537 -0.0510 7    VAL   B C   
2701  O  O   . VAL   B 7   ? 1.0616 1.0625 1.3046 -0.0181 -0.1480 -0.0465 7    VAL   B O   
2702  C  CB  . VAL   B 7   ? 1.1270 1.1242 1.4120 -0.0265 -0.1584 -0.0567 7    VAL   B CB  
2703  C  CG1 . VAL   B 7   ? 1.2227 1.2109 1.4938 -0.0246 -0.1576 -0.0540 7    VAL   B CG1 
2704  C  CG2 . VAL   B 7   ? 1.1394 1.1339 1.4275 -0.0223 -0.1700 -0.0628 7    VAL   B CG2 
2705  N  N   . THR   B 8   ? 1.0302 1.0318 1.2779 -0.0127 -0.1612 -0.0542 8    THR   B N   
2706  C  CA  . THR   B 8   ? 1.0398 1.0386 1.2674 -0.0060 -0.1625 -0.0525 8    THR   B CA  
2707  C  C   . THR   B 8   ? 1.0414 1.0291 1.2609 -0.0028 -0.1677 -0.0536 8    THR   B C   
2708  O  O   . THR   B 8   ? 1.1777 1.1593 1.4039 -0.0024 -0.1755 -0.0582 8    THR   B O   
2709  C  CB  . THR   B 8   ? 1.0528 1.0543 1.2762 -0.0011 -0.1678 -0.0553 8    THR   B CB  
2710  O  OG1 . THR   B 8   ? 1.0438 1.0557 1.2752 -0.0043 -0.1626 -0.0541 8    THR   B OG1 
2711  C  CG2 . THR   B 8   ? 1.0674 1.0660 1.2702 0.0059  -0.1683 -0.0531 8    THR   B CG2 
2712  N  N   . ALA   B 9   ? 1.0132 0.9981 1.2187 -0.0007 -0.1636 -0.0494 9    ALA   B N   
2713  C  CA  . ALA   B 9   ? 0.9873 0.9615 1.1830 0.0027  -0.1676 -0.0498 9    ALA   B CA  
2714  C  C   . ALA   B 9   ? 0.9809 0.9517 1.1584 0.0109  -0.1713 -0.0498 9    ALA   B C   
2715  O  O   . ALA   B 9   ? 1.0356 0.9969 1.2038 0.0149  -0.1759 -0.0509 9    ALA   B O   
2716  C  CB  . ALA   B 9   ? 1.0341 1.0064 1.2269 -0.0005 -0.1604 -0.0452 9    ALA   B CB  
2717  N  N   . GLN   B 10  ? 0.9967 0.9747 1.1689 0.0133  -0.1691 -0.0485 10   GLN   B N   
2718  C  CA  . GLN   B 10  ? 0.9929 0.9681 1.1489 0.0211  -0.1722 -0.0486 10   GLN   B CA  
2719  C  C   . GLN   B 10  ? 1.0265 1.0107 1.1838 0.0217  -0.1704 -0.0485 10   GLN   B C   
2720  O  O   . GLN   B 10  ? 1.0489 1.0418 1.2081 0.0185  -0.1630 -0.0448 10   GLN   B O   
2721  C  CB  . GLN   B 10  ? 0.9781 0.9515 1.1195 0.0242  -0.1674 -0.0440 10   GLN   B CB  
2722  C  CG  . GLN   B 10  ? 0.9787 0.9522 1.1050 0.0315  -0.1681 -0.0431 10   GLN   B CG  
2723  C  CD  . GLN   B 10  ? 1.0662 1.0323 1.1881 0.0370  -0.1769 -0.0479 10   GLN   B CD  
2724  O  OE1 . GLN   B 10  ? 1.1387 1.0952 1.2596 0.0385  -0.1830 -0.0509 10   GLN   B OE1 
2725  N  NE2 . GLN   B 10  ? 1.1005 1.0705 1.2195 0.0400  -0.1779 -0.0489 10   GLN   B NE2 
2726  N  N   . LYS   B 11  ? 1.0699 1.0516 1.2258 0.0258  -0.1774 -0.0527 11   LYS   B N   
2727  C  CA  . LYS   B 11  ? 1.0755 1.0644 1.2311 0.0272  -0.1764 -0.0529 11   LYS   B CA  
2728  C  C   . LYS   B 11  ? 1.0742 1.0676 1.2168 0.0301  -0.1697 -0.0479 11   LYS   B C   
2729  O  O   . LYS   B 11  ? 1.0942 1.0833 1.2259 0.0328  -0.1679 -0.0453 11   LYS   B O   
2730  C  CB  . LYS   B 11  ? 1.0836 1.0662 1.2353 0.0328  -0.1855 -0.0579 11   LYS   B CB  
2731  N  N   . PRO   B 12  ? 1.0154 1.0173 1.1589 0.0295  -0.1659 -0.0464 12   PRO   B N   
2732  C  CA  . PRO   B 12  ? 1.0151 1.0210 1.1465 0.0325  -0.1602 -0.0420 12   PRO   B CA  
2733  C  C   . PRO   B 12  ? 1.0450 1.0428 1.1604 0.0406  -0.1640 -0.0426 12   PRO   B C   
2734  O  O   . PRO   B 12  ? 1.1062 1.0973 1.2190 0.0446  -0.1711 -0.0467 12   PRO   B O   
2735  C  CB  . PRO   B 12  ? 1.0311 1.0459 1.1674 0.0309  -0.1576 -0.0418 12   PRO   B CB  
2736  C  CG  . PRO   B 12  ? 1.0102 1.0278 1.1633 0.0251  -0.1595 -0.0449 12   PRO   B CG  
2737  C  CD  . PRO   B 12  ? 1.0444 1.0528 1.2006 0.0260  -0.1666 -0.0488 12   PRO   B CD  
2738  N  N   . THR   B 13  ? 1.0066 1.0047 1.1112 0.0433  -0.1593 -0.0385 13   THR   B N   
2739  C  CA  . THR   B 13  ? 0.9906 0.9812 1.0797 0.0511  -0.1616 -0.0383 13   THR   B CA  
2740  C  C   . THR   B 13  ? 1.0435 1.0389 1.1237 0.0551  -0.1575 -0.0356 13   THR   B C   
2741  O  O   . THR   B 13  ? 1.0769 1.0661 1.1441 0.0620  -0.1589 -0.0355 13   THR   B O   
2742  C  CB  . THR   B 13  ? 0.9909 0.9771 1.0739 0.0521  -0.1597 -0.0357 13   THR   B CB  
2743  O  OG1 . THR   B 13  ? 1.0040 0.9983 1.0853 0.0505  -0.1519 -0.0307 13   THR   B OG1 
2744  C  CG2 . THR   B 13  ? 1.0113 0.9946 1.1049 0.0466  -0.1617 -0.0374 13   THR   B CG2 
2745  N  N   . ALA   B 14  ? 1.0262 1.0319 1.1129 0.0510  -0.1522 -0.0334 14   ALA   B N   
2746  C  CA  . ALA   B 14  ? 0.9961 1.0071 1.0757 0.0539  -0.1476 -0.0305 14   ALA   B CA  
2747  C  C   . ALA   B 14  ? 1.0103 1.0203 1.0887 0.0566  -0.1511 -0.0335 14   ALA   B C   
2748  O  O   . ALA   B 14  ? 1.0352 1.0457 1.1231 0.0535  -0.1549 -0.0369 14   ALA   B O   
2749  C  CB  . ALA   B 14  ? 0.9721 0.9941 1.0587 0.0483  -0.1405 -0.0267 14   ALA   B CB  
2750  N  N   . VAL   B 15  ? 1.0251 1.0334 1.0920 0.0626  -0.1497 -0.0322 15   VAL   B N   
2751  C  CA  . VAL   B 15  ? 0.9925 0.9996 1.0562 0.0657  -0.1521 -0.0344 15   VAL   B CA  
2752  C  C   . VAL   B 15  ? 1.0112 1.0292 1.0793 0.0624  -0.1458 -0.0314 15   VAL   B C   
2753  O  O   . VAL   B 15  ? 1.0200 1.0435 1.0857 0.0619  -0.1395 -0.0271 15   VAL   B O   
2754  C  CB  . VAL   B 15  ? 1.0174 1.0151 1.0649 0.0745  -0.1539 -0.0346 15   VAL   B CB  
2755  C  CG1 . VAL   B 15  ? 1.0490 1.0433 1.0921 0.0782  -0.1572 -0.0374 15   VAL   B CG1 
2756  C  CG2 . VAL   B 15  ? 1.0397 1.0265 1.0817 0.0777  -0.1593 -0.0368 15   VAL   B CG2 
2757  N  N   . ASN   B 16  ? 1.0264 1.0477 1.1016 0.0600  -0.1476 -0.0338 16   ASN   B N   
2758  C  CA  . ASN   B 16  ? 1.0099 1.0408 1.0890 0.0571  -0.1421 -0.0314 16   ASN   B CA  
2759  C  C   . ASN   B 16  ? 1.0609 1.0894 1.1354 0.0609  -0.1445 -0.0335 16   ASN   B C   
2760  O  O   . ASN   B 16  ? 1.1578 1.1930 1.2384 0.0578  -0.1425 -0.0334 16   ASN   B O   
2761  C  CB  . ASN   B 16  ? 1.0519 1.0913 1.1458 0.0490  -0.1399 -0.0311 16   ASN   B CB  
2762  C  CG  . ASN   B 16  ? 1.0660 1.1045 1.1700 0.0464  -0.1454 -0.0358 16   ASN   B CG  
2763  O  OD1 . ASN   B 16  ? 1.0835 1.1151 1.1892 0.0475  -0.1514 -0.0392 16   ASN   B OD1 
2764  N  ND2 . ASN   B 16  ? 1.1036 1.1495 1.2154 0.0427  -0.1432 -0.0358 16   ASN   B ND2 
2765  N  N   . GLY   B 17  ? 1.0843 1.1027 1.1471 0.0679  -0.1488 -0.0355 17   GLY   B N   
2766  C  CA  . GLY   B 17  ? 1.1259 1.1406 1.1811 0.0727  -0.1504 -0.0369 17   GLY   B CA  
2767  C  C   . GLY   B 17  ? 1.1213 1.1229 1.1655 0.0799  -0.1575 -0.0405 17   GLY   B C   
2768  O  O   . GLY   B 17  ? 1.1051 1.1010 1.1524 0.0797  -0.1638 -0.0440 17   GLY   B O   
2769  N  N   . CYS   B 18  ? 1.1520 1.1480 1.1830 0.0863  -0.1567 -0.0400 18   CYS   B N   
2770  C  CA  . CYS   B 18  ? 1.1528 1.1350 1.1705 0.0942  -0.1628 -0.0430 18   CYS   B CA  
2771  C  C   . CYS   B 18  ? 1.1489 1.1261 1.1564 0.0996  -0.1634 -0.0438 18   CYS   B C   
2772  O  O   . CYS   B 18  ? 1.1765 1.1572 1.1785 0.1009  -0.1564 -0.0400 18   CYS   B O   
2773  C  CB  . CYS   B 18  ? 1.1669 1.1437 1.1736 0.0985  -0.1600 -0.0402 18   CYS   B CB  
2774  S  SG  . CYS   B 18  ? 1.3470 1.3317 1.3491 0.0988  -0.1485 -0.0333 18   CYS   B SG  
2775  N  N   . VAL   B 19  ? 1.1458 1.1142 1.1506 0.1029  -0.1719 -0.0490 19   VAL   B N   
2776  C  CA  . VAL   B 19  ? 1.1759 1.1379 1.1707 0.1084  -0.1740 -0.0506 19   VAL   B CA  
2777  C  C   . VAL   B 19  ? 1.2151 1.1606 1.1944 0.1171  -0.1814 -0.0541 19   VAL   B C   
2778  O  O   . VAL   B 19  ? 1.1743 1.1143 1.1564 0.1172  -0.1887 -0.0578 19   VAL   B O   
2779  C  CB  . VAL   B 19  ? 1.1365 1.1045 1.1442 0.1038  -0.1777 -0.0537 19   VAL   B CB  
2780  C  CG1 . VAL   B 19  ? 1.1448 1.1278 1.1651 0.0961  -0.1697 -0.0499 19   VAL   B CG1 
2781  C  CG2 . VAL   B 19  ? 1.1266 1.0929 1.1456 0.1009  -0.1864 -0.0588 19   VAL   B CG2 
2782  N  N   . THR   B 20  ? 1.2465 1.1836 1.2088 0.1246  -0.1792 -0.0529 20   THR   B N   
2783  C  CA  . THR   B 20  ? 1.2329 1.1530 1.1780 0.1337  -0.1861 -0.0563 20   THR   B CA  
2784  C  C   . THR   B 20  ? 1.3361 1.2508 1.2765 0.1371  -0.1908 -0.0596 20   THR   B C   
2785  O  O   . THR   B 20  ? 1.3602 1.2784 1.2972 0.1376  -0.1848 -0.0568 20   THR   B O   
2786  C  CB  . THR   B 20  ? 1.2360 1.1481 1.1628 0.1410  -0.1800 -0.0524 20   THR   B CB  
2787  O  OG1 . THR   B 20  ? 1.2572 1.1783 1.1842 0.1392  -0.1693 -0.0469 20   THR   B OG1 
2788  C  CG2 . THR   B 20  ? 1.2479 1.1583 1.1744 0.1409  -0.1799 -0.0516 20   THR   B CG2 
2789  N  N   . GLY   B 21  ? 1.4729 1.3788 1.4130 0.1396  -0.2017 -0.0655 21   GLY   B N   
2790  C  CA  . GLY   B 21  ? 1.5016 1.4003 1.4358 0.1439  -0.2077 -0.0692 21   GLY   B CA  
2791  C  C   . GLY   B 21  ? 1.4803 1.3652 1.4090 0.1491  -0.2203 -0.0756 21   GLY   B C   
2792  O  O   . GLY   B 21  ? 1.4789 1.3543 1.3986 0.1532  -0.2233 -0.0765 21   GLY   B O   
2793  N  N   . HIS   B 22  ? 1.3662 1.2504 1.3011 0.1487  -0.2279 -0.0803 22   HIS   B N   
2794  C  CA  . HIS   B 22  ? 1.3482 1.2185 1.2770 0.1545  -0.2407 -0.0869 22   HIS   B CA  
2795  C  C   . HIS   B 22  ? 1.3174 1.1957 1.2684 0.1478  -0.2486 -0.0918 22   HIS   B C   
2796  O  O   . HIS   B 22  ? 1.3249 1.2006 1.2780 0.1496  -0.2553 -0.0959 22   HIS   B O   
2797  C  CB  . HIS   B 22  ? 1.3887 1.2457 1.2969 0.1638  -0.2427 -0.0879 22   HIS   B CB  
2798  C  CG  . HIS   B 22  ? 1.3737 1.2248 1.2622 0.1695  -0.2329 -0.0823 22   HIS   B CG  
2799  N  ND1 . HIS   B 22  ? 1.4049 1.2461 1.2798 0.1746  -0.2322 -0.0812 22   HIS   B ND1 
2800  C  CD2 . HIS   B 22  ? 1.3650 1.2189 1.2458 0.1707  -0.2233 -0.0776 22   HIS   B CD2 
2801  C  CE1 . HIS   B 22  ? 1.4102 1.2484 1.2700 0.1789  -0.2224 -0.0759 22   HIS   B CE1 
2802  N  NE2 . HIS   B 22  ? 1.3767 1.2224 1.2399 0.1766  -0.2169 -0.0737 22   HIS   B NE2 
2803  N  N   . PHE   B 23  ? 1.3102 1.1982 1.2783 0.1402  -0.2474 -0.0912 23   PHE   B N   
2804  C  CA  . PHE   B 23  ? 1.2831 1.1805 1.2745 0.1328  -0.2529 -0.0950 23   PHE   B CA  
2805  C  C   . PHE   B 23  ? 1.3227 1.2086 1.3146 0.1367  -0.2669 -0.1023 23   PHE   B C   
2806  O  O   . PHE   B 23  ? 1.3221 1.2082 1.3223 0.1366  -0.2743 -0.1069 23   PHE   B O   
2807  C  CB  . PHE   B 23  ? 1.2398 1.1499 1.2474 0.1239  -0.2465 -0.0918 23   PHE   B CB  
2808  C  CG  . PHE   B 23  ? 1.1946 1.1166 1.2271 0.1153  -0.2489 -0.0942 23   PHE   B CG  
2809  C  CD1 . PHE   B 23  ? 1.2306 1.1617 1.2734 0.1119  -0.2472 -0.0945 23   PHE   B CD1 
2810  C  CD2 . PHE   B 23  ? 1.2039 1.1278 1.2498 0.1105  -0.2523 -0.0960 23   PHE   B CD2 
2811  C  CE1 . PHE   B 23  ? 1.2063 1.1485 1.2724 0.1040  -0.2488 -0.0966 23   PHE   B CE1 
2812  C  CE2 . PHE   B 23  ? 1.2306 1.1653 1.2997 0.1025  -0.2537 -0.0980 23   PHE   B CE2 
2813  C  CZ  . PHE   B 23  ? 1.2422 1.1861 1.3216 0.0993  -0.2519 -0.0983 23   PHE   B CZ  
2814  N  N   . THR   B 24  ? 1.4006 1.2756 1.3831 0.1406  -0.2711 -0.1035 24   THR   B N   
2815  C  CA  . THR   B 24  ? 1.4401 1.3052 1.4259 0.1428  -0.2843 -0.1103 24   THR   B CA  
2816  C  C   . THR   B 24  ? 1.4865 1.3360 1.4564 0.1525  -0.2944 -0.1153 24   THR   B C   
2817  O  O   . THR   B 24  ? 1.5109 1.3601 1.4914 0.1519  -0.3037 -0.1208 24   THR   B O   
2818  C  CB  . THR   B 24  ? 1.4049 1.2631 1.3844 0.1440  -0.2846 -0.1094 24   THR   B CB  
2819  O  OG1 . THR   B 24  ? 1.4807 1.3264 1.4342 0.1529  -0.2813 -0.1068 24   THR   B OG1 
2820  C  CG2 . THR   B 24  ? 1.2876 1.1606 1.2823 0.1348  -0.2748 -0.1045 24   THR   B CG2 
2821  N  N   . SER   B 25  ? 1.6060 1.4418 1.5501 0.1616  -0.2928 -0.1136 25   SER   B N   
2822  C  CA  . SER   B 25  ? 1.6535 1.4746 1.5795 0.1712  -0.2999 -0.1171 25   SER   B CA  
2823  C  C   . SER   B 25  ? 1.6571 1.4772 1.5655 0.1754  -0.2889 -0.1113 25   SER   B C   
2824  O  O   . SER   B 25  ? 1.6853 1.5119 1.5911 0.1729  -0.2773 -0.1050 25   SER   B O   
2825  C  CB  . SER   B 25  ? 1.6881 1.4890 1.5966 0.1802  -0.3106 -0.1217 25   SER   B CB  
2826  O  OG  . SER   B 25  ? 1.7300 1.5191 1.6123 0.1883  -0.3045 -0.1177 25   SER   B OG  
2827  N  N   . ALA   B 26  ? 1.6319 1.4433 1.5279 0.1819  -0.2927 -0.1133 26   ALA   B N   
2828  C  CA  . ALA   B 26  ? 1.5896 1.3999 1.4694 0.1856  -0.2818 -0.1077 26   ALA   B CA  
2829  C  C   . ALA   B 26  ? 1.6655 1.4623 1.5210 0.1935  -0.2773 -0.1045 26   ALA   B C   
2830  O  O   . ALA   B 26  ? 1.6336 1.4305 1.4768 0.1960  -0.2666 -0.0990 26   ALA   B O   
2831  C  CB  . ALA   B 26  ? 1.6092 1.4128 1.4809 0.1909  -0.2867 -0.1106 26   ALA   B CB  
2832  N  N   . GLU   B 27  ? 1.7961 1.5820 1.6455 0.1971  -0.2846 -0.1077 27   GLU   B N   
2833  C  CA  . GLU   B 27  ? 1.8424 1.6116 1.6662 0.2065  -0.2830 -0.1061 27   GLU   B CA  
2834  C  C   . GLU   B 27  ? 1.8337 1.6086 1.6597 0.2032  -0.2745 -0.1013 27   GLU   B C   
2835  O  O   . GLU   B 27  ? 1.8588 1.6218 1.6642 0.2106  -0.2707 -0.0989 27   GLU   B O   
2836  C  CB  . GLU   B 27  ? 1.8733 1.6234 1.6855 0.2144  -0.2980 -0.1133 27   GLU   B CB  
2837  C  CG  . GLU   B 27  ? 1.9463 1.6895 1.7563 0.2183  -0.3081 -0.1188 27   GLU   B CG  
2838  C  CD  . GLU   B 27  ? 2.1011 1.8257 1.9010 0.2258  -0.3239 -0.1263 27   GLU   B CD  
2839  O  OE1 . GLU   B 27  ? 2.1095 1.8298 1.9104 0.2256  -0.3280 -0.1279 27   GLU   B OE1 
2840  O  OE2 . GLU   B 27  ? 2.1824 1.8963 1.9731 0.2320  -0.3326 -0.1308 27   GLU   B OE2 
2841  N  N   . ASP   B 28  ? 1.6917 1.4838 1.5413 0.1927  -0.2714 -0.0999 28   ASP   B N   
2842  C  CA  . ASP   B 28  ? 1.6719 1.4697 1.5243 0.1894  -0.2639 -0.0956 28   ASP   B CA  
2843  C  C   . ASP   B 28  ? 1.5193 1.3372 1.3874 0.1804  -0.2514 -0.0895 28   ASP   B C   
2844  O  O   . ASP   B 28  ? 1.5157 1.3461 1.4010 0.1736  -0.2512 -0.0901 28   ASP   B O   
2845  C  CB  . ASP   B 28  ? 1.5990 1.3959 1.4637 0.1858  -0.2729 -0.0999 28   ASP   B CB  
2846  C  CG  . ASP   B 28  ? 1.5500 1.3560 1.4381 0.1784  -0.2813 -0.1048 28   ASP   B CG  
2847  O  OD1 . ASP   B 28  ? 1.5997 1.4122 1.4942 0.1765  -0.2807 -0.1052 28   ASP   B OD1 
2848  O  OD2 . ASP   B 28  ? 1.4910 1.2976 1.3916 0.1746  -0.2882 -0.1083 28   ASP   B OD2 
2849  N  N   . LEU   B 29  ? 1.4763 1.2969 1.3380 0.1807  -0.2410 -0.0837 29   LEU   B N   
2850  C  CA  . LEU   B 29  ? 1.4050 1.2439 1.2807 0.1725  -0.2294 -0.0779 29   LEU   B CA  
2851  C  C   . LEU   B 29  ? 1.4024 1.2529 1.2993 0.1633  -0.2306 -0.0784 29   LEU   B C   
2852  O  O   . LEU   B 29  ? 1.3954 1.2412 1.2895 0.1643  -0.2320 -0.0784 29   LEU   B O   
2853  C  CB  . LEU   B 29  ? 1.3606 1.1975 1.2214 0.1768  -0.2181 -0.0717 29   LEU   B CB  
2854  C  CG  . LEU   B 29  ? 1.3261 1.1802 1.1992 0.1694  -0.2061 -0.0653 29   LEU   B CG  
2855  C  CD1 . LEU   B 29  ? 1.3585 1.2263 1.2450 0.1629  -0.2020 -0.0639 29   LEU   B CD1 
2856  C  CD2 . LEU   B 29  ? 1.3685 1.2176 1.2250 0.1754  -0.1966 -0.0601 29   LEU   B CD2 
2857  N  N   . ASN   B 30  ? 1.3628 1.2279 1.2802 0.1547  -0.2300 -0.0787 30   ASN   B N   
2858  C  CA  . ASN   B 30  ? 1.3213 1.1984 1.2589 0.1455  -0.2291 -0.0783 30   ASN   B CA  
2859  C  C   . ASN   B 30  ? 1.2953 1.1858 1.2380 0.1403  -0.2164 -0.0714 30   ASN   B C   
2860  O  O   . ASN   B 30  ? 1.2883 1.1829 1.2256 0.1414  -0.2087 -0.0675 30   ASN   B O   
2861  C  CB  . ASN   B 30  ? 1.2815 1.1672 1.2393 0.1387  -0.2348 -0.0822 30   ASN   B CB  
2862  C  CG  . ASN   B 30  ? 1.2939 1.1674 1.2478 0.1438  -0.2476 -0.0890 30   ASN   B CG  
2863  O  OD1 . ASN   B 30  ? 1.3235 1.1978 1.2795 0.1444  -0.2506 -0.0913 30   ASN   B OD1 
2864  N  ND2 . ASN   B 30  ? 1.3141 1.1756 1.2618 0.1477  -0.2555 -0.0926 30   ASN   B ND2 
2865  N  N   . LEU   B 31  ? 1.2266 1.1233 1.1797 0.1349  -0.2145 -0.0700 31   LEU   B N   
2866  C  CA  . LEU   B 31  ? 1.1597 1.0715 1.1238 0.1278  -0.2044 -0.0646 31   LEU   B CA  
2867  C  C   . LEU   B 31  ? 1.1789 1.1009 1.1650 0.1185  -0.2072 -0.0666 31   LEU   B C   
2868  O  O   . LEU   B 31  ? 1.2250 1.1429 1.2164 0.1172  -0.2133 -0.0696 31   LEU   B O   
2869  C  CB  . LEU   B 31  ? 1.1460 1.0555 1.1018 0.1299  -0.1989 -0.0607 31   LEU   B CB  
2870  C  CG  . LEU   B 31  ? 1.1051 1.0289 1.0741 0.1220  -0.1907 -0.0560 31   LEU   B CG  
2871  C  CD1 . LEU   B 31  ? 1.1328 1.0689 1.1064 0.1185  -0.1818 -0.0517 31   LEU   B CD1 
2872  C  CD2 . LEU   B 31  ? 1.1202 1.0398 1.0801 0.1252  -0.1872 -0.0531 31   LEU   B CD2 
2873  N  N   . LEU   B 32  ? 1.1319 1.0666 1.1308 0.1124  -0.2029 -0.0651 32   LEU   B N   
2874  C  CA  . LEU   B 32  ? 1.0986 1.0440 1.1185 0.1033  -0.2035 -0.0662 32   LEU   B CA  
2875  C  C   . LEU   B 32  ? 1.1036 1.0607 1.1299 0.0975  -0.1935 -0.0605 32   LEU   B C   
2876  O  O   . LEU   B 32  ? 1.1021 1.0643 1.1229 0.0981  -0.1857 -0.0561 32   LEU   B O   
2877  C  CB  . LEU   B 32  ? 1.0936 1.0454 1.1246 0.1000  -0.2057 -0.0686 32   LEU   B CB  
2878  C  CG  . LEU   B 32  ? 1.1295 1.0725 1.1604 0.1037  -0.2168 -0.0751 32   LEU   B CG  
2879  C  CD1 . LEU   B 32  ? 1.1481 1.0780 1.1576 0.1136  -0.2195 -0.0760 32   LEU   B CD1 
2880  C  CD2 . LEU   B 32  ? 1.1192 1.0719 1.1654 0.0984  -0.2173 -0.0767 32   LEU   B CD2 
2881  N  N   . ILE   B 33  ? 1.1196 1.0806 1.1577 0.0918  -0.1940 -0.0606 33   ILE   B N   
2882  C  CA  . ILE   B 33  ? 1.0919 1.0627 1.1360 0.0864  -0.1855 -0.0556 33   ILE   B CA  
2883  C  C   . ILE   B 33  ? 1.0726 1.0538 1.1367 0.0773  -0.1848 -0.0563 33   ILE   B C   
2884  O  O   . ILE   B 33  ? 1.0533 1.0320 1.1271 0.0752  -0.1917 -0.0608 33   ILE   B O   
2885  C  CB  . ILE   B 33  ? 1.0651 1.0291 1.1018 0.0888  -0.1856 -0.0545 33   ILE   B CB  
2886  C  CG1 . ILE   B 33  ? 1.0420 1.0008 1.0607 0.0961  -0.1813 -0.0511 33   ILE   B CG1 
2887  C  CG2 . ILE   B 33  ? 1.0925 1.0652 1.1399 0.0819  -0.1803 -0.0513 33   ILE   B CG2 
2888  C  CD1 . ILE   B 33  ? 1.0954 1.0441 1.1044 0.1005  -0.1838 -0.0514 33   ILE   B CD1 
2889  N  N   . ALA   B 34  ? 1.0416 1.0342 1.1118 0.0722  -0.1764 -0.0519 34   ALA   B N   
2890  C  CA  . ALA   B 34  ? 1.0311 1.0340 1.1189 0.0637  -0.1740 -0.0517 34   ALA   B CA  
2891  C  C   . ALA   B 34  ? 1.0292 1.0366 1.1205 0.0594  -0.1682 -0.0478 34   ALA   B C   
2892  O  O   . ALA   B 34  ? 1.0089 1.0192 1.0926 0.0606  -0.1619 -0.0433 34   ALA   B O   
2893  C  CB  . ALA   B 34  ? 1.0372 1.0492 1.1293 0.0612  -0.1695 -0.0502 34   ALA   B CB  
2894  N  N   . LYS   B 35  ? 1.0409 1.0488 1.1441 0.0543  -0.1705 -0.0495 35   LYS   B N   
2895  C  CA  . LYS   B 35  ? 1.0135 1.0247 1.1214 0.0497  -0.1658 -0.0463 35   LYS   B CA  
2896  C  C   . LYS   B 35  ? 0.9841 1.0036 1.1095 0.0416  -0.1636 -0.0467 35   LYS   B C   
2897  O  O   . LYS   B 35  ? 0.9887 1.0057 1.1238 0.0383  -0.1671 -0.0492 35   LYS   B O   
2898  C  CB  . LYS   B 35  ? 1.0236 1.0247 1.1269 0.0523  -0.1706 -0.0480 35   LYS   B CB  
2899  C  CG  . LYS   B 35  ? 0.9960 0.9876 1.0819 0.0608  -0.1733 -0.0482 35   LYS   B CG  
2900  C  CD  . LYS   B 35  ? 1.0260 1.0087 1.1067 0.0629  -0.1765 -0.0488 35   LYS   B CD  
2901  C  CE  . LYS   B 35  ? 1.1497 1.1216 1.2134 0.0719  -0.1804 -0.0500 35   LYS   B CE  
2902  N  NZ  . LYS   B 35  ? 1.1925 1.1544 1.2478 0.0754  -0.1832 -0.0504 35   LYS   B NZ  
2903  N  N   . ASN   B 36  ? 0.9820 1.0109 1.1111 0.0384  -0.1577 -0.0441 36   ASN   B N   
2904  C  CA  . ASN   B 36  ? 0.9818 1.0190 1.1260 0.0312  -0.1544 -0.0439 36   ASN   B CA  
2905  C  C   . ASN   B 36  ? 1.0012 1.0375 1.1570 0.0298  -0.1606 -0.0491 36   ASN   B C   
2906  O  O   . ASN   B 36  ? 1.0174 1.0572 1.1754 0.0304  -0.1614 -0.0505 36   ASN   B O   
2907  C  CB  . ASN   B 36  ? 0.9949 1.0333 1.1448 0.0262  -0.1506 -0.0416 36   ASN   B CB  
2908  C  CG  . ASN   B 36  ? 0.9968 1.0443 1.1582 0.0193  -0.1443 -0.0395 36   ASN   B CG  
2909  O  OD1 . ASN   B 36  ? 1.0699 1.1240 1.2308 0.0186  -0.1405 -0.0378 36   ASN   B OD1 
2910  N  ND2 . ASN   B 36  ? 1.0012 1.0485 1.1725 0.0143  -0.1431 -0.0396 36   ASN   B ND2 
2911  N  N   . THR   B 37  ? 0.9939 1.0252 1.1573 0.0280  -0.1652 -0.0519 37   THR   B N   
2912  C  CA  . THR   B 37  ? 0.9583 0.9885 1.1347 0.0265  -0.1716 -0.0571 37   THR   B CA  
2913  C  C   . THR   B 37  ? 0.9988 1.0180 1.1695 0.0319  -0.1810 -0.0614 37   THR   B C   
2914  O  O   . THR   B 37  ? 1.0729 1.0886 1.2544 0.0297  -0.1863 -0.0650 37   THR   B O   
2915  C  CB  . THR   B 37  ? 0.9902 1.0239 1.1828 0.0192  -0.1692 -0.0571 37   THR   B CB  
2916  O  OG1 . THR   B 37  ? 1.0581 1.0861 1.2462 0.0191  -0.1687 -0.0555 37   THR   B OG1 
2917  C  CG2 . THR   B 37  ? 1.0373 1.0812 1.2361 0.0138  -0.1604 -0.0533 37   THR   B CG2 
2918  N  N   . ARG   B 38  ? 1.0524 1.0656 1.2062 0.0389  -0.1830 -0.0610 38   ARG   B N   
2919  C  CA  . ARG   B 38  ? 1.0889 1.0901 1.2335 0.0450  -0.1911 -0.0644 38   ARG   B CA  
2920  C  C   . ARG   B 38  ? 1.0520 1.0481 1.1803 0.0528  -0.1934 -0.0648 38   ARG   B C   
2921  O  O   . ARG   B 38  ? 0.9867 0.9842 1.1029 0.0555  -0.1875 -0.0606 38   ARG   B O   
2922  C  CB  . ARG   B 38  ? 1.0439 1.0401 1.1821 0.0452  -0.1892 -0.0619 38   ARG   B CB  
2923  C  CG  . ARG   B 38  ? 1.0834 1.0788 1.2358 0.0395  -0.1910 -0.0636 38   ARG   B CG  
2924  C  CD  . ARG   B 38  ? 1.1422 1.1313 1.3028 0.0405  -0.2012 -0.0700 38   ARG   B CD  
2925  N  NE  . ARG   B 38  ? 1.1656 1.1591 1.3466 0.0331  -0.2015 -0.0718 38   ARG   B NE  
2926  C  CZ  . ARG   B 38  ? 1.2148 1.2037 1.4067 0.0324  -0.2098 -0.0771 38   ARG   B CZ  
2927  N  NH1 . ARG   B 38  ? 1.1866 1.1656 1.3705 0.0387  -0.2194 -0.0815 38   ARG   B NH1 
2928  N  NH2 . ARG   B 38  ? 1.3010 1.2951 1.5125 0.0252  -0.2086 -0.0781 38   ARG   B NH2 
2929  N  N   . LEU   B 39  ? 1.0698 1.0599 1.1981 0.0565  -0.2019 -0.0699 39   LEU   B N   
2930  C  CA  . LEU   B 39  ? 1.0613 1.0445 1.1735 0.0645  -0.2050 -0.0709 39   LEU   B CA  
2931  C  C   . LEU   B 39  ? 1.1086 1.0779 1.2100 0.0706  -0.2130 -0.0741 39   LEU   B C   
2932  O  O   . LEU   B 39  ? 1.1378 1.1025 1.2480 0.0696  -0.2208 -0.0788 39   LEU   B O   
2933  C  CB  . LEU   B 39  ? 1.1074 1.0931 1.2261 0.0647  -0.2091 -0.0745 39   LEU   B CB  
2934  C  CG  . LEU   B 39  ? 1.1337 1.1109 1.2369 0.0730  -0.2138 -0.0765 39   LEU   B CG  
2935  C  CD1 . LEU   B 39  ? 1.1118 1.0900 1.1991 0.0767  -0.2060 -0.0714 39   LEU   B CD1 
2936  C  CD2 . LEU   B 39  ? 1.0749 1.0555 1.1881 0.0720  -0.2183 -0.0804 39   LEU   B CD2 
2937  N  N   . GLU   B 40  ? 1.2228 1.1856 1.3058 0.0769  -0.2107 -0.0715 40   GLU   B N   
2938  C  CA  . GLU   B 40  ? 1.2586 1.2074 1.3285 0.0836  -0.2175 -0.0741 40   GLU   B CA  
2939  C  C   . GLU   B 40  ? 1.2545 1.1944 1.3080 0.0922  -0.2213 -0.0758 40   GLU   B C   
2940  O  O   . GLU   B 40  ? 1.2421 1.1856 1.2871 0.0944  -0.2149 -0.0723 40   GLU   B O   
2941  C  CB  . GLU   B 40  ? 1.2474 1.1943 1.3081 0.0846  -0.2118 -0.0697 40   GLU   B CB  
2942  C  CG  . GLU   B 40  ? 1.2561 1.2147 1.3296 0.0764  -0.2040 -0.0657 40   GLU   B CG  
2943  C  CD  . GLU   B 40  ? 1.3075 1.2622 1.3775 0.0762  -0.2024 -0.0637 40   GLU   B CD  
2944  O  OE1 . GLU   B 40  ? 1.3354 1.2830 1.3891 0.0825  -0.2012 -0.0618 40   GLU   B OE1 
2945  O  OE2 . GLU   B 40  ? 1.3394 1.2974 1.4226 0.0698  -0.2021 -0.0639 40   GLU   B OE2 
2946  N  N   . ILE   B 41  ? 1.2308 1.1590 1.2801 0.0970  -0.2318 -0.0814 41   ILE   B N   
2947  C  CA  . ILE   B 41  ? 1.2225 1.1409 1.2566 0.1053  -0.2368 -0.0839 41   ILE   B CA  
2948  C  C   . ILE   B 41  ? 1.1821 1.0848 1.1981 0.1133  -0.2417 -0.0853 41   ILE   B C   
2949  O  O   . ILE   B 41  ? 1.1705 1.0662 1.1901 0.1132  -0.2494 -0.0891 41   ILE   B O   
2950  C  CB  . ILE   B 41  ? 1.2029 1.1207 1.2474 0.1046  -0.2457 -0.0897 41   ILE   B CB  
2951  C  CG1 . ILE   B 41  ? 1.1228 1.0565 1.1868 0.0960  -0.2403 -0.0881 41   ILE   B CG1 
2952  C  CG2 . ILE   B 41  ? 1.2357 1.1440 1.2633 0.1132  -0.2494 -0.0915 41   ILE   B CG2 
2953  C  CD1 . ILE   B 41  ? 1.1585 1.0942 1.2390 0.0931  -0.2485 -0.0938 41   ILE   B CD1 
2954  N  N   . TYR   B 42  ? 1.1517 1.0491 1.1484 0.1201  -0.2369 -0.0821 42   TYR   B N   
2955  C  CA  . TYR   B 42  ? 1.2256 1.1084 1.2028 0.1284  -0.2394 -0.0823 42   TYR   B CA  
2956  C  C   . TYR   B 42  ? 1.2899 1.1607 1.2486 0.1377  -0.2433 -0.0844 42   TYR   B C   
2957  O  O   . TYR   B 42  ? 1.2618 1.1367 1.2218 0.1377  -0.2423 -0.0845 42   TYR   B O   
2958  C  CB  . TYR   B 42  ? 1.2539 1.1405 1.2237 0.1285  -0.2288 -0.0759 42   TYR   B CB  
2959  C  CG  . TYR   B 42  ? 1.2542 1.1480 1.2376 0.1213  -0.2264 -0.0743 42   TYR   B CG  
2960  C  CD1 . TYR   B 42  ? 1.2618 1.1714 1.2628 0.1122  -0.2199 -0.0714 42   TYR   B CD1 
2961  C  CD2 . TYR   B 42  ? 1.2321 1.1163 1.2108 0.1235  -0.2310 -0.0759 42   TYR   B CD2 
2962  C  CE1 . TYR   B 42  ? 1.2475 1.1628 1.2603 0.1058  -0.2177 -0.0700 42   TYR   B CE1 
2963  C  CE2 . TYR   B 42  ? 1.1987 1.0889 1.1897 0.1168  -0.2288 -0.0745 42   TYR   B CE2 
2964  C  CZ  . TYR   B 42  ? 1.2015 1.1070 1.2092 0.1081  -0.2222 -0.0716 42   TYR   B CZ  
2965  O  OH  . TYR   B 42  ? 1.2400 1.1503 1.2588 0.1018  -0.2200 -0.0701 42   TYR   B OH  
2966  N  N   . VAL   B 43  ? 1.3493 1.2044 1.2901 0.1459  -0.2480 -0.0860 43   VAL   B N   
2967  C  CA  . VAL   B 43  ? 1.3706 1.2120 1.2892 0.1561  -0.2500 -0.0869 43   VAL   B CA  
2968  C  C   . VAL   B 43  ? 1.3689 1.2047 1.2698 0.1617  -0.2422 -0.0821 43   VAL   B C   
2969  O  O   . VAL   B 43  ? 1.3544 1.1869 1.2541 0.1616  -0.2425 -0.0816 43   VAL   B O   
2970  C  CB  . VAL   B 43  ? 1.3370 1.1624 1.2487 0.1620  -0.2641 -0.0942 43   VAL   B CB  
2971  C  CG1 . VAL   B 43  ? 1.3667 1.1758 1.2520 0.1735  -0.2655 -0.0946 43   VAL   B CG1 
2972  C  CG2 . VAL   B 43  ? 1.3238 1.1558 1.2536 0.1567  -0.2712 -0.0987 43   VAL   B CG2 
2973  N  N   . VAL   B 44  ? 1.3587 1.1938 1.2467 0.1664  -0.2348 -0.0784 44   VAL   B N   
2974  C  CA  . VAL   B 44  ? 1.4168 1.2476 1.2886 0.1719  -0.2261 -0.0733 44   VAL   B CA  
2975  C  C   . VAL   B 44  ? 1.5405 1.3502 1.3895 0.1828  -0.2328 -0.0764 44   VAL   B C   
2976  O  O   . VAL   B 44  ? 1.5957 1.3949 1.4293 0.1902  -0.2348 -0.0777 44   VAL   B O   
2977  C  CB  . VAL   B 44  ? 1.3845 1.2228 1.2525 0.1723  -0.2154 -0.0681 44   VAL   B CB  
2978  C  CG1 . VAL   B 44  ? 1.4745 1.3103 1.3293 0.1769  -0.2059 -0.0627 44   VAL   B CG1 
2979  C  CG2 . VAL   B 44  ? 1.3278 1.1855 1.2178 0.1618  -0.2103 -0.0659 44   VAL   B CG2 
2980  N  N   . THR   B 45  ? 1.6005 1.4034 1.4461 0.1844  -0.2360 -0.0774 45   THR   B N   
2981  C  CA  . THR   B 45  ? 1.6566 1.4393 1.4797 0.1949  -0.2415 -0.0798 45   THR   B CA  
2982  C  C   . THR   B 45  ? 1.7847 1.5644 1.5919 0.2006  -0.2305 -0.0739 45   THR   B C   
2983  O  O   . THR   B 45  ? 1.7993 1.5925 1.6157 0.1954  -0.2207 -0.0686 45   THR   B O   
2984  C  CB  . THR   B 45  ? 1.6635 1.4392 1.4910 0.1938  -0.2513 -0.0844 45   THR   B CB  
2985  O  OG1 . THR   B 45  ? 1.7211 1.5012 1.5505 0.1916  -0.2448 -0.0804 45   THR   B OG1 
2986  C  CG2 . THR   B 45  ? 1.5291 1.3147 1.3804 0.1846  -0.2587 -0.0885 45   THR   B CG2 
2987  N  N   . ALA   B 46  ? 1.9593 1.7207 1.7422 0.2117  -0.2325 -0.0750 46   ALA   B N   
2988  C  CA  . ALA   B 46  ? 1.9713 1.7278 1.7375 0.2184  -0.2223 -0.0696 46   ALA   B CA  
2989  C  C   . ALA   B 46  ? 1.9603 1.7215 1.7320 0.2156  -0.2187 -0.0671 46   ALA   B C   
2990  O  O   . ALA   B 46  ? 2.0122 1.7790 1.7810 0.2164  -0.2076 -0.0613 46   ALA   B O   
2991  C  CB  . ALA   B 46  ? 1.9634 1.6971 1.7021 0.2311  -0.2268 -0.0721 46   ALA   B CB  
2992  N  N   . GLU   B 47  ? 1.8702 1.6290 1.6503 0.2122  -0.2281 -0.0714 47   GLU   B N   
2993  C  CA  . GLU   B 47  ? 1.9002 1.6646 1.6880 0.2083  -0.2251 -0.0692 47   GLU   B CA  
2994  C  C   . GLU   B 47  ? 1.8908 1.6772 1.7017 0.1971  -0.2176 -0.0652 47   GLU   B C   
2995  O  O   . GLU   B 47  ? 1.9370 1.7319 1.7491 0.1960  -0.2073 -0.0596 47   GLU   B O   
2996  C  CB  . GLU   B 47  ? 1.9486 1.7031 1.7384 0.2079  -0.2375 -0.0751 47   GLU   B CB  
2997  N  N   . GLY   B 48  ? 1.8844 1.6803 1.7139 0.1889  -0.2227 -0.0681 48   GLY   B N   
2998  C  CA  . GLY   B 48  ? 1.8225 1.6385 1.6738 0.1782  -0.2163 -0.0648 48   GLY   B CA  
2999  C  C   . GLY   B 48  ? 1.6923 1.5185 1.5612 0.1707  -0.2198 -0.0673 48   GLY   B C   
3000  O  O   . GLY   B 48  ? 1.7133 1.5427 1.5803 0.1717  -0.2170 -0.0664 48   GLY   B O   
3001  N  N   . LEU   B 49  ? 1.5217 1.3534 1.4080 0.1631  -0.2255 -0.0702 49   LEU   B N   
3002  C  CA  . LEU   B 49  ? 1.4142 1.2555 1.3187 0.1558  -0.2292 -0.0729 49   LEU   B CA  
3003  C  C   . LEU   B 49  ? 1.3654 1.1999 1.2778 0.1539  -0.2413 -0.0792 49   LEU   B C   
3004  O  O   . LEU   B 49  ? 1.3702 1.2012 1.2845 0.1527  -0.2435 -0.0798 49   LEU   B O   
3005  C  CB  . LEU   B 49  ? 1.3993 1.2599 1.3229 0.1457  -0.2206 -0.0685 49   LEU   B CB  
3006  C  CG  . LEU   B 49  ? 1.3366 1.2088 1.2609 0.1442  -0.2100 -0.0633 49   LEU   B CG  
3007  C  CD1 . LEU   B 49  ? 1.2116 1.1012 1.1555 0.1341  -0.2038 -0.0601 49   LEU   B CD1 
3008  C  CD2 . LEU   B 49  ? 1.3870 1.2577 1.3088 0.1464  -0.2127 -0.0656 49   LEU   B CD2 
3009  N  N   . ARG   B 50  ? 1.3292 1.1615 1.2465 0.1537  -0.2492 -0.0841 50   ARG   B N   
3010  C  CA  . ARG   B 50  ? 1.2912 1.1185 1.2191 0.1512  -0.2609 -0.0903 50   ARG   B CA  
3011  C  C   . ARG   B 50  ? 1.2486 1.0916 1.2019 0.1407  -0.2605 -0.0910 50   ARG   B C   
3012  O  O   . ARG   B 50  ? 1.2665 1.1164 1.2247 0.1393  -0.2591 -0.0911 50   ARG   B O   
3013  C  CB  . ARG   B 50  ? 1.3501 1.1617 1.2649 0.1594  -0.2719 -0.0962 50   ARG   B CB  
3014  C  CG  . ARG   B 50  ? 1.3477 1.1576 1.2782 0.1556  -0.2843 -0.1031 50   ARG   B CG  
3015  C  CD  . ARG   B 50  ? 1.3866 1.1769 1.3020 0.1647  -0.2974 -0.1096 50   ARG   B CD  
3016  N  NE  . ARG   B 50  ? 1.4284 1.2097 1.3230 0.1738  -0.2967 -0.1093 50   ARG   B NE  
3017  C  CZ  . ARG   B 50  ? 1.4587 1.2435 1.3562 0.1740  -0.2982 -0.1107 50   ARG   B CZ  
3018  N  NH1 . ARG   B 50  ? 1.4424 1.2400 1.3630 0.1657  -0.3004 -0.1127 50   ARG   B NH1 
3019  N  NH2 . ARG   B 50  ? 1.4673 1.2420 1.3436 0.1829  -0.2972 -0.1101 50   ARG   B NH2 
3020  N  N   . PRO   B 51  ? 1.1967 1.0454 1.1660 0.1334  -0.2612 -0.0914 51   PRO   B N   
3021  C  CA  . PRO   B 51  ? 1.2122 1.0752 1.2059 0.1235  -0.2605 -0.0920 51   PRO   B CA  
3022  C  C   . PRO   B 51  ? 1.2482 1.1075 1.2500 0.1236  -0.2714 -0.0986 51   PRO   B C   
3023  O  O   . PRO   B 51  ? 1.3385 1.1848 1.3357 0.1279  -0.2821 -0.1039 51   PRO   B O   
3024  C  CB  . PRO   B 51  ? 1.2398 1.1051 1.2447 0.1174  -0.2600 -0.0914 51   PRO   B CB  
3025  C  CG  . PRO   B 51  ? 1.2390 1.0966 1.2260 0.1230  -0.2559 -0.0880 51   PRO   B CG  
3026  C  CD  . PRO   B 51  ? 1.2426 1.0861 1.2078 0.1337  -0.2604 -0.0900 51   PRO   B CD  
3027  N  N   . VAL   B 52  ? 1.2574 1.1283 1.2723 0.1188  -0.2691 -0.0985 52   VAL   B N   
3028  C  CA  . VAL   B 52  ? 1.2654 1.1336 1.2880 0.1195  -0.2792 -0.1046 52   VAL   B CA  
3029  C  C   . VAL   B 52  ? 1.2478 1.1279 1.2976 0.1095  -0.2804 -0.1065 52   VAL   B C   
3030  O  O   . VAL   B 52  ? 1.1891 1.0641 1.2491 0.1083  -0.2903 -0.1120 52   VAL   B O   
3031  C  CB  . VAL   B 52  ? 1.2653 1.1344 1.2786 0.1239  -0.2772 -0.1039 52   VAL   B CB  
3032  C  CG1 . VAL   B 52  ? 1.2756 1.1409 1.2963 0.1251  -0.2884 -0.1106 52   VAL   B CG1 
3033  C  CG2 . VAL   B 52  ? 1.2291 1.0860 1.2153 0.1339  -0.2750 -0.1017 52   VAL   B CG2 
3034  N  N   . LYS   B 53  ? 1.2608 1.1564 1.3224 0.1026  -0.2705 -0.1020 53   LYS   B N   
3035  C  CA  . LYS   B 53  ? 1.2382 1.1463 1.3251 0.0929  -0.2694 -0.1028 53   LYS   B CA  
3036  C  C   . LYS   B 53  ? 1.2226 1.1450 1.3149 0.0869  -0.2561 -0.0961 53   LYS   B C   
3037  O  O   . LYS   B 53  ? 1.2157 1.1412 1.2970 0.0896  -0.2496 -0.0924 53   LYS   B O   
3038  C  CB  . LYS   B 53  ? 1.2329 1.1437 1.3309 0.0925  -0.2761 -0.1076 53   LYS   B CB  
3039  C  CG  . LYS   B 53  ? 1.2475 1.1649 1.3714 0.0845  -0.2803 -0.1112 53   LYS   B CG  
3040  C  CD  . LYS   B 53  ? 1.4034 1.3308 1.5419 0.0812  -0.2805 -0.1129 53   LYS   B CD  
3041  C  CE  . LYS   B 53  ? 1.5259 1.4552 1.6874 0.0764  -0.2889 -0.1186 53   LYS   B CE  
3042  N  NZ  . LYS   B 53  ? 1.4685 1.4039 1.6465 0.0681  -0.2844 -0.1168 53   LYS   B NZ  
3043  N  N   . GLU   B 54  ? 1.2353 1.1656 1.3440 0.0787  -0.2522 -0.0946 54   GLU   B N   
3044  C  CA  . GLU   B 54  ? 1.2283 1.1724 1.3446 0.0721  -0.2404 -0.0888 54   GLU   B CA  
3045  C  C   . GLU   B 54  ? 1.1912 1.1455 1.3319 0.0634  -0.2401 -0.0904 54   GLU   B C   
3046  O  O   . GLU   B 54  ? 1.1645 1.1160 1.3176 0.0602  -0.2456 -0.0938 54   GLU   B O   
3047  C  CB  . GLU   B 54  ? 1.2275 1.1710 1.3366 0.0712  -0.2335 -0.0839 54   GLU   B CB  
3048  C  CG  . GLU   B 54  ? 1.3119 1.2521 1.4305 0.0671  -0.2363 -0.0853 54   GLU   B CG  
3049  C  CD  . GLU   B 54  ? 1.2711 1.2234 1.4075 0.0576  -0.2287 -0.0822 54   GLU   B CD  
3050  O  OE1 . GLU   B 54  ? 1.2053 1.1680 1.3438 0.0549  -0.2208 -0.0785 54   GLU   B OE1 
3051  O  OE2 . GLU   B 54  ? 1.3666 1.3174 1.5143 0.0531  -0.2306 -0.0836 54   GLU   B OE2 
3052  N  N   . VAL   B 55  ? 1.2220 1.1878 1.3697 0.0597  -0.2335 -0.0879 55   VAL   B N   
3053  C  CA  . VAL   B 55  ? 1.2141 1.1893 1.3838 0.0527  -0.2335 -0.0898 55   VAL   B CA  
3054  C  C   . VAL   B 55  ? 1.2031 1.1910 1.3802 0.0459  -0.2216 -0.0842 55   VAL   B C   
3055  O  O   . VAL   B 55  ? 1.2020 1.1925 1.3669 0.0474  -0.2142 -0.0792 55   VAL   B O   
3056  C  CB  . VAL   B 55  ? 1.2006 1.1766 1.3724 0.0557  -0.2390 -0.0937 55   VAL   B CB  
3057  C  CG1 . VAL   B 55  ? 1.3394 1.3032 1.5084 0.0612  -0.2519 -0.1002 55   VAL   B CG1 
3058  C  CG2 . VAL   B 55  ? 1.2011 1.1780 1.3559 0.0605  -0.2339 -0.0902 55   VAL   B CG2 
3059  N  N   . GLY   B 56  ? 1.1672 1.1626 1.3648 0.0385  -0.2201 -0.0851 56   GLY   B N   
3060  C  CA  . GLY   B 56  ? 1.1542 1.1606 1.3597 0.0318  -0.2094 -0.0801 56   GLY   B CA  
3061  C  C   . GLY   B 56  ? 1.1565 1.1729 1.3756 0.0280  -0.2070 -0.0809 56   GLY   B C   
3062  O  O   . GLY   B 56  ? 1.1469 1.1649 1.3826 0.0253  -0.2120 -0.0852 56   GLY   B O   
3063  N  N   . MET   B 57  ? 1.1049 1.1282 1.3175 0.0278  -0.1994 -0.0767 57   MET   B N   
3064  C  CA  . MET   B 57  ? 1.0551 1.0883 1.2789 0.0242  -0.1958 -0.0766 57   MET   B CA  
3065  C  C   . MET   B 57  ? 1.0387 1.0804 1.2755 0.0162  -0.1870 -0.0731 57   MET   B C   
3066  O  O   . MET   B 57  ? 0.9946 1.0356 1.2271 0.0142  -0.1818 -0.0694 57   MET   B O   
3067  C  CB  . MET   B 57  ? 1.0093 1.0448 1.2192 0.0282  -0.1923 -0.0740 57   MET   B CB  
3068  C  CG  . MET   B 57  ? 1.0182 1.0442 1.2123 0.0366  -0.1996 -0.0766 57   MET   B CG  
3069  S  SD  . MET   B 57  ? 1.0584 1.0876 1.2403 0.0406  -0.1962 -0.0746 57   MET   B SD  
3070  C  CE  . MET   B 57  ? 1.0404 1.0773 1.2408 0.0369  -0.1984 -0.0782 57   MET   B CE  
3071  N  N   . TYR   B 58  ? 1.0631 1.1125 1.3157 0.0120  -0.1855 -0.0745 58   TYR   B N   
3072  C  CA  . TYR   B 58  ? 1.0481 1.1060 1.3135 0.0046  -0.1768 -0.0715 58   TYR   B CA  
3073  C  C   . TYR   B 58  ? 1.0084 1.0730 1.2653 0.0040  -0.1682 -0.0666 58   TYR   B C   
3074  O  O   . TYR   B 58  ? 1.0142 1.0867 1.2806 0.0003  -0.1636 -0.0658 58   TYR   B O   
3075  C  CB  . TYR   B 58  ? 1.0543 1.1167 1.3410 0.0007  -0.1795 -0.0755 58   TYR   B CB  
3076  C  CG  . TYR   B 58  ? 1.0761 1.1334 1.3754 -0.0011 -0.1857 -0.0794 58   TYR   B CG  
3077  C  CD1 . TYR   B 58  ? 1.1360 1.1860 1.4348 0.0036  -0.1970 -0.0849 58   TYR   B CD1 
3078  C  CD2 . TYR   B 58  ? 1.1095 1.1686 1.4207 -0.0074 -0.1804 -0.0776 58   TYR   B CD2 
3079  C  CE1 . TYR   B 58  ? 1.2228 1.2678 1.5338 0.0019  -0.2032 -0.0887 58   TYR   B CE1 
3080  C  CE2 . TYR   B 58  ? 1.1595 1.2137 1.4831 -0.0094 -0.1860 -0.0811 58   TYR   B CE2 
3081  C  CZ  . TYR   B 58  ? 1.2051 1.2525 1.5290 -0.0049 -0.1975 -0.0867 58   TYR   B CZ  
3082  O  OH  . TYR   B 58  ? 1.1433 1.1857 1.4799 -0.0070 -0.2033 -0.0903 58   TYR   B OH  
3083  N  N   . GLY   B 59  ? 0.9523 1.0138 1.1914 0.0077  -0.1660 -0.0632 59   GLY   B N   
3084  C  CA  . GLY   B 59  ? 0.9413 1.0085 1.1714 0.0079  -0.1589 -0.0589 59   GLY   B CA  
3085  C  C   . GLY   B 59  ? 0.9599 1.0224 1.1722 0.0120  -0.1574 -0.0556 59   GLY   B C   
3086  O  O   . GLY   B 59  ? 0.9621 1.0169 1.1690 0.0147  -0.1618 -0.0568 59   GLY   B O   
3087  N  N   . LYS   B 60  ? 0.9732 1.0401 1.1766 0.0124  -0.1512 -0.0515 60   LYS   B N   
3088  C  CA  . LYS   B 60  ? 0.9571 1.0205 1.1443 0.0164  -0.1494 -0.0482 60   LYS   B CA  
3089  C  C   . LYS   B 60  ? 0.9399 1.0015 1.1157 0.0223  -0.1519 -0.0489 60   LYS   B C   
3090  O  O   . LYS   B 60  ? 0.9464 1.0139 1.1220 0.0216  -0.1483 -0.0476 60   LYS   B O   
3091  C  CB  . LYS   B 60  ? 0.9615 1.0308 1.1466 0.0127  -0.1406 -0.0429 60   LYS   B CB  
3092  C  CG  . LYS   B 60  ? 0.9502 1.0175 1.1387 0.0093  -0.1383 -0.0413 60   LYS   B CG  
3093  C  CD  . LYS   B 60  ? 0.9517 1.0251 1.1403 0.0050  -0.1299 -0.0366 60   LYS   B CD  
3094  C  CE  . LYS   B 60  ? 0.9885 1.0623 1.1628 0.0084  -0.1267 -0.0327 60   LYS   B CE  
3095  N  NZ  . LYS   B 60  ? 1.0422 1.1105 1.2094 0.0098  -0.1266 -0.0308 60   LYS   B NZ  
3096  N  N   . ILE   B 61  ? 0.9609 1.0138 1.1269 0.0282  -0.1578 -0.0510 61   ILE   B N   
3097  C  CA  . ILE   B 61  ? 0.9836 1.0330 1.1374 0.0346  -0.1603 -0.0517 61   ILE   B CA  
3098  C  C   . ILE   B 61  ? 0.9760 1.0306 1.1213 0.0347  -0.1526 -0.0466 61   ILE   B C   
3099  O  O   . ILE   B 61  ? 0.9505 1.0048 1.0892 0.0349  -0.1486 -0.0431 61   ILE   B O   
3100  C  CB  . ILE   B 61  ? 0.9706 1.0087 1.1129 0.0412  -0.1669 -0.0540 61   ILE   B CB  
3101  C  CG1 . ILE   B 61  ? 1.0055 1.0385 1.1567 0.0416  -0.1758 -0.0598 61   ILE   B CG1 
3102  C  CG2 . ILE   B 61  ? 0.9425 0.9767 1.0691 0.0479  -0.1669 -0.0531 61   ILE   B CG2 
3103  C  CD1 . ILE   B 61  ? 1.0019 1.0231 1.1438 0.0473  -0.1831 -0.0626 61   ILE   B CD1 
3104  N  N   . ALA   B 62  ? 0.9948 1.0546 1.1412 0.0342  -0.1504 -0.0463 62   ALA   B N   
3105  C  CA  . ALA   B 62  ? 0.9532 1.0187 1.0936 0.0338  -0.1434 -0.0419 62   ALA   B CA  
3106  C  C   . ALA   B 62  ? 0.9526 1.0139 1.0801 0.0401  -0.1446 -0.0420 62   ALA   B C   
3107  O  O   . ALA   B 62  ? 0.9277 0.9888 1.0449 0.0426  -0.1405 -0.0384 62   ALA   B O   
3108  C  CB  . ALA   B 62  ? 0.9840 1.0586 1.1357 0.0279  -0.1392 -0.0412 62   ALA   B CB  
3109  N  N   . VAL   B 63  ? 1.0592 1.1172 1.1875 0.0427  -0.1501 -0.0459 63   VAL   B N   
3110  C  CA  . VAL   B 63  ? 1.0724 1.1240 1.1876 0.0495  -0.1524 -0.0466 63   VAL   B CA  
3111  C  C   . VAL   B 63  ? 1.0867 1.1276 1.1974 0.0546  -0.1610 -0.0510 63   VAL   B C   
3112  O  O   . VAL   B 63  ? 1.0847 1.1248 1.2062 0.0525  -0.1665 -0.0550 63   VAL   B O   
3113  C  CB  . VAL   B 63  ? 1.0850 1.1405 1.2027 0.0491  -0.1519 -0.0476 63   VAL   B CB  
3114  C  CG1 . VAL   B 63  ? 1.1186 1.1666 1.2212 0.0564  -0.1535 -0.0478 63   VAL   B CG1 
3115  C  CG2 . VAL   B 63  ? 1.0487 1.1146 1.1718 0.0436  -0.1438 -0.0435 63   VAL   B CG2 
3116  N  N   . MET   B 64  ? 0.9882 1.0207 1.0834 0.0613  -0.1620 -0.0503 64   MET   B N   
3117  C  CA  . MET   B 64  ? 1.0275 1.0483 1.1153 0.0674  -0.1704 -0.0545 64   MET   B CA  
3118  C  C   . MET   B 64  ? 1.1211 1.1344 1.1917 0.0749  -0.1702 -0.0538 64   MET   B C   
3119  O  O   . MET   B 64  ? 1.1184 1.1308 1.1785 0.0774  -0.1646 -0.0497 64   MET   B O   
3120  C  CB  . MET   B 64  ? 1.0677 1.0833 1.1533 0.0681  -0.1722 -0.0545 64   MET   B CB  
3121  C  CG  . MET   B 64  ? 1.0850 1.0873 1.1603 0.0753  -0.1807 -0.0586 64   MET   B CG  
3122  S  SD  . MET   B 64  ? 1.0030 0.9979 1.0732 0.0770  -0.1827 -0.0583 64   MET   B SD  
3123  C  CE  . MET   B 64  ? 1.0430 1.0364 1.0961 0.0816  -0.1746 -0.0525 64   MET   B CE  
3124  N  N   . GLU   B 65  ? 1.1289 1.1367 1.1968 0.0786  -0.1762 -0.0577 65   GLU   B N   
3125  C  CA  . GLU   B 65  ? 1.1096 1.1095 1.1610 0.0859  -0.1761 -0.0573 65   GLU   B CA  
3126  C  C   . GLU   B 65  ? 1.1313 1.1204 1.1783 0.0914  -0.1864 -0.0631 65   GLU   B C   
3127  O  O   . GLU   B 65  ? 1.0939 1.0857 1.1536 0.0884  -0.1920 -0.0672 65   GLU   B O   
3128  C  CB  . GLU   B 65  ? 1.1263 1.1340 1.1788 0.0837  -0.1695 -0.0544 65   GLU   B CB  
3129  C  CG  . GLU   B 65  ? 1.1692 1.1830 1.2178 0.0819  -0.1595 -0.0482 65   GLU   B CG  
3130  C  CD  . GLU   B 65  ? 1.2693 1.2739 1.3014 0.0886  -0.1580 -0.0461 65   GLU   B CD  
3131  O  OE1 . GLU   B 65  ? 1.2674 1.2603 1.2866 0.0959  -0.1627 -0.0486 65   GLU   B OE1 
3132  O  OE2 . GLU   B 65  ? 1.2631 1.2716 1.2945 0.0870  -0.1521 -0.0421 65   GLU   B OE2 
3133  N  N   . LEU   B 66  ? 1.1767 1.1531 1.2056 0.0996  -0.1889 -0.0636 66   LEU   B N   
3134  C  CA  . LEU   B 66  ? 1.1624 1.1265 1.1828 0.1064  -0.1985 -0.0688 66   LEU   B CA  
3135  C  C   . LEU   B 66  ? 1.1312 1.0920 1.1406 0.1109  -0.1964 -0.0680 66   LEU   B C   
3136  O  O   . LEU   B 66  ? 1.0654 1.0282 1.0665 0.1117  -0.1878 -0.0631 66   LEU   B O   
3137  C  CB  . LEU   B 66  ? 1.1375 1.0879 1.1432 0.1134  -0.2028 -0.0700 66   LEU   B CB  
3138  C  CG  . LEU   B 66  ? 1.1001 1.0495 1.1144 0.1108  -0.2081 -0.0725 66   LEU   B CG  
3139  C  CD1 . LEU   B 66  ? 1.1685 1.1052 1.1651 0.1179  -0.2093 -0.0719 66   LEU   B CD1 
3140  C  CD2 . LEU   B 66  ? 1.1178 1.0639 1.1417 0.1106  -0.2191 -0.0790 66   LEU   B CD2 
3141  N  N   . PHE   B 67  ? 1.1238 1.0792 1.1337 0.1137  -0.2046 -0.0730 67   PHE   B N   
3142  C  CA  . PHE   B 67  ? 1.1305 1.0818 1.1307 0.1180  -0.2042 -0.0732 67   PHE   B CA  
3143  C  C   . PHE   B 67  ? 1.2257 1.1655 1.2218 0.1238  -0.2163 -0.0797 67   PHE   B C   
3144  O  O   . PHE   B 67  ? 1.1799 1.1176 1.1843 0.1230  -0.2244 -0.0840 67   PHE   B O   
3145  C  CB  . PHE   B 67  ? 1.1506 1.1157 1.1644 0.1112  -0.1986 -0.0712 67   PHE   B CB  
3146  C  CG  . PHE   B 67  ? 1.1275 1.1005 1.1618 0.1054  -0.2045 -0.0755 67   PHE   B CG  
3147  C  CD1 . PHE   B 67  ? 1.1020 1.0826 1.1521 0.0989  -0.2048 -0.0759 67   PHE   B CD1 
3148  C  CD2 . PHE   B 67  ? 1.0916 1.0645 1.1297 0.1063  -0.2091 -0.0789 67   PHE   B CD2 
3149  C  CE1 . PHE   B 67  ? 1.0418 1.0297 1.1113 0.0936  -0.2094 -0.0796 67   PHE   B CE1 
3150  C  CE2 . PHE   B 67  ? 0.9923 0.9729 1.0502 0.1010  -0.2140 -0.0827 67   PHE   B CE2 
3151  C  CZ  . PHE   B 67  ? 0.9835 0.9717 1.0573 0.0946  -0.2139 -0.0830 67   PHE   B CZ  
3152  N  N   . ARG   B 68  ? 1.3048 1.2365 1.2876 0.1300  -0.2176 -0.0805 68   ARG   B N   
3153  C  CA  . ARG   B 68  ? 1.2835 1.2024 1.2589 0.1369  -0.2292 -0.0866 68   ARG   B CA  
3154  C  C   . ARG   B 68  ? 1.2816 1.2001 1.2539 0.1388  -0.2291 -0.0872 68   ARG   B C   
3155  O  O   . ARG   B 68  ? 1.3042 1.2137 1.2576 0.1451  -0.2257 -0.0850 68   ARG   B O   
3156  C  CB  . ARG   B 68  ? 1.2860 1.1872 1.2385 0.1465  -0.2326 -0.0873 68   ARG   B CB  
3157  C  CG  . ARG   B 68  ? 1.3288 1.2156 1.2723 0.1541  -0.2451 -0.0937 68   ARG   B CG  
3158  C  CD  . ARG   B 68  ? 1.3659 1.2347 1.2854 0.1638  -0.2475 -0.0939 68   ARG   B CD  
3159  N  NE  . ARG   B 68  ? 1.3420 1.2110 1.2647 0.1619  -0.2478 -0.0935 68   ARG   B NE  
3160  C  CZ  . ARG   B 68  ? 1.3749 1.2289 1.2832 0.1691  -0.2545 -0.0961 68   ARG   B CZ  
3161  N  NH1 . ARG   B 68  ? 1.4911 1.3281 1.3801 0.1787  -0.2613 -0.0994 68   ARG   B NH1 
3162  N  NH2 . ARG   B 68  ? 1.3650 1.2203 1.2778 0.1667  -0.2544 -0.0956 68   ARG   B NH2 
3163  N  N   . PRO   B 69  ? 1.2942 1.2219 1.2844 0.1337  -0.2329 -0.0903 69   PRO   B N   
3164  C  CA  . PRO   B 69  ? 1.3157 1.2442 1.3045 0.1350  -0.2326 -0.0908 69   PRO   B CA  
3165  C  C   . PRO   B 69  ? 1.3778 1.2906 1.3536 0.1441  -0.2437 -0.0964 69   PRO   B C   
3166  O  O   . PRO   B 69  ? 1.3972 1.3002 1.3691 0.1483  -0.2528 -0.1006 69   PRO   B O   
3167  C  CB  . PRO   B 69  ? 1.2603 1.2046 1.2746 0.1260  -0.2328 -0.0923 69   PRO   B CB  
3168  C  CG  . PRO   B 69  ? 1.3140 1.2575 1.3396 0.1244  -0.2411 -0.0966 69   PRO   B CG  
3169  C  CD  . PRO   B 69  ? 1.2732 1.2085 1.2849 0.1278  -0.2392 -0.0942 69   PRO   B CD  
3170  N  N   . LYS   B 70  ? 1.3918 1.3019 1.3607 0.1471  -0.2432 -0.0965 70   LYS   B N   
3171  C  CA  . LYS   B 70  ? 1.4055 1.2992 1.3585 0.1567  -0.2528 -0.1011 70   LYS   B CA  
3172  C  C   . LYS   B 70  ? 1.4225 1.3144 1.3882 0.1571  -0.2665 -0.1086 70   LYS   B C   
3173  O  O   . LYS   B 70  ? 1.4140 1.3177 1.4009 0.1510  -0.2690 -0.1110 70   LYS   B O   
3174  C  CB  . LYS   B 70  ? 1.3666 1.2602 1.3139 0.1584  -0.2496 -0.1000 70   LYS   B CB  
3175  N  N   . GLY   B 71  ? 1.4918 1.3687 1.4447 0.1644  -0.2755 -0.1123 71   GLY   B N   
3176  C  CA  . GLY   B 71  ? 1.5208 1.3944 1.4847 0.1653  -0.2893 -0.1197 71   GLY   B CA  
3177  C  C   . GLY   B 71  ? 1.5456 1.4252 1.5239 0.1598  -0.2909 -0.1204 71   GLY   B C   
3178  O  O   . GLY   B 71  ? 1.5599 1.4519 1.5626 0.1525  -0.2935 -0.1228 71   GLY   B O   
3179  N  N   . GLU   B 72  ? 1.5800 1.4502 1.5431 0.1637  -0.2892 -0.1185 72   GLU   B N   
3180  C  CA  . GLU   B 72  ? 1.5263 1.4011 1.5002 0.1588  -0.2893 -0.1183 72   GLU   B CA  
3181  C  C   . GLU   B 72  ? 1.5163 1.3738 1.4688 0.1670  -0.2935 -0.1191 72   GLU   B C   
3182  O  O   . GLU   B 72  ? 1.5310 1.3797 1.4615 0.1728  -0.2871 -0.1151 72   GLU   B O   
3183  C  CB  . GLU   B 72  ? 1.4925 1.3826 1.4756 0.1504  -0.2754 -0.1113 72   GLU   B CB  
3184  C  CG  . GLU   B 72  ? 1.5010 1.4092 1.5106 0.1403  -0.2726 -0.1112 72   GLU   B CG  
3185  C  CD  . GLU   B 72  ? 1.5427 1.4530 1.5715 0.1375  -0.2836 -0.1176 72   GLU   B CD  
3186  O  OE1 . GLU   B 72  ? 1.5299 1.4503 1.5774 0.1327  -0.2856 -0.1199 72   GLU   B OE1 
3187  O  OE2 . GLU   B 72  ? 1.5578 1.4599 1.5837 0.1399  -0.2901 -0.1202 72   GLU   B OE2 
3188  N  N   . SER   B 73  ? 1.5431 1.3958 1.5022 0.1674  -0.3038 -0.1242 73   SER   B N   
3189  C  CA  . SER   B 73  ? 1.5590 1.3949 1.4978 0.1752  -0.3079 -0.1251 73   SER   B CA  
3190  C  C   . SER   B 73  ? 1.5688 1.4089 1.5027 0.1723  -0.2961 -0.1185 73   SER   B C   
3191  O  O   . SER   B 73  ? 1.5576 1.3857 1.4684 0.1794  -0.2923 -0.1157 73   SER   B O   
3192  C  CB  . SER   B 73  ? 1.5227 1.3524 1.4707 0.1760  -0.3222 -0.1323 73   SER   B CB  
3193  O  OG  . SER   B 73  ? 1.5525 1.3981 1.5286 0.1656  -0.3218 -0.1330 73   SER   B OG  
3194  N  N   . LYS   B 74  ? 1.5587 1.4159 1.5142 0.1621  -0.2897 -0.1158 74   LYS   B N   
3195  C  CA  . LYS   B 74  ? 1.4252 1.2884 1.3802 0.1582  -0.2793 -0.1099 74   LYS   B CA  
3196  C  C   . LYS   B 74  ? 1.3758 1.2572 1.3441 0.1497  -0.2668 -0.1042 74   LYS   B C   
3197  O  O   . LYS   B 74  ? 1.3312 1.2204 1.3090 0.1468  -0.2662 -0.1048 74   LYS   B O   
3198  C  CB  . LYS   B 74  ? 1.3961 1.2606 1.3639 0.1542  -0.2848 -0.1126 74   LYS   B CB  
3199  C  CG  . LYS   B 74  ? 1.4643 1.3102 1.4166 0.1627  -0.2956 -0.1172 74   LYS   B CG  
3200  C  CD  . LYS   B 74  ? 1.5205 1.3614 1.4832 0.1638  -0.3107 -0.1254 74   LYS   B CD  
3201  C  CE  . LYS   B 74  ? 1.5182 1.3373 1.4598 0.1745  -0.3219 -0.1301 74   LYS   B CE  
3202  N  NZ  . LYS   B 74  ? 1.3354 1.1469 1.2826 0.1777  -0.3374 -0.1383 74   LYS   B NZ  
3203  N  N   . ASP   B 75  ? 1.3480 1.2357 1.3164 0.1460  -0.2572 -0.0988 75   ASP   B N   
3204  C  CA  . ASP   B 75  ? 1.2586 1.1635 1.2408 0.1373  -0.2458 -0.0934 75   ASP   B CA  
3205  C  C   . ASP   B 75  ? 1.2222 1.1403 1.2307 0.1280  -0.2483 -0.0956 75   ASP   B C   
3206  O  O   . ASP   B 75  ? 1.2063 1.1214 1.2226 0.1270  -0.2560 -0.0995 75   ASP   B O   
3207  C  CB  . ASP   B 75  ? 1.2343 1.1411 1.2089 0.1365  -0.2359 -0.0874 75   ASP   B CB  
3208  C  CG  . ASP   B 75  ? 1.2386 1.1397 1.1929 0.1424  -0.2278 -0.0827 75   ASP   B CG  
3209  O  OD1 . ASP   B 75  ? 1.2535 1.1654 1.2121 0.1381  -0.2183 -0.0780 75   ASP   B OD1 
3210  O  OD2 . ASP   B 75  ? 1.2949 1.1807 1.2290 0.1513  -0.2307 -0.0835 75   ASP   B OD2 
3211  N  N   . LEU   B 76  ? 1.2132 1.1457 1.2352 0.1211  -0.2412 -0.0928 76   LEU   B N   
3212  C  CA  . LEU   B 76  ? 1.1697 1.1162 1.2163 0.1116  -0.2403 -0.0934 76   LEU   B CA  
3213  C  C   . LEU   B 76  ? 1.1372 1.0950 1.1885 0.1051  -0.2285 -0.0870 76   LEU   B C   
3214  O  O   . LEU   B 76  ? 1.1586 1.1166 1.1975 0.1071  -0.2203 -0.0821 76   LEU   B O   
3215  C  CB  . LEU   B 76  ? 1.1146 1.0687 1.1737 0.1086  -0.2419 -0.0956 76   LEU   B CB  
3216  C  CG  . LEU   B 76  ? 1.1534 1.0968 1.2074 0.1153  -0.2535 -0.1018 76   LEU   B CG  
3217  C  CD1 . LEU   B 76  ? 1.1252 1.0767 1.1913 0.1124  -0.2539 -0.1034 76   LEU   B CD1 
3218  C  CD2 . LEU   B 76  ? 1.1851 1.1231 1.2475 0.1155  -0.2639 -0.1072 76   LEU   B CD2 
3219  N  N   . LEU   B 77  ? 1.0848 1.0522 1.1547 0.0974  -0.2275 -0.0871 77   LEU   B N   
3220  C  CA  . LEU   B 77  ? 1.0888 1.0659 1.1637 0.0914  -0.2174 -0.0815 77   LEU   B CA  
3221  C  C   . LEU   B 77  ? 1.1043 1.0963 1.1979 0.0829  -0.2121 -0.0801 77   LEU   B C   
3222  O  O   . LEU   B 77  ? 1.0884 1.0845 1.1987 0.0789  -0.2170 -0.0839 77   LEU   B O   
3223  C  CB  . LEU   B 77  ? 1.1143 1.0885 1.1929 0.0899  -0.2201 -0.0823 77   LEU   B CB  
3224  C  CG  . LEU   B 77  ? 1.0714 1.0557 1.1576 0.0830  -0.2109 -0.0773 77   LEU   B CG  
3225  C  CD1 . LEU   B 77  ? 1.0829 1.0664 1.1530 0.0863  -0.2026 -0.0718 77   LEU   B CD1 
3226  C  CD2 . LEU   B 77  ? 1.0601 1.0401 1.1507 0.0819  -0.2152 -0.0791 77   LEU   B CD2 
3227  N  N   . PHE   B 78  ? 1.1138 1.1137 1.2051 0.0802  -0.2021 -0.0747 78   PHE   B N   
3228  C  CA  . PHE   B 78  ? 1.0834 1.0968 1.1903 0.0725  -0.1962 -0.0728 78   PHE   B CA  
3229  C  C   . PHE   B 78  ? 1.0918 1.1129 1.2064 0.0662  -0.1894 -0.0689 78   PHE   B C   
3230  O  O   . PHE   B 78  ? 1.0976 1.1179 1.2018 0.0674  -0.1837 -0.0646 78   PHE   B O   
3231  C  CB  . PHE   B 78  ? 1.0837 1.1010 1.1840 0.0734  -0.1901 -0.0698 78   PHE   B CB  
3232  C  CG  . PHE   B 78  ? 1.0633 1.0940 1.1782 0.0656  -0.1835 -0.0675 78   PHE   B CG  
3233  C  CD1 . PHE   B 78  ? 1.0505 1.0862 1.1794 0.0627  -0.1869 -0.0709 78   PHE   B CD1 
3234  C  CD2 . PHE   B 78  ? 1.0591 1.0973 1.1734 0.0616  -0.1740 -0.0619 78   PHE   B CD2 
3235  C  CE1 . PHE   B 78  ? 1.0487 1.0960 1.1900 0.0560  -0.1805 -0.0687 78   PHE   B CE1 
3236  C  CE2 . PHE   B 78  ? 1.0486 1.0980 1.1749 0.0549  -0.1682 -0.0599 78   PHE   B CE2 
3237  C  CZ  . PHE   B 78  ? 1.0443 1.0982 1.1838 0.0522  -0.1712 -0.0633 78   PHE   B CZ  
3238  N  N   . ILE   B 79  ? 1.0532 1.0818 1.1861 0.0595  -0.1897 -0.0703 79   ILE   B N   
3239  C  CA  . ILE   B 79  ? 1.0177 1.0527 1.1590 0.0534  -0.1840 -0.0672 79   ILE   B CA  
3240  C  C   . ILE   B 79  ? 1.0078 1.0549 1.1629 0.0464  -0.1779 -0.0654 79   ILE   B C   
3241  O  O   . ILE   B 79  ? 1.0184 1.0688 1.1863 0.0441  -0.1812 -0.0688 79   ILE   B O   
3242  C  CB  . ILE   B 79  ? 1.0232 1.0543 1.1735 0.0519  -0.1901 -0.0706 79   ILE   B CB  
3243  C  CG1 . ILE   B 79  ? 1.0055 1.0244 1.1408 0.0586  -0.1953 -0.0717 79   ILE   B CG1 
3244  C  CG2 . ILE   B 79  ? 1.0320 1.0711 1.1943 0.0443  -0.1838 -0.0677 79   ILE   B CG2 
3245  C  CD1 . ILE   B 79  ? 0.9887 1.0063 1.1099 0.0605  -0.1885 -0.0665 79   ILE   B CD1 
3246  N  N   . LEU   B 80  ? 0.9709 1.0241 1.1232 0.0433  -0.1691 -0.0602 80   LEU   B N   
3247  C  CA  . LEU   B 80  ? 0.9482 1.0121 1.1127 0.0364  -0.1627 -0.0580 80   LEU   B CA  
3248  C  C   . LEU   B 80  ? 0.9839 1.0507 1.1529 0.0318  -0.1582 -0.0551 80   LEU   B C   
3249  O  O   . LEU   B 80  ? 1.0057 1.0693 1.1639 0.0340  -0.1558 -0.0521 80   LEU   B O   
3250  C  CB  . LEU   B 80  ? 0.9725 1.0411 1.1298 0.0368  -0.1565 -0.0545 80   LEU   B CB  
3251  C  CG  . LEU   B 80  ? 0.9476 1.0267 1.1143 0.0304  -0.1492 -0.0517 80   LEU   B CG  
3252  C  CD1 . LEU   B 80  ? 0.9825 1.0658 1.1665 0.0257  -0.1513 -0.0548 80   LEU   B CD1 
3253  C  CD2 . LEU   B 80  ? 0.8783 0.9604 1.0389 0.0317  -0.1458 -0.0500 80   LEU   B CD2 
3254  N  N   . THR   B 81  ? 0.9642 1.0362 1.1489 0.0258  -0.1571 -0.0560 81   THR   B N   
3255  C  CA  . THR   B 81  ? 0.9435 1.0176 1.1326 0.0213  -0.1526 -0.0532 81   THR   B CA  
3256  C  C   . THR   B 81  ? 0.9863 1.0688 1.1769 0.0166  -0.1436 -0.0486 81   THR   B C   
3257  O  O   . THR   B 81  ? 0.9727 1.0596 1.1612 0.0168  -0.1408 -0.0476 81   THR   B O   
3258  C  CB  . THR   B 81  ? 0.9425 1.0167 1.1475 0.0172  -0.1558 -0.0565 81   THR   B CB  
3259  O  OG1 . THR   B 81  ? 0.9115 0.9941 1.1301 0.0116  -0.1514 -0.0561 81   THR   B OG1 
3260  C  CG2 . THR   B 81  ? 0.9654 1.0328 1.1724 0.0214  -0.1657 -0.0621 81   THR   B CG2 
3261  N  N   . ALA   B 82  ? 1.0519 1.1362 1.2457 0.0126  -0.1391 -0.0459 82   ALA   B N   
3262  C  CA  . ALA   B 82  ? 1.0425 1.1335 1.2362 0.0086  -0.1310 -0.0415 82   ALA   B CA  
3263  C  C   . ALA   B 82  ? 1.0519 1.1495 1.2590 0.0035  -0.1281 -0.0423 82   ALA   B C   
3264  O  O   . ALA   B 82  ? 1.0596 1.1628 1.2657 0.0014  -0.1226 -0.0396 82   ALA   B O   
3265  C  CB  . ALA   B 82  ? 1.0609 1.1508 1.2523 0.0064  -0.1273 -0.0383 82   ALA   B CB  
3266  N  N   . LYS   B 83  ? 0.9817 1.0787 1.2019 0.0015  -0.1318 -0.0460 83   LYS   B N   
3267  C  CA  . LYS   B 83  ? 0.9344 1.0374 1.1682 -0.0027 -0.1295 -0.0472 83   LYS   B CA  
3268  C  C   . LYS   B 83  ? 0.9637 1.0680 1.1987 0.0002  -0.1336 -0.0504 83   LYS   B C   
3269  O  O   . LYS   B 83  ? 0.9329 1.0410 1.1810 -0.0023 -0.1342 -0.0529 83   LYS   B O   
3270  C  CB  . LYS   B 83  ? 0.9696 1.0719 1.2183 -0.0066 -0.1308 -0.0495 83   LYS   B CB  
3271  C  CG  . LYS   B 83  ? 1.0172 1.1182 1.2655 -0.0100 -0.1259 -0.0462 83   LYS   B CG  
3272  C  CD  . LYS   B 83  ? 0.9844 1.0889 1.2488 -0.0160 -0.1219 -0.0465 83   LYS   B CD  
3273  C  CE  . LYS   B 83  ? 0.9340 1.0342 1.2016 -0.0185 -0.1210 -0.0457 83   LYS   B CE  
3274  N  NZ  . LYS   B 83  ? 0.9355 1.0387 1.2207 -0.0238 -0.1181 -0.0469 83   LYS   B NZ  
3275  N  N   . TYR   B 84  ? 0.9738 1.0746 1.1952 0.0057  -0.1364 -0.0503 84   TYR   B N   
3276  C  CA  . TYR   B 84  ? 0.9439 1.0451 1.1623 0.0092  -0.1395 -0.0524 84   TYR   B CA  
3277  C  C   . TYR   B 84  ? 0.9608 1.0577 1.1856 0.0121  -0.1482 -0.0580 84   TYR   B C   
3278  O  O   . TYR   B 84  ? 1.0275 1.1251 1.2533 0.0143  -0.1513 -0.0605 84   TYR   B O   
3279  C  CB  . TYR   B 84  ? 0.9913 1.1002 1.2152 0.0057  -0.1337 -0.0509 84   TYR   B CB  
3280  C  CG  . TYR   B 84  ? 1.0147 1.1267 1.2293 0.0041  -0.1262 -0.0456 84   TYR   B CG  
3281  C  CD1 . TYR   B 84  ? 1.0474 1.1569 1.2472 0.0083  -0.1260 -0.0435 84   TYR   B CD1 
3282  C  CD2 . TYR   B 84  ? 1.0144 1.1311 1.2346 -0.0014 -0.1196 -0.0426 84   TYR   B CD2 
3283  C  CE1 . TYR   B 84  ? 1.0248 1.1372 1.2169 0.0070  -0.1196 -0.0388 84   TYR   B CE1 
3284  C  CE2 . TYR   B 84  ? 1.0473 1.1663 1.2586 -0.0025 -0.1135 -0.0380 84   TYR   B CE2 
3285  C  CZ  . TYR   B 84  ? 1.0345 1.1517 1.2324 0.0016  -0.1137 -0.0362 84   TYR   B CZ  
3286  O  OH  . TYR   B 84  ? 1.0086 1.1282 1.1988 0.0006  -0.1083 -0.0318 84   TYR   B OH  
3287  N  N   . ASN   B 85  ? 0.9466 1.0386 1.1751 0.0124  -0.1529 -0.0602 85   ASN   B N   
3288  C  CA  . ASN   B 85  ? 0.9714 1.0582 1.2050 0.0156  -0.1623 -0.0657 85   ASN   B CA  
3289  C  C   . ASN   B 85  ? 0.9692 1.0481 1.1860 0.0231  -0.1676 -0.0668 85   ASN   B C   
3290  O  O   . ASN   B 85  ? 0.9634 1.0365 1.1681 0.0261  -0.1679 -0.0651 85   ASN   B O   
3291  C  CB  . ASN   B 85  ? 0.9536 1.0373 1.1963 0.0134  -0.1654 -0.0676 85   ASN   B CB  
3292  C  CG  . ASN   B 85  ? 0.9258 1.0162 1.1825 0.0061  -0.1586 -0.0655 85   ASN   B CG  
3293  O  OD1 . ASN   B 85  ? 0.9341 1.0242 1.1869 0.0037  -0.1535 -0.0618 85   ASN   B OD1 
3294  N  ND2 . ASN   B 85  ? 0.8983 0.9944 1.1710 0.0027  -0.1583 -0.0677 85   ASN   B ND2 
3295  N  N   . ALA   B 86  ? 1.0122 1.0904 1.2276 0.0265  -0.1715 -0.0695 86   ALA   B N   
3296  C  CA  . ALA   B 86  ? 1.0215 1.0910 1.2209 0.0340  -0.1769 -0.0709 86   ALA   B CA  
3297  C  C   . ALA   B 86  ? 1.0305 1.0933 1.2348 0.0375  -0.1876 -0.0770 86   ALA   B C   
3298  O  O   . ALA   B 86  ? 1.0353 1.1018 1.2562 0.0345  -0.1909 -0.0805 86   ALA   B O   
3299  C  CB  . ALA   B 86  ? 1.0482 1.1198 1.2399 0.0364  -0.1743 -0.0697 86   ALA   B CB  
3300  N  N   . CYS   B 87  ? 1.0390 1.0915 1.2288 0.0440  -0.1930 -0.0782 87   CYS   B N   
3301  C  CA  . CYS   B 87  ? 1.1135 1.1581 1.3057 0.0481  -0.2040 -0.0842 87   CYS   B CA  
3302  C  C   . CYS   B 87  ? 1.0979 1.1304 1.2690 0.0565  -0.2086 -0.0848 87   CYS   B C   
3303  O  O   . CYS   B 87  ? 1.0532 1.0828 1.2109 0.0582  -0.2039 -0.0808 87   CYS   B O   
3304  C  CB  . CYS   B 87  ? 1.1040 1.1479 1.3094 0.0445  -0.2075 -0.0865 87   CYS   B CB  
3305  S  SG  . CYS   B 87  ? 1.0635 1.1011 1.2563 0.0456  -0.2052 -0.0831 87   CYS   B SG  
3306  N  N   . ILE   B 88  ? 1.1390 1.1644 1.3076 0.0619  -0.2178 -0.0898 88   ILE   B N   
3307  C  CA  . ILE   B 88  ? 1.1312 1.1436 1.2799 0.0706  -0.2234 -0.0912 88   ILE   B CA  
3308  C  C   . ILE   B 88  ? 1.2015 1.2050 1.3532 0.0732  -0.2340 -0.0966 88   ILE   B C   
3309  O  O   . ILE   B 88  ? 1.2092 1.2143 1.3763 0.0715  -0.2410 -0.1015 88   ILE   B O   
3310  C  CB  . ILE   B 88  ? 1.0767 1.0858 1.2169 0.0757  -0.2259 -0.0928 88   ILE   B CB  
3311  C  CG1 . ILE   B 88  ? 1.0692 1.0883 1.2100 0.0720  -0.2158 -0.0881 88   ILE   B CG1 
3312  C  CG2 . ILE   B 88  ? 1.1011 1.0965 1.2183 0.0846  -0.2294 -0.0930 88   ILE   B CG2 
3313  C  CD1 . ILE   B 88  ? 0.9556 0.9712 1.0857 0.0772  -0.2168 -0.0887 88   ILE   B CD1 
3314  N  N   . LEU   B 89  ? 1.1995 1.1936 1.3366 0.0775  -0.2353 -0.0956 89   LEU   B N   
3315  C  CA  . LEU   B 89  ? 1.1837 1.1690 1.3224 0.0795  -0.2443 -0.0999 89   LEU   B CA  
3316  C  C   . LEU   B 89  ? 1.2031 1.1730 1.3215 0.0894  -0.2523 -0.1028 89   LEU   B C   
3317  O  O   . LEU   B 89  ? 1.1746 1.1397 1.2740 0.0946  -0.2480 -0.0996 89   LEU   B O   
3318  C  CB  . LEU   B 89  ? 1.1846 1.1714 1.3237 0.0759  -0.2389 -0.0963 89   LEU   B CB  
3319  C  CG  . LEU   B 89  ? 1.1245 1.1256 1.2792 0.0668  -0.2292 -0.0922 89   LEU   B CG  
3320  C  CD1 . LEU   B 89  ? 1.0603 1.0615 1.2118 0.0643  -0.2237 -0.0883 89   LEU   B CD1 
3321  C  CD2 . LEU   B 89  ? 1.1493 1.1574 1.3278 0.0609  -0.2331 -0.0961 89   LEU   B CD2 
3322  N  N   . GLU   B 90  ? 1.2695 1.2315 1.3924 0.0921  -0.2639 -0.1090 90   GLU   B N   
3323  C  CA  . GLU   B 90  ? 1.2731 1.2189 1.3776 0.1016  -0.2732 -0.1127 90   GLU   B CA  
3324  C  C   . GLU   B 90  ? 1.3077 1.2459 1.4145 0.1021  -0.2804 -0.1158 90   GLU   B C   
3325  O  O   . GLU   B 90  ? 1.3611 1.3056 1.4885 0.0958  -0.2830 -0.1181 90   GLU   B O   
3326  C  CB  . GLU   B 90  ? 1.3002 1.2420 1.4069 0.1057  -0.2827 -0.1183 90   GLU   B CB  
3327  C  CG  . GLU   B 90  ? 1.3932 1.3169 1.4775 0.1166  -0.2919 -0.1218 90   GLU   B CG  
3328  C  CD  . GLU   B 90  ? 1.3804 1.2984 1.4704 0.1204  -0.3049 -0.1292 90   GLU   B CD  
3329  O  OE1 . GLU   B 90  ? 1.3148 1.2435 1.4222 0.1158  -0.3047 -0.1305 90   GLU   B OE1 
3330  O  OE2 . GLU   B 90  ? 1.4682 1.3710 1.5452 0.1282  -0.3155 -0.1337 90   GLU   B OE2 
3331  N  N   . TYR   B 91  ? 1.3271 1.2511 1.4124 0.1099  -0.2836 -0.1159 91   TYR   B N   
3332  C  CA  . TYR   B 91  ? 1.4114 1.3260 1.4952 0.1115  -0.2906 -0.1188 91   TYR   B CA  
3333  C  C   . TYR   B 91  ? 1.5087 1.4119 1.5927 0.1169  -0.3056 -0.1266 91   TYR   B C   
3334  O  O   . TYR   B 91  ? 1.5307 1.4258 1.6014 0.1240  -0.3103 -0.1288 91   TYR   B O   
3335  C  CB  . TYR   B 91  ? 1.3610 1.2658 1.4210 0.1174  -0.2860 -0.1148 91   TYR   B CB  
3336  C  CG  . TYR   B 91  ? 1.3851 1.2793 1.4402 0.1197  -0.2921 -0.1171 91   TYR   B CG  
3337  C  CD1 . TYR   B 91  ? 1.5254 1.4040 1.5704 0.1273  -0.3047 -0.1230 91   TYR   B CD1 
3338  C  CD2 . TYR   B 91  ? 1.3763 1.2752 1.4356 0.1148  -0.2855 -0.1132 91   TYR   B CD2 
3339  C  CE1 . TYR   B 91  ? 1.6067 1.4746 1.6464 0.1297  -0.3107 -0.1253 91   TYR   B CE1 
3340  C  CE2 . TYR   B 91  ? 1.4145 1.3029 1.4687 0.1172  -0.2912 -0.1153 91   TYR   B CE2 
3341  C  CZ  . TYR   B 91  ? 1.5430 1.4159 1.5874 0.1246  -0.3039 -0.1214 91   TYR   B CZ  
3342  O  OH  . TYR   B 91  ? 1.5445 1.4062 1.5833 0.1273  -0.3102 -0.1237 91   TYR   B OH  
3343  N  N   . LYS   B 92  ? 1.7464 1.6487 1.8456 0.1136  -0.3132 -0.1309 92   LYS   B N   
3344  C  CA  . LYS   B 92  ? 1.8365 1.7296 1.9400 0.1177  -0.3282 -0.1388 92   LYS   B CA  
3345  C  C   . LYS   B 92  ? 1.8996 1.7867 2.0107 0.1162  -0.3356 -0.1423 92   LYS   B C   
3346  O  O   . LYS   B 92  ? 1.9010 1.7985 2.0346 0.1075  -0.3334 -0.1422 92   LYS   B O   
3347  C  CB  . LYS   B 92  ? 1.7886 1.6927 1.9140 0.1131  -0.3309 -0.1419 92   LYS   B CB  
3348  N  N   . GLN   B 93  ? 1.8295 1.6991 1.9215 0.1248  -0.3446 -0.1456 93   GLN   B N   
3349  C  CA  . GLN   B 93  ? 1.7935 1.6541 1.8870 0.1251  -0.3522 -0.1489 93   GLN   B CA  
3350  C  C   . GLN   B 93  ? 1.8183 1.6651 1.9096 0.1317  -0.3690 -0.1572 93   GLN   B C   
3351  O  O   . GLN   B 93  ? 1.8747 1.7089 1.9447 0.1411  -0.3741 -0.1590 93   GLN   B O   
3352  C  CB  . GLN   B 93  ? 1.7976 1.6484 1.8672 0.1300  -0.3468 -0.1445 93   GLN   B CB  
3353  C  CG  . GLN   B 93  ? 1.8033 1.6388 1.8656 0.1344  -0.3574 -0.1490 93   GLN   B CG  
3354  C  CD  . GLN   B 93  ? 1.9187 1.7452 1.9575 0.1393  -0.3511 -0.1443 93   GLN   B CD  
3355  O  OE1 . GLN   B 93  ? 1.9305 1.7607 1.9563 0.1408  -0.3399 -0.1383 93   GLN   B OE1 
3356  N  NE2 . GLN   B 93  ? 1.9565 1.7712 1.9901 0.1418  -0.3582 -0.1472 93   GLN   B NE2 
3357  N  N   . SER   B 94  ? 1.7878 1.6360 1.9003 0.1270  -0.3776 -0.1623 94   SER   B N   
3358  C  CA  . SER   B 94  ? 1.7962 1.6320 1.9097 0.1326  -0.3946 -0.1708 94   SER   B CA  
3359  C  C   . SER   B 94  ? 1.8294 1.6508 1.9333 0.1358  -0.4016 -0.1732 94   SER   B C   
3360  O  O   . SER   B 94  ? 1.8579 1.6827 1.9811 0.1295  -0.4049 -0.1754 94   SER   B O   
3361  C  CB  . SER   B 94  ? 1.7691 1.6163 1.9145 0.1254  -0.4004 -0.1755 94   SER   B CB  
3362  O  OG  . SER   B 94  ? 1.6499 1.4850 1.7974 0.1306  -0.4175 -0.1840 94   SER   B OG  
3363  N  N   . GLY   B 95  ? 1.8461 1.6512 1.9199 0.1458  -0.4035 -0.1726 95   GLY   B N   
3364  C  CA  . GLY   B 95  ? 1.8438 1.6348 1.9052 0.1496  -0.4088 -0.1741 95   GLY   B CA  
3365  C  C   . GLY   B 95  ? 1.8785 1.6785 1.9471 0.1419  -0.3970 -0.1681 95   GLY   B C   
3366  O  O   . GLY   B 95  ? 1.8768 1.6745 1.9263 0.1447  -0.3872 -0.1622 95   GLY   B O   
3367  N  N   . GLU   B 96  ? 1.8361 1.6470 1.9327 0.1323  -0.3977 -0.1695 96   GLU   B N   
3368  C  CA  . GLU   B 96  ? 1.8353 1.6542 1.9402 0.1247  -0.3874 -0.1643 96   GLU   B CA  
3369  C  C   . GLU   B 96  ? 1.7652 1.6051 1.8951 0.1138  -0.3765 -0.1603 96   GLU   B C   
3370  O  O   . GLU   B 96  ? 1.6863 1.5338 1.8252 0.1068  -0.3679 -0.1560 96   GLU   B O   
3371  C  CB  . GLU   B 96  ? 1.8342 1.6446 1.9477 0.1231  -0.3970 -0.1689 96   GLU   B CB  
3372  N  N   . SER   B 97  ? 1.7740 1.6231 1.9145 0.1123  -0.3765 -0.1614 97   SER   B N   
3373  C  CA  . SER   B 97  ? 1.7461 1.6145 1.9117 0.1022  -0.3675 -0.1586 97   SER   B CA  
3374  C  C   . SER   B 97  ? 1.7527 1.6295 1.9072 0.1028  -0.3551 -0.1522 97   SER   B C   
3375  O  O   . SER   B 97  ? 1.7970 1.6733 1.9458 0.1072  -0.3576 -0.1537 97   SER   B O   
3376  C  CB  . SER   B 97  ? 1.7078 1.5808 1.8969 0.0995  -0.3774 -0.1651 97   SER   B CB  
3377  O  OG  . SER   B 97  ? 1.6989 1.5606 1.8933 0.1017  -0.3916 -0.1721 97   SER   B OG  
3378  N  N   . ILE   B 98  ? 1.7974 1.6818 1.9495 0.0983  -0.3418 -0.1451 98   ILE   B N   
3379  C  CA  . ILE   B 98  ? 1.7902 1.6826 1.9317 0.0984  -0.3294 -0.1386 98   ILE   B CA  
3380  C  C   . ILE   B 98  ? 1.8114 1.7222 1.9761 0.0888  -0.3206 -0.1359 98   ILE   B C   
3381  O  O   . ILE   B 98  ? 1.7578 1.6761 1.9405 0.0809  -0.3170 -0.1348 98   ILE   B O   
3382  C  CB  . ILE   B 98  ? 1.6814 1.5703 1.8042 0.1003  -0.3203 -0.1325 98   ILE   B CB  
3383  C  CG1 . ILE   B 98  ? 1.7397 1.6098 1.8396 0.1098  -0.3285 -0.1352 98   ILE   B CG1 
3384  C  CG2 . ILE   B 98  ? 1.6431 1.5388 1.7543 0.1014  -0.3089 -0.1265 98   ILE   B CG2 
3385  C  CD1 . ILE   B 98  ? 1.6290 1.4955 1.7078 0.1131  -0.3189 -0.1289 98   ILE   B CD1 
3386  N  N   . ASP   B 99  ? 1.9810 1.8984 2.1442 0.0896  -0.3167 -0.1345 99   ASP   B N   
3387  C  CA  . ASP   B 99  ? 1.9821 1.9164 2.1651 0.0813  -0.3081 -0.1317 99   ASP   B CA  
3388  C  C   . ASP   B 99  ? 1.9550 1.8948 2.1260 0.0834  -0.2994 -0.1271 99   ASP   B C   
3389  O  O   . ASP   B 99  ? 1.9529 1.8852 2.1094 0.0908  -0.3044 -0.1292 99   ASP   B O   
3390  C  CB  . ASP   B 99  ? 2.0208 1.9596 2.2276 0.0780  -0.3167 -0.1378 99   ASP   B CB  
3391  C  CG  . ASP   B 99  ? 2.1108 2.0626 2.3439 0.0675  -0.3108 -0.1365 99   ASP   B CG  
3392  O  OD1 . ASP   B 99  ? 2.0802 2.0418 2.3144 0.0623  -0.2980 -0.1301 99   ASP   B OD1 
3393  O  OD2 . ASP   B 99  ? 2.1082 2.0598 2.3606 0.0645  -0.3189 -0.1416 99   ASP   B OD2 
3394  N  N   . ILE   B 100 ? 1.7143 1.6665 1.8912 0.0769  -0.2868 -0.1211 100  ILE   B N   
3395  C  CA  . ILE   B 100 ? 1.5461 1.5045 1.7129 0.0777  -0.2774 -0.1161 100  ILE   B CA  
3396  C  C   . ILE   B 100 ? 1.5150 1.4848 1.7003 0.0732  -0.2766 -0.1176 100  ILE   B C   
3397  O  O   . ILE   B 100 ? 1.4784 1.4602 1.6816 0.0650  -0.2699 -0.1155 100  ILE   B O   
3398  C  CB  . ILE   B 100 ? 1.4576 1.4226 1.6199 0.0736  -0.2647 -0.1089 100  ILE   B CB  
3399  C  CG1 . ILE   B 100 ? 1.4588 1.4125 1.6018 0.0788  -0.2651 -0.1073 100  ILE   B CG1 
3400  C  CG2 . ILE   B 100 ? 1.3538 1.3262 1.5086 0.0738  -0.2554 -0.1042 100  ILE   B CG2 
3401  C  CD1 . ILE   B 100 ? 1.3991 1.3429 1.5176 0.0882  -0.2663 -0.1067 100  ILE   B CD1 
3402  N  N   . ILE   B 101 ? 1.4460 1.4116 1.6260 0.0786  -0.2832 -0.1213 101  ILE   B N   
3403  C  CA  . ILE   B 101 ? 1.3795 1.3545 1.5773 0.0752  -0.2843 -0.1237 101  ILE   B CA  
3404  C  C   . ILE   B 101 ? 1.3360 1.3213 1.5310 0.0725  -0.2726 -0.1180 101  ILE   B C   
3405  O  O   . ILE   B 101 ? 1.3460 1.3278 1.5210 0.0766  -0.2671 -0.1139 101  ILE   B O   
3406  C  CB  . ILE   B 101 ? 1.3620 1.3279 1.5554 0.0824  -0.2969 -0.1301 101  ILE   B CB  
3407  C  CG1 . ILE   B 101 ? 1.3847 1.3432 1.5527 0.0903  -0.2950 -0.1279 101  ILE   B CG1 
3408  C  CG2 . ILE   B 101 ? 1.4610 1.4146 1.6531 0.0862  -0.3089 -0.1355 101  ILE   B CG2 
3409  C  CD1 . ILE   B 101 ? 1.4902 1.4399 1.6521 0.0976  -0.3060 -0.1336 101  ILE   B CD1 
3410  N  N   . THR   B 102 ? 1.4546 1.4526 1.6703 0.0657  -0.2687 -0.1179 102  THR   B N   
3411  C  CA  . THR   B 102 ? 1.4111 1.4197 1.6269 0.0623  -0.2577 -0.1129 102  THR   B CA  
3412  C  C   . THR   B 102 ? 1.3985 1.4071 1.6133 0.0662  -0.2620 -0.1158 102  THR   B C   
3413  O  O   . THR   B 102 ? 1.4052 1.4201 1.6389 0.0632  -0.2655 -0.1194 102  THR   B O   
3414  C  CB  . THR   B 102 ? 1.4032 1.4249 1.6407 0.0527  -0.2500 -0.1106 102  THR   B CB  
3415  O  OG1 . THR   B 102 ? 1.4500 1.4695 1.6912 0.0496  -0.2496 -0.1098 102  THR   B OG1 
3416  C  CG2 . THR   B 102 ? 1.3594 1.3899 1.5918 0.0495  -0.2375 -0.1041 102  THR   B CG2 
3417  N  N   . ARG   B 103 ? 1.3153 1.3168 1.5082 0.0729  -0.2615 -0.1142 103  ARG   B N   
3418  C  CA  . ARG   B 103 ? 1.2739 1.2743 1.4630 0.0772  -0.2649 -0.1165 103  ARG   B CA  
3419  C  C   . ARG   B 103 ? 1.2499 1.2636 1.4491 0.0716  -0.2558 -0.1133 103  ARG   B C   
3420  O  O   . ARG   B 103 ? 1.2803 1.2960 1.4851 0.0730  -0.2593 -0.1162 103  ARG   B O   
3421  C  CB  . ARG   B 103 ? 1.2447 1.2328 1.4063 0.0860  -0.2659 -0.1152 103  ARG   B CB  
3422  C  CG  . ARG   B 103 ? 1.2679 1.2412 1.4171 0.0926  -0.2754 -0.1187 103  ARG   B CG  
3423  C  CD  . ARG   B 103 ? 1.3358 1.2988 1.4800 0.1000  -0.2879 -0.1252 103  ARG   B CD  
3424  N  NE  . ARG   B 103 ? 1.3253 1.2851 1.4537 0.1053  -0.2855 -0.1236 103  ARG   B NE  
3425  C  CZ  . ARG   B 103 ? 1.3416 1.2885 1.4447 0.1135  -0.2862 -0.1225 103  ARG   B CZ  
3426  N  NH1 . ARG   B 103 ? 1.3984 1.3339 1.4881 0.1179  -0.2896 -0.1229 103  ARG   B NH1 
3427  N  NH2 . ARG   B 103 ? 1.3076 1.2525 1.3981 0.1174  -0.2830 -0.1208 103  ARG   B NH2 
3428  N  N   . ALA   B 104 ? 1.2676 1.2899 1.4692 0.0656  -0.2445 -0.1074 104  ALA   B N   
3429  C  CA  . ALA   B 104 ? 1.2615 1.2958 1.4710 0.0605  -0.2353 -0.1040 104  ALA   B CA  
3430  C  C   . ALA   B 104 ? 1.2364 1.2796 1.4547 0.0527  -0.2256 -0.0992 104  ALA   B C   
3431  O  O   . ALA   B 104 ? 1.2559 1.2953 1.4646 0.0531  -0.2228 -0.0963 104  ALA   B O   
3432  C  CB  . ALA   B 104 ? 1.2661 1.2981 1.4566 0.0647  -0.2304 -0.1005 104  ALA   B CB  
3433  N  N   . HIS   B 105 ? 1.2707 1.3252 1.5065 0.0462  -0.2204 -0.0984 105  HIS   B N   
3434  C  CA  . HIS   B 105 ? 1.2660 1.3287 1.5104 0.0388  -0.2110 -0.0940 105  HIS   B CA  
3435  C  C   . HIS   B 105 ? 1.3159 1.3895 1.5690 0.0342  -0.2032 -0.0916 105  HIS   B C   
3436  O  O   . HIS   B 105 ? 1.3307 1.4062 1.5885 0.0358  -0.2063 -0.0944 105  HIS   B O   
3437  C  CB  . HIS   B 105 ? 1.2674 1.3314 1.5299 0.0345  -0.2145 -0.0968 105  HIS   B CB  
3438  C  CG  . HIS   B 105 ? 1.3336 1.4034 1.6173 0.0318  -0.2183 -0.1012 105  HIS   B CG  
3439  N  ND1 . HIS   B 105 ? 1.3509 1.4310 1.6535 0.0244  -0.2118 -0.0999 105  HIS   B ND1 
3440  C  CD2 . HIS   B 105 ? 1.3865 1.4534 1.6749 0.0358  -0.2278 -0.1068 105  HIS   B CD2 
3441  C  CE1 . HIS   B 105 ? 1.3883 1.4719 1.7073 0.0238  -0.2169 -0.1045 105  HIS   B CE1 
3442  N  NE2 . HIS   B 105 ? 1.4437 1.5196 1.7548 0.0307  -0.2269 -0.1089 105  HIS   B NE2 
3443  N  N   . GLY   B 106 ? 1.2033 1.2834 1.4580 0.0287  -0.1933 -0.0865 106  GLY   B N   
3444  C  CA  . GLY   B 106 ? 1.1390 1.2287 1.4006 0.0243  -0.1853 -0.0837 106  GLY   B CA  
3445  C  C   . GLY   B 106 ? 1.1273 1.2208 1.3821 0.0205  -0.1751 -0.0775 106  GLY   B C   
3446  O  O   . GLY   B 106 ? 1.1439 1.2321 1.3848 0.0229  -0.1744 -0.0751 106  GLY   B O   
3447  N  N   . ASN   B 107 ? 1.1001 1.2024 1.3643 0.0150  -0.1674 -0.0750 107  ASN   B N   
3448  C  CA  . ASN   B 107 ? 1.0208 1.1268 1.2804 0.0109  -0.1580 -0.0694 107  ASN   B CA  
3449  C  C   . ASN   B 107 ? 1.0365 1.1459 1.2861 0.0116  -0.1523 -0.0661 107  ASN   B C   
3450  O  O   . ASN   B 107 ? 1.0588 1.1745 1.3167 0.0088  -0.1488 -0.0660 107  ASN   B O   
3451  C  CB  . ASN   B 107 ? 0.9809 1.0932 1.2575 0.0041  -0.1530 -0.0687 107  ASN   B CB  
3452  C  CG  . ASN   B 107 ? 0.9925 1.1061 1.2638 0.0005  -0.1452 -0.0636 107  ASN   B CG  
3453  O  OD1 . ASN   B 107 ? 1.0279 1.1451 1.2921 -0.0008 -0.1385 -0.0596 107  ASN   B OD1 
3454  N  ND2 . ASN   B 107 ? 1.0003 1.1105 1.2745 -0.0008 -0.1464 -0.0636 107  ASN   B ND2 
3455  N  N   . VAL   B 108 ? 1.0367 1.1420 1.2691 0.0150  -0.1510 -0.0632 108  VAL   B N   
3456  C  CA  . VAL   B 108 ? 1.0536 1.1612 1.2760 0.0162  -0.1465 -0.0603 108  VAL   B CA  
3457  C  C   . VAL   B 108 ? 1.1346 1.2492 1.3590 0.0107  -0.1372 -0.0557 108  VAL   B C   
3458  O  O   . VAL   B 108 ? 1.1852 1.3018 1.4010 0.0111  -0.1328 -0.0527 108  VAL   B O   
3459  C  CB  . VAL   B 108 ? 0.9989 1.0995 1.2028 0.0220  -0.1482 -0.0588 108  VAL   B CB  
3460  C  CG1 . VAL   B 108 ? 1.0286 1.1219 1.2289 0.0280  -0.1571 -0.0635 108  VAL   B CG1 
3461  C  CG2 . VAL   B 108 ? 0.9949 1.0927 1.1931 0.0217  -0.1465 -0.0562 108  VAL   B CG2 
3462  N  N   . GLN   B 109 ? 1.2489 1.3670 1.4845 0.0056  -0.1341 -0.0550 109  GLN   B N   
3463  C  CA  . GLN   B 109 ? 1.2920 1.4162 1.5299 0.0005  -0.1255 -0.0510 109  GLN   B CA  
3464  C  C   . GLN   B 109 ? 1.3343 1.4637 1.5761 -0.0006 -0.1229 -0.0513 109  GLN   B C   
3465  O  O   . GLN   B 109 ? 1.3588 1.4893 1.6103 -0.0001 -0.1266 -0.0551 109  GLN   B O   
3466  C  CB  . GLN   B 109 ? 1.3135 1.4397 1.5641 -0.0045 -0.1230 -0.0509 109  GLN   B CB  
3467  C  CG  . GLN   B 109 ? 1.3798 1.5121 1.6363 -0.0100 -0.1147 -0.0479 109  GLN   B CG  
3468  C  CD  . GLN   B 109 ? 1.4581 1.5903 1.7036 -0.0114 -0.1087 -0.0428 109  GLN   B CD  
3469  O  OE1 . GLN   B 109 ? 1.4771 1.6117 1.7147 -0.0113 -0.1050 -0.0402 109  GLN   B OE1 
3470  N  NE2 . GLN   B 109 ? 1.4291 1.5586 1.6745 -0.0128 -0.1080 -0.0415 109  GLN   B NE2 
3471  N  N   . ASP   B 110 ? 1.2069 1.3392 1.4410 -0.0020 -0.1166 -0.0473 110  ASP   B N   
3472  C  CA  . ASP   B 110 ? 1.1844 1.3217 1.4212 -0.0038 -0.1127 -0.0467 110  ASP   B CA  
3473  C  C   . ASP   B 110 ? 1.2255 1.3673 1.4684 -0.0095 -0.1053 -0.0438 110  ASP   B C   
3474  O  O   . ASP   B 110 ? 1.2453 1.3867 1.4811 -0.0110 -0.1013 -0.0401 110  ASP   B O   
3475  C  CB  . ASP   B 110 ? 1.1878 1.3243 1.4106 -0.0011 -0.1112 -0.0443 110  ASP   B CB  
3476  C  CG  . ASP   B 110 ? 1.1662 1.2974 1.3814 0.0048  -0.1177 -0.0469 110  ASP   B CG  
3477  O  OD1 . ASP   B 110 ? 1.1845 1.3154 1.4062 0.0065  -0.1221 -0.0507 110  ASP   B OD1 
3478  O  OD2 . ASP   B 110 ? 1.1623 1.2894 1.3649 0.0080  -0.1181 -0.0450 110  ASP   B OD2 
3479  N  N   . ARG   B 111 ? 1.2582 1.4041 1.5139 -0.0125 -0.1034 -0.0454 111  ARG   B N   
3480  C  CA  . ARG   B 111 ? 1.2323 1.3818 1.4942 -0.0176 -0.0961 -0.0430 111  ARG   B CA  
3481  C  C   . ARG   B 111 ? 1.2169 1.3670 1.4667 -0.0188 -0.0904 -0.0383 111  ARG   B C   
3482  O  O   . ARG   B 111 ? 1.2454 1.3946 1.4920 -0.0210 -0.0868 -0.0354 111  ARG   B O   
3483  C  CB  . ARG   B 111 ? 1.1761 1.3300 1.4508 -0.0196 -0.0943 -0.0451 111  ARG   B CB  
3484  N  N   . ILE   B 112 ? 1.1949 1.3460 1.4374 -0.0170 -0.0901 -0.0378 112  ILE   B N   
3485  C  CA  . ILE   B 112 ? 1.2409 1.3925 1.4719 -0.0177 -0.0856 -0.0337 112  ILE   B CA  
3486  C  C   . ILE   B 112 ? 1.2311 1.3794 1.4501 -0.0140 -0.0888 -0.0326 112  ILE   B C   
3487  O  O   . ILE   B 112 ? 1.2468 1.3927 1.4633 -0.0100 -0.0940 -0.0349 112  ILE   B O   
3488  C  CB  . ILE   B 112 ? 1.2397 1.3943 1.4699 -0.0183 -0.0828 -0.0334 112  ILE   B CB  
3489  C  CG1 . ILE   B 112 ? 1.2295 1.3842 1.4476 -0.0188 -0.0791 -0.0294 112  ILE   B CG1 
3490  C  CG2 . ILE   B 112 ? 1.2402 1.3943 1.4715 -0.0146 -0.0881 -0.0369 112  ILE   B CG2 
3491  C  CD1 . ILE   B 112 ? 1.2538 1.4087 1.4704 -0.0223 -0.0741 -0.0261 112  ILE   B CD1 
3492  N  N   . GLY   B 113 ? 1.2587 1.4065 1.4698 -0.0150 -0.0857 -0.0289 113  GLY   B N   
3493  C  CA  . GLY   B 113 ? 1.2283 1.3735 1.4282 -0.0116 -0.0877 -0.0274 113  GLY   B CA  
3494  C  C   . GLY   B 113 ? 1.3487 1.4935 1.5430 -0.0132 -0.0844 -0.0237 113  GLY   B C   
3495  O  O   . GLY   B 113 ? 1.3827 1.5277 1.5818 -0.0162 -0.0820 -0.0229 113  GLY   B O   
3496  N  N   . ARG   B 114 ? 1.4842 1.6284 1.6685 -0.0111 -0.0841 -0.0214 114  ARG   B N   
3497  C  CA  . ARG   B 114 ? 1.5376 1.6813 1.7163 -0.0118 -0.0819 -0.0181 114  ARG   B CA  
3498  C  C   . ARG   B 114 ? 1.4796 1.6193 1.6540 -0.0080 -0.0857 -0.0186 114  ARG   B C   
3499  O  O   . ARG   B 114 ? 1.4753 1.6135 1.6432 -0.0042 -0.0877 -0.0187 114  ARG   B O   
3500  C  CB  . ARG   B 114 ? 1.5486 1.6946 1.7202 -0.0122 -0.0787 -0.0150 114  ARG   B CB  
3501  C  CG  . ARG   B 114 ? 1.5271 1.6740 1.6956 -0.0147 -0.0752 -0.0116 114  ARG   B CG  
3502  C  CD  . ARG   B 114 ? 1.6385 1.7854 1.8130 -0.0185 -0.0726 -0.0115 114  ARG   B CD  
3503  N  NE  . ARG   B 114 ? 1.7173 1.8660 1.8987 -0.0209 -0.0710 -0.0133 114  ARG   B NE  
3504  C  CZ  . ARG   B 114 ? 1.6900 1.8406 1.8710 -0.0236 -0.0671 -0.0119 114  ARG   B CZ  
3505  N  NH1 . ARG   B 114 ? 1.6926 1.8436 1.8666 -0.0244 -0.0649 -0.0090 114  ARG   B NH1 
3506  N  NH2 . ARG   B 114 ? 1.6362 1.7880 1.8241 -0.0254 -0.0655 -0.0137 114  ARG   B NH2 
3507  N  N   . PRO   B 115 ? 1.2514 1.3888 1.4288 -0.0085 -0.0869 -0.0190 115  PRO   B N   
3508  C  CA  . PRO   B 115 ? 1.1486 1.2816 1.3208 -0.0047 -0.0904 -0.0193 115  PRO   B CA  
3509  C  C   . PRO   B 115 ? 1.1988 1.3319 1.3610 -0.0023 -0.0891 -0.0163 115  PRO   B C   
3510  O  O   . PRO   B 115 ? 1.2240 1.3596 1.3839 -0.0044 -0.0853 -0.0132 115  PRO   B O   
3511  C  CB  . PRO   B 115 ? 1.1414 1.2728 1.3177 -0.0071 -0.0899 -0.0189 115  PRO   B CB  
3512  C  CG  . PRO   B 115 ? 1.1933 1.3273 1.3794 -0.0114 -0.0876 -0.0200 115  PRO   B CG  
3513  C  CD  . PRO   B 115 ? 1.2808 1.4189 1.4658 -0.0127 -0.0844 -0.0189 115  PRO   B CD  
3514  N  N   . SER   B 116 ? 1.1701 1.3002 1.3264 0.0023  -0.0920 -0.0172 116  SER   B N   
3515  C  CA  . SER   B 116 ? 1.1105 1.2407 1.2580 0.0049  -0.0903 -0.0143 116  SER   B CA  
3516  C  C   . SER   B 116 ? 1.1605 1.2895 1.3047 0.0053  -0.0895 -0.0120 116  SER   B C   
3517  O  O   . SER   B 116 ? 1.1381 1.2638 1.2840 0.0057  -0.0918 -0.0133 116  SER   B O   
3518  C  CB  . SER   B 116 ? 1.0942 1.2203 1.2356 0.0101  -0.0934 -0.0158 116  SER   B CB  
3519  O  OG  . SER   B 116 ? 1.1138 1.2415 1.2557 0.0101  -0.0930 -0.0168 116  SER   B OG  
3520  N  N   . GLU   B 117 ? 1.1517 1.2833 1.2912 0.0053  -0.0863 -0.0087 117  GLU   B N   
3521  C  CA  . GLU   B 117 ? 1.1335 1.2645 1.2696 0.0060  -0.0853 -0.0062 117  GLU   B CA  
3522  C  C   . GLU   B 117 ? 1.1229 1.2485 1.2537 0.0109  -0.0884 -0.0071 117  GLU   B C   
3523  O  O   . GLU   B 117 ? 1.1422 1.2646 1.2737 0.0112  -0.0901 -0.0077 117  GLU   B O   
3524  C  CB  . GLU   B 117 ? 1.1897 1.3249 1.3227 0.0053  -0.0818 -0.0028 117  GLU   B CB  
3525  C  CG  . GLU   B 117 ? 1.2245 1.3643 1.3612 0.0012  -0.0793 -0.0023 117  GLU   B CG  
3526  C  CD  . GLU   B 117 ? 1.4036 1.5469 1.5394 -0.0011 -0.0764 0.0009  117  GLU   B CD  
3527  O  OE1 . GLU   B 117 ? 1.3465 1.4892 1.4793 0.0005  -0.0763 0.0027  117  GLU   B OE1 
3528  O  OE2 . GLU   B 117 ? 1.5067 1.6532 1.6447 -0.0044 -0.0744 0.0015  117  GLU   B OE2 
3529  N  N   . THR   B 118 ? 1.1304 1.2542 1.2554 0.0151  -0.0888 -0.0071 118  THR   B N   
3530  C  CA  . THR   B 118 ? 1.1431 1.2610 1.2616 0.0205  -0.0914 -0.0078 118  THR   B CA  
3531  C  C   . THR   B 118 ? 1.1420 1.2545 1.2624 0.0219  -0.0965 -0.0118 118  THR   B C   
3532  O  O   . THR   B 118 ? 1.1849 1.2912 1.2994 0.0265  -0.0993 -0.0129 118  THR   B O   
3533  C  CB  . THR   B 118 ? 1.1224 1.2391 1.2341 0.0245  -0.0902 -0.0069 118  THR   B CB  
3534  O  OG1 . THR   B 118 ? 1.1212 1.2373 1.2343 0.0245  -0.0918 -0.0094 118  THR   B OG1 
3535  C  CG2 . THR   B 118 ? 1.1104 1.2330 1.2219 0.0228  -0.0854 -0.0031 118  THR   B CG2 
3536  N  N   . GLY   B 119 ? 1.0888 1.2031 1.2171 0.0182  -0.0976 -0.0140 119  GLY   B N   
3537  C  CA  . GLY   B 119 ? 1.0858 1.1959 1.2185 0.0184  -0.1022 -0.0176 119  GLY   B CA  
3538  C  C   . GLY   B 119 ? 1.0376 1.1437 1.1694 0.0216  -0.1066 -0.0212 119  GLY   B C   
3539  O  O   . GLY   B 119 ? 1.0129 1.1196 1.1410 0.0234  -0.1058 -0.0210 119  GLY   B O   
3540  N  N   . ILE   B 120 ? 1.0051 1.1067 1.1404 0.0225  -0.1116 -0.0246 120  ILE   B N   
3541  C  CA  . ILE   B 120 ? 0.9545 1.0520 1.0903 0.0255  -0.1169 -0.0286 120  ILE   B CA  
3542  C  C   . ILE   B 120 ? 0.9744 1.0652 1.0976 0.0323  -0.1189 -0.0287 120  ILE   B C   
3543  O  O   . ILE   B 120 ? 1.0273 1.1131 1.1443 0.0354  -0.1203 -0.0282 120  ILE   B O   
3544  C  CB  . ILE   B 120 ? 0.8836 0.9781 1.0276 0.0244  -0.1220 -0.0324 120  ILE   B CB  
3545  C  CG1 . ILE   B 120 ? 0.9016 1.0021 1.0578 0.0178  -0.1191 -0.0320 120  ILE   B CG1 
3546  C  CG2 . ILE   B 120 ? 0.9182 1.0091 1.0635 0.0274  -0.1277 -0.0367 120  ILE   B CG2 
3547  C  CD1 . ILE   B 120 ? 0.8561 0.9539 1.0220 0.0162  -0.1236 -0.0355 120  ILE   B CD1 
3548  N  N   . ILE   B 121 ? 0.9718 1.0618 1.0905 0.0348  -0.1190 -0.0292 121  ILE   B N   
3549  C  CA  . ILE   B 121 ? 0.9456 1.0282 1.0515 0.0416  -0.1207 -0.0293 121  ILE   B CA  
3550  C  C   . ILE   B 121 ? 0.9527 1.0294 1.0580 0.0450  -0.1272 -0.0340 121  ILE   B C   
3551  O  O   . ILE   B 121 ? 0.9448 1.0247 1.0559 0.0430  -0.1277 -0.0356 121  ILE   B O   
3552  C  CB  . ILE   B 121 ? 0.9544 1.0398 1.0537 0.0424  -0.1149 -0.0256 121  ILE   B CB  
3553  C  CG1 . ILE   B 121 ? 0.9568 1.0484 1.0578 0.0390  -0.1091 -0.0213 121  ILE   B CG1 
3554  C  CG2 . ILE   B 121 ? 1.0175 1.0945 1.1033 0.0496  -0.1160 -0.0256 121  ILE   B CG2 
3555  C  CD1 . ILE   B 121 ? 0.9923 1.0860 1.0868 0.0403  -0.1037 -0.0176 121  ILE   B CD1 
3556  N  N   . GLY   B 122 ? 0.9784 1.0461 1.0765 0.0503  -0.1323 -0.0362 122  GLY   B N   
3557  C  CA  . GLY   B 122 ? 0.9540 1.0148 1.0498 0.0545  -0.1392 -0.0408 122  GLY   B CA  
3558  C  C   . GLY   B 122 ? 0.9671 1.0190 1.0467 0.0619  -0.1397 -0.0402 122  GLY   B C   
3559  O  O   . GLY   B 122 ? 1.0087 1.0557 1.0793 0.0653  -0.1387 -0.0385 122  GLY   B O   
3560  N  N   . ILE   B 123 ? 0.9791 1.0288 1.0545 0.0645  -0.1407 -0.0414 123  ILE   B N   
3561  C  CA  . ILE   B 123 ? 1.0440 1.0842 1.1032 0.0718  -0.1409 -0.0410 123  ILE   B CA  
3562  C  C   . ILE   B 123 ? 1.0814 1.1145 1.1381 0.0759  -0.1482 -0.0458 123  ILE   B C   
3563  O  O   . ILE   B 123 ? 1.0759 1.1138 1.1439 0.0724  -0.1510 -0.0485 123  ILE   B O   
3564  C  CB  . ILE   B 123 ? 1.0471 1.0911 1.1008 0.0714  -0.1326 -0.0362 123  ILE   B CB  
3565  C  CG1 . ILE   B 123 ? 1.0059 1.0588 1.0697 0.0660  -0.1302 -0.0360 123  ILE   B CG1 
3566  C  CG2 . ILE   B 123 ? 1.0272 1.0756 1.0803 0.0695  -0.1263 -0.0316 123  ILE   B CG2 
3567  C  CD1 . ILE   B 123 ? 0.9699 1.0267 1.0293 0.0651  -0.1225 -0.0316 123  ILE   B CD1 
3568  N  N   . ILE   B 124 ? 1.1149 1.1361 1.1566 0.0836  -0.1515 -0.0470 124  ILE   B N   
3569  C  CA  . ILE   B 124 ? 1.1943 1.2071 1.2313 0.0885  -0.1590 -0.0517 124  ILE   B CA  
3570  C  C   . ILE   B 124 ? 1.3658 1.3702 1.3856 0.0950  -0.1562 -0.0498 124  ILE   B C   
3571  O  O   . ILE   B 124 ? 1.3626 1.3628 1.3710 0.0983  -0.1514 -0.0463 124  ILE   B O   
3572  C  CB  . ILE   B 124 ? 1.1588 1.1630 1.1947 0.0921  -0.1682 -0.0563 124  ILE   B CB  
3573  C  CG1 . ILE   B 124 ? 1.0597 1.0728 1.1145 0.0850  -0.1706 -0.0582 124  ILE   B CG1 
3574  C  CG2 . ILE   B 124 ? 1.2771 1.2715 1.3066 0.0980  -0.1764 -0.0611 124  ILE   B CG2 
3575  C  CD1 . ILE   B 124 ? 0.9900 0.9963 1.0461 0.0871  -0.1786 -0.0621 124  ILE   B CD1 
3576  N  N   . ASP   B 125 ? 1.6501 1.6520 1.6682 0.0968  -0.1589 -0.0521 125  ASP   B N   
3577  C  CA  . ASP   B 125 ? 1.6735 1.6673 1.6756 0.1027  -0.1560 -0.0504 125  ASP   B CA  
3578  C  C   . ASP   B 125 ? 1.6902 1.6697 1.6743 0.1111  -0.1583 -0.0507 125  ASP   B C   
3579  O  O   . ASP   B 125 ? 1.7000 1.6734 1.6836 0.1137  -0.1658 -0.0544 125  ASP   B O   
3580  C  CB  . ASP   B 125 ? 1.6763 1.6679 1.6797 0.1041  -0.1611 -0.0541 125  ASP   B CB  
3581  C  CG  . ASP   B 125 ? 1.7423 1.7270 1.7310 0.1089  -0.1571 -0.0519 125  ASP   B CG  
3582  O  OD1 . ASP   B 125 ? 1.7631 1.7557 1.7556 0.1047  -0.1498 -0.0484 125  ASP   B OD1 
3583  O  OD2 . ASP   B 125 ? 1.7684 1.7392 1.7413 0.1170  -0.1614 -0.0539 125  ASP   B OD2 
3584  N  N   . PRO   B 126 ? 1.5539 1.5274 1.5231 0.1156  -0.1518 -0.0467 126  PRO   B N   
3585  C  CA  . PRO   B 126 ? 1.5335 1.4924 1.4845 0.1242  -0.1537 -0.0471 126  PRO   B CA  
3586  C  C   . PRO   B 126 ? 1.5734 1.5193 1.5155 0.1309  -0.1639 -0.0527 126  PRO   B C   
3587  O  O   . PRO   B 126 ? 1.5825 1.5181 1.5161 0.1362  -0.1699 -0.0553 126  PRO   B O   
3588  C  CB  . PRO   B 126 ? 1.4786 1.4344 1.4169 0.1272  -0.1440 -0.0417 126  PRO   B CB  
3589  C  CG  . PRO   B 126 ? 1.4474 1.4179 1.3990 0.1192  -0.1367 -0.0381 126  PRO   B CG  
3590  C  CD  . PRO   B 126 ? 1.5408 1.5201 1.5089 0.1132  -0.1422 -0.0418 126  PRO   B CD  
3591  N  N   . GLU   B 127 ? 1.5847 1.5309 1.5288 0.1307  -0.1664 -0.0548 127  GLU   B N   
3592  C  CA  . GLU   B 127 ? 1.5626 1.4980 1.5008 0.1364  -0.1769 -0.0606 127  GLU   B CA  
3593  C  C   . GLU   B 127 ? 1.5499 1.4935 1.5075 0.1311  -0.1850 -0.0655 127  GLU   B C   
3594  O  O   . GLU   B 127 ? 1.5074 1.4474 1.4663 0.1332  -0.1922 -0.0699 127  GLU   B O   
3595  C  CB  . GLU   B 127 ? 1.5532 1.4831 1.4810 0.1401  -0.1748 -0.0599 127  GLU   B CB  
3596  C  CG  . GLU   B 127 ? 1.6197 1.5512 1.5394 0.1398  -0.1628 -0.0534 127  GLU   B CG  
3597  C  CD  . GLU   B 127 ? 1.7736 1.6975 1.6808 0.1442  -0.1604 -0.0525 127  GLU   B CD  
3598  O  OE1 . GLU   B 127 ? 1.7949 1.7158 1.7034 0.1457  -0.1675 -0.0568 127  GLU   B OE1 
3599  O  OE2 . GLU   B 127 ? 1.8034 1.7244 1.6999 0.1461  -0.1512 -0.0475 127  GLU   B OE2 
3600  N  N   . CYS   B 128 ? 1.5501 1.5046 1.5230 0.1243  -0.1836 -0.0647 128  CYS   B N   
3601  C  CA  . CYS   B 128 ? 1.4396 1.4020 1.4318 0.1188  -0.1903 -0.0689 128  CYS   B CA  
3602  C  C   . CYS   B 128 ? 1.3965 1.3643 1.3991 0.1163  -0.1933 -0.0717 128  CYS   B C   
3603  O  O   . CYS   B 128 ? 1.4093 1.3754 1.4197 0.1170  -0.2026 -0.0772 128  CYS   B O   
3604  C  CB  . CYS   B 128 ? 1.3494 1.3014 1.3381 0.1236  -0.2006 -0.0739 128  CYS   B CB  
3605  S  SG  . CYS   B 128 ? 1.3804 1.3263 1.3579 0.1264  -0.1974 -0.0709 128  CYS   B SG  
3606  N  N   . ARG   B 129 ? 1.3928 1.3676 1.3965 0.1132  -0.1854 -0.0680 129  ARG   B N   
3607  C  CA  . ARG   B 129 ? 1.3688 1.3486 1.3815 0.1109  -0.1874 -0.0702 129  ARG   B CA  
3608  C  C   . ARG   B 129 ? 1.3760 1.3721 1.4108 0.1013  -0.1843 -0.0696 129  ARG   B C   
3609  O  O   . ARG   B 129 ? 1.3847 1.3854 1.4302 0.0992  -0.1877 -0.0726 129  ARG   B O   
3610  C  CB  . ARG   B 129 ? 1.4156 1.3919 1.4156 0.1138  -0.1815 -0.0671 129  ARG   B CB  
3611  C  CG  . ARG   B 129 ? 1.4368 1.4062 1.4331 0.1184  -0.1887 -0.0715 129  ARG   B CG  
3612  C  CD  . ARG   B 129 ? 1.4434 1.4061 1.4240 0.1227  -0.1836 -0.0687 129  ARG   B CD  
3613  N  NE  . ARG   B 129 ? 1.5586 1.5333 1.5505 0.1162  -0.1777 -0.0666 129  ARG   B NE  
3614  C  CZ  . ARG   B 129 ? 1.5925 1.5652 1.5758 0.1175  -0.1723 -0.0638 129  ARG   B CZ  
3615  N  NH1 . ARG   B 129 ? 1.5192 1.4781 1.4822 0.1252  -0.1717 -0.0629 129  ARG   B NH1 
3616  N  NH2 . ARG   B 129 ? 1.5477 1.5321 1.5427 0.1108  -0.1669 -0.0618 129  ARG   B NH2 
3617  N  N   . MET   B 130 ? 1.3644 1.3688 1.4058 0.0957  -0.1777 -0.0658 130  MET   B N   
3618  C  CA  . MET   B 130 ? 1.2089 1.2272 1.2704 0.0871  -0.1754 -0.0655 130  MET   B CA  
3619  C  C   . MET   B 130 ? 1.1915 1.2137 1.2559 0.0836  -0.1714 -0.0625 130  MET   B C   
3620  O  O   . MET   B 130 ? 1.1978 1.2133 1.2491 0.0876  -0.1693 -0.0602 130  MET   B O   
3621  C  CB  . MET   B 130 ? 1.1617 1.1893 1.2284 0.0823  -0.1681 -0.0624 130  MET   B CB  
3622  C  CG  . MET   B 130 ? 1.1930 1.2248 1.2544 0.0798  -0.1582 -0.0563 130  MET   B CG  
3623  S  SD  . MET   B 130 ? 1.2568 1.2886 1.3097 0.0808  -0.1521 -0.0532 130  MET   B SD  
3624  C  CE  . MET   B 130 ? 1.3550 1.3699 1.3889 0.0913  -0.1587 -0.0562 130  MET   B CE  
3625  N  N   . ILE   B 131 ? 1.1426 1.1755 1.2243 0.0763  -0.1701 -0.0626 131  ILE   B N   
3626  C  CA  . ILE   B 131 ? 1.0501 1.0881 1.1366 0.0721  -0.1658 -0.0596 131  ILE   B CA  
3627  C  C   . ILE   B 131 ? 1.0648 1.1150 1.1603 0.0649  -0.1572 -0.0556 131  ILE   B C   
3628  O  O   . ILE   B 131 ? 1.1252 1.1830 1.2347 0.0600  -0.1574 -0.0571 131  ILE   B O   
3629  C  CB  . ILE   B 131 ? 1.0037 1.0423 1.1023 0.0699  -0.1721 -0.0634 131  ILE   B CB  
3630  C  CG1 . ILE   B 131 ? 1.0235 1.0493 1.1121 0.0770  -0.1806 -0.0672 131  ILE   B CG1 
3631  C  CG2 . ILE   B 131 ? 1.0014 1.0466 1.1066 0.0644  -0.1667 -0.0601 131  ILE   B CG2 
3632  C  CD1 . ILE   B 131 ? 1.0016 1.0274 1.1002 0.0748  -0.1854 -0.0698 131  ILE   B CD1 
3633  N  N   . GLY   B 132 ? 1.0244 1.0763 1.1122 0.0644  -0.1498 -0.0506 132  GLY   B N   
3634  C  CA  . GLY   B 132 ? 0.9604 1.0230 1.0554 0.0580  -0.1419 -0.0466 132  GLY   B CA  
3635  C  C   . GLY   B 132 ? 0.9303 0.9991 1.0340 0.0528  -0.1392 -0.0447 132  GLY   B C   
3636  O  O   . GLY   B 132 ? 0.9708 1.0357 1.0688 0.0548  -0.1393 -0.0436 132  GLY   B O   
3637  N  N   . LEU   B 133 ? 0.9347 1.0127 1.0518 0.0463  -0.1366 -0.0444 133  LEU   B N   
3638  C  CA  . LEU   B 133 ? 0.9132 0.9973 1.0384 0.0409  -0.1332 -0.0423 133  LEU   B CA  
3639  C  C   . LEU   B 133 ? 0.9341 1.0264 1.0614 0.0362  -0.1254 -0.0381 133  LEU   B C   
3640  O  O   . LEU   B 133 ? 0.9775 1.0738 1.1085 0.0343  -0.1238 -0.0383 133  LEU   B O   
3641  C  CB  . LEU   B 133 ? 0.8874 0.9743 1.0272 0.0373  -0.1372 -0.0459 133  LEU   B CB  
3642  C  CG  . LEU   B 133 ? 0.8770 0.9561 1.0166 0.0415  -0.1457 -0.0506 133  LEU   B CG  
3643  C  CD1 . LEU   B 133 ? 0.8736 0.9568 1.0298 0.0372  -0.1488 -0.0540 133  LEU   B CD1 
3644  C  CD2 . LEU   B 133 ? 0.8827 0.9561 1.0142 0.0442  -0.1465 -0.0494 133  LEU   B CD2 
3645  N  N   . ARG   B 134 ? 0.9252 1.0197 1.0499 0.0346  -0.1209 -0.0343 134  ARG   B N   
3646  C  CA  . ARG   B 134 ? 0.9615 1.0640 1.0900 0.0294  -0.1143 -0.0306 134  ARG   B CA  
3647  C  C   . ARG   B 134 ? 0.9983 1.1045 1.1361 0.0247  -0.1136 -0.0303 134  ARG   B C   
3648  O  O   . ARG   B 134 ? 0.9695 1.0750 1.1044 0.0248  -0.1122 -0.0282 134  ARG   B O   
3649  C  CB  . ARG   B 134 ? 0.9154 1.0177 1.0340 0.0313  -0.1096 -0.0263 134  ARG   B CB  
3650  C  CG  . ARG   B 134 ? 0.9973 1.1065 1.1178 0.0274  -0.1038 -0.0233 134  ARG   B CG  
3651  C  CD  . ARG   B 134 ? 1.0411 1.1567 1.1689 0.0219  -0.1005 -0.0212 134  ARG   B CD  
3652  N  NE  . ARG   B 134 ? 1.0407 1.1540 1.1657 0.0231  -0.1007 -0.0199 134  ARG   B NE  
3653  C  CZ  . ARG   B 134 ? 1.0524 1.1676 1.1732 0.0230  -0.0968 -0.0162 134  ARG   B CZ  
3654  N  NH1 . ARG   B 134 ? 1.0577 1.1771 1.1770 0.0215  -0.0924 -0.0134 134  ARG   B NH1 
3655  N  NH2 . ARG   B 134 ? 1.0462 1.1591 1.1648 0.0243  -0.0975 -0.0153 134  ARG   B NH2 
3656  N  N   . LEU   B 135 ? 0.9734 1.0834 1.1225 0.0208  -0.1144 -0.0325 135  LEU   B N   
3657  C  CA  . LEU   B 135 ? 0.9795 1.0927 1.1379 0.0161  -0.1132 -0.0323 135  LEU   B CA  
3658  C  C   . LEU   B 135 ? 1.0313 1.1512 1.1921 0.0112  -0.1066 -0.0286 135  LEU   B C   
3659  O  O   . LEU   B 135 ? 1.0236 1.1449 1.1858 0.0086  -0.1040 -0.0265 135  LEU   B O   
3660  C  CB  . LEU   B 135 ? 0.9780 1.0918 1.1483 0.0144  -0.1170 -0.0364 135  LEU   B CB  
3661  C  CG  . LEU   B 135 ? 0.9497 1.0570 1.1192 0.0191  -0.1245 -0.0408 135  LEU   B CG  
3662  C  CD1 . LEU   B 135 ? 0.9903 1.1000 1.1741 0.0162  -0.1274 -0.0445 135  LEU   B CD1 
3663  C  CD2 . LEU   B 135 ? 0.9189 1.0201 1.0830 0.0219  -0.1276 -0.0410 135  LEU   B CD2 
3664  N  N   . TYR   B 136 ? 1.0520 1.1753 1.2126 0.0103  -0.1042 -0.0280 136  TYR   B N   
3665  C  CA  . TYR   B 136 ? 1.0808 1.2100 1.2439 0.0057  -0.0985 -0.0251 136  TYR   B CA  
3666  C  C   . TYR   B 136 ? 1.0897 1.2200 1.2446 0.0072  -0.0958 -0.0227 136  TYR   B C   
3667  O  O   . TYR   B 136 ? 1.1207 1.2474 1.2692 0.0114  -0.0979 -0.0235 136  TYR   B O   
3668  C  CB  . TYR   B 136 ? 1.1213 1.2542 1.2948 0.0019  -0.0977 -0.0270 136  TYR   B CB  
3669  C  CG  . TYR   B 136 ? 1.1101 1.2417 1.2933 0.0010  -0.1011 -0.0303 136  TYR   B CG  
3670  C  CD1 . TYR   B 136 ? 1.0996 1.2322 1.2881 -0.0025 -0.0991 -0.0292 136  TYR   B CD1 
3671  C  CD2 . TYR   B 136 ? 1.1177 1.2471 1.3051 0.0035  -0.1064 -0.0344 136  TYR   B CD2 
3672  C  CE1 . TYR   B 136 ? 1.0702 1.2016 1.2686 -0.0037 -0.1019 -0.0321 136  TYR   B CE1 
3673  C  CE2 . TYR   B 136 ? 1.1055 1.2339 1.3030 0.0025  -0.1097 -0.0375 136  TYR   B CE2 
3674  C  CZ  . TYR   B 136 ? 1.0549 1.1845 1.2581 -0.0013 -0.1072 -0.0363 136  TYR   B CZ  
3675  O  OH  . TYR   B 136 ? 1.1410 1.2697 1.3552 -0.0026 -0.1103 -0.0394 136  TYR   B OH  
3676  N  N   . ASP   B 137 ? 1.1090 1.2438 1.2641 0.0036  -0.0910 -0.0196 137  ASP   B N   
3677  C  CA  . ASP   B 137 ? 1.0931 1.2295 1.2418 0.0042  -0.0880 -0.0170 137  ASP   B CA  
3678  C  C   . ASP   B 137 ? 1.1090 1.2474 1.2604 0.0031  -0.0875 -0.0184 137  ASP   B C   
3679  O  O   . ASP   B 137 ? 1.1244 1.2655 1.2832 -0.0003 -0.0866 -0.0196 137  ASP   B O   
3680  C  CB  . ASP   B 137 ? 1.1484 1.2885 1.2963 0.0010  -0.0838 -0.0134 137  ASP   B CB  
3681  C  CG  . ASP   B 137 ? 1.2622 1.4004 1.4047 0.0034  -0.0839 -0.0113 137  ASP   B CG  
3682  O  OD1 . ASP   B 137 ? 1.2905 1.4255 1.4265 0.0077  -0.0851 -0.0112 137  ASP   B OD1 
3683  O  OD2 . ASP   B 137 ? 1.2090 1.3483 1.3530 0.0013  -0.0826 -0.0098 137  ASP   B OD2 
3684  N  N   . GLY   B 138 ? 1.2384 1.3747 1.3836 0.0063  -0.0880 -0.0184 138  GLY   B N   
3685  C  CA  . GLY   B 138 ? 1.2612 1.3985 1.4075 0.0059  -0.0877 -0.0197 138  GLY   B CA  
3686  C  C   . GLY   B 138 ? 1.2375 1.3708 1.3846 0.0094  -0.0925 -0.0236 138  GLY   B C   
3687  O  O   . GLY   B 138 ? 1.2287 1.3626 1.3772 0.0093  -0.0926 -0.0250 138  GLY   B O   
3688  N  N   . LEU   B 139 ? 1.1987 1.3275 1.3446 0.0127  -0.0966 -0.0255 139  LEU   B N   
3689  C  CA  . LEU   B 139 ? 1.1851 1.3102 1.3338 0.0156  -0.1021 -0.0298 139  LEU   B CA  
3690  C  C   . LEU   B 139 ? 1.1387 1.2569 1.2806 0.0208  -0.1064 -0.0310 139  LEU   B C   
3691  O  O   . LEU   B 139 ? 1.0934 1.2106 1.2317 0.0212  -0.1053 -0.0289 139  LEU   B O   
3692  C  CB  . LEU   B 139 ? 1.1991 1.3277 1.3604 0.0118  -0.1033 -0.0322 139  LEU   B CB  
3693  C  CG  . LEU   B 139 ? 1.1961 1.3300 1.3644 0.0079  -0.1003 -0.0323 139  LEU   B CG  
3694  C  CD1 . LEU   B 139 ? 1.1753 1.3126 1.3558 0.0039  -0.0999 -0.0337 139  LEU   B CD1 
3695  C  CD2 . LEU   B 139 ? 1.1997 1.3313 1.3666 0.0110  -0.1032 -0.0350 139  LEU   B CD2 
3696  N  N   . PHE   B 140 ? 1.0772 1.1902 1.2172 0.0249  -0.1116 -0.0345 140  PHE   B N   
3697  C  CA  . PHE   B 140 ? 1.0431 1.1481 1.1747 0.0308  -0.1162 -0.0360 140  PHE   B CA  
3698  C  C   . PHE   B 140 ? 1.0516 1.1528 1.1879 0.0332  -0.1233 -0.0412 140  PHE   B C   
3699  O  O   . PHE   B 140 ? 1.1182 1.2168 1.2515 0.0360  -0.1254 -0.0430 140  PHE   B O   
3700  C  CB  . PHE   B 140 ? 1.0322 1.1326 1.1505 0.0351  -0.1141 -0.0338 140  PHE   B CB  
3701  C  CG  . PHE   B 140 ? 0.9843 1.0756 1.0917 0.0414  -0.1176 -0.0346 140  PHE   B CG  
3702  C  CD1 . PHE   B 140 ? 0.9619 1.0520 1.0667 0.0420  -0.1168 -0.0328 140  PHE   B CD1 
3703  C  CD2 . PHE   B 140 ? 1.0013 1.0848 1.1001 0.0472  -0.1213 -0.0368 140  PHE   B CD2 
3704  C  CE1 . PHE   B 140 ? 0.9556 1.0369 1.0496 0.0481  -0.1197 -0.0334 140  PHE   B CE1 
3705  C  CE2 . PHE   B 140 ? 0.9594 1.0337 1.0468 0.0534  -0.1243 -0.0374 140  PHE   B CE2 
3706  C  CZ  . PHE   B 140 ? 0.9355 1.0087 1.0206 0.0538  -0.1233 -0.0357 140  PHE   B CZ  
3707  N  N   . LYS   B 141 ? 1.0419 1.1429 1.1859 0.0322  -0.1270 -0.0435 141  LYS   B N   
3708  C  CA  . LYS   B 141 ? 1.0287 1.1266 1.1791 0.0343  -0.1343 -0.0487 141  LYS   B CA  
3709  C  C   . LYS   B 141 ? 1.0272 1.1150 1.1653 0.0417  -0.1399 -0.0508 141  LYS   B C   
3710  O  O   . LYS   B 141 ? 1.0024 1.0848 1.1295 0.0450  -0.1395 -0.0489 141  LYS   B O   
3711  C  CB  . LYS   B 141 ? 0.9681 1.0679 1.1299 0.0311  -0.1365 -0.0504 141  LYS   B CB  
3712  C  CG  . LYS   B 141 ? 0.9860 1.0915 1.1640 0.0271  -0.1378 -0.0533 141  LYS   B CG  
3713  C  CD  . LYS   B 141 ? 0.9787 1.0873 1.1682 0.0227  -0.1374 -0.0536 141  LYS   B CD  
3714  C  CE  . LYS   B 141 ? 1.0025 1.1171 1.2088 0.0184  -0.1374 -0.0560 141  LYS   B CE  
3715  N  NZ  . LYS   B 141 ? 1.0522 1.1639 1.2657 0.0213  -0.1455 -0.0616 141  LYS   B NZ  
3716  N  N   . VAL   B 142 ? 1.0283 1.1129 1.1675 0.0447  -0.1453 -0.0547 142  VAL   B N   
3717  C  CA  . VAL   B 142 ? 1.0577 1.1318 1.1842 0.0522  -0.1509 -0.0569 142  VAL   B CA  
3718  C  C   . VAL   B 142 ? 1.1023 1.1732 1.2371 0.0540  -0.1598 -0.0627 142  VAL   B C   
3719  O  O   . VAL   B 142 ? 1.0962 1.1700 1.2397 0.0531  -0.1624 -0.0656 142  VAL   B O   
3720  C  CB  . VAL   B 142 ? 1.0497 1.1213 1.1666 0.0551  -0.1488 -0.0559 142  VAL   B CB  
3721  C  CG1 . VAL   B 142 ? 1.1149 1.1743 1.2175 0.0633  -0.1547 -0.0582 142  VAL   B CG1 
3722  C  CG2 . VAL   B 142 ? 1.0747 1.1497 1.1850 0.0529  -0.1401 -0.0503 142  VAL   B CG2 
3723  N  N   . ILE   B 143 ? 1.1016 1.1671 1.2348 0.0563  -0.1646 -0.0644 143  ILE   B N   
3724  C  CA  . ILE   B 143 ? 1.1084 1.1685 1.2466 0.0595  -0.1744 -0.0702 143  ILE   B CA  
3725  C  C   . ILE   B 143 ? 1.1432 1.1920 1.2649 0.0677  -0.1792 -0.0720 143  ILE   B C   
3726  O  O   . ILE   B 143 ? 1.1587 1.1995 1.2653 0.0723  -0.1788 -0.0702 143  ILE   B O   
3727  C  CB  . ILE   B 143 ? 1.0962 1.1537 1.2383 0.0591  -0.1782 -0.0717 143  ILE   B CB  
3728  C  CG1 . ILE   B 143 ? 1.0765 1.1433 1.2296 0.0517  -0.1716 -0.0684 143  ILE   B CG1 
3729  C  CG2 . ILE   B 143 ? 1.1164 1.1714 1.2694 0.0604  -0.1879 -0.0779 143  ILE   B CG2 
3730  C  CD1 . ILE   B 143 ? 1.1014 1.1660 1.2614 0.0508  -0.1761 -0.0707 143  ILE   B CD1 
3731  N  N   . PRO   B 144 ? 1.1742 1.2215 1.2975 0.0701  -0.1835 -0.0752 144  PRO   B N   
3732  C  CA  . PRO   B 144 ? 1.2567 1.2918 1.3633 0.0784  -0.1886 -0.0771 144  PRO   B CA  
3733  C  C   . PRO   B 144 ? 1.2761 1.3018 1.3800 0.0833  -0.1982 -0.0816 144  PRO   B C   
3734  O  O   . PRO   B 144 ? 1.2282 1.2567 1.3470 0.0812  -0.2044 -0.0858 144  PRO   B O   
3735  C  CB  . PRO   B 144 ? 1.3268 1.3641 1.4388 0.0788  -0.1910 -0.0798 144  PRO   B CB  
3736  C  CG  . PRO   B 144 ? 1.2635 1.3148 1.3926 0.0704  -0.1845 -0.0778 144  PRO   B CG  
3737  C  CD  . PRO   B 144 ? 1.2002 1.2565 1.3394 0.0656  -0.1832 -0.0770 144  PRO   B CD  
3738  N  N   . LEU   B 145 ? 1.3166 1.3307 1.4014 0.0900  -0.1994 -0.0807 145  LEU   B N   
3739  C  CA  . LEU   B 145 ? 1.2968 1.3004 1.3758 0.0952  -0.2079 -0.0844 145  LEU   B CA  
3740  C  C   . LEU   B 145 ? 1.4468 1.4389 1.5172 0.1029  -0.2177 -0.0895 145  LEU   B C   
3741  O  O   . LEU   B 145 ? 1.5624 1.5476 1.6342 0.1063  -0.2274 -0.0944 145  LEU   B O   
3742  C  CB  . LEU   B 145 ? 1.2866 1.2831 1.3487 0.0986  -0.2036 -0.0805 145  LEU   B CB  
3743  C  CG  . LEU   B 145 ? 1.2502 1.2544 1.3211 0.0925  -0.1985 -0.0775 145  LEU   B CG  
3744  C  CD1 . LEU   B 145 ? 1.2630 1.2583 1.3168 0.0973  -0.1965 -0.0748 145  LEU   B CD1 
3745  C  CD2 . LEU   B 145 ? 1.1577 1.1655 1.2459 0.0890  -0.2054 -0.0819 145  LEU   B CD2 
3746  N  N   . ASP   B 146 ? 1.5460 1.5353 1.6068 0.1061  -0.2156 -0.0886 146  ASP   B N   
3747  C  CA  . ASP   B 146 ? 1.5630 1.5426 1.6177 0.1128  -0.2249 -0.0937 146  ASP   B CA  
3748  C  C   . ASP   B 146 ? 1.5759 1.5612 1.6511 0.1101  -0.2335 -0.0995 146  ASP   B C   
3749  O  O   . ASP   B 146 ? 1.6413 1.6398 1.7343 0.1029  -0.2294 -0.0987 146  ASP   B O   
3750  C  CB  . ASP   B 146 ? 1.5698 1.5488 1.6156 0.1146  -0.2201 -0.0914 146  ASP   B CB  
3751  C  CG  . ASP   B 146 ? 1.6072 1.6011 1.6648 0.1062  -0.2095 -0.0868 146  ASP   B CG  
3752  O  OD1 . ASP   B 146 ? 1.6163 1.6102 1.6645 0.1065  -0.2021 -0.0828 146  ASP   B OD1 
3753  O  OD2 . ASP   B 146 ? 1.5961 1.6013 1.6728 0.0991  -0.2086 -0.0872 146  ASP   B OD2 
3754  N  N   . ARG   B 147 ? 1.5344 1.5103 1.6082 0.1152  -0.2448 -0.1051 147  ARG   B N   
3755  C  CA  . ARG   B 147 ? 1.5785 1.5583 1.6717 0.1135  -0.2544 -0.1113 147  ARG   B CA  
3756  C  C   . ARG   B 147 ? 1.5380 1.5301 1.6531 0.1050  -0.2521 -0.1110 147  ARG   B C   
3757  O  O   . ARG   B 147 ? 1.5369 1.5384 1.6562 0.0987  -0.2417 -0.1058 147  ARG   B O   
3758  C  CB  . ARG   B 147 ? 1.5663 1.5507 1.6662 0.1133  -0.2552 -0.1130 147  ARG   B CB  
3759  N  N   . ASP   B 148 ? 1.5565 1.5484 1.6861 0.1046  -0.2619 -0.1167 148  ASP   B N   
3760  C  CA  . ASP   B 148 ? 1.5207 1.5207 1.6682 0.0978  -0.2610 -0.1168 148  ASP   B CA  
3761  C  C   . ASP   B 148 ? 1.5228 1.5389 1.6879 0.0885  -0.2509 -0.1131 148  ASP   B C   
3762  O  O   . ASP   B 148 ? 1.5607 1.5844 1.7404 0.0859  -0.2517 -0.1152 148  ASP   B O   
3763  C  CB  . ASP   B 148 ? 1.5811 1.5791 1.7436 0.0988  -0.2733 -0.1240 148  ASP   B CB  
3764  C  CG  . ASP   B 148 ? 1.7687 1.7509 1.9157 0.1067  -0.2832 -0.1275 148  ASP   B CG  
3765  O  OD1 . ASP   B 148 ? 1.8013 1.7726 1.9242 0.1134  -0.2821 -0.1254 148  ASP   B OD1 
3766  O  OD2 . ASP   B 148 ? 1.8928 1.8733 2.0515 0.1062  -0.2918 -0.1321 148  ASP   B OD2 
3767  N  N   . ASN   B 149 ? 1.3818 1.4028 1.5455 0.0838  -0.2417 -0.1078 149  ASN   B N   
3768  C  CA  . ASN   B 149 ? 1.2908 1.3263 1.4704 0.0750  -0.2323 -0.1043 149  ASN   B CA  
3769  C  C   . ASN   B 149 ? 1.2561 1.2968 1.4518 0.0692  -0.2324 -0.1048 149  ASN   B C   
3770  O  O   . ASN   B 149 ? 1.2622 1.3085 1.4589 0.0642  -0.2238 -0.1001 149  ASN   B O   
3771  C  CB  . ASN   B 149 ? 1.2378 1.2758 1.4042 0.0736  -0.2209 -0.0974 149  ASN   B CB  
3772  C  CG  . ASN   B 149 ? 1.2247 1.2761 1.4040 0.0663  -0.2119 -0.0942 149  ASN   B CG  
3773  O  OD1 . ASN   B 149 ? 1.2040 1.2639 1.4033 0.0609  -0.2122 -0.0961 149  ASN   B OD1 
3774  N  ND2 . ASN   B 149 ? 1.2015 1.2545 1.3691 0.0660  -0.2035 -0.0892 149  ASN   B ND2 
3775  N  N   . LYS   B 150 ? 1.2661 1.3048 1.4748 0.0700  -0.2423 -0.1107 150  LYS   B N   
3776  C  CA  . LYS   B 150 ? 1.2352 1.2766 1.4585 0.0653  -0.2438 -0.1119 150  LYS   B CA  
3777  C  C   . LYS   B 150 ? 1.2487 1.3031 1.4866 0.0562  -0.2330 -0.1076 150  LYS   B C   
3778  O  O   . LYS   B 150 ? 1.2492 1.3048 1.4901 0.0525  -0.2297 -0.1054 150  LYS   B O   
3779  C  CB  . LYS   B 150 ? 1.1317 1.1714 1.3711 0.0665  -0.2556 -0.1192 150  LYS   B CB  
3780  N  N   . GLU   B 151 ? 1.2097 1.2734 1.4560 0.0528  -0.2274 -0.1062 151  GLU   B N   
3781  C  CA  . GLU   B 151 ? 1.1793 1.2546 1.4387 0.0446  -0.2172 -0.1022 151  GLU   B CA  
3782  C  C   . GLU   B 151 ? 1.1774 1.2544 1.4220 0.0432  -0.2067 -0.0955 151  GLU   B C   
3783  O  O   . GLU   B 151 ? 1.1814 1.2670 1.4339 0.0368  -0.1980 -0.0917 151  GLU   B O   
3784  C  CB  . GLU   B 151 ? 1.2127 1.2970 1.4890 0.0416  -0.2161 -0.1041 151  GLU   B CB  
3785  C  CG  . GLU   B 151 ? 1.2640 1.3468 1.5554 0.0436  -0.2272 -0.1111 151  GLU   B CG  
3786  C  CD  . GLU   B 151 ? 1.4000 1.4861 1.7111 0.0387  -0.2293 -0.1133 151  GLU   B CD  
3787  O  OE1 . GLU   B 151 ? 1.5412 1.6373 1.8706 0.0321  -0.2232 -0.1123 151  GLU   B OE1 
3788  O  OE2 . GLU   B 151 ? 1.4219 1.5000 1.7302 0.0415  -0.2369 -0.1161 151  GLU   B OE2 
3789  N  N   . LEU   B 152 ? 1.1803 1.2491 1.4037 0.0492  -0.2075 -0.0940 152  LEU   B N   
3790  C  CA  . LEU   B 152 ? 1.1458 1.2156 1.3547 0.0486  -0.1983 -0.0879 152  LEU   B CA  
3791  C  C   . LEU   B 152 ? 1.1354 1.2146 1.3494 0.0445  -0.1904 -0.0851 152  LEU   B C   
3792  O  O   . LEU   B 152 ? 1.1304 1.2167 1.3473 0.0391  -0.1816 -0.0806 152  LEU   B O   
3793  C  CB  . LEU   B 152 ? 1.1421 1.2130 1.3507 0.0450  -0.1936 -0.0845 152  LEU   B CB  
3794  C  CG  . LEU   B 152 ? 1.1423 1.2029 1.3432 0.0495  -0.2010 -0.0869 152  LEU   B CG  
3795  C  CD1 . LEU   B 152 ? 1.1594 1.2212 1.3601 0.0459  -0.1960 -0.0834 152  LEU   B CD1 
3796  C  CD2 . LEU   B 152 ? 1.0932 1.1436 1.2728 0.0575  -0.2039 -0.0868 152  LEU   B CD2 
3797  N  N   . LYS   B 153 ? 1.1290 1.2078 1.3443 0.0473  -0.1942 -0.0880 153  LYS   B N   
3798  C  CA  . LYS   B 153 ? 1.0840 1.1697 1.3006 0.0449  -0.1876 -0.0856 153  LYS   B CA  
3799  C  C   . LYS   B 153 ? 1.0848 1.1681 1.2828 0.0464  -0.1808 -0.0803 153  LYS   B C   
3800  O  O   . LYS   B 153 ? 1.1371 1.2112 1.3187 0.0522  -0.1837 -0.0801 153  LYS   B O   
3801  C  CB  . LYS   B 153 ? 1.0571 1.1409 1.2766 0.0488  -0.1942 -0.0901 153  LYS   B CB  
3802  N  N   . ALA   B 154 ? 1.1006 1.1920 1.3012 0.0412  -0.1716 -0.0759 154  ALA   B N   
3803  C  CA  . ALA   B 154 ? 1.0841 1.1744 1.2691 0.0419  -0.1648 -0.0708 154  ALA   B CA  
3804  C  C   . ALA   B 154 ? 1.0822 1.1800 1.2704 0.0382  -0.1579 -0.0682 154  ALA   B C   
3805  O  O   . ALA   B 154 ? 1.0440 1.1493 1.2469 0.0333  -0.1558 -0.0690 154  ALA   B O   
3806  C  CB  . ALA   B 154 ? 1.0399 1.1309 1.2215 0.0393  -0.1601 -0.0670 154  ALA   B CB  
3807  N  N   . PHE   B 155 ? 1.0809 1.1761 1.2547 0.0405  -0.1540 -0.0651 155  PHE   B N   
3808  C  CA  . PHE   B 155 ? 1.0487 1.1501 1.2229 0.0370  -0.1468 -0.0619 155  PHE   B CA  
3809  C  C   . PHE   B 155 ? 1.0753 1.1784 1.2412 0.0347  -0.1395 -0.0564 155  PHE   B C   
3810  O  O   . PHE   B 155 ? 1.1163 1.2134 1.2709 0.0381  -0.1403 -0.0550 155  PHE   B O   
3811  C  CB  . PHE   B 155 ? 1.0412 1.1386 1.2069 0.0413  -0.1484 -0.0629 155  PHE   B CB  
3812  C  CG  . PHE   B 155 ? 0.9807 1.0680 1.1282 0.0479  -0.1506 -0.0622 155  PHE   B CG  
3813  C  CD1 . PHE   B 155 ? 1.0541 1.1328 1.1970 0.0539  -0.1589 -0.0663 155  PHE   B CD1 
3814  C  CD2 . PHE   B 155 ? 1.0301 1.1164 1.1653 0.0482  -0.1443 -0.0576 155  PHE   B CD2 
3815  C  CE1 . PHE   B 155 ? 1.1337 1.2022 1.2590 0.0603  -0.1605 -0.0656 155  PHE   B CE1 
3816  C  CE2 . PHE   B 155 ? 1.0736 1.1505 1.1926 0.0543  -0.1455 -0.0568 155  PHE   B CE2 
3817  C  CZ  . PHE   B 155 ? 1.1453 1.2130 1.2587 0.0604  -0.1534 -0.0607 155  PHE   B CZ  
3818  N  N   . ASN   B 156 ? 1.0329 1.1437 1.2045 0.0291  -0.1327 -0.0534 156  ASN   B N   
3819  C  CA  . ASN   B 156 ? 1.0362 1.1498 1.2026 0.0261  -0.1259 -0.0484 156  ASN   B CA  
3820  C  C   . ASN   B 156 ? 1.0826 1.1965 1.2396 0.0266  -0.1212 -0.0454 156  ASN   B C   
3821  O  O   . ASN   B 156 ? 1.1366 1.2560 1.2988 0.0231  -0.1175 -0.0445 156  ASN   B O   
3822  C  CB  . ASN   B 156 ? 1.0414 1.1626 1.2200 0.0196  -0.1217 -0.0472 156  ASN   B CB  
3823  C  CG  . ASN   B 156 ? 1.0821 1.2027 1.2612 0.0183  -0.1212 -0.0457 156  ASN   B CG  
3824  O  OD1 . ASN   B 156 ? 1.1113 1.2272 1.2799 0.0215  -0.1219 -0.0442 156  ASN   B OD1 
3825  N  ND2 . ASN   B 156 ? 1.0724 1.1976 1.2635 0.0136  -0.1197 -0.0460 156  ASN   B ND2 
3826  N  N   . ILE   B 157 ? 1.1698 1.2777 1.3132 0.0309  -0.1211 -0.0436 157  ILE   B N   
3827  C  CA  . ILE   B 157 ? 1.1907 1.2984 1.3253 0.0315  -0.1165 -0.0406 157  ILE   B CA  
3828  C  C   . ILE   B 157 ? 1.1941 1.3083 1.3302 0.0263  -0.1095 -0.0361 157  ILE   B C   
3829  O  O   . ILE   B 157 ? 1.1644 1.2798 1.3012 0.0249  -0.1082 -0.0344 157  ILE   B O   
3830  C  CB  . ILE   B 157 ? 1.2439 1.3428 1.3637 0.0378  -0.1180 -0.0400 157  ILE   B CB  
3831  C  CG1 . ILE   B 157 ? 1.2747 1.3663 1.3920 0.0433  -0.1254 -0.0446 157  ILE   B CG1 
3832  C  CG2 . ILE   B 157 ? 1.2855 1.3840 1.3971 0.0382  -0.1130 -0.0369 157  ILE   B CG2 
3833  C  CD1 . ILE   B 157 ? 1.3221 1.4037 1.4230 0.0501  -0.1266 -0.0440 157  ILE   B CD1 
3834  N  N   . ARG   B 158 ? 1.1853 1.3032 1.3219 0.0237  -0.1054 -0.0345 158  ARG   B N   
3835  C  CA  . ARG   B 158 ? 1.1547 1.2785 1.2927 0.0189  -0.0993 -0.0305 158  ARG   B CA  
3836  C  C   . ARG   B 158 ? 1.2027 1.3238 1.3298 0.0209  -0.0962 -0.0270 158  ARG   B C   
3837  O  O   . ARG   B 158 ? 1.2006 1.3168 1.3193 0.0248  -0.0965 -0.0269 158  ARG   B O   
3838  C  CB  . ARG   B 158 ? 1.2245 1.3527 1.3670 0.0155  -0.0965 -0.0305 158  ARG   B CB  
3839  C  CG  . ARG   B 158 ? 1.2652 1.3977 1.4200 0.0123  -0.0976 -0.0332 158  ARG   B CG  
3840  C  CD  . ARG   B 158 ? 1.2951 1.4335 1.4539 0.0070  -0.0922 -0.0307 158  ARG   B CD  
3841  N  NE  . ARG   B 158 ? 1.4293 1.5693 1.5846 0.0049  -0.0887 -0.0270 158  ARG   B NE  
3842  C  CZ  . ARG   B 158 ? 1.3769 1.5199 1.5376 0.0016  -0.0872 -0.0261 158  ARG   B CZ  
3843  N  NH1 . ARG   B 158 ? 1.3181 1.4632 1.4886 -0.0004 -0.0882 -0.0284 158  ARG   B NH1 
3844  N  NH2 . ARG   B 158 ? 1.2624 1.4062 1.4190 0.0004  -0.0846 -0.0228 158  ARG   B NH2 
3845  N  N   . LEU   B 159 ? 1.2438 1.3680 1.3713 0.0184  -0.0930 -0.0240 159  LEU   B N   
3846  C  CA  . LEU   B 159 ? 1.2531 1.3756 1.3723 0.0202  -0.0900 -0.0205 159  LEU   B CA  
3847  C  C   . LEU   B 159 ? 1.2851 1.4139 1.4069 0.0153  -0.0848 -0.0171 159  LEU   B C   
3848  O  O   . LEU   B 159 ? 1.3053 1.4389 1.4339 0.0112  -0.0837 -0.0166 159  LEU   B O   
3849  C  CB  . LEU   B 159 ? 1.2249 1.3450 1.3425 0.0222  -0.0918 -0.0203 159  LEU   B CB  
3850  C  CG  . LEU   B 159 ? 1.2385 1.3531 1.3458 0.0271  -0.0913 -0.0186 159  LEU   B CG  
3851  C  CD1 . LEU   B 159 ? 1.1892 1.3015 1.2970 0.0287  -0.0943 -0.0196 159  LEU   B CD1 
3852  C  CD2 . LEU   B 159 ? 1.3039 1.4220 1.4087 0.0253  -0.0856 -0.0141 159  LEU   B CD2 
3853  N  N   . GLU   B 160 ? 1.3035 1.4319 1.4199 0.0158  -0.0816 -0.0148 160  GLU   B N   
3854  C  CA  . GLU   B 160 ? 1.2676 1.4015 1.3866 0.0112  -0.0773 -0.0119 160  GLU   B CA  
3855  C  C   . GLU   B 160 ? 1.2182 1.3553 1.3384 0.0095  -0.0753 -0.0091 160  GLU   B C   
3856  O  O   . GLU   B 160 ? 1.1421 1.2842 1.2675 0.0051  -0.0736 -0.0080 160  GLU   B O   
3857  C  CB  . GLU   B 160 ? 1.1669 1.2992 1.2801 0.0123  -0.0745 -0.0101 160  GLU   B CB  
3858  N  N   . GLU   B 161 ? 1.2385 1.3723 1.3536 0.0132  -0.0757 -0.0082 161  GLU   B N   
3859  C  CA  . GLU   B 161 ? 1.2148 1.3509 1.3303 0.0124  -0.0740 -0.0055 161  GLU   B CA  
3860  C  C   . GLU   B 161 ? 1.2174 1.3546 1.3379 0.0110  -0.0765 -0.0071 161  GLU   B C   
3861  O  O   . GLU   B 161 ? 1.2088 1.3420 1.3288 0.0136  -0.0801 -0.0098 161  GLU   B O   
3862  C  CB  . GLU   B 161 ? 1.1542 1.2858 1.2622 0.0174  -0.0733 -0.0041 161  GLU   B CB  
3863  C  CG  . GLU   B 161 ? 1.2156 1.3458 1.3185 0.0189  -0.0699 -0.0019 161  GLU   B CG  
3864  C  CD  . GLU   B 161 ? 1.2486 1.3745 1.3478 0.0209  -0.0711 -0.0040 161  GLU   B CD  
3865  O  OE1 . GLU   B 161 ? 1.2310 1.3524 1.3286 0.0236  -0.0752 -0.0072 161  GLU   B OE1 
3866  O  OE2 . GLU   B 161 ? 1.2671 1.3939 1.3653 0.0196  -0.0681 -0.0025 161  GLU   B OE2 
3867  N  N   . LEU   B 162 ? 1.2447 1.3867 1.3699 0.0068  -0.0747 -0.0055 162  LEU   B N   
3868  C  CA  . LEU   B 162 ? 1.2639 1.4068 1.3945 0.0047  -0.0765 -0.0070 162  LEU   B CA  
3869  C  C   . LEU   B 162 ? 1.3063 1.4489 1.4358 0.0055  -0.0766 -0.0053 162  LEU   B C   
3870  O  O   . LEU   B 162 ? 1.3181 1.4620 1.4518 0.0031  -0.0770 -0.0056 162  LEU   B O   
3871  C  CB  . LEU   B 162 ? 1.2575 1.4049 1.3937 -0.0004 -0.0746 -0.0067 162  LEU   B CB  
3872  C  CG  . LEU   B 162 ? 1.2127 1.3607 1.3497 -0.0014 -0.0740 -0.0078 162  LEU   B CG  
3873  C  CD1 . LEU   B 162 ? 1.1893 1.3411 1.3310 -0.0062 -0.0720 -0.0075 162  LEU   B CD1 
3874  C  CD2 . LEU   B 162 ? 1.2393 1.3839 1.3774 0.0011  -0.0774 -0.0114 162  LEU   B CD2 
3875  N  N   . HIS   B 163 ? 1.3909 1.5318 1.5148 0.0089  -0.0757 -0.0035 163  HIS   B N   
3876  C  CA  . HIS   B 163 ? 1.4023 1.5432 1.5249 0.0098  -0.0753 -0.0016 163  HIS   B CA  
3877  C  C   . HIS   B 163 ? 1.4238 1.5595 1.5399 0.0154  -0.0765 -0.0017 163  HIS   B C   
3878  O  O   . HIS   B 163 ? 1.4854 1.6213 1.5979 0.0174  -0.0742 0.0008  163  HIS   B O   
3879  C  CB  . HIS   B 163 ? 1.4153 1.5611 1.5388 0.0074  -0.0719 0.0018  163  HIS   B CB  
3880  C  CG  . HIS   B 163 ? 1.5244 1.6744 1.6530 0.0023  -0.0709 0.0021  163  HIS   B CG  
3881  N  ND1 . HIS   B 163 ? 1.5713 1.7213 1.7035 -0.0001 -0.0722 0.0010  163  HIS   B ND1 
3882  C  CD2 . HIS   B 163 ? 1.5726 1.7264 1.7029 -0.0008 -0.0688 0.0034  163  HIS   B CD2 
3883  C  CE1 . HIS   B 163 ? 1.6035 1.7569 1.7388 -0.0042 -0.0705 0.0017  163  HIS   B CE1 
3884  N  NE2 . HIS   B 163 ? 1.6528 1.8084 1.7868 -0.0047 -0.0687 0.0031  163  HIS   B NE2 
3885  N  N   . VAL   B 164 ? 1.2194 1.3500 1.3339 0.0180  -0.0801 -0.0048 164  VAL   B N   
3886  C  CA  . VAL   B 164 ? 1.1767 1.3009 1.2837 0.0239  -0.0817 -0.0053 164  VAL   B CA  
3887  C  C   . VAL   B 164 ? 1.1398 1.2625 1.2455 0.0253  -0.0825 -0.0045 164  VAL   B C   
3888  O  O   . VAL   B 164 ? 1.1298 1.2532 1.2403 0.0231  -0.0846 -0.0058 164  VAL   B O   
3889  C  CB  . VAL   B 164 ? 1.1300 1.2488 1.2355 0.0265  -0.0860 -0.0092 164  VAL   B CB  
3890  C  CG1 . VAL   B 164 ? 1.1253 1.2365 1.2212 0.0329  -0.0874 -0.0095 164  VAL   B CG1 
3891  C  CG2 . VAL   B 164 ? 1.1427 1.2637 1.2506 0.0244  -0.0853 -0.0101 164  VAL   B CG2 
3892  N  N   . ILE   B 165 ? 1.1090 1.2295 1.2084 0.0292  -0.0805 -0.0022 165  ILE   B N   
3893  C  CA  . ILE   B 165 ? 1.0651 1.1834 1.1621 0.0315  -0.0811 -0.0013 165  ILE   B CA  
3894  C  C   . ILE   B 165 ? 1.0965 1.2064 1.1877 0.0364  -0.0854 -0.0042 165  ILE   B C   
3895  O  O   . ILE   B 165 ? 1.1371 1.2453 1.2307 0.0359  -0.0887 -0.0060 165  ILE   B O   
3896  C  CB  . ILE   B 165 ? 1.0736 1.1935 1.1670 0.0336  -0.0766 0.0025  165  ILE   B CB  
3897  C  CG1 . ILE   B 165 ? 1.0599 1.1873 1.1584 0.0293  -0.0727 0.0049  165  ILE   B CG1 
3898  C  CG2 . ILE   B 165 ? 1.1200 1.2398 1.2131 0.0346  -0.0768 0.0038  165  ILE   B CG2 
3899  C  CD1 . ILE   B 165 ? 1.1110 1.2442 1.2164 0.0244  -0.0726 0.0058  165  ILE   B CD1 
3900  N  N   . ASP   B 166 ? 1.0886 1.1927 1.1719 0.0414  -0.0856 -0.0047 166  ASP   B N   
3901  C  CA  . ASP   B 166 ? 1.0790 1.1739 1.1549 0.0470  -0.0899 -0.0075 166  ASP   B CA  
3902  C  C   . ASP   B 166 ? 1.0103 1.1002 1.0799 0.0503  -0.0905 -0.0088 166  ASP   B C   
3903  O  O   . ASP   B 166 ? 1.0387 1.1301 1.1056 0.0508  -0.0860 -0.0063 166  ASP   B O   
3904  C  CB  . ASP   B 166 ? 1.0827 1.1730 1.1510 0.0517  -0.0887 -0.0056 166  ASP   B CB  
3905  C  CG  . ASP   B 166 ? 1.0672 1.1471 1.1273 0.0576  -0.0938 -0.0087 166  ASP   B CG  
3906  O  OD1 . ASP   B 166 ? 1.0259 1.1041 1.0899 0.0564  -0.0989 -0.0119 166  ASP   B OD1 
3907  O  OD2 . ASP   B 166 ? 1.0499 1.1231 1.0996 0.0635  -0.0925 -0.0078 166  ASP   B OD2 
3908  N  N   . VAL   B 167 ? 1.0289 1.1125 1.0965 0.0528  -0.0962 -0.0128 167  VAL   B N   
3909  C  CA  . VAL   B 167 ? 1.0414 1.1195 1.1029 0.0562  -0.0977 -0.0147 167  VAL   B CA  
3910  C  C   . VAL   B 167 ? 1.0436 1.1106 1.0956 0.0629  -0.1030 -0.0176 167  VAL   B C   
3911  O  O   . VAL   B 167 ? 1.0286 1.0936 1.0830 0.0631  -0.1075 -0.0199 167  VAL   B O   
3912  C  CB  . VAL   B 167 ? 0.9850 1.0673 1.0550 0.0520  -0.1001 -0.0173 167  VAL   B CB  
3913  C  CG1 . VAL   B 167 ? 0.9604 1.0441 1.0390 0.0492  -0.1050 -0.0204 167  VAL   B CG1 
3914  C  CG2 . VAL   B 167 ? 0.9730 1.0482 1.0361 0.0563  -0.1030 -0.0198 167  VAL   B CG2 
3915  N  N   . LYS   B 168 ? 1.0451 1.1045 1.0860 0.0684  -0.1025 -0.0176 168  LYS   B N   
3916  C  CA  . LYS   B 168 ? 1.0581 1.1055 1.0878 0.0755  -0.1076 -0.0204 168  LYS   B CA  
3917  C  C   . LYS   B 168 ? 1.1219 1.1631 1.1440 0.0792  -0.1087 -0.0219 168  LYS   B C   
3918  O  O   . LYS   B 168 ? 1.1668 1.2113 1.1884 0.0778  -0.1034 -0.0193 168  LYS   B O   
3919  C  CB  . LYS   B 168 ? 1.0003 1.0421 1.0197 0.0806  -0.1044 -0.0177 168  LYS   B CB  
3920  C  CG  . LYS   B 168 ? 0.9702 1.0171 0.9957 0.0778  -0.1035 -0.0162 168  LYS   B CG  
3921  C  CD  . LYS   B 168 ? 0.9652 1.0048 0.9881 0.0808  -0.1105 -0.0198 168  LYS   B CD  
3922  C  CE  . LYS   B 168 ? 1.0355 1.0815 1.0685 0.0760  -0.1112 -0.0196 168  LYS   B CE  
3923  N  NZ  . LYS   B 168 ? 1.0971 1.1443 1.1269 0.0771  -0.1065 -0.0158 168  LYS   B NZ  
3924  N  N   . PHE   B 169 ? 1.1156 1.1474 1.1318 0.0839  -0.1159 -0.0262 169  PHE   B N   
3925  C  CA  . PHE   B 169 ? 1.1462 1.1698 1.1526 0.0888  -0.1175 -0.0278 169  PHE   B CA  
3926  C  C   . PHE   B 169 ? 1.1746 1.1889 1.1648 0.0956  -0.1131 -0.0248 169  PHE   B C   
3927  O  O   . PHE   B 169 ? 1.1994 1.2081 1.1827 0.0995  -0.1134 -0.0243 169  PHE   B O   
3928  C  CB  . PHE   B 169 ? 1.2147 1.2306 1.2196 0.0922  -0.1272 -0.0335 169  PHE   B CB  
3929  C  CG  . PHE   B 169 ? 1.2488 1.2720 1.2674 0.0870  -0.1311 -0.0366 169  PHE   B CG  
3930  C  CD1 . PHE   B 169 ? 1.2661 1.2899 1.2844 0.0867  -0.1302 -0.0370 169  PHE   B CD1 
3931  C  CD2 . PHE   B 169 ? 1.2222 1.2507 1.2538 0.0827  -0.1356 -0.0393 169  PHE   B CD2 
3932  C  CE1 . PHE   B 169 ? 1.2149 1.2452 1.2457 0.0822  -0.1336 -0.0399 169  PHE   B CE1 
3933  C  CE2 . PHE   B 169 ? 1.1110 1.1459 1.1555 0.0781  -0.1388 -0.0421 169  PHE   B CE2 
3934  C  CZ  . PHE   B 169 ? 1.0982 1.1342 1.1424 0.0780  -0.1378 -0.0424 169  PHE   B CZ  
3935  N  N   . LEU   B 170 ? 1.1588 1.1709 1.1426 0.0972  -0.1087 -0.0229 170  LEU   B N   
3936  C  CA  . LEU   B 170 ? 1.1896 1.1933 1.1587 0.1032  -0.1030 -0.0196 170  LEU   B CA  
3937  C  C   . LEU   B 170 ? 1.3060 1.2937 1.2586 0.1121  -0.1083 -0.0226 170  LEU   B C   
3938  O  O   . LEU   B 170 ? 1.3405 1.3240 1.2929 0.1134  -0.1158 -0.0271 170  LEU   B O   
3939  C  CB  . LEU   B 170 ? 1.1777 1.1858 1.1474 0.1009  -0.0955 -0.0159 170  LEU   B CB  
3940  C  CG  . LEU   B 170 ? 1.1573 1.1777 1.1375 0.0947  -0.0879 -0.0113 170  LEU   B CG  
3941  C  CD1 . LEU   B 170 ? 1.2106 1.2316 1.1875 0.0944  -0.0802 -0.0074 170  LEU   B CD1 
3942  C  CD2 . LEU   B 170 ? 1.1510 1.1701 1.1282 0.0970  -0.0857 -0.0093 170  LEU   B CD2 
3943  N  N   . TYR   B 171 ? 1.3035 1.2819 1.2421 0.1185  -0.1046 -0.0202 171  TYR   B N   
3944  C  CA  . TYR   B 171 ? 1.3076 1.2694 1.2282 0.1276  -0.1090 -0.0228 171  TYR   B CA  
3945  C  C   . TYR   B 171 ? 1.3902 1.3450 1.2993 0.1314  -0.1040 -0.0207 171  TYR   B C   
3946  O  O   . TYR   B 171 ? 1.4150 1.3778 1.3298 0.1271  -0.0964 -0.0169 171  TYR   B O   
3947  C  CB  . TYR   B 171 ? 1.2772 1.2309 1.1872 0.1333  -0.1078 -0.0215 171  TYR   B CB  
3948  C  CG  . TYR   B 171 ? 1.2772 1.2313 1.1925 0.1326  -0.1154 -0.0251 171  TYR   B CG  
3949  C  CD1 . TYR   B 171 ? 1.2992 1.2460 1.2124 0.1352  -0.1259 -0.0308 171  TYR   B CD1 
3950  C  CD2 . TYR   B 171 ? 1.2906 1.2516 1.2127 0.1296  -0.1122 -0.0227 171  TYR   B CD2 
3951  C  CE1 . TYR   B 171 ? 1.3120 1.2587 1.2305 0.1345  -0.1329 -0.0341 171  TYR   B CE1 
3952  C  CE2 . TYR   B 171 ? 1.2515 1.2121 1.1779 0.1292  -0.1190 -0.0258 171  TYR   B CE2 
3953  C  CZ  . TYR   B 171 ? 1.2855 1.2389 1.2103 0.1314  -0.1293 -0.0315 171  TYR   B CZ  
3954  O  OH  . TYR   B 171 ? 1.2679 1.2208 1.1977 0.1307  -0.1361 -0.0347 171  TYR   B OH  
3955  N  N   . GLY   B 172 ? 1.4729 1.4119 1.3651 0.1397  -0.1083 -0.0232 172  GLY   B N   
3956  C  CA  . GLY   B 172 ? 1.5397 1.4698 1.4186 0.1443  -0.1038 -0.0214 172  GLY   B CA  
3957  C  C   . GLY   B 172 ? 1.5783 1.5163 1.4669 0.1389  -0.1037 -0.0219 172  GLY   B C   
3958  O  O   . GLY   B 172 ? 1.5406 1.4736 1.4210 0.1410  -0.0989 -0.0198 172  GLY   B O   
3959  N  N   . CYS   B 173 ? 1.6410 1.5910 1.5470 0.1318  -0.1087 -0.0245 173  CYS   B N   
3960  C  CA  . CYS   B 173 ? 1.6419 1.6005 1.5588 0.1261  -0.1091 -0.0254 173  CYS   B CA  
3961  C  C   . CYS   B 173 ? 1.6740 1.6206 1.5790 0.1320  -0.1140 -0.0285 173  CYS   B C   
3962  O  O   . CYS   B 173 ? 1.6818 1.6173 1.5776 0.1382  -0.1221 -0.0327 173  CYS   B O   
3963  C  CB  . CYS   B 173 ? 1.6175 1.5886 1.5535 0.1189  -0.1148 -0.0285 173  CYS   B CB  
3964  S  SG  . CYS   B 173 ? 1.6748 1.6391 1.6107 0.1226  -0.1275 -0.0350 173  CYS   B SG  
3965  N  N   . GLN   B 174 ? 1.6380 1.5864 1.5428 0.1303  -0.1094 -0.0266 174  GLN   B N   
3966  C  CA  . GLN   B 174 ? 1.6493 1.5886 1.5463 0.1345  -0.1151 -0.0302 174  GLN   B CA  
3967  C  C   . GLN   B 174 ? 1.5710 1.5183 1.4830 0.1301  -0.1240 -0.0353 174  GLN   B C   
3968  O  O   . GLN   B 174 ? 1.5595 1.4985 1.4667 0.1348  -0.1332 -0.0403 174  GLN   B O   
3969  C  CB  . GLN   B 174 ? 1.7154 1.6538 1.6075 0.1340  -0.1075 -0.0266 174  GLN   B CB  
3970  C  CG  . GLN   B 174 ? 1.8653 1.7972 1.7447 0.1375  -0.0972 -0.0209 174  GLN   B CG  
3971  C  CD  . GLN   B 174 ? 1.9000 1.8125 1.7566 0.1483  -0.0989 -0.0217 174  GLN   B CD  
3972  O  OE1 . GLN   B 174 ? 1.8805 1.7823 1.7279 0.1539  -0.1075 -0.0263 174  GLN   B OE1 
3973  N  NE2 . GLN   B 174 ? 1.8659 1.7736 1.7132 0.1513  -0.0906 -0.0171 174  GLN   B NE2 
3974  N  N   . ALA   B 175 ? 1.5199 1.4831 1.4505 0.1212  -0.1214 -0.0342 175  ALA   B N   
3975  C  CA  . ALA   B 175 ? 1.4483 1.4208 1.3953 0.1160  -0.1283 -0.0383 175  ALA   B CA  
3976  C  C   . ALA   B 175 ? 1.4110 1.3953 1.3722 0.1097  -0.1267 -0.0371 175  ALA   B C   
3977  O  O   . ALA   B 175 ? 1.4390 1.4269 1.3994 0.1079  -0.1193 -0.0325 175  ALA   B O   
3978  C  CB  . ALA   B 175 ? 1.4038 1.3837 1.3590 0.1113  -0.1262 -0.0381 175  ALA   B CB  
3979  N  N   . PRO   B 176 ? 1.3606 1.3512 1.3353 0.1062  -0.1336 -0.0411 176  PRO   B N   
3980  C  CA  . PRO   B 176 ? 1.3445 1.3446 1.3314 0.1008  -0.1327 -0.0403 176  PRO   B CA  
3981  C  C   . PRO   B 176 ? 1.3378 1.3501 1.3335 0.0938  -0.1236 -0.0352 176  PRO   B C   
3982  O  O   . PRO   B 176 ? 1.3221 1.3445 1.3300 0.0875  -0.1219 -0.0349 176  PRO   B O   
3983  C  CB  . PRO   B 176 ? 1.2577 1.2633 1.2591 0.0975  -0.1407 -0.0453 176  PRO   B CB  
3984  C  CG  . PRO   B 176 ? 1.3043 1.3052 1.3026 0.1003  -0.1447 -0.0483 176  PRO   B CG  
3985  C  CD  . PRO   B 176 ? 1.3669 1.3544 1.3450 0.1080  -0.1429 -0.0468 176  PRO   B CD  
3986  N  N   . THR   B 177 ? 1.2991 1.3103 1.2888 0.0949  -0.1180 -0.0313 177  THR   B N   
3987  C  CA  . THR   B 177 ? 1.2302 1.2514 1.2262 0.0893  -0.1093 -0.0262 177  THR   B CA  
3988  C  C   . THR   B 177 ? 1.2441 1.2724 1.2487 0.0856  -0.1086 -0.0251 177  THR   B C   
3989  O  O   . THR   B 177 ? 1.2599 1.2819 1.2586 0.0897  -0.1115 -0.0261 177  THR   B O   
3990  C  CB  . THR   B 177 ? 1.2802 1.2949 1.2629 0.0936  -0.1022 -0.0220 177  THR   B CB  
3991  O  OG1 . THR   B 177 ? 1.3121 1.3197 1.2863 0.0970  -0.1024 -0.0228 177  THR   B OG1 
3992  C  CG2 . THR   B 177 ? 1.2714 1.2969 1.2620 0.0877  -0.0937 -0.0170 177  THR   B CG2 
3993  N  N   . ILE   B 178 ? 1.2640 1.3047 1.2817 0.0781  -0.1047 -0.0230 178  ILE   B N   
3994  C  CA  . ILE   B 178 ? 1.1446 1.1927 1.1707 0.0740  -0.1031 -0.0214 178  ILE   B CA  
3995  C  C   . ILE   B 178 ? 1.1533 1.2076 1.1804 0.0713  -0.0947 -0.0162 178  ILE   B C   
3996  O  O   . ILE   B 178 ? 1.1608 1.2202 1.1915 0.0678  -0.0907 -0.0144 178  ILE   B O   
3997  C  CB  . ILE   B 178 ? 1.1006 1.1578 1.1420 0.0675  -0.1065 -0.0238 178  ILE   B CB  
3998  C  CG1 . ILE   B 178 ? 1.1339 1.1986 1.1828 0.0625  -0.1038 -0.0232 178  ILE   B CG1 
3999  C  CG2 . ILE   B 178 ? 1.1130 1.1647 1.1552 0.0702  -0.1150 -0.0290 178  ILE   B CG2 
4000  C  CD1 . ILE   B 178 ? 1.0144 1.0884 1.0781 0.0559  -0.1055 -0.0247 178  ILE   B CD1 
4001  N  N   . CYS   B 179 ? 1.1514 1.2050 1.1756 0.0728  -0.0921 -0.0138 179  CYS   B N   
4002  C  CA  . CYS   B 179 ? 1.1353 1.1960 1.1628 0.0698  -0.0847 -0.0090 179  CYS   B CA  
4003  C  C   . CYS   B 179 ? 1.0787 1.1490 1.1184 0.0639  -0.0852 -0.0087 179  CYS   B C   
4004  O  O   . CYS   B 179 ? 1.0147 1.0830 1.0551 0.0649  -0.0893 -0.0105 179  CYS   B O   
4005  C  CB  . CYS   B 179 ? 1.0855 1.1393 1.1019 0.0756  -0.0807 -0.0062 179  CYS   B CB  
4006  S  SG  . CYS   B 179 ? 1.0656 1.1291 1.0884 0.0716  -0.0723 -0.0007 179  CYS   B SG  
4007  N  N   . PHE   B 180 ? 1.1236 1.2037 1.1725 0.0578  -0.0813 -0.0064 180  PHE   B N   
4008  C  CA  . PHE   B 180 ? 1.1397 1.2287 1.1997 0.0520  -0.0814 -0.0059 180  PHE   B CA  
4009  C  C   . PHE   B 180 ? 1.1059 1.2024 1.1700 0.0487  -0.0751 -0.0015 180  PHE   B C   
4010  O  O   . PHE   B 180 ? 1.1404 1.2367 1.2013 0.0495  -0.0706 0.0009  180  PHE   B O   
4011  C  CB  . PHE   B 180 ? 1.1282 1.2217 1.1973 0.0472  -0.0851 -0.0089 180  PHE   B CB  
4012  C  CG  . PHE   B 180 ? 1.1400 1.2380 1.2126 0.0437  -0.0823 -0.0081 180  PHE   B CG  
4013  C  CD1 . PHE   B 180 ? 1.1807 1.2734 1.2460 0.0471  -0.0815 -0.0083 180  PHE   B CD1 
4014  C  CD2 . PHE   B 180 ? 1.1267 1.2336 1.2094 0.0372  -0.0808 -0.0073 180  PHE   B CD2 
4015  C  CE1 . PHE   B 180 ? 1.2288 1.3253 1.2972 0.0438  -0.0790 -0.0076 180  PHE   B CE1 
4016  C  CE2 . PHE   B 180 ? 1.1686 1.2791 1.2541 0.0341  -0.0785 -0.0067 180  PHE   B CE2 
4017  C  CZ  . PHE   B 180 ? 1.2106 1.3160 1.2892 0.0373  -0.0776 -0.0068 180  PHE   B CZ  
4018  N  N   . VAL   B 181 ? 1.0840 1.1867 1.1553 0.0451  -0.0749 -0.0005 181  VAL   B N   
4019  C  CA  . VAL   B 181 ? 1.1112 1.2211 1.1873 0.0420  -0.0700 0.0033  181  VAL   B CA  
4020  C  C   . VAL   B 181 ? 1.1567 1.2745 1.2430 0.0354  -0.0711 0.0029  181  VAL   B C   
4021  O  O   . VAL   B 181 ? 1.1822 1.3004 1.2717 0.0341  -0.0743 0.0012  181  VAL   B O   
4022  C  CB  . VAL   B 181 ? 1.0472 1.1558 1.1203 0.0451  -0.0686 0.0054  181  VAL   B CB  
4023  C  CG1 . VAL   B 181 ? 1.0361 1.1535 1.1169 0.0408  -0.0652 0.0085  181  VAL   B CG1 
4024  C  CG2 . VAL   B 181 ? 1.0543 1.1559 1.1174 0.0513  -0.0656 0.0069  181  VAL   B CG2 
4025  N  N   . TYR   B 182 ? 1.1706 1.2940 1.2616 0.0313  -0.0683 0.0043  182  TYR   B N   
4026  C  CA  . TYR   B 182 ? 1.1763 1.3066 1.2759 0.0253  -0.0688 0.0041  182  TYR   B CA  
4027  C  C   . TYR   B 182 ? 1.1895 1.3262 1.2933 0.0224  -0.0651 0.0075  182  TYR   B C   
4028  O  O   . TYR   B 182 ? 1.2090 1.3458 1.3104 0.0246  -0.0618 0.0101  182  TYR   B O   
4029  C  CB  . TYR   B 182 ? 1.1678 1.2988 1.2694 0.0228  -0.0694 0.0023  182  TYR   B CB  
4030  C  CG  . TYR   B 182 ? 1.1891 1.3193 1.2872 0.0238  -0.0660 0.0039  182  TYR   B CG  
4031  C  CD1 . TYR   B 182 ? 1.1896 1.3128 1.2794 0.0292  -0.0656 0.0037  182  TYR   B CD1 
4032  C  CD2 . TYR   B 182 ? 1.1983 1.3340 1.3011 0.0194  -0.0634 0.0055  182  TYR   B CD2 
4033  C  CE1 . TYR   B 182 ? 1.2197 1.3416 1.3062 0.0301  -0.0622 0.0053  182  TYR   B CE1 
4034  C  CE2 . TYR   B 182 ? 1.1910 1.3256 1.2910 0.0202  -0.0603 0.0069  182  TYR   B CE2 
4035  C  CZ  . TYR   B 182 ? 1.2180 1.3457 1.3099 0.0254  -0.0595 0.0069  182  TYR   B CZ  
4036  O  OH  . TYR   B 182 ? 1.2556 1.3817 1.3444 0.0263  -0.0561 0.0085  182  TYR   B OH  
4037  N  N   . GLN   B 183 ? 1.2633 1.4051 1.3734 0.0177  -0.0659 0.0075  183  GLN   B N   
4038  C  CA  . GLN   B 183 ? 1.2821 1.4301 1.3967 0.0144  -0.0632 0.0103  183  GLN   B CA  
4039  C  C   . GLN   B 183 ? 1.3521 1.5036 1.4707 0.0099  -0.0628 0.0099  183  GLN   B C   
4040  O  O   . GLN   B 183 ? 1.2948 1.4454 1.4148 0.0081  -0.0649 0.0074  183  GLN   B O   
4041  C  CB  . GLN   B 183 ? 1.2549 1.4055 1.3726 0.0129  -0.0643 0.0110  183  GLN   B CB  
4042  C  CG  . GLN   B 183 ? 1.2636 1.4201 1.3856 0.0100  -0.0621 0.0138  183  GLN   B CG  
4043  C  CD  . GLN   B 183 ? 1.3046 1.4627 1.4283 0.0096  -0.0630 0.0148  183  GLN   B CD  
4044  O  OE1 . GLN   B 183 ? 1.3041 1.4600 1.4251 0.0132  -0.0631 0.0154  183  GLN   B OE1 
4045  N  NE2 . GLN   B 183 ? 1.3288 1.4902 1.4562 0.0054  -0.0638 0.0149  183  GLN   B NE2 
4046  N  N   . ASP   B 184 ? 1.3447 1.4996 1.4650 0.0084  -0.0599 0.0122  184  ASP   B N   
4047  C  CA  . ASP   B 184 ? 1.3280 1.4863 1.4517 0.0043  -0.0590 0.0123  184  ASP   B CA  
4048  C  C   . ASP   B 184 ? 1.4121 1.5759 1.5407 0.0009  -0.0584 0.0143  184  ASP   B C   
4049  O  O   . ASP   B 184 ? 1.4442 1.6094 1.5735 0.0023  -0.0581 0.0159  184  ASP   B O   
4050  C  CB  . ASP   B 184 ? 1.3194 1.4768 1.4412 0.0054  -0.0563 0.0134  184  ASP   B CB  
4051  C  CG  . ASP   B 184 ? 1.4409 1.5953 1.5606 0.0052  -0.0572 0.0111  184  ASP   B CG  
4052  O  OD1 . ASP   B 184 ? 1.4943 1.6481 1.6151 0.0037  -0.0599 0.0086  184  ASP   B OD1 
4053  O  OD2 . ASP   B 184 ? 1.4728 1.6251 1.5897 0.0066  -0.0551 0.0118  184  ASP   B OD2 
4054  N  N   . PRO   B 185 ? 1.4514 1.6181 1.5831 -0.0032 -0.0584 0.0142  185  PRO   B N   
4055  C  CA  . PRO   B 185 ? 1.4135 1.5848 1.5491 -0.0059 -0.0577 0.0164  185  PRO   B CA  
4056  C  C   . PRO   B 185 ? 1.4687 1.6418 1.6055 -0.0038 -0.0551 0.0189  185  PRO   B C   
4057  O  O   . PRO   B 185 ? 1.5011 1.6775 1.6411 -0.0039 -0.0549 0.0207  185  PRO   B O   
4058  C  CB  . PRO   B 185 ? 1.3838 1.5565 1.5211 -0.0098 -0.0578 0.0156  185  PRO   B CB  
4059  C  CG  . PRO   B 185 ? 1.4339 1.6029 1.5681 -0.0087 -0.0577 0.0136  185  PRO   B CG  
4060  C  CD  . PRO   B 185 ? 1.4921 1.6576 1.6236 -0.0055 -0.0591 0.0121  185  PRO   B CD  
4061  N  N   . GLN   B 186 ? 1.4337 1.6043 1.5680 -0.0016 -0.0530 0.0190  186  GLN   B N   
4062  C  CA  . GLN   B 186 ? 1.4220 1.5938 1.5575 0.0004  -0.0497 0.0216  186  GLN   B CA  
4063  C  C   . GLN   B 186 ? 1.4561 1.6261 1.5892 0.0050  -0.0488 0.0226  186  GLN   B C   
4064  O  O   . GLN   B 186 ? 1.4542 1.6265 1.5900 0.0063  -0.0460 0.0251  186  GLN   B O   
4065  C  CB  . GLN   B 186 ? 1.4273 1.5959 1.5599 0.0014  -0.0473 0.0215  186  GLN   B CB  
4066  C  CG  . GLN   B 186 ? 1.4621 1.6321 1.5968 -0.0029 -0.0479 0.0206  186  GLN   B CG  
4067  C  CD  . GLN   B 186 ? 1.5165 1.6819 1.6463 -0.0024 -0.0497 0.0177  186  GLN   B CD  
4068  O  OE1 . GLN   B 186 ? 1.5832 1.7437 1.7077 0.0015  -0.0496 0.0168  186  GLN   B OE1 
4069  N  NE2 . GLN   B 186 ? 1.4967 1.6635 1.6283 -0.0062 -0.0515 0.0163  186  GLN   B NE2 
4070  N  N   . GLY   B 187 ? 1.4949 1.6607 1.6233 0.0074  -0.0510 0.0207  187  GLY   B N   
4071  C  CA  . GLY   B 187 ? 1.4476 1.6113 1.5732 0.0118  -0.0506 0.0215  187  GLY   B CA  
4072  C  C   . GLY   B 187 ? 1.4139 1.5709 1.5326 0.0153  -0.0526 0.0191  187  GLY   B C   
4073  O  O   . GLY   B 187 ? 1.4345 1.5897 1.5524 0.0137  -0.0552 0.0165  187  GLY   B O   
4074  N  N   . ARG   B 188 ? 1.2576 1.4107 1.3716 0.0203  -0.0514 0.0199  188  ARG   B N   
4075  C  CA  . ARG   B 188 ? 1.2196 1.3652 1.3261 0.0245  -0.0534 0.0176  188  ARG   B CA  
4076  C  C   . ARG   B 188 ? 1.2744 1.4147 1.3746 0.0285  -0.0506 0.0182  188  ARG   B C   
4077  O  O   . ARG   B 188 ? 1.3138 1.4542 1.4130 0.0309  -0.0464 0.0209  188  ARG   B O   
4078  C  CB  . ARG   B 188 ? 1.1680 1.3114 1.2720 0.0279  -0.0545 0.0178  188  ARG   B CB  
4079  C  CG  . ARG   B 188 ? 1.2047 1.3515 1.3133 0.0247  -0.0575 0.0171  188  ARG   B CG  
4080  C  CD  . ARG   B 188 ? 1.1553 1.2965 1.2598 0.0268  -0.0614 0.0143  188  ARG   B CD  
4081  N  NE  . ARG   B 188 ? 1.0875 1.2309 1.1954 0.0246  -0.0636 0.0140  188  ARG   B NE  
4082  C  CZ  . ARG   B 188 ? 1.0893 1.2310 1.1952 0.0274  -0.0641 0.0148  188  ARG   B CZ  
4083  N  NH1 . ARG   B 188 ? 1.0800 1.2180 1.1806 0.0325  -0.0623 0.0159  188  ARG   B NH1 
4084  N  NH2 . ARG   B 188 ? 1.1784 1.3216 1.2872 0.0252  -0.0662 0.0144  188  ARG   B NH2 
4085  N  N   . HIS   B 189 ? 1.2339 1.3692 1.3295 0.0294  -0.0527 0.0156  189  HIS   B N   
4086  C  CA  . HIS   B 189 ? 1.2202 1.3496 1.3089 0.0331  -0.0503 0.0159  189  HIS   B CA  
4087  C  C   . HIS   B 189 ? 1.1902 1.3109 1.2703 0.0380  -0.0539 0.0129  189  HIS   B C   
4088  O  O   . HIS   B 189 ? 1.1827 1.3028 1.2639 0.0375  -0.0584 0.0105  189  HIS   B O   
4089  C  CB  . HIS   B 189 ? 1.2720 1.4034 1.3633 0.0295  -0.0495 0.0156  189  HIS   B CB  
4090  C  CG  . HIS   B 189 ? 1.2853 1.4253 1.3860 0.0235  -0.0488 0.0168  189  HIS   B CG  
4091  N  ND1 . HIS   B 189 ? 1.3467 1.4923 1.4528 0.0220  -0.0459 0.0197  189  HIS   B ND1 
4092  C  CD2 . HIS   B 189 ? 1.3230 1.4666 1.4284 0.0187  -0.0509 0.0153  189  HIS   B CD2 
4093  C  CE1 . HIS   B 189 ? 1.3782 1.5301 1.4915 0.0167  -0.0467 0.0199  189  HIS   B CE1 
4094  N  NE2 . HIS   B 189 ? 1.3624 1.5130 1.4750 0.0146  -0.0494 0.0173  189  HIS   B NE2 
4095  N  N   . VAL   B 190 ? 1.1878 1.3012 1.2593 0.0427  -0.0519 0.0132  190  VAL   B N   
4096  C  CA  . VAL   B 190 ? 1.1523 1.2561 1.2142 0.0480  -0.0556 0.0104  190  VAL   B CA  
4097  C  C   . VAL   B 190 ? 1.1467 1.2463 1.2045 0.0487  -0.0559 0.0089  190  VAL   B C   
4098  O  O   . VAL   B 190 ? 1.2038 1.3035 1.2605 0.0484  -0.0512 0.0113  190  VAL   B O   
4099  C  CB  . VAL   B 190 ? 1.1305 1.2272 1.1832 0.0546  -0.0532 0.0119  190  VAL   B CB  
4100  C  CG1 . VAL   B 190 ? 1.1554 1.2421 1.1986 0.0599  -0.0583 0.0085  190  VAL   B CG1 
4101  C  CG2 . VAL   B 190 ? 1.1471 1.2488 1.2045 0.0539  -0.0517 0.0140  190  VAL   B CG2 
4102  N  N   . LYS   B 191 ? 1.1225 1.2178 1.1779 0.0497  -0.0615 0.0050  191  LYS   B N   
4103  C  CA  . LYS   B 191 ? 1.1496 1.2404 1.2008 0.0507  -0.0627 0.0032  191  LYS   B CA  
4104  C  C   . LYS   B 191 ? 1.1654 1.2471 1.2088 0.0559  -0.0685 -0.0007 191  LYS   B C   
4105  O  O   . LYS   B 191 ? 1.1828 1.2626 1.2257 0.0577  -0.0720 -0.0022 191  LYS   B O   
4106  C  CB  . LYS   B 191 ? 1.1896 1.2879 1.2505 0.0444  -0.0640 0.0020  191  LYS   B CB  
4107  C  CG  . LYS   B 191 ? 1.2432 1.3387 1.3007 0.0446  -0.0627 0.0018  191  LYS   B CG  
4108  C  CD  . LYS   B 191 ? 1.2349 1.3338 1.2988 0.0408  -0.0666 -0.0013 191  LYS   B CD  
4109  C  CE  . LYS   B 191 ? 1.2037 1.3125 1.2787 0.0343  -0.0660 -0.0005 191  LYS   B CE  
4110  N  NZ  . LYS   B 191 ? 1.2604 1.3728 1.3402 0.0303  -0.0661 -0.0014 191  LYS   B NZ  
4111  N  N   . THR   B 192 ? 1.2101 1.2856 1.2473 0.0585  -0.0697 -0.0023 192  THR   B N   
4112  C  CA  . THR   B 192 ? 1.2295 1.2963 1.2599 0.0633  -0.0761 -0.0065 192  THR   B CA  
4113  C  C   . THR   B 192 ? 1.2289 1.2959 1.2620 0.0615  -0.0793 -0.0094 192  THR   B C   
4114  O  O   . THR   B 192 ? 1.1943 1.2639 1.2286 0.0591  -0.0757 -0.0078 192  THR   B O   
4115  C  CB  . THR   B 192 ? 1.2150 1.2695 1.2301 0.0712  -0.0751 -0.0059 192  THR   B CB  
4116  O  OG1 . THR   B 192 ? 1.2363 1.2886 1.2463 0.0720  -0.0694 -0.0031 192  THR   B OG1 
4117  C  CG2 . THR   B 192 ? 1.1990 1.2517 1.2104 0.0741  -0.0730 -0.0038 192  THR   B CG2 
4118  N  N   . TYR   B 193 ? 1.2437 1.3082 1.2782 0.0627  -0.0863 -0.0137 193  TYR   B N   
4119  C  CA  . TYR   B 193 ? 1.2506 1.3144 1.2875 0.0621  -0.0905 -0.0172 193  TYR   B CA  
4120  C  C   . TYR   B 193 ? 1.2769 1.3295 1.3045 0.0690  -0.0970 -0.0210 193  TYR   B C   
4121  O  O   . TYR   B 193 ? 1.2553 1.3024 1.2773 0.0730  -0.0993 -0.0217 193  TYR   B O   
4122  C  CB  . TYR   B 193 ? 1.2412 1.3145 1.2926 0.0559  -0.0932 -0.0192 193  TYR   B CB  
4123  C  CG  . TYR   B 193 ? 1.2673 1.3507 1.3276 0.0491  -0.0879 -0.0162 193  TYR   B CG  
4124  C  CD1 . TYR   B 193 ? 1.2940 1.3781 1.3514 0.0482  -0.0830 -0.0136 193  TYR   B CD1 
4125  C  CD2 . TYR   B 193 ? 1.2862 1.3781 1.3574 0.0438  -0.0879 -0.0160 193  TYR   B CD2 
4126  C  CE1 . TYR   B 193 ? 1.3181 1.4110 1.3835 0.0420  -0.0787 -0.0111 193  TYR   B CE1 
4127  C  CE2 . TYR   B 193 ? 1.3037 1.4041 1.3821 0.0379  -0.0835 -0.0134 193  TYR   B CE2 
4128  C  CZ  . TYR   B 193 ? 1.3165 1.4174 1.3921 0.0371  -0.0792 -0.0111 193  TYR   B CZ  
4129  O  OH  . TYR   B 193 ? 1.3181 1.4269 1.4007 0.0314  -0.0754 -0.0087 193  TYR   B OH  
4130  N  N   . GLU   B 194 ? 1.2214 1.2706 1.2473 0.0705  -0.1002 -0.0238 194  GLU   B N   
4131  C  CA  . GLU   B 194 ? 1.1817 1.2207 1.2000 0.0767  -0.1075 -0.0281 194  GLU   B CA  
4132  C  C   . GLU   B 194 ? 1.1894 1.2337 1.2201 0.0735  -0.1137 -0.0325 194  GLU   B C   
4133  O  O   . GLU   B 194 ? 1.2592 1.3111 1.2988 0.0684  -0.1119 -0.0323 194  GLU   B O   
4134  C  CB  . GLU   B 194 ? 1.2403 1.2696 1.2453 0.0820  -0.1064 -0.0278 194  GLU   B CB  
4135  C  CG  . GLU   B 194 ? 1.3164 1.3413 1.3105 0.0844  -0.0985 -0.0228 194  GLU   B CG  
4136  C  CD  . GLU   B 194 ? 1.3643 1.3738 1.3399 0.0933  -0.0996 -0.0233 194  GLU   B CD  
4137  O  OE1 . GLU   B 194 ? 1.3575 1.3608 1.3274 0.0962  -0.1025 -0.0255 194  GLU   B OE1 
4138  O  OE2 . GLU   B 194 ? 1.3282 1.3316 1.2946 0.0975  -0.0974 -0.0214 194  GLU   B OE2 
4139  N  N   . VAL   B 195 ? 1.1686 1.2088 1.2001 0.0763  -0.1209 -0.0364 195  VAL   B N   
4140  C  CA  . VAL   B 195 ? 1.2049 1.2508 1.2500 0.0729  -0.1267 -0.0405 195  VAL   B CA  
4141  C  C   . VAL   B 195 ? 1.2687 1.3074 1.3096 0.0775  -0.1330 -0.0447 195  VAL   B C   
4142  O  O   . VAL   B 195 ? 1.3297 1.3587 1.3630 0.0836  -0.1394 -0.0479 195  VAL   B O   
4143  C  CB  . VAL   B 195 ? 1.2341 1.2806 1.2847 0.0725  -0.1309 -0.0424 195  VAL   B CB  
4144  C  CG1 . VAL   B 195 ? 1.2145 1.2693 1.2820 0.0673  -0.1346 -0.0456 195  VAL   B CG1 
4145  C  CG2 . VAL   B 195 ? 1.2005 1.2512 1.2507 0.0699  -0.1246 -0.0378 195  VAL   B CG2 
4146  N  N   . SER   B 196 ? 1.3091 1.3522 1.3548 0.0748  -0.1313 -0.0448 196  SER   B N   
4147  C  CA  . SER   B 196 ? 1.3531 1.3902 1.3959 0.0789  -0.1372 -0.0488 196  SER   B CA  
4148  C  C   . SER   B 196 ? 1.3783 1.4199 1.4355 0.0769  -0.1444 -0.0537 196  SER   B C   
4149  O  O   . SER   B 196 ? 1.3658 1.4176 1.4372 0.0709  -0.1429 -0.0541 196  SER   B O   
4150  C  CB  . SER   B 196 ? 1.4841 1.5241 1.5268 0.0768  -0.1327 -0.0471 196  SER   B CB  
4151  O  OG  . SER   B 196 ? 1.6089 1.6438 1.6504 0.0806  -0.1389 -0.0514 196  SER   B OG  
4152  N  N   . LEU   B 197 ? 1.3512 1.3850 1.4047 0.0820  -0.1520 -0.0575 197  LEU   B N   
4153  C  CA  . LEU   B 197 ? 1.3577 1.3946 1.4249 0.0809  -0.1597 -0.0627 197  LEU   B CA  
4154  C  C   . LEU   B 197 ? 1.4759 1.5143 1.5481 0.0811  -0.1624 -0.0655 197  LEU   B C   
4155  O  O   . LEU   B 197 ? 1.4726 1.5197 1.5612 0.0765  -0.1640 -0.0678 197  LEU   B O   
4156  C  CB  . LEU   B 197 ? 1.3540 1.3804 1.4142 0.0874  -0.1682 -0.0665 197  LEU   B CB  
4157  C  CG  . LEU   B 197 ? 1.3270 1.3502 1.3819 0.0883  -0.1675 -0.0648 197  LEU   B CG  
4158  C  CD1 . LEU   B 197 ? 1.4017 1.4117 1.4462 0.0963  -0.1767 -0.0690 197  LEU   B CD1 
4159  C  CD2 . LEU   B 197 ? 1.2827 1.3169 1.3553 0.0813  -0.1667 -0.0649 197  LEU   B CD2 
4160  N  N   . ARG   B 198 ? 1.5211 1.5506 1.5791 0.0866  -0.1628 -0.0654 198  ARG   B N   
4161  C  CA  . ARG   B 198 ? 1.4975 1.5270 1.5583 0.0877  -0.1656 -0.0681 198  ARG   B CA  
4162  C  C   . ARG   B 198 ? 1.5481 1.5902 1.6222 0.0800  -0.1592 -0.0659 198  ARG   B C   
4163  O  O   . ARG   B 198 ? 1.5760 1.6245 1.6640 0.0775  -0.1624 -0.0691 198  ARG   B O   
4164  C  CB  . ARG   B 198 ? 1.4783 1.4958 1.5197 0.0944  -0.1650 -0.0670 198  ARG   B CB  
4165  N  N   . GLU   B 199 ? 1.7057 1.7518 1.7762 0.0763  -0.1503 -0.0605 199  GLU   B N   
4166  C  CA  . GLU   B 199 ? 1.7534 1.8107 1.8349 0.0692  -0.1441 -0.0582 199  GLU   B CA  
4167  C  C   . GLU   B 199 ? 1.7242 1.7918 1.8195 0.0625  -0.1413 -0.0570 199  GLU   B C   
4168  O  O   . GLU   B 199 ? 1.7745 1.8513 1.8792 0.0566  -0.1364 -0.0552 199  GLU   B O   
4169  C  CB  . GLU   B 199 ? 1.8329 1.8887 1.9035 0.0686  -0.1362 -0.0533 199  GLU   B CB  
4170  C  CG  . GLU   B 199 ? 1.8358 1.8965 1.9056 0.0644  -0.1287 -0.0482 199  GLU   B CG  
4171  C  CD  . GLU   B 199 ? 1.8389 1.8992 1.9005 0.0632  -0.1210 -0.0435 199  GLU   B CD  
4172  O  OE1 . GLU   B 199 ? 1.8606 1.9115 1.9087 0.0685  -0.1209 -0.0431 199  GLU   B OE1 
4173  O  OE2 . GLU   B 199 ? 1.7497 1.8188 1.8183 0.0570  -0.1151 -0.0404 199  GLU   B OE2 
4174  N  N   . LYS   B 200 ? 1.5423 1.6081 1.6387 0.0636  -0.1446 -0.0580 200  LYS   B N   
4175  C  CA  . LYS   B 200 ? 1.4047 1.4791 1.5132 0.0577  -0.1424 -0.0569 200  LYS   B CA  
4176  C  C   . LYS   B 200 ? 1.4280 1.5099 1.5379 0.0519  -0.1333 -0.0518 200  LYS   B C   
4177  O  O   . LYS   B 200 ? 1.3486 1.4397 1.4709 0.0459  -0.1303 -0.0512 200  LYS   B O   
4178  C  CB  . LYS   B 200 ? 1.2708 1.3514 1.3966 0.0548  -0.1468 -0.0611 200  LYS   B CB  
4179  N  N   . GLU   B 201 ? 1.3760 1.4537 1.4728 0.0539  -0.1289 -0.0480 201  GLU   B N   
4180  C  CA  . GLU   B 201 ? 1.3431 1.4267 1.4398 0.0492  -0.1208 -0.0431 201  GLU   B CA  
4181  C  C   . GLU   B 201 ? 1.2965 1.3737 1.3794 0.0529  -0.1180 -0.0398 201  GLU   B C   
4182  O  O   . GLU   B 201 ? 1.3280 1.3958 1.4008 0.0591  -0.1220 -0.0414 201  GLU   B O   
4183  C  CB  . GLU   B 201 ? 1.3690 1.4562 1.4671 0.0466  -0.1170 -0.0419 201  GLU   B CB  
4184  N  N   . PHE   B 202 ? 1.2477 1.3298 1.3302 0.0491  -0.1111 -0.0353 202  PHE   B N   
4185  C  CA  . PHE   B 202 ? 1.2507 1.3281 1.3218 0.0519  -0.1071 -0.0316 202  PHE   B CA  
4186  C  C   . PHE   B 202 ? 1.3188 1.3916 1.3802 0.0542  -0.1036 -0.0298 202  PHE   B C   
4187  O  O   . PHE   B 202 ? 1.4171 1.4936 1.4825 0.0512  -0.1020 -0.0297 202  PHE   B O   
4188  C  CB  . PHE   B 202 ? 1.2091 1.2941 1.2851 0.0468  -0.1015 -0.0277 202  PHE   B CB  
4189  C  CG  . PHE   B 202 ? 1.1668 1.2532 1.2471 0.0463  -0.1038 -0.0283 202  PHE   B CG  
4190  C  CD1 . PHE   B 202 ? 1.1981 1.2766 1.2718 0.0518  -0.1085 -0.0305 202  PHE   B CD1 
4191  C  CD2 . PHE   B 202 ? 1.1460 1.2411 1.2363 0.0404  -0.1012 -0.0268 202  PHE   B CD2 
4192  C  CE1 . PHE   B 202 ? 1.2120 1.2915 1.2895 0.0513  -0.1106 -0.0310 202  PHE   B CE1 
4193  C  CE2 . PHE   B 202 ? 1.1166 1.2127 1.2105 0.0399  -0.1031 -0.0272 202  PHE   B CE2 
4194  C  CZ  . PHE   B 202 ? 1.1697 1.2581 1.2575 0.0452  -0.1077 -0.0293 202  PHE   B CZ  
4195  N  N   . ASN   B 203 ? 1.2870 1.3513 1.3353 0.0594  -0.1021 -0.0280 203  ASN   B N   
4196  C  CA  . ASN   B 203 ? 1.2619 1.3212 1.3002 0.0616  -0.0976 -0.0254 203  ASN   B CA  
4197  C  C   . ASN   B 203 ? 1.2212 1.2798 1.2537 0.0621  -0.0913 -0.0207 203  ASN   B C   
4198  O  O   . ASN   B 203 ? 1.2136 1.2711 1.2448 0.0637  -0.0921 -0.0204 203  ASN   B O   
4199  C  CB  . ASN   B 203 ? 1.3062 1.3533 1.3323 0.0690  -0.1020 -0.0282 203  ASN   B CB  
4200  C  CG  . ASN   B 203 ? 1.4209 1.4688 1.4526 0.0688  -0.1078 -0.0326 203  ASN   B CG  
4201  O  OD1 . ASN   B 203 ? 1.4826 1.5386 1.5242 0.0635  -0.1061 -0.0325 203  ASN   B OD1 
4202  N  ND2 . ASN   B 203 ? 1.4087 1.4474 1.4337 0.0750  -0.1147 -0.0365 203  ASN   B ND2 
4203  N  N   . LYS   B 204 ? 1.2023 1.2615 1.2316 0.0607  -0.0850 -0.0172 204  LYS   B N   
4204  C  CA  . LYS   B 204 ? 1.1954 1.2556 1.2218 0.0603  -0.0785 -0.0126 204  LYS   B CA  
4205  C  C   . LYS   B 204 ? 1.1968 1.2466 1.2107 0.0674  -0.0791 -0.0123 204  LYS   B C   
4206  O  O   . LYS   B 204 ? 1.2643 1.3039 1.2679 0.0733  -0.0827 -0.0147 204  LYS   B O   
4207  C  CB  . LYS   B 204 ? 1.1412 1.2019 1.1654 0.0585  -0.0722 -0.0092 204  LYS   B CB  
4208  N  N   . GLY   B 205 ? 1.1909 1.2430 1.2053 0.0672  -0.0757 -0.0095 205  GLY   B N   
4209  C  CA  . GLY   B 205 ? 1.2187 1.2617 1.2222 0.0737  -0.0765 -0.0094 205  GLY   B CA  
4210  C  C   . GLY   B 205 ? 1.2155 1.2512 1.2074 0.0779  -0.0696 -0.0055 205  GLY   B C   
4211  O  O   . GLY   B 205 ? 1.2746 1.3114 1.2663 0.0761  -0.0645 -0.0030 205  GLY   B O   
4212  N  N   . PRO   B 206 ? 1.1940 1.2217 1.1760 0.0838  -0.0693 -0.0049 206  PRO   B N   
4213  C  CA  . PRO   B 206 ? 1.2057 1.2263 1.1767 0.0880  -0.0620 -0.0008 206  PRO   B CA  
4214  C  C   . PRO   B 206 ? 1.2382 1.2680 1.2174 0.0834  -0.0539 0.0041  206  PRO   B C   
4215  O  O   . PRO   B 206 ? 1.2615 1.2888 1.2367 0.0840  -0.0472 0.0075  206  PRO   B O   
4216  C  CB  . PRO   B 206 ? 1.2339 1.2432 1.1922 0.0958  -0.0646 -0.0020 206  PRO   B CB  
4217  C  CG  . PRO   B 206 ? 1.2053 1.2183 1.1706 0.0943  -0.0726 -0.0060 206  PRO   B CG  
4218  C  CD  . PRO   B 206 ? 1.2140 1.2351 1.1909 0.0885  -0.0766 -0.0087 206  PRO   B CD  
4219  N  N   . TRP   B 207 ? 1.2022 1.2422 1.1929 0.0788  -0.0544 0.0046  207  TRP   B N   
4220  C  CA  . TRP   B 207 ? 1.2158 1.2636 1.2136 0.0753  -0.0472 0.0092  207  TRP   B CA  
4221  C  C   . TRP   B 207 ? 1.2717 1.3327 1.2849 0.0683  -0.0491 0.0089  207  TRP   B C   
4222  O  O   . TRP   B 207 ? 1.2932 1.3564 1.3106 0.0667  -0.0556 0.0054  207  TRP   B O   
4223  C  CB  . TRP   B 207 ? 1.2472 1.2884 1.2361 0.0812  -0.0431 0.0117  207  TRP   B CB  
4224  C  CG  . TRP   B 207 ? 1.2745 1.3111 1.2587 0.0853  -0.0488 0.0090  207  TRP   B CG  
4225  C  CD1 . TRP   B 207 ? 1.2495 1.2732 1.2198 0.0925  -0.0531 0.0062  207  TRP   B CD1 
4226  C  CD2 . TRP   B 207 ? 1.2725 1.3166 1.2654 0.0825  -0.0508 0.0088  207  TRP   B CD2 
4227  N  NE1 . TRP   B 207 ? 1.2194 1.2426 1.1901 0.0941  -0.0578 0.0043  207  TRP   B NE1 
4228  C  CE2 . TRP   B 207 ? 1.2374 1.2730 1.2217 0.0880  -0.0563 0.0059  207  TRP   B CE2 
4229  C  CE3 . TRP   B 207 ? 1.2270 1.2838 1.2337 0.0760  -0.0488 0.0107  207  TRP   B CE3 
4230  C  CZ2 . TRP   B 207 ? 1.2257 1.2653 1.2153 0.0869  -0.0594 0.0050  207  TRP   B CZ2 
4231  C  CZ3 . TRP   B 207 ? 1.2232 1.2837 1.2345 0.0752  -0.0518 0.0099  207  TRP   B CZ3 
4232  C  CH2 . TRP   B 207 ? 1.2204 1.2724 1.2233 0.0805  -0.0569 0.0071  207  TRP   B CH2 
4233  N  N   . LYS   B 208 ? 1.2764 1.3458 1.2979 0.0640  -0.0434 0.0127  208  LYS   B N   
4234  C  CA  . LYS   B 208 ? 1.1935 1.2751 1.2289 0.0573  -0.0447 0.0128  208  LYS   B CA  
4235  C  C   . LYS   B 208 ? 1.1683 1.2562 1.2097 0.0553  -0.0382 0.0172  208  LYS   B C   
4236  O  O   . LYS   B 208 ? 1.2531 1.3393 1.2923 0.0560  -0.0324 0.0201  208  LYS   B O   
4237  C  CB  . LYS   B 208 ? 1.1735 1.2608 1.2164 0.0515  -0.0468 0.0112  208  LYS   B CB  
4238  C  CG  . LYS   B 208 ? 1.2280 1.3125 1.2677 0.0514  -0.0428 0.0127  208  LYS   B CG  
4239  C  CD  . LYS   B 208 ? 1.2449 1.3326 1.2894 0.0471  -0.0461 0.0102  208  LYS   B CD  
4240  C  CE  . LYS   B 208 ? 1.2991 1.3985 1.3568 0.0398  -0.0463 0.0108  208  LYS   B CE  
4241  N  NZ  . LYS   B 208 ? 1.2751 1.3775 1.3373 0.0357  -0.0485 0.0088  208  LYS   B NZ  
4242  N  N   . GLN   B 209 ? 1.2388 1.3337 1.2877 0.0528  -0.0394 0.0177  209  GLN   B N   
4243  C  CA  . GLN   B 209 ? 1.3324 1.4329 1.3869 0.0518  -0.0341 0.0215  209  GLN   B CA  
4244  C  C   . GLN   B 209 ? 1.3820 1.4940 1.4498 0.0445  -0.0344 0.0222  209  GLN   B C   
4245  O  O   . GLN   B 209 ? 1.3720 1.4884 1.4449 0.0416  -0.0390 0.0202  209  GLN   B O   
4246  C  CB  . GLN   B 209 ? 1.3817 1.4804 1.4334 0.0556  -0.0351 0.0216  209  GLN   B CB  
4247  N  N   . GLU   B 210 ? 1.7447 1.8612 1.8179 0.0418  -0.0293 0.0252  210  GLU   B N   
4248  C  CA  . GLU   B 210 ? 1.7294 1.8551 1.8137 0.0349  -0.0303 0.0253  210  GLU   B CA  
4249  C  C   . GLU   B 210 ? 1.6968 1.8301 1.7892 0.0319  -0.0328 0.0253  210  GLU   B C   
4250  O  O   . GLU   B 210 ? 1.6816 1.8205 1.7804 0.0269  -0.0360 0.0239  210  GLU   B O   
4251  C  CB  . GLU   B 210 ? 1.7712 1.8999 1.8601 0.0328  -0.0244 0.0286  210  GLU   B CB  
4252  N  N   . ASN   B 211 ? 1.4561 1.5893 1.5478 0.0350  -0.0315 0.0268  211  ASN   B N   
4253  C  CA  . ASN   B 211 ? 1.3768 1.5175 1.4766 0.0321  -0.0334 0.0272  211  ASN   B CA  
4254  C  C   . ASN   B 211 ? 1.3588 1.4976 1.4557 0.0368  -0.0320 0.0286  211  ASN   B C   
4255  O  O   . ASN   B 211 ? 1.3927 1.5340 1.4930 0.0379  -0.0272 0.0317  211  ASN   B O   
4256  C  CB  . ASN   B 211 ? 1.4012 1.5505 1.5116 0.0271  -0.0309 0.0295  211  ASN   B CB  
4257  C  CG  . ASN   B 211 ? 1.3797 1.5361 1.4979 0.0222  -0.0349 0.0286  211  ASN   B CG  
4258  O  OD1 . ASN   B 211 ? 1.3695 1.5258 1.4868 0.0231  -0.0381 0.0274  211  ASN   B OD1 
4259  N  ND2 . ASN   B 211 ? 1.4117 1.5738 1.5372 0.0172  -0.0347 0.0292  211  ASN   B ND2 
4260  N  N   . VAL   B 212 ? 1.3089 1.4431 1.4001 0.0396  -0.0360 0.0262  212  VAL   B N   
4261  C  CA  . VAL   B 212 ? 1.2091 1.3397 1.2957 0.0447  -0.0349 0.0273  212  VAL   B CA  
4262  C  C   . VAL   B 212 ? 1.1334 1.2709 1.2276 0.0422  -0.0368 0.0277  212  VAL   B C   
4263  O  O   . VAL   B 212 ? 1.1236 1.2680 1.2258 0.0367  -0.0388 0.0274  212  VAL   B O   
4264  C  CB  . VAL   B 212 ? 1.2043 1.3250 1.2798 0.0497  -0.0383 0.0244  212  VAL   B CB  
4265  C  CG1 . VAL   B 212 ? 1.2424 1.3645 1.3202 0.0471  -0.0447 0.0213  212  VAL   B CG1 
4266  C  CG2 . VAL   B 212 ? 1.2696 1.3838 1.3370 0.0565  -0.0353 0.0259  212  VAL   B CG2 
4267  N  N   . GLU   B 213 ? 1.1055 1.2407 1.1966 0.0464  -0.0363 0.0285  213  GLU   B N   
4268  C  CA  . GLU   B 213 ? 1.0865 1.2277 1.1841 0.0446  -0.0379 0.0293  213  GLU   B CA  
4269  C  C   . GLU   B 213 ? 1.1165 1.2602 1.2174 0.0399  -0.0435 0.0265  213  GLU   B C   
4270  O  O   . GLU   B 213 ? 1.1470 1.2859 1.2433 0.0399  -0.0469 0.0237  213  GLU   B O   
4271  C  CB  . GLU   B 213 ? 1.0803 1.2165 1.1719 0.0503  -0.0376 0.0297  213  GLU   B CB  
4272  C  CG  . GLU   B 213 ? 1.0878 1.2298 1.1857 0.0490  -0.0390 0.0306  213  GLU   B CG  
4273  C  CD  . GLU   B 213 ? 1.1308 1.2667 1.2218 0.0529  -0.0422 0.0291  213  GLU   B CD  
4274  O  OE1 . GLU   B 213 ? 1.1375 1.2721 1.2279 0.0507  -0.0473 0.0263  213  GLU   B OE1 
4275  O  OE2 . GLU   B 213 ? 1.1541 1.2866 1.2406 0.0583  -0.0395 0.0306  213  GLU   B OE2 
4276  N  N   . ALA   B 214 ? 1.1040 1.2550 1.2131 0.0361  -0.0445 0.0275  214  ALA   B N   
4277  C  CA  . ALA   B 214 ? 1.0418 1.1957 1.1547 0.0311  -0.0488 0.0255  214  ALA   B CA  
4278  C  C   . ALA   B 214 ? 1.0495 1.1997 1.1590 0.0321  -0.0530 0.0234  214  ALA   B C   
4279  O  O   . ALA   B 214 ? 1.1283 1.2789 1.2393 0.0286  -0.0564 0.0213  214  ALA   B O   
4280  C  CB  . ALA   B 214 ? 1.0657 1.2281 1.1878 0.0266  -0.0484 0.0273  214  ALA   B CB  
4281  N  N   . GLU   B 215 ? 1.0332 1.1799 1.1384 0.0368  -0.0527 0.0240  215  GLU   B N   
4282  C  CA  . GLU   B 215 ? 1.0487 1.1905 1.1498 0.0383  -0.0567 0.0218  215  GLU   B CA  
4283  C  C   . GLU   B 215 ? 1.1095 1.2423 1.2014 0.0433  -0.0576 0.0199  215  GLU   B C   
4284  O  O   . GLU   B 215 ? 1.1354 1.2628 1.2222 0.0467  -0.0598 0.0188  215  GLU   B O   
4285  C  CB  . GLU   B 215 ? 1.0057 1.1491 1.1080 0.0400  -0.0566 0.0234  215  GLU   B CB  
4286  N  N   . ALA   B 216 ? 1.0898 1.2204 1.1790 0.0439  -0.0562 0.0194  216  ALA   B N   
4287  C  CA  . ALA   B 216 ? 1.0388 1.1603 1.1187 0.0486  -0.0577 0.0173  216  ALA   B CA  
4288  C  C   . ALA   B 216 ? 1.0469 1.1652 1.1264 0.0470  -0.0635 0.0135  216  ALA   B C   
4289  O  O   . ALA   B 216 ? 1.0599 1.1814 1.1443 0.0424  -0.0651 0.0121  216  ALA   B O   
4290  C  CB  . ALA   B 216 ? 1.0390 1.1592 1.1166 0.0491  -0.0548 0.0178  216  ALA   B CB  
4291  N  N   . SER   B 217 ? 1.0357 1.1476 1.1097 0.0507  -0.0665 0.0119  217  SER   B N   
4292  C  CA  . SER   B 217 ? 1.0174 1.1262 1.0920 0.0494  -0.0721 0.0084  217  SER   B CA  
4293  C  C   . SER   B 217 ? 1.0737 1.1728 1.1398 0.0543  -0.0757 0.0053  217  SER   B C   
4294  O  O   . SER   B 217 ? 1.0924 1.1895 1.1605 0.0525  -0.0803 0.0020  217  SER   B O   
4295  C  CB  . SER   B 217 ? 1.1488 1.2584 1.2255 0.0488  -0.0737 0.0087  217  SER   B CB  
4296  O  OG  . SER   B 217 ? 1.0757 1.1822 1.1466 0.0540  -0.0714 0.0108  217  SER   B OG  
4297  N  N   . MET   B 218 ? 1.0522 1.1447 1.1090 0.0604  -0.0738 0.0063  218  MET   B N   
4298  C  CA  . MET   B 218 ? 1.0436 1.1254 1.0906 0.0660  -0.0776 0.0034  218  MET   B CA  
4299  C  C   . MET   B 218 ? 1.0790 1.1562 1.1191 0.0692  -0.0757 0.0033  218  MET   B C   
4300  O  O   . MET   B 218 ? 1.0823 1.1604 1.1197 0.0710  -0.0700 0.0066  218  MET   B O   
4301  C  CB  . MET   B 218 ? 1.0299 1.1056 1.0693 0.0716  -0.0774 0.0042  218  MET   B CB  
4302  C  CG  . MET   B 218 ? 1.0801 1.1445 1.1102 0.0768  -0.0830 0.0006  218  MET   B CG  
4303  S  SD  . MET   B 218 ? 1.2059 1.2635 1.2293 0.0818  -0.0848 0.0005  218  MET   B SD  
4304  C  CE  . MET   B 218 ? 1.1590 1.2280 1.1941 0.0759  -0.0820 0.0034  218  MET   B CE  
4305  N  N   . VAL   B 219 ? 1.0641 1.1362 1.1017 0.0699  -0.0805 -0.0003 219  VAL   B N   
4306  C  CA  . VAL   B 219 ? 0.9798 1.0448 1.0085 0.0742  -0.0800 -0.0010 219  VAL   B CA  
4307  C  C   . VAL   B 219 ? 1.0275 1.0804 1.0449 0.0810  -0.0848 -0.0039 219  VAL   B C   
4308  O  O   . VAL   B 219 ? 1.0428 1.0935 1.0625 0.0802  -0.0913 -0.0075 219  VAL   B O   
4309  C  CB  . VAL   B 219 ? 1.0176 1.0857 1.0517 0.0702  -0.0821 -0.0031 219  VAL   B CB  
4310  C  CG1 . VAL   B 219 ? 1.0060 1.0674 1.0308 0.0744  -0.0806 -0.0031 219  VAL   B CG1 
4311  C  CG2 . VAL   B 219 ? 1.0623 1.1423 1.1081 0.0630  -0.0784 -0.0008 219  VAL   B CG2 
4312  N  N   . ILE   B 220 ? 1.0557 1.1004 1.0610 0.0876  -0.0817 -0.0022 220  ILE   B N   
4313  C  CA  . ILE   B 220 ? 1.0338 1.0653 1.0259 0.0950  -0.0860 -0.0048 220  ILE   B CA  
4314  C  C   . ILE   B 220 ? 1.1426 1.1657 1.1239 0.0998  -0.0850 -0.0052 220  ILE   B C   
4315  O  O   . ILE   B 220 ? 1.1817 1.2047 1.1587 0.1016  -0.0779 -0.0015 220  ILE   B O   
4316  C  CB  . ILE   B 220 ? 1.0511 1.0782 1.0360 0.0999  -0.0830 -0.0025 220  ILE   B CB  
4317  C  CG1 . ILE   B 220 ? 1.1019 1.1378 1.0974 0.0952  -0.0829 -0.0013 220  ILE   B CG1 
4318  C  CG2 . ILE   B 220 ? 1.0982 1.1112 1.0695 0.1073  -0.0884 -0.0056 220  ILE   B CG2 
4319  C  CD1 . ILE   B 220 ? 1.0548 1.0893 1.0455 0.0990  -0.0780 0.0020  220  ILE   B CD1 
4320  N  N   . ALA   B 221 ? 1.1975 1.2133 1.1743 0.1020  -0.0920 -0.0096 221  ALA   B N   
4321  C  CA  . ALA   B 221 ? 1.1266 1.1336 1.0926 0.1067  -0.0919 -0.0104 221  ALA   B CA  
4322  C  C   . ALA   B 221 ? 1.1530 1.1459 1.1013 0.1158  -0.0910 -0.0099 221  ALA   B C   
4323  O  O   . ALA   B 221 ? 1.1436 1.1287 1.0859 0.1198  -0.0968 -0.0127 221  ALA   B O   
4324  C  CB  . ALA   B 221 ? 1.0646 1.0692 1.0330 0.1057  -0.1000 -0.0154 221  ALA   B CB  
4325  N  N   . VAL   B 222 ? 1.1730 1.1624 1.1129 0.1192  -0.0836 -0.0063 222  VAL   B N   
4326  C  CA  . VAL   B 222 ? 1.2457 1.2210 1.1677 0.1283  -0.0815 -0.0053 222  VAL   B CA  
4327  C  C   . VAL   B 222 ? 1.2363 1.1980 1.1450 0.1342  -0.0876 -0.0093 222  VAL   B C   
4328  O  O   . VAL   B 222 ? 1.2681 1.2310 1.1783 0.1325  -0.0877 -0.0099 222  VAL   B O   
4329  C  CB  . VAL   B 222 ? 1.2582 1.2350 1.1771 0.1296  -0.0706 0.0003  222  VAL   B CB  
4330  C  CG1 . VAL   B 222 ? 1.3160 1.2777 1.2158 0.1393  -0.0678 0.0014  222  VAL   B CG1 
4331  C  CG2 . VAL   B 222 ? 1.1567 1.1475 1.0898 0.1236  -0.0653 0.0038  222  VAL   B CG2 
4332  N  N   . PRO   B 223 ? 1.2202 1.1687 1.1159 0.1414  -0.0933 -0.0122 223  PRO   B N   
4333  C  CA  . PRO   B 223 ? 1.3199 1.2546 1.2025 0.1475  -0.1003 -0.0164 223  PRO   B CA  
4334  C  C   . PRO   B 223 ? 1.4213 1.3477 1.2909 0.1522  -0.0946 -0.0141 223  PRO   B C   
4335  O  O   . PRO   B 223 ? 1.4031 1.3337 1.2731 0.1512  -0.0846 -0.0090 223  PRO   B O   
4336  C  CB  . PRO   B 223 ? 1.3370 1.2588 1.2067 0.1548  -0.1053 -0.0187 223  PRO   B CB  
4337  C  CG  . PRO   B 223 ? 1.3368 1.2689 1.2191 0.1498  -0.1050 -0.0178 223  PRO   B CG  
4338  C  CD  . PRO   B 223 ? 1.3210 1.2671 1.2147 0.1437  -0.0948 -0.0123 223  PRO   B CD  
4339  N  N   . GLU   B 224 ? 1.4790 1.3929 1.3366 0.1577  -0.1011 -0.0179 224  GLU   B N   
4340  C  CA  . GLU   B 224 ? 1.5165 1.4228 1.3628 0.1614  -0.0965 -0.0162 224  GLU   B CA  
4341  C  C   . GLU   B 224 ? 1.5345 1.4323 1.3662 0.1676  -0.0863 -0.0111 224  GLU   B C   
4342  O  O   . GLU   B 224 ? 1.5607 1.4604 1.3916 0.1665  -0.0782 -0.0073 224  GLU   B O   
4343  C  CB  . GLU   B 224 ? 1.5861 1.4789 1.4206 0.1672  -0.1061 -0.0215 224  GLU   B CB  
4344  C  CG  . GLU   B 224 ? 1.7046 1.5920 1.5310 0.1693  -0.1028 -0.0205 224  GLU   B CG  
4345  C  CD  . GLU   B 224 ? 1.8270 1.6990 1.6392 0.1764  -0.1124 -0.0257 224  GLU   B CD  
4346  O  OE1 . GLU   B 224 ? 1.8352 1.7094 1.6554 0.1746  -0.1230 -0.0310 224  GLU   B OE1 
4347  O  OE2 . GLU   B 224 ? 1.9152 1.7725 1.7083 0.1840  -0.1095 -0.0246 224  GLU   B OE2 
4348  N  N   . PRO   B 225 ? 1.5178 1.4063 1.3380 0.1739  -0.0858 -0.0106 225  PRO   B N   
4349  C  CA  . PRO   B 225 ? 1.4831 1.3625 1.2887 0.1804  -0.0755 -0.0056 225  PRO   B CA  
4350  C  C   . PRO   B 225 ? 1.4886 1.3802 1.3048 0.1748  -0.0636 0.0003  225  PRO   B C   
4351  O  O   . PRO   B 225 ? 1.4902 1.3752 1.2967 0.1783  -0.0562 0.0034  225  PRO   B O   
4352  C  CB  . PRO   B 225 ? 1.4613 1.3370 1.2626 0.1840  -0.0763 -0.0056 225  PRO   B CB  
4353  C  CG  . PRO   B 225 ? 1.5470 1.4190 1.3489 0.1845  -0.0895 -0.0120 225  PRO   B CG  
4354  C  CD  . PRO   B 225 ? 1.5158 1.3995 1.3341 0.1764  -0.0949 -0.0148 225  PRO   B CD  
4355  N  N   . PHE   B 226 ? 1.4788 1.3879 1.3150 0.1663  -0.0620 0.0017  226  PHE   B N   
4356  C  CA  . PHE   B 226 ? 1.4026 1.3242 1.2508 0.1603  -0.0520 0.0068  226  PHE   B CA  
4357  C  C   . PHE   B 226 ? 1.3991 1.3341 1.2640 0.1513  -0.0546 0.0056  226  PHE   B C   
4358  O  O   . PHE   B 226 ? 1.4280 1.3672 1.2964 0.1485  -0.0481 0.0086  226  PHE   B O   
4359  C  CB  . PHE   B 226 ? 1.3193 1.2504 1.1769 0.1579  -0.0464 0.0103  226  PHE   B CB  
4360  N  N   . GLY   B 227 ? 1.3825 1.3237 1.2575 0.1468  -0.0640 0.0011  227  GLY   B N   
4361  C  CA  . GLY   B 227 ? 1.3154 1.2678 1.2049 0.1390  -0.0673 -0.0006 227  GLY   B CA  
4362  C  C   . GLY   B 227 ? 1.2651 1.2350 1.1732 0.1301  -0.0616 0.0028  227  GLY   B C   
4363  O  O   . GLY   B 227 ? 1.2881 1.2608 1.1967 0.1302  -0.0527 0.0075  227  GLY   B O   
4364  N  N   . GLY   B 228 ? 1.2432 1.2247 1.1667 0.1226  -0.0665 0.0005  228  GLY   B N   
4365  C  CA  . GLY   B 228 ? 1.2168 1.2142 1.1574 0.1142  -0.0619 0.0034  228  GLY   B CA  
4366  C  C   . GLY   B 228 ? 1.1836 1.1903 1.1366 0.1093  -0.0669 0.0016  228  GLY   B C   
4367  O  O   . GLY   B 228 ? 1.2261 1.2292 1.1784 0.1101  -0.0751 -0.0028 228  GLY   B O   
4368  N  N   . ALA   B 229 ? 1.2106 1.2288 1.1750 0.1042  -0.0618 0.0049  229  ALA   B N   
4369  C  CA  . ALA   B 229 ? 1.1343 1.1616 1.1107 0.0992  -0.0654 0.0039  229  ALA   B CA  
4370  C  C   . ALA   B 229 ? 1.1019 1.1363 1.0837 0.0978  -0.0590 0.0082  229  ALA   B C   
4371  O  O   . ALA   B 229 ? 1.1418 1.1796 1.1252 0.0972  -0.0516 0.0121  229  ALA   B O   
4372  C  CB  . ALA   B 229 ? 1.1097 1.1478 1.1002 0.0911  -0.0684 0.0022  229  ALA   B CB  
4373  N  N   . ILE   B 230 ? 1.0800 1.1164 1.0652 0.0974  -0.0619 0.0074  230  ILE   B N   
4374  C  CA  . ILE   B 230 ? 1.1174 1.1609 1.1086 0.0960  -0.0568 0.0111  230  ILE   B CA  
4375  C  C   . ILE   B 230 ? 1.1166 1.1729 1.1234 0.0879  -0.0591 0.0107  230  ILE   B C   
4376  O  O   . ILE   B 230 ? 1.0998 1.1565 1.1100 0.0855  -0.0657 0.0072  230  ILE   B O   
4377  C  CB  . ILE   B 230 ? 1.0497 1.0851 1.0317 0.1023  -0.0578 0.0109  230  ILE   B CB  
4378  C  CG1 . ILE   B 230 ? 1.0652 1.0880 1.0313 0.1105  -0.0541 0.0120  230  ILE   B CG1 
4379  C  CG2 . ILE   B 230 ? 1.0453 1.0888 1.0350 0.1004  -0.0537 0.0141  230  ILE   B CG2 
4380  C  CD1 . ILE   B 230 ? 1.1394 1.1512 1.0933 0.1178  -0.0564 0.0109  230  ILE   B CD1 
4381  N  N   . ILE   B 231 ? 1.1155 1.1819 1.1318 0.0836  -0.0535 0.0143  231  ILE   B N   
4382  C  CA  . ILE   B 231 ? 1.0787 1.1567 1.1088 0.0762  -0.0549 0.0144  231  ILE   B CA  
4383  C  C   . ILE   B 231 ? 1.0899 1.1722 1.1238 0.0764  -0.0528 0.0167  231  ILE   B C   
4384  O  O   . ILE   B 231 ? 1.1160 1.2039 1.1544 0.0757  -0.0470 0.0204  231  ILE   B O   
4385  C  CB  . ILE   B 231 ? 1.0604 1.1470 1.0993 0.0706  -0.0513 0.0162  231  ILE   B CB  
4386  C  CG1 . ILE   B 231 ? 1.0914 1.1724 1.1245 0.0718  -0.0518 0.0146  231  ILE   B CG1 
4387  C  CG2 . ILE   B 231 ? 1.0308 1.1265 1.0812 0.0635  -0.0546 0.0150  231  ILE   B CG2 
4388  C  CD1 . ILE   B 231 ? 1.0870 1.1657 1.1202 0.0702  -0.0591 0.0102  231  ILE   B CD1 
4389  N  N   . ILE   B 232 ? 1.0707 1.1504 1.1034 0.0774  -0.0578 0.0146  232  ILE   B N   
4390  C  CA  . ILE   B 232 ? 1.0967 1.1801 1.1328 0.0776  -0.0564 0.0165  232  ILE   B CA  
4391  C  C   . ILE   B 232 ? 1.1174 1.2126 1.1669 0.0702  -0.0564 0.0175  232  ILE   B C   
4392  O  O   . ILE   B 232 ? 1.1325 1.2309 1.1874 0.0652  -0.0602 0.0152  232  ILE   B O   
4393  C  CB  . ILE   B 232 ? 1.0928 1.1686 1.1225 0.0811  -0.0618 0.0138  232  ILE   B CB  
4394  C  CG1 . ILE   B 232 ? 1.1422 1.2051 1.1576 0.0886  -0.0626 0.0123  232  ILE   B CG1 
4395  C  CG2 . ILE   B 232 ? 1.1642 1.2427 1.1959 0.0824  -0.0597 0.0161  232  ILE   B CG2 
4396  C  CD1 . ILE   B 232 ? 1.1960 1.2543 1.2031 0.0951  -0.0562 0.0158  232  ILE   B CD1 
4397  N  N   . GLY   B 233 ? 1.2179 1.3196 1.2728 0.0695  -0.0519 0.0209  233  GLY   B N   
4398  C  CA  . GLY   B 233 ? 1.2019 1.3142 1.2685 0.0633  -0.0517 0.0222  233  GLY   B CA  
4399  C  C   . GLY   B 233 ? 1.2126 1.3276 1.2820 0.0641  -0.0517 0.0236  233  GLY   B C   
4400  O  O   . GLY   B 233 ? 1.2167 1.3252 1.2791 0.0687  -0.0532 0.0229  233  GLY   B O   
4401  N  N   . GLN   B 234 ? 1.1117 1.2362 1.1911 0.0595  -0.0504 0.0255  234  GLN   B N   
4402  C  CA  . GLN   B 234 ? 1.0941 1.2221 1.1771 0.0600  -0.0503 0.0271  234  GLN   B CA  
4403  C  C   . GLN   B 234 ? 1.1633 1.2912 1.2448 0.0651  -0.0449 0.0302  234  GLN   B C   
4404  O  O   . GLN   B 234 ? 1.2154 1.3397 1.2926 0.0695  -0.0449 0.0307  234  GLN   B O   
4405  C  CB  . GLN   B 234 ? 1.0249 1.1624 1.1185 0.0536  -0.0512 0.0279  234  GLN   B CB  
4406  N  N   . GLU   B 235 ? 1.1039 1.2355 1.1889 0.0647  -0.0399 0.0324  235  GLU   B N   
4407  C  CA  . GLU   B 235 ? 1.0897 1.2224 1.1754 0.0688  -0.0338 0.0357  235  GLU   B CA  
4408  C  C   . GLU   B 235 ? 1.1614 1.2863 1.2380 0.0739  -0.0297 0.0362  235  GLU   B C   
4409  O  O   . GLU   B 235 ? 1.2208 1.3432 1.2942 0.0792  -0.0248 0.0386  235  GLU   B O   
4410  C  CB  . GLU   B 235 ? 1.0347 1.1784 1.1333 0.0644  -0.0308 0.0382  235  GLU   B CB  
4411  N  N   . SER   B 236 ? 1.1279 1.2483 1.1995 0.0728  -0.0314 0.0342  236  SER   B N   
4412  C  CA  . SER   B 236 ? 1.1244 1.2372 1.1872 0.0772  -0.0274 0.0348  236  SER   B CA  
4413  C  C   . SER   B 236 ? 1.1438 1.2463 1.1951 0.0797  -0.0323 0.0311  236  SER   B C   
4414  O  O   . SER   B 236 ? 1.1541 1.2567 1.2065 0.0766  -0.0386 0.0281  236  SER   B O   
4415  C  CB  . SER   B 236 ? 1.1263 1.2441 1.1953 0.0735  -0.0235 0.0363  236  SER   B CB  
4416  O  OG  . SER   B 236 ? 1.1924 1.3122 1.2640 0.0681  -0.0282 0.0337  236  SER   B OG  
4417  N  N   . ILE   B 237 ? 1.1684 1.2616 1.2089 0.0853  -0.0293 0.0314  237  ILE   B N   
4418  C  CA  . ILE   B 237 ? 1.1462 1.2282 1.1744 0.0888  -0.0336 0.0281  237  ILE   B CA  
4419  C  C   . ILE   B 237 ? 1.1675 1.2451 1.1904 0.0905  -0.0291 0.0292  237  ILE   B C   
4420  O  O   . ILE   B 237 ? 1.2621 1.3353 1.2792 0.0956  -0.0228 0.0319  237  ILE   B O   
4421  C  CB  . ILE   B 237 ? 1.1998 1.2718 1.2165 0.0960  -0.0349 0.0273  237  ILE   B CB  
4422  C  CG1 . ILE   B 237 ? 1.1896 1.2643 1.2105 0.0938  -0.0408 0.0253  237  ILE   B CG1 
4423  C  CG2 . ILE   B 237 ? 1.1889 1.2476 1.1910 0.1015  -0.0376 0.0246  237  ILE   B CG2 
4424  C  CD1 . ILE   B 237 ? 1.1808 1.2474 1.1923 0.1005  -0.0411 0.0253  237  ILE   B CD1 
4425  N  N   . THR   B 238 ? 1.1565 1.2356 1.1818 0.0864  -0.0319 0.0273  238  THR   B N   
4426  C  CA  . THR   B 238 ? 1.1805 1.2560 1.2015 0.0875  -0.0276 0.0284  238  THR   B CA  
4427  C  C   . THR   B 238 ? 1.1979 1.2618 1.2062 0.0914  -0.0323 0.0249  238  THR   B C   
4428  O  O   . THR   B 238 ? 1.1484 1.2109 1.1564 0.0901  -0.0396 0.0211  238  THR   B O   
4429  C  CB  . THR   B 238 ? 1.2849 1.3714 1.3188 0.0799  -0.0262 0.0294  238  THR   B CB  
4430  O  OG1 . THR   B 238 ? 1.3066 1.3958 1.3445 0.0751  -0.0330 0.0259  238  THR   B OG1 
4431  C  CG2 . THR   B 238 ? 1.2827 1.3805 1.3295 0.0760  -0.0231 0.0323  238  THR   B CG2 
4432  N  N   . TYR   B 239 ? 1.3194 1.3742 1.3168 0.0966  -0.0278 0.0262  239  TYR   B N   
4433  C  CA  . TYR   B 239 ? 1.2928 1.3358 1.2774 0.1008  -0.0315 0.0232  239  TYR   B CA  
4434  C  C   . TYR   B 239 ? 1.3014 1.3462 1.2882 0.0977  -0.0290 0.0238  239  TYR   B C   
4435  O  O   . TYR   B 239 ? 1.2875 1.3368 1.2790 0.0961  -0.0216 0.0276  239  TYR   B O   
4436  C  CB  . TYR   B 239 ? 1.2515 1.2805 1.2192 0.1101  -0.0286 0.0240  239  TYR   B CB  
4437  C  CG  . TYR   B 239 ? 1.3091 1.3252 1.2624 0.1150  -0.0305 0.0219  239  TYR   B CG  
4438  C  CD1 . TYR   B 239 ? 1.3562 1.3699 1.3064 0.1156  -0.0243 0.0243  239  TYR   B CD1 
4439  C  CD2 . TYR   B 239 ? 1.2783 1.2843 1.2213 0.1191  -0.0386 0.0174  239  TYR   B CD2 
4440  C  CE1 . TYR   B 239 ? 1.3327 1.3343 1.2694 0.1201  -0.0260 0.0225  239  TYR   B CE1 
4441  C  CE2 . TYR   B 239 ? 1.2478 1.2419 1.1777 0.1238  -0.0408 0.0154  239  TYR   B CE2 
4442  C  CZ  . TYR   B 239 ? 1.3252 1.3169 1.2515 0.1244  -0.0343 0.0180  239  TYR   B CZ  
4443  O  OH  . TYR   B 239 ? 1.3220 1.3013 1.2345 0.1293  -0.0361 0.0162  239  TYR   B OH  
4444  N  N   . HIS   B 240 ? 1.3681 1.4092 1.3518 0.0968  -0.0351 0.0201  240  HIS   B N   
4445  C  CA  . HIS   B 240 ? 1.3975 1.4408 1.3842 0.0932  -0.0340 0.0200  240  HIS   B CA  
4446  C  C   . HIS   B 240 ? 1.3833 1.4140 1.3564 0.0982  -0.0380 0.0169  240  HIS   B C   
4447  O  O   . HIS   B 240 ? 1.3776 1.4036 1.3467 0.1001  -0.0457 0.0129  240  HIS   B O   
4448  C  CB  . HIS   B 240 ? 1.3775 1.4331 1.3792 0.0847  -0.0382 0.0184  240  HIS   B CB  
4449  C  CG  . HIS   B 240 ? 1.3906 1.4587 1.4059 0.0793  -0.0345 0.0214  240  HIS   B CG  
4450  N  ND1 . HIS   B 240 ? 1.4329 1.5085 1.4566 0.0748  -0.0292 0.0243  240  HIS   B ND1 
4451  C  CD2 . HIS   B 240 ? 1.3865 1.4606 1.4084 0.0777  -0.0357 0.0218  240  HIS   B CD2 
4452  C  CE1 . HIS   B 240 ? 1.4481 1.5338 1.4831 0.0708  -0.0276 0.0262  240  HIS   B CE1 
4453  N  NE2 . HIS   B 240 ? 1.4206 1.5056 1.4545 0.0725  -0.0314 0.0248  240  HIS   B NE2 
4454  N  N   . ASN   B 241 ? 1.3407 1.3656 1.3067 0.1005  -0.0331 0.0188  241  ASN   B N   
4455  C  CA  . ASN   B 241 ? 1.3197 1.3329 1.2731 0.1050  -0.0371 0.0157  241  ASN   B CA  
4456  C  C   . ASN   B 241 ? 1.3718 1.3833 1.3229 0.1044  -0.0309 0.0183  241  ASN   B C   
4457  O  O   . ASN   B 241 ? 1.4333 1.4363 1.3739 0.1097  -0.0242 0.0213  241  ASN   B O   
4458  C  CB  . ASN   B 241 ? 1.3324 1.3309 1.2687 0.1141  -0.0387 0.0146  241  ASN   B CB  
4459  C  CG  . ASN   B 241 ? 1.3249 1.3119 1.2496 0.1184  -0.0454 0.0104  241  ASN   B CG  
4460  O  OD1 . ASN   B 241 ? 1.3443 1.3362 1.2763 0.1140  -0.0513 0.0072  241  ASN   B OD1 
4461  N  ND2 . ASN   B 241 ? 1.3334 1.3050 1.2399 0.1271  -0.0447 0.0103  241  ASN   B ND2 
4462  N  N   . GLY   B 242 ? 1.4054 1.4243 1.3659 0.0983  -0.0330 0.0171  242  GLY   B N   
4463  C  CA  . GLY   B 242 ? 1.3893 1.4072 1.3488 0.0969  -0.0280 0.0191  242  GLY   B CA  
4464  C  C   . GLY   B 242 ? 1.4486 1.4689 1.4104 0.0966  -0.0178 0.0245  242  GLY   B C   
4465  O  O   . GLY   B 242 ? 1.4156 1.4482 1.3915 0.0908  -0.0149 0.0268  242  GLY   B O   
4466  N  N   . ASP   B 243 ? 1.5389 1.5469 1.4864 0.1032  -0.0124 0.0266  243  ASP   B N   
4467  C  CA  . ASP   B 243 ? 1.6092 1.6180 1.5580 0.1038  -0.0019 0.0319  243  ASP   B CA  
4468  C  C   . ASP   B 243 ? 1.6403 1.6547 1.5948 0.1043  0.0006  0.0339  243  ASP   B C   
4469  O  O   . ASP   B 243 ? 1.6421 1.6671 1.6096 0.0997  0.0061  0.0373  243  ASP   B O   
4470  C  CB  . ASP   B 243 ? 1.6394 1.6320 1.5697 0.1117  0.0033  0.0335  243  ASP   B CB  
4471  N  N   . LYS   B 244 ? 1.5760 1.5831 1.5209 0.1099  -0.0038 0.0317  244  LYS   B N   
4472  C  CA  . LYS   B 244 ? 1.5033 1.5127 1.4501 0.1121  -0.0009 0.0338  244  LYS   B CA  
4473  C  C   . LYS   B 244 ? 1.4453 1.4699 1.4095 0.1050  -0.0047 0.0330  244  LYS   B C   
4474  O  O   . LYS   B 244 ? 1.4121 1.4418 1.3823 0.1006  -0.0124 0.0294  244  LYS   B O   
4475  C  CB  . LYS   B 244 ? 1.4530 1.4487 1.3831 0.1205  -0.0050 0.0313  244  LYS   B CB  
4476  N  N   . TYR   B 245 ? 1.5009 1.5326 1.4732 0.1041  0.0010  0.0365  245  TYR   B N   
4477  C  CA  . TYR   B 245 ? 1.5043 1.5495 1.4920 0.0982  -0.0021 0.0362  245  TYR   B CA  
4478  C  C   . TYR   B 245 ? 1.4902 1.5375 1.4802 0.1010  0.0038  0.0396  245  TYR   B C   
4479  O  O   . TYR   B 245 ? 1.5289 1.5798 1.5243 0.1004  0.0121  0.0437  245  TYR   B O   
4480  C  CB  . TYR   B 245 ? 1.5101 1.5680 1.5136 0.0896  -0.0015 0.0369  245  TYR   B CB  
4481  C  CG  . TYR   B 245 ? 1.4658 1.5373 1.4850 0.0840  -0.0025 0.0378  245  TYR   B CG  
4482  C  CD1 . TYR   B 245 ? 1.4709 1.5444 1.4913 0.0838  -0.0090 0.0352  245  TYR   B CD1 
4483  C  CD2 . TYR   B 245 ? 1.4271 1.5090 1.4597 0.0791  0.0029  0.0411  245  TYR   B CD2 
4484  C  CE1 . TYR   B 245 ? 1.4616 1.5467 1.4953 0.0791  -0.0101 0.0359  245  TYR   B CE1 
4485  C  CE2 . TYR   B 245 ? 1.4812 1.5750 1.5275 0.0744  0.0014  0.0417  245  TYR   B CE2 
4486  C  CZ  . TYR   B 245 ? 1.4932 1.5883 1.5396 0.0745  -0.0051 0.0391  245  TYR   B CZ  
4487  O  OH  . TYR   B 245 ? 1.4877 1.5935 1.5463 0.0703  -0.0070 0.0395  245  TYR   B OH  
4488  N  N   . LEU   B 246 ? 1.4010 1.4464 1.3876 0.1039  -0.0005 0.0378  246  LEU   B N   
4489  C  CA  . LEU   B 246 ? 1.3526 1.4007 1.3421 0.1064  0.0037  0.0405  246  LEU   B CA  
4490  C  C   . LEU   B 246 ? 1.3488 1.4081 1.3508 0.1012  -0.0020 0.0390  246  LEU   B C   
4491  O  O   . LEU   B 246 ? 1.3849 1.4441 1.3866 0.0991  -0.0102 0.0351  246  LEU   B O   
4492  C  CB  . LEU   B 246 ? 1.3334 1.3673 1.3055 0.1156  0.0041  0.0400  246  LEU   B CB  
4493  C  CG  . LEU   B 246 ? 1.4240 1.4509 1.3885 0.1215  0.0145  0.0444  246  LEU   B CG  
4494  C  CD1 . LEU   B 246 ? 1.4999 1.5143 1.4489 0.1305  0.0148  0.0441  246  LEU   B CD1 
4495  C  CD2 . LEU   B 246 ? 1.3954 1.4352 1.3764 0.1172  0.0222  0.0488  246  LEU   B CD2 
4496  N  N   . ALA   B 247 ? 1.3139 1.3822 1.3267 0.0995  0.0024  0.0421  247  ALA   B N   
4497  C  CA  . ALA   B 247 ? 1.2304 1.3090 1.2548 0.0948  -0.0026 0.0410  247  ALA   B CA  
4498  C  C   . ALA   B 247 ? 1.2341 1.3162 1.2626 0.0975  0.0020  0.0439  247  ALA   B C   
4499  O  O   . ALA   B 247 ? 1.2789 1.3649 1.3132 0.0978  0.0098  0.0477  247  ALA   B O   
4500  C  CB  . ALA   B 247 ? 1.2377 1.3287 1.2772 0.0862  -0.0037 0.0411  247  ALA   B CB  
4501  N  N   . ILE   B 248 ? 1.2497 1.3305 1.2757 0.0994  -0.0028 0.0421  248  ILE   B N   
4502  C  CA  . ILE   B 248 ? 1.2384 1.3226 1.2683 0.1019  0.0002  0.0444  248  ILE   B CA  
4503  C  C   . ILE   B 248 ? 1.3137 1.4084 1.3555 0.0962  -0.0056 0.0431  248  ILE   B C   
4504  O  O   . ILE   B 248 ? 1.2872 1.3828 1.3299 0.0921  -0.0127 0.0398  248  ILE   B O   
4505  C  CB  . ILE   B 248 ? 1.2881 1.3596 1.3023 0.1104  0.0000  0.0437  248  ILE   B CB  
4506  C  CG1 . ILE   B 248 ? 1.2857 1.3523 1.2937 0.1102  -0.0097 0.0391  248  ILE   B CG1 
4507  C  CG2 . ILE   B 248 ? 1.3276 1.3872 1.3281 0.1166  0.0056  0.0449  248  ILE   B CG2 
4508  C  CD1 . ILE   B 248 ? 1.3937 1.4481 1.3871 0.1181  -0.0111 0.0379  248  ILE   B CD1 
4509  N  N   . ALA   B 249 ? 1.3389 1.4412 1.3898 0.0960  -0.0023 0.0457  249  ALA   B N   
4510  C  CA  . ALA   B 249 ? 1.2917 1.4031 1.3530 0.0916  -0.0072 0.0449  249  ALA   B CA  
4511  C  C   . ALA   B 249 ? 1.3661 1.4743 1.4232 0.0973  -0.0063 0.0457  249  ALA   B C   
4512  O  O   . ALA   B 249 ? 1.4286 1.5435 1.4942 0.0979  -0.0018 0.0487  249  ALA   B O   
4513  C  CB  . ALA   B 249 ? 1.2328 1.3574 1.3107 0.0854  -0.0048 0.0471  249  ALA   B CB  
4514  N  N   . PRO   B 250 ? 1.5212 1.6191 1.5656 0.1016  -0.0106 0.0432  250  PRO   B N   
4515  C  CA  . PRO   B 250 ? 1.4942 1.5873 1.5326 0.1078  -0.0094 0.0439  250  PRO   B CA  
4516  C  C   . PRO   B 250 ? 1.4287 1.5319 1.4790 0.1047  -0.0111 0.0448  250  PRO   B C   
4517  O  O   . PRO   B 250 ? 1.4636 1.5726 1.5207 0.0988  -0.0171 0.0428  250  PRO   B O   
4518  C  CB  . PRO   B 250 ? 1.5369 1.6183 1.5615 0.1110  -0.0161 0.0401  250  PRO   B CB  
4519  C  CG  . PRO   B 250 ? 1.5548 1.6329 1.5759 0.1084  -0.0186 0.0379  250  PRO   B CG  
4520  C  CD  . PRO   B 250 ? 1.5422 1.6328 1.5780 0.1008  -0.0173 0.0391  250  PRO   B CD  
4521  N  N   . PRO   B 251 ? 1.3958 1.5011 1.4487 0.1087  -0.0059 0.0477  251  PRO   B N   
4522  C  CA  . PRO   B 251 ? 1.3721 1.4860 1.4352 0.1065  -0.0080 0.0484  251  PRO   B CA  
4523  C  C   . PRO   B 251 ? 1.3971 1.5061 1.4539 0.1067  -0.0157 0.0452  251  PRO   B C   
4524  O  O   . PRO   B 251 ? 1.4297 1.5456 1.4946 0.1014  -0.0206 0.0441  251  PRO   B O   
4525  C  CB  . PRO   B 251 ? 1.4189 1.5328 1.4826 0.1127  -0.0006 0.0518  251  PRO   B CB  
4526  C  CG  . PRO   B 251 ? 1.4040 1.5042 1.4511 0.1198  0.0026  0.0517  251  PRO   B CG  
4527  C  CD  . PRO   B 251 ? 1.4173 1.5150 1.4616 0.1164  0.0015  0.0502  251  PRO   B CD  
4528  N  N   . ILE   B 252 ? 1.3808 1.4774 1.4228 0.1128  -0.0170 0.0436  252  ILE   B N   
4529  C  CA  . ILE   B 252 ? 1.3668 1.4584 1.4032 0.1138  -0.0236 0.0409  252  ILE   B CA  
4530  C  C   . ILE   B 252 ? 1.4185 1.5120 1.4580 0.1070  -0.0311 0.0376  252  ILE   B C   
4531  O  O   . ILE   B 252 ? 1.4382 1.5337 1.4807 0.1045  -0.0361 0.0362  252  ILE   B O   
4532  C  CB  . ILE   B 252 ? 1.2952 1.3723 1.3148 0.1219  -0.0235 0.0398  252  ILE   B CB  
4533  C  CG1 . ILE   B 252 ? 1.3441 1.4152 1.3578 0.1227  -0.0309 0.0367  252  ILE   B CG1 
4534  C  CG2 . ILE   B 252 ? 1.3436 1.4130 1.3543 0.1230  -0.0234 0.0383  252  ILE   B CG2 
4535  C  CD1 . ILE   B 252 ? 1.4242 1.5022 1.4458 0.1217  -0.0315 0.0380  252  ILE   B CD1 
4536  N  N   . ILE   B 253 ? 1.3933 1.4866 1.4326 0.1039  -0.0315 0.0365  253  ILE   B N   
4537  C  CA  . ILE   B 253 ? 1.4090 1.5037 1.4511 0.0978  -0.0381 0.0333  253  ILE   B CA  
4538  C  C   . ILE   B 253 ? 1.4489 1.5560 1.5052 0.0905  -0.0391 0.0341  253  ILE   B C   
4539  O  O   . ILE   B 253 ? 1.4442 1.5530 1.5035 0.0853  -0.0443 0.0317  253  ILE   B O   
4540  C  CB  . ILE   B 253 ? 1.3740 1.4646 1.4116 0.0967  -0.0386 0.0316  253  ILE   B CB  
4541  C  CG1 . ILE   B 253 ? 1.3685 1.4683 1.4160 0.0922  -0.0342 0.0338  253  ILE   B CG1 
4542  C  CG2 . ILE   B 253 ? 1.3804 1.4588 1.4038 0.1043  -0.0368 0.0312  253  ILE   B CG2 
4543  C  CD1 . ILE   B 253 ? 1.3126 1.4107 1.3588 0.0888  -0.0367 0.0315  253  ILE   B CD1 
4544  N  N   . LYS   B 254 ? 1.4450 1.5606 1.5103 0.0899  -0.0342 0.0374  254  LYS   B N   
4545  C  CA  . LYS   B 254 ? 1.4203 1.5469 1.4983 0.0833  -0.0357 0.0381  254  LYS   B CA  
4546  C  C   . LYS   B 254 ? 1.4724 1.6000 1.5521 0.0818  -0.0408 0.0369  254  LYS   B C   
4547  O  O   . LYS   B 254 ? 1.5357 1.6705 1.6238 0.0761  -0.0434 0.0367  254  LYS   B O   
4548  C  CB  . LYS   B 254 ? 1.3374 1.4728 1.4254 0.0833  -0.0295 0.0417  254  LYS   B CB  
4549  N  N   . GLN   B 255 ? 1.5299 1.6499 1.6011 0.0867  -0.0424 0.0361  255  GLN   B N   
4550  C  CA  . GLN   B 255 ? 1.5335 1.6544 1.6064 0.0856  -0.0466 0.0354  255  GLN   B CA  
4551  C  C   . GLN   B 255 ? 1.5427 1.6598 1.6131 0.0815  -0.0530 0.0320  255  GLN   B C   
4552  O  O   . GLN   B 255 ? 1.5466 1.6665 1.6210 0.0783  -0.0563 0.0316  255  GLN   B O   
4553  C  CB  . GLN   B 255 ? 1.5251 1.6395 1.5906 0.0925  -0.0457 0.0360  255  GLN   B CB  
4554  N  N   . SER   B 256 ? 1.5222 1.6327 1.5860 0.0817  -0.0546 0.0296  256  SER   B N   
4555  C  CA  . SER   B 256 ? 1.5037 1.6114 1.5669 0.0775  -0.0603 0.0264  256  SER   B CA  
4556  C  C   . SER   B 256 ? 1.4737 1.5806 1.5363 0.0753  -0.0604 0.0249  256  SER   B C   
4557  O  O   . SER   B 256 ? 1.5148 1.6235 1.5776 0.0767  -0.0561 0.0264  256  SER   B O   
4558  C  CB  . SER   B 256 ? 1.4624 1.5601 1.5167 0.0811  -0.0645 0.0240  256  SER   B CB  
4559  O  OG  . SER   B 256 ? 1.4192 1.5148 1.4745 0.0766  -0.0696 0.0210  256  SER   B OG  
4560  N  N   . THR   B 257 ? 1.3314 1.4352 1.3933 0.0721  -0.0652 0.0218  257  THR   B N   
4561  C  CA  . THR   B 257 ? 1.3471 1.4506 1.4093 0.0695  -0.0659 0.0200  257  THR   B CA  
4562  C  C   . THR   B 257 ? 1.3146 1.4076 1.3677 0.0730  -0.0697 0.0167  257  THR   B C   
4563  O  O   . THR   B 257 ? 1.2529 1.3410 1.3036 0.0734  -0.0741 0.0147  257  THR   B O   
4564  C  CB  . THR   B 257 ? 1.3598 1.4696 1.4306 0.0621  -0.0682 0.0190  257  THR   B CB  
4565  O  OG1 . THR   B 257 ? 1.3183 1.4376 1.3973 0.0589  -0.0650 0.0219  257  THR   B OG1 
4566  C  CG2 . THR   B 257 ? 1.3780 1.4865 1.4486 0.0599  -0.0694 0.0168  257  THR   B CG2 
4567  N  N   . ILE   B 258 ? 1.3602 1.4493 1.4081 0.0757  -0.0683 0.0162  258  ILE   B N   
4568  C  CA  . ILE   B 258 ? 1.3366 1.4153 1.3754 0.0794  -0.0723 0.0129  258  ILE   B CA  
4569  C  C   . ILE   B 258 ? 1.3335 1.4132 1.3773 0.0741  -0.0773 0.0096  258  ILE   B C   
4570  O  O   . ILE   B 258 ? 1.3040 1.3906 1.3549 0.0692  -0.0760 0.0100  258  ILE   B O   
4571  C  CB  . ILE   B 258 ? 1.3483 1.4219 1.3791 0.0844  -0.0689 0.0136  258  ILE   B CB  
4572  C  CG1 . ILE   B 258 ? 1.3414 1.4161 1.3697 0.0887  -0.0625 0.0175  258  ILE   B CG1 
4573  C  CG2 . ILE   B 258 ? 1.3195 1.3810 1.3392 0.0894  -0.0735 0.0102  258  ILE   B CG2 
4574  C  CD1 . ILE   B 258 ? 1.3162 1.3828 1.3356 0.0951  -0.0632 0.0175  258  ILE   B CD1 
4575  N  N   . VAL   B 259 ? 1.2760 1.3485 1.3163 0.0753  -0.0829 0.0063  259  VAL   B N   
4576  C  CA  . VAL   B 259 ? 1.2048 1.2783 1.2512 0.0702  -0.0878 0.0032  259  VAL   B CA  
4577  C  C   . VAL   B 259 ? 1.2484 1.3121 1.2881 0.0736  -0.0930 -0.0008 259  VAL   B C   
4578  O  O   . VAL   B 259 ? 1.2821 1.3466 1.3265 0.0702  -0.0963 -0.0035 259  VAL   B O   
4579  C  CB  . VAL   B 259 ? 1.1828 1.2584 1.2346 0.0669  -0.0898 0.0031  259  VAL   B CB  
4580  C  CG1 . VAL   B 259 ? 1.1796 1.2654 1.2394 0.0622  -0.0857 0.0063  259  VAL   B CG1 
4581  C  CG2 . VAL   B 259 ? 1.2025 1.2710 1.2464 0.0724  -0.0907 0.0033  259  VAL   B CG2 
4582  N  N   . CYS   B 260 ? 1.2196 1.2738 1.2483 0.0805  -0.0940 -0.0014 260  CYS   B N   
4583  C  CA  . CYS   B 260 ? 1.2260 1.2699 1.2471 0.0846  -0.0995 -0.0053 260  CYS   B CA  
4584  C  C   . CYS   B 260 ? 1.2506 1.2867 1.2589 0.0920  -0.0970 -0.0043 260  CYS   B C   
4585  O  O   . CYS   B 260 ? 1.2614 1.2983 1.2656 0.0952  -0.0914 -0.0008 260  CYS   B O   
4586  C  CB  . CYS   B 260 ? 1.2600 1.2969 1.2790 0.0860  -0.1053 -0.0080 260  CYS   B CB  
4587  S  SG  . CYS   B 260 ? 1.3774 1.4122 1.3905 0.0902  -0.1020 -0.0049 260  CYS   B SG  
4588  N  N   . HIS   B 261 ? 1.2078 1.2360 1.2097 0.0951  -0.1012 -0.0076 261  HIS   B N   
4589  C  CA  . HIS   B 261 ? 1.1485 1.1684 1.1376 0.1020  -0.0989 -0.0070 261  HIS   B CA  
4590  C  C   . HIS   B 261 ? 1.1801 1.1881 1.1606 0.1064  -0.1064 -0.0117 261  HIS   B C   
4591  O  O   . HIS   B 261 ? 1.2400 1.2494 1.2276 0.1025  -0.1122 -0.0152 261  HIS   B O   
4592  C  CB  . HIS   B 261 ? 1.1151 1.1416 1.1075 0.0996  -0.0935 -0.0046 261  HIS   B CB  
4593  C  CG  . HIS   B 261 ? 1.1747 1.1989 1.1673 0.0987  -0.0976 -0.0079 261  HIS   B CG  
4594  N  ND1 . HIS   B 261 ? 1.1967 1.2278 1.2011 0.0920  -0.1012 -0.0101 261  HIS   B ND1 
4595  C  CD2 . HIS   B 261 ? 1.1784 1.1937 1.1603 0.1038  -0.0985 -0.0092 261  HIS   B CD2 
4596  C  CE1 . HIS   B 261 ? 1.1551 1.1822 1.1569 0.0930  -0.1043 -0.0128 261  HIS   B CE1 
4597  N  NE2 . HIS   B 261 ? 1.1768 1.1942 1.1648 0.1002  -0.1029 -0.0124 261  HIS   B NE2 
4598  N  N   . ASN   B 262 ? 1.1932 1.1892 1.1587 0.1145  -0.1066 -0.0119 262  ASN   B N   
4599  C  CA  . ASN   B 262 ? 1.2410 1.2243 1.1965 0.1197  -0.1140 -0.0165 262  ASN   B CA  
4600  C  C   . ASN   B 262 ? 1.2691 1.2421 1.2084 0.1278  -0.1107 -0.0152 262  ASN   B C   
4601  O  O   . ASN   B 262 ? 1.2611 1.2325 1.1937 0.1316  -0.1042 -0.0115 262  ASN   B O   
4602  C  CB  . ASN   B 262 ? 1.2220 1.1976 1.1742 0.1221  -0.1205 -0.0194 262  ASN   B CB  
4603  C  CG  . ASN   B 262 ? 1.2671 1.2290 1.2088 0.1277  -0.1288 -0.0243 262  ASN   B CG  
4604  O  OD1 . ASN   B 262 ? 1.3100 1.2594 1.2357 0.1358  -0.1292 -0.0246 262  ASN   B OD1 
4605  N  ND2 . ASN   B 262 ? 1.2564 1.2202 1.2068 0.1236  -0.1355 -0.0284 262  ASN   B ND2 
4606  N  N   . ARG   B 263 ? 1.2728 1.2383 1.2055 0.1306  -0.1148 -0.0182 263  ARG   B N   
4607  C  CA  . ARG   B 263 ? 1.2983 1.2526 1.2141 0.1387  -0.1116 -0.0171 263  ARG   B CA  
4608  C  C   . ARG   B 263 ? 1.3887 1.3277 1.2890 0.1470  -0.1161 -0.0192 263  ARG   B C   
4609  O  O   . ARG   B 263 ? 1.4119 1.3452 1.3122 0.1474  -0.1253 -0.0240 263  ARG   B O   
4610  C  CB  . ARG   B 263 ? 1.2948 1.2459 1.2080 0.1391  -0.1142 -0.0193 263  ARG   B CB  
4611  C  CG  . ARG   B 263 ? 1.3278 1.2728 1.2280 0.1448  -0.1067 -0.0159 263  ARG   B CG  
4612  C  CD  . ARG   B 263 ? 1.3090 1.2457 1.2008 0.1481  -0.1101 -0.0186 263  ARG   B CD  
4613  N  NE  . ARG   B 263 ? 1.2669 1.2114 1.1719 0.1415  -0.1157 -0.0218 263  ARG   B NE  
4614  C  CZ  . ARG   B 263 ? 1.3048 1.2432 1.2092 0.1426  -0.1258 -0.0273 263  ARG   B CZ  
4615  N  NH1 . ARG   B 263 ? 1.3577 1.2817 1.2486 0.1499  -0.1319 -0.0304 263  ARG   B NH1 
4616  N  NH2 . ARG   B 263 ? 1.2016 1.1482 1.1194 0.1364  -0.1299 -0.0298 263  ARG   B NH2 
4617  N  N   . VAL   B 264 ? 1.4160 1.3484 1.3036 0.1535  -0.1095 -0.0158 264  VAL   B N   
4618  C  CA  . VAL   B 264 ? 1.4210 1.3379 1.2920 0.1622  -0.1128 -0.0174 264  VAL   B CA  
4619  C  C   . VAL   B 264 ? 1.4664 1.3680 1.3211 0.1694  -0.1172 -0.0205 264  VAL   B C   
4620  O  O   . VAL   B 264 ? 1.4697 1.3643 1.3225 0.1704  -0.1273 -0.0258 264  VAL   B O   
4621  C  CB  . VAL   B 264 ? 1.4674 1.3830 1.3311 0.1666  -0.1035 -0.0124 264  VAL   B CB  
4622  C  CG1 . VAL   B 264 ? 1.5716 1.4708 1.4180 0.1756  -0.1072 -0.0143 264  VAL   B CG1 
4623  C  CG2 . VAL   B 264 ? 1.4288 1.3597 1.3091 0.1594  -0.0997 -0.0096 264  VAL   B CG2 
4624  N  N   . ASP   B 265 ? 1.5876 1.4837 1.4305 0.1745  -0.1098 -0.0173 265  ASP   B N   
4625  C  CA  . ASP   B 265 ? 1.6451 1.5260 1.4715 0.1817  -0.1137 -0.0200 265  ASP   B CA  
4626  C  C   . ASP   B 265 ? 1.6113 1.4981 1.4471 0.1764  -0.1182 -0.0227 265  ASP   B C   
4627  O  O   . ASP   B 265 ? 1.5769 1.4781 1.4271 0.1691  -0.1129 -0.0200 265  ASP   B O   
4628  C  CB  . ASP   B 265 ? 1.7056 1.5781 1.5160 0.1889  -0.1040 -0.0156 265  ASP   B CB  
4629  C  CG  . ASP   B 265 ? 1.7190 1.6063 1.5413 0.1833  -0.0922 -0.0096 265  ASP   B CG  
4630  O  OD1 . ASP   B 265 ? 1.6694 1.5712 1.5090 0.1746  -0.0923 -0.0095 265  ASP   B OD1 
4631  O  OD2 . ASP   B 265 ? 1.7784 1.6624 1.5924 0.1880  -0.0830 -0.0051 265  ASP   B OD2 
4632  N  N   . PRO   B 266 ? 1.5565 1.4323 1.3846 0.1801  -0.1280 -0.0280 266  PRO   B N   
4633  C  CA  . PRO   B 266 ? 1.5040 1.3837 1.3388 0.1764  -0.1316 -0.0304 266  PRO   B CA  
4634  C  C   . PRO   B 266 ? 1.4866 1.3683 1.3175 0.1769  -0.1221 -0.0260 266  PRO   B C   
4635  O  O   . PRO   B 266 ? 1.4821 1.3732 1.3240 0.1711  -0.1216 -0.0261 266  PRO   B O   
4636  C  CB  . PRO   B 266 ? 1.4695 1.3324 1.2905 0.1836  -0.1427 -0.0363 266  PRO   B CB  
4637  C  CG  . PRO   B 266 ? 1.4641 1.3191 1.2789 0.1874  -0.1473 -0.0381 266  PRO   B CG  
4638  C  CD  . PRO   B 266 ? 1.4933 1.3518 1.3057 0.1882  -0.1365 -0.0323 266  PRO   B CD  
4639  N  N   . ASN   B 267 ? 1.5258 1.3985 1.3411 0.1838  -0.1143 -0.0222 267  ASN   B N   
4640  C  CA  . ASN   B 267 ? 1.5312 1.4047 1.3419 0.1848  -0.1042 -0.0176 267  ASN   B CA  
4641  C  C   . ASN   B 267 ? 1.4644 1.3578 1.2956 0.1748  -0.0971 -0.0138 267  ASN   B C   
4642  O  O   . ASN   B 267 ? 1.3912 1.2895 1.2266 0.1718  -0.0936 -0.0124 267  ASN   B O   
4643  C  CB  . ASN   B 267 ? 1.5533 1.4151 1.3463 0.1933  -0.0963 -0.0138 267  ASN   B CB  
4644  C  CG  . ASN   B 267 ? 1.5568 1.4212 1.3475 0.1936  -0.0841 -0.0081 267  ASN   B CG  
4645  O  OD1 . ASN   B 267 ? 1.5725 1.4492 1.3745 0.1890  -0.0755 -0.0035 267  ASN   B OD1 
4646  N  ND2 . ASN   B 267 ? 1.5357 1.3879 1.3115 0.1992  -0.0834 -0.0085 267  ASN   B ND2 
4647  N  N   . GLY   B 268 ? 1.4681 1.3726 1.3120 0.1699  -0.0951 -0.0120 268  GLY   B N   
4648  C  CA  . GLY   B 268 ? 1.4245 1.3470 1.2866 0.1612  -0.0884 -0.0083 268  GLY   B CA  
4649  C  C   . GLY   B 268 ? 1.4504 1.3769 1.3120 0.1622  -0.0767 -0.0022 268  GLY   B C   
4650  O  O   . GLY   B 268 ? 1.4614 1.4013 1.3363 0.1557  -0.0704 0.0012  268  GLY   B O   
4651  N  N   . SER   B 269 ? 1.4775 1.3929 1.3248 0.1701  -0.0737 -0.0007 269  SER   B N   
4652  C  CA  . SER   B 269 ? 1.4729 1.3917 1.3199 0.1716  -0.0625 0.0050  269  SER   B CA  
4653  C  C   . SER   B 269 ? 1.4782 1.4071 1.3367 0.1680  -0.0615 0.0064  269  SER   B C   
4654  O  O   . SER   B 269 ? 1.4887 1.4264 1.3545 0.1660  -0.0527 0.0112  269  SER   B O   
4655  C  CB  . SER   B 269 ? 1.6301 1.5309 1.4546 0.1826  -0.0586 0.0062  269  SER   B CB  
4656  O  OG  . SER   B 269 ? 1.6688 1.5556 1.4800 0.1887  -0.0681 0.0015  269  SER   B OG  
4657  N  N   . ARG   B 270 ? 1.4963 1.4240 1.3569 0.1671  -0.0705 0.0024  270  ARG   B N   
4658  C  CA  . ARG   B 270 ? 1.4243 1.3603 1.2950 0.1638  -0.0708 0.0032  270  ARG   B CA  
4659  C  C   . ARG   B 270 ? 1.3908 1.3367 1.2769 0.1555  -0.0790 -0.0003 270  ARG   B C   
4660  O  O   . ARG   B 270 ? 1.3861 1.3251 1.2686 0.1563  -0.0881 -0.0052 270  ARG   B O   
4661  C  CB  . ARG   B 270 ? 1.4642 1.3867 1.3200 0.1720  -0.0732 0.0021  270  ARG   B CB  
4662  C  CG  . ARG   B 270 ? 1.5533 1.4686 1.3967 0.1795  -0.0635 0.0065  270  ARG   B CG  
4663  C  CD  . ARG   B 270 ? 1.7158 1.6161 1.5431 0.1879  -0.0671 0.0046  270  ARG   B CD  
4664  N  NE  . ARG   B 270 ? 1.7866 1.6743 1.6031 0.1911  -0.0773 -0.0009 270  ARG   B NE  
4665  C  CZ  . ARG   B 270 ? 1.8978 1.7711 1.7004 0.1977  -0.0842 -0.0044 270  ARG   B CZ  
4666  N  NH1 . ARG   B 270 ? 2.0559 1.9257 1.8538 0.2015  -0.0822 -0.0030 270  ARG   B NH1 
4667  N  NH2 . ARG   B 270 ? 1.8482 1.7100 1.6413 0.2007  -0.0933 -0.0093 270  ARG   B NH2 
4668  N  N   . TYR   B 271 ? 1.3364 1.2981 1.2396 0.1477  -0.0755 0.0022  271  TYR   B N   
4669  C  CA  . TYR   B 271 ? 1.2641 1.2365 1.1831 0.1395  -0.0814 -0.0002 271  TYR   B CA  
4670  C  C   . TYR   B 271 ? 1.2753 1.2535 1.2008 0.1377  -0.0803 0.0014  271  TYR   B C   
4671  O  O   . TYR   B 271 ? 1.3079 1.2898 1.2339 0.1392  -0.0728 0.0057  271  TYR   B O   
4672  C  CB  . TYR   B 271 ? 1.2184 1.2042 1.1514 0.1316  -0.0781 0.0014  271  TYR   B CB  
4673  C  CG  . TYR   B 271 ? 1.2162 1.1985 1.1466 0.1313  -0.0811 -0.0011 271  TYR   B CG  
4674  C  CD1 . TYR   B 271 ? 1.2210 1.1996 1.1438 0.1345  -0.0752 0.0013  271  TYR   B CD1 
4675  C  CD2 . TYR   B 271 ? 1.2449 1.2277 1.1807 0.1277  -0.0897 -0.0057 271  TYR   B CD2 
4676  C  CE1 . TYR   B 271 ? 1.2588 1.2338 1.1787 0.1343  -0.0782 -0.0011 271  TYR   B CE1 
4677  C  CE2 . TYR   B 271 ? 1.3091 1.2890 1.2431 0.1275  -0.0927 -0.0081 271  TYR   B CE2 
4678  C  CZ  . TYR   B 271 ? 1.3108 1.2866 1.2364 0.1309  -0.0871 -0.0058 271  TYR   B CZ  
4679  O  OH  . TYR   B 271 ? 1.2794 1.2520 1.2027 0.1309  -0.0901 -0.0082 271  TYR   B OH  
4680  N  N   . LEU   B 272 ? 1.2654 1.2445 1.1965 0.1346  -0.0879 -0.0019 272  LEU   B N   
4681  C  CA  . LEU   B 272 ? 1.2181 1.2034 1.1567 0.1319  -0.0874 -0.0006 272  LEU   B CA  
4682  C  C   . LEU   B 272 ? 1.1822 1.1834 1.1387 0.1225  -0.0858 0.0008  272  LEU   B C   
4683  O  O   . LEU   B 272 ? 1.2233 1.2287 1.1872 0.1174  -0.0893 -0.0014 272  LEU   B O   
4684  C  CB  . LEU   B 272 ? 1.2254 1.2029 1.1607 0.1333  -0.0962 -0.0049 272  LEU   B CB  
4685  C  CG  . LEU   B 272 ? 1.1914 1.1527 1.1090 0.1427  -0.0987 -0.0065 272  LEU   B CG  
4686  C  CD1 . LEU   B 272 ? 1.1446 1.0989 1.0613 0.1426  -0.1088 -0.0115 272  LEU   B CD1 
4687  C  CD2 . LEU   B 272 ? 1.2239 1.1853 1.1373 0.1466  -0.0919 -0.0024 272  LEU   B CD2 
4688  N  N   . LEU   B 273 ? 1.1913 1.2008 1.1546 0.1205  -0.0806 0.0044  273  LEU   B N   
4689  C  CA  . LEU   B 273 ? 1.1953 1.2191 1.1746 0.1121  -0.0792 0.0059  273  LEU   B CA  
4690  C  C   . LEU   B 273 ? 1.2050 1.2316 1.1889 0.1106  -0.0808 0.0063  273  LEU   B C   
4691  O  O   . LEU   B 273 ? 1.2600 1.2817 1.2368 0.1160  -0.0788 0.0077  273  LEU   B O   
4692  C  CB  . LEU   B 273 ? 1.2116 1.2444 1.1963 0.1105  -0.0709 0.0103  273  LEU   B CB  
4693  C  CG  . LEU   B 273 ? 1.2193 1.2512 1.2015 0.1107  -0.0684 0.0105  273  LEU   B CG  
4694  C  CD1 . LEU   B 273 ? 1.1827 1.2241 1.1719 0.1085  -0.0602 0.0150  273  LEU   B CD1 
4695  C  CD2 . LEU   B 273 ? 1.2120 1.2461 1.2001 0.1053  -0.0743 0.0070  273  LEU   B CD2 
4696  N  N   . GLY   B 274 ? 1.1816 1.2156 1.1768 0.1036  -0.0841 0.0050  274  GLY   B N   
4697  C  CA  . GLY   B 274 ? 1.2135 1.2507 1.2138 0.1014  -0.0855 0.0055  274  GLY   B CA  
4698  C  C   . GLY   B 274 ? 1.2377 1.2879 1.2517 0.0937  -0.0832 0.0075  274  GLY   B C   
4699  O  O   . GLY   B 274 ? 1.2905 1.3461 1.3110 0.0889  -0.0834 0.0068  274  GLY   B O   
4700  N  N   . ASP   B 275 ? 1.1953 1.2504 1.2132 0.0930  -0.0809 0.0100  275  ASP   B N   
4701  C  CA  . ASP   B 275 ? 1.2428 1.3097 1.2727 0.0865  -0.0786 0.0121  275  ASP   B CA  
4702  C  C   . ASP   B 275 ? 1.2046 1.2723 1.2397 0.0819  -0.0833 0.0104  275  ASP   B C   
4703  O  O   . ASP   B 275 ? 1.1775 1.2380 1.2094 0.0824  -0.0886 0.0070  275  ASP   B O   
4704  C  CB  . ASP   B 275 ? 1.2386 1.3111 1.2703 0.0886  -0.0726 0.0163  275  ASP   B CB  
4705  C  CG  . ASP   B 275 ? 1.2311 1.3000 1.2590 0.0923  -0.0731 0.0171  275  ASP   B CG  
4706  O  OD1 . ASP   B 275 ? 1.2388 1.3006 1.2625 0.0931  -0.0782 0.0145  275  ASP   B OD1 
4707  O  OD2 . ASP   B 275 ? 1.2540 1.3276 1.2839 0.0944  -0.0684 0.0204  275  ASP   B OD2 
4708  N  N   . MET   B 276 ? 1.1896 1.2658 1.2330 0.0776  -0.0815 0.0125  276  MET   B N   
4709  C  CA  . MET   B 276 ? 1.1617 1.2386 1.2099 0.0732  -0.0850 0.0114  276  MET   B CA  
4710  C  C   . MET   B 276 ? 1.1570 1.2316 1.2024 0.0761  -0.0851 0.0127  276  MET   B C   
4711  O  O   . MET   B 276 ? 1.1391 1.2124 1.1866 0.0734  -0.0881 0.0117  276  MET   B O   
4712  C  CB  . MET   B 276 ? 1.1552 1.2420 1.2136 0.0662  -0.0836 0.0125  276  MET   B CB  
4713  C  CG  . MET   B 276 ? 1.2296 1.3208 1.2909 0.0643  -0.0814 0.0126  276  MET   B CG  
4714  S  SD  . MET   B 276 ? 1.2375 1.3397 1.3099 0.0566  -0.0797 0.0142  276  MET   B SD  
4715  C  CE  . MET   B 276 ? 1.0957 1.1948 1.1709 0.0521  -0.0845 0.0113  276  MET   B CE  
4716  N  N   . GLU   B 277 ? 1.1720 1.2457 1.2124 0.0817  -0.0816 0.0150  277  GLU   B N   
4717  C  CA  . GLU   B 277 ? 1.1646 1.2352 1.2013 0.0855  -0.0816 0.0162  277  GLU   B CA  
4718  C  C   . GLU   B 277 ? 1.1896 1.2483 1.2148 0.0922  -0.0838 0.0144  277  GLU   B C   
4719  O  O   . GLU   B 277 ? 1.2607 1.3158 1.2813 0.0964  -0.0834 0.0155  277  GLU   B O   
4720  C  CB  . GLU   B 277 ? 1.2464 1.3244 1.2864 0.0874  -0.0760 0.0202  277  GLU   B CB  
4721  C  CG  . GLU   B 277 ? 1.2957 1.3854 1.3467 0.0813  -0.0735 0.0221  277  GLU   B CG  
4722  C  CD  . GLU   B 277 ? 1.4370 1.5342 1.4922 0.0834  -0.0681 0.0258  277  GLU   B CD  
4723  O  OE1 . GLU   B 277 ? 1.4516 1.5455 1.5017 0.0896  -0.0654 0.0272  277  GLU   B OE1 
4724  O  OE2 . GLU   B 277 ? 1.4430 1.5495 1.5072 0.0788  -0.0665 0.0273  277  GLU   B OE2 
4725  N  N   . GLY   B 278 ? 1.1568 1.2089 1.1770 0.0934  -0.0866 0.0115  278  GLY   B N   
4726  C  CA  . GLY   B 278 ? 1.2007 1.2405 1.2094 0.0996  -0.0898 0.0092  278  GLY   B CA  
4727  C  C   . GLY   B 278 ? 1.2913 1.3261 1.2904 0.1069  -0.0861 0.0104  278  GLY   B C   
4728  O  O   . GLY   B 278 ? 1.3355 1.3589 1.3236 0.1126  -0.0889 0.0083  278  GLY   B O   
4729  N  N   . ARG   B 279 ? 1.2321 1.2744 1.2346 0.1070  -0.0799 0.0137  279  ARG   B N   
4730  C  CA  . ARG   B 279 ? 1.2439 1.2813 1.2374 0.1139  -0.0754 0.0152  279  ARG   B CA  
4731  C  C   . ARG   B 279 ? 1.2519 1.2830 1.2394 0.1151  -0.0773 0.0126  279  ARG   B C   
4732  O  O   . ARG   B 279 ? 1.2711 1.3066 1.2652 0.1095  -0.0796 0.0111  279  ARG   B O   
4733  C  CB  . ARG   B 279 ? 1.2266 1.2743 1.2271 0.1132  -0.0680 0.0194  279  ARG   B CB  
4734  C  CG  . ARG   B 279 ? 1.3188 1.3726 1.3254 0.1124  -0.0666 0.0218  279  ARG   B CG  
4735  C  CD  . ARG   B 279 ? 1.3743 1.4360 1.3859 0.1140  -0.0592 0.0259  279  ARG   B CD  
4736  N  NE  . ARG   B 279 ? 1.3733 1.4465 1.3969 0.1072  -0.0574 0.0271  279  ARG   B NE  
4737  C  CZ  . ARG   B 279 ? 1.4331 1.5159 1.4673 0.1024  -0.0575 0.0285  279  ARG   B CZ  
4738  N  NH1 . ARG   B 279 ? 1.3622 1.4451 1.3970 0.1037  -0.0588 0.0292  279  ARG   B NH1 
4739  N  NH2 . ARG   B 279 ? 1.4790 1.5709 1.5229 0.0963  -0.0566 0.0292  279  ARG   B NH2 
4740  N  N   . LEU   B 280 ? 1.3305 1.3508 1.3049 0.1228  -0.0765 0.0122  280  LEU   B N   
4741  C  CA  . LEU   B 280 ? 1.2896 1.3016 1.2557 0.1253  -0.0789 0.0096  280  LEU   B CA  
4742  C  C   . LEU   B 280 ? 1.2665 1.2770 1.2263 0.1303  -0.0716 0.0126  280  LEU   B C   
4743  O  O   . LEU   B 280 ? 1.2711 1.2759 1.2222 0.1371  -0.0678 0.0145  280  LEU   B O   
4744  C  CB  . LEU   B 280 ? 1.2591 1.2571 1.2135 0.1303  -0.0857 0.0057  280  LEU   B CB  
4745  C  CG  . LEU   B 280 ? 1.1797 1.1657 1.1216 0.1355  -0.0886 0.0030  280  LEU   B CG  
4746  C  CD1 . LEU   B 280 ? 1.2244 1.2150 1.1731 0.1301  -0.0908 0.0011  280  LEU   B CD1 
4747  C  CD2 . LEU   B 280 ? 1.0797 1.0527 1.0118 0.1397  -0.0961 -0.0010 280  LEU   B CD2 
4748  N  N   . PHE   B 281 ? 1.2605 1.2762 1.2248 0.1271  -0.0694 0.0131  281  PHE   B N   
4749  C  CA  . PHE   B 281 ? 1.2381 1.2530 1.1977 0.1309  -0.0621 0.0161  281  PHE   B CA  
4750  C  C   . PHE   B 281 ? 1.2856 1.2884 1.2323 0.1355  -0.0645 0.0135  281  PHE   B C   
4751  O  O   . PHE   B 281 ? 1.2925 1.2896 1.2364 0.1347  -0.0721 0.0093  281  PHE   B O   
4752  C  CB  . PHE   B 281 ? 1.2143 1.2428 1.1874 0.1244  -0.0573 0.0187  281  PHE   B CB  
4753  C  CG  . PHE   B 281 ? 1.2103 1.2511 1.1966 0.1194  -0.0553 0.0211  281  PHE   B CG  
4754  C  CD1 . PHE   B 281 ? 1.2341 1.2800 1.2287 0.1134  -0.0609 0.0191  281  PHE   B CD1 
4755  C  CD2 . PHE   B 281 ? 1.2228 1.2699 1.2135 0.1208  -0.0478 0.0254  281  PHE   B CD2 
4756  C  CE1 . PHE   B 281 ? 1.3065 1.3627 1.3121 0.1092  -0.0594 0.0213  281  PHE   B CE1 
4757  C  CE2 . PHE   B 281 ? 1.2572 1.3154 1.2601 0.1165  -0.0467 0.0274  281  PHE   B CE2 
4758  C  CZ  . PHE   B 281 ? 1.3176 1.3800 1.3273 0.1109  -0.0526 0.0253  281  PHE   B CZ  
4759  N  N   . MET   B 282 ? 1.3721 1.3713 1.3115 0.1404  -0.0576 0.0162  282  MET   B N   
4760  C  CA  . MET   B 282 ? 1.3389 1.3257 1.2643 0.1459  -0.0585 0.0144  282  MET   B CA  
4761  C  C   . MET   B 282 ? 1.3281 1.3200 1.2566 0.1444  -0.0513 0.0175  282  MET   B C   
4762  O  O   . MET   B 282 ? 1.3758 1.3703 1.3045 0.1469  -0.0428 0.0217  282  MET   B O   
4763  C  CB  . MET   B 282 ? 1.3128 1.2850 1.2208 0.1558  -0.0572 0.0146  282  MET   B CB  
4764  C  CG  . MET   B 282 ? 1.3019 1.2608 1.1942 0.1622  -0.0569 0.0135  282  MET   B CG  
4765  S  SD  . MET   B 282 ? 1.3521 1.3021 1.2390 0.1616  -0.0689 0.0070  282  MET   B SD  
4766  C  CE  . MET   B 282 ? 1.6000 1.5286 1.4627 0.1738  -0.0710 0.0054  282  MET   B CE  
4767  N  N   . LEU   B 283 ? 1.3661 1.3596 1.2976 0.1404  -0.0546 0.0153  283  LEU   B N   
4768  C  CA  . LEU   B 283 ? 1.3625 1.3591 1.2955 0.1393  -0.0486 0.0176  283  LEU   B CA  
4769  C  C   . LEU   B 283 ? 1.3937 1.3744 1.3080 0.1476  -0.0477 0.0169  283  LEU   B C   
4770  O  O   . LEU   B 283 ? 1.3941 1.3653 1.2999 0.1497  -0.0552 0.0126  283  LEU   B O   
4771  C  CB  . LEU   B 283 ? 1.3031 1.3089 1.2481 0.1310  -0.0525 0.0158  283  LEU   B CB  
4772  C  CG  . LEU   B 283 ? 1.3123 1.3238 1.2622 0.1278  -0.0469 0.0181  283  LEU   B CG  
4773  C  CD1 . LEU   B 283 ? 1.3427 1.3613 1.2981 0.1279  -0.0371 0.0234  283  LEU   B CD1 
4774  C  CD2 . LEU   B 283 ? 1.2833 1.3055 1.2470 0.1191  -0.0513 0.0162  283  LEU   B CD2 
4775  N  N   . LEU   B 284 ? 1.4154 1.3927 1.3231 0.1526  -0.0387 0.0209  284  LEU   B N   
4776  C  CA  . LEU   B 284 ? 1.4318 1.3939 1.3213 0.1607  -0.0364 0.0208  284  LEU   B CA  
4777  C  C   . LEU   B 284 ? 1.4451 1.4110 1.3378 0.1582  -0.0304 0.0232  284  LEU   B C   
4778  O  O   . LEU   B 284 ? 1.4684 1.4453 1.3725 0.1545  -0.0227 0.0273  284  LEU   B O   
4779  C  CB  . LEU   B 284 ? 1.4480 1.4010 1.3254 0.1692  -0.0301 0.0236  284  LEU   B CB  
4780  C  CG  . LEU   B 284 ? 1.4434 1.3908 1.3156 0.1725  -0.0359 0.0213  284  LEU   B CG  
4781  C  CD1 . LEU   B 284 ? 1.4612 1.4218 1.3477 0.1686  -0.0319 0.0243  284  LEU   B CD1 
4782  C  CD2 . LEU   B 284 ? 1.6385 1.5678 1.4891 0.1835  -0.0339 0.0214  284  LEU   B CD2 
4783  N  N   . LEU   B 285 ? 1.4428 1.3994 1.3257 0.1602  -0.0341 0.0206  285  LEU   B N   
4784  C  CA  . LEU   B 285 ? 1.4831 1.4404 1.3659 0.1591  -0.0283 0.0227  285  LEU   B CA  
4785  C  C   . LEU   B 285 ? 1.5700 1.5121 1.4338 0.1688  -0.0216 0.0250  285  LEU   B C   
4786  O  O   . LEU   B 285 ? 1.6095 1.5358 1.4557 0.1759  -0.0263 0.0221  285  LEU   B O   
4787  C  CB  . LEU   B 285 ? 1.4184 1.3752 1.3024 0.1555  -0.0360 0.0187  285  LEU   B CB  
4788  C  CG  . LEU   B 285 ? 1.3842 1.3567 1.2876 0.1457  -0.0412 0.0169  285  LEU   B CG  
4789  C  CD1 . LEU   B 285 ? 1.4288 1.3973 1.3305 0.1460  -0.0518 0.0119  285  LEU   B CD1 
4790  C  CD2 . LEU   B 285 ? 1.2695 1.2481 1.1804 0.1399  -0.0416 0.0164  285  LEU   B CD2 
4791  N  N   . GLU   B 286 ? 1.5870 1.5333 1.4542 0.1692  -0.0105 0.0303  286  GLU   B N   
4792  C  CA  . GLU   B 286 ? 1.6048 1.5371 1.4548 0.1781  -0.0025 0.0332  286  GLU   B CA  
4793  C  C   . GLU   B 286 ? 1.6926 1.6168 1.5335 0.1794  -0.0017 0.0326  286  GLU   B C   
4794  O  O   . GLU   B 286 ? 1.6793 1.6138 1.5325 0.1727  0.0007  0.0340  286  GLU   B O   
4795  C  CB  . GLU   B 286 ? 1.6258 1.5662 1.4845 0.1778  0.0096  0.0391  286  GLU   B CB  
4796  N  N   . LYS   B 287 ? 1.7725 1.6780 1.5916 0.1882  -0.0041 0.0306  287  LYS   B N   
4797  C  CA  . LYS   B 287 ? 1.7179 1.6129 1.5252 0.1908  -0.0050 0.0294  287  LYS   B CA  
4798  C  C   . LYS   B 287 ? 1.8186 1.7044 1.6144 0.1967  0.0074  0.0345  287  LYS   B C   
4799  O  O   . LYS   B 287 ? 1.8000 1.6851 1.5942 0.2003  0.0160  0.0384  287  LYS   B O   
4800  C  CB  . LYS   B 287 ? 1.6422 1.5212 1.4319 0.1971  -0.0159 0.0238  287  LYS   B CB  
4801  N  N   . GLU   B 288 ? 1.9108 1.7898 1.6990 0.1977  0.0086  0.0344  288  GLU   B N   
4802  C  CA  . GLU   B 288 ? 1.9707 1.8392 1.7464 0.2033  0.0201  0.0389  288  GLU   B CA  
4803  C  C   . GLU   B 288 ? 2.0976 1.9452 1.8490 0.2116  0.0153  0.0359  288  GLU   B C   
4804  O  O   . GLU   B 288 ? 2.1183 1.9656 1.8702 0.2087  0.0083  0.0325  288  GLU   B O   
4805  C  CB  . GLU   B 288 ? 1.9175 1.7989 1.7092 0.1956  0.0275  0.0426  288  GLU   B CB  
4806  N  N   . GLU   B 289 ? 2.4522 2.2817 2.1818 0.2221  0.0192  0.0370  289  GLU   B N   
4807  C  CA  . GLU   B 289 ? 2.4455 2.2528 2.1492 0.2314  0.0147  0.0341  289  GLU   B CA  
4808  C  C   . GLU   B 289 ? 2.4029 2.2017 2.0969 0.2343  0.0250  0.0381  289  GLU   B C   
4809  O  O   . GLU   B 289 ? 2.3788 2.1665 2.0594 0.2414  0.0358  0.0425  289  GLU   B O   
4810  C  CB  . GLU   B 289 ? 2.3920 2.1830 2.0760 0.2418  0.0137  0.0332  289  GLU   B CB  
4811  N  N   . GLN   B 290 ? 2.1483 1.9518 1.8486 0.2289  0.0218  0.0367  290  GLN   B N   
4812  C  CA  . GLN   B 290 ? 2.1310 1.9286 1.8251 0.2301  0.0314  0.0406  290  GLN   B CA  
4813  C  C   . GLN   B 290 ? 2.1650 1.9387 1.8312 0.2400  0.0275  0.0381  290  GLN   B C   
4814  O  O   . GLN   B 290 ? 2.1961 1.9613 1.8523 0.2437  0.0151  0.0324  290  GLN   B O   
4815  C  CB  . GLN   B 290 ? 2.0998 1.9147 1.8152 0.2191  0.0307  0.0408  290  GLN   B CB  
4816  C  CG  . GLN   B 290 ? 2.0743 1.9123 1.8170 0.2092  0.0349  0.0435  290  GLN   B CG  
4817  C  CD  . GLN   B 290 ? 2.0714 1.9107 1.8159 0.2115  0.0487  0.0497  290  GLN   B CD  
4818  O  OE1 . GLN   B 290 ? 2.1861 2.0285 1.9334 0.2131  0.0494  0.0502  290  GLN   B OE1 
4819  N  NE2 . GLN   B 290 ? 1.9222 1.7593 1.6659 0.2114  0.0601  0.0545  290  GLN   B NE2 
4820  N  N   . MET   B 291 ? 2.1271 1.8903 1.7814 0.2440  0.0382  0.0423  291  MET   B N   
4821  C  CA  . MET   B 291 ? 2.0558 1.7941 1.6810 0.2546  0.0369  0.0410  291  MET   B CA  
4822  C  C   . MET   B 291 ? 2.0588 1.7945 1.6817 0.2527  0.0260  0.0361  291  MET   B C   
4823  O  O   . MET   B 291 ? 2.0181 1.7352 1.6192 0.2610  0.0180  0.0321  291  MET   B O   
4824  C  CB  . MET   B 291 ? 1.9712 1.6991 1.5849 0.2593  0.0529  0.0476  291  MET   B CB  
4825  C  CG  . MET   B 291 ? 2.0276 1.7486 1.6326 0.2659  0.0630  0.0518  291  MET   B CG  
4826  S  SD  . MET   B 291 ? 2.0741 1.7901 1.6714 0.2711  0.0503  0.0462  291  MET   B SD  
4827  C  CE  . MET   B 291 ? 1.8541 1.5389 1.4145 0.2843  0.0439  0.0425  291  MET   B CE  
4828  N  N   . ASP   B 292 ? 2.1521 1.9060 1.7971 0.2421  0.0253  0.0362  292  ASP   B N   
4829  C  CA  . ASP   B 292 ? 2.1700 1.9242 1.8162 0.2392  0.0144  0.0313  292  ASP   B CA  
4830  C  C   . ASP   B 292 ? 2.2058 1.9661 1.8595 0.2368  -0.0011 0.0246  292  ASP   B C   
4831  O  O   . ASP   B 292 ? 2.1562 1.9192 1.8143 0.2336  -0.0108 0.0201  292  ASP   B O   
4832  C  CB  . ASP   B 292 ? 2.1209 1.8925 1.7886 0.2286  0.0193  0.0338  292  ASP   B CB  
4833  C  CG  . ASP   B 292 ? 2.1894 1.9858 1.8859 0.2178  0.0188  0.0343  292  ASP   B CG  
4834  O  OD1 . ASP   B 292 ? 2.1891 1.9893 1.8892 0.2187  0.0210  0.0356  292  ASP   B OD1 
4835  O  OD2 . ASP   B 292 ? 2.2621 2.0737 1.9771 0.2085  0.0161  0.0335  292  ASP   B OD2 
4836  N  N   . GLY   B 293 ? 2.1734 1.9358 1.8290 0.2382  -0.0034 0.0237  293  GLY   B N   
4837  C  CA  . GLY   B 293 ? 2.1271 1.8967 1.7920 0.2353  -0.0171 0.0178  293  GLY   B CA  
4838  C  C   . GLY   B 293 ? 2.1388 1.9337 1.8333 0.2234  -0.0174 0.0184  293  GLY   B C   
4839  O  O   . GLY   B 293 ? 2.1171 1.9184 1.8188 0.2221  -0.0202 0.0175  293  GLY   B O   
4840  N  N   . THR   B 294 ? 2.1747 1.9831 1.8853 0.2150  -0.0141 0.0201  294  THR   B N   
4841  C  CA  . THR   B 294 ? 2.1556 1.9875 1.8938 0.2034  -0.0150 0.0204  294  THR   B CA  
4842  C  C   . THR   B 294 ? 2.1704 2.0118 1.9186 0.2015  -0.0086 0.0239  294  THR   B C   
4843  O  O   . THR   B 294 ? 2.1895 2.0251 1.9299 0.2060  0.0023  0.0287  294  THR   B O   
4844  C  CB  . THR   B 294 ? 2.0850 1.9268 1.8351 0.1964  -0.0085 0.0234  294  THR   B CB  
4845  N  N   . VAL   B 295 ? 2.0471 1.9031 1.8127 0.1948  -0.0153 0.0214  295  VAL   B N   
4846  C  CA  . VAL   B 295 ? 2.0335 1.8986 1.8088 0.1930  -0.0117 0.0236  295  VAL   B CA  
4847  C  C   . VAL   B 295 ? 2.0342 1.9213 1.8352 0.1820  -0.0080 0.0261  295  VAL   B C   
4848  O  O   . VAL   B 295 ? 2.0207 1.9176 1.8340 0.1749  -0.0137 0.0236  295  VAL   B O   
4849  C  CB  . VAL   B 295 ? 2.0043 1.8667 1.7773 0.1952  -0.0227 0.0187  295  VAL   B CB  
4850  C  CG1 . VAL   B 295 ? 1.9861 1.8651 1.7780 0.1888  -0.0218 0.0200  295  VAL   B CG1 
4851  C  CG2 . VAL   B 295 ? 2.0239 1.8650 1.7716 0.2071  -0.0229 0.0181  295  VAL   B CG2 
4852  N  N   . THR   B 296 ? 2.0753 1.9697 1.8839 0.1808  0.0016  0.0310  296  THR   B N   
4853  C  CA  . THR   B 296 ? 2.0579 1.9722 1.8899 0.1710  0.0061  0.0338  296  THR   B CA  
4854  C  C   . THR   B 296 ? 2.0248 1.9490 1.8678 0.1689  0.0051  0.0341  296  THR   B C   
4855  O  O   . THR   B 296 ? 2.0323 1.9487 1.8654 0.1755  0.0088  0.0357  296  THR   B O   
4856  C  CB  . THR   B 296 ? 2.0757 1.9909 1.9092 0.1710  0.0193  0.0397  296  THR   B CB  
4857  O  OG1 . THR   B 296 ? 2.0828 1.9911 1.9090 0.1714  0.0200  0.0394  296  THR   B OG1 
4858  C  CG2 . THR   B 296 ? 2.0701 2.0058 1.9281 0.1615  0.0237  0.0427  296  THR   B CG2 
4859  N  N   . LEU   B 297 ? 1.8661 1.8069 1.7287 0.1599  0.0003  0.0327  297  LEU   B N   
4860  C  CA  . LEU   B 297 ? 1.7325 1.6844 1.6077 0.1567  -0.0002 0.0334  297  LEU   B CA  
4861  C  C   . LEU   B 297 ? 1.7148 1.6722 1.5962 0.1569  0.0117  0.0392  297  LEU   B C   
4862  O  O   . LEU   B 297 ? 1.6680 1.6373 1.5639 0.1505  0.0170  0.0421  297  LEU   B O   
4863  C  CB  . LEU   B 297 ? 1.6712 1.6392 1.5657 0.1468  -0.0070 0.0309  297  LEU   B CB  
4864  C  CG  . LEU   B 297 ? 1.6200 1.6017 1.5302 0.1418  -0.0081 0.0316  297  LEU   B CG  
4865  C  CD1 . LEU   B 297 ? 1.6945 1.6687 1.5958 0.1473  -0.0131 0.0293  297  LEU   B CD1 
4866  C  CD2 . LEU   B 297 ? 1.4230 1.4191 1.3507 0.1321  -0.0140 0.0294  297  LEU   B CD2 
4867  N  N   . LYS   B 298 ? 1.7499 1.6980 1.6198 0.1646  0.0161  0.0410  298  LYS   B N   
4868  C  CA  . LYS   B 298 ? 1.7424 1.6958 1.6188 0.1652  0.0276  0.0465  298  LYS   B CA  
4869  C  C   . LYS   B 298 ? 1.7762 1.7484 1.6747 0.1574  0.0268  0.0474  298  LYS   B C   
4870  O  O   . LYS   B 298 ? 1.7276 1.7121 1.6417 0.1516  0.0328  0.0506  298  LYS   B O   
4871  C  CB  . LYS   B 298 ? 1.7096 1.6485 1.5683 0.1755  0.0320  0.0479  298  LYS   B CB  
4872  N  N   . ASP   B 299 ? 1.8397 1.8142 1.7400 0.1571  0.0189  0.0443  299  ASP   B N   
4873  C  CA  . ASP   B 299 ? 1.8441 1.8343 1.7627 0.1511  0.0181  0.0451  299  ASP   B CA  
4874  C  C   . ASP   B 299 ? 1.8062 1.7975 1.7257 0.1491  0.0066  0.0403  299  ASP   B C   
4875  O  O   . ASP   B 299 ? 1.8021 1.7808 1.7068 0.1540  0.0002  0.0367  299  ASP   B O   
4876  C  CB  . ASP   B 299 ? 1.8635 1.8537 1.7822 0.1558  0.0269  0.0494  299  ASP   B CB  
4877  C  CG  . ASP   B 299 ? 1.9216 1.9293 1.8611 0.1495  0.0279  0.0511  299  ASP   B CG  
4878  O  OD1 . ASP   B 299 ? 1.9328 1.9538 1.8888 0.1416  0.0287  0.0521  299  ASP   B OD1 
4879  O  OD2 . ASP   B 299 ? 1.8944 1.9019 1.8331 0.1529  0.0280  0.0516  299  ASP   B OD2 
4880  N  N   . LEU   B 300 ? 1.6324 1.6388 1.5696 0.1418  0.0039  0.0402  300  LEU   B N   
4881  C  CA  . LEU   B 300 ? 1.5436 1.5531 1.4845 0.1391  -0.0056 0.0364  300  LEU   B CA  
4882  C  C   . LEU   B 300 ? 1.5076 1.5215 1.4532 0.1407  -0.0034 0.0383  300  LEU   B C   
4883  O  O   . LEU   B 300 ? 1.5005 1.5263 1.4599 0.1371  0.0022  0.0417  300  LEU   B O   
4884  C  CB  . LEU   B 300 ? 1.4621 1.4851 1.4192 0.1294  -0.0106 0.0347  300  LEU   B CB  
4885  C  CG  . LEU   B 300 ? 1.4367 1.4573 1.3918 0.1266  -0.0142 0.0323  300  LEU   B CG  
4886  C  CD1 . LEU   B 300 ? 1.3301 1.3651 1.3021 0.1180  -0.0122 0.0338  300  LEU   B CD1 
4887  C  CD2 . LEU   B 300 ? 1.4383 1.4543 1.3891 0.1263  -0.0249 0.0270  300  LEU   B CD2 
4888  N  N   . ARG   B 301 ? 1.4759 1.4805 1.4105 0.1461  -0.0082 0.0359  301  ARG   B N   
4889  C  CA  . ARG   B 301 ? 1.4604 1.4668 1.3967 0.1487  -0.0065 0.0374  301  ARG   B CA  
4890  C  C   . ARG   B 301 ? 1.4555 1.4659 1.3973 0.1449  -0.0160 0.0338  301  ARG   B C   
4891  O  O   . ARG   B 301 ? 1.4004 1.4045 1.3360 0.1446  -0.0242 0.0295  301  ARG   B O   
4892  C  CB  . ARG   B 301 ? 1.4477 1.4383 1.3650 0.1593  -0.0029 0.0382  301  ARG   B CB  
4893  C  CG  . ARG   B 301 ? 1.4639 1.4572 1.3837 0.1631  0.0048  0.0422  301  ARG   B CG  
4894  C  CD  . ARG   B 301 ? 1.4814 1.4837 1.4119 0.1612  0.0157  0.0473  301  ARG   B CD  
4895  N  NE  . ARG   B 301 ? 1.6021 1.5972 1.5245 0.1630  0.0201  0.0482  301  ARG   B NE  
4896  C  CZ  . ARG   B 301 ? 1.5471 1.5269 1.4514 0.1716  0.0249  0.0493  301  ARG   B CZ  
4897  N  NH1 . ARG   B 301 ? 1.6312 1.6011 1.5233 0.1795  0.0264  0.0496  301  ARG   B NH1 
4898  N  NH2 . ARG   B 301 ? 1.4941 1.4678 1.3916 0.1726  0.0283  0.0500  301  ARG   B NH2 
4899  N  N   . VAL   B 302 ? 1.4885 1.5097 1.4426 0.1417  -0.0148 0.0356  302  VAL   B N   
4900  C  CA  . VAL   B 302 ? 1.4512 1.4767 1.4113 0.1380  -0.0226 0.0328  302  VAL   B CA  
4901  C  C   . VAL   B 302 ? 1.4092 1.4319 1.3656 0.1431  -0.0210 0.0341  302  VAL   B C   
4902  O  O   . VAL   B 302 ? 1.4024 1.4321 1.3660 0.1437  -0.0140 0.0380  302  VAL   B O   
4903  C  CB  . VAL   B 302 ? 1.3784 1.4200 1.3573 0.1285  -0.0238 0.0334  302  VAL   B CB  
4904  C  CG1 . VAL   B 302 ? 1.3888 1.4350 1.3738 0.1259  -0.0293 0.0319  302  VAL   B CG1 
4905  C  CG2 . VAL   B 302 ? 1.3691 1.4117 1.3500 0.1234  -0.0282 0.0307  302  VAL   B CG2 
4906  N  N   . GLU   B 303 ? 1.3719 1.3847 1.3179 0.1468  -0.0276 0.0308  303  GLU   B N   
4907  C  CA  . GLU   B 303 ? 1.4090 1.4171 1.3494 0.1523  -0.0271 0.0315  303  GLU   B CA  
4908  C  C   . GLU   B 303 ? 1.3958 1.4057 1.3403 0.1487  -0.0359 0.0282  303  GLU   B C   
4909  O  O   . GLU   B 303 ? 1.3334 1.3409 1.2774 0.1453  -0.0434 0.0243  303  GLU   B O   
4910  C  CB  . GLU   B 303 ? 1.4268 1.4176 1.3469 0.1622  -0.0256 0.0309  303  GLU   B CB  
4911  C  CG  . GLU   B 303 ? 1.5332 1.5182 1.4463 0.1687  -0.0243 0.0318  303  GLU   B CG  
4912  C  CD  . GLU   B 303 ? 1.5601 1.5565 1.4850 0.1680  -0.0161 0.0365  303  GLU   B CD  
4913  O  OE1 . GLU   B 303 ? 1.6121 1.6058 1.5327 0.1731  -0.0071 0.0401  303  GLU   B OE1 
4914  O  OE2 . GLU   B 303 ? 1.4595 1.4672 1.3979 0.1625  -0.0186 0.0367  303  GLU   B OE2 
4915  N  N   . LEU   B 304 ? 1.4149 1.4291 1.3641 0.1494  -0.0346 0.0298  304  LEU   B N   
4916  C  CA  . LEU   B 304 ? 1.3551 1.3710 1.3084 0.1461  -0.0419 0.0273  304  LEU   B CA  
4917  C  C   . LEU   B 304 ? 1.3821 1.3836 1.3202 0.1535  -0.0458 0.0250  304  LEU   B C   
4918  O  O   . LEU   B 304 ? 1.3919 1.3880 1.3222 0.1604  -0.0408 0.0273  304  LEU   B O   
4919  C  CB  . LEU   B 304 ? 1.2847 1.3136 1.2520 0.1425  -0.0390 0.0302  304  LEU   B CB  
4920  C  CG  . LEU   B 304 ? 1.2674 1.2987 1.2397 0.1383  -0.0463 0.0278  304  LEU   B CG  
4921  C  CD1 . LEU   B 304 ? 1.2948 1.3271 1.2706 0.1319  -0.0529 0.0243  304  LEU   B CD1 
4922  C  CD2 . LEU   B 304 ? 1.2669 1.3111 1.2530 0.1344  -0.0436 0.0307  304  LEU   B CD2 
4923  N  N   . LEU   B 305 ? 1.3491 1.3445 1.2834 0.1519  -0.0546 0.0206  305  LEU   B N   
4924  C  CA  . LEU   B 305 ? 1.3659 1.3461 1.2849 0.1588  -0.0594 0.0179  305  LEU   B CA  
4925  C  C   . LEU   B 305 ? 1.4601 1.4404 1.3813 0.1582  -0.0636 0.0169  305  LEU   B C   
4926  O  O   . LEU   B 305 ? 1.5567 1.5254 1.4654 0.1651  -0.0651 0.0160  305  LEU   B O   
4927  C  CB  . LEU   B 305 ? 1.4233 1.3947 1.3354 0.1584  -0.0670 0.0132  305  LEU   B CB  
4928  C  CG  . LEU   B 305 ? 1.4373 1.4080 1.3473 0.1579  -0.0649 0.0131  305  LEU   B CG  
4929  C  CD1 . LEU   B 305 ? 1.3087 1.2699 1.2120 0.1581  -0.0739 0.0080  305  LEU   B CD1 
4930  C  CD2 . LEU   B 305 ? 1.4987 1.4630 1.3977 0.1655  -0.0565 0.0164  305  LEU   B CD2 
4931  N  N   . GLY   B 306 ? 1.4257 1.4179 1.3616 0.1505  -0.0655 0.0171  306  GLY   B N   
4932  C  CA  . GLY   B 306 ? 1.4545 1.4467 1.3928 0.1495  -0.0694 0.0163  306  GLY   B CA  
4933  C  C   . GLY   B 306 ? 1.4015 1.4029 1.3532 0.1403  -0.0743 0.0147  306  GLY   B C   
4934  O  O   . GLY   B 306 ? 1.3720 1.3824 1.3332 0.1344  -0.0731 0.0152  306  GLY   B O   
4935  N  N   . GLU   B 307 ? 1.5695 1.5680 1.5216 0.1391  -0.0796 0.0128  307  GLU   B N   
4936  C  CA  . GLU   B 307 ? 1.5529 1.5590 1.5169 0.1308  -0.0839 0.0115  307  GLU   B CA  
4937  C  C   . GLU   B 307 ? 1.5544 1.5509 1.5139 0.1302  -0.0922 0.0069  307  GLU   B C   
4938  O  O   . GLU   B 307 ? 1.5671 1.5519 1.5154 0.1361  -0.0952 0.0052  307  GLU   B O   
4939  C  CB  . GLU   B 307 ? 1.5333 1.5469 1.5048 0.1287  -0.0819 0.0141  307  GLU   B CB  
4940  C  CG  . GLU   B 307 ? 1.5287 1.5551 1.5147 0.1200  -0.0817 0.0150  307  GLU   B CG  
4941  C  CD  . GLU   B 307 ? 1.5906 1.6229 1.5827 0.1184  -0.0806 0.0172  307  GLU   B CD  
4942  O  OE1 . GLU   B 307 ? 1.5800 1.6050 1.5654 0.1226  -0.0825 0.0168  307  GLU   B OE1 
4943  O  OE2 . GLU   B 307 ? 1.6132 1.6571 1.6163 0.1132  -0.0780 0.0194  307  GLU   B OE2 
4944  N  N   . THR   B 308 ? 1.2976 1.2989 1.2662 0.1230  -0.0961 0.0047  308  THR   B N   
4945  C  CA  . THR   B 308 ? 1.2671 1.2607 1.2343 0.1214  -0.1040 0.0003  308  THR   B CA  
4946  C  C   . THR   B 308 ? 1.2231 1.2249 1.2034 0.1130  -0.1062 -0.0001 308  THR   B C   
4947  O  O   . THR   B 308 ? 1.2714 1.2825 1.2591 0.1098  -0.1022 0.0030  308  THR   B O   
4948  C  CB  . THR   B 308 ? 1.2566 1.2451 1.2199 0.1223  -0.1072 -0.0028 308  THR   B CB  
4949  O  OG1 . THR   B 308 ? 1.2629 1.2623 1.2371 0.1158  -0.1050 -0.0020 308  THR   B OG1 
4950  C  CG2 . THR   B 308 ? 1.3027 1.2826 1.2520 0.1308  -0.1043 -0.0021 308  THR   B CG2 
4951  N  N   . SER   B 309 ? 1.1919 1.1900 1.1752 0.1095  -0.1125 -0.0040 309  SER   B N   
4952  C  CA  . SER   B 309 ? 1.1270 1.1326 1.1228 0.1012  -0.1140 -0.0043 309  SER   B CA  
4953  C  C   . SER   B 309 ? 1.1076 1.1241 1.1126 0.0959  -0.1106 -0.0031 309  SER   B C   
4954  O  O   . SER   B 309 ? 1.1523 1.1683 1.1545 0.0978  -0.1098 -0.0036 309  SER   B O   
4955  C  CB  . SER   B 309 ? 1.1161 1.1145 1.1134 0.0990  -0.1214 -0.0089 309  SER   B CB  
4956  O  OG  . SER   B 309 ? 1.1532 1.1423 1.1438 0.1026  -0.1247 -0.0099 309  SER   B OG  
4957  N  N   . ILE   B 310 ? 1.0839 1.1097 1.0993 0.0895  -0.1086 -0.0013 310  ILE   B N   
4958  C  CA  . ILE   B 310 ? 1.1036 1.1397 1.1278 0.0842  -0.1055 -0.0001 310  ILE   B CA  
4959  C  C   . ILE   B 310 ? 1.1620 1.1951 1.1876 0.0826  -0.1096 -0.0038 310  ILE   B C   
4960  O  O   . ILE   B 310 ? 1.1533 1.1861 1.1854 0.0778  -0.1135 -0.0063 310  ILE   B O   
4961  C  CB  . ILE   B 310 ? 1.0805 1.1250 1.1147 0.0775  -0.1039 0.0017  310  ILE   B CB  
4962  C  CG1 . ILE   B 310 ? 1.0908 1.1369 1.1228 0.0799  -0.1009 0.0049  310  ILE   B CG1 
4963  C  CG2 . ILE   B 310 ? 1.1031 1.1580 1.1452 0.0728  -0.1002 0.0034  310  ILE   B CG2 
4964  C  CD1 . ILE   B 310 ? 1.0944 1.1491 1.1352 0.0740  -0.0987 0.0072  310  ILE   B CD1 
4965  N  N   . ALA   B 311 ? 1.1275 1.1580 1.1470 0.0867  -0.1087 -0.0042 311  ALA   B N   
4966  C  CA  . ALA   B 311 ? 1.1008 1.1259 1.1187 0.0872  -0.1134 -0.0081 311  ALA   B CA  
4967  C  C   . ALA   B 311 ? 1.1139 1.1475 1.1425 0.0805  -0.1129 -0.0086 311  ALA   B C   
4968  O  O   . ALA   B 311 ? 1.2133 1.2547 1.2449 0.0789  -0.1079 -0.0059 311  ALA   B O   
4969  C  CB  . ALA   B 311 ? 1.2004 1.2191 1.2067 0.0944  -0.1121 -0.0080 311  ALA   B CB  
4970  N  N   . GLU   B 312 ? 1.1145 1.1467 1.1494 0.0766  -0.1180 -0.0121 312  GLU   B N   
4971  C  CA  . GLU   B 312 ? 1.1579 1.1961 1.2013 0.0717  -0.1181 -0.0133 312  GLU   B CA  
4972  C  C   . GLU   B 312 ? 1.2347 1.2687 1.2712 0.0761  -0.1192 -0.0148 312  GLU   B C   
4973  O  O   . GLU   B 312 ? 1.1906 1.2300 1.2273 0.0758  -0.1147 -0.0127 312  GLU   B O   
4974  C  CB  . GLU   B 312 ? 1.0770 1.1146 1.1295 0.0666  -0.1231 -0.0166 312  GLU   B CB  
4975  C  CG  . GLU   B 312 ? 1.1268 1.1723 1.1910 0.0600  -0.1225 -0.0175 312  GLU   B CG  
4976  C  CD  . GLU   B 312 ? 1.2158 1.2721 1.2854 0.0556  -0.1160 -0.0136 312  GLU   B CD  
4977  O  OE1 . GLU   B 312 ? 1.2009 1.2597 1.2683 0.0560  -0.1123 -0.0102 312  GLU   B OE1 
4978  O  OE2 . GLU   B 312 ? 1.2428 1.3047 1.3187 0.0519  -0.1150 -0.0140 312  GLU   B OE2 
4979  N  N   . CYS   B 313 ? 1.3791 1.4025 1.4085 0.0808  -0.1250 -0.0185 313  CYS   B N   
4980  C  CA  . CYS   B 313 ? 1.4154 1.4328 1.4364 0.0859  -0.1267 -0.0202 313  CYS   B CA  
4981  C  C   . CYS   B 313 ? 1.4305 1.4371 1.4363 0.0944  -0.1269 -0.0198 313  CYS   B C   
4982  O  O   . CYS   B 313 ? 1.4318 1.4347 1.4342 0.0963  -0.1274 -0.0192 313  CYS   B O   
4983  C  CB  . CYS   B 313 ? 1.4686 1.4818 1.4937 0.0846  -0.1341 -0.0253 313  CYS   B CB  
4984  S  SG  . CYS   B 313 ? 1.5545 1.5553 1.5754 0.0880  -0.1429 -0.0298 313  CYS   B SG  
4985  N  N   . LEU   B 314 ? 1.3319 1.3331 1.3280 0.0997  -0.1263 -0.0201 314  LEU   B N   
4986  C  CA  . LEU   B 314 ? 1.2305 1.2202 1.2107 0.1084  -0.1264 -0.0199 314  LEU   B CA  
4987  C  C   . LEU   B 314 ? 1.2742 1.2536 1.2455 0.1133  -0.1317 -0.0237 314  LEU   B C   
4988  O  O   . LEU   B 314 ? 1.3554 1.3385 1.3313 0.1107  -0.1322 -0.0248 314  LEU   B O   
4989  C  CB  . LEU   B 314 ? 1.2331 1.2262 1.2080 0.1112  -0.1176 -0.0149 314  LEU   B CB  
4990  C  CG  . LEU   B 314 ? 1.2656 1.2637 1.2432 0.1103  -0.1132 -0.0114 314  LEU   B CG  
4991  C  CD1 . LEU   B 314 ? 1.2805 1.2825 1.2544 0.1130  -0.1047 -0.0067 314  LEU   B CD1 
4992  C  CD2 . LEU   B 314 ? 1.2349 1.2220 1.2036 0.1154  -0.1177 -0.0133 314  LEU   B CD2 
4993  N  N   . THR   B 315 ? 1.2245 1.1905 1.1823 0.1207  -0.1358 -0.0257 315  THR   B N   
4994  C  CA  . THR   B 315 ? 1.2459 1.2006 1.1924 0.1266  -0.1406 -0.0291 315  THR   B CA  
4995  C  C   . THR   B 315 ? 1.2499 1.1900 1.1781 0.1361  -0.1417 -0.0294 315  THR   B C   
4996  O  O   . THR   B 315 ? 1.2650 1.1997 1.1908 0.1377  -0.1451 -0.0306 315  THR   B O   
4997  C  CB  . THR   B 315 ? 1.2487 1.2012 1.2026 0.1237  -0.1502 -0.0347 315  THR   B CB  
4998  O  OG1 . THR   B 315 ? 1.2822 1.2224 1.2237 0.1304  -0.1555 -0.0381 315  THR   B OG1 
4999  C  CG2 . THR   B 315 ? 1.1962 1.1458 1.1548 0.1220  -0.1560 -0.0372 315  THR   B CG2 
5000  N  N   . TYR   B 316 ? 1.2430 1.1761 1.1579 0.1425  -0.1385 -0.0282 316  TYR   B N   
5001  C  CA  . TYR   B 316 ? 1.2843 1.2014 1.1800 0.1523  -0.1402 -0.0291 316  TYR   B CA  
5002  C  C   . TYR   B 316 ? 1.3124 1.2175 1.2028 0.1553  -0.1516 -0.0354 316  TYR   B C   
5003  O  O   . TYR   B 316 ? 1.3728 1.2777 1.2659 0.1540  -0.1558 -0.0382 316  TYR   B O   
5004  C  CB  . TYR   B 316 ? 1.3323 1.2450 1.2152 0.1582  -0.1329 -0.0258 316  TYR   B CB  
5005  C  CG  . TYR   B 316 ? 1.3444 1.2396 1.2059 0.1690  -0.1337 -0.0264 316  TYR   B CG  
5006  C  CD1 . TYR   B 316 ? 1.3610 1.2535 1.2164 0.1726  -0.1293 -0.0236 316  TYR   B CD1 
5007  C  CD2 . TYR   B 316 ? 1.4201 1.3009 1.2671 0.1756  -0.1393 -0.0299 316  TYR   B CD2 
5008  C  CE1 . TYR   B 316 ? 1.4778 1.3536 1.3129 0.1828  -0.1299 -0.0241 316  TYR   B CE1 
5009  C  CE2 . TYR   B 316 ? 1.5176 1.3812 1.3436 0.1859  -0.1402 -0.0305 316  TYR   B CE2 
5010  C  CZ  . TYR   B 316 ? 1.5142 1.3752 1.3342 0.1895  -0.1353 -0.0276 316  TYR   B CZ  
5011  O  OH  . TYR   B 316 ? 1.5138 1.3571 1.3123 0.1999  -0.1360 -0.0282 316  TYR   B OH  
5012  N  N   . LEU   B 317 ? 1.3140 1.2092 1.1976 0.1591  -0.1570 -0.0377 317  LEU   B N   
5013  C  CA  . LEU   B 317 ? 1.3644 1.2462 1.2409 0.1633  -0.1683 -0.0438 317  LEU   B CA  
5014  C  C   . LEU   B 317 ? 1.4328 1.2980 1.2865 0.1740  -0.1687 -0.0443 317  LEU   B C   
5015  O  O   . LEU   B 317 ? 1.4481 1.3101 1.2971 0.1761  -0.1697 -0.0455 317  LEU   B O   
5016  C  CB  . LEU   B 317 ? 1.3232 1.2007 1.2020 0.1627  -0.1743 -0.0462 317  LEU   B CB  
5017  C  CG  . LEU   B 317 ? 1.2873 1.1798 1.1857 0.1530  -0.1721 -0.0446 317  LEU   B CG  
5018  C  CD1 . LEU   B 317 ? 1.2445 1.1310 1.1454 0.1524  -0.1798 -0.0480 317  LEU   B CD1 
5019  C  CD2 . LEU   B 317 ? 1.2532 1.1583 1.1686 0.1449  -0.1724 -0.0453 317  LEU   B CD2 
5020  N  N   . ASP   B 318 ? 1.4836 1.3378 1.3227 0.1811  -0.1677 -0.0434 318  ASP   B N   
5021  C  CA  . ASP   B 318 ? 1.5239 1.3621 1.3401 0.1918  -0.1661 -0.0430 318  ASP   B CA  
5022  C  C   . ASP   B 318 ? 1.5561 1.3854 1.3600 0.1979  -0.1638 -0.0413 318  ASP   B C   
5023  O  O   . ASP   B 318 ? 1.5662 1.3984 1.3778 0.1947  -0.1669 -0.0423 318  ASP   B O   
5024  C  CB  . ASP   B 318 ? 1.5597 1.3835 1.3656 0.1969  -0.1770 -0.0490 318  ASP   B CB  
5025  C  CG  . ASP   B 318 ? 1.6644 1.4723 1.4465 0.2076  -0.1745 -0.0482 318  ASP   B CG  
5026  O  OD1 . ASP   B 318 ? 1.6805 1.4931 1.4597 0.2083  -0.1641 -0.0433 318  ASP   B OD1 
5027  O  OD2 . ASP   B 318 ? 1.7494 1.5397 1.5155 0.2154  -0.1828 -0.0525 318  ASP   B OD2 
5028  N  N   . ASN   B 319 ? 1.5358 1.3541 1.3204 0.2069  -0.1580 -0.0388 319  ASN   B N   
5029  C  CA  . ASN   B 319 ? 1.5646 1.3730 1.3349 0.2142  -0.1545 -0.0368 319  ASN   B CA  
5030  C  C   . ASN   B 319 ? 1.5286 1.3517 1.3115 0.2090  -0.1456 -0.0316 319  ASN   B C   
5031  O  O   . ASN   B 319 ? 1.4453 1.2642 1.2241 0.2116  -0.1456 -0.0311 319  ASN   B O   
5032  C  CB  . ASN   B 319 ? 1.5942 1.3880 1.3557 0.2185  -0.1660 -0.0422 319  ASN   B CB  
5033  C  CG  . ASN   B 319 ? 1.6226 1.4013 1.3719 0.2239  -0.1762 -0.0479 319  ASN   B CG  
5034  O  OD1 . ASN   B 319 ? 1.6296 1.3926 1.3575 0.2336  -0.1752 -0.0479 319  ASN   B OD1 
5035  N  ND2 . ASN   B 319 ? 1.6422 1.4250 1.4051 0.2178  -0.1862 -0.0528 319  ASN   B ND2 
5036  N  N   . GLY   B 320 ? 1.5092 1.3491 1.3073 0.2017  -0.1383 -0.0279 320  GLY   B N   
5037  C  CA  . GLY   B 320 ? 1.4748 1.3296 1.2861 0.1963  -0.1302 -0.0231 320  GLY   B CA  
5038  C  C   . GLY   B 320 ? 1.4301 1.2966 1.2602 0.1872  -0.1347 -0.0246 320  GLY   B C   
5039  O  O   . GLY   B 320 ? 1.4218 1.2999 1.2622 0.1830  -0.1286 -0.0208 320  GLY   B O   
5040  N  N   . VAL   B 321 ? 1.3946 1.2584 1.2298 0.1840  -0.1451 -0.0299 321  VAL   B N   
5041  C  CA  . VAL   B 321 ? 1.3084 1.1825 1.1614 0.1753  -0.1492 -0.0313 321  VAL   B CA  
5042  C  C   . VAL   B 321 ? 1.3050 1.1952 1.1759 0.1662  -0.1468 -0.0302 321  VAL   B C   
5043  O  O   . VAL   B 321 ? 1.3257 1.2147 1.1975 0.1654  -0.1505 -0.0329 321  VAL   B O   
5044  C  CB  . VAL   B 321 ? 1.3253 1.1886 1.1762 0.1762  -0.1614 -0.0375 321  VAL   B CB  
5045  C  CG1 . VAL   B 321 ? 1.3108 1.1845 1.1800 0.1673  -0.1644 -0.0384 321  VAL   B CG1 
5046  C  CG2 . VAL   B 321 ? 1.4637 1.3102 1.2956 0.1857  -0.1639 -0.0385 321  VAL   B CG2 
5047  N  N   . VAL   B 322 ? 1.2918 1.1965 1.1764 0.1595  -0.1407 -0.0265 322  VAL   B N   
5048  C  CA  . VAL   B 322 ? 1.2415 1.1617 1.1438 0.1503  -0.1385 -0.0254 322  VAL   B CA  
5049  C  C   . VAL   B 322 ? 1.1838 1.1101 1.1003 0.1430  -0.1434 -0.0274 322  VAL   B C   
5050  O  O   . VAL   B 322 ? 1.1840 1.1099 1.1007 0.1432  -0.1427 -0.0262 322  VAL   B O   
5051  C  CB  . VAL   B 322 ? 1.2453 1.1774 1.1526 0.1482  -0.1276 -0.0195 322  VAL   B CB  
5052  C  CG1 . VAL   B 322 ? 1.1775 1.1249 1.1022 0.1388  -0.1258 -0.0187 322  VAL   B CG1 
5053  C  CG2 . VAL   B 322 ? 1.2868 1.2120 1.1795 0.1558  -0.1219 -0.0172 322  VAL   B CG2 
5054  N  N   . PHE   B 323 ? 1.1566 1.0882 1.0849 0.1369  -0.1481 -0.0303 323  PHE   B N   
5055  C  CA  . PHE   B 323 ? 1.1390 1.0778 1.0824 0.1292  -0.1514 -0.0317 323  PHE   B CA  
5056  C  C   . PHE   B 323 ? 1.1601 1.1149 1.1171 0.1217  -0.1439 -0.0274 323  PHE   B C   
5057  O  O   . PHE   B 323 ? 1.2249 1.1872 1.1867 0.1190  -0.1404 -0.0262 323  PHE   B O   
5058  C  CB  . PHE   B 323 ? 1.0904 1.0270 1.0412 0.1260  -0.1601 -0.0370 323  PHE   B CB  
5059  C  CG  . PHE   B 323 ? 1.0874 1.0317 1.0544 0.1178  -0.1624 -0.0380 323  PHE   B CG  
5060  C  CD1 . PHE   B 323 ? 1.1103 1.0484 1.0769 0.1181  -0.1669 -0.0397 323  PHE   B CD1 
5061  C  CD2 . PHE   B 323 ? 1.0999 1.0573 1.0821 0.1098  -0.1595 -0.0369 323  PHE   B CD2 
5062  C  CE1 . PHE   B 323 ? 1.1106 1.0554 1.0921 0.1105  -0.1684 -0.0404 323  PHE   B CE1 
5063  C  CE2 . PHE   B 323 ? 1.1158 1.0798 1.1124 0.1024  -0.1609 -0.0376 323  PHE   B CE2 
5064  C  CZ  . PHE   B 323 ? 1.1403 1.0980 1.1366 0.1026  -0.1651 -0.0392 323  PHE   B CZ  
5065  N  N   . VAL   B 324 ? 1.1267 1.0863 1.0896 0.1185  -0.1419 -0.0255 324  VAL   B N   
5066  C  CA  . VAL   B 324 ? 1.0768 1.0507 1.0523 0.1115  -0.1357 -0.0217 324  VAL   B CA  
5067  C  C   . VAL   B 324 ? 1.0988 1.0772 1.0880 0.1039  -0.1400 -0.0241 324  VAL   B C   
5068  O  O   . VAL   B 324 ? 1.1165 1.0911 1.1068 0.1032  -0.1432 -0.0251 324  VAL   B O   
5069  C  CB  . VAL   B 324 ? 1.1165 1.0923 1.0881 0.1138  -0.1298 -0.0175 324  VAL   B CB  
5070  C  CG1 . VAL   B 324 ? 1.1807 1.1702 1.1652 0.1067  -0.1247 -0.0141 324  VAL   B CG1 
5071  C  CG2 . VAL   B 324 ? 1.1594 1.1316 1.1190 0.1209  -0.1247 -0.0150 324  VAL   B CG2 
5072  N  N   . GLY   B 325 ? 1.1088 1.0948 1.1085 0.0983  -0.1403 -0.0251 325  GLY   B N   
5073  C  CA  . GLY   B 325 ? 1.0673 1.0593 1.0813 0.0905  -0.1426 -0.0265 325  GLY   B CA  
5074  C  C   . GLY   B 325 ? 1.0932 1.0964 1.1151 0.0852  -0.1358 -0.0221 325  GLY   B C   
5075  O  O   . GLY   B 325 ? 1.1566 1.1670 1.1784 0.0849  -0.1298 -0.0188 325  GLY   B O   
5076  N  N   . SER   B 326 ? 1.0339 1.0381 1.0623 0.0812  -0.1369 -0.0222 326  SER   B N   
5077  C  CA  . SER   B 326 ? 0.9867 0.9994 1.0201 0.0773  -0.1311 -0.0180 326  SER   B CA  
5078  C  C   . SER   B 326 ? 0.9837 1.0013 1.0300 0.0695  -0.1320 -0.0188 326  SER   B C   
5079  O  O   . SER   B 326 ? 0.9522 0.9642 1.0018 0.0682  -0.1374 -0.0222 326  SER   B O   
5080  C  CB  . SER   B 326 ? 1.0663 1.0738 1.0912 0.0819  -0.1301 -0.0161 326  SER   B CB  
5081  O  OG  . SER   B 326 ? 1.1009 1.1167 1.1288 0.0797  -0.1239 -0.0117 326  SER   B OG  
5082  N  N   . ARG   B 327 ? 0.9823 1.0102 1.0356 0.0646  -0.1266 -0.0157 327  ARG   B N   
5083  C  CA  . ARG   B 327 ? 0.9485 0.9818 1.0132 0.0572  -0.1259 -0.0156 327  ARG   B CA  
5084  C  C   . ARG   B 327 ? 0.9253 0.9603 0.9903 0.0556  -0.1228 -0.0124 327  ARG   B C   
5085  O  O   . ARG   B 327 ? 0.9502 0.9857 1.0222 0.0506  -0.1233 -0.0128 327  ARG   B O   
5086  C  CB  . ARG   B 327 ? 0.9984 1.0415 1.0708 0.0526  -0.1223 -0.0145 327  ARG   B CB  
5087  C  CG  . ARG   B 327 ? 1.0176 1.0602 1.0940 0.0519  -0.1257 -0.0181 327  ARG   B CG  
5088  C  CD  . ARG   B 327 ? 1.0350 1.0782 1.1228 0.0460  -0.1284 -0.0207 327  ARG   B CD  
5089  N  NE  . ARG   B 327 ? 1.0652 1.1166 1.1615 0.0396  -0.1236 -0.0182 327  ARG   B NE  
5090  C  CZ  . ARG   B 327 ? 1.1592 1.2187 1.2595 0.0367  -0.1198 -0.0167 327  ARG   B CZ  
5091  N  NH1 . ARG   B 327 ? 1.1790 1.2400 1.2758 0.0395  -0.1196 -0.0170 327  ARG   B NH1 
5092  N  NH2 . ARG   B 327 ? 1.1509 1.2164 1.2581 0.0311  -0.1159 -0.0147 327  ARG   B NH2 
5093  N  N   . LEU   B 328 ? 0.9263 0.9626 0.9842 0.0594  -0.1193 -0.0092 328  LEU   B N   
5094  C  CA  . LEU   B 328 ? 0.9260 0.9634 0.9834 0.0586  -0.1168 -0.0064 328  LEU   B CA  
5095  C  C   . LEU   B 328 ? 0.9416 0.9691 0.9913 0.0632  -0.1201 -0.0074 328  LEU   B C   
5096  O  O   . LEU   B 328 ? 1.0189 1.0439 1.0703 0.0611  -0.1208 -0.0070 328  LEU   B O   
5097  C  CB  . LEU   B 328 ? 0.9212 0.9658 0.9764 0.0601  -0.1114 -0.0023 328  LEU   B CB  
5098  C  CG  . LEU   B 328 ? 0.9108 0.9652 0.9731 0.0557  -0.1080 -0.0011 328  LEU   B CG  
5099  C  CD1 . LEU   B 328 ? 0.9072 0.9681 0.9675 0.0576  -0.1031 0.0028  328  LEU   B CD1 
5100  C  CD2 . LEU   B 328 ? 0.9048 0.9627 0.9762 0.0485  -0.1078 -0.0014 328  LEU   B CD2 
5101  N  N   . GLY   B 329 ? 0.9630 0.9840 1.0039 0.0696  -0.1224 -0.0088 329  GLY   B N   
5102  C  CA  . GLY   B 329 ? 0.9969 1.0076 1.0294 0.0746  -0.1257 -0.0100 329  GLY   B CA  
5103  C  C   . GLY   B 329 ? 1.0323 1.0332 1.0602 0.0779  -0.1320 -0.0143 329  GLY   B C   
5104  O  O   . GLY   B 329 ? 1.0233 1.0254 1.0566 0.0754  -0.1344 -0.0170 329  GLY   B O   
5105  N  N   . ASP   B 330 ? 1.0289 1.0199 1.0470 0.0838  -0.1348 -0.0153 330  ASP   B N   
5106  C  CA  . ASP   B 330 ? 1.0432 1.0235 1.0559 0.0875  -0.1415 -0.0197 330  ASP   B CA  
5107  C  C   . ASP   B 330 ? 1.0893 1.0691 1.0964 0.0917  -0.1414 -0.0206 330  ASP   B C   
5108  O  O   . ASP   B 330 ? 1.0866 1.0701 1.0883 0.0950  -0.1361 -0.0174 330  ASP   B O   
5109  C  CB  . ASP   B 330 ? 1.0556 1.0249 1.0576 0.0933  -0.1442 -0.0202 330  ASP   B CB  
5110  C  CG  . ASP   B 330 ? 1.0385 1.0030 1.0458 0.0895  -0.1485 -0.0223 330  ASP   B CG  
5111  O  OD1 . ASP   B 330 ? 1.0646 1.0357 1.0838 0.0822  -0.1475 -0.0221 330  ASP   B OD1 
5112  O  OD2 . ASP   B 330 ? 1.0491 1.0027 1.0484 0.0939  -0.1528 -0.0242 330  ASP   B OD2 
5113  N  N   . SER   B 331 ? 1.0719 1.0470 1.0805 0.0914  -0.1472 -0.0248 331  SER   B N   
5114  C  CA  . SER   B 331 ? 1.0276 0.9989 1.0282 0.0967  -0.1482 -0.0262 331  SER   B CA  
5115  C  C   . SER   B 331 ? 1.0944 1.0527 1.0791 0.1056  -0.1509 -0.0272 331  SER   B C   
5116  O  O   . SER   B 331 ? 1.1078 1.0586 1.0890 0.1072  -0.1544 -0.0284 331  SER   B O   
5117  C  CB  . SER   B 331 ? 1.0357 1.0060 1.0432 0.0938  -0.1540 -0.0306 331  SER   B CB  
5118  O  OG  . SER   B 331 ? 1.0904 1.0727 1.1101 0.0871  -0.1503 -0.0292 331  SER   B OG  
5119  N  N   . GLN   B 332 ? 1.1369 1.0922 1.1114 0.1116  -0.1491 -0.0266 332  GLN   B N   
5120  C  CA  . GLN   B 332 ? 1.1733 1.1160 1.1314 0.1206  -0.1505 -0.0271 332  GLN   B CA  
5121  C  C   . GLN   B 332 ? 1.1959 1.1313 1.1432 0.1267  -0.1523 -0.0290 332  GLN   B C   
5122  O  O   . GLN   B 332 ? 1.1399 1.0811 1.0920 0.1243  -0.1510 -0.0291 332  GLN   B O   
5123  C  CB  . GLN   B 332 ? 1.1328 1.0788 1.0859 0.1235  -0.1430 -0.0221 332  GLN   B CB  
5124  C  CG  . GLN   B 332 ? 1.1093 1.0688 1.0692 0.1202  -0.1348 -0.0177 332  GLN   B CG  
5125  C  CD  . GLN   B 332 ? 1.1489 1.1115 1.1051 0.1232  -0.1281 -0.0132 332  GLN   B CD  
5126  O  OE1 . GLN   B 332 ? 1.1664 1.1372 1.1245 0.1230  -0.1213 -0.0096 332  GLN   B OE1 
5127  N  NE2 . GLN   B 332 ? 1.1814 1.1372 1.1324 0.1260  -0.1300 -0.0133 332  GLN   B NE2 
5128  N  N   . LEU   B 333 ? 1.2573 1.1785 1.1893 0.1349  -0.1558 -0.0307 333  LEU   B N   
5129  C  CA  . LEU   B 333 ? 1.2351 1.1468 1.1517 0.1431  -0.1558 -0.0314 333  LEU   B CA  
5130  C  C   . LEU   B 333 ? 1.2474 1.1574 1.1531 0.1493  -0.1481 -0.0269 333  LEU   B C   
5131  O  O   . LEU   B 333 ? 1.3090 1.2140 1.2098 0.1519  -0.1484 -0.0263 333  LEU   B O   
5132  C  CB  . LEU   B 333 ? 1.2309 1.1264 1.1369 0.1486  -0.1655 -0.0368 333  LEU   B CB  
5133  C  CG  . LEU   B 333 ? 1.2582 1.1532 1.1719 0.1450  -0.1733 -0.0416 333  LEU   B CG  
5134  C  CD1 . LEU   B 333 ? 1.2865 1.1644 1.1871 0.1521  -0.1826 -0.0468 333  LEU   B CD1 
5135  C  CD2 . LEU   B 333 ? 1.2646 1.1677 1.1818 0.1433  -0.1688 -0.0401 333  LEU   B CD2 
5136  N  N   . VAL   B 334 ? 1.2152 1.1293 1.1174 0.1514  -0.1411 -0.0237 334  VAL   B N   
5137  C  CA  . VAL   B 334 ? 1.2601 1.1732 1.1529 0.1573  -0.1331 -0.0193 334  VAL   B CA  
5138  C  C   . VAL   B 334 ? 1.3053 1.2051 1.1802 0.1665  -0.1332 -0.0203 334  VAL   B C   
5139  O  O   . VAL   B 334 ? 1.3539 1.2519 1.2276 0.1664  -0.1356 -0.0223 334  VAL   B O   
5140  C  CB  . VAL   B 334 ? 1.2569 1.1858 1.1606 0.1526  -0.1238 -0.0142 334  VAL   B CB  
5141  C  CG1 . VAL   B 334 ? 1.2207 1.1613 1.1396 0.1447  -0.1232 -0.0128 334  VAL   B CG1 
5142  C  CG2 . VAL   B 334 ? 1.2395 1.1740 1.1481 0.1494  -0.1228 -0.0145 334  VAL   B CG2 
5143  N  N   . LYS   B 335 ? 1.3171 1.2071 1.1778 0.1746  -0.1307 -0.0188 335  LYS   B N   
5144  C  CA  . LYS   B 335 ? 1.3631 1.2410 1.2058 0.1839  -0.1282 -0.0184 335  LYS   B CA  
5145  C  C   . LYS   B 335 ? 1.4117 1.2986 1.2559 0.1847  -0.1164 -0.0125 335  LYS   B C   
5146  O  O   . LYS   B 335 ? 1.4129 1.3052 1.2601 0.1850  -0.1108 -0.0090 335  LYS   B O   
5147  C  CB  . LYS   B 335 ? 1.3860 1.2468 1.2111 0.1928  -0.1320 -0.0204 335  LYS   B CB  
5148  N  N   . LEU   B 336 ? 1.4594 1.3487 1.3029 0.1847  -0.1127 -0.0115 336  LEU   B N   
5149  C  CA  . LEU   B 336 ? 1.5134 1.4083 1.3557 0.1870  -0.1016 -0.0061 336  LEU   B CA  
5150  C  C   . LEU   B 336 ? 1.6132 1.4921 1.4345 0.1984  -0.0986 -0.0053 336  LEU   B C   
5151  O  O   . LEU   B 336 ? 1.6320 1.4966 1.4386 0.2041  -0.1031 -0.0084 336  LEU   B O   
5152  C  CB  . LEU   B 336 ? 1.5065 1.4086 1.3549 0.1831  -0.0989 -0.0054 336  LEU   B CB  
5153  C  CG  . LEU   B 336 ? 1.3709 1.2876 1.2389 0.1723  -0.1019 -0.0064 336  LEU   B CG  
5154  C  CD1 . LEU   B 336 ? 1.3251 1.2519 1.2005 0.1686  -0.0954 -0.0036 336  LEU   B CD1 
5155  C  CD2 . LEU   B 336 ? 1.4389 1.3664 1.3200 0.1667  -0.1011 -0.0048 336  LEU   B CD2 
5156  N  N   . ASN   B 337 ? 1.6815 1.5621 1.5008 0.2018  -0.0912 -0.0013 337  ASN   B N   
5157  C  CA  . ASN   B 337 ? 1.7050 1.5707 1.5045 0.2128  -0.0872 -0.0001 337  ASN   B CA  
5158  C  C   . ASN   B 337 ? 1.7927 1.6597 1.5880 0.2161  -0.0769 0.0041  337  ASN   B C   
5159  O  O   . ASN   B 337 ? 1.7719 1.6516 1.5800 0.2097  -0.0730 0.0060  337  ASN   B O   
5160  C  CB  . ASN   B 337 ? 1.6844 1.5506 1.4835 0.2156  -0.0841 0.0022  337  ASN   B CB  
5161  C  CG  . ASN   B 337 ? 1.5808 1.4378 1.3752 0.2165  -0.0942 -0.0022 337  ASN   B CG  
5162  O  OD1 . ASN   B 337 ? 1.6241 1.4637 1.4002 0.2248  -0.0981 -0.0047 337  ASN   B OD1 
5163  N  ND2 . ASN   B 337 ? 1.4968 1.3648 1.3072 0.2082  -0.0983 -0.0031 337  ASN   B ND2 
5164  N  N   . VAL   B 338 ? 1.8847 1.7377 1.6614 0.2263  -0.0722 0.0055  338  VAL   B N   
5165  C  CA  . VAL   B 338 ? 1.9492 1.8010 1.7198 0.2305  -0.0619 0.0096  338  VAL   B CA  
5166  C  C   . VAL   B 338 ? 2.0376 1.9013 1.8180 0.2299  -0.0505 0.0154  338  VAL   B C   
5167  O  O   . VAL   B 338 ? 2.0290 1.9042 1.8200 0.2260  -0.0428 0.0191  338  VAL   B O   
5168  C  CB  . VAL   B 338 ? 1.9109 1.7403 1.6553 0.2423  -0.0621 0.0083  338  VAL   B CB  
5169  C  CG1 . VAL   B 338 ? 1.9056 1.7236 1.6414 0.2428  -0.0744 0.0021  338  VAL   B CG1 
5170  C  CG2 . VAL   B 338 ? 2.0180 1.8375 1.7503 0.2503  -0.0600 0.0092  338  VAL   B CG2 
5171  N  N   . ASP   B 339 ? 2.2093 2.0713 1.9878 0.2332  -0.0499 0.0163  339  ASP   B N   
5172  C  CA  . ASP   B 339 ? 2.2219 2.0929 2.0076 0.2343  -0.0394 0.0216  339  ASP   B CA  
5173  C  C   . ASP   B 339 ? 2.2464 2.1358 2.0542 0.2248  -0.0412 0.0222  339  ASP   B C   
5174  O  O   . ASP   B 339 ? 2.2205 2.1098 2.0317 0.2211  -0.0505 0.0186  339  ASP   B O   
5175  C  CB  . ASP   B 339 ? 2.2512 2.1084 2.0203 0.2447  -0.0368 0.0223  339  ASP   B CB  
5176  N  N   . SER   B 340 ? 2.1072 2.0119 1.9301 0.2208  -0.0325 0.0268  340  SER   B N   
5177  C  CA  . SER   B 340 ? 2.0793 2.0006 1.9218 0.2131  -0.0331 0.0280  340  SER   B CA  
5178  C  C   . SER   B 340 ? 2.1244 2.0403 1.9621 0.2168  -0.0366 0.0270  340  SER   B C   
5179  O  O   . SER   B 340 ? 2.1754 2.0822 2.0012 0.2255  -0.0317 0.0287  340  SER   B O   
5180  C  CB  . SER   B 340 ? 2.0571 1.9927 1.9133 0.2111  -0.0222 0.0334  340  SER   B CB  
5181  O  OG  . SER   B 340 ? 1.9893 1.9268 1.8464 0.2099  -0.0172 0.0349  340  SER   B OG  
5182  N  N   . ASN   B 341 ? 2.0839 2.0046 1.9300 0.2105  -0.0451 0.0241  341  ASN   B N   
5183  C  CA  . ASN   B 341 ? 2.1374 2.0530 1.9796 0.2132  -0.0491 0.0229  341  ASN   B CA  
5184  C  C   . ASN   B 341 ? 2.1539 2.0806 2.0062 0.2137  -0.0413 0.0275  341  ASN   B C   
5185  O  O   . ASN   B 341 ? 2.1301 2.0662 1.9904 0.2131  -0.0326 0.0315  341  ASN   B O   
5186  C  CB  . ASN   B 341 ? 2.1549 2.0717 2.0030 0.2063  -0.0601 0.0185  341  ASN   B CB  
5187  C  CG  . ASN   B 341 ? 2.0936 2.0281 1.9624 0.1968  -0.0604 0.0199  341  ASN   B CG  
5188  O  OD1 . ASN   B 341 ? 2.0950 2.0427 1.9759 0.1935  -0.0536 0.0236  341  ASN   B OD1 
5189  N  ND2 . ASN   B 341 ? 2.0141 1.9481 1.8865 0.1925  -0.0686 0.0169  341  ASN   B ND2 
5190  N  N   . GLU   B 342 ? 2.2263 2.1516 2.0785 0.2149  -0.0445 0.0269  342  GLU   B N   
5191  C  CA  . GLU   B 342 ? 2.2312 2.1660 2.0924 0.2160  -0.0380 0.0309  342  GLU   B CA  
5192  C  C   . GLU   B 342 ? 2.2197 2.1743 2.1025 0.2072  -0.0349 0.0335  342  GLU   B C   
5193  O  O   . GLU   B 342 ? 2.2093 2.1732 2.1007 0.2084  -0.0272 0.0375  342  GLU   B O   
5194  C  CB  . GLU   B 342 ? 2.2338 2.1632 2.0912 0.2178  -0.0437 0.0291  342  GLU   B CB  
5195  C  CG  . GLU   B 342 ? 2.2424 2.1696 2.1016 0.2114  -0.0548 0.0246  342  GLU   B CG  
5196  C  CD  . GLU   B 342 ? 2.2172 2.1255 2.0580 0.2166  -0.0619 0.0202  342  GLU   B CD  
5197  O  OE1 . GLU   B 342 ? 2.1798 2.0794 2.0095 0.2210  -0.0603 0.0196  342  GLU   B OE1 
5198  O  OE2 . GLU   B 342 ? 2.1957 2.0976 2.0332 0.2162  -0.0693 0.0173  342  GLU   B OE2 
5199  N  N   . GLN   B 343 ? 2.1501 2.1113 2.0422 0.1984  -0.0409 0.0312  343  GLN   B N   
5200  C  CA  . GLN   B 343 ? 2.1050 2.0838 2.0163 0.1900  -0.0386 0.0333  343  GLN   B CA  
5201  C  C   . GLN   B 343 ? 2.0578 2.0408 1.9728 0.1865  -0.0359 0.0337  343  GLN   B C   
5202  O  O   . GLN   B 343 ? 2.0185 2.0157 1.9489 0.1801  -0.0331 0.0357  343  GLN   B O   
5203  C  CB  . GLN   B 343 ? 2.0512 2.0357 1.9718 0.1820  -0.0468 0.0308  343  GLN   B CB  
5204  C  CG  . GLN   B 343 ? 2.0953 2.0775 2.0147 0.1842  -0.0495 0.0307  343  GLN   B CG  
5205  C  CD  . GLN   B 343 ? 2.1254 2.1210 2.0581 0.1831  -0.0440 0.0346  343  GLN   B CD  
5206  O  OE1 . GLN   B 343 ? 2.0994 2.1053 2.0417 0.1815  -0.0375 0.0376  343  GLN   B OE1 
5207  N  NE2 . GLN   B 343 ? 2.1108 2.1060 2.0443 0.1838  -0.0468 0.0345  343  GLN   B NE2 
5208  N  N   . GLY   B 344 ? 2.0454 2.0159 1.9463 0.1907  -0.0368 0.0318  344  GLY   B N   
5209  C  CA  . GLY   B 344 ? 2.0084 1.9809 1.9108 0.1878  -0.0350 0.0317  344  GLY   B CA  
5210  C  C   . GLY   B 344 ? 1.9305 1.8979 1.8297 0.1836  -0.0442 0.0270  344  GLY   B C   
5211  O  O   . GLY   B 344 ? 1.8890 1.8499 1.7806 0.1851  -0.0442 0.0259  344  GLY   B O   
5212  N  N   . SER   B 345 ? 1.9229 1.8926 1.8278 0.1785  -0.0519 0.0243  345  SER   B N   
5213  C  CA  . SER   B 345 ? 1.8329 1.7979 1.7361 0.1744  -0.0610 0.0197  345  SER   B CA  
5214  C  C   . SER   B 345 ? 1.8375 1.7847 1.7219 0.1817  -0.0646 0.0166  345  SER   B C   
5215  O  O   . SER   B 345 ? 1.8436 1.7801 1.7186 0.1856  -0.0700 0.0141  345  SER   B O   
5216  C  CB  . SER   B 345 ? 1.7737 1.7416 1.6839 0.1695  -0.0677 0.0177  345  SER   B CB  
5217  O  OG  . SER   B 345 ? 1.6882 1.6560 1.6024 0.1634  -0.0754 0.0139  345  SER   B OG  
5218  N  N   . TYR   B 346 ? 1.7170 1.6603 1.5953 0.1839  -0.0620 0.0167  346  TYR   B N   
5219  C  CA  . TYR   B 346 ? 1.6696 1.5964 1.5312 0.1895  -0.0675 0.0129  346  TYR   B CA  
5220  C  C   . TYR   B 346 ? 1.5837 1.5079 1.4481 0.1846  -0.0787 0.0078  346  TYR   B C   
5221  O  O   . TYR   B 346 ? 1.5630 1.4728 1.4142 0.1893  -0.0852 0.0039  346  TYR   B O   
5222  C  CB  . TYR   B 346 ? 1.7166 1.6409 1.5733 0.1908  -0.0642 0.0133  346  TYR   B CB  
5223  C  CG  . TYR   B 346 ? 1.8395 1.7701 1.6987 0.1926  -0.0528 0.0185  346  TYR   B CG  
5224  C  CD1 . TYR   B 346 ? 1.8026 1.7505 1.6800 0.1848  -0.0482 0.0214  346  TYR   B CD1 
5225  C  CD2 . TYR   B 346 ? 1.9427 1.8617 1.7860 0.2019  -0.0465 0.0204  346  TYR   B CD2 
5226  C  CE1 . TYR   B 346 ? 1.8024 1.7565 1.6835 0.1860  -0.0380 0.0260  346  TYR   B CE1 
5227  C  CE2 . TYR   B 346 ? 1.9889 1.9137 1.8354 0.2032  -0.0356 0.0252  346  TYR   B CE2 
5228  C  CZ  . TYR   B 346 ? 1.8998 1.8425 1.7659 0.1951  -0.0315 0.0280  346  TYR   B CZ  
5229  O  OH  . TYR   B 346 ? 1.8421 1.7909 1.7127 0.1961  -0.0208 0.0327  346  TYR   B OH  
5230  N  N   . VAL   B 347 ? 1.5811 1.5186 1.4625 0.1753  -0.0810 0.0076  347  VAL   B N   
5231  C  CA  . VAL   B 347 ? 1.5369 1.4724 1.4222 0.1706  -0.0908 0.0031  347  VAL   B CA  
5232  C  C   . VAL   B 347 ? 1.5213 1.4492 1.4007 0.1740  -0.0945 0.0020  347  VAL   B C   
5233  O  O   . VAL   B 347 ? 1.5324 1.4648 1.4144 0.1753  -0.0896 0.0052  347  VAL   B O   
5234  C  CB  . VAL   B 347 ? 1.5001 1.4514 1.4045 0.1600  -0.0913 0.0036  347  VAL   B CB  
5235  C  CG1 . VAL   B 347 ? 1.4170 1.3658 1.3257 0.1551  -0.1009 -0.0012 347  VAL   B CG1 
5236  C  CG2 . VAL   B 347 ? 1.4410 1.4007 1.3514 0.1570  -0.0862 0.0055  347  VAL   B CG2 
5237  N  N   . VAL   B 348 ? 1.4348 1.3511 1.3069 0.1756  -0.1034 -0.0028 348  VAL   B N   
5238  C  CA  . VAL   B 348 ? 1.3649 1.2726 1.2313 0.1784  -0.1083 -0.0046 348  VAL   B CA  
5239  C  C   . VAL   B 348 ? 1.3370 1.2432 1.2098 0.1724  -0.1180 -0.0093 348  VAL   B C   
5240  O  O   . VAL   B 348 ? 1.3562 1.2554 1.2247 0.1731  -0.1236 -0.0130 348  VAL   B O   
5241  C  CB  . VAL   B 348 ? 1.4063 1.2965 1.2519 0.1893  -0.1088 -0.0056 348  VAL   B CB  
5242  C  CG1 . VAL   B 348 ? 1.3885 1.2673 1.2278 0.1913  -0.1173 -0.0094 348  VAL   B CG1 
5243  C  CG2 . VAL   B 348 ? 1.4960 1.3880 1.3368 0.1951  -0.0988 -0.0005 348  VAL   B CG2 
5244  N  N   . ALA   B 349 ? 1.3225 1.2357 1.2066 0.1664  -0.1199 -0.0092 349  ALA   B N   
5245  C  CA  . ALA   B 349 ? 1.2880 1.2010 1.1804 0.1601  -0.1283 -0.0133 349  ALA   B CA  
5246  C  C   . ALA   B 349 ? 1.3018 1.1977 1.1812 0.1656  -0.1367 -0.0181 349  ALA   B C   
5247  O  O   . ALA   B 349 ? 1.3815 1.2666 1.2474 0.1733  -0.1365 -0.0178 349  ALA   B O   
5248  C  CB  . ALA   B 349 ? 1.3657 1.2875 1.2705 0.1535  -0.1281 -0.0120 349  ALA   B CB  
5249  N  N   . MET   B 350 ? 1.3040 1.1973 1.1875 0.1621  -0.1442 -0.0225 350  MET   B N   
5250  C  CA  . MET   B 350 ? 1.3024 1.1791 1.1732 0.1679  -0.1527 -0.0274 350  MET   B CA  
5251  C  C   . MET   B 350 ? 1.3161 1.1909 1.1962 0.1621  -0.1622 -0.0322 350  MET   B C   
5252  O  O   . MET   B 350 ? 1.3739 1.2349 1.2449 0.1664  -0.1699 -0.0363 350  MET   B O   
5253  C  CB  . MET   B 350 ? 1.3224 1.1934 1.1834 0.1729  -0.1525 -0.0284 350  MET   B CB  
5254  C  CG  . MET   B 350 ? 1.3562 1.2084 1.1998 0.1812  -0.1599 -0.0327 350  MET   B CG  
5255  S  SD  . MET   B 350 ? 1.5338 1.3813 1.3690 0.1852  -0.1602 -0.0341 350  MET   B SD  
5256  C  CE  . MET   B 350 ? 1.3458 1.1973 1.1959 0.1771  -0.1701 -0.0395 350  MET   B CE  
5257  N  N   . GLU   B 351 ? 1.4767 1.3645 1.3745 0.1527  -0.1618 -0.0319 351  GLU   B N   
5258  C  CA  . GLU   B 351 ? 1.4911 1.3786 1.3998 0.1465  -0.1694 -0.0358 351  GLU   B CA  
5259  C  C   . GLU   B 351 ? 1.4587 1.3627 1.3860 0.1366  -0.1652 -0.0334 351  GLU   B C   
5260  O  O   . GLU   B 351 ? 1.4577 1.3711 1.3897 0.1344  -0.1604 -0.0314 351  GLU   B O   
5261  C  CB  . GLU   B 351 ? 1.5102 1.3887 1.4164 0.1480  -0.1784 -0.0414 351  GLU   B CB  
5262  C  CG  . GLU   B 351 ? 1.6101 1.4801 1.5195 0.1463  -0.1879 -0.0461 351  GLU   B CG  
5263  C  CD  . GLU   B 351 ? 1.6812 1.5451 1.5926 0.1461  -0.1971 -0.0518 351  GLU   B CD  
5264  O  OE1 . GLU   B 351 ? 1.6234 1.4859 1.5289 0.1495  -0.1970 -0.0525 351  GLU   B OE1 
5265  O  OE2 . GLU   B 351 ? 1.7672 1.6276 1.6865 0.1424  -0.2045 -0.0557 351  GLU   B OE2 
5266  N  N   . THR   B 352 ? 1.2777 1.1848 1.2147 0.1310  -0.1667 -0.0336 352  THR   B N   
5267  C  CA  . THR   B 352 ? 1.2068 1.1283 1.1604 0.1218  -0.1627 -0.0314 352  THR   B CA  
5268  C  C   . THR   B 352 ? 1.2070 1.1281 1.1725 0.1154  -0.1695 -0.0355 352  THR   B C   
5269  O  O   . THR   B 352 ? 1.2539 1.1648 1.2167 0.1168  -0.1761 -0.0388 352  THR   B O   
5270  C  CB  . THR   B 352 ? 1.1541 1.0806 1.1098 0.1202  -0.1575 -0.0274 352  THR   B CB  
5271  O  OG1 . THR   B 352 ? 1.2134 1.1278 1.1608 0.1243  -0.1622 -0.0292 352  THR   B OG1 
5272  C  CG2 . THR   B 352 ? 1.1485 1.0812 1.0988 0.1238  -0.1490 -0.0224 352  THR   B CG2 
5273  N  N   . PHE   B 353 ? 1.1516 1.0839 1.1308 0.1083  -0.1676 -0.0351 353  PHE   B N   
5274  C  CA  . PHE   B 353 ? 1.1587 1.0926 1.1516 0.1013  -0.1727 -0.0385 353  PHE   B CA  
5275  C  C   . PHE   B 353 ? 1.1093 1.0542 1.1149 0.0935  -0.1674 -0.0353 353  PHE   B C   
5276  O  O   . PHE   B 353 ? 1.1109 1.0654 1.1178 0.0921  -0.1601 -0.0310 353  PHE   B O   
5277  C  CB  . PHE   B 353 ? 1.1153 1.0521 1.1137 0.0998  -0.1755 -0.0413 353  PHE   B CB  
5278  C  CG  . PHE   B 353 ? 1.0931 1.0203 1.0774 0.1080  -0.1789 -0.0434 353  PHE   B CG  
5279  C  CD1 . PHE   B 353 ? 1.1033 1.0169 1.0802 0.1127  -0.1875 -0.0480 353  PHE   B CD1 
5280  C  CD2 . PHE   B 353 ? 1.1629 1.0940 1.1407 0.1112  -0.1735 -0.0408 353  PHE   B CD2 
5281  C  CE1 . PHE   B 353 ? 1.1800 1.0836 1.1425 0.1207  -0.1908 -0.0500 353  PHE   B CE1 
5282  C  CE2 . PHE   B 353 ? 1.1869 1.1083 1.1506 0.1192  -0.1762 -0.0426 353  PHE   B CE2 
5283  C  CZ  . PHE   B 353 ? 1.2199 1.1271 1.1754 0.1241  -0.1849 -0.0472 353  PHE   B CZ  
5284  N  N   . THR   B 354 ? 1.0905 1.0336 1.1053 0.0884  -0.1710 -0.0373 354  THR   B N   
5285  C  CA  . THR   B 354 ? 1.0609 1.0121 1.0855 0.0817  -0.1660 -0.0342 354  THR   B CA  
5286  C  C   . THR   B 354 ? 1.0410 1.0050 1.0779 0.0751  -0.1617 -0.0328 354  THR   B C   
5287  O  O   . THR   B 354 ? 1.0372 1.0027 1.0810 0.0729  -0.1649 -0.0358 354  THR   B O   
5288  C  CB  . THR   B 354 ? 1.0293 0.9744 1.0605 0.0780  -0.1708 -0.0368 354  THR   B CB  
5289  O  OG1 . THR   B 354 ? 1.1638 1.0960 1.1830 0.0845  -0.1758 -0.0387 354  THR   B OG1 
5290  C  CG2 . THR   B 354 ? 1.0089 0.9600 1.0466 0.0724  -0.1653 -0.0331 354  THR   B CG2 
5291  N  N   . ASN   B 355 ? 1.0179 0.9906 1.0572 0.0722  -0.1546 -0.0283 355  ASN   B N   
5292  C  CA  . ASN   B 355 ? 1.0228 1.0070 1.0738 0.0654  -0.1502 -0.0266 355  ASN   B CA  
5293  C  C   . ASN   B 355 ? 1.0260 1.0139 1.0816 0.0608  -0.1459 -0.0234 355  ASN   B C   
5294  O  O   . ASN   B 355 ? 1.0545 1.0446 1.1039 0.0630  -0.1415 -0.0197 355  ASN   B O   
5295  C  CB  . ASN   B 355 ? 1.0090 1.0006 1.0564 0.0676  -0.1456 -0.0242 355  ASN   B CB  
5296  C  CG  . ASN   B 355 ? 1.0289 1.0324 1.0873 0.0608  -0.1407 -0.0222 355  ASN   B CG  
5297  O  OD1 . ASN   B 355 ? 0.9901 0.9962 1.0592 0.0545  -0.1409 -0.0230 355  ASN   B OD1 
5298  N  ND2 . ASN   B 355 ? 1.0248 1.0350 1.0803 0.0623  -0.1360 -0.0195 355  ASN   B ND2 
5299  N  N   . LEU   B 356 ? 1.0204 1.0083 1.0868 0.0546  -0.1473 -0.0249 356  LEU   B N   
5300  C  CA  . LEU   B 356 ? 0.9676 0.9585 1.0391 0.0495  -0.1431 -0.0221 356  LEU   B CA  
5301  C  C   . LEU   B 356 ? 1.0391 1.0414 1.1166 0.0450  -0.1367 -0.0189 356  LEU   B C   
5302  O  O   . LEU   B 356 ? 1.0169 1.0217 1.0971 0.0412  -0.1328 -0.0161 356  LEU   B O   
5303  C  CB  . LEU   B 356 ? 0.9677 0.9543 1.0492 0.0443  -0.1463 -0.0248 356  LEU   B CB  
5304  C  CG  . LEU   B 356 ? 0.9794 0.9546 1.0577 0.0476  -0.1536 -0.0288 356  LEU   B CG  
5305  C  CD1 . LEU   B 356 ? 0.9805 0.9532 1.0708 0.0414  -0.1555 -0.0309 356  LEU   B CD1 
5306  C  CD2 . LEU   B 356 ? 1.0350 1.0029 1.1008 0.0530  -0.1539 -0.0272 356  LEU   B CD2 
5307  N  N   . GLY   B 357 ? 1.0627 1.0711 1.1418 0.0453  -0.1359 -0.0193 357  GLY   B N   
5308  C  CA  . GLY   B 357 ? 1.0305 1.0494 1.1151 0.0412  -0.1303 -0.0166 357  GLY   B CA  
5309  C  C   . GLY   B 357 ? 0.9791 1.0031 1.0561 0.0447  -0.1259 -0.0128 357  GLY   B C   
5310  O  O   . GLY   B 357 ? 0.9484 0.9690 1.0160 0.0509  -0.1270 -0.0127 357  GLY   B O   
5311  N  N   . PRO   B 358 ? 1.0765 1.1086 1.1575 0.0407  -0.1207 -0.0097 358  PRO   B N   
5312  C  CA  . PRO   B 358 ? 1.0890 1.1244 1.1795 0.0337  -0.1185 -0.0092 358  PRO   B CA  
5313  C  C   . PRO   B 358 ? 1.0957 1.1255 1.1854 0.0322  -0.1183 -0.0082 358  PRO   B C   
5314  O  O   . PRO   B 358 ? 1.1134 1.1394 1.1949 0.0362  -0.1184 -0.0066 358  PRO   B O   
5315  C  CB  . PRO   B 358 ? 1.0881 1.1330 1.1795 0.0318  -0.1132 -0.0059 358  PRO   B CB  
5316  C  CG  . PRO   B 358 ? 1.1059 1.1510 1.1879 0.0376  -0.1121 -0.0035 358  PRO   B CG  
5317  C  CD  . PRO   B 358 ? 1.0875 1.1262 1.1640 0.0430  -0.1165 -0.0063 358  PRO   B CD  
5318  N  N   . ILE   B 359 ? 1.0037 1.0325 1.1017 0.0265  -0.1178 -0.0090 359  ILE   B N   
5319  C  CA  . ILE   B 359 ? 0.9753 0.9983 1.0729 0.0247  -0.1172 -0.0080 359  ILE   B CA  
5320  C  C   . ILE   B 359 ? 1.0048 1.0331 1.1046 0.0203  -0.1115 -0.0045 359  ILE   B C   
5321  O  O   . ILE   B 359 ? 0.9711 1.0023 1.0795 0.0150  -0.1093 -0.0049 359  ILE   B O   
5322  C  CB  . ILE   B 359 ? 0.9348 0.9516 1.0402 0.0215  -0.1207 -0.0114 359  ILE   B CB  
5323  C  CG1 . ILE   B 359 ? 0.9644 0.9746 1.0659 0.0265  -0.1271 -0.0149 359  ILE   B CG1 
5324  C  CG2 . ILE   B 359 ? 0.9542 0.9654 1.0593 0.0191  -0.1190 -0.0098 359  ILE   B CG2 
5325  C  CD1 . ILE   B 359 ? 0.9488 0.9511 1.0564 0.0243  -0.1314 -0.0182 359  ILE   B CD1 
5326  N  N   . VAL   B 360 ? 0.9875 1.0167 1.0796 0.0230  -0.1092 -0.0012 360  VAL   B N   
5327  C  CA  . VAL   B 360 ? 0.9360 0.9698 1.0283 0.0198  -0.1043 0.0021  360  VAL   B CA  
5328  C  C   . VAL   B 360 ? 0.9901 1.0176 1.0821 0.0169  -0.1027 0.0035  360  VAL   B C   
5329  O  O   . VAL   B 360 ? 1.0148 1.0446 1.1096 0.0126  -0.0987 0.0053  360  VAL   B O   
5330  C  CB  . VAL   B 360 ? 0.9185 0.9571 1.0035 0.0240  -0.1029 0.0049  360  VAL   B CB  
5331  C  CG1 . VAL   B 360 ? 0.9554 1.0014 1.0424 0.0252  -0.1028 0.0042  360  VAL   B CG1 
5332  C  CG2 . VAL   B 360 ? 0.9256 0.9586 1.0024 0.0298  -0.1055 0.0051  360  VAL   B CG2 
5333  N  N   . ASP   B 361 ? 0.9610 0.9801 1.0487 0.0193  -0.1054 0.0028  361  ASP   B N   
5334  C  CA  . ASP   B 361 ? 0.9491 0.9610 1.0369 0.0164  -0.1041 0.0037  361  ASP   B CA  
5335  C  C   . ASP   B 361 ? 1.0163 1.0193 1.1037 0.0182  -0.1087 0.0010  361  ASP   B C   
5336  O  O   . ASP   B 361 ? 1.0227 1.0245 1.1064 0.0229  -0.1127 -0.0009 361  ASP   B O   
5337  C  CB  . ASP   B 361 ? 0.9753 0.9858 1.0546 0.0181  -0.1015 0.0075  361  ASP   B CB  
5338  C  CG  . ASP   B 361 ? 1.0090 1.0129 1.0888 0.0140  -0.0987 0.0090  361  ASP   B CG  
5339  O  OD1 . ASP   B 361 ? 1.0479 1.0494 1.1358 0.0093  -0.0980 0.0072  361  ASP   B OD1 
5340  O  OD2 . ASP   B 361 ? 0.9560 0.9566 1.0281 0.0155  -0.0971 0.0118  361  ASP   B OD2 
5341  N  N   . MET   B 362 ? 1.0715 1.0677 1.1624 0.0144  -0.1080 0.0007  362  MET   B N   
5342  C  CA  . MET   B 362 ? 1.0753 1.0621 1.1660 0.0156  -0.1124 -0.0018 362  MET   B CA  
5343  C  C   . MET   B 362 ? 1.0633 1.0423 1.1533 0.0125  -0.1099 -0.0001 362  MET   B C   
5344  O  O   . MET   B 362 ? 1.0735 1.0542 1.1636 0.0093  -0.1048 0.0028  362  MET   B O   
5345  C  CB  . MET   B 362 ? 1.0993 1.0861 1.2001 0.0135  -0.1161 -0.0061 362  MET   B CB  
5346  C  CG  . MET   B 362 ? 1.1291 1.1172 1.2425 0.0063  -0.1131 -0.0068 362  MET   B CG  
5347  S  SD  . MET   B 362 ? 1.0740 1.0635 1.2014 0.0036  -0.1176 -0.0120 362  MET   B SD  
5348  C  CE  . MET   B 362 ? 1.0574 1.0510 1.1778 0.0103  -0.1223 -0.0137 362  MET   B CE  
5349  N  N   . CYS   B 363 ? 1.0876 1.0572 1.1759 0.0139  -0.1137 -0.0018 363  CYS   B N   
5350  C  CA  . CYS   B 363 ? 1.1050 1.0656 1.1926 0.0113  -0.1120 -0.0006 363  CYS   B CA  
5351  C  C   . CYS   B 363 ? 1.1185 1.0705 1.2095 0.0116  -0.1174 -0.0043 363  CYS   B C   
5352  O  O   . CYS   B 363 ? 1.1480 1.0997 1.2368 0.0159  -0.1227 -0.0070 363  CYS   B O   
5353  C  CB  . CYS   B 363 ? 1.1544 1.1116 1.2293 0.0152  -0.1103 0.0029  363  CYS   B CB  
5354  S  SG  . CYS   B 363 ? 1.2470 1.1994 1.3108 0.0236  -0.1162 0.0018  363  CYS   B SG  
5355  N  N   . VAL   B 364 ? 1.0450 0.9897 1.1414 0.0070  -0.1160 -0.0044 364  VAL   B N   
5356  C  CA  . VAL   B 364 ? 1.1458 1.0819 1.2472 0.0063  -0.1212 -0.0081 364  VAL   B CA  
5357  C  C   . VAL   B 364 ? 1.2111 1.1363 1.3035 0.0083  -0.1215 -0.0065 364  VAL   B C   
5358  O  O   . VAL   B 364 ? 1.2876 1.2100 1.3775 0.0057  -0.1163 -0.0031 364  VAL   B O   
5359  C  CB  . VAL   B 364 ? 1.1772 1.1133 1.2945 -0.0009 -0.1197 -0.0099 364  VAL   B CB  
5360  C  CG1 . VAL   B 364 ? 1.2224 1.1500 1.3456 -0.0013 -0.1260 -0.0141 364  VAL   B CG1 
5361  C  CG2 . VAL   B 364 ? 1.2109 1.1581 1.3377 -0.0033 -0.1184 -0.0111 364  VAL   B CG2 
5362  N  N   . VAL   B 365 ? 1.2537 1.1719 1.3403 0.0130  -0.1277 -0.0089 365  VAL   B N   
5363  C  CA  . VAL   B 365 ? 1.3143 1.2224 1.3900 0.0161  -0.1284 -0.0073 365  VAL   B CA  
5364  C  C   . VAL   B 365 ? 1.4573 1.3554 1.5343 0.0175  -0.1352 -0.0113 365  VAL   B C   
5365  O  O   . VAL   B 365 ? 1.4938 1.3930 1.5714 0.0207  -0.1409 -0.0148 365  VAL   B O   
5366  C  CB  . VAL   B 365 ? 1.3025 1.2132 1.3639 0.0232  -0.1282 -0.0048 365  VAL   B CB  
5367  C  CG1 . VAL   B 365 ? 1.3725 1.2728 1.4232 0.0265  -0.1289 -0.0032 365  VAL   B CG1 
5368  C  CG2 . VAL   B 365 ? 1.2737 1.1946 1.3340 0.0222  -0.1222 -0.0011 365  VAL   B CG2 
5369  N  N   . ASP   B 366 ? 1.7144 1.6022 1.7914 0.0151  -0.1348 -0.0109 366  ASP   B N   
5370  C  CA  . ASP   B 366 ? 1.7426 1.6196 1.8199 0.0164  -0.1414 -0.0145 366  ASP   B CA  
5371  C  C   . ASP   B 366 ? 1.7642 1.6333 1.8251 0.0234  -0.1437 -0.0132 366  ASP   B C   
5372  O  O   . ASP   B 366 ? 1.7943 1.6546 1.8501 0.0230  -0.1421 -0.0113 366  ASP   B O   
5373  C  CB  . ASP   B 366 ? 1.7897 1.6597 1.8780 0.0094  -0.1398 -0.0151 366  ASP   B CB  
5374  C  CG  . ASP   B 366 ? 1.8691 1.7279 1.9592 0.0102  -0.1471 -0.0192 366  ASP   B CG  
5375  O  OD1 . ASP   B 366 ? 1.8702 1.7295 1.9598 0.0141  -0.1540 -0.0231 366  ASP   B OD1 
5376  O  OD2 . ASP   B 366 ? 1.9078 1.7570 1.9995 0.0071  -0.1460 -0.0186 366  ASP   B OD2 
5377  N  N   . LEU   B 367 ? 1.6075 1.4796 1.6601 0.0302  -0.1474 -0.0143 367  LEU   B N   
5378  C  CA  . LEU   B 367 ? 1.5976 1.4643 1.6346 0.0376  -0.1487 -0.0127 367  LEU   B CA  
5379  C  C   . LEU   B 367 ? 1.6364 1.4892 1.6688 0.0400  -0.1548 -0.0155 367  LEU   B C   
5380  O  O   . LEU   B 367 ? 1.6693 1.5142 1.6912 0.0433  -0.1544 -0.0136 367  LEU   B O   
5381  C  CB  . LEU   B 367 ? 1.6000 1.4742 1.6300 0.0440  -0.1500 -0.0128 367  LEU   B CB  
5382  C  CG  . LEU   B 367 ? 1.5168 1.4039 1.5471 0.0436  -0.1441 -0.0094 367  LEU   B CG  
5383  C  CD1 . LEU   B 367 ? 1.5100 1.4030 1.5347 0.0499  -0.1462 -0.0102 367  LEU   B CD1 
5384  C  CD2 . LEU   B 367 ? 1.4836 1.3697 1.5059 0.0447  -0.1394 -0.0048 367  LEU   B CD2 
5385  N  N   . GLU   B 368 ? 1.5986 1.4480 1.6382 0.0390  -0.1608 -0.0203 368  GLU   B N   
5386  C  CA  . GLU   B 368 ? 1.5781 1.4138 1.6137 0.0414  -0.1673 -0.0234 368  GLU   B CA  
5387  C  C   . GLU   B 368 ? 1.6526 1.4805 1.6962 0.0347  -0.1660 -0.0233 368  GLU   B C   
5388  O  O   . GLU   B 368 ? 1.6445 1.4609 1.6880 0.0351  -0.1716 -0.0263 368  GLU   B O   
5389  C  CB  . GLU   B 368 ? 1.6209 1.4552 1.6601 0.0435  -0.1750 -0.0287 368  GLU   B CB  
5390  C  CG  . GLU   B 368 ? 1.6550 1.4963 1.6859 0.0503  -0.1762 -0.0289 368  GLU   B CG  
5391  C  CD  . GLU   B 368 ? 1.6943 1.5346 1.7293 0.0519  -0.1836 -0.0342 368  GLU   B CD  
5392  O  OE1 . GLU   B 368 ? 1.7363 1.5650 1.7684 0.0544  -0.1908 -0.0380 368  GLU   B OE1 
5393  O  OE2 . GLU   B 368 ? 1.6052 1.4558 1.6460 0.0510  -0.1825 -0.0347 368  GLU   B OE2 
5394  N  N   . ARG   B 369 ? 1.6773 1.5106 1.7273 0.0289  -0.1586 -0.0197 369  ARG   B N   
5395  C  CA  . ARG   B 369 ? 1.6552 1.4814 1.7121 0.0224  -0.1555 -0.0187 369  ARG   B CA  
5396  C  C   . ARG   B 369 ? 1.7056 1.5253 1.7752 0.0183  -0.1612 -0.0235 369  ARG   B C   
5397  O  O   . ARG   B 369 ? 1.7126 1.5206 1.7827 0.0166  -0.1631 -0.0244 369  ARG   B O   
5398  C  CB  . ARG   B 369 ? 1.5709 1.3870 1.6141 0.0257  -0.1539 -0.0156 369  ARG   B CB  
5399  C  CG  . ARG   B 369 ? 1.6571 1.4791 1.6936 0.0259  -0.1462 -0.0103 369  ARG   B CG  
5400  C  CD  . ARG   B 369 ? 1.8005 1.6251 1.8480 0.0176  -0.1390 -0.0078 369  ARG   B CD  
5401  N  NE  . ARG   B 369 ? 1.8085 1.6430 1.8712 0.0124  -0.1381 -0.0098 369  ARG   B NE  
5402  C  CZ  . ARG   B 369 ? 1.7930 1.6297 1.8677 0.0049  -0.1327 -0.0087 369  ARG   B CZ  
5403  N  NH1 . ARG   B 369 ? 1.8297 1.6596 1.9025 0.0016  -0.1270 -0.0053 369  ARG   B NH1 
5404  N  NH2 . ARG   B 369 ? 1.7291 1.5747 1.8178 0.0009  -0.1328 -0.0110 369  ARG   B NH2 
5405  N  N   . GLN   B 370 ? 1.7009 1.5283 1.7810 0.0168  -0.1643 -0.0268 370  GLN   B N   
5406  C  CA  . GLN   B 370 ? 1.7034 1.5264 1.7967 0.0136  -0.1708 -0.0320 370  GLN   B CA  
5407  C  C   . GLN   B 370 ? 1.7024 1.5332 1.8151 0.0051  -0.1669 -0.0324 370  GLN   B C   
5408  O  O   . GLN   B 370 ? 1.7203 1.5516 1.8459 0.0027  -0.1723 -0.0370 370  GLN   B O   
5409  C  CB  . GLN   B 370 ? 1.7408 1.5647 1.8298 0.0198  -0.1791 -0.0364 370  GLN   B CB  
5410  C  CG  . GLN   B 370 ? 1.7595 1.5973 1.8487 0.0216  -0.1769 -0.0356 370  GLN   B CG  
5411  C  CD  . GLN   B 370 ? 1.8168 1.6549 1.9039 0.0269  -0.1852 -0.0404 370  GLN   B CD  
5412  O  OE1 . GLN   B 370 ? 1.8354 1.6627 1.9159 0.0312  -0.1927 -0.0437 370  GLN   B OE1 
5413  N  NE2 . GLN   B 370 ? 1.7727 1.6223 1.8645 0.0266  -0.1839 -0.0407 370  GLN   B NE2 
5414  N  N   . GLY   B 371 ? 1.6956 1.5321 1.8106 0.0009  -0.1577 -0.0279 371  GLY   B N   
5415  C  CA  . GLY   B 371 ? 1.6925 1.5359 1.8257 -0.0070 -0.1532 -0.0280 371  GLY   B CA  
5416  C  C   . GLY   B 371 ? 1.6778 1.5317 1.8208 -0.0070 -0.1567 -0.0314 371  GLY   B C   
5417  O  O   . GLY   B 371 ? 1.6715 1.5273 1.8319 -0.0125 -0.1583 -0.0345 371  GLY   B O   
5418  N  N   . GLN   B 372 ? 1.6234 1.4838 1.7556 -0.0010 -0.1582 -0.0310 372  GLN   B N   
5419  C  CA  . GLN   B 372 ? 1.6019 1.4719 1.7410 -0.0002 -0.1615 -0.0341 372  GLN   B CA  
5420  C  C   . GLN   B 372 ? 1.5595 1.4417 1.6952 0.0001  -0.1547 -0.0303 372  GLN   B C   
5421  O  O   . GLN   B 372 ? 1.5559 1.4461 1.7041 -0.0054 -0.1501 -0.0297 372  GLN   B O   
5422  C  CB  . GLN   B 372 ? 1.6219 1.4872 1.7513 0.0073  -0.1708 -0.0379 372  GLN   B CB  
5423  C  CG  . GLN   B 372 ? 1.5883 1.4607 1.7248 0.0085  -0.1759 -0.0419 372  GLN   B CG  
5424  C  CD  . GLN   B 372 ? 1.6238 1.4949 1.7796 0.0028  -0.1804 -0.0466 372  GLN   B CD  
5425  O  OE1 . GLN   B 372 ? 1.6568 1.5240 1.8234 -0.0034 -0.1779 -0.0462 372  GLN   B OE1 
5426  N  NE2 . GLN   B 372 ? 1.6475 1.5219 1.8081 0.0049  -0.1870 -0.0510 372  GLN   B NE2 
5427  N  N   . GLY   B 373 ? 1.5415 1.4253 1.6612 0.0064  -0.1537 -0.0277 373  GLY   B N   
5428  C  CA  . GLY   B 373 ? 1.4543 1.3495 1.5710 0.0067  -0.1477 -0.0242 373  GLY   B CA  
5429  C  C   . GLY   B 373 ? 1.4004 1.3023 1.5123 0.0121  -0.1515 -0.0261 373  GLY   B C   
5430  O  O   . GLY   B 373 ? 1.3893 1.2945 1.5108 0.0110  -0.1557 -0.0299 373  GLY   B O   
5431  N  N   . GLN   B 374 ? 1.3417 1.2451 1.4389 0.0182  -0.1505 -0.0235 374  GLN   B N   
5432  C  CA  . GLN   B 374 ? 1.2380 1.1484 1.3296 0.0233  -0.1524 -0.0242 374  GLN   B CA  
5433  C  C   . GLN   B 374 ? 1.2764 1.1989 1.3706 0.0208  -0.1453 -0.0207 374  GLN   B C   
5434  O  O   . GLN   B 374 ? 1.2607 1.1856 1.3616 0.0150  -0.1396 -0.0183 374  GLN   B O   
5435  C  CB  . GLN   B 374 ? 1.2158 1.1206 1.2908 0.0315  -0.1551 -0.0235 374  GLN   B CB  
5436  C  CG  . GLN   B 374 ? 1.4024 1.2936 1.4732 0.0333  -0.1602 -0.0256 374  GLN   B CG  
5437  C  CD  . GLN   B 374 ? 1.4737 1.3586 1.5283 0.0421  -0.1638 -0.0257 374  GLN   B CD  
5438  O  OE1 . GLN   B 374 ? 1.4431 1.3260 1.4939 0.0468  -0.1694 -0.0290 374  GLN   B OE1 
5439  N  NE2 . GLN   B 374 ? 1.4626 1.3437 1.5072 0.0445  -0.1607 -0.0222 374  GLN   B NE2 
5440  N  N   . LEU   B 375 ? 1.2342 1.1640 1.3229 0.0251  -0.1455 -0.0204 375  LEU   B N   
5441  C  CA  . LEU   B 375 ? 1.1562 1.0975 1.2474 0.0230  -0.1396 -0.0175 375  LEU   B CA  
5442  C  C   . LEU   B 375 ? 1.1349 1.0802 1.2138 0.0297  -0.1391 -0.0156 375  LEU   B C   
5443  O  O   . LEU   B 375 ? 1.1491 1.0935 1.2237 0.0346  -0.1437 -0.0180 375  LEU   B O   
5444  C  CB  . LEU   B 375 ? 1.1656 1.1137 1.2697 0.0192  -0.1407 -0.0204 375  LEU   B CB  
5445  C  CG  . LEU   B 375 ? 1.1908 1.1506 1.3002 0.0159  -0.1349 -0.0182 375  LEU   B CG  
5446  C  CD1 . LEU   B 375 ? 1.1961 1.1570 1.3098 0.0101  -0.1282 -0.0148 375  LEU   B CD1 
5447  C  CD2 . LEU   B 375 ? 1.1310 1.0963 1.2518 0.0136  -0.1375 -0.0217 375  LEU   B CD2 
5448  N  N   . VAL   B 376 ? 1.0770 1.0261 1.1499 0.0301  -0.1337 -0.0112 376  VAL   B N   
5449  C  CA  . VAL   B 376 ? 1.0787 1.0335 1.1424 0.0358  -0.1324 -0.0091 376  VAL   B CA  
5450  C  C   . VAL   B 376 ? 1.1016 1.0680 1.1709 0.0327  -0.1280 -0.0075 376  VAL   B C   
5451  O  O   . VAL   B 376 ? 1.1215 1.0911 1.1973 0.0271  -0.1238 -0.0058 376  VAL   B O   
5452  C  CB  . VAL   B 376 ? 1.0495 1.0010 1.1024 0.0392  -0.1301 -0.0055 376  VAL   B CB  
5453  C  CG1 . VAL   B 376 ? 1.0011 0.9579 1.0453 0.0459  -0.1297 -0.0040 376  VAL   B CG1 
5454  C  CG2 . VAL   B 376 ? 1.0753 1.0145 1.1237 0.0409  -0.1336 -0.0068 376  VAL   B CG2 
5455  N  N   . THR   B 377 ? 1.1092 1.0817 1.1758 0.0365  -0.1288 -0.0079 377  THR   B N   
5456  C  CA  . THR   B 377 ? 1.0745 1.0580 1.1463 0.0340  -0.1252 -0.0067 377  THR   B CA  
5457  C  C   . THR   B 377 ? 1.0420 1.0311 1.1054 0.0390  -0.1228 -0.0038 377  THR   B C   
5458  O  O   . THR   B 377 ? 1.0261 1.0124 1.0817 0.0451  -0.1253 -0.0044 377  THR   B O   
5459  C  CB  . THR   B 377 ? 1.0307 1.0170 1.1097 0.0330  -0.1283 -0.0105 377  THR   B CB  
5460  O  OG1 . THR   B 377 ? 0.9818 0.9641 1.0537 0.0394  -0.1330 -0.0127 377  THR   B OG1 
5461  C  CG2 . THR   B 377 ? 1.0137 0.9960 1.1036 0.0276  -0.1304 -0.0134 377  THR   B CG2 
5462  N  N   . CYS   B 378 ? 1.0496 1.0464 1.1148 0.0363  -0.1179 -0.0007 378  CYS   B N   
5463  C  CA  . CYS   B 378 ? 1.0405 1.0453 1.1019 0.0397  -0.1157 0.0013  378  CYS   B CA  
5464  C  C   . CYS   B 378 ? 1.0273 1.0368 1.0932 0.0396  -0.1171 -0.0011 378  CYS   B C   
5465  O  O   . CYS   B 378 ? 1.0185 1.0326 1.0929 0.0345  -0.1159 -0.0019 378  CYS   B O   
5466  C  CB  . CYS   B 378 ? 0.9809 0.9926 1.0439 0.0365  -0.1108 0.0048  378  CYS   B CB  
5467  S  SG  . CYS   B 378 ? 1.0442 1.0497 1.1025 0.0356  -0.1092 0.0075  378  CYS   B SG  
5468  N  N   . SER   B 379 ? 1.0151 1.0232 1.0750 0.0454  -0.1196 -0.0022 379  SER   B N   
5469  C  CA  . SER   B 379 ? 0.9799 0.9907 1.0424 0.0463  -0.1214 -0.0047 379  SER   B CA  
5470  C  C   . SER   B 379 ? 0.9851 1.0016 1.0420 0.0510  -0.1192 -0.0027 379  SER   B C   
5471  O  O   . SER   B 379 ? 1.0069 1.0224 1.0566 0.0554  -0.1179 -0.0004 379  SER   B O   
5472  C  CB  . SER   B 379 ? 0.9989 1.0005 1.0593 0.0490  -0.1272 -0.0086 379  SER   B CB  
5473  O  OG  . SER   B 379 ? 1.0334 1.0305 1.1011 0.0440  -0.1292 -0.0106 379  SER   B OG  
5474  N  N   . GLY   B 380 ? 0.9759 0.9984 1.0367 0.0499  -0.1184 -0.0035 380  GLY   B N   
5475  C  CA  . GLY   B 380 ? 0.9594 0.9867 1.0155 0.0543  -0.1165 -0.0021 380  GLY   B CA  
5476  C  C   . GLY   B 380 ? 0.9820 1.0185 1.0400 0.0527  -0.1114 0.0017  380  GLY   B C   
5477  O  O   . GLY   B 380 ? 1.0669 1.1065 1.1294 0.0481  -0.1093 0.0033  380  GLY   B O   
5478  N  N   . ALA   B 381 ? 0.9264 0.9670 0.9806 0.0568  -0.1093 0.0032  381  ALA   B N   
5479  C  CA  . ALA   B 381 ? 0.9195 0.9690 0.9755 0.0561  -0.1049 0.0067  381  ALA   B CA  
5480  C  C   . ALA   B 381 ? 0.9225 0.9725 0.9720 0.0626  -0.1033 0.0083  381  ALA   B C   
5481  O  O   . ALA   B 381 ? 0.9343 0.9792 0.9784 0.0672  -0.1050 0.0066  381  ALA   B O   
5482  C  CB  . ALA   B 381 ? 0.9103 0.9676 0.9735 0.0514  -0.1029 0.0066  381  ALA   B CB  
5483  N  N   . PHE   B 382 ? 0.9643 1.0204 1.0144 0.0632  -0.1000 0.0116  382  PHE   B N   
5484  C  CA  . PHE   B 382 ? 0.9504 1.0088 0.9964 0.0690  -0.0975 0.0137  382  PHE   B CA  
5485  C  C   . PHE   B 382 ? 0.9338 0.9827 0.9708 0.0754  -0.0996 0.0126  382  PHE   B C   
5486  O  O   . PHE   B 382 ? 0.9374 0.9795 0.9717 0.0755  -0.1023 0.0116  382  PHE   B O   
5487  C  CB  . PHE   B 382 ? 0.9372 1.0020 0.9860 0.0688  -0.0950 0.0140  382  PHE   B CB  
5488  C  CG  . PHE   B 382 ? 0.9642 1.0364 1.0213 0.0620  -0.0939 0.0142  382  PHE   B CG  
5489  C  CD1 . PHE   B 382 ? 0.9444 1.0220 1.0059 0.0585  -0.0924 0.0163  382  PHE   B CD1 
5490  C  CD2 . PHE   B 382 ? 1.0077 1.0809 1.0677 0.0594  -0.0945 0.0121  382  PHE   B CD2 
5491  C  CE1 . PHE   B 382 ? 0.9745 1.0581 1.0427 0.0526  -0.0914 0.0165  382  PHE   B CE1 
5492  C  CE2 . PHE   B 382 ? 0.9729 1.0527 1.0403 0.0533  -0.0934 0.0123  382  PHE   B CE2 
5493  C  CZ  . PHE   B 382 ? 0.9316 1.0164 1.0029 0.0499  -0.0917 0.0145  382  PHE   B CZ  
5494  N  N   . LYS   B 383 ? 0.9350 0.9830 0.9672 0.0808  -0.0981 0.0128  383  LYS   B N   
5495  C  CA  . LYS   B 383 ? 0.9463 0.9847 0.9687 0.0876  -0.0998 0.0118  383  LYS   B CA  
5496  C  C   . LYS   B 383 ? 0.9988 1.0272 1.0182 0.0868  -0.1053 0.0083  383  LYS   B C   
5497  O  O   . LYS   B 383 ? 1.0231 1.0431 1.0357 0.0907  -0.1075 0.0076  383  LYS   B O   
5498  C  CB  . LYS   B 383 ? 0.9915 1.0294 1.0090 0.0928  -0.0976 0.0120  383  LYS   B CB  
5499  C  CG  . LYS   B 383 ? 1.0626 1.0955 1.0781 0.0925  -0.1006 0.0086  383  LYS   B CG  
5500  C  CD  . LYS   B 383 ? 1.1018 1.1353 1.1129 0.0970  -0.0974 0.0093  383  LYS   B CD  
5501  C  CE  . LYS   B 383 ? 1.1791 1.2072 1.1807 0.1050  -0.0951 0.0109  383  LYS   B CE  
5502  N  NZ  . LYS   B 383 ? 1.2318 1.2545 1.2255 0.1102  -0.0943 0.0099  383  LYS   B NZ  
5503  N  N   . GLU   B 384 ? 0.9679 0.9972 0.9931 0.0814  -0.1076 0.0059  384  GLU   B N   
5504  C  CA  . GLU   B 384 ? 0.9641 0.9844 0.9879 0.0804  -0.1129 0.0022  384  GLU   B CA  
5505  C  C   . GLU   B 384 ? 0.9636 0.9823 0.9920 0.0755  -0.1145 0.0021  384  GLU   B C   
5506  O  O   . GLU   B 384 ? 0.9861 0.9985 1.0159 0.0733  -0.1187 -0.0010 384  GLU   B O   
5507  C  CB  . GLU   B 384 ? 0.9757 0.9971 1.0039 0.0775  -0.1148 -0.0005 384  GLU   B CB  
5508  C  CG  . GLU   B 384 ? 0.9849 1.0102 1.0107 0.0805  -0.1121 0.0002  384  GLU   B CG  
5509  C  CD  . GLU   B 384 ? 1.0637 1.0800 1.0784 0.0883  -0.1137 -0.0011 384  GLU   B CD  
5510  O  OE1 . GLU   B 384 ? 1.1397 1.1462 1.1485 0.0912  -0.1179 -0.0032 384  GLU   B OE1 
5511  O  OE2 . GLU   B 384 ? 1.0840 1.1026 1.0953 0.0916  -0.1107 0.0001  384  GLU   B OE2 
5512  N  N   . GLY   B 385 ? 1.0181 1.0422 1.0488 0.0737  -0.1113 0.0052  385  GLY   B N   
5513  C  CA  . GLY   B 385 ? 1.0430 1.0644 1.0764 0.0697  -0.1124 0.0054  385  GLY   B CA  
5514  C  C   . GLY   B 385 ? 1.0846 1.0945 1.1114 0.0730  -0.1164 0.0034  385  GLY   B C   
5515  O  O   . GLY   B 385 ? 1.1017 1.1065 1.1203 0.0795  -0.1173 0.0033  385  GLY   B O   
5516  N  N   . SER   B 386 ? 1.0172 1.0225 1.0477 0.0685  -0.1188 0.0019  386  SER   B N   
5517  C  CA  . SER   B 386 ? 1.0187 1.0125 1.0441 0.0709  -0.1233 -0.0006 386  SER   B CA  
5518  C  C   . SER   B 386 ? 1.0255 1.0159 1.0564 0.0650  -0.1244 -0.0011 386  SER   B C   
5519  O  O   . SER   B 386 ? 1.0563 1.0526 1.0954 0.0589  -0.1222 -0.0005 386  SER   B O   
5520  C  CB  . SER   B 386 ? 1.0422 1.0305 1.0658 0.0732  -0.1277 -0.0045 386  SER   B CB  
5521  O  OG  . SER   B 386 ? 1.0348 1.0275 1.0676 0.0678  -0.1284 -0.0064 386  SER   B OG  
5522  N  N   . LEU   B 387 ? 1.0140 0.9944 1.0399 0.0671  -0.1276 -0.0023 387  LEU   B N   
5523  C  CA  . LEU   B 387 ? 1.0283 1.0030 1.0591 0.0620  -0.1295 -0.0037 387  LEU   B CA  
5524  C  C   . LEU   B 387 ? 1.0477 1.0136 1.0781 0.0633  -0.1354 -0.0081 387  LEU   B C   
5525  O  O   . LEU   B 387 ? 1.0651 1.0231 1.0864 0.0694  -0.1385 -0.0092 387  LEU   B O   
5526  C  CB  . LEU   B 387 ? 0.9948 0.9643 1.0203 0.0630  -0.1284 -0.0014 387  LEU   B CB  
5527  C  CG  . LEU   B 387 ? 1.0047 0.9827 1.0319 0.0609  -0.1232 0.0026  387  LEU   B CG  
5528  C  CD1 . LEU   B 387 ? 0.9943 0.9664 1.0162 0.0619  -0.1226 0.0047  387  LEU   B CD1 
5529  C  CD2 . LEU   B 387 ? 1.0682 1.0523 1.1056 0.0535  -0.1209 0.0027  387  LEU   B CD2 
5530  N  N   . ARG   B 388 ? 1.0627 1.0296 1.1027 0.0579  -0.1371 -0.0107 388  ARG   B N   
5531  C  CA  . ARG   B 388 ? 1.0787 1.0370 1.1202 0.0583  -0.1433 -0.0152 388  ARG   B CA  
5532  C  C   . ARG   B 388 ? 1.1105 1.0624 1.1573 0.0535  -0.1445 -0.0159 388  ARG   B C   
5533  O  O   . ARG   B 388 ? 1.0947 1.0513 1.1494 0.0473  -0.1406 -0.0141 388  ARG   B O   
5534  C  CB  . ARG   B 388 ? 1.0217 0.9849 1.0713 0.0557  -0.1450 -0.0180 388  ARG   B CB  
5535  C  CG  . ARG   B 388 ? 1.0304 1.0015 1.0766 0.0588  -0.1422 -0.0165 388  ARG   B CG  
5536  C  CD  . ARG   B 388 ? 1.0428 1.0081 1.0764 0.0672  -0.1446 -0.0171 388  ARG   B CD  
5537  N  NE  . ARG   B 388 ? 1.0915 1.0645 1.1222 0.0701  -0.1411 -0.0152 388  ARG   B NE  
5538  C  CZ  . ARG   B 388 ? 1.0012 0.9737 1.0293 0.0733  -0.1433 -0.0174 388  ARG   B CZ  
5539  N  NH1 . ARG   B 388 ? 1.0071 0.9715 1.0346 0.0746  -0.1496 -0.0217 388  ARG   B NH1 
5540  N  NH2 . ARG   B 388 ? 1.0421 1.0218 1.0679 0.0754  -0.1392 -0.0151 388  ARG   B NH2 
5541  N  N   . ILE   B 389 ? 1.1468 1.0875 1.1889 0.0564  -0.1498 -0.0185 389  ILE   B N   
5542  C  CA  . ILE   B 389 ? 1.0946 1.0278 1.1416 0.0521  -0.1515 -0.0196 389  ILE   B CA  
5543  C  C   . ILE   B 389 ? 1.1001 1.0279 1.1542 0.0505  -0.1579 -0.0247 389  ILE   B C   
5544  O  O   . ILE   B 389 ? 1.1301 1.0508 1.1774 0.0559  -0.1637 -0.0277 389  ILE   B O   
5545  C  CB  . ILE   B 389 ? 1.0615 0.9851 1.0976 0.0565  -0.1525 -0.0183 389  ILE   B CB  
5546  C  CG1 . ILE   B 389 ? 1.0295 0.9586 1.0588 0.0586  -0.1466 -0.0135 389  ILE   B CG1 
5547  C  CG2 . ILE   B 389 ? 1.1416 1.0571 1.1832 0.0518  -0.1542 -0.0195 389  ILE   B CG2 
5548  C  CD1 . ILE   B 389 ? 1.0305 0.9610 1.0491 0.0664  -0.1466 -0.0126 389  ILE   B CD1 
5549  N  N   . ILE   B 390 ? 1.1033 1.0340 1.1710 0.0431  -0.1571 -0.0257 390  ILE   B N   
5550  C  CA  . ILE   B 390 ? 1.1773 1.1061 1.2553 0.0405  -0.1625 -0.0304 390  ILE   B CA  
5551  C  C   . ILE   B 390 ? 1.2469 1.1672 1.3321 0.0362  -0.1652 -0.0323 390  ILE   B C   
5552  O  O   . ILE   B 390 ? 1.2392 1.1618 1.3324 0.0300  -0.1603 -0.0301 390  ILE   B O   
5553  C  CB  . ILE   B 390 ? 1.1093 1.0495 1.1989 0.0355  -0.1593 -0.0303 390  ILE   B CB  
5554  C  CG1 . ILE   B 390 ? 1.0987 1.0469 1.1806 0.0397  -0.1562 -0.0280 390  ILE   B CG1 
5555  C  CG2 . ILE   B 390 ? 1.0950 1.0339 1.1953 0.0335  -0.1654 -0.0354 390  ILE   B CG2 
5556  C  CD1 . ILE   B 390 ? 1.1158 1.0756 1.2069 0.0349  -0.1513 -0.0266 390  ILE   B CD1 
5557  N  N   . ARG   B 391 ? 1.2498 1.1597 1.3320 0.0395  -0.1728 -0.0363 391  ARG   B N   
5558  C  CA  . ARG   B 391 ? 1.2683 1.1691 1.3577 0.0359  -0.1766 -0.0389 391  ARG   B CA  
5559  C  C   . ARG   B 391 ? 1.3083 1.2063 1.4068 0.0353  -0.1846 -0.0447 391  ARG   B C   
5560  O  O   . ARG   B 391 ? 1.3293 1.2287 1.4232 0.0399  -0.1884 -0.0469 391  ARG   B O   
5561  C  CB  . ARG   B 391 ? 1.3374 1.2264 1.4139 0.0407  -0.1792 -0.0385 391  ARG   B CB  
5562  C  CG  . ARG   B 391 ? 1.4078 1.2899 1.4712 0.0493  -0.1858 -0.0412 391  ARG   B CG  
5563  C  CD  . ARG   B 391 ? 1.4874 1.3553 1.5434 0.0524  -0.1912 -0.0431 391  ARG   B CD  
5564  N  NE  . ARG   B 391 ? 1.5799 1.4428 1.6495 0.0459  -0.1943 -0.0459 391  ARG   B NE  
5565  C  CZ  . ARG   B 391 ? 1.6051 1.4600 1.6792 0.0463  -0.2029 -0.0513 391  ARG   B CZ  
5566  N  NH1 . ARG   B 391 ? 1.6897 1.5399 1.7546 0.0532  -0.2096 -0.0546 391  ARG   B NH1 
5567  N  NH2 . ARG   B 391 ? 1.6522 1.5034 1.7403 0.0398  -0.2050 -0.0534 391  ARG   B NH2 
5568  N  N   . ASN   B 392 ? 1.3649 1.2583 1.4761 0.0298  -0.1872 -0.0472 392  ASN   B N   
5569  C  CA  . ASN   B 392 ? 1.3532 1.2442 1.4752 0.0287  -0.1952 -0.0530 392  ASN   B CA  
5570  C  C   . ASN   B 392 ? 1.4019 1.2799 1.5135 0.0353  -0.2046 -0.0570 392  ASN   B C   
5571  O  O   . ASN   B 392 ? 1.4232 1.2911 1.5345 0.0346  -0.2077 -0.0582 392  ASN   B O   
5572  C  CB  . ASN   B 392 ? 1.3510 1.2426 1.4926 0.0199  -0.1943 -0.0543 392  ASN   B CB  
5573  C  CG  . ASN   B 392 ? 1.3664 1.2709 1.5226 0.0142  -0.1894 -0.0536 392  ASN   B CG  
5574  O  OD1 . ASN   B 392 ? 1.3897 1.2983 1.5519 0.0151  -0.1938 -0.0570 392  ASN   B OD1 
5575  N  ND2 . ASN   B 392 ? 1.3602 1.2703 1.5220 0.0086  -0.1804 -0.0493 392  ASN   B ND2 
5576  N  N   . LEU   B 406 ? 1.4284 1.3282 1.5419 0.0418  -0.2083 -0.0613 710  LEU   B N   
5577  C  CA  . LEU   B 406 ? 1.3754 1.2820 1.4799 0.0427  -0.1991 -0.0554 710  LEU   B CA  
5578  C  C   . LEU   B 406 ? 1.3927 1.2938 1.4769 0.0518  -0.2003 -0.0543 710  LEU   B C   
5579  O  O   . LEU   B 406 ? 1.3898 1.2896 1.4675 0.0571  -0.2044 -0.0567 710  LEU   B O   
5580  C  CB  . LEU   B 406 ? 1.2960 1.2164 1.4087 0.0390  -0.1931 -0.0533 710  LEU   B CB  
5581  C  CG  . LEU   B 406 ? 1.2046 1.1326 1.3362 0.0298  -0.1888 -0.0527 710  LEU   B CG  
5582  C  CD1 . LEU   B 406 ? 1.0629 1.0036 1.1973 0.0275  -0.1814 -0.0494 710  LEU   B CD1 
5583  C  CD2 . LEU   B 406 ? 1.2743 1.1987 1.4088 0.0254  -0.1848 -0.0502 710  LEU   B CD2 
5584  N  N   . HIS   B 407 ? 1.4287 1.3262 1.5029 0.0538  -0.1964 -0.0507 711  HIS   B N   
5585  C  CA  . HIS   B 407 ? 1.4378 1.3306 1.4933 0.0622  -0.1960 -0.0489 711  HIS   B CA  
5586  C  C   . HIS   B 407 ? 1.4163 1.3189 1.4682 0.0615  -0.1865 -0.0430 711  HIS   B C   
5587  O  O   . HIS   B 407 ? 1.3892 1.2965 1.4486 0.0556  -0.1812 -0.0401 711  HIS   B O   
5588  C  CB  . HIS   B 407 ? 1.4796 1.3586 1.5260 0.0658  -0.2005 -0.0501 711  HIS   B CB  
5589  C  CG  . HIS   B 407 ? 1.5581 1.4274 1.6108 0.0648  -0.2099 -0.0559 711  HIS   B CG  
5590  N  ND1 . HIS   B 407 ? 1.6389 1.4961 1.6802 0.0719  -0.2180 -0.0598 711  HIS   B ND1 
5591  C  CD2 . HIS   B 407 ? 1.5787 1.4484 1.6484 0.0575  -0.2125 -0.0586 711  HIS   B CD2 
5592  C  CE1 . HIS   B 407 ? 1.6463 1.4969 1.6974 0.0691  -0.2257 -0.0648 711  HIS   B CE1 
5593  N  NE2 . HIS   B 407 ? 1.5832 1.4416 1.6522 0.0602  -0.2224 -0.0641 711  HIS   B NE2 
5594  N  N   . ILE   B 408 ? 1.4386 1.3443 1.4793 0.0676  -0.1843 -0.0412 712  ILE   B N   
5595  C  CA  . ILE   B 408 ? 1.3705 1.2868 1.4089 0.0672  -0.1758 -0.0360 712  ILE   B CA  
5596  C  C   . ILE   B 408 ? 1.3550 1.2668 1.3773 0.0748  -0.1741 -0.0334 712  ILE   B C   
5597  O  O   . ILE   B 408 ? 1.3749 1.2813 1.3866 0.0818  -0.1774 -0.0351 712  ILE   B O   
5598  C  CB  . ILE   B 408 ? 1.3670 1.2936 1.4096 0.0664  -0.1735 -0.0358 712  ILE   B CB  
5599  C  CG1 . ILE   B 408 ? 1.3771 1.3101 1.4367 0.0584  -0.1735 -0.0374 712  ILE   B CG1 
5600  C  CG2 . ILE   B 408 ? 1.3327 1.2687 1.3706 0.0676  -0.1657 -0.0307 712  ILE   B CG2 
5601  C  CD1 . ILE   B 408 ? 1.4343 1.3615 1.4993 0.0585  -0.1817 -0.0431 712  ILE   B CD1 
5602  N  N   . ARG   B 409 ? 1.2372 1.1509 1.2574 0.0737  -0.1689 -0.0294 713  ARG   B N   
5603  C  CA  . ARG   B 409 ? 1.1805 1.0920 1.1871 0.0806  -0.1662 -0.0264 713  ARG   B CA  
5604  C  C   . ARG   B 409 ? 1.1118 1.0361 1.1197 0.0798  -0.1588 -0.0221 713  ARG   B C   
5605  O  O   . ARG   B 409 ? 1.0980 1.0297 1.1142 0.0738  -0.1545 -0.0196 713  ARG   B O   
5606  C  CB  . ARG   B 409 ? 1.1739 1.0782 1.1768 0.0805  -0.1661 -0.0250 713  ARG   B CB  
5607  C  CG  . ARG   B 409 ? 1.2099 1.1103 1.1985 0.0882  -0.1642 -0.0225 713  ARG   B CG  
5608  C  CD  . ARG   B 409 ? 1.2603 1.1625 1.2488 0.0862  -0.1596 -0.0185 713  ARG   B CD  
5609  N  NE  . ARG   B 409 ? 1.3649 1.2590 1.3405 0.0930  -0.1600 -0.0173 713  ARG   B NE  
5610  C  CZ  . ARG   B 409 ? 1.3804 1.2768 1.3467 0.0998  -0.1570 -0.0149 713  ARG   B CZ  
5611  N  NH1 . ARG   B 409 ? 1.2899 1.1957 1.2575 0.1010  -0.1538 -0.0138 713  ARG   B NH1 
5612  N  NH2 . ARG   B 409 ? 1.4667 1.3557 1.4224 0.1055  -0.1572 -0.0137 713  ARG   B NH2 
5613  N  N   . THR   B 410 ? 1.1534 1.0798 1.1530 0.0859  -0.1575 -0.0212 714  THR   B N   
5614  C  CA  . THR   B 410 ? 1.1115 1.0500 1.1125 0.0856  -0.1508 -0.0174 714  THR   B CA  
5615  C  C   . THR   B 410 ? 1.0908 1.0297 1.0837 0.0899  -0.1466 -0.0134 714  THR   B C   
5616  O  O   . THR   B 410 ? 1.0679 0.9994 1.0494 0.0971  -0.1480 -0.0136 714  THR   B O   
5617  C  CB  . THR   B 410 ? 1.0852 1.0268 1.0828 0.0895  -0.1507 -0.0182 714  THR   B CB  
5618  O  OG1 . THR   B 410 ? 1.1155 1.0594 1.1223 0.0849  -0.1536 -0.0214 714  THR   B OG1 
5619  C  CG2 . THR   B 410 ? 1.0307 0.9837 1.0288 0.0898  -0.1436 -0.0139 714  THR   B CG2 
5620  N  N   . VAL   B 411 ? 1.0599 1.0074 1.0585 0.0856  -0.1416 -0.0099 715  VAL   B N   
5621  C  CA  . VAL   B 411 ? 1.0267 0.9776 1.0197 0.0893  -0.1371 -0.0059 715  VAL   B CA  
5622  C  C   . VAL   B 411 ? 1.0696 1.0328 1.0662 0.0888  -0.1321 -0.0034 715  VAL   B C   
5623  O  O   . VAL   B 411 ? 1.1060 1.0777 1.1118 0.0826  -0.1294 -0.0021 715  VAL   B O   
5624  C  CB  . VAL   B 411 ? 1.0201 0.9707 1.0158 0.0854  -0.1354 -0.0038 715  VAL   B CB  
5625  C  CG1 . VAL   B 411 ? 1.0212 0.9742 1.0104 0.0902  -0.1319 -0.0002 715  VAL   B CG1 
5626  C  CG2 . VAL   B 411 ? 1.0746 1.0137 1.0690 0.0843  -0.1402 -0.0064 715  VAL   B CG2 
5627  N  N   . PRO   B 412 ? 1.0113 0.9757 1.0011 0.0951  -0.1304 -0.0026 716  PRO   B N   
5628  C  CA  . PRO   B 412 ? 1.0149 0.9911 1.0088 0.0945  -0.1253 0.0002  716  PRO   B CA  
5629  C  C   . PRO   B 412 ? 1.0516 1.0348 1.0485 0.0927  -0.1211 0.0040  716  PRO   B C   
5630  O  O   . PRO   B 412 ? 1.0822 1.0604 1.0750 0.0945  -0.1216 0.0050  716  PRO   B O   
5631  C  CB  . PRO   B 412 ? 1.0118 0.9852 0.9962 0.1026  -0.1243 0.0004  716  PRO   B CB  
5632  C  CG  . PRO   B 412 ? 1.0356 0.9984 1.0105 0.1079  -0.1266 0.0000  716  PRO   B CG  
5633  C  CD  . PRO   B 412 ? 1.0822 1.0374 1.0599 0.1035  -0.1320 -0.0031 716  PRO   B CD  
5634  N  N   . LEU   B 413 ? 1.0118 1.0063 1.0159 0.0892  -0.1172 0.0061  717  LEU   B N   
5635  C  CA  . LEU   B 413 ? 0.9793 0.9811 0.9860 0.0882  -0.1134 0.0098  717  LEU   B CA  
5636  C  C   . LEU   B 413 ? 0.9724 0.9844 0.9812 0.0903  -0.1089 0.0124  717  LEU   B C   
5637  O  O   . LEU   B 413 ? 0.9704 0.9874 0.9799 0.0916  -0.1062 0.0153  717  LEU   B O   
5638  C  CB  . LEU   B 413 ? 0.9730 0.9782 0.9876 0.0805  -0.1132 0.0101  717  LEU   B CB  
5639  C  CG  . LEU   B 413 ? 0.9795 0.9756 0.9934 0.0777  -0.1164 0.0085  717  LEU   B CG  
5640  C  CD1 . LEU   B 413 ? 0.9730 0.9723 0.9957 0.0697  -0.1160 0.0080  717  LEU   B CD1 
5641  C  CD2 . LEU   B 413 ? 0.9853 0.9778 0.9938 0.0805  -0.1158 0.0108  717  LEU   B CD2 
5642  N  N   . TYR   B 414 ? 0.9952 1.0100 1.0051 0.0908  -0.1082 0.0113  718  TYR   B N   
5643  C  CA  . TYR   B 414 ? 1.0034 1.0272 1.0153 0.0928  -0.1038 0.0136  718  TYR   B CA  
5644  C  C   . TYR   B 414 ? 1.0058 1.0404 1.0265 0.0877  -0.1009 0.0161  718  TYR   B C   
5645  O  O   . TYR   B 414 ? 1.0231 1.0654 1.0461 0.0895  -0.0972 0.0188  718  TYR   B O   
5646  C  CB  . TYR   B 414 ? 1.0289 1.0504 1.0335 0.1008  -0.1017 0.0154  718  TYR   B CB  
5647  C  CG  . TYR   B 414 ? 1.0285 1.0375 1.0228 0.1062  -0.1050 0.0128  718  TYR   B CG  
5648  C  CD1 . TYR   B 414 ? 1.0712 1.0765 1.0606 0.1097  -0.1053 0.0111  718  TYR   B CD1 
5649  C  CD2 . TYR   B 414 ? 1.0737 1.0741 1.0628 0.1080  -0.1081 0.0121  718  TYR   B CD2 
5650  C  CE1 . TYR   B 414 ? 1.1435 1.1365 1.1228 0.1149  -0.1089 0.0086  718  TYR   B CE1 
5651  C  CE2 . TYR   B 414 ? 1.1527 1.1410 1.1321 0.1129  -0.1116 0.0095  718  TYR   B CE2 
5652  C  CZ  . TYR   B 414 ? 1.1583 1.1428 1.1326 0.1165  -0.1122 0.0077  718  TYR   B CZ  
5653  O  OH  . TYR   B 414 ? 1.1155 1.0872 1.0794 0.1218  -0.1162 0.0050  718  TYR   B OH  
5654  N  N   . GLU   B 415 ? 0.9491 0.9840 0.9748 0.0812  -0.1026 0.0152  719  GLU   B N   
5655  C  CA  . GLU   B 415 ? 0.9423 0.9839 0.9742 0.0762  -0.1009 0.0172  719  GLU   B CA  
5656  C  C   . GLU   B 415 ? 0.9397 0.9793 0.9761 0.0696  -0.1028 0.0153  719  GLU   B C   
5657  O  O   . GLU   B 415 ? 0.9889 1.0200 1.0227 0.0694  -0.1060 0.0129  719  GLU   B O   
5658  C  CB  . GLU   B 415 ? 0.9476 0.9863 0.9757 0.0787  -0.1011 0.0191  719  GLU   B CB  
5659  C  CG  . GLU   B 415 ? 0.9820 1.0280 1.0146 0.0760  -0.0991 0.0219  719  GLU   B CG  
5660  C  CD  . GLU   B 415 ? 1.0632 1.1062 1.0913 0.0800  -0.0994 0.0237  719  GLU   B CD  
5661  O  OE1 . GLU   B 415 ? 1.1494 1.1847 1.1708 0.0848  -0.1009 0.0229  719  GLU   B OE1 
5662  O  OE2 . GLU   B 415 ? 1.0791 1.1270 1.1099 0.0785  -0.0984 0.0259  719  GLU   B OE2 
5663  N  N   . SER   B 416 ? 0.9666 1.0137 1.0098 0.0643  -0.1009 0.0162  720  SER   B N   
5664  C  CA  . SER   B 416 ? 0.9790 1.0250 1.0273 0.0580  -0.1020 0.0143  720  SER   B CA  
5665  C  C   . SER   B 416 ? 0.9326 0.9730 0.9801 0.0552  -0.1030 0.0146  720  SER   B C   
5666  O  O   . SER   B 416 ? 0.9312 0.9746 0.9789 0.0542  -0.1012 0.0171  720  SER   B O   
5667  C  CB  . SER   B 416 ? 0.9626 1.0181 1.0178 0.0535  -0.0994 0.0152  720  SER   B CB  
5668  O  OG  . SER   B 416 ? 0.9145 0.9755 0.9702 0.0562  -0.0979 0.0155  720  SER   B OG  
5669  N  N   . PRO   B 417 ? 1.0131 1.0452 1.0599 0.0540  -0.1057 0.0122  721  PRO   B N   
5670  C  CA  . PRO   B 417 ? 0.9863 1.0133 1.0336 0.0502  -0.1059 0.0126  721  PRO   B CA  
5671  C  C   . PRO   B 417 ? 1.0031 1.0344 1.0580 0.0433  -0.1040 0.0124  721  PRO   B C   
5672  O  O   . PRO   B 417 ? 1.0093 1.0434 1.0695 0.0411  -0.1044 0.0104  721  PRO   B O   
5673  C  CB  . PRO   B 417 ? 0.9940 1.0108 1.0387 0.0515  -0.1096 0.0098  721  PRO   B CB  
5674  C  CG  . PRO   B 417 ? 1.0106 1.0283 1.0572 0.0526  -0.1115 0.0071  721  PRO   B CG  
5675  C  CD  . PRO   B 417 ? 1.0266 1.0533 1.0727 0.0555  -0.1090 0.0088  721  PRO   B CD  
5676  N  N   . ARG   B 418 ? 0.9721 1.0034 1.0271 0.0403  -0.1019 0.0146  722  ARG   B N   
5677  C  CA  . ARG   B 418 ? 0.9301 0.9651 0.9912 0.0342  -0.0995 0.0149  722  ARG   B CA  
5678  C  C   . ARG   B 418 ? 0.9354 0.9629 0.9980 0.0298  -0.0991 0.0143  722  ARG   B C   
5679  O  O   . ARG   B 418 ? 0.9326 0.9607 1.0020 0.0252  -0.0985 0.0127  722  ARG   B O   
5680  C  CB  . ARG   B 418 ? 0.9257 0.9674 0.9858 0.0340  -0.0968 0.0179  722  ARG   B CB  
5681  C  CG  . ARG   B 418 ? 0.9384 0.9887 0.9995 0.0370  -0.0965 0.0183  722  ARG   B CG  
5682  C  CD  . ARG   B 418 ? 0.9860 1.0405 1.0532 0.0346  -0.0963 0.0161  722  ARG   B CD  
5683  N  NE  . ARG   B 418 ? 1.0156 1.0755 1.0879 0.0294  -0.0939 0.0167  722  ARG   B NE  
5684  C  CZ  . ARG   B 418 ? 1.0263 1.0885 1.1045 0.0260  -0.0936 0.0147  722  ARG   B CZ  
5685  N  NH1 . ARG   B 418 ? 1.0100 1.0694 1.0900 0.0269  -0.0959 0.0119  722  ARG   B NH1 
5686  N  NH2 . ARG   B 418 ? 1.0486 1.1157 1.1308 0.0217  -0.0911 0.0155  722  ARG   B NH2 
5687  N  N   . LYS   B 419 ? 0.9433 0.9638 1.0002 0.0311  -0.0993 0.0158  723  LYS   B N   
5688  C  CA  . LYS   B 419 ? 0.9493 0.9621 1.0072 0.0270  -0.0984 0.0156  723  LYS   B CA  
5689  C  C   . LYS   B 419 ? 0.9793 0.9825 1.0312 0.0304  -0.1011 0.0152  723  LYS   B C   
5690  O  O   . LYS   B 419 ? 1.0101 1.0127 1.0552 0.0356  -0.1023 0.0165  723  LYS   B O   
5691  C  CB  . LYS   B 419 ? 0.9493 0.9629 1.0056 0.0241  -0.0947 0.0185  723  LYS   B CB  
5692  C  CG  . LYS   B 419 ? 0.9404 0.9624 1.0025 0.0202  -0.0920 0.0189  723  LYS   B CG  
5693  C  CD  . LYS   B 419 ? 0.9556 0.9771 1.0263 0.0152  -0.0912 0.0164  723  LYS   B CD  
5694  C  CE  . LYS   B 419 ? 0.9704 1.0012 1.0473 0.0128  -0.0897 0.0158  723  LYS   B CE  
5695  N  NZ  . LYS   B 419 ? 1.0155 1.0483 1.0928 0.0090  -0.0856 0.0179  723  LYS   B NZ  
5696  N  N   . ILE   B 420 ? 1.0009 0.9964 1.0558 0.0275  -0.1020 0.0134  724  ILE   B N   
5697  C  CA  . ILE   B 420 ? 1.0263 1.0120 1.0761 0.0303  -0.1049 0.0126  724  ILE   B CA  
5698  C  C   . ILE   B 420 ? 1.0605 1.0376 1.1111 0.0260  -0.1032 0.0132  724  ILE   B C   
5699  O  O   . ILE   B 420 ? 1.0844 1.0620 1.1430 0.0203  -0.1011 0.0123  724  ILE   B O   
5700  C  CB  . ILE   B 420 ? 1.0150 0.9982 1.0670 0.0325  -0.1094 0.0089  724  ILE   B CB  
5701  C  CG1 . ILE   B 420 ? 1.0511 1.0233 1.0968 0.0357  -0.1125 0.0081  724  ILE   B CG1 
5702  C  CG2 . ILE   B 420 ? 0.9724 0.9568 1.0351 0.0269  -0.1095 0.0062  724  ILE   B CG2 
5703  C  CD1 . ILE   B 420 ? 1.0158 0.9851 1.0590 0.0405  -0.1173 0.0052  724  ILE   B CD1 
5704  N  N   . CYS   B 421 ? 1.0672 1.0363 1.1099 0.0286  -0.1038 0.0146  725  CYS   B N   
5705  C  CA  . CYS   B 421 ? 1.0807 1.0400 1.1229 0.0252  -0.1023 0.0152  725  CYS   B CA  
5706  C  C   . CYS   B 421 ? 1.1189 1.0684 1.1539 0.0295  -0.1058 0.0146  725  CYS   B C   
5707  O  O   . CYS   B 421 ? 1.0888 1.0395 1.1177 0.0355  -0.1086 0.0145  725  CYS   B O   
5708  C  CB  . CYS   B 421 ? 1.0736 1.0326 1.1116 0.0234  -0.0978 0.0188  725  CYS   B CB  
5709  S  SG  . CYS   B 421 ? 1.1372 1.0940 1.1625 0.0300  -0.0990 0.0216  725  CYS   B SG  
5710  N  N   . TYR   B 422 ? 1.1233 1.0627 1.1589 0.0265  -0.1055 0.0143  726  TYR   B N   
5711  C  CA  . TYR   B 422 ? 1.1704 1.0995 1.2002 0.0299  -0.1091 0.0132  726  TYR   B CA  
5712  C  C   . TYR   B 422 ? 1.2292 1.1490 1.2517 0.0295  -0.1067 0.0160  726  TYR   B C   
5713  O  O   . TYR   B 422 ? 1.2565 1.1713 1.2828 0.0241  -0.1035 0.0167  726  TYR   B O   
5714  C  CB  . TYR   B 422 ? 1.1565 1.0807 1.1945 0.0270  -0.1123 0.0094  726  TYR   B CB  
5715  C  CG  . TYR   B 422 ? 1.2143 1.1266 1.2466 0.0298  -0.1161 0.0081  726  TYR   B CG  
5716  C  CD1 . TYR   B 422 ? 1.2505 1.1610 1.2746 0.0369  -0.1204 0.0072  726  TYR   B CD1 
5717  C  CD2 . TYR   B 422 ? 1.2518 1.1543 1.2872 0.0255  -0.1153 0.0078  726  TYR   B CD2 
5718  C  CE1 . TYR   B 422 ? 1.2432 1.1422 1.2616 0.0396  -0.1240 0.0059  726  TYR   B CE1 
5719  C  CE2 . TYR   B 422 ? 1.2731 1.1643 1.3034 0.0280  -0.1190 0.0065  726  TYR   B CE2 
5720  C  CZ  . TYR   B 422 ? 1.2518 1.1412 1.2734 0.0351  -0.1235 0.0055  726  TYR   B CZ  
5721  O  OH  . TYR   B 422 ? 1.3155 1.1930 1.3315 0.0376  -0.1273 0.0042  726  TYR   B OH  
5722  N  N   . GLN   B 423 ? 1.2495 1.1666 1.2614 0.0355  -0.1082 0.0176  727  GLN   B N   
5723  C  CA  . GLN   B 423 ? 1.2844 1.1919 1.2876 0.0364  -0.1067 0.0202  727  GLN   B CA  
5724  C  C   . GLN   B 423 ? 1.3329 1.2291 1.3330 0.0383  -0.1104 0.0183  727  GLN   B C   
5725  O  O   . GLN   B 423 ? 1.3202 1.2149 1.3139 0.0444  -0.1142 0.0175  727  GLN   B O   
5726  C  CB  . GLN   B 423 ? 1.3213 1.2326 1.3153 0.0420  -0.1065 0.0230  727  GLN   B CB  
5727  C  CG  . GLN   B 423 ? 1.2613 1.1632 1.2457 0.0434  -0.1052 0.0257  727  GLN   B CG  
5728  C  CD  . GLN   B 423 ? 1.3091 1.2173 1.2883 0.0460  -0.1035 0.0287  727  GLN   B CD  
5729  O  OE1 . GLN   B 423 ? 1.3377 1.2475 1.3105 0.0522  -0.1056 0.0295  727  GLN   B OE1 
5730  N  NE2 . GLN   B 423 ? 1.3417 1.2536 1.3240 0.0415  -0.0996 0.0302  727  GLN   B NE2 
5731  N  N   . GLU   B 424 ? 1.3365 1.2245 1.3414 0.0329  -0.1092 0.0175  728  GLU   B N   
5732  C  CA  . GLU   B 424 ? 1.3195 1.1966 1.3233 0.0338  -0.1131 0.0152  728  GLU   B CA  
5733  C  C   . GLU   B 424 ? 1.3397 1.2074 1.3305 0.0389  -0.1140 0.0172  728  GLU   B C   
5734  O  O   . GLU   B 424 ? 1.3563 1.2186 1.3419 0.0437  -0.1185 0.0156  728  GLU   B O   
5735  C  CB  . GLU   B 424 ? 1.3655 1.2365 1.3787 0.0265  -0.1111 0.0141  728  GLU   B CB  
5736  C  CG  . GLU   B 424 ? 1.4517 1.3140 1.4680 0.0264  -0.1160 0.0106  728  GLU   B CG  
5737  C  CD  . GLU   B 424 ? 1.5497 1.4047 1.5750 0.0192  -0.1135 0.0100  728  GLU   B CD  
5738  O  OE1 . GLU   B 424 ? 1.5671 1.4264 1.5989 0.0139  -0.1080 0.0117  728  GLU   B OE1 
5739  O  OE2 . GLU   B 424 ? 1.7043 1.5490 1.7302 0.0189  -0.1168 0.0080  728  GLU   B OE2 
5740  N  N   . VAL   B 425 ? 1.3310 1.1965 1.3159 0.0382  -0.1098 0.0208  729  VAL   B N   
5741  C  CA  . VAL   B 425 ? 1.3557 1.2122 1.3282 0.0430  -0.1106 0.0229  729  VAL   B CA  
5742  C  C   . VAL   B 425 ? 1.3609 1.2212 1.3266 0.0510  -0.1147 0.0224  729  VAL   B C   
5743  O  O   . VAL   B 425 ? 1.3324 1.1841 1.2908 0.0555  -0.1179 0.0217  729  VAL   B O   
5744  C  CB  . VAL   B 425 ? 1.4349 1.2906 1.4017 0.0418  -0.1057 0.0269  729  VAL   B CB  
5745  C  CG1 . VAL   B 425 ? 1.5084 1.3571 1.4618 0.0480  -0.1070 0.0291  729  VAL   B CG1 
5746  C  CG2 . VAL   B 425 ? 1.4131 1.2615 1.3846 0.0345  -0.1013 0.0276  729  VAL   B CG2 
5747  N  N   . SER   B 426 ? 1.4440 1.3172 1.4124 0.0529  -0.1145 0.0225  730  SER   B N   
5748  C  CA  . SER   B 426 ? 1.4401 1.3183 1.4029 0.0605  -0.1173 0.0225  730  SER   B CA  
5749  C  C   . SER   B 426 ? 1.4129 1.2914 1.3782 0.0631  -0.1215 0.0189  730  SER   B C   
5750  O  O   . SER   B 426 ? 1.4039 1.2847 1.3637 0.0698  -0.1237 0.0188  730  SER   B O   
5751  C  CB  . SER   B 426 ? 1.4349 1.3265 1.3998 0.0614  -0.1151 0.0243  730  SER   B CB  
5752  O  OG  . SER   B 426 ? 1.4652 1.3560 1.4273 0.0591  -0.1116 0.0274  730  SER   B OG  
5753  N  N   . GLN   B 427 ? 1.3610 1.2371 1.3344 0.0581  -0.1226 0.0161  731  GLN   B N   
5754  C  CA  . GLN   B 427 ? 1.3367 1.2131 1.3130 0.0601  -0.1270 0.0124  731  GLN   B CA  
5755  C  C   . GLN   B 427 ? 1.3265 1.2153 1.3037 0.0640  -0.1269 0.0124  731  GLN   B C   
5756  O  O   . GLN   B 427 ? 1.3231 1.2117 1.2945 0.0704  -0.1296 0.0116  731  GLN   B O   
5757  C  CB  . GLN   B 427 ? 1.3357 1.2001 1.3035 0.0652  -0.1313 0.0109  731  GLN   B CB  
5758  N  N   . CYS   B 428 ? 1.3714 1.2707 1.3558 0.0598  -0.1235 0.0135  732  CYS   B N   
5759  C  CA  . CYS   B 428 ? 1.3322 1.2437 1.3188 0.0625  -0.1230 0.0137  732  CYS   B CA  
5760  C  C   . CYS   B 428 ? 1.3093 1.2300 1.3059 0.0561  -0.1199 0.0138  732  CYS   B C   
5761  O  O   . CYS   B 428 ? 1.3178 1.2359 1.3187 0.0501  -0.1175 0.0145  732  CYS   B O   
5762  C  CB  . CYS   B 428 ? 1.3302 1.2459 1.3093 0.0681  -0.1215 0.0168  732  CYS   B CB  
5763  S  SG  . CYS   B 428 ? 1.4561 1.3749 1.4355 0.0641  -0.1170 0.0205  732  CYS   B SG  
5764  N  N   . PHE   B 429 ? 1.2474 1.1787 1.2472 0.0576  -0.1196 0.0135  733  PHE   B N   
5765  C  CA  . PHE   B 429 ? 1.2055 1.1464 1.2143 0.0523  -0.1168 0.0136  733  PHE   B CA  
5766  C  C   . PHE   B 429 ? 1.1822 1.1327 1.1896 0.0536  -0.1136 0.0167  733  PHE   B C   
5767  O  O   . PHE   B 429 ? 1.1486 1.1026 1.1510 0.0594  -0.1142 0.0178  733  PHE   B O   
5768  C  CB  . PHE   B 429 ? 1.1383 1.0838 1.1529 0.0524  -0.1191 0.0105  733  PHE   B CB  
5769  C  CG  . PHE   B 429 ? 1.1565 1.0945 1.1758 0.0493  -0.1221 0.0071  733  PHE   B CG  
5770  C  CD1 . PHE   B 429 ? 1.2200 1.1589 1.2490 0.0421  -0.1204 0.0063  733  PHE   B CD1 
5771  C  CD2 . PHE   B 429 ? 1.1589 1.0888 1.1735 0.0536  -0.1268 0.0046  733  PHE   B CD2 
5772  C  CE1 . PHE   B 429 ? 1.1799 1.1123 1.2149 0.0391  -0.1234 0.0030  733  PHE   B CE1 
5773  C  CE2 . PHE   B 429 ? 1.1697 1.0927 1.1894 0.0508  -0.1303 0.0011  733  PHE   B CE2 
5774  C  CZ  . PHE   B 429 ? 1.1690 1.0934 1.1994 0.0434  -0.1287 0.0003  733  PHE   B CZ  
5775  N  N   . GLY   B 430 ? 1.1384 1.0930 1.1507 0.0482  -0.1102 0.0182  734  GLY   B N   
5776  C  CA  . GLY   B 430 ? 1.1442 1.1090 1.1573 0.0484  -0.1076 0.0204  734  GLY   B CA  
5777  C  C   . GLY   B 430 ? 1.1445 1.1192 1.1658 0.0461  -0.1069 0.0190  734  GLY   B C   
5778  O  O   . GLY   B 430 ? 1.1308 1.1055 1.1591 0.0406  -0.1061 0.0174  734  GLY   B O   
5779  N  N   . VAL   B 431 ? 1.0865 1.0693 1.1073 0.0501  -0.1073 0.0193  735  VAL   B N   
5780  C  CA  . VAL   B 431 ? 1.0013 0.9934 1.0291 0.0482  -0.1065 0.0182  735  VAL   B CA  
5781  C  C   . VAL   B 431 ? 1.0133 1.0152 1.0411 0.0497  -0.1043 0.0207  735  VAL   B C   
5782  O  O   . VAL   B 431 ? 0.9967 0.9992 1.0191 0.0546  -0.1047 0.0225  735  VAL   B O   
5783  C  CB  . VAL   B 431 ? 1.0103 1.0020 1.0383 0.0517  -0.1094 0.0154  735  VAL   B CB  
5784  C  CG1 . VAL   B 431 ? 1.0191 1.0196 1.0543 0.0493  -0.1085 0.0142  735  VAL   B CG1 
5785  C  CG2 . VAL   B 431 ? 1.0637 1.0452 1.0915 0.0507  -0.1124 0.0128  735  VAL   B CG2 
5786  N  N   . LEU   B 432 ? 0.9780 0.9874 1.0121 0.0455  -0.1022 0.0208  736  LEU   B N   
5787  C  CA  . LEU   B 432 ? 0.9548 0.9738 0.9903 0.0461  -0.1004 0.0228  736  LEU   B CA  
5788  C  C   . LEU   B 432 ? 0.9477 0.9741 0.9870 0.0481  -0.1008 0.0215  736  LEU   B C   
5789  O  O   . LEU   B 432 ? 0.9441 0.9715 0.9883 0.0452  -0.1010 0.0193  736  LEU   B O   
5790  C  CB  . LEU   B 432 ? 0.9509 0.9726 0.9901 0.0402  -0.0977 0.0238  736  LEU   B CB  
5791  C  CG  . LEU   B 432 ? 0.9572 0.9728 0.9922 0.0379  -0.0963 0.0257  736  LEU   B CG  
5792  C  CD1 . LEU   B 432 ? 0.9527 0.9713 0.9920 0.0321  -0.0934 0.0261  736  LEU   B CD1 
5793  C  CD2 . LEU   B 432 ? 0.9985 1.0144 1.0270 0.0423  -0.0969 0.0283  736  LEU   B CD2 
5794  N  N   . SER   B 433 ? 0.9683 0.9995 1.0052 0.0532  -0.1008 0.0228  737  SER   B N   
5795  C  CA  . SER   B 433 ? 0.9420 0.9786 0.9809 0.0563  -0.1008 0.0219  737  SER   B CA  
5796  C  C   . SER   B 433 ? 0.9349 0.9819 0.9767 0.0573  -0.0987 0.0239  737  SER   B C   
5797  O  O   . SER   B 433 ? 0.9605 1.0097 1.0012 0.0582  -0.0982 0.0262  737  SER   B O   
5798  C  CB  . SER   B 433 ? 0.9493 0.9802 0.9820 0.0626  -0.1027 0.0212  737  SER   B CB  
5799  O  OG  . SER   B 433 ? 0.9683 1.0029 0.9984 0.0675  -0.1018 0.0236  737  SER   B OG  
5800  N  N   . SER   B 434 ? 0.9289 0.9818 0.9745 0.0577  -0.0979 0.0231  738  SER   B N   
5801  C  CA  . SER   B 434 ? 0.9211 0.9843 0.9713 0.0575  -0.0957 0.0247  738  SER   B CA  
5802  C  C   . SER   B 434 ? 0.9326 0.9989 0.9821 0.0629  -0.0949 0.0247  738  SER   B C   
5803  O  O   . SER   B 434 ? 1.0044 1.0680 1.0531 0.0638  -0.0955 0.0227  738  SER   B O   
5804  C  CB  . SER   B 434 ? 0.9138 0.9813 0.9699 0.0515  -0.0946 0.0237  738  SER   B CB  
5805  O  OG  . SER   B 434 ? 0.9524 1.0293 1.0132 0.0513  -0.0927 0.0247  738  SER   B OG  
5806  N  N   . ARG   B 435 ? 0.9206 0.9926 0.9709 0.0664  -0.0935 0.0270  739  ARG   B N   
5807  C  CA  . ARG   B 435 ? 0.9196 0.9949 0.9696 0.0717  -0.0918 0.0276  739  ARG   B CA  
5808  C  C   . ARG   B 435 ? 0.9178 1.0038 0.9750 0.0700  -0.0893 0.0289  739  ARG   B C   
5809  O  O   . ARG   B 435 ? 0.9201 1.0117 0.9815 0.0675  -0.0890 0.0304  739  ARG   B O   
5810  C  CB  . ARG   B 435 ? 0.9373 1.0110 0.9835 0.0775  -0.0919 0.0293  739  ARG   B CB  
5811  C  CG  . ARG   B 435 ? 1.0345 1.1095 1.0792 0.0837  -0.0898 0.0298  739  ARG   B CG  
5812  C  CD  . ARG   B 435 ? 1.0921 1.1649 1.1330 0.0896  -0.0898 0.0314  739  ARG   B CD  
5813  N  NE  . ARG   B 435 ? 1.0849 1.1652 1.1312 0.0892  -0.0892 0.0337  739  ARG   B NE  
5814  C  CZ  . ARG   B 435 ? 1.0979 1.1755 1.1422 0.0890  -0.0913 0.0345  739  ARG   B CZ  
5815  N  NH1 . ARG   B 435 ? 1.1323 1.2000 1.1696 0.0889  -0.0938 0.0333  739  ARG   B NH1 
5816  N  NH2 . ARG   B 435 ? 1.1276 1.2124 1.1771 0.0891  -0.0910 0.0365  739  ARG   B NH2 
5817  N  N   . ILE   B 436 ? 0.9959 1.0842 1.0542 0.0716  -0.0875 0.0283  740  ILE   B N   
5818  C  CA  . ILE   B 436 ? 0.9237 1.0216 0.9888 0.0701  -0.0848 0.0295  740  ILE   B CA  
5819  C  C   . ILE   B 436 ? 0.9040 1.0066 0.9705 0.0755  -0.0823 0.0318  740  ILE   B C   
5820  O  O   . ILE   B 436 ? 0.9603 1.0589 1.0221 0.0810  -0.0813 0.0317  740  ILE   B O   
5821  C  CB  . ILE   B 436 ? 0.8982 0.9962 0.9639 0.0687  -0.0839 0.0278  740  ILE   B CB  
5822  C  CG1 . ILE   B 436 ? 0.9598 1.0513 1.0234 0.0648  -0.0866 0.0250  740  ILE   B CG1 
5823  C  CG2 . ILE   B 436 ? 0.8900 0.9978 0.9631 0.0661  -0.0813 0.0290  740  ILE   B CG2 
5824  C  CD1 . ILE   B 436 ? 0.9711 1.0627 1.0374 0.0588  -0.0881 0.0248  740  ILE   B CD1 
5825  N  N   . GLU   B 437 ? 0.9201 1.0310 0.9933 0.0742  -0.0814 0.0337  741  GLU   B N   
5826  C  CA  . GLU   B 437 ? 1.0163 1.1328 1.0929 0.0789  -0.0789 0.0360  741  GLU   B CA  
5827  C  C   . GLU   B 437 ? 1.0366 1.1633 1.1224 0.0762  -0.0765 0.0371  741  GLU   B C   
5828  O  O   . GLU   B 437 ? 0.9977 1.1273 1.0869 0.0706  -0.0776 0.0365  741  GLU   B O   
5829  C  CB  . GLU   B 437 ? 1.0547 1.1708 1.1309 0.0810  -0.0808 0.0372  741  GLU   B CB  
5830  C  CG  . GLU   B 437 ? 1.0385 1.1440 1.1054 0.0838  -0.0831 0.0362  741  GLU   B CG  
5831  C  CD  . GLU   B 437 ? 1.1723 1.2772 1.2380 0.0881  -0.0840 0.0377  741  GLU   B CD  
5832  O  OE1 . GLU   B 437 ? 1.1832 1.2929 1.2533 0.0862  -0.0853 0.0389  741  GLU   B OE1 
5833  O  OE2 . GLU   B 437 ? 1.2259 1.3255 1.2860 0.0938  -0.0835 0.0378  741  GLU   B OE2 
5834  N  N   . VAL   B 438 ? 1.1240 1.2557 1.2136 0.0802  -0.0730 0.0388  742  VAL   B N   
5835  C  CA  . VAL   B 438 ? 1.0943 1.2353 1.1929 0.0782  -0.0701 0.0399  742  VAL   B CA  
5836  C  C   . VAL   B 438 ? 1.2037 1.3527 1.3105 0.0795  -0.0698 0.0421  742  VAL   B C   
5837  O  O   . VAL   B 438 ? 1.3197 1.4678 1.4256 0.0846  -0.0692 0.0432  742  VAL   B O   
5838  C  CB  . VAL   B 438 ? 1.0720 1.2123 1.1692 0.0815  -0.0658 0.0402  742  VAL   B CB  
5839  C  CG1 . VAL   B 438 ? 1.1634 1.3025 1.2589 0.0886  -0.0631 0.0418  742  VAL   B CG1 
5840  C  CG2 . VAL   B 438 ? 1.2171 1.3659 1.3230 0.0785  -0.0630 0.0412  742  VAL   B CG2 
5841  N  N   . GLN   B 439 ? 1.2272 1.3838 1.3422 0.0749  -0.0705 0.0426  743  GLN   B N   
5842  C  CA  . GLN   B 439 ? 1.3118 1.4763 1.4357 0.0760  -0.0709 0.0444  743  GLN   B CA  
5843  C  C   . GLN   B 439 ? 1.3894 1.5595 1.5198 0.0802  -0.0660 0.0462  743  GLN   B C   
5844  O  O   . GLN   B 439 ? 1.3493 1.5223 1.4828 0.0789  -0.0626 0.0464  743  GLN   B O   
5845  C  CB  . GLN   B 439 ? 1.3256 1.4961 1.4562 0.0702  -0.0733 0.0442  743  GLN   B CB  
5846  C  CG  . GLN   B 439 ? 1.4969 1.6774 1.6394 0.0711  -0.0731 0.0459  743  GLN   B CG  
5847  C  CD  . GLN   B 439 ? 1.5288 1.7099 1.6723 0.0717  -0.0777 0.0462  743  GLN   B CD  
5848  O  OE1 . GLN   B 439 ? 1.4858 1.6593 1.6204 0.0714  -0.0809 0.0453  743  GLN   B OE1 
5849  N  NE2 . GLN   B 439 ? 1.4278 1.6176 1.5823 0.0727  -0.0782 0.0475  743  GLN   B NE2 
5850  N  N   . ASP   B 440 ? 1.4867 1.6580 1.6189 0.0855  -0.0653 0.0476  744  ASP   B N   
5851  C  CA  . ASP   B 440 ? 1.5277 1.7034 1.6653 0.0904  -0.0599 0.0495  744  ASP   B CA  
5852  C  C   . ASP   B 440 ? 1.5840 1.7695 1.7343 0.0916  -0.0600 0.0513  744  ASP   B C   
5853  O  O   . ASP   B 440 ? 1.5511 1.7400 1.7056 0.0885  -0.0647 0.0510  744  ASP   B O   
5854  C  CB  . ASP   B 440 ? 1.5318 1.6991 1.6596 0.0968  -0.0578 0.0496  744  ASP   B CB  
5855  C  CG  . ASP   B 440 ? 1.6260 1.7915 1.7521 0.1011  -0.0602 0.0501  744  ASP   B CG  
5856  O  OD1 . ASP   B 440 ? 1.6075 1.7685 1.7283 0.0990  -0.0652 0.0489  744  ASP   B OD1 
5857  O  OD2 . ASP   B 440 ? 1.6890 1.8573 1.8189 0.1066  -0.0568 0.0519  744  ASP   B OD2 
5858  N  N   . THR   B 441 ? 1.6055 1.7951 1.7616 0.0965  -0.0549 0.0533  745  THR   B N   
5859  C  CA  . THR   B 441 ? 1.5642 1.7651 1.7357 0.0970  -0.0535 0.0551  745  THR   B CA  
5860  C  C   . THR   B 441 ? 1.5630 1.7663 1.7381 0.0988  -0.0582 0.0553  745  THR   B C   
5861  O  O   . THR   B 441 ? 1.4943 1.7068 1.6821 0.0972  -0.0600 0.0559  745  THR   B O   
5862  C  CB  . THR   B 441 ? 1.4566 1.6599 1.6324 0.1022  -0.0461 0.0572  745  THR   B CB  
5863  O  OG1 . THR   B 441 ? 1.4689 1.6684 1.6402 0.1088  -0.0454 0.0579  745  THR   B OG1 
5864  C  CG2 . THR   B 441 ? 1.4216 1.6182 1.5882 0.1020  -0.0419 0.0568  745  THR   B CG2 
5865  N  N   . SER   B 442 ? 1.7418 1.9370 1.9063 0.1024  -0.0604 0.0547  746  SER   B N   
5866  C  CA  . SER   B 442 ? 1.7669 1.9634 1.9335 0.1045  -0.0650 0.0548  746  SER   B CA  
5867  C  C   . SER   B 442 ? 1.7974 1.9954 1.9656 0.0989  -0.0714 0.0535  746  SER   B C   
5868  O  O   . SER   B 442 ? 1.7918 1.9927 1.9644 0.1000  -0.0756 0.0537  746  SER   B O   
5869  C  CB  . SER   B 442 ? 1.7573 1.9432 1.9106 0.1093  -0.0660 0.0543  746  SER   B CB  
5870  O  OG  . SER   B 442 ? 1.7818 1.9578 1.9221 0.1064  -0.0675 0.0525  746  SER   B OG  
5871  N  N   . GLY   B 443 ? 1.7785 1.9745 1.9433 0.0930  -0.0723 0.0522  747  GLY   B N   
5872  C  CA  . GLY   B 443 ? 1.7614 1.9561 1.9241 0.0880  -0.0780 0.0509  747  GLY   B CA  
5873  C  C   . GLY   B 443 ? 1.7639 1.9472 1.9119 0.0869  -0.0808 0.0494  747  GLY   B C   
5874  O  O   . GLY   B 443 ? 1.7341 1.9148 1.8786 0.0820  -0.0843 0.0482  747  GLY   B O   
5875  N  N   . GLY   B 444 ? 1.7886 1.9648 1.9281 0.0915  -0.0793 0.0494  748  GLY   B N   
5876  C  CA  . GLY   B 444 ? 1.7490 1.9139 1.8751 0.0906  -0.0814 0.0480  748  GLY   B CA  
5877  C  C   . GLY   B 444 ? 1.6877 1.8485 1.8086 0.0882  -0.0785 0.0468  748  GLY   B C   
5878  O  O   . GLY   B 444 ? 1.6671 1.8334 1.7940 0.0854  -0.0759 0.0470  748  GLY   B O   
5879  N  N   . THR   B 445 ? 1.4889 1.6395 1.5985 0.0894  -0.0790 0.0457  749  THR   B N   
5880  C  CA  . THR   B 445 ? 1.3480 1.4938 1.4522 0.0883  -0.0767 0.0444  749  THR   B CA  
5881  C  C   . THR   B 445 ? 1.3433 1.4809 1.4388 0.0940  -0.0754 0.0442  749  THR   B C   
5882  O  O   . THR   B 445 ? 1.3635 1.4946 1.4525 0.0961  -0.0782 0.0439  749  THR   B O   
5883  C  CB  . THR   B 445 ? 1.1860 1.3268 1.2852 0.0823  -0.0794 0.0425  749  THR   B CB  
5884  O  OG1 . THR   B 445 ? 1.2660 1.3996 1.3582 0.0824  -0.0830 0.0420  749  THR   B OG1 
5885  C  CG2 . THR   B 445 ? 1.2330 1.3813 1.3399 0.0769  -0.0802 0.0427  749  THR   B CG2 
5886  N  N   . THR   B 446 ? 1.3302 1.4679 1.4252 0.0969  -0.0713 0.0445  750  THR   B N   
5887  C  CA  . THR   B 446 ? 1.2929 1.4214 1.3781 0.1019  -0.0702 0.0438  750  THR   B CA  
5888  C  C   . THR   B 446 ? 1.1991 1.3196 1.2765 0.0983  -0.0722 0.0413  750  THR   B C   
5889  O  O   . THR   B 446 ? 1.1490 1.2726 1.2298 0.0928  -0.0726 0.0405  750  THR   B O   
5890  C  CB  . THR   B 446 ? 1.3743 1.5059 1.4620 0.1068  -0.0646 0.0453  750  THR   B CB  
5891  O  OG1 . THR   B 446 ? 1.4345 1.5563 1.5115 0.1124  -0.0636 0.0446  750  THR   B OG1 
5892  C  CG2 . THR   B 446 ? 1.3206 1.4566 1.4126 0.1031  -0.0618 0.0451  750  THR   B CG2 
5893  N  N   . ALA   B 447 ? 1.2499 1.3600 1.3171 0.1014  -0.0738 0.0400  751  ALA   B N   
5894  C  CA  . ALA   B 447 ? 1.2493 1.3518 1.3099 0.0988  -0.0755 0.0374  751  ALA   B CA  
5895  C  C   . ALA   B 447 ? 1.2675 1.3693 1.3262 0.1015  -0.0719 0.0372  751  ALA   B C   
5896  O  O   . ALA   B 447 ? 1.3174 1.4263 1.3820 0.1034  -0.0678 0.0391  751  ALA   B O   
5897  C  CB  . ALA   B 447 ? 1.2308 1.3221 1.2817 0.1008  -0.0790 0.0359  751  ALA   B CB  
5898  N  N   . LEU   B 448 ? 1.1266 1.2197 1.1775 0.1018  -0.0734 0.0349  752  LEU   B N   
5899  C  CA  . LEU   B 448 ? 1.1562 1.2473 1.2037 0.1052  -0.0701 0.0347  752  LEU   B CA  
5900  C  C   . LEU   B 448 ? 1.1688 1.2475 1.2044 0.1097  -0.0720 0.0326  752  LEU   B C   
5901  O  O   . LEU   B 448 ? 1.1908 1.2658 1.2214 0.1135  -0.0696 0.0323  752  LEU   B O   
5902  C  CB  . LEU   B 448 ? 1.1941 1.2898 1.2464 0.0998  -0.0695 0.0339  752  LEU   B CB  
5903  C  CG  . LEU   B 448 ? 1.1705 1.2629 1.2220 0.0939  -0.0740 0.0312  752  LEU   B CG  
5904  C  CD1 . LEU   B 448 ? 1.2073 1.2904 1.2503 0.0962  -0.0751 0.0288  752  LEU   B CD1 
5905  C  CD2 . LEU   B 448 ? 1.0025 1.1038 1.0630 0.0875  -0.0733 0.0316  752  LEU   B CD2 
5906  N  N   . ARG   B 449 ? 1.1624 1.2342 1.1932 0.1096  -0.0762 0.0312  753  ARG   B N   
5907  C  CA  . ARG   B 449 ? 1.1218 1.1813 1.1414 0.1141  -0.0787 0.0292  753  ARG   B CA  
5908  C  C   . ARG   B 449 ? 1.1289 1.1846 1.1466 0.1140  -0.0819 0.0292  753  ARG   B C   
5909  O  O   . ARG   B 449 ? 1.1812 1.2422 1.2053 0.1088  -0.0833 0.0297  753  ARG   B O   
5910  C  CB  . ARG   B 449 ? 1.1245 1.1776 1.1403 0.1111  -0.0820 0.0259  753  ARG   B CB  
5911  C  CG  . ARG   B 449 ? 1.1030 1.1515 1.1188 0.1062  -0.0872 0.0237  753  ARG   B CG  
5912  C  CD  . ARG   B 449 ? 1.1231 1.1688 1.1390 0.1021  -0.0898 0.0207  753  ARG   B CD  
5913  N  NE  . ARG   B 449 ? 1.1758 1.2311 1.2007 0.0964  -0.0880 0.0213  753  ARG   B NE  
5914  C  CZ  . ARG   B 449 ? 1.1569 1.2156 1.1830 0.0969  -0.0854 0.0215  753  ARG   B CZ  
5915  N  NH1 . ARG   B 449 ? 1.1162 1.1701 1.1351 0.1032  -0.0836 0.0214  753  ARG   B NH1 
5916  N  NH2 . ARG   B 449 ? 1.1423 1.2089 1.1764 0.0911  -0.0844 0.0217  753  ARG   B NH2 
5917  N  N   . PRO   B 450 ? 1.1347 1.1811 1.1433 0.1198  -0.0831 0.0286  754  PRO   B N   
5918  C  CA  . PRO   B 450 ? 1.1467 1.1884 1.1528 0.1196  -0.0865 0.0284  754  PRO   B CA  
5919  C  C   . PRO   B 450 ? 1.1356 1.1711 1.1403 0.1141  -0.0913 0.0255  754  PRO   B C   
5920  O  O   . PRO   B 450 ? 1.1852 1.2136 1.1848 0.1145  -0.0933 0.0230  754  PRO   B O   
5921  C  CB  . PRO   B 450 ? 1.2055 1.2384 1.2017 0.1279  -0.0860 0.0285  754  PRO   B CB  
5922  C  CG  . PRO   B 450 ? 1.2552 1.2915 1.2510 0.1326  -0.0809 0.0298  754  PRO   B CG  
5923  C  CD  . PRO   B 450 ? 1.2028 1.2425 1.2027 0.1273  -0.0810 0.0285  754  PRO   B CD  
5924  N  N   . SER   B 451 ? 1.1478 1.1865 1.1576 0.1088  -0.0929 0.0260  755  SER   B N   
5925  C  CA  . SER   B 451 ? 1.0790 1.1136 1.0897 0.1027  -0.0965 0.0237  755  SER   B CA  
5926  C  C   . SER   B 451 ? 1.1183 1.1442 1.1236 0.1035  -0.0996 0.0233  755  SER   B C   
5927  O  O   . SER   B 451 ? 1.1991 1.2221 1.1996 0.1091  -0.0991 0.0246  755  SER   B O   
5928  C  CB  . SER   B 451 ? 1.0992 1.1434 1.1193 0.0958  -0.0954 0.0247  755  SER   B CB  
5929  O  OG  . SER   B 451 ? 1.1725 1.2250 1.1978 0.0953  -0.0923 0.0254  755  SER   B OG  
5930  N  N   . ALA   B 452 ? 1.1124 1.1340 1.1188 0.0980  -0.1025 0.0215  756  ALA   B N   
5931  C  CA  . ALA   B 452 ? 1.1336 1.1467 1.1354 0.0979  -0.1052 0.0212  756  ALA   B CA  
5932  C  C   . ALA   B 452 ? 1.1947 1.2124 1.1983 0.0982  -0.1038 0.0241  756  ALA   B C   
5933  O  O   . ALA   B 452 ? 1.2892 1.3012 1.2870 0.1024  -0.1047 0.0249  756  ALA   B O   
5934  C  CB  . ALA   B 452 ? 1.0200 1.0286 1.0244 0.0913  -0.1079 0.0190  756  ALA   B CB  
5935  N  N   . SER   B 453 ? 1.1924 1.2196 1.2034 0.0938  -0.1019 0.0257  757  SER   B N   
5936  C  CA  . SER   B 453 ? 1.2239 1.2558 1.2368 0.0943  -0.1010 0.0283  757  SER   B CA  
5937  C  C   . SER   B 453 ? 1.2802 1.3150 1.2913 0.1015  -0.0993 0.0301  757  SER   B C   
5938  O  O   . SER   B 453 ? 1.3147 1.3472 1.3227 0.1046  -0.1000 0.0315  757  SER   B O   
5939  C  CB  . SER   B 453 ? 1.2123 1.2546 1.2336 0.0891  -0.0993 0.0294  757  SER   B CB  
5940  O  OG  . SER   B 453 ? 1.2325 1.2830 1.2582 0.0910  -0.0967 0.0300  757  SER   B OG  
5941  N  N   . THR   B 454 ? 1.2696 1.3097 1.2830 0.1043  -0.0968 0.0303  758  THR   B N   
5942  C  CA  . THR   B 454 ? 1.3015 1.3451 1.3144 0.1111  -0.0944 0.0322  758  THR   B CA  
5943  C  C   . THR   B 454 ? 1.3118 1.3446 1.3148 0.1173  -0.0958 0.0315  758  THR   B C   
5944  O  O   . THR   B 454 ? 1.3325 1.3655 1.3338 0.1225  -0.0950 0.0332  758  THR   B O   
5945  C  CB  . THR   B 454 ? 1.2771 1.3278 1.2942 0.1126  -0.0908 0.0327  758  THR   B CB  
5946  O  OG1 . THR   B 454 ? 1.2578 1.3005 1.2677 0.1158  -0.0910 0.0307  758  THR   B OG1 
5947  C  CG2 . THR   B 454 ? 1.2424 1.3010 1.2676 0.1057  -0.0902 0.0325  758  THR   B CG2 
5948  N  N   . GLN   B 455 ? 1.2674 1.2904 1.2640 0.1169  -0.0982 0.0289  759  GLN   B N   
5949  C  CA  . GLN   B 455 ? 1.2780 1.2895 1.2646 0.1226  -0.1000 0.0278  759  GLN   B CA  
5950  C  C   . GLN   B 455 ? 1.3014 1.3040 1.2839 0.1200  -0.1039 0.0268  759  GLN   B C   
5951  O  O   . GLN   B 455 ? 1.3596 1.3512 1.3349 0.1213  -0.1067 0.0245  759  GLN   B O   
5952  C  CB  . GLN   B 455 ? 1.3054 1.3108 1.2868 0.1247  -0.1006 0.0254  759  GLN   B CB  
5953  C  CG  . GLN   B 455 ? 1.3115 1.3239 1.2956 0.1272  -0.0965 0.0262  759  GLN   B CG  
5954  C  CD  . GLN   B 455 ? 1.3547 1.3722 1.3391 0.1338  -0.0923 0.0290  759  GLN   B CD  
5955  O  OE1 . GLN   B 455 ? 1.3463 1.3574 1.3228 0.1408  -0.0913 0.0289  759  GLN   B OE1 
5956  N  NE2 . GLN   B 455 ? 1.3729 1.4019 1.3667 0.1316  -0.0899 0.0315  759  GLN   B NE2 
5957  N  N   . ALA   B 456 ? 1.2641 1.2701 1.2503 0.1165  -0.1042 0.0283  760  ALA   B N   
5958  C  CA  . ALA   B 456 ? 1.2245 1.2207 1.2055 0.1149  -0.1073 0.0277  760  ALA   B CA  
5959  C  C   . ALA   B 456 ? 1.2555 1.2476 1.2303 0.1217  -0.1076 0.0292  760  ALA   B C   
5960  O  O   . ALA   B 456 ? 1.3365 1.3343 1.3123 0.1270  -0.1052 0.0308  760  ALA   B O   
5961  C  CB  . ALA   B 456 ? 1.2134 1.2131 1.1998 0.1079  -0.1076 0.0285  760  ALA   B CB  
5962  N  N   . LEU   B 457 ? 1.2359 1.2178 1.2046 0.1214  -0.1104 0.0286  761  LEU   B N   
5963  C  CA  . LEU   B 457 ? 1.1847 1.1614 1.1467 0.1281  -0.1109 0.0298  761  LEU   B CA  
5964  C  C   . LEU   B 457 ? 1.1984 1.1796 1.1629 0.1274  -0.1107 0.0323  761  LEU   B C   
5965  O  O   . LEU   B 457 ? 1.2573 1.2410 1.2207 0.1332  -0.1098 0.0341  761  LEU   B O   
5966  C  CB  . LEU   B 457 ? 1.2293 1.1912 1.1819 0.1293  -0.1143 0.0278  761  LEU   B CB  
5967  C  CG  . LEU   B 457 ? 1.3065 1.2621 1.2573 0.1272  -0.1161 0.0246  761  LEU   B CG  
5968  C  CD1 . LEU   B 457 ? 1.3520 1.2931 1.2949 0.1274  -0.1199 0.0227  761  LEU   B CD1 
5969  C  CD2 . LEU   B 457 ? 1.2280 1.1856 1.1771 0.1326  -0.1146 0.0238  761  LEU   B CD2 
5970  N  N   . SER   B 458 ? 1.1972 1.1788 1.1648 0.1206  -0.1115 0.0324  762  SER   B N   
5971  C  CA  . SER   B 458 ? 1.1976 1.1841 1.1678 0.1195  -0.1113 0.0347  762  SER   B CA  
5972  C  C   . SER   B 458 ? 1.1635 1.1603 1.1428 0.1133  -0.1098 0.0351  762  SER   B C   
5973  O  O   . SER   B 458 ? 1.2000 1.1975 1.1823 0.1089  -0.1092 0.0334  762  SER   B O   
5974  C  CB  . SER   B 458 ? 1.2497 1.2252 1.2131 0.1177  -0.1136 0.0348  762  SER   B CB  
5975  O  OG  . SER   B 458 ? 1.2918 1.2587 1.2530 0.1128  -0.1148 0.0327  762  SER   B OG  
5976  N  N   . SER   B 459 ? 1.1392 1.1437 1.1227 0.1133  -0.1093 0.0371  763  SER   B N   
5977  C  CA  . SER   B 459 ? 1.1495 1.1651 1.1420 0.1088  -0.1076 0.0375  763  SER   B CA  
5978  C  C   . SER   B 459 ? 1.1757 1.1950 1.1700 0.1075  -0.1085 0.0394  763  SER   B C   
5979  O  O   . SER   B 459 ? 1.2427 1.2664 1.2382 0.1124  -0.1089 0.0409  763  SER   B O   
5980  C  CB  . SER   B 459 ? 1.2234 1.2490 1.2221 0.1124  -0.1052 0.0379  763  SER   B CB  
5981  O  OG  . SER   B 459 ? 1.2553 1.2871 1.2567 0.1172  -0.1049 0.0399  763  SER   B OG  
5982  N  N   . SER   B 460 ? 1.1645 1.1822 1.1591 0.1012  -0.1089 0.0393  764  SER   B N   
5983  C  CA  . SER   B 460 ? 1.1848 1.2062 1.1810 0.0996  -0.1098 0.0409  764  SER   B CA  
5984  C  C   . SER   B 460 ? 1.1865 1.2193 1.1918 0.0956  -0.1084 0.0410  764  SER   B C   
5985  O  O   . SER   B 460 ? 1.1319 1.1672 1.1410 0.0920  -0.1066 0.0396  764  SER   B O   
5986  C  CB  . SER   B 460 ? 1.2092 1.2201 1.1983 0.0959  -0.1110 0.0410  764  SER   B CB  
5987  O  OG  . SER   B 460 ? 1.2232 1.2292 1.2119 0.0904  -0.1097 0.0394  764  SER   B OG  
5988  N  N   . VAL   B 461 ? 1.2368 1.2763 1.2458 0.0964  -0.1094 0.0424  765  VAL   B N   
5989  C  CA  . VAL   B 461 ? 1.2302 1.2790 1.2467 0.0921  -0.1087 0.0426  765  VAL   B CA  
5990  C  C   . VAL   B 461 ? 1.2631 1.3077 1.2753 0.0893  -0.1106 0.0434  765  VAL   B C   
5991  O  O   . VAL   B 461 ? 1.2775 1.3153 1.2830 0.0924  -0.1128 0.0443  765  VAL   B O   
5992  C  CB  . VAL   B 461 ? 1.2244 1.2858 1.2502 0.0955  -0.1083 0.0435  765  VAL   B CB  
5993  C  CG1 . VAL   B 461 ? 1.2052 1.2759 1.2392 0.0906  -0.1074 0.0434  765  VAL   B CG1 
5994  C  CG2 . VAL   B 461 ? 1.1836 1.2472 1.2115 0.0997  -0.1061 0.0430  765  VAL   B CG2 
5995  N  N   . SER   B 462 ? 1.2893 1.3371 1.3047 0.0836  -0.1098 0.0431  766  SER   B N   
5996  C  CA  . SER   B 462 ? 1.2903 1.3335 1.3009 0.0807  -0.1112 0.0439  766  SER   B CA  
5997  C  C   . SER   B 462 ? 1.3437 1.3933 1.3572 0.0839  -0.1140 0.0450  766  SER   B C   
5998  O  O   . SER   B 462 ? 1.3036 1.3637 1.3257 0.0865  -0.1142 0.0452  766  SER   B O   
5999  C  CB  . SER   B 462 ? 1.1899 1.2348 1.2032 0.0739  -0.1092 0.0431  766  SER   B CB  
6000  O  OG  . SER   B 462 ? 1.2160 1.2533 1.2224 0.0709  -0.1096 0.0437  766  SER   B OG  
6001  N  N   . SER   B 463 ? 1.3690 1.4119 1.3753 0.0839  -0.1163 0.0459  767  SER   B N   
6002  C  CA  . SER   B 463 ? 1.4523 1.5007 1.4611 0.0866  -0.1198 0.0468  767  SER   B CA  
6003  C  C   . SER   B 463 ? 1.5575 1.5983 1.5582 0.0835  -0.1212 0.0472  767  SER   B C   
6004  O  O   . SER   B 463 ? 1.6800 1.7104 1.6706 0.0857  -0.1230 0.0480  767  SER   B O   
6005  C  CB  . SER   B 463 ? 1.4954 1.5430 1.5027 0.0936  -0.1224 0.0475  767  SER   B CB  
6006  O  OG  . SER   B 463 ? 1.6113 1.6638 1.6213 0.0960  -0.1263 0.0481  767  SER   B OG  
6007  N  N   . SER   B 464 ? 1.6424 1.6876 1.6468 0.0787  -0.1203 0.0468  768  SER   B N   
6008  C  CA  . SER   B 464 ? 1.7653 1.8028 1.7615 0.0757  -0.1211 0.0472  768  SER   B CA  
6009  C  C   . SER   B 464 ? 1.8957 1.9388 1.8945 0.0766  -0.1249 0.0474  768  SER   B C   
6010  O  O   . SER   B 464 ? 1.9796 2.0146 1.9692 0.0775  -0.1275 0.0481  768  SER   B O   
6011  C  CB  . SER   B 464 ? 1.7326 1.7676 1.7284 0.0691  -0.1169 0.0466  768  SER   B CB  
6012  O  OG  . SER   B 464 ? 1.6834 1.7091 1.6737 0.0681  -0.1141 0.0464  768  SER   B OG  
6013  N  N   . LYS   B 465 ? 1.8970 1.9533 1.9080 0.0764  -0.1255 0.0469  769  LYS   B N   
6014  C  CA  . LYS   B 465 ? 1.9359 1.9985 1.9512 0.0765  -0.1292 0.0468  769  LYS   B CA  
6015  C  C   . LYS   B 465 ? 1.9902 2.0471 1.9990 0.0716  -0.1287 0.0466  769  LYS   B C   
6016  O  O   . LYS   B 465 ? 1.9839 2.0442 1.9944 0.0712  -0.1319 0.0463  769  LYS   B O   
6017  C  CB  . LYS   B 465 ? 1.8695 1.9301 1.8817 0.0824  -0.1346 0.0474  769  LYS   B CB  
6018  N  N   . LEU   B 466 ? 2.1119 2.1602 2.1137 0.0679  -0.1245 0.0466  770  LEU   B N   
6019  C  CA  . LEU   B 466 ? 2.0618 2.1033 2.0564 0.0633  -0.1230 0.0466  770  LEU   B CA  
6020  C  C   . LEU   B 466 ? 2.0350 2.0864 2.0383 0.0599  -0.1231 0.0458  770  LEU   B C   
6021  O  O   . LEU   B 466 ? 2.0567 2.1054 2.0555 0.0586  -0.1250 0.0458  770  LEU   B O   
6022  C  CB  . LEU   B 466 ? 1.9858 2.0192 1.9755 0.0596  -0.1177 0.0467  770  LEU   B CB  
6023  C  CG  . LEU   B 466 ? 2.0056 2.0240 1.9821 0.0605  -0.1168 0.0477  770  LEU   B CG  
6024  C  CD1 . LEU   B 466 ? 2.0423 2.0576 2.0147 0.0667  -0.1206 0.0485  770  LEU   B CD1 
6025  C  CD2 . LEU   B 466 ? 1.9628 1.9768 1.9394 0.0573  -0.1118 0.0474  770  LEU   B CD2 
6026  N  N   . PHE   B 467 ? 1.9094 1.9716 1.9244 0.0587  -0.1211 0.0450  771  PHE   B N   
6027  C  CA  . PHE   B 467 ? 1.9189 1.9909 1.9430 0.0554  -0.1207 0.0442  771  PHE   B CA  
6028  C  C   . PHE   B 467 ? 2.0133 2.0977 2.0495 0.0586  -0.1230 0.0440  771  PHE   B C   
6029  O  O   . PHE   B 467 ? 2.0313 2.1192 2.0721 0.0610  -0.1215 0.0441  771  PHE   B O   
6030  C  CB  . PHE   B 467 ? 1.7383 1.8110 1.7650 0.0505  -0.1154 0.0434  771  PHE   B CB  
6031  C  CG  . PHE   B 467 ? 1.6718 1.7323 1.6883 0.0483  -0.1123 0.0437  771  PHE   B CG  
6032  C  CD1 . PHE   B 467 ? 1.6241 1.6768 1.6326 0.0451  -0.1112 0.0440  771  PHE   B CD1 
6033  C  CD2 . PHE   B 467 ? 1.6420 1.6985 1.6572 0.0497  -0.1103 0.0438  771  PHE   B CD2 
6034  C  CE1 . PHE   B 467 ? 1.5101 1.5516 1.5102 0.0430  -0.1077 0.0444  771  PHE   B CE1 
6035  C  CE2 . PHE   B 467 ? 1.5533 1.5987 1.5603 0.0475  -0.1074 0.0440  771  PHE   B CE2 
6036  C  CZ  . PHE   B 467 ? 1.4945 1.5327 1.4944 0.0441  -0.1058 0.0444  771  PHE   B CZ  
6037  N  N   . SER   B 468 ? 2.1766 2.2674 2.2179 0.0588  -0.1267 0.0437  772  SER   B N   
6038  C  CA  . SER   B 468 ? 2.1659 2.2680 2.2191 0.0622  -0.1293 0.0437  772  SER   B CA  
6039  C  C   . SER   B 468 ? 2.1675 2.2796 2.2321 0.0608  -0.1252 0.0434  772  SER   B C   
6040  O  O   . SER   B 468 ? 2.1773 2.2947 2.2482 0.0644  -0.1245 0.0438  772  SER   B O   
6041  C  CB  . SER   B 468 ? 2.1617 2.2682 2.2187 0.0621  -0.1343 0.0432  772  SER   B CB  
6042  O  OG  . SER   B 468 ? 2.1492 2.2671 2.2191 0.0653  -0.1367 0.0433  772  SER   B OG  
6043  N  N   . SER   B 469 ? 2.0068 2.1212 2.0737 0.0558  -0.1223 0.0427  773  SER   B N   
6044  C  CA  . SER   B 469 ? 1.9276 2.0508 2.0044 0.0543  -0.1185 0.0423  773  SER   B CA  
6045  C  C   . SER   B 469 ? 1.7514 1.8690 1.8233 0.0517  -0.1138 0.0419  773  SER   B C   
6046  O  O   . SER   B 469 ? 1.6737 1.7870 1.7421 0.0542  -0.1124 0.0422  773  SER   B O   
6047  C  CB  . SER   B 469 ? 1.8861 2.0172 1.9708 0.0507  -0.1189 0.0417  773  SER   B CB  
6048  O  OG  . SER   B 469 ? 1.8717 2.0085 1.9625 0.0530  -0.1236 0.0419  773  SER   B OG  
6049  N  N   . THR   B 476 ? 1.4264 1.6125 1.5744 0.0498  -0.0815 0.0424  780  THR   B N   
6050  C  CA  . THR   B 476 ? 1.4683 1.6638 1.6280 0.0503  -0.0802 0.0437  780  THR   B CA  
6051  C  C   . THR   B 476 ? 1.5033 1.7012 1.6662 0.0530  -0.0746 0.0446  780  THR   B C   
6052  O  O   . THR   B 476 ? 1.5356 1.7360 1.7021 0.0577  -0.0726 0.0460  780  THR   B O   
6053  C  CB  . THR   B 476 ? 1.5403 1.7403 1.7054 0.0450  -0.0822 0.0431  780  THR   B CB  
6054  O  OG1 . THR   B 476 ? 1.5295 1.7293 1.6946 0.0442  -0.0874 0.0429  780  THR   B OG1 
6055  C  CG2 . THR   B 476 ? 1.5588 1.7680 1.7362 0.0447  -0.0795 0.0443  780  THR   B CG2 
6056  N  N   . SER   B 477 ? 1.4082 1.6048 1.5691 0.0504  -0.0720 0.0439  781  SER   B N   
6057  C  CA  . SER   B 477 ? 1.4094 1.6075 1.5725 0.0530  -0.0666 0.0448  781  SER   B CA  
6058  C  C   . SER   B 477 ? 1.3645 1.5575 1.5214 0.0589  -0.0647 0.0453  781  SER   B C   
6059  O  O   . SER   B 477 ? 1.3420 1.5285 1.4908 0.0601  -0.0674 0.0444  781  SER   B O   
6060  C  CB  . SER   B 477 ? 1.4432 1.6384 1.6022 0.0498  -0.0648 0.0436  781  SER   B CB  
6061  O  OG  . SER   B 477 ? 1.4228 1.6156 1.5791 0.0534  -0.0600 0.0441  781  SER   B OG  
6062  N  N   . PHE   B 478 ? 1.3567 1.5522 1.5172 0.0627  -0.0597 0.0469  782  PHE   B N   
6063  C  CA  . PHE   B 478 ? 1.3657 1.5577 1.5222 0.0690  -0.0578 0.0478  782  PHE   B CA  
6064  C  C   . PHE   B 478 ? 1.3682 1.5503 1.5122 0.0713  -0.0567 0.0465  782  PHE   B C   
6065  O  O   . PHE   B 478 ? 1.3409 1.5187 1.4798 0.0767  -0.0552 0.0470  782  PHE   B O   
6066  C  CB  . PHE   B 478 ? 1.2641 1.4629 1.4301 0.0726  -0.0526 0.0501  782  PHE   B CB  
6067  C  CG  . PHE   B 478 ? 1.2256 1.4301 1.3995 0.0750  -0.0542 0.0514  782  PHE   B CG  
6068  C  CD1 . PHE   B 478 ? 1.3910 1.5993 1.5697 0.0713  -0.0599 0.0507  782  PHE   B CD1 
6069  C  CD2 . PHE   B 478 ? 1.2536 1.4590 1.4296 0.0811  -0.0504 0.0532  782  PHE   B CD2 
6070  C  CE1 . PHE   B 478 ? 1.4544 1.6679 1.6405 0.0733  -0.0621 0.0516  782  PHE   B CE1 
6071  C  CE2 . PHE   B 478 ? 1.3471 1.5582 1.5313 0.0834  -0.0522 0.0542  782  PHE   B CE2 
6072  C  CZ  . PHE   B 478 ? 1.4402 1.6556 1.6299 0.0793  -0.0586 0.0533  782  PHE   B CZ  
6073  N  N   . GLY   B 479 ? 1.3020 1.4801 1.4408 0.0674  -0.0578 0.0447  783  GLY   B N   
6074  C  CA  . GLY   B 479 ? 1.2915 1.4600 1.4189 0.0693  -0.0580 0.0431  783  GLY   B CA  
6075  C  C   . GLY   B 479 ? 1.3049 1.4683 1.4267 0.0654  -0.0629 0.0409  783  GLY   B C   
6076  O  O   . GLY   B 479 ? 1.2847 1.4399 1.3977 0.0663  -0.0641 0.0392  783  GLY   B O   
6077  N  N   . GLU   B 480 ? 1.2959 1.4638 1.4229 0.0612  -0.0659 0.0409  784  GLU   B N   
6078  C  CA  . GLU   B 480 ? 1.2538 1.4174 1.3763 0.0568  -0.0697 0.0391  784  GLU   B CA  
6079  C  C   . GLU   B 480 ? 1.2214 1.3767 1.3354 0.0594  -0.0720 0.0382  784  GLU   B C   
6080  O  O   . GLU   B 480 ? 1.2494 1.4043 1.3628 0.0635  -0.0723 0.0393  784  GLU   B O   
6081  C  CB  . GLU   B 480 ? 1.3030 1.4720 1.4313 0.0529  -0.0725 0.0396  784  GLU   B CB  
6082  C  CG  . GLU   B 480 ? 1.3538 1.5281 1.4878 0.0479  -0.0720 0.0393  784  GLU   B CG  
6083  C  CD  . GLU   B 480 ? 1.4815 1.6581 1.6180 0.0440  -0.0757 0.0392  784  GLU   B CD  
6084  O  OE1 . GLU   B 480 ? 1.4858 1.6567 1.6162 0.0435  -0.0785 0.0385  784  GLU   B OE1 
6085  O  OE2 . GLU   B 480 ? 1.5356 1.7189 1.6797 0.0417  -0.0757 0.0398  784  GLU   B OE2 
6086  N  N   . GLU   B 481 ? 1.0468 1.1954 1.1546 0.0570  -0.0736 0.0362  785  GLU   B N   
6087  C  CA  . GLU   B 481 ? 0.9681 1.1083 1.0680 0.0590  -0.0758 0.0351  785  GLU   B CA  
6088  C  C   . GLU   B 481 ? 0.9450 1.0839 1.0442 0.0563  -0.0790 0.0352  785  GLU   B C   
6089  O  O   . GLU   B 481 ? 0.9637 1.1053 1.0659 0.0516  -0.0800 0.0349  785  GLU   B O   
6090  C  CB  . GLU   B 481 ? 0.9689 1.1024 1.0634 0.0575  -0.0762 0.0327  785  GLU   B CB  
6091  C  CG  . GLU   B 481 ? 1.0809 1.2136 1.1739 0.0608  -0.0734 0.0324  785  GLU   B CG  
6092  C  CD  . GLU   B 481 ? 1.1087 1.2351 1.1969 0.0593  -0.0746 0.0298  785  GLU   B CD  
6093  O  OE1 . GLU   B 481 ? 1.0858 1.2102 1.1740 0.0548  -0.0770 0.0283  785  GLU   B OE1 
6094  O  OE2 . GLU   B 481 ? 1.0827 1.2059 1.1672 0.0628  -0.0730 0.0292  785  GLU   B OE2 
6095  N  N   . VAL   B 482 ? 0.9206 1.0547 1.0153 0.0598  -0.0804 0.0355  786  VAL   B N   
6096  C  CA  . VAL   B 482 ? 0.8779 1.0080 0.9695 0.0578  -0.0835 0.0354  786  VAL   B CA  
6097  C  C   . VAL   B 482 ? 0.8931 1.0132 0.9765 0.0591  -0.0848 0.0340  786  VAL   B C   
6098  O  O   . VAL   B 482 ? 0.9607 1.0770 1.0406 0.0631  -0.0840 0.0335  786  VAL   B O   
6099  C  CB  . VAL   B 482 ? 0.8799 1.0136 0.9739 0.0606  -0.0846 0.0373  786  VAL   B CB  
6100  C  CG1 . VAL   B 482 ? 0.9542 1.0840 1.0442 0.0667  -0.0844 0.0379  786  VAL   B CG1 
6101  C  CG2 . VAL   B 482 ? 0.9262 1.0572 1.0179 0.0572  -0.0875 0.0373  786  VAL   B CG2 
6102  N  N   . GLU   B 483 ? 0.8862 1.0015 0.9666 0.0556  -0.0869 0.0334  787  GLU   B N   
6103  C  CA  . GLU   B 483 ? 0.8925 0.9981 0.9661 0.0559  -0.0884 0.0321  787  GLU   B CA  
6104  C  C   . GLU   B 483 ? 0.8989 1.0008 0.9685 0.0588  -0.0901 0.0333  787  GLU   B C   
6105  O  O   . GLU   B 483 ? 0.9179 1.0235 0.9895 0.0583  -0.0909 0.0348  787  GLU   B O   
6106  C  CB  . GLU   B 483 ? 0.8908 0.9932 0.9641 0.0499  -0.0890 0.0307  787  GLU   B CB  
6107  C  CG  . GLU   B 483 ? 0.9287 1.0238 0.9988 0.0490  -0.0895 0.0284  787  GLU   B CG  
6108  C  CD  . GLU   B 483 ? 0.9688 1.0646 1.0421 0.0432  -0.0890 0.0270  787  GLU   B CD  
6109  O  OE1 . GLU   B 483 ? 0.9842 1.0855 1.0616 0.0421  -0.0877 0.0265  787  GLU   B OE1 
6110  O  OE2 . GLU   B 483 ? 0.9611 1.0516 1.0327 0.0398  -0.0896 0.0264  787  GLU   B OE2 
6111  N  N   . VAL   B 484 ? 0.9059 1.0000 0.9695 0.0620  -0.0911 0.0327  788  VAL   B N   
6112  C  CA  . VAL   B 484 ? 0.9131 1.0022 0.9718 0.0650  -0.0928 0.0337  788  VAL   B CA  
6113  C  C   . VAL   B 484 ? 0.9296 1.0081 0.9821 0.0633  -0.0943 0.0323  788  VAL   B C   
6114  O  O   . VAL   B 484 ? 0.9247 0.9977 0.9738 0.0654  -0.0946 0.0308  788  VAL   B O   
6115  C  CB  . VAL   B 484 ? 0.9166 1.0068 0.9743 0.0718  -0.0923 0.0347  788  VAL   B CB  
6116  C  CG1 . VAL   B 484 ? 1.0148 1.0999 1.0675 0.0750  -0.0942 0.0358  788  VAL   B CG1 
6117  C  CG2 . VAL   B 484 ? 0.9129 1.0139 0.9782 0.0730  -0.0903 0.0362  788  VAL   B CG2 
6118  N  N   . HIS   B 485 ? 0.9617 1.0372 1.0127 0.0594  -0.0951 0.0326  789  HIS   B N   
6119  C  CA  . HIS   B 485 ? 0.9786 1.0442 1.0246 0.0570  -0.0960 0.0315  789  HIS   B CA  
6120  C  C   . HIS   B 485 ? 1.0213 1.0796 1.0606 0.0610  -0.0977 0.0324  789  HIS   B C   
6121  O  O   . HIS   B 485 ? 1.0319 1.0921 1.0699 0.0632  -0.0983 0.0342  789  HIS   B O   
6122  C  CB  . HIS   B 485 ? 1.0073 1.0723 1.0543 0.0512  -0.0954 0.0317  789  HIS   B CB  
6123  C  CG  . HIS   B 485 ? 0.9666 1.0362 1.0193 0.0466  -0.0939 0.0304  789  HIS   B CG  
6124  N  ND1 . HIS   B 485 ? 0.9729 1.0375 1.0258 0.0420  -0.0933 0.0289  789  HIS   B ND1 
6125  C  CD2 . HIS   B 485 ? 0.9558 1.0342 1.0142 0.0461  -0.0928 0.0303  789  HIS   B CD2 
6126  C  CE1 . HIS   B 485 ? 1.0254 1.0958 1.0840 0.0389  -0.0921 0.0279  789  HIS   B CE1 
6127  N  NE2 . HIS   B 485 ? 1.0138 1.0924 1.0754 0.0414  -0.0918 0.0287  789  HIS   B NE2 
6128  N  N   . ASN   B 486 ? 1.0554 1.1049 1.0903 0.0618  -0.0986 0.0310  790  ASN   B N   
6129  C  CA  . ASN   B 486 ? 1.0733 1.1147 1.1012 0.0654  -0.1002 0.0316  790  ASN   B CA  
6130  C  C   . ASN   B 486 ? 1.0063 1.0372 1.0306 0.0630  -0.1011 0.0299  790  ASN   B C   
6131  O  O   . ASN   B 486 ? 0.9736 1.0039 1.0012 0.0599  -0.1008 0.0279  790  ASN   B O   
6132  C  CB  . ASN   B 486 ? 1.0276 1.0708 1.0539 0.0724  -0.1006 0.0321  790  ASN   B CB  
6133  C  CG  . ASN   B 486 ? 1.0993 1.1454 1.1283 0.0736  -0.0998 0.0305  790  ASN   B CG  
6134  O  OD1 . ASN   B 486 ? 1.0901 1.1446 1.1250 0.0721  -0.0982 0.0306  790  ASN   B OD1 
6135  N  ND2 . ASN   B 486 ? 1.1830 1.2212 1.2071 0.0763  -0.1011 0.0290  790  ASN   B ND2 
6136  N  N   . LEU   B 487 ? 1.0538 1.0764 1.0719 0.0640  -0.1021 0.0307  791  LEU   B N   
6137  C  CA  . LEU   B 487 ? 1.0487 1.0605 1.0633 0.0621  -0.1030 0.0293  791  LEU   B CA  
6138  C  C   . LEU   B 487 ? 1.1023 1.1087 1.1124 0.0676  -0.1050 0.0283  791  LEU   B C   
6139  O  O   . LEU   B 487 ? 1.0840 1.0917 1.0907 0.0732  -0.1056 0.0296  791  LEU   B O   
6140  C  CB  . LEU   B 487 ? 1.0732 1.0777 1.0827 0.0603  -0.1028 0.0309  791  LEU   B CB  
6141  C  CG  . LEU   B 487 ? 1.0365 1.0287 1.0416 0.0592  -0.1037 0.0298  791  LEU   B CG  
6142  C  CD1 . LEU   B 487 ? 1.0190 1.0098 1.0298 0.0538  -0.1030 0.0275  791  LEU   B CD1 
6143  C  CD2 . LEU   B 487 ? 1.1312 1.1169 1.1309 0.0577  -0.1029 0.0318  791  LEU   B CD2 
6144  N  N   . LEU   B 488 ? 1.1539 1.1546 1.1644 0.0662  -0.1061 0.0258  792  LEU   B N   
6145  C  CA  . LEU   B 488 ? 1.1428 1.1367 1.1482 0.0711  -0.1084 0.0244  792  LEU   B CA  
6146  C  C   . LEU   B 488 ? 1.1225 1.1043 1.1236 0.0694  -0.1099 0.0236  792  LEU   B C   
6147  O  O   . LEU   B 488 ? 1.0972 1.0762 1.1020 0.0635  -0.1095 0.0226  792  LEU   B O   
6148  C  CB  . LEU   B 488 ? 1.1165 1.1125 1.1251 0.0715  -0.1092 0.0219  792  LEU   B CB  
6149  C  CG  . LEU   B 488 ? 1.0065 1.0138 1.0190 0.0735  -0.1073 0.0227  792  LEU   B CG  
6150  C  CD1 . LEU   B 488 ? 0.9815 0.9888 0.9953 0.0746  -0.1082 0.0202  792  LEU   B CD1 
6151  C  CD2 . LEU   B 488 ? 1.0513 1.0609 1.0597 0.0798  -0.1067 0.0250  792  LEU   B CD2 
6152  N  N   . ILE   B 489 ? 1.1907 1.1654 1.1843 0.0745  -0.1116 0.0241  793  ILE   B N   
6153  C  CA  . ILE   B 489 ? 1.2166 1.1788 1.2054 0.0737  -0.1134 0.0231  793  ILE   B CA  
6154  C  C   . ILE   B 489 ? 1.2357 1.1927 1.2216 0.0778  -0.1163 0.0205  793  ILE   B C   
6155  O  O   . ILE   B 489 ? 1.2332 1.1898 1.2137 0.0845  -0.1171 0.0210  793  ILE   B O   
6156  C  CB  . ILE   B 489 ? 1.2042 1.1609 1.1857 0.0766  -0.1134 0.0255  793  ILE   B CB  
6157  C  CG1 . ILE   B 489 ? 1.1604 1.1246 1.1437 0.0750  -0.1110 0.0282  793  ILE   B CG1 
6158  C  CG2 . ILE   B 489 ? 1.2789 1.2237 1.2575 0.0732  -0.1142 0.0249  793  ILE   B CG2 
6159  C  CD1 . ILE   B 489 ? 1.1585 1.1219 1.1455 0.0678  -0.1091 0.0285  793  ILE   B CD1 
6160  N  N   . ILE   B 490 ? 1.2346 1.1874 1.2242 0.0741  -0.1179 0.0177  794  ILE   B N   
6161  C  CA  . ILE   B 490 ? 1.2438 1.1922 1.2313 0.0776  -0.1210 0.0148  794  ILE   B CA  
6162  C  C   . ILE   B 490 ? 1.2535 1.1886 1.2373 0.0769  -0.1242 0.0129  794  ILE   B C   
6163  O  O   . ILE   B 490 ? 1.2511 1.1826 1.2395 0.0708  -0.1239 0.0124  794  ILE   B O   
6164  C  CB  . ILE   B 490 ? 1.2399 1.1943 1.2351 0.0743  -0.1212 0.0125  794  ILE   B CB  
6165  C  CG1 . ILE   B 490 ? 1.2410 1.2083 1.2413 0.0730  -0.1177 0.0146  794  ILE   B CG1 
6166  C  CG2 . ILE   B 490 ? 1.2444 1.1951 1.2355 0.0796  -0.1244 0.0100  794  ILE   B CG2 
6167  C  CD1 . ILE   B 490 ? 1.1963 1.1695 1.2043 0.0692  -0.1176 0.0126  794  ILE   B CD1 
6168  N  N   . ASP   B 491 ? 1.2436 1.1715 1.2195 0.0832  -0.1270 0.0119  795  ASP   B N   
6169  C  CA  . ASP   B 491 ? 1.2646 1.1791 1.2360 0.0833  -0.1303 0.0102  795  ASP   B CA  
6170  C  C   . ASP   B 491 ? 1.2606 1.1711 1.2380 0.0791  -0.1334 0.0064  795  ASP   B C   
6171  O  O   . ASP   B 491 ? 1.2876 1.2025 1.2678 0.0801  -0.1346 0.0044  795  ASP   B O   
6172  C  CB  . ASP   B 491 ? 1.2944 1.2022 1.2553 0.0915  -0.1326 0.0099  795  ASP   B CB  
6173  C  CG  . ASP   B 491 ? 1.3955 1.2890 1.3517 0.0919  -0.1367 0.0075  795  ASP   B CG  
6174  O  OD1 . ASP   B 491 ? 1.4152 1.3031 1.3727 0.0875  -0.1363 0.0082  795  ASP   B OD1 
6175  O  OD2 . ASP   B 491 ? 1.4347 1.3222 1.3859 0.0965  -0.1403 0.0049  795  ASP   B OD2 
6176  N  N   . GLN   B 492 ? 1.2668 1.1687 1.2464 0.0745  -0.1347 0.0053  796  GLN   B N   
6177  C  CA  . GLN   B 492 ? 1.2723 1.1713 1.2598 0.0697  -0.1375 0.0018  796  GLN   B CA  
6178  C  C   . GLN   B 492 ? 1.2851 1.1751 1.2678 0.0743  -0.1433 -0.0020 796  GLN   B C   
6179  O  O   . GLN   B 492 ? 1.2435 1.1312 1.2328 0.0711  -0.1466 -0.0054 796  GLN   B O   
6180  C  CB  . GLN   B 492 ? 1.2612 1.1549 1.2545 0.0627  -0.1363 0.0020  796  GLN   B CB  
6181  C  CG  . GLN   B 492 ? 1.3062 1.1877 1.2919 0.0643  -0.1374 0.0028  796  GLN   B CG  
6182  C  CD  . GLN   B 492 ? 1.3367 1.2114 1.3295 0.0571  -0.1369 0.0021  796  GLN   B CD  
6183  O  OE1 . GLN   B 492 ? 1.3272 1.2048 1.3239 0.0521  -0.1323 0.0046  796  GLN   B OE1 
6184  N  NE2 . GLN   B 492 ? 1.3686 1.2342 1.3634 0.0563  -0.1417 -0.0015 796  GLN   B NE2 
6185  N  N   . HIS   B 493 ? 1.3009 1.1859 1.2723 0.0819  -0.1448 -0.0015 797  HIS   B N   
6186  C  CA  . HIS   B 493 ? 1.2790 1.1542 1.2440 0.0869  -0.1503 -0.0049 797  HIS   B CA  
6187  C  C   . HIS   B 493 ? 1.3025 1.1820 1.2612 0.0940  -0.1505 -0.0051 797  HIS   B C   
6188  O  O   . HIS   B 493 ? 1.3855 1.2629 1.3445 0.0955  -0.1541 -0.0084 797  HIS   B O   
6189  C  CB  . HIS   B 493 ? 1.2927 1.1554 1.2483 0.0904  -0.1523 -0.0046 797  HIS   B CB  
6190  C  CG  . HIS   B 493 ? 1.2722 1.1300 1.2322 0.0841  -0.1513 -0.0036 797  HIS   B CG  
6191  N  ND1 . HIS   B 493 ? 1.2886 1.1478 1.2457 0.0837  -0.1470 0.0003  797  HIS   B ND1 
6192  C  CD2 . HIS   B 493 ? 1.2645 1.1156 1.2316 0.0781  -0.1537 -0.0061 797  HIS   B CD2 
6193  C  CE1 . HIS   B 493 ? 1.3616 1.2146 1.3228 0.0778  -0.1466 0.0004  797  HIS   B CE1 
6194  N  NE2 . HIS   B 493 ? 1.3255 1.1738 1.2934 0.0742  -0.1504 -0.0034 797  HIS   B NE2 
6195  N  N   . THR   B 494 ? 1.2863 1.1706 1.2389 0.0990  -0.1468 -0.0017 798  THR   B N   
6196  C  CA  . THR   B 494 ? 1.3189 1.2078 1.2663 0.1056  -0.1460 -0.0015 798  THR   B CA  
6197  C  C   . THR   B 494 ? 1.2705 1.1730 1.2264 0.1024  -0.1425 -0.0005 798  THR   B C   
6198  O  O   . THR   B 494 ? 1.2727 1.1783 1.2264 0.1064  -0.1425 -0.0014 798  THR   B O   
6199  C  CB  . THR   B 494 ? 1.3598 1.2487 1.2984 0.1123  -0.1432 0.0017  798  THR   B CB  
6200  O  OG1 . THR   B 494 ? 1.3924 1.2923 1.3366 0.1094  -0.1383 0.0054  798  THR   B OG1 
6201  C  CG2 . THR   B 494 ? 1.4232 1.2994 1.3543 0.1145  -0.1460 0.0013  798  THR   B CG2 
6202  N  N   . PHE   B 495 ? 1.2848 1.1948 1.2498 0.0954  -0.1395 0.0012  799  PHE   B N   
6203  C  CA  . PHE   B 495 ? 1.2421 1.1654 1.2151 0.0922  -0.1358 0.0025  799  PHE   B CA  
6204  C  C   . PHE   B 495 ? 1.2332 1.1647 1.2024 0.0976  -0.1319 0.0057  799  PHE   B C   
6205  O  O   . PHE   B 495 ? 1.1504 1.0909 1.1231 0.0979  -0.1297 0.0061  799  PHE   B O   
6206  C  CB  . PHE   B 495 ? 1.1687 1.0934 1.1467 0.0903  -0.1383 -0.0008 799  PHE   B CB  
6207  C  CG  . PHE   B 495 ? 1.1767 1.0997 1.1640 0.0826  -0.1400 -0.0029 799  PHE   B CG  
6208  C  CD1 . PHE   B 495 ? 1.1688 1.1000 1.1648 0.0760  -0.1361 -0.0009 799  PHE   B CD1 
6209  C  CD2 . PHE   B 495 ? 1.2588 1.1715 1.2460 0.0820  -0.1454 -0.0067 799  PHE   B CD2 
6210  C  CE1 . PHE   B 495 ? 1.1454 1.0752 1.1505 0.0688  -0.1369 -0.0025 799  PHE   B CE1 
6211  C  CE2 . PHE   B 495 ? 1.3156 1.2272 1.3129 0.0745  -0.1466 -0.0085 799  PHE   B CE2 
6212  C  CZ  . PHE   B 495 ? 1.2641 1.1844 1.2705 0.0679  -0.1420 -0.0062 799  PHE   B CZ  
6213  N  N   . GLU   B 496 ? 1.2521 1.1803 1.2145 0.1018  -0.1310 0.0079  800  GLU   B N   
6214  C  CA  . GLU   B 496 ? 1.2643 1.2009 1.2250 0.1063  -0.1271 0.0111  800  GLU   B CA  
6215  C  C   . GLU   B 496 ? 1.2962 1.2431 1.2647 0.1010  -0.1235 0.0139  800  GLU   B C   
6216  O  O   . GLU   B 496 ? 1.2830 1.2277 1.2546 0.0955  -0.1237 0.0142  800  GLU   B O   
6217  C  CB  . GLU   B 496 ? 1.3126 1.2424 1.2639 0.1129  -0.1274 0.0125  800  GLU   B CB  
6218  C  CG  . GLU   B 496 ? 1.3947 1.3174 1.3368 0.1208  -0.1293 0.0110  800  GLU   B CG  
6219  C  CD  . GLU   B 496 ? 1.5648 1.4824 1.4982 0.1276  -0.1287 0.0128  800  GLU   B CD  
6220  O  OE1 . GLU   B 496 ? 1.5564 1.4680 1.4877 0.1261  -0.1300 0.0135  800  GLU   B OE1 
6221  O  OE2 . GLU   B 496 ? 1.6153 1.5349 1.5441 0.1346  -0.1268 0.0138  800  GLU   B OE2 
6222  N  N   . VAL   B 497 ? 1.3499 1.3077 1.3213 0.1029  -0.1202 0.0159  801  VAL   B N   
6223  C  CA  . VAL   B 497 ? 1.3567 1.3245 1.3343 0.0993  -0.1170 0.0187  801  VAL   B CA  
6224  C  C   . VAL   B 497 ? 1.3842 1.3498 1.3568 0.1031  -0.1165 0.0212  801  VAL   B C   
6225  O  O   . VAL   B 497 ? 1.3719 1.3420 1.3425 0.1088  -0.1148 0.0230  801  VAL   B O   
6226  C  CB  . VAL   B 497 ? 1.3572 1.3372 1.3402 0.1002  -0.1139 0.0198  801  VAL   B CB  
6227  C  CG1 . VAL   B 497 ? 1.3466 1.3363 1.3371 0.0950  -0.1114 0.0220  801  VAL   B CG1 
6228  C  CG2 . VAL   B 497 ? 1.3409 1.3207 1.3259 0.0989  -0.1149 0.0171  801  VAL   B CG2 
6229  N  N   . LEU   B 498 ? 1.3199 1.2784 1.2905 0.1000  -0.1178 0.0214  802  LEU   B N   
6230  C  CA  . LEU   B 498 ? 1.2631 1.2176 1.2280 0.1034  -0.1179 0.0235  802  LEU   B CA  
6231  C  C   . LEU   B 498 ? 1.2047 1.1695 1.1736 0.1030  -0.1153 0.0266  802  LEU   B C   
6232  O  O   . LEU   B 498 ? 1.2118 1.1811 1.1793 0.1088  -0.1143 0.0282  802  LEU   B O   
6233  C  CB  . LEU   B 498 ? 1.3168 1.2602 1.2786 0.0996  -0.1198 0.0229  802  LEU   B CB  
6234  C  CG  . LEU   B 498 ? 1.2951 1.2281 1.2548 0.0983  -0.1229 0.0196  802  LEU   B CG  
6235  C  CD1 . LEU   B 498 ? 1.3070 1.2303 1.2653 0.0938  -0.1240 0.0195  802  LEU   B CD1 
6236  C  CD2 . LEU   B 498 ? 1.2372 1.1638 1.1889 0.1059  -0.1251 0.0184  802  LEU   B CD2 
6237  N  N   . HIS   B 499 ? 1.1999 1.1684 1.1741 0.0965  -0.1142 0.0272  803  HIS   B N   
6238  C  CA  . HIS   B 499 ? 1.2105 1.1887 1.1887 0.0959  -0.1122 0.0298  803  HIS   B CA  
6239  C  C   . HIS   B 499 ? 1.1845 1.1736 1.1715 0.0916  -0.1102 0.0295  803  HIS   B C   
6240  O  O   . HIS   B 499 ? 1.1675 1.1558 1.1578 0.0873  -0.1103 0.0275  803  HIS   B O   
6241  C  CB  . HIS   B 499 ? 1.2490 1.2223 1.2246 0.0926  -0.1124 0.0313  803  HIS   B CB  
6242  C  CG  . HIS   B 499 ? 1.2768 1.2563 1.2525 0.0952  -0.1118 0.0339  803  HIS   B CG  
6243  N  ND1 . HIS   B 499 ? 1.3346 1.3096 1.3038 0.1009  -0.1131 0.0353  803  HIS   B ND1 
6244  C  CD2 . HIS   B 499 ? 1.2713 1.2609 1.2529 0.0931  -0.1105 0.0353  803  HIS   B CD2 
6245  C  CE1 . HIS   B 499 ? 1.3191 1.3015 1.2907 0.1022  -0.1127 0.0373  803  HIS   B CE1 
6246  N  NE2 . HIS   B 499 ? 1.2562 1.2473 1.2352 0.0974  -0.1112 0.0373  803  HIS   B NE2 
6247  N  N   . ALA   B 500 ? 1.1712 1.1704 1.1622 0.0929  -0.1087 0.0315  804  ALA   B N   
6248  C  CA  . ALA   B 500 ? 1.1395 1.1497 1.1388 0.0891  -0.1067 0.0317  804  ALA   B CA  
6249  C  C   . ALA   B 500 ? 1.1396 1.1563 1.1416 0.0882  -0.1061 0.0341  804  ALA   B C   
6250  O  O   . ALA   B 500 ? 1.1756 1.1997 1.1802 0.0922  -0.1055 0.0355  804  ALA   B O   
6251  C  CB  . ALA   B 500 ? 1.1658 1.1828 1.1683 0.0929  -0.1054 0.0313  804  ALA   B CB  
6252  N  N   . HIS   B 501 ? 1.1294 1.1427 1.1307 0.0831  -0.1062 0.0344  805  HIS   B N   
6253  C  CA  . HIS   B 501 ? 1.1361 1.1555 1.1400 0.0813  -0.1058 0.0362  805  HIS   B CA  
6254  C  C   . HIS   B 501 ? 1.1297 1.1603 1.1422 0.0783  -0.1041 0.0360  805  HIS   B C   
6255  O  O   . HIS   B 501 ? 1.0810 1.1115 1.0964 0.0735  -0.1031 0.0345  805  HIS   B O   
6256  C  CB  . HIS   B 501 ? 1.1451 1.1569 1.1449 0.0766  -0.1060 0.0366  805  HIS   B CB  
6257  C  CG  . HIS   B 501 ? 1.1245 1.1408 1.1253 0.0751  -0.1060 0.0384  805  HIS   B CG  
6258  N  ND1 . HIS   B 501 ? 1.1395 1.1591 1.1391 0.0798  -0.1075 0.0400  805  HIS   B ND1 
6259  C  CD2 . HIS   B 501 ? 1.1196 1.1375 1.1224 0.0696  -0.1048 0.0386  805  HIS   B CD2 
6260  C  CE1 . HIS   B 501 ? 1.1673 1.1900 1.1678 0.0773  -0.1077 0.0411  805  HIS   B CE1 
6261  N  NE2 . HIS   B 501 ? 1.1527 1.1742 1.1548 0.0712  -0.1059 0.0404  805  HIS   B NE2 
6262  N  N   . GLN   B 502 ? 1.1421 1.1822 1.1591 0.0810  -0.1038 0.0373  806  GLN   B N   
6263  C  CA  . GLN   B 502 ? 1.1048 1.1554 1.1300 0.0780  -0.1023 0.0373  806  GLN   B CA  
6264  C  C   . GLN   B 502 ? 1.0538 1.1064 1.0798 0.0743  -0.1029 0.0385  806  GLN   B C   
6265  O  O   . GLN   B 502 ? 1.0834 1.1351 1.1067 0.0769  -0.1046 0.0399  806  GLN   B O   
6266  C  CB  . GLN   B 502 ? 1.1347 1.1948 1.1654 0.0827  -0.1014 0.0382  806  GLN   B CB  
6267  C  CG  . GLN   B 502 ? 1.1484 1.2194 1.1877 0.0795  -0.1000 0.0384  806  GLN   B CG  
6268  C  CD  . GLN   B 502 ? 1.1405 1.2213 1.1861 0.0836  -0.0996 0.0400  806  GLN   B CD  
6269  O  OE1 . GLN   B 502 ? 1.0867 1.1722 1.1355 0.0830  -0.1009 0.0411  806  GLN   B OE1 
6270  N  NE2 . GLN   B 502 ? 1.1523 1.2360 1.2000 0.0879  -0.0976 0.0399  806  GLN   B NE2 
6271  N  N   . PHE   B 503 ? 1.0228 1.0776 1.0521 0.0685  -0.1016 0.0377  807  PHE   B N   
6272  C  CA  . PHE   B 503 ? 1.0510 1.1061 1.0798 0.0648  -0.1020 0.0386  807  PHE   B CA  
6273  C  C   . PHE   B 503 ? 1.1118 1.1775 1.1467 0.0660  -0.1027 0.0397  807  PHE   B C   
6274  O  O   . PHE   B 503 ? 1.1282 1.2011 1.1682 0.0698  -0.1025 0.0400  807  PHE   B O   
6275  C  CB  . PHE   B 503 ? 1.0266 1.0802 1.0569 0.0584  -0.1001 0.0374  807  PHE   B CB  
6276  C  CG  . PHE   B 503 ? 1.0316 1.0738 1.0558 0.0561  -0.0998 0.0368  807  PHE   B CG  
6277  C  CD1 . PHE   B 503 ? 1.0601 1.0980 1.0841 0.0564  -0.0995 0.0352  807  PHE   B CD1 
6278  C  CD2 . PHE   B 503 ? 1.0850 1.1204 1.1036 0.0539  -0.0997 0.0379  807  PHE   B CD2 
6279  C  CE1 . PHE   B 503 ? 1.0957 1.1230 1.1151 0.0541  -0.0992 0.0345  807  PHE   B CE1 
6280  C  CE2 . PHE   B 503 ? 1.0993 1.1239 1.1127 0.0516  -0.0989 0.0375  807  PHE   B CE2 
6281  C  CZ  . PHE   B 503 ? 1.0797 1.1006 1.0942 0.0516  -0.0987 0.0358  807  PHE   B CZ  
6282  N  N   . LEU   B 504 ? 1.1308 1.1971 1.1653 0.0627  -0.1032 0.0403  808  LEU   B N   
6283  C  CA  . LEU   B 504 ? 1.0978 1.1732 1.1378 0.0634  -0.1046 0.0412  808  LEU   B CA  
6284  C  C   . LEU   B 504 ? 1.1019 1.1875 1.1512 0.0615  -0.1027 0.0405  808  LEU   B C   
6285  O  O   . LEU   B 504 ? 1.1799 1.2652 1.2307 0.0587  -0.1005 0.0393  808  LEU   B O   
6286  C  CB  . LEU   B 504 ? 1.1106 1.1827 1.1466 0.0601  -0.1058 0.0417  808  LEU   B CB  
6287  C  CG  . LEU   B 504 ? 1.1717 1.2330 1.1976 0.0619  -0.1076 0.0427  808  LEU   B CG  
6288  C  CD1 . LEU   B 504 ? 1.2551 1.3116 1.2759 0.0579  -0.1077 0.0430  808  LEU   B CD1 
6289  C  CD2 . LEU   B 504 ? 1.2456 1.3094 1.2716 0.0679  -0.1108 0.0437  808  LEU   B CD2 
6290  N  N   . GLN   B 505 ? 1.0785 1.1734 1.1345 0.0632  -0.1038 0.0413  809  GLN   B N   
6291  C  CA  . GLN   B 505 ? 1.0874 1.1919 1.1523 0.0610  -0.1020 0.0408  809  GLN   B CA  
6292  C  C   . GLN   B 505 ? 1.1227 1.2270 1.1875 0.0551  -0.1017 0.0402  809  GLN   B C   
6293  O  O   . GLN   B 505 ? 1.1868 1.2865 1.2466 0.0536  -0.1035 0.0407  809  GLN   B O   
6294  C  CB  . GLN   B 505 ? 1.1201 1.2344 1.1932 0.0643  -0.1031 0.0418  809  GLN   B CB  
6295  C  CG  . GLN   B 505 ? 1.2125 1.3364 1.2949 0.0629  -0.1006 0.0415  809  GLN   B CG  
6296  C  CD  . GLN   B 505 ? 1.2887 1.4223 1.3804 0.0665  -0.1010 0.0427  809  GLN   B CD  
6297  O  OE1 . GLN   B 505 ? 1.2632 1.3990 1.3567 0.0678  -0.1042 0.0434  809  GLN   B OE1 
6298  N  NE2 . GLN   B 505 ? 1.3281 1.4673 1.4256 0.0683  -0.0978 0.0428  809  GLN   B NE2 
6299  N  N   . ASN   B 506 ? 1.1131 1.2219 1.1828 0.0521  -0.0992 0.0393  810  ASN   B N   
6300  C  CA  . ASN   B 506 ? 1.1143 1.2224 1.1838 0.0465  -0.0983 0.0385  810  ASN   B CA  
6301  C  C   . ASN   B 506 ? 1.1091 1.2064 1.1701 0.0440  -0.0980 0.0381  810  ASN   B C   
6302  O  O   . ASN   B 506 ? 1.1377 1.2322 1.1962 0.0402  -0.0978 0.0380  810  ASN   B O   
6303  C  CB  . ASN   B 506 ? 1.1623 1.2755 1.2348 0.0450  -0.1003 0.0391  810  ASN   B CB  
6304  C  CG  . ASN   B 506 ? 1.1577 1.2819 1.2401 0.0464  -0.1002 0.0394  810  ASN   B CG  
6305  O  OD1 . ASN   B 506 ? 1.1915 1.3193 1.2775 0.0504  -0.0996 0.0399  810  ASN   B OD1 
6306  N  ND2 . ASN   B 506 ? 1.1771 1.3066 1.2640 0.0431  -0.1004 0.0392  810  ASN   B ND2 
6307  N  N   . GLU   B 507 ? 1.1068 1.1975 1.1634 0.0463  -0.0977 0.0379  811  GLU   B N   
6308  C  CA  . GLU   B 507 ? 1.0891 1.1694 1.1386 0.0440  -0.0971 0.0375  811  GLU   B CA  
6309  C  C   . GLU   B 507 ? 1.0981 1.1762 1.1491 0.0423  -0.0950 0.0358  811  GLU   B C   
6310  O  O   . GLU   B 507 ? 1.0631 1.1424 1.1156 0.0456  -0.0951 0.0353  811  GLU   B O   
6311  C  CB  . GLU   B 507 ? 1.0933 1.1661 1.1356 0.0479  -0.0989 0.0385  811  GLU   B CB  
6312  C  CG  . GLU   B 507 ? 1.1457 1.2074 1.1814 0.0459  -0.0978 0.0381  811  GLU   B CG  
6313  C  CD  . GLU   B 507 ? 1.1244 1.1773 1.1514 0.0480  -0.0994 0.0394  811  GLU   B CD  
6314  O  OE1 . GLU   B 507 ? 1.1422 1.1940 1.1669 0.0530  -0.1013 0.0401  811  GLU   B OE1 
6315  O  OE2 . GLU   B 507 ? 1.0744 1.1210 1.0964 0.0448  -0.0985 0.0399  811  GLU   B OE2 
6316  N  N   . TYR   B 508 ? 1.1407 1.2155 1.1914 0.0374  -0.0933 0.0349  812  TYR   B N   
6317  C  CA  . TYR   B 508 ? 1.1117 1.1841 1.1646 0.0351  -0.0917 0.0331  812  TYR   B CA  
6318  C  C   . TYR   B 508 ? 1.0984 1.1600 1.1457 0.0334  -0.0912 0.0329  812  TYR   B C   
6319  O  O   . TYR   B 508 ? 1.1278 1.1850 1.1715 0.0307  -0.0903 0.0338  812  TYR   B O   
6320  C  CB  . TYR   B 508 ? 1.1277 1.2054 1.1862 0.0305  -0.0899 0.0321  812  TYR   B CB  
6321  C  CG  . TYR   B 508 ? 1.1398 1.2184 1.2027 0.0292  -0.0889 0.0300  812  TYR   B CG  
6322  C  CD1 . TYR   B 508 ? 1.1448 1.2162 1.2067 0.0267  -0.0882 0.0286  812  TYR   B CD1 
6323  C  CD2 . TYR   B 508 ? 1.1267 1.2129 1.1948 0.0306  -0.0888 0.0293  812  TYR   B CD2 
6324  C  CE1 . TYR   B 508 ? 1.1505 1.2224 1.2167 0.0257  -0.0880 0.0264  812  TYR   B CE1 
6325  C  CE2 . TYR   B 508 ? 1.1290 1.2151 1.2002 0.0298  -0.0884 0.0272  812  TYR   B CE2 
6326  C  CZ  . TYR   B 508 ? 1.1269 1.2058 1.1971 0.0274  -0.0883 0.0256  812  TYR   B CZ  
6327  O  OH  . TYR   B 508 ? 1.1049 1.1830 1.1783 0.0267  -0.0885 0.0233  812  TYR   B OH  
6328  N  N   . ALA   B 509 ? 1.0245 1.0811 1.0705 0.0353  -0.0918 0.0319  813  ALA   B N   
6329  C  CA  . ALA   B 509 ? 1.0224 1.0685 1.0639 0.0335  -0.0913 0.0316  813  ALA   B CA  
6330  C  C   . ALA   B 509 ? 1.0078 1.0528 1.0540 0.0283  -0.0893 0.0299  813  ALA   B C   
6331  O  O   . ALA   B 509 ? 1.0914 1.1420 1.1436 0.0276  -0.0892 0.0282  813  ALA   B O   
6332  C  CB  . ALA   B 509 ? 0.9909 1.0315 1.0292 0.0376  -0.0932 0.0311  813  ALA   B CB  
6333  N  N   . LEU   B 510 ? 0.9909 1.0287 1.0347 0.0247  -0.0874 0.0303  814  LEU   B N   
6334  C  CA  . LEU   B 510 ? 0.9693 1.0065 1.0187 0.0196  -0.0851 0.0287  814  LEU   B CA  
6335  C  C   . LEU   B 510 ? 0.9807 1.0085 1.0296 0.0181  -0.0847 0.0277  814  LEU   B C   
6336  O  O   . LEU   B 510 ? 1.0308 1.0588 1.0857 0.0165  -0.0851 0.0254  814  LEU   B O   
6337  C  CB  . LEU   B 510 ? 1.0205 1.0585 1.0696 0.0157  -0.0822 0.0299  814  LEU   B CB  
6338  C  CG  . LEU   B 510 ? 1.0296 1.0771 1.0806 0.0162  -0.0826 0.0305  814  LEU   B CG  
6339  C  CD1 . LEU   B 510 ? 1.0561 1.1027 1.1059 0.0122  -0.0798 0.0314  814  LEU   B CD1 
6340  C  CD2 . LEU   B 510 ? 1.0153 1.0708 1.0739 0.0163  -0.0834 0.0285  814  LEU   B CD2 
6341  N  N   . SER   B 511 ? 0.9793 0.9985 1.0214 0.0185  -0.0841 0.0293  815  SER   B N   
6342  C  CA  . SER   B 511 ? 1.0054 1.0151 1.0474 0.0160  -0.0829 0.0287  815  SER   B CA  
6343  C  C   . SER   B 511 ? 1.0384 1.0406 1.0734 0.0201  -0.0851 0.0294  815  SER   B C   
6344  O  O   . SER   B 511 ? 1.0882 1.0903 1.1165 0.0239  -0.0864 0.0312  815  SER   B O   
6345  C  CB  . SER   B 511 ? 1.0976 1.1024 1.1378 0.0116  -0.0787 0.0302  815  SER   B CB  
6346  O  OG  . SER   B 511 ? 1.1056 1.1114 1.1387 0.0134  -0.0784 0.0326  815  SER   B OG  
6347  N  N   . LEU   B 512 ? 1.0806 1.0763 1.1176 0.0192  -0.0858 0.0278  816  LEU   B N   
6348  C  CA  . LEU   B 512 ? 1.0914 1.0791 1.1219 0.0230  -0.0882 0.0280  816  LEU   B CA  
6349  C  C   . LEU   B 512 ? 1.1415 1.1191 1.1734 0.0195  -0.0869 0.0272  816  LEU   B C   
6350  O  O   . LEU   B 512 ? 1.1782 1.1565 1.2184 0.0158  -0.0863 0.0250  816  LEU   B O   
6351  C  CB  . LEU   B 512 ? 1.0081 1.0000 1.0399 0.0276  -0.0921 0.0263  816  LEU   B CB  
6352  C  CG  . LEU   B 512 ? 1.0269 1.0109 1.0529 0.0318  -0.0949 0.0259  816  LEU   B CG  
6353  C  CD1 . LEU   B 512 ? 1.0563 1.0397 1.0738 0.0367  -0.0957 0.0284  816  LEU   B CD1 
6354  C  CD2 . LEU   B 512 ? 1.0351 1.0224 1.0647 0.0345  -0.0979 0.0233  816  LEU   B CD2 
6355  N  N   . VAL   B 513 ? 1.1616 1.1294 1.1855 0.0207  -0.0864 0.0290  817  VAL   B N   
6356  C  CA  . VAL   B 513 ? 1.2188 1.1761 1.2438 0.0172  -0.0847 0.0285  817  VAL   B CA  
6357  C  C   . VAL   B 513 ? 1.2288 1.1763 1.2443 0.0212  -0.0866 0.0297  817  VAL   B C   
6358  O  O   . VAL   B 513 ? 1.2337 1.1812 1.2407 0.0254  -0.0875 0.0318  817  VAL   B O   
6359  C  CB  . VAL   B 513 ? 1.2119 1.1663 1.2384 0.0116  -0.0792 0.0301  817  VAL   B CB  
6360  C  CG1 . VAL   B 513 ? 1.1961 1.1490 1.2128 0.0132  -0.0772 0.0333  817  VAL   B CG1 
6361  C  CG2 . VAL   B 513 ? 1.2680 1.2117 1.2972 0.0076  -0.0768 0.0297  817  VAL   B CG2 
6362  N  N   . SER   B 514 ? 1.2783 1.2180 1.2958 0.0202  -0.0878 0.0281  818  SER   B N   
6363  C  CA  . SER   B 514 ? 1.3117 1.2406 1.3207 0.0233  -0.0894 0.0289  818  SER   B CA  
6364  C  C   . SER   B 514 ? 1.3573 1.2755 1.3662 0.0184  -0.0853 0.0300  818  SER   B C   
6365  O  O   . SER   B 514 ? 1.4698 1.3863 1.4879 0.0137  -0.0842 0.0281  818  SER   B O   
6366  C  CB  . SER   B 514 ? 1.3046 1.2319 1.3155 0.0263  -0.0942 0.0260  818  SER   B CB  
6367  O  OG  . SER   B 514 ? 1.3305 1.2466 1.3333 0.0292  -0.0958 0.0267  818  SER   B OG  
6368  N  N   . CYS   B 515 ? 1.3662 1.2772 1.3651 0.0194  -0.0830 0.0330  819  CYS   B N   
6369  C  CA  . CYS   B 515 ? 1.4212 1.3207 1.4184 0.0152  -0.0786 0.0345  819  CYS   B CA  
6370  C  C   . CYS   B 515 ? 1.5036 1.3928 1.4868 0.0190  -0.0785 0.0373  819  CYS   B C   
6371  O  O   . CYS   B 515 ? 1.4815 1.3743 1.4570 0.0241  -0.0808 0.0386  819  CYS   B O   
6372  C  CB  . CYS   B 515 ? 1.4159 1.3180 1.4175 0.0098  -0.0729 0.0357  819  CYS   B CB  
6373  S  SG  . CYS   B 515 ? 1.4064 1.3101 1.3969 0.0120  -0.0704 0.0392  819  CYS   B SG  
6374  N  N   . LYS   B 516 ? 1.5179 1.3944 1.4984 0.0167  -0.0760 0.0382  820  LYS   B N   
6375  C  CA  . LYS   B 516 ? 1.5521 1.4173 1.5190 0.0191  -0.0743 0.0413  820  LYS   B CA  
6376  C  C   . LYS   B 516 ? 1.5178 1.3813 1.4816 0.0158  -0.0684 0.0439  820  LYS   B C   
6377  O  O   . LYS   B 516 ? 1.4630 1.3277 1.4355 0.0100  -0.0640 0.0435  820  LYS   B O   
6378  C  CB  . LYS   B 516 ? 1.4685 1.3198 1.4329 0.0182  -0.0739 0.0413  820  LYS   B CB  
6379  N  N   . LEU   B 517 ? 1.4603 1.3209 1.4117 0.0197  -0.0685 0.0466  821  LEU   B N   
6380  C  CA  . LEU   B 517 ? 1.5183 1.3779 1.4653 0.0177  -0.0637 0.0489  821  LEU   B CA  
6381  C  C   . LEU   B 517 ? 1.6589 1.5031 1.5916 0.0190  -0.0608 0.0521  821  LEU   B C   
6382  O  O   . LEU   B 517 ? 1.6960 1.5340 1.6194 0.0239  -0.0643 0.0528  821  LEU   B O   
6383  C  CB  . LEU   B 517 ? 1.5111 1.3825 1.4563 0.0211  -0.0666 0.0491  821  LEU   B CB  
6384  C  CG  . LEU   B 517 ? 1.4363 1.3211 1.3939 0.0176  -0.0659 0.0472  821  LEU   B CG  
6385  C  CD1 . LEU   B 517 ? 1.3383 1.2316 1.2921 0.0203  -0.0675 0.0481  821  LEU   B CD1 
6386  C  CD2 . LEU   B 517 ? 1.4376 1.3184 1.4012 0.0109  -0.0594 0.0475  821  LEU   B CD2 
6387  N  N   . GLY   B 518 ? 1.8889 1.7264 1.8197 0.0147  -0.0542 0.0540  822  GLY   B N   
6388  C  CA  . GLY   B 518 ? 1.9119 1.7342 1.8280 0.0158  -0.0505 0.0574  822  GLY   B CA  
6389  C  C   . GLY   B 518 ? 1.9144 1.7233 1.8270 0.0156  -0.0497 0.0579  822  GLY   B C   
6390  O  O   . GLY   B 518 ? 1.9175 1.7255 1.8410 0.0114  -0.0484 0.0561  822  GLY   B O   
6391  N  N   . LYS   B 519 ? 1.7544 1.5521 1.6515 0.0203  -0.0508 0.0602  823  LYS   B N   
6392  C  CA  . LYS   B 519 ? 1.7152 1.5003 1.6078 0.0211  -0.0511 0.0606  823  LYS   B CA  
6393  C  C   . LYS   B 519 ? 1.6778 1.4676 1.5702 0.0266  -0.0589 0.0586  823  LYS   B C   
6394  O  O   . LYS   B 519 ? 1.7065 1.4889 1.5996 0.0266  -0.0601 0.0578  823  LYS   B O   
6395  C  CB  . LYS   B 519 ? 1.6869 1.4550 1.5621 0.0230  -0.0473 0.0643  823  LYS   B CB  
6396  C  CG  . LYS   B 519 ? 1.6750 1.4373 1.5481 0.0184  -0.0392 0.0666  823  LYS   B CG  
6397  C  CD  . LYS   B 519 ? 1.7492 1.5162 1.6395 0.0108  -0.0343 0.0650  823  LYS   B CD  
6398  C  CE  . LYS   B 519 ? 1.7240 1.4821 1.6203 0.0077  -0.0329 0.0642  823  LYS   B CE  
6399  N  NZ  . LYS   B 519 ? 1.7101 1.4739 1.6245 0.0004  -0.0287 0.0624  823  LYS   B NZ  
6400  N  N   . ASP   B 520 ? 1.6360 1.4379 1.5280 0.0312  -0.0640 0.0578  824  ASP   B N   
6401  C  CA  . ASP   B 520 ? 1.5766 1.3855 1.4696 0.0366  -0.0711 0.0559  824  ASP   B CA  
6402  C  C   . ASP   B 520 ? 1.5507 1.3612 1.4551 0.0342  -0.0726 0.0530  824  ASP   B C   
6403  O  O   . ASP   B 520 ? 1.5619 1.3763 1.4781 0.0283  -0.0696 0.0515  824  ASP   B O   
6404  C  CB  . ASP   B 520 ? 1.5405 1.3652 1.4374 0.0392  -0.0744 0.0550  824  ASP   B CB  
6405  C  CG  . ASP   B 520 ? 1.5330 1.3647 1.4295 0.0456  -0.0811 0.0537  824  ASP   B CG  
6406  O  OD1 . ASP   B 520 ? 1.5828 1.4206 1.4886 0.0453  -0.0835 0.0511  824  ASP   B OD1 
6407  O  OD2 . ASP   B 520 ? 1.5662 1.3971 1.4530 0.0512  -0.0839 0.0551  824  ASP   B OD2 
6408  N  N   . PRO   B 521 ? 1.5404 1.3470 1.4414 0.0386  -0.0772 0.0520  825  PRO   B N   
6409  C  CA  . PRO   B 521 ? 1.5107 1.3172 1.4214 0.0363  -0.0789 0.0491  825  PRO   B CA  
6410  C  C   . PRO   B 521 ? 1.5699 1.3907 1.4894 0.0388  -0.0841 0.0461  825  PRO   B C   
6411  O  O   . PRO   B 521 ? 1.5446 1.3679 1.4743 0.0363  -0.0854 0.0433  825  PRO   B O   
6412  C  CB  . PRO   B 521 ? 1.4815 1.2738 1.3817 0.0399  -0.0807 0.0499  825  PRO   B CB  
6413  C  CG  . PRO   B 521 ? 1.5254 1.3181 1.4130 0.0470  -0.0835 0.0519  825  PRO   B CG  
6414  C  CD  . PRO   B 521 ? 1.5525 1.3523 1.4396 0.0456  -0.0807 0.0536  825  PRO   B CD  
6415  N  N   . ASN   B 522 ? 1.5275 1.3576 1.4434 0.0439  -0.0869 0.0467  826  ASN   B N   
6416  C  CA  . ASN   B 522 ? 1.4774 1.3212 1.4010 0.0466  -0.0911 0.0442  826  ASN   B CA  
6417  C  C   . ASN   B 522 ? 1.5450 1.3991 1.4814 0.0410  -0.0890 0.0425  826  ASN   B C   
6418  O  O   . ASN   B 522 ? 1.5428 1.3993 1.4804 0.0374  -0.0851 0.0440  826  ASN   B O   
6419  C  CB  . ASN   B 522 ? 1.4648 1.3166 1.3828 0.0527  -0.0940 0.0454  826  ASN   B CB  
6420  C  CG  . ASN   B 522 ? 1.5085 1.3505 1.4130 0.0581  -0.0955 0.0476  826  ASN   B CG  
6421  O  OD1 . ASN   B 522 ? 1.5045 1.3481 1.4026 0.0607  -0.0956 0.0496  826  ASN   B OD1 
6422  N  ND2 . ASN   B 522 ? 1.6231 1.4545 1.5229 0.0601  -0.0971 0.0471  826  ASN   B ND2 
6423  N  N   . THR   B 523 ? 1.5526 1.4129 1.4981 0.0407  -0.0918 0.0395  827  THR   B N   
6424  C  CA  . THR   B 523 ? 1.5449 1.4175 1.5020 0.0372  -0.0911 0.0378  827  THR   B CA  
6425  C  C   . THR   B 523 ? 1.5415 1.4267 1.4981 0.0418  -0.0935 0.0380  827  THR   B C   
6426  O  O   . THR   B 523 ? 1.5306 1.4162 1.4808 0.0481  -0.0969 0.0383  827  THR   B O   
6427  C  CB  . THR   B 523 ? 1.5590 1.4322 1.5254 0.0353  -0.0934 0.0343  827  THR   B CB  
6428  O  OG1 . THR   B 523 ? 1.5661 1.4347 1.5266 0.0411  -0.0979 0.0334  827  THR   B OG1 
6429  C  CG2 . THR   B 523 ? 1.5644 1.4282 1.5356 0.0290  -0.0900 0.0340  827  THR   B CG2 
6430  N  N   . TYR   B 524 ? 1.5281 1.4236 1.4917 0.0387  -0.0916 0.0378  828  TYR   B N   
6431  C  CA  . TYR   B 524 ? 1.5125 1.4193 1.4756 0.0420  -0.0928 0.0386  828  TYR   B CA  
6432  C  C   . TYR   B 524 ? 1.4803 1.3996 1.4547 0.0399  -0.0932 0.0363  828  TYR   B C   
6433  O  O   . TYR   B 524 ? 1.5118 1.4309 1.4943 0.0352  -0.0920 0.0344  828  TYR   B O   
6434  C  CB  . TYR   B 524 ? 1.5254 1.4306 1.4828 0.0406  -0.0897 0.0413  828  TYR   B CB  
6435  C  CG  . TYR   B 524 ? 1.5554 1.4499 1.4999 0.0445  -0.0902 0.0438  828  TYR   B CG  
6436  C  CD1 . TYR   B 524 ? 1.5331 1.4270 1.4720 0.0510  -0.0944 0.0438  828  TYR   B CD1 
6437  C  CD2 . TYR   B 524 ? 1.5462 1.4310 1.4836 0.0418  -0.0864 0.0461  828  TYR   B CD2 
6438  C  CE1 . TYR   B 524 ? 1.5545 1.4388 1.4818 0.0548  -0.0952 0.0460  828  TYR   B CE1 
6439  C  CE2 . TYR   B 524 ? 1.5467 1.4213 1.4716 0.0457  -0.0871 0.0483  828  TYR   B CE2 
6440  C  CZ  . TYR   B 524 ? 1.5803 1.4548 1.5004 0.0521  -0.0917 0.0482  828  TYR   B CZ  
6441  O  OH  . TYR   B 524 ? 1.6472 1.5114 1.5547 0.0562  -0.0926 0.0503  828  TYR   B OH  
6442  N  N   . PHE   B 525 ? 1.3699 1.3002 1.3452 0.0433  -0.0950 0.0366  829  PHE   B N   
6443  C  CA  . PHE   B 525 ? 1.3196 1.2623 1.3046 0.0419  -0.0953 0.0348  829  PHE   B CA  
6444  C  C   . PHE   B 525 ? 1.2742 1.2242 1.2600 0.0401  -0.0931 0.0364  829  PHE   B C   
6445  O  O   . PHE   B 525 ? 1.2657 1.2211 1.2482 0.0441  -0.0947 0.0377  829  PHE   B O   
6446  C  CB  . PHE   B 525 ? 1.2695 1.2190 1.2554 0.0476  -0.0989 0.0336  829  PHE   B CB  
6447  C  CG  . PHE   B 525 ? 1.2130 1.1593 1.2018 0.0483  -0.1012 0.0309  829  PHE   B CG  
6448  C  CD1 . PHE   B 525 ? 1.2329 1.1777 1.2290 0.0431  -0.1002 0.0288  829  PHE   B CD1 
6449  C  CD2 . PHE   B 525 ? 1.1914 1.1363 1.1758 0.0546  -0.1044 0.0305  829  PHE   B CD2 
6450  C  CE1 . PHE   B 525 ? 1.2454 1.1869 1.2440 0.0442  -0.1031 0.0261  829  PHE   B CE1 
6451  C  CE2 . PHE   B 525 ? 1.1912 1.1322 1.1770 0.0558  -0.1068 0.0279  829  PHE   B CE2 
6452  C  CZ  . PHE   B 525 ? 1.2179 1.1571 1.2107 0.0506  -0.1064 0.0256  829  PHE   B CZ  
6453  N  N   . ILE   B 526 ? 1.2230 1.1733 1.2136 0.0342  -0.0896 0.0363  830  ILE   B N   
6454  C  CA  . ILE   B 526 ? 1.1901 1.1460 1.1808 0.0322  -0.0874 0.0377  830  ILE   B CA  
6455  C  C   . ILE   B 526 ? 1.1880 1.1567 1.1884 0.0309  -0.0878 0.0360  830  ILE   B C   
6456  O  O   . ILE   B 526 ? 1.1623 1.1330 1.1708 0.0274  -0.0869 0.0339  830  ILE   B O   
6457  C  CB  . ILE   B 526 ? 1.1587 1.1066 1.1475 0.0270  -0.0827 0.0389  830  ILE   B CB  
6458  C  CG1 . ILE   B 526 ? 1.2343 1.1683 1.2141 0.0281  -0.0821 0.0404  830  ILE   B CG1 
6459  C  CG2 . ILE   B 526 ? 1.1433 1.0946 1.1287 0.0263  -0.0810 0.0408  830  ILE   B CG2 
6460  C  CD1 . ILE   B 526 ? 1.2107 1.1354 1.1913 0.0224  -0.0771 0.0409  830  ILE   B CD1 
6461  N  N   . VAL   B 527 ? 1.1785 1.1558 1.1783 0.0336  -0.0891 0.0369  831  VAL   B N   
6462  C  CA  . VAL   B 527 ? 1.1115 1.1010 1.1194 0.0331  -0.0897 0.0356  831  VAL   B CA  
6463  C  C   . VAL   B 527 ? 1.1214 1.1153 1.1288 0.0310  -0.0879 0.0370  831  VAL   B C   
6464  O  O   . VAL   B 527 ? 1.1923 1.1854 1.1932 0.0338  -0.0891 0.0388  831  VAL   B O   
6465  C  CB  . VAL   B 527 ? 1.0928 1.0891 1.1012 0.0389  -0.0932 0.0353  831  VAL   B CB  
6466  C  CG1 . VAL   B 527 ? 1.0531 1.0604 1.0703 0.0382  -0.0933 0.0336  831  VAL   B CG1 
6467  C  CG2 . VAL   B 527 ? 1.1595 1.1486 1.1643 0.0424  -0.0952 0.0346  831  VAL   B CG2 
6468  N  N   . GLY   B 528 ? 1.1065 1.1047 1.1205 0.0262  -0.0854 0.0360  832  GLY   B N   
6469  C  CA  . GLY   B 528 ? 1.0777 1.0810 1.0920 0.0243  -0.0840 0.0370  832  GLY   B CA  
6470  C  C   . GLY   B 528 ? 1.0372 1.0532 1.0586 0.0255  -0.0857 0.0359  832  GLY   B C   
6471  O  O   . GLY   B 528 ? 1.0168 1.0372 1.0453 0.0248  -0.0860 0.0339  832  GLY   B O   
6472  N  N   . THR   B 529 ? 1.0540 1.0751 1.0733 0.0276  -0.0871 0.0371  833  THR   B N   
6473  C  CA  . THR   B 529 ? 1.0601 1.0930 1.0860 0.0288  -0.0887 0.0364  833  THR   B CA  
6474  C  C   . THR   B 529 ? 1.0868 1.1244 1.1143 0.0257  -0.0873 0.0369  833  THR   B C   
6475  O  O   . THR   B 529 ? 1.0432 1.0747 1.0670 0.0223  -0.0847 0.0375  833  THR   B O   
6476  C  CB  . THR   B 529 ? 1.0713 1.1075 1.0953 0.0347  -0.0921 0.0373  833  THR   B CB  
6477  O  OG1 . THR   B 529 ? 1.1356 1.1722 1.1551 0.0360  -0.0934 0.0390  833  THR   B OG1 
6478  C  CG2 . THR   B 529 ? 1.0525 1.0802 1.0710 0.0379  -0.0932 0.0375  833  THR   B CG2 
6479  N  N   . ALA   B 530 ? 1.1206 1.1684 1.1534 0.0268  -0.0887 0.0366  834  ALA   B N   
6480  C  CA  . ALA   B 530 ? 1.0837 1.1366 1.1179 0.0244  -0.0882 0.0369  834  ALA   B CA  
6481  C  C   . ALA   B 530 ? 1.0659 1.1291 1.1050 0.0274  -0.0908 0.0370  834  ALA   B C   
6482  O  O   . ALA   B 530 ? 1.0843 1.1540 1.1300 0.0284  -0.0910 0.0360  834  ALA   B O   
6483  C  CB  . ALA   B 530 ? 1.0502 1.1050 1.0897 0.0194  -0.0851 0.0356  834  ALA   B CB  
6484  N  N   . MET   B 531 ? 1.1310 1.1954 1.1671 0.0288  -0.0929 0.0382  835  MET   B N   
6485  C  CA  . MET   B 531 ? 1.1646 1.2391 1.2065 0.0314  -0.0954 0.0384  835  MET   B CA  
6486  C  C   . MET   B 531 ? 1.1530 1.2357 1.2023 0.0280  -0.0940 0.0374  835  MET   B C   
6487  O  O   . MET   B 531 ? 1.1749 1.2558 1.2224 0.0245  -0.0928 0.0373  835  MET   B O   
6488  C  CB  . MET   B 531 ? 1.2033 1.2762 1.2401 0.0339  -0.0986 0.0397  835  MET   B CB  
6489  C  CG  . MET   B 531 ? 1.2490 1.3138 1.2783 0.0376  -0.1002 0.0407  835  MET   B CG  
6490  S  SD  . MET   B 531 ? 1.1080 1.1774 1.1422 0.0425  -0.1013 0.0405  835  MET   B SD  
6491  C  CE  . MET   B 531 ? 1.2417 1.3231 1.2837 0.0455  -0.1045 0.0410  835  MET   B CE  
6492  N  N   . VAL   B 532 ? 1.1030 1.1939 1.1600 0.0294  -0.0940 0.0367  836  VAL   B N   
6493  C  CA  . VAL   B 532 ? 1.1177 1.2163 1.1818 0.0266  -0.0926 0.0357  836  VAL   B CA  
6494  C  C   . VAL   B 532 ? 1.1206 1.2286 1.1908 0.0290  -0.0945 0.0363  836  VAL   B C   
6495  O  O   . VAL   B 532 ? 1.1508 1.2613 1.2226 0.0332  -0.0959 0.0369  836  VAL   B O   
6496  C  CB  . VAL   B 532 ? 1.1454 1.2449 1.2135 0.0257  -0.0903 0.0342  836  VAL   B CB  
6497  C  CG1 . VAL   B 532 ? 1.1347 1.2255 1.1986 0.0229  -0.0884 0.0334  836  VAL   B CG1 
6498  C  CG2 . VAL   B 532 ? 1.1634 1.2651 1.2333 0.0303  -0.0912 0.0343  836  VAL   B CG2 
6499  N  N   . TYR   B 533 ? 1.1272 1.2402 1.2009 0.0262  -0.0945 0.0360  837  TYR   B N   
6500  C  CA  . TYR   B 533 ? 1.1478 1.2704 1.2290 0.0275  -0.0958 0.0364  837  TYR   B CA  
6501  C  C   . TYR   B 533 ? 1.1609 1.2886 1.2475 0.0238  -0.0937 0.0353  837  TYR   B C   
6502  O  O   . TYR   B 533 ? 1.2042 1.3277 1.2877 0.0201  -0.0920 0.0345  837  TYR   B O   
6503  C  CB  . TYR   B 533 ? 1.1538 1.2769 1.2335 0.0283  -0.0994 0.0373  837  TYR   B CB  
6504  C  CG  . TYR   B 533 ? 1.1531 1.2695 1.2257 0.0318  -0.1018 0.0382  837  TYR   B CG  
6505  C  CD1 . TYR   B 533 ? 1.1899 1.3099 1.2657 0.0365  -0.1038 0.0390  837  TYR   B CD1 
6506  C  CD2 . TYR   B 533 ? 1.2295 1.3358 1.2922 0.0304  -0.1019 0.0385  837  TYR   B CD2 
6507  C  CE1 . TYR   B 533 ? 1.3253 1.4390 1.3945 0.0399  -0.1062 0.0399  837  TYR   B CE1 
6508  C  CE2 . TYR   B 533 ? 1.2911 1.3905 1.3466 0.0338  -0.1041 0.0394  837  TYR   B CE2 
6509  C  CZ  . TYR   B 533 ? 1.3250 1.4282 1.3837 0.0385  -0.1065 0.0401  837  TYR   B CZ  
6510  O  OH  . TYR   B 533 ? 1.3507 1.4469 1.4021 0.0421  -0.1089 0.0410  837  TYR   B OH  
6511  N  N   . PRO   B 534 ? 1.1154 1.2517 1.2099 0.0247  -0.0934 0.0354  838  PRO   B N   
6512  C  CA  . PRO   B 534 ? 1.1493 1.2899 1.2485 0.0215  -0.0910 0.0344  838  PRO   B CA  
6513  C  C   . PRO   B 534 ? 1.2207 1.3612 1.3191 0.0175  -0.0915 0.0340  838  PRO   B C   
6514  O  O   . PRO   B 534 ? 1.2875 1.4278 1.3865 0.0142  -0.0893 0.0329  838  PRO   B O   
6515  C  CB  . PRO   B 534 ? 1.1983 1.3477 1.3058 0.0239  -0.0908 0.0349  838  PRO   B CB  
6516  C  CG  . PRO   B 534 ? 1.1853 1.3342 1.2922 0.0287  -0.0920 0.0360  838  PRO   B CG  
6517  C  CD  . PRO   B 534 ? 1.1385 1.2804 1.2381 0.0291  -0.0945 0.0364  838  PRO   B CD  
6518  N  N   . GLU   B 535 ? 1.2114 1.3516 1.3080 0.0178  -0.0944 0.0347  839  GLU   B N   
6519  C  CA  . GLU   B 535 ? 1.1993 1.3387 1.2941 0.0144  -0.0953 0.0343  839  GLU   B CA  
6520  C  C   . GLU   B 535 ? 1.2359 1.3655 1.3213 0.0123  -0.0943 0.0341  839  GLU   B C   
6521  O  O   . GLU   B 535 ? 1.3127 1.4408 1.3971 0.0087  -0.0922 0.0333  839  GLU   B O   
6522  C  CB  . GLU   B 535 ? 1.2581 1.4008 1.3549 0.0160  -0.0995 0.0350  839  GLU   B CB  
6523  C  CG  . GLU   B 535 ? 1.2981 1.4377 1.3913 0.0200  -0.1026 0.0360  839  GLU   B CG  
6524  C  CD  . GLU   B 535 ? 1.2231 1.3676 1.3220 0.0240  -0.1022 0.0367  839  GLU   B CD  
6525  O  OE1 . GLU   B 535 ? 1.1708 1.3151 1.2705 0.0241  -0.0989 0.0364  839  GLU   B OE1 
6526  O  OE2 . GLU   B 535 ? 1.2382 1.3866 1.3410 0.0271  -0.1052 0.0374  839  GLU   B OE2 
6527  N  N   . GLU   B 536 ? 1.2355 1.3583 1.3141 0.0145  -0.0955 0.0349  840  GLU   B N   
6528  C  CA  . GLU   B 536 ? 1.1960 1.3087 1.2653 0.0128  -0.0940 0.0349  840  GLU   B CA  
6529  C  C   . GLU   B 536 ? 1.2003 1.3114 1.2711 0.0102  -0.0899 0.0339  840  GLU   B C   
6530  O  O   . GLU   B 536 ? 1.2133 1.3231 1.2850 0.0117  -0.0889 0.0338  840  GLU   B O   
6531  C  CB  . GLU   B 536 ? 1.2352 1.3411 1.2977 0.0161  -0.0958 0.0360  840  GLU   B CB  
6532  N  N   . ALA   B 537 ? 1.2327 1.3437 1.3039 0.0065  -0.0878 0.0331  841  ALA   B N   
6533  C  CA  . ALA   B 537 ? 1.2105 1.3206 1.2842 0.0038  -0.0841 0.0319  841  ALA   B CA  
6534  C  C   . ALA   B 537 ? 1.2059 1.3066 1.2736 0.0033  -0.0821 0.0322  841  ALA   B C   
6535  O  O   . ALA   B 537 ? 1.2209 1.3205 1.2908 0.0038  -0.0810 0.0316  841  ALA   B O   
6536  C  CB  . ALA   B 537 ? 1.1983 1.3103 1.2735 0.0001  -0.0825 0.0311  841  ALA   B CB  
6537  N  N   . GLU   B 538 ? 1.0667 1.1601 1.1266 0.0023  -0.0817 0.0331  842  GLU   B N   
6538  C  CA  . GLU   B 538 ? 1.0689 1.1525 1.1222 0.0018  -0.0795 0.0337  842  GLU   B CA  
6539  C  C   . GLU   B 538 ? 1.1157 1.1955 1.1642 0.0058  -0.0822 0.0349  842  GLU   B C   
6540  O  O   . GLU   B 538 ? 1.0727 1.1551 1.1198 0.0084  -0.0858 0.0356  842  GLU   B O   
6541  C  CB  . GLU   B 538 ? 1.1119 1.1887 1.1581 -0.0006 -0.0774 0.0343  842  GLU   B CB  
6542  C  CG  . GLU   B 538 ? 1.1714 1.2379 1.2119 -0.0023 -0.0734 0.0348  842  GLU   B CG  
6543  C  CD  . GLU   B 538 ? 1.2449 1.3127 1.2927 -0.0054 -0.0696 0.0334  842  GLU   B CD  
6544  O  OE1 . GLU   B 538 ? 1.1874 1.2595 1.2400 -0.0080 -0.0678 0.0323  842  GLU   B OE1 
6545  O  OE2 . GLU   B 538 ? 1.3040 1.3680 1.3526 -0.0051 -0.0686 0.0333  842  GLU   B OE2 
6546  N  N   . PRO   B 539 ? 1.1573 1.2316 1.2042 0.0064  -0.0809 0.0350  843  PRO   B N   
6547  C  CA  . PRO   B 539 ? 1.1260 1.1963 1.1680 0.0104  -0.0834 0.0361  843  PRO   B CA  
6548  C  C   . PRO   B 539 ? 1.1270 1.1879 1.1582 0.0109  -0.0837 0.0376  843  PRO   B C   
6549  O  O   . PRO   B 539 ? 1.1056 1.1580 1.1317 0.0086  -0.0802 0.0380  843  PRO   B O   
6550  C  CB  . PRO   B 539 ? 1.0930 1.1600 1.1370 0.0103  -0.0817 0.0354  843  PRO   B CB  
6551  C  CG  . PRO   B 539 ? 1.0886 1.1530 1.1346 0.0057  -0.0775 0.0345  843  PRO   B CG  
6552  C  CD  . PRO   B 539 ? 1.1325 1.2041 1.1827 0.0036  -0.0773 0.0339  843  PRO   B CD  
6553  N  N   . LYS   B 540 ? 1.1712 1.2331 1.1989 0.0141  -0.0877 0.0385  844  LYS   B N   
6554  C  CA  . LYS   B 540 ? 1.1830 1.2357 1.1995 0.0150  -0.0885 0.0398  844  LYS   B CA  
6555  C  C   . LYS   B 540 ? 1.1737 1.2200 1.1833 0.0191  -0.0910 0.0411  844  LYS   B C   
6556  O  O   . LYS   B 540 ? 1.1510 1.1904 1.1512 0.0210  -0.0931 0.0421  844  LYS   B O   
6557  C  CB  . LYS   B 540 ? 1.1791 1.2363 1.1954 0.0152  -0.0917 0.0397  844  LYS   B CB  
6558  N  N   . GLN   B 541 ? 1.2252 1.2728 1.2385 0.0209  -0.0911 0.0409  845  GLN   B N   
6559  C  CA  . GLN   B 541 ? 1.2169 1.2583 1.2239 0.0249  -0.0933 0.0420  845  GLN   B CA  
6560  C  C   . GLN   B 541 ? 1.2036 1.2468 1.2159 0.0259  -0.0924 0.0413  845  GLN   B C   
6561  O  O   . GLN   B 541 ? 1.2030 1.2554 1.2247 0.0255  -0.0924 0.0402  845  GLN   B O   
6562  C  CB  . GLN   B 541 ? 1.2695 1.3150 1.2758 0.0291  -0.0987 0.0424  845  GLN   B CB  
6563  C  CG  . GLN   B 541 ? 1.3074 1.3665 1.3255 0.0302  -0.1009 0.0415  845  GLN   B CG  
6564  C  CD  . GLN   B 541 ? 1.3876 1.4508 1.4060 0.0340  -0.1062 0.0420  845  GLN   B CD  
6565  O  OE1 . GLN   B 541 ? 1.4176 1.4740 1.4273 0.0353  -0.1086 0.0427  845  GLN   B OE1 
6566  N  NE2 . GLN   B 541 ? 1.4112 1.4853 1.4398 0.0360  -0.1080 0.0415  845  GLN   B NE2 
6567  N  N   . GLY   B 542 ? 1.3136 1.3474 1.3191 0.0274  -0.0919 0.0421  846  GLY   B N   
6568  C  CA  . GLY   B 542 ? 1.2907 1.3240 1.2996 0.0285  -0.0912 0.0415  846  GLY   B CA  
6569  C  C   . GLY   B 542 ? 1.3224 1.3465 1.3226 0.0323  -0.0929 0.0428  846  GLY   B C   
6570  O  O   . GLY   B 542 ? 1.3641 1.3857 1.3579 0.0353  -0.0957 0.0440  846  GLY   B O   
6571  N  N   . ARG   B 543 ? 1.1943 1.2130 1.1940 0.0323  -0.0914 0.0425  847  ARG   B N   
6572  C  CA  . ARG   B 543 ? 1.2047 1.2130 1.1953 0.0353  -0.0923 0.0437  847  ARG   B CA  
6573  C  C   . ARG   B 543 ? 1.1906 1.1925 1.1819 0.0338  -0.0899 0.0430  847  ARG   B C   
6574  O  O   . ARG   B 543 ? 1.1846 1.1922 1.1838 0.0334  -0.0899 0.0414  847  ARG   B O   
6575  C  CB  . ARG   B 543 ? 1.1917 1.2037 1.1816 0.0413  -0.0969 0.0442  847  ARG   B CB  
6576  N  N   . ILE   B 544 ? 1.2198 1.2092 1.2023 0.0332  -0.0881 0.0442  848  ILE   B N   
6577  C  CA  . ILE   B 544 ? 1.1915 1.1734 1.1736 0.0326  -0.0866 0.0438  848  ILE   B CA  
6578  C  C   . ILE   B 544 ? 1.1908 1.1690 1.1672 0.0382  -0.0901 0.0445  848  ILE   B C   
6579  O  O   . ILE   B 544 ? 1.2393 1.2139 1.2076 0.0415  -0.0922 0.0460  848  ILE   B O   
6580  C  CB  . ILE   B 544 ? 1.1708 1.1408 1.1471 0.0286  -0.0821 0.0448  848  ILE   B CB  
6581  C  CG1 . ILE   B 544 ? 1.1800 1.1539 1.1632 0.0230  -0.0782 0.0439  848  ILE   B CG1 
6582  C  CG2 . ILE   B 544 ? 1.0940 1.0548 1.0686 0.0286  -0.0812 0.0446  848  ILE   B CG2 
6583  C  CD1 . ILE   B 544 ? 1.1232 1.0863 1.0999 0.0195  -0.0732 0.0455  848  ILE   B CD1 
6584  N  N   . VAL   B 545 ? 1.1726 1.1515 1.1530 0.0396  -0.0911 0.0432  849  VAL   B N   
6585  C  CA  . VAL   B 545 ? 1.2024 1.1785 1.1782 0.0452  -0.0944 0.0436  849  VAL   B CA  
6586  C  C   . VAL   B 545 ? 1.2783 1.2436 1.2512 0.0443  -0.0931 0.0432  849  VAL   B C   
6587  O  O   . VAL   B 545 ? 1.2311 1.1960 1.2100 0.0401  -0.0907 0.0418  849  VAL   B O   
6588  C  CB  . VAL   B 545 ? 1.1745 1.1623 1.1579 0.0487  -0.0972 0.0424  849  VAL   B CB  
6589  C  CG1 . VAL   B 545 ? 1.2099 1.1949 1.1886 0.0549  -0.1003 0.0430  849  VAL   B CG1 
6590  C  CG2 . VAL   B 545 ? 1.2115 1.2100 1.1993 0.0487  -0.0980 0.0427  849  VAL   B CG2 
6591  N  N   . VAL   B 546 ? 1.3498 1.3063 1.3139 0.0482  -0.0947 0.0445  850  VAL   B N   
6592  C  CA  . VAL   B 546 ? 1.2743 1.2200 1.2350 0.0478  -0.0939 0.0441  850  VAL   B CA  
6593  C  C   . VAL   B 546 ? 1.3286 1.2751 1.2881 0.0538  -0.0976 0.0436  850  VAL   B C   
6594  O  O   . VAL   B 546 ? 1.3550 1.3023 1.3093 0.0589  -0.1003 0.0448  850  VAL   B O   
6595  C  CB  . VAL   B 546 ? 1.2544 1.1863 1.2043 0.0469  -0.0918 0.0462  850  VAL   B CB  
6596  C  CG1 . VAL   B 546 ? 1.3701 1.2914 1.3190 0.0448  -0.0900 0.0457  850  VAL   B CG1 
6597  C  CG2 . VAL   B 546 ? 1.2635 1.1953 1.2130 0.0424  -0.0882 0.0472  850  VAL   B CG2 
6598  N  N   . PHE   B 547 ? 1.3212 1.2674 1.2855 0.0533  -0.0980 0.0416  851  PHE   B N   
6599  C  CA  . PHE   B 547 ? 1.3092 1.2554 1.2721 0.0590  -0.1012 0.0409  851  PHE   B CA  
6600  C  C   . PHE   B 547 ? 1.3866 1.3195 1.3438 0.0591  -0.1013 0.0406  851  PHE   B C   
6601  O  O   . PHE   B 547 ? 1.3905 1.3152 1.3469 0.0543  -0.0986 0.0407  851  PHE   B O   
6602  C  CB  . PHE   B 547 ? 1.2652 1.2215 1.2372 0.0595  -0.1022 0.0387  851  PHE   B CB  
6603  C  CG  . PHE   B 547 ? 1.2587 1.2283 1.2362 0.0607  -0.1026 0.0390  851  PHE   B CG  
6604  C  CD1 . PHE   B 547 ? 1.2881 1.2626 1.2638 0.0666  -0.1049 0.0400  851  PHE   B CD1 
6605  C  CD2 . PHE   B 547 ? 1.2589 1.2360 1.2440 0.0560  -0.1006 0.0382  851  PHE   B CD2 
6606  C  CE1 . PHE   B 547 ? 1.2555 1.2422 1.2372 0.0674  -0.1052 0.0403  851  PHE   B CE1 
6607  C  CE2 . PHE   B 547 ? 1.2052 1.1941 1.1954 0.0569  -0.1010 0.0384  851  PHE   B CE2 
6608  C  CZ  . PHE   B 547 ? 1.1826 1.1763 1.1714 0.0625  -0.1032 0.0395  851  PHE   B CZ  
6609  N  N   . GLN   B 548 ? 1.4105 1.3414 1.3642 0.0648  -0.1042 0.0402  852  GLN   B N   
6610  C  CA  . GLN   B 548 ? 1.3997 1.3182 1.3477 0.0660  -0.1051 0.0398  852  GLN   B CA  
6611  C  C   . GLN   B 548 ? 1.4290 1.3502 1.3775 0.0717  -0.1083 0.0383  852  GLN   B C   
6612  O  O   . GLN   B 548 ? 1.4482 1.3747 1.3945 0.0773  -0.1100 0.0393  852  GLN   B O   
6613  C  CB  . GLN   B 548 ? 1.3865 1.2944 1.3234 0.0681  -0.1050 0.0422  852  GLN   B CB  
6614  C  CG  . GLN   B 548 ? 1.4416 1.3374 1.3711 0.0713  -0.1067 0.0421  852  GLN   B CG  
6615  C  CD  . GLN   B 548 ? 1.4583 1.3402 1.3787 0.0694  -0.1048 0.0440  852  GLN   B CD  
6616  O  OE1 . GLN   B 548 ? 1.5082 1.3816 1.4295 0.0646  -0.1026 0.0434  852  GLN   B OE1 
6617  N  NE2 . GLN   B 548 ? 1.4384 1.3176 1.3502 0.0732  -0.1056 0.0462  852  GLN   B NE2 
6618  N  N   . TYR   B 549 ? 1.4855 1.4034 1.4372 0.0704  -0.1089 0.0360  853  TYR   B N   
6619  C  CA  . TYR   B 549 ? 1.5197 1.4383 1.4706 0.0759  -0.1118 0.0344  853  TYR   B CA  
6620  C  C   . TYR   B 549 ? 1.6048 1.5092 1.5485 0.0773  -0.1134 0.0339  853  TYR   B C   
6621  O  O   . TYR   B 549 ? 1.6140 1.5122 1.5604 0.0734  -0.1134 0.0320  853  TYR   B O   
6622  C  CB  . TYR   B 549 ? 1.3878 1.3136 1.3473 0.0741  -0.1121 0.0318  853  TYR   B CB  
6623  C  CG  . TYR   B 549 ? 1.4053 1.3322 1.3630 0.0804  -0.1147 0.0305  853  TYR   B CG  
6624  C  CD1 . TYR   B 549 ? 1.4871 1.4235 1.4453 0.0856  -0.1149 0.0315  853  TYR   B CD1 
6625  C  CD2 . TYR   B 549 ? 1.4413 1.3596 1.3971 0.0812  -0.1169 0.0281  853  TYR   B CD2 
6626  C  CE1 . TYR   B 549 ? 1.5162 1.4533 1.4724 0.0917  -0.1166 0.0304  853  TYR   B CE1 
6627  C  CE2 . TYR   B 549 ? 1.4469 1.3653 1.3998 0.0875  -0.1192 0.0269  853  TYR   B CE2 
6628  C  CZ  . TYR   B 549 ? 1.4619 1.3898 1.4149 0.0928  -0.1187 0.0282  853  TYR   B CZ  
6629  O  OH  . TYR   B 549 ? 1.4569 1.3847 1.4067 0.0992  -0.1202 0.0272  853  TYR   B OH  
6630  N  N   . SER   B 550 ? 1.6821 1.5812 1.6170 0.0830  -0.1149 0.0354  854  SER   B N   
6631  C  CA  . SER   B 550 ? 1.7525 1.6375 1.6800 0.0844  -0.1163 0.0350  854  SER   B CA  
6632  C  C   . SER   B 550 ? 1.8108 1.6930 1.7311 0.0926  -0.1192 0.0351  854  SER   B C   
6633  O  O   . SER   B 550 ? 1.7918 1.6620 1.7057 0.0943  -0.1208 0.0345  854  SER   B O   
6634  C  CB  . SER   B 550 ? 1.7853 1.6604 1.7069 0.0811  -0.1143 0.0371  854  SER   B CB  
6635  O  OG  . SER   B 550 ? 1.7484 1.6217 1.6761 0.0733  -0.1116 0.0364  854  SER   B OG  
6636  N  N   . ASP   B 551 ? 1.7857 1.6782 1.7072 0.0977  -0.1198 0.0359  855  ASP   B N   
6637  C  CA  . ASP   B 551 ? 1.7885 1.6794 1.7044 0.1058  -0.1221 0.0359  855  ASP   B CA  
6638  C  C   . ASP   B 551 ? 1.7781 1.6823 1.7006 0.1089  -0.1219 0.0352  855  ASP   B C   
6639  O  O   . ASP   B 551 ? 1.7791 1.6911 1.7021 0.1135  -0.1218 0.0368  855  ASP   B O   
6640  C  CB  . ASP   B 551 ? 1.7850 1.6722 1.6931 0.1102  -0.1227 0.0384  855  ASP   B CB  
6641  N  N   . GLY   B 552 ? 1.8004 1.7071 1.7285 0.1063  -0.1218 0.0329  856  GLY   B N   
6642  C  CA  . GLY   B 552 ? 1.7904 1.7085 1.7243 0.1089  -0.1212 0.0321  856  GLY   B CA  
6643  C  C   . GLY   B 552 ? 1.8025 1.7342 1.7431 0.1079  -0.1192 0.0340  856  GLY   B C   
6644  O  O   . GLY   B 552 ? 1.7570 1.6989 1.7028 0.1103  -0.1183 0.0338  856  GLY   B O   
6645  N  N   . LYS   B 553 ? 1.8773 1.8090 1.8179 0.1043  -0.1184 0.0357  857  LYS   B N   
6646  C  CA  . LYS   B 553 ? 1.8325 1.7755 1.7780 0.1038  -0.1171 0.0375  857  LYS   B CA  
6647  C  C   . LYS   B 553 ? 1.7777 1.7211 1.7265 0.0962  -0.1155 0.0378  857  LYS   B C   
6648  O  O   . LYS   B 553 ? 1.7912 1.7242 1.7352 0.0928  -0.1153 0.0379  857  LYS   B O   
6649  C  CB  . LYS   B 553 ? 1.8276 1.7696 1.7678 0.1094  -0.1184 0.0397  857  LYS   B CB  
6650  N  N   . LEU   B 554 ? 1.5652 1.5205 1.5222 0.0935  -0.1140 0.0379  858  LEU   B N   
6651  C  CA  . LEU   B 554 ? 1.5225 1.4799 1.4828 0.0869  -0.1122 0.0384  858  LEU   B CA  
6652  C  C   . LEU   B 554 ? 1.5619 1.5198 1.5184 0.0882  -0.1126 0.0408  858  LEU   B C   
6653  O  O   . LEU   B 554 ? 1.5992 1.5651 1.5576 0.0926  -0.1137 0.0418  858  LEU   B O   
6654  C  CB  . LEU   B 554 ? 1.4357 1.4052 1.4058 0.0839  -0.1107 0.0374  858  LEU   B CB  
6655  C  CG  . LEU   B 554 ? 1.4408 1.4104 1.4150 0.0763  -0.1086 0.0369  858  LEU   B CG  
6656  C  CD1 . LEU   B 554 ? 1.4498 1.4085 1.4218 0.0730  -0.1084 0.0353  858  LEU   B CD1 
6657  C  CD2 . LEU   B 554 ? 1.4279 1.4089 1.4112 0.0744  -0.1075 0.0357  858  LEU   B CD2 
6658  N  N   . GLN   B 555 ? 1.5334 1.4823 1.4845 0.0847  -0.1119 0.0417  859  GLN   B N   
6659  C  CA  . GLN   B 555 ? 1.4473 1.3945 1.3930 0.0860  -0.1126 0.0438  859  GLN   B CA  
6660  C  C   . GLN   B 555 ? 1.4052 1.3539 1.3531 0.0796  -0.1102 0.0443  859  GLN   B C   
6661  O  O   . GLN   B 555 ? 1.4017 1.3443 1.3497 0.0743  -0.1079 0.0437  859  GLN   B O   
6662  C  CB  . GLN   B 555 ? 1.4917 1.4247 1.4262 0.0886  -0.1136 0.0448  859  GLN   B CB  
6663  N  N   . THR   B 556 ? 1.4291 1.3858 1.3791 0.0803  -0.1109 0.0454  860  THR   B N   
6664  C  CA  . THR   B 556 ? 1.4856 1.4446 1.4374 0.0748  -0.1089 0.0458  860  THR   B CA  
6665  C  C   . THR   B 556 ? 1.5050 1.4518 1.4460 0.0740  -0.1084 0.0476  860  THR   B C   
6666  O  O   . THR   B 556 ? 1.5727 1.5182 1.5079 0.0779  -0.1108 0.0490  860  THR   B O   
6667  C  CB  . THR   B 556 ? 1.5163 1.4885 1.4747 0.0760  -0.1102 0.0461  860  THR   B CB  
6668  O  OG1 . THR   B 556 ? 1.4850 1.4680 1.4531 0.0768  -0.1101 0.0446  860  THR   B OG1 
6669  C  CG2 . THR   B 556 ? 1.4737 1.4475 1.4331 0.0706  -0.1083 0.0465  860  THR   B CG2 
6670  N  N   . VAL   B 557 ? 1.4405 1.3779 1.3787 0.0689  -0.1052 0.0475  861  VAL   B N   
6671  C  CA  . VAL   B 557 ? 1.4454 1.3696 1.3728 0.0678  -0.1037 0.0493  861  VAL   B CA  
6672  C  C   . VAL   B 557 ? 1.5310 1.4574 1.4578 0.0643  -0.1020 0.0503  861  VAL   B C   
6673  O  O   . VAL   B 557 ? 1.5582 1.4792 1.4844 0.0588  -0.0979 0.0505  861  VAL   B O   
6674  C  CB  . VAL   B 557 ? 1.4185 1.3314 1.3441 0.0640  -0.1007 0.0489  861  VAL   B CB  
6675  C  CG1 . VAL   B 557 ? 1.4466 1.3443 1.3600 0.0635  -0.0989 0.0510  861  VAL   B CG1 
6676  C  CG2 . VAL   B 557 ? 1.3903 1.3022 1.3177 0.0671  -0.1028 0.0474  861  VAL   B CG2 
6677  N  N   . ALA   B 558 ? 1.5850 1.5193 1.5123 0.0674  -0.1049 0.0508  862  ALA   B N   
6678  C  CA  . ALA   B 558 ? 1.5334 1.4707 1.4601 0.0650  -0.1043 0.0515  862  ALA   B CA  
6679  C  C   . ALA   B 558 ? 1.5058 1.4531 1.4434 0.0596  -0.1016 0.0501  862  ALA   B C   
6680  O  O   . ALA   B 558 ? 1.4942 1.4430 1.4384 0.0565  -0.0993 0.0487  862  ALA   B O   
6681  C  CB  . ALA   B 558 ? 1.6079 1.5305 1.5221 0.0633  -0.1018 0.0533  862  ALA   B CB  
6682  N  N   . GLU   B 559 ? 1.4766 1.4305 1.4159 0.0587  -0.1023 0.0503  863  GLU   B N   
6683  C  CA  . GLU   B 559 ? 1.4401 1.4033 1.3888 0.0538  -0.1000 0.0492  863  GLU   B CA  
6684  C  C   . GLU   B 559 ? 1.4828 1.4403 1.4251 0.0505  -0.0977 0.0503  863  GLU   B C   
6685  O  O   . GLU   B 559 ? 1.5689 1.5150 1.4994 0.0522  -0.0978 0.0519  863  GLU   B O   
6686  C  CB  . GLU   B 559 ? 1.4481 1.4262 1.4063 0.0562  -0.1032 0.0482  863  GLU   B CB  
6687  N  N   . LYS   B 560 ? 1.3504 1.3151 1.2999 0.0461  -0.0954 0.0494  864  LYS   B N   
6688  C  CA  . LYS   B 560 ? 1.3053 1.2658 1.2497 0.0429  -0.0929 0.0502  864  LYS   B CA  
6689  C  C   . LYS   B 560 ? 1.2884 1.2620 1.2429 0.0404  -0.0931 0.0489  864  LYS   B C   
6690  O  O   . LYS   B 560 ? 1.2712 1.2493 1.2340 0.0362  -0.0899 0.0477  864  LYS   B O   
6691  C  CB  . LYS   B 560 ? 1.2371 1.1868 1.1776 0.0382  -0.0870 0.0508  864  LYS   B CB  
6692  N  N   . GLU   B 561 ? 1.3265 1.3058 1.2804 0.0430  -0.0971 0.0491  865  GLU   B N   
6693  C  CA  . GLU   B 561 ? 1.2462 1.2377 1.2093 0.0410  -0.0977 0.0479  865  GLU   B CA  
6694  C  C   . GLU   B 561 ? 1.1846 1.1722 1.1449 0.0361  -0.0936 0.0481  865  GLU   B C   
6695  O  O   . GLU   B 561 ? 1.1991 1.1793 1.1495 0.0367  -0.0940 0.0492  865  GLU   B O   
6696  C  CB  . GLU   B 561 ? 1.3067 1.3046 1.2701 0.0452  -0.1033 0.0480  865  GLU   B CB  
6697  C  CG  . GLU   B 561 ? 1.4263 1.4335 1.3961 0.0427  -0.1038 0.0472  865  GLU   B CG  
6698  C  CD  . GLU   B 561 ? 1.5536 1.5628 1.5203 0.0461  -0.1091 0.0475  865  GLU   B CD  
6699  O  OE1 . GLU   B 561 ? 1.6911 1.7047 1.6604 0.0507  -0.1135 0.0475  865  GLU   B OE1 
6700  O  OE2 . GLU   B 561 ? 1.5084 1.5145 1.4700 0.0443  -0.1091 0.0477  865  GLU   B OE2 
6701  N  N   . VAL   B 562 ? 1.1846 1.1769 1.1534 0.0316  -0.0898 0.0470  866  VAL   B N   
6702  C  CA  . VAL   B 562 ? 1.1727 1.1624 1.1408 0.0268  -0.0854 0.0469  866  VAL   B CA  
6703  C  C   . VAL   B 562 ? 1.1625 1.1633 1.1372 0.0258  -0.0872 0.0459  866  VAL   B C   
6704  O  O   . VAL   B 562 ? 1.1539 1.1647 1.1349 0.0284  -0.0913 0.0452  866  VAL   B O   
6705  C  CB  . VAL   B 562 ? 1.1584 1.1467 1.1327 0.0225  -0.0804 0.0461  866  VAL   B CB  
6706  C  CG1 . VAL   B 562 ? 1.1399 1.1146 1.1060 0.0226  -0.0778 0.0474  866  VAL   B CG1 
6707  C  CG2 . VAL   B 562 ? 1.1735 1.1724 1.1596 0.0230  -0.0822 0.0443  866  VAL   B CG2 
6708  N  N   . LYS   B 563 ? 1.0891 1.0878 1.0621 0.0221  -0.0839 0.0460  867  LYS   B N   
6709  C  CA  . LYS   B 563 ? 1.1221 1.1296 1.0997 0.0209  -0.0853 0.0451  867  LYS   B CA  
6710  C  C   . LYS   B 563 ? 1.1487 1.1628 1.1366 0.0162  -0.0813 0.0437  867  LYS   B C   
6711  O  O   . LYS   B 563 ? 1.1317 1.1434 1.1183 0.0127  -0.0777 0.0437  867  LYS   B O   
6712  C  CB  . LYS   B 563 ? 1.1387 1.1379 1.1045 0.0211  -0.0854 0.0463  867  LYS   B CB  
6713  N  N   . GLY   B 564 ? 1.1571 1.1790 1.1549 0.0163  -0.0820 0.0425  868  GLY   B N   
6714  C  CA  . GLY   B 564 ? 1.1051 1.1332 1.1129 0.0125  -0.0789 0.0409  868  GLY   B CA  
6715  C  C   . GLY   B 564 ? 1.0853 1.1161 1.0996 0.0135  -0.0794 0.0399  868  GLY   B C   
6716  O  O   . GLY   B 564 ? 1.0757 1.1062 1.0882 0.0175  -0.0825 0.0403  868  GLY   B O   
6717  N  N   . ALA   B 565 ? 1.0812 1.1145 1.1030 0.0100  -0.0765 0.0385  869  ALA   B N   
6718  C  CA  . ALA   B 565 ? 1.0303 1.0663 1.0590 0.0105  -0.0769 0.0370  869  ALA   B CA  
6719  C  C   . ALA   B 565 ? 1.0278 1.0536 1.0539 0.0088  -0.0741 0.0372  869  ALA   B C   
6720  O  O   . ALA   B 565 ? 1.0396 1.0604 1.0649 0.0051  -0.0700 0.0374  869  ALA   B O   
6721  C  CB  . ALA   B 565 ? 1.0552 1.1002 1.0941 0.0080  -0.0761 0.0351  869  ALA   B CB  
6722  N  N   . VAL   B 566 ? 1.0202 1.0430 1.0451 0.0117  -0.0761 0.0371  870  VAL   B N   
6723  C  CA  . VAL   B 566 ? 1.0417 1.0548 1.0650 0.0101  -0.0737 0.0371  870  VAL   B CA  
6724  C  C   . VAL   B 566 ? 1.0847 1.1023 1.1185 0.0078  -0.0733 0.0346  870  VAL   B C   
6725  O  O   . VAL   B 566 ? 1.1006 1.1188 1.1368 0.0101  -0.0758 0.0335  870  VAL   B O   
6726  C  CB  . VAL   B 566 ? 1.0634 1.0698 1.0794 0.0143  -0.0762 0.0382  870  VAL   B CB  
6727  C  CG1 . VAL   B 566 ? 1.1096 1.1048 1.1229 0.0123  -0.0735 0.0385  870  VAL   B CG1 
6728  C  CG2 . VAL   B 566 ? 1.0838 1.0881 1.0906 0.0174  -0.0780 0.0403  870  VAL   B CG2 
6729  N  N   . TYR   B 567 ? 1.0977 1.1179 1.1374 0.0034  -0.0701 0.0337  871  TYR   B N   
6730  C  CA  . TYR   B 567 ? 1.0701 1.0956 1.1202 0.0014  -0.0702 0.0312  871  TYR   B CA  
6731  C  C   . TYR   B 567 ? 1.1413 1.1601 1.1937 0.0007  -0.0702 0.0300  871  TYR   B C   
6732  O  O   . TYR   B 567 ? 1.1320 1.1538 1.1895 0.0023  -0.0730 0.0281  871  TYR   B O   
6733  C  CB  . TYR   B 567 ? 1.0650 1.0937 1.1207 -0.0032 -0.0666 0.0305  871  TYR   B CB  
6734  C  CG  . TYR   B 567 ? 1.0297 1.0668 1.0858 -0.0027 -0.0674 0.0307  871  TYR   B CG  
6735  C  CD1 . TYR   B 567 ? 1.0344 1.0806 1.0947 -0.0002 -0.0708 0.0295  871  TYR   B CD1 
6736  C  CD2 . TYR   B 567 ? 1.0647 1.1003 1.1166 -0.0046 -0.0646 0.0321  871  TYR   B CD2 
6737  C  CE1 . TYR   B 567 ? 1.0359 1.0896 1.0971 0.0000  -0.0715 0.0297  871  TYR   B CE1 
6738  C  CE2 . TYR   B 567 ? 1.1107 1.1536 1.1630 -0.0043 -0.0656 0.0322  871  TYR   B CE2 
6739  C  CZ  . TYR   B 567 ? 1.0993 1.1514 1.1567 -0.0022 -0.0690 0.0310  871  TYR   B CZ  
6740  O  OH  . TYR   B 567 ? 1.1635 1.2227 1.2217 -0.0021 -0.0699 0.0311  871  TYR   B OH  
6741  N  N   . SER   B 568 ? 1.2363 1.2454 1.2851 -0.0015 -0.0669 0.0313  872  SER   B N   
6742  C  CA  . SER   B 568 ? 1.2579 1.2598 1.3093 -0.0027 -0.0665 0.0303  872  SER   B CA  
6743  C  C   . SER   B 568 ? 1.2734 1.2638 1.3150 -0.0020 -0.0647 0.0328  872  SER   B C   
6744  O  O   . SER   B 568 ? 1.2799 1.2668 1.3143 -0.0025 -0.0619 0.0350  872  SER   B O   
6745  C  CB  . SER   B 568 ? 1.2436 1.2455 1.3052 -0.0080 -0.0630 0.0286  872  SER   B CB  
6746  O  OG  . SER   B 568 ? 1.2247 1.2340 1.2960 -0.0082 -0.0659 0.0256  872  SER   B OG  
6747  N  N   . MET   B 569 ? 1.2384 1.2225 1.2791 -0.0007 -0.0664 0.0322  873  MET   B N   
6748  C  CA  . MET   B 569 ? 1.1979 1.1699 1.2302 -0.0004 -0.0645 0.0343  873  MET   B CA  
6749  C  C   . MET   B 569 ? 1.2199 1.1856 1.2583 -0.0029 -0.0639 0.0327  873  MET   B C   
6750  O  O   . MET   B 569 ? 1.2181 1.1881 1.2638 -0.0022 -0.0675 0.0301  873  MET   B O   
6751  C  CB  . MET   B 569 ? 1.0961 1.0655 1.1181 0.0053  -0.0684 0.0357  873  MET   B CB  
6752  C  CG  . MET   B 569 ? 1.0788 1.0574 1.0985 0.0086  -0.0710 0.0362  873  MET   B CG  
6753  S  SD  . MET   B 569 ? 1.0415 1.0181 1.0527 0.0153  -0.0759 0.0371  873  MET   B SD  
6754  C  CE  . MET   B 569 ? 1.1767 1.1414 1.1748 0.0159  -0.0735 0.0403  873  MET   B CE  
6755  N  N   . VAL   B 570 ? 1.2188 1.1741 1.2543 -0.0057 -0.0595 0.0343  874  VAL   B N   
6756  C  CA  . VAL   B 570 ? 1.2790 1.2266 1.3194 -0.0081 -0.0587 0.0332  874  VAL   B CA  
6757  C  C   . VAL   B 570 ? 1.3354 1.2698 1.3646 -0.0073 -0.0560 0.0361  874  VAL   B C   
6758  O  O   . VAL   B 570 ? 1.3338 1.2645 1.3545 -0.0073 -0.0525 0.0388  874  VAL   B O   
6759  C  CB  . VAL   B 570 ? 1.2291 1.1782 1.2822 -0.0141 -0.0545 0.0318  874  VAL   B CB  
6760  C  CG1 . VAL   B 570 ? 1.1417 1.1035 1.2045 -0.0147 -0.0568 0.0292  874  VAL   B CG1 
6761  C  CG2 . VAL   B 570 ? 1.2512 1.1952 1.3005 -0.0173 -0.0475 0.0345  874  VAL   B CG2 
6762  N  N   . GLU   B 571 ? 1.3543 1.2813 1.3829 -0.0064 -0.0580 0.0355  875  GLU   B N   
6763  C  CA  . GLU   B 571 ? 1.3840 1.2972 1.4037 -0.0068 -0.0545 0.0381  875  GLU   B CA  
6764  C  C   . GLU   B 571 ? 1.4302 1.3385 1.4554 -0.0129 -0.0473 0.0390  875  GLU   B C   
6765  O  O   . GLU   B 571 ? 1.4749 1.3879 1.5138 -0.0171 -0.0461 0.0367  875  GLU   B O   
6766  C  CB  . GLU   B 571 ? 1.4001 1.3062 1.4194 -0.0052 -0.0580 0.0369  875  GLU   B CB  
6767  C  CG  . GLU   B 571 ? 1.4538 1.3448 1.4644 -0.0059 -0.0542 0.0395  875  GLU   B CG  
6768  C  CD  . GLU   B 571 ? 1.5066 1.3913 1.5266 -0.0124 -0.0486 0.0392  875  GLU   B CD  
6769  O  OE1 . GLU   B 571 ? 1.5174 1.4094 1.5515 -0.0162 -0.0482 0.0368  875  GLU   B OE1 
6770  O  OE2 . GLU   B 571 ? 1.5261 1.3981 1.5397 -0.0135 -0.0446 0.0415  875  GLU   B OE2 
6771  N  N   . PHE   B 572 ? 1.4410 1.3396 1.4557 -0.0133 -0.0422 0.0423  876  PHE   B N   
6772  C  CA  . PHE   B 572 ? 1.4341 1.3267 1.4525 -0.0187 -0.0342 0.0437  876  PHE   B CA  
6773  C  C   . PHE   B 572 ? 1.4462 1.3228 1.4547 -0.0187 -0.0304 0.0465  876  PHE   B C   
6774  O  O   . PHE   B 572 ? 1.4452 1.3144 1.4396 -0.0166 -0.0277 0.0496  876  PHE   B O   
6775  C  CB  . PHE   B 572 ? 1.3844 1.2814 1.3991 -0.0193 -0.0304 0.0453  876  PHE   B CB  
6776  C  CG  . PHE   B 572 ? 1.4031 1.2967 1.4244 -0.0250 -0.0221 0.0462  876  PHE   B CG  
6777  C  CD1 . PHE   B 572 ? 1.4315 1.3317 1.4701 -0.0296 -0.0209 0.0436  876  PHE   B CD1 
6778  C  CD2 . PHE   B 572 ? 1.4263 1.3098 1.4362 -0.0254 -0.0155 0.0497  876  PHE   B CD2 
6779  C  CE1 . PHE   B 572 ? 1.4677 1.3651 1.5133 -0.0347 -0.0129 0.0444  876  PHE   B CE1 
6780  C  CE2 . PHE   B 572 ? 1.4850 1.3650 1.5008 -0.0304 -0.0073 0.0507  876  PHE   B CE2 
6781  C  CZ  . PHE   B 572 ? 1.4978 1.3852 1.5321 -0.0352 -0.0058 0.0481  876  PHE   B CZ  
6782  N  N   . ASN   B 573 ? 1.4131 1.2840 1.4288 -0.0212 -0.0302 0.0453  877  ASN   B N   
6783  C  CA  . ASN   B 573 ? 1.4275 1.2828 1.4359 -0.0220 -0.0260 0.0477  877  ASN   B CA  
6784  C  C   . ASN   B 573 ? 1.4217 1.2695 1.4118 -0.0160 -0.0292 0.0500  877  ASN   B C   
6785  O  O   . ASN   B 573 ? 1.4630 1.3006 1.4402 -0.0151 -0.0247 0.0534  877  ASN   B O   
6786  C  CB  . ASN   B 573 ? 1.4415 1.2895 1.4495 -0.0266 -0.0163 0.0504  877  ASN   B CB  
6787  C  CG  . ASN   B 573 ? 1.4544 1.3115 1.4797 -0.0320 -0.0129 0.0485  877  ASN   B CG  
6788  O  OD1 . ASN   B 573 ? 1.4800 1.3412 1.5046 -0.0331 -0.0088 0.0496  877  ASN   B OD1 
6789  N  ND2 . ASN   B 573 ? 1.4623 1.3224 1.5033 -0.0354 -0.0147 0.0455  877  ASN   B ND2 
6790  N  N   . GLY   B 574 ? 1.4571 1.3101 1.4460 -0.0115 -0.0370 0.0481  878  GLY   B N   
6791  C  CA  . GLY   B 574 ? 1.4408 1.2887 1.4141 -0.0053 -0.0408 0.0498  878  GLY   B CA  
6792  C  C   . GLY   B 574 ? 1.4640 1.3173 1.4280 -0.0017 -0.0417 0.0514  878  GLY   B C   
6793  O  O   . GLY   B 574 ? 1.4928 1.3421 1.4438 0.0036  -0.0449 0.0529  878  GLY   B O   
6794  N  N   . LYS   B 575 ? 1.4543 1.3163 1.4247 -0.0046 -0.0391 0.0509  879  LYS   B N   
6795  C  CA  . LYS   B 575 ? 1.4026 1.2716 1.3667 -0.0017 -0.0405 0.0518  879  LYS   B CA  
6796  C  C   . LYS   B 575 ? 1.3619 1.2474 1.3370 -0.0009 -0.0458 0.0487  879  LYS   B C   
6797  O  O   . LYS   B 575 ? 1.3826 1.2731 1.3684 -0.0019 -0.0486 0.0461  879  LYS   B O   
6798  C  CB  . LYS   B 575 ? 1.3525 1.2175 1.3137 -0.0051 -0.0332 0.0539  879  LYS   B CB  
6799  N  N   . LEU   B 576 ? 1.3367 1.2301 1.3086 0.0010  -0.0472 0.0491  880  LEU   B N   
6800  C  CA  . LEU   B 576 ? 1.3136 1.2222 1.2948 0.0019  -0.0516 0.0466  880  LEU   B CA  
6801  C  C   . LEU   B 576 ? 1.3272 1.2418 1.3113 -0.0010 -0.0481 0.0469  880  LEU   B C   
6802  O  O   . LEU   B 576 ? 1.2863 1.1972 1.2599 0.0004  -0.0465 0.0491  880  LEU   B O   
6803  C  CB  . LEU   B 576 ? 1.2911 1.2044 1.2656 0.0082  -0.0581 0.0466  880  LEU   B CB  
6804  C  CG  . LEU   B 576 ? 1.1727 1.1011 1.1556 0.0098  -0.0627 0.0444  880  LEU   B CG  
6805  C  CD1 . LEU   B 576 ? 1.1989 1.1303 1.1894 0.0108  -0.0664 0.0419  880  LEU   B CD1 
6806  C  CD2 . LEU   B 576 ? 1.1522 1.0846 1.1270 0.0151  -0.0667 0.0455  880  LEU   B CD2 
6807  N  N   . LEU   B 577 ? 1.3086 1.2318 1.3064 -0.0050 -0.0470 0.0446  881  LEU   B N   
6808  C  CA  . LEU   B 577 ? 1.3028 1.2327 1.3052 -0.0079 -0.0437 0.0445  881  LEU   B CA  
6809  C  C   . LEU   B 577 ? 1.2590 1.2031 1.2671 -0.0058 -0.0490 0.0424  881  LEU   B C   
6810  O  O   . LEU   B 577 ? 1.2751 1.2265 1.2943 -0.0067 -0.0515 0.0398  881  LEU   B O   
6811  C  CB  . LEU   B 577 ? 1.3208 1.2500 1.3350 -0.0139 -0.0384 0.0434  881  LEU   B CB  
6812  C  CG  . LEU   B 577 ? 1.2945 1.2265 1.3124 -0.0177 -0.0328 0.0439  881  LEU   B CG  
6813  C  CD1 . LEU   B 577 ? 1.3057 1.2270 1.3097 -0.0173 -0.0276 0.0473  881  LEU   B CD1 
6814  C  CD2 . LEU   B 577 ? 1.2956 1.2285 1.3283 -0.0232 -0.0286 0.0422  881  LEU   B CD2 
6815  N  N   . ALA   B 578 ? 1.1951 1.1426 1.1956 -0.0029 -0.0509 0.0436  882  ALA   B N   
6816  C  CA  . ALA   B 578 ? 1.1679 1.1285 1.1732 -0.0008 -0.0555 0.0420  882  ALA   B CA  
6817  C  C   . ALA   B 578 ? 1.1983 1.1646 1.2068 -0.0037 -0.0525 0.0419  882  ALA   B C   
6818  O  O   . ALA   B 578 ? 1.2842 1.2437 1.2852 -0.0049 -0.0484 0.0439  882  ALA   B O   
6819  C  CB  . ALA   B 578 ? 1.1116 1.0729 1.1074 0.0049  -0.0604 0.0432  882  ALA   B CB  
6820  N  N   . SER   B 579 ? 1.1681 1.1461 1.1869 -0.0047 -0.0544 0.0397  883  SER   B N   
6821  C  CA  . SER   B 579 ? 1.1513 1.1356 1.1721 -0.0066 -0.0526 0.0396  883  SER   B CA  
6822  C  C   . SER   B 579 ? 1.1206 1.1124 1.1377 -0.0026 -0.0576 0.0397  883  SER   B C   
6823  O  O   . SER   B 579 ? 1.1190 1.1170 1.1394 0.0003  -0.0622 0.0386  883  SER   B O   
6824  C  CB  . SER   B 579 ? 1.1628 1.1548 1.1972 -0.0105 -0.0511 0.0371  883  SER   B CB  
6825  O  OG  . SER   B 579 ? 1.1873 1.1858 1.2298 -0.0092 -0.0553 0.0348  883  SER   B OG  
6826  N  N   . ILE   B 580 ? 1.1045 1.0950 1.1144 -0.0023 -0.0566 0.0412  884  ILE   B N   
6827  C  CA  . ILE   B 580 ? 1.0857 1.0832 1.0927 0.0010  -0.0611 0.0413  884  ILE   B CA  
6828  C  C   . ILE   B 580 ? 1.1201 1.1228 1.1301 -0.0019 -0.0589 0.0409  884  ILE   B C   
6829  O  O   . ILE   B 580 ? 1.1511 1.1470 1.1538 -0.0032 -0.0555 0.0423  884  ILE   B O   
6830  C  CB  . ILE   B 580 ? 1.0804 1.0701 1.0742 0.0048  -0.0632 0.0435  884  ILE   B CB  
6831  C  CG1 . ILE   B 580 ? 1.0958 1.0792 1.0864 0.0074  -0.0647 0.0440  884  ILE   B CG1 
6832  C  CG2 . ILE   B 580 ? 1.0854 1.0829 1.0780 0.0081  -0.0683 0.0434  884  ILE   B CG2 
6833  C  CD1 . ILE   B 580 ? 1.1586 1.1275 1.1401 0.0063  -0.0604 0.0459  884  ILE   B CD1 
6834  N  N   . ASN   B 581 ? 1.0879 1.1019 1.1082 -0.0027 -0.0607 0.0389  885  ASN   B N   
6835  C  CA  . ASN   B 581 ? 1.0732 1.0935 1.0980 -0.0053 -0.0591 0.0381  885  ASN   B CA  
6836  C  C   . ASN   B 581 ? 1.1210 1.1360 1.1477 -0.0098 -0.0529 0.0381  885  ASN   B C   
6837  O  O   . ASN   B 581 ? 1.1743 1.1906 1.2098 -0.0121 -0.0511 0.0367  885  ASN   B O   
6838  C  CB  . ASN   B 581 ? 1.0567 1.0776 1.0736 -0.0032 -0.0614 0.0392  885  ASN   B CB  
6839  C  CG  . ASN   B 581 ? 1.0670 1.0968 1.0866 0.0004  -0.0672 0.0386  885  ASN   B CG  
6840  O  OD1 . ASN   B 581 ? 1.0686 1.1032 1.0947 0.0016  -0.0692 0.0376  885  ASN   B OD1 
6841  N  ND2 . ASN   B 581 ? 1.1649 1.1966 1.1797 0.0022  -0.0700 0.0393  885  ASN   B ND2 
6842  N  N   . SER   B 582 ? 1.1169 1.1255 1.1357 -0.0108 -0.0494 0.0396  886  SER   B N   
6843  C  CA  . SER   B 582 ? 1.1555 1.1588 1.1763 -0.0149 -0.0428 0.0398  886  SER   B CA  
6844  C  C   . SER   B 582 ? 1.2174 1.2069 1.2286 -0.0150 -0.0387 0.0421  886  SER   B C   
6845  O  O   . SER   B 582 ? 1.2754 1.2581 1.2834 -0.0174 -0.0328 0.0432  886  SER   B O   
6846  C  CB  . SER   B 582 ? 1.1908 1.1967 1.2104 -0.0165 -0.0406 0.0398  886  SER   B CB  
6847  O  OG  . SER   B 582 ? 1.2224 1.2216 1.2284 -0.0141 -0.0414 0.0417  886  SER   B OG  
6848  N  N   . THR   B 583 ? 1.2092 1.1941 1.2158 -0.0122 -0.0415 0.0429  887  THR   B N   
6849  C  CA  . THR   B 583 ? 1.2319 1.2030 1.2277 -0.0116 -0.0382 0.0452  887  THR   B CA  
6850  C  C   . THR   B 583 ? 1.2291 1.1973 1.2301 -0.0120 -0.0383 0.0447  887  THR   B C   
6851  O  O   . THR   B 583 ? 1.2291 1.2025 1.2331 -0.0094 -0.0437 0.0437  887  THR   B O   
6852  C  CB  . THR   B 583 ? 1.1876 1.1537 1.1693 -0.0070 -0.0422 0.0469  887  THR   B CB  
6853  O  OG1 . THR   B 583 ? 1.1857 1.1524 1.1616 -0.0068 -0.0418 0.0474  887  THR   B OG1 
6854  C  CG2 . THR   B 583 ? 1.2579 1.2094 1.2280 -0.0058 -0.0395 0.0493  887  THR   B CG2 
6855  N  N   . VAL   B 584 ? 1.2432 1.2029 1.2453 -0.0152 -0.0322 0.0456  888  VAL   B N   
6856  C  CA  . VAL   B 584 ? 1.2132 1.1676 1.2183 -0.0156 -0.0320 0.0454  888  VAL   B CA  
6857  C  C   . VAL   B 584 ? 1.3006 1.2415 1.2903 -0.0129 -0.0310 0.0483  888  VAL   B C   
6858  O  O   . VAL   B 584 ? 1.4010 1.3315 1.3835 -0.0144 -0.0249 0.0504  888  VAL   B O   
6859  C  CB  . VAL   B 584 ? 1.2177 1.1706 1.2341 -0.0208 -0.0261 0.0446  888  VAL   B CB  
6860  C  CG1 . VAL   B 584 ? 1.2097 1.1592 1.2313 -0.0210 -0.0276 0.0438  888  VAL   B CG1 
6861  C  CG2 . VAL   B 584 ? 1.2313 1.1964 1.2611 -0.0234 -0.0265 0.0420  888  VAL   B CG2 
6862  N  N   . ARG   B 585 ? 1.2762 1.2171 1.2605 -0.0085 -0.0369 0.0484  889  ARG   B N   
6863  C  CA  . ARG   B 585 ? 1.2583 1.1871 1.2277 -0.0051 -0.0372 0.0509  889  ARG   B CA  
6864  C  C   . ARG   B 585 ? 1.2685 1.1899 1.2393 -0.0055 -0.0364 0.0510  889  ARG   B C   
6865  O  O   . ARG   B 585 ? 1.2699 1.1981 1.2511 -0.0058 -0.0395 0.0489  889  ARG   B O   
6866  C  CB  . ARG   B 585 ? 1.2521 1.1856 1.2149 0.0003  -0.0445 0.0508  889  ARG   B CB  
6867  C  CG  . ARG   B 585 ? 1.2955 1.2170 1.2425 0.0043  -0.0456 0.0532  889  ARG   B CG  
6868  C  CD  . ARG   B 585 ? 1.2650 1.1923 1.2068 0.0092  -0.0526 0.0531  889  ARG   B CD  
6869  N  NE  . ARG   B 585 ? 1.2875 1.2239 1.2328 0.0083  -0.0534 0.0522  889  ARG   B NE  
6870  C  CZ  . ARG   B 585 ? 1.2846 1.2252 1.2251 0.0118  -0.0585 0.0522  889  ARG   B CZ  
6871  N  NH1 . ARG   B 585 ? 1.2770 1.2146 1.2098 0.0167  -0.0636 0.0529  889  ARG   B NH1 
6872  N  NH2 . ARG   B 585 ? 1.2850 1.2330 1.2289 0.0103  -0.0587 0.0514  889  ARG   B NH2 
6873  N  N   . LEU   B 586 ? 1.3358 1.2429 1.2958 -0.0054 -0.0321 0.0536  890  LEU   B N   
6874  C  CA  . LEU   B 586 ? 1.3334 1.2321 1.2924 -0.0051 -0.0319 0.0540  890  LEU   B CA  
6875  C  C   . LEU   B 586 ? 1.3363 1.2281 1.2809 0.0006  -0.0365 0.0556  890  LEU   B C   
6876  O  O   . LEU   B 586 ? 1.3381 1.2240 1.2697 0.0032  -0.0363 0.0575  890  LEU   B O   
6877  C  CB  . LEU   B 586 ? 1.3317 1.2184 1.2900 -0.0094 -0.0235 0.0557  890  LEU   B CB  
6878  C  CG  . LEU   B 586 ? 1.3567 1.2354 1.3177 -0.0105 -0.0225 0.0558  890  LEU   B CG  
6879  C  CD1 . LEU   B 586 ? 1.3072 1.1961 1.2816 -0.0106 -0.0281 0.0525  890  LEU   B CD1 
6880  C  CD2 . LEU   B 586 ? 1.4994 1.3701 1.4650 -0.0159 -0.0135 0.0569  890  LEU   B CD2 
6881  N  N   . TYR   B 587 ? 1.3028 1.1953 1.2498 0.0029  -0.0409 0.0546  891  TYR   B N   
6882  C  CA  . TYR   B 587 ? 1.3109 1.1980 1.2459 0.0086  -0.0457 0.0558  891  TYR   B CA  
6883  C  C   . TYR   B 587 ? 1.3444 1.2186 1.2749 0.0086  -0.0437 0.0569  891  TYR   B C   
6884  O  O   . TYR   B 587 ? 1.3640 1.2374 1.3043 0.0046  -0.0409 0.0558  891  TYR   B O   
6885  C  CB  . TYR   B 587 ? 1.2673 1.1669 1.2080 0.0123  -0.0533 0.0537  891  TYR   B CB  
6886  C  CG  . TYR   B 587 ? 1.2688 1.1785 1.2089 0.0145  -0.0568 0.0533  891  TYR   B CG  
6887  C  CD1 . TYR   B 587 ? 1.3405 1.2461 1.2679 0.0190  -0.0597 0.0549  891  TYR   B CD1 
6888  C  CD2 . TYR   B 587 ? 1.3238 1.2472 1.2763 0.0122  -0.0576 0.0512  891  TYR   B CD2 
6889  C  CE1 . TYR   B 587 ? 1.3690 1.2841 1.2969 0.0208  -0.0634 0.0544  891  TYR   B CE1 
6890  C  CE2 . TYR   B 587 ? 1.3130 1.2456 1.2655 0.0140  -0.0609 0.0508  891  TYR   B CE2 
6891  C  CZ  . TYR   B 587 ? 1.2740 1.2026 1.2146 0.0182  -0.0638 0.0524  891  TYR   B CZ  
6892  O  OH  . TYR   B 587 ? 1.2474 1.1854 1.1894 0.0197  -0.0672 0.0518  891  TYR   B OH  
6893  N  N   . GLU   B 588 ? 1.3840 1.2479 1.2997 0.0130  -0.0455 0.0590  892  GLU   B N   
6894  C  CA  . GLU   B 588 ? 1.4053 1.2571 1.3155 0.0140  -0.0447 0.0600  892  GLU   B CA  
6895  C  C   . GLU   B 588 ? 1.4660 1.3195 1.3706 0.0204  -0.0522 0.0596  892  GLU   B C   
6896  O  O   . GLU   B 588 ? 1.4365 1.2970 1.3376 0.0243  -0.0569 0.0595  892  GLU   B O   
6897  C  CB  . GLU   B 588 ? 1.4126 1.2472 1.3087 0.0134  -0.0385 0.0633  892  GLU   B CB  
6898  C  CG  . GLU   B 588 ? 1.4821 1.3147 1.3827 0.0076  -0.0304 0.0640  892  GLU   B CG  
6899  C  CD  . GLU   B 588 ? 1.6236 1.4381 1.5113 0.0066  -0.0231 0.0673  892  GLU   B CD  
6900  O  OE1 . GLU   B 588 ? 1.6763 1.4812 1.5470 0.0111  -0.0242 0.0695  892  GLU   B OE1 
6901  O  OE2 . GLU   B 588 ? 1.6808 1.4902 1.5753 0.0014  -0.0160 0.0678  892  GLU   B OE2 
6902  N  N   . TRP   B 589 ? 1.4878 1.3353 1.3925 0.0213  -0.0534 0.0593  893  TRP   B N   
6903  C  CA  . TRP   B 589 ? 1.5611 1.4092 1.4607 0.0274  -0.0600 0.0590  893  TRP   B CA  
6904  C  C   . TRP   B 589 ? 1.6775 1.5096 1.5598 0.0309  -0.0592 0.0619  893  TRP   B C   
6905  O  O   . TRP   B 589 ? 1.7322 1.5512 1.6102 0.0287  -0.0548 0.0632  893  TRP   B O   
6906  C  CB  . TRP   B 589 ? 1.5357 1.3864 1.4450 0.0267  -0.0621 0.0568  893  TRP   B CB  
6907  C  CG  . TRP   B 589 ? 1.5454 1.4002 1.4531 0.0327  -0.0690 0.0558  893  TRP   B CG  
6908  C  CD1 . TRP   B 589 ? 1.5942 1.4421 1.4999 0.0348  -0.0710 0.0554  893  TRP   B CD1 
6909  C  CD2 . TRP   B 589 ? 1.5367 1.4033 1.4453 0.0373  -0.0745 0.0550  893  TRP   B CD2 
6910  N  NE1 . TRP   B 589 ? 1.5608 1.4154 1.4656 0.0407  -0.0772 0.0545  893  TRP   B NE1 
6911  C  CE2 . TRP   B 589 ? 1.5453 1.4117 1.4524 0.0423  -0.0793 0.0542  893  TRP   B CE2 
6912  C  CE3 . TRP   B 589 ? 1.5435 1.4208 1.4545 0.0378  -0.0758 0.0548  893  TRP   B CE3 
6913  C  CZ2 . TRP   B 589 ? 1.5635 1.4401 1.4717 0.0476  -0.0848 0.0535  893  TRP   B CZ2 
6914  C  CZ3 . TRP   B 589 ? 1.5796 1.4670 1.4920 0.0429  -0.0815 0.0540  893  TRP   B CZ3 
6915  C  CH2 . TRP   B 589 ? 1.5663 1.4534 1.4776 0.0477  -0.0858 0.0534  893  TRP   B CH2 
6916  N  N   . THR   B 590 ? 1.7465 1.5791 1.6187 0.0363  -0.0635 0.0628  894  THR   B N   
6917  C  CA  . THR   B 590 ? 1.7798 1.5969 1.6343 0.0399  -0.0629 0.0655  894  THR   B CA  
6918  C  C   . THR   B 590 ? 1.8067 1.6179 1.6556 0.0448  -0.0672 0.0656  894  THR   B C   
6919  O  O   . THR   B 590 ? 1.7656 1.5864 1.6230 0.0468  -0.0719 0.0636  894  THR   B O   
6920  C  CB  . THR   B 590 ? 1.8171 1.6361 1.6626 0.0436  -0.0659 0.0664  894  THR   B CB  
6921  O  OG1 . THR   B 590 ? 1.9033 1.7049 1.7314 0.0452  -0.0628 0.0693  894  THR   B OG1 
6922  C  CG2 . THR   B 590 ? 1.8667 1.6940 1.7118 0.0501  -0.0742 0.0654  894  THR   B CG2 
6923  N  N   . THR   B 591 ? 1.8482 1.6428 1.6817 0.0471  -0.0654 0.0682  895  THR   B N   
6924  C  CA  . THR   B 591 ? 1.9051 1.6914 1.7320 0.0513  -0.0685 0.0685  895  THR   B CA  
6925  C  C   . THR   B 591 ? 1.9263 1.7230 1.7544 0.0578  -0.0768 0.0671  895  THR   B C   
6926  O  O   . THR   B 591 ? 1.9178 1.7161 1.7495 0.0601  -0.0800 0.0659  895  THR   B O   
6927  C  CB  . THR   B 591 ? 1.9112 1.6778 1.7197 0.0532  -0.0654 0.0717  895  THR   B CB  
6928  O  OG1 . THR   B 591 ? 1.9536 1.7192 1.7508 0.0577  -0.0685 0.0728  895  THR   B OG1 
6929  C  CG2 . THR   B 591 ? 1.8598 1.6167 1.6681 0.0466  -0.0564 0.0732  895  THR   B CG2 
6930  N  N   . GLU   B 592 ? 2.0031 1.8073 1.8289 0.0607  -0.0804 0.0671  896  GLU   B N   
6931  C  CA  . GLU   B 592 ? 1.9831 1.7982 1.8117 0.0667  -0.0879 0.0658  896  GLU   B CA  
6932  C  C   . GLU   B 592 ? 1.9819 1.8154 1.8281 0.0645  -0.0895 0.0632  896  GLU   B C   
6933  O  O   . GLU   B 592 ? 1.9659 1.8116 1.8170 0.0681  -0.0946 0.0621  896  GLU   B O   
6934  C  CB  . GLU   B 592 ? 2.0279 1.8431 1.8473 0.0710  -0.0916 0.0668  896  GLU   B CB  
6935  C  CG  . GLU   B 592 ? 2.1155 1.9119 1.9158 0.0738  -0.0904 0.0694  896  GLU   B CG  
6936  C  CD  . GLU   B 592 ? 2.1680 1.9565 1.9619 0.0693  -0.0843 0.0710  896  GLU   B CD  
6937  O  OE1 . GLU   B 592 ? 2.1396 1.9294 1.9418 0.0628  -0.0782 0.0707  896  GLU   B OE1 
6938  O  OE2 . GLU   B 592 ? 2.2156 1.9964 1.9961 0.0725  -0.0858 0.0724  896  GLU   B OE2 
6939  N  N   . LYS   B 593 ? 1.9422 1.7775 1.7982 0.0587  -0.0851 0.0621  897  LYS   B N   
6940  C  CA  . LYS   B 593 ? 1.8224 1.6733 1.6946 0.0565  -0.0863 0.0595  897  LYS   B CA  
6941  C  C   . LYS   B 593 ? 1.8427 1.7072 1.7211 0.0560  -0.0878 0.0588  897  LYS   B C   
6942  O  O   . LYS   B 593 ? 1.7858 1.6616 1.6687 0.0600  -0.0928 0.0578  897  LYS   B O   
6943  C  CB  . LYS   B 593 ? 1.7313 1.5863 1.6065 0.0613  -0.0912 0.0582  897  LYS   B CB  
6944  N  N   . GLU   B 594 ? 1.9442 1.8071 1.8229 0.0511  -0.0831 0.0594  898  GLU   B N   
6945  C  CA  . GLU   B 594 ? 1.9333 1.8073 1.8170 0.0498  -0.0838 0.0588  898  GLU   B CA  
6946  C  C   . GLU   B 594 ? 1.9309 1.8035 1.8190 0.0429  -0.0772 0.0589  898  GLU   B C   
6947  O  O   . GLU   B 594 ? 1.9478 1.8076 1.8299 0.0402  -0.0722 0.0603  898  GLU   B O   
6948  C  CB  . GLU   B 594 ? 1.9606 1.8308 1.8323 0.0545  -0.0871 0.0603  898  GLU   B CB  
6949  C  CG  . GLU   B 594 ? 1.9994 1.8757 1.8721 0.0526  -0.0867 0.0603  898  GLU   B CG  
6950  C  CD  . GLU   B 594 ? 2.0657 1.9604 1.9542 0.0510  -0.0887 0.0580  898  GLU   B CD  
6951  O  OE1 . GLU   B 594 ? 1.9928 1.8963 1.8902 0.0527  -0.0916 0.0565  898  GLU   B OE1 
6952  O  OE2 . GLU   B 594 ? 2.0886 1.9885 1.9799 0.0481  -0.0873 0.0577  898  GLU   B OE2 
6953  N  N   . LEU   B 595 ? 1.7315 1.6173 1.6307 0.0401  -0.0771 0.0573  899  LEU   B N   
6954  C  CA  . LEU   B 595 ? 1.6423 1.5285 1.5467 0.0339  -0.0712 0.0572  899  LEU   B CA  
6955  C  C   . LEU   B 595 ? 1.5762 1.4564 1.4701 0.0337  -0.0691 0.0590  899  LEU   B C   
6956  O  O   . LEU   B 595 ? 1.6498 1.5335 1.5387 0.0377  -0.0736 0.0592  899  LEU   B O   
6957  C  CB  . LEU   B 595 ? 1.5900 1.4926 1.5100 0.0312  -0.0722 0.0547  899  LEU   B CB  
6958  C  CG  . LEU   B 595 ? 1.4145 1.3249 1.3485 0.0286  -0.0722 0.0523  899  LEU   B CG  
6959  C  CD1 . LEU   B 595 ? 1.3695 1.2720 1.3069 0.0233  -0.0665 0.0522  899  LEU   B CD1 
6960  C  CD2 . LEU   B 595 ? 1.4206 1.3332 1.3554 0.0333  -0.0772 0.0514  899  LEU   B CD2 
6961  N  N   . ARG   B 596 ? 1.4418 1.3134 1.3333 0.0291  -0.0623 0.0601  900  ARG   B N   
6962  C  CA  . ARG   B 596 ? 1.4789 1.3445 1.3603 0.0289  -0.0596 0.0618  900  ARG   B CA  
6963  C  C   . ARG   B 596 ? 1.4509 1.3171 1.3390 0.0226  -0.0525 0.0617  900  ARG   B C   
6964  O  O   . ARG   B 596 ? 1.4696 1.3326 1.3643 0.0185  -0.0477 0.0616  900  ARG   B O   
6965  C  CB  . ARG   B 596 ? 1.5433 1.3907 1.4063 0.0319  -0.0581 0.0646  900  ARG   B CB  
6966  C  CG  . ARG   B 596 ? 1.5700 1.4125 1.4201 0.0345  -0.0590 0.0659  900  ARG   B CG  
6967  C  CD  . ARG   B 596 ? 1.6100 1.4647 1.4626 0.0390  -0.0676 0.0644  900  ARG   B CD  
6968  N  NE  . ARG   B 596 ? 1.6826 1.5407 1.5317 0.0395  -0.0690 0.0643  900  ARG   B NE  
6969  C  CZ  . ARG   B 596 ? 1.5591 1.4299 1.4197 0.0361  -0.0685 0.0626  900  ARG   B CZ  
6970  N  NH1 . ARG   B 596 ? 1.4001 1.2807 1.2760 0.0317  -0.0659 0.0611  900  ARG   B NH1 
6971  N  NH2 . ARG   B 596 ? 1.5874 1.4609 1.4437 0.0375  -0.0713 0.0624  900  ARG   B NH2 
6972  N  N   . THR   B 597 ? 1.4485 1.3185 1.3349 0.0219  -0.0519 0.0618  901  THR   B N   
6973  C  CA  . THR   B 597 ? 1.4181 1.2893 1.3106 0.0163  -0.0453 0.0617  901  THR   B CA  
6974  C  C   . THR   B 597 ? 1.4486 1.3032 1.3315 0.0141  -0.0374 0.0642  901  THR   B C   
6975  O  O   . THR   B 597 ? 1.5044 1.3463 1.3709 0.0172  -0.0367 0.0665  901  THR   B O   
6976  C  CB  . THR   B 597 ? 1.4548 1.3320 1.3450 0.0168  -0.0468 0.0613  901  THR   B CB  
6977  O  OG1 . THR   B 597 ? 1.4756 1.3666 1.3723 0.0198  -0.0545 0.0594  901  THR   B OG1 
6978  C  CG2 . THR   B 597 ? 1.4527 1.3343 1.3523 0.0111  -0.0405 0.0607  901  THR   B CG2 
6979  N  N   . GLU   B 598 ? 1.4819 1.3363 1.3753 0.0087  -0.0313 0.0638  902  GLU   B N   
6980  C  CA  . GLU   B 598 ? 1.5166 1.3568 1.4035 0.0057  -0.0224 0.0663  902  GLU   B CA  
6981  C  C   . GLU   B 598 ? 1.5685 1.4109 1.4573 0.0024  -0.0171 0.0665  902  GLU   B C   
6982  O  O   . GLU   B 598 ? 1.6348 1.4658 1.5097 0.0033  -0.0128 0.0688  902  GLU   B O   
6983  C  CB  . GLU   B 598 ? 1.4687 1.3062 1.3663 0.0015  -0.0181 0.0659  902  GLU   B CB  
6984  C  CG  . GLU   B 598 ? 1.5943 1.4169 1.4861 -0.0019 -0.0082 0.0686  902  GLU   B CG  
6985  C  CD  . GLU   B 598 ? 1.6328 1.4558 1.5399 -0.0076 -0.0031 0.0677  902  GLU   B CD  
6986  O  OE1 . GLU   B 598 ? 1.5643 1.3970 1.4843 -0.0084 -0.0078 0.0651  902  GLU   B OE1 
6987  O  OE2 . GLU   B 598 ? 1.7136 1.5267 1.6196 -0.0112 0.0058  0.0697  902  GLU   B OE2 
6988  N  N   . CYS   B 599 ? 1.6388 1.4956 1.5441 -0.0012 -0.0174 0.0640  903  CYS   B N   
6989  C  CA  . CYS   B 599 ? 1.6740 1.5344 1.5835 -0.0046 -0.0123 0.0638  903  CYS   B CA  
6990  C  C   . CYS   B 599 ? 1.6365 1.5148 1.5585 -0.0050 -0.0178 0.0609  903  CYS   B C   
6991  O  O   . CYS   B 599 ? 1.5799 1.4680 1.5101 -0.0036 -0.0242 0.0588  903  CYS   B O   
6992  C  CB  . CYS   B 599 ? 1.7143 1.5707 1.6334 -0.0104 -0.0035 0.0642  903  CYS   B CB  
6993  S  SG  . CYS   B 599 ? 1.7408 1.6022 1.6759 -0.0128 -0.0056 0.0622  903  CYS   B SG  
6994  N  N   . ASN   B 600 ? 1.6195 1.5014 1.5424 -0.0067 -0.0150 0.0607  904  ASN   B N   
6995  C  CA  . ASN   B 600 ? 1.5287 1.4267 1.4630 -0.0074 -0.0193 0.0580  904  ASN   B CA  
6996  C  C   . ASN   B 600 ? 1.5338 1.4352 1.4776 -0.0125 -0.0126 0.0575  904  ASN   B C   
6997  O  O   . ASN   B 600 ? 1.5515 1.4425 1.4876 -0.0139 -0.0055 0.0595  904  ASN   B O   
6998  C  CB  . ASN   B 600 ? 1.5379 1.4381 1.4617 -0.0032 -0.0250 0.0582  904  ASN   B CB  
6999  C  CG  . ASN   B 600 ? 1.4602 1.3695 1.3868 0.0006  -0.0340 0.0567  904  ASN   B CG  
7000  O  OD1 . ASN   B 600 ? 1.4315 1.3495 1.3706 -0.0004 -0.0363 0.0549  904  ASN   B OD1 
7001  N  ND2 . ASN   B 600 ? 1.4562 1.3633 1.3713 0.0052  -0.0391 0.0574  904  ASN   B ND2 
7002  N  N   . HIS   B 601 ? 1.4390 1.3544 1.3993 -0.0150 -0.0147 0.0547  905  HIS   B N   
7003  C  CA  . HIS   B 601 ? 1.4185 1.3396 1.3892 -0.0193 -0.0097 0.0536  905  HIS   B CA  
7004  C  C   . HIS   B 601 ? 1.3796 1.3155 1.3576 -0.0187 -0.0153 0.0512  905  HIS   B C   
7005  O  O   . HIS   B 601 ? 1.3529 1.2993 1.3419 -0.0186 -0.0204 0.0489  905  HIS   B O   
7006  C  CB  . HIS   B 601 ? 1.3652 1.2879 1.3509 -0.0237 -0.0057 0.0525  905  HIS   B CB  
7007  C  CG  . HIS   B 601 ? 1.3741 1.2993 1.3689 -0.0282 0.0012  0.0521  905  HIS   B CG  
7008  N  ND1 . HIS   B 601 ? 1.3840 1.3217 1.3882 -0.0294 -0.0007 0.0498  905  HIS   B ND1 
7009  C  CD2 . HIS   B 601 ? 1.4000 1.3166 1.3960 -0.0316 0.0101  0.0536  905  HIS   B CD2 
7010  C  CE1 . HIS   B 601 ? 1.3657 1.3026 1.3767 -0.0333 0.0065  0.0499  905  HIS   B CE1 
7011  N  NE2 . HIS   B 601 ? 1.3720 1.2965 1.3786 -0.0347 0.0133  0.0522  905  HIS   B NE2 
7012  N  N   . TYR   B 602 ? 1.3582 1.2943 1.3298 -0.0181 -0.0144 0.0517  906  TYR   B N   
7013  C  CA  . TYR   B 602 ? 1.3305 1.2796 1.3081 -0.0176 -0.0193 0.0497  906  TYR   B CA  
7014  C  C   . TYR   B 602 ? 1.3496 1.3058 1.3405 -0.0221 -0.0149 0.0481  906  TYR   B C   
7015  O  O   . TYR   B 602 ? 1.3784 1.3278 1.3676 -0.0246 -0.0075 0.0493  906  TYR   B O   
7016  C  CB  . TYR   B 602 ? 1.3507 1.2960 1.3140 -0.0145 -0.0215 0.0509  906  TYR   B CB  
7017  C  CG  . TYR   B 602 ? 1.3804 1.3142 1.3279 -0.0104 -0.0237 0.0530  906  TYR   B CG  
7018  C  CD1 . TYR   B 602 ? 1.3706 1.3084 1.3171 -0.0067 -0.0312 0.0525  906  TYR   B CD1 
7019  C  CD2 . TYR   B 602 ? 1.4171 1.3357 1.3503 -0.0099 -0.0181 0.0556  906  TYR   B CD2 
7020  C  CE1 . TYR   B 602 ? 1.3660 1.2932 1.2980 -0.0026 -0.0336 0.0543  906  TYR   B CE1 
7021  C  CE2 . TYR   B 602 ? 1.4645 1.3719 1.3823 -0.0057 -0.0204 0.0576  906  TYR   B CE2 
7022  C  CZ  . TYR   B 602 ? 1.4517 1.3636 1.3693 -0.0021 -0.0283 0.0568  906  TYR   B CZ  
7023  O  OH  . TYR   B 602 ? 1.5952 1.4960 1.4977 0.0022  -0.0308 0.0587  906  TYR   B OH  
7024  N  N   . ASN   B 603 ? 1.3889 1.3583 1.3932 -0.0230 -0.0191 0.0454  907  ASN   B N   
7025  C  CA  . ASN   B 603 ? 1.3557 1.3329 1.3737 -0.0268 -0.0159 0.0435  907  ASN   B CA  
7026  C  C   . ASN   B 603 ? 1.3039 1.2903 1.3230 -0.0263 -0.0189 0.0422  907  ASN   B C   
7027  O  O   . ASN   B 603 ? 1.3146 1.3027 1.3258 -0.0230 -0.0240 0.0426  907  ASN   B O   
7028  C  CB  . ASN   B 603 ? 1.3692 1.3541 1.4021 -0.0283 -0.0185 0.0411  907  ASN   B CB  
7029  C  CG  . ASN   B 603 ? 1.3626 1.3392 1.3949 -0.0285 -0.0172 0.0420  907  ASN   B CG  
7030  O  OD1 . ASN   B 603 ? 1.3468 1.3250 1.3791 -0.0260 -0.0226 0.0414  907  ASN   B OD1 
7031  N  ND2 . ASN   B 603 ? 1.3834 1.3508 1.4153 -0.0313 -0.0098 0.0435  907  ASN   B ND2 
7032  N  N   . ASN   B 604 ? 1.2668 1.2594 1.2968 -0.0296 -0.0157 0.0407  908  ASN   B N   
7033  C  CA  . ASN   B 604 ? 1.2289 1.2311 1.2626 -0.0297 -0.0180 0.0391  908  ASN   B CA  
7034  C  C   . ASN   B 604 ? 1.2516 1.2663 1.2989 -0.0300 -0.0230 0.0363  908  ASN   B C   
7035  O  O   . ASN   B 604 ? 1.2534 1.2766 1.3057 -0.0304 -0.0247 0.0348  908  ASN   B O   
7036  C  CB  . ASN   B 604 ? 1.2253 1.2256 1.2612 -0.0327 -0.0110 0.0393  908  ASN   B CB  
7037  C  CG  . ASN   B 604 ? 1.2661 1.2666 1.3150 -0.0365 -0.0059 0.0384  908  ASN   B CG  
7038  O  OD1 . ASN   B 604 ? 1.3149 1.3072 1.3628 -0.0374 -0.0021 0.0397  908  ASN   B OD1 
7039  N  ND2 . ASN   B 604 ? 1.2963 1.3063 1.3580 -0.0387 -0.0057 0.0360  908  ASN   B ND2 
7040  N  N   . ILE   B 605 ? 1.2770 1.2921 1.3297 -0.0297 -0.0251 0.0356  909  ILE   B N   
7041  C  CA  . ILE   B 605 ? 1.2438 1.2690 1.3072 -0.0292 -0.0303 0.0331  909  ILE   B CA  
7042  C  C   . ILE   B 605 ? 1.2874 1.3118 1.3454 -0.0255 -0.0358 0.0336  909  ILE   B C   
7043  O  O   . ILE   B 605 ? 1.2600 1.2753 1.3085 -0.0240 -0.0350 0.0356  909  ILE   B O   
7044  C  CB  . ILE   B 605 ? 1.1788 1.2055 1.2555 -0.0323 -0.0279 0.0312  909  ILE   B CB  
7045  C  CG1 . ILE   B 605 ? 1.2014 1.2184 1.2760 -0.0328 -0.0255 0.0325  909  ILE   B CG1 
7046  C  CG2 . ILE   B 605 ? 1.1962 1.2241 1.2790 -0.0358 -0.0223 0.0307  909  ILE   B CG2 
7047  C  CD1 . ILE   B 605 ? 1.2029 1.2204 1.2910 -0.0361 -0.0233 0.0306  909  ILE   B CD1 
7048  N  N   . MET   B 606 ? 1.3188 1.3523 1.3825 -0.0237 -0.0412 0.0318  910  MET   B N   
7049  C  CA  . MET   B 606 ? 1.2928 1.3260 1.3532 -0.0202 -0.0460 0.0321  910  MET   B CA  
7050  C  C   . MET   B 606 ? 1.2824 1.3106 1.3473 -0.0211 -0.0451 0.0315  910  MET   B C   
7051  O  O   . MET   B 606 ? 1.2888 1.3215 1.3646 -0.0229 -0.0454 0.0292  910  MET   B O   
7052  C  CB  . MET   B 606 ? 1.2981 1.3421 1.3636 -0.0180 -0.0513 0.0304  910  MET   B CB  
7053  C  CG  . MET   B 606 ? 1.3469 1.3915 1.4059 -0.0137 -0.0561 0.0314  910  MET   B CG  
7054  S  SD  . MET   B 606 ? 1.6118 1.6686 1.6743 -0.0114 -0.0607 0.0304  910  MET   B SD  
7055  C  CE  . MET   B 606 ? 1.3516 1.4061 1.4047 -0.0114 -0.0599 0.0323  910  MET   B CE  
7056  N  N   . ALA   B 607 ? 1.1942 1.2129 1.2510 -0.0199 -0.0442 0.0334  911  ALA   B N   
7057  C  CA  . ALA   B 607 ? 1.1377 1.1508 1.1981 -0.0208 -0.0435 0.0329  911  ALA   B CA  
7058  C  C   . ALA   B 607 ? 1.1577 1.1757 1.2221 -0.0179 -0.0494 0.0312  911  ALA   B C   
7059  O  O   . ALA   B 607 ? 1.1030 1.1162 1.1610 -0.0150 -0.0518 0.0321  911  ALA   B O   
7060  C  CB  . ALA   B 607 ? 1.1466 1.1476 1.1962 -0.0200 -0.0410 0.0356  911  ALA   B CB  
7061  N  N   . LEU   B 608 ? 1.1699 1.1965 1.2446 -0.0187 -0.0514 0.0286  912  LEU   B N   
7062  C  CA  . LEU   B 608 ? 1.1140 1.1453 1.1921 -0.0157 -0.0568 0.0268  912  LEU   B CA  
7063  C  C   . LEU   B 608 ? 1.1339 1.1601 1.2171 -0.0165 -0.0574 0.0254  912  LEU   B C   
7064  O  O   . LEU   B 608 ? 1.1406 1.1657 1.2215 -0.0132 -0.0614 0.0249  912  LEU   B O   
7065  C  CB  . LEU   B 608 ? 1.0964 1.1380 1.1824 -0.0160 -0.0587 0.0246  912  LEU   B CB  
7066  C  CG  . LEU   B 608 ? 1.1145 1.1632 1.1965 -0.0127 -0.0619 0.0251  912  LEU   B CG  
7067  C  CD1 . LEU   B 608 ? 1.1472 1.1943 1.2204 -0.0121 -0.0605 0.0276  912  LEU   B CD1 
7068  C  CD2 . LEU   B 608 ? 1.0625 1.1195 1.1534 -0.0147 -0.0617 0.0230  912  LEU   B CD2 
7069  N  N   . TYR   B 609 ? 1.0984 1.1219 1.1891 -0.0207 -0.0537 0.0245  913  TYR   B N   
7070  C  CA  . TYR   B 609 ? 1.1072 1.1254 1.2038 -0.0221 -0.0541 0.0230  913  TYR   B CA  
7071  C  C   . TYR   B 609 ? 1.1168 1.1241 1.2081 -0.0239 -0.0495 0.0254  913  TYR   B C   
7072  O  O   . TYR   B 609 ? 1.1660 1.1707 1.2550 -0.0263 -0.0441 0.0272  913  TYR   B O   
7073  C  CB  . TYR   B 609 ? 1.0931 1.1159 1.2035 -0.0256 -0.0533 0.0201  913  TYR   B CB  
7074  C  CG  . TYR   B 609 ? 1.0539 1.0865 1.1690 -0.0236 -0.0579 0.0177  913  TYR   B CG  
7075  C  CD1 . TYR   B 609 ? 1.0626 1.0963 1.1772 -0.0200 -0.0636 0.0160  913  TYR   B CD1 
7076  C  CD2 . TYR   B 609 ? 1.0624 1.1023 1.1813 -0.0251 -0.0564 0.0172  913  TYR   B CD2 
7077  C  CE1 . TYR   B 609 ? 1.0210 1.0627 1.1388 -0.0179 -0.0674 0.0140  913  TYR   B CE1 
7078  C  CE2 . TYR   B 609 ? 1.0705 1.1186 1.1929 -0.0231 -0.0604 0.0151  913  TYR   B CE2 
7079  C  CZ  . TYR   B 609 ? 0.9930 1.0417 1.1147 -0.0195 -0.0657 0.0136  913  TYR   B CZ  
7080  O  OH  . TYR   B 609 ? 0.9753 1.0312 1.0996 -0.0173 -0.0694 0.0117  913  TYR   B OH  
7081  N  N   . LEU   B 610 ? 1.1263 1.1268 1.2148 -0.0224 -0.0514 0.0255  914  LEU   B N   
7082  C  CA  . LEU   B 610 ? 1.1215 1.1106 1.2041 -0.0237 -0.0473 0.0279  914  LEU   B CA  
7083  C  C   . LEU   B 610 ? 1.1441 1.1281 1.2339 -0.0251 -0.0485 0.0261  914  LEU   B C   
7084  O  O   . LEU   B 610 ? 1.1969 1.1804 1.2848 -0.0218 -0.0538 0.0249  914  LEU   B O   
7085  C  CB  . LEU   B 610 ? 1.1299 1.1143 1.1978 -0.0194 -0.0489 0.0305  914  LEU   B CB  
7086  C  CG  . LEU   B 610 ? 1.1558 1.1300 1.2147 -0.0208 -0.0432 0.0337  914  LEU   B CG  
7087  C  CD1 . LEU   B 610 ? 1.1897 1.1663 1.2519 -0.0244 -0.0376 0.0343  914  LEU   B CD1 
7088  C  CD2 . LEU   B 610 ? 1.1799 1.1511 1.2245 -0.0161 -0.0455 0.0361  914  LEU   B CD2 
7089  N  N   . LYS   B 611 ? 1.1533 1.1336 1.2518 -0.0299 -0.0437 0.0258  915  LYS   B N   
7090  C  CA  . LYS   B 611 ? 1.2023 1.1769 1.3088 -0.0320 -0.0443 0.0241  915  LYS   B CA  
7091  C  C   . LYS   B 611 ? 1.2776 1.2413 1.3819 -0.0353 -0.0373 0.0267  915  LYS   B C   
7092  O  O   . LYS   B 611 ? 1.2999 1.2623 1.4020 -0.0375 -0.0311 0.0289  915  LYS   B O   
7093  C  CB  . LYS   B 611 ? 1.1772 1.1588 1.3004 -0.0351 -0.0458 0.0204  915  LYS   B CB  
7094  C  CG  . LYS   B 611 ? 1.1230 1.1135 1.2491 -0.0317 -0.0532 0.0173  915  LYS   B CG  
7095  C  CD  . LYS   B 611 ? 1.1335 1.1200 1.2525 -0.0273 -0.0590 0.0168  915  LYS   B CD  
7096  C  CE  . LYS   B 611 ? 1.0962 1.0908 1.2125 -0.0227 -0.0650 0.0152  915  LYS   B CE  
7097  N  NZ  . LYS   B 611 ? 1.1526 1.1529 1.2803 -0.0232 -0.0693 0.0111  915  LYS   B NZ  
7098  N  N   . THR   B 612 ? 1.3042 1.2594 1.4087 -0.0356 -0.0382 0.0266  916  THR   B N   
7099  C  CA  . THR   B 612 ? 1.3075 1.2507 1.4079 -0.0381 -0.0318 0.0294  916  THR   B CA  
7100  C  C   . THR   B 612 ? 1.2887 1.2261 1.3998 -0.0412 -0.0321 0.0276  916  THR   B C   
7101  O  O   . THR   B 612 ? 1.2965 1.2338 1.4091 -0.0390 -0.0386 0.0253  916  THR   B O   
7102  C  CB  . THR   B 612 ? 1.3039 1.2392 1.3861 -0.0338 -0.0322 0.0326  916  THR   B CB  
7103  O  OG1 . THR   B 612 ? 1.3638 1.2865 1.4415 -0.0361 -0.0260 0.0353  916  THR   B OG1 
7104  C  CG2 . THR   B 612 ? 1.3196 1.2551 1.3977 -0.0293 -0.0401 0.0311  916  THR   B CG2 
7105  N  N   . LYS   B 613 ? 1.3369 1.2692 1.4556 -0.0462 -0.0248 0.0286  917  LYS   B N   
7106  C  CA  . LYS   B 613 ? 1.2837 1.2095 1.4133 -0.0499 -0.0238 0.0273  917  LYS   B CA  
7107  C  C   . LYS   B 613 ? 1.4073 1.3204 1.5295 -0.0520 -0.0155 0.0313  917  LYS   B C   
7108  O  O   . LYS   B 613 ? 1.3956 1.3075 1.5231 -0.0559 -0.0076 0.0328  917  LYS   B O   
7109  C  CB  . LYS   B 613 ? 1.2172 1.1502 1.3667 -0.0544 -0.0230 0.0241  917  LYS   B CB  
7110  C  CG  . LYS   B 613 ? 1.2806 1.2080 1.4431 -0.0581 -0.0232 0.0222  917  LYS   B CG  
7111  C  CD  . LYS   B 613 ? 1.3385 1.2704 1.5199 -0.0638 -0.0184 0.0207  917  LYS   B CD  
7112  C  CE  . LYS   B 613 ? 1.3554 1.2875 1.5536 -0.0664 -0.0231 0.0167  917  LYS   B CE  
7113  N  NZ  . LYS   B 613 ? 1.4106 1.3517 1.6110 -0.0627 -0.0333 0.0126  917  LYS   B NZ  
7114  N  N   . GLY   B 614 ? 1.4445 1.3477 1.5539 -0.0490 -0.0171 0.0331  918  GLY   B N   
7115  C  CA  . GLY   B 614 ? 1.5239 1.4134 1.6246 -0.0505 -0.0098 0.0369  918  GLY   B CA  
7116  C  C   . GLY   B 614 ? 1.5459 1.4320 1.6306 -0.0484 -0.0047 0.0409  918  GLY   B C   
7117  O  O   . GLY   B 614 ? 1.5295 1.4113 1.5979 -0.0436 -0.0076 0.0427  918  GLY   B O   
7118  N  N   . ASP   B 615 ? 1.7446 1.6321 1.8339 -0.0518 0.0029  0.0422  919  ASP   B N   
7119  C  CA  . ASP   B 615 ? 1.7509 1.6352 1.8254 -0.0499 0.0077  0.0456  919  ASP   B CA  
7120  C  C   . ASP   B 615 ? 1.7315 1.6278 1.8117 -0.0506 0.0083  0.0444  919  ASP   B C   
7121  O  O   . ASP   B 615 ? 1.7340 1.6287 1.8021 -0.0488 0.0114  0.0469  919  ASP   B O   
7122  C  CB  . ASP   B 615 ? 1.8280 1.6982 1.8975 -0.0528 0.0181  0.0494  919  ASP   B CB  
7123  C  CG  . ASP   B 615 ? 1.8886 1.7445 1.9430 -0.0502 0.0180  0.0520  919  ASP   B CG  
7124  O  OD1 . ASP   B 615 ? 1.8564 1.7062 1.9176 -0.0523 0.0180  0.0513  919  ASP   B OD1 
7125  O  OD2 . ASP   B 615 ? 1.9010 1.7513 1.9366 -0.0458 0.0179  0.0547  919  ASP   B OD2 
7126  N  N   . PHE   B 616 ? 1.6521 1.5598 1.7498 -0.0530 0.0052  0.0407  920  PHE   B N   
7127  C  CA  . PHE   B 616 ? 1.6449 1.5646 1.7488 -0.0535 0.0048  0.0392  920  PHE   B CA  
7128  C  C   . PHE   B 616 ? 1.6189 1.5478 1.7165 -0.0485 -0.0041 0.0375  920  PHE   B C   
7129  O  O   . PHE   B 616 ? 1.6094 1.5402 1.7081 -0.0462 -0.0114 0.0355  920  PHE   B O   
7130  C  CB  . PHE   B 616 ? 1.6438 1.5713 1.7697 -0.0581 0.0053  0.0358  920  PHE   B CB  
7131  C  CG  . PHE   B 616 ? 1.6794 1.6021 1.8144 -0.0633 0.0155  0.0373  920  PHE   B CG  
7132  C  CD1 . PHE   B 616 ? 1.7027 1.6137 1.8257 -0.0638 0.0240  0.0416  920  PHE   B CD1 
7133  C  CD2 . PHE   B 616 ? 1.6568 1.5869 1.8127 -0.0677 0.0165  0.0344  920  PHE   B CD2 
7134  C  CE1 . PHE   B 616 ? 1.6945 1.6008 1.8261 -0.0685 0.0341  0.0431  920  PHE   B CE1 
7135  C  CE2 . PHE   B 616 ? 1.6223 1.5487 1.7879 -0.0725 0.0262  0.0357  920  PHE   B CE2 
7136  C  CZ  . PHE   B 616 ? 1.6610 1.5754 1.8144 -0.0729 0.0353  0.0402  920  PHE   B CZ  
7137  N  N   . ILE   B 617 ? 1.4600 1.3947 1.5515 -0.0469 -0.0036 0.0383  921  ILE   B N   
7138  C  CA  . ILE   B 617 ? 1.3873 1.3308 1.4730 -0.0425 -0.0112 0.0371  921  ILE   B CA  
7139  C  C   . ILE   B 617 ? 1.3520 1.3081 1.4490 -0.0440 -0.0120 0.0346  921  ILE   B C   
7140  O  O   . ILE   B 617 ? 1.3775 1.3340 1.4766 -0.0466 -0.0058 0.0356  921  ILE   B O   
7141  C  CB  . ILE   B 617 ? 1.4019 1.3407 1.4688 -0.0385 -0.0108 0.0402  921  ILE   B CB  
7142  C  CG1 . ILE   B 617 ? 1.4005 1.3268 1.4557 -0.0364 -0.0108 0.0425  921  ILE   B CG1 
7143  C  CG2 . ILE   B 617 ? 1.3577 1.3071 1.4212 -0.0346 -0.0179 0.0389  921  ILE   B CG2 
7144  C  CD1 . ILE   B 617 ? 1.4597 1.3750 1.5011 -0.0361 -0.0042 0.0463  921  ILE   B CD1 
7145  N  N   . LEU   B 618 ? 1.3133 1.2789 1.4167 -0.0423 -0.0194 0.0315  922  LEU   B N   
7146  C  CA  . LEU   B 618 ? 1.2646 1.2421 1.3775 -0.0431 -0.0210 0.0291  922  LEU   B CA  
7147  C  C   . LEU   B 618 ? 1.2534 1.2374 1.3565 -0.0387 -0.0260 0.0293  922  LEU   B C   
7148  O  O   . LEU   B 618 ? 1.2742 1.2580 1.3706 -0.0348 -0.0316 0.0292  922  LEU   B O   
7149  C  CB  . LEU   B 618 ? 1.2165 1.1998 1.3450 -0.0445 -0.0256 0.0251  922  LEU   B CB  
7150  C  CG  . LEU   B 618 ? 1.1947 1.1886 1.3350 -0.0464 -0.0257 0.0226  922  LEU   B CG  
7151  C  CD1 . LEU   B 618 ? 1.2314 1.2240 1.3727 -0.0497 -0.0173 0.0246  922  LEU   B CD1 
7152  C  CD2 . LEU   B 618 ? 1.1876 1.1847 1.3441 -0.0486 -0.0289 0.0188  922  LEU   B CD2 
7153  N  N   . VAL   B 619 ? 1.2317 1.2214 1.3345 -0.0393 -0.0237 0.0296  923  VAL   B N   
7154  C  CA  . VAL   B 619 ? 1.1754 1.1717 1.2703 -0.0357 -0.0278 0.0298  923  VAL   B CA  
7155  C  C   . VAL   B 619 ? 1.1411 1.1489 1.2470 -0.0368 -0.0298 0.0270  923  VAL   B C   
7156  O  O   . VAL   B 619 ? 1.1664 1.1759 1.2822 -0.0405 -0.0257 0.0261  923  VAL   B O   
7157  C  CB  . VAL   B 619 ? 1.2106 1.2017 1.2921 -0.0348 -0.0238 0.0331  923  VAL   B CB  
7158  C  CG1 . VAL   B 619 ? 1.2337 1.2323 1.3088 -0.0314 -0.0284 0.0330  923  VAL   B CG1 
7159  C  CG2 . VAL   B 619 ? 1.2055 1.1845 1.2753 -0.0334 -0.0221 0.0359  923  VAL   B CG2 
7160  N  N   . GLY   B 620 ? 1.0933 1.1085 1.1974 -0.0334 -0.0359 0.0258  924  GLY   B N   
7161  C  CA  . GLY   B 620 ? 1.1030 1.1286 1.2167 -0.0338 -0.0386 0.0230  924  GLY   B CA  
7162  C  C   . GLY   B 620 ? 1.1639 1.1963 1.2708 -0.0305 -0.0421 0.0234  924  GLY   B C   
7163  O  O   . GLY   B 620 ? 1.2054 1.2350 1.3012 -0.0275 -0.0437 0.0254  924  GLY   B O   
7164  N  N   . ASP   B 621 ? 1.1934 1.2344 1.3075 -0.0311 -0.0435 0.0214  925  ASP   B N   
7165  C  CA  . ASP   B 621 ? 1.1866 1.2343 1.2958 -0.0289 -0.0456 0.0218  925  ASP   B CA  
7166  C  C   . ASP   B 621 ? 1.1662 1.2227 1.2853 -0.0290 -0.0487 0.0187  925  ASP   B C   
7167  O  O   . ASP   B 621 ? 1.1792 1.2365 1.3085 -0.0318 -0.0471 0.0168  925  ASP   B O   
7168  C  CB  . ASP   B 621 ? 1.2281 1.2739 1.3322 -0.0308 -0.0405 0.0238  925  ASP   B CB  
7169  C  CG  . ASP   B 621 ? 1.2862 1.3392 1.3874 -0.0294 -0.0424 0.0238  925  ASP   B CG  
7170  O  OD1 . ASP   B 621 ? 1.3288 1.3854 1.4261 -0.0261 -0.0472 0.0238  925  ASP   B OD1 
7171  O  OD2 . ASP   B 621 ? 1.2690 1.3235 1.3717 -0.0316 -0.0388 0.0239  925  ASP   B OD2 
7172  N  N   . LEU   B 622 ? 1.0814 1.1442 1.1979 -0.0258 -0.0531 0.0182  926  LEU   B N   
7173  C  CA  . LEU   B 622 ? 0.9678 1.0380 1.0922 -0.0251 -0.0565 0.0154  926  LEU   B CA  
7174  C  C   . LEU   B 622 ? 1.0092 1.0829 1.1432 -0.0286 -0.0538 0.0136  926  LEU   B C   
7175  O  O   . LEU   B 622 ? 1.0555 1.1329 1.1977 -0.0285 -0.0565 0.0108  926  LEU   B O   
7176  C  CB  . LEU   B 622 ? 0.9027 0.9794 1.0223 -0.0220 -0.0595 0.0159  926  LEU   B CB  
7177  C  CG  . LEU   B 622 ? 0.8983 0.9766 1.0146 -0.0177 -0.0644 0.0156  926  LEU   B CG  
7178  C  CD1 . LEU   B 622 ? 1.0904 1.1615 1.1987 -0.0163 -0.0641 0.0179  926  LEU   B CD1 
7179  C  CD2 . LEU   B 622 ? 0.9137 0.9987 1.0268 -0.0154 -0.0660 0.0163  926  LEU   B CD2 
7180  N  N   . MET   B 623 ? 1.0318 1.1042 1.1646 -0.0313 -0.0488 0.0150  927  MET   B N   
7181  C  CA  . MET   B 623 ? 1.0022 1.0785 1.1437 -0.0342 -0.0461 0.0134  927  MET   B CA  
7182  C  C   . MET   B 623 ? 1.0145 1.0858 1.1632 -0.0378 -0.0414 0.0132  927  MET   B C   
7183  O  O   . MET   B 623 ? 1.0840 1.1541 1.2340 -0.0405 -0.0360 0.0141  927  MET   B O   
7184  C  CB  . MET   B 623 ? 1.0099 1.0888 1.1457 -0.0345 -0.0436 0.0150  927  MET   B CB  
7185  C  CG  . MET   B 623 ? 0.9512 1.0350 1.0805 -0.0312 -0.0478 0.0155  927  MET   B CG  
7186  S  SD  . MET   B 623 ? 1.0662 1.1544 1.1912 -0.0317 -0.0462 0.0164  927  MET   B SD  
7187  C  CE  . MET   B 623 ? 0.9744 1.0694 1.1107 -0.0334 -0.0461 0.0134  927  MET   B CE  
7188  N  N   . ARG   B 624 ? 1.0190 1.0873 1.1729 -0.0379 -0.0435 0.0118  928  ARG   B N   
7189  C  CA  . ARG   B 624 ? 1.0881 1.1509 1.2496 -0.0412 -0.0396 0.0116  928  ARG   B CA  
7190  C  C   . ARG   B 624 ? 1.1557 1.2123 1.3111 -0.0434 -0.0325 0.0148  928  ARG   B C   
7191  O  O   . ARG   B 624 ? 1.2009 1.2573 1.3628 -0.0466 -0.0271 0.0148  928  ARG   B O   
7192  C  CB  . ARG   B 624 ? 1.0875 1.1554 1.2639 -0.0437 -0.0395 0.0084  928  ARG   B CB  
7193  C  CG  . ARG   B 624 ? 1.0648 1.1280 1.2517 -0.0473 -0.0358 0.0077  928  ARG   B CG  
7194  C  CD  . ARG   B 624 ? 1.1046 1.1718 1.3052 -0.0479 -0.0402 0.0037  928  ARG   B CD  
7195  N  NE  . ARG   B 624 ? 1.2235 1.2966 1.4353 -0.0501 -0.0383 0.0018  928  ARG   B NE  
7196  C  CZ  . ARG   B 624 ? 1.2907 1.3626 1.5127 -0.0540 -0.0325 0.0017  928  ARG   B CZ  
7197  N  NH1 . ARG   B 624 ? 1.2777 1.3423 1.4986 -0.0563 -0.0268 0.0041  928  ARG   B NH1 
7198  N  NH2 . ARG   B 624 ? 1.3703 1.4484 1.6040 -0.0555 -0.0320 -0.0007 928  ARG   B NH2 
7199  N  N   . SER   B 625 ? 1.1720 1.2231 1.3145 -0.0414 -0.0323 0.0176  929  SER   B N   
7200  C  CA  . SER   B 625 ? 1.1862 1.2298 1.3207 -0.0428 -0.0259 0.0207  929  SER   B CA  
7201  C  C   . SER   B 625 ? 1.2139 1.2484 1.3473 -0.0435 -0.0242 0.0219  929  SER   B C   
7202  O  O   . SER   B 625 ? 1.2596 1.2891 1.3825 -0.0409 -0.0263 0.0236  929  SER   B O   
7203  C  CB  . SER   B 625 ? 1.1453 1.1884 1.2653 -0.0399 -0.0269 0.0231  929  SER   B CB  
7204  O  OG  . SER   B 625 ? 1.0589 1.1105 1.1803 -0.0392 -0.0291 0.0219  929  SER   B OG  
7205  N  N   . VAL   B 626 ? 1.2376 1.2698 1.3824 -0.0471 -0.0205 0.0208  930  VAL   B N   
7206  C  CA  . VAL   B 626 ? 1.2263 1.2494 1.3709 -0.0482 -0.0183 0.0220  930  VAL   B CA  
7207  C  C   . VAL   B 626 ? 1.2260 1.2399 1.3615 -0.0496 -0.0105 0.0256  930  VAL   B C   
7208  O  O   . VAL   B 626 ? 1.2333 1.2480 1.3672 -0.0508 -0.0057 0.0266  930  VAL   B O   
7209  C  CB  . VAL   B 626 ? 1.1763 1.2004 1.3377 -0.0515 -0.0181 0.0192  930  VAL   B CB  
7210  C  CG1 . VAL   B 626 ? 1.1275 1.1573 1.2945 -0.0493 -0.0266 0.0159  930  VAL   B CG1 
7211  C  CG2 . VAL   B 626 ? 1.2948 1.3240 1.4677 -0.0547 -0.0135 0.0181  930  VAL   B CG2 
7212  N  N   . LEU   B 627 ? 1.2290 1.2335 1.3582 -0.0492 -0.0093 0.0275  931  LEU   B N   
7213  C  CA  . LEU   B 627 ? 1.2805 1.2745 1.3971 -0.0493 -0.0029 0.0313  931  LEU   B CA  
7214  C  C   . LEU   B 627 ? 1.3543 1.3381 1.4685 -0.0497 -0.0018 0.0326  931  LEU   B C   
7215  O  O   . LEU   B 627 ? 1.3511 1.3334 1.4589 -0.0466 -0.0075 0.0325  931  LEU   B O   
7216  C  CB  . LEU   B 627 ? 1.1918 1.1859 1.2924 -0.0453 -0.0057 0.0330  931  LEU   B CB  
7217  C  CG  . LEU   B 627 ? 1.2176 1.1992 1.3026 -0.0442 -0.0012 0.0368  931  LEU   B CG  
7218  C  CD1 . LEU   B 627 ? 1.3281 1.3045 1.4136 -0.0473 0.0080  0.0385  931  LEU   B CD1 
7219  C  CD2 . LEU   B 627 ? 1.1947 1.1765 1.2646 -0.0398 -0.0057 0.0381  931  LEU   B CD2 
7220  N  N   . LEU   B 628 ? 1.3503 1.3270 1.4697 -0.0533 0.0057  0.0338  932  LEU   B N   
7221  C  CA  . LEU   B 628 ? 1.3183 1.2850 1.4367 -0.0542 0.0073  0.0350  932  LEU   B CA  
7222  C  C   . LEU   B 628 ? 1.3367 1.2909 1.4381 -0.0531 0.0133  0.0392  932  LEU   B C   
7223  O  O   . LEU   B 628 ? 1.3424 1.2932 1.4407 -0.0546 0.0206  0.0412  932  LEU   B O   
7224  C  CB  . LEU   B 628 ? 1.3360 1.3029 1.4728 -0.0591 0.0114  0.0333  932  LEU   B CB  
7225  C  CG  . LEU   B 628 ? 1.4387 1.3976 1.5798 -0.0606 0.0115  0.0333  932  LEU   B CG  
7226  C  CD1 . LEU   B 628 ? 1.4348 1.3978 1.5775 -0.0579 0.0014  0.0305  932  LEU   B CD1 
7227  C  CD2 . LEU   B 628 ? 1.4700 1.4279 1.6293 -0.0661 0.0176  0.0323  932  LEU   B CD2 
7228  N  N   . LEU   B 629 ? 1.3730 1.3201 1.4626 -0.0500 0.0099  0.0406  933  LEU   B N   
7229  C  CA  . LEU   B 629 ? 1.3986 1.3323 1.4709 -0.0483 0.0144  0.0446  933  LEU   B CA  
7230  C  C   . LEU   B 629 ? 1.4163 1.3393 1.4899 -0.0500 0.0173  0.0457  933  LEU   B C   
7231  O  O   . LEU   B 629 ? 1.4497 1.3758 1.5373 -0.0523 0.0150  0.0433  933  LEU   B O   
7232  C  CB  . LEU   B 629 ? 1.3713 1.3047 1.4273 -0.0429 0.0079  0.0455  933  LEU   B CB  
7233  C  CG  . LEU   B 629 ? 1.3586 1.3013 1.4101 -0.0402 0.0037  0.0447  933  LEU   B CG  
7234  C  CD1 . LEU   B 629 ? 1.3011 1.2413 1.3374 -0.0350 -0.0025 0.0459  933  LEU   B CD1 
7235  C  CD2 . LEU   B 629 ? 1.3314 1.2725 1.3791 -0.0417 0.0104  0.0463  933  LEU   B CD2 
7236  N  N   . ALA   B 630 ? 1.4021 1.3118 1.4603 -0.0486 0.0219  0.0493  934  ALA   B N   
7237  C  CA  . ALA   B 630 ? 1.4644 1.3623 1.5216 -0.0500 0.0252  0.0509  934  ALA   B CA  
7238  C  C   . ALA   B 630 ? 1.5312 1.4158 1.5664 -0.0461 0.0267  0.0546  934  ALA   B C   
7239  O  O   . ALA   B 630 ? 1.5593 1.4386 1.5829 -0.0452 0.0316  0.0571  934  ALA   B O   
7240  C  CB  . ALA   B 630 ? 1.4749 1.3686 1.5444 -0.0556 0.0348  0.0515  934  ALA   B CB  
7241  N  N   . TYR   B 631 ? 1.5428 1.4219 1.5721 -0.0437 0.0221  0.0548  935  TYR   B N   
7242  C  CA  . TYR   B 631 ? 1.6041 1.4706 1.6124 -0.0395 0.0223  0.0581  935  TYR   B CA  
7243  C  C   . TYR   B 631 ? 1.7242 1.5749 1.7283 -0.0422 0.0317  0.0612  935  TYR   B C   
7244  O  O   . TYR   B 631 ? 1.7249 1.5703 1.7348 -0.0440 0.0322  0.0610  935  TYR   B O   
7245  C  CB  . TYR   B 631 ? 1.6075 1.4754 1.6113 -0.0355 0.0131  0.0569  935  TYR   B CB  
7246  C  CG  . TYR   B 631 ? 1.6941 1.5476 1.6790 -0.0316 0.0133  0.0600  935  TYR   B CG  
7247  C  CD1 . TYR   B 631 ? 1.6781 1.5260 1.6449 -0.0276 0.0135  0.0624  935  TYR   B CD1 
7248  C  CD2 . TYR   B 631 ? 1.6682 1.5133 1.6530 -0.0318 0.0127  0.0603  935  TYR   B CD2 
7249  C  CE1 . TYR   B 631 ? 1.6792 1.5136 1.6284 -0.0238 0.0132  0.0651  935  TYR   B CE1 
7250  C  CE2 . TYR   B 631 ? 1.6284 1.4600 1.5956 -0.0281 0.0127  0.0631  935  TYR   B CE2 
7251  C  CZ  . TYR   B 631 ? 1.6889 1.5152 1.6384 -0.0240 0.0129  0.0655  935  TYR   B CZ  
7252  O  OH  . TYR   B 631 ? 1.7691 1.5816 1.7009 -0.0200 0.0125  0.0681  935  TYR   B OH  
7253  N  N   . LYS   B 632 ? 1.8946 1.7376 1.8886 -0.0423 0.0395  0.0641  936  LYS   B N   
7254  C  CA  . LYS   B 632 ? 1.8999 1.7267 1.8878 -0.0444 0.0494  0.0676  936  LYS   B CA  
7255  C  C   . LYS   B 632 ? 1.9218 1.7357 1.8928 -0.0404 0.0468  0.0698  936  LYS   B C   
7256  O  O   . LYS   B 632 ? 1.9122 1.7232 1.8659 -0.0351 0.0424  0.0709  936  LYS   B O   
7257  C  CB  . LYS   B 632 ? 1.9122 1.7329 1.8904 -0.0445 0.0578  0.0703  936  LYS   B CB  
7258  N  N   . PRO   B 633 ? 1.8282 1.6339 1.8036 -0.0426 0.0491  0.0703  937  PRO   B N   
7259  C  CA  . PRO   B 633 ? 1.7873 1.5831 1.7488 -0.0385 0.0446  0.0716  937  PRO   B CA  
7260  C  C   . PRO   B 633 ? 1.8300 1.6096 1.7674 -0.0346 0.0487  0.0758  937  PRO   B C   
7261  O  O   . PRO   B 633 ? 1.8507 1.6295 1.7732 -0.0289 0.0419  0.0760  937  PRO   B O   
7262  C  CB  . PRO   B 633 ? 1.7497 1.5397 1.7233 -0.0429 0.0480  0.0714  937  PRO   B CB  
7263  C  CG  . PRO   B 633 ? 1.8274 1.6294 1.8243 -0.0485 0.0503  0.0686  937  PRO   B CG  
7264  C  CD  . PRO   B 633 ? 1.8239 1.6298 1.8184 -0.0489 0.0553  0.0696  937  PRO   B CD  
7265  N  N   . MET   B 634 ? 1.8289 1.5952 1.7622 -0.0373 0.0598  0.0790  938  MET   B N   
7266  C  CA  . MET   B 634 ? 1.7853 1.5339 1.6943 -0.0333 0.0641  0.0831  938  MET   B CA  
7267  C  C   . MET   B 634 ? 1.8440 1.5953 1.7395 -0.0291 0.0618  0.0835  938  MET   B C   
7268  O  O   . MET   B 634 ? 1.8774 1.6180 1.7515 -0.0238 0.0597  0.0856  938  MET   B O   
7269  C  CB  . MET   B 634 ? 1.6765 1.4102 1.5847 -0.0373 0.0774  0.0865  938  MET   B CB  
7270  N  N   . GLU   B 635 ? 1.8329 1.5985 1.7407 -0.0314 0.0615  0.0813  939  GLU   B N   
7271  C  CA  . GLU   B 635 ? 1.7632 1.5319 1.6594 -0.0278 0.0590  0.0814  939  GLU   B CA  
7272  C  C   . GLU   B 635 ? 1.7544 1.5317 1.6450 -0.0226 0.0465  0.0793  939  GLU   B C   
7273  O  O   . GLU   B 635 ? 1.7588 1.5315 1.6319 -0.0176 0.0433  0.0804  939  GLU   B O   
7274  C  CB  . GLU   B 635 ? 1.7066 1.4879 1.6183 -0.0318 0.0625  0.0796  939  GLU   B CB  
7275  N  N   . GLY   B 636 ? 1.7703 1.5598 1.6755 -0.0234 0.0392  0.0762  940  GLY   B N   
7276  C  CA  . GLY   B 636 ? 1.7185 1.5174 1.6205 -0.0188 0.0278  0.0741  940  GLY   B CA  
7277  C  C   . GLY   B 636 ? 1.6870 1.5004 1.5939 -0.0182 0.0236  0.0720  940  GLY   B C   
7278  O  O   . GLY   B 636 ? 1.6505 1.4650 1.5454 -0.0134 0.0176  0.0720  940  GLY   B O   
7279  N  N   . ASN   B 637 ? 1.6630 1.4872 1.5873 -0.0230 0.0267  0.0700  941  ASN   B N   
7280  C  CA  . ASN   B 637 ? 1.5821 1.4210 1.5136 -0.0231 0.0230  0.0677  941  ASN   B CA  
7281  C  C   . ASN   B 637 ? 1.5759 1.4258 1.5298 -0.0288 0.0260  0.0653  941  ASN   B C   
7282  O  O   . ASN   B 637 ? 1.5999 1.4445 1.5620 -0.0328 0.0323  0.0659  941  ASN   B O   
7283  C  CB  . ASN   B 637 ? 1.5942 1.4270 1.5115 -0.0214 0.0269  0.0697  941  ASN   B CB  
7284  C  CG  . ASN   B 637 ? 1.6525 1.4981 1.5696 -0.0188 0.0194  0.0676  941  ASN   B CG  
7285  O  OD1 . ASN   B 637 ? 1.6860 1.5321 1.5928 -0.0140 0.0118  0.0675  941  ASN   B OD1 
7286  N  ND2 . ASN   B 637 ? 1.6133 1.4690 1.5418 -0.0220 0.0216  0.0660  941  ASN   B ND2 
7287  N  N   . PHE   B 638 ? 1.5574 1.4229 1.5214 -0.0291 0.0209  0.0624  942  PHE   B N   
7288  C  CA  . PHE   B 638 ? 1.4962 1.3733 1.4812 -0.0339 0.0225  0.0597  942  PHE   B CA  
7289  C  C   . PHE   B 638 ? 1.4334 1.3106 1.4207 -0.0368 0.0303  0.0605  942  PHE   B C   
7290  O  O   . PHE   B 638 ? 1.4614 1.3352 1.4355 -0.0343 0.0314  0.0620  942  PHE   B O   
7291  C  CB  . PHE   B 638 ? 1.4403 1.3341 1.4356 -0.0328 0.0133  0.0561  942  PHE   B CB  
7292  C  CG  . PHE   B 638 ? 1.4198 1.3151 1.4092 -0.0284 0.0046  0.0555  942  PHE   B CG  
7293  C  CD1 . PHE   B 638 ? 1.4386 1.3359 1.4373 -0.0291 0.0011  0.0538  942  PHE   B CD1 
7294  C  CD2 . PHE   B 638 ? 1.4385 1.3339 1.4141 -0.0235 -0.0005 0.0563  942  PHE   B CD2 
7295  C  CE1 . PHE   B 638 ? 1.4342 1.3329 1.4275 -0.0248 -0.0066 0.0532  942  PHE   B CE1 
7296  C  CE2 . PHE   B 638 ? 1.4629 1.3603 1.4342 -0.0195 -0.0082 0.0556  942  PHE   B CE2 
7297  C  CZ  . PHE   B 638 ? 1.4628 1.3619 1.4428 -0.0200 -0.0111 0.0542  942  PHE   B CZ  
7298  N  N   . GLU   B 639 ? 1.4058 1.2873 1.4104 -0.0418 0.0353  0.0592  943  GLU   B N   
7299  C  CA  . GLU   B 639 ? 1.3849 1.2689 1.3956 -0.0448 0.0424  0.0594  943  GLU   B CA  
7300  C  C   . GLU   B 639 ? 1.3594 1.2592 1.3917 -0.0480 0.0394  0.0556  943  GLU   B C   
7301  O  O   . GLU   B 639 ? 1.3907 1.2948 1.4360 -0.0498 0.0361  0.0535  943  GLU   B O   
7302  C  CB  . GLU   B 639 ? 1.4011 1.2719 1.4110 -0.0480 0.0539  0.0623  943  GLU   B CB  
7303  N  N   . GLU   B 640 ? 1.3090 1.2168 1.3447 -0.0486 0.0403  0.0545  944  GLU   B N   
7304  C  CA  . GLU   B 640 ? 1.3182 1.2410 1.3732 -0.0511 0.0370  0.0508  944  GLU   B CA  
7305  C  C   . GLU   B 640 ? 1.3130 1.2356 1.3851 -0.0564 0.0445  0.0503  944  GLU   B C   
7306  O  O   . GLU   B 640 ? 1.3920 1.3067 1.4615 -0.0582 0.0540  0.0527  944  GLU   B O   
7307  C  CB  . GLU   B 640 ? 1.3712 1.3019 1.4236 -0.0499 0.0357  0.0500  944  GLU   B CB  
7308  C  CG  . GLU   B 640 ? 1.4345 1.3783 1.5067 -0.0531 0.0353  0.0468  944  GLU   B CG  
7309  C  CD  . GLU   B 640 ? 1.4649 1.4182 1.5350 -0.0514 0.0315  0.0454  944  GLU   B CD  
7310  O  OE1 . GLU   B 640 ? 1.4738 1.4256 1.5291 -0.0475 0.0269  0.0464  944  GLU   B OE1 
7311  O  OE2 . GLU   B 640 ? 1.5212 1.4835 1.6048 -0.0539 0.0328  0.0433  944  GLU   B OE2 
7312  N  N   . ILE   B 641 ? 1.3403 1.2716 1.4301 -0.0586 0.0402  0.0471  945  ILE   B N   
7313  C  CA  . ILE   B 641 ? 1.3812 1.3137 1.4897 -0.0637 0.0463  0.0461  945  ILE   B CA  
7314  C  C   . ILE   B 641 ? 1.4945 1.4392 1.6164 -0.0656 0.0467  0.0436  945  ILE   B C   
7315  O  O   . ILE   B 641 ? 1.5465 1.4897 1.6757 -0.0687 0.0553  0.0444  945  ILE   B O   
7316  C  CB  . ILE   B 641 ? 1.4350 1.3687 1.5557 -0.0653 0.0416  0.0439  945  ILE   B CB  
7317  C  CG1 . ILE   B 641 ? 1.4524 1.3741 1.5589 -0.0630 0.0405  0.0463  945  ILE   B CG1 
7318  C  CG2 . ILE   B 641 ? 1.5098 1.4434 1.6499 -0.0707 0.0483  0.0430  945  ILE   B CG2 
7319  C  CD1 . ILE   B 641 ? 1.4982 1.4191 1.6163 -0.0648 0.0369  0.0443  945  ILE   B CD1 
7320  N  N   . ALA   B 642 ? 1.5129 1.4694 1.6383 -0.0636 0.0377  0.0405  946  ALA   B N   
7321  C  CA  . ALA   B 642 ? 1.5323 1.5006 1.6693 -0.0648 0.0371  0.0379  946  ALA   B CA  
7322  C  C   . ALA   B 642 ? 1.4496 1.4277 1.5827 -0.0613 0.0271  0.0357  946  ALA   B C   
7323  O  O   . ALA   B 642 ? 1.3460 1.3235 1.4721 -0.0584 0.0202  0.0354  946  ALA   B O   
7324  C  CB  . ALA   B 642 ? 1.5387 1.5127 1.6987 -0.0692 0.0384  0.0351  946  ALA   B CB  
7325  N  N   . ARG   B 643 ? 1.4743 1.4614 1.6120 -0.0614 0.0266  0.0342  947  ARG   B N   
7326  C  CA  . ARG   B 643 ? 1.3792 1.3767 1.5162 -0.0586 0.0180  0.0318  947  ARG   B CA  
7327  C  C   . ARG   B 643 ? 1.4026 1.4110 1.5574 -0.0610 0.0172  0.0284  947  ARG   B C   
7328  O  O   . ARG   B 643 ? 1.4708 1.4786 1.6363 -0.0644 0.0240  0.0283  947  ARG   B O   
7329  C  CB  . ARG   B 643 ? 1.3037 1.3004 1.4240 -0.0555 0.0176  0.0337  947  ARG   B CB  
7330  N  N   . ASP   B 644 ? 1.3456 1.3635 1.5036 -0.0590 0.0090  0.0256  948  ASP   B N   
7331  C  CA  . ASP   B 644 ? 1.3288 1.3572 1.5009 -0.0603 0.0072  0.0223  948  ASP   B CA  
7332  C  C   . ASP   B 644 ? 1.2814 1.3171 1.4466 -0.0567 -0.0004 0.0212  948  ASP   B C   
7333  O  O   . ASP   B 644 ? 1.2978 1.3331 1.4569 -0.0540 -0.0065 0.0210  948  ASP   B O   
7334  C  CB  . ASP   B 644 ? 1.4137 1.4454 1.6036 -0.0625 0.0046  0.0192  948  ASP   B CB  
7335  C  CG  . ASP   B 644 ? 1.4749 1.5174 1.6793 -0.0634 0.0017  0.0154  948  ASP   B CG  
7336  O  OD1 . ASP   B 644 ? 1.4942 1.5388 1.7057 -0.0657 0.0075  0.0154  948  ASP   B OD1 
7337  O  OD2 . ASP   B 644 ? 1.4827 1.5313 1.6915 -0.0616 -0.0064 0.0125  948  ASP   B OD2 
7338  N  N   . PHE   B 645 ? 1.2203 1.2619 1.3858 -0.0566 0.0005  0.0206  949  PHE   B N   
7339  C  CA  . PHE   B 645 ? 1.2430 1.2917 1.4025 -0.0535 -0.0058 0.0196  949  PHE   B CA  
7340  C  C   . PHE   B 645 ? 1.2562 1.3147 1.4291 -0.0544 -0.0080 0.0163  949  PHE   B C   
7341  O  O   . PHE   B 645 ? 1.2923 1.3532 1.4675 -0.0557 -0.0039 0.0163  949  PHE   B O   
7342  C  CB  . PHE   B 645 ? 1.2661 1.3117 1.4106 -0.0520 -0.0031 0.0224  949  PHE   B CB  
7343  C  CG  . PHE   B 645 ? 1.2422 1.2788 1.3713 -0.0499 -0.0030 0.0255  949  PHE   B CG  
7344  C  CD1 . PHE   B 645 ? 1.3105 1.3432 1.4390 -0.0491 -0.0058 0.0256  949  PHE   B CD1 
7345  C  CD2 . PHE   B 645 ? 1.1522 1.1839 1.2671 -0.0485 -0.0004 0.0280  949  PHE   B CD2 
7346  C  CE1 . PHE   B 645 ? 1.3027 1.3271 1.4169 -0.0469 -0.0059 0.0284  949  PHE   B CE1 
7347  C  CE2 . PHE   B 645 ? 1.2214 1.2448 1.3221 -0.0463 -0.0007 0.0307  949  PHE   B CE2 
7348  C  CZ  . PHE   B 645 ? 1.3260 1.3458 1.4263 -0.0455 -0.0034 0.0309  949  PHE   B CZ  
7349  N  N   . ASN   B 646 ? 1.2212 1.2850 1.4019 -0.0534 -0.0147 0.0134  950  ASN   B N   
7350  C  CA  . ASN   B 646 ? 1.2192 1.2919 1.4109 -0.0535 -0.0180 0.0100  950  ASN   B CA  
7351  C  C   . ASN   B 646 ? 1.2068 1.2848 1.3930 -0.0498 -0.0257 0.0088  950  ASN   B C   
7352  O  O   . ASN   B 646 ? 1.2332 1.3125 1.4231 -0.0484 -0.0314 0.0068  950  ASN   B O   
7353  C  CB  . ASN   B 646 ? 1.2557 1.3297 1.4640 -0.0558 -0.0187 0.0071  950  ASN   B CB  
7354  C  CG  . ASN   B 646 ? 1.3197 1.4025 1.5387 -0.0554 -0.0229 0.0035  950  ASN   B CG  
7355  O  OD1 . ASN   B 646 ? 1.4212 1.5067 1.6466 -0.0542 -0.0293 0.0006  950  ASN   B OD1 
7356  N  ND2 . ASN   B 646 ? 1.2655 1.3523 1.4850 -0.0561 -0.0196 0.0036  950  ASN   B ND2 
7357  N  N   . PRO   B 647 ? 1.1457 1.2267 1.3232 -0.0482 -0.0261 0.0098  951  PRO   B N   
7358  C  CA  . PRO   B 647 ? 1.1153 1.1997 1.2850 -0.0446 -0.0324 0.0097  951  PRO   B CA  
7359  C  C   . PRO   B 647 ? 1.1158 1.2062 1.2938 -0.0431 -0.0385 0.0063  951  PRO   B C   
7360  O  O   . PRO   B 647 ? 1.1504 1.2456 1.3377 -0.0442 -0.0387 0.0040  951  PRO   B O   
7361  C  CB  . PRO   B 647 ? 1.1224 1.2095 1.2846 -0.0441 -0.0308 0.0111  951  PRO   B CB  
7362  C  CG  . PRO   B 647 ? 1.1409 1.2231 1.3021 -0.0468 -0.0235 0.0128  951  PRO   B CG  
7363  C  CD  . PRO   B 647 ? 1.1561 1.2373 1.3306 -0.0496 -0.0206 0.0112  951  PRO   B CD  
7364  N  N   . ASN   B 648 ? 1.0955 1.1848 1.2693 -0.0403 -0.0437 0.0061  952  ASN   B N   
7365  C  CA  . ASN   B 648 ? 1.0953 1.1886 1.2736 -0.0379 -0.0501 0.0032  952  ASN   B CA  
7366  C  C   . ASN   B 648 ? 1.0720 1.1616 1.2420 -0.0349 -0.0536 0.0044  952  ASN   B C   
7367  O  O   . ASN   B 648 ? 1.1216 1.2052 1.2871 -0.0355 -0.0513 0.0065  952  ASN   B O   
7368  C  CB  . ASN   B 648 ? 1.1100 1.2037 1.3022 -0.0398 -0.0510 0.0000  952  ASN   B CB  
7369  C  CG  . ASN   B 648 ? 1.0867 1.1836 1.2826 -0.0369 -0.0581 -0.0033 952  ASN   B CG  
7370  O  OD1 . ASN   B 648 ? 1.0569 1.1576 1.2470 -0.0339 -0.0612 -0.0034 952  ASN   B OD1 
7371  N  ND2 . ASN   B 648 ? 1.0662 1.1613 1.2719 -0.0377 -0.0605 -0.0059 952  ASN   B ND2 
7372  N  N   . TRP   B 649 ? 0.9723 1.0651 1.1400 -0.0314 -0.0591 0.0031  953  TRP   B N   
7373  C  CA  . TRP   B 649 ? 0.9109 1.0005 1.0708 -0.0281 -0.0623 0.0042  953  TRP   B CA  
7374  C  C   . TRP   B 649 ? 0.9821 1.0658 1.1461 -0.0285 -0.0637 0.0030  953  TRP   B C   
7375  O  O   . TRP   B 649 ? 1.0128 1.0971 1.1853 -0.0287 -0.0667 -0.0001 953  TRP   B O   
7376  C  CB  . TRP   B 649 ? 0.9385 1.0327 1.0957 -0.0242 -0.0672 0.0030  953  TRP   B CB  
7377  C  CG  . TRP   B 649 ? 0.9774 1.0772 1.1307 -0.0236 -0.0662 0.0041  953  TRP   B CG  
7378  C  CD1 . TRP   B 649 ? 1.0099 1.1152 1.1663 -0.0225 -0.0682 0.0023  953  TRP   B CD1 
7379  C  CD2 . TRP   B 649 ? 1.0441 1.1443 1.1897 -0.0239 -0.0634 0.0071  953  TRP   B CD2 
7380  N  NE1 . TRP   B 649 ? 1.0265 1.1358 1.1780 -0.0224 -0.0665 0.0041  953  TRP   B NE1 
7381  C  CE2 . TRP   B 649 ? 1.0613 1.1675 1.2063 -0.0232 -0.0638 0.0070  953  TRP   B CE2 
7382  C  CE3 . TRP   B 649 ? 0.9745 1.0700 1.1134 -0.0245 -0.0609 0.0099  953  TRP   B CE3 
7383  C  CZ2 . TRP   B 649 ? 1.0101 1.1181 1.1487 -0.0234 -0.0620 0.0093  953  TRP   B CZ2 
7384  C  CZ3 . TRP   B 649 ? 0.9496 1.0467 1.0816 -0.0243 -0.0593 0.0122  953  TRP   B CZ3 
7385  C  CH2 . TRP   B 649 ? 0.9462 1.0496 1.0784 -0.0239 -0.0599 0.0118  953  TRP   B CH2 
7386  N  N   . MET   B 650 ? 0.9748 1.0525 1.1322 -0.0284 -0.0621 0.0054  954  MET   B N   
7387  C  CA  . MET   B 650 ? 0.9224 0.9934 1.0818 -0.0286 -0.0633 0.0048  954  MET   B CA  
7388  C  C   . MET   B 650 ? 0.9368 1.0052 1.0868 -0.0243 -0.0672 0.0058  954  MET   B C   
7389  O  O   . MET   B 650 ? 0.9780 1.0466 1.1185 -0.0225 -0.0664 0.0084  954  MET   B O   
7390  C  CB  . MET   B 650 ? 0.9903 1.0552 1.1496 -0.0322 -0.0575 0.0070  954  MET   B CB  
7391  C  CG  . MET   B 650 ? 1.0240 1.0816 1.1861 -0.0330 -0.0581 0.0065  954  MET   B CG  
7392  S  SD  . MET   B 650 ? 1.0387 1.0890 1.2028 -0.0377 -0.0503 0.0089  954  MET   B SD  
7393  C  CE  . MET   B 650 ? 1.1205 1.1678 1.2679 -0.0357 -0.0474 0.0133  954  MET   B CE  
7394  N  N   . SER   B 651 ? 0.9699 1.0353 1.1225 -0.0226 -0.0716 0.0036  955  SER   B N   
7395  C  CA  . SER   B 651 ? 0.9735 1.0365 1.1178 -0.0181 -0.0756 0.0040  955  SER   B CA  
7396  C  C   . SER   B 651 ? 0.9920 1.0466 1.1340 -0.0180 -0.0760 0.0046  955  SER   B C   
7397  O  O   . SER   B 651 ? 1.0272 1.0790 1.1603 -0.0144 -0.0779 0.0061  955  SER   B O   
7398  C  CB  . SER   B 651 ? 0.9739 1.0398 1.1208 -0.0148 -0.0811 0.0009  955  SER   B CB  
7399  O  OG  . SER   B 651 ? 0.9861 1.0496 1.1428 -0.0167 -0.0832 -0.0023 955  SER   B OG  
7400  N  N   . ALA   B 652 ? 0.9686 1.0189 1.1186 -0.0217 -0.0743 0.0035  956  ALA   B N   
7401  C  CA  . ALA   B 652 ? 0.9957 1.0374 1.1436 -0.0219 -0.0745 0.0041  956  ALA   B CA  
7402  C  C   . ALA   B 652 ? 1.0049 1.0432 1.1622 -0.0272 -0.0702 0.0038  956  ALA   B C   
7403  O  O   . ALA   B 652 ? 0.9822 1.0251 1.1498 -0.0301 -0.0688 0.0021  956  ALA   B O   
7404  C  CB  . ALA   B 652 ? 0.9716 1.0105 1.1198 -0.0185 -0.0810 0.0014  956  ALA   B CB  
7405  N  N   . VAL   B 653 ? 1.0565 1.0867 1.2106 -0.0284 -0.0678 0.0057  957  VAL   B N   
7406  C  CA  . VAL   B 653 ? 1.0872 1.1132 1.2488 -0.0335 -0.0622 0.0063  957  VAL   B CA  
7407  C  C   . VAL   B 653 ? 1.1324 1.1485 1.2912 -0.0337 -0.0620 0.0072  957  VAL   B C   
7408  O  O   . VAL   B 653 ? 1.1778 1.1901 1.3262 -0.0299 -0.0650 0.0083  957  VAL   B O   
7409  C  CB  . VAL   B 653 ? 1.0911 1.1186 1.2480 -0.0354 -0.0555 0.0095  957  VAL   B CB  
7410  C  CG1 . VAL   B 653 ? 1.1333 1.1564 1.2752 -0.0325 -0.0547 0.0130  957  VAL   B CG1 
7411  C  CG2 . VAL   B 653 ? 1.1318 1.1558 1.2975 -0.0406 -0.0490 0.0100  957  VAL   B CG2 
7412  N  N   . GLU   B 654 ? 1.1232 1.1347 1.2917 -0.0383 -0.0584 0.0068  958  GLU   B N   
7413  C  CA  . GLU   B 654 ? 1.1135 1.1155 1.2824 -0.0392 -0.0586 0.0069  958  GLU   B CA  
7414  C  C   . GLU   B 654 ? 1.1768 1.1748 1.3557 -0.0449 -0.0518 0.0077  958  GLU   B C   
7415  O  O   . GLU   B 654 ? 1.1922 1.1958 1.3811 -0.0480 -0.0484 0.0069  958  GLU   B O   
7416  C  CB  . GLU   B 654 ? 1.0652 1.0667 1.2400 -0.0374 -0.0663 0.0030  958  GLU   B CB  
7417  C  CG  . GLU   B 654 ? 1.1106 1.1019 1.2830 -0.0372 -0.0677 0.0032  958  GLU   B CG  
7418  C  CD  . GLU   B 654 ? 1.1766 1.1626 1.3320 -0.0335 -0.0671 0.0067  958  GLU   B CD  
7419  O  OE1 . GLU   B 654 ? 1.1823 1.1735 1.3285 -0.0294 -0.0692 0.0075  958  GLU   B OE1 
7420  O  OE2 . GLU   B 654 ? 1.1950 1.1717 1.3466 -0.0346 -0.0645 0.0085  958  GLU   B OE2 
7421  N  N   . ILE   B 655 ? 1.2181 1.2063 1.3946 -0.0462 -0.0495 0.0092  959  ILE   B N   
7422  C  CA  . ILE   B 655 ? 1.2244 1.2074 1.4106 -0.0516 -0.0427 0.0101  959  ILE   B CA  
7423  C  C   . ILE   B 655 ? 1.2235 1.2045 1.4242 -0.0538 -0.0469 0.0063  959  ILE   B C   
7424  O  O   . ILE   B 655 ? 1.2127 1.1887 1.4096 -0.0513 -0.0525 0.0051  959  ILE   B O   
7425  C  CB  . ILE   B 655 ? 1.1615 1.1340 1.3355 -0.0519 -0.0368 0.0145  959  ILE   B CB  
7426  C  CG1 . ILE   B 655 ? 1.1625 1.1369 1.3212 -0.0489 -0.0345 0.0177  959  ILE   B CG1 
7427  C  CG2 . ILE   B 655 ? 1.2215 1.1884 1.4052 -0.0575 -0.0288 0.0157  959  ILE   B CG2 
7428  C  CD1 . ILE   B 655 ? 1.1928 1.1576 1.3402 -0.0497 -0.0272 0.0221  959  ILE   B CD1 
7429  N  N   . LEU   B 656 ? 1.2256 1.2108 1.4433 -0.0581 -0.0446 0.0042  960  LEU   B N   
7430  C  CA  . LEU   B 656 ? 1.2059 1.1883 1.4390 -0.0610 -0.0475 0.0009  960  LEU   B CA  
7431  C  C   . LEU   B 656 ? 1.2809 1.2527 1.5152 -0.0648 -0.0409 0.0035  960  LEU   B C   
7432  O  O   . LEU   B 656 ? 1.2831 1.2467 1.5132 -0.0638 -0.0440 0.0035  960  LEU   B O   
7433  C  CB  . LEU   B 656 ? 1.1899 1.1810 1.4419 -0.0642 -0.0478 -0.0025 960  LEU   B CB  
7434  C  CG  . LEU   B 656 ? 1.1907 1.1915 1.4416 -0.0604 -0.0547 -0.0054 960  LEU   B CG  
7435  C  CD1 . LEU   B 656 ? 1.2030 1.2114 1.4728 -0.0634 -0.0552 -0.0088 960  LEU   B CD1 
7436  C  CD2 . LEU   B 656 ? 1.1452 1.1435 1.3900 -0.0558 -0.0644 -0.0079 960  LEU   B CD2 
7437  N  N   . ASP   B 657 ? 1.2863 1.2576 1.5257 -0.0689 -0.0315 0.0061  961  ASP   B N   
7438  C  CA  . ASP   B 657 ? 1.2900 1.2505 1.5282 -0.0722 -0.0237 0.0094  961  ASP   B CA  
7439  C  C   . ASP   B 657 ? 1.3213 1.2798 1.5478 -0.0724 -0.0145 0.0141  961  ASP   B C   
7440  O  O   . ASP   B 657 ? 1.3317 1.2967 1.5495 -0.0695 -0.0153 0.0148  961  ASP   B O   
7441  C  CB  . ASP   B 657 ? 1.2870 1.2468 1.5473 -0.0781 -0.0206 0.0073  961  ASP   B CB  
7442  C  CG  . ASP   B 657 ? 1.2953 1.2645 1.5696 -0.0810 -0.0166 0.0062  961  ASP   B CG  
7443  O  OD1 . ASP   B 657 ? 1.3644 1.3341 1.6320 -0.0816 -0.0087 0.0096  961  ASP   B OD1 
7444  O  OD2 . ASP   B 657 ? 1.2742 1.2502 1.5655 -0.0824 -0.0218 0.0018  961  ASP   B OD2 
7445  N  N   . ASP   B 658 ? 1.3833 1.3325 1.6096 -0.0758 -0.0057 0.0174  962  ASP   B N   
7446  C  CA  . ASP   B 658 ? 1.3872 1.3322 1.6003 -0.0756 0.0031  0.0221  962  ASP   B CA  
7447  C  C   . ASP   B 658 ? 1.4146 1.3687 1.6335 -0.0768 0.0073  0.0220  962  ASP   B C   
7448  O  O   . ASP   B 658 ? 1.4537 1.4057 1.6595 -0.0755 0.0128  0.0254  962  ASP   B O   
7449  C  CB  . ASP   B 658 ? 1.4185 1.3512 1.6320 -0.0793 0.0124  0.0254  962  ASP   B CB  
7450  C  CG  . ASP   B 658 ? 1.4800 1.4013 1.6807 -0.0771 0.0101  0.0271  962  ASP   B CG  
7451  O  OD1 . ASP   B 658 ? 1.5141 1.4332 1.7239 -0.0782 0.0050  0.0244  962  ASP   B OD1 
7452  O  OD2 . ASP   B 658 ? 1.4910 1.4052 1.6723 -0.0742 0.0131  0.0309  962  ASP   B OD2 
7453  N  N   . ASP   B 659 ? 1.3682 1.3317 1.6060 -0.0792 0.0047  0.0181  963  ASP   B N   
7454  C  CA  . ASP   B 659 ? 1.3760 1.3479 1.6214 -0.0808 0.0092  0.0178  963  ASP   B CA  
7455  C  C   . ASP   B 659 ? 1.3944 1.3787 1.6442 -0.0783 0.0009  0.0140  963  ASP   B C   
7456  O  O   . ASP   B 659 ? 1.4278 1.4183 1.6742 -0.0773 0.0030  0.0146  963  ASP   B O   
7457  C  CB  . ASP   B 659 ? 1.3960 1.3677 1.6624 -0.0867 0.0162  0.0171  963  ASP   B CB  
7458  C  CG  . ASP   B 659 ? 1.3913 1.3502 1.6551 -0.0897 0.0255  0.0209  963  ASP   B CG  
7459  O  OD1 . ASP   B 659 ? 1.4038 1.3537 1.6537 -0.0876 0.0239  0.0229  963  ASP   B OD1 
7460  O  OD2 . ASP   B 659 ? 1.3835 1.3413 1.6591 -0.0940 0.0346  0.0221  963  ASP   B OD2 
7461  N  N   . ASN   B 660 ? 1.3803 1.3678 1.6375 -0.0772 -0.0085 0.0100  964  ASN   B N   
7462  C  CA  . ASN   B 660 ? 1.3798 1.3782 1.6416 -0.0746 -0.0166 0.0061  964  ASN   B CA  
7463  C  C   . ASN   B 660 ? 1.3886 1.3872 1.6330 -0.0690 -0.0240 0.0063  964  ASN   B C   
7464  O  O   . ASN   B 660 ? 1.3343 1.3262 1.5719 -0.0672 -0.0278 0.0065  964  ASN   B O   
7465  C  CB  . ASN   B 660 ? 1.2906 1.2924 1.5722 -0.0767 -0.0226 0.0012  964  ASN   B CB  
7466  C  CG  . ASN   B 660 ? 1.2926 1.2962 1.5938 -0.0821 -0.0160 0.0005  964  ASN   B CG  
7467  O  OD1 . ASN   B 660 ? 1.3138 1.3220 1.6173 -0.0835 -0.0096 0.0019  964  ASN   B OD1 
7468  N  ND2 . ASN   B 660 ? 1.3094 1.3096 1.6256 -0.0853 -0.0175 -0.0017 964  ASN   B ND2 
7469  N  N   . PHE   B 661 ? 1.4661 1.4726 1.7043 -0.0661 -0.0262 0.0060  965  PHE   B N   
7470  C  CA  . PHE   B 661 ? 1.4328 1.4409 1.6557 -0.0607 -0.0326 0.0063  965  PHE   B CA  
7471  C  C   . PHE   B 661 ? 1.3965 1.4145 1.6257 -0.0586 -0.0399 0.0023  965  PHE   B C   
7472  O  O   . PHE   B 661 ? 1.4315 1.4561 1.6733 -0.0609 -0.0386 0.0003  965  PHE   B O   
7473  C  CB  . PHE   B 661 ? 1.4608 1.4678 1.6676 -0.0590 -0.0276 0.0104  965  PHE   B CB  
7474  C  CG  . PHE   B 661 ? 1.5429 1.5409 1.7457 -0.0619 -0.0184 0.0143  965  PHE   B CG  
7475  C  CD1 . PHE   B 661 ? 1.5319 1.5196 1.7254 -0.0612 -0.0176 0.0165  965  PHE   B CD1 
7476  C  CD2 . PHE   B 661 ? 1.5477 1.5471 1.7558 -0.0652 -0.0104 0.0157  965  PHE   B CD2 
7477  C  CE1 . PHE   B 661 ? 1.5324 1.5109 1.7213 -0.0636 -0.0090 0.0202  965  PHE   B CE1 
7478  C  CE2 . PHE   B 661 ? 1.5599 1.5501 1.7634 -0.0675 -0.0016 0.0193  965  PHE   B CE2 
7479  C  CZ  . PHE   B 661 ? 1.5786 1.5582 1.7724 -0.0667 -0.0009 0.0216  965  PHE   B CZ  
7480  N  N   . LEU   B 662 ? 1.2442 1.2628 1.4645 -0.0540 -0.0474 0.0012  966  LEU   B N   
7481  C  CA  . LEU   B 662 ? 1.1669 1.1930 1.3917 -0.0513 -0.0550 -0.0027 966  LEU   B CA  
7482  C  C   . LEU   B 662 ? 1.0872 1.1171 1.2971 -0.0464 -0.0579 -0.0014 966  LEU   B C   
7483  O  O   . LEU   B 662 ? 1.0619 1.0872 1.2581 -0.0440 -0.0574 0.0015  966  LEU   B O   
7484  C  CB  . LEU   B 662 ? 1.1305 1.1531 1.3619 -0.0504 -0.0623 -0.0062 966  LEU   B CB  
7485  C  CG  . LEU   B 662 ? 1.0563 1.0834 1.2878 -0.0463 -0.0714 -0.0100 966  LEU   B CG  
7486  C  CD1 . LEU   B 662 ? 1.0600 1.0949 1.3057 -0.0480 -0.0728 -0.0134 966  LEU   B CD1 
7487  C  CD2 . LEU   B 662 ? 1.0664 1.0866 1.2990 -0.0449 -0.0776 -0.0124 966  LEU   B CD2 
7488  N  N   . GLY   B 663 ? 1.0714 1.1097 1.2843 -0.0449 -0.0610 -0.0035 967  GLY   B N   
7489  C  CA  . GLY   B 663 ? 1.0431 1.0856 1.2437 -0.0404 -0.0639 -0.0025 967  GLY   B CA  
7490  C  C   . GLY   B 663 ? 0.9683 1.0178 1.1735 -0.0380 -0.0699 -0.0061 967  GLY   B C   
7491  O  O   . GLY   B 663 ? 0.9499 1.0021 1.1683 -0.0400 -0.0717 -0.0094 967  GLY   B O   
7492  N  N   . ALA   B 664 ? 0.9001 0.9525 1.0943 -0.0336 -0.0731 -0.0054 968  ALA   B N   
7493  C  CA  . ALA   B 664 ? 0.9421 1.0008 1.1381 -0.0309 -0.0779 -0.0081 968  ALA   B CA  
7494  C  C   . ALA   B 664 ? 0.9889 1.0541 1.1793 -0.0305 -0.0746 -0.0060 968  ALA   B C   
7495  O  O   . ALA   B 664 ? 0.9869 1.0512 1.1663 -0.0291 -0.0723 -0.0027 968  ALA   B O   
7496  C  CB  . ALA   B 664 ? 0.9909 1.0474 1.1792 -0.0257 -0.0845 -0.0093 968  ALA   B CB  
7497  N  N   . GLU   B 665 ? 1.0160 1.0874 1.2143 -0.0316 -0.0746 -0.0080 969  GLU   B N   
7498  C  CA  . GLU   B 665 ? 0.9966 1.0742 1.1904 -0.0313 -0.0720 -0.0064 969  GLU   B CA  
7499  C  C   . GLU   B 665 ? 0.9937 1.0770 1.1906 -0.0289 -0.0767 -0.0094 969  GLU   B C   
7500  O  O   . GLU   B 665 ? 0.9874 1.0702 1.1921 -0.0283 -0.0812 -0.0129 969  GLU   B O   
7501  C  CB  . GLU   B 665 ? 0.9955 1.0742 1.1945 -0.0358 -0.0650 -0.0048 969  GLU   B CB  
7502  C  CG  . GLU   B 665 ? 1.0502 1.1303 1.2647 -0.0393 -0.0641 -0.0077 969  GLU   B CG  
7503  C  CD  . GLU   B 665 ? 1.1458 1.2282 1.3649 -0.0432 -0.0569 -0.0062 969  GLU   B CD  
7504  O  OE1 . GLU   B 665 ? 1.1468 1.2324 1.3586 -0.0426 -0.0542 -0.0042 969  GLU   B OE1 
7505  O  OE2 . GLU   B 665 ? 1.2058 1.2864 1.4362 -0.0468 -0.0537 -0.0070 969  GLU   B OE2 
7506  N  N   . ASN   B 666 ? 1.0533 1.1414 1.2432 -0.0272 -0.0758 -0.0079 970  ASN   B N   
7507  C  CA  . ASN   B 666 ? 1.0817 1.1752 1.2736 -0.0252 -0.0789 -0.0101 970  ASN   B CA  
7508  C  C   . ASN   B 666 ? 1.1008 1.1971 1.3060 -0.0283 -0.0783 -0.0129 970  ASN   B C   
7509  O  O   . ASN   B 666 ? 1.0754 1.1725 1.2856 -0.0322 -0.0728 -0.0117 970  ASN   B O   
7510  C  CB  . ASN   B 666 ? 1.0886 1.1867 1.2720 -0.0241 -0.0764 -0.0075 970  ASN   B CB  
7511  C  CG  . ASN   B 666 ? 1.1450 1.2486 1.3301 -0.0225 -0.0786 -0.0094 970  ASN   B CG  
7512  O  OD1 . ASN   B 666 ? 1.1725 1.2799 1.3635 -0.0250 -0.0761 -0.0100 970  ASN   B OD1 
7513  N  ND2 . ASN   B 666 ? 1.1419 1.2457 1.3210 -0.0181 -0.0830 -0.0101 970  ASN   B ND2 
7514  N  N   . ALA   B 667 ? 1.0746 1.1721 1.2852 -0.0263 -0.0837 -0.0166 971  ALA   B N   
7515  C  CA  . ALA   B 667 ? 1.0206 1.1166 1.2237 -0.0212 -0.0896 -0.0178 971  ALA   B CA  
7516  C  C   . ALA   B 667 ? 1.0287 1.1197 1.2368 -0.0200 -0.0952 -0.0211 971  ALA   B C   
7517  O  O   . ALA   B 667 ? 1.0347 1.1265 1.2528 -0.0206 -0.0984 -0.0247 971  ALA   B O   
7518  C  CB  . ALA   B 667 ? 1.1402 1.2412 1.3424 -0.0190 -0.0916 -0.0192 971  ALA   B CB  
7519  N  N   . PHE   B 668 ? 1.0565 1.1420 1.2574 -0.0180 -0.0967 -0.0199 972  PHE   B N   
7520  C  CA  . PHE   B 668 ? 1.0052 1.0846 1.2094 -0.0168 -0.1021 -0.0228 972  PHE   B CA  
7521  C  C   . PHE   B 668 ? 0.9667 1.0452 1.1855 -0.0217 -0.1008 -0.0246 972  PHE   B C   
7522  O  O   . PHE   B 668 ? 0.9581 1.0352 1.1863 -0.0217 -0.1057 -0.0286 972  PHE   B O   
7523  C  CB  . PHE   B 668 ? 0.9543 1.0329 1.1561 -0.0119 -0.1092 -0.0262 972  PHE   B CB  
7524  C  CG  . PHE   B 668 ? 0.9634 1.0441 1.1523 -0.0075 -0.1092 -0.0243 972  PHE   B CG  
7525  C  CD1 . PHE   B 668 ? 0.9685 1.0448 1.1461 -0.0031 -0.1112 -0.0231 972  PHE   B CD1 
7526  C  CD2 . PHE   B 668 ? 1.0264 1.1135 1.2151 -0.0077 -0.1068 -0.0236 972  PHE   B CD2 
7527  C  CE1 . PHE   B 668 ? 0.9973 1.0757 1.1643 0.0009  -0.1107 -0.0212 972  PHE   B CE1 
7528  C  CE2 . PHE   B 668 ? 1.0213 1.1103 1.1991 -0.0039 -0.1065 -0.0218 972  PHE   B CE2 
7529  C  CZ  . PHE   B 668 ? 1.0079 1.0927 1.1753 0.0003  -0.1083 -0.0205 972  PHE   B CZ  
7530  N  N   . ASN   B 669 ? 0.9754 1.0545 1.1961 -0.0259 -0.0940 -0.0216 973  ASN   B N   
7531  C  CA  . ASN   B 669 ? 0.9786 1.0571 1.2129 -0.0310 -0.0907 -0.0224 973  ASN   B CA  
7532  C  C   . ASN   B 669 ? 0.9601 1.0321 1.1923 -0.0331 -0.0876 -0.0200 973  ASN   B C   
7533  O  O   . ASN   B 669 ? 0.9325 1.0019 1.1523 -0.0314 -0.0858 -0.0167 973  ASN   B O   
7534  C  CB  . ASN   B 669 ? 1.0066 1.0910 1.2454 -0.0343 -0.0843 -0.0208 973  ASN   B CB  
7535  C  CG  . ASN   B 669 ? 1.0037 1.0942 1.2480 -0.0332 -0.0872 -0.0237 973  ASN   B CG  
7536  O  OD1 . ASN   B 669 ? 1.0182 1.1082 1.2691 -0.0316 -0.0934 -0.0276 973  ASN   B OD1 
7537  N  ND2 . ASN   B 669 ? 1.0428 1.1385 1.2839 -0.0337 -0.0831 -0.0219 973  ASN   B ND2 
7538  N  N   . LEU   B 670 ? 0.9710 1.0403 1.2160 -0.0367 -0.0870 -0.0217 974  LEU   B N   
7539  C  CA  . LEU   B 670 ? 0.9579 1.0213 1.2036 -0.0399 -0.0823 -0.0193 974  LEU   B CA  
7540  C  C   . LEU   B 670 ? 1.0040 1.0699 1.2599 -0.0452 -0.0746 -0.0180 974  LEU   B C   
7541  O  O   . LEU   B 670 ? 1.0065 1.0782 1.2729 -0.0468 -0.0742 -0.0201 974  LEU   B O   
7542  C  CB  . LEU   B 670 ? 0.9450 1.0022 1.1974 -0.0401 -0.0874 -0.0221 974  LEU   B CB  
7543  C  CG  . LEU   B 670 ? 0.8995 0.9512 1.1404 -0.0353 -0.0937 -0.0226 974  LEU   B CG  
7544  C  CD1 . LEU   B 670 ? 0.9136 0.9594 1.1641 -0.0365 -0.0984 -0.0259 974  LEU   B CD1 
7545  C  CD2 . LEU   B 670 ? 0.9167 0.9644 1.1435 -0.0343 -0.0896 -0.0181 974  LEU   B CD2 
7546  N  N   . PHE   B 671 ? 1.0407 1.1016 1.2931 -0.0478 -0.0682 -0.0145 975  PHE   B N   
7547  C  CA  . PHE   B 671 ? 1.0571 1.1186 1.3182 -0.0527 -0.0601 -0.0129 975  PHE   B CA  
7548  C  C   . PHE   B 671 ? 1.0920 1.1450 1.3512 -0.0552 -0.0552 -0.0101 975  PHE   B C   
7549  O  O   . PHE   B 671 ? 1.0763 1.1239 1.3225 -0.0529 -0.0563 -0.0080 975  PHE   B O   
7550  C  CB  . PHE   B 671 ? 1.0655 1.1317 1.3190 -0.0526 -0.0547 -0.0101 975  PHE   B CB  
7551  C  CG  . PHE   B 671 ? 1.0916 1.1533 1.3281 -0.0512 -0.0511 -0.0056 975  PHE   B CG  
7552  C  CD1 . PHE   B 671 ? 1.0874 1.1499 1.3104 -0.0466 -0.0556 -0.0048 975  PHE   B CD1 
7553  C  CD2 . PHE   B 671 ? 1.1020 1.1584 1.3364 -0.0542 -0.0433 -0.0022 975  PHE   B CD2 
7554  C  CE1 . PHE   B 671 ? 1.0607 1.1194 1.2692 -0.0452 -0.0528 -0.0010 975  PHE   B CE1 
7555  C  CE2 . PHE   B 671 ? 1.1034 1.1552 1.3221 -0.0526 -0.0406 0.0016  975  PHE   B CE2 
7556  C  CZ  . PHE   B 671 ? 1.0788 1.1319 1.2850 -0.0481 -0.0457 0.0021  975  PHE   B CZ  
7557  N  N   . VAL   B 672 ? 1.1381 1.1900 1.4105 -0.0600 -0.0496 -0.0101 976  VAL   B N   
7558  C  CA  . VAL   B 672 ? 1.1912 1.2347 1.4631 -0.0630 -0.0436 -0.0073 976  VAL   B CA  
7559  C  C   . VAL   B 672 ? 1.2047 1.2487 1.4792 -0.0666 -0.0335 -0.0044 976  VAL   B C   
7560  O  O   . VAL   B 672 ? 1.1975 1.2473 1.4856 -0.0690 -0.0312 -0.0062 976  VAL   B O   
7561  C  CB  . VAL   B 672 ? 1.2028 1.2425 1.4897 -0.0655 -0.0466 -0.0103 976  VAL   B CB  
7562  C  CG1 . VAL   B 672 ? 1.2352 1.2657 1.5215 -0.0688 -0.0399 -0.0072 976  VAL   B CG1 
7563  C  CG2 . VAL   B 672 ? 1.1691 1.2078 1.4523 -0.0615 -0.0570 -0.0135 976  VAL   B CG2 
7564  N  N   . CYS   B 673 ? 1.2616 1.2993 1.5226 -0.0666 -0.0274 0.0000  977  CYS   B N   
7565  C  CA  . CYS   B 673 ? 1.2984 1.3339 1.5598 -0.0697 -0.0172 0.0032  977  CYS   B CA  
7566  C  C   . CYS   B 673 ? 1.3464 1.3718 1.6085 -0.0727 -0.0114 0.0057  977  CYS   B C   
7567  O  O   . CYS   B 673 ? 1.3305 1.3499 1.5887 -0.0716 -0.0153 0.0055  977  CYS   B O   
7568  C  CB  . CYS   B 673 ? 1.2969 1.3329 1.5406 -0.0671 -0.0145 0.0065  977  CYS   B CB  
7569  S  SG  . CYS   B 673 ? 1.4985 1.5245 1.7225 -0.0642 -0.0153 0.0100  977  CYS   B SG  
7570  N  N   . GLN   B 674 ? 1.3777 1.4004 1.6440 -0.0762 -0.0017 0.0080  978  GLN   B N   
7571  C  CA  . GLN   B 674 ? 1.3852 1.3991 1.6571 -0.0799 0.0049  0.0099  978  GLN   B CA  
7572  C  C   . GLN   B 674 ? 1.4138 1.4221 1.6776 -0.0814 0.0161  0.0144  978  GLN   B C   
7573  O  O   . GLN   B 674 ? 1.4555 1.4687 1.7171 -0.0809 0.0194  0.0150  978  GLN   B O   
7574  C  CB  . GLN   B 674 ? 1.3308 1.3485 1.6270 -0.0839 0.0044  0.0062  978  GLN   B CB  
7575  C  CG  . GLN   B 674 ? 1.3580 1.3685 1.6642 -0.0887 0.0134  0.0081  978  GLN   B CG  
7576  C  CD  . GLN   B 674 ? 1.3678 1.3836 1.6996 -0.0925 0.0124  0.0042  978  GLN   B CD  
7577  O  OE1 . GLN   B 674 ? 1.3137 1.3352 1.6544 -0.0914 0.0027  -0.0002 978  GLN   B OE1 
7578  N  NE2 . GLN   B 674 ? 1.4616 1.4753 1.8055 -0.0970 0.0224  0.0058  978  GLN   B NE2 
7579  N  N   . LYS   B 675 ? 1.4252 1.4224 1.6833 -0.0828 0.0219  0.0176  979  LYS   B N   
7580  C  CA  . LYS   B 675 ? 1.4999 1.4898 1.7511 -0.0845 0.0333  0.0219  979  LYS   B CA  
7581  C  C   . LYS   B 675 ? 1.5641 1.5518 1.8344 -0.0899 0.0414  0.0219  979  LYS   B C   
7582  O  O   . LYS   B 675 ? 1.5720 1.5614 1.8589 -0.0923 0.0378  0.0189  979  LYS   B O   
7583  C  CB  . LYS   B 675 ? 1.5205 1.4985 1.7505 -0.0822 0.0352  0.0260  979  LYS   B CB  
7584  C  CG  . LYS   B 675 ? 1.4682 1.4395 1.6979 -0.0821 0.0308  0.0256  979  LYS   B CG  
7585  C  CD  . LYS   B 675 ? 1.4335 1.3920 1.6423 -0.0800 0.0346  0.0300  979  LYS   B CD  
7586  C  CE  . LYS   B 675 ? 1.4843 1.4336 1.6917 -0.0831 0.0473  0.0340  979  LYS   B CE  
7587  N  NZ  . LYS   B 675 ? 1.5747 1.5095 1.7657 -0.0819 0.0510  0.0379  979  LYS   B NZ  
7588  N  N   . ASP   B 676 ? 1.6571 1.6408 1.9252 -0.0916 0.0524  0.0251  980  ASP   B N   
7589  C  CA  . ASP   B 676 ? 1.6612 1.6440 1.9483 -0.0967 0.0615  0.0253  980  ASP   B CA  
7590  C  C   . ASP   B 676 ? 1.5592 1.5285 1.8435 -0.0992 0.0697  0.0289  980  ASP   B C   
7591  O  O   . ASP   B 676 ? 1.5086 1.4681 1.7762 -0.0982 0.0776  0.0334  980  ASP   B O   
7592  C  CB  . ASP   B 676 ? 1.7490 1.7350 2.0360 -0.0971 0.0697  0.0268  980  ASP   B CB  
7593  C  CG  . ASP   B 676 ? 1.7562 1.7555 2.0473 -0.0949 0.0624  0.0233  980  ASP   B CG  
7594  O  OD1 . ASP   B 676 ? 1.7103 1.7186 2.0208 -0.0965 0.0567  0.0190  980  ASP   B OD1 
7595  O  OD2 . ASP   B 676 ? 1.8251 1.8252 2.0998 -0.0916 0.0622  0.0248  980  ASP   B OD2 
7596  N  N   . THR   B 681 ? 2.2181 2.1646 2.4736 -0.1013 0.1369  0.0476  985  THR   B N   
7597  C  CA  . THR   B 681 ? 2.2599 2.1951 2.4893 -0.0978 0.1433  0.0519  985  THR   B CA  
7598  C  C   . THR   B 681 ? 2.3628 2.2911 2.5686 -0.0937 0.1353  0.0531  985  THR   B C   
7599  O  O   . THR   B 681 ? 2.3631 2.2834 2.5659 -0.0945 0.1349  0.0544  985  THR   B O   
7600  C  CB  . THR   B 681 ? 2.2436 2.1860 2.4695 -0.0957 0.1437  0.0510  985  THR   B CB  
7601  O  OG1 . THR   B 681 ? 2.2528 2.2050 2.4732 -0.0926 0.1303  0.0478  985  THR   B OG1 
7602  C  CG2 . THR   B 681 ? 2.1481 2.1002 2.4001 -0.0994 0.1491  0.0488  985  THR   B CG2 
7603  N  N   . ASP   B 682 ? 2.4132 2.3447 2.6027 -0.0895 0.1289  0.0526  986  ASP   B N   
7604  C  CA  . ASP   B 682 ? 2.4117 2.3377 2.5791 -0.0852 0.1210  0.0536  986  ASP   B CA  
7605  C  C   . ASP   B 682 ? 2.3885 2.3257 2.5507 -0.0819 0.1102  0.0508  986  ASP   B C   
7606  O  O   . ASP   B 682 ? 2.3910 2.3326 2.5501 -0.0800 0.0995  0.0488  986  ASP   B O   
7607  C  CB  . ASP   B 682 ? 2.4008 2.3100 2.5435 -0.0826 0.1291  0.0587  986  ASP   B CB  
7608  C  CG  . ASP   B 682 ? 2.4545 2.3509 2.5895 -0.0829 0.1310  0.0613  986  ASP   B CG  
7609  O  OD1 . ASP   B 682 ? 2.4728 2.3730 2.6243 -0.0859 0.1280  0.0594  986  ASP   B OD1 
7610  O  OD2 . ASP   B 682 ? 2.4431 2.3252 2.5553 -0.0799 0.1352  0.0651  986  ASP   B OD2 
7611  N  N   . GLU   B 683 ? 2.2872 2.2287 2.4482 -0.0811 0.1132  0.0505  987  GLU   B N   
7612  C  CA  . GLU   B 683 ? 2.2127 2.1659 2.3720 -0.0786 0.1036  0.0475  987  GLU   B CA  
7613  C  C   . GLU   B 683 ? 2.2526 2.2197 2.4324 -0.0804 0.0944  0.0429  987  GLU   B C   
7614  O  O   . GLU   B 683 ? 2.1806 2.1559 2.3573 -0.0779 0.0841  0.0405  987  GLU   B O   
7615  C  CB  . GLU   B 683 ? 2.1033 2.0593 2.2626 -0.0784 0.1094  0.0477  987  GLU   B CB  
7616  C  CG  . GLU   B 683 ? 2.0945 2.0575 2.2786 -0.0826 0.1155  0.0460  987  GLU   B CG  
7617  C  CD  . GLU   B 683 ? 1.9494 1.9116 2.1325 -0.0826 0.1245  0.0472  987  GLU   B CD  
7618  O  OE1 . GLU   B 683 ? 1.9449 1.9086 2.1143 -0.0793 0.1213  0.0471  987  GLU   B OE1 
7619  O  OE2 . GLU   B 683 ? 1.8919 1.8518 2.0880 -0.0857 0.1348  0.0482  987  GLU   B OE2 
7620  N  N   . GLU   B 684 ? 2.4840 2.4536 2.6850 -0.0846 0.0981  0.0416  988  GLU   B N   
7621  C  CA  . GLU   B 684 ? 2.4736 2.4549 2.6940 -0.0862 0.0892  0.0371  988  GLU   B CA  
7622  C  C   . GLU   B 684 ? 2.4795 2.4570 2.6959 -0.0855 0.0822  0.0368  988  GLU   B C   
7623  O  O   . GLU   B 684 ? 2.4467 2.4329 2.6700 -0.0847 0.0718  0.0333  988  GLU   B O   
7624  C  CB  . GLU   B 684 ? 2.4662 2.4520 2.7120 -0.0909 0.0953  0.0355  988  GLU   B CB  
7625  C  CG  . GLU   B 684 ? 2.5043 2.4786 2.7533 -0.0941 0.1063  0.0388  988  GLU   B CG  
7626  C  CD  . GLU   B 684 ? 2.5090 2.4824 2.7710 -0.0967 0.1025  0.0372  988  GLU   B CD  
7627  O  OE1 . GLU   B 684 ? 2.4836 2.4654 2.7521 -0.0959 0.0911  0.0335  988  GLU   B OE1 
7628  O  OE2 . GLU   B 684 ? 2.5196 2.4836 2.7853 -0.0996 0.1110  0.0398  988  GLU   B OE2 
7629  N  N   . ARG   B 685 ? 2.2925 2.2567 2.4972 -0.0855 0.0877  0.0405  989  ARG   B N   
7630  C  CA  . ARG   B 685 ? 2.1987 2.1584 2.3996 -0.0849 0.0817  0.0404  989  ARG   B CA  
7631  C  C   . ARG   B 685 ? 2.0668 2.0277 2.2494 -0.0800 0.0720  0.0402  989  ARG   B C   
7632  O  O   . ARG   B 685 ? 2.0270 1.9885 2.2091 -0.0789 0.0641  0.0388  989  ARG   B O   
7633  C  CB  . ARG   B 685 ? 2.2733 2.2179 2.4672 -0.0864 0.0910  0.0445  989  ARG   B CB  
7634  C  CG  . ARG   B 685 ? 2.3258 2.2695 2.5396 -0.0915 0.1008  0.0447  989  ARG   B CG  
7635  C  CD  . ARG   B 685 ? 2.3308 2.2587 2.5363 -0.0928 0.1110  0.0492  989  ARG   B CD  
7636  N  NE  . ARG   B 685 ? 2.3593 2.2807 2.5581 -0.0919 0.1054  0.0495  989  ARG   B NE  
7637  C  CZ  . ARG   B 685 ? 2.4205 2.3269 2.6014 -0.0906 0.1104  0.0536  989  ARG   B CZ  
7638  N  NH1 . ARG   B 685 ? 2.4374 2.3335 2.6045 -0.0897 0.1208  0.0577  989  ARG   B NH1 
7639  N  NH2 . ARG   B 685 ? 2.4288 2.3302 2.6050 -0.0898 0.1047  0.0536  989  ARG   B NH2 
7640  N  N   . GLN   B 686 ? 2.0273 1.9883 2.1951 -0.0770 0.0724  0.0415  990  GLN   B N   
7641  C  CA  . GLN   B 686 ? 1.9022 1.8667 2.0557 -0.0726 0.0627  0.0408  990  GLN   B CA  
7642  C  C   . GLN   B 686 ? 1.8617 1.8413 2.0267 -0.0722 0.0548  0.0367  990  GLN   B C   
7643  O  O   . GLN   B 686 ? 1.8444 1.8285 2.0005 -0.0695 0.0517  0.0364  990  GLN   B O   
7644  C  CB  . GLN   B 686 ? 1.9223 1.8789 2.0536 -0.0693 0.0662  0.0442  990  GLN   B CB  
7645  C  CG  . GLN   B 686 ? 1.9628 1.9032 2.0815 -0.0695 0.0754  0.0485  990  GLN   B CG  
7646  C  CD  . GLN   B 686 ? 2.1001 2.0343 2.2091 -0.0691 0.0846  0.0512  990  GLN   B CD  
7647  O  OE1 . GLN   B 686 ? 2.1025 2.0448 2.2182 -0.0697 0.0855  0.0497  990  GLN   B OE1 
7648  N  NE2 . GLN   B 686 ? 2.1754 2.0943 2.2676 -0.0678 0.0915  0.0552  990  GLN   B NE2 
7649  N  N   . HIS   B 687 ? 1.7962 1.7833 1.9811 -0.0747 0.0515  0.0333  991  HIS   B N   
7650  C  CA  . HIS   B 687 ? 1.6866 1.6869 1.8808 -0.0738 0.0429  0.0293  991  HIS   B CA  
7651  C  C   . HIS   B 687 ? 1.6924 1.6975 1.9045 -0.0758 0.0376  0.0258  991  HIS   B C   
7652  O  O   . HIS   B 687 ? 1.7031 1.7056 1.9291 -0.0795 0.0428  0.0256  991  HIS   B O   
7653  C  CB  . HIS   B 687 ? 1.7026 1.7102 1.9045 -0.0749 0.0466  0.0282  991  HIS   B CB  
7654  C  CG  . HIS   B 687 ? 1.6807 1.7013 1.8961 -0.0746 0.0386  0.0237  991  HIS   B CG  
7655  N  ND1 . HIS   B 687 ? 1.6540 1.6812 1.8906 -0.0778 0.0397  0.0208  991  HIS   B ND1 
7656  C  CD2 . HIS   B 687 ? 1.6613 1.6889 1.8719 -0.0715 0.0291  0.0217  991  HIS   B CD2 
7657  C  CE1 . HIS   B 687 ? 1.6437 1.6810 1.8870 -0.0763 0.0311  0.0171  991  HIS   B CE1 
7658  N  NE2 . HIS   B 687 ? 1.6577 1.6954 1.8854 -0.0726 0.0248  0.0177  991  HIS   B NE2 
7659  N  N   . LEU   B 688 ? 1.6493 1.6614 1.8613 -0.0732 0.0273  0.0230  992  LEU   B N   
7660  C  CA  . LEU   B 688 ? 1.5506 1.5674 1.7775 -0.0742 0.0205  0.0193  992  LEU   B CA  
7661  C  C   . LEU   B 688 ? 1.5403 1.5688 1.7827 -0.0750 0.0171  0.0153  992  LEU   B C   
7662  O  O   . LEU   B 688 ? 1.5658 1.6010 1.8027 -0.0724 0.0134  0.0145  992  LEU   B O   
7663  C  CB  . LEU   B 688 ? 1.4326 1.4489 1.6486 -0.0704 0.0114  0.0187  992  LEU   B CB  
7664  C  CG  . LEU   B 688 ? 1.4129 1.4194 1.6089 -0.0681 0.0137  0.0227  992  LEU   B CG  
7665  C  CD1 . LEU   B 688 ? 1.3655 1.3744 1.5506 -0.0637 0.0046  0.0220  992  LEU   B CD1 
7666  C  CD2 . LEU   B 688 ? 1.5012 1.4972 1.6991 -0.0706 0.0186  0.0245  992  LEU   B CD2 
7667  N  N   . GLN   B 689 ? 1.4758 1.5068 1.7380 -0.0784 0.0181  0.0129  993  GLN   B N   
7668  C  CA  . GLN   B 689 ? 1.4555 1.4972 1.7338 -0.0792 0.0148  0.0089  993  GLN   B CA  
7669  C  C   . GLN   B 689 ? 1.4124 1.4588 1.6980 -0.0777 0.0039  0.0047  993  GLN   B C   
7670  O  O   . GLN   B 689 ? 1.3667 1.4080 1.6550 -0.0783 0.0011  0.0041  993  GLN   B O   
7671  C  CB  . GLN   B 689 ? 1.4563 1.4985 1.7533 -0.0838 0.0226  0.0085  993  GLN   B CB  
7672  C  CG  . GLN   B 689 ? 1.5545 1.5905 1.8446 -0.0853 0.0344  0.0128  993  GLN   B CG  
7673  C  CD  . GLN   B 689 ? 1.6016 1.6370 1.9110 -0.0900 0.0428  0.0126  993  GLN   B CD  
7674  O  OE1 . GLN   B 689 ? 1.6220 1.6594 1.9491 -0.0925 0.0399  0.0098  993  GLN   B OE1 
7675  N  NE2 . GLN   B 689 ? 1.6167 1.6493 1.9233 -0.0912 0.0531  0.0156  993  GLN   B NE2 
7676  N  N   . GLU   B 690 ? 1.4482 1.5037 1.7367 -0.0755 -0.0023 0.0017  994  GLU   B N   
7677  C  CA  . GLU   B 690 ? 1.4154 1.4753 1.7091 -0.0734 -0.0130 -0.0024 994  GLU   B CA  
7678  C  C   . GLU   B 690 ? 1.3703 1.4318 1.6859 -0.0766 -0.0146 -0.0060 994  GLU   B C   
7679  O  O   . GLU   B 690 ? 1.3615 1.4278 1.6919 -0.0793 -0.0107 -0.0073 994  GLU   B O   
7680  C  CB  . GLU   B 690 ? 1.4189 1.4873 1.7093 -0.0702 -0.0183 -0.0044 994  GLU   B CB  
7681  C  CG  . GLU   B 690 ? 1.4622 1.5303 1.7342 -0.0678 -0.0157 -0.0010 994  GLU   B CG  
7682  C  CD  . GLU   B 690 ? 1.5248 1.6015 1.7955 -0.0653 -0.0200 -0.0030 994  GLU   B CD  
7683  O  OE1 . GLU   B 690 ? 1.4733 1.5529 1.7414 -0.0621 -0.0284 -0.0053 994  GLU   B OE1 
7684  O  OE2 . GLU   B 690 ? 1.5833 1.6633 1.8554 -0.0663 -0.0149 -0.0022 994  GLU   B OE2 
7685  N  N   . VAL   B 691 ? 1.2976 1.3554 1.6157 -0.0761 -0.0207 -0.0078 995  VAL   B N   
7686  C  CA  . VAL   B 691 ? 1.2496 1.3076 1.5883 -0.0794 -0.0224 -0.0111 995  VAL   B CA  
7687  C  C   . VAL   B 691 ? 1.1926 1.2527 1.5350 -0.0766 -0.0343 -0.0157 995  VAL   B C   
7688  O  O   . VAL   B 691 ? 1.1369 1.1950 1.4931 -0.0786 -0.0377 -0.0185 995  VAL   B O   
7689  C  CB  . VAL   B 691 ? 1.2460 1.2945 1.5864 -0.0828 -0.0160 -0.0084 995  VAL   B CB  
7690  C  CG1 . VAL   B 691 ? 1.2647 1.3103 1.6010 -0.0853 -0.0039 -0.0039 995  VAL   B CG1 
7691  C  CG2 . VAL   B 691 ? 1.3084 1.3496 1.6322 -0.0799 -0.0202 -0.0068 995  VAL   B CG2 
7692  N  N   . GLY   B 692 ? 1.1392 1.2030 1.4693 -0.0719 -0.0408 -0.0166 996  GLY   B N   
7693  C  CA  . GLY   B 692 ? 1.0680 1.1338 1.4002 -0.0686 -0.0518 -0.0209 996  GLY   B CA  
7694  C  C   . GLY   B 692 ? 1.0348 1.1050 1.3531 -0.0636 -0.0571 -0.0213 996  GLY   B C   
7695  O  O   . GLY   B 692 ? 1.0814 1.1494 1.3824 -0.0613 -0.0550 -0.0178 996  GLY   B O   
7696  N  N   . LEU   B 693 ? 0.9776 1.0537 1.3030 -0.0616 -0.0639 -0.0254 997  LEU   B N   
7697  C  CA  . LEU   B 693 ? 0.9747 1.0548 1.2877 -0.0568 -0.0687 -0.0259 997  LEU   B CA  
7698  C  C   . LEU   B 693 ? 0.9739 1.0539 1.2895 -0.0534 -0.0793 -0.0305 997  LEU   B C   
7699  O  O   . LEU   B 693 ? 1.0227 1.1032 1.3542 -0.0549 -0.0831 -0.0344 997  LEU   B O   
7700  C  CB  . LEU   B 693 ? 0.9999 1.0877 1.3165 -0.0574 -0.0654 -0.0259 997  LEU   B CB  
7701  C  CG  . LEU   B 693 ? 1.0361 1.1237 1.3470 -0.0599 -0.0552 -0.0213 997  LEU   B CG  
7702  C  CD1 . LEU   B 693 ? 1.0350 1.1298 1.3525 -0.0608 -0.0520 -0.0220 997  LEU   B CD1 
7703  C  CD2 . LEU   B 693 ? 1.0215 1.1059 1.3115 -0.0570 -0.0541 -0.0174 997  LEU   B CD2 
7704  N  N   . PHE   B 694 ? 1.0065 1.0858 1.3067 -0.0484 -0.0840 -0.0301 998  PHE   B N   
7705  C  CA  . PHE   B 694 ? 1.0054 1.0828 1.3052 -0.0445 -0.0940 -0.0341 998  PHE   B CA  
7706  C  C   . PHE   B 694 ? 0.9625 1.0407 1.2455 -0.0389 -0.0979 -0.0335 998  PHE   B C   
7707  O  O   . PHE   B 694 ? 0.9677 1.0434 1.2362 -0.0372 -0.0954 -0.0299 998  PHE   B O   
7708  C  CB  . PHE   B 694 ? 0.9866 1.0560 1.2875 -0.0451 -0.0966 -0.0346 998  PHE   B CB  
7709  C  CG  . PHE   B 694 ? 0.9452 1.0116 1.2492 -0.0419 -0.1066 -0.0394 998  PHE   B CG  
7710  C  CD1 . PHE   B 694 ? 0.9417 1.0102 1.2632 -0.0436 -0.1109 -0.0439 998  PHE   B CD1 
7711  C  CD2 . PHE   B 694 ? 0.9678 1.0290 1.2571 -0.0370 -0.1119 -0.0393 998  PHE   B CD2 
7712  C  CE1 . PHE   B 694 ? 1.0141 1.0789 1.3375 -0.0403 -0.1209 -0.0485 998  PHE   B CE1 
7713  C  CE2 . PHE   B 694 ? 0.9900 1.0474 1.2805 -0.0337 -0.1212 -0.0436 998  PHE   B CE2 
7714  C  CZ  . PHE   B 694 ? 1.0060 1.0649 1.3133 -0.0352 -0.1260 -0.0483 998  PHE   B CZ  
7715  N  N   . HIS   B 695 ? 0.9587 1.0404 1.2438 -0.0358 -0.1039 -0.0370 999  HIS   B N   
7716  C  CA  . HIS   B 695 ? 0.9461 1.0274 1.2162 -0.0301 -0.1084 -0.0369 999  HIS   B CA  
7717  C  C   . HIS   B 695 ? 0.9480 1.0217 1.2130 -0.0269 -0.1152 -0.0387 999  HIS   B C   
7718  O  O   . HIS   B 695 ? 0.9605 1.0321 1.2324 -0.0253 -0.1225 -0.0432 999  HIS   B O   
7719  C  CB  . HIS   B 695 ? 0.9257 1.0122 1.1990 -0.0279 -0.1123 -0.0399 999  HIS   B CB  
7720  C  CG  . HIS   B 695 ? 0.9373 1.0244 1.1947 -0.0227 -0.1143 -0.0387 999  HIS   B CG  
7721  N  ND1 . HIS   B 695 ? 0.9635 1.0548 1.2121 -0.0228 -0.1085 -0.0349 999  HIS   B ND1 
7722  C  CD2 . HIS   B 695 ? 0.9600 1.0435 1.2088 -0.0172 -0.1213 -0.0408 999  HIS   B CD2 
7723  C  CE1 . HIS   B 695 ? 0.9665 1.0574 1.2028 -0.0178 -0.1117 -0.0347 999  HIS   B CE1 
7724  N  NE2 . HIS   B 695 ? 0.9439 1.0299 1.1796 -0.0143 -0.1191 -0.0381 999  HIS   B NE2 
7725  N  N   . LEU   B 696 ? 0.9564 1.0257 1.2092 -0.0257 -0.1131 -0.0354 1000 LEU   B N   
7726  C  CA  . LEU   B 696 ? 0.9440 1.0057 1.1902 -0.0221 -0.1193 -0.0369 1000 LEU   B CA  
7727  C  C   . LEU   B 696 ? 0.9163 0.9775 1.1523 -0.0158 -0.1256 -0.0387 1000 LEU   B C   
7728  O  O   . LEU   B 696 ? 0.9437 0.9994 1.1794 -0.0126 -0.1331 -0.0423 1000 LEU   B O   
7729  C  CB  . LEU   B 696 ? 0.9084 0.9657 1.1441 -0.0223 -0.1151 -0.0327 1000 LEU   B CB  
7730  C  CG  . LEU   B 696 ? 0.9004 0.9502 1.1255 -0.0175 -0.1209 -0.0335 1000 LEU   B CG  
7731  C  CD1 . LEU   B 696 ? 0.9075 0.9510 1.1420 -0.0196 -0.1244 -0.0362 1000 LEU   B CD1 
7732  C  CD2 . LEU   B 696 ? 0.9011 0.9494 1.1130 -0.0163 -0.1163 -0.0289 1000 LEU   B CD2 
7733  N  N   . GLY   B 697 ? 0.8845 0.9507 1.1119 -0.0140 -0.1227 -0.0365 1001 GLY   B N   
7734  C  CA  . GLY   B 697 ? 0.9070 0.9724 1.1235 -0.0080 -0.1274 -0.0375 1001 GLY   B CA  
7735  C  C   . GLY   B 697 ? 0.9540 1.0156 1.1547 -0.0040 -0.1268 -0.0345 1001 GLY   B C   
7736  O  O   . GLY   B 697 ? 0.9957 1.0558 1.1864 0.0014  -0.1303 -0.0351 1001 GLY   B O   
7737  N  N   . GLU   B 698 ? 0.9710 1.0308 1.1690 -0.0062 -0.1223 -0.0312 1002 GLU   B N   
7738  C  CA  . GLU   B 698 ? 0.9609 1.0171 1.1448 -0.0025 -0.1217 -0.0283 1002 GLU   B CA  
7739  C  C   . GLU   B 698 ? 0.9684 1.0286 1.1485 -0.0052 -0.1141 -0.0235 1002 GLU   B C   
7740  O  O   . GLU   B 698 ? 0.9717 1.0355 1.1599 -0.0102 -0.1094 -0.0225 1002 GLU   B O   
7741  C  CB  . GLU   B 698 ? 0.9773 1.0249 1.1599 -0.0014 -0.1254 -0.0295 1002 GLU   B CB  
7742  C  CG  . GLU   B 698 ? 1.0330 1.0751 1.2124 0.0035  -0.1334 -0.0334 1002 GLU   B CG  
7743  C  CD  . GLU   B 698 ? 1.0680 1.1106 1.2337 0.0096  -0.1344 -0.0323 1002 GLU   B CD  
7744  O  OE1 . GLU   B 698 ? 1.0508 1.0963 1.2082 0.0104  -0.1294 -0.0282 1002 GLU   B OE1 
7745  O  OE2 . GLU   B 698 ? 1.0883 1.1279 1.2515 0.0138  -0.1403 -0.0356 1002 GLU   B OE2 
7746  N  N   . PHE   B 699 ? 0.8995 0.9586 1.0671 -0.0017 -0.1130 -0.0206 1003 PHE   B N   
7747  C  CA  . PHE   B 699 ? 0.9223 0.9844 1.0851 -0.0035 -0.1067 -0.0162 1003 PHE   B CA  
7748  C  C   . PHE   B 699 ? 0.9429 0.9985 1.1014 -0.0037 -0.1059 -0.0144 1003 PHE   B C   
7749  O  O   . PHE   B 699 ? 0.9470 0.9987 1.0962 0.0008  -0.1084 -0.0138 1003 PHE   B O   
7750  C  CB  . PHE   B 699 ? 0.9858 1.0521 1.1386 0.0003  -0.1057 -0.0140 1003 PHE   B CB  
7751  C  CG  . PHE   B 699 ? 0.9529 1.0243 1.1033 -0.0022 -0.0996 -0.0100 1003 PHE   B CG  
7752  C  CD1 . PHE   B 699 ? 0.9947 1.0723 1.1505 -0.0053 -0.0965 -0.0099 1003 PHE   B CD1 
7753  C  CD2 . PHE   B 699 ? 0.9018 0.9713 1.0441 -0.0011 -0.0974 -0.0067 1003 PHE   B CD2 
7754  C  CE1 . PHE   B 699 ? 1.0136 1.0951 1.1665 -0.0073 -0.0915 -0.0065 1003 PHE   B CE1 
7755  C  CE2 . PHE   B 699 ? 0.8765 0.9499 1.0162 -0.0031 -0.0926 -0.0035 1003 PHE   B CE2 
7756  C  CZ  . PHE   B 699 ? 0.8925 0.9717 1.0373 -0.0062 -0.0897 -0.0034 1003 PHE   B CZ  
7757  N  N   . VAL   B 700 ? 0.9511 1.0054 1.1160 -0.0086 -0.1021 -0.0134 1004 VAL   B N   
7758  C  CA  . VAL   B 700 ? 0.9151 0.9624 1.0771 -0.0093 -0.1014 -0.0119 1004 VAL   B CA  
7759  C  C   . VAL   B 700 ? 0.9010 0.9487 1.0523 -0.0081 -0.0973 -0.0075 1004 VAL   B C   
7760  O  O   . VAL   B 700 ? 0.8983 0.9506 1.0496 -0.0106 -0.0924 -0.0052 1004 VAL   B O   
7761  C  CB  . VAL   B 700 ? 0.9034 0.9483 1.0768 -0.0150 -0.0987 -0.0126 1004 VAL   B CB  
7762  C  CG1 . VAL   B 700 ? 0.9110 0.9486 1.0802 -0.0160 -0.0966 -0.0104 1004 VAL   B CG1 
7763  C  CG2 . VAL   B 700 ? 0.9047 0.9483 1.0891 -0.0157 -0.1038 -0.0173 1004 VAL   B CG2 
7764  N  N   . ASN   B 701 ? 0.9112 0.9537 1.0534 -0.0043 -0.0995 -0.0066 1005 ASN   B N   
7765  C  CA  . ASN   B 701 ? 0.9072 0.9499 1.0392 -0.0024 -0.0965 -0.0027 1005 ASN   B CA  
7766  C  C   . ASN   B 701 ? 0.9513 0.9869 1.0807 -0.0042 -0.0942 -0.0007 1005 ASN   B C   
7767  O  O   . ASN   B 701 ? 0.9544 0.9908 1.0789 -0.0051 -0.0901 0.0026  1005 ASN   B O   
7768  C  CB  . ASN   B 701 ? 0.9082 0.9507 1.0309 0.0038  -0.1001 -0.0026 1005 ASN   B CB  
7769  C  CG  . ASN   B 701 ? 0.9008 0.9513 1.0210 0.0057  -0.0991 -0.0016 1005 ASN   B CG  
7770  O  OD1 . ASN   B 701 ? 0.9210 0.9771 1.0451 0.0024  -0.0956 -0.0006 1005 ASN   B OD1 
7771  N  ND2 . ASN   B 701 ? 0.9014 0.9521 1.0151 0.0110  -0.1019 -0.0019 1005 ASN   B ND2 
7772  N  N   . VAL   B 702 ? 0.9213 0.9496 1.0537 -0.0047 -0.0969 -0.0026 1006 VAL   B N   
7773  C  CA  . VAL   B 702 ? 0.9291 0.9497 1.0593 -0.0065 -0.0948 -0.0009 1006 VAL   B CA  
7774  C  C   . VAL   B 702 ? 0.9556 0.9714 1.0968 -0.0105 -0.0957 -0.0036 1006 VAL   B C   
7775  O  O   . VAL   B 702 ? 1.0274 1.0422 1.1736 -0.0092 -0.1009 -0.0072 1006 VAL   B O   
7776  C  CB  . VAL   B 702 ? 0.9354 0.9504 1.0545 -0.0013 -0.0978 0.0001  1006 VAL   B CB  
7777  C  CG1 . VAL   B 702 ? 0.9399 0.9531 1.0588 0.0028  -0.1041 -0.0033 1006 VAL   B CG1 
7778  C  CG2 . VAL   B 702 ? 0.9605 0.9665 1.0775 -0.0030 -0.0962 0.0015  1006 VAL   B CG2 
7779  N  N   . PHE   B 703 ? 1.0570 1.0695 1.2020 -0.0151 -0.0907 -0.0018 1007 PHE   B N   
7780  C  CA  . PHE   B 703 ? 1.0335 1.0396 1.1879 -0.0190 -0.0908 -0.0036 1007 PHE   B CA  
7781  C  C   . PHE   B 703 ? 1.0802 1.0766 1.2267 -0.0178 -0.0908 -0.0019 1007 PHE   B C   
7782  O  O   . PHE   B 703 ? 1.1242 1.1191 1.2599 -0.0161 -0.0879 0.0017  1007 PHE   B O   
7783  C  CB  . PHE   B 703 ? 1.0319 1.0396 1.1960 -0.0251 -0.0844 -0.0026 1007 PHE   B CB  
7784  C  CG  . PHE   B 703 ? 1.0203 1.0361 1.1957 -0.0272 -0.0847 -0.0051 1007 PHE   B CG  
7785  C  CD1 . PHE   B 703 ? 1.0053 1.0212 1.1922 -0.0280 -0.0895 -0.0094 1007 PHE   B CD1 
7786  C  CD2 . PHE   B 703 ? 1.0266 1.0495 1.2013 -0.0284 -0.0802 -0.0033 1007 PHE   B CD2 
7787  C  CE1 . PHE   B 703 ? 1.0108 1.0340 1.2082 -0.0298 -0.0899 -0.0118 1007 PHE   B CE1 
7788  C  CE2 . PHE   B 703 ? 1.0036 1.0337 1.1885 -0.0302 -0.0804 -0.0056 1007 PHE   B CE2 
7789  C  CZ  . PHE   B 703 ? 0.9935 1.0239 1.1899 -0.0309 -0.0852 -0.0098 1007 PHE   B CZ  
7790  N  N   . CYS   B 704 ? 1.1229 1.1126 1.2752 -0.0188 -0.0941 -0.0044 1008 CYS   B N   
7791  C  CA  . CYS   B 704 ? 1.1403 1.1204 1.2844 -0.0167 -0.0955 -0.0033 1008 CYS   B CA  
7792  C  C   . CYS   B 704 ? 1.1642 1.1371 1.3190 -0.0206 -0.0965 -0.0056 1008 CYS   B C   
7793  O  O   . CYS   B 704 ? 1.1552 1.1283 1.3183 -0.0205 -0.1021 -0.0097 1008 CYS   B O   
7794  C  CB  . CYS   B 704 ? 1.1445 1.1237 1.2788 -0.0100 -0.1019 -0.0046 1008 CYS   B CB  
7795  S  SG  . CYS   B 704 ? 1.2323 1.2004 1.3542 -0.0065 -0.1032 -0.0027 1008 CYS   B SG  
7796  N  N   . HIS   B 705 ? 1.1738 1.1400 1.3282 -0.0240 -0.0914 -0.0030 1009 HIS   B N   
7797  C  CA  . HIS   B 705 ? 1.1926 1.1518 1.3582 -0.0284 -0.0914 -0.0048 1009 HIS   B CA  
7798  C  C   . HIS   B 705 ? 1.1797 1.1303 1.3409 -0.0251 -0.0981 -0.0070 1009 HIS   B C   
7799  O  O   . HIS   B 705 ? 1.1868 1.1328 1.3340 -0.0207 -0.0992 -0.0050 1009 HIS   B O   
7800  C  CB  . HIS   B 705 ? 1.2197 1.1734 1.3851 -0.0328 -0.0832 -0.0011 1009 HIS   B CB  
7801  C  CG  . HIS   B 705 ? 1.2349 1.1946 1.4114 -0.0381 -0.0769 -0.0004 1009 HIS   B CG  
7802  N  ND1 . HIS   B 705 ? 1.2562 1.2160 1.4499 -0.0433 -0.0759 -0.0029 1009 HIS   B ND1 
7803  C  CD2 . HIS   B 705 ? 1.2346 1.2003 1.4075 -0.0388 -0.0713 0.0023  1009 HIS   B CD2 
7804  C  CE1 . HIS   B 705 ? 1.2591 1.2248 1.4593 -0.0468 -0.0696 -0.0016 1009 HIS   B CE1 
7805  N  NE2 . HIS   B 705 ? 1.2266 1.1957 1.4139 -0.0442 -0.0667 0.0016  1009 HIS   B NE2 
7806  N  N   . GLY   B 706 ? 1.1495 1.0976 1.3229 -0.0272 -0.1027 -0.0111 1010 GLY   B N   
7807  C  CA  . GLY   B 706 ? 1.1698 1.1095 1.3396 -0.0239 -0.1099 -0.0137 1010 GLY   B CA  
7808  C  C   . GLY   B 706 ? 1.1399 1.0816 1.3202 -0.0234 -0.1176 -0.0191 1010 GLY   B C   
7809  O  O   . GLY   B 706 ? 1.1222 1.0729 1.3092 -0.0237 -0.1184 -0.0208 1010 GLY   B O   
7810  N  N   . SER   B 707 ? 1.1529 1.0857 1.3346 -0.0225 -0.1236 -0.0220 1011 SER   B N   
7811  C  CA  . SER   B 707 ? 1.1760 1.1084 1.3648 -0.0208 -0.1324 -0.0275 1011 SER   B CA  
7812  C  C   . SER   B 707 ? 1.2212 1.1474 1.3951 -0.0134 -0.1394 -0.0288 1011 SER   B C   
7813  O  O   . SER   B 707 ? 1.2803 1.2014 1.4404 -0.0103 -0.1377 -0.0257 1011 SER   B O   
7814  C  CB  . SER   B 707 ? 1.1904 1.1171 1.3956 -0.0260 -0.1348 -0.0307 1011 SER   B CB  
7815  O  OG  . SER   B 707 ? 1.1677 1.1012 1.3900 -0.0325 -0.1298 -0.0308 1011 SER   B OG  
7816  N  N   . LEU   B 708 ? 1.2469 1.1732 1.4238 -0.0105 -0.1475 -0.0335 1012 LEU   B N   
7817  C  CA  . LEU   B 708 ? 1.3479 1.2668 1.5118 -0.0035 -0.1548 -0.0355 1012 LEU   B CA  
7818  C  C   . LEU   B 708 ? 1.3851 1.2948 1.5571 -0.0044 -0.1627 -0.0404 1012 LEU   B C   
7819  O  O   . LEU   B 708 ? 1.3827 1.2864 1.5469 0.0013  -0.1706 -0.0436 1012 LEU   B O   
7820  C  CB  . LEU   B 708 ? 1.3368 1.2624 1.4934 0.0021  -0.1578 -0.0365 1012 LEU   B CB  
7821  C  CG  . LEU   B 708 ? 1.2093 1.1451 1.3613 0.0018  -0.1499 -0.0319 1012 LEU   B CG  
7822  C  CD1 . LEU   B 708 ? 1.1278 1.0706 1.2744 0.0066  -0.1523 -0.0330 1012 LEU   B CD1 
7823  C  CD2 . LEU   B 708 ? 1.2054 1.1376 1.3440 0.0037  -0.1450 -0.0272 1012 LEU   B CD2 
7824  N  N   . VAL   B 709 ? 1.3692 1.2775 1.5570 -0.0114 -0.1605 -0.0410 1013 VAL   B N   
7825  C  CA  . VAL   B 709 ? 1.4286 1.3293 1.6280 -0.0137 -0.1675 -0.0458 1013 VAL   B CA  
7826  C  C   . VAL   B 709 ? 1.5043 1.3957 1.7048 -0.0174 -0.1640 -0.0437 1013 VAL   B C   
7827  O  O   . VAL   B 709 ? 1.5333 1.4222 1.7206 -0.0159 -0.1585 -0.0391 1013 VAL   B O   
7828  C  CB  . VAL   B 709 ? 1.4073 1.3157 1.6275 -0.0189 -0.1684 -0.0491 1013 VAL   B CB  
7829  C  CG1 . VAL   B 709 ? 1.3330 1.2462 1.5515 -0.0139 -0.1757 -0.0530 1013 VAL   B CG1 
7830  C  CG2 . VAL   B 709 ? 1.3409 1.2589 1.5683 -0.0244 -0.1577 -0.0448 1013 VAL   B CG2 
7831  N  N   . MET   B 710 ? 1.5123 1.3983 1.7282 -0.0222 -0.1673 -0.0470 1014 MET   B N   
7832  C  CA  . MET   B 710 ? 1.5718 1.4485 1.7905 -0.0265 -0.1636 -0.0451 1014 MET   B CA  
7833  C  C   . MET   B 710 ? 1.5683 1.4341 1.7673 -0.0209 -0.1659 -0.0435 1014 MET   B C   
7834  O  O   . MET   B 710 ? 1.5143 1.3698 1.7123 -0.0192 -0.1732 -0.0468 1014 MET   B O   
7835  C  CB  . MET   B 710 ? 1.5948 1.4768 1.8188 -0.0325 -0.1516 -0.0398 1014 MET   B CB  
7836  C  CG  . MET   B 710 ? 1.5639 1.4363 1.7820 -0.0349 -0.1454 -0.0357 1014 MET   B CG  
7837  S  SD  . MET   B 710 ? 1.7714 1.6323 2.0056 -0.0414 -0.1470 -0.0381 1014 MET   B SD  
7838  C  CE  . MET   B 710 ? 1.6070 1.4775 1.8678 -0.0500 -0.1418 -0.0392 1014 MET   B CE  
7839  N  N   . PRO   B 719 ? 1.8442 1.7802 2.2500 -0.0877 -0.1138 -0.0466 1023 PRO   B N   
7840  C  CA  . PRO   B 719 ? 1.8487 1.7964 2.2683 -0.0876 -0.1175 -0.0504 1023 PRO   B CA  
7841  C  C   . PRO   B 719 ? 1.8604 1.8176 2.2708 -0.0861 -0.1099 -0.0466 1023 PRO   B C   
7842  O  O   . PRO   B 719 ? 1.8600 1.8216 2.2802 -0.0910 -0.0995 -0.0436 1023 PRO   B O   
7843  C  CB  . PRO   B 719 ? 1.8166 1.7627 2.2291 -0.0813 -0.1319 -0.0557 1023 PRO   B CB  
7844  C  CG  . PRO   B 719 ? 1.8458 1.7799 2.2375 -0.0774 -0.1346 -0.0540 1023 PRO   B CG  
7845  C  CD  . PRO   B 719 ? 1.8442 1.7743 2.2280 -0.0805 -0.1222 -0.0474 1023 PRO   B CD  
7846  N  N   . THR   B 720 ? 1.7508 1.7109 2.1430 -0.0795 -0.1151 -0.0468 1024 THR   B N   
7847  C  CA  . THR   B 720 ? 1.5825 1.5499 1.9620 -0.0774 -0.1084 -0.0429 1024 THR   B CA  
7848  C  C   . THR   B 720 ? 1.5560 1.5170 1.9152 -0.0762 -0.1009 -0.0368 1024 THR   B C   
7849  O  O   . THR   B 720 ? 1.6226 1.5741 1.9704 -0.0739 -0.1042 -0.0363 1024 THR   B O   
7850  C  CB  . THR   B 720 ? 1.5036 1.4764 1.8721 -0.0707 -0.1169 -0.0455 1024 THR   B CB  
7851  O  OG1 . THR   B 720 ? 1.5189 1.4833 1.8716 -0.0654 -0.1249 -0.0467 1024 THR   B OG1 
7852  C  CG2 . THR   B 720 ? 1.5068 1.4865 1.8938 -0.0713 -0.1241 -0.0513 1024 THR   B CG2 
7853  N  N   . GLN   B 721 ? 1.4671 1.4332 1.8210 -0.0773 -0.0912 -0.0323 1025 GLN   B N   
7854  C  CA  . GLN   B 721 ? 1.4286 1.3888 1.7654 -0.0770 -0.0829 -0.0264 1025 GLN   B CA  
7855  C  C   . GLN   B 721 ? 1.4377 1.4014 1.7527 -0.0709 -0.0839 -0.0242 1025 GLN   B C   
7856  O  O   . GLN   B 721 ? 1.4347 1.4080 1.7504 -0.0690 -0.0852 -0.0253 1025 GLN   B O   
7857  C  CB  . GLN   B 721 ? 1.4317 1.3935 1.7771 -0.0827 -0.0704 -0.0226 1025 GLN   B CB  
7858  C  CG  . GLN   B 721 ? 1.4653 1.4192 1.8247 -0.0885 -0.0660 -0.0222 1025 GLN   B CG  
7859  C  CD  . GLN   B 721 ? 1.4932 1.4350 1.8363 -0.0876 -0.0629 -0.0183 1025 GLN   B CD  
7860  O  OE1 . GLN   B 721 ? 1.5337 1.4696 1.8658 -0.0836 -0.0707 -0.0197 1025 GLN   B OE1 
7861  N  NE2 . GLN   B 721 ? 1.4608 1.3982 1.8017 -0.0911 -0.0514 -0.0134 1025 GLN   B NE2 
7862  N  N   . GLY   B 722 ? 1.5157 1.4717 1.8121 -0.0678 -0.0830 -0.0209 1026 GLY   B N   
7863  C  CA  . GLY   B 722 ? 1.4748 1.4335 1.7509 -0.0624 -0.0828 -0.0182 1026 GLY   B CA  
7864  C  C   . GLY   B 722 ? 1.4473 1.4070 1.7145 -0.0561 -0.0934 -0.0214 1026 GLY   B C   
7865  O  O   . GLY   B 722 ? 1.5389 1.4985 1.8159 -0.0556 -0.1015 -0.0263 1026 GLY   B O   
7866  N  N   . SER   B 723 ? 1.2428 1.2028 1.4908 -0.0509 -0.0934 -0.0187 1027 SER   B N   
7867  C  CA  . SER   B 723 ? 1.2140 1.1765 1.4529 -0.0446 -0.1021 -0.0213 1027 SER   B CA  
7868  C  C   . SER   B 723 ? 1.2029 1.1701 1.4252 -0.0405 -0.0993 -0.0178 1027 SER   B C   
7869  O  O   . SER   B 723 ? 1.1623 1.1241 1.3704 -0.0383 -0.0967 -0.0143 1027 SER   B O   
7870  C  CB  . SER   B 723 ? 1.1659 1.1185 1.3986 -0.0414 -0.1092 -0.0233 1027 SER   B CB  
7871  O  OG  . SER   B 723 ? 1.0870 1.0419 1.3087 -0.0348 -0.1162 -0.0250 1027 SER   B OG  
7872  N  N   . VAL   B 724 ? 1.1738 1.1508 1.3979 -0.0392 -0.1000 -0.0188 1028 VAL   B N   
7873  C  CA  . VAL   B 724 ? 1.1106 1.0929 1.3204 -0.0352 -0.0982 -0.0159 1028 VAL   B CA  
7874  C  C   . VAL   B 724 ? 1.0688 1.0551 1.2744 -0.0297 -0.1061 -0.0191 1028 VAL   B C   
7875  O  O   . VAL   B 724 ? 1.0555 1.0480 1.2708 -0.0303 -0.1089 -0.0222 1028 VAL   B O   
7876  C  CB  . VAL   B 724 ? 1.0984 1.0884 1.3122 -0.0386 -0.0905 -0.0134 1028 VAL   B CB  
7877  C  CG1 . VAL   B 724 ? 1.1481 1.1426 1.3467 -0.0345 -0.0889 -0.0104 1028 VAL   B CG1 
7878  C  CG2 . VAL   B 724 ? 1.0938 1.0789 1.3122 -0.0440 -0.0824 -0.0105 1028 VAL   B CG2 
7879  N  N   . LEU   B 725 ? 1.0726 1.0547 1.2634 -0.0242 -0.1096 -0.0183 1029 LEU   B N   
7880  C  CA  . LEU   B 725 ? 1.0632 1.0481 1.2466 -0.0182 -0.1160 -0.0204 1029 LEU   B CA  
7881  C  C   . LEU   B 725 ? 1.0635 1.0569 1.2392 -0.0163 -0.1122 -0.0176 1029 LEU   B C   
7882  O  O   . LEU   B 725 ? 1.0990 1.0933 1.2685 -0.0174 -0.1061 -0.0134 1029 LEU   B O   
7883  C  CB  . LEU   B 725 ? 1.0269 1.0035 1.1975 -0.0130 -0.1206 -0.0204 1029 LEU   B CB  
7884  C  CG  . LEU   B 725 ? 0.9834 0.9509 1.1586 -0.0128 -0.1269 -0.0240 1029 LEU   B CG  
7885  C  CD1 . LEU   B 725 ? 1.0628 1.0233 1.2226 -0.0067 -0.1307 -0.0234 1029 LEU   B CD1 
7886  C  CD2 . LEU   B 725 ? 1.0474 1.0177 1.2325 -0.0124 -0.1335 -0.0291 1029 LEU   B CD2 
7887  N  N   . PHE   B 726 ? 1.0117 1.0110 1.1874 -0.0132 -0.1162 -0.0199 1030 PHE   B N   
7888  C  CA  . PHE   B 726 ? 0.9515 0.9584 1.1192 -0.0108 -0.1133 -0.0173 1030 PHE   B CA  
7889  C  C   . PHE   B 726 ? 0.9422 0.9498 1.1015 -0.0044 -0.1191 -0.0192 1030 PHE   B C   
7890  O  O   . PHE   B 726 ? 0.9815 0.9862 1.1444 -0.0026 -0.1255 -0.0232 1030 PHE   B O   
7891  C  CB  . PHE   B 726 ? 0.9542 0.9697 1.1317 -0.0150 -0.1091 -0.0172 1030 PHE   B CB  
7892  C  CG  . PHE   B 726 ? 0.9298 0.9485 1.1193 -0.0160 -0.1135 -0.0217 1030 PHE   B CG  
7893  C  CD1 . PHE   B 726 ? 0.9734 0.9903 1.1777 -0.0209 -0.1136 -0.0241 1030 PHE   B CD1 
7894  C  CD2 . PHE   B 726 ? 0.9247 0.9485 1.1113 -0.0122 -0.1172 -0.0235 1030 PHE   B CD2 
7895  C  CE1 . PHE   B 726 ? 0.9519 0.9722 1.1684 -0.0217 -0.1179 -0.0284 1030 PHE   B CE1 
7896  C  CE2 . PHE   B 726 ? 0.9225 0.9489 1.1198 -0.0128 -0.1214 -0.0277 1030 PHE   B CE2 
7897  C  CZ  . PHE   B 726 ? 0.9247 0.9495 1.1373 -0.0176 -0.1220 -0.0302 1030 PHE   B CZ  
7898  N  N   . GLY   B 727 ? 0.9373 0.9484 1.0853 -0.0009 -0.1169 -0.0162 1031 GLY   B N   
7899  C  CA  . GLY   B 727 ? 0.9356 0.9488 1.0761 0.0050  -0.1209 -0.0173 1031 GLY   B CA  
7900  C  C   . GLY   B 727 ? 0.9419 0.9648 1.0829 0.0046  -0.1176 -0.0160 1031 GLY   B C   
7901  O  O   . GLY   B 727 ? 0.9211 0.9487 1.0647 0.0007  -0.1119 -0.0133 1031 GLY   B O   
7902  N  N   . THR   B 728 ? 0.9530 0.9783 1.0909 0.0087  -0.1212 -0.0179 1032 THR   B N   
7903  C  CA  . THR   B 728 ? 0.9150 0.9491 1.0547 0.0081  -0.1187 -0.0172 1032 THR   B CA  
7904  C  C   . THR   B 728 ? 0.9139 0.9500 1.0421 0.0140  -0.1192 -0.0158 1032 THR   B C   
7905  O  O   . THR   B 728 ? 0.9197 0.9507 1.0388 0.0186  -0.1212 -0.0152 1032 THR   B O   
7906  C  CB  . THR   B 728 ? 0.9127 0.9488 1.0627 0.0064  -0.1220 -0.0213 1032 THR   B CB  
7907  O  OG1 . THR   B 728 ? 0.9421 0.9724 1.0890 0.0111  -0.1289 -0.0248 1032 THR   B OG1 
7908  C  CG2 . THR   B 728 ? 0.9126 0.9485 1.0759 0.0001  -0.1203 -0.0223 1032 THR   B CG2 
7909  N  N   . VAL   B 729 ? 0.9735 1.0172 1.1028 0.0138  -0.1171 -0.0152 1033 VAL   B N   
7910  C  CA  . VAL   B 729 ? 0.9667 1.0131 1.0868 0.0188  -0.1169 -0.0139 1033 VAL   B CA  
7911  C  C   . VAL   B 729 ? 0.9572 0.9985 1.0731 0.0241  -0.1228 -0.0172 1033 VAL   B C   
7912  O  O   . VAL   B 729 ? 1.0065 1.0454 1.1124 0.0296  -0.1236 -0.0162 1033 VAL   B O   
7913  C  CB  . VAL   B 729 ? 0.9142 0.9697 1.0376 0.0165  -0.1131 -0.0125 1033 VAL   B CB  
7914  C  CG1 . VAL   B 729 ? 1.0134 1.0713 1.1298 0.0215  -0.1139 -0.0123 1033 VAL   B CG1 
7915  C  CG2 . VAL   B 729 ? 0.8913 0.9511 1.0146 0.0131  -0.1074 -0.0087 1033 VAL   B CG2 
7916  N  N   . ASN   B 730 ? 0.9395 0.9787 1.0629 0.0226  -0.1269 -0.0211 1034 ASN   B N   
7917  C  CA  . ASN   B 730 ? 0.9400 0.9735 1.0594 0.0277  -0.1331 -0.0247 1034 ASN   B CA  
7918  C  C   . ASN   B 730 ? 0.9841 1.0077 1.0997 0.0302  -0.1377 -0.0264 1034 ASN   B C   
7919  O  O   . ASN   B 730 ? 1.0121 1.0295 1.1258 0.0337  -0.1439 -0.0301 1034 ASN   B O   
7920  C  CB  . ASN   B 730 ? 0.9578 0.9933 1.0873 0.0253  -0.1363 -0.0285 1034 ASN   B CB  
7921  C  CG  . ASN   B 730 ? 1.0506 1.0943 1.1811 0.0247  -0.1330 -0.0274 1034 ASN   B CG  
7922  O  OD1 . ASN   B 730 ? 1.0878 1.1309 1.2108 0.0295  -0.1346 -0.0279 1034 ASN   B OD1 
7923  N  ND2 . ASN   B 730 ? 1.0684 1.1192 1.2078 0.0189  -0.1283 -0.0259 1034 ASN   B ND2 
7924  N  N   . GLY   B 731 ? 1.0631 1.0845 1.1770 0.0286  -0.1352 -0.0239 1035 GLY   B N   
7925  C  CA  . GLY   B 731 ? 1.0570 1.0687 1.1675 0.0307  -0.1393 -0.0255 1035 GLY   B CA  
7926  C  C   . GLY   B 731 ? 1.0304 1.0378 1.1520 0.0268  -0.1435 -0.0292 1035 GLY   B C   
7927  O  O   . GLY   B 731 ? 1.0172 1.0160 1.1369 0.0281  -0.1475 -0.0309 1035 GLY   B O   
7928  N  N   . MET   B 732 ? 0.9870 1.0002 1.1207 0.0220  -0.1427 -0.0307 1036 MET   B N   
7929  C  CA  . MET   B 732 ? 0.9393 0.9501 1.0862 0.0174  -0.1457 -0.0340 1036 MET   B CA  
7930  C  C   . MET   B 732 ? 0.9413 0.9496 1.0917 0.0130  -0.1420 -0.0317 1036 MET   B C   
7931  O  O   . MET   B 732 ? 0.9488 0.9617 1.0977 0.0105  -0.1353 -0.0277 1036 MET   B O   
7932  C  CB  . MET   B 732 ? 0.9472 0.9663 1.1062 0.0130  -0.1438 -0.0351 1036 MET   B CB  
7933  C  CG  . MET   B 732 ? 0.9810 0.9988 1.1557 0.0085  -0.1472 -0.0390 1036 MET   B CG  
7934  S  SD  . MET   B 732 ? 1.0320 1.0522 1.2198 0.0002  -0.1407 -0.0368 1036 MET   B SD  
7935  C  CE  . MET   B 732 ? 0.9724 0.9949 1.1797 -0.0039 -0.1446 -0.0419 1036 MET   B CE  
7936  N  N   . ILE   B 733 ? 0.9494 0.9497 1.1039 0.0123  -0.1464 -0.0344 1037 ILE   B N   
7937  C  CA  . ILE   B 733 ? 0.9816 0.9787 1.1406 0.0077  -0.1431 -0.0326 1037 ILE   B CA  
7938  C  C   . ILE   B 733 ? 1.0065 1.0035 1.1826 0.0020  -0.1446 -0.0357 1037 ILE   B C   
7939  O  O   . ILE   B 733 ? 1.0258 1.0202 1.2077 0.0032  -0.1515 -0.0403 1037 ILE   B O   
7940  C  CB  . ILE   B 733 ? 0.9624 0.9495 1.1112 0.0115  -0.1461 -0.0323 1037 ILE   B CB  
7941  C  CG1 . ILE   B 733 ? 0.9616 0.9498 1.0946 0.0171  -0.1438 -0.0289 1037 ILE   B CG1 
7942  C  CG2 . ILE   B 733 ? 0.9660 0.9491 1.1201 0.0065  -0.1427 -0.0307 1037 ILE   B CG2 
7943  C  CD1 . ILE   B 733 ? 0.9716 0.9505 1.0929 0.0234  -0.1489 -0.0301 1037 ILE   B CD1 
7944  N  N   . GLY   B 734 ? 0.9868 0.9866 1.1711 -0.0041 -0.1381 -0.0332 1038 GLY   B N   
7945  C  CA  . GLY   B 734 ? 0.9798 0.9820 1.1817 -0.0101 -0.1376 -0.0355 1038 GLY   B CA  
7946  C  C   . GLY   B 734 ? 1.0413 1.0394 1.2493 -0.0154 -0.1327 -0.0335 1038 GLY   B C   
7947  O  O   . GLY   B 734 ? 1.0152 1.0099 1.2134 -0.0149 -0.1287 -0.0297 1038 GLY   B O   
7948  N  N   . LEU   B 735 ? 1.1537 1.1523 1.3786 -0.0205 -0.1331 -0.0361 1039 LEU   B N   
7949  C  CA  . LEU   B 735 ? 1.1324 1.1261 1.3660 -0.0258 -0.1294 -0.0351 1039 LEU   B CA  
7950  C  C   . LEU   B 735 ? 1.1460 1.1464 1.3953 -0.0322 -0.1232 -0.0346 1039 LEU   B C   
7951  O  O   . LEU   B 735 ? 1.1555 1.1617 1.4160 -0.0330 -0.1260 -0.0379 1039 LEU   B O   
7952  C  CB  . LEU   B 735 ? 1.1355 1.1210 1.3757 -0.0255 -0.1372 -0.0395 1039 LEU   B CB  
7953  C  CG  . LEU   B 735 ? 1.1958 1.1737 1.4403 -0.0296 -0.1342 -0.0381 1039 LEU   B CG  
7954  C  CD1 . LEU   B 735 ? 1.2136 1.1896 1.4428 -0.0285 -0.1275 -0.0325 1039 LEU   B CD1 
7955  C  CD2 . LEU   B 735 ? 1.2768 1.2451 1.5208 -0.0271 -0.1430 -0.0419 1039 LEU   B CD2 
7956  N  N   . VAL   B 736 ? 1.1209 1.1205 1.3706 -0.0363 -0.1147 -0.0305 1040 VAL   B N   
7957  C  CA  . VAL   B 736 ? 1.1077 1.1119 1.3728 -0.0426 -0.1082 -0.0299 1040 VAL   B CA  
7958  C  C   . VAL   B 736 ? 1.1903 1.1868 1.4630 -0.0471 -0.1050 -0.0291 1040 VAL   B C   
7959  O  O   . VAL   B 736 ? 1.1664 1.1557 1.4276 -0.0461 -0.1030 -0.0262 1040 VAL   B O   
7960  C  CB  . VAL   B 736 ? 1.0202 1.0306 1.2789 -0.0436 -0.0996 -0.0255 1040 VAL   B CB  
7961  C  CG1 . VAL   B 736 ? 1.0946 1.1096 1.3695 -0.0495 -0.0934 -0.0253 1040 VAL   B CG1 
7962  C  CG2 . VAL   B 736 ? 1.0856 1.1028 1.3360 -0.0390 -0.1028 -0.0260 1040 VAL   B CG2 
7963  N  N   . THR   B 737 ? 1.2483 1.2461 1.5407 -0.0521 -0.1047 -0.0318 1041 THR   B N   
7964  C  CA  . THR   B 737 ? 1.2872 1.2785 1.5897 -0.0574 -0.1003 -0.0309 1041 THR   B CA  
7965  C  C   . THR   B 737 ? 1.3075 1.3050 1.6286 -0.0634 -0.0936 -0.0309 1041 THR   B C   
7966  O  O   . THR   B 737 ? 1.2587 1.2644 1.5897 -0.0634 -0.0960 -0.0337 1041 THR   B O   
7967  C  CB  . THR   B 737 ? 1.2551 1.2389 1.5646 -0.0572 -0.1088 -0.0351 1041 THR   B CB  
7968  O  OG1 . THR   B 737 ? 1.3497 1.3277 1.6708 -0.0630 -0.1037 -0.0341 1041 THR   B OG1 
7969  C  CG2 . THR   B 737 ? 1.2441 1.2328 1.5674 -0.0565 -0.1172 -0.0410 1041 THR   B CG2 
7970  N  N   . SER   B 738 ? 1.3822 1.3753 1.7073 -0.0682 -0.0848 -0.0275 1042 SER   B N   
7971  C  CA  . SER   B 738 ? 1.3634 1.3612 1.7043 -0.0739 -0.0764 -0.0264 1042 SER   B CA  
7972  C  C   . SER   B 738 ? 1.3436 1.3400 1.7076 -0.0785 -0.0789 -0.0303 1042 SER   B C   
7973  O  O   . SER   B 738 ? 1.3840 1.3725 1.7499 -0.0788 -0.0834 -0.0319 1042 SER   B O   
7974  C  CB  . SER   B 738 ? 1.3897 1.3826 1.7222 -0.0765 -0.0650 -0.0205 1042 SER   B CB  
7975  O  OG  . SER   B 738 ? 1.4175 1.4098 1.7276 -0.0719 -0.0639 -0.0170 1042 SER   B OG  
7976  N  N   . LEU   B 739 ? 1.3831 1.3873 1.7651 -0.0819 -0.0762 -0.0320 1043 LEU   B N   
7977  C  CA  . LEU   B 739 ? 1.4795 1.4840 1.8856 -0.0862 -0.0792 -0.0363 1043 LEU   B CA  
7978  C  C   . LEU   B 739 ? 1.5510 1.5546 1.9712 -0.0928 -0.0676 -0.0333 1043 LEU   B C   
7979  O  O   . LEU   B 739 ? 1.5155 1.5187 1.9264 -0.0939 -0.0573 -0.0282 1043 LEU   B O   
7980  C  CB  . LEU   B 739 ? 1.4236 1.4378 1.8428 -0.0849 -0.0863 -0.0414 1043 LEU   B CB  
7981  C  CG  . LEU   B 739 ? 1.3298 1.3449 1.7352 -0.0781 -0.0974 -0.0443 1043 LEU   B CG  
7982  C  CD1 . LEU   B 739 ? 1.2950 1.3191 1.7145 -0.0775 -0.1030 -0.0490 1043 LEU   B CD1 
7983  C  CD2 . LEU   B 739 ? 1.3384 1.3441 1.7401 -0.0762 -0.1060 -0.0469 1043 LEU   B CD2 
7984  N  N   . SER   B 740 ? 1.6278 1.6311 2.0710 -0.0972 -0.0695 -0.0368 1044 SER   B N   
7985  C  CA  . SER   B 740 ? 1.6369 1.6418 2.0992 -0.1037 -0.0592 -0.0351 1044 SER   B CA  
7986  C  C   . SER   B 740 ? 1.6102 1.6270 2.0890 -0.1046 -0.0594 -0.0380 1044 SER   B C   
7987  O  O   . SER   B 740 ? 1.6324 1.6549 2.1129 -0.1010 -0.0696 -0.0425 1044 SER   B O   
7988  C  CB  . SER   B 740 ? 1.6542 1.6524 2.1340 -0.1083 -0.0608 -0.0373 1044 SER   B CB  
7989  O  OG  . SER   B 740 ? 1.7076 1.7106 2.2051 -0.1080 -0.0719 -0.0439 1044 SER   B OG  
7990  N  N   . GLU   B 741 ? 1.6228 1.6428 2.1133 -0.1093 -0.0479 -0.0353 1045 GLU   B N   
7991  C  CA  . GLU   B 741 ? 1.5942 1.6257 2.0970 -0.1096 -0.0464 -0.0370 1045 GLU   B CA  
7992  C  C   . GLU   B 741 ? 1.5901 1.6273 2.1163 -0.1105 -0.0565 -0.0438 1045 GLU   B C   
7993  O  O   . GLU   B 741 ? 1.5655 1.6114 2.0954 -0.1078 -0.0618 -0.0470 1045 GLU   B O   
7994  C  CB  . GLU   B 741 ? 1.5504 1.5833 2.0626 -0.1146 -0.0318 -0.0329 1045 GLU   B CB  
7995  C  CG  . GLU   B 741 ? 1.5493 1.5935 2.0695 -0.1141 -0.0296 -0.0340 1045 GLU   B CG  
7996  C  CD  . GLU   B 741 ? 1.5741 1.6198 2.1056 -0.1189 -0.0153 -0.0304 1045 GLU   B CD  
7997  O  OE1 . GLU   B 741 ? 1.5742 1.6130 2.1138 -0.1235 -0.0081 -0.0281 1045 GLU   B OE1 
7998  O  OE2 . GLU   B 741 ? 1.5723 1.6257 2.1042 -0.1181 -0.0111 -0.0297 1045 GLU   B OE2 
7999  N  N   . SER   B 742 ? 1.7583 1.7905 2.3005 -0.1140 -0.0594 -0.0462 1046 SER   B N   
8000  C  CA  . SER   B 742 ? 1.7471 1.7840 2.3114 -0.1145 -0.0702 -0.0531 1046 SER   B CA  
8001  C  C   . SER   B 742 ? 1.7287 1.7654 2.2792 -0.1079 -0.0846 -0.0572 1046 SER   B C   
8002  O  O   . SER   B 742 ? 1.6751 1.7193 2.2337 -0.1055 -0.0924 -0.0618 1046 SER   B O   
8003  C  CB  . SER   B 742 ? 1.7697 1.8002 2.3532 -0.1198 -0.0704 -0.0547 1046 SER   B CB  
8004  O  OG  . SER   B 742 ? 1.8258 1.8447 2.3919 -0.1191 -0.0699 -0.0518 1046 SER   B OG  
8005  N  N   . TRP   B 743 ? 1.5992 1.6268 2.1280 -0.1045 -0.0881 -0.0556 1047 TRP   B N   
8006  C  CA  . TRP   B 743 ? 1.5630 1.5889 2.0784 -0.0981 -0.1015 -0.0594 1047 TRP   B CA  
8007  C  C   . TRP   B 743 ? 1.5299 1.5641 2.0341 -0.0933 -0.1034 -0.0596 1047 TRP   B C   
8008  O  O   . TRP   B 743 ? 1.4873 1.5246 1.9931 -0.0893 -0.1145 -0.0646 1047 TRP   B O   
8009  C  CB  . TRP   B 743 ? 1.5431 1.5581 2.0359 -0.0954 -0.1027 -0.0566 1047 TRP   B CB  
8010  C  CG  . TRP   B 743 ? 1.5763 1.5824 2.0768 -0.0964 -0.1109 -0.0602 1047 TRP   B CG  
8011  C  CD1 . TRP   B 743 ? 1.5338 1.5406 2.0600 -0.1003 -0.1159 -0.0651 1047 TRP   B CD1 
8012  C  CD2 . TRP   B 743 ? 1.6298 1.6249 2.1123 -0.0934 -0.1153 -0.0593 1047 TRP   B CD2 
8013  N  NE1 . TRP   B 743 ? 1.4562 1.4529 1.9812 -0.1000 -0.1232 -0.0673 1047 TRP   B NE1 
8014  C  CE2 . TRP   B 743 ? 1.5949 1.5842 2.0930 -0.0957 -0.1228 -0.0638 1047 TRP   B CE2 
8015  C  CE3 . TRP   B 743 ? 1.6270 1.6167 2.0822 -0.0889 -0.1136 -0.0552 1047 TRP   B CE3 
8016  C  CZ2 . TRP   B 743 ? 1.6702 1.6481 2.1566 -0.0936 -0.1286 -0.0643 1047 TRP   B CZ2 
8017  C  CZ3 . TRP   B 743 ? 1.6217 1.6006 2.0658 -0.0867 -0.1192 -0.0557 1047 TRP   B CZ3 
8018  C  CH2 . TRP   B 743 ? 1.6372 1.6101 2.0965 -0.0890 -0.1265 -0.0601 1047 TRP   B CH2 
8019  N  N   . TYR   B 744 ? 1.5290 1.5665 2.0219 -0.0935 -0.0928 -0.0543 1048 TYR   B N   
8020  C  CA  . TYR   B 744 ? 1.4219 1.4675 1.9054 -0.0896 -0.0934 -0.0542 1048 TYR   B CA  
8021  C  C   . TYR   B 744 ? 1.4378 1.4927 1.9433 -0.0907 -0.0973 -0.0590 1048 TYR   B C   
8022  O  O   . TYR   B 744 ? 1.4266 1.4850 1.9296 -0.0861 -0.1071 -0.0630 1048 TYR   B O   
8023  C  CB  . TYR   B 744 ? 1.3713 1.4184 1.8427 -0.0908 -0.0805 -0.0477 1048 TYR   B CB  
8024  C  CG  . TYR   B 744 ? 1.2850 1.3400 1.7460 -0.0871 -0.0798 -0.0470 1048 TYR   B CG  
8025  C  CD1 . TYR   B 744 ? 1.2619 1.3157 1.7004 -0.0812 -0.0851 -0.0463 1048 TYR   B CD1 
8026  C  CD2 . TYR   B 744 ? 1.2565 1.3198 1.7301 -0.0897 -0.0735 -0.0467 1048 TYR   B CD2 
8027  C  CE1 . TYR   B 744 ? 1.2111 1.2719 1.6403 -0.0781 -0.0844 -0.0455 1048 TYR   B CE1 
8028  C  CE2 . TYR   B 744 ? 1.2620 1.3320 1.7257 -0.0864 -0.0728 -0.0459 1048 TYR   B CE2 
8029  C  CZ  . TYR   B 744 ? 1.2196 1.2883 1.6612 -0.0807 -0.0783 -0.0454 1048 TYR   B CZ  
8030  O  OH  . TYR   B 744 ? 1.1651 1.2402 1.5972 -0.0776 -0.0777 -0.0446 1048 TYR   B OH  
8031  N  N   . ASN   B 745 ? 1.4553 1.5138 1.9828 -0.0966 -0.0895 -0.0586 1049 ASN   B N   
8032  C  CA  . ASN   B 745 ? 1.4117 1.4793 1.9626 -0.0981 -0.0924 -0.0631 1049 ASN   B CA  
8033  C  C   . ASN   B 745 ? 1.3920 1.4590 1.9520 -0.0954 -0.1075 -0.0701 1049 ASN   B C   
8034  O  O   . ASN   B 745 ? 1.3783 1.4515 1.9410 -0.0920 -0.1148 -0.0739 1049 ASN   B O   
8035  C  CB  . ASN   B 745 ? 1.4083 1.4779 1.9837 -0.1053 -0.0826 -0.0619 1049 ASN   B CB  
8036  C  CG  . ASN   B 745 ? 1.4531 1.5220 2.0198 -0.1080 -0.0673 -0.0551 1049 ASN   B CG  
8037  O  OD1 . ASN   B 745 ? 1.4594 1.5307 2.0078 -0.1048 -0.0636 -0.0520 1049 ASN   B OD1 
8038  N  ND2 . ASN   B 745 ? 1.5060 1.5713 2.0862 -0.1138 -0.0581 -0.0527 1049 ASN   B ND2 
8039  N  N   . LEU   B 746 ? 1.4026 1.4614 1.9669 -0.0968 -0.1126 -0.0718 1050 LEU   B N   
8040  C  CA  . LEU   B 746 ? 1.3979 1.4548 1.9710 -0.0943 -0.1274 -0.0787 1050 LEU   B CA  
8041  C  C   . LEU   B 746 ? 1.4215 1.4773 1.9723 -0.0865 -0.1371 -0.0805 1050 LEU   B C   
8042  O  O   . LEU   B 746 ? 1.4155 1.4755 1.9727 -0.0833 -0.1468 -0.0857 1050 LEU   B O   
8043  C  CB  . LEU   B 746 ? 1.4128 1.4597 1.9898 -0.0967 -0.1308 -0.0797 1050 LEU   B CB  
8044  C  CG  . LEU   B 746 ? 1.4834 1.5290 2.0809 -0.0971 -0.1434 -0.0869 1050 LEU   B CG  
8045  C  CD1 . LEU   B 746 ? 1.4886 1.5243 2.0891 -0.1009 -0.1420 -0.0858 1050 LEU   B CD1 
8046  C  CD2 . LEU   B 746 ? 1.5071 1.5504 2.0925 -0.0897 -0.1589 -0.0922 1050 LEU   B CD2 
8047  N  N   . LEU   B 747 ? 1.3900 1.4399 1.9145 -0.0833 -0.1347 -0.0762 1051 LEU   B N   
8048  C  CA  . LEU   B 747 ? 1.3499 1.3984 1.8525 -0.0759 -0.1428 -0.0774 1051 LEU   B CA  
8049  C  C   . LEU   B 747 ? 1.3894 1.4475 1.8901 -0.0734 -0.1416 -0.0775 1051 LEU   B C   
8050  O  O   . LEU   B 747 ? 1.4100 1.4689 1.9030 -0.0678 -0.1510 -0.0810 1051 LEU   B O   
8051  C  CB  . LEU   B 747 ? 1.2327 1.2742 1.7092 -0.0733 -0.1387 -0.0722 1051 LEU   B CB  
8052  C  CG  . LEU   B 747 ? 1.2436 1.2741 1.7153 -0.0731 -0.1435 -0.0729 1051 LEU   B CG  
8053  C  CD1 . LEU   B 747 ? 1.2836 1.3086 1.7285 -0.0698 -0.1394 -0.0678 1051 LEU   B CD1 
8054  C  CD2 . LEU   B 747 ? 1.2664 1.2935 1.7400 -0.0687 -0.1582 -0.0795 1051 LEU   B CD2 
8055  N  N   . LEU   B 748 ? 1.3915 1.4563 1.8981 -0.0773 -0.1299 -0.0737 1052 LEU   B N   
8056  C  CA  . LEU   B 748 ? 1.3800 1.4538 1.8860 -0.0755 -0.1281 -0.0737 1052 LEU   B CA  
8057  C  C   . LEU   B 748 ? 1.4528 1.5318 1.9774 -0.0743 -0.1379 -0.0804 1052 LEU   B C   
8058  O  O   . LEU   B 748 ? 1.4628 1.5447 1.9790 -0.0692 -0.1444 -0.0827 1052 LEU   B O   
8059  C  CB  . LEU   B 748 ? 1.3708 1.4500 1.8831 -0.0804 -0.1139 -0.0689 1052 LEU   B CB  
8060  C  CG  . LEU   B 748 ? 1.3184 1.3980 1.8067 -0.0780 -0.1065 -0.0632 1052 LEU   B CG  
8061  C  CD1 . LEU   B 748 ? 1.3173 1.3875 1.7861 -0.0767 -0.1059 -0.0599 1052 LEU   B CD1 
8062  C  CD2 . LEU   B 748 ? 1.3104 1.3953 1.8051 -0.0824 -0.0934 -0.0591 1052 LEU   B CD2 
8063  N  N   . ASP   B 749 ? 1.5727 1.6525 2.1227 -0.0790 -0.1392 -0.0836 1053 ASP   B N   
8064  C  CA  . ASP   B 749 ? 1.5827 1.6665 2.1513 -0.0778 -0.1500 -0.0905 1053 ASP   B CA  
8065  C  C   . ASP   B 749 ? 1.5733 1.6504 2.1286 -0.0713 -0.1644 -0.0949 1053 ASP   B C   
8066  O  O   . ASP   B 749 ? 1.5397 1.6198 2.0936 -0.0666 -0.1727 -0.0989 1053 ASP   B O   
8067  C  CB  . ASP   B 749 ? 1.6191 1.7036 2.2171 -0.0841 -0.1493 -0.0931 1053 ASP   B CB  
8068  C  CG  . ASP   B 749 ? 1.6943 1.7884 2.3175 -0.0854 -0.1521 -0.0977 1053 ASP   B CG  
8069  O  OD1 . ASP   B 749 ? 1.7087 1.8089 2.3258 -0.0818 -0.1532 -0.0983 1053 ASP   B OD1 
8070  O  OD2 . ASP   B 749 ? 1.7344 1.8298 2.3838 -0.0902 -0.1531 -0.1006 1053 ASP   B OD2 
8071  N  N   . MET   B 750 ? 1.4404 1.5077 1.9851 -0.0706 -0.1672 -0.0942 1054 MET   B N   
8072  C  CA  . MET   B 750 ? 1.4112 1.4708 1.9412 -0.0642 -0.1801 -0.0980 1054 MET   B CA  
8073  C  C   . MET   B 750 ? 1.3884 1.4491 1.8942 -0.0575 -0.1816 -0.0965 1054 MET   B C   
8074  O  O   . MET   B 750 ? 1.3744 1.4328 1.8740 -0.0518 -0.1927 -0.1010 1054 MET   B O   
8075  C  CB  . MET   B 750 ? 1.4094 1.4584 1.9296 -0.0649 -0.1803 -0.0961 1054 MET   B CB  
8076  C  CG  . MET   B 750 ? 1.4214 1.4658 1.9620 -0.0678 -0.1881 -0.1012 1054 MET   B CG  
8077  S  SD  . MET   B 750 ? 1.5329 1.5751 2.0731 -0.0607 -0.2061 -0.1093 1054 MET   B SD  
8078  C  CE  . MET   B 750 ? 1.5279 1.5799 2.1040 -0.0654 -0.2085 -0.1145 1054 MET   B CE  
8079  N  N   . GLN   B 751 ? 1.3893 1.4530 1.8811 -0.0582 -0.1704 -0.0903 1055 GLN   B N   
8080  C  CA  . GLN   B 751 ? 1.3897 1.4557 1.8610 -0.0527 -0.1705 -0.0885 1055 GLN   B CA  
8081  C  C   . GLN   B 751 ? 1.4487 1.5217 1.9298 -0.0504 -0.1761 -0.0929 1055 GLN   B C   
8082  O  O   . GLN   B 751 ? 1.4587 1.5289 1.9300 -0.0443 -0.1861 -0.0965 1055 GLN   B O   
8083  C  CB  . GLN   B 751 ? 1.3104 1.3804 1.7710 -0.0550 -0.1569 -0.0815 1055 GLN   B CB  
8084  C  CG  . GLN   B 751 ? 1.2280 1.2908 1.6732 -0.0557 -0.1515 -0.0767 1055 GLN   B CG  
8085  C  CD  . GLN   B 751 ? 1.1387 1.2024 1.5602 -0.0525 -0.1457 -0.0716 1055 GLN   B CD  
8086  O  OE1 . GLN   B 751 ? 1.1640 1.2222 1.5663 -0.0473 -0.1503 -0.0711 1055 GLN   B OE1 
8087  N  NE2 . GLN   B 751 ? 1.1302 1.2009 1.5531 -0.0553 -0.1356 -0.0678 1055 GLN   B NE2 
8088  N  N   . ASN   B 752 ? 1.4449 1.5268 1.9453 -0.0551 -0.1696 -0.0927 1056 ASN   B N   
8089  C  CA  . ASN   B 752 ? 1.4362 1.5252 1.9466 -0.0531 -0.1743 -0.0966 1056 ASN   B CA  
8090  C  C   . ASN   B 752 ? 1.4327 1.5179 1.9529 -0.0500 -0.1889 -0.1039 1056 ASN   B C   
8091  O  O   . ASN   B 752 ? 1.4473 1.5323 1.9600 -0.0443 -0.1974 -0.1073 1056 ASN   B O   
8092  C  CB  . ASN   B 752 ? 1.4051 1.5036 1.9378 -0.0592 -0.1652 -0.0956 1056 ASN   B CB  
8093  C  CG  . ASN   B 752 ? 1.4072 1.5076 1.9322 -0.0631 -0.1505 -0.0884 1056 ASN   B CG  
8094  O  OD1 . ASN   B 752 ? 1.4754 1.5731 1.9772 -0.0603 -0.1470 -0.0842 1056 ASN   B OD1 
8095  N  ND2 . ASN   B 752 ? 1.3724 1.4771 1.9172 -0.0694 -0.1418 -0.0870 1056 ASN   B ND2 
8096  N  N   . ARG   B 753 ? 1.4165 1.4980 1.9533 -0.0537 -0.1921 -0.1065 1057 ARG   B N   
8097  C  CA  . ARG   B 753 ? 1.4213 1.4985 1.9683 -0.0510 -0.2066 -0.1137 1057 ARG   B CA  
8098  C  C   . ARG   B 753 ? 1.4496 1.5179 1.9712 -0.0430 -0.2163 -0.1153 1057 ARG   B C   
8099  O  O   . ARG   B 753 ? 1.4605 1.5277 1.9808 -0.0377 -0.2271 -0.1204 1057 ARG   B O   
8100  C  CB  . ARG   B 753 ? 1.3776 1.4507 1.9430 -0.0563 -0.2079 -0.1154 1057 ARG   B CB  
8101  N  N   . LEU   B 754 ? 1.4413 1.5032 1.9414 -0.0417 -0.2121 -0.1107 1058 LEU   B N   
8102  C  CA  . LEU   B 754 ? 1.4251 1.4781 1.9004 -0.0341 -0.2202 -0.1117 1058 LEU   B CA  
8103  C  C   . LEU   B 754 ? 1.4936 1.5503 1.9534 -0.0287 -0.2201 -0.1109 1058 LEU   B C   
8104  O  O   . LEU   B 754 ? 1.4954 1.5460 1.9414 -0.0218 -0.2299 -0.1141 1058 LEU   B O   
8105  C  CB  . LEU   B 754 ? 1.3609 1.4069 1.8184 -0.0343 -0.2147 -0.1068 1058 LEU   B CB  
8106  C  CG  . LEU   B 754 ? 1.3563 1.3953 1.8249 -0.0377 -0.2182 -0.1087 1058 LEU   B CG  
8107  C  CD1 . LEU   B 754 ? 1.3489 1.3804 1.7977 -0.0370 -0.2134 -0.1039 1058 LEU   B CD1 
8108  C  CD2 . LEU   B 754 ? 1.4406 1.4728 1.9138 -0.0335 -0.2335 -0.1160 1058 LEU   B CD2 
8109  N  N   . ASN   B 755 ? 1.7063 1.7722 2.1673 -0.0315 -0.2094 -0.1066 1059 ASN   B N   
8110  C  CA  . ASN   B 755 ? 1.7371 1.8063 2.1833 -0.0266 -0.2090 -0.1056 1059 ASN   B CA  
8111  C  C   . ASN   B 755 ? 1.7233 1.7942 2.1786 -0.0229 -0.2194 -0.1119 1059 ASN   B C   
8112  O  O   . ASN   B 755 ? 1.7175 1.7879 2.1578 -0.0172 -0.2224 -0.1123 1059 ASN   B O   
8113  C  CB  . ASN   B 755 ? 1.7209 1.7994 2.1680 -0.0307 -0.1957 -0.1001 1059 ASN   B CB  
8114  C  CG  . ASN   B 755 ? 1.7123 1.7884 2.1436 -0.0323 -0.1861 -0.0936 1059 ASN   B CG  
8115  O  OD1 . ASN   B 755 ? 1.7149 1.7836 2.1265 -0.0280 -0.1890 -0.0924 1059 ASN   B OD1 
8116  N  ND2 . ASN   B 755 ? 1.7049 1.7869 2.1449 -0.0384 -0.1746 -0.0894 1059 ASN   B ND2 
8117  N  N   . LYS   B 756 ? 1.5577 1.6305 2.0377 -0.0261 -0.2249 -0.1168 1060 LYS   B N   
8118  C  CA  . LYS   B 756 ? 1.4821 1.5560 1.9721 -0.0224 -0.2359 -0.1233 1060 LYS   B CA  
8119  C  C   . LYS   B 756 ? 1.4339 1.4962 1.9099 -0.0153 -0.2496 -0.1279 1060 LYS   B C   
8120  O  O   . LYS   B 756 ? 1.4664 1.5268 1.9345 -0.0091 -0.2575 -0.1313 1060 LYS   B O   
8121  C  CB  . LYS   B 756 ? 1.3357 1.4157 1.8580 -0.0283 -0.2372 -0.1271 1060 LYS   B CB  
8122  N  N   . VAL   B 757 ? 1.4419 1.4957 1.9139 -0.0157 -0.2526 -0.1281 1061 VAL   B N   
8123  C  CA  . VAL   B 757 ? 1.4355 1.4773 1.8956 -0.0090 -0.2661 -0.1329 1061 VAL   B CA  
8124  C  C   . VAL   B 757 ? 1.4344 1.4689 1.8625 -0.0024 -0.2650 -0.1294 1061 VAL   B C   
8125  O  O   . VAL   B 757 ? 1.4298 1.4581 1.8436 0.0051  -0.2738 -0.1326 1061 VAL   B O   
8126  C  CB  . VAL   B 757 ? 1.3961 1.4315 1.8686 -0.0122 -0.2713 -0.1357 1061 VAL   B CB  
8127  C  CG1 . VAL   B 757 ? 1.3733 1.4160 1.8790 -0.0186 -0.2728 -0.1395 1061 VAL   B CG1 
8128  C  CG2 . VAL   B 757 ? 1.3862 1.4190 1.8502 -0.0161 -0.2613 -0.1296 1061 VAL   B CG2 
8129  N  N   . ILE   B 758 ? 1.4151 1.4502 1.8312 -0.0048 -0.2541 -0.1229 1062 ILE   B N   
8130  C  CA  . ILE   B 758 ? 1.3852 1.4133 1.7723 0.0012  -0.2530 -0.1195 1062 ILE   B CA  
8131  C  C   . ILE   B 758 ? 1.4340 1.4676 1.8097 0.0046  -0.2490 -0.1173 1062 ILE   B C   
8132  O  O   . ILE   B 758 ? 1.4620 1.5057 1.8438 0.0001  -0.2388 -0.1134 1062 ILE   B O   
8133  C  CB  . ILE   B 758 ? 1.3608 1.3880 1.7399 -0.0024 -0.2430 -0.1134 1062 ILE   B CB  
8134  C  CG1 . ILE   B 758 ? 1.3172 1.3370 1.7050 -0.0049 -0.2477 -0.1157 1062 ILE   B CG1 
8135  C  CG2 . ILE   B 758 ? 1.3605 1.3828 1.7111 0.0036  -0.2403 -0.1094 1062 ILE   B CG2 
8136  C  CD1 . ILE   B 758 ? 1.2477 1.2738 1.6545 -0.0139 -0.2384 -0.1128 1062 ILE   B CD1 
8137  N  N   . LYS   B 759 ? 1.4445 1.4709 1.8030 0.0126  -0.2571 -0.1199 1063 LYS   B N   
8138  C  CA  . LYS   B 759 ? 1.3875 1.4176 1.7345 0.0165  -0.2548 -0.1185 1063 LYS   B CA  
8139  C  C   . LYS   B 759 ? 1.4215 1.4510 1.7460 0.0183  -0.2456 -0.1119 1063 LYS   B C   
8140  O  O   . LYS   B 759 ? 1.4436 1.4650 1.7536 0.0208  -0.2462 -0.1103 1063 LYS   B O   
8141  C  CB  . LYS   B 759 ? 1.3350 1.3569 1.6737 0.0245  -0.2677 -0.1243 1063 LYS   B CB  
8142  N  N   . SER   B 760 ? 1.3143 1.3526 1.6368 0.0167  -0.2369 -0.1081 1064 SER   B N   
8143  C  CA  . SER   B 760 ? 1.1687 1.2081 1.4724 0.0178  -0.2277 -0.1017 1064 SER   B CA  
8144  C  C   . SER   B 760 ? 1.1432 1.1751 1.4246 0.0263  -0.2325 -0.1023 1064 SER   B C   
8145  O  O   . SER   B 760 ? 1.1761 1.2044 1.4574 0.0309  -0.2412 -0.1071 1064 SER   B O   
8146  C  CB  . SER   B 760 ? 1.1094 1.1607 1.4207 0.0126  -0.2171 -0.0978 1064 SER   B CB  
8147  O  OG  . SER   B 760 ? 1.1930 1.2457 1.4862 0.0143  -0.2092 -0.0922 1064 SER   B OG  
8148  N  N   . VAL   B 761 ? 1.1509 1.1803 1.4132 0.0286  -0.2265 -0.0974 1065 VAL   B N   
8149  C  CA  . VAL   B 761 ? 1.1381 1.1596 1.3785 0.0369  -0.2303 -0.0976 1065 VAL   B CA  
8150  C  C   . VAL   B 761 ? 1.1320 1.1594 1.3679 0.0384  -0.2264 -0.0961 1065 VAL   B C   
8151  O  O   . VAL   B 761 ? 1.1917 1.2128 1.4143 0.0452  -0.2316 -0.0980 1065 VAL   B O   
8152  C  CB  . VAL   B 761 ? 1.1355 1.1514 1.3575 0.0393  -0.2259 -0.0932 1065 VAL   B CB  
8153  C  CG1 . VAL   B 761 ? 1.0845 1.0920 1.2836 0.0481  -0.2289 -0.0931 1065 VAL   B CG1 
8154  C  CG2 . VAL   B 761 ? 1.1066 1.1159 1.3329 0.0381  -0.2303 -0.0950 1065 VAL   B CG2 
8155  N  N   . GLY   B 762 ? 1.1042 1.1427 1.3497 0.0325  -0.2175 -0.0927 1066 GLY   B N   
8156  C  CA  . GLY   B 762 ? 1.1268 1.1707 1.3691 0.0337  -0.2143 -0.0916 1066 GLY   B CA  
8157  C  C   . GLY   B 762 ? 1.0994 1.1510 1.3618 0.0298  -0.2156 -0.0947 1066 GLY   B C   
8158  O  O   . GLY   B 762 ? 1.1329 1.1907 1.3955 0.0294  -0.2116 -0.0934 1066 GLY   B O   
8159  N  N   . LYS   B 763 ? 1.0966 1.1480 1.3765 0.0269  -0.2213 -0.0989 1067 LYS   B N   
8160  C  CA  . LYS   B 763 ? 1.0875 1.1479 1.3906 0.0212  -0.2200 -0.1008 1067 LYS   B CA  
8161  C  C   . LYS   B 763 ? 1.1016 1.1717 1.4103 0.0144  -0.2073 -0.0951 1067 LYS   B C   
8162  O  O   . LYS   B 763 ? 1.1293 1.2076 1.4449 0.0120  -0.2024 -0.0941 1067 LYS   B O   
8163  C  CB  . LYS   B 763 ? 1.1382 1.2005 1.4443 0.0246  -0.2252 -0.1045 1067 LYS   B CB  
8164  N  N   . ILE   B 764 ? 1.1225 1.1911 1.4273 0.0117  -0.2023 -0.0915 1068 ILE   B N   
8165  C  CA  . ILE   B 764 ? 1.0704 1.1462 1.3778 0.0057  -0.1906 -0.0859 1068 ILE   B CA  
8166  C  C   . ILE   B 764 ? 1.1196 1.1981 1.4467 -0.0008 -0.1887 -0.0867 1068 ILE   B C   
8167  O  O   . ILE   B 764 ? 1.1160 1.1882 1.4448 -0.0008 -0.1932 -0.0883 1068 ILE   B O   
8168  C  CB  . ILE   B 764 ? 1.0203 1.0923 1.3078 0.0076  -0.1855 -0.0809 1068 ILE   B CB  
8169  C  CG1 . ILE   B 764 ? 1.0208 1.0884 1.2890 0.0147  -0.1885 -0.0807 1068 ILE   B CG1 
8170  C  CG2 . ILE   B 764 ? 1.0072 1.0870 1.2958 0.0022  -0.1738 -0.0752 1068 ILE   B CG2 
8171  C  CD1 . ILE   B 764 ? 1.0079 1.0726 1.2574 0.0167  -0.1832 -0.0756 1068 ILE   B CD1 
8172  N  N   . GLU   B 765 ? 1.1745 1.2619 1.5161 -0.0064 -0.1817 -0.0853 1069 GLU   B N   
8173  C  CA  . GLU   B 765 ? 1.1781 1.2683 1.5398 -0.0127 -0.1792 -0.0859 1069 GLU   B CA  
8174  C  C   . GLU   B 765 ? 1.1784 1.2666 1.5342 -0.0161 -0.1718 -0.0811 1069 GLU   B C   
8175  O  O   . GLU   B 765 ? 1.1739 1.2647 1.5186 -0.0170 -0.1634 -0.0759 1069 GLU   B O   
8176  C  CB  . GLU   B 765 ? 1.1707 1.2707 1.5490 -0.0172 -0.1733 -0.0858 1069 GLU   B CB  
8177  C  CG  . GLU   B 765 ? 1.2421 1.3457 1.6391 -0.0243 -0.1671 -0.0847 1069 GLU   B CG  
8178  C  CD  . GLU   B 765 ? 1.3062 1.4064 1.7202 -0.0255 -0.1752 -0.0898 1069 GLU   B CD  
8179  O  OE1 . GLU   B 765 ? 1.4253 1.5285 1.8542 -0.0248 -0.1814 -0.0948 1069 GLU   B OE1 
8180  O  OE2 . GLU   B 765 ? 1.3183 1.4127 1.7311 -0.0269 -0.1756 -0.0891 1069 GLU   B OE2 
8181  N  N   . HIS   B 766 ? 1.1265 1.2096 1.4898 -0.0179 -0.1751 -0.0827 1070 HIS   B N   
8182  C  CA  . HIS   B 766 ? 1.1566 1.2369 1.5149 -0.0211 -0.1686 -0.0784 1070 HIS   B CA  
8183  C  C   . HIS   B 766 ? 1.1765 1.2639 1.5386 -0.0265 -0.1564 -0.0734 1070 HIS   B C   
8184  O  O   . HIS   B 766 ? 1.1732 1.2594 1.5220 -0.0270 -0.1499 -0.0684 1070 HIS   B O   
8185  C  CB  . HIS   B 766 ? 1.2254 1.3007 1.5971 -0.0237 -0.1731 -0.0814 1070 HIS   B CB  
8186  C  CG  . HIS   B 766 ? 1.2418 1.3153 1.6137 -0.0285 -0.1653 -0.0771 1070 HIS   B CG  
8187  N  ND1 . HIS   B 766 ? 1.2678 1.3471 1.6525 -0.0349 -0.1556 -0.0742 1070 HIS   B ND1 
8188  C  CD2 . HIS   B 766 ? 1.2221 1.2877 1.5834 -0.0275 -0.1660 -0.0754 1070 HIS   B CD2 
8189  C  CE1 . HIS   B 766 ? 1.2381 1.3130 1.6191 -0.0377 -0.1507 -0.0708 1070 HIS   B CE1 
8190  N  NE2 . HIS   B 766 ? 1.2067 1.2736 1.5739 -0.0333 -0.1570 -0.0716 1070 HIS   B NE2 
8191  N  N   . SER   B 767 ? 1.1316 1.2262 1.5113 -0.0304 -0.1533 -0.0746 1071 SER   B N   
8192  C  CA  . SER   B 767 ? 1.0972 1.1975 1.4807 -0.0356 -0.1415 -0.0698 1071 SER   B CA  
8193  C  C   . SER   B 767 ? 1.0462 1.1494 1.4123 -0.0334 -0.1361 -0.0657 1071 SER   B C   
8194  O  O   . SER   B 767 ? 1.0143 1.1186 1.3741 -0.0361 -0.1271 -0.0608 1071 SER   B O   
8195  C  CB  . SER   B 767 ? 1.1190 1.2261 1.5254 -0.0399 -0.1392 -0.0721 1071 SER   B CB  
8196  O  OG  . SER   B 767 ? 1.2324 1.3448 1.6395 -0.0372 -0.1414 -0.0741 1071 SER   B OG  
8197  N  N   . PHE   B 768 ? 1.0505 1.1544 1.4079 -0.0283 -0.1415 -0.0676 1072 PHE   B N   
8198  C  CA  . PHE   B 768 ? 1.0061 1.1121 1.3465 -0.0260 -0.1369 -0.0638 1072 PHE   B CA  
8199  C  C   . PHE   B 768 ? 0.9623 1.0625 1.2844 -0.0238 -0.1359 -0.0603 1072 PHE   B C   
8200  O  O   . PHE   B 768 ? 0.9737 1.0757 1.2863 -0.0251 -0.1283 -0.0555 1072 PHE   B O   
8201  C  CB  . PHE   B 768 ? 1.0312 1.1384 1.3669 -0.0210 -0.1432 -0.0668 1072 PHE   B CB  
8202  C  CG  . PHE   B 768 ? 0.9560 1.0655 1.2756 -0.0187 -0.1387 -0.0632 1072 PHE   B CG  
8203  C  CD1 . PHE   B 768 ? 0.9623 1.0758 1.2787 -0.0223 -0.1290 -0.0583 1072 PHE   B CD1 
8204  C  CD2 . PHE   B 768 ? 0.9674 1.0747 1.2750 -0.0129 -0.1443 -0.0646 1072 PHE   B CD2 
8205  C  CE1 . PHE   B 768 ? 0.9779 1.0935 1.2803 -0.0204 -0.1253 -0.0551 1072 PHE   B CE1 
8206  C  CE2 . PHE   B 768 ? 0.9562 1.0657 1.2501 -0.0111 -0.1400 -0.0613 1072 PHE   B CE2 
8207  C  CZ  . PHE   B 768 ? 0.9715 1.0853 1.2632 -0.0150 -0.1307 -0.0565 1072 PHE   B CZ  
8208  N  N   . TRP   B 769 ? 0.9804 1.0736 1.2972 -0.0201 -0.1437 -0.0628 1073 TRP   B N   
8209  C  CA  . TRP   B 769 ? 0.9852 1.0724 1.2853 -0.0177 -0.1431 -0.0597 1073 TRP   B CA  
8210  C  C   . TRP   B 769 ? 1.0090 1.0968 1.3098 -0.0226 -0.1345 -0.0552 1073 TRP   B C   
8211  O  O   . TRP   B 769 ? 0.9958 1.0837 1.2829 -0.0219 -0.1293 -0.0508 1073 TRP   B O   
8212  C  CB  . TRP   B 769 ? 0.9855 1.0645 1.2842 -0.0142 -0.1524 -0.0635 1073 TRP   B CB  
8213  C  CG  . TRP   B 769 ? 0.9781 1.0501 1.2613 -0.0117 -0.1525 -0.0609 1073 TRP   B CG  
8214  C  CD1 . TRP   B 769 ? 0.9771 1.0420 1.2619 -0.0117 -0.1566 -0.0624 1073 TRP   B CD1 
8215  C  CD2 . TRP   B 769 ? 0.9665 1.0378 1.2310 -0.0086 -0.1486 -0.0566 1073 TRP   B CD2 
8216  N  NE1 . TRP   B 769 ? 0.9709 1.0308 1.2390 -0.0087 -0.1553 -0.0593 1073 TRP   B NE1 
8217  C  CE2 . TRP   B 769 ? 0.9545 1.0185 1.2105 -0.0068 -0.1505 -0.0557 1073 TRP   B CE2 
8218  C  CE3 . TRP   B 769 ? 0.9855 1.0619 1.2406 -0.0074 -0.1437 -0.0535 1073 TRP   B CE3 
8219  C  CZ2 . TRP   B 769 ? 0.9391 1.0009 1.1779 -0.0037 -0.1476 -0.0518 1073 TRP   B CZ2 
8220  C  CZ3 . TRP   B 769 ? 0.9784 1.0526 1.2169 -0.0045 -0.1410 -0.0497 1073 TRP   B CZ3 
8221  C  CH2 . TRP   B 769 ? 0.9393 1.0065 1.1700 -0.0026 -0.1429 -0.0489 1073 TRP   B CH2 
8222  N  N   . ARG   B 770 ? 1.0312 1.1192 1.3482 -0.0275 -0.1327 -0.0563 1074 ARG   B N   
8223  C  CA  . ARG   B 770 ? 0.9922 1.0784 1.3099 -0.0319 -0.1255 -0.0525 1074 ARG   B CA  
8224  C  C   . ARG   B 770 ? 1.0016 1.0938 1.3213 -0.0360 -0.1153 -0.0485 1074 ARG   B C   
8225  O  O   . ARG   B 770 ? 0.9857 1.0759 1.2995 -0.0382 -0.1088 -0.0443 1074 ARG   B O   
8226  C  CB  . ARG   B 770 ? 0.9769 1.0600 1.3112 -0.0354 -0.1279 -0.0553 1074 ARG   B CB  
8227  C  CG  . ARG   B 770 ? 1.0184 1.0935 1.3487 -0.0319 -0.1370 -0.0583 1074 ARG   B CG  
8228  C  CD  . ARG   B 770 ? 0.9737 1.0437 1.2833 -0.0283 -0.1362 -0.0549 1074 ARG   B CD  
8229  N  NE  . ARG   B 770 ? 0.9407 1.0022 1.2451 -0.0248 -0.1443 -0.0575 1074 ARG   B NE  
8230  C  CZ  . ARG   B 770 ? 0.9863 1.0425 1.2729 -0.0205 -0.1456 -0.0555 1074 ARG   B CZ  
8231  N  NH1 . ARG   B 770 ? 0.9745 1.0331 1.2475 -0.0194 -0.1395 -0.0509 1074 ARG   B NH1 
8232  N  NH2 . ARG   B 770 ? 1.0526 1.1007 1.3350 -0.0170 -0.1534 -0.0583 1074 ARG   B NH2 
8233  N  N   . SER   B 771 ? 1.0897 1.1886 1.4173 -0.0368 -0.1140 -0.0497 1075 SER   B N   
8234  C  CA  . SER   B 771 ? 1.1053 1.2094 1.4344 -0.0404 -0.1044 -0.0461 1075 SER   B CA  
8235  C  C   . SER   B 771 ? 1.1153 1.2186 1.4255 -0.0388 -0.0997 -0.0412 1075 SER   B C   
8236  O  O   . SER   B 771 ? 1.1570 1.2594 1.4539 -0.0343 -0.1037 -0.0411 1075 SER   B O   
8237  C  CB  . SER   B 771 ? 1.1350 1.2460 1.4722 -0.0401 -0.1050 -0.0485 1075 SER   B CB  
8238  O  OG  . SER   B 771 ? 1.1875 1.3002 1.5447 -0.0423 -0.1081 -0.0526 1075 SER   B OG  
8239  N  N   . PHE   B 772 ? 1.0301 1.1334 1.3394 -0.0426 -0.0911 -0.0372 1076 PHE   B N   
8240  C  CA  . PHE   B 772 ? 1.0409 1.1428 1.3336 -0.0417 -0.0863 -0.0325 1076 PHE   B CA  
8241  C  C   . PHE   B 772 ? 1.0356 1.1424 1.3188 -0.0390 -0.0859 -0.0315 1076 PHE   B C   
8242  O  O   . PHE   B 772 ? 1.0589 1.1700 1.3446 -0.0412 -0.0803 -0.0301 1076 PHE   B O   
8243  C  CB  . PHE   B 772 ? 1.0704 1.1715 1.3664 -0.0465 -0.0770 -0.0290 1076 PHE   B CB  
8244  C  CG  . PHE   B 772 ? 1.0973 1.1957 1.3770 -0.0459 -0.0723 -0.0242 1076 PHE   B CG  
8245  C  CD1 . PHE   B 772 ? 1.0882 1.1905 1.3586 -0.0449 -0.0690 -0.0218 1076 PHE   B CD1 
8246  C  CD2 . PHE   B 772 ? 1.0993 1.1912 1.3732 -0.0462 -0.0715 -0.0222 1076 PHE   B CD2 
8247  C  CE1 . PHE   B 772 ? 1.1085 1.2083 1.3646 -0.0442 -0.0654 -0.0177 1076 PHE   B CE1 
8248  C  CE2 . PHE   B 772 ? 1.0766 1.1660 1.3359 -0.0454 -0.0676 -0.0180 1076 PHE   B CE2 
8249  C  CZ  . PHE   B 772 ? 1.1023 1.1957 1.3528 -0.0444 -0.0647 -0.0158 1076 PHE   B CZ  
8250  N  N   . HIS   B 773 ? 1.0450 1.1507 1.3166 -0.0342 -0.0915 -0.0321 1077 HIS   B N   
8251  C  CA  . HIS   B 773 ? 1.1256 1.2357 1.3892 -0.0315 -0.0917 -0.0315 1077 HIS   B CA  
8252  C  C   . HIS   B 773 ? 1.1993 1.3089 1.4477 -0.0307 -0.0875 -0.0269 1077 HIS   B C   
8253  O  O   . HIS   B 773 ? 1.1856 1.2909 1.4248 -0.0287 -0.0890 -0.0254 1077 HIS   B O   
8254  C  CB  . HIS   B 773 ? 1.1601 1.2694 1.4202 -0.0265 -0.1000 -0.0349 1077 HIS   B CB  
8255  C  CG  . HIS   B 773 ? 1.2247 1.3376 1.4753 -0.0236 -0.0998 -0.0339 1077 HIS   B CG  
8256  N  ND1 . HIS   B 773 ? 1.2899 1.4084 1.5441 -0.0256 -0.0956 -0.0333 1077 HIS   B ND1 
8257  C  CD2 . HIS   B 773 ? 1.2052 1.3166 1.4428 -0.0190 -0.1030 -0.0333 1077 HIS   B CD2 
8258  C  CE1 . HIS   B 773 ? 1.3264 1.4467 1.5704 -0.0224 -0.0965 -0.0325 1077 HIS   B CE1 
8259  N  NE2 . HIS   B 773 ? 1.2826 1.3987 1.5166 -0.0184 -0.1007 -0.0324 1077 HIS   B NE2 
8260  N  N   . THR   B 774 ? 1.3125 1.4266 1.5589 -0.0321 -0.0824 -0.0249 1078 THR   B N   
8261  C  CA  . THR   B 774 ? 1.3448 1.4597 1.5776 -0.0309 -0.0792 -0.0211 1078 THR   B CA  
8262  C  C   . THR   B 774 ? 1.4694 1.5895 1.7008 -0.0295 -0.0797 -0.0218 1078 THR   B C   
8263  O  O   . THR   B 774 ? 1.4721 1.5955 1.7135 -0.0312 -0.0790 -0.0239 1078 THR   B O   
8264  C  CB  . THR   B 774 ? 1.3378 1.4518 1.5692 -0.0347 -0.0717 -0.0175 1078 THR   B CB  
8265  O  OG1 . THR   B 774 ? 1.2570 1.3653 1.4882 -0.0357 -0.0713 -0.0166 1078 THR   B OG1 
8266  C  CG2 . THR   B 774 ? 1.4093 1.5248 1.6278 -0.0336 -0.0688 -0.0140 1078 THR   B CG2 
8267  N  N   . GLU   B 775 ? 1.6632 1.7839 1.8827 -0.0263 -0.0810 -0.0203 1079 GLU   B N   
8268  C  CA  . GLU   B 775 ? 1.6923 1.8173 1.9088 -0.0248 -0.0812 -0.0205 1079 GLU   B CA  
8269  C  C   . GLU   B 775 ? 1.6889 1.8177 1.9119 -0.0285 -0.0759 -0.0200 1079 GLU   B C   
8270  O  O   . GLU   B 775 ? 1.7058 1.8379 1.9347 -0.0284 -0.0768 -0.0223 1079 GLU   B O   
8271  C  CB  . GLU   B 775 ? 1.7118 1.8372 1.9150 -0.0223 -0.0806 -0.0175 1079 GLU   B CB  
8272  C  CG  . GLU   B 775 ? 1.7382 1.8593 1.9342 -0.0192 -0.0839 -0.0169 1079 GLU   B CG  
8273  C  CD  . GLU   B 775 ? 1.7378 1.8559 1.9309 -0.0212 -0.0806 -0.0140 1079 GLU   B CD  
8274  O  OE1 . GLU   B 775 ? 1.6937 1.8124 1.8909 -0.0250 -0.0759 -0.0128 1079 GLU   B OE1 
8275  O  OE2 . GLU   B 775 ? 1.7205 1.8353 1.9068 -0.0186 -0.0827 -0.0130 1079 GLU   B OE2 
8276  N  N   . ARG   B 776 ? 1.5775 1.7051 1.7993 -0.0317 -0.0703 -0.0171 1080 ARG   B N   
8277  C  CA  . ARG   B 776 ? 1.5354 1.6653 1.7621 -0.0351 -0.0645 -0.0163 1080 ARG   B CA  
8278  C  C   . ARG   B 776 ? 1.5600 1.6914 1.8019 -0.0371 -0.0647 -0.0196 1080 ARG   B C   
8279  O  O   . ARG   B 776 ? 1.5562 1.6915 1.8033 -0.0372 -0.0647 -0.0213 1080 ARG   B O   
8280  C  CB  . ARG   B 776 ? 1.5199 1.6465 1.7417 -0.0377 -0.0588 -0.0127 1080 ARG   B CB  
8281  N  N   . LYS   B 777 ? 1.6308 1.7590 1.8803 -0.0387 -0.0650 -0.0205 1081 LYS   B N   
8282  C  CA  . LYS   B 777 ? 1.5823 1.7119 1.8479 -0.0411 -0.0647 -0.0235 1081 LYS   B CA  
8283  C  C   . LYS   B 777 ? 1.5139 1.6399 1.7858 -0.0406 -0.0697 -0.0258 1081 LYS   B C   
8284  O  O   . LYS   B 777 ? 1.5541 1.6756 1.8189 -0.0401 -0.0701 -0.0240 1081 LYS   B O   
8285  C  CB  . LYS   B 777 ? 1.5506 1.6800 1.8216 -0.0454 -0.0564 -0.0213 1081 LYS   B CB  
8286  N  N   . THR   B 778 ? 1.3180 1.4460 1.6035 -0.0407 -0.0737 -0.0300 1082 THR   B N   
8287  C  CA  . THR   B 778 ? 1.2593 1.3840 1.5533 -0.0405 -0.0789 -0.0329 1082 THR   B CA  
8288  C  C   . THR   B 778 ? 1.1841 1.3101 1.4963 -0.0449 -0.0756 -0.0344 1082 THR   B C   
8289  O  O   . THR   B 778 ? 1.1610 1.2917 1.4830 -0.0460 -0.0740 -0.0361 1082 THR   B O   
8290  C  CB  . THR   B 778 ? 1.2476 1.3725 1.5410 -0.0360 -0.0881 -0.0369 1082 THR   B CB  
8291  O  OG1 . THR   B 778 ? 1.1860 1.3073 1.4877 -0.0356 -0.0939 -0.0401 1082 THR   B OG1 
8292  C  CG2 . THR   B 778 ? 1.2399 1.3703 1.5403 -0.0354 -0.0892 -0.0394 1082 THR   B CG2 
8293  N  N   . GLU   B 779 ? 1.1534 1.2748 1.4699 -0.0473 -0.0740 -0.0337 1083 GLU   B N   
8294  C  CA  . GLU   B 779 ? 1.1063 1.2274 1.4396 -0.0518 -0.0702 -0.0346 1083 GLU   B CA  
8295  C  C   . GLU   B 779 ? 1.1108 1.2281 1.4528 -0.0516 -0.0768 -0.0378 1083 GLU   B C   
8296  O  O   . GLU   B 779 ? 1.1283 1.2413 1.4599 -0.0485 -0.0823 -0.0380 1083 GLU   B O   
8297  C  CB  . GLU   B 779 ? 1.0934 1.2113 1.4223 -0.0553 -0.0607 -0.0298 1083 GLU   B CB  
8298  N  N   . PRO   B 780 ? 1.0623 1.1808 1.4236 -0.0549 -0.0763 -0.0404 1084 PRO   B N   
8299  C  CA  . PRO   B 780 ? 1.0150 1.1301 1.3862 -0.0548 -0.0834 -0.0440 1084 PRO   B CA  
8300  C  C   . PRO   B 780 ? 1.0381 1.1463 1.4068 -0.0572 -0.0804 -0.0415 1084 PRO   B C   
8301  O  O   . PRO   B 780 ? 0.9836 1.0903 1.3497 -0.0603 -0.0714 -0.0374 1084 PRO   B O   
8302  C  CB  . PRO   B 780 ? 0.9939 1.1137 1.3881 -0.0578 -0.0834 -0.0476 1084 PRO   B CB  
8303  C  CG  . PRO   B 780 ? 1.0582 1.1844 1.4530 -0.0583 -0.0778 -0.0464 1084 PRO   B CG  
8304  C  CD  . PRO   B 780 ? 1.0783 1.2026 1.4545 -0.0581 -0.0708 -0.0410 1084 PRO   B CD  
8305  N  N   . ALA   B 781 ? 1.0626 1.1660 1.4318 -0.0555 -0.0881 -0.0442 1085 ALA   B N   
8306  C  CA  . ALA   B 781 ? 0.9638 1.0598 1.3266 -0.0564 -0.0868 -0.0419 1085 ALA   B CA  
8307  C  C   . ALA   B 781 ? 0.9967 1.0910 1.3766 -0.0620 -0.0817 -0.0418 1085 ALA   B C   
8308  O  O   . ALA   B 781 ? 1.0354 1.1342 1.4340 -0.0647 -0.0812 -0.0445 1085 ALA   B O   
8309  C  CB  . ALA   B 781 ? 0.8735 0.9645 1.2299 -0.0522 -0.0971 -0.0448 1085 ALA   B CB  
8310  N  N   . THR   B 782 ? 1.0227 1.1103 1.3962 -0.0637 -0.0776 -0.0386 1086 THR   B N   
8311  C  CA  . THR   B 782 ? 0.9865 1.0713 1.3737 -0.0691 -0.0711 -0.0375 1086 THR   B CA  
8312  C  C   . THR   B 782 ? 1.0165 1.0923 1.3934 -0.0694 -0.0700 -0.0348 1086 THR   B C   
8313  O  O   . THR   B 782 ? 1.0651 1.1378 1.4225 -0.0661 -0.0704 -0.0321 1086 THR   B O   
8314  C  CB  . THR   B 782 ? 0.9863 1.0745 1.3760 -0.0725 -0.0597 -0.0338 1086 THR   B CB  
8315  O  OG1 . THR   B 782 ? 1.0570 1.1406 1.4565 -0.0774 -0.0525 -0.0319 1086 THR   B OG1 
8316  C  CG2 . THR   B 782 ? 0.9773 1.0643 1.3447 -0.0701 -0.0553 -0.0292 1086 THR   B CG2 
8317  N  N   . GLY   B 783 ? 1.0458 1.1175 1.4363 -0.0734 -0.0684 -0.0355 1087 GLY   B N   
8318  C  CA  . GLY   B 783 ? 1.0992 1.1618 1.4807 -0.0741 -0.0662 -0.0327 1087 GLY   B CA  
8319  C  C   . GLY   B 783 ? 1.0956 1.1532 1.4676 -0.0699 -0.0763 -0.0349 1087 GLY   B C   
8320  O  O   . GLY   B 783 ? 1.1480 1.1976 1.5130 -0.0702 -0.0758 -0.0331 1087 GLY   B O   
8321  N  N   . PHE   B 784 ? 1.0548 1.1163 1.4257 -0.0658 -0.0853 -0.0387 1088 PHE   B N   
8322  C  CA  . PHE   B 784 ? 1.0643 1.1210 1.4248 -0.0610 -0.0951 -0.0410 1088 PHE   B CA  
8323  C  C   . PHE   B 784 ? 1.1258 1.1839 1.5011 -0.0602 -0.1049 -0.0472 1088 PHE   B C   
8324  O  O   . PHE   B 784 ? 1.1636 1.2288 1.5498 -0.0604 -0.1064 -0.0499 1088 PHE   B O   
8325  C  CB  . PHE   B 784 ? 1.0009 1.0597 1.3413 -0.0556 -0.0970 -0.0393 1088 PHE   B CB  
8326  C  CG  . PHE   B 784 ? 1.0265 1.0815 1.3495 -0.0550 -0.0906 -0.0339 1088 PHE   B CG  
8327  C  CD1 . PHE   B 784 ? 1.0325 1.0799 1.3429 -0.0523 -0.0939 -0.0329 1088 PHE   B CD1 
8328  C  CD2 . PHE   B 784 ? 1.0511 1.1097 1.3704 -0.0571 -0.0814 -0.0298 1088 PHE   B CD2 
8329  C  CE1 . PHE   B 784 ? 1.0398 1.0837 1.3346 -0.0516 -0.0884 -0.0281 1088 PHE   B CE1 
8330  C  CE2 . PHE   B 784 ? 1.0306 1.0853 1.3337 -0.0564 -0.0760 -0.0250 1088 PHE   B CE2 
8331  C  CZ  . PHE   B 784 ? 1.0603 1.1079 1.3515 -0.0536 -0.0796 -0.0241 1088 PHE   B CZ  
8332  N  N   . ILE   B 785 ? 1.1294 1.1801 1.5043 -0.0589 -0.1118 -0.0495 1089 ILE   B N   
8333  C  CA  . ILE   B 785 ? 1.1513 1.2011 1.5368 -0.0571 -0.1228 -0.0557 1089 ILE   B CA  
8334  C  C   . ILE   B 785 ? 1.1313 1.1761 1.4980 -0.0503 -0.1313 -0.0568 1089 ILE   B C   
8335  O  O   . ILE   B 785 ? 1.1220 1.1600 1.4747 -0.0488 -0.1305 -0.0542 1089 ILE   B O   
8336  C  CB  . ILE   B 785 ? 1.1219 1.1666 1.5245 -0.0615 -0.1244 -0.0579 1089 ILE   B CB  
8337  C  CG1 . ILE   B 785 ? 1.1630 1.2126 1.5831 -0.0681 -0.1145 -0.0561 1089 ILE   B CG1 
8338  C  CG2 . ILE   B 785 ? 1.0993 1.1432 1.5132 -0.0594 -0.1365 -0.0646 1089 ILE   B CG2 
8339  C  CD1 . ILE   B 785 ? 1.2583 1.3038 1.6964 -0.0729 -0.1146 -0.0578 1089 ILE   B CD1 
8340  N  N   . ASP   B 786 ? 1.1103 1.1582 1.4765 -0.0461 -0.1390 -0.0607 1090 ASP   B N   
8341  C  CA  . ASP   B 786 ? 1.1008 1.1438 1.4494 -0.0393 -0.1470 -0.0621 1090 ASP   B CA  
8342  C  C   . ASP   B 786 ? 1.1239 1.1583 1.4766 -0.0381 -0.1561 -0.0662 1090 ASP   B C   
8343  O  O   . ASP   B 786 ? 1.1693 1.2037 1.5346 -0.0377 -0.1641 -0.0716 1090 ASP   B O   
8344  C  CB  . ASP   B 786 ? 1.0830 1.1315 1.4295 -0.0352 -0.1519 -0.0648 1090 ASP   B CB  
8345  C  CG  . ASP   B 786 ? 1.0951 1.1387 1.4215 -0.0278 -0.1584 -0.0654 1090 ASP   B CG  
8346  O  OD1 . ASP   B 786 ? 1.0639 1.0999 1.3783 -0.0256 -0.1597 -0.0640 1090 ASP   B OD1 
8347  O  OD2 . ASP   B 786 ? 1.1013 1.1484 1.4237 -0.0241 -0.1619 -0.0671 1090 ASP   B OD2 
8348  N  N   . GLY   B 787 ? 1.1183 1.1449 1.4603 -0.0376 -0.1550 -0.0638 1091 GLY   B N   
8349  C  CA  . GLY   B 787 ? 1.1472 1.1647 1.4917 -0.0363 -0.1636 -0.0676 1091 GLY   B CA  
8350  C  C   . GLY   B 787 ? 1.1618 1.1758 1.4981 -0.0295 -0.1749 -0.0722 1091 GLY   B C   
8351  O  O   . GLY   B 787 ? 1.1983 1.2076 1.5439 -0.0288 -0.1840 -0.0774 1091 GLY   B O   
8352  N  N   . ASP   B 788 ? 1.2008 1.2167 1.5194 -0.0242 -0.1746 -0.0703 1092 ASP   B N   
8353  C  CA  . ASP   B 788 ? 1.2581 1.2696 1.5664 -0.0170 -0.1847 -0.0742 1092 ASP   B CA  
8354  C  C   . ASP   B 788 ? 1.2543 1.2684 1.5786 -0.0172 -0.1923 -0.0801 1092 ASP   B C   
8355  O  O   . ASP   B 788 ? 1.2714 1.2788 1.5941 -0.0129 -0.2029 -0.0850 1092 ASP   B O   
8356  C  CB  . ASP   B 788 ? 1.2545 1.2690 1.5436 -0.0121 -0.1814 -0.0709 1092 ASP   B CB  
8357  C  CG  . ASP   B 788 ? 1.2402 1.2519 1.5136 -0.0114 -0.1749 -0.0654 1092 ASP   B CG  
8358  O  OD1 . ASP   B 788 ? 1.2490 1.2516 1.5146 -0.0090 -0.1787 -0.0659 1092 ASP   B OD1 
8359  O  OD2 . ASP   B 788 ? 1.1726 1.1910 1.4419 -0.0132 -0.1661 -0.0608 1092 ASP   B OD2 
8360  N  N   . LEU   B 789 ? 1.2434 1.2671 1.5833 -0.0220 -0.1873 -0.0798 1093 LEU   B N   
8361  C  CA  . LEU   B 789 ? 1.1734 1.2005 1.5321 -0.0231 -0.1938 -0.0854 1093 LEU   B CA  
8362  C  C   . LEU   B 789 ? 1.1867 1.2095 1.5637 -0.0274 -0.1979 -0.0888 1093 LEU   B C   
8363  O  O   . LEU   B 789 ? 1.2291 1.2468 1.6119 -0.0249 -0.2089 -0.0945 1093 LEU   B O   
8364  C  CB  . LEU   B 789 ? 1.1519 1.1904 1.5219 -0.0271 -0.1860 -0.0836 1093 LEU   B CB  
8365  C  CG  . LEU   B 789 ? 1.2175 1.2612 1.6104 -0.0296 -0.1906 -0.0886 1093 LEU   B CG  
8366  C  CD1 . LEU   B 789 ? 1.3223 1.3644 1.7089 -0.0229 -0.2012 -0.0933 1093 LEU   B CD1 
8367  C  CD2 . LEU   B 789 ? 1.3015 1.3560 1.7063 -0.0348 -0.1804 -0.0857 1093 LEU   B CD2 
8368  N  N   . ILE   B 790 ? 1.2095 1.2338 1.5955 -0.0338 -0.1891 -0.0852 1094 ILE   B N   
8369  C  CA  . ILE   B 790 ? 1.1924 1.2122 1.5954 -0.0385 -0.1914 -0.0876 1094 ILE   B CA  
8370  C  C   . ILE   B 790 ? 1.2199 1.2279 1.6136 -0.0340 -0.2019 -0.0910 1094 ILE   B C   
8371  O  O   . ILE   B 790 ? 1.2625 1.2663 1.6711 -0.0356 -0.2096 -0.0959 1094 ILE   B O   
8372  C  CB  . ILE   B 790 ? 1.1557 1.1767 1.5620 -0.0448 -0.1789 -0.0819 1094 ILE   B CB  
8373  C  CG1 . ILE   B 790 ? 1.1402 1.1722 1.5609 -0.0499 -0.1697 -0.0798 1094 ILE   B CG1 
8374  C  CG2 . ILE   B 790 ? 1.1821 1.1959 1.6003 -0.0489 -0.1808 -0.0834 1094 ILE   B CG2 
8375  C  CD1 . ILE   B 790 ? 1.1909 1.2278 1.6375 -0.0531 -0.1741 -0.0850 1094 ILE   B CD1 
8376  N  N   . GLU   B 791 ? 1.1849 1.1871 1.5542 -0.0282 -0.2028 -0.0887 1095 GLU   B N   
8377  C  CA  . GLU   B 791 ? 1.2015 1.1918 1.5607 -0.0238 -0.2120 -0.0915 1095 GLU   B CA  
8378  C  C   . GLU   B 791 ? 1.2537 1.2402 1.6109 -0.0177 -0.2249 -0.0978 1095 GLU   B C   
8379  O  O   . GLU   B 791 ? 1.3013 1.2779 1.6567 -0.0150 -0.2343 -0.1017 1095 GLU   B O   
8380  C  CB  . GLU   B 791 ? 1.2492 1.2341 1.5833 -0.0197 -0.2080 -0.0867 1095 GLU   B CB  
8381  C  CG  . GLU   B 791 ? 1.2580 1.2429 1.5919 -0.0249 -0.1973 -0.0811 1095 GLU   B CG  
8382  C  CD  . GLU   B 791 ? 1.3287 1.3056 1.6401 -0.0206 -0.1962 -0.0777 1095 GLU   B CD  
8383  O  OE1 . GLU   B 791 ? 1.3684 1.3426 1.6619 -0.0135 -0.2003 -0.0780 1095 GLU   B OE1 
8384  O  OE2 . GLU   B 791 ? 1.3465 1.3196 1.6584 -0.0242 -0.1909 -0.0746 1095 GLU   B OE2 
8385  N  N   . SER   B 792 ? 1.2753 1.2688 1.6322 -0.0153 -0.2257 -0.0988 1096 SER   B N   
8386  C  CA  . SER   B 792 ? 1.2861 1.2754 1.6390 -0.0089 -0.2378 -0.1046 1096 SER   B CA  
8387  C  C   . SER   B 792 ? 1.3628 1.3515 1.7388 -0.0115 -0.2469 -0.1111 1096 SER   B C   
8388  O  O   . SER   B 792 ? 1.4206 1.4038 1.7938 -0.0061 -0.2585 -0.1166 1096 SER   B O   
8389  C  CB  . SER   B 792 ? 1.2960 1.2929 1.6420 -0.0057 -0.2356 -0.1036 1096 SER   B CB  
8390  O  OG  . SER   B 792 ? 1.3382 1.3449 1.7060 -0.0104 -0.2341 -0.1055 1096 SER   B OG  
8391  N  N   . PHE   B 793 ? 1.4901 1.4843 1.8888 -0.0195 -0.2418 -0.1107 1097 PHE   B N   
8392  C  CA  . PHE   B 793 ? 1.5106 1.5036 1.9331 -0.0226 -0.2503 -0.1168 1097 PHE   B CA  
8393  C  C   . PHE   B 793 ? 1.5461 1.5256 1.9627 -0.0192 -0.2614 -0.1209 1097 PHE   B C   
8394  O  O   . PHE   B 793 ? 1.5877 1.5637 2.0172 -0.0183 -0.2729 -0.1275 1097 PHE   B O   
8395  C  CB  . PHE   B 793 ? 1.5137 1.5139 1.9591 -0.0319 -0.2407 -0.1144 1097 PHE   B CB  
8396  C  CG  . PHE   B 793 ? 1.5584 1.5580 2.0306 -0.0363 -0.2477 -0.1200 1097 PHE   B CG  
8397  C  CD1 . PHE   B 793 ? 1.5908 1.5809 2.0670 -0.0380 -0.2523 -0.1218 1097 PHE   B CD1 
8398  C  CD2 . PHE   B 793 ? 1.5709 1.5799 2.0656 -0.0390 -0.2491 -0.1233 1097 PHE   B CD2 
8399  C  CE1 . PHE   B 793 ? 1.6092 1.5989 2.1115 -0.0424 -0.2586 -0.1269 1097 PHE   B CE1 
8400  C  CE2 . PHE   B 793 ? 1.6122 1.6213 2.1332 -0.0433 -0.2553 -0.1284 1097 PHE   B CE2 
8401  C  CZ  . PHE   B 793 ? 1.6272 1.6268 2.1525 -0.0452 -0.2600 -0.1302 1097 PHE   B CZ  
8402  N  N   . LEU   B 794 ? 1.4405 1.4122 1.8380 -0.0171 -0.2585 -0.1173 1098 LEU   B N   
8403  C  CA  . LEU   B 794 ? 1.4119 1.3699 1.8006 -0.0130 -0.2689 -0.1209 1098 LEU   B CA  
8404  C  C   . LEU   B 794 ? 1.4177 1.3689 1.7892 -0.0037 -0.2800 -0.1250 1098 LEU   B C   
8405  O  O   . LEU   B 794 ? 1.4905 1.4306 1.8590 0.0001  -0.2915 -0.1300 1098 LEU   B O   
8406  C  CB  . LEU   B 794 ? 1.3659 1.3176 1.7380 -0.0131 -0.2621 -0.1156 1098 LEU   B CB  
8407  C  CG  . LEU   B 794 ? 1.3437 1.3010 1.7294 -0.0218 -0.2501 -0.1108 1098 LEU   B CG  
8408  C  CD1 . LEU   B 794 ? 1.3753 1.3245 1.7439 -0.0209 -0.2455 -0.1064 1098 LEU   B CD1 
8409  C  CD2 . LEU   B 794 ? 1.4111 1.3691 1.8252 -0.0283 -0.2539 -0.1151 1098 LEU   B CD2 
8410  N  N   . ASP   B 795 ? 1.4076 1.3646 1.7676 0.0002  -0.2769 -0.1231 1099 ASP   B N   
8411  C  CA  . ASP   B 795 ? 1.4460 1.3961 1.7868 0.0095  -0.2858 -0.1261 1099 ASP   B CA  
8412  C  C   . ASP   B 795 ? 1.5033 1.4573 1.8562 0.0112  -0.2941 -0.1317 1099 ASP   B C   
8413  O  O   . ASP   B 795 ? 1.5283 1.4759 1.8656 0.0191  -0.3021 -0.1346 1099 ASP   B O   
8414  C  CB  . ASP   B 795 ? 1.4132 1.3654 1.7299 0.0138  -0.2772 -0.1201 1099 ASP   B CB  
8415  C  CG  . ASP   B 795 ? 1.4347 1.3827 1.7378 0.0130  -0.2695 -0.1146 1099 ASP   B CG  
8416  O  OD1 . ASP   B 795 ? 1.4041 1.3602 1.7138 0.0068  -0.2581 -0.1094 1099 ASP   B OD1 
8417  O  OD2 . ASP   B 795 ? 1.4733 1.4097 1.7583 0.0190  -0.2748 -0.1153 1099 ASP   B OD2 
8418  N  N   . ILE   B 796 ? 1.5921 1.5560 1.9717 0.0043  -0.2923 -0.1334 1100 ILE   B N   
8419  C  CA  . ILE   B 796 ? 1.6670 1.6351 2.0590 0.0059  -0.3003 -0.1388 1100 ILE   B CA  
8420  C  C   . ILE   B 796 ? 1.8061 1.7660 2.2115 0.0067  -0.3146 -0.1464 1100 ILE   B C   
8421  O  O   . ILE   B 796 ? 1.7545 1.7067 2.1619 0.0048  -0.3170 -0.1471 1100 ILE   B O   
8422  C  CB  . ILE   B 796 ? 1.6311 1.6145 2.0452 -0.0011 -0.2914 -0.1369 1100 ILE   B CB  
8423  C  CG1 . ILE   B 796 ? 1.7367 1.7239 2.1811 -0.0092 -0.2920 -0.1395 1100 ILE   B CG1 
8424  C  CG2 . ILE   B 796 ? 1.5507 1.5417 1.9553 -0.0041 -0.2759 -0.1288 1100 ILE   B CG2 
8425  C  CD1 . ILE   B 796 ? 1.6760 1.6779 2.1414 -0.0162 -0.2818 -0.1370 1100 ILE   B CD1 
8426  N  N   . SER   B 797 ? 2.0956 2.0566 2.5099 0.0096  -0.3244 -0.1523 1101 SER   B N   
8427  C  CA  . SER   B 797 ? 2.1543 2.1068 2.5801 0.0113  -0.3396 -0.1602 1101 SER   B CA  
8428  C  C   . SER   B 797 ? 2.1186 2.0768 2.5760 0.0020  -0.3382 -0.1617 1101 SER   B C   
8429  O  O   . SER   B 797 ? 2.1192 2.0899 2.5934 -0.0053 -0.3270 -0.1580 1101 SER   B O   
8430  C  CB  . SER   B 797 ? 2.1761 2.1292 2.6043 0.0168  -0.3501 -0.1660 1101 SER   B CB  
8431  O  OG  . SER   B 797 ? 2.1527 2.1204 2.6046 0.0110  -0.3447 -0.1658 1101 SER   B OG  
8432  N  N   . ARG   B 798 ? 1.9526 1.9010 2.4179 0.0023  -0.3499 -0.1674 1102 ARG   B N   
8433  C  CA  . ARG   B 798 ? 1.8969 1.8500 2.3942 -0.0062 -0.3504 -0.1698 1102 ARG   B CA  
8434  C  C   . ARG   B 798 ? 1.9315 1.8967 2.4562 -0.0097 -0.3522 -0.1734 1102 ARG   B C   
8435  O  O   . ARG   B 798 ? 1.9110 1.8855 2.4621 -0.0184 -0.3451 -0.1722 1102 ARG   B O   
8436  C  CB  . ARG   B 798 ? 1.8586 1.7979 2.3579 -0.0043 -0.3642 -0.1758 1102 ARG   B CB  
8437  C  CG  . ARG   B 798 ? 1.7876 1.7298 2.3179 -0.0135 -0.3638 -0.1777 1102 ARG   B CG  
8438  C  CD  . ARG   B 798 ? 1.7669 1.7190 2.3050 -0.0219 -0.3458 -0.1698 1102 ARG   B CD  
8439  N  NE  . ARG   B 798 ? 1.7473 1.6975 2.3059 -0.0296 -0.3442 -0.1702 1102 ARG   B NE  
8440  C  CZ  . ARG   B 798 ? 1.7317 1.6719 2.2779 -0.0301 -0.3422 -0.1677 1102 ARG   B CZ  
8441  N  NH1 . ARG   B 798 ? 1.7009 1.6320 2.2151 -0.0232 -0.3424 -0.1650 1102 ARG   B NH1 
8442  N  NH2 . ARG   B 798 ? 1.7536 1.6930 2.3203 -0.0377 -0.3398 -0.1677 1102 ARG   B NH2 
8443  N  N   . PRO   B 799 ? 2.0134 1.9789 2.5341 -0.0034 -0.3611 -0.1778 1103 PRO   B N   
8444  C  CA  . PRO   B 799 ? 2.0078 1.9865 2.5532 -0.0068 -0.3604 -0.1800 1103 PRO   B CA  
8445  C  C   . PRO   B 799 ? 1.9825 1.9753 2.5316 -0.0120 -0.3431 -0.1728 1103 PRO   B C   
8446  O  O   . PRO   B 799 ? 1.9551 1.9588 2.5313 -0.0199 -0.3364 -0.1721 1103 PRO   B O   
8447  C  CB  . PRO   B 799 ? 2.0185 1.9922 2.5495 0.0028  -0.3724 -0.1849 1103 PRO   B CB  
8448  C  CG  . PRO   B 799 ? 2.0067 1.9633 2.5177 0.0096  -0.3845 -0.1885 1103 PRO   B CG  
8449  C  CD  . PRO   B 799 ? 1.9798 1.9318 2.4775 0.0069  -0.3750 -0.1825 1103 PRO   B CD  
8450  N  N   . LYS   B 800 ? 1.9700 1.9623 2.4917 -0.0076 -0.3360 -0.1675 1104 LYS   B N   
8451  C  CA  . LYS   B 800 ? 1.8532 1.8579 2.3754 -0.0118 -0.3201 -0.1607 1104 LYS   B CA  
8452  C  C   . LYS   B 800 ? 1.8004 1.8088 2.3318 -0.0202 -0.3074 -0.1551 1104 LYS   B C   
8453  O  O   . LYS   B 800 ? 1.7292 1.7491 2.2739 -0.0262 -0.2954 -0.1511 1104 LYS   B O   
8454  C  CB  . LYS   B 800 ? 1.8424 1.8443 2.3324 -0.0050 -0.3161 -0.1564 1104 LYS   B CB  
8455  C  CG  . LYS   B 800 ? 1.9411 1.9396 2.4201 0.0034  -0.3269 -0.1611 1104 LYS   B CG  
8456  C  CD  . LYS   B 800 ? 2.0030 1.9963 2.4485 0.0103  -0.3230 -0.1566 1104 LYS   B CD  
8457  C  CE  . LYS   B 800 ? 1.9507 1.9425 2.3854 0.0179  -0.3305 -0.1600 1104 LYS   B CE  
8458  N  NZ  . LYS   B 800 ? 1.9227 1.9108 2.3265 0.0235  -0.3244 -0.1547 1104 LYS   B NZ  
8459  N  N   . MET   B 801 ? 1.8620 1.8600 2.3855 -0.0203 -0.3097 -0.1548 1105 MET   B N   
8460  C  CA  . MET   B 801 ? 1.7949 1.7944 2.3283 -0.0281 -0.2993 -0.1503 1105 MET   B CA  
8461  C  C   . MET   B 801 ? 1.8158 1.8247 2.3847 -0.0364 -0.2968 -0.1524 1105 MET   B C   
8462  O  O   . MET   B 801 ? 1.7610 1.7762 2.3406 -0.0436 -0.2838 -0.1473 1105 MET   B O   
8463  C  CB  . MET   B 801 ? 1.7928 1.7783 2.3158 -0.0263 -0.3062 -0.1518 1105 MET   B CB  
8464  C  CG  . MET   B 801 ? 1.6922 1.6749 2.2025 -0.0294 -0.2946 -0.1449 1105 MET   B CG  
8465  S  SD  . MET   B 801 ? 1.6790 1.6442 2.1715 -0.0254 -0.3031 -0.1464 1105 MET   B SD  
8466  C  CE  . MET   B 801 ? 1.7628 1.7200 2.2233 -0.0133 -0.3124 -0.1484 1105 MET   B CE  
8467  N  N   . GLN   B 802 ? 1.9273 1.9369 2.5148 -0.0353 -0.3091 -0.1598 1106 GLN   B N   
8468  C  CA  . GLN   B 802 ? 1.9195 1.9388 2.5425 -0.0427 -0.3074 -0.1623 1106 GLN   B CA  
8469  C  C   . GLN   B 802 ? 1.8973 1.9305 2.5291 -0.0444 -0.2987 -0.1600 1106 GLN   B C   
8470  O  O   . GLN   B 802 ? 1.9011 1.9441 2.5573 -0.0518 -0.2896 -0.1582 1106 GLN   B O   
8471  C  CB  . GLN   B 802 ? 1.9245 1.9389 2.5645 -0.0406 -0.3248 -0.1714 1106 GLN   B CB  
8472  C  CG  . GLN   B 802 ? 1.9174 1.9168 2.5483 -0.0385 -0.3348 -0.1743 1106 GLN   B CG  
8473  C  CD  . GLN   B 802 ? 1.9543 1.9459 2.5891 -0.0326 -0.3544 -0.1835 1106 GLN   B CD  
8474  O  OE1 . GLN   B 802 ? 1.9184 1.9162 2.5662 -0.0307 -0.3609 -0.1881 1106 GLN   B OE1 
8475  N  NE2 . GLN   B 802 ? 1.9171 1.8943 2.5398 -0.0292 -0.3641 -0.1863 1106 GLN   B NE2 
8476  N  N   . GLU   B 803 ? 1.7796 1.8135 2.3914 -0.0375 -0.3009 -0.1597 1107 GLU   B N   
8477  C  CA  . GLU   B 803 ? 1.7205 1.7670 2.3392 -0.0385 -0.2932 -0.1577 1107 GLU   B CA  
8478  C  C   . GLU   B 803 ? 1.7113 1.7652 2.3277 -0.0444 -0.2748 -0.1494 1107 GLU   B C   
8479  O  O   . GLU   B 803 ? 1.6943 1.7596 2.3262 -0.0483 -0.2664 -0.1477 1107 GLU   B O   
8480  C  CB  . GLU   B 803 ? 1.5999 1.6442 2.1953 -0.0297 -0.2993 -0.1589 1107 GLU   B CB  
8481  N  N   . VAL   B 804 ? 1.6931 1.7403 2.2906 -0.0449 -0.2684 -0.1442 1108 VAL   B N   
8482  C  CA  . VAL   B 804 ? 1.6000 1.6528 2.1917 -0.0495 -0.2516 -0.1363 1108 VAL   B CA  
8483  C  C   . VAL   B 804 ? 1.5980 1.6528 2.2114 -0.0582 -0.2434 -0.1343 1108 VAL   B C   
8484  O  O   . VAL   B 804 ? 1.6181 1.6817 2.2420 -0.0636 -0.2306 -0.1299 1108 VAL   B O   
8485  C  CB  . VAL   B 804 ? 1.5693 1.6143 2.1276 -0.0449 -0.2485 -0.1314 1108 VAL   B CB  
8486  C  CG1 . VAL   B 804 ? 1.5588 1.6055 2.0973 -0.0379 -0.2506 -0.1311 1108 VAL   B CG1 
8487  C  CG2 . VAL   B 804 ? 1.6135 1.6454 2.1627 -0.0417 -0.2591 -0.1346 1108 VAL   B CG2 
8488  N  N   . VAL   B 805 ? 1.6091 1.6554 2.2290 -0.0595 -0.2504 -0.1372 1109 VAL   B N   
8489  C  CA  . VAL   B 805 ? 1.6490 1.6963 2.2904 -0.0679 -0.2431 -0.1356 1109 VAL   B CA  
8490  C  C   . VAL   B 805 ? 1.6970 1.7542 2.3732 -0.0731 -0.2432 -0.1393 1109 VAL   B C   
8491  O  O   . VAL   B 805 ? 1.7097 1.7699 2.4067 -0.0807 -0.2349 -0.1374 1109 VAL   B O   
8492  C  CB  . VAL   B 805 ? 1.7002 1.7350 2.3392 -0.0677 -0.2514 -0.1381 1109 VAL   B CB  
8493  C  CG1 . VAL   B 805 ? 1.6589 1.6839 2.2633 -0.0615 -0.2528 -0.1352 1109 VAL   B CG1 
8494  C  CG2 . VAL   B 805 ? 1.7558 1.7875 2.4109 -0.0654 -0.2683 -0.1470 1109 VAL   B CG2 
8495  N  N   . ALA   B 806 ? 1.6804 1.7426 2.3632 -0.0691 -0.2522 -0.1445 1110 ALA   B N   
8496  C  CA  . ALA   B 806 ? 1.6756 1.7474 2.3918 -0.0730 -0.2541 -0.1488 1110 ALA   B CA  
8497  C  C   . ALA   B 806 ? 1.7501 1.8321 2.4825 -0.0806 -0.2370 -0.1433 1110 ALA   B C   
8498  O  O   . ALA   B 806 ? 1.7639 1.8505 2.4813 -0.0800 -0.2260 -0.1376 1110 ALA   B O   
8499  C  CB  . ALA   B 806 ? 1.6472 1.7236 2.3611 -0.0667 -0.2633 -0.1533 1110 ALA   B CB  
8500  N  N   . ASN   B 807 ? 1.7965 1.8815 2.5596 -0.0876 -0.2349 -0.1450 1111 ASN   B N   
8501  C  CA  . ASN   B 807 ? 1.7694 1.8632 2.5515 -0.0952 -0.2189 -0.1403 1111 ASN   B CA  
8502  C  C   . ASN   B 807 ? 1.7733 1.8642 2.5332 -0.0970 -0.2037 -0.1315 1111 ASN   B C   
8503  O  O   . ASN   B 807 ? 1.7879 1.8823 2.5285 -0.0941 -0.1968 -0.1273 1111 ASN   B O   
8504  C  CB  . ASN   B 807 ? 1.6633 1.7698 2.4593 -0.0946 -0.2165 -0.1416 1111 ASN   B CB  
8505  N  N   . LEU   B 808 ? 1.7095 1.7937 2.4719 -0.1019 -0.1984 -0.1288 1112 LEU   B N   
8506  C  CA  . LEU   B 808 ? 1.7182 1.7996 2.4619 -0.1041 -0.1836 -0.1206 1112 LEU   B CA  
8507  C  C   . LEU   B 808 ? 1.7294 1.8060 2.4868 -0.1114 -0.1756 -0.1179 1112 LEU   B C   
8508  O  O   . LEU   B 808 ? 1.7118 1.7800 2.4731 -0.1121 -0.1839 -0.1211 1112 LEU   B O   
8509  C  CB  . LEU   B 808 ? 1.8026 1.8753 2.5101 -0.0974 -0.1878 -0.1185 1112 LEU   B CB  
8510  C  CG  . LEU   B 808 ? 1.8580 1.9325 2.5434 -0.0972 -0.1736 -0.1106 1112 LEU   B CG  
8511  C  CD1 . LEU   B 808 ? 1.7728 1.8590 2.4642 -0.0965 -0.1686 -0.1101 1112 LEU   B CD1 
8512  C  CD2 . LEU   B 808 ? 1.8192 1.8855 2.4701 -0.0906 -0.1778 -0.1086 1112 LEU   B CD2 
8513  N  N   . GLU   B 819 ? 1.5652 1.6412 2.4082 -0.1235 -0.1950 -0.1333 1123 GLU   B N   
8514  C  CA  . GLU   B 819 ? 1.5881 1.6586 2.4144 -0.1157 -0.2123 -0.1388 1123 GLU   B CA  
8515  C  C   . GLU   B 819 ? 1.6564 1.7130 2.4559 -0.1131 -0.2156 -0.1368 1123 GLU   B C   
8516  O  O   . GLU   B 819 ? 1.6070 1.6567 2.4141 -0.1179 -0.2129 -0.1358 1123 GLU   B O   
8517  C  CB  . GLU   B 819 ? 1.4186 1.4908 2.2729 -0.1158 -0.2278 -0.1478 1123 GLU   B CB  
8518  N  N   . ALA   B 820 ? 1.7110 1.7634 2.4790 -0.1053 -0.2209 -0.1362 1124 ALA   B N   
8519  C  CA  . ALA   B 820 ? 1.7317 1.7712 2.4718 -0.1013 -0.2254 -0.1349 1124 ALA   B CA  
8520  C  C   . ALA   B 820 ? 1.7170 1.7514 2.4429 -0.0928 -0.2427 -0.1410 1124 ALA   B C   
8521  O  O   . ALA   B 820 ? 1.6998 1.7405 2.4206 -0.0881 -0.2463 -0.1428 1124 ALA   B O   
8522  C  CB  . ALA   B 820 ? 1.7164 1.7547 2.4280 -0.1001 -0.2121 -0.1265 1124 ALA   B CB  
8523  N  N   . THR   B 821 ? 1.7202 1.7428 2.4396 -0.0908 -0.2535 -0.1444 1125 THR   B N   
8524  C  CA  . THR   B 821 ? 1.6945 1.7106 2.4014 -0.0827 -0.2706 -0.1507 1125 THR   B CA  
8525  C  C   . THR   B 821 ? 1.6704 1.6790 2.3386 -0.0754 -0.2703 -0.1470 1125 THR   B C   
8526  O  O   . THR   B 821 ? 1.6429 1.6502 2.2951 -0.0770 -0.2581 -0.1400 1125 THR   B O   
8527  C  CB  . THR   B 821 ? 1.6969 1.7035 2.4173 -0.0837 -0.2838 -0.1571 1125 THR   B CB  
8528  O  OG1 . THR   B 821 ? 1.7202 1.7149 2.4217 -0.0837 -0.2814 -0.1536 1125 THR   B OG1 
8529  C  CG2 . THR   B 821 ? 1.6717 1.6850 2.4310 -0.0924 -0.2810 -0.1593 1125 THR   B CG2 
8530  N  N   . ALA   B 822 ? 1.6704 1.6735 2.3237 -0.0673 -0.2842 -0.1519 1126 ALA   B N   
8531  C  CA  . ALA   B 822 ? 1.6303 1.6264 2.2477 -0.0598 -0.2847 -0.1489 1126 ALA   B CA  
8532  C  C   . ALA   B 822 ? 1.6775 1.6622 2.2792 -0.0604 -0.2820 -0.1455 1126 ALA   B C   
8533  O  O   . ALA   B 822 ? 1.6970 1.6795 2.2736 -0.0580 -0.2738 -0.1396 1126 ALA   B O   
8534  C  CB  . ALA   B 822 ? 1.6879 1.6782 2.2938 -0.0510 -0.3011 -0.1555 1126 ALA   B CB  
8535  N  N   . ASP   B 823 ? 1.7538 1.7311 2.3704 -0.0637 -0.2887 -0.1493 1127 ASP   B N   
8536  C  CA  . ASP   B 823 ? 1.7490 1.7136 2.3498 -0.0632 -0.2888 -0.1472 1127 ASP   B CA  
8537  C  C   . ASP   B 823 ? 1.7534 1.7203 2.3534 -0.0697 -0.2720 -0.1393 1127 ASP   B C   
8538  O  O   . ASP   B 823 ? 1.7797 1.7374 2.3591 -0.0680 -0.2691 -0.1357 1127 ASP   B O   
8539  C  CB  . ASP   B 823 ? 1.7792 1.7352 2.3974 -0.0651 -0.3012 -0.1538 1127 ASP   B CB  
8540  C  CG  . ASP   B 823 ? 1.7796 1.7318 2.3983 -0.0584 -0.3190 -0.1621 1127 ASP   B CG  
8541  O  OD1 . ASP   B 823 ? 1.7701 1.7318 2.3993 -0.0573 -0.3214 -0.1647 1127 ASP   B OD1 
8542  O  OD2 . ASP   B 823 ? 1.8145 1.7534 2.4228 -0.0543 -0.3307 -0.1661 1127 ASP   B OD2 
8543  N  N   . ASP   B 824 ? 1.6899 1.6678 2.3124 -0.0770 -0.2610 -0.1368 1128 ASP   B N   
8544  C  CA  . ASP   B 824 ? 1.6894 1.6690 2.3087 -0.0825 -0.2445 -0.1289 1128 ASP   B CA  
8545  C  C   . ASP   B 824 ? 1.5968 1.5775 2.1856 -0.0774 -0.2370 -0.1230 1128 ASP   B C   
8546  O  O   . ASP   B 824 ? 1.5766 1.5508 2.1468 -0.0773 -0.2302 -0.1178 1128 ASP   B O   
8547  C  CB  . ASP   B 824 ? 1.7106 1.7023 2.3583 -0.0903 -0.2338 -0.1272 1128 ASP   B CB  
8548  C  CG  . ASP   B 824 ? 1.7115 1.7047 2.3927 -0.0952 -0.2412 -0.1335 1128 ASP   B CG  
8549  O  OD1 . ASP   B 824 ? 1.7510 1.7340 2.4360 -0.0955 -0.2505 -0.1373 1128 ASP   B OD1 
8550  O  OD2 . ASP   B 824 ? 1.6723 1.6769 2.3765 -0.0988 -0.2377 -0.1347 1128 ASP   B OD2 
8551  N  N   . LEU   B 825 ? 1.5658 1.5544 2.1493 -0.0732 -0.2387 -0.1239 1129 LEU   B N   
8552  C  CA  . LEU   B 825 ? 1.5211 1.5132 2.0800 -0.0693 -0.2305 -0.1183 1129 LEU   B CA  
8553  C  C   . LEU   B 825 ? 1.5166 1.4982 2.0447 -0.0616 -0.2367 -0.1177 1129 LEU   B C   
8554  O  O   . LEU   B 825 ? 1.4819 1.4629 1.9887 -0.0599 -0.2280 -0.1117 1129 LEU   B O   
8555  C  CB  . LEU   B 825 ? 1.5181 1.5212 2.0825 -0.0671 -0.2318 -0.1202 1129 LEU   B CB  
8556  C  CG  . LEU   B 825 ? 1.5602 1.5723 2.1140 -0.0672 -0.2191 -0.1140 1129 LEU   B CG  
8557  C  CD1 . LEU   B 825 ? 1.4936 1.5173 2.0661 -0.0683 -0.2196 -0.1168 1129 LEU   B CD1 
8558  C  CD2 . LEU   B 825 ? 1.6569 1.6646 2.1780 -0.0594 -0.2209 -0.1117 1129 LEU   B CD2 
8559  N  N   . ILE   B 826 ? 1.5531 1.5263 2.0783 -0.0568 -0.2514 -0.1240 1130 ILE   B N   
8560  C  CA  . ILE   B 826 ? 1.5252 1.4871 2.0217 -0.0495 -0.2572 -0.1236 1130 ILE   B CA  
8561  C  C   . ILE   B 826 ? 1.5354 1.4899 2.0225 -0.0523 -0.2495 -0.1186 1130 ILE   B C   
8562  O  O   . ILE   B 826 ? 1.5212 1.4706 1.9824 -0.0476 -0.2467 -0.1147 1130 ILE   B O   
8563  C  CB  . ILE   B 826 ? 1.5096 1.4623 2.0072 -0.0445 -0.2744 -0.1315 1130 ILE   B CB  
8564  C  CG1 . ILE   B 826 ? 1.5121 1.4709 2.0155 -0.0406 -0.2825 -0.1364 1130 ILE   B CG1 
8565  C  CG2 . ILE   B 826 ? 1.4991 1.4390 1.9669 -0.0369 -0.2799 -0.1310 1130 ILE   B CG2 
8566  C  CD1 . ILE   B 826 ? 1.5506 1.4996 2.0558 -0.0358 -0.2998 -0.1444 1130 ILE   B CD1 
8567  N  N   . LYS   B 827 ? 1.4813 1.4350 1.9896 -0.0598 -0.2462 -0.1186 1131 LYS   B N   
8568  C  CA  . LYS   B 827 ? 1.4691 1.4157 1.9695 -0.0629 -0.2381 -0.1136 1131 LYS   B CA  
8569  C  C   . LYS   B 827 ? 1.4708 1.4240 1.9592 -0.0644 -0.2229 -0.1057 1131 LYS   B C   
8570  O  O   . LYS   B 827 ? 1.5150 1.4622 1.9818 -0.0620 -0.2182 -0.1012 1131 LYS   B O   
8571  C  CB  . LYS   B 827 ? 1.4231 1.3681 1.9507 -0.0712 -0.2368 -0.1152 1131 LYS   B CB  
8572  N  N   . VAL   B 828 ? 1.5233 1.4888 2.0249 -0.0678 -0.2156 -0.1043 1132 VAL   B N   
8573  C  CA  . VAL   B 828 ? 1.4737 1.4457 1.9665 -0.0698 -0.2010 -0.0970 1132 VAL   B CA  
8574  C  C   . VAL   B 828 ? 1.4496 1.4201 1.9120 -0.0624 -0.2008 -0.0940 1132 VAL   B C   
8575  O  O   . VAL   B 828 ? 1.4457 1.4116 1.8904 -0.0616 -0.1941 -0.0888 1132 VAL   B O   
8576  C  CB  . VAL   B 828 ? 1.3644 1.3496 1.8769 -0.0740 -0.1950 -0.0970 1132 VAL   B CB  
8577  C  CG1 . VAL   B 828 ? 1.2790 1.2698 1.7839 -0.0767 -0.1797 -0.0897 1132 VAL   B CG1 
8578  C  CG2 . VAL   B 828 ? 1.4216 1.4083 1.9657 -0.0809 -0.1964 -0.1007 1132 VAL   B CG2 
8579  N  N   . VAL   B 829 ? 1.4449 1.4193 1.9013 -0.0567 -0.2083 -0.0973 1133 VAL   B N   
8580  C  CA  . VAL   B 829 ? 1.4459 1.4191 1.8747 -0.0495 -0.2085 -0.0947 1133 VAL   B CA  
8581  C  C   . VAL   B 829 ? 1.5369 1.4976 1.9459 -0.0454 -0.2124 -0.0939 1133 VAL   B C   
8582  O  O   . VAL   B 829 ? 1.5237 1.4827 1.9113 -0.0422 -0.2068 -0.0891 1133 VAL   B O   
8583  C  CB  . VAL   B 829 ? 1.3723 1.3491 1.7989 -0.0438 -0.2179 -0.0994 1133 VAL   B CB  
8584  C  CG1 . VAL   B 829 ? 1.3444 1.3219 1.7447 -0.0373 -0.2157 -0.0960 1133 VAL   B CG1 
8585  C  CG2 . VAL   B 829 ? 1.3491 1.3375 1.7983 -0.0482 -0.2152 -0.1010 1133 VAL   B CG2 
8586  N  N   . GLU   B 830 ? 1.7165 1.6680 2.1327 -0.0453 -0.2222 -0.0988 1134 GLU   B N   
8587  C  CA  . GLU   B 830 ? 1.7430 1.6819 2.1403 -0.0407 -0.2273 -0.0988 1134 GLU   B CA  
8588  C  C   . GLU   B 830 ? 1.7689 1.7046 2.1575 -0.0438 -0.2163 -0.0923 1134 GLU   B C   
8589  O  O   . GLU   B 830 ? 1.8051 1.7340 2.1710 -0.0389 -0.2161 -0.0897 1134 GLU   B O   
8590  C  CB  . GLU   B 830 ? 1.7468 1.6765 2.1562 -0.0409 -0.2396 -0.1054 1134 GLU   B CB  
8591  N  N   . GLU   B 831 ? 1.5306 1.4707 1.9366 -0.0517 -0.2070 -0.0897 1135 GLU   B N   
8592  C  CA  . GLU   B 831 ? 1.5517 1.4895 1.9481 -0.0545 -0.1954 -0.0830 1135 GLU   B CA  
8593  C  C   . GLU   B 831 ? 1.5385 1.4831 1.9165 -0.0511 -0.1877 -0.0778 1135 GLU   B C   
8594  O  O   . GLU   B 831 ? 1.5166 1.4568 1.8756 -0.0488 -0.1827 -0.0732 1135 GLU   B O   
8595  C  CB  . GLU   B 831 ? 1.5391 1.4802 1.9581 -0.0635 -0.1866 -0.0812 1135 GLU   B CB  
8596  N  N   . LEU   B 832 ? 1.5068 1.4620 1.8903 -0.0506 -0.1869 -0.0787 1136 LEU   B N   
8597  C  CA  . LEU   B 832 ? 1.4311 1.3933 1.7987 -0.0477 -0.1798 -0.0740 1136 LEU   B CA  
8598  C  C   . LEU   B 832 ? 1.4491 1.4066 1.7923 -0.0392 -0.1859 -0.0742 1136 LEU   B C   
8599  O  O   . LEU   B 832 ? 1.4287 1.3877 1.7544 -0.0366 -0.1796 -0.0693 1136 LEU   B O   
8600  C  CB  . LEU   B 832 ? 1.3477 1.3220 1.7281 -0.0494 -0.1779 -0.0752 1136 LEU   B CB  
8601  C  CG  . LEU   B 832 ? 1.2965 1.2777 1.7011 -0.0574 -0.1703 -0.0745 1136 LEU   B CG  
8602  C  CD1 . LEU   B 832 ? 1.2237 1.2169 1.6352 -0.0575 -0.1679 -0.0750 1136 LEU   B CD1 
8603  C  CD2 . LEU   B 832 ? 1.2497 1.2291 1.6513 -0.0621 -0.1579 -0.0683 1136 LEU   B CD2 
8604  N  N   . THR   B 833 ? 1.4576 1.4091 1.7991 -0.0346 -0.1980 -0.0797 1137 THR   B N   
8605  C  CA  . THR   B 833 ? 1.4832 1.4287 1.8007 -0.0263 -0.2032 -0.0797 1137 THR   B CA  
8606  C  C   . THR   B 833 ? 1.4848 1.4214 1.7881 -0.0255 -0.1998 -0.0759 1137 THR   B C   
8607  O  O   . THR   B 833 ? 1.4707 1.4052 1.7528 -0.0199 -0.1984 -0.0730 1137 THR   B O   
8608  C  CB  . THR   B 833 ? 1.4798 1.4190 1.7977 -0.0214 -0.2170 -0.0865 1137 THR   B CB  
8609  O  OG1 . THR   B 833 ? 1.5084 1.4373 1.8330 -0.0231 -0.2229 -0.0894 1137 THR   B OG1 
8610  C  CG2 . THR   B 833 ? 1.4292 1.3768 1.7651 -0.0233 -0.2205 -0.0905 1137 THR   B CG2 
8611  N  N   . ARG   B 834 ? 1.4617 1.3936 1.7767 -0.0312 -0.1975 -0.0756 1138 ARG   B N   
8612  C  CA  . ARG   B 834 ? 1.4650 1.3873 1.7672 -0.0304 -0.1951 -0.0725 1138 ARG   B CA  
8613  C  C   . ARG   B 834 ? 1.4284 1.3555 1.7206 -0.0319 -0.1827 -0.0654 1138 ARG   B C   
8614  O  O   . ARG   B 834 ? 1.4498 1.3712 1.7392 -0.0346 -0.1773 -0.0621 1138 ARG   B O   
8615  C  CB  . ARG   B 834 ? 1.4796 1.3946 1.7980 -0.0361 -0.1970 -0.0747 1138 ARG   B CB  
8616  N  N   . ILE   B 835 ? 1.4442 1.3809 1.7305 -0.0301 -0.1783 -0.0631 1139 ILE   B N   
8617  C  CA  . ILE   B 835 ? 1.4391 1.3795 1.7143 -0.0307 -0.1676 -0.0566 1139 ILE   B CA  
8618  C  C   . ILE   B 835 ? 1.4380 1.3798 1.6914 -0.0234 -0.1681 -0.0545 1139 ILE   B C   
8619  O  O   . ILE   B 835 ? 1.4626 1.4050 1.7040 -0.0229 -0.1608 -0.0493 1139 ILE   B O   
8620  C  CB  . ILE   B 835 ? 1.3609 1.3119 1.6496 -0.0368 -0.1585 -0.0542 1139 ILE   B CB  
8621  C  CG1 . ILE   B 835 ? 1.3464 1.3076 1.6333 -0.0339 -0.1593 -0.0549 1139 ILE   B CG1 
8622  C  CG2 . ILE   B 835 ? 1.3567 1.3079 1.6691 -0.0435 -0.1587 -0.0570 1139 ILE   B CG2 
8623  C  CD1 . ILE   B 835 ? 1.2614 1.2323 1.5577 -0.0391 -0.1495 -0.0518 1139 ILE   B CD1 
8624  N  N   . HIS   B 836 ? 1.4323 1.3744 1.6799 -0.0177 -0.1761 -0.0581 1140 HIS   B N   
8625  C  CA  . HIS   B 836 ? 1.4315 1.3755 1.6592 -0.0111 -0.1753 -0.0556 1140 HIS   B CA  
8626  C  C   . HIS   B 836 ? 1.4432 1.3778 1.6570 -0.0036 -0.1845 -0.0585 1140 HIS   B C   
8627  O  O   . HIS   B 836 ? 1.4352 1.3681 1.6309 0.0020  -0.1832 -0.0559 1140 HIS   B O   
8628  C  CB  . HIS   B 836 ? 1.3986 1.3539 1.6288 -0.0106 -0.1733 -0.0555 1140 HIS   B CB  
8629  C  CG  . HIS   B 836 ? 1.4068 1.3646 1.6517 -0.0115 -0.1801 -0.0610 1140 HIS   B CG  
8630  N  ND1 . HIS   B 836 ? 1.4760 1.4305 1.7149 -0.0054 -0.1896 -0.0653 1140 HIS   B ND1 
8631  C  CD2 . HIS   B 836 ? 1.4087 1.3718 1.6743 -0.0177 -0.1790 -0.0629 1140 HIS   B CD2 
8632  C  CE1 . HIS   B 836 ? 1.4743 1.4319 1.7294 -0.0077 -0.1945 -0.0698 1140 HIS   B CE1 
8633  N  NE2 . HIS   B 836 ? 1.4552 1.4185 1.7273 -0.0153 -0.1882 -0.0685 1140 HIS   B NE2 
8634  N  N   . SER   C 3   ? 1.5902 1.2727 1.1183 0.0482  -0.0922 0.0064  868  SER   C N   
8635  C  CA  . SER   C 3   ? 1.6879 1.3850 1.2345 0.0434  -0.0802 0.0077  868  SER   C CA  
8636  C  C   . SER   C 3   ? 1.6773 1.3689 1.2186 0.0445  -0.0639 0.0119  868  SER   C C   
8637  O  O   . SER   C 3   ? 1.6475 1.3559 1.2102 0.0399  -0.0565 0.0138  868  SER   C O   
8638  C  CB  . SER   C 3   ? 1.7409 1.4333 1.2819 0.0437  -0.0801 0.0055  868  SER   C CB  
8639  O  OG  . SER   C 3   ? 1.7501 1.4531 1.3037 0.0408  -0.0933 0.0019  868  SER   C OG  
8640  N  N   . LEU   C 4   ? 1.6484 1.3163 1.1612 0.0506  -0.0582 0.0134  869  LEU   C N   
8641  C  CA  . LEU   C 4   ? 1.6235 1.2839 1.1293 0.0521  -0.0424 0.0175  869  LEU   C CA  
8642  C  C   . LEU   C 4   ? 1.5424 1.2009 1.0463 0.0532  -0.0431 0.0197  869  LEU   C C   
8643  O  O   . LEU   C 4   ? 1.4541 1.1024 0.9476 0.0555  -0.0320 0.0232  869  LEU   C O   
8644  C  CB  . LEU   C 4   ? 1.6525 1.2877 1.1282 0.0584  -0.0355 0.0183  869  LEU   C CB  
8645  C  CG  . LEU   C 4   ? 1.6339 1.2640 1.1066 0.0588  -0.0167 0.0219  869  LEU   C CG  
8646  C  CD1 . LEU   C 4   ? 1.6121 1.2609 1.1086 0.0534  -0.0104 0.0212  869  LEU   C CD1 
8647  C  CD2 . LEU   C 4   ? 1.5532 1.1548 0.9916 0.0664  -0.0109 0.0229  869  LEU   C CD2 
8648  N  N   . THR   C 5   ? 1.5479 1.2161 1.0618 0.0517  -0.0570 0.0176  870  THR   C N   
8649  C  CA  . THR   C 5   ? 1.5581 1.2249 1.0701 0.0530  -0.0612 0.0189  870  THR   C CA  
8650  C  C   . THR   C 5   ? 1.5533 1.2453 1.0955 0.0470  -0.0673 0.0181  870  THR   C C   
8651  O  O   . THR   C 5   ? 1.5494 1.2423 1.0921 0.0481  -0.0749 0.0181  870  THR   C O   
8652  C  CB  . THR   C 5   ? 1.6053 1.2528 1.0923 0.0593  -0.0737 0.0169  870  THR   C CB  
8653  O  OG1 . THR   C 5   ? 1.5796 1.2309 1.0699 0.0586  -0.0864 0.0127  870  THR   C OG1 
8654  C  CG2 . THR   C 5   ? 1.6562 1.2762 1.1105 0.0662  -0.0660 0.0188  870  THR   C CG2 
8655  N  N   . THR   C 6   ? 1.5527 1.2645 1.1193 0.0412  -0.0646 0.0173  871  THR   C N   
8656  C  CA  . THR   C 6   ? 1.4815 1.2171 1.0768 0.0356  -0.0692 0.0167  871  THR   C CA  
8657  C  C   . THR   C 6   ? 1.4634 1.2096 1.0738 0.0321  -0.0558 0.0199  871  THR   C C   
8658  O  O   . THR   C 6   ? 1.4499 1.1922 1.0575 0.0319  -0.0437 0.0215  871  THR   C O   
8659  C  CB  . THR   C 6   ? 1.5171 1.2674 1.1294 0.0316  -0.0764 0.0135  871  THR   C CB  
8660  O  OG1 . THR   C 6   ? 1.5457 1.2815 1.1393 0.0353  -0.0848 0.0108  871  THR   C OG1 
8661  C  CG2 . THR   C 6   ? 1.5453 1.3144 1.1797 0.0278  -0.0863 0.0122  871  THR   C CG2 
8662  N  N   . CYS   C 7   ? 1.4503 1.2095 1.0767 0.0294  -0.0580 0.0208  872  CYS   C N   
8663  C  CA  . CYS   C 7   ? 1.4005 1.1698 1.0418 0.0261  -0.0463 0.0236  872  CYS   C CA  
8664  C  C   . CYS   C 7   ? 1.4355 1.2265 1.1035 0.0201  -0.0444 0.0225  872  CYS   C C   
8665  O  O   . CYS   C 7   ? 1.4436 1.2493 1.1277 0.0172  -0.0539 0.0203  872  CYS   C O   
8666  C  CB  . CYS   C 7   ? 1.3785 1.1518 1.0249 0.0260  -0.0493 0.0251  872  CYS   C CB  
8667  S  SG  . CYS   C 7   ? 1.3653 1.1491 1.0286 0.0221  -0.0349 0.0285  872  CYS   C SG  
8668  N  N   . GLU   C 8   ? 1.4822 1.2752 1.1554 0.0183  -0.0318 0.0240  873  GLU   C N   
8669  C  CA  . GLU   C 8   ? 1.4629 1.2753 1.1604 0.0130  -0.0295 0.0229  873  GLU   C CA  
8670  C  C   . GLU   C 8   ? 1.4477 1.2798 1.1690 0.0088  -0.0331 0.0229  873  GLU   C C   
8671  O  O   . GLU   C 8   ? 1.4626 1.3111 1.2030 0.0049  -0.0366 0.0211  873  GLU   C O   
8672  C  CB  . GLU   C 8   ? 1.5068 1.3181 1.2067 0.0121  -0.0149 0.0247  873  GLU   C CB  
8673  C  CG  . GLU   C 8   ? 1.6367 1.4319 1.3172 0.0156  -0.0103 0.0245  873  GLU   C CG  
8674  C  CD  . GLU   C 8   ? 1.6654 1.4706 1.3576 0.0129  -0.0100 0.0223  873  GLU   C CD  
8675  O  OE1 . GLU   C 8   ? 1.6006 1.4250 1.3169 0.0081  -0.0094 0.0217  873  GLU   C OE1 
8676  O  OE2 . GLU   C 8   ? 1.7254 1.5185 1.4018 0.0158  -0.0103 0.0211  873  GLU   C OE2 
8677  N  N   . VAL   C 9   ? 1.4257 1.2558 1.1455 0.0096  -0.0322 0.0249  874  VAL   C N   
8678  C  CA  . VAL   C 9   ? 1.3436 1.1911 1.0854 0.0058  -0.0331 0.0254  874  VAL   C CA  
8679  C  C   . VAL   C 9   ? 1.3465 1.2009 1.0934 0.0057  -0.0464 0.0237  874  VAL   C C   
8680  O  O   . VAL   C 9   ? 1.3342 1.2062 1.1015 0.0020  -0.0510 0.0223  874  VAL   C O   
8681  C  CB  . VAL   C 9   ? 1.2892 1.1311 1.0278 0.0065  -0.0239 0.0286  874  VAL   C CB  
8682  C  CG1 . VAL   C 9   ? 1.3362 1.1939 1.0946 0.0033  -0.0262 0.0290  874  VAL   C CG1 
8683  C  CG2 . VAL   C 9   ? 1.3331 1.1723 1.0727 0.0056  -0.0105 0.0301  874  VAL   C CG2 
8684  N  N   . CYS   C 10  ? 1.3572 1.1981 1.0863 0.0100  -0.0529 0.0237  875  CYS   C N   
8685  C  CA  . CYS   C 10  ? 1.2803 1.1280 1.0152 0.0101  -0.0654 0.0221  875  CYS   C CA  
8686  C  C   . CYS   C 10  ? 1.3078 1.1506 1.0344 0.0119  -0.0764 0.0192  875  CYS   C C   
8687  O  O   . CYS   C 10  ? 1.3099 1.1621 1.0466 0.0109  -0.0869 0.0174  875  CYS   C O   
8688  C  CB  . CYS   C 10  ? 1.3011 1.1393 1.0247 0.0135  -0.0670 0.0239  875  CYS   C CB  
8689  S  SG  . CYS   C 10  ? 1.2631 1.0729 0.9519 0.0204  -0.0674 0.0245  875  CYS   C SG  
8690  N  N   . GLY   C 11  ? 1.3745 1.2030 1.0837 0.0145  -0.0741 0.0186  876  GLY   C N   
8691  C  CA  . GLY   C 11  ? 1.3982 1.2210 1.0988 0.0162  -0.0844 0.0156  876  GLY   C CA  
8692  C  C   . GLY   C 11  ? 1.4432 1.2468 1.1196 0.0220  -0.0919 0.0151  876  GLY   C C   
8693  O  O   . GLY   C 11  ? 1.4512 1.2499 1.1208 0.0235  -0.1019 0.0123  876  GLY   C O   
8694  N  N   . ALA   C 12  ? 1.6040 1.3959 1.2669 0.0253  -0.0876 0.0176  877  ALA   C N   
8695  C  CA  . ALA   C 12  ? 1.6257 1.3991 1.2652 0.0312  -0.0953 0.0171  877  ALA   C CA  
8696  C  C   . ALA   C 12  ? 1.6539 1.4067 1.2683 0.0355  -0.0934 0.0165  877  ALA   C C   
8697  O  O   . ALA   C 12  ? 1.6778 1.4234 1.2846 0.0359  -0.0810 0.0185  877  ALA   C O   
8698  C  CB  . ALA   C 12  ? 1.6271 1.3936 1.2593 0.0335  -0.0902 0.0202  877  ALA   C CB  
8699  N  N   . CYS   C 13  ? 1.5673 1.3107 1.1692 0.0388  -0.1057 0.0136  878  CYS   C N   
8700  C  CA  . CYS   C 13  ? 1.5136 1.2365 1.0904 0.0434  -0.1058 0.0125  878  CYS   C CA  
8701  C  C   . CYS   C 13  ? 1.5445 1.2449 1.0937 0.0503  -0.1091 0.0133  878  CYS   C C   
8702  O  O   . CYS   C 13  ? 1.5040 1.2023 1.0503 0.0526  -0.1222 0.0113  878  CYS   C O   
8703  C  CB  . CYS   C 13  ? 1.4854 1.2120 1.0663 0.0424  -0.1174 0.0085  878  CYS   C CB  
8704  S  SG  . CYS   C 13  ? 1.7205 1.4291 1.2796 0.0455  -0.1138 0.0071  878  CYS   C SG  
8705  N  N   . PHE   C 14  ? 1.5837 1.2670 1.1129 0.0538  -0.0974 0.0162  879  PHE   C N   
8706  C  CA  . PHE   C 14  ? 1.6088 1.2683 1.1092 0.0608  -0.0984 0.0174  879  PHE   C CA  
8707  C  C   . PHE   C 14  ? 1.7232 1.3616 1.1973 0.0663  -0.1040 0.0151  879  PHE   C C   
8708  O  O   . PHE   C 14  ? 1.6715 1.3124 1.1484 0.0647  -0.1042 0.0132  879  PHE   C O   
8709  C  CB  . PHE   C 14  ? 1.5906 1.2417 1.0825 0.0618  -0.0821 0.0219  879  PHE   C CB  
8710  C  CG  . PHE   C 14  ? 1.5308 1.1980 1.0434 0.0577  -0.0777 0.0241  879  PHE   C CG  
8711  C  CD1 . PHE   C 14  ? 1.4966 1.1851 1.0362 0.0511  -0.0704 0.0249  879  PHE   C CD1 
8712  C  CD2 . PHE   C 14  ? 1.5591 1.2194 1.0635 0.0608  -0.0814 0.0254  879  PHE   C CD2 
8713  C  CE1 . PHE   C 14  ? 1.5033 1.2058 1.0610 0.0476  -0.0668 0.0268  879  PHE   C CE1 
8714  C  CE2 . PHE   C 14  ? 1.4075 1.0819 0.9301 0.0573  -0.0775 0.0275  879  PHE   C CE2 
8715  C  CZ  . PHE   C 14  ? 1.4732 1.1685 1.0224 0.0507  -0.0703 0.0281  879  PHE   C CZ  
8716  N  N   . GLU   C 15  ? 1.7766 1.3932 1.2239 0.0732  -0.1089 0.0153  880  GLU   C N   
8717  C  CA  . GLU   C 15  ? 1.8493 1.4442 1.2697 0.0790  -0.1144 0.0131  880  GLU   C CA  
8718  C  C   . GLU   C 15  ? 1.8546 1.4313 1.2536 0.0823  -0.0991 0.0160  880  GLU   C C   
8719  O  O   . GLU   C 15  ? 1.8619 1.4257 1.2449 0.0852  -0.0997 0.0143  880  GLU   C O   
8720  C  CB  . GLU   C 15  ? 1.9255 1.5042 1.3258 0.0854  -0.1280 0.0114  880  GLU   C CB  
8721  C  CG  . GLU   C 15  ? 1.9670 1.5592 1.3835 0.0833  -0.1456 0.0070  880  GLU   C CG  
8722  C  CD  . GLU   C 15  ? 2.2216 1.7969 1.6177 0.0900  -0.1599 0.0049  880  GLU   C CD  
8723  O  OE1 . GLU   C 15  ? 2.2931 1.8420 1.6570 0.0972  -0.1578 0.0058  880  GLU   C OE1 
8724  O  OE2 . GLU   C 15  ? 2.3001 1.8882 1.7124 0.0883  -0.1733 0.0023  880  GLU   C OE2 
8725  N  N   . THR   C 16  ? 1.8645 1.4410 1.2647 0.0815  -0.0851 0.0202  881  THR   C N   
8726  C  CA  . THR   C 16  ? 1.8592 1.4184 1.2400 0.0847  -0.0692 0.0236  881  THR   C CA  
8727  C  C   . THR   C 16  ? 1.8244 1.4010 1.2286 0.0784  -0.0538 0.0266  881  THR   C C   
8728  O  O   . THR   C 16  ? 1.8021 1.3956 1.2276 0.0740  -0.0525 0.0279  881  THR   C O   
8729  C  CB  . THR   C 16  ? 1.8576 1.3945 1.2120 0.0912  -0.0667 0.0262  881  THR   C CB  
8730  O  OG1 . THR   C 16  ? 1.8652 1.4157 1.2370 0.0880  -0.0663 0.0281  881  THR   C OG1 
8731  C  CG2 . THR   C 16  ? 1.8692 1.3871 1.1986 0.0981  -0.0821 0.0231  881  THR   C CG2 
8732  N  N   . ARG   C 17  ? 1.7568 1.3280 1.1557 0.0784  -0.0420 0.0277  882  ARG   C N   
8733  C  CA  . ARG   C 17  ? 1.6812 1.2662 1.0999 0.0732  -0.0263 0.0307  882  ARG   C CA  
8734  C  C   . ARG   C 17  ? 1.6994 1.2785 1.1141 0.0742  -0.0161 0.0350  882  ARG   C C   
8735  O  O   . ARG   C 17  ? 1.6518 1.2491 1.0907 0.0687  -0.0100 0.0367  882  ARG   C O   
8736  C  CB  . ARG   C 17  ? 1.6009 1.1772 1.0103 0.0745  -0.0155 0.0312  882  ARG   C CB  
8737  N  N   . LYS   C 18  ? 1.7547 1.3081 1.1384 0.0813  -0.0150 0.0366  883  LYS   C N   
8738  C  CA  . LYS   C 18  ? 1.7236 1.2675 1.0991 0.0831  -0.0050 0.0409  883  LYS   C CA  
8739  C  C   . LYS   C 18  ? 1.6935 1.2499 1.0837 0.0807  -0.0132 0.0408  883  LYS   C C   
8740  O  O   . LYS   C 18  ? 1.6980 1.2412 1.0746 0.0837  -0.0068 0.0442  883  LYS   C O   
8741  C  CB  . LYS   C 18  ? 1.7865 1.2979 1.1226 0.0920  -0.0032 0.0423  883  LYS   C CB  
8742  N  N   . GLY   C 19  ? 1.5937 1.1712 1.0065 0.0763  -0.0261 0.0374  884  GLY   C N   
8743  C  CA  . GLY   C 19  ? 1.5740 1.1667 1.0043 0.0735  -0.0352 0.0367  884  GLY   C CA  
8744  C  C   . GLY   C 19  ? 1.5690 1.1909 1.0354 0.0652  -0.0331 0.0362  884  GLY   C C   
8745  O  O   . GLY   C 19  ? 1.5886 1.2230 1.0719 0.0617  -0.0301 0.0379  884  GLY   C O   
8746  N  N   . LEU   C 20  ? 1.6109 1.2430 1.0884 0.0623  -0.0350 0.0336  885  LEU   C N   
8747  C  CA  . LEU   C 20  ? 1.5635 1.2210 1.0728 0.0548  -0.0305 0.0334  885  LEU   C CA  
8748  C  C   . LEU   C 20  ? 1.5597 1.2195 1.0765 0.0523  -0.0133 0.0373  885  LEU   C C   
8749  O  O   . LEU   C 20  ? 1.4936 1.1741 1.0373 0.0464  -0.0096 0.0377  885  LEU   C O   
8750  C  CB  . LEU   C 20  ? 1.4844 1.1463 0.9973 0.0535  -0.0335 0.0304  885  LEU   C CB  
8751  C  CG  . LEU   C 20  ? 1.3891 1.0730 0.9293 0.0470  -0.0297 0.0293  885  LEU   C CG  
8752  C  CD1 . LEU   C 20  ? 1.3897 1.0718 0.9317 0.0457  -0.0124 0.0322  885  LEU   C CD1 
8753  C  CD2 . LEU   C 20  ? 1.4367 1.1438 1.0047 0.0416  -0.0351 0.0287  885  LEU   C CD2 
8754  N  N   . SER   C 21  ? 1.5592 1.1976 1.0527 0.0569  -0.0026 0.0401  886  SER   C N   
8755  C  CA  . SER   C 21  ? 1.5646 1.2033 1.0642 0.0549  0.0138  0.0440  886  SER   C CA  
8756  C  C   . SER   C 21  ? 1.5626 1.2049 1.0685 0.0539  0.0137  0.0461  886  SER   C C   
8757  O  O   . SER   C 21  ? 1.5877 1.2439 1.1145 0.0490  0.0221  0.0480  886  SER   C O   
8758  C  CB  . SER   C 21  ? 1.6003 1.2137 1.0717 0.0605  0.0250  0.0465  886  SER   C CB  
8759  O  OG  . SER   C 21  ? 1.6557 1.2485 1.0985 0.0673  0.0153  0.0455  886  SER   C OG  
8760  N  N   . SER   C 22  ? 1.5410 1.1704 1.0286 0.0586  0.0043  0.0458  887  SER   C N   
8761  C  CA  . SER   C 22  ? 1.5509 1.1843 1.0448 0.0578  0.0027  0.0475  887  SER   C CA  
8762  C  C   . SER   C 22  ? 1.5512 1.2117 1.0763 0.0517  -0.0055 0.0454  887  SER   C C   
8763  O  O   . SER   C 22  ? 1.6273 1.2980 1.1675 0.0486  -0.0018 0.0471  887  SER   C O   
8764  C  CB  . SER   C 22  ? 1.5787 1.1927 1.0465 0.0646  -0.0068 0.0473  887  SER   C CB  
8765  O  OG  . SER   C 22  ? 1.5456 1.1707 1.0220 0.0640  -0.0236 0.0435  887  SER   C OG  
8766  N  N   . HIS   C 23  ? 1.5472 1.2192 1.0820 0.0501  -0.0166 0.0416  888  HIS   C N   
8767  C  CA  . HIS   C 23  ? 1.5130 1.2113 1.0786 0.0440  -0.0224 0.0398  888  HIS   C CA  
8768  C  C   . HIS   C 23  ? 1.5948 1.3080 1.1823 0.0383  -0.0101 0.0411  888  HIS   C C   
8769  O  O   . HIS   C 23  ? 1.6301 1.3611 1.2406 0.0336  -0.0096 0.0415  888  HIS   C O   
8770  C  CB  . HIS   C 23  ? 1.4515 1.1584 1.0229 0.0434  -0.0358 0.0357  888  HIS   C CB  
8771  C  CG  . HIS   C 23  ? 1.4479 1.1814 1.0508 0.0370  -0.0405 0.0339  888  HIS   C CG  
8772  N  ND1 . HIS   C 23  ? 1.4993 1.2460 1.1187 0.0344  -0.0425 0.0347  888  HIS   C ND1 
8773  C  CD2 . HIS   C 23  ? 1.4673 1.2161 1.0872 0.0331  -0.0435 0.0314  888  HIS   C CD2 
8774  C  CE1 . HIS   C 23  ? 1.4635 1.2320 1.1083 0.0292  -0.0464 0.0328  888  HIS   C CE1 
8775  N  NE2 . HIS   C 23  ? 1.4214 1.1916 1.0672 0.0283  -0.0469 0.0308  888  HIS   C NE2 
8776  N  N   . ALA   C 24  ? 1.7445 1.4504 1.3252 0.0387  -0.0002 0.0419  889  ALA   C N   
8777  C  CA  . ALA   C 24  ? 1.7407 1.4615 1.3433 0.0333  0.0104  0.0426  889  ALA   C CA  
8778  C  C   . ALA   C 24  ? 1.7520 1.4770 1.3652 0.0309  0.0201  0.0458  889  ALA   C C   
8779  O  O   . ALA   C 24  ? 1.7606 1.5042 1.3990 0.0254  0.0239  0.0458  889  ALA   C O   
8780  C  CB  . ALA   C 24  ? 1.7585 1.4681 1.3492 0.0351  0.0201  0.0431  889  ALA   C CB  
8781  N  N   . ARG   C 25  ? 1.6447 1.3521 1.2386 0.0349  0.0235  0.0485  890  ARG   C N   
8782  C  CA  . ARG   C 25  ? 1.6464 1.3570 1.2495 0.0328  0.0310  0.0514  890  ARG   C CA  
8783  C  C   . ARG   C 25  ? 1.6542 1.3858 1.2810 0.0286  0.0220  0.0499  890  ARG   C C   
8784  O  O   . ARG   C 25  ? 1.6925 1.4389 1.3414 0.0237  0.0278  0.0506  890  ARG   C O   
8785  C  CB  . ARG   C 25  ? 1.6094 1.2968 1.1858 0.0385  0.0334  0.0542  890  ARG   C CB  
8786  N  N   . SER   C 26  ? 1.6049 1.3379 1.2275 0.0306  0.0077  0.0476  891  SER   C N   
8787  C  CA  . SER   C 26  ? 1.5894 1.3385 1.2299 0.0279  -0.0011 0.0465  891  SER   C CA  
8788  C  C   . SER   C 26  ? 1.6151 1.3891 1.2862 0.0215  -0.0012 0.0449  891  SER   C C   
8789  O  O   . SER   C 26  ? 1.6002 1.3884 1.2874 0.0191  -0.0076 0.0441  891  SER   C O   
8790  C  CB  . SER   C 26  ? 1.4881 1.2339 1.1185 0.0315  -0.0165 0.0440  891  SER   C CB  
8791  O  OG  . SER   C 26  ? 1.4139 1.1748 1.0587 0.0288  -0.0251 0.0406  891  SER   C OG  
8792  N  N   . HIS   C 27  ? 1.5936 1.3731 1.2729 0.0189  0.0058  0.0443  892  HIS   C N   
8793  C  CA  . HIS   C 27  ? 1.5711 1.3730 1.2783 0.0131  0.0060  0.0428  892  HIS   C CA  
8794  C  C   . HIS   C 27  ? 1.6829 1.4909 1.4046 0.0095  0.0184  0.0450  892  HIS   C C   
8795  O  O   . HIS   C 27  ? 1.7053 1.5313 1.4501 0.0049  0.0192  0.0438  892  HIS   C O   
8796  C  CB  . HIS   C 27  ? 1.5285 1.3347 1.2383 0.0122  0.0045  0.0404  892  HIS   C CB  
8797  C  CG  . HIS   C 27  ? 1.4778 1.2875 1.1854 0.0134  -0.0097 0.0373  892  HIS   C CG  
8798  N  ND1 . HIS   C 27  ? 1.4156 1.2369 1.1345 0.0123  -0.0201 0.0360  892  HIS   C ND1 
8799  C  CD2 . HIS   C 27  ? 1.4647 1.2676 1.1606 0.0157  -0.0151 0.0352  892  HIS   C CD2 
8800  C  CE1 . HIS   C 27  ? 1.4120 1.2339 1.1270 0.0136  -0.0312 0.0334  892  HIS   C CE1 
8801  N  NE2 . HIS   C 27  ? 1.4163 1.2270 1.1172 0.0156  -0.0287 0.0328  892  HIS   C NE2 
8802  N  N   . LEU   C 28  ? 1.7678 1.5610 1.4766 0.0116  0.0280  0.0482  893  LEU   C N   
8803  C  CA  . LEU   C 28  ? 1.8238 1.6224 1.5469 0.0082  0.0391  0.0504  893  LEU   C CA  
8804  C  C   . LEU   C 28  ? 1.7216 1.5064 1.4314 0.0107  0.0423  0.0534  893  LEU   C C   
8805  O  O   . LEU   C 28  ? 1.6751 1.4634 1.3867 0.0111  0.0342  0.0531  893  LEU   C O   
8806  C  CB  . LEU   C 28  ? 1.8268 1.6221 1.5513 0.0070  0.0518  0.0514  893  LEU   C CB  
8807  C  CG  . LEU   C 28  ? 1.7166 1.5306 1.4650 0.0023  0.0536  0.0493  893  LEU   C CG  
8808  C  CD1 . LEU   C 28  ? 1.7488 1.5551 1.4929 0.0027  0.0660  0.0505  893  LEU   C CD1 
8809  C  CD2 . LEU   C 28  ? 1.6186 1.4499 1.3925 -0.0026 0.0548  0.0492  893  LEU   C CD2 
8810  N  N   . ASP   D 6   ? 1.7365 1.6902 1.7537 -0.0671 -0.0240 0.0094  75   ASP   D N   
8811  C  CA  . ASP   D 6   ? 1.8611 1.8157 1.8895 -0.0733 -0.0222 0.0121  75   ASP   D CA  
8812  C  C   . ASP   D 6   ? 1.8874 1.8480 1.9225 -0.0724 -0.0173 0.0154  75   ASP   D C   
8813  O  O   . ASP   D 6   ? 1.8163 1.7782 1.8453 -0.0668 -0.0155 0.0154  75   ASP   D O   
8814  C  CB  . ASP   D 6   ? 1.8548 1.7969 1.8787 -0.0752 -0.0195 0.0134  75   ASP   D CB  
8815  C  CG  . ASP   D 6   ? 1.8469 1.7894 1.8831 -0.0828 -0.0200 0.0148  75   ASP   D CG  
8816  O  OD1 . ASP   D 6   ? 1.7317 1.6730 1.7747 -0.0851 -0.0146 0.0184  75   ASP   D OD1 
8817  O  OD2 . ASP   D 6   ? 1.8335 1.7770 1.8724 -0.0863 -0.0258 0.0123  75   ASP   D OD2 
8818  N  N   . ASP   D 7   ? 2.0999 2.0644 2.1479 -0.0777 -0.0153 0.0180  76   ASP   D N   
8819  C  CA  . ASP   D 7   ? 2.1010 2.0710 2.1564 -0.0772 -0.0101 0.0215  76   ASP   D CA  
8820  C  C   . ASP   D 7   ? 2.0296 1.9969 2.0950 -0.0823 -0.0054 0.0250  76   ASP   D C   
8821  O  O   . ASP   D 7   ? 2.0369 2.0118 2.1140 -0.0844 -0.0028 0.0274  76   ASP   D O   
8822  C  CB  . ASP   D 7   ? 2.1520 2.1354 2.2167 -0.0778 -0.0134 0.0207  76   ASP   D CB  
8823  C  CG  . ASP   D 7   ? 2.2073 2.1942 2.2639 -0.0731 -0.0176 0.0175  76   ASP   D CG  
8824  O  OD1 . ASP   D 7   ? 2.2036 2.1892 2.2525 -0.0675 -0.0149 0.0178  76   ASP   D OD1 
8825  O  OD2 . ASP   D 7   ? 2.2165 2.2074 2.2748 -0.0750 -0.0235 0.0146  76   ASP   D OD2 
8826  N  N   . SER   D 8   ? 1.8563 1.8130 1.9176 -0.0843 -0.0040 0.0254  77   SER   D N   
8827  C  CA  . SER   D 8   ? 1.8603 1.8143 1.9323 -0.0898 0.0002  0.0286  77   SER   D CA  
8828  C  C   . SER   D 8   ? 1.8356 1.7863 1.9070 -0.0873 0.0093  0.0329  77   SER   D C   
8829  O  O   . SER   D 8   ? 1.7351 1.6807 1.7936 -0.0810 0.0124  0.0333  77   SER   D O   
8830  C  CB  . SER   D 8   ? 1.7703 1.7132 1.8377 -0.0927 -0.0010 0.0276  77   SER   D CB  
8831  O  OG  . SER   D 8   ? 1.6467 1.5880 1.7267 -0.0989 0.0021  0.0303  77   SER   D OG  
8832  N  N   . CYS   D 9   ? 1.9435 1.8971 2.0292 -0.0922 0.0135  0.0361  78   CYS   D N   
8833  C  CA  . CYS   D 9   ? 1.9507 1.9007 2.0375 -0.0906 0.0229  0.0407  78   CYS   D CA  
8834  C  C   . CYS   D 9   ? 1.9673 1.9066 2.0557 -0.0947 0.0272  0.0429  78   CYS   D C   
8835  O  O   . CYS   D 9   ? 1.9873 1.9299 2.0914 -0.1010 0.0285  0.0446  78   CYS   D O   
8836  C  CB  . CYS   D 9   ? 1.9583 1.9203 2.0614 -0.0929 0.0253  0.0431  78   CYS   D CB  
8837  S  SG  . CYS   D 9   ? 2.1081 2.0839 2.2129 -0.0902 0.0185  0.0401  78   CYS   D SG  
8838  N  N   . GLN   D 10  ? 1.7175 1.6438 1.7897 -0.0910 0.0292  0.0426  79   GLN   D N   
8839  C  CA  . GLN   D 10  ? 1.6448 1.5592 1.7158 -0.0942 0.0333  0.0445  79   GLN   D CA  
8840  C  C   . GLN   D 10  ? 1.5294 1.4349 1.5944 -0.0908 0.0438  0.0491  79   GLN   D C   
8841  O  O   . GLN   D 10  ? 1.5465 1.4543 1.6065 -0.0855 0.0473  0.0505  79   GLN   D O   
8842  C  CB  . GLN   D 10  ? 1.6415 1.5464 1.6980 -0.0924 0.0279  0.0409  79   GLN   D CB  
8843  C  CG  . GLN   D 10  ? 1.6805 1.5936 1.7410 -0.0948 0.0178  0.0363  79   GLN   D CG  
8844  C  CD  . GLN   D 10  ? 1.7271 1.6312 1.7726 -0.0924 0.0127  0.0326  79   GLN   D CD  
8845  O  OE1 . GLN   D 10  ? 1.6944 1.5900 1.7241 -0.0863 0.0148  0.0324  79   GLN   D OE1 
8846  N  NE2 . GLN   D 10  ? 1.7907 1.6966 1.8410 -0.0969 0.0056  0.0296  79   GLN   D NE2 
8847  N  N   . VAL   D 11  ? 1.5211 1.4160 1.5867 -0.0940 0.0490  0.0516  80   VAL   D N   
8848  C  CA  . VAL   D 11  ? 1.5278 1.4126 1.5878 -0.0914 0.0598  0.0564  80   VAL   D CA  
8849  C  C   . VAL   D 11  ? 1.5130 1.3811 1.5574 -0.0896 0.0615  0.0563  80   VAL   D C   
8850  O  O   . VAL   D 11  ? 1.5101 1.3727 1.5604 -0.0953 0.0617  0.0567  80   VAL   D O   
8851  C  CB  . VAL   D 11  ? 1.5605 1.4491 1.6398 -0.0976 0.0667  0.0606  80   VAL   D CB  
8852  C  CG1 . VAL   D 11  ? 1.5342 1.4125 1.6063 -0.0938 0.0787  0.0658  80   VAL   D CG1 
8853  C  CG2 . VAL   D 11  ? 1.5274 1.4335 1.6241 -0.1002 0.0634  0.0601  80   VAL   D CG2 
8854  N  N   . ILE   D 12  ? 1.5249 1.3844 1.5495 -0.0816 0.0628  0.0558  81   ILE   D N   
8855  C  CA  . ILE   D 12  ? 1.5355 1.3797 1.5427 -0.0786 0.0625  0.0548  81   ILE   D CA  
8856  C  C   . ILE   D 12  ? 1.5641 1.3941 1.5594 -0.0741 0.0728  0.0592  81   ILE   D C   
8857  O  O   . ILE   D 12  ? 1.5961 1.4281 1.5893 -0.0698 0.0780  0.0617  81   ILE   D O   
8858  C  CB  . ILE   D 12  ? 1.5583 1.4037 1.5516 -0.0725 0.0542  0.0499  81   ILE   D CB  
8859  C  CG1 . ILE   D 12  ? 1.5641 1.4225 1.5686 -0.0770 0.0445  0.0457  81   ILE   D CG1 
8860  C  CG2 . ILE   D 12  ? 1.5551 1.3844 1.5292 -0.0682 0.0542  0.0488  81   ILE   D CG2 
8861  C  CD1 . ILE   D 12  ? 1.5460 1.4122 1.5438 -0.0716 0.0378  0.0418  81   ILE   D CD1 
8862  N  N   . PRO   D 13  ? 1.5382 1.3533 1.5252 -0.0749 0.0764  0.0606  82   PRO   D N   
8863  C  CA  . PRO   D 13  ? 1.5704 1.3702 1.5430 -0.0697 0.0860  0.0646  82   PRO   D CA  
8864  C  C   . PRO   D 13  ? 1.5409 1.3332 1.4911 -0.0599 0.0835  0.0624  82   PRO   D C   
8865  O  O   . PRO   D 13  ? 1.5622 1.3556 1.5051 -0.0577 0.0750  0.0578  82   PRO   D O   
8866  C  CB  . PRO   D 13  ? 1.5438 1.3306 1.5154 -0.0742 0.0891  0.0660  82   PRO   D CB  
8867  C  CG  . PRO   D 13  ? 1.6067 1.3990 1.5828 -0.0782 0.0785  0.0611  82   PRO   D CG  
8868  C  CD  . PRO   D 13  ? 1.5368 1.3484 1.5292 -0.0813 0.0725  0.0589  82   PRO   D CD  
8869  N  N   . VAL   D 14  ? 1.5652 1.3491 1.5043 -0.0538 0.0913  0.0658  83   VAL   D N   
8870  C  CA  . VAL   D 14  ? 1.6583 1.4359 1.5773 -0.0439 0.0894  0.0641  83   VAL   D CA  
8871  C  C   . VAL   D 14  ? 1.7789 1.5359 1.6780 -0.0394 0.0936  0.0654  83   VAL   D C   
8872  O  O   . VAL   D 14  ? 1.8778 1.6240 1.7760 -0.0410 0.1030  0.0701  83   VAL   D O   
8873  C  CB  . VAL   D 14  ? 1.7039 1.4852 1.6220 -0.0393 0.0946  0.0667  83   VAL   D CB  
8874  C  CG1 . VAL   D 14  ? 1.7024 1.4763 1.5992 -0.0289 0.0918  0.0646  83   VAL   D CG1 
8875  C  CG2 . VAL   D 14  ? 1.6965 1.4976 1.6344 -0.0438 0.0910  0.0657  83   VAL   D CG2 
8876  N  N   . LEU   D 15  ? 1.7320 1.4833 1.6151 -0.0332 0.0869  0.0614  84   LEU   D N   
8877  C  CA  . LEU   D 15  ? 1.8491 1.5805 1.7103 -0.0266 0.0907  0.0626  84   LEU   D CA  
8878  C  C   . LEU   D 15  ? 1.9588 1.6826 1.8112 -0.0209 0.0996  0.0669  84   LEU   D C   
8879  O  O   . LEU   D 15  ? 1.9843 1.7139 1.8326 -0.0152 0.0971  0.0656  84   LEU   D O   
8880  C  CB  . LEU   D 15  ? 1.8122 1.5408 1.6583 -0.0197 0.0816  0.0574  84   LEU   D CB  
8881  C  CG  . LEU   D 15  ? 1.7069 1.4272 1.5463 -0.0208 0.0769  0.0546  84   LEU   D CG  
8882  C  CD1 . LEU   D 15  ? 1.6429 1.3586 1.4651 -0.0119 0.0698  0.0502  84   LEU   D CD1 
8883  C  CD2 . LEU   D 15  ? 1.6509 1.3534 1.4832 -0.0227 0.0850  0.0586  84   LEU   D CD2 
8884  N  N   . PRO   D 16  ? 2.1810 1.8918 2.0304 -0.0223 0.1102  0.0722  85   PRO   D N   
8885  C  CA  . PRO   D 16  ? 2.2475 1.9532 2.0924 -0.0183 0.1199  0.0769  85   PRO   D CA  
8886  C  C   . PRO   D 16  ? 2.2507 1.9474 2.0735 -0.0070 0.1186  0.0758  85   PRO   D C   
8887  O  O   . PRO   D 16  ? 2.2573 1.9611 2.0812 -0.0035 0.1192  0.0762  85   PRO   D O   
8888  C  CB  . PRO   D 16  ? 2.2824 1.9725 2.1249 -0.0215 0.1308  0.0822  85   PRO   D CB  
8889  C  CG  . PRO   D 16  ? 2.2690 1.9642 2.1260 -0.0306 0.1268  0.0806  85   PRO   D CG  
8890  C  CD  . PRO   D 16  ? 2.2225 1.9230 2.0737 -0.0280 0.1141  0.0741  85   PRO   D CD  
8891  N  N   . GLN   D 17  ? 2.1340 1.8148 1.9364 -0.0009 0.1167  0.0743  86   GLN   D N   
8892  C  CA  . GLN   D 17  ? 2.0830 1.7548 1.8640 0.0102  0.1141  0.0726  86   GLN   D CA  
8893  C  C   . GLN   D 17  ? 2.1211 1.8034 1.9022 0.0123  0.1010  0.0659  86   GLN   D C   
8894  O  O   . GLN   D 17  ? 2.1226 1.7965 1.8915 0.0158  0.0956  0.0628  86   GLN   D O   
8895  C  CB  . GLN   D 17  ? 2.0528 1.7005 1.8107 0.0163  0.1198  0.0749  86   GLN   D CB  
8896  C  CG  . GLN   D 17  ? 2.0460 1.6820 1.8036 0.0139  0.1337  0.0819  86   GLN   D CG  
8897  C  CD  . GLN   D 17  ? 1.9704 1.5809 1.7038 0.0201  0.1398  0.0844  86   GLN   D CD  
8898  O  OE1 . GLN   D 17  ? 1.9802 1.5822 1.7018 0.0228  0.1339  0.0813  86   GLN   D OE1 
8899  N  NE2 . GLN   D 17  ? 1.9228 1.5210 1.6488 0.0225  0.1518  0.0902  86   GLN   D NE2 
8900  N  N   . VAL   D 18  ? 2.1805 1.8818 1.9765 0.0100  0.0960  0.0637  87   VAL   D N   
8901  C  CA  . VAL   D 18  ? 2.1318 1.8448 1.9303 0.0116  0.0842  0.0577  87   VAL   D CA  
8902  C  C   . VAL   D 18  ? 2.1284 1.8460 1.9214 0.0188  0.0816  0.0563  87   VAL   D C   
8903  O  O   . VAL   D 18  ? 2.1314 1.8485 1.9248 0.0202  0.0883  0.0599  87   VAL   D O   
8904  C  CB  . VAL   D 18  ? 2.1206 1.8525 1.9423 0.0019  0.0795  0.0557  87   VAL   D CB  
8905  C  CG1 . VAL   D 18  ? 2.1094 1.8577 1.9466 -0.0007 0.0802  0.0567  87   VAL   D CG1 
8906  C  CG2 . VAL   D 18  ? 2.0666 1.8044 1.8877 0.0026  0.0685  0.0498  87   VAL   D CG2 
8907  N  N   . MET   D 19  ? 2.0264 1.7481 1.8139 0.0237  0.0718  0.0510  88   MET   D N   
8908  C  CA  . MET   D 19  ? 1.9955 1.7212 1.7773 0.0309  0.0680  0.0490  88   MET   D CA  
8909  C  C   . MET   D 19  ? 1.9159 1.6503 1.6983 0.0335  0.0565  0.0427  88   MET   D C   
8910  O  O   . MET   D 19  ? 1.8999 1.6306 1.6704 0.0418  0.0518  0.0400  88   MET   D O   
8911  C  CB  . MET   D 19  ? 2.0164 1.7226 1.7755 0.0404  0.0727  0.0511  88   MET   D CB  
8912  C  CG  . MET   D 19  ? 2.0246 1.7156 1.7658 0.0461  0.0690  0.0486  88   MET   D CG  
8913  S  SD  . MET   D 19  ? 2.0901 1.7555 1.8117 0.0496  0.0800  0.0541  88   MET   D SD  
8914  C  CE  . MET   D 19  ? 2.0900 1.7583 1.8274 0.0376  0.0849  0.0568  88   MET   D CE  
8915  N  N   . MET   D 20  ? 1.8801 1.6258 1.6763 0.0266  0.0518  0.0402  89   MET   D N   
8916  C  CA  . MET   D 20  ? 1.8200 1.5720 1.6160 0.0289  0.0417  0.0345  89   MET   D CA  
8917  C  C   . MET   D 20  ? 1.7562 1.5290 1.5702 0.0246  0.0363  0.0320  89   MET   D C   
8918  O  O   . MET   D 20  ? 1.7585 1.5413 1.5863 0.0189  0.0399  0.0345  89   MET   D O   
8919  C  CB  . MET   D 20  ? 1.7921 1.5385 1.5865 0.0257  0.0398  0.0331  89   MET   D CB  
8920  C  CG  . MET   D 20  ? 1.8097 1.5560 1.5969 0.0311  0.0308  0.0275  89   MET   D CG  
8921  S  SD  . MET   D 20  ? 1.8577 1.6069 1.6519 0.0247  0.0266  0.0249  89   MET   D SD  
8922  C  CE  . MET   D 20  ? 1.8299 1.5797 1.6156 0.0326  0.0165  0.0185  89   MET   D CE  
8923  N  N   . ILE   D 21  ? 1.6630 1.4418 1.4765 0.0277  0.0277  0.0269  90   ILE   D N   
8924  C  CA  . ILE   D 21  ? 1.5487 1.3460 1.3782 0.0234  0.0218  0.0238  90   ILE   D CA  
8925  C  C   . ILE   D 21  ? 1.5216 1.3200 1.3535 0.0203  0.0170  0.0207  90   ILE   D C   
8926  O  O   . ILE   D 21  ? 1.5124 1.3089 1.3374 0.0253  0.0109  0.0166  90   ILE   D O   
8927  C  CB  . ILE   D 21  ? 1.5014 1.3053 1.3291 0.0298  0.0161  0.0205  90   ILE   D CB  
8928  C  CG1 . ILE   D 21  ? 1.4466 1.2513 1.2747 0.0313  0.0211  0.0239  90   ILE   D CG1 
8929  C  CG2 . ILE   D 21  ? 1.4675 1.2885 1.3095 0.0263  0.0092  0.0166  90   ILE   D CG2 
8930  C  CD1 . ILE   D 21  ? 1.3916 1.2000 1.2158 0.0382  0.0160  0.0210  90   ILE   D CD1 
8931  N  N   . LEU   D 22  ? 1.4869 1.2878 1.3285 0.0122  0.0197  0.0226  91   LEU   D N   
8932  C  CA  . LEU   D 22  ? 1.4151 1.2161 1.2588 0.0088  0.0158  0.0200  91   LEU   D CA  
8933  C  C   . LEU   D 22  ? 1.3261 1.1440 1.1832 0.0056  0.0092  0.0164  91   LEU   D C   
8934  O  O   . LEU   D 22  ? 1.3012 1.1301 1.1726 -0.0012 0.0100  0.0176  91   LEU   D O   
8935  C  CB  . LEU   D 22  ? 1.3905 1.1862 1.2387 0.0015  0.0212  0.0234  91   LEU   D CB  
8936  C  CG  . LEU   D 22  ? 1.3706 1.1649 1.2200 -0.0021 0.0173  0.0209  91   LEU   D CG  
8937  C  CD1 . LEU   D 22  ? 1.4254 1.2091 1.2590 0.0053  0.0135  0.0178  91   LEU   D CD1 
8938  C  CD2 . LEU   D 22  ? 1.3730 1.1595 1.2249 -0.0084 0.0230  0.0246  91   LEU   D CD2 
8939  N  N   . ILE   D 23  ? 1.3073 1.1273 1.1599 0.0106  0.0028  0.0120  92   ILE   D N   
8940  C  CA  . ILE   D 23  ? 1.3225 1.1574 1.1869 0.0077  -0.0030 0.0085  92   ILE   D CA  
8941  C  C   . ILE   D 23  ? 1.3655 1.2001 1.2343 0.0017  -0.0043 0.0077  92   ILE   D C   
8942  O  O   . ILE   D 23  ? 1.3710 1.1936 1.2297 0.0034  -0.0040 0.0072  92   ILE   D O   
8943  C  CB  . ILE   D 23  ? 1.3278 1.1649 1.1870 0.0149  -0.0091 0.0040  92   ILE   D CB  
8944  C  CG1 . ILE   D 23  ? 1.2665 1.1063 1.1240 0.0201  -0.0089 0.0045  92   ILE   D CG1 
8945  C  CG2 . ILE   D 23  ? 1.2746 1.1251 1.1448 0.0119  -0.0147 0.0004  92   ILE   D CG2 
8946  C  CD1 . ILE   D 23  ? 1.2396 1.0812 1.0927 0.0271  -0.0151 0.0000  92   ILE   D CD1 
8947  N  N   . PRO   D 24  ? 1.3404 1.1873 1.2234 -0.0051 -0.0058 0.0074  93   PRO   D N   
8948  C  CA  . PRO   D 24  ? 1.2354 1.0814 1.1222 -0.0110 -0.0072 0.0067  93   PRO   D CA  
8949  C  C   . PRO   D 24  ? 1.2998 1.1399 1.1773 -0.0068 -0.0115 0.0028  93   PRO   D C   
8950  O  O   . PRO   D 24  ? 1.3160 1.1608 1.1916 -0.0017 -0.0157 -0.0004 93   PRO   D O   
8951  C  CB  . PRO   D 24  ? 1.1669 1.0287 1.0689 -0.0164 -0.0100 0.0057  93   PRO   D CB  
8952  C  CG  . PRO   D 24  ? 1.1970 1.0656 1.1045 -0.0158 -0.0073 0.0080  93   PRO   D CG  
8953  C  CD  . PRO   D 24  ? 1.2949 1.1564 1.1904 -0.0076 -0.0064 0.0078  93   PRO   D CD  
8954  N  N   . GLY   D 25  ? 1.4128 1.2420 1.2844 -0.0088 -0.0103 0.0034  94   GLY   D N   
8955  C  CA  . GLY   D 25  ? 1.4649 1.2872 1.3273 -0.0051 -0.0141 0.0000  94   GLY   D CA  
8956  C  C   . GLY   D 25  ? 1.5056 1.3122 1.3524 0.0011  -0.0117 0.0008  94   GLY   D C   
8957  O  O   . GLY   D 25  ? 1.4943 1.2900 1.3331 0.0012  -0.0118 0.0003  94   GLY   D O   
8958  N  N   . GLN   D 26  ? 1.4810 1.2859 1.3226 0.0066  -0.0099 0.0019  95   GLN   D N   
8959  C  CA  . GLN   D 26  ? 1.4722 1.2612 1.2981 0.0127  -0.0073 0.0031  95   GLN   D CA  
8960  C  C   . GLN   D 26  ? 1.4737 1.2509 1.2962 0.0081  -0.0017 0.0068  95   GLN   D C   
8961  O  O   . GLN   D 26  ? 1.4862 1.2674 1.3184 0.0013  0.0023  0.0100  95   GLN   D O   
8962  C  CB  . GLN   D 26  ? 1.5362 1.3251 1.3587 0.0177  -0.0049 0.0048  95   GLN   D CB  
8963  C  CG  . GLN   D 26  ? 1.5593 1.3532 1.3787 0.0254  -0.0104 0.0010  95   GLN   D CG  
8964  C  CD  . GLN   D 26  ? 1.5230 1.3137 1.3364 0.0309  -0.0080 0.0029  95   GLN   D CD  
8965  O  OE1 . GLN   D 26  ? 1.5142 1.3056 1.3313 0.0276  -0.0026 0.0069  95   GLN   D OE1 
8966  N  NE2 . GLN   D 26  ? 1.4504 1.2373 1.2544 0.0394  -0.0121 0.0000  95   GLN   D NE2 
8967  N  N   . THR   D 27  ? 1.3983 1.1610 1.2073 0.0116  -0.0016 0.0062  96   THR   D N   
8968  C  CA  . THR   D 27  ? 1.3679 1.1173 1.1718 0.0081  0.0041  0.0099  96   THR   D CA  
8969  C  C   . THR   D 27  ? 1.3730 1.1114 1.1663 0.0128  0.0100  0.0135  96   THR   D C   
8970  O  O   . THR   D 27  ? 1.4044 1.1394 1.1878 0.0208  0.0083  0.0121  96   THR   D O   
8971  C  CB  . THR   D 27  ? 1.3749 1.1129 1.1691 0.0093  0.0019  0.0078  96   THR   D CB  
8972  O  OG1 . THR   D 27  ? 1.5146 1.2409 1.2924 0.0185  0.0011  0.0066  96   THR   D OG1 
8973  C  CG2 . THR   D 27  ? 1.3805 1.1289 1.1822 0.0072  -0.0047 0.0034  96   THR   D CG2 
8974  N  N   . LEU   D 28  ? 1.3395 1.0720 1.1350 0.0077  0.0170  0.0181  97   LEU   D N   
8975  C  CA  . LEU   D 28  ? 1.3504 1.0725 1.1368 0.0114  0.0239  0.0222  97   LEU   D CA  
8976  C  C   . LEU   D 28  ? 1.3973 1.1006 1.1717 0.0114  0.0290  0.0248  97   LEU   D C   
8977  O  O   . LEU   D 28  ? 1.4510 1.1523 1.2329 0.0039  0.0338  0.0280  97   LEU   D O   
8978  C  CB  . LEU   D 28  ? 1.3315 1.0633 1.1320 0.0055  0.0290  0.0259  97   LEU   D CB  
8979  C  CG  . LEU   D 28  ? 1.3150 1.0354 1.1076 0.0078  0.0377  0.0310  97   LEU   D CG  
8980  C  CD1 . LEU   D 28  ? 1.3742 1.0926 1.1557 0.0171  0.0363  0.0299  97   LEU   D CD1 
8981  C  CD2 . LEU   D 28  ? 1.3373 1.0663 1.1461 0.0000  0.0435  0.0349  97   LEU   D CD2 
8982  N  N   . PRO   D 29  ? 1.3792 1.0679 1.1351 0.0195  0.0283  0.0238  98   PRO   D N   
8983  C  CA  . PRO   D 29  ? 1.3748 1.0442 1.1179 0.0199  0.0336  0.0266  98   PRO   D CA  
8984  C  C   . PRO   D 29  ? 1.4123 1.0745 1.1548 0.0178  0.0434  0.0325  98   PRO   D C   
8985  O  O   . PRO   D 29  ? 1.4359 1.1052 1.1832 0.0187  0.0459  0.0343  98   PRO   D O   
8986  C  CB  . PRO   D 29  ? 1.4055 1.0629 1.1291 0.0305  0.0300  0.0239  98   PRO   D CB  
8987  C  CG  . PRO   D 29  ? 1.4606 1.1286 1.1860 0.0359  0.0261  0.0219  98   PRO   D CG  
8988  C  CD  . PRO   D 29  ? 1.3957 1.0847 1.1418 0.0290  0.0227  0.0202  98   PRO   D CD  
8989  N  N   . LEU   D 30  ? 1.4279 1.0753 1.1643 0.0151  0.0494  0.0358  99   LEU   D N   
8990  C  CA  . LEU   D 30  ? 1.5024 1.1436 1.2410 0.0115  0.0596  0.0417  99   LEU   D CA  
8991  C  C   . LEU   D 30  ? 1.6501 1.2710 1.3766 0.0111  0.0653  0.0446  99   LEU   D C   
8992  O  O   . LEU   D 30  ? 1.6793 1.2968 1.4059 0.0080  0.0619  0.0426  99   LEU   D O   
8993  C  CB  . LEU   D 30  ? 1.5130 1.1706 1.2752 0.0012  0.0611  0.0432  99   LEU   D CB  
8994  C  CG  . LEU   D 30  ? 1.5024 1.1670 1.2744 -0.0010 0.0679  0.0474  99   LEU   D CG  
8995  C  CD1 . LEU   D 30  ? 1.5220 1.1897 1.2861 0.0073  0.0660  0.0463  99   LEU   D CD1 
8996  C  CD2 . LEU   D 30  ? 1.3985 1.0820 1.1940 -0.0102 0.0661  0.0471  99   LEU   D CD2 
8997  N  N   . GLN   D 31  ? 1.7123 1.3191 1.4277 0.0144  0.0742  0.0493  100  GLN   D N   
8998  C  CA  . GLN   D 31  ? 1.7365 1.3230 1.4403 0.0138  0.0813  0.0529  100  GLN   D CA  
8999  C  C   . GLN   D 31  ? 1.8017 1.3837 1.5093 0.0108  0.0929  0.0593  100  GLN   D C   
9000  O  O   . GLN   D 31  ? 1.8513 1.4255 1.5467 0.0177  0.0976  0.0617  100  GLN   D O   
9001  C  CB  . GLN   D 31  ? 1.6522 1.2205 1.3307 0.0243  0.0795  0.0515  100  GLN   D CB  
9002  N  N   . LEU   D 32  ? 1.8451 1.4318 1.5698 0.0006  0.0976  0.0621  101  LEU   D N   
9003  C  CA  . LEU   D 32  ? 1.8868 1.4723 1.6199 -0.0037 0.1085  0.0681  101  LEU   D CA  
9004  C  C   . LEU   D 32  ? 2.0082 1.5710 1.7277 -0.0030 0.1183  0.0728  101  LEU   D C   
9005  O  O   . LEU   D 32  ? 2.0781 1.6276 1.7853 -0.0013 0.1162  0.0715  101  LEU   D O   
9006  C  CB  . LEU   D 32  ? 1.9081 1.5112 1.6683 -0.0152 0.1082  0.0685  101  LEU   D CB  
9007  C  CG  . LEU   D 32  ? 1.8081 1.4332 1.5831 -0.0177 0.0975  0.0633  101  LEU   D CG  
9008  C  CD1 . LEU   D 32  ? 1.7357 1.3627 1.5131 -0.0211 0.0888  0.0588  101  LEU   D CD1 
9009  C  CD2 . LEU   D 32  ? 1.7762 1.4188 1.5749 -0.0254 0.1001  0.0654  101  LEU   D CD2 
9010  N  N   . PHE   D 33  ? 2.0995 1.6578 1.8217 -0.0044 0.1295  0.0786  102  PHE   D N   
9011  C  CA  . PHE   D 33  ? 2.1324 1.6686 1.8416 -0.0035 0.1403  0.0839  102  PHE   D CA  
9012  C  C   . PHE   D 33  ? 2.1841 1.7225 1.9092 -0.0108 0.1521  0.0900  102  PHE   D C   
9013  O  O   . PHE   D 33  ? 2.1863 1.7185 1.9193 -0.0181 0.1577  0.0928  102  PHE   D O   
9014  C  CB  . PHE   D 33  ? 2.1086 1.6273 1.7901 0.0089  0.1427  0.0847  102  PHE   D CB  
9015  N  N   . HIS   D 34  ? 2.2475 1.7940 1.9773 -0.0086 0.1562  0.0921  103  HIS   D N   
9016  C  CA  . HIS   D 34  ? 2.2306 1.7817 1.9776 -0.0154 0.1671  0.0977  103  HIS   D CA  
9017  C  C   . HIS   D 34  ? 2.2503 1.8172 2.0249 -0.0277 0.1639  0.0966  103  HIS   D C   
9018  O  O   . HIS   D 34  ? 2.2217 1.8060 2.0078 -0.0302 0.1530  0.0915  103  HIS   D O   
9019  C  CB  . HIS   D 34  ? 2.0918 1.6535 1.8419 -0.0114 0.1690  0.0987  103  HIS   D CB  
9020  N  N   . PRO   D 35  ? 2.2797 1.8403 2.0649 -0.0353 0.1729  0.1011  104  PRO   D N   
9021  C  CA  . PRO   D 35  ? 2.2548 1.8278 2.0643 -0.0468 0.1686  0.0995  104  PRO   D CA  
9022  C  C   . PRO   D 35  ? 2.2428 1.8407 2.0772 -0.0525 0.1637  0.0977  104  PRO   D C   
9023  O  O   . PRO   D 35  ? 2.1893 1.7999 2.0376 -0.0585 0.1542  0.0934  104  PRO   D O   
9024  C  CB  . PRO   D 35  ? 2.2269 1.7872 2.0423 -0.0527 0.1813  0.1056  104  PRO   D CB  
9025  C  CG  . PRO   D 35  ? 2.3512 1.8874 2.1382 -0.0439 0.1881  0.1083  104  PRO   D CG  
9026  C  CD  . PRO   D 35  ? 2.3484 1.8861 2.1192 -0.0331 0.1855  0.1068  104  PRO   D CD  
9027  N  N   . GLN   D 36  ? 2.3622 1.9670 2.2024 -0.0508 0.1702  0.1009  105  GLN   D N   
9028  C  CA  . GLN   D 36  ? 2.3175 1.9457 2.1810 -0.0558 0.1659  0.0993  105  GLN   D CA  
9029  C  C   . GLN   D 36  ? 2.2904 1.9325 2.1550 -0.0548 0.1511  0.0924  105  GLN   D C   
9030  O  O   . GLN   D 36  ? 2.2541 1.9130 2.1394 -0.0620 0.1446  0.0898  105  GLN   D O   
9031  C  CB  . GLN   D 36  ? 2.2529 1.8841 2.1149 -0.0508 0.1734  0.1028  105  GLN   D CB  
9032  N  N   . GLU   D 37  ? 2.1793 1.8135 2.0214 -0.0456 0.1456  0.0892  106  GLU   D N   
9033  C  CA  . GLU   D 37  ? 2.0983 1.7436 1.9397 -0.0440 0.1321  0.0826  106  GLU   D CA  
9034  C  C   . GLU   D 37  ? 2.0697 1.7162 1.9196 -0.0513 0.1257  0.0797  106  GLU   D C   
9035  O  O   . GLU   D 37  ? 2.0013 1.6643 1.8691 -0.0575 0.1185  0.0766  106  GLU   D O   
9036  C  CB  . GLU   D 37  ? 2.0110 1.6453 1.8262 -0.0327 0.1284  0.0801  106  GLU   D CB  
9037  N  N   . VAL   D 38  ? 2.0895 1.7176 1.9265 -0.0507 0.1288  0.0808  107  VAL   D N   
9038  C  CA  . VAL   D 38  ? 2.0209 1.6472 1.8614 -0.0561 0.1221  0.0777  107  VAL   D CA  
9039  C  C   . VAL   D 38  ? 1.9863 1.6245 1.8535 -0.0678 0.1222  0.0785  107  VAL   D C   
9040  O  O   . VAL   D 38  ? 1.9198 1.5654 1.7957 -0.0727 0.1132  0.0743  107  VAL   D O   
9041  C  CB  . VAL   D 38  ? 1.9727 1.5754 1.7939 -0.0531 0.1273  0.0797  107  VAL   D CB  
9042  C  CG1 . VAL   D 38  ? 1.8918 1.4910 1.7119 -0.0565 0.1192  0.0756  107  VAL   D CG1 
9043  C  CG2 . VAL   D 38  ? 2.0184 1.6087 1.8137 -0.0411 0.1288  0.0798  107  VAL   D CG2 
9044  N  N   . SER   D 39  ? 2.0272 1.6670 1.9076 -0.0722 0.1320  0.0836  108  SER   D N   
9045  C  CA  . SER   D 39  ? 1.9734 1.6249 1.8805 -0.0831 0.1321  0.0845  108  SER   D CA  
9046  C  C   . SER   D 39  ? 1.9387 1.6124 1.8613 -0.0856 0.1222  0.0802  108  SER   D C   
9047  O  O   . SER   D 39  ? 1.8817 1.5645 1.8203 -0.0931 0.1154  0.0775  108  SER   D O   
9048  C  CB  . SER   D 39  ? 2.0300 1.6796 1.9483 -0.0864 0.1452  0.0910  108  SER   D CB  
9049  O  OG  . SER   D 39  ? 2.0783 1.7067 1.9794 -0.0824 0.1554  0.0953  108  SER   D OG  
9050  N  N   . MET   D 40  ? 1.9810 1.6630 1.8987 -0.0792 0.1212  0.0795  109  MET   D N   
9051  C  CA  . MET   D 40  ? 1.9917 1.6938 1.9216 -0.0805 0.1117  0.0754  109  MET   D CA  
9052  C  C   . MET   D 40  ? 1.9696 1.6731 1.8920 -0.0793 0.0997  0.0693  109  MET   D C   
9053  O  O   . MET   D 40  ? 1.9329 1.6494 1.8697 -0.0848 0.0916  0.0659  109  MET   D O   
9054  C  CB  . MET   D 40  ? 1.9784 1.6871 1.9024 -0.0732 0.1136  0.0761  109  MET   D CB  
9055  N  N   . VAL   D 41  ? 1.9418 1.6314 1.8413 -0.0718 0.0986  0.0679  110  VAL   D N   
9056  C  CA  . VAL   D 41  ? 1.8736 1.5631 1.7644 -0.0698 0.0880  0.0622  110  VAL   D CA  
9057  C  C   . VAL   D 41  ? 1.8716 1.5610 1.7742 -0.0786 0.0840  0.0608  110  VAL   D C   
9058  O  O   . VAL   D 41  ? 1.8189 1.5204 1.7312 -0.0821 0.0750  0.0566  110  VAL   D O   
9059  C  CB  . VAL   D 41  ? 1.8621 1.5340 1.7269 -0.0609 0.0888  0.0617  110  VAL   D CB  
9060  C  CG1 . VAL   D 41  ? 1.7817 1.4553 1.6382 -0.0580 0.0779  0.0557  110  VAL   D CG1 
9061  C  CG2 . VAL   D 41  ? 1.8485 1.5181 1.7012 -0.0522 0.0936  0.0637  110  VAL   D CG2 
9062  N  N   . ARG   D 42  ? 1.9118 1.5867 1.8129 -0.0821 0.0909  0.0642  111  ARG   D N   
9063  C  CA  . ARG   D 42  ? 1.8857 1.5581 1.7969 -0.0903 0.0875  0.0630  111  ARG   D CA  
9064  C  C   . ARG   D 42  ? 1.8970 1.5877 1.8335 -0.0987 0.0830  0.0618  111  ARG   D C   
9065  O  O   . ARG   D 42  ? 1.9048 1.6008 1.8475 -0.1028 0.0739  0.0576  111  ARG   D O   
9066  C  CB  . ARG   D 42  ? 1.8372 1.4927 1.7462 -0.0933 0.0977  0.0679  111  ARG   D CB  
9067  N  N   . ASN   D 43  ? 1.8974 1.5978 1.8483 -0.1010 0.0890  0.0653  112  ASN   D N   
9068  C  CA  . ASN   D 43  ? 1.8998 1.6181 1.8747 -0.1083 0.0844  0.0640  112  ASN   D CA  
9069  C  C   . ASN   D 43  ? 1.9113 1.6436 1.8854 -0.1054 0.0735  0.0587  112  ASN   D C   
9070  O  O   . ASN   D 43  ? 1.8779 1.6202 1.8650 -0.1110 0.0654  0.0555  112  ASN   D O   
9071  C  CB  . ASN   D 43  ? 1.8715 1.5969 1.8610 -0.1105 0.0935  0.0690  112  ASN   D CB  
9072  C  CG  . ASN   D 43  ? 1.8554 1.5970 1.8715 -0.1192 0.0898  0.0683  112  ASN   D CG  
9073  O  OD1 . ASN   D 43  ? 1.8552 1.6006 1.8789 -0.1243 0.0811  0.0646  112  ASN   D OD1 
9074  N  ND2 . ASN   D 43  ? 1.8794 1.6303 1.9096 -0.1207 0.0963  0.0719  112  ASN   D ND2 
9075  N  N   . LEU   D 44  ? 1.9162 1.6491 1.8751 -0.0966 0.0731  0.0578  113  LEU   D N   
9076  C  CA  . LEU   D 44  ? 1.8564 1.6024 1.8143 -0.0935 0.0636  0.0530  113  LEU   D CA  
9077  C  C   . LEU   D 44  ? 1.8585 1.6014 1.8099 -0.0941 0.0541  0.0480  113  LEU   D C   
9078  O  O   . LEU   D 44  ? 1.8639 1.6186 1.8251 -0.0974 0.0459  0.0444  113  LEU   D O   
9079  C  CB  . LEU   D 44  ? 1.8045 1.5499 1.7467 -0.0837 0.0654  0.0531  113  LEU   D CB  
9080  C  CG  . LEU   D 44  ? 1.7556 1.5153 1.7065 -0.0820 0.0672  0.0543  113  LEU   D CG  
9081  C  CD1 . LEU   D 44  ? 1.6725 1.4308 1.6060 -0.0721 0.0660  0.0528  113  LEU   D CD1 
9082  C  CD2 . LEU   D 44  ? 1.7354 1.5132 1.7044 -0.0874 0.0595  0.0514  113  LEU   D CD2 
9083  N  N   . ILE   D 45  ? 1.8782 1.6045 1.8125 -0.0908 0.0552  0.0477  114  ILE   D N   
9084  C  CA  . ILE   D 45  ? 1.8192 1.5414 1.7452 -0.0903 0.0466  0.0429  114  ILE   D CA  
9085  C  C   . ILE   D 45  ? 1.8616 1.5889 1.8040 -0.0995 0.0412  0.0412  114  ILE   D C   
9086  O  O   . ILE   D 45  ? 1.8975 1.6298 1.8396 -0.1000 0.0322  0.0366  114  ILE   D O   
9087  C  CB  . ILE   D 45  ? 1.6940 1.3962 1.6004 -0.0860 0.0498  0.0436  114  ILE   D CB  
9088  C  CG1 . ILE   D 45  ? 1.7298 1.4259 1.6201 -0.0769 0.0553  0.0455  114  ILE   D CG1 
9089  C  CG2 . ILE   D 45  ? 1.5671 1.2657 1.4633 -0.0840 0.0410  0.0385  114  ILE   D CG2 
9090  C  CD1 . ILE   D 45  ? 1.7177 1.3940 1.5936 -0.0744 0.0625  0.0487  114  ILE   D CD1 
9091  N  N   . GLN   D 46  ? 1.8350 1.5612 1.7922 -0.1067 0.0467  0.0448  115  GLN   D N   
9092  C  CA  . GLN   D 46  ? 1.8164 1.5484 1.7914 -0.1157 0.0415  0.0433  115  GLN   D CA  
9093  C  C   . GLN   D 46  ? 1.8667 1.6182 1.8599 -0.1188 0.0379  0.0425  115  GLN   D C   
9094  O  O   . GLN   D 46  ? 1.8787 1.6364 1.8913 -0.1267 0.0373  0.0434  115  GLN   D O   
9095  C  CB  . GLN   D 46  ? 1.7388 1.4609 1.7229 -0.1224 0.0487  0.0474  115  GLN   D CB  
9096  N  N   . LYS   D 47  ? 1.8726 1.6338 1.8602 -0.1128 0.0353  0.0408  116  LYS   D N   
9097  C  CA  . LYS   D 47  ? 1.8959 1.6752 1.8990 -0.1149 0.0316  0.0399  116  LYS   D CA  
9098  C  C   . LYS   D 47  ? 1.9272 1.7144 1.9203 -0.1084 0.0250  0.0359  116  LYS   D C   
9099  O  O   . LYS   D 47  ? 1.9256 1.7086 1.9081 -0.1064 0.0184  0.0319  116  LYS   D O   
9100  C  CB  . LYS   D 47  ? 1.8496 1.6346 1.8634 -0.1156 0.0406  0.0448  116  LYS   D CB  
9101  N  N   . ASP   D 48  ? 1.9891 1.7875 1.9856 -0.1051 0.0270  0.0370  117  ASP   D N   
9102  C  CA  . ASP   D 48  ? 1.9782 1.7837 1.9653 -0.0986 0.0218  0.0336  117  ASP   D CA  
9103  C  C   . ASP   D 48  ? 2.0094 1.8036 1.9751 -0.0901 0.0240  0.0332  117  ASP   D C   
9104  O  O   . ASP   D 48  ? 2.0185 1.8164 1.9752 -0.0848 0.0188  0.0297  117  ASP   D O   
9105  C  CB  . ASP   D 48  ? 1.9598 1.7800 1.9573 -0.0977 0.0234  0.0350  117  ASP   D CB  
9106  C  CG  . ASP   D 48  ? 2.0213 1.8385 2.0217 -0.0971 0.0338  0.0404  117  ASP   D CG  
9107  O  OD1 . ASP   D 48  ? 2.0570 1.8725 2.0700 -0.1034 0.0383  0.0434  117  ASP   D OD1 
9108  O  OD2 . ASP   D 48  ? 2.0438 1.8597 2.0335 -0.0902 0.0376  0.0415  117  ASP   D OD2 
9109  N  N   . ARG   D 49  ? 1.9189 1.6998 1.8767 -0.0886 0.0319  0.0368  118  ARG   D N   
9110  C  CA  . ARG   D 49  ? 1.8468 1.6145 1.7835 -0.0806 0.0343  0.0367  118  ARG   D CA  
9111  C  C   . ARG   D 49  ? 1.8209 1.5941 1.7497 -0.0727 0.0352  0.0365  118  ARG   D C   
9112  O  O   . ARG   D 49  ? 1.8068 1.5728 1.7188 -0.0654 0.0338  0.0347  118  ARG   D O   
9113  C  CB  . ARG   D 49  ? 1.8514 1.6119 1.7767 -0.0791 0.0273  0.0324  118  ARG   D CB  
9114  N  N   . THR   D 50  ? 1.7990 1.5845 1.7399 -0.0739 0.0376  0.0385  119  THR   D N   
9115  C  CA  . THR   D 50  ? 1.7167 1.5101 1.6531 -0.0674 0.0370  0.0378  119  THR   D CA  
9116  C  C   . THR   D 50  ? 1.6817 1.4749 1.6208 -0.0660 0.0459  0.0426  119  THR   D C   
9117  O  O   . THR   D 50  ? 1.7112 1.5094 1.6657 -0.0722 0.0500  0.0456  119  THR   D O   
9118  C  CB  . THR   D 50  ? 1.7040 1.5150 1.6527 -0.0697 0.0296  0.0346  119  THR   D CB  
9119  O  OG1 . THR   D 50  ? 1.7402 1.5511 1.6852 -0.0702 0.0216  0.0300  119  THR   D OG1 
9120  C  CG2 . THR   D 50  ? 1.6105 1.4300 1.5559 -0.0633 0.0292  0.0340  119  THR   D CG2 
9121  N  N   . PHE   D 51  ? 1.5826 1.3700 1.5070 -0.0579 0.0486  0.0432  120  PHE   D N   
9122  C  CA  . PHE   D 51  ? 1.5063 1.2939 1.4310 -0.0551 0.0563  0.0473  120  PHE   D CA  
9123  C  C   . PHE   D 51  ? 1.4901 1.2883 1.4126 -0.0494 0.0524  0.0451  120  PHE   D C   
9124  O  O   . PHE   D 51  ? 1.4779 1.2836 1.3997 -0.0480 0.0442  0.0406  120  PHE   D O   
9125  C  CB  . PHE   D 51  ? 1.4743 1.2432 1.3822 -0.0502 0.0640  0.0505  120  PHE   D CB  
9126  C  CG  . PHE   D 51  ? 1.4525 1.2110 1.3401 -0.0425 0.0598  0.0473  120  PHE   D CG  
9127  C  CD1 . PHE   D 51  ? 1.4894 1.2517 1.3679 -0.0348 0.0560  0.0449  120  PHE   D CD1 
9128  C  CD2 . PHE   D 51  ? 1.4561 1.2008 1.3341 -0.0429 0.0596  0.0468  120  PHE   D CD2 
9129  C  CE1 . PHE   D 51  ? 1.4847 1.2378 1.3457 -0.0277 0.0519  0.0418  120  PHE   D CE1 
9130  C  CE2 . PHE   D 51  ? 1.4494 1.1846 1.3091 -0.0355 0.0557  0.0439  120  PHE   D CE2 
9131  C  CZ  . PHE   D 51  ? 1.4506 1.1902 1.3021 -0.0279 0.0518  0.0413  120  PHE   D CZ  
9132  N  N   . ALA   D 52  ? 1.5084 1.3066 1.4294 -0.0459 0.0587  0.0483  121  ALA   D N   
9133  C  CA  . ALA   D 52  ? 1.4180 1.2261 1.3380 -0.0408 0.0559  0.0468  121  ALA   D CA  
9134  C  C   . ALA   D 52  ? 1.4955 1.2914 1.3956 -0.0313 0.0588  0.0475  121  ALA   D C   
9135  O  O   . ALA   D 52  ? 1.6311 1.4151 1.5239 -0.0294 0.0672  0.0516  121  ALA   D O   
9136  C  CB  . ALA   D 52  ? 1.3723 1.1924 1.3087 -0.0447 0.0598  0.0497  121  ALA   D CB  
9137  N  N   . VAL   D 53  ? 1.4145 1.2127 1.3055 -0.0252 0.0519  0.0433  122  VAL   D N   
9138  C  CA  . VAL   D 53  ? 1.5145 1.3032 1.3877 -0.0157 0.0530  0.0431  122  VAL   D CA  
9139  C  C   . VAL   D 53  ? 1.5856 1.3852 1.4640 -0.0131 0.0530  0.0434  122  VAL   D C   
9140  O  O   . VAL   D 53  ? 1.5213 1.3364 1.4120 -0.0159 0.0473  0.0409  122  VAL   D O   
9141  C  CB  . VAL   D 53  ? 1.5042 1.2889 1.3652 -0.0103 0.0452  0.0382  122  VAL   D CB  
9142  C  CG1 . VAL   D 53  ? 1.6222 1.3987 1.4662 -0.0002 0.0450  0.0375  122  VAL   D CG1 
9143  C  CG2 . VAL   D 53  ? 1.5129 1.2854 1.3676 -0.0124 0.0458  0.0382  122  VAL   D CG2 
9144  N  N   . LEU   D 54  ? 1.7125 1.5036 1.5813 -0.0078 0.0594  0.0467  123  LEU   D N   
9145  C  CA  . LEU   D 54  ? 1.7159 1.5156 1.5893 -0.0056 0.0610  0.0478  123  LEU   D CA  
9146  C  C   . LEU   D 54  ? 1.8283 1.6230 1.6857 0.0043  0.0574  0.0454  123  LEU   D C   
9147  O  O   . LEU   D 54  ? 1.8705 1.6496 1.7101 0.0105  0.0585  0.0454  123  LEU   D O   
9148  C  CB  . LEU   D 54  ? 1.7131 1.5075 1.5891 -0.0073 0.0718  0.0537  123  LEU   D CB  
9149  C  CG  . LEU   D 54  ? 1.6596 1.4686 1.5579 -0.0159 0.0740  0.0557  123  LEU   D CG  
9150  C  CD1 . LEU   D 54  ? 1.7154 1.5405 1.6226 -0.0151 0.0686  0.0534  123  LEU   D CD1 
9151  C  CD2 . LEU   D 54  ? 1.5915 1.4049 1.5016 -0.0241 0.0707  0.0544  123  LEU   D CD2 
9152  N  N   . ALA   D 55  ? 2.0041 1.8116 1.8678 0.0058  0.0529  0.0433  124  ALA   D N   
9153  C  CA  . ALA   D 55  ? 2.0490 1.8539 1.9002 0.0147  0.0486  0.0406  124  ALA   D CA  
9154  C  C   . ALA   D 55  ? 2.0972 1.9052 1.9496 0.0173  0.0530  0.0433  124  ALA   D C   
9155  O  O   . ALA   D 55  ? 2.0869 1.9066 1.9551 0.0114  0.0557  0.0453  124  ALA   D O   
9156  C  CB  . ALA   D 55  ? 1.9673 1.7845 1.8242 0.0148  0.0384  0.0350  124  ALA   D CB  
9157  N  N   . TYR   D 56  ? 2.0161 1.8131 1.8517 0.0262  0.0537  0.0433  125  TYR   D N   
9158  C  CA  . TYR   D 56  ? 2.0324 1.8300 1.8663 0.0299  0.0579  0.0457  125  TYR   D CA  
9159  C  C   . TYR   D 56  ? 2.0457 1.8453 1.8716 0.0376  0.0506  0.0417  125  TYR   D C   
9160  O  O   . TYR   D 56  ? 2.0657 1.8582 1.8809 0.0441  0.0532  0.0431  125  TYR   D O   
9161  C  CB  . TYR   D 56  ? 2.0492 1.8292 1.8693 0.0335  0.0680  0.0508  125  TYR   D CB  
9162  C  CG  . TYR   D 56  ? 2.0736 1.8454 1.8946 0.0283  0.0737  0.0536  125  TYR   D CG  
9163  C  CD1 . TYR   D 56  ? 2.0585 1.8391 1.8976 0.0190  0.0785  0.0565  125  TYR   D CD1 
9164  C  CD2 . TYR   D 56  ? 2.0658 1.8207 1.8695 0.0327  0.0739  0.0532  125  TYR   D CD2 
9165  C  CE1 . TYR   D 56  ? 2.0275 1.8004 1.8681 0.0140  0.0834  0.0590  125  TYR   D CE1 
9166  C  CE2 . TYR   D 56  ? 1.9923 1.7391 1.7966 0.0279  0.0791  0.0558  125  TYR   D CE2 
9167  C  CZ  . TYR   D 56  ? 2.0157 1.7716 1.8387 0.0184  0.0838  0.0586  125  TYR   D CZ  
9168  O  OH  . TYR   D 56  ? 2.0398 1.7875 1.8639 0.0135  0.0887  0.0611  125  TYR   D OH  
9169  N  N   . ALA   D 64  ? 2.0369 1.8484 1.8958 0.0217  0.0751  0.0558  133  ALA   D N   
9170  C  CA  . ALA   D 64  ? 2.0616 1.8929 1.9394 0.0159  0.0688  0.0531  133  ALA   D CA  
9171  C  C   . ALA   D 64  ? 2.0746 1.9144 1.9701 0.0057  0.0695  0.0539  133  ALA   D C   
9172  O  O   . ALA   D 64  ? 2.0545 1.8860 1.9502 0.0025  0.0764  0.0574  133  ALA   D O   
9173  C  CB  . ALA   D 64  ? 2.0555 1.8917 1.9290 0.0197  0.0579  0.0472  133  ALA   D CB  
9174  N  N   . GLN   D 65  ? 1.9258 1.7817 1.8358 0.0008  0.0620  0.0505  134  GLN   D N   
9175  C  CA  . GLN   D 65  ? 1.7538 1.6210 1.6834 -0.0087 0.0627  0.0516  134  GLN   D CA  
9176  C  C   . GLN   D 65  ? 1.6794 1.5545 1.6158 -0.0131 0.0540  0.0472  134  GLN   D C   
9177  O  O   . GLN   D 65  ? 1.6035 1.4921 1.5565 -0.0195 0.0512  0.0465  134  GLN   D O   
9178  C  CB  . GLN   D 65  ? 1.7112 1.5920 1.6552 -0.0112 0.0642  0.0531  134  GLN   D CB  
9179  C  CG  . GLN   D 65  ? 1.7511 1.6394 1.6921 -0.0059 0.0581  0.0500  134  GLN   D CG  
9180  C  CD  . GLN   D 65  ? 1.8191 1.7021 1.7519 0.0004  0.0639  0.0528  134  GLN   D CD  
9181  O  OE1 . GLN   D 65  ? 1.8807 1.7487 1.7967 0.0067  0.0678  0.0542  134  GLN   D OE1 
9182  N  NE2 . GLN   D 65  ? 1.7355 1.6303 1.6795 -0.0010 0.0643  0.0536  134  GLN   D NE2 
9183  N  N   . PHE   D 66  ? 1.7333 1.5999 1.6573 -0.0097 0.0497  0.0443  135  PHE   D N   
9184  C  CA  . PHE   D 66  ? 1.6869 1.5593 1.6159 -0.0135 0.0421  0.0403  135  PHE   D CA  
9185  C  C   . PHE   D 66  ? 1.6996 1.5578 1.6172 -0.0127 0.0429  0.0400  135  PHE   D C   
9186  O  O   . PHE   D 66  ? 1.7142 1.5580 1.6180 -0.0079 0.0481  0.0423  135  PHE   D O   
9187  C  CB  . PHE   D 66  ? 1.6937 1.5736 1.6202 -0.0094 0.0335  0.0354  135  PHE   D CB  
9188  C  CG  . PHE   D 66  ? 1.6941 1.5901 1.6342 -0.0117 0.0308  0.0347  135  PHE   D CG  
9189  C  CD1 . PHE   D 66  ? 1.6963 1.5942 1.6358 -0.0083 0.0341  0.0367  135  PHE   D CD1 
9190  C  CD2 . PHE   D 66  ? 1.6649 1.5731 1.6169 -0.0169 0.0248  0.0318  135  PHE   D CD2 
9191  C  CE1 . PHE   D 66  ? 1.7000 1.6122 1.6515 -0.0103 0.0314  0.0359  135  PHE   D CE1 
9192  C  CE2 . PHE   D 66  ? 1.6331 1.5555 1.5968 -0.0188 0.0222  0.0311  135  PHE   D CE2 
9193  C  CZ  . PHE   D 66  ? 1.6544 1.5788 1.6180 -0.0156 0.0255  0.0331  135  PHE   D CZ  
9194  N  N   . GLY   D 67  ? 1.5193 1.3810 1.4419 -0.0171 0.0376  0.0372  136  GLY   D N   
9195  C  CA  . GLY   D 67  ? 1.4943 1.3430 1.4066 -0.0166 0.0378  0.0367  136  GLY   D CA  
9196  C  C   . GLY   D 67  ? 1.3893 1.2438 1.3077 -0.0210 0.0308  0.0330  136  GLY   D C   
9197  O  O   . GLY   D 67  ? 1.4183 1.2867 1.3482 -0.0241 0.0258  0.0307  136  GLY   D O   
9198  N  N   . THR   D 68  ? 1.3384 1.1815 1.2483 -0.0210 0.0308  0.0324  137  THR   D N   
9199  C  CA  . THR   D 68  ? 1.3038 1.1495 1.2169 -0.0246 0.0247  0.0290  137  THR   D CA  
9200  C  C   . THR   D 68  ? 1.3669 1.2027 1.2799 -0.0295 0.0285  0.0312  137  THR   D C   
9201  O  O   . THR   D 68  ? 1.4341 1.2556 1.3354 -0.0263 0.0337  0.0335  137  THR   D O   
9202  C  CB  . THR   D 68  ? 1.2943 1.1353 1.1943 -0.0180 0.0191  0.0248  137  THR   D CB  
9203  O  OG1 . THR   D 68  ? 1.3220 1.1684 1.2190 -0.0119 0.0168  0.0233  137  THR   D OG1 
9204  C  CG2 . THR   D 68  ? 1.2527 1.0998 1.1581 -0.0216 0.0124  0.0210  137  THR   D CG2 
9205  N  N   . THR   D 69  ? 1.3500 1.1923 1.2753 -0.0370 0.0258  0.0304  138  THR   D N   
9206  C  CA  . THR   D 69  ? 1.2921 1.1244 1.2170 -0.0416 0.0282  0.0318  138  THR   D CA  
9207  C  C   . THR   D 69  ? 1.2857 1.1066 1.1954 -0.0373 0.0250  0.0290  138  THR   D C   
9208  O  O   . THR   D 69  ? 1.3182 1.1420 1.2215 -0.0324 0.0194  0.0252  138  THR   D O   
9209  C  CB  . THR   D 69  ? 1.2514 1.0928 1.1923 -0.0502 0.0249  0.0310  138  THR   D CB  
9210  O  OG1 . THR   D 69  ? 1.2327 1.0828 1.1748 -0.0495 0.0167  0.0264  138  THR   D OG1 
9211  C  CG2 . THR   D 69  ? 1.3487 1.2004 1.3053 -0.0547 0.0285  0.0341  138  THR   D CG2 
9212  N  N   . ALA   D 70  ? 1.3225 1.1304 1.2270 -0.0394 0.0286  0.0308  139  ALA   D N   
9213  C  CA  . ALA   D 70  ? 1.3234 1.1190 1.2130 -0.0354 0.0261  0.0285  139  ALA   D CA  
9214  C  C   . ALA   D 70  ? 1.3882 1.1765 1.2810 -0.0419 0.0270  0.0293  139  ALA   D C   
9215  O  O   . ALA   D 70  ? 1.4405 1.2237 1.3382 -0.0462 0.0335  0.0334  139  ALA   D O   
9216  C  CB  . ALA   D 70  ? 1.3525 1.1344 1.2250 -0.0276 0.0307  0.0302  139  ALA   D CB  
9217  N  N   . GLU   D 71  ? 1.3423 1.1295 1.2322 -0.0426 0.0207  0.0255  140  GLU   D N   
9218  C  CA  . GLU   D 71  ? 1.4016 1.1827 1.2950 -0.0490 0.0201  0.0255  140  GLU   D CA  
9219  C  C   . GLU   D 71  ? 1.3878 1.1512 1.2645 -0.0451 0.0217  0.0255  140  GLU   D C   
9220  O  O   . GLU   D 71  ? 1.3408 1.1006 1.2054 -0.0390 0.0174  0.0221  140  GLU   D O   
9221  C  CB  . GLU   D 71  ? 1.3593 1.1502 1.2606 -0.0527 0.0121  0.0214  140  GLU   D CB  
9222  C  CG  . GLU   D 71  ? 1.3908 1.1752 1.2958 -0.0594 0.0108  0.0212  140  GLU   D CG  
9223  C  CD  . GLU   D 71  ? 1.3705 1.1617 1.2791 -0.0616 0.0026  0.0167  140  GLU   D CD  
9224  O  OE1 . GLU   D 71  ? 1.2875 1.0902 1.1987 -0.0591 -0.0014 0.0143  140  GLU   D OE1 
9225  O  OE2 . GLU   D 71  ? 1.4506 1.2350 1.3589 -0.0657 0.0002  0.0156  140  GLU   D OE2 
9226  N  N   . ILE   D 72  ? 1.4217 1.1740 1.2982 -0.0488 0.0278  0.0291  141  ILE   D N   
9227  C  CA  . ILE   D 72  ? 1.4034 1.1379 1.2646 -0.0460 0.0297  0.0294  141  ILE   D CA  
9228  C  C   . ILE   D 72  ? 1.3954 1.1287 1.2546 -0.0477 0.0223  0.0250  141  ILE   D C   
9229  O  O   . ILE   D 72  ? 1.4351 1.1754 1.3070 -0.0548 0.0189  0.0240  141  ILE   D O   
9230  C  CB  . ILE   D 72  ? 1.3809 1.1049 1.2448 -0.0509 0.0380  0.0343  141  ILE   D CB  
9231  C  CG1 . ILE   D 72  ? 1.4238 1.1548 1.2972 -0.0520 0.0446  0.0385  141  ILE   D CG1 
9232  C  CG2 . ILE   D 72  ? 1.4020 1.1067 1.2469 -0.0454 0.0422  0.0358  141  ILE   D CG2 
9233  C  CD1 . ILE   D 72  ? 1.5301 1.2521 1.4084 -0.0570 0.0535  0.0437  141  ILE   D CD1 
9234  N  N   . TYR   D 73  ? 1.3414 1.0661 1.1845 -0.0407 0.0194  0.0223  142  TYR   D N   
9235  C  CA  . TYR   D 73  ? 1.3409 1.0621 1.1795 -0.0412 0.0131  0.0183  142  TYR   D CA  
9236  C  C   . TYR   D 73  ? 1.4120 1.1142 1.2337 -0.0374 0.0150  0.0186  142  TYR   D C   
9237  O  O   . TYR   D 73  ? 1.4828 1.1802 1.2989 -0.0370 0.0102  0.0153  142  TYR   D O   
9238  C  CB  . TYR   D 73  ? 1.3415 1.0736 1.1790 -0.0364 0.0060  0.0136  142  TYR   D CB  
9239  C  CG  . TYR   D 73  ? 1.3415 1.0696 1.1649 -0.0265 0.0056  0.0123  142  TYR   D CG  
9240  C  CD1 . TYR   D 73  ? 1.3821 1.0994 1.1909 -0.0210 0.0028  0.0095  142  TYR   D CD1 
9241  C  CD2 . TYR   D 73  ? 1.3411 1.0762 1.1659 -0.0227 0.0077  0.0135  142  TYR   D CD2 
9242  C  CE1 . TYR   D 73  ? 1.3872 1.1011 1.1840 -0.0118 0.0019  0.0081  142  TYR   D CE1 
9243  C  CE2 . TYR   D 73  ? 1.3381 1.0694 1.1504 -0.0136 0.0067  0.0120  142  TYR   D CE2 
9244  C  CZ  . TYR   D 73  ? 1.3590 1.0798 1.1577 -0.0082 0.0037  0.0093  142  TYR   D CZ  
9245  O  OH  . TYR   D 73  ? 1.3772 1.0945 1.1643 0.0009  0.0022  0.0076  142  TYR   D OH  
9246  N  N   . ALA   D 74  ? 1.4096 1.1004 1.2227 -0.0345 0.0220  0.0223  143  ALA   D N   
9247  C  CA  . ALA   D 74  ? 1.4381 1.1095 1.2358 -0.0319 0.0247  0.0233  143  ALA   D CA  
9248  C  C   . ALA   D 74  ? 1.4511 1.1130 1.2492 -0.0347 0.0341  0.0289  143  ALA   D C   
9249  O  O   . ALA   D 74  ? 1.5040 1.1725 1.3087 -0.0349 0.0386  0.0318  143  ALA   D O   
9250  C  CB  . ALA   D 74  ? 1.4232 1.0877 1.2030 -0.0214 0.0223  0.0208  143  ALA   D CB  
9251  N  N   . TYR   D 75  ? 1.5141 1.1604 1.3058 -0.0371 0.0373  0.0306  144  TYR   D N   
9252  C  CA  . TYR   D 75  ? 1.5420 1.1777 1.3335 -0.0398 0.0470  0.0362  144  TYR   D CA  
9253  C  C   . TYR   D 75  ? 1.6589 1.2734 1.4334 -0.0371 0.0495  0.0370  144  TYR   D C   
9254  O  O   . TYR   D 75  ? 1.6771 1.2867 1.4525 -0.0413 0.0462  0.0353  144  TYR   D O   
9255  C  CB  . TYR   D 75  ? 1.4616 1.1054 1.2741 -0.0506 0.0493  0.0386  144  TYR   D CB  
9256  C  CG  . TYR   D 75  ? 1.5490 1.1830 1.3638 -0.0540 0.0598  0.0445  144  TYR   D CG  
9257  C  CD1 . TYR   D 75  ? 1.6162 1.2575 1.4395 -0.0545 0.0660  0.0482  144  TYR   D CD1 
9258  C  CD2 . TYR   D 75  ? 1.6094 1.2263 1.4178 -0.0566 0.0638  0.0465  144  TYR   D CD2 
9259  C  CE1 . TYR   D 75  ? 1.6540 1.2862 1.4798 -0.0575 0.0764  0.0538  144  TYR   D CE1 
9260  C  CE2 . TYR   D 75  ? 1.6253 1.2328 1.4362 -0.0598 0.0741  0.0522  144  TYR   D CE2 
9261  C  CZ  . TYR   D 75  ? 1.6578 1.2731 1.4775 -0.0602 0.0806  0.0559  144  TYR   D CZ  
9262  O  OH  . TYR   D 75  ? 1.7954 1.4015 1.6180 -0.0632 0.0914  0.0616  144  TYR   D OH  
9263  N  N   . ARG   D 76  ? 1.6749 1.2763 1.4332 -0.0299 0.0551  0.0395  145  ARG   D N   
9264  C  CA  . ARG   D 76  ? 1.7948 1.3749 1.5350 -0.0264 0.0580  0.0406  145  ARG   D CA  
9265  C  C   . ARG   D 76  ? 1.9091 1.4763 1.6435 -0.0258 0.0691  0.0466  145  ARG   D C   
9266  O  O   . ARG   D 76  ? 1.9382 1.5063 1.6671 -0.0200 0.0725  0.0484  145  ARG   D O   
9267  C  CB  . ARG   D 76  ? 1.7976 1.3720 1.5191 -0.0159 0.0523  0.0366  145  ARG   D CB  
9268  N  N   . GLU   D 77  ? 1.9665 1.5213 1.7020 -0.0316 0.0747  0.0498  146  GLU   D N   
9269  C  CA  . GLU   D 77  ? 2.0345 1.5739 1.7631 -0.0313 0.0859  0.0558  146  GLU   D CA  
9270  C  C   . GLU   D 77  ? 2.1471 1.6640 1.8510 -0.0240 0.0875  0.0559  146  GLU   D C   
9271  O  O   . GLU   D 77  ? 2.0787 1.5868 1.7785 -0.0263 0.0845  0.0542  146  GLU   D O   
9272  C  CB  . GLU   D 77  ? 1.9190 1.4581 1.6648 -0.0425 0.0916  0.0593  146  GLU   D CB  
9273  C  CG  . GLU   D 77  ? 1.8988 1.4564 1.6681 -0.0495 0.0936  0.0611  146  GLU   D CG  
9274  C  CD  . GLU   D 77  ? 1.9282 1.4810 1.7110 -0.0585 0.1027  0.0663  146  GLU   D CD  
9275  O  OE1 . GLU   D 77  ? 1.9468 1.4813 1.7178 -0.0567 0.1114  0.0704  146  GLU   D OE1 
9276  O  OE2 . GLU   D 77  ? 1.8957 1.4628 1.7011 -0.0672 0.1012  0.0662  146  GLU   D OE2 
9277  N  N   . GLU   D 78  ? 2.1917 1.6985 1.8786 -0.0151 0.0921  0.0580  147  GLU   D N   
9278  C  CA  . GLU   D 78  ? 2.1997 1.6838 1.8616 -0.0072 0.0941  0.0585  147  GLU   D CA  
9279  C  C   . GLU   D 78  ? 2.2731 1.7397 1.9262 -0.0067 0.1067  0.0651  147  GLU   D C   
9280  O  O   . GLU   D 78  ? 2.3011 1.7509 1.9320 0.0023  0.1097  0.0664  147  GLU   D O   
9281  C  CB  . GLU   D 78  ? 2.1396 1.6239 1.7853 0.0044  0.0876  0.0546  147  GLU   D CB  
9282  C  CG  . GLU   D 78  ? 2.1465 1.6375 1.7910 0.0066  0.0760  0.0481  147  GLU   D CG  
9283  C  CD  . GLU   D 78  ? 2.2208 1.7364 1.8856 0.0020  0.0689  0.0446  147  GLU   D CD  
9284  O  OE1 . GLU   D 78  ? 2.2531 1.7805 1.9223 0.0051  0.0684  0.0445  147  GLU   D OE1 
9285  O  OE2 . GLU   D 78  ? 2.2470 1.7699 1.9231 -0.0045 0.0639  0.0420  147  GLU   D OE2 
9286  N  N   . GLY   D 82  ? 2.4099 1.7913 1.9614 0.0356  0.1433  0.0832  151  GLY   D N   
9287  C  CA  . GLY   D 82  ? 2.4405 1.8068 1.9923 0.0292  0.1534  0.0883  151  GLY   D CA  
9288  C  C   . GLY   D 82  ? 2.4278 1.8067 2.0053 0.0177  0.1614  0.0926  151  GLY   D C   
9289  O  O   . GLY   D 82  ? 2.4298 1.7971 2.0100 0.0119  0.1716  0.0977  151  GLY   D O   
9290  N  N   . ILE   D 83  ? 2.3835 1.7860 1.9803 0.0145  0.1568  0.0905  152  ILE   D N   
9291  C  CA  . ILE   D 83  ? 2.3750 1.7916 1.9979 0.0037  0.1631  0.0939  152  ILE   D CA  
9292  C  C   . ILE   D 83  ? 2.3917 1.8298 2.0380 -0.0050 0.1531  0.0891  152  ILE   D C   
9293  O  O   . ILE   D 83  ? 2.3855 1.8234 2.0269 -0.0039 0.1436  0.0842  152  ILE   D O   
9294  C  CB  . ILE   D 83  ? 2.3441 1.7695 1.9707 0.0069  0.1680  0.0964  152  ILE   D CB  
9295  C  CG1 . ILE   D 83  ? 2.4061 1.8435 2.0270 0.0147  0.1566  0.0907  152  ILE   D CG1 
9296  C  CG2 . ILE   D 83  ? 2.2821 1.6855 1.8890 0.0132  0.1806  0.1024  152  ILE   D CG2 
9297  C  CD1 . ILE   D 83  ? 2.3861 1.8453 2.0253 0.0123  0.1559  0.0906  152  ILE   D CD1 
9298  N  N   . GLU   D 84  ? 2.3905 1.8470 2.0619 -0.0134 0.1553  0.0906  153  GLU   D N   
9299  C  CA  . GLU   D 84  ? 2.3589 1.8369 2.0533 -0.0215 0.1459  0.0862  153  GLU   D CA  
9300  C  C   . GLU   D 84  ? 2.3395 1.8337 2.0334 -0.0156 0.1356  0.0810  153  GLU   D C   
9301  O  O   . GLU   D 84  ? 2.2367 1.7474 1.9443 -0.0172 0.1356  0.0813  153  GLU   D O   
9302  C  CB  . GLU   D 84  ? 2.2325 1.7228 1.9536 -0.0325 0.1522  0.0898  153  GLU   D CB  
9303  N  N   . ILE   D 85  ? 2.4472 1.9360 2.1248 -0.0086 0.1269  0.0763  154  ILE   D N   
9304  C  CA  . ILE   D 85  ? 2.3999 1.9018 2.0749 -0.0022 0.1166  0.0709  154  ILE   D CA  
9305  C  C   . ILE   D 85  ? 2.3387 1.8612 2.0343 -0.0096 0.1072  0.0664  154  ILE   D C   
9306  O  O   . ILE   D 85  ? 2.3549 1.8745 2.0518 -0.0134 0.1026  0.0639  154  ILE   D O   
9307  C  CB  . ILE   D 85  ? 2.3963 1.8835 2.0459 0.0085  0.1114  0.0678  154  ILE   D CB  
9308  C  CG1 . ILE   D 85  ? 2.3769 1.8415 2.0042 0.0160  0.1207  0.0724  154  ILE   D CG1 
9309  C  CG2 . ILE   D 85  ? 2.3550 1.8567 2.0042 0.0146  0.1010  0.0623  154  ILE   D CG2 
9310  C  CD1 . ILE   D 85  ? 2.3474 1.7893 1.9540 0.0201  0.1212  0.0723  154  ILE   D CD1 
9311  N  N   . VAL   D 86  ? 2.0951 1.6374 1.8058 -0.0113 0.1042  0.0651  155  VAL   D N   
9312  C  CA  . VAL   D 86  ? 1.9955 1.5579 1.7257 -0.0179 0.0955  0.0610  155  VAL   D CA  
9313  C  C   . VAL   D 86  ? 1.9347 1.5098 1.6622 -0.0111 0.0870  0.0563  155  VAL   D C   
9314  O  O   . VAL   D 86  ? 1.9475 1.5271 1.6736 -0.0068 0.0895  0.0577  155  VAL   D O   
9315  C  CB  . VAL   D 86  ? 1.9443 1.5204 1.6990 -0.0279 0.0999  0.0639  155  VAL   D CB  
9316  C  CG1 . VAL   D 86  ? 1.8232 1.4179 1.5961 -0.0344 0.0904  0.0594  155  VAL   D CG1 
9317  C  CG2 . VAL   D 86  ? 2.0151 1.5782 1.7730 -0.0342 0.1096  0.0691  155  VAL   D CG2 
9318  N  N   . LYS   D 87  ? 1.8312 1.4120 1.5583 -0.0104 0.0771  0.0509  156  LYS   D N   
9319  C  CA  . LYS   D 87  ? 1.7264 1.3195 1.4521 -0.0043 0.0687  0.0462  156  LYS   D CA  
9320  C  C   . LYS   D 87  ? 1.7023 1.3149 1.4478 -0.0115 0.0615  0.0427  156  LYS   D C   
9321  O  O   . LYS   D 87  ? 1.7103 1.3219 1.4573 -0.0147 0.0566  0.0399  156  LYS   D O   
9322  C  CB  . LYS   D 87  ? 1.7486 1.3294 1.4536 0.0048  0.0635  0.0427  156  LYS   D CB  
9323  N  N   . VAL   D 88  ? 1.6407 1.2704 1.4006 -0.0137 0.0609  0.0429  157  VAL   D N   
9324  C  CA  . VAL   D 88  ? 1.5082 1.1569 1.2856 -0.0193 0.0537  0.0394  157  VAL   D CA  
9325  C  C   . VAL   D 88  ? 1.4532 1.1125 1.2273 -0.0124 0.0465  0.0351  157  VAL   D C   
9326  O  O   . VAL   D 88  ? 1.5194 1.1736 1.2810 -0.0042 0.0476  0.0353  157  VAL   D O   
9327  C  CB  . VAL   D 88  ? 1.4525 1.1139 1.2508 -0.0279 0.0577  0.0424  157  VAL   D CB  
9328  C  CG1 . VAL   D 88  ? 1.5622 1.2131 1.3650 -0.0348 0.0652  0.0468  157  VAL   D CG1 
9329  C  CG2 . VAL   D 88  ? 1.4547 1.1225 1.2543 -0.0241 0.0615  0.0446  157  VAL   D CG2 
9330  N  N   . LYS   D 89  ? 1.4378 1.1116 1.2233 -0.0157 0.0390  0.0311  158  LYS   D N   
9331  C  CA  . LYS   D 89  ? 1.3420 1.0284 1.1283 -0.0106 0.0323  0.0271  158  LYS   D CA  
9332  C  C   . LYS   D 89  ? 1.3431 1.0485 1.1497 -0.0178 0.0293  0.0262  158  LYS   D C   
9333  O  O   . LYS   D 89  ? 1.3800 1.0879 1.1969 -0.0255 0.0286  0.0262  158  LYS   D O   
9334  C  CB  . LYS   D 89  ? 1.2928 0.9752 1.0683 -0.0053 0.0251  0.0222  158  LYS   D CB  
9335  N  N   . ALA   D 90  ? 1.3287 1.0469 1.1408 -0.0152 0.0276  0.0253  159  ALA   D N   
9336  C  CA  . ALA   D 90  ? 1.2754 1.0116 1.1061 -0.0214 0.0251  0.0247  159  ALA   D CA  
9337  C  C   . ALA   D 90  ? 1.2835 1.0317 1.1149 -0.0166 0.0182  0.0205  159  ALA   D C   
9338  O  O   . ALA   D 90  ? 1.3205 1.0638 1.1393 -0.0084 0.0165  0.0187  159  ALA   D O   
9339  C  CB  . ALA   D 90  ? 1.3218 1.0625 1.1620 -0.0247 0.0320  0.0293  159  ALA   D CB  
9340  N  N   . ILE   D 91  ? 1.3168 1.0807 1.1632 -0.0216 0.0144  0.0188  160  ILE   D N   
9341  C  CA  . ILE   D 91  ? 1.2765 1.0529 1.1258 -0.0182 0.0081  0.0149  160  ILE   D CA  
9342  C  C   . ILE   D 91  ? 1.2895 1.0813 1.1540 -0.0221 0.0087  0.0162  160  ILE   D C   
9343  O  O   . ILE   D 91  ? 1.2505 1.0461 1.1267 -0.0295 0.0114  0.0187  160  ILE   D O   
9344  C  CB  . ILE   D 91  ? 1.2456 1.0247 1.0961 -0.0200 0.0015  0.0107  160  ILE   D CB  
9345  C  CG1 . ILE   D 91  ? 1.2665 1.0593 1.1216 -0.0170 -0.0044 0.0068  160  ILE   D CG1 
9346  C  CG2 . ILE   D 91  ? 1.2990 1.0807 1.1611 -0.0292 0.0017  0.0117  160  ILE   D CG2 
9347  C  CD1 . ILE   D 91  ? 1.1980 0.9909 1.0502 -0.0161 -0.0102 0.0026  160  ILE   D CD1 
9348  N  N   . GLY   D 92  ? 1.3345 1.1350 1.1991 -0.0171 0.0061  0.0144  161  GLY   D N   
9349  C  CA  . GLY   D 92  ? 1.3223 1.1370 1.1999 -0.0197 0.0066  0.0156  161  GLY   D CA  
9350  C  C   . GLY   D 92  ? 1.2534 1.0814 1.1455 -0.0263 0.0022  0.0137  161  GLY   D C   
9351  O  O   . GLY   D 92  ? 1.2370 1.0701 1.1288 -0.0249 -0.0037 0.0097  161  GLY   D O   
9352  N  N   . ARG   D 93  ? 1.2151 1.0486 1.1198 -0.0332 0.0050  0.0165  162  ARG   D N   
9353  C  CA  . ARG   D 93  ? 1.1960 1.0409 1.1138 -0.0395 0.0007  0.0148  162  ARG   D CA  
9354  C  C   . ARG   D 93  ? 1.2432 1.1033 1.1711 -0.0395 -0.0011 0.0144  162  ARG   D C   
9355  O  O   . ARG   D 93  ? 1.2374 1.1042 1.1641 -0.0361 -0.0059 0.0110  162  ARG   D O   
9356  C  CB  . ARG   D 93  ? 1.2417 1.0842 1.1688 -0.0475 0.0036  0.0176  162  ARG   D CB  
9357  C  CG  . ARG   D 93  ? 1.1909 1.0207 1.1105 -0.0491 0.0029  0.0168  162  ARG   D CG  
9358  C  CD  . ARG   D 93  ? 1.2187 1.0493 1.1324 -0.0467 -0.0041 0.0119  162  ARG   D CD  
9359  N  NE  . ARG   D 93  ? 1.2175 1.0363 1.1245 -0.0486 -0.0053 0.0109  162  ARG   D NE  
9360  C  CZ  . ARG   D 93  ? 1.2104 1.0237 1.1067 -0.0445 -0.0092 0.0075  162  ARG   D CZ  
9361  N  NH1 . ARG   D 93  ? 1.1887 1.0066 1.0797 -0.0381 -0.0122 0.0048  162  ARG   D NH1 
9362  N  NH2 . ARG   D 93  ? 1.2872 1.0898 1.1783 -0.0467 -0.0101 0.0068  162  ARG   D NH2 
9363  N  N   . GLN   D 94  ? 1.3206 1.1863 1.2591 -0.0434 0.0029  0.0177  163  GLN   D N   
9364  C  CA  . GLN   D 94  ? 1.3181 1.1982 1.2671 -0.0441 0.0012  0.0174  163  GLN   D CA  
9365  C  C   . GLN   D 94  ? 1.3641 1.2441 1.3115 -0.0404 0.0066  0.0205  163  GLN   D C   
9366  O  O   . GLN   D 94  ? 1.3707 1.2407 1.3130 -0.0397 0.0127  0.0238  163  GLN   D O   
9367  C  CB  . GLN   D 94  ? 1.3238 1.2124 1.2884 -0.0524 -0.0002 0.0181  163  GLN   D CB  
9368  C  CG  . GLN   D 94  ? 1.3942 1.2745 1.3623 -0.0578 0.0041  0.0212  163  GLN   D CG  
9369  C  CD  . GLN   D 94  ? 1.4783 1.3643 1.4593 -0.0657 0.0005  0.0204  163  GLN   D CD  
9370  O  OE1 . GLN   D 94  ? 1.5181 1.4104 1.5011 -0.0666 -0.0059 0.0170  163  GLN   D OE1 
9371  N  NE2 . GLN   D 94  ? 1.4735 1.3568 1.4632 -0.0713 0.0046  0.0236  163  GLN   D NE2 
9372  N  N   . ARG   D 95  ? 1.3151 1.2055 1.2658 -0.0376 0.0045  0.0194  164  ARG   D N   
9373  C  CA  . ARG   D 95  ? 1.2905 1.1814 1.2394 -0.0335 0.0089  0.0219  164  ARG   D CA  
9374  C  C   . ARG   D 95  ? 1.3110 1.2100 1.2741 -0.0391 0.0126  0.0252  164  ARG   D C   
9375  O  O   . ARG   D 95  ? 1.3904 1.2972 1.3658 -0.0455 0.0102  0.0248  164  ARG   D O   
9376  C  CB  . ARG   D 95  ? 1.2286 1.1265 1.1744 -0.0278 0.0046  0.0189  164  ARG   D CB  
9377  C  CG  . ARG   D 95  ? 1.1761 1.0672 1.1089 -0.0217 0.0006  0.0153  164  ARG   D CG  
9378  C  CD  . ARG   D 95  ? 1.1491 1.0516 1.0864 -0.0204 -0.0057 0.0114  164  ARG   D CD  
9379  N  NE  . ARG   D 95  ? 1.2032 1.1177 1.1549 -0.0271 -0.0073 0.0116  164  ARG   D NE  
9380  C  CZ  . ARG   D 95  ? 1.2326 1.1589 1.1913 -0.0273 -0.0115 0.0093  164  ARG   D CZ  
9381  N  NH1 . ARG   D 95  ? 1.1877 1.1166 1.1419 -0.0215 -0.0143 0.0068  164  ARG   D NH1 
9382  N  NH2 . ARG   D 95  ? 1.2958 1.2314 1.2666 -0.0335 -0.0129 0.0096  164  ARG   D NH2 
9383  N  N   . PHE   D 96  ? 1.3233 1.2202 1.2847 -0.0363 0.0184  0.0285  165  PHE   D N   
9384  C  CA  . PHE   D 96  ? 1.3765 1.2792 1.3511 -0.0413 0.0233  0.0322  165  PHE   D CA  
9385  C  C   . PHE   D 96  ? 1.4521 1.3542 1.4233 -0.0365 0.0285  0.0350  165  PHE   D C   
9386  O  O   . PHE   D 96  ? 1.4789 1.3713 1.4356 -0.0296 0.0305  0.0352  165  PHE   D O   
9387  C  CB  . PHE   D 96  ? 1.3787 1.2734 1.3569 -0.0468 0.0280  0.0351  165  PHE   D CB  
9388  C  CG  . PHE   D 96  ? 1.3360 1.2150 1.3011 -0.0430 0.0347  0.0380  165  PHE   D CG  
9389  C  CD1 . PHE   D 96  ? 1.3646 1.2405 1.3283 -0.0405 0.0422  0.0419  165  PHE   D CD1 
9390  C  CD2 . PHE   D 96  ? 1.3375 1.2043 1.2913 -0.0418 0.0339  0.0368  165  PHE   D CD2 
9391  C  CE1 . PHE   D 96  ? 1.4006 1.2613 1.3514 -0.0367 0.0487  0.0447  165  PHE   D CE1 
9392  C  CE2 . PHE   D 96  ? 1.3497 1.2015 1.2910 -0.0382 0.0402  0.0395  165  PHE   D CE2 
9393  C  CZ  . PHE   D 96  ? 1.3954 1.2440 1.3349 -0.0356 0.0477  0.0435  165  PHE   D CZ  
9394  N  N   . LYS   D 97  ? 1.4160 1.3288 1.4009 -0.0400 0.0305  0.0370  166  LYS   D N   
9395  C  CA  . LYS   D 97  ? 1.4211 1.3337 1.4061 -0.0371 0.0369  0.0406  166  LYS   D CA  
9396  C  C   . LYS   D 97  ? 1.4100 1.3186 1.4027 -0.0419 0.0449  0.0453  166  LYS   D C   
9397  O  O   . LYS   D 97  ? 1.3995 1.3125 1.4049 -0.0491 0.0440  0.0455  166  LYS   D O   
9398  C  CB  . LYS   D 97  ? 1.3773 1.3046 1.3727 -0.0375 0.0340  0.0397  166  LYS   D CB  
9399  N  N   . VAL   D 98  ? 1.4531 1.3529 1.4384 -0.0379 0.0528  0.0490  167  VAL   D N   
9400  C  CA  . VAL   D 98  ? 1.4219 1.3169 1.4140 -0.0420 0.0615  0.0538  167  VAL   D CA  
9401  C  C   . VAL   D 98  ? 1.4033 1.3103 1.4109 -0.0447 0.0647  0.0562  167  VAL   D C   
9402  O  O   . VAL   D 98  ? 1.3371 1.2504 1.3434 -0.0406 0.0633  0.0556  167  VAL   D O   
9403  C  CB  . VAL   D 98  ? 1.4372 1.3150 1.4128 -0.0364 0.0694  0.0569  167  VAL   D CB  
9404  C  CG1 . VAL   D 98  ? 1.4832 1.3494 1.4423 -0.0326 0.0655  0.0541  167  VAL   D CG1 
9405  C  CG2 . VAL   D 98  ? 1.5771 1.4534 1.5445 -0.0293 0.0731  0.0585  167  VAL   D CG2 
9406  N  N   . LEU   D 99  ? 1.4247 1.3348 1.4476 -0.0517 0.0688  0.0590  168  LEU   D N   
9407  C  CA  . LEU   D 99  ? 1.3677 1.2902 1.4081 -0.0554 0.0713  0.0612  168  LEU   D CA  
9408  C  C   . LEU   D 99  ? 1.3750 1.2909 1.4195 -0.0565 0.0826  0.0668  168  LEU   D C   
9409  O  O   . LEU   D 99  ? 1.4061 1.3205 1.4465 -0.0518 0.0886  0.0695  168  LEU   D O   
9410  C  CB  . LEU   D 99  ? 1.3698 1.3045 1.4279 -0.0633 0.0644  0.0589  168  LEU   D CB  
9411  C  CG  . LEU   D 99  ? 1.3307 1.2706 1.3842 -0.0625 0.0537  0.0534  168  LEU   D CG  
9412  C  CD1 . LEU   D 99  ? 1.3299 1.2802 1.3994 -0.0700 0.0471  0.0512  168  LEU   D CD1 
9413  C  CD2 . LEU   D 99  ? 1.3381 1.2843 1.3859 -0.0566 0.0508  0.0517  168  LEU   D CD2 
9414  N  N   . GLU   D 100 ? 1.4177 1.3296 1.4706 -0.0626 0.0859  0.0687  169  GLU   D N   
9415  C  CA  . GLU   D 100 ? 1.4725 1.3745 1.5260 -0.0633 0.0974  0.0740  169  GLU   D CA  
9416  C  C   . GLU   D 100 ? 1.5299 1.4140 1.5643 -0.0597 0.0998  0.0742  169  GLU   D C   
9417  O  O   . GLU   D 100 ? 1.5065 1.3876 1.5319 -0.0589 0.0923  0.0703  169  GLU   D O   
9418  C  CB  . GLU   D 100 ? 1.3905 1.2989 1.4666 -0.0724 0.0999  0.0761  169  GLU   D CB  
9419  N  N   . LEU   D 101 ? 1.5873 1.4593 1.6151 -0.0573 0.1108  0.0790  170  LEU   D N   
9420  C  CA  . LEU   D 101 ? 1.6541 1.5075 1.6616 -0.0528 0.1142  0.0798  170  LEU   D CA  
9421  C  C   . LEU   D 101 ? 1.7647 1.6070 1.7744 -0.0549 0.1267  0.0856  170  LEU   D C   
9422  O  O   . LEU   D 101 ? 1.8205 1.6469 1.8121 -0.0488 0.1335  0.0881  170  LEU   D O   
9423  C  CB  . LEU   D 101 ? 1.6344 1.4804 1.6199 -0.0426 0.1132  0.0785  170  LEU   D CB  
9424  C  CG  . LEU   D 101 ? 1.6422 1.4858 1.6137 -0.0387 0.1029  0.0731  170  LEU   D CG  
9425  C  CD1 . LEU   D 101 ? 1.6213 1.4632 1.5773 -0.0295 0.1006  0.0715  170  LEU   D CD1 
9426  C  CD2 . LEU   D 101 ? 1.6585 1.4862 1.6172 -0.0383 0.1039  0.0731  170  LEU   D CD2 
9427  N  N   . ARG   D 102 ? 1.9167 1.7669 1.9485 -0.0633 0.1297  0.0877  171  ARG   D N   
9428  C  CA  . ARG   D 102 ? 1.9332 1.7743 1.9702 -0.0660 0.1421  0.0934  171  ARG   D CA  
9429  C  C   . ARG   D 102 ? 1.9788 1.8005 1.9984 -0.0641 0.1455  0.0944  171  ARG   D C   
9430  O  O   . ARG   D 102 ? 1.9935 1.8128 2.0083 -0.0657 0.1376  0.0906  171  ARG   D O   
9431  C  CB  . ARG   D 102 ? 1.8945 1.7477 1.9593 -0.0763 0.1422  0.0944  171  ARG   D CB  
9432  N  N   . THR   D 103 ? 1.9463 1.7535 1.9552 -0.0601 0.1575  0.0994  172  THR   D N   
9433  C  CA  . THR   D 103 ? 1.8662 1.6530 1.8565 -0.0573 0.1622  0.1009  172  THR   D CA  
9434  C  C   . THR   D 103 ? 1.7568 1.5371 1.7595 -0.0642 0.1722  0.1058  172  THR   D C   
9435  O  O   . THR   D 103 ? 1.7032 1.4770 1.7063 -0.0687 0.1702  0.1048  172  THR   D O   
9436  C  CB  . THR   D 103 ? 1.7711 1.5423 1.7353 -0.0464 0.1683  0.1031  172  THR   D CB  
9437  O  OG1 . THR   D 103 ? 1.8004 1.5788 1.7555 -0.0400 0.1598  0.0990  172  THR   D OG1 
9438  C  CG2 . THR   D 103 ? 1.7041 1.4551 1.6471 -0.0429 0.1699  0.1032  172  THR   D CG2 
9439  N  N   . ILE   D 108 ? 2.3159 2.0183 2.2329 -0.0536 0.1647  0.1001  177  ILE   D N   
9440  C  CA  . ILE   D 108 ? 2.2315 1.9460 2.1471 -0.0515 0.1510  0.0937  177  ILE   D CA  
9441  C  C   . ILE   D 108 ? 2.1649 1.8992 2.0965 -0.0528 0.1484  0.0930  177  ILE   D C   
9442  O  O   . ILE   D 108 ? 2.1744 1.9099 2.1110 -0.0519 0.1575  0.0973  177  ILE   D O   
9443  C  CB  . ILE   D 108 ? 2.2252 1.9432 2.1486 -0.0582 0.1421  0.0897  177  ILE   D CB  
9444  C  CG1 . ILE   D 108 ? 2.2617 1.9873 2.2106 -0.0692 0.1455  0.0920  177  ILE   D CG1 
9445  C  CG2 . ILE   D 108 ? 2.2179 1.9161 2.1204 -0.0545 0.1424  0.0892  177  ILE   D CG2 
9446  C  CD1 . ILE   D 108 ? 2.2314 1.9585 2.1878 -0.0760 0.1372  0.0883  177  ILE   D CD1 
9447  N  N   . GLN   D 109 ? 2.0185 1.7680 1.9580 -0.0546 0.1366  0.0876  178  GLN   D N   
9448  C  CA  . GLN   D 109 ? 1.8718 1.6396 1.8245 -0.0550 0.1331  0.0865  178  GLN   D CA  
9449  C  C   . GLN   D 109 ? 1.7688 1.5522 1.7349 -0.0603 0.1209  0.0811  178  GLN   D C   
9450  O  O   . GLN   D 109 ? 1.8022 1.5825 1.7574 -0.0581 0.1127  0.0768  178  GLN   D O   
9451  C  CB  . GLN   D 109 ? 1.8265 1.5916 1.7611 -0.0448 0.1322  0.0855  178  GLN   D CB  
9452  C  CG  . GLN   D 109 ? 1.7875 1.5696 1.7338 -0.0445 0.1298  0.0848  178  GLN   D CG  
9453  C  CD  . GLN   D 109 ? 1.8029 1.5790 1.7316 -0.0346 0.1325  0.0856  178  GLN   D CD  
9454  O  OE1 . GLN   D 109 ? 1.7846 1.5686 1.7203 -0.0335 0.1362  0.0876  178  GLN   D OE1 
9455  N  NE2 . GLN   D 109 ? 1.7846 1.5463 1.6902 -0.0270 0.1306  0.0840  178  GLN   D NE2 
9456  N  N   . GLN   D 110 ? 1.7204 1.5201 1.7092 -0.0669 0.1198  0.0814  179  GLN   D N   
9457  C  CA  . GLN   D 110 ? 1.7101 1.5255 1.7112 -0.0711 0.1082  0.0765  179  GLN   D CA  
9458  C  C   . GLN   D 110 ? 1.7148 1.5426 1.7156 -0.0665 0.1039  0.0745  179  GLN   D C   
9459  O  O   . GLN   D 110 ? 1.7726 1.5976 1.7658 -0.0606 0.1098  0.0770  179  GLN   D O   
9460  C  CB  . GLN   D 110 ? 1.6956 1.5209 1.7219 -0.0814 0.1083  0.0775  179  GLN   D CB  
9461  N  N   . ALA   D 111 ? 1.6475 1.4886 1.6563 -0.0689 0.0933  0.0698  180  ALA   D N   
9462  C  CA  . ALA   D 111 ? 1.5788 1.4314 1.5870 -0.0645 0.0887  0.0676  180  ALA   D CA  
9463  C  C   . ALA   D 111 ? 1.5471 1.4165 1.5722 -0.0703 0.0797  0.0641  180  ALA   D C   
9464  O  O   . ALA   D 111 ? 1.5304 1.4003 1.5562 -0.0734 0.0724  0.0606  180  ALA   D O   
9465  C  CB  . ALA   D 111 ? 1.5662 1.4114 1.5524 -0.0559 0.0843  0.0645  180  ALA   D CB  
9466  N  N   . LYS   D 112 ? 1.5194 1.4019 1.5576 -0.0714 0.0803  0.0651  181  LYS   D N   
9467  C  CA  . LYS   D 112 ? 1.4546 1.3530 1.5059 -0.0751 0.0713  0.0615  181  LYS   D CA  
9468  C  C   . LYS   D 112 ? 1.4851 1.3860 1.5231 -0.0687 0.0641  0.0574  181  LYS   D C   
9469  O  O   . LYS   D 112 ? 1.4748 1.3714 1.5000 -0.0616 0.0670  0.0581  181  LYS   D O   
9470  C  CB  . LYS   D 112 ? 1.4056 1.3169 1.4752 -0.0781 0.0744  0.0640  181  LYS   D CB  
9471  N  N   . VAL   D 113 ? 1.5433 1.4511 1.5848 -0.0713 0.0547  0.0530  182  VAL   D N   
9472  C  CA  . VAL   D 113 ? 1.5209 1.4274 1.5483 -0.0661 0.0476  0.0487  182  VAL   D CA  
9473  C  C   . VAL   D 113 ? 1.5248 1.4460 1.5626 -0.0690 0.0390  0.0450  182  VAL   D C   
9474  O  O   . VAL   D 113 ? 1.5624 1.4899 1.6143 -0.0758 0.0361  0.0445  182  VAL   D O   
9475  C  CB  . VAL   D 113 ? 1.5179 1.4114 1.5335 -0.0659 0.0461  0.0472  182  VAL   D CB  
9476  C  CG1 . VAL   D 113 ? 1.5234 1.4194 1.5314 -0.0635 0.0369  0.0420  182  VAL   D CG1 
9477  C  CG2 . VAL   D 113 ? 1.4966 1.3746 1.4958 -0.0601 0.0535  0.0499  182  VAL   D CG2 
9478  N  N   . GLN   D 114 ? 1.4383 1.3649 1.4697 -0.0637 0.0350  0.0426  183  GLN   D N   
9479  C  CA  . GLN   D 114 ? 1.4194 1.3587 1.4583 -0.0656 0.0268  0.0390  183  GLN   D CA  
9480  C  C   . GLN   D 114 ? 1.4052 1.3401 1.4304 -0.0615 0.0208  0.0348  183  GLN   D C   
9481  O  O   . GLN   D 114 ? 1.4298 1.3615 1.4431 -0.0547 0.0210  0.0339  183  GLN   D O   
9482  C  CB  . GLN   D 114 ? 1.3524 1.3028 1.3970 -0.0634 0.0270  0.0395  183  GLN   D CB  
9483  N  N   . ILE   D 115 ? 1.4446 1.3788 1.4713 -0.0653 0.0155  0.0322  184  ILE   D N   
9484  C  CA  . ILE   D 115 ? 1.4509 1.3804 1.4648 -0.0614 0.0104  0.0283  184  ILE   D CA  
9485  C  C   . ILE   D 115 ? 1.4670 1.4061 1.4800 -0.0575 0.0058  0.0256  184  ILE   D C   
9486  O  O   . ILE   D 115 ? 1.5737 1.5245 1.5980 -0.0605 0.0030  0.0251  184  ILE   D O   
9487  C  CB  . ILE   D 115 ? 1.5267 1.4543 1.5433 -0.0665 0.0055  0.0260  184  ILE   D CB  
9488  C  CG1 . ILE   D 115 ? 1.4528 1.3695 1.4693 -0.0700 0.0101  0.0285  184  ILE   D CG1 
9489  C  CG2 . ILE   D 115 ? 1.5021 1.4258 1.5062 -0.0623 0.0002  0.0219  184  ILE   D CG2 
9490  C  CD1 . ILE   D 115 ? 1.3487 1.2517 1.3494 -0.0645 0.0145  0.0296  184  ILE   D CD1 
9491  N  N   . LEU   D 116 ? 1.4070 1.3411 1.4066 -0.0507 0.0051  0.0239  185  LEU   D N   
9492  C  CA  . LEU   D 116 ? 1.4403 1.3832 1.4393 -0.0469 0.0009  0.0213  185  LEU   D CA  
9493  C  C   . LEU   D 116 ? 1.5152 1.4638 1.5170 -0.0492 -0.0061 0.0174  185  LEU   D C   
9494  O  O   . LEU   D 116 ? 1.5030 1.4459 1.5023 -0.0518 -0.0080 0.0161  185  LEU   D O   
9495  C  CB  . LEU   D 116 ? 1.3867 1.3226 1.3714 -0.0389 0.0017  0.0203  185  LEU   D CB  
9496  C  CG  . LEU   D 116 ? 1.3340 1.2640 1.3127 -0.0344 0.0078  0.0236  185  LEU   D CG  
9497  C  CD1 . LEU   D 116 ? 1.2455 1.1744 1.2138 -0.0266 0.0052  0.0211  185  LEU   D CD1 
9498  C  CD2 . LEU   D 116 ? 1.3226 1.2603 1.3129 -0.0373 0.0119  0.0269  185  LEU   D CD2 
9499  N  N   . PRO   D 117 ? 1.6632 1.6225 1.6698 -0.0484 -0.0099 0.0155  186  PRO   D N   
9500  C  CA  . PRO   D 117 ? 1.6629 1.6279 1.6727 -0.0508 -0.0160 0.0121  186  PRO   D CA  
9501  C  C   . PRO   D 117 ? 1.6388 1.5990 1.6374 -0.0460 -0.0192 0.0086  186  PRO   D C   
9502  O  O   . PRO   D 117 ? 1.6125 1.5719 1.6044 -0.0402 -0.0189 0.0078  186  PRO   D O   
9503  C  CB  . PRO   D 117 ? 1.6779 1.6555 1.6965 -0.0512 -0.0178 0.0119  186  PRO   D CB  
9504  C  CG  . PRO   D 117 ? 1.6492 1.6263 1.6640 -0.0460 -0.0139 0.0137  186  PRO   D CG  
9505  C  CD  . PRO   D 117 ? 1.6295 1.5965 1.6402 -0.0460 -0.0082 0.0168  186  PRO   D CD  
9506  N  N   . GLU   D 118 ? 1.4952 1.4523 1.4920 -0.0485 -0.0226 0.0064  187  GLU   D N   
9507  C  CA  . GLU   D 118 ? 1.4193 1.3740 1.4077 -0.0446 -0.0263 0.0027  187  GLU   D CA  
9508  C  C   . GLU   D 118 ? 1.3807 1.3435 1.3750 -0.0475 -0.0310 0.0003  187  GLU   D C   
9509  O  O   . GLU   D 118 ? 1.4063 1.3665 1.4017 -0.0516 -0.0332 -0.0005 187  GLU   D O   
9510  C  CB  . GLU   D 118 ? 1.3971 1.3393 1.3757 -0.0438 -0.0259 0.0021  187  GLU   D CB  
9511  C  CG  . GLU   D 118 ? 1.3099 1.2498 1.2805 -0.0399 -0.0297 -0.0019 187  GLU   D CG  
9512  C  CD  . GLU   D 118 ? 1.2669 1.2046 1.2295 -0.0325 -0.0291 -0.0030 187  GLU   D CD  
9513  O  OE1 . GLU   D 118 ? 1.2508 1.1805 1.2070 -0.0297 -0.0257 -0.0012 187  GLU   D OE1 
9514  O  OE2 . GLU   D 118 ? 1.2387 1.1821 1.2013 -0.0293 -0.0321 -0.0058 187  GLU   D OE2 
9515  N  N   . CYS   D 119 ? 1.3826 1.3545 1.3800 -0.0452 -0.0327 -0.0009 188  CYS   D N   
9516  C  CA  . CYS   D 119 ? 1.3235 1.3042 1.3277 -0.0480 -0.0364 -0.0025 188  CYS   D CA  
9517  C  C   . CYS   D 119 ? 1.2595 1.2382 1.2574 -0.0458 -0.0397 -0.0061 188  CYS   D C   
9518  O  O   . CYS   D 119 ? 1.1815 1.1612 1.1751 -0.0407 -0.0401 -0.0079 188  CYS   D O   
9519  C  CB  . CYS   D 119 ? 1.3214 1.3123 1.3320 -0.0466 -0.0361 -0.0019 188  CYS   D CB  
9520  S  SG  . CYS   D 119 ? 1.4157 1.4066 1.4290 -0.0456 -0.0310 0.0020  188  CYS   D SG  
9521  N  N   . VAL   D 120 ? 1.2683 1.2442 1.2659 -0.0495 -0.0422 -0.0072 189  VAL   D N   
9522  C  CA  . VAL   D 120 ? 1.1916 1.1646 1.1827 -0.0475 -0.0450 -0.0105 189  VAL   D CA  
9523  C  C   . VAL   D 120 ? 1.1809 1.1628 1.1770 -0.0484 -0.0477 -0.0120 189  VAL   D C   
9524  O  O   . VAL   D 120 ? 1.2302 1.2164 1.2330 -0.0529 -0.0492 -0.0111 189  VAL   D O   
9525  C  CB  . VAL   D 120 ? 1.1129 1.0767 1.0994 -0.0505 -0.0463 -0.0111 189  VAL   D CB  
9526  C  CG1 . VAL   D 120 ? 1.1344 1.0958 1.1146 -0.0485 -0.0491 -0.0144 189  VAL   D CG1 
9527  C  CG2 . VAL   D 120 ? 1.1881 1.1420 1.1684 -0.0490 -0.0434 -0.0097 189  VAL   D CG2 
9528  N  N   . LEU   D 121 ? 1.1891 1.1738 1.1823 -0.0441 -0.0483 -0.0143 190  LEU   D N   
9529  C  CA  . LEU   D 121 ? 1.1494 1.1427 1.1475 -0.0444 -0.0500 -0.0154 190  LEU   D CA  
9530  C  C   . LEU   D 121 ? 1.1548 1.1454 1.1477 -0.0437 -0.0521 -0.0182 190  LEU   D C   
9531  O  O   . LEU   D 121 ? 1.1993 1.1828 1.1847 -0.0410 -0.0520 -0.0199 190  LEU   D O   
9532  C  CB  . LEU   D 121 ? 1.1196 1.1196 1.1202 -0.0401 -0.0487 -0.0156 190  LEU   D CB  
9533  C  CG  . LEU   D 121 ? 1.0517 1.0585 1.0598 -0.0412 -0.0472 -0.0130 190  LEU   D CG  
9534  C  CD1 . LEU   D 121 ? 1.1021 1.1035 1.1086 -0.0412 -0.0446 -0.0106 190  LEU   D CD1 
9535  C  CD2 . LEU   D 121 ? 0.9362 0.9504 0.9472 -0.0375 -0.0471 -0.0139 190  LEU   D CD2 
9536  N  N   . PRO   D 122 ? 1.1371 1.1328 1.1332 -0.0457 -0.0540 -0.0188 191  PRO   D N   
9537  C  CA  . PRO   D 122 ? 1.1744 1.1679 1.1653 -0.0444 -0.0554 -0.0215 191  PRO   D CA  
9538  C  C   . PRO   D 122 ? 1.1375 1.1348 1.1278 -0.0392 -0.0539 -0.0232 191  PRO   D C   
9539  O  O   . PRO   D 122 ? 1.0938 1.0962 1.0882 -0.0369 -0.0525 -0.0226 191  PRO   D O   
9540  C  CB  . PRO   D 122 ? 1.2362 1.2341 1.2312 -0.0482 -0.0576 -0.0211 191  PRO   D CB  
9541  C  CG  . PRO   D 122 ? 1.2251 1.2312 1.2291 -0.0496 -0.0568 -0.0188 191  PRO   D CG  
9542  C  CD  . PRO   D 122 ? 1.1622 1.1653 1.1666 -0.0493 -0.0548 -0.0170 191  PRO   D CD  
9543  N  N   . SER   D 123 ? 1.1341 1.1287 1.1194 -0.0375 -0.0544 -0.0256 192  SER   D N   
9544  C  CA  . SER   D 123 ? 1.1185 1.1174 1.1047 -0.0330 -0.0530 -0.0274 192  SER   D CA  
9545  C  C   . SER   D 123 ? 1.1293 1.1382 1.1235 -0.0338 -0.0527 -0.0265 192  SER   D C   
9546  O  O   . SER   D 123 ? 1.1988 1.2098 1.1951 -0.0375 -0.0540 -0.0255 192  SER   D O   
9547  C  CB  . SER   D 123 ? 1.1782 1.1722 1.1579 -0.0314 -0.0531 -0.0297 192  SER   D CB  
9548  O  OG  . SER   D 123 ? 1.2154 1.2155 1.1983 -0.0283 -0.0516 -0.0311 192  SER   D OG  
9549  N  N   . THR   D 124 ? 1.1430 1.1575 1.1414 -0.0302 -0.0513 -0.0271 193  THR   D N   
9550  C  CA  . THR   D 124 ? 1.1368 1.1606 1.1429 -0.0307 -0.0509 -0.0263 193  THR   D CA  
9551  C  C   . THR   D 124 ? 1.1518 1.1776 1.1579 -0.0323 -0.0512 -0.0270 193  THR   D C   
9552  O  O   . THR   D 124 ? 1.1382 1.1699 1.1494 -0.0345 -0.0515 -0.0257 193  THR   D O   
9553  C  CB  . THR   D 124 ? 1.1188 1.1476 1.1290 -0.0261 -0.0497 -0.0275 193  THR   D CB  
9554  O  OG1 . THR   D 124 ? 1.1252 1.1501 1.1315 -0.0222 -0.0491 -0.0300 193  THR   D OG1 
9555  C  CG2 . THR   D 124 ? 1.0636 1.0927 1.0755 -0.0251 -0.0497 -0.0260 193  THR   D CG2 
9556  N  N   . MET   D 125 ? 1.1891 1.2094 1.1890 -0.0312 -0.0509 -0.0288 194  MET   D N   
9557  C  CA  . MET   D 125 ? 1.2482 1.2689 1.2464 -0.0319 -0.0506 -0.0295 194  MET   D CA  
9558  C  C   . MET   D 125 ? 1.2809 1.2961 1.2739 -0.0358 -0.0529 -0.0289 194  MET   D C   
9559  O  O   . MET   D 125 ? 1.3177 1.3325 1.3084 -0.0365 -0.0530 -0.0293 194  MET   D O   
9560  C  CB  . MET   D 125 ? 1.2453 1.2631 1.2396 -0.0280 -0.0485 -0.0319 194  MET   D CB  
9561  C  CG  . MET   D 125 ? 1.1709 1.1947 1.1715 -0.0239 -0.0465 -0.0330 194  MET   D CG  
9562  S  SD  . MET   D 125 ? 1.1073 1.1416 1.1173 -0.0244 -0.0453 -0.0322 194  MET   D SD  
9563  C  CE  . MET   D 125 ? 1.0888 1.1284 1.1052 -0.0258 -0.0470 -0.0302 194  MET   D CE  
9564  N  N   . SER   D 126 ? 1.2683 1.2787 1.2592 -0.0383 -0.0549 -0.0279 195  SER   D N   
9565  C  CA  . SER   D 126 ? 1.2586 1.2628 1.2445 -0.0418 -0.0576 -0.0278 195  SER   D CA  
9566  C  C   . SER   D 126 ? 1.3231 1.3321 1.3128 -0.0448 -0.0592 -0.0266 195  SER   D C   
9567  O  O   . SER   D 126 ? 1.4085 1.4131 1.3930 -0.0462 -0.0612 -0.0273 195  SER   D O   
9568  C  CB  . SER   D 126 ? 1.2442 1.2438 1.2296 -0.0443 -0.0592 -0.0266 195  SER   D CB  
9569  O  OG  . SER   D 126 ? 1.2648 1.2709 1.2586 -0.0465 -0.0593 -0.0244 195  SER   D OG  
9570  N  N   . ALA   D 127 ? 1.3141 1.3318 1.3124 -0.0453 -0.0585 -0.0250 196  ALA   D N   
9571  C  CA  . ALA   D 127 ? 1.3130 1.3357 1.3154 -0.0479 -0.0601 -0.0239 196  ALA   D CA  
9572  C  C   . ALA   D 127 ? 1.3562 1.3797 1.3556 -0.0460 -0.0589 -0.0250 196  ALA   D C   
9573  O  O   . ALA   D 127 ? 1.3532 1.3742 1.3490 -0.0477 -0.0609 -0.0251 196  ALA   D O   
9574  C  CB  . ALA   D 127 ? 1.2916 1.3232 1.3035 -0.0483 -0.0592 -0.0220 196  ALA   D CB  
9575  N  N   . VAL   D 128 ? 1.4774 1.5042 1.4782 -0.0423 -0.0555 -0.0260 197  VAL   D N   
9576  C  CA  . VAL   D 128 ? 1.4990 1.5271 1.4983 -0.0405 -0.0535 -0.0269 197  VAL   D CA  
9577  C  C   . VAL   D 128 ? 1.5084 1.5283 1.4983 -0.0383 -0.0523 -0.0288 197  VAL   D C   
9578  O  O   . VAL   D 128 ? 1.5219 1.5417 1.5095 -0.0365 -0.0500 -0.0296 197  VAL   D O   
9579  C  CB  . VAL   D 128 ? 1.4875 1.5236 1.4944 -0.0377 -0.0504 -0.0269 197  VAL   D CB  
9580  C  CG1 . VAL   D 128 ? 1.4417 1.4856 1.4568 -0.0396 -0.0514 -0.0250 197  VAL   D CG1 
9581  C  CG2 . VAL   D 128 ? 1.4561 1.4912 1.4635 -0.0347 -0.0491 -0.0281 197  VAL   D CG2 
9582  N  N   . GLN   D 129 ? 1.4402 1.4529 1.4245 -0.0384 -0.0536 -0.0296 198  GLN   D N   
9583  C  CA  . GLN   D 129 ? 1.4426 1.4472 1.4178 -0.0359 -0.0524 -0.0316 198  GLN   D CA  
9584  C  C   . GLN   D 129 ? 1.5052 1.5050 1.4731 -0.0367 -0.0531 -0.0319 198  GLN   D C   
9585  O  O   . GLN   D 129 ? 1.5559 1.5518 1.5204 -0.0398 -0.0569 -0.0313 198  GLN   D O   
9586  C  CB  . GLN   D 129 ? 1.4206 1.4176 1.3905 -0.0366 -0.0545 -0.0321 198  GLN   D CB  
9587  C  CG  . GLN   D 129 ? 1.4449 1.4341 1.4063 -0.0332 -0.0527 -0.0343 198  GLN   D CG  
9588  C  CD  . GLN   D 129 ? 1.4346 1.4286 1.4001 -0.0288 -0.0485 -0.0353 198  GLN   D CD  
9589  O  OE1 . GLN   D 129 ? 1.4005 1.3973 1.3669 -0.0270 -0.0457 -0.0358 198  GLN   D OE1 
9590  N  NE2 . GLN   D 129 ? 1.4549 1.4496 1.4229 -0.0269 -0.0480 -0.0358 198  GLN   D NE2 
9591  N  N   . LEU   D 130 ? 1.4756 1.4756 1.4414 -0.0336 -0.0493 -0.0328 199  LEU   D N   
9592  C  CA  . LEU   D 130 ? 1.4569 1.4508 1.4140 -0.0335 -0.0493 -0.0331 199  LEU   D CA  
9593  C  C   . LEU   D 130 ? 1.4857 1.4678 1.4309 -0.0334 -0.0514 -0.0345 199  LEU   D C   
9594  O  O   . LEU   D 130 ? 1.5103 1.4884 1.4525 -0.0312 -0.0501 -0.0358 199  LEU   D O   
9595  C  CB  . LEU   D 130 ? 1.4028 1.3989 1.3603 -0.0300 -0.0438 -0.0337 199  LEU   D CB  
9596  C  CG  . LEU   D 130 ? 1.3604 1.3665 1.3277 -0.0303 -0.0417 -0.0324 199  LEU   D CG  
9597  C  CD1 . LEU   D 130 ? 1.3537 1.3668 1.3303 -0.0278 -0.0387 -0.0330 199  LEU   D CD1 
9598  C  CD2 . LEU   D 130 ? 1.3225 1.3260 1.2847 -0.0290 -0.0386 -0.0323 199  LEU   D CD2 
9599  N  N   . GLU   D 131 ? 1.5091 1.4851 1.4471 -0.0355 -0.0550 -0.0344 200  GLU   D N   
9600  C  CA  . GLU   D 131 ? 1.5410 1.5054 1.4678 -0.0358 -0.0581 -0.0357 200  GLU   D CA  
9601  C  C   . GLU   D 131 ? 1.5708 1.5275 1.4878 -0.0315 -0.0543 -0.0375 200  GLU   D C   
9602  O  O   . GLU   D 131 ? 1.6111 1.5596 1.5210 -0.0308 -0.0556 -0.0388 200  GLU   D O   
9603  C  CB  . GLU   D 131 ? 1.5587 1.5182 1.4800 -0.0387 -0.0632 -0.0354 200  GLU   D CB  
9604  C  CG  . GLU   D 131 ? 1.5358 1.5001 1.4656 -0.0433 -0.0682 -0.0340 200  GLU   D CG  
9605  C  CD  . GLU   D 131 ? 1.5469 1.5239 1.4896 -0.0443 -0.0663 -0.0321 200  GLU   D CD  
9606  O  OE1 . GLU   D 131 ? 1.5253 1.5062 1.4688 -0.0426 -0.0634 -0.0317 200  GLU   D OE1 
9607  O  OE2 . GLU   D 131 ? 1.5406 1.5234 1.4923 -0.0466 -0.0676 -0.0311 200  GLU   D OE2 
9608  N  N   . SER   D 132 ? 1.5155 1.4746 1.4324 -0.0286 -0.0492 -0.0374 201  SER   D N   
9609  C  CA  . SER   D 132 ? 1.5110 1.4632 1.4194 -0.0243 -0.0448 -0.0390 201  SER   D CA  
9610  C  C   . SER   D 132 ? 1.5660 1.5218 1.4803 -0.0218 -0.0418 -0.0399 201  SER   D C   
9611  O  O   . SER   D 132 ? 1.6002 1.5488 1.5069 -0.0187 -0.0397 -0.0414 201  SER   D O   
9612  C  CB  . SER   D 132 ? 1.3921 1.3455 1.2990 -0.0219 -0.0398 -0.0385 201  SER   D CB  
9613  O  OG  . SER   D 132 ? 1.3152 1.2799 1.2347 -0.0208 -0.0353 -0.0378 201  SER   D OG  
9614  N  N   . LEU   D 133 ? 1.5527 1.5191 1.4798 -0.0230 -0.0418 -0.0390 202  LEU   D N   
9615  C  CA  . LEU   D 133 ? 1.5098 1.4801 1.4431 -0.0207 -0.0399 -0.0398 202  LEU   D CA  
9616  C  C   . LEU   D 133 ? 1.5865 1.5522 1.5173 -0.0223 -0.0439 -0.0402 202  LEU   D C   
9617  O  O   . LEU   D 133 ? 1.6788 1.6441 1.6108 -0.0198 -0.0426 -0.0412 202  LEU   D O   
9618  C  CB  . LEU   D 133 ? 1.4534 1.4363 1.4006 -0.0209 -0.0384 -0.0387 202  LEU   D CB  
9619  C  CG  . LEU   D 133 ? 1.4483 1.4381 1.4023 -0.0182 -0.0331 -0.0389 202  LEU   D CG  
9620  C  CD1 . LEU   D 133 ? 1.4150 1.4012 1.3627 -0.0182 -0.0310 -0.0384 202  LEU   D CD1 
9621  C  CD2 . LEU   D 133 ? 1.4302 1.4315 1.3974 -0.0195 -0.0335 -0.0377 202  LEU   D CD2 
9622  N  N   . ASN   D 134 ? 1.6154 1.5780 1.5437 -0.0264 -0.0489 -0.0392 203  ASN   D N   
9623  C  CA  . ASN   D 134 ? 1.6333 1.5895 1.5578 -0.0282 -0.0527 -0.0396 203  ASN   D CA  
9624  C  C   . ASN   D 134 ? 1.7570 1.7035 1.6716 -0.0249 -0.0513 -0.0416 203  ASN   D C   
9625  O  O   . ASN   D 134 ? 1.8187 1.7626 1.7330 -0.0243 -0.0520 -0.0421 203  ASN   D O   
9626  C  CB  . ASN   D 134 ? 1.6159 1.5672 1.5363 -0.0326 -0.0579 -0.0389 203  ASN   D CB  
9627  C  CG  . ASN   D 134 ? 1.5942 1.5545 1.5253 -0.0365 -0.0603 -0.0368 203  ASN   D CG  
9628  O  OD1 . ASN   D 134 ? 1.5808 1.5491 1.5212 -0.0365 -0.0587 -0.0358 203  ASN   D OD1 
9629  N  ND2 . ASN   D 134 ? 1.5684 1.5268 1.4976 -0.0398 -0.0642 -0.0362 203  ASN   D ND2 
9630  N  N   . LYS   D 135 ? 1.8666 1.8074 1.7726 -0.0223 -0.0491 -0.0427 204  LYS   D N   
9631  C  CA  . LYS   D 135 ? 1.8868 1.8163 1.7810 -0.0194 -0.0483 -0.0446 204  LYS   D CA  
9632  C  C   . LYS   D 135 ? 1.8871 1.8180 1.7842 -0.0158 -0.0454 -0.0457 204  LYS   D C   
9633  O  O   . LYS   D 135 ? 1.8452 1.7685 1.7364 -0.0153 -0.0472 -0.0467 204  LYS   D O   
9634  C  CB  . LYS   D 135 ? 1.8289 1.7536 1.7147 -0.0166 -0.0450 -0.0453 204  LYS   D CB  
9635  C  CG  . LYS   D 135 ? 1.7537 1.6715 1.6309 -0.0192 -0.0490 -0.0449 204  LYS   D CG  
9636  C  CD  . LYS   D 135 ? 1.7549 1.6741 1.6301 -0.0174 -0.0452 -0.0444 204  LYS   D CD  
9637  C  CE  . LYS   D 135 ? 1.7795 1.6970 1.6519 -0.0211 -0.0501 -0.0434 204  LYS   D CE  
9638  N  NZ  . LYS   D 135 ? 1.7741 1.6940 1.6458 -0.0200 -0.0468 -0.0424 204  LYS   D NZ  
9639  N  N   . CYS   D 136 ? 2.2641 2.2044 2.1706 -0.0131 -0.0410 -0.0456 205  CYS   D N   
9640  C  CA  . CYS   D 136 ? 2.2905 2.2326 2.2006 -0.0093 -0.0385 -0.0468 205  CYS   D CA  
9641  C  C   . CYS   D 136 ? 2.2415 2.1929 2.1632 -0.0104 -0.0397 -0.0459 205  CYS   D C   
9642  O  O   . CYS   D 136 ? 2.2382 2.1953 2.1669 -0.0071 -0.0372 -0.0467 205  CYS   D O   
9643  C  CB  . CYS   D 136 ? 2.3238 2.2686 2.2356 -0.0047 -0.0327 -0.0479 205  CYS   D CB  
9644  S  SG  . CYS   D 136 ? 2.4350 2.3762 2.3453 0.0009  -0.0301 -0.0503 205  CYS   D SG  
9645  N  N   . GLN   D 137 ? 1.9227 1.8754 1.8466 -0.0149 -0.0437 -0.0442 206  GLN   D N   
9646  C  CA  . GLN   D 137 ? 1.8362 1.7957 1.7691 -0.0159 -0.0449 -0.0432 206  GLN   D CA  
9647  C  C   . GLN   D 137 ? 1.8530 1.8068 1.7824 -0.0139 -0.0457 -0.0443 206  GLN   D C   
9648  O  O   . GLN   D 137 ? 1.8729 1.8313 1.8086 -0.0131 -0.0458 -0.0438 206  GLN   D O   
9649  C  CB  . GLN   D 137 ? 1.7191 1.6810 1.6551 -0.0212 -0.0485 -0.0411 206  GLN   D CB  
9650  C  CG  . GLN   D 137 ? 1.6684 1.6392 1.6150 -0.0225 -0.0490 -0.0395 206  GLN   D CG  
9651  C  CD  . GLN   D 137 ? 1.5812 1.5620 1.5371 -0.0195 -0.0458 -0.0398 206  GLN   D CD  
9652  O  OE1 . GLN   D 137 ? 1.5104 1.4960 1.4726 -0.0183 -0.0458 -0.0395 206  GLN   D OE1 
9653  N  NE2 . GLN   D 137 ? 1.5478 1.5313 1.5044 -0.0182 -0.0433 -0.0403 206  GLN   D NE2 
9654  N  N   . ILE   D 138 ? 1.8224 1.7655 1.7410 -0.0127 -0.0461 -0.0456 207  ILE   D N   
9655  C  CA  . ILE   D 138 ? 1.8348 1.7714 1.7488 -0.0103 -0.0466 -0.0468 207  ILE   D CA  
9656  C  C   . ILE   D 138 ? 1.8817 1.8207 1.7976 -0.0044 -0.0428 -0.0487 207  ILE   D C   
9657  O  O   . ILE   D 138 ? 1.9152 1.8534 1.8286 -0.0022 -0.0399 -0.0498 207  ILE   D O   
9658  C  CB  . ILE   D 138 ? 1.7760 1.6997 1.6775 -0.0117 -0.0490 -0.0475 207  ILE   D CB  
9659  C  CG1 . ILE   D 138 ? 1.7770 1.6983 1.6787 -0.0171 -0.0532 -0.0458 207  ILE   D CG1 
9660  C  CG2 . ILE   D 138 ? 1.8335 1.7493 1.7280 -0.0074 -0.0480 -0.0494 207  ILE   D CG2 
9661  C  CD1 . ILE   D 138 ? 1.7135 1.6218 1.6041 -0.0186 -0.0561 -0.0465 207  ILE   D CD1 
9662  N  N   . PHE   D 139 ? 1.9302 1.8719 1.8508 -0.0018 -0.0427 -0.0492 208  PHE   D N   
9663  C  CA  . PHE   D 139 ? 1.9379 1.8829 1.8624 0.0039  -0.0397 -0.0511 208  PHE   D CA  
9664  C  C   . PHE   D 139 ? 1.9662 1.9011 1.8816 0.0073  -0.0399 -0.0529 208  PHE   D C   
9665  O  O   . PHE   D 139 ? 2.0317 1.9595 1.9411 0.0057  -0.0427 -0.0524 208  PHE   D O   
9666  C  CB  . PHE   D 139 ? 1.9089 1.8632 1.8443 0.0051  -0.0401 -0.0507 208  PHE   D CB  
9667  C  CG  . PHE   D 139 ? 1.9389 1.9010 1.8816 0.0009  -0.0412 -0.0485 208  PHE   D CG  
9668  C  CD1 . PHE   D 139 ? 1.9131 1.8822 1.8614 -0.0003 -0.0393 -0.0480 208  PHE   D CD1 
9669  C  CD2 . PHE   D 139 ? 1.9019 1.8641 1.8459 -0.0016 -0.0439 -0.0468 208  PHE   D CD2 
9670  C  CE1 . PHE   D 139 ? 1.8552 1.8313 1.8100 -0.0040 -0.0404 -0.0460 208  PHE   D CE1 
9671  C  CE2 . PHE   D 139 ? 1.8400 1.8094 1.7908 -0.0053 -0.0448 -0.0448 208  PHE   D CE2 
9672  C  CZ  . PHE   D 139 ? 1.8393 1.8158 1.7956 -0.0065 -0.0432 -0.0444 208  PHE   D CZ  
9673  N  N   . PRO   D 140 ? 1.8389 1.7729 1.7533 0.0122  -0.0369 -0.0550 209  PRO   D N   
9674  C  CA  . PRO   D 140 ? 1.9096 1.8345 1.8160 0.0160  -0.0371 -0.0568 209  PRO   D CA  
9675  C  C   . PRO   D 140 ? 1.9535 1.8794 1.8632 0.0179  -0.0391 -0.0570 209  PRO   D C   
9676  O  O   . PRO   D 140 ? 1.8681 1.8025 1.7871 0.0173  -0.0399 -0.0561 209  PRO   D O   
9677  C  CB  . PRO   D 140 ? 1.7940 1.7207 1.7020 0.0210  -0.0327 -0.0588 209  PRO   D CB  
9678  C  CG  . PRO   D 140 ? 1.7047 1.6369 1.6164 0.0187  -0.0304 -0.0578 209  PRO   D CG  
9679  C  CD  . PRO   D 140 ? 1.7364 1.6766 1.6561 0.0143  -0.0328 -0.0557 209  PRO   D CD  
9680  N  N   . SER   D 141 ? 1.8643 1.7806 1.7653 0.0207  -0.0400 -0.0583 210  SER   D N   
9681  C  CA  . SER   D 141 ? 1.9119 1.8259 1.8127 0.0227  -0.0422 -0.0585 210  SER   D CA  
9682  C  C   . SER   D 141 ? 1.9235 1.8473 1.8355 0.0272  -0.0413 -0.0597 210  SER   D C   
9683  O  O   . SER   D 141 ? 1.9099 1.8396 1.8280 0.0303  -0.0385 -0.0612 210  SER   D O   
9684  C  CB  . SER   D 141 ? 1.9546 1.8559 1.8435 0.0255  -0.0428 -0.0600 210  SER   D CB  
9685  O  OG  . SER   D 141 ? 1.9601 1.8552 1.8445 0.0250  -0.0455 -0.0592 210  SER   D OG  
9686  N  N   . LYS   D 142 ? 2.0343 1.9594 1.9489 0.0276  -0.0436 -0.0590 211  LYS   D N   
9687  C  CA  . LYS   D 142 ? 2.0070 1.9411 1.9321 0.0314  -0.0439 -0.0601 211  LYS   D CA  
9688  C  C   . LYS   D 142 ? 2.2205 2.1498 2.1429 0.0379  -0.0447 -0.0626 211  LYS   D C   
9689  O  O   . LYS   D 142 ? 2.2518 2.1732 2.1668 0.0386  -0.0469 -0.0622 211  LYS   D O   
9690  C  CB  . LYS   D 142 ? 1.8291 1.7669 1.7581 0.0286  -0.0461 -0.0579 211  LYS   D CB  
9691  N  N   . PRO   D 143 ? 2.4741 2.4081 2.4026 0.0427  -0.0428 -0.0651 212  PRO   D N   
9692  C  CA  . PRO   D 143 ? 2.4828 2.4125 2.4093 0.0492  -0.0438 -0.0677 212  PRO   D CA  
9693  C  C   . PRO   D 143 ? 2.4709 2.4043 2.4031 0.0523  -0.0470 -0.0683 212  PRO   D C   
9694  O  O   . PRO   D 143 ? 2.4482 2.3911 2.3903 0.0511  -0.0476 -0.0677 212  PRO   D O   
9695  C  CB  . PRO   D 143 ? 2.4686 2.4039 2.4023 0.0528  -0.0404 -0.0700 212  PRO   D CB  
9696  C  CG  . PRO   D 143 ? 2.4163 2.3551 2.3512 0.0479  -0.0373 -0.0684 212  PRO   D CG  
9697  C  CD  . PRO   D 143 ? 2.3884 2.3307 2.3252 0.0424  -0.0393 -0.0657 212  PRO   D CD  
9698  N  N   . VAL   D 144 ? 2.3234 2.2486 2.2485 0.0568  -0.0492 -0.0697 213  VAL   D N   
9699  C  CA  . VAL   D 144 ? 2.2711 2.1980 2.1998 0.0608  -0.0526 -0.0706 213  VAL   D CA  
9700  C  C   . VAL   D 144 ? 2.2203 2.1527 2.1580 0.0676  -0.0530 -0.0742 213  VAL   D C   
9701  O  O   . VAL   D 144 ? 2.1684 2.1115 2.1190 0.0690  -0.0536 -0.0752 213  VAL   D O   
9702  C  CB  . VAL   D 144 ? 2.2070 2.1211 2.1223 0.0618  -0.0551 -0.0698 213  VAL   D CB  
9703  C  CG1 . VAL   D 144 ? 2.1691 2.0785 2.0774 0.0549  -0.0546 -0.0662 213  VAL   D CG1 
9704  C  CG2 . VAL   D 144 ? 2.2022 2.1065 2.1084 0.0657  -0.0546 -0.0717 213  VAL   D CG2 
9705  N  N   . SER   D 151 ? 1.8352 1.8136 1.8234 0.0597  -0.0444 -0.0737 220  SER   D N   
9706  C  CA  . SER   D 151 ? 1.8720 1.8563 1.8683 0.0614  -0.0484 -0.0744 220  SER   D CA  
9707  C  C   . SER   D 151 ? 1.8997 1.8872 1.8964 0.0559  -0.0493 -0.0715 220  SER   D C   
9708  O  O   . SER   D 151 ? 1.8363 1.8177 1.8228 0.0513  -0.0486 -0.0688 220  SER   D O   
9709  C  CB  . SER   D 151 ? 1.8411 1.8364 1.8542 0.0650  -0.0477 -0.0771 220  SER   D CB  
9710  O  OG  . SER   D 151 ? 1.8885 1.8884 1.9087 0.0674  -0.0523 -0.0783 220  SER   D OG  
9711  N  N   . TYR   D 152 ? 2.0287 2.0255 2.0372 0.0565  -0.0510 -0.0721 221  TYR   D N   
9712  C  CA  . TYR   D 152 ? 2.0234 2.0244 2.0339 0.0516  -0.0517 -0.0694 221  TYR   D CA  
9713  C  C   . TYR   D 152 ? 1.9867 1.9961 2.0055 0.0473  -0.0477 -0.0683 221  TYR   D C   
9714  O  O   . TYR   D 152 ? 1.9669 1.9793 1.9864 0.0428  -0.0477 -0.0658 221  TYR   D O   
9715  C  CB  . TYR   D 152 ? 2.0365 2.0421 2.0542 0.0546  -0.0560 -0.0706 221  TYR   D CB  
9716  N  N   . LYS   D 153 ? 1.8057 1.8185 1.8304 0.0488  -0.0441 -0.0698 222  LYS   D N   
9717  C  CA  . LYS   D 153 ? 1.6796 1.6982 1.7096 0.0449  -0.0397 -0.0685 222  LYS   D CA  
9718  C  C   . LYS   D 153 ? 1.6080 1.6194 1.6253 0.0399  -0.0377 -0.0657 222  LYS   D C   
9719  O  O   . LYS   D 153 ? 1.5568 1.5718 1.5761 0.0359  -0.0348 -0.0640 222  LYS   D O   
9720  C  CB  . LYS   D 153 ? 1.6298 1.6527 1.6686 0.0482  -0.0358 -0.0708 222  LYS   D CB  
9721  N  N   . TRP   D 154 ? 1.6193 1.6203 1.6236 0.0402  -0.0394 -0.0653 223  TRP   D N   
9722  C  CA  . TRP   D 154 ? 1.5412 1.5353 1.5339 0.0351  -0.0388 -0.0626 223  TRP   D CA  
9723  C  C   . TRP   D 154 ? 1.5223 1.5206 1.5173 0.0304  -0.0404 -0.0600 223  TRP   D C   
9724  O  O   . TRP   D 154 ? 1.4794 1.4788 1.4731 0.0257  -0.0387 -0.0580 223  TRP   D O   
9725  C  CB  . TRP   D 154 ? 1.4887 1.4711 1.4685 0.0365  -0.0410 -0.0627 223  TRP   D CB  
9726  C  CG  . TRP   D 154 ? 1.4805 1.4547 1.4484 0.0317  -0.0406 -0.0605 223  TRP   D CG  
9727  C  CD1 . TRP   D 154 ? 1.5690 1.5362 1.5286 0.0313  -0.0384 -0.0608 223  TRP   D CD1 
9728  C  CD2 . TRP   D 154 ? 1.4490 1.4205 1.4121 0.0269  -0.0427 -0.0578 223  TRP   D CD2 
9729  N  NE1 . TRP   D 154 ? 1.6317 1.5922 1.5819 0.0263  -0.0395 -0.0585 223  TRP   D NE1 
9730  C  CE2 . TRP   D 154 ? 1.5453 1.5086 1.4981 0.0235  -0.0419 -0.0566 223  TRP   D CE2 
9731  C  CE3 . TRP   D 154 ? 1.3716 1.3466 1.3383 0.0253  -0.0450 -0.0562 223  TRP   D CE3 
9732  C  CZ2 . TRP   D 154 ? 1.4877 1.4468 1.4349 0.0184  -0.0436 -0.0541 223  TRP   D CZ2 
9733  C  CZ3 . TRP   D 154 ? 1.3916 1.3625 1.3524 0.0204  -0.0461 -0.0535 223  TRP   D CZ3 
9734  C  CH2 . TRP   D 154 ? 1.4038 1.3672 1.3556 0.0168  -0.0454 -0.0525 223  TRP   D CH2 
9735  N  N   . TRP   D 155 ? 1.5362 1.5368 1.5348 0.0318  -0.0437 -0.0601 224  TRP   D N   
9736  C  CA  . TRP   D 155 ? 1.4189 1.4229 1.4191 0.0278  -0.0453 -0.0576 224  TRP   D CA  
9737  C  C   . TRP   D 155 ? 1.4140 1.4289 1.4260 0.0259  -0.0437 -0.0573 224  TRP   D C   
9738  O  O   . TRP   D 155 ? 1.4199 1.4379 1.4334 0.0222  -0.0444 -0.0551 224  TRP   D O   
9739  C  CB  . TRP   D 155 ? 1.4040 1.4063 1.4035 0.0306  -0.0490 -0.0580 224  TRP   D CB  
9740  C  CG  . TRP   D 155 ? 1.3262 1.3174 1.3132 0.0312  -0.0504 -0.0574 224  TRP   D CG  
9741  C  CD1 . TRP   D 155 ? 1.3436 1.3281 1.3253 0.0360  -0.0515 -0.0594 224  TRP   D CD1 
9742  C  CD2 . TRP   D 155 ? 1.2858 1.2710 1.2644 0.0268  -0.0508 -0.0544 224  TRP   D CD2 
9743  N  NE1 . TRP   D 155 ? 1.2883 1.2625 1.2581 0.0348  -0.0524 -0.0579 224  TRP   D NE1 
9744  C  CE2 . TRP   D 155 ? 1.3015 1.2761 1.2696 0.0291  -0.0519 -0.0548 224  TRP   D CE2 
9745  C  CE3 . TRP   D 155 ? 1.2674 1.2553 1.2467 0.0213  -0.0503 -0.0515 224  TRP   D CE3 
9746  C  CZ2 . TRP   D 155 ? 1.3292 1.2957 1.2879 0.0257  -0.0523 -0.0523 224  TRP   D CZ2 
9747  C  CZ3 . TRP   D 155 ? 1.2586 1.2389 1.2291 0.0180  -0.0508 -0.0491 224  TRP   D CZ3 
9748  C  CH2 . TRP   D 155 ? 1.2864 1.2562 1.2471 0.0201  -0.0517 -0.0495 224  TRP   D CH2 
9749  N  N   . GLN   D 156 ? 1.4811 1.5017 1.5019 0.0286  -0.0415 -0.0594 225  GLN   D N   
9750  C  CA  . GLN   D 156 ? 1.4965 1.5262 1.5275 0.0263  -0.0391 -0.0588 225  GLN   D CA  
9751  C  C   . GLN   D 156 ? 1.4842 1.5113 1.5096 0.0224  -0.0354 -0.0571 225  GLN   D C   
9752  O  O   . GLN   D 156 ? 1.4585 1.4890 1.4853 0.0182  -0.0347 -0.0550 225  GLN   D O   
9753  C  CB  . GLN   D 156 ? 1.5074 1.5443 1.5511 0.0306  -0.0379 -0.0617 225  GLN   D CB  
9754  C  CG  . GLN   D 156 ? 1.5869 1.6252 1.6355 0.0352  -0.0422 -0.0639 225  GLN   D CG  
9755  C  CD  . GLN   D 156 ? 1.6342 1.6739 1.6825 0.0335  -0.0460 -0.0624 225  GLN   D CD  
9756  O  OE1 . GLN   D 156 ? 1.5519 1.5987 1.6079 0.0309  -0.0457 -0.0613 225  GLN   D OE1 
9757  N  NE2 . GLN   D 156 ? 1.6311 1.6634 1.6702 0.0351  -0.0493 -0.0622 225  GLN   D NE2 
9758  N  N   . LYS   D 157 ? 1.4606 1.4812 1.4790 0.0240  -0.0332 -0.0580 226  LYS   D N   
9759  C  CA  . LYS   D 157 ? 1.3321 1.3478 1.3421 0.0206  -0.0305 -0.0565 226  LYS   D CA  
9760  C  C   . LYS   D 157 ? 1.2593 1.2701 1.2605 0.0159  -0.0332 -0.0539 226  LYS   D C   
9761  O  O   . LYS   D 157 ? 1.2189 1.2305 1.2185 0.0118  -0.0322 -0.0520 226  LYS   D O   
9762  C  CB  . LYS   D 157 ? 1.3550 1.3629 1.3572 0.0236  -0.0284 -0.0581 226  LYS   D CB  
9763  N  N   . TYR   D 158 ? 1.2874 1.2932 1.2834 0.0165  -0.0366 -0.0538 227  TYR   D N   
9764  C  CA  . TYR   D 158 ? 1.2671 1.2688 1.2564 0.0121  -0.0390 -0.0514 227  TYR   D CA  
9765  C  C   . TYR   D 158 ? 1.2471 1.2566 1.2434 0.0083  -0.0392 -0.0494 227  TYR   D C   
9766  O  O   . TYR   D 158 ? 1.2479 1.2562 1.2406 0.0039  -0.0390 -0.0474 227  TYR   D O   
9767  C  CB  . TYR   D 158 ? 1.2813 1.2781 1.2666 0.0141  -0.0421 -0.0516 227  TYR   D CB  
9768  C  CG  . TYR   D 158 ? 1.2200 1.2129 1.1998 0.0099  -0.0442 -0.0490 227  TYR   D CG  
9769  C  CD1 . TYR   D 158 ? 1.2653 1.2488 1.2347 0.0074  -0.0447 -0.0481 227  TYR   D CD1 
9770  C  CD2 . TYR   D 158 ? 1.2292 1.2278 1.2149 0.0085  -0.0456 -0.0475 227  TYR   D CD2 
9771  C  CE1 . TYR   D 158 ? 1.3248 1.3051 1.2906 0.0034  -0.0464 -0.0456 227  TYR   D CE1 
9772  C  CE2 . TYR   D 158 ? 1.2132 1.2085 1.1947 0.0047  -0.0470 -0.0450 227  TYR   D CE2 
9773  C  CZ  . TYR   D 158 ? 1.2366 1.2230 1.2087 0.0021  -0.0473 -0.0440 227  TYR   D CZ  
9774  O  OH  . TYR   D 158 ? 1.2552 1.2386 1.2244 -0.0018 -0.0485 -0.0415 227  TYR   D OH  
9775  N  N   . GLN   D 159 ? 1.2415 1.2591 1.2479 0.0102  -0.0399 -0.0499 228  GLN   D N   
9776  C  CA  . GLN   D 159 ? 1.2122 1.2372 1.2254 0.0070  -0.0402 -0.0481 228  GLN   D CA  
9777  C  C   . GLN   D 159 ? 1.2120 1.2408 1.2279 0.0045  -0.0371 -0.0475 228  GLN   D C   
9778  O  O   . GLN   D 159 ? 1.1994 1.2295 1.2144 0.0003  -0.0374 -0.0453 228  GLN   D O   
9779  C  CB  . GLN   D 159 ? 1.1867 1.2191 1.2101 0.0100  -0.0417 -0.0493 228  GLN   D CB  
9780  C  CG  . GLN   D 159 ? 1.1859 1.2268 1.2176 0.0071  -0.0414 -0.0478 228  GLN   D CG  
9781  C  CD  . GLN   D 159 ? 1.1552 1.2032 1.1971 0.0100  -0.0432 -0.0490 228  GLN   D CD  
9782  O  OE1 . GLN   D 159 ? 1.1398 1.1865 1.1802 0.0110  -0.0462 -0.0487 228  GLN   D OE1 
9783  N  NE2 . GLN   D 159 ? 1.1908 1.2459 1.2428 0.0112  -0.0413 -0.0504 228  GLN   D NE2 
9784  N  N   . LYS   D 160 ? 1.2344 1.2646 1.2535 0.0072  -0.0340 -0.0493 229  LYS   D N   
9785  C  CA  . LYS   D 160 ? 1.1417 1.1748 1.1630 0.0053  -0.0305 -0.0486 229  LYS   D CA  
9786  C  C   . LYS   D 160 ? 1.1512 1.1768 1.1611 0.0018  -0.0303 -0.0470 229  LYS   D C   
9787  O  O   . LYS   D 160 ? 1.2086 1.2363 1.2187 -0.0016 -0.0295 -0.0453 229  LYS   D O   
9788  C  CB  . LYS   D 160 ? 1.1232 1.1582 1.1496 0.0092  -0.0266 -0.0508 229  LYS   D CB  
9789  N  N   . ARG   D 161 ? 1.1811 1.1977 1.1808 0.0024  -0.0313 -0.0475 230  ARG   D N   
9790  C  CA  . ARG   D 161 ? 1.1823 1.1912 1.1711 -0.0009 -0.0316 -0.0462 230  ARG   D CA  
9791  C  C   . ARG   D 161 ? 1.2202 1.2284 1.2068 -0.0054 -0.0353 -0.0440 230  ARG   D C   
9792  O  O   . ARG   D 161 ? 1.2303 1.2393 1.2158 -0.0089 -0.0355 -0.0424 230  ARG   D O   
9793  C  CB  . ARG   D 161 ? 1.1334 1.1323 1.1120 0.0014  -0.0314 -0.0477 230  ARG   D CB  
9794  N  N   . LYS   D 162 ? 1.2169 1.2234 1.2030 -0.0051 -0.0381 -0.0438 231  LYS   D N   
9795  C  CA  . LYS   D 162 ? 1.2236 1.2282 1.2070 -0.0093 -0.0411 -0.0417 231  LYS   D CA  
9796  C  C   . LYS   D 162 ? 1.2001 1.2130 1.1912 -0.0122 -0.0415 -0.0398 231  LYS   D C   
9797  O  O   . LYS   D 162 ? 1.1925 1.2044 1.1814 -0.0164 -0.0431 -0.0380 231  LYS   D O   
9798  C  CB  . LYS   D 162 ? 1.1555 1.1571 1.1376 -0.0079 -0.0431 -0.0418 231  LYS   D CB  
9799  C  CG  . LYS   D 162 ? 1.1575 1.1559 1.1364 -0.0121 -0.0456 -0.0395 231  LYS   D CG  
9800  C  CD  . LYS   D 162 ? 1.1974 1.1921 1.1744 -0.0104 -0.0470 -0.0393 231  LYS   D CD  
9801  C  CE  . LYS   D 162 ? 1.2590 1.2483 1.2316 -0.0149 -0.0487 -0.0371 231  LYS   D CE  
9802  N  NZ  . LYS   D 162 ? 1.2516 1.2363 1.2215 -0.0138 -0.0495 -0.0365 231  LYS   D NZ  
9803  N  N   . PHE   D 163 ? 1.1621 1.1832 1.1625 -0.0100 -0.0405 -0.0404 232  PHE   D N   
9804  C  CA  . PHE   D 163 ? 1.1180 1.1472 1.1262 -0.0122 -0.0407 -0.0388 232  PHE   D CA  
9805  C  C   . PHE   D 163 ? 1.2141 1.2480 1.2265 -0.0122 -0.0379 -0.0391 232  PHE   D C   
9806  O  O   . PHE   D 163 ? 1.2320 1.2739 1.2535 -0.0116 -0.0371 -0.0390 232  PHE   D O   
9807  C  CB  . PHE   D 163 ? 1.0787 1.1132 1.0941 -0.0099 -0.0419 -0.0391 232  PHE   D CB  
9808  C  CG  . PHE   D 163 ? 1.0592 1.0883 1.0697 -0.0094 -0.0441 -0.0387 232  PHE   D CG  
9809  C  CD1 . PHE   D 163 ? 1.0572 1.0848 1.0656 -0.0130 -0.0458 -0.0363 232  PHE   D CD1 
9810  C  CD2 . PHE   D 163 ? 1.0500 1.0750 1.0579 -0.0053 -0.0444 -0.0406 232  PHE   D CD2 
9811  C  CE1 . PHE   D 163 ? 1.0084 1.0305 1.0122 -0.0126 -0.0472 -0.0357 232  PHE   D CE1 
9812  C  CE2 . PHE   D 163 ? 1.0274 1.0464 1.0299 -0.0047 -0.0462 -0.0401 232  PHE   D CE2 
9813  C  CZ  . PHE   D 163 ? 1.0032 1.0207 1.0036 -0.0084 -0.0473 -0.0376 232  PHE   D CZ  
9814  N  N   . HIS   D 164 ? 1.2197 1.2483 1.2253 -0.0127 -0.0362 -0.0395 233  HIS   D N   
9815  C  CA  . HIS   D 164 ? 1.1328 1.1643 1.1408 -0.0124 -0.0328 -0.0396 233  HIS   D CA  
9816  C  C   . HIS   D 164 ? 1.1116 1.1473 1.1222 -0.0162 -0.0337 -0.0374 233  HIS   D C   
9817  O  O   . HIS   D 164 ? 1.0820 1.1255 1.1014 -0.0161 -0.0325 -0.0371 233  HIS   D O   
9818  C  CB  . HIS   D 164 ? 1.1170 1.1402 1.1151 -0.0118 -0.0309 -0.0404 233  HIS   D CB  
9819  C  CG  . HIS   D 164 ? 1.2029 1.2277 1.2021 -0.0112 -0.0268 -0.0403 233  HIS   D CG  
9820  N  ND1 . HIS   D 164 ? 1.2496 1.2706 1.2421 -0.0138 -0.0265 -0.0390 233  HIS   D ND1 
9821  C  CD2 . HIS   D 164 ? 1.2157 1.2452 1.2220 -0.0082 -0.0225 -0.0415 233  HIS   D CD2 
9822  C  CE1 . HIS   D 164 ? 1.2188 1.2415 1.2133 -0.0123 -0.0220 -0.0392 233  HIS   D CE1 
9823  N  NE2 . HIS   D 164 ? 1.2134 1.2417 1.2170 -0.0091 -0.0193 -0.0406 233  HIS   D NE2 
9824  N  N   . CYS   D 165 ? 1.2075 1.2382 1.2108 -0.0196 -0.0362 -0.0361 234  CYS   D N   
9825  C  CA  . CYS   D 165 ? 1.2270 1.2613 1.2324 -0.0231 -0.0373 -0.0341 234  CYS   D CA  
9826  C  C   . CYS   D 165 ? 1.1873 1.2292 1.2014 -0.0242 -0.0392 -0.0328 234  CYS   D C   
9827  O  O   . CYS   D 165 ? 1.1686 1.2130 1.1844 -0.0274 -0.0411 -0.0310 234  CYS   D O   
9828  C  CB  . CYS   D 165 ? 1.2847 1.3117 1.2809 -0.0264 -0.0402 -0.0331 234  CYS   D CB  
9829  S  SG  . CYS   D 165 ? 1.4539 1.4729 1.4432 -0.0267 -0.0430 -0.0337 234  CYS   D SG  
9830  N  N   . ALA   D 166 ? 1.0677 1.1124 1.0867 -0.0216 -0.0391 -0.0338 235  ALA   D N   
9831  C  CA  . ALA   D 166 ? 1.0571 1.1094 1.0849 -0.0218 -0.0402 -0.0330 235  ALA   D CA  
9832  C  C   . ALA   D 166 ? 1.0418 1.1010 1.0766 -0.0218 -0.0381 -0.0327 235  ALA   D C   
9833  O  O   . ALA   D 166 ? 1.0206 1.0861 1.0626 -0.0220 -0.0389 -0.0320 235  ALA   D O   
9834  C  CB  . ALA   D 166 ? 1.1230 1.1761 1.1539 -0.0182 -0.0405 -0.0345 235  ALA   D CB  
9835  N  N   . ASN   D 167 ? 1.0448 1.1023 1.0775 -0.0213 -0.0352 -0.0333 236  ASN   D N   
9836  C  CA  . ASN   D 167 ? 1.0200 1.0830 1.0585 -0.0216 -0.0328 -0.0329 236  ASN   D CA  
9837  C  C   . ASN   D 167 ? 0.9812 1.0448 1.0177 -0.0253 -0.0343 -0.0307 236  ASN   D C   
9838  O  O   . ASN   D 167 ? 0.9854 1.0548 1.0281 -0.0260 -0.0336 -0.0298 236  ASN   D O   
9839  C  CB  . ASN   D 167 ? 1.0101 1.0703 1.0463 -0.0196 -0.0286 -0.0341 236  ASN   D CB  
9840  C  CG  . ASN   D 167 ? 1.0433 1.1046 1.0839 -0.0158 -0.0270 -0.0363 236  ASN   D CG  
9841  O  OD1 . ASN   D 167 ? 1.1532 1.2097 1.1893 -0.0138 -0.0246 -0.0376 236  ASN   D OD1 
9842  N  ND2 . ASN   D 167 ? 1.0796 1.1472 1.1293 -0.0146 -0.0284 -0.0369 236  ASN   D ND2 
9843  N  N   . LEU   D 168 ? 1.0046 1.0622 1.0329 -0.0276 -0.0368 -0.0298 237  LEU   D N   
9844  C  CA  . LEU   D 168 ? 1.0336 1.0918 1.0606 -0.0310 -0.0390 -0.0278 237  LEU   D CA  
9845  C  C   . LEU   D 168 ? 1.0091 1.0738 1.0436 -0.0323 -0.0413 -0.0265 237  LEU   D C   
9846  O  O   . LEU   D 168 ? 0.9518 1.0194 0.9881 -0.0347 -0.0426 -0.0249 237  LEU   D O   
9847  C  CB  . LEU   D 168 ? 1.0604 1.1104 1.0777 -0.0330 -0.0416 -0.0276 237  LEU   D CB  
9848  C  CG  . LEU   D 168 ? 0.9861 1.0287 0.9950 -0.0312 -0.0394 -0.0291 237  LEU   D CG  
9849  C  CD1 . LEU   D 168 ? 1.1944 1.2290 1.1947 -0.0329 -0.0427 -0.0292 237  LEU   D CD1 
9850  C  CD2 . LEU   D 168 ? 0.9458 0.9875 0.9519 -0.0314 -0.0373 -0.0286 237  LEU   D CD2 
9851  N  N   . THR   D 169 ? 1.0038 1.0706 1.0422 -0.0304 -0.0416 -0.0273 238  THR   D N   
9852  C  CA  . THR   D 169 ? 0.9760 1.0472 1.0197 -0.0310 -0.0436 -0.0261 238  THR   D CA  
9853  C  C   . THR   D 169 ? 0.9565 1.0347 1.0088 -0.0287 -0.0423 -0.0267 238  THR   D C   
9854  O  O   . THR   D 169 ? 0.9504 1.0300 1.0053 -0.0267 -0.0399 -0.0282 238  THR   D O   
9855  C  CB  . THR   D 169 ? 1.0239 1.0906 1.0642 -0.0303 -0.0451 -0.0265 238  THR   D CB  
9856  O  OG1 . THR   D 169 ? 1.0351 1.1019 1.0771 -0.0264 -0.0438 -0.0285 238  THR   D OG1 
9857  C  CG2 . THR   D 169 ? 1.0446 1.1034 1.0761 -0.0320 -0.0460 -0.0266 238  THR   D CG2 
9858  N  N   . SER   D 170 ? 1.0798 1.1622 1.1369 -0.0290 -0.0440 -0.0257 239  SER   D N   
9859  C  CA  . SER   D 170 ? 1.0875 1.1765 1.1528 -0.0271 -0.0434 -0.0261 239  SER   D CA  
9860  C  C   . SER   D 170 ? 1.0831 1.1722 1.1509 -0.0234 -0.0440 -0.0279 239  SER   D C   
9861  O  O   . SER   D 170 ? 1.0796 1.1735 1.1537 -0.0217 -0.0446 -0.0283 239  SER   D O   
9862  C  CB  . SER   D 170 ? 1.0841 1.1775 1.1529 -0.0291 -0.0449 -0.0240 239  SER   D CB  
9863  O  OG  . SER   D 170 ? 1.1015 1.1927 1.1679 -0.0298 -0.0467 -0.0228 239  SER   D OG  
9864  N  N   . TRP   D 171 ? 0.9856 1.0691 1.0480 -0.0220 -0.0441 -0.0290 240  TRP   D N   
9865  C  CA  . TRP   D 171 ? 0.9358 1.0180 0.9990 -0.0182 -0.0449 -0.0308 240  TRP   D CA  
9866  C  C   . TRP   D 171 ? 0.9574 1.0366 1.0189 -0.0159 -0.0433 -0.0331 240  TRP   D C   
9867  O  O   . TRP   D 171 ? 0.9679 1.0437 1.0246 -0.0176 -0.0417 -0.0330 240  TRP   D O   
9868  C  CB  . TRP   D 171 ? 0.9096 0.9870 0.9671 -0.0184 -0.0467 -0.0297 240  TRP   D CB  
9869  C  CG  . TRP   D 171 ? 0.9245 1.0046 0.9839 -0.0201 -0.0479 -0.0275 240  TRP   D CG  
9870  C  CD1 . TRP   D 171 ? 0.9479 1.0260 1.0040 -0.0236 -0.0484 -0.0251 240  TRP   D CD1 
9871  C  CD2 . TRP   D 171 ? 0.9398 1.0249 1.0051 -0.0183 -0.0488 -0.0274 240  TRP   D CD2 
9872  N  NE1 . TRP   D 171 ? 0.9822 1.0640 1.0418 -0.0239 -0.0491 -0.0235 240  TRP   D NE1 
9873  C  CE2 . TRP   D 171 ? 0.9630 1.0488 1.0277 -0.0207 -0.0494 -0.0248 240  TRP   D CE2 
9874  C  CE3 . TRP   D 171 ? 0.9324 1.0213 1.0036 -0.0149 -0.0493 -0.0294 240  TRP   D CE3 
9875  C  CZ2 . TRP   D 171 ? 0.9646 1.0543 1.0335 -0.0195 -0.0502 -0.0241 240  TRP   D CZ2 
9876  C  CZ3 . TRP   D 171 ? 0.8863 0.9789 0.9617 -0.0139 -0.0506 -0.0288 240  TRP   D CZ3 
9877  C  CH2 . TRP   D 171 ? 0.9177 1.0105 0.9914 -0.0161 -0.0509 -0.0262 240  TRP   D CH2 
9878  N  N   . PRO   D 172 ? 0.9475 1.0275 1.0125 -0.0119 -0.0438 -0.0354 241  PRO   D N   
9879  C  CA  . PRO   D 172 ? 0.9656 1.0432 1.0300 -0.0094 -0.0421 -0.0377 241  PRO   D CA  
9880  C  C   . PRO   D 172 ? 1.0115 1.0815 1.0675 -0.0080 -0.0432 -0.0382 241  PRO   D C   
9881  O  O   . PRO   D 172 ? 1.0015 1.0683 1.0534 -0.0080 -0.0453 -0.0373 241  PRO   D O   
9882  C  CB  . PRO   D 172 ? 0.9524 1.0354 1.0264 -0.0056 -0.0427 -0.0400 241  PRO   D CB  
9883  C  CG  . PRO   D 172 ? 0.9666 1.0531 1.0440 -0.0058 -0.0452 -0.0390 241  PRO   D CG  
9884  C  CD  . PRO   D 172 ? 0.9623 1.0458 1.0327 -0.0093 -0.0459 -0.0361 241  PRO   D CD  
9885  N  N   . ARG   D 173 ? 1.0559 1.1226 1.1093 -0.0065 -0.0413 -0.0398 242  ARG   D N   
9886  C  CA  . ARG   D 173 ? 1.0860 1.1452 1.1317 -0.0047 -0.0418 -0.0408 242  ARG   D CA  
9887  C  C   . ARG   D 173 ? 1.0698 1.1272 1.1148 -0.0019 -0.0447 -0.0414 242  ARG   D C   
9888  O  O   . ARG   D 173 ? 1.0816 1.1330 1.1190 -0.0028 -0.0461 -0.0402 242  ARG   D O   
9889  C  CB  . ARG   D 173 ? 1.1382 1.1966 1.1852 -0.0018 -0.0394 -0.0432 242  ARG   D CB  
9890  C  CG  . ARG   D 173 ? 1.1767 1.2298 1.2161 -0.0037 -0.0370 -0.0427 242  ARG   D CG  
9891  C  CD  . ARG   D 173 ? 1.2099 1.2618 1.2505 -0.0002 -0.0342 -0.0451 242  ARG   D CD  
9892  N  NE  . ARG   D 173 ? 1.3346 1.3925 1.3832 -0.0001 -0.0307 -0.0455 242  ARG   D NE  
9893  C  CZ  . ARG   D 173 ? 1.4366 1.4976 1.4924 0.0035  -0.0284 -0.0477 242  ARG   D CZ  
9894  N  NH1 . ARG   D 173 ? 1.3848 1.4435 1.4405 0.0074  -0.0295 -0.0499 242  ARG   D NH1 
9895  N  NH2 . ARG   D 173 ? 1.4422 1.5087 1.5058 0.0032  -0.0248 -0.0477 242  ARG   D NH2 
9896  N  N   . TRP   D 174 ? 0.9860 1.0480 1.0387 0.0018  -0.0456 -0.0434 243  TRP   D N   
9897  C  CA  . TRP   D 174 ? 0.9953 1.0544 1.0464 0.0056  -0.0485 -0.0445 243  TRP   D CA  
9898  C  C   . TRP   D 174 ? 1.0140 1.0709 1.0606 0.0039  -0.0503 -0.0422 243  TRP   D C   
9899  O  O   . TRP   D 174 ? 1.0752 1.1264 1.1162 0.0064  -0.0521 -0.0424 243  TRP   D O   
9900  C  CB  . TRP   D 174 ? 1.0343 1.0994 1.0954 0.0097  -0.0499 -0.0472 243  TRP   D CB  
9901  C  CG  . TRP   D 174 ? 1.0060 1.0797 1.0772 0.0083  -0.0497 -0.0468 243  TRP   D CG  
9902  C  CD1 . TRP   D 174 ? 1.0162 1.0961 1.0962 0.0076  -0.0472 -0.0477 243  TRP   D CD1 
9903  C  CD2 . TRP   D 174 ? 0.9507 1.0274 1.0244 0.0077  -0.0519 -0.0456 243  TRP   D CD2 
9904  N  NE1 . TRP   D 174 ? 1.0052 1.0915 1.0928 0.0064  -0.0479 -0.0471 243  TRP   D NE1 
9905  C  CE2 . TRP   D 174 ? 0.9982 1.0828 1.0820 0.0066  -0.0509 -0.0459 243  TRP   D CE2 
9906  C  CE3 . TRP   D 174 ? 0.9395 1.0125 1.0075 0.0082  -0.0543 -0.0442 243  TRP   D CE3 
9907  C  CZ2 . TRP   D 174 ? 1.0153 1.1041 1.1035 0.0059  -0.0527 -0.0450 243  TRP   D CZ2 
9908  C  CZ3 . TRP   D 174 ? 0.9561 1.0333 1.0282 0.0077  -0.0557 -0.0433 243  TRP   D CZ3 
9909  C  CH2 . TRP   D 174 ? 0.9842 1.0693 1.0664 0.0066  -0.0551 -0.0437 243  TRP   D CH2 
9910  N  N   . LEU   D 175 ? 0.9819 1.0428 1.0308 0.0000  -0.0497 -0.0399 244  LEU   D N   
9911  C  CA  . LEU   D 175 ? 0.9408 0.9998 0.9861 -0.0016 -0.0510 -0.0374 244  LEU   D CA  
9912  C  C   . LEU   D 175 ? 0.9798 1.0316 1.0160 -0.0045 -0.0503 -0.0356 244  LEU   D C   
9913  O  O   . LEU   D 175 ? 1.0000 1.0467 1.0309 -0.0041 -0.0511 -0.0344 244  LEU   D O   
9914  C  CB  . LEU   D 175 ? 0.8889 0.9548 0.9403 -0.0045 -0.0507 -0.0357 244  LEU   D CB  
9915  C  CG  . LEU   D 175 ? 0.8892 0.9529 0.9366 -0.0069 -0.0512 -0.0327 244  LEU   D CG  
9916  C  CD1 . LEU   D 175 ? 0.9708 1.0328 1.0171 -0.0033 -0.0530 -0.0328 244  LEU   D CD1 
9917  C  CD2 . LEU   D 175 ? 0.9630 1.0323 1.0146 -0.0109 -0.0505 -0.0307 244  LEU   D CD2 
9918  N  N   . TYR   D 176 ? 1.0010 1.0516 1.0351 -0.0073 -0.0488 -0.0354 245  TYR   D N   
9919  C  CA  . TYR   D 176 ? 0.9851 1.0284 1.0109 -0.0100 -0.0486 -0.0340 245  TYR   D CA  
9920  C  C   . TYR   D 176 ? 1.0006 1.0362 1.0198 -0.0067 -0.0491 -0.0355 245  TYR   D C   
9921  O  O   . TYR   D 176 ? 1.0488 1.0775 1.0610 -0.0082 -0.0494 -0.0343 245  TYR   D O   
9922  C  CB  . TYR   D 176 ? 1.0069 1.0498 1.0311 -0.0133 -0.0473 -0.0338 245  TYR   D CB  
9923  C  CG  . TYR   D 176 ? 0.9779 1.0268 1.0069 -0.0170 -0.0471 -0.0319 245  TYR   D CG  
9924  C  CD1 . TYR   D 176 ? 0.9787 1.0269 1.0064 -0.0207 -0.0480 -0.0294 245  TYR   D CD1 
9925  C  CD2 . TYR   D 176 ? 0.9392 0.9944 0.9742 -0.0168 -0.0458 -0.0326 245  TYR   D CD2 
9926  C  CE1 . TYR   D 176 ? 1.0191 1.0728 1.0513 -0.0238 -0.0480 -0.0278 245  TYR   D CE1 
9927  C  CE2 . TYR   D 176 ? 0.9291 0.9891 0.9678 -0.0199 -0.0457 -0.0310 245  TYR   D CE2 
9928  C  CZ  . TYR   D 176 ? 0.9515 1.0109 0.9887 -0.0233 -0.0470 -0.0286 245  TYR   D CZ  
9929  O  OH  . TYR   D 176 ? 0.9090 0.9732 0.9500 -0.0262 -0.0471 -0.0269 245  TYR   D OH  
9930  N  N   . SER   D 177 ? 0.9951 1.0318 1.0168 -0.0021 -0.0493 -0.0383 246  SER   D N   
9931  C  CA  . SER   D 177 ? 0.9867 1.0163 1.0025 0.0018  -0.0502 -0.0399 246  SER   D CA  
9932  C  C   . SER   D 177 ? 1.0148 1.0415 1.0280 0.0036  -0.0519 -0.0389 246  SER   D C   
9933  O  O   . SER   D 177 ? 1.0413 1.0598 1.0464 0.0047  -0.0523 -0.0386 246  SER   D O   
9934  C  CB  . SER   D 177 ? 0.9758 1.0083 0.9965 0.0064  -0.0502 -0.0431 246  SER   D CB  
9935  O  OG  . SER   D 177 ? 0.9332 0.9662 0.9543 0.0054  -0.0480 -0.0440 246  SER   D OG  
9936  N  N   . LEU   D 178 ? 1.0236 1.0564 1.0429 0.0041  -0.0527 -0.0383 247  LEU   D N   
9937  C  CA  . LEU   D 178 ? 0.9861 1.0158 1.0024 0.0063  -0.0541 -0.0374 247  LEU   D CA  
9938  C  C   . LEU   D 178 ? 0.9724 0.9957 0.9814 0.0029  -0.0530 -0.0343 247  LEU   D C   
9939  O  O   . LEU   D 178 ? 1.0331 1.0492 1.0354 0.0051  -0.0534 -0.0338 247  LEU   D O   
9940  C  CB  . LEU   D 178 ? 0.9221 0.9593 0.9460 0.0068  -0.0551 -0.0371 247  LEU   D CB  
9941  C  CG  . LEU   D 178 ? 0.9120 0.9554 0.9442 0.0104  -0.0565 -0.0402 247  LEU   D CG  
9942  C  CD1 . LEU   D 178 ? 0.9065 0.9551 0.9442 0.0115  -0.0581 -0.0399 247  LEU   D CD1 
9943  C  CD2 . LEU   D 178 ? 0.9518 0.9905 0.9811 0.0157  -0.0583 -0.0431 247  LEU   D CD2 
9944  N  N   . TYR   D 179 ? 0.9508 0.9764 0.9613 -0.0025 -0.0516 -0.0324 248  TYR   D N   
9945  C  CA  . TYR   D 179 ? 0.9505 0.9709 0.9560 -0.0063 -0.0506 -0.0295 248  TYR   D CA  
9946  C  C   . TYR   D 179 ? 0.9804 0.9940 0.9797 -0.0082 -0.0501 -0.0298 248  TYR   D C   
9947  O  O   . TYR   D 179 ? 1.0362 1.0469 1.0333 -0.0125 -0.0495 -0.0277 248  TYR   D O   
9948  C  CB  . TYR   D 179 ? 0.9652 0.9921 0.9765 -0.0110 -0.0499 -0.0271 248  TYR   D CB  
9949  C  CG  . TYR   D 179 ? 0.9946 1.0272 1.0110 -0.0097 -0.0502 -0.0262 248  TYR   D CG  
9950  C  CD1 . TYR   D 179 ? 1.0125 1.0532 1.0363 -0.0087 -0.0509 -0.0276 248  TYR   D CD1 
9951  C  CD2 . TYR   D 179 ? 1.0093 1.0389 1.0233 -0.0096 -0.0495 -0.0239 248  TYR   D CD2 
9952  C  CE1 . TYR   D 179 ? 1.0439 1.0894 1.0721 -0.0075 -0.0513 -0.0269 248  TYR   D CE1 
9953  C  CE2 . TYR   D 179 ? 1.0283 1.0626 1.0463 -0.0081 -0.0497 -0.0231 248  TYR   D CE2 
9954  C  CZ  . TYR   D 179 ? 1.0745 1.1167 1.0996 -0.0071 -0.0509 -0.0247 248  TYR   D CZ  
9955  O  OH  . TYR   D 179 ? 1.1341 1.1808 1.1631 -0.0055 -0.0514 -0.0241 248  TYR   D OH  
9956  N  N   . ASP   D 180 ? 0.9867 0.9975 0.9833 -0.0052 -0.0505 -0.0325 249  ASP   D N   
9957  C  CA  . ASP   D 180 ? 1.0449 1.0489 1.0351 -0.0068 -0.0502 -0.0330 249  ASP   D CA  
9958  C  C   . ASP   D 180 ? 1.0871 1.0811 1.0687 -0.0044 -0.0504 -0.0331 249  ASP   D C   
9959  O  O   . ASP   D 180 ? 1.1335 1.1254 1.1133 0.0008  -0.0512 -0.0349 249  ASP   D O   
9960  C  CB  . ASP   D 180 ? 1.0725 1.0790 1.0646 -0.0049 -0.0500 -0.0357 249  ASP   D CB  
9961  C  CG  . ASP   D 180 ? 1.1349 1.1337 1.1195 -0.0059 -0.0496 -0.0364 249  ASP   D CG  
9962  O  OD1 . ASP   D 180 ? 1.1355 1.1304 1.1164 -0.0103 -0.0497 -0.0346 249  ASP   D OD1 
9963  O  OD2 . ASP   D 180 ? 1.1417 1.1383 1.1242 -0.0021 -0.0495 -0.0389 249  ASP   D OD2 
9964  N  N   . ALA   D 181 ? 1.0551 1.0425 1.0314 -0.0081 -0.0499 -0.0312 250  ALA   D N   
9965  C  CA  . ALA   D 181 ? 1.0605 1.0376 1.0283 -0.0063 -0.0497 -0.0309 250  ALA   D CA  
9966  C  C   . ALA   D 181 ? 1.1856 1.1580 1.1484 -0.0013 -0.0505 -0.0339 250  ALA   D C   
9967  O  O   . ALA   D 181 ? 1.2091 1.1778 1.1685 0.0035  -0.0510 -0.0348 250  ALA   D O   
9968  C  CB  . ALA   D 181 ? 1.1386 1.1095 1.1024 -0.0115 -0.0491 -0.0289 250  ALA   D CB  
9969  N  N   . GLU   D 182 ? 1.3567 1.3288 1.3187 -0.0021 -0.0505 -0.0356 251  GLU   D N   
9970  C  CA  . GLU   D 182 ? 1.3996 1.3664 1.3564 0.0025  -0.0510 -0.0384 251  GLU   D CA  
9971  C  C   . GLU   D 182 ? 1.3684 1.3406 1.3302 0.0082  -0.0518 -0.0407 251  GLU   D C   
9972  O  O   . GLU   D 182 ? 1.3696 1.3365 1.3269 0.0132  -0.0527 -0.0425 251  GLU   D O   
9973  C  CB  . GLU   D 182 ? 1.4229 1.3887 1.3781 0.0007  -0.0505 -0.0397 251  GLU   D CB  
9974  C  CG  . GLU   D 182 ? 1.4552 1.4192 1.4089 -0.0057 -0.0504 -0.0376 251  GLU   D CG  
9975  C  CD  . GLU   D 182 ? 1.5760 1.5303 1.5226 -0.0081 -0.0507 -0.0358 251  GLU   D CD  
9976  O  OE1 . GLU   D 182 ? 1.6396 1.5852 1.5785 -0.0052 -0.0509 -0.0369 251  GLU   D OE1 
9977  O  OE2 . GLU   D 182 ? 1.5616 1.5170 1.5107 -0.0128 -0.0506 -0.0332 251  GLU   D OE2 
9978  N  N   . THR   D 183 ? 1.2014 1.1840 1.1726 0.0077  -0.0517 -0.0409 252  THR   D N   
9979  C  CA  . THR   D 183 ? 1.1397 1.1279 1.1170 0.0128  -0.0528 -0.0431 252  THR   D CA  
9980  C  C   . THR   D 183 ? 1.1381 1.1226 1.1123 0.0161  -0.0543 -0.0426 252  THR   D C   
9981  O  O   . THR   D 183 ? 1.1435 1.1254 1.1162 0.0216  -0.0560 -0.0449 252  THR   D O   
9982  C  CB  . THR   D 183 ? 1.1283 1.1277 1.1162 0.0110  -0.0523 -0.0430 252  THR   D CB  
9983  O  OG1 . THR   D 183 ? 1.1399 1.1422 1.1302 0.0090  -0.0507 -0.0438 252  THR   D OG1 
9984  C  CG2 . THR   D 183 ? 1.1233 1.1284 1.1183 0.0160  -0.0540 -0.0452 252  THR   D CG2 
9985  N  N   . LEU   D 184 ? 1.1296 1.1135 1.1028 0.0129  -0.0538 -0.0397 253  LEU   D N   
9986  C  CA  . LEU   D 184 ? 1.0982 1.0779 1.0675 0.0160  -0.0547 -0.0388 253  LEU   D CA  
9987  C  C   . LEU   D 184 ? 1.1021 1.0703 1.0608 0.0195  -0.0552 -0.0395 253  LEU   D C   
9988  O  O   . LEU   D 184 ? 1.1181 1.0834 1.0744 0.0254  -0.0571 -0.0414 253  LEU   D O   
9989  C  CB  . LEU   D 184 ? 1.0270 1.0072 0.9964 0.0115  -0.0531 -0.0351 253  LEU   D CB  
9990  C  CG  . LEU   D 184 ? 0.9690 0.9601 0.9483 0.0089  -0.0530 -0.0342 253  LEU   D CG  
9991  C  CD1 . LEU   D 184 ? 0.9594 0.9504 0.9386 0.0040  -0.0511 -0.0305 253  LEU   D CD1 
9992  C  CD2 . LEU   D 184 ? 0.9989 0.9945 0.9825 0.0139  -0.0550 -0.0359 253  LEU   D CD2 
9993  N  N   . MET   D 185 ? 1.0970 1.0582 1.0493 0.0162  -0.0537 -0.0382 254  MET   D N   
9994  C  CA  . MET   D 185 ? 1.0603 1.0097 1.0020 0.0192  -0.0539 -0.0386 254  MET   D CA  
9995  C  C   . MET   D 185 ? 1.1400 1.0882 1.0806 0.0254  -0.0559 -0.0424 254  MET   D C   
9996  O  O   . MET   D 185 ? 1.1687 1.1096 1.1026 0.0305  -0.0573 -0.0434 254  MET   D O   
9997  C  CB  . MET   D 185 ? 1.0510 0.9941 0.9875 0.0142  -0.0522 -0.0370 254  MET   D CB  
9998  C  CG  . MET   D 185 ? 1.0844 1.0278 1.0221 0.0086  -0.0504 -0.0334 254  MET   D CG  
9999  S  SD  . MET   D 185 ? 1.1939 1.1318 1.1282 0.0023  -0.0494 -0.0322 254  MET   D SD  
10000 C  CE  . MET   D 185 ? 1.2547 1.1791 1.1768 0.0068  -0.0499 -0.0338 254  MET   D CE  
10001 N  N   . ASP   D 186 ? 1.1600 1.1153 1.1074 0.0252  -0.0561 -0.0446 255  ASP   D N   
10002 C  CA  . ASP   D 186 ? 1.1520 1.1075 1.1005 0.0312  -0.0578 -0.0483 255  ASP   D CA  
10003 C  C   . ASP   D 186 ? 1.1232 1.0820 1.0757 0.0366  -0.0604 -0.0499 255  ASP   D C   
10004 O  O   . ASP   D 186 ? 1.1464 1.1002 1.0951 0.0425  -0.0626 -0.0523 255  ASP   D O   
10005 C  CB  . ASP   D 186 ? 1.2028 1.1660 1.1590 0.0296  -0.0567 -0.0499 255  ASP   D CB  
10006 C  CG  . ASP   D 186 ? 1.2585 1.2250 1.2196 0.0355  -0.0580 -0.0537 255  ASP   D CG  
10007 O  OD1 . ASP   D 186 ? 1.2227 1.1829 1.1782 0.0381  -0.0579 -0.0554 255  ASP   D OD1 
10008 O  OD2 . ASP   D 186 ? 1.1906 1.1661 1.1617 0.0375  -0.0592 -0.0550 255  ASP   D OD2 
10009 N  N   . ARG   D 187 ? 1.1299 1.0963 1.0893 0.0350  -0.0606 -0.0487 256  ARG   D N   
10010 C  CA  . ARG   D 187 ? 1.1573 1.1268 1.1206 0.0399  -0.0636 -0.0503 256  ARG   D CA  
10011 C  C   . ARG   D 187 ? 1.1318 1.0907 1.0843 0.0437  -0.0649 -0.0494 256  ARG   D C   
10012 O  O   . ARG   D 187 ? 1.1764 1.1326 1.1274 0.0501  -0.0682 -0.0520 256  ARG   D O   
10013 C  CB  . ARG   D 187 ? 1.1676 1.1468 1.1399 0.0368  -0.0632 -0.0488 256  ARG   D CB  
10014 C  CG  . ARG   D 187 ? 1.1874 1.1781 1.1720 0.0351  -0.0628 -0.0504 256  ARG   D CG  
10015 C  CD  . ARG   D 187 ? 1.1210 1.1190 1.1116 0.0302  -0.0614 -0.0479 256  ARG   D CD  
10016 N  NE  . ARG   D 187 ? 1.1828 1.1829 1.1756 0.0326  -0.0635 -0.0477 256  ARG   D NE  
10017 C  CZ  . ARG   D 187 ? 1.2072 1.2140 1.2058 0.0294  -0.0629 -0.0459 256  ARG   D CZ  
10018 N  NH1 . ARG   D 187 ? 1.2034 1.2154 1.2060 0.0237  -0.0603 -0.0441 256  ARG   D NH1 
10019 N  NH2 . ARG   D 187 ? 1.2042 1.2121 1.2040 0.0323  -0.0651 -0.0460 256  ARG   D NH2 
10020 N  N   . ILE   D 188 ? 1.0853 1.0381 1.0305 0.0399  -0.0625 -0.0459 257  ILE   D N   
10021 C  CA  . ILE   D 188 ? 1.0577 0.9988 0.9912 0.0431  -0.0628 -0.0446 257  ILE   D CA  
10022 C  C   . ILE   D 188 ? 1.0875 1.0192 1.0126 0.0478  -0.0642 -0.0468 257  ILE   D C   
10023 O  O   . ILE   D 188 ? 1.1300 1.0547 1.0485 0.0539  -0.0666 -0.0481 257  ILE   D O   
10024 C  CB  . ILE   D 188 ? 1.0185 0.9552 0.9472 0.0373  -0.0591 -0.0402 257  ILE   D CB  
10025 C  CG1 . ILE   D 188 ? 1.0081 0.9542 0.9452 0.0337  -0.0581 -0.0383 257  ILE   D CG1 
10026 C  CG2 . ILE   D 188 ? 1.0718 0.9950 0.9874 0.0402  -0.0584 -0.0386 257  ILE   D CG2 
10027 C  CD1 . ILE   D 188 ? 1.0096 0.9525 0.9437 0.0285  -0.0547 -0.0341 257  ILE   D CD1 
10028 N  N   . LYS   D 189 ? 1.0771 1.0080 1.0020 0.0453  -0.0629 -0.0474 258  LYS   D N   
10029 C  CA  . LYS   D 189 ? 1.0512 0.9732 0.9682 0.0498  -0.0641 -0.0496 258  LYS   D CA  
10030 C  C   . LYS   D 189 ? 1.0737 0.9993 0.9953 0.0569  -0.0680 -0.0537 258  LYS   D C   
10031 O  O   . LYS   D 189 ? 1.1212 1.0383 1.0350 0.0629  -0.0704 -0.0551 258  LYS   D O   
10032 C  CB  . LYS   D 189 ? 1.1312 1.0530 1.0483 0.0460  -0.0621 -0.0498 258  LYS   D CB  
10033 C  CG  . LYS   D 189 ? 1.1783 1.0939 1.0891 0.0396  -0.0590 -0.0462 258  LYS   D CG  
10034 C  CD  . LYS   D 189 ? 1.1771 1.0966 1.0917 0.0346  -0.0574 -0.0463 258  LYS   D CD  
10035 C  CE  . LYS   D 189 ? 1.2577 1.1773 1.1728 0.0387  -0.0585 -0.0499 258  LYS   D CE  
10036 N  NZ  . LYS   D 189 ? 1.4124 1.3310 1.3264 0.0343  -0.0568 -0.0497 258  LYS   D NZ  
10037 N  N   . LYS   D 190 ? 1.1186 1.0566 1.0532 0.0563  -0.0687 -0.0556 259  LYS   D N   
10038 C  CA  . LYS   D 190 ? 1.1131 1.0556 1.0545 0.0627  -0.0725 -0.0596 259  LYS   D CA  
10039 C  C   . LYS   D 190 ? 1.1662 1.1038 1.1029 0.0684  -0.0762 -0.0604 259  LYS   D C   
10040 O  O   . LYS   D 190 ? 1.2029 1.1359 1.1368 0.0751  -0.0798 -0.0634 259  LYS   D O   
10041 C  CB  . LYS   D 190 ? 1.0287 0.9857 0.9856 0.0603  -0.0721 -0.0608 259  LYS   D CB  
10042 N  N   . GLN   D 191 ? 1.1799 1.1176 1.1150 0.0661  -0.0755 -0.0576 260  GLN   D N   
10043 C  CA  . GLN   D 191 ? 1.1912 1.1232 1.1204 0.0715  -0.0787 -0.0579 260  GLN   D CA  
10044 C  C   . GLN   D 191 ? 1.2171 1.1337 1.1302 0.0751  -0.0788 -0.0571 260  GLN   D C   
10045 O  O   . GLN   D 191 ? 1.2244 1.1344 1.1316 0.0822  -0.0828 -0.0593 260  GLN   D O   
10046 C  CB  . GLN   D 191 ? 1.1626 1.0980 1.0933 0.0677  -0.0771 -0.0547 260  GLN   D CB  
10047 C  CG  . GLN   D 191 ? 1.1997 1.1492 1.1452 0.0651  -0.0776 -0.0556 260  GLN   D CG  
10048 C  CD  . GLN   D 191 ? 1.2862 1.2370 1.2327 0.0681  -0.0804 -0.0557 260  GLN   D CD  
10049 O  OE1 . GLN   D 191 ? 1.2522 1.1932 1.1885 0.0734  -0.0827 -0.0559 260  GLN   D OE1 
10050 N  NE2 . GLN   D 191 ? 1.3827 1.3449 1.3409 0.0649  -0.0802 -0.0555 260  GLN   D NE2 
10051 N  N   . LEU   D 192 ? 1.2179 1.1280 1.1234 0.0703  -0.0745 -0.0538 261  LEU   D N   
10052 C  CA  . LEU   D 192 ? 1.1989 1.0940 1.0893 0.0731  -0.0739 -0.0530 261  LEU   D CA  
10053 C  C   . LEU   D 192 ? 1.2619 1.1533 1.1503 0.0791  -0.0772 -0.0569 261  LEU   D C   
10054 O  O   . LEU   D 192 ? 1.3378 1.2178 1.2149 0.0851  -0.0794 -0.0578 261  LEU   D O   
10055 C  CB  . LEU   D 192 ? 1.1094 1.0003 0.9953 0.0660  -0.0688 -0.0492 261  LEU   D CB  
10056 C  CG  . LEU   D 192 ? 1.0883 0.9814 0.9754 0.0601  -0.0653 -0.0450 261  LEU   D CG  
10057 C  CD1 . LEU   D 192 ? 1.0667 0.9572 0.9519 0.0527  -0.0608 -0.0418 261  LEU   D CD1 
10058 C  CD2 . LEU   D 192 ? 1.1183 1.0021 0.9954 0.0642  -0.0655 -0.0433 261  LEU   D CD2 
10059 N  N   . ARG   D 193 ? 1.2520 1.1529 1.1511 0.0779  -0.0776 -0.0594 262  ARG   D N   
10060 C  CA  . ARG   D 193 ? 1.2976 1.1960 1.1962 0.0834  -0.0803 -0.0632 262  ARG   D CA  
10061 C  C   . ARG   D 193 ? 1.3559 1.2528 1.2545 0.0918  -0.0860 -0.0666 262  ARG   D C   
10062 O  O   . ARG   D 193 ? 1.4200 1.3096 1.3127 0.0978  -0.0887 -0.0692 262  ARG   D O   
10063 C  CB  . ARG   D 193 ? 1.1953 1.1055 1.1071 0.0807  -0.0792 -0.0652 262  ARG   D CB  
10064 N  N   . GLU   D 194 ? 1.3505 1.2537 1.2555 0.0927  -0.0882 -0.0668 263  GLU   D N   
10065 C  CA  . GLU   D 194 ? 1.3859 1.2867 1.2902 0.1009  -0.0943 -0.0703 263  GLU   D CA  
10066 C  C   . GLU   D 194 ? 1.3781 1.2627 1.2644 0.1056  -0.0956 -0.0690 263  GLU   D C   
10067 O  O   . GLU   D 194 ? 1.4143 1.2937 1.2969 0.1135  -0.1010 -0.0721 263  GLU   D O   
10068 C  CB  . GLU   D 194 ? 1.3763 1.2880 1.2924 0.1007  -0.0967 -0.0711 263  GLU   D CB  
10069 C  CG  . GLU   D 194 ? 1.3722 1.2994 1.3059 0.0964  -0.0954 -0.0723 263  GLU   D CG  
10070 C  CD  . GLU   D 194 ? 1.4408 1.3765 1.3817 0.0915  -0.0939 -0.0701 263  GLU   D CD  
10071 O  OE1 . GLU   D 194 ? 1.4564 1.3861 1.3890 0.0922  -0.0943 -0.0680 263  GLU   D OE1 
10072 O  OE2 . GLU   D 194 ? 1.4952 1.4431 1.4495 0.0870  -0.0920 -0.0703 263  GLU   D OE2 
10073 N  N   . TRP   D 195 ? 1.3287 1.2050 1.2041 0.1013  -0.0908 -0.0645 264  TRP   D N   
10074 C  CA  . TRP   D 195 ? 1.3192 1.1790 1.1767 0.1056  -0.0909 -0.0629 264  TRP   D CA  
10075 C  C   . TRP   D 195 ? 1.4682 1.3175 1.3159 0.1072  -0.0900 -0.0633 264  TRP   D C   
10076 O  O   . TRP   D 195 ? 1.5129 1.3570 1.3567 0.1144  -0.0945 -0.0668 264  TRP   D O   
10077 C  CB  . TRP   D 195 ? 1.2628 1.1187 1.1140 0.1003  -0.0859 -0.0577 264  TRP   D CB  
10078 C  CG  . TRP   D 195 ? 1.2540 1.1195 1.1139 0.0988  -0.0867 -0.0572 264  TRP   D CG  
10079 C  CD1 . TRP   D 195 ? 1.2894 1.1631 1.1587 0.1030  -0.0920 -0.0608 264  TRP   D CD1 
10080 C  CD2 . TRP   D 195 ? 1.1889 1.0568 1.0496 0.0928  -0.0821 -0.0529 264  TRP   D CD2 
10081 N  NE1 . TRP   D 195 ? 1.1562 1.0368 1.0313 0.1001  -0.0911 -0.0590 264  TRP   D NE1 
10082 C  CE2 . TRP   D 195 ? 1.1259 1.0032 0.9958 0.0939  -0.0849 -0.0541 264  TRP   D CE2 
10083 C  CE3 . TRP   D 195 ? 1.1734 1.0364 1.0284 0.0866  -0.0759 -0.0482 264  TRP   D CE3 
10084 C  CZ2 . TRP   D 195 ? 1.1083 0.9901 0.9810 0.0892  -0.0817 -0.0508 264  TRP   D CZ2 
10085 C  CZ3 . TRP   D 195 ? 1.1478 1.0159 1.0067 0.0819  -0.0727 -0.0449 264  TRP   D CZ3 
10086 C  CH2 . TRP   D 195 ? 1.0861 0.9633 0.9534 0.0834  -0.0756 -0.0462 264  TRP   D CH2 
10087 N  N   . ASP   D 196 ? 1.4918 1.3381 1.3358 0.1006  -0.0845 -0.0599 265  ASP   D N   
10088 C  CA  . ASP   D 196 ? 1.5192 1.3554 1.3538 0.1012  -0.0831 -0.0600 265  ASP   D CA  
10089 C  C   . ASP   D 196 ? 1.6076 1.4537 1.4536 0.0990  -0.0832 -0.0626 265  ASP   D C   
10090 O  O   . ASP   D 196 ? 1.7454 1.5967 1.5963 0.0918  -0.0791 -0.0606 265  ASP   D O   
10091 C  CB  . ASP   D 196 ? 1.5583 1.3858 1.3835 0.0951  -0.0773 -0.0551 265  ASP   D CB  
10092 C  CG  . ASP   D 196 ? 1.6880 1.5029 1.5017 0.0960  -0.0760 -0.0549 265  ASP   D CG  
10093 O  OD1 . ASP   D 196 ? 1.7580 1.5691 1.5686 0.1026  -0.0798 -0.0585 265  ASP   D OD1 
10094 O  OD2 . ASP   D 196 ? 1.7137 1.5227 1.5219 0.0901  -0.0712 -0.0513 265  ASP   D OD2 
10095 N  N   . GLU   D 197 ? 1.6142 1.4626 1.4642 0.1055  -0.0877 -0.0670 266  GLU   D N   
10096 C  CA  . GLU   D 197 ? 1.6910 1.5481 1.5513 0.1040  -0.0872 -0.0694 266  GLU   D CA  
10097 C  C   . GLU   D 197 ? 1.7945 1.6420 1.6449 0.1013  -0.0838 -0.0679 266  GLU   D C   
10098 O  O   . GLU   D 197 ? 1.7612 1.5997 1.6037 0.1066  -0.0856 -0.0700 266  GLU   D O   
10099 C  CB  . GLU   D 197 ? 1.6644 1.5258 1.5318 0.1117  -0.0926 -0.0745 266  GLU   D CB  
10100 C  CG  . GLU   D 197 ? 1.7049 1.5757 1.5827 0.1142  -0.0965 -0.0762 266  GLU   D CG  
10101 C  CD  . GLU   D 197 ? 1.8620 1.7325 1.7427 0.1234  -0.1032 -0.0812 266  GLU   D CD  
10102 O  OE1 . GLU   D 197 ? 1.9015 1.7734 1.7862 0.1263  -0.1042 -0.0841 266  GLU   D OE1 
10103 O  OE2 . GLU   D 197 ? 1.8700 1.7386 1.7490 0.1279  -0.1076 -0.0821 266  GLU   D OE2 
10104 N  N   . ASN   D 198 ? 2.0062 1.8552 1.8570 0.0931  -0.0790 -0.0644 267  ASN   D N   
10105 C  CA  . ASN   D 198 ? 2.0872 1.9259 1.9277 0.0899  -0.0757 -0.0625 267  ASN   D CA  
10106 C  C   . ASN   D 198 ? 2.0997 1.9475 1.9493 0.0829  -0.0726 -0.0619 267  ASN   D C   
10107 O  O   . ASN   D 198 ? 2.1518 2.0087 2.0111 0.0842  -0.0736 -0.0648 267  ASN   D O   
10108 C  CB  . ASN   D 198 ? 2.1209 1.9475 1.9487 0.0877  -0.0733 -0.0584 267  ASN   D CB  
10109 C  CG  . ASN   D 198 ? 2.1512 1.9608 1.9627 0.0940  -0.0747 -0.0589 267  ASN   D CG  
10110 O  OD1 . ASN   D 198 ? 2.1088 1.9165 1.9190 0.1014  -0.0787 -0.0626 267  ASN   D OD1 
10111 N  ND2 . ASN   D 198 ? 2.1641 1.9614 1.9637 0.0909  -0.0712 -0.0552 267  ASN   D ND2 
10112 N  N   . LEU   D 199 ? 1.9105 1.7559 1.7572 0.0755  -0.0688 -0.0582 268  LEU   D N   
10113 C  CA  . LEU   D 199 ? 1.8594 1.7084 1.7098 0.0698  -0.0662 -0.0578 268  LEU   D CA  
10114 C  C   . LEU   D 199 ? 1.8817 1.7401 1.7406 0.0620  -0.0637 -0.0550 268  LEU   D C   
10115 O  O   . LEU   D 199 ? 1.9371 1.7943 1.7946 0.0596  -0.0627 -0.0522 268  LEU   D O   
10116 C  CB  . LEU   D 199 ? 1.8935 1.7283 1.7308 0.0683  -0.0646 -0.0565 268  LEU   D CB  
10117 C  CG  . LEU   D 199 ? 1.9489 1.7705 1.7740 0.0753  -0.0665 -0.0583 268  LEU   D CG  
10118 C  CD1 . LEU   D 199 ? 1.9412 1.7499 1.7540 0.0764  -0.0659 -0.0556 268  LEU   D CD1 
10119 C  CD2 . LEU   D 199 ? 1.8298 1.6447 1.6491 0.0745  -0.0656 -0.0594 268  LEU   D CD2 
10120 N  N   . LYS   D 200 ? 1.9004 1.7672 1.7674 0.0583  -0.0626 -0.0558 269  LYS   D N   
10121 C  CA  . LYS   D 200 ? 1.8055 1.6811 1.6804 0.0509  -0.0604 -0.0535 269  LYS   D CA  
10122 C  C   . LYS   D 200 ? 1.8379 1.7078 1.7078 0.0448  -0.0581 -0.0516 269  LYS   D C   
10123 O  O   . LYS   D 200 ? 1.7757 1.6527 1.6521 0.0389  -0.0567 -0.0503 269  LYS   D O   
10124 C  CB  . LYS   D 200 ? 1.6191 1.5090 1.5074 0.0511  -0.0608 -0.0556 269  LYS   D CB  
10125 N  N   . ASP   D 201 ? 1.9327 1.7898 1.7912 0.0462  -0.0580 -0.0517 270  ASP   D N   
10126 C  CA  . ASP   D 201 ? 2.0006 1.8505 1.8533 0.0405  -0.0564 -0.0500 270  ASP   D CA  
10127 C  C   . ASP   D 201 ? 2.0050 1.8483 1.8531 0.0361  -0.0548 -0.0462 270  ASP   D C   
10128 O  O   . ASP   D 201 ? 1.9689 1.8190 1.8233 0.0339  -0.0541 -0.0442 270  ASP   D O   
10129 C  CB  . ASP   D 201 ? 2.0230 1.8620 1.8657 0.0442  -0.0570 -0.0522 270  ASP   D CB  
10130 C  CG  . ASP   D 201 ? 2.1100 1.9392 1.9437 0.0508  -0.0583 -0.0529 270  ASP   D CG  
10131 O  OD1 . ASP   D 201 ? 2.1205 1.9427 1.9485 0.0495  -0.0575 -0.0502 270  ASP   D OD1 
10132 O  OD2 . ASP   D 201 ? 2.1759 2.0043 2.0083 0.0573  -0.0601 -0.0561 270  ASP   D OD2 
10133 N  N   . ASP   D 202 ? 2.2105 2.0405 2.0479 0.0350  -0.0540 -0.0451 271  ASP   D N   
10134 C  CA  . ASP   D 202 ? 2.2184 2.0407 2.0512 0.0306  -0.0520 -0.0414 271  ASP   D CA  
10135 C  C   . ASP   D 202 ? 2.1931 2.0187 2.0284 0.0323  -0.0512 -0.0395 271  ASP   D C   
10136 O  O   . ASP   D 202 ? 2.1897 2.0171 2.0285 0.0270  -0.0491 -0.0363 271  ASP   D O   
10137 C  CB  . ASP   D 202 ? 2.2666 2.0725 2.0858 0.0326  -0.0516 -0.0412 271  ASP   D CB  
10138 N  N   . SER   D 203 ? 1.9068 1.7332 1.7406 0.0396  -0.0531 -0.0417 272  SER   D N   
10139 C  CA  . SER   D 203 ? 1.7954 1.6248 1.6309 0.0429  -0.0533 -0.0408 272  SER   D CA  
10140 C  C   . SER   D 203 ? 1.7403 1.5770 1.5834 0.0370  -0.0511 -0.0375 272  SER   D C   
10141 O  O   . SER   D 203 ? 1.7313 1.5611 1.5694 0.0355  -0.0487 -0.0343 272  SER   D O   
10142 C  CB  . SER   D 203 ? 1.7736 1.6120 1.6154 0.0490  -0.0566 -0.0445 272  SER   D CB  
10143 O  OG  . SER   D 203 ? 1.8007 1.6506 1.6529 0.0462  -0.0570 -0.0462 272  SER   D OG  
10144 N  N   . LEU   D 204 ? 1.6878 1.5383 1.5431 0.0336  -0.0516 -0.0381 273  LEU   D N   
10145 C  CA  . LEU   D 204 ? 1.5038 1.3624 1.3673 0.0284  -0.0498 -0.0352 273  LEU   D CA  
10146 C  C   . LEU   D 204 ? 1.5324 1.3945 1.4011 0.0205  -0.0485 -0.0339 273  LEU   D C   
10147 O  O   . LEU   D 204 ? 1.6332 1.4955 1.5018 0.0199  -0.0497 -0.0360 273  LEU   D O   
10148 C  CB  . LEU   D 204 ? 1.4153 1.2870 1.2887 0.0308  -0.0516 -0.0369 273  LEU   D CB  
10149 C  CG  . LEU   D 204 ? 1.3732 1.2427 1.2429 0.0387  -0.0537 -0.0386 273  LEU   D CG  
10150 C  CD1 . LEU   D 204 ? 1.2236 1.1056 1.1037 0.0415  -0.0564 -0.0417 273  LEU   D CD1 
10151 C  CD2 . LEU   D 204 ? 1.3941 1.2602 1.2607 0.0389  -0.0520 -0.0356 273  LEU   D CD2 
10152 N  N   . PRO   D 205 ? 1.4684 1.3332 1.3417 0.0148  -0.0463 -0.0306 274  PRO   D N   
10153 C  CA  . PRO   D 205 ? 1.4099 1.2776 1.2882 0.0074  -0.0457 -0.0295 274  PRO   D CA  
10154 C  C   . PRO   D 205 ? 1.3223 1.2035 1.2112 0.0056  -0.0472 -0.0310 274  PRO   D C   
10155 O  O   . PRO   D 205 ? 1.2917 1.1810 1.1853 0.0095  -0.0484 -0.0326 274  PRO   D O   
10156 C  CB  . PRO   D 205 ? 1.3387 1.2047 1.2189 0.0026  -0.0428 -0.0254 274  PRO   D CB  
10157 C  CG  . PRO   D 205 ? 1.3185 1.1871 1.1990 0.0071  -0.0421 -0.0246 274  PRO   D CG  
10158 C  CD  . PRO   D 205 ? 1.4093 1.2729 1.2821 0.0150  -0.0442 -0.0276 274  PRO   D CD  
10159 N  N   . SER   D 206 ? 1.4002 1.2835 1.2927 -0.0005 -0.0473 -0.0304 275  SER   D N   
10160 C  CA  . SER   D 206 ? 1.3896 1.2837 1.2902 -0.0023 -0.0486 -0.0319 275  SER   D CA  
10161 C  C   . SER   D 206 ? 1.3671 1.2699 1.2771 -0.0077 -0.0478 -0.0293 275  SER   D C   
10162 O  O   . SER   D 206 ? 1.3941 1.3071 1.3114 -0.0065 -0.0481 -0.0297 275  SER   D O   
10163 C  CB  . SER   D 206 ? 1.4423 1.3316 1.3390 -0.0045 -0.0498 -0.0335 275  SER   D CB  
10164 O  OG  . SER   D 206 ? 1.4466 1.3295 1.3414 -0.0104 -0.0494 -0.0313 275  SER   D OG  
10165 N  N   . ASN   D 207 ? 1.2906 1.1895 1.2009 -0.0136 -0.0470 -0.0269 276  ASN   D N   
10166 C  CA  . ASN   D 207 ? 1.2688 1.1756 1.1883 -0.0187 -0.0463 -0.0244 276  ASN   D CA  
10167 C  C   . ASN   D 207 ? 1.2521 1.1645 1.1753 -0.0158 -0.0447 -0.0230 276  ASN   D C   
10168 O  O   . ASN   D 207 ? 1.2723 1.1778 1.1903 -0.0135 -0.0429 -0.0216 276  ASN   D O   
10169 C  CB  . ASN   D 207 ? 1.2661 1.1661 1.1851 -0.0245 -0.0453 -0.0218 276  ASN   D CB  
10170 C  CG  . ASN   D 207 ? 1.3297 1.2375 1.2587 -0.0296 -0.0442 -0.0190 276  ASN   D CG  
10171 O  OD1 . ASN   D 207 ? 1.2990 1.2058 1.2293 -0.0297 -0.0415 -0.0163 276  ASN   D OD1 
10172 N  ND2 . ASN   D 207 ? 1.3931 1.3082 1.3289 -0.0335 -0.0463 -0.0195 276  ASN   D ND2 
10173 N  N   . PRO   D 208 ? 1.2829 1.2069 1.2143 -0.0156 -0.0454 -0.0235 277  PRO   D N   
10174 C  CA  . PRO   D 208 ? 1.2779 1.2064 1.2117 -0.0117 -0.0445 -0.0229 277  PRO   D CA  
10175 C  C   . PRO   D 208 ? 1.2785 1.2045 1.2128 -0.0136 -0.0418 -0.0193 277  PRO   D C   
10176 O  O   . PRO   D 208 ? 1.2716 1.1974 1.2041 -0.0094 -0.0408 -0.0188 277  PRO   D O   
10177 C  CB  . PRO   D 208 ? 1.2317 1.1731 1.1751 -0.0127 -0.0457 -0.0238 277  PRO   D CB  
10178 C  CG  . PRO   D 208 ? 1.2594 1.2014 1.2027 -0.0144 -0.0474 -0.0259 277  PRO   D CG  
10179 C  CD  . PRO   D 208 ? 1.3309 1.2636 1.2690 -0.0184 -0.0471 -0.0247 277  PRO   D CD  
10180 N  N   . ILE   D 209 ? 1.2342 1.1579 1.1707 -0.0196 -0.0405 -0.0169 278  ILE   D N   
10181 C  CA  . ILE   D 209 ? 1.2061 1.1262 1.1428 -0.0212 -0.0371 -0.0133 278  ILE   D CA  
10182 C  C   . ILE   D 209 ? 1.2091 1.1173 1.1347 -0.0164 -0.0354 -0.0131 278  ILE   D C   
10183 O  O   . ILE   D 209 ? 1.1824 1.0888 1.1057 -0.0133 -0.0331 -0.0114 278  ILE   D O   
10184 C  CB  . ILE   D 209 ? 1.2198 1.1387 1.1614 -0.0286 -0.0362 -0.0111 278  ILE   D CB  
10185 C  CG1 . ILE   D 209 ? 1.2634 1.1944 1.2162 -0.0329 -0.0379 -0.0110 278  ILE   D CG1 
10186 C  CG2 . ILE   D 209 ? 1.2002 1.1134 1.1411 -0.0300 -0.0320 -0.0074 278  ILE   D CG2 
10187 C  CD1 . ILE   D 209 ? 1.2367 1.1705 1.1902 -0.0344 -0.0416 -0.0140 278  ILE   D CD1 
10188 N  N   . ASP   D 210 ? 1.2449 1.1443 1.1626 -0.0152 -0.0366 -0.0149 279  ASP   D N   
10189 C  CA  . ASP   D 210 ? 1.2022 1.0893 1.1084 -0.0105 -0.0352 -0.0147 279  ASP   D CA  
10190 C  C   . ASP   D 210 ? 1.2006 1.0883 1.1022 -0.0027 -0.0371 -0.0174 279  ASP   D C   
10191 O  O   . ASP   D 210 ? 1.2171 1.0974 1.1110 0.0020  -0.0357 -0.0166 279  ASP   D O   
10192 C  CB  . ASP   D 210 ? 1.1982 1.0754 1.0977 -0.0120 -0.0360 -0.0158 279  ASP   D CB  
10193 C  CG  . ASP   D 210 ? 1.2147 1.0926 1.1200 -0.0197 -0.0357 -0.0143 279  ASP   D CG  
10194 O  OD1 . ASP   D 210 ? 1.2209 1.0983 1.1304 -0.0238 -0.0328 -0.0109 279  ASP   D OD1 
10195 O  OD2 . ASP   D 210 ? 1.2759 1.1549 1.1819 -0.0216 -0.0386 -0.0165 279  ASP   D OD2 
10196 N  N   . PHE   D 211 ? 1.2465 1.1424 1.1524 -0.0011 -0.0403 -0.0206 280  PHE   D N   
10197 C  CA  . PHE   D 211 ? 1.2186 1.1161 1.1220 0.0062  -0.0424 -0.0233 280  PHE   D CA  
10198 C  C   . PHE   D 211 ? 1.1904 1.0913 1.0956 0.0087  -0.0413 -0.0218 280  PHE   D C   
10199 O  O   . PHE   D 211 ? 1.2311 1.1261 1.1292 0.0148  -0.0418 -0.0225 280  PHE   D O   
10200 C  CB  . PHE   D 211 ? 1.2084 1.1159 1.1187 0.0066  -0.0452 -0.0265 280  PHE   D CB  
10201 C  CG  . PHE   D 211 ? 1.1754 1.0847 1.0844 0.0139  -0.0477 -0.0298 280  PHE   D CG  
10202 C  CD1 . PHE   D 211 ? 1.1472 1.0642 1.0617 0.0167  -0.0485 -0.0301 280  PHE   D CD1 
10203 C  CD2 . PHE   D 211 ? 1.1884 1.0916 1.0911 0.0179  -0.0493 -0.0326 280  PHE   D CD2 
10204 C  CE1 . PHE   D 211 ? 1.1375 1.0562 1.0518 0.0233  -0.0513 -0.0333 280  PHE   D CE1 
10205 C  CE2 . PHE   D 211 ? 1.1815 1.0867 1.0843 0.0246  -0.0518 -0.0357 280  PHE   D CE2 
10206 C  CZ  . PHE   D 211 ? 1.1555 1.0684 1.0643 0.0272  -0.0529 -0.0361 280  PHE   D CZ  
10207 N  N   . SER   D 212 ? 1.1595 1.0693 1.0738 0.0043  -0.0401 -0.0197 281  SER   D N   
10208 C  CA  . SER   D 212 ? 1.1191 1.0323 1.0354 0.0064  -0.0390 -0.0182 281  SER   D CA  
10209 C  C   . SER   D 212 ? 1.1596 1.0608 1.0661 0.0088  -0.0359 -0.0155 281  SER   D C   
10210 O  O   . SER   D 212 ? 1.1581 1.0561 1.0593 0.0147  -0.0362 -0.0159 281  SER   D O   
10211 C  CB  . SER   D 212 ? 1.0690 0.9926 0.9964 0.0006  -0.0378 -0.0160 281  SER   D CB  
10212 O  OG  . SER   D 212 ? 1.1172 1.0363 1.0446 -0.0046 -0.0344 -0.0126 281  SER   D OG  
10213 N  N   . TYR   D 213 ? 1.1877 1.0816 1.0915 0.0044  -0.0328 -0.0129 282  TYR   D N   
10214 C  CA  . TYR   D 213 ? 1.1686 1.0504 1.0629 0.0064  -0.0290 -0.0101 282  TYR   D CA  
10215 C  C   . TYR   D 213 ? 1.1895 1.0597 1.0709 0.0130  -0.0304 -0.0121 282  TYR   D C   
10216 O  O   . TYR   D 213 ? 1.2392 1.0996 1.1111 0.0172  -0.0282 -0.0105 282  TYR   D O   
10217 C  CB  . TYR   D 213 ? 1.1693 1.0464 1.0651 -0.0003 -0.0252 -0.0067 282  TYR   D CB  
10218 C  CG  . TYR   D 213 ? 1.1429 1.0301 1.0507 -0.0062 -0.0233 -0.0042 282  TYR   D CG  
10219 C  CD1 . TYR   D 213 ? 1.1224 1.0147 1.0332 -0.0042 -0.0218 -0.0027 282  TYR   D CD1 
10220 C  CD2 . TYR   D 213 ? 1.1705 1.0621 1.0867 -0.0134 -0.0234 -0.0035 282  TYR   D CD2 
10221 C  CE1 . TYR   D 213 ? 1.1009 1.0026 1.0228 -0.0092 -0.0201 -0.0005 282  TYR   D CE1 
10222 C  CE2 . TYR   D 213 ? 1.1330 1.0340 1.0606 -0.0185 -0.0221 -0.0014 282  TYR   D CE2 
10223 C  CZ  . TYR   D 213 ? 1.1309 1.0371 1.0614 -0.0163 -0.0203 0.0001  282  TYR   D CZ  
10224 O  OH  . TYR   D 213 ? 1.2278 1.1434 1.1697 -0.0212 -0.0190 0.0022  282  TYR   D OH  
10225 N  N   . ARG   D 214 ? 1.3016 1.1719 1.1819 0.0143  -0.0340 -0.0155 283  ARG   D N   
10226 C  CA  . ARG   D 214 ? 1.3367 1.1964 1.2052 0.0210  -0.0357 -0.0176 283  ARG   D CA  
10227 C  C   . ARG   D 214 ? 1.3373 1.2003 1.2047 0.0284  -0.0389 -0.0202 283  ARG   D C   
10228 O  O   . ARG   D 214 ? 1.3593 1.2122 1.2158 0.0348  -0.0394 -0.0207 283  ARG   D O   
10229 C  CB  . ARG   D 214 ? 1.3742 1.2327 1.2419 0.0201  -0.0381 -0.0204 283  ARG   D CB  
10230 C  CG  . ARG   D 214 ? 1.4390 1.2885 1.2962 0.0274  -0.0405 -0.0232 283  ARG   D CG  
10231 C  CD  . ARG   D 214 ? 1.4793 1.3129 1.3237 0.0288  -0.0377 -0.0210 283  ARG   D CD  
10232 N  NE  . ARG   D 214 ? 1.5950 1.4204 1.4303 0.0343  -0.0405 -0.0241 283  ARG   D NE  
10233 C  CZ  . ARG   D 214 ? 1.5955 1.4206 1.4314 0.0324  -0.0420 -0.0261 283  ARG   D CZ  
10234 N  NH1 . ARG   D 214 ? 1.5391 1.3709 1.3834 0.0252  -0.0412 -0.0254 283  ARG   D NH1 
10235 N  NH2 . ARG   D 214 ? 1.6801 1.4978 1.5078 0.0381  -0.0445 -0.0289 283  ARG   D NH2 
10236 N  N   . VAL   D 215 ? 1.2029 1.0795 1.0812 0.0277  -0.0411 -0.0217 284  VAL   D N   
10237 C  CA  . VAL   D 215 ? 1.1344 1.0143 1.0127 0.0343  -0.0443 -0.0241 284  VAL   D CA  
10238 C  C   . VAL   D 215 ? 1.1282 1.0035 1.0014 0.0368  -0.0421 -0.0214 284  VAL   D C   
10239 O  O   . VAL   D 215 ? 1.1574 1.0284 1.0243 0.0438  -0.0445 -0.0230 284  VAL   D O   
10240 C  CB  . VAL   D 215 ? 1.0886 0.9840 0.9802 0.0327  -0.0471 -0.0264 284  VAL   D CB  
10241 C  CG1 . VAL   D 215 ? 1.1393 1.0390 1.0328 0.0385  -0.0500 -0.0282 284  VAL   D CG1 
10242 C  CG2 . VAL   D 215 ? 1.0954 0.9933 0.9895 0.0329  -0.0496 -0.0298 284  VAL   D CG2 
10243 N  N   . ALA   D 216 ? 1.1329 1.0084 1.0084 0.0315  -0.0375 -0.0173 285  ALA   D N   
10244 C  CA  . ALA   D 216 ? 1.1261 0.9970 0.9966 0.0339  -0.0348 -0.0146 285  ALA   D CA  
10245 C  C   . ALA   D 216 ? 1.2486 1.1026 1.1034 0.0388  -0.0328 -0.0133 285  ALA   D C   
10246 O  O   . ALA   D 216 ? 1.2645 1.1122 1.1114 0.0443  -0.0323 -0.0125 285  ALA   D O   
10247 C  CB  . ALA   D 216 ? 1.0808 0.9571 0.9593 0.0269  -0.0302 -0.0105 285  ALA   D CB  
10248 N  N   . ALA   D 217 ? 1.1987 1.0443 1.0479 0.0373  -0.0318 -0.0132 286  ALA   D N   
10249 C  CA  . ALA   D 217 ? 1.2337 1.0626 1.0672 0.0423  -0.0300 -0.0122 286  ALA   D CA  
10250 C  C   . ALA   D 217 ? 1.2840 1.1075 1.1094 0.0500  -0.0353 -0.0165 286  ALA   D C   
10251 O  O   . ALA   D 217 ? 1.3596 1.1685 1.1708 0.0552  -0.0346 -0.0160 286  ALA   D O   
10252 C  CB  . ALA   D 217 ? 1.3424 1.1630 1.1728 0.0368  -0.0255 -0.0093 286  ALA   D CB  
10253 N  N   . CYS   D 218 ? 1.3659 1.2002 1.1998 0.0511  -0.0405 -0.0205 287  CYS   D N   
10254 C  CA  . CYS   D 218 ? 1.3678 1.1983 1.1957 0.0589  -0.0458 -0.0248 287  CYS   D CA  
10255 C  C   . CYS   D 218 ? 1.3586 1.1946 1.1889 0.0646  -0.0498 -0.0271 287  CYS   D C   
10256 O  O   . CYS   D 218 ? 1.3710 1.2022 1.1952 0.0720  -0.0544 -0.0304 287  CYS   D O   
10257 C  CB  . CYS   D 218 ? 1.3926 1.2301 1.2278 0.0572  -0.0489 -0.0282 287  CYS   D CB  
10258 S  SG  . CYS   D 218 ? 1.8989 1.7228 1.7235 0.0564  -0.0473 -0.0280 287  CYS   D SG  
10259 N  N   . LEU   D 219 ? 1.2263 1.0721 1.0655 0.0615  -0.0486 -0.0255 288  LEU   D N   
10260 C  CA  . LEU   D 219 ? 1.1191 0.9701 0.9609 0.0666  -0.0525 -0.0276 288  LEU   D CA  
10261 C  C   . LEU   D 219 ? 1.1740 1.0113 1.0011 0.0728  -0.0515 -0.0259 288  LEU   D C   
10262 O  O   . LEU   D 219 ? 1.2132 1.0421 1.0332 0.0704  -0.0458 -0.0217 288  LEU   D O   
10263 C  CB  . LEU   D 219 ? 1.0904 0.9560 0.9462 0.0610  -0.0513 -0.0264 288  LEU   D CB  
10264 C  CG  . LEU   D 219 ? 1.0753 0.9557 0.9457 0.0584  -0.0548 -0.0297 288  LEU   D CG  
10265 C  CD1 . LEU   D 219 ? 1.0606 0.9546 0.9441 0.0523  -0.0533 -0.0281 288  LEU   D CD1 
10266 C  CD2 . LEU   D 219 ? 1.1404 1.0225 1.0113 0.0658  -0.0611 -0.0343 288  LEU   D CD2 
10267 N  N   . PRO   D 220 ? 1.1636 0.9981 0.9860 0.0809  -0.0569 -0.0293 289  PRO   D N   
10268 C  CA  . PRO   D 220 ? 1.1391 0.9613 0.9476 0.0873  -0.0565 -0.0279 289  PRO   D CA  
10269 C  C   . PRO   D 220 ? 1.1541 0.9826 0.9676 0.0853  -0.0542 -0.0255 289  PRO   D C   
10270 O  O   . PRO   D 220 ? 1.1913 1.0239 1.0071 0.0898  -0.0589 -0.0279 289  PRO   D O   
10271 C  CB  . PRO   D 220 ? 1.1441 0.9635 0.9486 0.0962  -0.0643 -0.0330 289  PRO   D CB  
10272 C  CG  . PRO   D 220 ? 1.1272 0.9633 0.9491 0.0934  -0.0685 -0.0367 289  PRO   D CG  
10273 C  CD  . PRO   D 220 ? 1.1193 0.9612 0.9487 0.0848  -0.0639 -0.0346 289  PRO   D CD  
10274 N  N   . ILE   D 221 ? 1.1584 0.9879 0.9743 0.0785  -0.0474 -0.0208 290  ILE   D N   
10275 C  CA  . ILE   D 221 ? 1.1695 1.0058 0.9913 0.0759  -0.0446 -0.0182 290  ILE   D CA  
10276 C  C   . ILE   D 221 ? 1.1897 1.0129 0.9993 0.0762  -0.0376 -0.0132 290  ILE   D C   
10277 O  O   . ILE   D 221 ? 1.2244 1.0373 1.0262 0.0748  -0.0336 -0.0110 290  ILE   D O   
10278 C  CB  . ILE   D 221 ? 1.1469 0.9997 0.9866 0.0667  -0.0428 -0.0172 290  ILE   D CB  
10279 C  CG1 . ILE   D 221 ? 1.2065 1.0578 1.0479 0.0601  -0.0386 -0.0151 290  ILE   D CG1 
10280 C  CG2 . ILE   D 221 ? 1.1372 1.0038 0.9895 0.0667  -0.0490 -0.0218 290  ILE   D CG2 
10281 C  CD1 . ILE   D 221 ? 1.1650 1.0318 1.0229 0.0522  -0.0387 -0.0154 290  ILE   D CD1 
10282 N  N   . ASP   D 222 ? 1.2456 1.0691 1.0539 0.0779  -0.0360 -0.0115 291  ASP   D N   
10283 C  CA  . ASP   D 222 ? 1.3138 1.1259 1.1115 0.0785  -0.0289 -0.0065 291  ASP   D CA  
10284 C  C   . ASP   D 222 ? 1.3084 1.1277 1.1170 0.0689  -0.0219 -0.0022 291  ASP   D C   
10285 O  O   . ASP   D 222 ? 1.2944 1.1277 1.1182 0.0623  -0.0232 -0.0032 291  ASP   D O   
10286 C  CB  . ASP   D 222 ? 1.3355 1.1455 1.1279 0.0844  -0.0302 -0.0066 291  ASP   D CB  
10287 C  CG  . ASP   D 222 ? 1.3534 1.1812 1.1622 0.0811  -0.0335 -0.0083 291  ASP   D CG  
10288 O  OD1 . ASP   D 222 ? 1.3256 1.1665 1.1492 0.0741  -0.0340 -0.0090 291  ASP   D OD1 
10289 O  OD2 . ASP   D 222 ? 1.4183 1.2464 1.2248 0.0856  -0.0358 -0.0091 291  ASP   D OD2 
10290 N  N   . ASP   D 223 ? 1.2996 1.1090 1.1004 0.0684  -0.0144 0.0026  292  ASP   D N   
10291 C  CA  . ASP   D 223 ? 1.2983 1.1127 1.1088 0.0596  -0.0074 0.0069  292  ASP   D CA  
10292 C  C   . ASP   D 223 ? 1.2645 1.0957 1.0914 0.0544  -0.0074 0.0074  292  ASP   D C   
10293 O  O   . ASP   D 223 ? 1.2365 1.0770 1.0763 0.0463  -0.0048 0.0091  292  ASP   D O   
10294 C  CB  . ASP   D 223 ? 1.2923 1.0912 1.0903 0.0610  0.0010  0.0120  292  ASP   D CB  
10295 C  CG  . ASP   D 223 ? 1.3259 1.1111 1.1135 0.0611  0.0032  0.0128  292  ASP   D CG  
10296 O  OD1 . ASP   D 223 ? 1.3512 1.1415 1.1449 0.0579  -0.0006 0.0101  292  ASP   D OD1 
10297 O  OD2 . ASP   D 223 ? 1.2592 1.0286 1.0327 0.0644  0.0091  0.0161  292  ASP   D OD2 
10298 N  N   . VAL   D 224 ? 1.3056 1.1410 1.1325 0.0589  -0.0106 0.0059  293  VAL   D N   
10299 C  CA  . VAL   D 224 ? 1.2874 1.1384 1.1297 0.0539  -0.0105 0.0065  293  VAL   D CA  
10300 C  C   . VAL   D 224 ? 1.2449 1.1107 1.1018 0.0490  -0.0159 0.0030  293  VAL   D C   
10301 O  O   . VAL   D 224 ? 1.2741 1.1517 1.1449 0.0418  -0.0143 0.0043  293  VAL   D O   
10302 C  CB  . VAL   D 224 ? 1.3320 1.1834 1.1705 0.0599  -0.0125 0.0057  293  VAL   D CB  
10303 C  CG1 . VAL   D 224 ? 1.3868 1.2248 1.2127 0.0633  -0.0055 0.0101  293  VAL   D CG1 
10304 C  CG2 . VAL   D 224 ? 1.3080 1.1565 1.1397 0.0675  -0.0208 0.0006  293  VAL   D CG2 
10305 N  N   . LEU   D 225 ? 1.2556 1.1207 1.1097 0.0529  -0.0224 -0.0015 294  LEU   D N   
10306 C  CA  . LEU   D 225 ? 1.1924 1.0701 1.0594 0.0483  -0.0266 -0.0045 294  LEU   D CA  
10307 C  C   . LEU   D 225 ? 1.1813 1.0586 1.0520 0.0414  -0.0230 -0.0026 294  LEU   D C   
10308 O  O   . LEU   D 225 ? 1.1635 1.0525 1.0474 0.0347  -0.0232 -0.0026 294  LEU   D O   
10309 C  CB  . LEU   D 225 ? 1.1664 1.0428 1.0297 0.0543  -0.0338 -0.0096 294  LEU   D CB  
10310 C  CG  . LEU   D 225 ? 1.0869 0.9745 0.9586 0.0566  -0.0396 -0.0131 294  LEU   D CG  
10311 C  CD1 . LEU   D 225 ? 1.0697 0.9571 0.9395 0.0589  -0.0379 -0.0111 294  LEU   D CD1 
10312 C  CD2 . LEU   D 225 ? 1.1360 1.0192 1.0018 0.0638  -0.0461 -0.0178 294  LEU   D CD2 
10313 N  N   . ARG   D 226 ? 1.2111 1.0743 1.0700 0.0430  -0.0196 -0.0008 295  ARG   D N   
10314 C  CA  . ARG   D 226 ? 1.1785 1.0401 1.0404 0.0365  -0.0163 0.0011  295  ARG   D CA  
10315 C  C   . ARG   D 226 ? 1.1972 1.0666 1.0706 0.0287  -0.0113 0.0049  295  ARG   D C   
10316 O  O   . ARG   D 226 ? 1.1884 1.0662 1.0726 0.0220  -0.0118 0.0046  295  ARG   D O   
10317 C  CB  . ARG   D 226 ? 1.2105 1.0546 1.0570 0.0398  -0.0130 0.0027  295  ARG   D CB  
10318 C  CG  . ARG   D 226 ? 1.1861 1.0238 1.0243 0.0449  -0.0183 -0.0013 295  ARG   D CG  
10319 C  CD  . ARG   D 226 ? 1.2074 1.0273 1.0301 0.0480  -0.0150 0.0004  295  ARG   D CD  
10320 N  NE  . ARG   D 226 ? 1.2304 1.0459 1.0474 0.0518  -0.0202 -0.0036 295  ARG   D NE  
10321 C  CZ  . ARG   D 226 ? 1.3191 1.1209 1.1246 0.0535  -0.0186 -0.0030 295  ARG   D CZ  
10322 N  NH1 . ARG   D 226 ? 1.3236 1.1139 1.1215 0.0518  -0.0118 0.0014  295  ARG   D NH1 
10323 N  NH2 . ARG   D 226 ? 1.3518 1.1513 1.1537 0.0569  -0.0238 -0.0069 295  ARG   D NH2 
10324 N  N   . ILE   D 227 ? 1.1944 1.0614 1.0658 0.0297  -0.0065 0.0083  296  ILE   D N   
10325 C  CA  . ILE   D 227 ? 1.1720 1.0468 1.0554 0.0224  -0.0017 0.0119  296  ILE   D CA  
10326 C  C   . ILE   D 227 ? 1.1226 1.0143 1.0205 0.0191  -0.0055 0.0102  296  ILE   D C   
10327 O  O   . ILE   D 227 ? 1.1179 1.0181 1.0277 0.0124  -0.0031 0.0123  296  ILE   D O   
10328 C  CB  . ILE   D 227 ? 1.1734 1.0404 1.0510 0.0240  0.0054  0.0165  296  ILE   D CB  
10329 C  CG1 . ILE   D 227 ? 1.2761 1.1456 1.1510 0.0297  0.0039  0.0159  296  ILE   D CG1 
10330 C  CG2 . ILE   D 227 ? 1.1658 1.0153 1.0278 0.0280  0.0092  0.0182  296  ILE   D CG2 
10331 C  CD1 . ILE   D 227 ? 1.3383 1.2000 1.2071 0.0317  0.0113  0.0204  296  ILE   D CD1 
10332 N  N   . GLN   D 228 ? 1.1113 1.0078 1.0087 0.0238  -0.0113 0.0064  297  GLN   D N   
10333 C  CA  . GLN   D 228 ? 1.1356 1.0476 1.0466 0.0205  -0.0149 0.0046  297  GLN   D CA  
10334 C  C   . GLN   D 228 ? 1.0897 1.0089 1.0091 0.0153  -0.0181 0.0024  297  GLN   D C   
10335 O  O   . GLN   D 228 ? 1.0904 1.0203 1.0219 0.0092  -0.0179 0.0030  297  GLN   D O   
10336 C  CB  . GLN   D 228 ? 1.1765 1.0912 1.0850 0.0271  -0.0200 0.0013  297  GLN   D CB  
10337 C  CG  . GLN   D 228 ? 1.2070 1.1202 1.1121 0.0309  -0.0180 0.0031  297  GLN   D CG  
10338 C  CD  . GLN   D 228 ? 1.3495 1.2693 1.2567 0.0355  -0.0242 -0.0007 297  GLN   D CD  
10339 O  OE1 . GLN   D 228 ? 1.3576 1.2702 1.2551 0.0426  -0.0258 -0.0016 297  GLN   D OE1 
10340 N  NE2 . GLN   D 228 ? 1.3437 1.2769 1.2638 0.0315  -0.0278 -0.0030 297  GLN   D NE2 
10341 N  N   . LEU   D 229 ? 1.0765 0.9897 0.9892 0.0180  -0.0211 -0.0004 298  LEU   D N   
10342 C  CA  . LEU   D 229 ? 1.0335 0.9516 0.9524 0.0135  -0.0236 -0.0024 298  LEU   D CA  
10343 C  C   . LEU   D 229 ? 1.1148 1.0318 1.0380 0.0063  -0.0193 0.0008  298  LEU   D C   
10344 O  O   . LEU   D 229 ? 1.1315 1.0570 1.0646 0.0005  -0.0208 0.0002  298  LEU   D O   
10345 C  CB  . LEU   D 229 ? 1.0415 0.9513 0.9509 0.0182  -0.0267 -0.0055 298  LEU   D CB  
10346 C  CG  . LEU   D 229 ? 1.0399 0.9514 0.9466 0.0251  -0.0319 -0.0095 298  LEU   D CG  
10347 C  CD1 . LEU   D 229 ? 1.0498 0.9516 0.9466 0.0297  -0.0343 -0.0120 298  LEU   D CD1 
10348 C  CD2 . LEU   D 229 ? 1.0248 0.9508 0.9442 0.0224  -0.0354 -0.0119 298  LEU   D CD2 
10349 N  N   . LEU   D 230 ? 1.1051 1.0113 1.0211 0.0066  -0.0142 0.0043  299  LEU   D N   
10350 C  CA  . LEU   D 230 ? 1.0531 0.9577 0.9739 -0.0003 -0.0099 0.0075  299  LEU   D CA  
10351 C  C   . LEU   D 230 ? 1.0738 0.9904 1.0085 -0.0060 -0.0084 0.0095  299  LEU   D C   
10352 O  O   . LEU   D 230 ? 1.0797 1.0012 1.0234 -0.0127 -0.0083 0.0102  299  LEU   D O   
10353 C  CB  . LEU   D 230 ? 1.0642 0.9548 0.9747 0.0016  -0.0040 0.0110  299  LEU   D CB  
10354 C  CG  . LEU   D 230 ? 1.1405 1.0176 1.0368 0.0065  -0.0049 0.0094  299  LEU   D CG  
10355 C  CD1 . LEU   D 230 ? 1.2456 1.1087 1.1329 0.0069  0.0016  0.0134  299  LEU   D CD1 
10356 C  CD2 . LEU   D 230 ? 1.1711 1.0499 1.0701 0.0033  -0.0089 0.0066  299  LEU   D CD2 
10357 N  N   . LYS   D 231 ? 1.0764 0.9978 1.0128 -0.0032 -0.0077 0.0103  300  LYS   D N   
10358 C  CA  . LYS   D 231 ? 1.0786 1.0113 1.0279 -0.0080 -0.0063 0.0122  300  LYS   D CA  
10359 C  C   . LYS   D 231 ? 1.1160 1.0619 1.0754 -0.0107 -0.0118 0.0091  300  LYS   D C   
10360 O  O   . LYS   D 231 ? 1.1295 1.0845 1.1002 -0.0159 -0.0113 0.0104  300  LYS   D O   
10361 C  CB  . LYS   D 231 ? 1.1009 1.0329 1.0474 -0.0038 -0.0032 0.0143  300  LYS   D CB  
10362 C  CG  . LYS   D 231 ? 1.1218 1.0417 1.0605 -0.0026 0.0038  0.0184  300  LYS   D CG  
10363 C  CD  . LYS   D 231 ? 1.2263 1.1474 1.1658 -0.0006 0.0081  0.0213  300  LYS   D CD  
10364 C  CE  . LYS   D 231 ? 1.2741 1.1832 1.1978 0.0078  0.0094  0.0214  300  LYS   D CE  
10365 N  NZ  . LYS   D 231 ? 1.2948 1.2044 1.2127 0.0130  0.0022  0.0166  300  LYS   D NZ  
10366 N  N   . ILE   D 232 ? 1.1247 1.0711 1.0801 -0.0072 -0.0168 0.0051  301  ILE   D N   
10367 C  CA  . ILE   D 232 ? 1.0804 1.0381 1.0445 -0.0095 -0.0216 0.0022  301  ILE   D CA  
10368 C  C   . ILE   D 232 ? 1.1605 1.1205 1.1309 -0.0164 -0.0219 0.0025  301  ILE   D C   
10369 O  O   . ILE   D 232 ? 1.1418 1.0936 1.1069 -0.0173 -0.0215 0.0023  301  ILE   D O   
10370 C  CB  . ILE   D 232 ? 1.0390 0.9954 0.9973 -0.0041 -0.0262 -0.0020 301  ILE   D CB  
10371 C  CG1 . ILE   D 232 ? 1.0276 0.9867 0.9843 0.0017  -0.0279 -0.0033 301  ILE   D CG1 
10372 C  CG2 . ILE   D 232 ? 1.0953 1.0598 1.0605 -0.0071 -0.0301 -0.0048 301  ILE   D CG2 
10373 C  CD1 . ILE   D 232 ? 0.9895 0.9499 0.9440 0.0063  -0.0330 -0.0078 301  ILE   D CD1 
10374 N  N   . GLY   D 233 ? 1.2522 1.2229 1.2339 -0.0211 -0.0229 0.0029  302  GLY   D N   
10375 C  CA  . GLY   D 233 ? 1.2651 1.2385 1.2535 -0.0277 -0.0237 0.0032  302  GLY   D CA  
10376 C  C   . GLY   D 233 ? 1.2668 1.2383 1.2520 -0.0281 -0.0275 -0.0001 302  GLY   D C   
10377 O  O   . GLY   D 233 ? 1.3189 1.2827 1.3002 -0.0300 -0.0269 0.0001  302  GLY   D O   
10378 N  N   . SER   D 234 ? 1.1295 1.1075 1.1163 -0.0262 -0.0311 -0.0031 303  SER   D N   
10379 C  CA  . SER   D 234 ? 1.0935 1.0704 1.0780 -0.0265 -0.0344 -0.0061 303  SER   D CA  
10380 C  C   . SER   D 234 ? 1.1048 1.0737 1.0791 -0.0206 -0.0351 -0.0084 303  SER   D C   
10381 O  O   . SER   D 234 ? 1.0965 1.0640 1.0669 -0.0154 -0.0347 -0.0087 303  SER   D O   
10382 C  CB  . SER   D 234 ? 1.1291 1.1165 1.1202 -0.0271 -0.0375 -0.0083 303  SER   D CB  
10383 O  OG  . SER   D 234 ? 1.1383 1.1283 1.1276 -0.0215 -0.0386 -0.0103 303  SER   D OG  
10384 N  N   . ALA   D 235 ? 1.1142 1.0779 1.0841 -0.0214 -0.0366 -0.0102 304  ALA   D N   
10385 C  CA  . ALA   D 235 ? 1.0461 1.0028 1.0071 -0.0159 -0.0378 -0.0127 304  ALA   D CA  
10386 C  C   . ALA   D 235 ? 1.0057 0.9694 0.9689 -0.0116 -0.0406 -0.0158 304  ALA   D C   
10387 O  O   . ALA   D 235 ? 1.0431 1.0029 1.0006 -0.0058 -0.0415 -0.0175 304  ALA   D O   
10388 C  CB  . ALA   D 235 ? 1.1127 1.0625 1.0690 -0.0179 -0.0387 -0.0139 304  ALA   D CB  
10389 N  N   . ILE   D 236 ? 1.0816 1.0554 1.0532 -0.0142 -0.0421 -0.0166 305  ILE   D N   
10390 C  CA  . ILE   D 236 ? 1.1074 1.0880 1.0821 -0.0105 -0.0443 -0.0195 305  ILE   D CA  
10391 C  C   . ILE   D 236 ? 1.1058 1.0894 1.0819 -0.0067 -0.0441 -0.0189 305  ILE   D C   
10392 O  O   . ILE   D 236 ? 1.1140 1.0975 1.0883 -0.0013 -0.0458 -0.0213 305  ILE   D O   
10393 C  CB  . ILE   D 236 ? 1.0909 1.0808 1.0737 -0.0143 -0.0456 -0.0202 305  ILE   D CB  
10394 C  CG1 . ILE   D 236 ? 1.0695 1.0558 1.0491 -0.0159 -0.0466 -0.0220 305  ILE   D CG1 
10395 C  CG2 . ILE   D 236 ? 1.0577 1.0561 1.0459 -0.0111 -0.0471 -0.0223 305  ILE   D CG2 
10396 C  CD1 . ILE   D 236 ? 1.0419 1.0360 1.0275 -0.0181 -0.0478 -0.0234 305  ILE   D CD1 
10397 N  N   . GLN   D 237 ? 1.0760 1.0617 1.0553 -0.0092 -0.0420 -0.0159 306  GLN   D N   
10398 C  CA  . GLN   D 237 ? 1.0641 1.0508 1.0430 -0.0052 -0.0415 -0.0151 306  GLN   D CA  
10399 C  C   . GLN   D 237 ? 1.1033 1.0789 1.0714 0.0002  -0.0410 -0.0153 306  GLN   D C   
10400 O  O   . GLN   D 237 ? 1.1186 1.0937 1.0842 0.0056  -0.0424 -0.0166 306  GLN   D O   
10401 C  CB  . GLN   D 237 ? 1.0398 1.0303 1.0238 -0.0090 -0.0389 -0.0116 306  GLN   D CB  
10402 C  CG  . GLN   D 237 ? 1.0055 1.0076 0.9999 -0.0124 -0.0401 -0.0117 306  GLN   D CG  
10403 C  CD  . GLN   D 237 ? 1.0096 1.0150 1.0096 -0.0175 -0.0376 -0.0082 306  GLN   D CD  
10404 O  OE1 . GLN   D 237 ? 0.9683 0.9682 0.9664 -0.0204 -0.0353 -0.0060 306  GLN   D OE1 
10405 N  NE2 . GLN   D 237 ? 1.0512 1.0656 1.0587 -0.0185 -0.0381 -0.0077 306  GLN   D NE2 
10406 N  N   . ARG   D 238 ? 1.0491 1.0155 1.0106 -0.0010 -0.0393 -0.0143 307  ARG   D N   
10407 C  CA  . ARG   D 238 ? 1.0281 0.9828 0.9783 0.0041  -0.0386 -0.0143 307  ARG   D CA  
10408 C  C   . ARG   D 238 ? 1.0421 0.9947 0.9881 0.0095  -0.0422 -0.0184 307  ARG   D C   
10409 O  O   . ARG   D 238 ? 1.0253 0.9724 0.9647 0.0156  -0.0433 -0.0194 307  ARG   D O   
10410 C  CB  . ARG   D 238 ? 1.0275 0.9730 0.9724 0.0007  -0.0355 -0.0119 307  ARG   D CB  
10411 C  CG  . ARG   D 238 ? 1.0210 0.9535 0.9542 0.0049  -0.0333 -0.0106 307  ARG   D CG  
10412 C  CD  . ARG   D 238 ? 1.0370 0.9616 0.9673 0.0003  -0.0299 -0.0080 307  ARG   D CD  
10413 N  NE  . ARG   D 238 ? 1.0884 1.0191 1.0279 -0.0062 -0.0272 -0.0049 307  ARG   D NE  
10414 C  CZ  . ARG   D 238 ? 1.1303 1.0655 1.0770 -0.0125 -0.0278 -0.0047 307  ARG   D CZ  
10415 N  NH1 . ARG   D 238 ? 1.1342 1.0677 1.0792 -0.0135 -0.0304 -0.0071 307  ARG   D NH1 
10416 N  NH2 . ARG   D 238 ? 1.1073 1.0486 1.0630 -0.0178 -0.0257 -0.0020 307  ARG   D NH2 
10417 N  N   . LEU   D 239 ? 1.0414 0.9977 0.9911 0.0075  -0.0441 -0.0207 308  LEU   D N   
10418 C  CA  . LEU   D 239 ? 1.0010 0.9576 0.9494 0.0125  -0.0474 -0.0246 308  LEU   D CA  
10419 C  C   . LEU   D 239 ? 1.0056 0.9713 0.9609 0.0157  -0.0498 -0.0266 308  LEU   D C   
10420 O  O   . LEU   D 239 ? 0.9868 0.9509 0.9398 0.0216  -0.0525 -0.0293 308  LEU   D O   
10421 C  CB  . LEU   D 239 ? 0.9904 0.9495 0.9416 0.0094  -0.0482 -0.0263 308  LEU   D CB  
10422 C  CG  . LEU   D 239 ? 0.9974 0.9491 0.9436 0.0054  -0.0465 -0.0250 308  LEU   D CG  
10423 C  CD1 . LEU   D 239 ? 0.9936 0.9494 0.9434 0.0031  -0.0477 -0.0271 308  LEU   D CD1 
10424 C  CD2 . LEU   D 239 ? 1.0906 1.0300 1.0256 0.0097  -0.0464 -0.0255 308  LEU   D CD2 
10425 N  N   . ARG   D 240 ? 1.0071 0.9825 0.9714 0.0117  -0.0492 -0.0254 309  ARG   D N   
10426 C  CA  . ARG   D 240 ? 0.9977 0.9812 0.9686 0.0145  -0.0514 -0.0269 309  ARG   D CA  
10427 C  C   . ARG   D 240 ? 1.0687 1.0470 1.0339 0.0195  -0.0518 -0.0263 309  ARG   D C   
10428 O  O   . ARG   D 240 ? 1.0915 1.0725 1.0586 0.0242  -0.0548 -0.0288 309  ARG   D O   
10429 C  CB  . ARG   D 240 ? 0.9870 0.9808 0.9677 0.0092  -0.0503 -0.0253 309  ARG   D CB  
10430 C  CG  . ARG   D 240 ? 0.9658 0.9672 0.9536 0.0072  -0.0515 -0.0275 309  ARG   D CG  
10431 C  CD  . ARG   D 240 ? 0.9709 0.9808 0.9667 0.0018  -0.0505 -0.0259 309  ARG   D CD  
10432 N  NE  . ARG   D 240 ? 1.0536 1.0694 1.0544 0.0029  -0.0509 -0.0252 309  ARG   D NE  
10433 C  CZ  . ARG   D 240 ? 1.0648 1.0872 1.0716 0.0055  -0.0530 -0.0274 309  ARG   D CZ  
10434 N  NH1 . ARG   D 240 ? 0.9788 1.0031 0.9880 0.0077  -0.0546 -0.0306 309  ARG   D NH1 
10435 N  NH2 . ARG   D 240 ? 1.1051 1.1322 1.1159 0.0061  -0.0533 -0.0265 309  ARG   D NH2 
10436 N  N   . CYS   D 241 ? 1.0855 1.0556 1.0432 0.0188  -0.0488 -0.0232 310  CYS   D N   
10437 C  CA  . CYS   D 241 ? 1.0829 1.0469 1.0338 0.0239  -0.0488 -0.0224 310  CYS   D CA  
10438 C  C   . CYS   D 241 ? 0.9981 0.9513 0.9383 0.0302  -0.0507 -0.0245 310  CYS   D C   
10439 O  O   . CYS   D 241 ? 1.0011 0.9523 0.9381 0.0363  -0.0536 -0.0264 310  CYS   D O   
10440 C  CB  . CYS   D 241 ? 1.0894 1.0496 1.0375 0.0207  -0.0442 -0.0180 310  CYS   D CB  
10441 S  SG  . CYS   D 241 ? 1.1437 1.0973 1.0837 0.0271  -0.0440 -0.0170 310  CYS   D SG  
10442 N  N   . GLU   D 242 ? 1.0053 0.9511 0.9395 0.0291  -0.0495 -0.0243 311  GLU   D N   
10443 C  CA  . GLU   D 242 ? 1.0183 0.9539 0.9425 0.0353  -0.0516 -0.0265 311  GLU   D CA  
10444 C  C   . GLU   D 242 ? 1.0117 0.9532 0.9410 0.0397  -0.0566 -0.0311 311  GLU   D C   
10445 O  O   . GLU   D 242 ? 1.0187 0.9545 0.9420 0.0465  -0.0598 -0.0334 311  GLU   D O   
10446 C  CB  . GLU   D 242 ? 1.0233 0.9516 0.9420 0.0328  -0.0497 -0.0258 311  GLU   D CB  
10447 C  CG  . GLU   D 242 ? 1.0303 0.9510 0.9432 0.0293  -0.0449 -0.0216 311  GLU   D CG  
10448 C  CD  . GLU   D 242 ? 1.0309 0.9503 0.9448 0.0237  -0.0432 -0.0208 311  GLU   D CD  
10449 O  OE1 . GLU   D 242 ? 1.0248 0.9502 0.9443 0.0225  -0.0455 -0.0234 311  GLU   D OE1 
10450 O  OE2 . GLU   D 242 ? 1.0380 0.9500 0.9472 0.0207  -0.0394 -0.0176 311  GLU   D OE2 
10451 N  N   . LEU   D 243 ? 1.0005 0.9529 0.9409 0.0359  -0.0573 -0.0324 312  LEU   D N   
10452 C  CA  . LEU   D 243 ? 0.9952 0.9543 0.9424 0.0395  -0.0614 -0.0365 312  LEU   D CA  
10453 C  C   . LEU   D 243 ? 1.0477 1.0106 0.9981 0.0434  -0.0641 -0.0375 312  LEU   D C   
10454 O  O   . LEU   D 243 ? 1.1192 1.0835 1.0718 0.0487  -0.0683 -0.0411 312  LEU   D O   
10455 C  CB  . LEU   D 243 ? 0.9844 0.9540 0.9424 0.0343  -0.0607 -0.0372 312  LEU   D CB  
10456 C  CG  . LEU   D 243 ? 0.9909 0.9651 0.9546 0.0368  -0.0633 -0.0412 312  LEU   D CG  
10457 C  CD1 . LEU   D 243 ? 1.0103 0.9749 0.9653 0.0426  -0.0654 -0.0434 312  LEU   D CD1 
10458 C  CD2 . LEU   D 243 ? 1.0611 1.0404 1.0300 0.0310  -0.0610 -0.0407 312  LEU   D CD2 
10459 N  N   . ASP   D 244 ? 1.0496 1.0140 1.0003 0.0410  -0.0619 -0.0344 313  ASP   D N   
10460 C  CA  . ASP   D 244 ? 1.0397 1.0063 0.9919 0.0450  -0.0645 -0.0353 313  ASP   D CA  
10461 C  C   . ASP   D 244 ? 1.0443 0.9984 0.9835 0.0518  -0.0660 -0.0355 313  ASP   D C   
10462 O  O   . ASP   D 244 ? 1.0283 0.9819 0.9671 0.0576  -0.0704 -0.0382 313  ASP   D O   
10463 C  CB  . ASP   D 244 ? 1.0476 1.0199 1.0044 0.0404  -0.0616 -0.0320 313  ASP   D CB  
10464 C  CG  . ASP   D 244 ? 1.0864 1.0685 1.0529 0.0414  -0.0646 -0.0338 313  ASP   D CG  
10465 O  OD1 . ASP   D 244 ? 1.1147 1.1029 1.0887 0.0426  -0.0678 -0.0373 313  ASP   D OD1 
10466 O  OD2 . ASP   D 244 ? 1.0812 1.0650 1.0482 0.0410  -0.0636 -0.0318 313  ASP   D OD2 
10467 N  N   . ILE   D 245 ? 1.0633 1.0067 0.9916 0.0513  -0.0626 -0.0328 314  ILE   D N   
10468 C  CA  . ILE   D 245 ? 1.0433 0.9733 0.9576 0.0580  -0.0635 -0.0328 314  ILE   D CA  
10469 C  C   . ILE   D 245 ? 1.0653 0.9927 0.9779 0.0644  -0.0692 -0.0375 314  ILE   D C   
10470 O  O   . ILE   D 245 ? 1.0901 1.0159 1.0009 0.0705  -0.0736 -0.0400 314  ILE   D O   
10471 C  CB  . ILE   D 245 ? 1.0364 0.9555 0.9403 0.0556  -0.0583 -0.0291 314  ILE   D CB  
10472 C  CG1 . ILE   D 245 ? 1.0352 0.9547 0.9390 0.0518  -0.0534 -0.0247 314  ILE   D CG1 
10473 C  CG2 . ILE   D 245 ? 1.0754 0.9796 0.9643 0.0626  -0.0596 -0.0299 314  ILE   D CG2 
10474 C  CD1 . ILE   D 245 ? 1.0356 0.9535 0.9396 0.0452  -0.0480 -0.0210 314  ILE   D CD1 
10475 N  N   . MET   D 246 ? 1.0544 0.9823 0.9689 0.0630  -0.0694 -0.0391 315  MET   D N   
10476 C  CA  . MET   D 246 ? 1.0736 0.9992 0.9870 0.0692  -0.0745 -0.0436 315  MET   D CA  
10477 C  C   . MET   D 246 ? 1.1014 1.0375 1.0265 0.0718  -0.0796 -0.0473 315  MET   D C   
10478 O  O   . MET   D 246 ? 1.1766 1.1093 1.0996 0.0787  -0.0848 -0.0509 315  MET   D O   
10479 C  CB  . MET   D 246 ? 1.0385 0.9651 0.9542 0.0665  -0.0735 -0.0446 315  MET   D CB  
10480 C  CG  . MET   D 246 ? 1.0382 0.9584 0.9471 0.0615  -0.0682 -0.0409 315  MET   D CG  
10481 S  SD  . MET   D 246 ? 1.0626 0.9866 0.9769 0.0584  -0.0679 -0.0428 315  MET   D SD  
10482 C  CE  . MET   D 246 ? 1.1550 1.0624 1.0533 0.0634  -0.0682 -0.0433 315  MET   D CE  
10483 N  N   . ASN   D 247 ? 1.0790 1.0277 1.0169 0.0664  -0.0783 -0.0468 316  ASN   D N   
10484 C  CA  . ASN   D 247 ? 1.1021 1.0609 1.0521 0.0684  -0.0827 -0.0503 316  ASN   D CA  
10485 C  C   . ASN   D 247 ? 1.1132 1.0704 1.0609 0.0725  -0.0857 -0.0505 316  ASN   D C   
10486 O  O   . ASN   D 247 ? 1.0842 1.0457 1.0386 0.0767  -0.0910 -0.0542 316  ASN   D O   
10487 C  CB  . ASN   D 247 ? 1.1768 1.1492 1.1409 0.0614  -0.0802 -0.0496 316  ASN   D CB  
10488 C  CG  . ASN   D 247 ? 1.1835 1.1597 1.1532 0.0595  -0.0794 -0.0514 316  ASN   D CG  
10489 O  OD1 . ASN   D 247 ? 1.1387 1.1075 1.1004 0.0592  -0.0776 -0.0506 316  ASN   D OD1 
10490 N  ND2 . ASN   D 247 ? 1.2949 1.2824 1.2781 0.0581  -0.0806 -0.0536 316  ASN   D ND2 
10491 N  N   . LYS   D 248 ? 1.1204 1.0714 1.0592 0.0715  -0.0824 -0.0467 317  LYS   D N   
10492 C  CA  . LYS   D 248 ? 1.0855 1.0353 1.0221 0.0746  -0.0844 -0.0463 317  LYS   D CA  
10493 C  C   . LYS   D 248 ? 1.1217 1.0562 1.0412 0.0810  -0.0851 -0.0455 317  LYS   D C   
10494 O  O   . LYS   D 248 ? 1.1326 1.0644 1.0494 0.0864  -0.0893 -0.0472 317  LYS   D O   
10495 C  CB  . LYS   D 248 ? 1.1144 1.0710 1.0561 0.0680  -0.0795 -0.0424 317  LYS   D CB  
10496 C  CG  . LYS   D 248 ? 1.0744 1.0464 1.0328 0.0634  -0.0803 -0.0436 317  LYS   D CG  
10497 C  CD  . LYS   D 248 ? 1.1590 1.1353 1.1199 0.0599  -0.0775 -0.0403 317  LYS   D CD  
10498 C  CE  . LYS   D 248 ? 1.1919 1.1825 1.1681 0.0541  -0.0768 -0.0405 317  LYS   D CE  
10499 N  NZ  . LYS   D 248 ? 1.1232 1.1177 1.1020 0.0466  -0.0711 -0.0368 317  LYS   D NZ  
10500 N  N   . CYS   D 249 ? 1.1901 1.1139 1.0978 0.0807  -0.0811 -0.0428 318  CYS   D N   
10501 C  CA  . CYS   D 249 ? 1.1457 1.0534 1.0358 0.0871  -0.0813 -0.0419 318  CYS   D CA  
10502 C  C   . CYS   D 249 ? 1.1085 1.0091 0.9930 0.0934  -0.0864 -0.0458 318  CYS   D C   
10503 O  O   . CYS   D 249 ? 1.1494 1.0419 1.0258 0.0935  -0.0841 -0.0449 318  CYS   D O   
10504 C  CB  . CYS   D 249 ? 1.0974 0.9968 0.9779 0.0833  -0.0739 -0.0368 318  CYS   D CB  
10505 S  SG  . CYS   D 249 ? 1.1188 1.0256 1.0055 0.0763  -0.0679 -0.0321 318  CYS   D SG  
10506 N  N   . THR   D 250 ? 1.1085 1.0121 0.9974 0.0990  -0.0934 -0.0503 319  THR   D N   
10507 C  CA  . THR   D 250 ? 1.1668 1.0671 1.0548 0.1047  -0.0992 -0.0548 319  THR   D CA  
10508 C  C   . THR   D 250 ? 1.2115 1.0960 1.0828 0.1139  -0.1034 -0.0562 319  THR   D C   
10509 O  O   . THR   D 250 ? 1.2303 1.1104 1.0992 0.1196  -0.1086 -0.0600 319  THR   D O   
10510 C  CB  . THR   D 250 ? 1.1811 1.0953 1.0866 0.1049  -0.1047 -0.0593 319  THR   D CB  
10511 O  OG1 . THR   D 250 ? 1.1638 1.0803 1.0717 0.1076  -0.1084 -0.0603 319  THR   D OG1 
10512 C  CG2 . THR   D 250 ? 1.1523 1.0805 1.0726 0.0962  -0.1002 -0.0580 319  THR   D CG2 
10513 N  N   . SER   D 251 ? 1.2241 1.0995 1.0833 0.1156  -0.1008 -0.0530 320  SER   D N   
10514 C  CA  . SER   D 251 ? 1.2612 1.1205 1.1029 0.1245  -0.1043 -0.0538 320  SER   D CA  
10515 C  C   . SER   D 251 ? 1.2658 1.1115 1.0908 0.1236  -0.0968 -0.0485 320  SER   D C   
10516 O  O   . SER   D 251 ? 1.2430 1.0923 1.0702 0.1178  -0.0904 -0.0442 320  SER   D O   
10517 C  CB  . SER   D 251 ? 1.3050 1.1667 1.1489 0.1283  -0.1093 -0.0557 320  SER   D CB  
10518 O  OG  . SER   D 251 ? 1.3714 1.2171 1.1976 0.1374  -0.1131 -0.0566 320  SER   D OG  
10519 N  N   . LEU   D 252 ? 1.2919 1.1220 1.1007 0.1294  -0.0975 -0.0486 321  LEU   D N   
10520 C  CA  . LEU   D 252 ? 1.3274 1.1432 1.1198 0.1290  -0.0901 -0.0436 321  LEU   D CA  
10521 C  C   . LEU   D 252 ? 1.3349 1.1345 1.1086 0.1377  -0.0919 -0.0432 321  LEU   D C   
10522 O  O   . LEU   D 252 ? 1.3341 1.1258 1.1001 0.1462  -0.0993 -0.0473 321  LEU   D O   
10523 C  CB  . LEU   D 252 ? 1.2838 1.0927 1.0704 0.1286  -0.0883 -0.0434 321  LEU   D CB  
10524 C  CG  . LEU   D 252 ? 1.1975 1.0189 0.9986 0.1194  -0.0844 -0.0424 321  LEU   D CG  
10525 C  CD1 . LEU   D 252 ? 1.1803 0.9943 0.9754 0.1211  -0.0850 -0.0437 321  LEU   D CD1 
10526 C  CD2 . LEU   D 252 ? 1.2161 1.0399 1.0190 0.1112  -0.0754 -0.0367 321  LEU   D CD2 
10527 N  N   . CYS   D 253 ? 1.3450 1.1393 1.1113 0.1358  -0.0851 -0.0383 322  CYS   D N   
10528 C  CA  . CYS   D 253 ? 1.3710 1.1515 1.1209 0.1432  -0.0858 -0.0374 322  CYS   D CA  
10529 C  C   . CYS   D 253 ? 1.3860 1.1493 1.1173 0.1442  -0.0775 -0.0322 322  CYS   D C   
10530 O  O   . CYS   D 253 ? 1.4161 1.1803 1.1497 0.1376  -0.0704 -0.0286 322  CYS   D O   
10531 C  CB  . CYS   D 253 ? 1.3805 1.1709 1.1392 0.1405  -0.0851 -0.0364 322  CYS   D CB  
10532 S  SG  . CYS   D 253 ? 1.3539 1.1616 1.1319 0.1409  -0.0951 -0.0426 322  CYS   D SG  
10533 N  N   . CYS   D 254 ? 1.4044 1.1515 1.1169 0.1525  -0.0784 -0.0316 323  CYS   D N   
10534 C  CA  . CYS   D 254 ? 1.4254 1.1551 1.1192 0.1540  -0.0699 -0.0263 323  CYS   D CA  
10535 C  C   . CYS   D 254 ? 1.4555 1.1921 1.1564 0.1460  -0.0602 -0.0207 323  CYS   D C   
10536 O  O   . CYS   D 254 ? 1.4774 1.2227 1.1860 0.1449  -0.0610 -0.0208 323  CYS   D O   
10537 C  CB  . CYS   D 254 ? 1.4213 1.1322 1.0933 0.1653  -0.0733 -0.0273 323  CYS   D CB  
10538 S  SG  . CYS   D 254 ? 1.6317 1.3189 1.2784 0.1686  -0.0629 -0.0209 323  CYS   D SG  
10539 N  N   . LYS   D 255 ? 1.4613 1.1940 1.1603 0.1404  -0.0512 -0.0160 324  LYS   D N   
10540 C  CA  . LYS   D 255 ? 1.4605 1.2010 1.1685 0.1323  -0.0422 -0.0108 324  LYS   D CA  
10541 C  C   . LYS   D 255 ? 1.5151 1.2443 1.2095 0.1369  -0.0374 -0.0073 324  LYS   D C   
10542 O  O   . LYS   D 255 ? 1.4450 1.1835 1.1489 0.1323  -0.0332 -0.0047 324  LYS   D O   
10543 C  CB  . LYS   D 255 ? 1.4532 1.1918 1.1629 0.1252  -0.0342 -0.0068 324  LYS   D CB  
10544 C  CG  . LYS   D 255 ? 1.4420 1.1959 1.1696 0.1145  -0.0276 -0.0032 324  LYS   D CG  
10545 C  CD  . LYS   D 255 ? 1.4291 1.1794 1.1574 0.1079  -0.0196 0.0009  324  LYS   D CD  
10546 C  CE  . LYS   D 255 ? 1.5445 1.2764 1.2553 0.1111  -0.0110 0.0061  324  LYS   D CE  
10547 N  NZ  . LYS   D 255 ? 1.5990 1.3250 1.3087 0.1057  -0.0040 0.0096  324  LYS   D NZ  
10548 N  N   . GLN   D 256 ? 1.6637 1.3726 1.3357 0.1463  -0.0381 -0.0073 325  GLN   D N   
10549 C  CA  . GLN   D 256 ? 1.6724 1.3664 1.3276 0.1513  -0.0319 -0.0033 325  GLN   D CA  
10550 C  C   . GLN   D 256 ? 1.6304 1.3272 1.2849 0.1564  -0.0375 -0.0057 325  GLN   D C   
10551 O  O   . GLN   D 256 ? 1.6336 1.3290 1.2857 0.1560  -0.0315 -0.0021 325  GLN   D O   
10552 C  CB  . GLN   D 256 ? 1.6754 1.3454 1.3054 0.1599  -0.0310 -0.0026 325  GLN   D CB  
10553 C  CG  . GLN   D 256 ? 1.7239 1.3877 1.3514 0.1549  -0.0228 0.0014  325  GLN   D CG  
10554 C  CD  . GLN   D 256 ? 1.8018 1.4638 1.4298 0.1495  -0.0103 0.0082  325  GLN   D CD  
10555 O  OE1 . GLN   D 256 ? 1.8859 1.5528 1.5232 0.1411  -0.0034 0.0116  325  GLN   D OE1 
10556 N  NE2 . GLN   D 256 ? 1.8291 1.4841 1.4474 0.1543  -0.0075 0.0102  325  GLN   D NE2 
10557 N  N   . CYS   D 257 ? 1.5487 1.2493 1.2057 0.1614  -0.0490 -0.0119 326  CYS   D N   
10558 C  CA  . CYS   D 257 ? 1.4651 1.1672 1.1208 0.1669  -0.0554 -0.0149 326  CYS   D CA  
10559 C  C   . CYS   D 257 ? 1.5424 1.2671 1.2220 0.1616  -0.0621 -0.0188 326  CYS   D C   
10560 O  O   . CYS   D 257 ? 1.6135 1.3421 1.2955 0.1638  -0.0655 -0.0201 326  CYS   D O   
10561 C  CB  . CYS   D 257 ? 1.4920 1.1767 1.1281 0.1789  -0.0640 -0.0190 326  CYS   D CB  
10562 S  SG  . CYS   D 257 ? 1.4309 1.1241 1.0773 0.1814  -0.0776 -0.0270 326  CYS   D SG  
10563 N  N   . GLN   D 258 ? 1.5482 1.2871 1.2450 0.1547  -0.0638 -0.0206 327  GLN   D N   
10564 C  CA  . GLN   D 258 ? 1.4863 1.2471 1.2066 0.1487  -0.0689 -0.0238 327  GLN   D CA  
10565 C  C   . GLN   D 258 ? 1.4963 1.2593 1.2181 0.1553  -0.0798 -0.0295 327  GLN   D C   
10566 O  O   . GLN   D 258 ? 1.5373 1.3130 1.2719 0.1525  -0.0819 -0.0305 327  GLN   D O   
10567 C  CB  . GLN   D 258 ? 1.4686 1.2423 1.2022 0.1403  -0.0617 -0.0197 327  GLN   D CB  
10568 C  CG  . GLN   D 258 ? 1.5434 1.3170 1.2786 0.1329  -0.0512 -0.0141 327  GLN   D CG  
10569 C  CD  . GLN   D 258 ? 1.6328 1.4177 1.3797 0.1262  -0.0450 -0.0104 327  GLN   D CD  
10570 O  OE1 . GLN   D 258 ? 1.6341 1.4273 1.3880 0.1269  -0.0491 -0.0123 327  GLN   D OE1 
10571 N  NE2 . GLN   D 258 ? 1.7162 1.5014 1.4655 0.1197  -0.0355 -0.0052 327  GLN   D NE2 
10572 N  N   . GLU   D 259 ? 1.5479 1.2991 1.2576 0.1639  -0.0872 -0.0335 328  GLU   D N   
10573 C  CA  . GLU   D 259 ? 1.5516 1.3031 1.2614 0.1709  -0.0979 -0.0390 328  GLU   D CA  
10574 C  C   . GLU   D 259 ? 1.5787 1.3299 1.2906 0.1752  -0.1072 -0.0447 328  GLU   D C   
10575 O  O   . GLU   D 259 ? 1.6422 1.4025 1.3655 0.1771  -0.1165 -0.0500 328  GLU   D O   
10576 C  CB  . GLU   D 259 ? 1.5775 1.3097 1.2644 0.1802  -0.0982 -0.0379 328  GLU   D CB  
10577 N  N   . THR   D 260 ? 1.7093 1.4498 1.4104 0.1770  -0.1049 -0.0437 329  THR   D N   
10578 C  CA  . THR   D 260 ? 1.7115 1.4511 1.4142 0.1812  -0.1133 -0.0490 329  THR   D CA  
10579 C  C   . THR   D 260 ? 1.6821 1.4377 1.4039 0.1723  -0.1110 -0.0491 329  THR   D C   
10580 O  O   . THR   D 260 ? 1.6847 1.4409 1.4067 0.1658  -0.1019 -0.0445 329  THR   D O   
10581 C  CB  . THR   D 260 ? 1.7530 1.4698 1.4310 0.1895  -0.1132 -0.0483 329  THR   D CB  
10582 O  OG1 . THR   D 260 ? 1.8218 1.5316 1.4914 0.1849  -0.1016 -0.0420 329  THR   D OG1 
10583 C  CG2 . THR   D 260 ? 1.7706 1.4726 1.4309 0.1989  -0.1172 -0.0492 329  THR   D CG2 
10584 N  N   . GLU   D 261 ? 1.5429 1.3113 1.2808 0.1723  -0.1192 -0.0546 330  GLU   D N   
10585 C  CA  . GLU   D 261 ? 1.4478 1.2294 1.2021 0.1660  -0.1187 -0.0558 330  GLU   D CA  
10586 C  C   . GLU   D 261 ? 1.4462 1.2152 1.1883 0.1708  -0.1203 -0.0571 330  GLU   D C   
10587 O  O   . GLU   D 261 ? 1.4461 1.2068 1.1809 0.1796  -0.1289 -0.0616 330  GLU   D O   
10588 C  CB  . GLU   D 261 ? 1.4856 1.2839 1.2605 0.1653  -0.1270 -0.0613 330  GLU   D CB  
10589 C  CG  . GLU   D 261 ? 1.5185 1.3280 1.3084 0.1618  -0.1290 -0.0642 330  GLU   D CG  
10590 C  CD  . GLU   D 261 ? 1.5407 1.3661 1.3511 0.1616  -0.1369 -0.0696 330  GLU   D CD  
10591 O  OE1 . GLU   D 261 ? 1.5090 1.3303 1.3171 0.1692  -0.1458 -0.0740 330  GLU   D OE1 
10592 O  OE2 . GLU   D 261 ? 1.5525 1.3942 1.3815 0.1537  -0.1342 -0.0694 330  GLU   D OE2 
10593 N  N   . ILE   D 262 ? 1.4180 1.1852 1.1580 0.1653  -0.1124 -0.0532 331  ILE   D N   
10594 C  CA  . ILE   D 262 ? 1.4056 1.1602 1.1333 0.1696  -0.1131 -0.0540 331  ILE   D CA  
10595 C  C   . ILE   D 262 ? 1.3912 1.1578 1.1347 0.1682  -0.1186 -0.0587 331  ILE   D C   
10596 O  O   . ILE   D 262 ? 1.4508 1.2117 1.1901 0.1758  -0.1266 -0.0634 331  ILE   D O   
10597 C  CB  . ILE   D 262 ? 1.3709 1.1165 1.0881 0.1648  -0.1023 -0.0478 331  ILE   D CB  
10598 C  CG1 . ILE   D 262 ? 1.3507 1.0877 1.0563 0.1653  -0.0963 -0.0431 331  ILE   D CG1 
10599 C  CG2 . ILE   D 262 ? 1.3758 1.1038 1.0753 0.1711  -0.1032 -0.0483 331  ILE   D CG2 
10600 C  CD1 . ILE   D 262 ? 1.3730 1.0899 1.0561 0.1761  -0.0997 -0.0438 331  ILE   D CD1 
10601 N  N   . THR   D 263 ? 1.3430 1.1263 1.1049 0.1588  -0.1146 -0.0576 332  THR   D N   
10602 C  CA  . THR   D 263 ? 1.3362 1.1308 1.1130 0.1573  -0.1188 -0.0617 332  THR   D CA  
10603 C  C   . THR   D 263 ? 1.3530 1.1687 1.1526 0.1486  -0.1170 -0.0616 332  THR   D C   
10604 O  O   . THR   D 263 ? 1.3238 1.1448 1.1272 0.1448  -0.1139 -0.0591 332  THR   D O   
10605 C  CB  . THR   D 263 ? 1.3361 1.1228 1.1051 0.1560  -0.1146 -0.0600 332  THR   D CB  
10606 O  OG1 . THR   D 263 ? 1.3247 1.1190 1.1047 0.1570  -0.1197 -0.0646 332  THR   D OG1 
10607 C  CG2 . THR   D 263 ? 1.3292 1.1208 1.1022 0.1460  -0.1046 -0.0546 332  THR   D CG2 
10608 N  N   . THR   D 264 ? 1.3731 1.2004 1.1875 0.1455  -0.1187 -0.0644 333  THR   D N   
10609 C  CA  . THR   D 264 ? 1.3254 1.1722 1.1613 0.1383  -0.1179 -0.0651 333  THR   D CA  
10610 C  C   . THR   D 264 ? 1.3223 1.1759 1.1667 0.1327  -0.1144 -0.0649 333  THR   D C   
10611 O  O   . THR   D 264 ? 1.3614 1.2069 1.1984 0.1361  -0.1155 -0.0662 333  THR   D O   
10612 C  CB  . THR   D 264 ? 1.3130 1.1686 1.1614 0.1426  -0.1266 -0.0705 333  THR   D CB  
10613 O  OG1 . THR   D 264 ? 1.3791 1.2532 1.2484 0.1354  -0.1252 -0.0710 333  THR   D OG1 
10614 C  CG2 . THR   D 264 ? 1.3221 1.1736 1.1696 0.1497  -0.1337 -0.0755 333  THR   D CG2 
10615 N  N   . LYS   D 265 ? 1.3335 1.2019 1.1932 0.1242  -0.1103 -0.0633 334  LYS   D N   
10616 C  CA  . LYS   D 265 ? 1.3632 1.2375 1.2296 0.1179  -0.1056 -0.0622 334  LYS   D CA  
10617 C  C   . LYS   D 265 ? 1.3978 1.2720 1.2672 0.1221  -0.1102 -0.0666 334  LYS   D C   
10618 O  O   . LYS   D 265 ? 1.3386 1.2054 1.2003 0.1220  -0.1077 -0.0658 334  LYS   D O   
10619 C  CB  . LYS   D 265 ? 1.2723 1.1635 1.1563 0.1096  -0.1026 -0.0611 334  LYS   D CB  
10620 N  N   . ASN   D 266 ? 1.5042 1.3865 1.3852 0.1261  -0.1170 -0.0714 335  ASN   D N   
10621 C  CA  . ASN   D 266 ? 1.5150 1.4011 1.4037 0.1291  -0.1209 -0.0757 335  ASN   D CA  
10622 C  C   . ASN   D 266 ? 1.5380 1.4085 1.4109 0.1367  -0.1239 -0.0772 335  ASN   D C   
10623 O  O   . ASN   D 266 ? 1.5900 1.4618 1.4670 0.1387  -0.1258 -0.0801 335  ASN   D O   
10624 C  CB  . ASN   D 266 ? 1.5097 1.4071 1.4143 0.1322  -0.1277 -0.0805 335  ASN   D CB  
10625 C  CG  . ASN   D 266 ? 1.5661 1.4559 1.4629 0.1392  -0.1339 -0.0822 335  ASN   D CG  
10626 O  OD1 . ASN   D 266 ? 1.6065 1.4821 1.4884 0.1466  -0.1377 -0.0834 335  ASN   D OD1 
10627 N  ND2 . ASN   D 266 ? 1.6262 1.5241 1.5315 0.1369  -0.1347 -0.0819 335  ASN   D ND2 
10628 N  N   . GLU   D 267 ? 1.4173 1.2727 1.2720 0.1412  -0.1243 -0.0754 336  GLU   D N   
10629 C  CA  . GLU   D 267 ? 1.3888 1.2277 1.2263 0.1479  -0.1262 -0.0761 336  GLU   D CA  
10630 C  C   . GLU   D 267 ? 1.3454 1.1759 1.1719 0.1432  -0.1184 -0.0716 336  GLU   D C   
10631 O  O   . GLU   D 267 ? 1.3471 1.1636 1.1591 0.1481  -0.1191 -0.0718 336  GLU   D O   
10632 C  CB  . GLU   D 267 ? 1.3678 1.1921 1.1887 0.1558  -0.1303 -0.0763 336  GLU   D CB  
10633 C  CG  . GLU   D 267 ? 1.3623 1.1922 1.1904 0.1597  -0.1370 -0.0794 336  GLU   D CG  
10634 C  CD  . GLU   D 267 ? 1.4171 1.2523 1.2557 0.1661  -0.1464 -0.0859 336  GLU   D CD  
10635 O  OE1 . GLU   D 267 ? 1.3568 1.1900 1.1956 0.1687  -0.1481 -0.0882 336  GLU   D OE1 
10636 O  OE2 . GLU   D 267 ? 1.4679 1.3094 1.3152 0.1687  -0.1523 -0.0888 336  GLU   D OE2 
10637 N  N   . ILE   D 268 ? 1.3115 1.1495 1.1441 0.1341  -0.1113 -0.0676 337  ILE   D N   
10638 C  CA  . ILE   D 268 ? 1.3066 1.1364 1.1293 0.1296  -0.1043 -0.0634 337  ILE   D CA  
10639 C  C   . ILE   D 268 ? 1.3131 1.1439 1.1390 0.1297  -0.1049 -0.0658 337  ILE   D C   
10640 O  O   . ILE   D 268 ? 1.3077 1.1521 1.1496 0.1277  -0.1067 -0.0686 337  ILE   D O   
10641 C  CB  . ILE   D 268 ? 1.2571 1.0954 1.0869 0.1198  -0.0973 -0.0589 337  ILE   D CB  
10642 C  CG1 . ILE   D 268 ? 1.2166 1.0525 1.0419 0.1205  -0.0965 -0.0566 337  ILE   D CG1 
10643 C  CG2 . ILE   D 268 ? 1.2217 1.0520 1.0428 0.1149  -0.0906 -0.0550 337  ILE   D CG2 
10644 C  CD1 . ILE   D 268 ? 1.1698 1.0119 1.0000 0.1118  -0.0896 -0.0520 337  ILE   D CD1 
10645 N  N   . PHE   D 269 ? 1.3070 1.1230 1.1173 0.1321  -0.1032 -0.0645 338  PHE   D N   
10646 C  CA  . PHE   D 269 ? 1.2940 1.1082 1.1044 0.1334  -0.1040 -0.0667 338  PHE   D CA  
10647 C  C   . PHE   D 269 ? 1.3326 1.1321 1.1271 0.1316  -0.0986 -0.0630 338  PHE   D C   
10648 O  O   . PHE   D 269 ? 1.3567 1.1440 1.1372 0.1323  -0.0957 -0.0596 338  PHE   D O   
10649 C  CB  . PHE   D 269 ? 1.2742 1.0845 1.0828 0.1433  -0.1121 -0.0721 338  PHE   D CB  
10650 C  CG  . PHE   D 269 ? 1.3416 1.1317 1.1288 0.1507  -0.1138 -0.0718 338  PHE   D CG  
10651 C  CD1 . PHE   D 269 ? 1.3986 1.1771 1.1718 0.1548  -0.1145 -0.0700 338  PHE   D CD1 
10652 C  CD2 . PHE   D 269 ? 1.3768 1.1591 1.1575 0.1541  -0.1148 -0.0736 338  PHE   D CD2 
10653 C  CE1 . PHE   D 269 ? 1.4093 1.1683 1.1620 0.1621  -0.1159 -0.0698 338  PHE   D CE1 
10654 C  CE2 . PHE   D 269 ? 1.4116 1.1751 1.1724 0.1611  -0.1165 -0.0734 338  PHE   D CE2 
10655 C  CZ  . PHE   D 269 ? 1.4229 1.1745 1.1695 0.1651  -0.1169 -0.0715 338  PHE   D CZ  
10656 N  N   . SER   D 270 ? 1.3725 1.1724 1.1688 0.1297  -0.0974 -0.0640 339  SER   D N   
10657 C  CA  . SER   D 270 ? 1.4578 1.2450 1.2411 0.1270  -0.0923 -0.0607 339  SER   D CA  
10658 C  C   . SER   D 270 ? 1.5373 1.3123 1.3094 0.1349  -0.0961 -0.0636 339  SER   D C   
10659 O  O   . SER   D 270 ? 1.5784 1.3589 1.3578 0.1364  -0.0987 -0.0670 339  SER   D O   
10660 C  CB  . SER   D 270 ? 1.5459 1.3423 1.3392 0.1180  -0.0873 -0.0590 339  SER   D CB  
10661 O  OG  . SER   D 270 ? 1.5295 1.3355 1.3314 0.1107  -0.0835 -0.0559 339  SER   D OG  
10662 N  N   . LEU   D 271 ? 1.5983 1.3563 1.3523 0.1402  -0.0963 -0.0621 340  LEU   D N   
10663 C  CA  . LEU   D 271 ? 1.6647 1.4087 1.4054 0.1476  -0.0994 -0.0643 340  LEU   D CA  
10664 C  C   . LEU   D 271 ? 1.7603 1.4995 1.4973 0.1426  -0.0945 -0.0624 340  LEU   D C   
10665 O  O   . LEU   D 271 ? 1.7711 1.5122 1.5115 0.1447  -0.0969 -0.0656 340  LEU   D O   
10666 C  CB  . LEU   D 271 ? 1.5938 1.3196 1.3146 0.1540  -0.1000 -0.0626 340  LEU   D CB  
10667 C  CG  . LEU   D 271 ? 1.6316 1.3433 1.3390 0.1633  -0.1048 -0.0656 340  LEU   D CG  
10668 C  CD1 . LEU   D 271 ? 1.5937 1.3114 1.3079 0.1716  -0.1140 -0.0713 340  LEU   D CD1 
10669 C  CD2 . LEU   D 271 ? 1.6347 1.3249 1.3190 0.1669  -0.1019 -0.0621 340  LEU   D CD2 
10670 N  N   . SER   D 272 ? 2.1566 1.8898 1.8871 0.1361  -0.0876 -0.0573 341  SER   D N   
10671 C  CA  . SER   D 272 ? 2.1888 1.9174 1.9162 0.1305  -0.0828 -0.0552 341  SER   D CA  
10672 C  C   . SER   D 272 ? 2.1911 1.9369 1.9366 0.1226  -0.0811 -0.0557 341  SER   D C   
10673 O  O   . SER   D 272 ? 2.1984 1.9592 1.9582 0.1201  -0.0822 -0.0565 341  SER   D O   
10674 C  CB  . SER   D 272 ? 2.2318 1.9479 1.9470 0.1263  -0.0761 -0.0496 341  SER   D CB  
10675 O  OG  . SER   D 272 ? 2.3000 2.0136 2.0149 0.1194  -0.0714 -0.0474 341  SER   D OG  
10676 N  N   . LEU   D 273 ? 2.0521 1.7951 1.7963 0.1188  -0.0785 -0.0552 342  LEU   D N   
10677 C  CA  . LEU   D 273 ? 2.0439 1.8001 1.8020 0.1102  -0.0756 -0.0545 342  LEU   D CA  
10678 C  C   . LEU   D 273 ? 2.0486 1.8079 1.8097 0.1020  -0.0703 -0.0497 342  LEU   D C   
10679 O  O   . LEU   D 273 ? 2.0015 1.7745 1.7762 0.0954  -0.0687 -0.0492 342  LEU   D O   
10680 C  CB  . LEU   D 273 ? 2.0539 1.8037 1.8073 0.1082  -0.0740 -0.0548 342  LEU   D CB  
10681 C  CG  . LEU   D 273 ? 2.0773 1.8080 1.8130 0.1081  -0.0706 -0.0516 342  LEU   D CG  
10682 C  CD1 . LEU   D 273 ? 2.0986 1.8289 1.8357 0.0982  -0.0644 -0.0469 342  LEU   D CD1 
10683 C  CD2 . LEU   D 273 ? 2.0298 1.7501 1.7563 0.1127  -0.0725 -0.0541 342  LEU   D CD2 
10684 N  N   . CYS   D 274 ? 2.0655 1.8123 1.8142 0.1027  -0.0674 -0.0462 343  CYS   D N   
10685 C  CA  . CYS   D 274 ? 2.0407 1.7876 1.7906 0.0947  -0.0614 -0.0413 343  CYS   D CA  
10686 C  C   . CYS   D 274 ? 1.9669 1.7292 1.7305 0.0913  -0.0613 -0.0407 343  CYS   D C   
10687 O  O   . CYS   D 274 ? 1.9684 1.7373 1.7397 0.0833  -0.0572 -0.0376 343  CYS   D O   
10688 C  CB  . CYS   D 274 ? 2.0734 1.8027 1.8065 0.0972  -0.0580 -0.0377 343  CYS   D CB  
10689 S  SG  . CYS   D 274 ? 2.2226 1.9323 1.9393 0.0977  -0.0554 -0.0364 343  CYS   D SG  
10690 N  N   . GLY   D 275 ? 1.8591 1.6270 1.6261 0.0974  -0.0660 -0.0435 344  GLY   D N   
10691 C  CA  . GLY   D 275 ? 1.5784 1.3601 1.3578 0.0947  -0.0662 -0.0431 344  GLY   D CA  
10692 C  C   . GLY   D 275 ? 1.4501 1.2317 1.2275 0.1028  -0.0713 -0.0457 344  GLY   D C   
10693 O  O   . GLY   D 275 ? 1.5291 1.2996 1.2952 0.1108  -0.0748 -0.0478 344  GLY   D O   
10694 N  N   . PRO   D 276 ? 1.3805 1.1745 1.1691 0.1013  -0.0723 -0.0459 345  PRO   D N   
10695 C  CA  . PRO   D 276 ? 1.3644 1.1565 1.1495 0.1086  -0.0767 -0.0476 345  PRO   D CA  
10696 C  C   . PRO   D 276 ? 1.3176 1.0972 1.0892 0.1091  -0.0725 -0.0433 345  PRO   D C   
10697 O  O   . PRO   D 276 ? 1.3080 1.0736 1.0648 0.1166  -0.0744 -0.0436 345  PRO   D O   
10698 C  CB  . PRO   D 276 ? 1.2791 1.0896 1.0821 0.1056  -0.0787 -0.0492 345  PRO   D CB  
10699 C  CG  . PRO   D 276 ? 1.2951 1.1145 1.1076 0.0959  -0.0734 -0.0463 345  PRO   D CG  
10700 C  CD  . PRO   D 276 ? 1.4199 1.2301 1.2248 0.0932  -0.0701 -0.0449 345  PRO   D CD  
10701 N  N   . MET   D 277 ? 1.3033 1.0874 1.0797 0.1012  -0.0666 -0.0390 346  MET   D N   
10702 C  CA  . MET   D 277 ? 1.2386 1.0109 1.0035 0.0997  -0.0606 -0.0341 346  MET   D CA  
10703 C  C   . MET   D 277 ? 1.3144 1.0806 1.0760 0.0938  -0.0554 -0.0313 346  MET   D C   
10704 O  O   . MET   D 277 ? 1.3735 1.1505 1.1473 0.0865  -0.0539 -0.0311 346  MET   D O   
10705 C  CB  . MET   D 277 ? 1.1923 0.9743 0.9660 0.0951  -0.0577 -0.0314 346  MET   D CB  
10706 C  CG  . MET   D 277 ? 1.1920 0.9631 0.9551 0.0944  -0.0517 -0.0265 346  MET   D CG  
10707 S  SD  . MET   D 277 ? 1.1739 0.9611 0.9521 0.0888  -0.0498 -0.0246 346  MET   D SD  
10708 C  CE  . MET   D 277 ? 1.2244 1.0146 1.0094 0.0777  -0.0422 -0.0200 346  MET   D CE  
10709 N  N   . ALA   D 278 ? 1.3010 1.0495 1.0459 0.0973  -0.0531 -0.0296 347  ALA   D N   
10710 C  CA  . ALA   D 278 ? 1.2862 1.0263 1.0262 0.0920  -0.0478 -0.0265 347  ALA   D CA  
10711 C  C   . ALA   D 278 ? 1.3252 1.0488 1.0497 0.0940  -0.0424 -0.0222 347  ALA   D C   
10712 O  O   . ALA   D 278 ? 1.3918 1.1084 1.1067 0.1011  -0.0441 -0.0225 347  ALA   D O   
10713 C  CB  . ALA   D 278 ? 1.3856 1.1199 1.1206 0.0951  -0.0512 -0.0298 347  ALA   D CB  
10714 N  N   . ALA   D 279 ? 1.3234 1.0405 1.0454 0.0877  -0.0359 -0.0181 348  ALA   D N   
10715 C  CA  . ALA   D 279 ? 1.3637 1.0672 1.0740 0.0878  -0.0292 -0.0131 348  ALA   D CA  
10716 C  C   . ALA   D 279 ? 1.3928 1.0755 1.0839 0.0930  -0.0278 -0.0124 348  ALA   D C   
10717 O  O   . ALA   D 279 ? 1.4992 1.1762 1.1888 0.0885  -0.0248 -0.0109 348  ALA   D O   
10718 C  CB  . ALA   D 279 ? 1.4040 1.1132 1.1246 0.0774  -0.0224 -0.0087 348  ALA   D CB  
10719 N  N   . TYR   D 280 ? 1.2928 0.9635 0.9689 0.1023  -0.0299 -0.0132 349  TYR   D N   
10720 C  CA  . TYR   D 280 ? 1.3563 1.0064 1.0128 0.1083  -0.0291 -0.0127 349  TYR   D CA  
10721 C  C   . TYR   D 280 ? 1.4004 1.0346 1.0435 0.1081  -0.0206 -0.0069 349  TYR   D C   
10722 O  O   . TYR   D 280 ? 1.3867 1.0247 1.0333 0.1062  -0.0167 -0.0040 349  TYR   D O   
10723 C  CB  . TYR   D 280 ? 1.4243 1.0689 1.0707 0.1195  -0.0371 -0.0174 349  TYR   D CB  
10724 C  CG  . TYR   D 280 ? 1.3664 1.0269 1.0265 0.1207  -0.0454 -0.0232 349  TYR   D CG  
10725 C  CD1 . TYR   D 280 ? 1.4242 1.1031 1.1007 0.1182  -0.0481 -0.0248 349  TYR   D CD1 
10726 C  CD2 . TYR   D 280 ? 1.3669 1.0234 1.0232 0.1247  -0.0503 -0.0270 349  TYR   D CD2 
10727 C  CE1 . TYR   D 280 ? 1.4282 1.1217 1.1178 0.1193  -0.0552 -0.0300 349  TYR   D CE1 
10728 C  CE2 . TYR   D 280 ? 1.4192 1.0902 1.0885 0.1260  -0.0573 -0.0322 349  TYR   D CE2 
10729 C  CZ  . TYR   D 280 ? 1.4685 1.1579 1.1546 0.1231  -0.0596 -0.0336 349  TYR   D CZ  
10730 O  OH  . TYR   D 280 ? 1.5598 1.2637 1.2595 0.1242  -0.0659 -0.0386 349  TYR   D OH  
10731 N  N   . VAL   D 281 ? 1.4049 1.0208 1.0326 0.1102  -0.0176 -0.0052 350  VAL   D N   
10732 C  CA  . VAL   D 281 ? 1.4460 1.0453 1.0604 0.1099  -0.0087 0.0005  350  VAL   D CA  
10733 C  C   . VAL   D 281 ? 1.5508 1.1293 1.1415 0.1212  -0.0103 -0.0001 350  VAL   D C   
10734 O  O   . VAL   D 281 ? 1.5675 1.1370 1.1487 0.1260  -0.0146 -0.0029 350  VAL   D O   
10735 C  CB  . VAL   D 281 ? 1.4178 1.0120 1.0344 0.1015  -0.0022 0.0039  350  VAL   D CB  
10736 C  CG1 . VAL   D 281 ? 1.4116 0.9934 1.0204 0.0991  0.0081  0.0104  350  VAL   D CG1 
10737 C  CG2 . VAL   D 281 ? 1.4426 1.0567 1.0814 0.0917  -0.0032 0.0030  350  VAL   D CG2 
10738 N  N   . ASN   D 282 ? 1.5341 1.1042 1.1147 0.1254  -0.0065 0.0028  351  ASN   D N   
10739 C  CA  . ASN   D 282 ? 1.5511 1.0998 1.1075 0.1362  -0.0071 0.0030  351  ASN   D CA  
10740 C  C   . ASN   D 282 ? 1.6308 1.1593 1.1724 0.1349  0.0015  0.0078  351  ASN   D C   
10741 O  O   . ASN   D 282 ? 1.6182 1.1500 1.1692 0.1254  0.0087  0.0117  351  ASN   D O   
10742 C  CB  . ASN   D 282 ? 1.5534 1.1008 1.1047 0.1409  -0.0059 0.0045  351  ASN   D CB  
10743 C  CG  . ASN   D 282 ? 1.5606 1.0960 1.1036 0.1381  0.0059  0.0114  351  ASN   D CG  
10744 O  OD1 . ASN   D 282 ? 1.5998 1.1351 1.1491 0.1296  0.0136  0.0155  351  ASN   D OD1 
10745 N  ND2 . ASN   D 282 ? 1.5095 1.0354 1.0394 0.1453  0.0072  0.0128  351  ASN   D ND2 
10746 N  N   . PRO   D 283 ? 1.6855 1.1923 1.2036 0.1446  0.0008  0.0078  352  PRO   D N   
10747 C  CA  . PRO   D 283 ? 1.6460 1.1331 1.1498 0.1434  0.0084  0.0119  352  PRO   D CA  
10748 C  C   . PRO   D 283 ? 1.6050 1.0844 1.1060 0.1387  0.0205  0.0190  352  PRO   D C   
10749 O  O   . PRO   D 283 ? 1.6929 1.1528 1.1786 0.1394  0.0275  0.0228  352  PRO   D O   
10750 C  CB  . PRO   D 283 ? 1.6461 1.1127 1.1251 0.1561  0.0036  0.0096  352  PRO   D CB  
10751 C  CG  . PRO   D 283 ? 1.6823 1.1539 1.1597 0.1635  -0.0026 0.0067  352  PRO   D CG  
10752 C  CD  . PRO   D 283 ? 1.6833 1.1819 1.1865 0.1569  -0.0072 0.0037  352  PRO   D CD  
10753 N  N   . HIS   D 284 ? 1.5716 1.0653 1.0866 0.1338  0.0235  0.0208  353  HIS   D N   
10754 C  CA  . HIS   D 284 ? 1.5660 1.0540 1.0806 0.1289  0.0353  0.0275  353  HIS   D CA  
10755 C  C   . HIS   D 284 ? 1.5328 1.0414 1.0732 0.1164  0.0389  0.0293  353  HIS   D C   
10756 O  O   . HIS   D 284 ? 1.4977 1.0049 1.0418 0.1113  0.0486  0.0347  353  HIS   D O   
10757 C  CB  . HIS   D 284 ? 1.6517 1.1336 1.1550 0.1364  0.0369  0.0289  353  HIS   D CB  
10758 C  CG  . HIS   D 284 ? 1.6915 1.1477 1.1659 0.1481  0.0373  0.0295  353  HIS   D CG  
10759 N  ND1 . HIS   D 284 ? 1.6971 1.1323 1.1550 0.1491  0.0482  0.0355  353  HIS   D ND1 
10760 C  CD2 . HIS   D 284 ? 1.6879 1.1358 1.1469 0.1595  0.0282  0.0249  353  HIS   D CD2 
10761 C  CE1 . HIS   D 284 ? 1.7726 1.1869 1.2050 0.1608  0.0458  0.0346  353  HIS   D CE1 
10762 N  NE2 . HIS   D 284 ? 1.7475 1.1692 1.1802 0.1673  0.0334  0.0281  353  HIS   D NE2 
10763 N  N   . GLY   D 285 ? 1.5273 1.0553 1.0860 0.1116  0.0315  0.0249  354  GLY   D N   
10764 C  CA  . GLY   D 285 ? 1.5298 1.0776 1.1128 0.1000  0.0336  0.0259  354  GLY   D CA  
10765 C  C   . GLY   D 285 ? 1.4942 1.0633 1.0933 0.0990  0.0283  0.0232  354  GLY   D C   
10766 O  O   . GLY   D 285 ? 1.4569 1.0445 1.0766 0.0906  0.0266  0.0221  354  GLY   D O   
10767 N  N   . TYR   D 286 ? 1.4535 1.0200 1.0437 0.1072  0.0258  0.0221  355  TYR   D N   
10768 C  CA  . TYR   D 286 ? 1.4498 1.0355 1.0543 0.1067  0.0204  0.0194  355  TYR   D CA  
10769 C  C   . TYR   D 286 ? 1.4196 1.0212 1.0374 0.1051  0.0107  0.0135  355  TYR   D C   
10770 O  O   . TYR   D 286 ? 1.4510 1.0458 1.0595 0.1111  0.0044  0.0096  355  TYR   D O   
10771 C  CB  . TYR   D 286 ? 1.4475 1.0241 1.0363 0.1175  0.0179  0.0185  355  TYR   D CB  
10772 C  CG  . TYR   D 286 ? 1.4335 0.9949 1.0094 0.1192  0.0282  0.0245  355  TYR   D CG  
10773 C  CD1 . TYR   D 286 ? 1.5053 1.0434 1.0601 0.1239  0.0334  0.0274  355  TYR   D CD1 
10774 C  CD2 . TYR   D 286 ? 1.4057 0.9759 0.9907 0.1159  0.0333  0.0276  355  TYR   D CD2 
10775 C  CE1 . TYR   D 286 ? 1.5548 1.0782 1.0975 0.1253  0.0437  0.0332  355  TYR   D CE1 
10776 C  CE2 . TYR   D 286 ? 1.4480 1.0040 1.0213 0.1174  0.0435  0.0334  355  TYR   D CE2 
10777 C  CZ  . TYR   D 286 ? 1.5525 1.0851 1.1047 0.1221  0.0488  0.0362  355  TYR   D CZ  
10778 O  OH  . TYR   D 286 ? 1.7114 1.2293 1.2516 0.1238  0.0595  0.0421  355  TYR   D OH  
10779 N  N   . VAL   D 287 ? 1.3447 0.9670 0.9842 0.0971  0.0096  0.0128  356  VAL   D N   
10780 C  CA  . VAL   D 287 ? 1.3271 0.9654 0.9800 0.0954  0.0010  0.0074  356  VAL   D CA  
10781 C  C   . VAL   D 287 ? 1.3182 0.9693 0.9778 0.0995  -0.0054 0.0040  356  VAL   D C   
10782 O  O   . VAL   D 287 ? 1.3152 0.9743 0.9826 0.0966  -0.0021 0.0064  356  VAL   D O   
10783 C  CB  . VAL   D 287 ? 1.4046 1.0567 1.0766 0.0839  0.0034  0.0085  356  VAL   D CB  
10784 C  CG1 . VAL   D 287 ? 1.3914 1.0572 1.0748 0.0826  -0.0050 0.0031  356  VAL   D CG1 
10785 C  CG2 . VAL   D 287 ? 1.4694 1.1079 1.1349 0.0796  0.0107  0.0126  356  VAL   D CG2 
10786 N  N   . HIS   D 288 ? 1.3130 0.9662 0.9704 0.1059  -0.0143 -0.0014 357  HIS   D N   
10787 C  CA  . HIS   D 288 ? 1.3030 0.9669 0.9658 0.1108  -0.0213 -0.0053 357  HIS   D CA  
10788 C  C   . HIS   D 288 ? 1.3396 1.0222 1.0203 0.1073  -0.0281 -0.0099 357  HIS   D C   
10789 O  O   . HIS   D 288 ? 1.3421 1.0227 1.0197 0.1117  -0.0342 -0.0141 357  HIS   D O   
10790 C  CB  . HIS   D 288 ? 1.3266 0.9764 0.9712 0.1227  -0.0267 -0.0081 357  HIS   D CB  
10791 C  CG  . HIS   D 288 ? 1.3395 0.9713 0.9655 0.1279  -0.0212 -0.0041 357  HIS   D CG  
10792 N  ND1 . HIS   D 288 ? 1.3409 0.9728 0.9632 0.1329  -0.0225 -0.0041 357  HIS   D ND1 
10793 C  CD2 . HIS   D 288 ? 1.3599 0.9721 0.9689 0.1295  -0.0144 0.0000  357  HIS   D CD2 
10794 C  CE1 . HIS   D 288 ? 1.4209 1.0340 1.0245 0.1374  -0.0164 -0.0001 357  HIS   D CE1 
10795 N  NE2 . HIS   D 288 ? 1.3733 0.9742 0.9687 0.1353  -0.0113 0.0025  357  HIS   D NE2 
10796 N  N   . GLU   D 289 ? 1.4133 1.1138 1.1123 0.1000  -0.0272 -0.0094 358  GLU   D N   
10797 C  CA  . GLU   D 289 ? 1.3999 1.1178 1.1145 0.0985  -0.0341 -0.0141 358  GLU   D CA  
10798 C  C   . GLU   D 289 ? 1.4197 1.1371 1.1295 0.1079  -0.0417 -0.0184 358  GLU   D C   
10799 O  O   . GLU   D 289 ? 1.4491 1.1712 1.1612 0.1097  -0.0424 -0.0181 358  GLU   D O   
10800 C  CB  . GLU   D 289 ? 1.3803 1.1168 1.1142 0.0900  -0.0322 -0.0129 358  GLU   D CB  
10801 C  CG  . GLU   D 289 ? 1.3843 1.1224 1.1246 0.0804  -0.0248 -0.0084 358  GLU   D CG  
10802 C  CD  . GLU   D 289 ? 1.4264 1.1661 1.1690 0.0776  -0.0189 -0.0040 358  GLU   D CD  
10803 O  OE1 . GLU   D 289 ? 1.4523 1.1790 1.1807 0.0836  -0.0163 -0.0020 358  GLU   D OE1 
10804 O  OE2 . GLU   D 289 ? 1.4061 1.1599 1.1645 0.0697  -0.0168 -0.0026 358  GLU   D OE2 
10805 N  N   . THR   D 290 ? 1.3187 1.0303 1.0218 0.1142  -0.0477 -0.0225 359  THR   D N   
10806 C  CA  . THR   D 290 ? 1.3158 1.0261 1.0144 0.1237  -0.0557 -0.0270 359  THR   D CA  
10807 C  C   . THR   D 290 ? 1.2655 0.9930 0.9811 0.1229  -0.0626 -0.0322 359  THR   D C   
10808 O  O   . THR   D 290 ? 1.2733 1.0008 0.9900 0.1236  -0.0655 -0.0350 359  THR   D O   
10809 C  CB  . THR   D 290 ? 1.3337 1.0240 1.0117 0.1328  -0.0579 -0.0281 359  THR   D CB  
10810 O  OG1 . THR   D 290 ? 1.4041 1.0925 1.0823 0.1315  -0.0589 -0.0298 359  THR   D OG1 
10811 C  CG2 . THR   D 290 ? 1.3108 0.9836 0.9718 0.1336  -0.0504 -0.0228 359  THR   D CG2 
10812 N  N   . LEU   D 291 ? 1.2412 0.9830 0.9696 0.1214  -0.0649 -0.0334 360  LEU   D N   
10813 C  CA  . LEU   D 291 ? 1.2399 0.9968 0.9832 0.1223  -0.0720 -0.0385 360  LEU   D CA  
10814 C  C   . LEU   D 291 ? 1.2403 0.9890 0.9748 0.1327  -0.0798 -0.0432 360  LEU   D C   
10815 O  O   . LEU   D 291 ? 1.2619 0.9992 0.9833 0.1400  -0.0820 -0.0433 360  LEU   D O   
10816 C  CB  . LEU   D 291 ? 1.1981 0.9692 0.9544 0.1196  -0.0728 -0.0385 360  LEU   D CB  
10817 C  CG  . LEU   D 291 ? 1.1819 0.9699 0.9557 0.1193  -0.0790 -0.0433 360  LEU   D CG  
10818 C  CD1 . LEU   D 291 ? 1.1941 0.9930 0.9806 0.1112  -0.0762 -0.0429 360  LEU   D CD1 
10819 C  CD2 . LEU   D 291 ? 1.2172 1.0155 1.0000 0.1188  -0.0806 -0.0434 360  LEU   D CD2 
10820 N  N   . THR   D 292 ? 1.2900 1.0433 1.0307 0.1337  -0.0840 -0.0471 361  THR   D N   
10821 C  CA  . THR   D 292 ? 1.2820 1.0299 1.0174 0.1434  -0.0921 -0.0521 361  THR   D CA  
10822 C  C   . THR   D 292 ? 1.2716 1.0357 1.0237 0.1449  -0.0988 -0.0566 361  THR   D C   
10823 O  O   . THR   D 292 ? 1.2758 1.0561 1.0456 0.1390  -0.0985 -0.0577 361  THR   D O   
10824 C  CB  . THR   D 292 ? 1.3014 1.0449 1.0342 0.1442  -0.0929 -0.0540 361  THR   D CB  
10825 O  OG1 . THR   D 292 ? 1.3137 1.0706 1.0615 0.1355  -0.0895 -0.0534 361  THR   D OG1 
10826 C  CG2 . THR   D 292 ? 1.3212 1.0448 1.0339 0.1457  -0.0881 -0.0504 361  THR   D CG2 
10827 N  N   . VAL   D 293 ? 1.3136 1.0729 1.0599 0.1527  -0.1046 -0.0589 362  VAL   D N   
10828 C  CA  . VAL   D 293 ? 1.3230 1.0959 1.0843 0.1551  -0.1118 -0.0635 362  VAL   D CA  
10829 C  C   . VAL   D 293 ? 1.3290 1.0948 1.0848 0.1654  -0.1207 -0.0689 362  VAL   D C   
10830 O  O   . VAL   D 293 ? 1.3545 1.1027 1.0917 0.1718  -0.1216 -0.0686 362  VAL   D O   
10831 C  CB  . VAL   D 293 ? 1.2996 1.0758 1.0625 0.1549  -0.1119 -0.0621 362  VAL   D CB  
10832 C  CG1 . VAL   D 293 ? 1.3134 1.0959 1.0812 0.1452  -0.1031 -0.0568 362  VAL   D CG1 
10833 C  CG2 . VAL   D 293 ? 1.3031 1.0613 1.0457 0.1636  -0.1144 -0.0618 362  VAL   D CG2 
10834 N  N   . TYR   D 294 ? 1.3121 1.0917 1.0849 0.1671  -0.1274 -0.0738 363  TYR   D N   
10835 C  CA  . TYR   D 294 ? 1.3479 1.1237 1.1196 0.1763  -0.1364 -0.0795 363  TYR   D CA  
10836 C  C   . TYR   D 294 ? 1.3477 1.1130 1.1081 0.1853  -0.1432 -0.0815 363  TYR   D C   
10837 O  O   . TYR   D 294 ? 1.3108 1.0620 1.0572 0.1942  -0.1486 -0.0840 363  TYR   D O   
10838 C  CB  . TYR   D 294 ? 1.3775 1.1727 1.1732 0.1743  -0.1406 -0.0840 363  TYR   D CB  
10839 C  CG  . TYR   D 294 ? 1.3321 1.1314 1.1339 0.1718  -0.1384 -0.0849 363  TYR   D CG  
10840 C  CD1 . TYR   D 294 ? 1.3729 1.1576 1.1602 0.1778  -0.1400 -0.0860 363  TYR   D CD1 
10841 C  CD2 . TYR   D 294 ? 1.3052 1.1214 1.1257 0.1635  -0.1343 -0.0845 363  TYR   D CD2 
10842 C  CE1 . TYR   D 294 ? 1.3842 1.1718 1.1761 0.1756  -0.1379 -0.0868 363  TYR   D CE1 
10843 C  CE2 . TYR   D 294 ? 1.3490 1.1679 1.1738 0.1613  -0.1320 -0.0852 363  TYR   D CE2 
10844 C  CZ  . TYR   D 294 ? 1.3799 1.1848 1.1907 0.1675  -0.1340 -0.0864 363  TYR   D CZ  
10845 O  OH  . TYR   D 294 ? 1.4562 1.2628 1.2702 0.1658  -0.1317 -0.0872 363  TYR   D OH  
10846 N  N   . LYS   D 295 ? 1.3424 1.1144 1.1085 0.1833  -0.1435 -0.0807 364  LYS   D N   
10847 C  CA  . LYS   D 295 ? 1.3696 1.1327 1.1260 0.1914  -0.1500 -0.0827 364  LYS   D CA  
10848 C  C   . LYS   D 295 ? 1.4031 1.1644 1.1537 0.1869  -0.1436 -0.0775 364  LYS   D C   
10849 O  O   . LYS   D 295 ? 1.4097 1.1863 1.1760 0.1791  -0.1400 -0.0761 364  LYS   D O   
10850 C  CB  . LYS   D 295 ? 1.3354 1.1119 1.1100 0.1946  -0.1595 -0.0888 364  LYS   D CB  
10851 N  N   . ALA   D 296 ? 1.4311 1.1734 1.1589 0.1918  -0.1416 -0.0747 365  ALA   D N   
10852 C  CA  . ALA   D 296 ? 1.4363 1.1748 1.1569 0.1894  -0.1362 -0.0702 365  ALA   D CA  
10853 C  C   . ALA   D 296 ? 1.4457 1.1752 1.1563 0.1987  -0.1440 -0.0730 365  ALA   D C   
10854 O  O   . ALA   D 296 ? 1.4005 1.1208 1.1031 0.2079  -0.1525 -0.0775 365  ALA   D O   
10855 C  CB  . ALA   D 296 ? 1.3926 1.1163 1.0951 0.1871  -0.1265 -0.0641 365  ALA   D CB  
10856 N  N   . CYS   D 297 ? 1.5305 1.2625 1.2414 0.1964  -0.1412 -0.0705 366  CYS   D N   
10857 C  CA  . CYS   D 297 ? 1.5371 1.2623 1.2404 0.2044  -0.1486 -0.0732 366  CYS   D CA  
10858 C  C   . CYS   D 297 ? 1.5272 1.2401 1.2134 0.2048  -0.1418 -0.0679 366  CYS   D C   
10859 O  O   . CYS   D 297 ? 1.5615 1.2768 1.2483 0.1969  -0.1315 -0.0623 366  CYS   D O   
10860 C  CB  . CYS   D 297 ? 1.5096 1.2541 1.2358 0.2019  -0.1548 -0.0772 366  CYS   D CB  
10861 S  SG  . CYS   D 297 ? 1.7805 1.5321 1.5202 0.2076  -0.1671 -0.0853 366  CYS   D SG  
10862 N  N   . ASN   D 298 ? 1.4466 1.1457 1.1172 0.2142  -0.1478 -0.0697 367  ASN   D N   
10863 C  CA  . ASN   D 298 ? 1.4782 1.1638 1.1309 0.2161  -0.1420 -0.0651 367  ASN   D CA  
10864 C  C   . ASN   D 298 ? 1.4918 1.1600 1.1241 0.2165  -0.1327 -0.0596 367  ASN   D C   
10865 O  O   . ASN   D 298 ? 1.4845 1.1471 1.1084 0.2132  -0.1233 -0.0539 367  ASN   D O   
10866 C  CB  . ASN   D 298 ? 1.4501 1.1508 1.1173 0.2073  -0.1359 -0.0618 367  ASN   D CB  
10867 C  CG  . ASN   D 298 ? 1.4852 1.2002 1.1694 0.2076  -0.1444 -0.0666 367  ASN   D CG  
10868 O  OD1 . ASN   D 298 ? 1.5772 1.2849 1.2547 0.2166  -0.1542 -0.0712 367  ASN   D OD1 
10869 N  ND2 . ASN   D 298 ? 1.5271 1.2626 1.2337 0.1980  -0.1412 -0.0658 367  ASN   D ND2 
10870 N  N   . LEU   D 299 ? 1.5202 1.1795 1.1446 0.2202  -0.1348 -0.0612 368  LEU   D N   
10871 C  CA  . LEU   D 299 ? 1.5104 1.1522 1.1150 0.2207  -0.1262 -0.0562 368  LEU   D CA  
10872 C  C   . LEU   D 299 ? 1.5100 1.1283 1.0892 0.2334  -0.1322 -0.0583 368  LEU   D C   
10873 O  O   . LEU   D 299 ? 1.5354 1.1532 1.1159 0.2406  -0.1435 -0.0645 368  LEU   D O   
10874 C  CB  . LEU   D 299 ? 1.4734 1.1225 1.0880 0.2137  -0.1218 -0.0552 368  LEU   D CB  
10875 C  CG  . LEU   D 299 ? 1.4845 1.1551 1.1221 0.2010  -0.1151 -0.0524 368  LEU   D CG  
10876 C  CD1 . LEU   D 299 ? 1.4837 1.1597 1.1290 0.1945  -0.1106 -0.0512 368  LEU   D CD1 
10877 C  CD2 . LEU   D 299 ? 1.4864 1.1548 1.1194 0.1963  -0.1052 -0.0462 368  LEU   D CD2 
10878 N  N   . ASN   D 300 ? 1.4883 1.0869 1.0445 0.2364  -0.1247 -0.0533 369  ASN   D N   
10879 C  CA  . ASN   D 300 ? 1.5070 1.0808 1.0361 0.2482  -0.1286 -0.0544 369  ASN   D CA  
10880 C  C   . ASN   D 300 ? 1.5147 1.0766 1.0323 0.2469  -0.1215 -0.0510 369  ASN   D C   
10881 O  O   . ASN   D 300 ? 1.4840 1.0469 1.0026 0.2389  -0.1097 -0.0449 369  ASN   D O   
10882 C  CB  . ASN   D 300 ? 1.5493 1.1068 1.0581 0.2541  -0.1257 -0.0514 369  ASN   D CB  
10883 C  CG  . ASN   D 300 ? 1.5662 1.1267 1.0775 0.2607  -0.1371 -0.0568 369  ASN   D CG  
10884 O  OD1 . ASN   D 300 ? 1.5931 1.1664 1.1204 0.2617  -0.1476 -0.0630 369  ASN   D OD1 
10885 N  ND2 . ASN   D 300 ? 1.5396 1.0881 1.0353 0.2654  -0.1351 -0.0546 369  ASN   D ND2 
10886 N  N   . LEU   D 301 ? 1.6185 1.1698 1.1262 0.2549  -0.1291 -0.0550 370  LEU   D N   
10887 C  CA  . LEU   D 301 ? 1.6562 1.1944 1.1513 0.2550  -0.1239 -0.0525 370  LEU   D CA  
10888 C  C   . LEU   D 301 ? 1.7174 1.2281 1.1814 0.2619  -0.1176 -0.0479 370  LEU   D C   
10889 O  O   . LEU   D 301 ? 1.7751 1.2710 1.2215 0.2721  -0.1234 -0.0498 370  LEU   D O   
10890 C  CB  . LEU   D 301 ? 1.6392 1.1765 1.1356 0.2614  -0.1349 -0.0589 370  LEU   D CB  
10891 C  CG  . LEU   D 301 ? 1.6158 1.1771 1.1404 0.2539  -0.1381 -0.0623 370  LEU   D CG  
10892 C  CD1 . LEU   D 301 ? 1.6379 1.2056 1.1700 0.2426  -0.1261 -0.0568 370  LEU   D CD1 
10893 C  CD2 . LEU   D 301 ? 1.6025 1.1860 1.1510 0.2504  -0.1439 -0.0659 370  LEU   D CD2 
10894 N  N   . ILE   D 302 ? 1.5951 1.0984 1.0522 0.2563  -0.1058 -0.0418 371  ILE   D N   
10895 C  CA  . ILE   D 302 ? 1.5640 1.0415 0.9928 0.2614  -0.0976 -0.0365 371  ILE   D CA  
10896 C  C   . ILE   D 302 ? 1.6350 1.0976 1.0502 0.2647  -0.0971 -0.0365 371  ILE   D C   
10897 O  O   . ILE   D 302 ? 1.6878 1.1580 1.1138 0.2562  -0.0912 -0.0342 371  ILE   D O   
10898 C  CB  . ILE   D 302 ? 1.5263 1.0068 0.9585 0.2519  -0.0832 -0.0289 371  ILE   D CB  
10899 C  CG1 . ILE   D 302 ? 1.5340 1.0241 0.9738 0.2508  -0.0833 -0.0286 371  ILE   D CG1 
10900 C  CG2 . ILE   D 302 ? 1.5534 1.0080 0.9586 0.2558  -0.0735 -0.0231 371  ILE   D CG2 
10901 C  CD1 . ILE   D 302 ? 1.6126 1.0859 1.0315 0.2633  -0.0902 -0.0310 371  ILE   D CD1 
10902 N  N   . GLY   D 303 ? 1.6644 1.1055 1.0557 0.2773  -0.1039 -0.0391 372  GLY   D N   
10903 C  CA  . GLY   D 303 ? 1.6845 1.1073 1.0582 0.2820  -0.1032 -0.0387 372  GLY   D CA  
10904 C  C   . GLY   D 303 ? 1.7524 1.1807 1.1334 0.2866  -0.1156 -0.0458 372  GLY   D C   
10905 O  O   . GLY   D 303 ? 1.6999 1.1381 1.0908 0.2911  -0.1274 -0.0520 372  GLY   D O   
10906 N  N   . ARG   D 304 ? 1.8067 1.2286 1.1834 0.2854  -0.1131 -0.0451 373  ARG   D N   
10907 C  CA  . ARG   D 304 ? 1.7697 1.1963 1.1532 0.2896  -0.1239 -0.0515 373  ARG   D CA  
10908 C  C   . ARG   D 304 ? 1.7474 1.1897 1.1505 0.2786  -0.1187 -0.0503 373  ARG   D C   
10909 O  O   . ARG   D 304 ? 1.7234 1.1632 1.1249 0.2705  -0.1066 -0.0441 373  ARG   D O   
10910 C  CB  . ARG   D 304 ? 1.7879 1.1870 1.1421 0.3021  -0.1282 -0.0528 373  ARG   D CB  
10911 N  N   . PRO   D 305 ? 1.7299 1.1885 1.1519 0.2782  -0.1278 -0.0562 374  PRO   D N   
10912 C  CA  . PRO   D 305 ? 1.7003 1.1746 1.1415 0.2679  -0.1233 -0.0555 374  PRO   D CA  
10913 C  C   . PRO   D 305 ? 1.7501 1.2072 1.1749 0.2666  -0.1148 -0.0510 374  PRO   D C   
10914 O  O   . PRO   D 305 ? 1.8121 1.2462 1.2125 0.2759  -0.1166 -0.0511 374  PRO   D O   
10915 C  CB  . PRO   D 305 ? 1.6822 1.1691 1.1383 0.2718  -0.1356 -0.0631 374  PRO   D CB  
10916 C  CG  . PRO   D 305 ? 1.6987 1.1882 1.1560 0.2792  -0.1454 -0.0675 374  PRO   D CG  
10917 C  CD  . PRO   D 305 ? 1.7497 1.2143 1.1780 0.2865  -0.1421 -0.0638 374  PRO   D CD  
10918 N  N   . SER   D 306 ? 1.6674 1.1354 1.1058 0.2547  -0.1056 -0.0471 375  SER   D N   
10919 C  CA  . SER   D 306 ? 1.7163 1.1699 1.1420 0.2516  -0.0967 -0.0424 375  SER   D CA  
10920 C  C   . SER   D 306 ? 1.7518 1.2236 1.1995 0.2412  -0.0944 -0.0428 375  SER   D C   
10921 O  O   . SER   D 306 ? 1.7340 1.2293 1.2061 0.2345  -0.0964 -0.0448 375  SER   D O   
10922 C  CB  . SER   D 306 ? 1.6862 1.1281 1.0996 0.2476  -0.0844 -0.0349 375  SER   D CB  
10923 O  OG  . SER   D 306 ? 1.7443 1.1753 1.1498 0.2423  -0.0746 -0.0299 375  SER   D OG  
10924 N  N   . THR   D 307 ? 1.7839 1.2441 1.2222 0.2400  -0.0901 -0.0409 376  THR   D N   
10925 C  CA  . THR   D 307 ? 1.7218 1.1963 1.1780 0.2306  -0.0875 -0.0410 376  THR   D CA  
10926 C  C   . THR   D 307 ? 1.7884 1.2535 1.2381 0.2226  -0.0755 -0.0345 376  THR   D C   
10927 O  O   . THR   D 307 ? 1.8348 1.3068 1.2946 0.2160  -0.0733 -0.0344 376  THR   D O   
10928 C  CB  . THR   D 307 ? 1.6857 1.1597 1.1423 0.2366  -0.0964 -0.0468 376  THR   D CB  
10929 O  OG1 . THR   D 307 ? 1.7147 1.1630 1.1444 0.2470  -0.0981 -0.0467 376  THR   D OG1 
10930 C  CG2 . THR   D 307 ? 1.6752 1.1661 1.1476 0.2410  -0.1076 -0.0534 376  THR   D CG2 
10931 N  N   . GLU   D 308 ? 1.9372 1.3861 1.3702 0.2233  -0.0675 -0.0290 377  GLU   D N   
10932 C  CA  . GLU   D 308 ? 1.9703 1.4130 1.4010 0.2143  -0.0554 -0.0225 377  GLU   D CA  
10933 C  C   . GLU   D 308 ? 1.9582 1.4247 1.4153 0.2014  -0.0511 -0.0210 377  GLU   D C   
10934 O  O   . GLU   D 308 ? 1.9447 1.4240 1.4129 0.1988  -0.0509 -0.0206 377  GLU   D O   
10935 C  CB  . GLU   D 308 ? 2.0149 1.4389 1.4262 0.2168  -0.0471 -0.0168 377  GLU   D CB  
10936 C  CG  . GLU   D 308 ? 2.0685 1.4667 1.4511 0.2296  -0.0499 -0.0173 377  GLU   D CG  
10937 C  CD  . GLU   D 308 ? 2.1344 1.5171 1.5007 0.2311  -0.0408 -0.0113 377  GLU   D CD  
10938 O  OE1 . GLU   D 308 ? 2.0456 1.4405 1.4228 0.2275  -0.0389 -0.0101 377  GLU   D OE1 
10939 O  OE2 . GLU   D 308 ? 2.1830 1.5414 1.5261 0.2353  -0.0351 -0.0077 377  GLU   D OE2 
10940 N  N   . HIS   D 309 ? 1.9949 1.4664 1.4611 0.1935  -0.0477 -0.0200 378  HIS   D N   
10941 C  CA  . HIS   D 309 ? 2.0003 1.4915 1.4892 0.1808  -0.0425 -0.0178 378  HIS   D CA  
10942 C  C   . HIS   D 309 ? 1.9312 1.4468 1.4419 0.1791  -0.0494 -0.0221 378  HIS   D C   
10943 O  O   . HIS   D 309 ? 1.9062 1.4365 1.4321 0.1714  -0.0456 -0.0200 378  HIS   D O   
10944 C  CB  . HIS   D 309 ? 2.0156 1.5006 1.5008 0.1749  -0.0312 -0.0109 378  HIS   D CB  
10945 C  CG  . HIS   D 309 ? 2.0450 1.5425 1.5480 0.1618  -0.0241 -0.0075 378  HIS   D CG  
10946 N  ND1 . HIS   D 309 ? 2.0672 1.5529 1.5640 0.1565  -0.0162 -0.0033 378  HIS   D ND1 
10947 C  CD2 . HIS   D 309 ? 1.9726 1.4927 1.4989 0.1529  -0.0237 -0.0077 378  HIS   D CD2 
10948 C  CE1 . HIS   D 309 ? 1.9856 1.4863 1.5016 0.1451  -0.0118 -0.0012 378  HIS   D CE1 
10949 N  NE2 . HIS   D 309 ? 1.9314 1.4529 1.4651 0.1428  -0.0162 -0.0038 378  HIS   D NE2 
10950 N  N   . SER   D 310 ? 1.7810 1.3008 1.2934 0.1864  -0.0597 -0.0283 379  SER   D N   
10951 C  CA  . SER   D 310 ? 1.7140 1.2567 1.2474 0.1850  -0.0664 -0.0326 379  SER   D CA  
10952 C  C   . SER   D 310 ? 1.7021 1.2637 1.2574 0.1739  -0.0640 -0.0326 379  SER   D C   
10953 O  O   . SER   D 310 ? 1.6727 1.2312 1.2275 0.1713  -0.0629 -0.0328 379  SER   D O   
10954 C  CB  . SER   D 310 ? 1.6841 1.2264 1.2150 0.1954  -0.0778 -0.0393 379  SER   D CB  
10955 O  OG  . SER   D 310 ? 1.5588 1.1231 1.1107 0.1939  -0.0839 -0.0433 379  SER   D OG  
10956 N  N   . TRP   D 311 ? 1.6316 1.2123 1.2055 0.1676  -0.0633 -0.0323 380  TRP   D N   
10957 C  CA  . TRP   D 311 ? 1.5559 1.1547 1.1503 0.1573  -0.0613 -0.0323 380  TRP   D CA  
10958 C  C   . TRP   D 311 ? 1.5309 1.1426 1.1377 0.1595  -0.0696 -0.0383 380  TRP   D C   
10959 O  O   . TRP   D 311 ? 1.5956 1.2184 1.2155 0.1526  -0.0684 -0.0389 380  TRP   D O   
10960 C  CB  . TRP   D 311 ? 1.5001 1.1140 1.1093 0.1499  -0.0575 -0.0297 380  TRP   D CB  
10961 C  CG  . TRP   D 311 ? 1.5303 1.1334 1.1302 0.1462  -0.0482 -0.0234 380  TRP   D CG  
10962 C  CD1 . TRP   D 311 ? 1.5577 1.1453 1.1457 0.1437  -0.0412 -0.0192 380  TRP   D CD1 
10963 C  CD2 . TRP   D 311 ? 1.5153 1.1217 1.1171 0.1449  -0.0447 -0.0205 380  TRP   D CD2 
10964 N  NE1 . TRP   D 311 ? 1.5159 1.0976 1.0992 0.1406  -0.0332 -0.0138 380  TRP   D NE1 
10965 C  CE2 . TRP   D 311 ? 1.5119 1.1049 1.1033 0.1414  -0.0352 -0.0144 380  TRP   D CE2 
10966 C  CE3 . TRP   D 311 ? 1.4601 1.0795 1.0718 0.1462  -0.0486 -0.0223 380  TRP   D CE3 
10967 C  CZ2 . TRP   D 311 ? 1.4948 1.0872 1.0854 0.1395  -0.0293 -0.0103 380  TRP   D CZ2 
10968 C  CZ3 . TRP   D 311 ? 1.4324 1.0509 1.0425 0.1444  -0.0431 -0.0183 380  TRP   D CZ3 
10969 C  CH2 . TRP   D 311 ? 1.4686 1.0738 1.0683 0.1412  -0.0335 -0.0123 380  TRP   D CH2 
10970 N  N   . PHE   D 312 ? 1.5474 1.1576 1.1503 0.1691  -0.0778 -0.0429 381  PHE   D N   
10971 C  CA  . PHE   D 312 ? 1.5746 1.1961 1.1890 0.1723  -0.0857 -0.0489 381  PHE   D CA  
10972 C  C   . PHE   D 312 ? 1.6024 1.2067 1.1995 0.1825  -0.0907 -0.0516 381  PHE   D C   
10973 O  O   . PHE   D 312 ? 1.6271 1.2236 1.2145 0.1918  -0.0965 -0.0540 381  PHE   D O   
10974 C  CB  . PHE   D 312 ? 1.5071 1.1447 1.1361 0.1744  -0.0919 -0.0524 381  PHE   D CB  
10975 C  CG  . PHE   D 312 ? 1.4406 1.0920 1.0830 0.1656  -0.0869 -0.0492 381  PHE   D CG  
10976 C  CD1 . PHE   D 312 ? 1.4975 1.1660 1.1586 0.1564  -0.0844 -0.0490 381  PHE   D CD1 
10977 C  CD2 . PHE   D 312 ? 1.4884 1.1346 1.1236 0.1667  -0.0844 -0.0462 381  PHE   D CD2 
10978 C  CE1 . PHE   D 312 ? 1.4928 1.1736 1.1660 0.1485  -0.0800 -0.0462 381  PHE   D CE1 
10979 C  CE2 . PHE   D 312 ? 1.5014 1.1600 1.1489 0.1587  -0.0797 -0.0433 381  PHE   D CE2 
10980 C  CZ  . PHE   D 312 ? 1.4863 1.1625 1.1531 0.1495  -0.0776 -0.0433 381  PHE   D CZ  
10981 N  N   . PRO   D 313 ? 1.6020 1.1986 1.1935 0.1812  -0.0886 -0.0513 382  PRO   D N   
10982 C  CA  . PRO   D 313 ? 1.6275 1.2061 1.2009 0.1909  -0.0928 -0.0535 382  PRO   D CA  
10983 C  C   . PRO   D 313 ? 1.6539 1.2384 1.2324 0.2002  -0.1035 -0.0601 382  PRO   D C   
10984 O  O   . PRO   D 313 ? 1.5997 1.2038 1.1985 0.1978  -0.1074 -0.0637 382  PRO   D O   
10985 C  CB  . PRO   D 313 ? 1.6305 1.2064 1.2041 0.1859  -0.0892 -0.0527 382  PRO   D CB  
10986 C  CG  . PRO   D 313 ? 1.6707 1.2533 1.2525 0.1741  -0.0803 -0.0476 382  PRO   D CG  
10987 C  CD  . PRO   D 313 ? 1.6205 1.2220 1.2195 0.1707  -0.0816 -0.0481 382  PRO   D CD  
10988 N  N   . GLY   D 314 ? 1.6601 1.2269 1.2197 0.2109  -0.1083 -0.0618 383  GLY   D N   
10989 C  CA  . GLY   D 314 ? 1.6859 1.2556 1.2479 0.2208  -0.1190 -0.0680 383  GLY   D CA  
10990 C  C   . GLY   D 314 ? 1.7536 1.3300 1.3205 0.2237  -0.1230 -0.0692 383  GLY   D C   
10991 O  O   . GLY   D 314 ? 1.7348 1.3121 1.3027 0.2325  -0.1325 -0.0743 383  GLY   D O   
10992 N  N   . TYR   D 315 ? 1.7527 1.3338 1.3230 0.2164  -0.1164 -0.0646 384  TYR   D N   
10993 C  CA  . TYR   D 315 ? 1.6996 1.2853 1.2725 0.2185  -0.1190 -0.0649 384  TYR   D CA  
10994 C  C   . TYR   D 315 ? 1.6703 1.2352 1.2198 0.2218  -0.1141 -0.0602 384  TYR   D C   
10995 O  O   . TYR   D 315 ? 1.6483 1.1999 1.1848 0.2186  -0.1061 -0.0555 384  TYR   D O   
10996 C  CB  . TYR   D 315 ? 1.5967 1.2051 1.1927 0.2081  -0.1154 -0.0636 384  TYR   D CB  
10997 C  CG  . TYR   D 315 ? 1.5362 1.1653 1.1553 0.2066  -0.1214 -0.0688 384  TYR   D CG  
10998 C  CD1 . TYR   D 315 ? 1.5735 1.2118 1.2023 0.2124  -0.1303 -0.0739 384  TYR   D CD1 
10999 C  CD2 . TYR   D 315 ? 1.5636 1.2022 1.1944 0.1998  -0.1181 -0.0688 384  TYR   D CD2 
11000 C  CE1 . TYR   D 315 ? 1.5678 1.2248 1.2182 0.2112  -0.1353 -0.0785 384  TYR   D CE1 
11001 C  CE2 . TYR   D 315 ? 1.6130 1.2698 1.2643 0.1988  -0.1230 -0.0734 384  TYR   D CE2 
11002 C  CZ  . TYR   D 315 ? 1.5833 1.2494 1.2447 0.2045  -0.1313 -0.0782 384  TYR   D CZ  
11003 O  OH  . TYR   D 315 ? 1.5948 1.2789 1.2773 0.2034  -0.1356 -0.0827 384  TYR   D OH  
11004 N  N   . ALA   D 316 ? 1.6218 1.1832 1.1655 0.2285  -0.1191 -0.0617 385  ALA   D N   
11005 C  CA  . ALA   D 316 ? 1.6046 1.1456 1.1252 0.2332  -0.1154 -0.0578 385  ALA   D CA  
11006 C  C   . ALA   D 316 ? 1.6262 1.1768 1.1547 0.2292  -0.1127 -0.0556 385  ALA   D C   
11007 O  O   . ALA   D 316 ? 1.6571 1.2224 1.2002 0.2305  -0.1198 -0.0597 385  ALA   D O   
11008 C  CB  . ALA   D 316 ? 1.6794 1.2032 1.1812 0.2470  -0.1245 -0.0618 385  ALA   D CB  
11009 N  N   . TRP   D 317 ? 1.6175 1.1594 1.1362 0.2246  -0.1026 -0.0492 386  TRP   D N   
11010 C  CA  . TRP   D 317 ? 1.6211 1.1723 1.1477 0.2193  -0.0982 -0.0462 386  TRP   D CA  
11011 C  C   . TRP   D 317 ? 1.5605 1.0945 1.0665 0.2280  -0.0991 -0.0451 386  TRP   D C   
11012 O  O   . TRP   D 317 ? 1.5767 1.0886 1.0597 0.2324  -0.0944 -0.0416 386  TRP   D O   
11013 C  CB  . TRP   D 317 ? 1.5996 1.1536 1.1308 0.2079  -0.0859 -0.0398 386  TRP   D CB  
11014 C  CG  . TRP   D 317 ? 1.5460 1.0774 1.0554 0.2095  -0.0787 -0.0353 386  TRP   D CG  
11015 C  CD1 . TRP   D 317 ? 1.5920 1.1159 1.0962 0.2088  -0.0773 -0.0352 386  TRP   D CD1 
11016 C  CD2 . TRP   D 317 ? 1.5921 1.1050 1.0814 0.2123  -0.0715 -0.0301 386  TRP   D CD2 
11017 N  NE1 . TRP   D 317 ? 1.6957 1.1975 1.1782 0.2107  -0.0697 -0.0303 386  TRP   D NE1 
11018 C  CE2 . TRP   D 317 ? 1.6787 1.1732 1.1517 0.2128  -0.0658 -0.0270 386  TRP   D CE2 
11019 C  CE3 . TRP   D 317 ? 1.5737 1.0832 1.0571 0.2143  -0.0691 -0.0277 386  TRP   D CE3 
11020 C  CZ2 . TRP   D 317 ? 1.7479 1.2211 1.1993 0.2153  -0.0575 -0.0215 386  TRP   D CZ2 
11021 C  CZ3 . TRP   D 317 ? 1.6095 1.0977 1.0710 0.2170  -0.0607 -0.0223 386  TRP   D CZ3 
11022 C  CH2 . TRP   D 317 ? 1.7092 1.1796 1.1552 0.2174  -0.0548 -0.0191 386  TRP   D CH2 
11023 N  N   . THR   D 318 ? 1.5264 1.0700 1.0405 0.2306  -0.1050 -0.0479 387  THR   D N   
11024 C  CA  . THR   D 318 ? 1.6044 1.1345 1.1016 0.2370  -0.1046 -0.0461 387  THR   D CA  
11025 C  C   . THR   D 318 ? 1.5269 1.0705 1.0372 0.2279  -0.0971 -0.0420 387  THR   D C   
11026 O  O   . THR   D 318 ? 1.5035 1.0696 1.0378 0.2211  -0.0992 -0.0440 387  THR   D O   
11027 C  CB  . THR   D 318 ? 1.5586 1.0871 1.0526 0.2480  -0.1177 -0.0526 387  THR   D CB  
11028 O  OG1 . THR   D 318 ? 1.5728 1.0963 1.0635 0.2546  -0.1261 -0.0576 387  THR   D OG1 
11029 C  CG2 . THR   D 318 ? 1.5788 1.0851 1.0469 0.2570  -0.1172 -0.0507 387  THR   D CG2 
11030 N  N   . VAL   D 319 ? 1.4951 1.0247 0.9898 0.2276  -0.0879 -0.0361 388  VAL   D N   
11031 C  CA  . VAL   D 319 ? 1.4544 0.9959 0.9609 0.2192  -0.0803 -0.0319 388  VAL   D CA  
11032 C  C   . VAL   D 319 ? 1.4525 1.0052 0.9681 0.2224  -0.0883 -0.0358 388  VAL   D C   
11033 O  O   . VAL   D 319 ? 1.5101 1.0519 1.0125 0.2331  -0.0966 -0.0395 388  VAL   D O   
11034 C  CB  . VAL   D 319 ? 1.4730 0.9959 0.9600 0.2193  -0.0689 -0.0249 388  VAL   D CB  
11035 C  CG1 . VAL   D 319 ? 1.4593 0.9941 0.9580 0.2121  -0.0621 -0.0210 388  VAL   D CG1 
11036 C  CG2 . VAL   D 319 ? 1.4794 0.9941 0.9615 0.2141  -0.0602 -0.0207 388  VAL   D CG2 
11037 N  N   . ALA   D 320 ? 1.4377 1.0122 0.9762 0.2133  -0.0862 -0.0352 389  ALA   D N   
11038 C  CA  . ALA   D 320 ? 1.4299 1.0163 0.9788 0.2150  -0.0926 -0.0383 389  ALA   D CA  
11039 C  C   . ALA   D 320 ? 1.4700 1.0612 1.0228 0.2087  -0.0836 -0.0330 389  ALA   D C   
11040 O  O   . ALA   D 320 ? 1.4392 1.0320 0.9952 0.2003  -0.0731 -0.0276 389  ALA   D O   
11041 C  CB  . ALA   D 320 ? 1.3848 0.9948 0.9598 0.2107  -0.1003 -0.0436 389  ALA   D CB  
11042 N  N   . GLN   D 321 ? 1.5014 1.0945 1.0537 0.2130  -0.0882 -0.0348 390  GLN   D N   
11043 C  CA  . GLN   D 321 ? 1.4444 1.0405 0.9983 0.2090  -0.0809 -0.0303 390  GLN   D CA  
11044 C  C   . GLN   D 321 ? 1.4359 1.0441 1.0006 0.2114  -0.0893 -0.0345 390  GLN   D C   
11045 O  O   . GLN   D 321 ? 1.4612 1.0700 1.0266 0.2182  -0.1007 -0.0406 390  GLN   D O   
11046 C  CB  . GLN   D 321 ? 1.4677 1.0395 0.9946 0.2152  -0.0738 -0.0255 390  GLN   D CB  
11047 C  CG  . GLN   D 321 ? 1.4967 1.0491 1.0011 0.2289  -0.0825 -0.0292 390  GLN   D CG  
11048 C  CD  . GLN   D 321 ? 1.5412 1.0714 1.0202 0.2349  -0.0753 -0.0243 390  GLN   D CD  
11049 O  OE1 . GLN   D 321 ? 1.5264 1.0519 1.0015 0.2294  -0.0628 -0.0178 390  GLN   D OE1 
11050 N  NE2 . GLN   D 321 ? 1.5421 1.0585 1.0039 0.2464  -0.0831 -0.0275 390  GLN   D NE2 
11051 N  N   . CYS   D 322 ? 1.4054 1.0217 0.9775 0.2061  -0.0836 -0.0312 391  CYS   D N   
11052 C  CA  . CYS   D 322 ? 1.3699 0.9998 0.9549 0.2065  -0.0904 -0.0346 391  CYS   D CA  
11053 C  C   . CYS   D 322 ? 1.4215 1.0357 0.9879 0.2190  -0.0987 -0.0380 391  CYS   D C   
11054 O  O   . CYS   D 322 ? 1.4566 1.0497 0.9991 0.2255  -0.0945 -0.0350 391  CYS   D O   
11055 C  CB  . CYS   D 322 ? 1.3649 1.0045 0.9592 0.1984  -0.0812 -0.0296 391  CYS   D CB  
11056 S  SG  . CYS   D 322 ? 1.3378 0.9924 0.9462 0.1986  -0.0878 -0.0328 391  CYS   D SG  
11057 N  N   . LYS   D 323 ? 1.4355 1.0594 1.0127 0.2224  -0.1106 -0.0445 392  LYS   D N   
11058 C  CA  . LYS   D 323 ? 1.3924 1.0039 0.9553 0.2339  -0.1204 -0.0488 392  LYS   D CA  
11059 C  C   . LYS   D 323 ? 1.3987 1.0044 0.9525 0.2356  -0.1163 -0.0456 392  LYS   D C   
11060 O  O   . LYS   D 323 ? 1.4147 1.0079 0.9538 0.2454  -0.1234 -0.0484 392  LYS   D O   
11061 C  CB  . LYS   D 323 ? 1.3781 1.0052 0.9598 0.2353  -0.1334 -0.0562 392  LYS   D CB  
11062 N  N   . ILE   D 324 ? 1.3878 1.0014 0.9491 0.2267  -0.1049 -0.0397 393  ILE   D N   
11063 C  CA  . ILE   D 324 ? 1.3897 1.0017 0.9468 0.2270  -0.1008 -0.0368 393  ILE   D CA  
11064 C  C   . ILE   D 324 ? 1.4016 1.0012 0.9443 0.2248  -0.0866 -0.0291 393  ILE   D C   
11065 O  O   . ILE   D 324 ? 1.4361 1.0152 0.9551 0.2329  -0.0843 -0.0270 393  ILE   D O   
11066 C  CB  . ILE   D 324 ? 1.3616 0.9991 0.9462 0.2180  -0.1017 -0.0379 393  ILE   D CB  
11067 C  CG1 . ILE   D 324 ? 1.3550 1.0049 0.9547 0.2202  -0.1153 -0.0455 393  ILE   D CG1 
11068 C  CG2 . ILE   D 324 ? 1.3640 0.9995 0.9439 0.2184  -0.0971 -0.0346 393  ILE   D CG2 
11069 C  CD1 . ILE   D 324 ? 1.3688 1.0079 0.9561 0.2310  -0.1256 -0.0499 393  ILE   D CD1 
11070 N  N   . CYS   D 325 ? 1.3861 0.9978 0.9434 0.2138  -0.0770 -0.0247 394  CYS   D N   
11071 C  CA  . CYS   D 325 ? 1.3953 0.9973 0.9425 0.2105  -0.0632 -0.0172 394  CYS   D CA  
11072 C  C   . CYS   D 325 ? 1.4131 0.9979 0.9439 0.2129  -0.0586 -0.0149 394  CYS   D C   
11073 O  O   . CYS   D 325 ? 1.4246 0.9981 0.9444 0.2113  -0.0470 -0.0087 394  CYS   D O   
11074 C  CB  . CYS   D 325 ? 1.3982 1.0213 0.9694 0.1975  -0.0555 -0.0137 394  CYS   D CB  
11075 S  SG  . CYS   D 325 ? 1.3498 0.9904 0.9427 0.1888  -0.0583 -0.0163 394  CYS   D SG  
11076 N  N   . ALA   D 326 ? 1.4156 0.9984 0.9452 0.2167  -0.0674 -0.0199 395  ALA   D N   
11077 C  CA  . ALA   D 326 ? 1.4329 0.9992 0.9467 0.2199  -0.0649 -0.0186 395  ALA   D CA  
11078 C  C   . ALA   D 326 ? 1.4651 1.0363 0.9872 0.2095  -0.0530 -0.0130 395  ALA   D C   
11079 O  O   . ALA   D 326 ? 1.5019 1.0558 1.0074 0.2110  -0.0451 -0.0087 395  ALA   D O   
11080 C  CB  . ALA   D 326 ? 1.4645 1.0030 0.9470 0.2315  -0.0637 -0.0171 395  ALA   D CB  
11081 N  N   . SER   D 327 ? 1.4268 1.0216 0.9753 0.1989  -0.0522 -0.0133 396  SER   D N   
11082 C  CA  . SER   D 327 ? 1.4525 1.0547 1.0123 0.1884  -0.0430 -0.0090 396  SER   D CA  
11083 C  C   . SER   D 327 ? 1.4627 1.0690 1.0288 0.1870  -0.0484 -0.0126 396  SER   D C   
11084 O  O   . SER   D 327 ? 1.4274 1.0428 1.0021 0.1896  -0.0591 -0.0186 396  SER   D O   
11085 C  CB  . SER   D 327 ? 1.4703 1.0947 1.0540 0.1780  -0.0392 -0.0072 396  SER   D CB  
11086 O  OG  . SER   D 327 ? 1.4923 1.1103 1.0684 0.1784  -0.0310 -0.0023 396  SER   D OG  
11087 N  N   . HIS   D 328 ? 1.4917 1.0903 1.0530 0.1832  -0.0409 -0.0089 397  HIS   D N   
11088 C  CA  . HIS   D 328 ? 1.4589 1.0597 1.0244 0.1820  -0.0452 -0.0120 397  HIS   D CA  
11089 C  C   . HIS   D 328 ? 1.4400 1.0662 1.0329 0.1734  -0.0492 -0.0149 397  HIS   D C   
11090 O  O   . HIS   D 328 ? 1.5360 1.1755 1.1443 0.1639  -0.0427 -0.0116 397  HIS   D O   
11091 C  CB  . HIS   D 328 ? 1.5028 1.0913 1.0592 0.1784  -0.0353 -0.0068 397  HIS   D CB  
11092 C  CG  . HIS   D 328 ? 1.4796 1.0712 1.0417 0.1757  -0.0384 -0.0093 397  HIS   D CG  
11093 N  ND1 . HIS   D 328 ? 1.4953 1.1004 1.0750 0.1647  -0.0336 -0.0074 397  HIS   D ND1 
11094 C  CD2 . HIS   D 328 ? 1.4447 1.0279 0.9976 0.1827  -0.0462 -0.0137 397  HIS   D CD2 
11095 C  CE1 . HIS   D 328 ? 1.4707 1.0749 1.0509 0.1652  -0.0380 -0.0104 397  HIS   D CE1 
11096 N  NE2 . HIS   D 328 ? 1.4234 1.0148 0.9880 0.1759  -0.0455 -0.0142 397  HIS   D NE2 
11097 N  N   . ILE   D 329 ? 1.4081 1.0412 1.0075 0.1770  -0.0598 -0.0211 398  ILE   D N   
11098 C  CA  . ILE   D 329 ? 1.3930 1.0490 1.0174 0.1695  -0.0637 -0.0242 398  ILE   D CA  
11099 C  C   . ILE   D 329 ? 1.3552 1.0112 0.9824 0.1666  -0.0638 -0.0252 398  ILE   D C   
11100 O  O   . ILE   D 329 ? 1.3415 1.0109 0.9847 0.1571  -0.0601 -0.0239 398  ILE   D O   
11101 C  CB  . ILE   D 329 ? 1.3195 0.9855 0.9524 0.1745  -0.0750 -0.0304 398  ILE   D CB  
11102 C  CG1 . ILE   D 329 ? 1.3861 1.0536 1.0181 0.1759  -0.0741 -0.0290 398  ILE   D CG1 
11103 C  CG2 . ILE   D 329 ? 1.2934 0.9820 0.9513 0.1675  -0.0789 -0.0336 398  ILE   D CG2 
11104 C  CD1 . ILE   D 329 ? 1.3939 1.0740 1.0395 0.1655  -0.0650 -0.0240 398  ILE   D CD1 
11105 N  N   . GLY   D 330 ? 1.3854 1.0258 0.9964 0.1747  -0.0680 -0.0275 399  GLY   D N   
11106 C  CA  . GLY   D 330 ? 1.3648 1.0039 0.9770 0.1728  -0.0684 -0.0286 399  GLY   D CA  
11107 C  C   . GLY   D 330 ? 1.3903 1.0107 0.9827 0.1835  -0.0741 -0.0315 399  GLY   D C   
11108 O  O   . GLY   D 330 ? 1.4002 1.0007 0.9708 0.1900  -0.0714 -0.0290 399  GLY   D O   
11109 N  N   . TRP   D 331 ? 1.3786 1.0053 0.9785 0.1855  -0.0819 -0.0367 400  TRP   D N   
11110 C  CA  . TRP   D 331 ? 1.4052 1.0162 0.9892 0.1951  -0.0880 -0.0400 400  TRP   D CA  
11111 C  C   . TRP   D 331 ? 1.3933 1.0169 0.9907 0.1989  -0.0995 -0.0471 400  TRP   D C   
11112 O  O   . TRP   D 331 ? 1.4920 1.1357 1.1115 0.1919  -0.1005 -0.0489 400  TRP   D O   
11113 C  CB  . TRP   D 331 ? 1.4596 1.0617 1.0369 0.1918  -0.0822 -0.0374 400  TRP   D CB  
11114 C  CG  . TRP   D 331 ? 1.4165 1.0075 0.9833 0.1868  -0.0704 -0.0303 400  TRP   D CG  
11115 C  CD1 . TRP   D 331 ? 1.4196 0.9873 0.9623 0.1925  -0.0658 -0.0270 400  TRP   D CD1 
11116 C  CD2 . TRP   D 331 ? 1.3798 0.9825 0.9606 0.1752  -0.0615 -0.0258 400  TRP   D CD2 
11117 N  NE1 . TRP   D 331 ? 1.4213 0.9858 0.9629 0.1850  -0.0544 -0.0205 400  TRP   D NE1 
11118 C  CE2 . TRP   D 331 ? 1.3962 0.9823 0.9613 0.1743  -0.0518 -0.0198 400  TRP   D CE2 
11119 C  CE3 . TRP   D 331 ? 1.3545 0.9799 0.9596 0.1657  -0.0609 -0.0262 400  TRP   D CE3 
11120 C  CZ2 . TRP   D 331 ? 1.4480 1.0399 1.0219 0.1642  -0.0419 -0.0144 400  TRP   D CZ2 
11121 C  CZ3 . TRP   D 331 ? 1.3537 0.9843 0.9664 0.1559  -0.0515 -0.0209 400  TRP   D CZ3 
11122 C  CH2 . TRP   D 331 ? 1.3960 1.0104 0.9939 0.1551  -0.0422 -0.0152 400  TRP   D CH2 
11123 N  N   . LYS   D 332 ? 1.3834 0.9948 0.9676 0.2100  -0.1079 -0.0513 401  LYS   D N   
11124 C  CA  . LYS   D 332 ? 1.4152 1.0362 1.0109 0.2143  -0.1188 -0.0581 401  LYS   D CA  
11125 C  C   . LYS   D 332 ? 1.5168 1.1277 1.1039 0.2176  -0.1200 -0.0595 401  LYS   D C   
11126 O  O   . LYS   D 332 ? 1.5210 1.1103 1.0850 0.2246  -0.1193 -0.0582 401  LYS   D O   
11127 C  CB  . LYS   D 332 ? 1.4628 1.0789 1.0524 0.2246  -0.1288 -0.0626 401  LYS   D CB  
11128 C  CG  . LYS   D 332 ? 1.4416 1.0700 1.0466 0.2287  -0.1403 -0.0700 401  LYS   D CG  
11129 C  CD  . LYS   D 332 ? 1.4630 1.0803 1.0559 0.2407  -0.1506 -0.0742 401  LYS   D CD  
11130 C  CE  . LYS   D 332 ? 1.4179 1.0450 1.0248 0.2460  -0.1627 -0.0818 401  LYS   D CE  
11131 N  NZ  . LYS   D 332 ? 1.5330 1.1569 1.1367 0.2546  -0.1728 -0.0861 401  LYS   D NZ  
11132 N  N   . PHE   D 333 ? 1.5304 1.1565 1.1357 0.2127  -0.1217 -0.0621 402  PHE   D N   
11133 C  CA  . PHE   D 333 ? 1.5465 1.1655 1.1464 0.2139  -0.1215 -0.0629 402  PHE   D CA  
11134 C  C   . PHE   D 333 ? 1.5891 1.2101 1.1929 0.2224  -0.1329 -0.0699 402  PHE   D C   
11135 O  O   . PHE   D 333 ? 1.5364 1.1764 1.1616 0.2203  -0.1380 -0.0740 402  PHE   D O   
11136 C  CB  . PHE   D 333 ? 1.4756 1.1083 1.0912 0.2024  -0.1145 -0.0605 402  PHE   D CB  
11137 C  CG  . PHE   D 333 ? 1.4941 1.1199 1.1021 0.1950  -0.1031 -0.0536 402  PHE   D CG  
11138 C  CD1 . PHE   D 333 ? 1.5180 1.1261 1.1087 0.1957  -0.0979 -0.0504 402  PHE   D CD1 
11139 C  CD2 . PHE   D 333 ? 1.4757 1.1126 1.0941 0.1873  -0.0977 -0.0501 402  PHE   D CD2 
11140 C  CE1 . PHE   D 333 ? 1.4982 1.1003 1.0833 0.1886  -0.0873 -0.0440 402  PHE   D CE1 
11141 C  CE2 . PHE   D 333 ? 1.4405 1.0717 1.0534 0.1805  -0.0873 -0.0438 402  PHE   D CE2 
11142 C  CZ  . PHE   D 333 ? 1.4509 1.0648 1.0474 0.1810  -0.0821 -0.0408 402  PHE   D CZ  
11143 N  N   . THR   D 334 ? 1.6856 1.2868 1.2689 0.2317  -0.1364 -0.0712 403  THR   D N   
11144 C  CA  . THR   D 334 ? 1.7038 1.3026 1.2866 0.2415  -0.1476 -0.0777 403  THR   D CA  
11145 C  C   . THR   D 334 ? 1.7292 1.3223 1.3081 0.2419  -0.1465 -0.0783 403  THR   D C   
11146 O  O   . THR   D 334 ? 1.7371 1.3157 1.3002 0.2400  -0.1390 -0.0738 403  THR   D O   
11147 C  CB  . THR   D 334 ? 1.7061 1.2846 1.2661 0.2532  -0.1534 -0.0789 403  THR   D CB  
11148 O  OG1 . THR   D 334 ? 1.7998 1.3549 1.3346 0.2575  -0.1493 -0.0759 403  THR   D OG1 
11149 C  CG2 . THR   D 334 ? 1.6680 1.2464 1.2250 0.2514  -0.1502 -0.0758 403  THR   D CG2 
11150 N  N   . ALA   D 335 ? 1.7166 1.3211 1.3103 0.2444  -0.1539 -0.0840 404  ALA   D N   
11151 C  CA  . ALA   D 335 ? 1.7438 1.3458 1.3370 0.2444  -0.1533 -0.0851 404  ALA   D CA  
11152 C  C   . ALA   D 335 ? 1.7723 1.3507 1.3411 0.2555  -0.1577 -0.0865 404  ALA   D C   
11153 O  O   . ALA   D 335 ? 1.7935 1.3661 1.3568 0.2655  -0.1672 -0.0908 404  ALA   D O   
11154 C  CB  . ALA   D 335 ? 1.7484 1.3708 1.3663 0.2438  -0.1595 -0.0907 404  ALA   D CB  
11155 N  N   . THR   D 336 ? 1.7512 1.3158 1.3055 0.2540  -0.1513 -0.0830 405  THR   D N   
11156 C  CA  . THR   D 336 ? 1.8367 1.3792 1.3685 0.2644  -0.1555 -0.0845 405  THR   D CA  
11157 C  C   . THR   D 336 ? 1.9170 1.4668 1.4596 0.2713  -0.1659 -0.0916 405  THR   D C   
11158 O  O   . THR   D 336 ? 1.9156 1.4605 1.4537 0.2814  -0.1758 -0.0962 405  THR   D O   
11159 C  CB  . THR   D 336 ? 1.7805 1.3078 1.2965 0.2609  -0.1465 -0.0796 405  THR   D CB  
11160 O  OG1 . THR   D 336 ? 1.8895 1.4305 1.4219 0.2532  -0.1433 -0.0799 405  THR   D OG1 
11161 C  CG2 . THR   D 336 ? 1.7514 1.2698 1.2561 0.2548  -0.1362 -0.0726 405  THR   D CG2 
11162 N  N   . LYS   D 337 ? 1.9795 1.5417 1.5372 0.2659  -0.1639 -0.0927 406  LYS   D N   
11163 C  CA  . LYS   D 337 ? 1.9889 1.5589 1.5583 0.2720  -0.1729 -0.0993 406  LYS   D CA  
11164 C  C   . LYS   D 337 ? 2.0103 1.6012 1.6032 0.2719  -0.1797 -0.1037 406  LYS   D C   
11165 O  O   . LYS   D 337 ? 2.0060 1.6042 1.6047 0.2675  -0.1776 -0.1017 406  LYS   D O   
11166 C  CB  . LYS   D 337 ? 2.0697 1.6466 1.6482 0.2662  -0.1682 -0.0989 406  LYS   D CB  
11167 N  N   . LYS   D 338 ? 2.0593 1.6598 1.6663 0.2772  -0.1880 -0.1099 407  LYS   D N   
11168 C  CA  . LYS   D 338 ? 2.0402 1.6604 1.6708 0.2777  -0.1950 -0.1146 407  LYS   D CA  
11169 C  C   . LYS   D 338 ? 2.1703 1.8139 1.8278 0.2691  -0.1915 -0.1155 407  LYS   D C   
11170 O  O   . LYS   D 338 ? 2.1147 1.7763 1.7927 0.2658  -0.1937 -0.1174 407  LYS   D O   
11171 C  CB  . LYS   D 338 ? 1.9605 1.5761 1.5904 0.2903  -0.2077 -0.1215 407  LYS   D CB  
11172 C  CG  . LYS   D 338 ? 1.8991 1.4880 1.4993 0.3001  -0.2106 -0.1211 407  LYS   D CG  
11173 C  CD  . LYS   D 338 ? 1.9242 1.4993 1.5068 0.3044  -0.2126 -0.1194 407  LYS   D CD  
11174 C  CE  . LYS   D 338 ? 1.7817 1.3296 1.3343 0.3149  -0.2159 -0.1192 407  LYS   D CE  
11175 N  NZ  . LYS   D 338 ? 1.7048 1.2386 1.2393 0.3193  -0.2175 -0.1174 407  LYS   D NZ  
11176 N  N   . ASP   D 339 ? 2.5198 2.1629 2.1771 0.2654  -0.1860 -0.1142 408  ASP   D N   
11177 C  CA  . ASP   D 339 ? 2.5460 2.2096 2.2266 0.2571  -0.1817 -0.1145 408  ASP   D CA  
11178 C  C   . ASP   D 339 ? 2.5087 2.1836 2.1980 0.2455  -0.1733 -0.1097 408  ASP   D C   
11179 O  O   . ASP   D 339 ? 2.4927 2.1877 2.2047 0.2395  -0.1720 -0.1108 408  ASP   D O   
11180 C  CB  . ASP   D 339 ? 2.5821 2.2393 2.2565 0.2561  -0.1774 -0.1137 408  ASP   D CB  
11181 C  CG  . ASP   D 339 ? 2.5935 2.2286 2.2411 0.2555  -0.1713 -0.1085 408  ASP   D CG  
11182 O  OD1 . ASP   D 339 ? 2.5689 2.1933 2.2025 0.2565  -0.1706 -0.1056 408  ASP   D OD1 
11183 O  OD2 . ASP   D 339 ? 2.5861 2.2142 2.2266 0.2540  -0.1671 -0.1071 408  ASP   D OD2 
11184 N  N   . MET   D 340 ? 2.2573 1.9194 1.9291 0.2425  -0.1677 -0.1043 409  MET   D N   
11185 C  CA  . MET   D 340 ? 2.0500 1.7208 1.7280 0.2316  -0.1593 -0.0993 409  MET   D CA  
11186 C  C   . MET   D 340 ? 1.8889 1.5807 1.5901 0.2284  -0.1622 -0.1016 409  MET   D C   
11187 O  O   . MET   D 340 ? 1.8687 1.5627 1.5740 0.2353  -0.1705 -0.1057 409  MET   D O   
11188 C  CB  . MET   D 340 ? 1.9356 1.5892 1.5919 0.2318  -0.1554 -0.0943 409  MET   D CB  
11189 C  CG  . MET   D 340 ? 1.9417 1.5715 1.5724 0.2370  -0.1538 -0.0924 409  MET   D CG  
11190 S  SD  . MET   D 340 ? 1.9958 1.6214 1.6214 0.2268  -0.1421 -0.0867 409  MET   D SD  
11191 C  CE  . MET   D 340 ? 1.7796 1.4044 1.4011 0.2184  -0.1335 -0.0800 409  MET   D CE  
11192 N  N   . SER   D 341 ? 1.8340 1.5410 1.5503 0.2180  -0.1554 -0.0991 410  SER   D N   
11193 C  CA  . SER   D 341 ? 1.7262 1.4533 1.4647 0.2137  -0.1568 -0.1006 410  SER   D CA  
11194 C  C   . SER   D 341 ? 1.6580 1.3913 1.3996 0.2023  -0.1473 -0.0949 410  SER   D C   
11195 O  O   . SER   D 341 ? 1.5743 1.3082 1.3160 0.1962  -0.1408 -0.0924 410  SER   D O   
11196 C  CB  . SER   D 341 ? 1.7133 1.4564 1.4730 0.2145  -0.1605 -0.1056 410  SER   D CB  
11197 O  OG  . SER   D 341 ? 1.6468 1.4101 1.4288 0.2081  -0.1592 -0.1060 410  SER   D OG  
11198 N  N   . PRO   D 342 ? 1.6666 1.4030 1.4093 0.1995  -0.1462 -0.0927 411  PRO   D N   
11199 C  CA  . PRO   D 342 ? 1.6294 1.3646 1.3712 0.2062  -0.1535 -0.0953 411  PRO   D CA  
11200 C  C   . PRO   D 342 ? 1.6224 1.3351 1.3392 0.2151  -0.1567 -0.0949 411  PRO   D C   
11201 O  O   . PRO   D 342 ? 1.6169 1.3147 1.3157 0.2138  -0.1508 -0.0907 411  PRO   D O   
11202 C  CB  . PRO   D 342 ? 1.5371 1.2818 1.2863 0.1982  -0.1485 -0.0916 411  PRO   D CB  
11203 C  CG  . PRO   D 342 ? 1.5349 1.2733 1.2744 0.1905  -0.1386 -0.0856 411  PRO   D CG  
11204 C  CD  . PRO   D 342 ? 1.6123 1.3507 1.3537 0.1896  -0.1370 -0.0867 411  PRO   D CD  
11205 N  N   . GLN   D 343 ? 1.5927 1.3019 1.3077 0.2244  -0.1662 -0.0994 412  GLN   D N   
11206 C  CA  . GLN   D 343 ? 1.6717 1.3587 1.3621 0.2339  -0.1700 -0.0995 412  GLN   D CA  
11207 C  C   . GLN   D 343 ? 1.6522 1.3276 1.3261 0.2319  -0.1645 -0.0941 412  GLN   D C   
11208 O  O   . GLN   D 343 ? 1.6565 1.3116 1.3071 0.2359  -0.1621 -0.0914 412  GLN   D O   
11209 C  CB  . GLN   D 343 ? 1.6909 1.3777 1.3847 0.2444  -0.1823 -0.1060 412  GLN   D CB  
11210 C  CG  . GLN   D 343 ? 1.6763 1.3619 1.3731 0.2510  -0.1885 -0.1110 412  GLN   D CG  
11211 C  CD  . GLN   D 343 ? 1.7694 1.4325 1.4407 0.2564  -0.1871 -0.1092 412  GLN   D CD  
11212 O  OE1 . GLN   D 343 ? 1.7909 1.4358 1.4411 0.2634  -0.1899 -0.1086 412  GLN   D OE1 
11213 N  NE2 . GLN   D 343 ? 1.8825 1.5458 1.5546 0.2530  -0.1822 -0.1081 412  GLN   D NE2 
11214 N  N   . LYS   D 344 ? 1.6018 1.2898 1.2876 0.2256  -0.1619 -0.0924 413  LYS   D N   
11215 C  CA  . LYS   D 344 ? 1.5613 1.2409 1.2343 0.2237  -0.1569 -0.0875 413  LYS   D CA  
11216 C  C   . LYS   D 344 ? 1.5332 1.2291 1.2220 0.2119  -0.1490 -0.0837 413  LYS   D C   
11217 O  O   . LYS   D 344 ? 1.5451 1.2606 1.2564 0.2074  -0.1507 -0.0862 413  LYS   D O   
11218 C  CB  . LYS   D 344 ? 1.5605 1.2358 1.2290 0.2319  -0.1653 -0.0907 413  LYS   D CB  
11219 N  N   . PHE   D 345 ? 1.5168 1.2047 1.1941 0.2069  -0.1403 -0.0777 414  PHE   D N   
11220 C  CA  . PHE   D 345 ? 1.4800 1.1824 1.1710 0.1966  -0.1335 -0.0741 414  PHE   D CA  
11221 C  C   . PHE   D 345 ? 1.4615 1.1513 1.1362 0.1956  -0.1270 -0.0685 414  PHE   D C   
11222 O  O   . PHE   D 345 ? 1.4871 1.1568 1.1398 0.2023  -0.1269 -0.0672 414  PHE   D O   
11223 C  CB  . PHE   D 345 ? 1.4975 1.2105 1.2006 0.1872  -0.1270 -0.0721 414  PHE   D CB  
11224 C  CG  . PHE   D 345 ? 1.5001 1.1981 1.1871 0.1856  -0.1203 -0.0682 414  PHE   D CG  
11225 C  CD1 . PHE   D 345 ? 1.4608 1.1484 1.1386 0.1913  -0.1234 -0.0706 414  PHE   D CD1 
11226 C  CD2 . PHE   D 345 ? 1.4910 1.1857 1.1730 0.1781  -0.1109 -0.0621 414  PHE   D CD2 
11227 C  CE1 . PHE   D 345 ? 1.4866 1.1602 1.1499 0.1894  -0.1171 -0.0669 414  PHE   D CE1 
11228 C  CE2 . PHE   D 345 ? 1.4692 1.1503 1.1376 0.1761  -0.1046 -0.0584 414  PHE   D CE2 
11229 C  CZ  . PHE   D 345 ? 1.4928 1.1632 1.1517 0.1817  -0.1077 -0.0608 414  PHE   D CZ  
11230 N  N   . TRP   D 346 ? 1.3870 1.0885 1.0725 0.1873  -0.1214 -0.0652 415  TRP   D N   
11231 C  CA  . TRP   D 346 ? 1.3896 1.0817 1.0628 0.1847  -0.1138 -0.0595 415  TRP   D CA  
11232 C  C   . TRP   D 346 ? 1.3677 1.0656 1.0472 0.1736  -0.1036 -0.0543 415  TRP   D C   
11233 O  O   . TRP   D 346 ? 1.3976 1.1124 1.0959 0.1664  -0.1028 -0.0552 415  TRP   D O   
11234 C  CB  . TRP   D 346 ? 1.3926 1.0918 1.0715 0.1852  -0.1159 -0.0597 415  TRP   D CB  
11235 C  CG  . TRP   D 346 ? 1.4043 1.0973 1.0769 0.1960  -0.1262 -0.0647 415  TRP   D CG  
11236 C  CD1 . TRP   D 346 ? 1.4197 1.1227 1.1053 0.1998  -0.1357 -0.0709 415  TRP   D CD1 
11237 C  CD2 . TRP   D 346 ? 1.3968 1.0716 1.0484 0.2045  -0.1282 -0.0641 415  TRP   D CD2 
11238 N  NE1 . TRP   D 346 ? 1.4033 1.0961 1.0782 0.2102  -0.1442 -0.0745 415  TRP   D NE1 
11239 C  CE2 . TRP   D 346 ? 1.3993 1.0742 1.0524 0.2134  -0.1398 -0.0703 415  TRP   D CE2 
11240 C  CE3 . TRP   D 346 ? 1.4137 1.0721 1.0455 0.2056  -0.1212 -0.0588 415  TRP   D CE3 
11241 C  CZ2 . TRP   D 346 ? 1.4321 1.0907 1.0667 0.2234  -0.1452 -0.0716 415  TRP   D CZ2 
11242 C  CZ3 . TRP   D 346 ? 1.4675 1.1094 1.0803 0.2157  -0.1259 -0.0599 415  TRP   D CZ3 
11243 C  CH2 . TRP   D 346 ? 1.4487 1.0906 1.0626 0.2246  -0.1380 -0.0663 415  TRP   D CH2 
11244 N  N   . GLY   D 347 ? 1.3025 0.9857 0.9660 0.1724  -0.0960 -0.0490 416  GLY   D N   
11245 C  CA  . GLY   D 347 ? 1.2927 0.9803 0.9616 0.1620  -0.0863 -0.0439 416  GLY   D CA  
11246 C  C   . GLY   D 347 ? 1.3142 0.9996 0.9794 0.1590  -0.0799 -0.0390 416  GLY   D C   
11247 O  O   . GLY   D 347 ? 1.3591 1.0268 1.0054 0.1627  -0.0757 -0.0357 416  GLY   D O   
11248 N  N   . LEU   D 348 ? 1.3358 1.0389 1.0187 0.1525  -0.0789 -0.0386 417  LEU   D N   
11249 C  CA  . LEU   D 348 ? 1.2978 1.0016 0.9798 0.1502  -0.0740 -0.0347 417  LEU   D CA  
11250 C  C   . LEU   D 348 ? 1.2653 0.9736 0.9537 0.1397  -0.0641 -0.0293 417  LEU   D C   
11251 O  O   . LEU   D 348 ? 1.2741 0.9978 0.9798 0.1320  -0.0635 -0.0298 417  LEU   D O   
11252 C  CB  . LEU   D 348 ? 1.2715 0.9919 0.9692 0.1499  -0.0795 -0.0379 417  LEU   D CB  
11253 C  CG  . LEU   D 348 ? 1.2746 0.9990 0.9766 0.1571  -0.0904 -0.0445 417  LEU   D CG  
11254 C  CD1 . LEU   D 348 ? 1.2375 0.9798 0.9575 0.1553  -0.0951 -0.0473 417  LEU   D CD1 
11255 C  CD2 . LEU   D 348 ? 1.3365 1.0411 1.0168 0.1685  -0.0950 -0.0461 417  LEU   D CD2 
11256 N  N   . THR   D 349 ? 1.2814 0.9763 0.9563 0.1395  -0.0565 -0.0241 418  THR   D N   
11257 C  CA  . THR   D 349 ? 1.3040 1.0023 0.9852 0.1297  -0.0473 -0.0190 418  THR   D CA  
11258 C  C   . THR   D 349 ? 1.3077 1.0233 1.0061 0.1228  -0.0451 -0.0175 418  THR   D C   
11259 O  O   . THR   D 349 ? 1.3272 1.0471 1.0273 0.1263  -0.0485 -0.0189 418  THR   D O   
11260 C  CB  . THR   D 349 ? 1.3116 0.9905 0.9746 0.1309  -0.0390 -0.0136 418  THR   D CB  
11261 O  OG1 . THR   D 349 ? 1.3131 0.9982 0.9859 0.1208  -0.0303 -0.0088 418  THR   D OG1 
11262 C  CG2 . THR   D 349 ? 1.3794 1.0474 1.0283 0.1384  -0.0385 -0.0124 418  THR   D CG2 
11263 N  N   . ARG   D 350 ? 1.3040 1.0289 1.0149 0.1129  -0.0396 -0.0147 419  ARG   D N   
11264 C  CA  . ARG   D 350 ? 1.2862 1.0299 1.0160 0.1057  -0.0387 -0.0142 419  ARG   D CA  
11265 C  C   . ARG   D 350 ? 1.3310 1.0726 1.0579 0.1055  -0.0334 -0.0102 419  ARG   D C   
11266 O  O   . ARG   D 350 ? 1.2725 1.0259 1.0092 0.1048  -0.0357 -0.0112 419  ARG   D O   
11267 C  CB  . ARG   D 350 ? 1.2231 0.9758 0.9656 0.0957  -0.0346 -0.0124 419  ARG   D CB  
11268 C  CG  . ARG   D 350 ? 1.1892 0.9621 0.9516 0.0899  -0.0372 -0.0142 419  ARG   D CG  
11269 C  CD  . ARG   D 350 ? 1.2527 1.0319 1.0251 0.0801  -0.0313 -0.0108 419  ARG   D CD  
11270 N  NE  . ARG   D 350 ? 1.2601 1.0413 1.0353 0.0764  -0.0252 -0.0064 419  ARG   D NE  
11271 C  CZ  . ARG   D 350 ? 1.2587 1.0298 1.0271 0.0740  -0.0175 -0.0015 419  ARG   D CZ  
11272 N  NH1 . ARG   D 350 ? 1.2982 1.0548 1.0546 0.0753  -0.0149 -0.0003 419  ARG   D NH1 
11273 N  NH2 . ARG   D 350 ? 1.2952 1.0710 1.0695 0.0699  -0.0121 0.0023  419  ARG   D NH2 
11274 N  N   . SER   D 351 ? 1.3726 1.0988 1.0857 0.1060  -0.0259 -0.0055 420  SER   D N   
11275 C  CA  . SER   D 351 ? 1.3288 1.0517 1.0385 0.1055  -0.0193 -0.0010 420  SER   D CA  
11276 C  C   . SER   D 351 ? 1.3963 1.1152 1.0973 0.1142  -0.0239 -0.0030 420  SER   D C   
11277 O  O   . SER   D 351 ? 1.4496 1.1715 1.1526 0.1135  -0.0204 -0.0005 420  SER   D O   
11278 C  CB  . SER   D 351 ? 1.2718 0.9769 0.9669 0.1055  -0.0106 0.0041  420  SER   D CB  
11279 O  OG  . SER   D 351 ? 1.4202 1.1100 1.0992 0.1123  -0.0137 0.0021  420  SER   D OG  
11280 N  N   . ALA   D 352 ? 1.3880 1.0999 1.0794 0.1226  -0.0317 -0.0076 421  ALA   D N   
11281 C  CA  . ALA   D 352 ? 1.4173 1.1232 1.0986 0.1318  -0.0372 -0.0100 421  ALA   D CA  
11282 C  C   . ALA   D 352 ? 1.4125 1.1362 1.1099 0.1314  -0.0451 -0.0145 421  ALA   D C   
11283 O  O   . ALA   D 352 ? 1.4438 1.1641 1.1349 0.1386  -0.0502 -0.0168 421  ALA   D O   
11284 C  CB  . ALA   D 352 ? 1.4670 1.1558 1.1298 0.1415  -0.0425 -0.0130 421  ALA   D CB  
11285 N  N   . LEU   D 353 ? 1.4107 1.1525 1.1281 0.1234  -0.0462 -0.0158 422  LEU   D N   
11286 C  CA  . LEU   D 353 ? 1.3574 1.1156 1.0902 0.1232  -0.0539 -0.0205 422  LEU   D CA  
11287 C  C   . LEU   D 353 ? 1.3327 1.1071 1.0821 0.1154  -0.0505 -0.0184 422  LEU   D C   
11288 O  O   . LEU   D 353 ? 1.3077 1.0834 1.0602 0.1087  -0.0424 -0.0136 422  LEU   D O   
11289 C  CB  . LEU   D 353 ? 1.3470 1.1133 1.0896 0.1215  -0.0592 -0.0247 422  LEU   D CB  
11290 C  CG  . LEU   D 353 ? 1.3384 1.0918 1.0678 0.1300  -0.0651 -0.0283 422  LEU   D CG  
11291 C  CD1 . LEU   D 353 ? 1.2800 1.0430 1.0211 0.1274  -0.0692 -0.0320 422  LEU   D CD1 
11292 C  CD2 . LEU   D 353 ? 1.2789 1.0278 1.0014 0.1394  -0.0727 -0.0320 422  LEU   D CD2 
11293 N  N   . LEU   D 354 ? 1.4123 1.1989 1.1728 0.1164  -0.0568 -0.0220 423  LEU   D N   
11294 C  CA  . LEU   D 354 ? 1.4258 1.2276 1.2014 0.1101  -0.0547 -0.0206 423  LEU   D CA  
11295 C  C   . LEU   D 354 ? 1.4466 1.2645 1.2385 0.1092  -0.0624 -0.0256 423  LEU   D C   
11296 O  O   . LEU   D 354 ? 1.4440 1.2606 1.2334 0.1161  -0.0696 -0.0295 423  LEU   D O   
11297 C  CB  . LEU   D 354 ? 1.4379 1.2327 1.2042 0.1142  -0.0524 -0.0182 423  LEU   D CB  
11298 C  CG  . LEU   D 354 ? 1.4811 1.2904 1.2615 0.1091  -0.0510 -0.0170 423  LEU   D CG  
11299 C  CD1 . LEU   D 354 ? 1.5139 1.3164 1.2870 0.1078  -0.0422 -0.0113 423  LEU   D CD1 
11300 C  CD2 . LEU   D 354 ? 1.4971 1.3103 1.2794 0.1150  -0.0593 -0.0214 423  LEU   D CD2 
11301 N  N   . PRO   D 355 ? 1.4435 1.2763 1.2522 0.1011  -0.0612 -0.0256 424  PRO   D N   
11302 C  CA  . PRO   D 355 ? 1.4387 1.2866 1.2631 0.1000  -0.0678 -0.0302 424  PRO   D CA  
11303 C  C   . PRO   D 355 ? 1.4538 1.3110 1.2864 0.0997  -0.0695 -0.0305 424  PRO   D C   
11304 O  O   . PRO   D 355 ? 1.4556 1.3139 1.2884 0.0962  -0.0640 -0.0265 424  PRO   D O   
11305 C  CB  . PRO   D 355 ? 1.4388 1.2977 1.2762 0.0911  -0.0644 -0.0291 424  PRO   D CB  
11306 C  CG  . PRO   D 355 ? 1.4419 1.2893 1.2687 0.0890  -0.0578 -0.0251 424  PRO   D CG  
11307 C  CD  . PRO   D 355 ? 1.4355 1.2710 1.2489 0.0928  -0.0541 -0.0217 424  PRO   D CD  
11308 N  N   . THR   D 356 ? 1.3599 1.2242 1.2001 0.1032  -0.0772 -0.0354 425  THR   D N   
11309 C  CA  . THR   D 356 ? 1.3220 1.1938 1.1690 0.1041  -0.0801 -0.0364 425  THR   D CA  
11310 C  C   . THR   D 356 ? 1.2799 1.1669 1.1445 0.1024  -0.0861 -0.0409 425  THR   D C   
11311 O  O   . THR   D 356 ? 1.2630 1.1520 1.1316 0.1034  -0.0896 -0.0442 425  THR   D O   
11312 C  CB  . THR   D 356 ? 1.3765 1.2351 1.2086 0.1135  -0.0842 -0.0378 425  THR   D CB  
11313 O  OG1 . THR   D 356 ? 1.3502 1.1989 1.1731 0.1203  -0.0895 -0.0413 425  THR   D OG1 
11314 C  CG2 . THR   D 356 ? 1.4088 1.2553 1.2262 0.1142  -0.0771 -0.0326 425  THR   D CG2 
11315 N  N   . ILE   D 357 ? 1.3165 1.2138 1.1912 0.1001  -0.0870 -0.0411 426  ILE   D N   
11316 C  CA  . ILE   D 357 ? 1.2862 1.1987 1.1788 0.0976  -0.0915 -0.0447 426  ILE   D CA  
11317 C  C   . ILE   D 357 ? 1.3081 1.2191 1.2001 0.1048  -0.0993 -0.0487 426  ILE   D C   
11318 O  O   . ILE   D 357 ? 1.3807 1.2911 1.2706 0.1058  -0.0992 -0.0475 426  ILE   D O   
11319 C  CB  . ILE   D 357 ? 1.2745 1.2003 1.1800 0.0893  -0.0868 -0.0418 426  ILE   D CB  
11320 C  CG1 . ILE   D 357 ? 1.2735 1.2006 1.1797 0.0821  -0.0795 -0.0378 426  ILE   D CG1 
11321 C  CG2 . ILE   D 357 ? 1.2925 1.2329 1.2155 0.0872  -0.0913 -0.0455 426  ILE   D CG2 
11322 C  CD1 . ILE   D 357 ? 1.3190 1.2574 1.2361 0.0746  -0.0751 -0.0348 426  ILE   D CD1 
11323 N  N   . PRO   D 358 ? 1.1823 1.0930 1.0769 0.1098  -0.1065 -0.0538 427  PRO   D N   
11324 C  CA  . PRO   D 358 ? 1.1598 1.0704 1.0568 0.1164  -0.1151 -0.0585 427  PRO   D CA  
11325 C  C   . PRO   D 358 ? 1.1781 1.0994 1.0867 0.1140  -0.1167 -0.0590 427  PRO   D C   
11326 O  O   . PRO   D 358 ? 1.1326 1.0495 1.0372 0.1196  -0.1221 -0.0611 427  PRO   D O   
11327 C  CB  . PRO   D 358 ? 1.0642 0.9808 0.9716 0.1175  -0.1200 -0.0631 427  PRO   D CB  
11328 C  CG  . PRO   D 358 ? 1.1496 1.0581 1.0473 0.1168  -0.1156 -0.0610 427  PRO   D CG  
11329 C  CD  . PRO   D 358 ? 1.1992 1.1061 1.0913 0.1106  -0.1065 -0.0550 427  PRO   D CD  
11330 N  N   . VAL   D 369 ? 1.5841 1.5647 1.5453 0.0693  -0.0844 -0.0388 438  VAL   D N   
11331 C  CA  . VAL   D 369 ? 1.5926 1.5750 1.5560 0.0648  -0.0809 -0.0377 438  VAL   D CA  
11332 C  C   . VAL   D 369 ? 1.6215 1.5969 1.5754 0.0622  -0.0742 -0.0329 438  VAL   D C   
11333 O  O   . VAL   D 369 ? 1.6217 1.5861 1.5629 0.0664  -0.0730 -0.0312 438  VAL   D O   
11334 C  CB  . VAL   D 369 ? 1.5444 1.5217 1.5047 0.0693  -0.0851 -0.0414 438  VAL   D CB  
11335 C  CG1 . VAL   D 369 ? 1.5169 1.5047 1.4913 0.0689  -0.0898 -0.0456 438  VAL   D CG1 
11336 C  CG2 . VAL   D 369 ? 1.5691 1.5337 1.5158 0.0776  -0.0889 -0.0428 438  VAL   D CG2 
11337 N  N   . ILE   D 370 ? 1.5078 1.4892 1.4679 0.0553  -0.0699 -0.0307 439  ILE   D N   
11338 C  CA  . ILE   D 370 ? 1.4161 1.3920 1.3697 0.0518  -0.0636 -0.0263 439  ILE   D CA  
11339 C  C   . ILE   D 370 ? 1.3360 1.3129 1.2919 0.0481  -0.0622 -0.0266 439  ILE   D C   
11340 O  O   . ILE   D 370 ? 1.3656 1.3506 1.3309 0.0462  -0.0648 -0.0293 439  ILE   D O   
11341 C  CB  . ILE   D 370 ? 1.3303 1.3133 1.2901 0.0464  -0.0592 -0.0226 439  ILE   D CB  
11342 C  CG1 . ILE   D 370 ? 1.4069 1.3875 1.3628 0.0506  -0.0602 -0.0221 439  ILE   D CG1 
11343 C  CG2 . ILE   D 370 ? 1.3268 1.3052 1.2821 0.0423  -0.0529 -0.0182 439  ILE   D CG2 
11344 C  CD1 . ILE   D 370 ? 1.4287 1.4149 1.3895 0.0459  -0.0557 -0.0183 439  ILE   D CD1 
11345 N  N   . LEU   D 371 ? 1.2751 1.2431 1.2220 0.0473  -0.0581 -0.0238 440  LEU   D N   
11346 C  CA  . LEU   D 371 ? 1.2194 1.1875 1.1677 0.0433  -0.0565 -0.0237 440  LEU   D CA  
11347 C  C   . LEU   D 371 ? 1.2632 1.2419 1.2226 0.0352  -0.0534 -0.0216 440  LEU   D C   
11348 O  O   . LEU   D 371 ? 1.2456 1.2248 1.2055 0.0319  -0.0493 -0.0179 440  LEU   D O   
11349 C  CB  . LEU   D 371 ? 1.2167 1.1716 1.1521 0.0447  -0.0530 -0.0213 440  LEU   D CB  
11350 C  CG  . LEU   D 371 ? 1.1766 1.1203 1.1009 0.0513  -0.0559 -0.0239 440  LEU   D CG  
11351 C  CD1 . LEU   D 371 ? 1.1552 1.1007 1.0827 0.0494  -0.0573 -0.0260 440  LEU   D CD1 
11352 C  CD2 . LEU   D 371 ? 1.2302 1.1732 1.1529 0.0584  -0.0618 -0.0275 440  LEU   D CD2 
11353 N  N   . CYS   D 372 ? 1.2720 1.2585 1.2401 0.0323  -0.0553 -0.0239 441  CYS   D N   
11354 C  CA  . CYS   D 372 ? 1.2860 1.2825 1.2645 0.0252  -0.0533 -0.0226 441  CYS   D CA  
11355 C  C   . CYS   D 372 ? 1.2648 1.2585 1.2417 0.0207  -0.0506 -0.0212 441  CYS   D C   
11356 O  O   . CYS   D 372 ? 1.2757 1.2604 1.2443 0.0228  -0.0503 -0.0216 441  CYS   D O   
11357 C  CB  . CYS   D 372 ? 1.2763 1.2832 1.2654 0.0248  -0.0567 -0.0258 441  CYS   D CB  
11358 S  SG  . CYS   D 372 ? 1.3836 1.3967 1.3782 0.0276  -0.0594 -0.0268 441  CYS   D SG  
11359 N  N   . LEU   D 373 ? 1.3004 1.3019 1.2855 0.0145  -0.0490 -0.0198 442  LEU   D N   
11360 C  CA  . LEU   D 373 ? 1.2695 1.2694 1.2545 0.0096  -0.0470 -0.0188 442  LEU   D CA  
11361 C  C   . LEU   D 373 ? 1.2554 1.2657 1.2506 0.0044  -0.0476 -0.0194 442  LEU   D C   
11362 O  O   . LEU   D 373 ? 1.2305 1.2400 1.2258 0.0009  -0.0470 -0.0194 442  LEU   D O   
11363 C  CB  . LEU   D 373 ? 1.2498 1.2438 1.2304 0.0069  -0.0428 -0.0147 442  LEU   D CB  
11364 C  CG  . LEU   D 373 ? 1.2537 1.2518 1.2382 0.0051  -0.0404 -0.0117 442  LEU   D CG  
11365 C  CD1 . LEU   D 373 ? 1.2810 1.2876 1.2751 -0.0018 -0.0394 -0.0101 442  LEU   D CD1 
11366 C  CD2 . LEU   D 373 ? 1.2184 1.2069 1.1949 0.0062  -0.0366 -0.0086 442  LEU   D CD2 
11367 O  OXT . LEU   D 373 ? 1.2177 1.2369 1.2207 0.0037  -0.0488 -0.0200 442  LEU   D OXT 
11368 N  N   . SER   E 2   ? 1.2694 1.4061 1.4255 -0.0631 -0.0398 0.0210  2    SER   E N   
11369 C  CA  . SER   E 2   ? 1.2687 1.4118 1.4306 -0.0646 -0.0441 0.0204  2    SER   E CA  
11370 C  C   . SER   E 2   ? 1.2850 1.4273 1.4491 -0.0687 -0.0492 0.0187  2    SER   E C   
11371 O  O   . SER   E 2   ? 1.2343 1.3720 1.3978 -0.0711 -0.0492 0.0185  2    SER   E O   
11372 C  CB  . SER   E 2   ? 1.1640 1.3085 1.3194 -0.0613 -0.0457 0.0188  2    SER   E CB  
11373 O  OG  . SER   E 2   ? 1.0732 1.2125 1.2191 -0.0605 -0.0472 0.0163  2    SER   E OG  
11374 N  N   . TYR   E 3   ? 1.2413 1.3877 1.4073 -0.0694 -0.0537 0.0176  3    TYR   E N   
11375 C  CA  . TYR   E 3   ? 1.1972 1.3428 1.3644 -0.0728 -0.0593 0.0159  3    TYR   E CA  
11376 C  C   . TYR   E 3   ? 1.2146 1.3598 1.3742 -0.0713 -0.0628 0.0136  3    TYR   E C   
11377 O  O   . TYR   E 3   ? 1.2579 1.4071 1.4175 -0.0689 -0.0624 0.0140  3    TYR   E O   
11378 C  CB  . TYR   E 3   ? 1.2100 1.3612 1.3897 -0.0756 -0.0615 0.0172  3    TYR   E CB  
11379 C  CG  . TYR   E 3   ? 1.1943 1.3475 1.3829 -0.0763 -0.0566 0.0200  3    TYR   E CG  
11380 C  CD1 . TYR   E 3   ? 1.2049 1.3537 1.3948 -0.0786 -0.0547 0.0205  3    TYR   E CD1 
11381 C  CD2 . TYR   E 3   ? 1.2493 1.4085 1.4446 -0.0744 -0.0534 0.0222  3    TYR   E CD2 
11382 C  CE1 . TYR   E 3   ? 1.2502 1.4002 1.4481 -0.0792 -0.0494 0.0232  3    TYR   E CE1 
11383 C  CE2 . TYR   E 3   ? 1.2838 1.4443 1.4869 -0.0748 -0.0482 0.0250  3    TYR   E CE2 
11384 C  CZ  . TYR   E 3   ? 1.2775 1.4334 1.4820 -0.0772 -0.0460 0.0256  3    TYR   E CZ  
11385 O  OH  . TYR   E 3   ? 1.2512 1.4079 1.4635 -0.0777 -0.0402 0.0285  3    TYR   E OH  
11386 N  N   . ASN   E 4   ? 1.1652 1.3052 1.3182 -0.0725 -0.0661 0.0114  4    ASN   E N   
11387 C  CA  . ASN   E 4   ? 1.1688 1.3073 1.3134 -0.0709 -0.0684 0.0094  4    ASN   E CA  
11388 C  C   . ASN   E 4   ? 1.1882 1.3237 1.3310 -0.0734 -0.0740 0.0076  4    ASN   E C   
11389 O  O   . ASN   E 4   ? 1.2136 1.3479 1.3612 -0.0765 -0.0763 0.0077  4    ASN   E O   
11390 C  CB  . ASN   E 4   ? 1.1692 1.3031 1.3045 -0.0682 -0.0655 0.0082  4    ASN   E CB  
11391 C  CG  . ASN   E 4   ? 1.1435 1.2793 1.2799 -0.0654 -0.0605 0.0098  4    ASN   E CG  
11392 O  OD1 . ASN   E 4   ? 1.0993 1.2382 1.2347 -0.0628 -0.0595 0.0099  4    ASN   E OD1 
11393 N  ND2 . ASN   E 4   ? 1.1401 1.2737 1.2782 -0.0659 -0.0575 0.0110  4    ASN   E ND2 
11394 N  N   . TYR   E 5   ? 1.1556 1.2895 1.2911 -0.0720 -0.0760 0.0060  5    TYR   E N   
11395 C  CA  . TYR   E 5   ? 1.1276 1.2589 1.2605 -0.0736 -0.0816 0.0045  5    TYR   E CA  
11396 C  C   . TYR   E 5   ? 1.1196 1.2453 1.2405 -0.0718 -0.0814 0.0025  5    TYR   E C   
11397 O  O   . TYR   E 5   ? 1.1205 1.2479 1.2381 -0.0692 -0.0796 0.0024  5    TYR   E O   
11398 C  CB  . TYR   E 5   ? 1.0934 1.2304 1.2319 -0.0734 -0.0840 0.0054  5    TYR   E CB  
11399 C  CG  . TYR   E 5   ? 1.0646 1.1991 1.1989 -0.0739 -0.0896 0.0039  5    TYR   E CG  
11400 C  CD1 . TYR   E 5   ? 1.0762 1.2081 1.2013 -0.0716 -0.0895 0.0028  5    TYR   E CD1 
11401 C  CD2 . TYR   E 5   ? 1.0931 1.2275 1.2327 -0.0766 -0.0950 0.0035  5    TYR   E CD2 
11402 C  CE1 . TYR   E 5   ? 1.0854 1.2140 1.2053 -0.0717 -0.0944 0.0016  5    TYR   E CE1 
11403 C  CE2 . TYR   E 5   ? 1.1266 1.2577 1.2612 -0.0766 -0.1005 0.0020  5    TYR   E CE2 
11404 C  CZ  . TYR   E 5   ? 1.1049 1.2328 1.2290 -0.0740 -0.1001 0.0011  5    TYR   E CZ  
11405 O  OH  . TYR   E 5   ? 1.0781 1.2017 1.1958 -0.0737 -0.1053 -0.0002 5    TYR   E OH  
11406 N  N   . VAL   E 6   ? 1.0785 1.1974 1.1934 -0.0729 -0.0829 0.0009  6    VAL   E N   
11407 C  CA  . VAL   E 6   ? 1.0504 1.1634 1.1540 -0.0711 -0.0826 -0.0011 6    VAL   E CA  
11408 C  C   . VAL   E 6   ? 1.0304 1.1401 1.1292 -0.0718 -0.0875 -0.0023 6    VAL   E C   
11409 O  O   . VAL   E 6   ? 1.0494 1.1578 1.1513 -0.0742 -0.0922 -0.0026 6    VAL   E O   
11410 C  CB  . VAL   E 6   ? 1.0042 1.1111 1.1027 -0.0715 -0.0812 -0.0022 6    VAL   E CB  
11411 C  CG1 . VAL   E 6   ? 0.9696 1.0785 1.0697 -0.0697 -0.0760 -0.0013 6    VAL   E CG1 
11412 C  CG2 . VAL   E 6   ? 1.0458 1.1504 1.1484 -0.0749 -0.0846 -0.0022 6    VAL   E CG2 
11413 N  N   . VAL   E 7   ? 0.9986 1.1067 1.0902 -0.0694 -0.0867 -0.0031 7    VAL   E N   
11414 C  CA  . VAL   E 7   ? 1.0312 1.1340 1.1152 -0.0694 -0.0907 -0.0044 7    VAL   E CA  
11415 C  C   . VAL   E 7   ? 1.0418 1.1390 1.1149 -0.0670 -0.0879 -0.0058 7    VAL   E C   
11416 O  O   . VAL   E 7   ? 1.0148 1.1139 1.0878 -0.0652 -0.0830 -0.0056 7    VAL   E O   
11417 C  CB  . VAL   E 7   ? 1.0224 1.1295 1.1098 -0.0690 -0.0932 -0.0034 7    VAL   E CB  
11418 C  CG1 . VAL   E 7   ? 1.0248 1.1353 1.1109 -0.0663 -0.0890 -0.0027 7    VAL   E CG1 
11419 C  CG2 . VAL   E 7   ? 1.0527 1.1535 1.1332 -0.0694 -0.0990 -0.0048 7    VAL   E CG2 
11420 N  N   . THR   E 8   ? 1.0638 1.1535 1.1275 -0.0668 -0.0910 -0.0072 8    THR   E N   
11421 C  CA  . THR   E 8   ? 1.0353 1.1184 1.0879 -0.0646 -0.0884 -0.0086 8    THR   E CA  
11422 C  C   . THR   E 8   ? 1.0338 1.1166 1.0820 -0.0627 -0.0876 -0.0082 8    THR   E C   
11423 O  O   . THR   E 8   ? 1.1051 1.1854 1.1503 -0.0630 -0.0919 -0.0083 8    THR   E O   
11424 C  CB  . THR   E 8   ? 1.0113 1.0849 1.0550 -0.0654 -0.0920 -0.0104 8    THR   E CB  
11425 O  OG1 . THR   E 8   ? 1.0666 1.1401 1.1146 -0.0673 -0.0924 -0.0106 8    THR   E OG1 
11426 C  CG2 . THR   E 8   ? 0.9852 1.0516 1.0171 -0.0628 -0.0888 -0.0117 8    THR   E CG2 
11427 N  N   . ALA   E 9   ? 0.9644 1.0498 1.0124 -0.0606 -0.0822 -0.0079 9    ALA   E N   
11428 C  CA  . ALA   E 9   ? 0.9987 1.0829 1.0418 -0.0586 -0.0804 -0.0076 9    ALA   E CA  
11429 C  C   . ALA   E 9   ? 1.0038 1.0790 1.0348 -0.0569 -0.0785 -0.0090 9    ALA   E C   
11430 O  O   . ALA   E 9   ? 1.0400 1.1121 1.0650 -0.0553 -0.0772 -0.0088 9    ALA   E O   
11431 C  CB  . ALA   E 9   ? 0.9962 1.0878 1.0462 -0.0574 -0.0757 -0.0066 9    ALA   E CB  
11432 N  N   . GLN   E 10  ? 0.9855 1.0562 1.0126 -0.0570 -0.0779 -0.0103 10   GLN   E N   
11433 C  CA  . GLN   E 10  ? 0.9806 1.0425 0.9962 -0.0552 -0.0757 -0.0116 10   GLN   E CA  
11434 C  C   . GLN   E 10  ? 0.9986 1.0552 1.0107 -0.0562 -0.0779 -0.0130 10   GLN   E C   
11435 O  O   . GLN   E 10  ? 1.0335 1.0944 1.0526 -0.0573 -0.0773 -0.0130 10   GLN   E O   
11436 C  CB  . GLN   E 10  ? 0.9655 1.0300 0.9824 -0.0530 -0.0689 -0.0116 10   GLN   E CB  
11437 C  CG  . GLN   E 10  ? 0.9873 1.0436 0.9943 -0.0511 -0.0657 -0.0130 10   GLN   E CG  
11438 C  CD  . GLN   E 10  ? 1.0528 1.0999 1.0475 -0.0499 -0.0666 -0.0132 10   GLN   E CD  
11439 O  OE1 . GLN   E 10  ? 1.1091 1.1569 1.1029 -0.0492 -0.0659 -0.0122 10   GLN   E OE1 
11440 N  NE2 . GLN   E 10  ? 1.1137 1.1516 1.0984 -0.0494 -0.0683 -0.0146 10   GLN   E NE2 
11441 N  N   . LYS   E 11  ? 1.0017 1.0485 1.0025 -0.0557 -0.0807 -0.0142 11   LYS   E N   
11442 C  CA  . LYS   E 11  ? 0.9879 1.0286 0.9843 -0.0565 -0.0829 -0.0157 11   LYS   E CA  
11443 C  C   . LYS   E 11  ? 1.0131 1.0517 1.0061 -0.0545 -0.0772 -0.0166 11   LYS   E C   
11444 O  O   . LYS   E 11  ? 1.0304 1.0713 1.0237 -0.0525 -0.0719 -0.0161 11   LYS   E O   
11445 C  CB  . LYS   E 11  ? 1.0241 1.0543 1.0087 -0.0564 -0.0881 -0.0169 11   LYS   E CB  
11446 N  N   . PRO   E 12  ? 1.0188 1.0535 1.0099 -0.0552 -0.0781 -0.0178 12   PRO   E N   
11447 C  CA  . PRO   E 12  ? 1.0044 1.0353 0.9904 -0.0529 -0.0732 -0.0189 12   PRO   E CA  
11448 C  C   . PRO   E 12  ? 0.9985 1.0219 0.9730 -0.0500 -0.0702 -0.0195 12   PRO   E C   
11449 O  O   . PRO   E 12  ? 1.0546 1.0697 1.0191 -0.0498 -0.0736 -0.0200 12   PRO   E O   
11450 C  CB  . PRO   E 12  ? 1.0651 1.0899 1.0474 -0.0542 -0.0767 -0.0202 12   PRO   E CB  
11451 C  CG  . PRO   E 12  ? 1.0618 1.0914 1.0529 -0.0576 -0.0817 -0.0194 12   PRO   E CG  
11452 C  CD  . PRO   E 12  ? 1.0597 1.0946 1.0552 -0.0581 -0.0832 -0.0180 12   PRO   E CD  
11453 N  N   . THR   E 13  ? 0.9992 1.0248 0.9747 -0.0477 -0.0639 -0.0194 13   THR   E N   
11454 C  CA  . THR   E 13  ? 1.0010 1.0195 0.9663 -0.0449 -0.0599 -0.0198 13   THR   E CA  
11455 C  C   . THR   E 13  ? 1.1228 1.1341 1.0803 -0.0427 -0.0568 -0.0214 13   THR   E C   
11456 O  O   . THR   E 13  ? 1.1744 1.1774 1.1210 -0.0403 -0.0541 -0.0218 13   THR   E O   
11457 C  CB  . THR   E 13  ? 1.0245 1.0499 0.9963 -0.0436 -0.0544 -0.0186 13   THR   E CB  
11458 O  OG1 . THR   E 13  ? 1.0590 1.0892 1.0374 -0.0424 -0.0497 -0.0192 13   THR   E OG1 
11459 C  CG2 . THR   E 13  ? 1.0473 1.0817 1.0293 -0.0457 -0.0571 -0.0171 13   THR   E CG2 
11460 N  N   . ALA   E 14  ? 1.1360 1.1500 1.0987 -0.0432 -0.0567 -0.0222 14   ALA   E N   
11461 C  CA  . ALA   E 14  ? 1.0940 1.1021 1.0506 -0.0410 -0.0535 -0.0237 14   ALA   E CA  
11462 C  C   . ALA   E 14  ? 1.0833 1.0804 1.0283 -0.0414 -0.0582 -0.0250 14   ALA   E C   
11463 O  O   . ALA   E 14  ? 1.0722 1.0692 1.0187 -0.0442 -0.0643 -0.0249 14   ALA   E O   
11464 C  CB  . ALA   E 14  ? 1.1218 1.1370 1.0884 -0.0410 -0.0516 -0.0240 14   ALA   E CB  
11465 N  N   . VAL   E 15  ? 1.1482 1.1360 1.0819 -0.0386 -0.0553 -0.0262 15   VAL   E N   
11466 C  CA  . VAL   E 15  ? 1.1396 1.1151 1.0600 -0.0383 -0.0593 -0.0276 15   VAL   E CA  
11467 C  C   . VAL   E 15  ? 1.1941 1.1677 1.1146 -0.0380 -0.0590 -0.0290 15   VAL   E C   
11468 O  O   . VAL   E 15  ? 1.1854 1.1600 1.1068 -0.0355 -0.0532 -0.0295 15   VAL   E O   
11469 C  CB  . VAL   E 15  ? 1.0983 1.0632 1.0042 -0.0350 -0.0561 -0.0280 15   VAL   E CB  
11470 C  CG1 . VAL   E 15  ? 1.1541 1.1060 1.0460 -0.0343 -0.0604 -0.0297 15   VAL   E CG1 
11471 C  CG2 . VAL   E 15  ? 1.1432 1.1092 1.0481 -0.0352 -0.0568 -0.0266 15   VAL   E CG2 
11472 N  N   . ASN   E 16  ? 1.2540 1.2244 1.1737 -0.0406 -0.0652 -0.0297 16   ASN   E N   
11473 C  CA  . ASN   E 16  ? 1.3079 1.2756 1.2271 -0.0405 -0.0654 -0.0310 16   ASN   E CA  
11474 C  C   . ASN   E 16  ? 1.3069 1.2608 1.2115 -0.0398 -0.0688 -0.0328 16   ASN   E C   
11475 O  O   . ASN   E 16  ? 1.3537 1.3032 1.2552 -0.0388 -0.0680 -0.0340 16   ASN   E O   
11476 C  CB  . ASN   E 16  ? 1.3246 1.3000 1.2558 -0.0442 -0.0691 -0.0303 16   ASN   E CB  
11477 C  CG  . ASN   E 16  ? 1.3091 1.2830 1.2408 -0.0477 -0.0763 -0.0299 16   ASN   E CG  
11478 O  OD1 . ASN   E 16  ? 1.3037 1.2801 1.2364 -0.0483 -0.0777 -0.0290 16   ASN   E OD1 
11479 N  ND2 . ASN   E 16  ? 1.3040 1.2741 1.2356 -0.0501 -0.0809 -0.0307 16   ASN   E ND2 
11480 N  N   . GLY   E 17  ? 1.2124 1.1589 1.1078 -0.0399 -0.0728 -0.0330 17   GLY   E N   
11481 C  CA  . GLY   E 17  ? 1.2415 1.1739 1.1222 -0.0390 -0.0767 -0.0349 17   GLY   E CA  
11482 C  C   . GLY   E 17  ? 1.2556 1.1797 1.1240 -0.0371 -0.0781 -0.0350 17   GLY   E C   
11483 O  O   . GLY   E 17  ? 1.2701 1.1991 1.1428 -0.0383 -0.0795 -0.0337 17   GLY   E O   
11484 N  N   . CYS   E 18  ? 1.2675 1.1781 1.1198 -0.0339 -0.0774 -0.0366 18   CYS   E N   
11485 C  CA  . CYS   E 18  ? 1.2593 1.1597 1.0972 -0.0314 -0.0784 -0.0368 18   CYS   E CA  
11486 C  C   . CYS   E 18  ? 1.2892 1.1734 1.1095 -0.0288 -0.0804 -0.0390 18   CYS   E C   
11487 O  O   . CYS   E 18  ? 1.3632 1.2444 1.1801 -0.0264 -0.0754 -0.0397 18   CYS   E O   
11488 C  CB  . CYS   E 18  ? 1.3129 1.2163 1.1502 -0.0283 -0.0698 -0.0352 18   CYS   E CB  
11489 S  SG  . CYS   E 18  ? 1.4508 1.3554 1.2884 -0.0243 -0.0589 -0.0353 18   CYS   E SG  
11490 N  N   . VAL   E 19  ? 1.3331 1.2069 1.1424 -0.0291 -0.0878 -0.0401 19   VAL   E N   
11491 C  CA  . VAL   E 19  ? 1.2678 1.1249 1.0591 -0.0266 -0.0912 -0.0424 19   VAL   E CA  
11492 C  C   . VAL   E 19  ? 1.2592 1.1045 1.0345 -0.0239 -0.0941 -0.0427 19   VAL   E C   
11493 O  O   . VAL   E 19  ? 1.2735 1.1236 1.0532 -0.0253 -0.0966 -0.0416 19   VAL   E O   
11494 C  CB  . VAL   E 19  ? 1.2393 1.0941 1.0337 -0.0304 -0.1001 -0.0441 19   VAL   E CB  
11495 C  CG1 . VAL   E 19  ? 1.3022 1.1641 1.1070 -0.0317 -0.0965 -0.0441 19   VAL   E CG1 
11496 C  CG2 . VAL   E 19  ? 1.2141 1.0767 1.0202 -0.0349 -0.1075 -0.0435 19   VAL   E CG2 
11497 N  N   . THR   E 20  ? 1.2872 1.1164 1.0433 -0.0199 -0.0938 -0.0444 20   THR   E N   
11498 C  CA  . THR   E 20  ? 1.2894 1.1038 1.0266 -0.0167 -0.0974 -0.0452 20   THR   E CA  
11499 C  C   . THR   E 20  ? 1.3502 1.1535 1.0793 -0.0182 -0.1090 -0.0479 20   THR   E C   
11500 O  O   . THR   E 20  ? 1.3685 1.1733 1.1037 -0.0210 -0.1127 -0.0492 20   THR   E O   
11501 C  CB  . THR   E 20  ? 1.3520 1.1543 1.0717 -0.0107 -0.0890 -0.0452 20   THR   E CB  
11502 O  OG1 . THR   E 20  ? 1.2986 1.1003 1.0189 -0.0097 -0.0847 -0.0462 20   THR   E OG1 
11503 C  CG2 . THR   E 20  ? 1.3451 1.1549 1.0693 -0.0088 -0.0795 -0.0426 20   THR   E CG2 
11504 N  N   . GLY   E 21  ? 1.4646 1.2564 1.1797 -0.0163 -0.1150 -0.0488 21   GLY   E N   
11505 C  CA  . GLY   E 21  ? 1.4841 1.2641 1.1903 -0.0173 -0.1264 -0.0516 21   GLY   E CA  
11506 C  C   . GLY   E 21  ? 1.5110 1.2827 1.2071 -0.0161 -0.1339 -0.0522 21   GLY   E C   
11507 O  O   . GLY   E 21  ? 1.5053 1.2748 1.1939 -0.0128 -0.1291 -0.0507 21   GLY   E O   
11508 N  N   . HIS   E 22  ? 1.5384 1.3053 1.2346 -0.0188 -0.1459 -0.0546 22   HIS   E N   
11509 C  CA  . HIS   E 22  ? 1.5508 1.3080 1.2365 -0.0176 -0.1552 -0.0558 22   HIS   E CA  
11510 C  C   . HIS   E 22  ? 1.5565 1.3238 1.2607 -0.0237 -0.1656 -0.0567 22   HIS   E C   
11511 O  O   . HIS   E 22  ? 1.5643 1.3237 1.2657 -0.0253 -0.1758 -0.0594 22   HIS   E O   
11512 C  CB  . HIS   E 22  ? 1.5875 1.3220 1.2475 -0.0128 -0.1598 -0.0587 22   HIS   E CB  
11513 C  CG  . HIS   E 22  ? 1.5773 1.3030 1.2223 -0.0076 -0.1490 -0.0582 22   HIS   E CG  
11514 N  ND1 . HIS   E 22  ? 1.6041 1.3268 1.2390 -0.0029 -0.1396 -0.0560 22   HIS   E ND1 
11515 C  CD2 . HIS   E 22  ? 1.5433 1.2632 1.1828 -0.0064 -0.1457 -0.0593 22   HIS   E CD2 
11516 C  CE1 . HIS   E 22  ? 1.5734 1.2889 1.1975 0.0010  -0.1309 -0.0559 22   HIS   E CE1 
11517 N  NE2 . HIS   E 22  ? 1.5221 1.2357 1.1484 -0.0009 -0.1345 -0.0580 22   HIS   E NE2 
11518 N  N   . PHE   E 23  ? 1.5694 1.3545 1.2933 -0.0271 -0.1627 -0.0541 23   PHE   E N   
11519 C  CA  . PHE   E 23  ? 1.5789 1.3767 1.3238 -0.0332 -0.1700 -0.0543 23   PHE   E CA  
11520 C  C   . PHE   E 23  ? 1.6359 1.4318 1.3806 -0.0336 -0.1798 -0.0551 23   PHE   E C   
11521 O  O   . PHE   E 23  ? 1.6308 1.4278 1.3843 -0.0373 -0.1901 -0.0569 23   PHE   E O   
11522 C  CB  . PHE   E 23  ? 1.4971 1.3151 1.2635 -0.0364 -0.1615 -0.0512 23   PHE   E CB  
11523 C  CG  . PHE   E 23  ? 1.4713 1.3030 1.2601 -0.0426 -0.1671 -0.0509 23   PHE   E CG  
11524 C  CD1 . PHE   E 23  ? 1.5109 1.3383 1.3029 -0.0458 -0.1757 -0.0533 23   PHE   E CD1 
11525 C  CD2 . PHE   E 23  ? 1.4115 1.2600 1.2182 -0.0451 -0.1636 -0.0482 23   PHE   E CD2 
11526 C  CE1 . PHE   E 23  ? 1.4810 1.3208 1.2940 -0.0515 -0.1803 -0.0529 23   PHE   E CE1 
11527 C  CE2 . PHE   E 23  ? 1.4416 1.3023 1.2685 -0.0505 -0.1683 -0.0478 23   PHE   E CE2 
11528 C  CZ  . PHE   E 23  ? 1.4857 1.3422 1.3161 -0.0538 -0.1764 -0.0501 23   PHE   E CZ  
11529 N  N   . THR   E 24  ? 1.6453 1.4375 1.3795 -0.0296 -0.1768 -0.0538 24   THR   E N   
11530 C  CA  . THR   E 24  ? 1.6989 1.4891 1.4318 -0.0293 -0.1854 -0.0544 24   THR   E CA  
11531 C  C   . THR   E 24  ? 1.7136 1.4826 1.4241 -0.0255 -0.1951 -0.0577 24   THR   E C   
11532 O  O   . THR   E 24  ? 1.7070 1.4737 1.4207 -0.0274 -0.2071 -0.0599 24   THR   E O   
11533 C  CB  . THR   E 24  ? 1.6763 1.4716 1.4077 -0.0267 -0.1776 -0.0514 24   THR   E CB  
11534 O  OG1 . THR   E 24  ? 1.6830 1.4645 1.3924 -0.0207 -0.1702 -0.0511 24   THR   E OG1 
11535 C  CG2 . THR   E 24  ? 1.5715 1.3870 1.3245 -0.0302 -0.1685 -0.0483 24   THR   E CG2 
11536 N  N   . SER   E 25  ? 1.7134 1.4667 1.4012 -0.0201 -0.1901 -0.0582 25   SER   E N   
11537 C  CA  . SER   E 25  ? 1.7522 1.4838 1.4164 -0.0159 -0.1985 -0.0615 25   SER   E CA  
11538 C  C   . SER   E 25  ? 1.7691 1.4884 1.4163 -0.0120 -0.1912 -0.0620 25   SER   E C   
11539 O  O   . SER   E 25  ? 1.7643 1.4881 1.4108 -0.0101 -0.1786 -0.0594 25   SER   E O   
11540 C  CB  . SER   E 25  ? 1.8405 1.5615 1.4881 -0.0109 -0.2008 -0.0613 25   SER   E CB  
11541 O  OG  . SER   E 25  ? 1.9599 1.6594 1.5849 -0.0069 -0.2101 -0.0647 25   SER   E OG  
11542 N  N   . ALA   E 26  ? 1.8418 1.5454 1.4754 -0.0107 -0.1993 -0.0655 26   ALA   E N   
11543 C  CA  . ALA   E 26  ? 1.8484 1.5405 1.4668 -0.0073 -0.1929 -0.0662 26   ALA   E CA  
11544 C  C   . ALA   E 26  ? 1.9046 1.5860 1.5022 -0.0004 -0.1823 -0.0645 26   ALA   E C   
11545 O  O   . ALA   E 26  ? 1.7871 1.4628 1.3755 0.0024  -0.1739 -0.0642 26   ALA   E O   
11546 C  CB  . ALA   E 26  ? 1.7468 1.4216 1.3516 -0.0065 -0.2045 -0.0704 26   ALA   E CB  
11547 N  N   . GLU   E 27  ? 2.0457 1.7245 1.6361 0.0024  -0.1821 -0.0632 27   GLU   E N   
11548 C  CA  . GLU   E 27  ? 2.0524 1.7206 1.6231 0.0090  -0.1720 -0.0613 27   GLU   E CA  
11549 C  C   . GLU   E 27  ? 2.0553 1.7401 1.6403 0.0078  -0.1607 -0.0572 27   GLU   E C   
11550 O  O   . GLU   E 27  ? 2.0907 1.7683 1.6618 0.0126  -0.1533 -0.0554 27   GLU   E O   
11551 C  CB  . GLU   E 27  ? 2.0896 1.7383 1.6369 0.0140  -0.1802 -0.0630 27   GLU   E CB  
11552 C  CG  . GLU   E 27  ? 2.1248 1.7818 1.6830 0.0115  -0.1883 -0.0626 27   GLU   E CG  
11553 C  CD  . GLU   E 27  ? 2.2058 1.8608 1.7697 0.0081  -0.2049 -0.0663 27   GLU   E CD  
11554 O  OE1 . GLU   E 27  ? 2.2389 1.8883 1.8012 0.0068  -0.2098 -0.0689 27   GLU   E OE1 
11555 O  OE2 . GLU   E 27  ? 2.2193 1.8785 1.7897 0.0067  -0.2129 -0.0665 27   GLU   E OE2 
11556 N  N   . ASP   E 28  ? 1.9133 1.6197 1.5254 0.0016  -0.1593 -0.0558 28   ASP   E N   
11557 C  CA  . ASP   E 28  ? 1.7359 1.4594 1.3638 0.0000  -0.1487 -0.0522 28   ASP   E CA  
11558 C  C   . ASP   E 28  ? 1.6032 1.3359 1.2411 -0.0012 -0.1383 -0.0510 28   ASP   E C   
11559 O  O   . ASP   E 28  ? 1.5950 1.3295 1.2392 -0.0039 -0.1417 -0.0527 28   ASP   E O   
11560 C  CB  . ASP   E 28  ? 1.6935 1.4348 1.3449 -0.0058 -0.1549 -0.0514 28   ASP   E CB  
11561 C  CG  . ASP   E 28  ? 1.7133 1.4482 1.3571 -0.0043 -0.1635 -0.0519 28   ASP   E CG  
11562 O  OD1 . ASP   E 28  ? 1.8398 1.5565 1.4596 0.0015  -0.1636 -0.0525 28   ASP   E OD1 
11563 O  OD2 . ASP   E 28  ? 1.6096 1.3571 1.2710 -0.0086 -0.1699 -0.0517 28   ASP   E OD2 
11564 N  N   . LEU   E 29  ? 1.5620 1.3004 1.2016 0.0008  -0.1257 -0.0481 29   LEU   E N   
11565 C  CA  . LEU   E 29  ? 1.5023 1.2533 1.1561 -0.0009 -0.1158 -0.0467 29   LEU   E CA  
11566 C  C   . LEU   E 29  ? 1.5072 1.2804 1.1873 -0.0064 -0.1147 -0.0447 29   LEU   E C   
11567 O  O   . LEU   E 29  ? 1.5009 1.2812 1.1860 -0.0059 -0.1091 -0.0422 29   LEU   E O   
11568 C  CB  . LEU   E 29  ? 1.4611 1.2063 1.1035 0.0042  -0.1026 -0.0449 29   LEU   E CB  
11569 C  CG  . LEU   E 29  ? 1.4273 1.1846 1.0844 0.0025  -0.0941 -0.0441 29   LEU   E CG  
11570 C  CD1 . LEU   E 29  ? 1.4278 1.1808 1.0840 0.0009  -0.1005 -0.0469 29   LEU   E CD1 
11571 C  CD2 . LEU   E 29  ? 1.4466 1.1995 1.0950 0.0074  -0.0807 -0.0424 29   LEU   E CD2 
11572 N  N   . ASN   E 30  ? 1.5062 1.2898 1.2028 -0.0114 -0.1199 -0.0456 30   ASN   E N   
11573 C  CA  . ASN   E 30  ? 1.4367 1.2404 1.1577 -0.0165 -0.1195 -0.0438 30   ASN   E CA  
11574 C  C   . ASN   E 30  ? 1.3877 1.2035 1.1214 -0.0173 -0.1090 -0.0422 30   ASN   E C   
11575 O  O   . ASN   E 30  ? 1.3877 1.1989 1.1170 -0.0161 -0.1058 -0.0433 30   ASN   E O   
11576 C  CB  . ASN   E 30  ? 1.4357 1.2444 1.1685 -0.0216 -0.1307 -0.0455 30   ASN   E CB  
11577 C  CG  . ASN   E 30  ? 1.4886 1.2899 1.2146 -0.0215 -0.1416 -0.0469 30   ASN   E CG  
11578 O  OD1 . ASN   E 30  ? 1.4887 1.2815 1.2099 -0.0225 -0.1514 -0.0495 30   ASN   E OD1 
11579 N  ND2 . ASN   E 30  ? 1.4669 1.2709 1.1926 -0.0203 -0.1401 -0.0451 30   ASN   E ND2 
11580 N  N   . LEU   E 31  ? 1.3633 1.1940 1.1124 -0.0192 -0.1039 -0.0397 31   LEU   E N   
11581 C  CA  . LEU   E 31  ? 1.3182 1.1634 1.0840 -0.0211 -0.0963 -0.0384 31   LEU   E CA  
11582 C  C   . LEU   E 31  ? 1.2843 1.1449 1.0709 -0.0267 -0.1017 -0.0378 31   LEU   E C   
11583 O  O   . LEU   E 31  ? 1.3186 1.1849 1.1113 -0.0282 -0.1049 -0.0367 31   LEU   E O   
11584 C  CB  . LEU   E 31  ? 1.2998 1.1498 1.0669 -0.0185 -0.0853 -0.0360 31   LEU   E CB  
11585 C  CG  . LEU   E 31  ? 1.2668 1.1304 1.0498 -0.0197 -0.0771 -0.0349 31   LEU   E CG  
11586 C  CD1 . LEU   E 31  ? 1.2770 1.1360 1.0569 -0.0192 -0.0769 -0.0367 31   LEU   E CD1 
11587 C  CD2 . LEU   E 31  ? 1.2710 1.1373 1.0539 -0.0167 -0.0660 -0.0329 31   LEU   E CD2 
11588 N  N   . LEU   E 32  ? 1.2295 1.0958 1.0263 -0.0295 -0.1028 -0.0386 32   LEU   E N   
11589 C  CA  . LEU   E 32  ? 1.2131 1.0931 1.0292 -0.0347 -0.1074 -0.0381 32   LEU   E CA  
11590 C  C   . LEU   E 32  ? 1.2368 1.1309 1.0682 -0.0358 -0.0992 -0.0363 32   LEU   E C   
11591 O  O   . LEU   E 32  ? 1.3069 1.2001 1.1379 -0.0350 -0.0951 -0.0369 32   LEU   E O   
11592 C  CB  . LEU   E 32  ? 1.2009 1.0760 1.0171 -0.0374 -0.1154 -0.0402 32   LEU   E CB  
11593 C  CG  . LEU   E 32  ? 1.2289 1.1012 1.0459 -0.0399 -0.1263 -0.0413 32   LEU   E CG  
11594 C  CD1 . LEU   E 32  ? 1.3487 1.2055 1.1454 -0.0359 -0.1297 -0.0426 32   LEU   E CD1 
11595 C  CD2 . LEU   E 32  ? 1.1905 1.0613 1.0125 -0.0434 -0.1328 -0.0431 32   LEU   E CD2 
11596 N  N   . ILE   E 33  ? 1.2268 1.1337 1.0715 -0.0375 -0.0972 -0.0343 33   ILE   E N   
11597 C  CA  . ILE   E 33  ? 1.2333 1.1536 1.0927 -0.0385 -0.0901 -0.0327 33   ILE   E CA  
11598 C  C   . ILE   E 33  ? 1.2258 1.1578 1.1023 -0.0432 -0.0945 -0.0322 33   ILE   E C   
11599 O  O   . ILE   E 33  ? 1.1754 1.1103 1.0567 -0.0456 -0.1007 -0.0318 33   ILE   E O   
11600 C  CB  . ILE   E 33  ? 1.2001 1.1260 1.0617 -0.0364 -0.0830 -0.0308 33   ILE   E CB  
11601 C  CG1 . ILE   E 33  ? 1.2182 1.1324 1.0634 -0.0317 -0.0773 -0.0312 33   ILE   E CG1 
11602 C  CG2 . ILE   E 33  ? 1.1543 1.0940 1.0316 -0.0375 -0.0768 -0.0295 33   ILE   E CG2 
11603 C  CD1 . ILE   E 33  ? 1.2739 1.1909 1.1189 -0.0298 -0.0714 -0.0293 33   ILE   E CD1 
11604 N  N   . ALA   E 34  ? 1.2159 1.1541 1.1012 -0.0442 -0.0913 -0.0321 34   ALA   E N   
11605 C  CA  . ALA   E 34  ? 1.1568 1.1065 1.0586 -0.0482 -0.0932 -0.0312 34   ALA   E CA  
11606 C  C   . ALA   E 34  ? 1.1706 1.1326 1.0839 -0.0476 -0.0861 -0.0294 34   ALA   E C   
11607 O  O   . ALA   E 34  ? 1.1727 1.1344 1.0838 -0.0450 -0.0796 -0.0296 34   ALA   E O   
11608 C  CB  . ALA   E 34  ? 1.0773 1.0237 0.9796 -0.0496 -0.0951 -0.0326 34   ALA   E CB  
11609 N  N   . LYS   E 35  ? 1.1587 1.1312 1.0842 -0.0500 -0.0874 -0.0278 35   LYS   E N   
11610 C  CA  . LYS   E 35  ? 1.1323 1.1170 1.0702 -0.0500 -0.0818 -0.0261 35   LYS   E CA  
11611 C  C   . LYS   E 35  ? 1.1001 1.0938 1.0519 -0.0536 -0.0849 -0.0253 35   LYS   E C   
11612 O  O   . LYS   E 35  ? 1.0962 1.0963 1.0559 -0.0557 -0.0878 -0.0241 35   LYS   E O   
11613 C  CB  . LYS   E 35  ? 1.1291 1.1174 1.0673 -0.0487 -0.0795 -0.0248 35   LYS   E CB  
11614 C  CG  . LYS   E 35  ? 1.0939 1.0717 1.0170 -0.0452 -0.0772 -0.0254 35   LYS   E CG  
11615 C  CD  . LYS   E 35  ? 1.1148 1.0977 1.0405 -0.0434 -0.0713 -0.0238 35   LYS   E CD  
11616 C  CE  . LYS   E 35  ? 1.1732 1.1524 1.0927 -0.0431 -0.0743 -0.0231 35   LYS   E CE  
11617 N  NZ  . LYS   E 35  ? 1.2137 1.1804 1.1165 -0.0395 -0.0717 -0.0237 35   LYS   E NZ  
11618 N  N   . ASN   E 36  ? 1.0891 1.0823 1.0431 -0.0543 -0.0842 -0.0259 36   ASN   E N   
11619 C  CA  . ASN   E 36  ? 1.0972 1.0972 1.0630 -0.0574 -0.0860 -0.0251 36   ASN   E CA  
11620 C  C   . ASN   E 36  ? 1.0946 1.0935 1.0635 -0.0610 -0.0933 -0.0251 36   ASN   E C   
11621 O  O   . ASN   E 36  ? 1.1114 1.1044 1.0780 -0.0627 -0.0969 -0.0262 36   ASN   E O   
11622 C  CB  . ASN   E 36  ? 1.1181 1.1302 1.0960 -0.0574 -0.0820 -0.0233 36   ASN   E CB  
11623 C  CG  . ASN   E 36  ? 1.0867 1.1049 1.0753 -0.0598 -0.0824 -0.0224 36   ASN   E CG  
11624 O  OD1 . ASN   E 36  ? 1.0801 1.0938 1.0668 -0.0605 -0.0832 -0.0232 36   ASN   E OD1 
11625 N  ND2 . ASN   E 36  ? 1.0931 1.1212 1.0926 -0.0608 -0.0815 -0.0206 36   ASN   E ND2 
11626 N  N   . THR   E 37  ? 1.1309 1.1357 1.1061 -0.0623 -0.0957 -0.0239 37   THR   E N   
11627 C  CA  . THR   E 37  ? 1.1216 1.1266 1.1017 -0.0657 -0.1027 -0.0238 37   THR   E CA  
11628 C  C   . THR   E 37  ? 1.2183 1.2165 1.1894 -0.0649 -0.1077 -0.0248 37   THR   E C   
11629 O  O   . THR   E 37  ? 1.2274 1.2238 1.2008 -0.0674 -0.1145 -0.0253 37   THR   E O   
11630 C  CB  . THR   E 37  ? 1.0841 1.1014 1.0795 -0.0679 -0.1022 -0.0217 37   THR   E CB  
11631 O  OG1 . THR   E 37  ? 1.0626 1.0852 1.0589 -0.0659 -0.0993 -0.0205 37   THR   E OG1 
11632 C  CG2 . THR   E 37  ? 1.1547 1.1777 1.1581 -0.0684 -0.0976 -0.0207 37   THR   E CG2 
11633 N  N   . ARG   E 38  ? 1.2643 1.2586 1.2254 -0.0615 -0.1043 -0.0250 38   ARG   E N   
11634 C  CA  . ARG   E 38  ? 1.2700 1.2570 1.2207 -0.0600 -0.1080 -0.0257 38   ARG   E CA  
11635 C  C   . ARG   E 38  ? 1.2890 1.2622 1.2234 -0.0576 -0.1088 -0.0278 38   ARG   E C   
11636 O  O   . ARG   E 38  ? 1.2957 1.2661 1.2259 -0.0560 -0.1039 -0.0283 38   ARG   E O   
11637 C  CB  . ARG   E 38  ? 1.2840 1.2755 1.2343 -0.0576 -0.1032 -0.0242 38   ARG   E CB  
11638 C  CG  . ARG   E 38  ? 1.2965 1.3020 1.2627 -0.0592 -0.1005 -0.0221 38   ARG   E CG  
11639 C  CD  . ARG   E 38  ? 1.3269 1.3375 1.3033 -0.0626 -0.1070 -0.0216 38   ARG   E CD  
11640 N  NE  . ARG   E 38  ? 1.3728 1.3776 1.3424 -0.0622 -0.1130 -0.0223 38   ARG   E NE  
11641 C  CZ  . ARG   E 38  ? 1.3734 1.3820 1.3508 -0.0646 -0.1192 -0.0220 38   ARG   E CZ  
11642 N  NH1 . ARG   E 38  ? 1.3665 1.3848 1.3591 -0.0676 -0.1198 -0.0209 38   ARG   E NH1 
11643 N  NH2 . ARG   E 38  ? 1.3664 1.3685 1.3359 -0.0636 -0.1248 -0.0228 38   ARG   E NH2 
11644 N  N   . LEU   E 39  ? 1.2747 1.2387 1.1994 -0.0572 -0.1152 -0.0291 39   LEU   E N   
11645 C  CA  . LEU   E 39  ? 1.2160 1.1653 1.1232 -0.0546 -0.1167 -0.0312 39   LEU   E CA  
11646 C  C   . LEU   E 39  ? 1.2521 1.1948 1.1477 -0.0516 -0.1176 -0.0312 39   LEU   E C   
11647 O  O   . LEU   E 39  ? 1.3032 1.2460 1.2005 -0.0528 -0.1241 -0.0312 39   LEU   E O   
11648 C  CB  . LEU   E 39  ? 1.2179 1.1602 1.1234 -0.0570 -0.1249 -0.0332 39   LEU   E CB  
11649 C  CG  . LEU   E 39  ? 1.2368 1.1626 1.1229 -0.0540 -0.1284 -0.0355 39   LEU   E CG  
11650 C  CD1 . LEU   E 39  ? 1.2431 1.1623 1.1180 -0.0506 -0.1211 -0.0359 39   LEU   E CD1 
11651 C  CD2 . LEU   E 39  ? 1.2262 1.1460 1.1125 -0.0568 -0.1374 -0.0375 39   LEU   E CD2 
11652 N  N   . GLU   E 40  ? 1.2534 1.1902 1.1375 -0.0477 -0.1111 -0.0310 40   GLU   E N   
11653 C  CA  . GLU   E 40  ? 1.2876 1.2166 1.1588 -0.0444 -0.1108 -0.0309 40   GLU   E CA  
11654 C  C   . GLU   E 40  ? 1.3429 1.2548 1.1947 -0.0416 -0.1143 -0.0331 40   GLU   E C   
11655 O  O   . GLU   E 40  ? 1.3212 1.2273 1.1669 -0.0405 -0.1116 -0.0342 40   GLU   E O   
11656 C  CB  . GLU   E 40  ? 1.2751 1.2083 1.1462 -0.0417 -0.1008 -0.0291 40   GLU   E CB  
11657 C  CG  . GLU   E 40  ? 1.2890 1.2384 1.1788 -0.0442 -0.0970 -0.0272 40   GLU   E CG  
11658 C  CD  . GLU   E 40  ? 1.3032 1.2581 1.1956 -0.0428 -0.0919 -0.0252 40   GLU   E CD  
11659 O  OE1 . GLU   E 40  ? 1.4188 1.3645 1.2977 -0.0394 -0.0890 -0.0252 40   GLU   E OE1 
11660 O  OE2 . GLU   E 40  ? 1.2669 1.2346 1.1743 -0.0449 -0.0906 -0.0237 40   GLU   E OE2 
11661 N  N   . ILE   E 41  ? 1.3276 1.2309 1.1693 -0.0404 -0.1206 -0.0338 41   ILE   E N   
11662 C  CA  . ILE   E 41  ? 1.3214 1.2071 1.1430 -0.0374 -0.1250 -0.0361 41   ILE   E CA  
11663 C  C   . ILE   E 41  ? 1.3797 1.2567 1.1861 -0.0328 -0.1212 -0.0352 41   ILE   E C   
11664 O  O   . ILE   E 41  ? 1.4017 1.2820 1.2105 -0.0328 -0.1231 -0.0341 41   ILE   E O   
11665 C  CB  . ILE   E 41  ? 1.2974 1.1782 1.1187 -0.0396 -0.1372 -0.0381 41   ILE   E CB  
11666 C  CG1 . ILE   E 41  ? 1.3161 1.2034 1.1510 -0.0440 -0.1406 -0.0390 41   ILE   E CG1 
11667 C  CG2 . ILE   E 41  ? 1.3387 1.2003 1.1374 -0.0357 -0.1416 -0.0403 41   ILE   E CG2 
11668 C  CD1 . ILE   E 41  ? 1.3445 1.2370 1.1913 -0.0481 -0.1506 -0.0397 41   ILE   E CD1 
11669 N  N   . TYR   E 42  ? 1.3791 1.2444 1.1695 -0.0287 -0.1157 -0.0358 42   TYR   E N   
11670 C  CA  . TYR   E 42  ? 1.3856 1.2414 1.1603 -0.0240 -0.1106 -0.0348 42   TYR   E CA  
11671 C  C   . TYR   E 42  ? 1.3922 1.2278 1.1436 -0.0201 -0.1143 -0.0371 42   TYR   E C   
11672 O  O   . TYR   E 42  ? 1.3749 1.2048 1.1226 -0.0205 -0.1176 -0.0391 42   TYR   E O   
11673 C  CB  . TYR   E 42  ? 1.3505 1.2123 1.1289 -0.0223 -0.0977 -0.0328 42   TYR   E CB  
11674 C  CG  . TYR   E 42  ? 1.2901 1.1689 1.0872 -0.0249 -0.0937 -0.0304 42   TYR   E CG  
11675 C  CD1 . TYR   E 42  ? 1.2869 1.1809 1.1040 -0.0293 -0.0944 -0.0300 42   TYR   E CD1 
11676 C  CD2 . TYR   E 42  ? 1.3726 1.2517 1.1668 -0.0230 -0.0891 -0.0284 42   TYR   E CD2 
11677 C  CE1 . TYR   E 42  ? 1.3355 1.2444 1.1690 -0.0314 -0.0910 -0.0279 42   TYR   E CE1 
11678 C  CE2 . TYR   E 42  ? 1.3546 1.2488 1.1656 -0.0253 -0.0857 -0.0263 42   TYR   E CE2 
11679 C  CZ  . TYR   E 42  ? 1.3169 1.2259 1.1473 -0.0294 -0.0868 -0.0261 42   TYR   E CZ  
11680 O  OH  . TYR   E 42  ? 1.3097 1.2327 1.1555 -0.0313 -0.0836 -0.0241 42   TYR   E OH  
11681 N  N   . VAL   E 43  ? 1.4303 1.2547 1.1656 -0.0161 -0.1140 -0.0367 43   VAL   E N   
11682 C  CA  . VAL   E 43  ? 1.4517 1.2555 1.1621 -0.0110 -0.1146 -0.0383 43   VAL   E CA  
11683 C  C   . VAL   E 43  ? 1.4628 1.2625 1.1641 -0.0068 -0.1017 -0.0363 43   VAL   E C   
11684 O  O   . VAL   E 43  ? 1.4586 1.2636 1.1633 -0.0061 -0.0958 -0.0339 43   VAL   E O   
11685 C  CB  . VAL   E 43  ? 1.4522 1.2438 1.1484 -0.0090 -0.1241 -0.0394 43   VAL   E CB  
11686 C  CG1 . VAL   E 43  ? 1.4920 1.2618 1.1607 -0.0028 -0.1223 -0.0404 43   VAL   E CG1 
11687 C  CG2 . VAL   E 43  ? 1.4617 1.2542 1.1645 -0.0126 -0.1373 -0.0420 43   VAL   E CG2 
11688 N  N   . VAL   E 44  ? 1.4458 1.2361 1.1361 -0.0040 -0.0972 -0.0374 44   VAL   E N   
11689 C  CA  . VAL   E 44  ? 1.4619 1.2482 1.1445 0.0001  -0.0844 -0.0356 44   VAL   E CA  
11690 C  C   . VAL   E 44  ? 1.5619 1.3305 1.2211 0.0054  -0.0835 -0.0352 44   VAL   E C   
11691 O  O   . VAL   E 44  ? 1.6237 1.3744 1.2621 0.0093  -0.0862 -0.0371 44   VAL   E O   
11692 C  CB  . VAL   E 44  ? 1.4238 1.2061 1.1028 0.0014  -0.0798 -0.0369 44   VAL   E CB  
11693 C  CG1 . VAL   E 44  ? 1.3848 1.1630 1.0565 0.0058  -0.0663 -0.0351 44   VAL   E CG1 
11694 C  CG2 . VAL   E 44  ? 1.4470 1.2464 1.1487 -0.0037 -0.0809 -0.0372 44   VAL   E CG2 
11695 N  N   . THR   E 45  ? 1.5662 1.3389 1.2278 0.0059  -0.0798 -0.0329 45   THR   E N   
11696 C  CA  . THR   E 45  ? 1.6112 1.3666 1.2500 0.0113  -0.0774 -0.0321 45   THR   E CA  
11697 C  C   . THR   E 45  ? 1.6731 1.4217 1.3024 0.0157  -0.0637 -0.0306 45   THR   E C   
11698 O  O   . THR   E 45  ? 1.6930 1.4534 1.3369 0.0140  -0.0556 -0.0297 45   THR   E O   
11699 C  CB  . THR   E 45  ? 1.6066 1.3675 1.2503 0.0105  -0.0781 -0.0300 45   THR   E CB  
11700 O  OG1 . THR   E 45  ? 1.6636 1.4372 1.3210 0.0095  -0.0664 -0.0271 45   THR   E OG1 
11701 C  CG2 . THR   E 45  ? 1.5786 1.3515 1.2384 0.0053  -0.0899 -0.0312 45   THR   E CG2 
11702 N  N   . ALA   E 46  ? 1.7264 1.4553 1.3307 0.0215  -0.0613 -0.0305 46   ALA   E N   
11703 C  CA  . ALA   E 46  ? 1.7709 1.4918 1.3648 0.0261  -0.0477 -0.0288 46   ALA   E CA  
11704 C  C   . ALA   E 46  ? 1.8143 1.5500 1.4251 0.0244  -0.0365 -0.0255 46   ALA   E C   
11705 O  O   . ALA   E 46  ? 1.8589 1.6008 1.4779 0.0247  -0.0260 -0.0245 46   ALA   E O   
11706 C  CB  . ALA   E 46  ? 1.7958 1.4926 1.3594 0.0326  -0.0473 -0.0288 46   ALA   E CB  
11707 N  N   . GLU   E 47  ? 1.8255 1.5675 1.4428 0.0225  -0.0392 -0.0240 47   GLU   E N   
11708 C  CA  . GLU   E 47  ? 1.7804 1.5367 1.4145 0.0206  -0.0297 -0.0210 47   GLU   E CA  
11709 C  C   . GLU   E 47  ? 1.7751 1.5535 1.4371 0.0150  -0.0293 -0.0212 47   GLU   E C   
11710 O  O   . GLU   E 47  ? 1.7720 1.5593 1.4456 0.0147  -0.0188 -0.0198 47   GLU   E O   
11711 C  CB  . GLU   E 47  ? 1.7701 1.5266 1.4031 0.0200  -0.0339 -0.0195 47   GLU   E CB  
11712 N  N   . GLY   E 48  ? 1.7215 1.5090 1.3948 0.0107  -0.0405 -0.0229 48   GLY   E N   
11713 C  CA  . GLY   E 48  ? 1.6220 1.4293 1.3203 0.0056  -0.0409 -0.0231 48   GLY   E CA  
11714 C  C   . GLY   E 48  ? 1.5289 1.3408 1.2340 0.0018  -0.0534 -0.0255 48   GLY   E C   
11715 O  O   . GLY   E 48  ? 1.5277 1.3308 1.2236 0.0028  -0.0578 -0.0278 48   GLY   E O   
11716 N  N   . LEU   E 49  ? 1.5029 1.3281 1.2240 -0.0024 -0.0592 -0.0250 49   LEU   E N   
11717 C  CA  . LEU   E 49  ? 1.4783 1.3103 1.2096 -0.0065 -0.0701 -0.0270 49   LEU   E CA  
11718 C  C   . LEU   E 49  ? 1.4714 1.3069 1.2066 -0.0086 -0.0787 -0.0267 49   LEU   E C   
11719 O  O   . LEU   E 49  ? 1.4812 1.3256 1.2256 -0.0095 -0.0751 -0.0245 49   LEU   E O   
11720 C  CB  . LEU   E 49  ? 1.4034 1.2533 1.1574 -0.0106 -0.0672 -0.0268 49   LEU   E CB  
11721 C  CG  . LEU   E 49  ? 1.3088 1.1567 1.0617 -0.0098 -0.0631 -0.0281 49   LEU   E CG  
11722 C  CD1 . LEU   E 49  ? 1.2550 1.1207 1.0300 -0.0132 -0.0590 -0.0274 49   LEU   E CD1 
11723 C  CD2 . LEU   E 49  ? 1.4049 1.2444 1.1501 -0.0105 -0.0730 -0.0308 49   LEU   E CD2 
11724 N  N   . ARG   E 50  ? 1.4552 1.2840 1.1843 -0.0093 -0.0901 -0.0289 50   ARG   E N   
11725 C  CA  . ARG   E 50  ? 1.4132 1.2448 1.1463 -0.0111 -0.0994 -0.0290 50   ARG   E CA  
11726 C  C   . ARG   E 50  ? 1.4063 1.2518 1.1592 -0.0166 -0.1068 -0.0300 50   ARG   E C   
11727 O  O   . ARG   E 50  ? 1.4467 1.2885 1.1983 -0.0177 -0.1121 -0.0323 50   ARG   E O   
11728 C  CB  . ARG   E 50  ? 1.4690 1.2814 1.1795 -0.0074 -0.1074 -0.0308 50   ARG   E CB  
11729 C  CG  . ARG   E 50  ? 1.4380 1.2519 1.1520 -0.0091 -0.1192 -0.0317 50   ARG   E CG  
11730 C  CD  . ARG   E 50  ? 1.4652 1.2585 1.1546 -0.0044 -0.1261 -0.0333 50   ARG   E CD  
11731 N  NE  . ARG   E 50  ? 1.4880 1.2675 1.1633 -0.0026 -0.1303 -0.0361 50   ARG   E NE  
11732 C  CZ  . ARG   E 50  ? 1.5101 1.2868 1.1865 -0.0046 -0.1423 -0.0390 50   ARG   E CZ  
11733 N  NH1 . ARG   E 50  ? 1.4466 1.2335 1.1382 -0.0084 -0.1514 -0.0396 50   ARG   E NH1 
11734 N  NH2 . ARG   E 50  ? 1.5617 1.3246 1.2237 -0.0025 -0.1453 -0.0415 50   ARG   E NH2 
11735 N  N   . PRO   E 51  ? 1.3837 1.2447 1.1549 -0.0199 -0.1072 -0.0284 51   PRO   E N   
11736 C  CA  . PRO   E 51  ? 1.3666 1.2405 1.1565 -0.0250 -0.1143 -0.0292 51   PRO   E CA  
11737 C  C   . PRO   E 51  ? 1.4447 1.3102 1.2285 -0.0256 -0.1269 -0.0318 51   PRO   E C   
11738 O  O   . PRO   E 51  ? 1.4991 1.3523 1.2677 -0.0226 -0.1319 -0.0325 51   PRO   E O   
11739 C  CB  . PRO   E 51  ? 1.2614 1.1493 1.0665 -0.0271 -0.1128 -0.0269 51   PRO   E CB  
11740 C  CG  . PRO   E 51  ? 1.3653 1.2527 1.1660 -0.0243 -0.1016 -0.0248 51   PRO   E CG  
11741 C  CD  . PRO   E 51  ? 1.4063 1.2746 1.1829 -0.0193 -0.0999 -0.0257 51   PRO   E CD  
11742 N  N   . VAL   E 52  ? 1.4012 1.2733 1.1972 -0.0295 -0.1321 -0.0331 52   VAL   E N   
11743 C  CA  . VAL   E 52  ? 1.3981 1.2627 1.1901 -0.0305 -0.1441 -0.0358 52   VAL   E CA  
11744 C  C   . VAL   E 52  ? 1.4053 1.2847 1.2194 -0.0359 -0.1501 -0.0358 52   VAL   E C   
11745 O  O   . VAL   E 52  ? 1.3771 1.2559 1.1936 -0.0369 -0.1596 -0.0368 52   VAL   E O   
11746 C  CB  . VAL   E 52  ? 1.4809 1.3339 1.2614 -0.0294 -0.1448 -0.0381 52   VAL   E CB  
11747 C  CG1 . VAL   E 52  ? 1.5527 1.4000 1.3328 -0.0314 -0.1575 -0.0410 52   VAL   E CG1 
11748 C  CG2 . VAL   E 52  ? 1.4821 1.3187 1.2390 -0.0236 -0.1396 -0.0382 52   VAL   E CG2 
11749 N  N   . LYS   E 53  ? 1.4114 1.3039 1.2417 -0.0392 -0.1447 -0.0347 53   LYS   E N   
11750 C  CA  . LYS   E 53  ? 1.4279 1.3355 1.2803 -0.0442 -0.1482 -0.0342 53   LYS   E CA  
11751 C  C   . LYS   E 53  ? 1.3862 1.3057 1.2512 -0.0461 -0.1391 -0.0324 53   LYS   E C   
11752 O  O   . LYS   E 53  ? 1.3813 1.2960 1.2386 -0.0441 -0.1326 -0.0326 53   LYS   E O   
11753 C  CB  . LYS   E 53  ? 1.4603 1.3636 1.3149 -0.0469 -0.1583 -0.0367 53   LYS   E CB  
11754 C  CG  . LYS   E 53  ? 1.4160 1.3338 1.2933 -0.0522 -0.1624 -0.0362 53   LYS   E CG  
11755 C  CD  . LYS   E 53  ? 1.4908 1.4098 1.3732 -0.0533 -0.1723 -0.0370 53   LYS   E CD  
11756 C  CE  . LYS   E 53  ? 1.5323 1.4602 1.4336 -0.0585 -0.1783 -0.0376 53   LYS   E CE  
11757 N  NZ  . LYS   E 53  ? 1.5974 1.5317 1.5100 -0.0603 -0.1860 -0.0376 53   LYS   E NZ  
11758 N  N   . GLU   E 54  ? 1.4257 1.3605 1.3100 -0.0495 -0.1385 -0.0308 54   GLU   E N   
11759 C  CA  . GLU   E 54  ? 1.4323 1.3783 1.3301 -0.0518 -0.1321 -0.0296 54   GLU   E CA  
11760 C  C   . GLU   E 54  ? 1.4336 1.3897 1.3492 -0.0564 -0.1376 -0.0295 54   GLU   E C   
11761 O  O   . GLU   E 54  ? 1.4625 1.4267 1.3882 -0.0579 -0.1404 -0.0284 54   GLU   E O   
11762 C  CB  . GLU   E 54  ? 1.4038 1.3589 1.3070 -0.0505 -0.1230 -0.0271 54   GLU   E CB  
11763 C  CG  . GLU   E 54  ? 1.3657 1.3331 1.2843 -0.0530 -0.1180 -0.0260 54   GLU   E CG  
11764 C  CD  . GLU   E 54  ? 1.4441 1.4242 1.3750 -0.0536 -0.1137 -0.0236 54   GLU   E CD  
11765 O  OE1 . GLU   E 54  ? 1.4873 1.4663 1.4123 -0.0508 -0.1086 -0.0226 54   GLU   E OE1 
11766 O  OE2 . GLU   E 54  ? 1.4553 1.4462 1.4015 -0.0567 -0.1154 -0.0227 54   GLU   E OE2 
11767 N  N   . VAL   E 55  ? 1.3388 1.2940 1.2579 -0.0587 -0.1390 -0.0306 55   VAL   E N   
11768 C  CA  . VAL   E 55  ? 1.3042 1.2678 1.2397 -0.0632 -0.1436 -0.0305 55   VAL   E CA  
11769 C  C   . VAL   E 55  ? 1.3660 1.3417 1.3150 -0.0649 -0.1361 -0.0286 55   VAL   E C   
11770 O  O   . VAL   E 55  ? 1.4094 1.3859 1.3545 -0.0626 -0.1283 -0.0278 55   VAL   E O   
11771 C  CB  . VAL   E 55  ? 1.2922 1.2468 1.2238 -0.0649 -0.1506 -0.0330 55   VAL   E CB  
11772 C  CG1 . VAL   E 55  ? 1.4394 1.3806 1.3556 -0.0625 -0.1578 -0.0352 55   VAL   E CG1 
11773 C  CG2 . VAL   E 55  ? 1.2613 1.2113 1.1868 -0.0640 -0.1450 -0.0336 55   VAL   E CG2 
11774 N  N   . GLY   E 56  ? 1.3701 1.3548 1.3351 -0.0687 -0.1385 -0.0278 56   GLY   E N   
11775 C  CA  . GLY   E 56  ? 1.3368 1.3321 1.3141 -0.0703 -0.1321 -0.0260 56   GLY   E CA  
11776 C  C   . GLY   E 56  ? 1.3397 1.3362 1.3263 -0.0741 -0.1351 -0.0265 56   GLY   E C   
11777 O  O   . GLY   E 56  ? 1.3261 1.3247 1.3213 -0.0770 -0.1417 -0.0268 56   GLY   E O   
11778 N  N   . MET   E 57  ? 1.3373 1.3327 1.3227 -0.0740 -0.1303 -0.0265 57   MET   E N   
11779 C  CA  . MET   E 57  ? 1.3425 1.3370 1.3343 -0.0773 -0.1323 -0.0270 57   MET   E CA  
11780 C  C   . MET   E 57  ? 1.2945 1.3010 1.3020 -0.0795 -0.1275 -0.0246 57   MET   E C   
11781 O  O   . MET   E 57  ? 1.2575 1.2708 1.2674 -0.0776 -0.1211 -0.0230 57   MET   E O   
11782 C  CB  . MET   E 57  ? 1.3750 1.3594 1.3545 -0.0756 -0.1301 -0.0286 57   MET   E CB  
11783 C  CG  . MET   E 57  ? 1.3725 1.3440 1.3348 -0.0729 -0.1338 -0.0309 57   MET   E CG  
11784 S  SD  . MET   E 57  ? 1.4719 1.4318 1.4265 -0.0738 -0.1364 -0.0332 57   MET   E SD  
11785 C  CE  . MET   E 57  ? 1.3947 1.3609 1.3673 -0.0797 -0.1419 -0.0327 57   MET   E CE  
11786 N  N   . TYR   E 58  ? 1.1855 1.1939 1.2036 -0.0833 -0.1307 -0.0245 58   TYR   E N   
11787 C  CA  . TYR   E 58  ? 1.0978 1.1155 1.1295 -0.0854 -0.1261 -0.0222 58   TYR   E CA  
11788 C  C   . TYR   E 58  ? 1.0993 1.1128 1.1265 -0.0848 -0.1214 -0.0225 58   TYR   E C   
11789 O  O   . TYR   E 58  ? 1.1432 1.1574 1.1776 -0.0876 -0.1210 -0.0219 58   TYR   E O   
11790 C  CB  . TYR   E 58  ? 1.1433 1.1651 1.1891 -0.0898 -0.1310 -0.0217 58   TYR   E CB  
11791 C  CG  . TYR   E 58  ? 1.1739 1.2026 1.2280 -0.0905 -0.1348 -0.0210 58   TYR   E CG  
11792 C  CD1 . TYR   E 58  ? 1.2551 1.2781 1.3023 -0.0898 -0.1418 -0.0229 58   TYR   E CD1 
11793 C  CD2 . TYR   E 58  ? 1.1615 1.2017 1.2298 -0.0917 -0.1315 -0.0184 58   TYR   E CD2 
11794 C  CE1 . TYR   E 58  ? 1.2579 1.2870 1.3125 -0.0902 -0.1456 -0.0223 58   TYR   E CE1 
11795 C  CE2 . TYR   E 58  ? 1.1604 1.2070 1.2364 -0.0922 -0.1349 -0.0177 58   TYR   E CE2 
11796 C  CZ  . TYR   E 58  ? 1.1912 1.2324 1.2607 -0.0915 -0.1420 -0.0197 58   TYR   E CZ  
11797 O  OH  . TYR   E 58  ? 1.2617 1.3093 1.3391 -0.0917 -0.1456 -0.0191 58   TYR   E OH  
11798 N  N   . GLY   E 59  ? 1.0986 1.1074 1.1135 -0.0811 -0.1176 -0.0233 59   GLY   E N   
11799 C  CA  . GLY   E 59  ? 1.1133 1.1181 1.1233 -0.0799 -0.1131 -0.0237 59   GLY   E CA  
11800 C  C   . GLY   E 59  ? 1.0956 1.0980 1.0945 -0.0754 -0.1084 -0.0243 59   GLY   E C   
11801 O  O   . GLY   E 59  ? 1.0660 1.0677 1.0595 -0.0735 -0.1093 -0.0246 59   GLY   E O   
11802 N  N   . LYS   E 60  ? 1.0940 1.0951 1.0900 -0.0737 -0.1033 -0.0243 60   LYS   E N   
11803 C  CA  . LYS   E 60  ? 1.0871 1.0849 1.0727 -0.0694 -0.0990 -0.0252 60   LYS   E CA  
11804 C  C   . LYS   E 60  ? 1.0847 1.0696 1.0566 -0.0684 -0.1017 -0.0276 60   LYS   E C   
11805 O  O   . LYS   E 60  ? 1.0726 1.0522 1.0429 -0.0695 -0.1027 -0.0284 60   LYS   E O   
11806 C  CB  . LYS   E 60  ? 1.0293 1.0321 1.0185 -0.0675 -0.0924 -0.0243 60   LYS   E CB  
11807 C  CG  . LYS   E 60  ? 0.9737 0.9883 0.9741 -0.0675 -0.0893 -0.0222 60   LYS   E CG  
11808 C  CD  . LYS   E 60  ? 1.0331 1.0515 1.0370 -0.0658 -0.0839 -0.0215 60   LYS   E CD  
11809 C  CE  . LYS   E 60  ? 1.0684 1.0837 1.0639 -0.0617 -0.0797 -0.0228 60   LYS   E CE  
11810 N  NZ  . LYS   E 60  ? 1.0414 1.0635 1.0394 -0.0595 -0.0766 -0.0221 60   LYS   E NZ  
11811 N  N   . ILE   E 61  ? 1.0880 1.0675 1.0498 -0.0662 -0.1032 -0.0287 61   ILE   E N   
11812 C  CA  . ILE   E 61  ? 1.0744 1.0408 1.0215 -0.0645 -0.1056 -0.0310 61   ILE   E CA  
11813 C  C   . ILE   E 61  ? 1.1029 1.0663 1.0450 -0.0619 -0.1000 -0.0316 61   ILE   E C   
11814 O  O   . ILE   E 61  ? 1.1076 1.0731 1.0468 -0.0585 -0.0942 -0.0314 61   ILE   E O   
11815 C  CB  . ILE   E 61  ? 1.0905 1.0518 1.0268 -0.0617 -0.1063 -0.0317 61   ILE   E CB  
11816 C  CG1 . ILE   E 61  ? 1.1276 1.0925 1.0693 -0.0639 -0.1119 -0.0311 61   ILE   E CG1 
11817 C  CG2 . ILE   E 61  ? 1.1555 1.1023 1.0759 -0.0599 -0.1091 -0.0341 61   ILE   E CG2 
11818 C  CD1 . ILE   E 61  ? 1.1020 1.0641 1.0349 -0.0610 -0.1115 -0.0311 61   ILE   E CD1 
11819 N  N   . ALA   E 62  ? 1.1222 1.0812 1.0644 -0.0636 -0.1016 -0.0324 62   ALA   E N   
11820 C  CA  . ALA   E 62  ? 1.0999 1.0553 1.0374 -0.0611 -0.0969 -0.0331 62   ALA   E CA  
11821 C  C   . ALA   E 62  ? 1.1318 1.0738 1.0536 -0.0587 -0.0983 -0.0355 62   ALA   E C   
11822 O  O   . ALA   E 62  ? 1.1288 1.0678 1.0441 -0.0552 -0.0934 -0.0362 62   ALA   E O   
11823 C  CB  . ALA   E 62  ? 1.0834 1.0408 1.0291 -0.0640 -0.0973 -0.0325 62   ALA   E CB  
11824 N  N   . VAL   E 63  ? 1.1991 1.1329 1.1150 -0.0605 -0.1051 -0.0368 63   VAL   E N   
11825 C  CA  . VAL   E 63  ? 1.2260 1.1459 1.1255 -0.0580 -0.1073 -0.0391 63   VAL   E CA  
11826 C  C   . VAL   E 63  ? 1.2312 1.1470 1.1249 -0.0581 -0.1125 -0.0397 63   VAL   E C   
11827 O  O   . VAL   E 63  ? 1.1963 1.1176 1.0991 -0.0614 -0.1172 -0.0389 63   VAL   E O   
11828 C  CB  . VAL   E 63  ? 1.2160 1.1270 1.1122 -0.0601 -0.1116 -0.0407 63   VAL   E CB  
11829 C  CG1 . VAL   E 63  ? 1.2855 1.1815 1.1639 -0.0572 -0.1139 -0.0432 63   VAL   E CG1 
11830 C  CG2 . VAL   E 63  ? 1.1940 1.1087 1.0956 -0.0599 -0.1065 -0.0400 63   VAL   E CG2 
11831 N  N   . MET   E 64  ? 1.2026 1.1087 1.0809 -0.0540 -0.1114 -0.0410 64   MET   E N   
11832 C  CA  . MET   E 64  ? 1.2305 1.1306 1.1004 -0.0532 -0.1162 -0.0417 64   MET   E CA  
11833 C  C   . MET   E 64  ? 1.2974 1.1820 1.1476 -0.0491 -0.1161 -0.0438 64   MET   E C   
11834 O  O   . MET   E 64  ? 1.2777 1.1607 1.1208 -0.0450 -0.1090 -0.0436 64   MET   E O   
11835 C  CB  . MET   E 64  ? 1.2324 1.1414 1.1068 -0.0519 -0.1122 -0.0398 64   MET   E CB  
11836 C  CG  . MET   E 64  ? 1.1972 1.0993 1.0618 -0.0506 -0.1168 -0.0404 64   MET   E CG  
11837 S  SD  . MET   E 64  ? 1.1303 1.0398 0.9960 -0.0479 -0.1102 -0.0383 64   MET   E SD  
11838 C  CE  . MET   E 64  ? 1.1996 1.1042 1.0549 -0.0428 -0.1005 -0.0385 64   MET   E CE  
11839 N  N   . GLU   E 65  ? 1.3986 1.2718 1.2403 -0.0502 -0.1241 -0.0460 65   GLU   E N   
11840 C  CA  . GLU   E 65  ? 1.4331 1.2901 1.2553 -0.0463 -0.1250 -0.0482 65   GLU   E CA  
11841 C  C   . GLU   E 65  ? 1.4295 1.2760 1.2422 -0.0467 -0.1344 -0.0500 65   GLU   E C   
11842 O  O   . GLU   E 65  ? 1.4178 1.2672 1.2398 -0.0511 -0.1420 -0.0504 65   GLU   E O   
11843 C  CB  . GLU   E 65  ? 1.4564 1.3076 1.2761 -0.0467 -0.1249 -0.0496 65   GLU   E CB  
11844 C  CG  . GLU   E 65  ? 1.4703 1.3259 1.2911 -0.0438 -0.1152 -0.0487 65   GLU   E CG  
11845 C  CD  . GLU   E 65  ? 1.5855 1.4379 1.3953 -0.0385 -0.1084 -0.0483 65   GLU   E CD  
11846 O  OE1 . GLU   E 65  ? 1.5565 1.3964 1.3505 -0.0357 -0.1111 -0.0497 65   GLU   E OE1 
11847 O  OE2 . GLU   E 65  ? 1.6326 1.4947 1.4497 -0.0370 -0.1004 -0.0467 65   GLU   E OE2 
11848 N  N   . LEU   E 66  ? 1.4174 1.2518 1.2118 -0.0420 -0.1336 -0.0511 66   LEU   E N   
11849 C  CA  . LEU   E 66  ? 1.4261 1.2471 1.2070 -0.0410 -0.1424 -0.0532 66   LEU   E CA  
11850 C  C   . LEU   E 66  ? 1.4455 1.2510 1.2129 -0.0400 -0.1469 -0.0561 66   LEU   E C   
11851 O  O   . LEU   E 66  ? 1.4324 1.2346 1.1947 -0.0379 -0.1410 -0.0563 66   LEU   E O   
11852 C  CB  . LEU   E 66  ? 1.3943 1.2090 1.1609 -0.0360 -0.1390 -0.0527 66   LEU   E CB  
11853 C  CG  . LEU   E 66  ? 1.3380 1.1635 1.1142 -0.0372 -0.1390 -0.0507 66   LEU   E CG  
11854 C  CD1 . LEU   E 66  ? 1.3439 1.1605 1.1034 -0.0319 -0.1354 -0.0503 66   LEU   E CD1 
11855 C  CD2 . LEU   E 66  ? 1.3766 1.2035 1.1606 -0.0414 -0.1501 -0.0517 66   LEU   E CD2 
11856 N  N   . PHE   E 67  ? 1.5267 1.3226 1.2884 -0.0414 -0.1576 -0.0584 67   PHE   E N   
11857 C  CA  . PHE   E 67  ? 1.5191 1.2988 1.2669 -0.0405 -0.1635 -0.0614 67   PHE   E CA  
11858 C  C   . PHE   E 67  ? 1.5494 1.3189 1.2898 -0.0410 -0.1754 -0.0638 67   PHE   E C   
11859 O  O   . PHE   E 67  ? 1.5102 1.2882 1.2623 -0.0440 -0.1802 -0.0630 67   PHE   E O   
11860 C  CB  . PHE   E 67  ? 1.4730 1.2570 1.2328 -0.0448 -0.1645 -0.0618 67   PHE   E CB  
11861 C  CG  . PHE   E 67  ? 1.4174 1.2114 1.1965 -0.0512 -0.1716 -0.0615 67   PHE   E CG  
11862 C  CD1 . PHE   E 67  ? 1.3987 1.2102 1.1965 -0.0541 -0.1678 -0.0586 67   PHE   E CD1 
11863 C  CD2 . PHE   E 67  ? 1.4671 1.2529 1.2462 -0.0544 -0.1817 -0.0640 67   PHE   E CD2 
11864 C  CE1 . PHE   E 67  ? 1.4114 1.2321 1.2271 -0.0598 -0.1737 -0.0582 67   PHE   E CE1 
11865 C  CE2 . PHE   E 67  ? 1.3945 1.1899 1.1926 -0.0604 -0.1877 -0.0636 67   PHE   E CE2 
11866 C  CZ  . PHE   E 67  ? 1.3907 1.2035 1.2070 -0.0630 -0.1834 -0.0606 67   PHE   E CZ  
11867 N  N   . ARG   E 68  ? 1.6940 1.4449 1.4147 -0.0379 -0.1803 -0.0667 68   ARG   E N   
11868 C  CA  . ARG   E 68  ? 1.7419 1.4804 1.4533 -0.0379 -0.1927 -0.0696 68   ARG   E CA  
11869 C  C   . ARG   E 68  ? 1.7521 1.4796 1.4596 -0.0399 -0.2003 -0.0726 68   ARG   E C   
11870 O  O   . ARG   E 68  ? 1.7521 1.4650 1.4412 -0.0358 -0.1985 -0.0743 68   ARG   E O   
11871 C  CB  . ARG   E 68  ? 1.7057 1.4293 1.3931 -0.0312 -0.1923 -0.0704 68   ARG   E CB  
11872 C  CG  . ARG   E 68  ? 1.7490 1.4605 1.4270 -0.0308 -0.2053 -0.0733 68   ARG   E CG  
11873 C  CD  . ARG   E 68  ? 1.7477 1.4432 1.4003 -0.0237 -0.2045 -0.0740 68   ARG   E CD  
11874 N  NE  . ARG   E 68  ? 1.7235 1.4278 1.3775 -0.0213 -0.1948 -0.0707 68   ARG   E NE  
11875 C  CZ  . ARG   E 68  ? 1.7167 1.4130 1.3567 -0.0169 -0.1958 -0.0706 68   ARG   E CZ  
11876 N  NH1 . ARG   E 68  ? 1.7897 1.4695 1.4134 -0.0146 -0.2067 -0.0736 68   ARG   E NH1 
11877 N  NH2 . ARG   E 68  ? 1.7150 1.4196 1.3569 -0.0149 -0.1859 -0.0674 68   ARG   E NH2 
11878 N  N   . PRO   E 69  ? 1.7789 1.5124 1.5031 -0.0461 -0.2085 -0.0735 69   PRO   E N   
11879 C  CA  . PRO   E 69  ? 1.7755 1.4993 1.4980 -0.0485 -0.2154 -0.0762 69   PRO   E CA  
11880 C  C   . PRO   E 69  ? 1.8948 1.5969 1.5942 -0.0446 -0.2246 -0.0801 69   PRO   E C   
11881 O  O   . PRO   E 69  ? 1.9100 1.6048 1.5960 -0.0405 -0.2271 -0.0807 69   PRO   E O   
11882 C  CB  . PRO   E 69  ? 1.7406 1.4767 1.4873 -0.0559 -0.2224 -0.0760 69   PRO   E CB  
11883 C  CG  . PRO   E 69  ? 1.7217 1.4766 1.4847 -0.0574 -0.2157 -0.0724 69   PRO   E CG  
11884 C  CD  . PRO   E 69  ? 1.7571 1.5077 1.5042 -0.0512 -0.2110 -0.0717 69   PRO   E CD  
11885 N  N   . LYS   E 70  ? 2.0195 1.7106 1.7137 -0.0458 -0.2297 -0.0827 70   LYS   E N   
11886 C  CA  . LYS   E 70  ? 2.0344 1.7037 1.7068 -0.0423 -0.2393 -0.0867 70   LYS   E CA  
11887 C  C   . LYS   E 70  ? 1.9925 1.6591 1.6666 -0.0437 -0.2516 -0.0886 70   LYS   E C   
11888 O  O   . LYS   E 70  ? 1.9527 1.6291 1.6474 -0.0499 -0.2586 -0.0889 70   LYS   E O   
11889 C  CB  . LYS   E 70  ? 2.0101 1.6709 1.6821 -0.0450 -0.2438 -0.0891 70   LYS   E CB  
11890 N  N   . GLY   E 71  ? 1.9894 1.6424 1.6419 -0.0376 -0.2542 -0.0900 71   GLY   E N   
11891 C  CA  . GLY   E 71  ? 1.9391 1.5894 1.5916 -0.0378 -0.2652 -0.0916 71   GLY   E CA  
11892 C  C   . GLY   E 71  ? 1.9443 1.6156 1.6193 -0.0415 -0.2624 -0.0884 71   GLY   E C   
11893 O  O   . GLY   E 71  ? 1.9016 1.5845 1.5990 -0.0479 -0.2685 -0.0885 71   GLY   E O   
11894 N  N   . GLU   E 72  ? 1.9066 1.5829 1.5761 -0.0375 -0.2529 -0.0856 72   GLU   E N   
11895 C  CA  . GLU   E 72  ? 1.8826 1.5778 1.5710 -0.0402 -0.2495 -0.0825 72   GLU   E CA  
11896 C  C   . GLU   E 72  ? 1.8678 1.5575 1.5396 -0.0340 -0.2458 -0.0814 72   GLU   E C   
11897 O  O   . GLU   E 72  ? 1.8993 1.5803 1.5529 -0.0285 -0.2371 -0.0806 72   GLU   E O   
11898 C  CB  . GLU   E 72  ? 1.8661 1.5800 1.5736 -0.0437 -0.2375 -0.0788 72   GLU   E CB  
11899 C  CG  . GLU   E 72  ? 1.8767 1.6015 1.6075 -0.0511 -0.2417 -0.0789 72   GLU   E CG  
11900 C  CD  . GLU   E 72  ? 1.9366 1.6708 1.6851 -0.0555 -0.2509 -0.0792 72   GLU   E CD  
11901 O  OE1 . GLU   E 72  ? 1.9117 1.6611 1.6733 -0.0566 -0.2459 -0.0762 72   GLU   E OE1 
11902 O  OE2 . GLU   E 72  ? 2.0197 1.7457 1.7688 -0.0577 -0.2632 -0.0825 72   GLU   E OE2 
11903 N  N   . SER   E 73  ? 1.7928 1.4875 1.4712 -0.0348 -0.2522 -0.0813 73   SER   E N   
11904 C  CA  . SER   E 73  ? 1.7501 1.4368 1.4108 -0.0288 -0.2506 -0.0807 73   SER   E CA  
11905 C  C   . SER   E 73  ? 1.7653 1.4608 1.4251 -0.0261 -0.2350 -0.0766 73   SER   E C   
11906 O  O   . SER   E 73  ? 1.7586 1.4416 1.3963 -0.0198 -0.2294 -0.0763 73   SER   E O   
11907 C  CB  . SER   E 73  ? 1.7261 1.4182 1.3965 -0.0306 -0.2605 -0.0812 73   SER   E CB  
11908 O  OG  . SER   E 73  ? 1.7247 1.4391 1.4202 -0.0352 -0.2558 -0.0779 73   SER   E OG  
11909 N  N   . LYS   E 74  ? 1.7717 1.4879 1.4551 -0.0309 -0.2276 -0.0736 74   LYS   E N   
11910 C  CA  . LYS   E 74  ? 1.7279 1.4542 1.4137 -0.0290 -0.2133 -0.0698 74   LYS   E CA  
11911 C  C   . LYS   E 74  ? 1.6814 1.4235 1.3872 -0.0337 -0.2059 -0.0679 74   LYS   E C   
11912 O  O   . LYS   E 74  ? 1.6532 1.3983 1.3708 -0.0383 -0.2114 -0.0692 74   LYS   E O   
11913 C  CB  . LYS   E 74  ? 1.6503 1.3864 1.3429 -0.0287 -0.2121 -0.0675 74   LYS   E CB  
11914 C  CG  . LYS   E 74  ? 1.6202 1.3734 1.3388 -0.0351 -0.2178 -0.0668 74   LYS   E CG  
11915 C  CD  . LYS   E 74  ? 1.6906 1.4450 1.4090 -0.0340 -0.2231 -0.0665 74   LYS   E CD  
11916 C  CE  . LYS   E 74  ? 1.7564 1.5254 1.4997 -0.0402 -0.2310 -0.0666 74   LYS   E CE  
11917 N  NZ  . LYS   E 74  ? 1.7332 1.5045 1.4783 -0.0393 -0.2369 -0.0663 74   LYS   E NZ  
11918 N  N   . ASP   E 75  ? 1.6704 1.4223 1.3800 -0.0322 -0.1932 -0.0647 75   ASP   E N   
11919 C  CA  . ASP   E 75  ? 1.5857 1.3511 1.3115 -0.0355 -0.1853 -0.0629 75   ASP   E CA  
11920 C  C   . ASP   E 75  ? 1.5519 1.3353 1.3040 -0.0421 -0.1885 -0.0616 75   ASP   E C   
11921 O  O   . ASP   E 75  ? 1.5405 1.3302 1.3003 -0.0435 -0.1929 -0.0609 75   ASP   E O   
11922 C  CB  . ASP   E 75  ? 1.5125 1.2840 1.2364 -0.0322 -0.1715 -0.0600 75   ASP   E CB  
11923 C  CG  . ASP   E 75  ? 1.5445 1.3002 1.2456 -0.0261 -0.1657 -0.0609 75   ASP   E CG  
11924 O  OD1 . ASP   E 75  ? 1.5845 1.3271 1.2745 -0.0253 -0.1704 -0.0636 75   ASP   E OD1 
11925 O  OD2 . ASP   E 75  ? 1.5092 1.2658 1.2042 -0.0222 -0.1560 -0.0589 75   ASP   E OD2 
11926 N  N   . LEU   E 76  ? 1.5228 1.3140 1.2882 -0.0460 -0.1860 -0.0612 76   LEU   E N   
11927 C  CA  . LEU   E 76  ? 1.4570 1.2654 1.2475 -0.0520 -0.1868 -0.0595 76   LEU   E CA  
11928 C  C   . LEU   E 76  ? 1.4336 1.2558 1.2352 -0.0525 -0.1750 -0.0565 76   LEU   E C   
11929 O  O   . LEU   E 76  ? 1.4477 1.2653 1.2399 -0.0494 -0.1676 -0.0563 76   LEU   E O   
11930 C  CB  . LEU   E 76  ? 1.4068 1.2126 1.2050 -0.0567 -0.1947 -0.0616 76   LEU   E CB  
11931 C  CG  . LEU   E 76  ? 1.4549 1.2496 1.2467 -0.0571 -0.2077 -0.0646 76   LEU   E CG  
11932 C  CD1 . LEU   E 76  ? 1.4669 1.2623 1.2711 -0.0626 -0.2148 -0.0662 76   LEU   E CD1 
11933 C  CD2 . LEU   E 76  ? 1.5296 1.3324 1.3290 -0.0575 -0.2110 -0.0635 76   LEU   E CD2 
11934 N  N   . LEU   E 77  ? 1.4094 1.2482 1.2315 -0.0565 -0.1735 -0.0542 77   LEU   E N   
11935 C  CA  . LEU   E 77  ? 1.3344 1.1869 1.1677 -0.0568 -0.1630 -0.0513 77   LEU   E CA  
11936 C  C   . LEU   E 77  ? 1.3220 1.1832 1.1720 -0.0617 -0.1626 -0.0506 77   LEU   E C   
11937 O  O   . LEU   E 77  ? 1.3142 1.1817 1.1784 -0.0662 -0.1686 -0.0505 77   LEU   E O   
11938 C  CB  . LEU   E 77  ? 1.2955 1.1602 1.1384 -0.0570 -0.1606 -0.0489 77   LEU   E CB  
11939 C  CG  . LEU   E 77  ? 1.2144 1.0914 1.0661 -0.0564 -0.1497 -0.0461 77   LEU   E CG  
11940 C  CD1 . LEU   E 77  ? 1.2970 1.1656 1.1332 -0.0515 -0.1423 -0.0465 77   LEU   E CD1 
11941 C  CD2 . LEU   E 77  ? 1.1792 1.0664 1.0384 -0.0563 -0.1477 -0.0440 77   LEU   E CD2 
11942 N  N   . PHE   E 78  ? 1.3148 1.1766 1.1636 -0.0606 -0.1552 -0.0501 78   PHE   E N   
11943 C  CA  . PHE   E 78  ? 1.2993 1.1702 1.1637 -0.0646 -0.1531 -0.0489 78   PHE   E CA  
11944 C  C   . PHE   E 78  ? 1.2510 1.1366 1.1270 -0.0643 -0.1440 -0.0459 78   PHE   E C   
11945 O  O   . PHE   E 78  ? 1.2304 1.1159 1.0989 -0.0602 -0.1367 -0.0453 78   PHE   E O   
11946 C  CB  . PHE   E 78  ? 1.2597 1.1213 1.1165 -0.0641 -0.1520 -0.0504 78   PHE   E CB  
11947 C  CG  . PHE   E 78  ? 1.2114 1.0817 1.0837 -0.0681 -0.1497 -0.0491 78   PHE   E CG  
11948 C  CD1 . PHE   E 78  ? 1.2259 1.0971 1.1090 -0.0733 -0.1566 -0.0496 78   PHE   E CD1 
11949 C  CD2 . PHE   E 78  ? 1.1831 1.0611 1.0599 -0.0667 -0.1406 -0.0472 78   PHE   E CD2 
11950 C  CE1 . PHE   E 78  ? 1.1998 1.0785 1.0968 -0.0769 -0.1539 -0.0481 78   PHE   E CE1 
11951 C  CE2 . PHE   E 78  ? 1.1833 1.0685 1.0733 -0.0701 -0.1385 -0.0459 78   PHE   E CE2 
11952 C  CZ  . PHE   E 78  ? 1.1735 1.0588 1.0733 -0.0752 -0.1448 -0.0462 78   PHE   E CZ  
11953 N  N   . ILE   E 79  ? 1.2159 1.1138 1.1102 -0.0687 -0.1443 -0.0442 79   ILE   E N   
11954 C  CA  . ILE   E 79  ? 1.1806 1.0928 1.0871 -0.0688 -0.1369 -0.0413 79   ILE   E CA  
11955 C  C   . ILE   E 79  ? 1.2108 1.1302 1.1319 -0.0728 -0.1359 -0.0402 79   ILE   E C   
11956 O  O   . ILE   E 79  ? 1.2259 1.1464 1.1562 -0.0771 -0.1419 -0.0403 79   ILE   E O   
11957 C  CB  . ILE   E 79  ? 1.1346 1.0555 1.0483 -0.0692 -0.1382 -0.0399 79   ILE   E CB  
11958 C  CG1 . ILE   E 79  ? 1.1546 1.0711 1.0549 -0.0644 -0.1352 -0.0401 79   ILE   E CG1 
11959 C  CG2 . ILE   E 79  ? 1.1675 1.1035 1.0978 -0.0711 -0.1329 -0.0372 79   ILE   E CG2 
11960 C  CD1 . ILE   E 79  ? 1.1289 1.0518 1.0341 -0.0646 -0.1372 -0.0389 79   ILE   E CD1 
11961 N  N   . LEU   E 80  ? 1.1995 1.1230 1.1224 -0.0714 -0.1283 -0.0390 80   LEU   E N   
11962 C  CA  . LEU   E 80  ? 1.1350 1.0647 1.0702 -0.0744 -0.1261 -0.0376 80   LEU   E CA  
11963 C  C   . LEU   E 80  ? 1.1425 1.0857 1.0882 -0.0737 -0.1194 -0.0350 80   LEU   E C   
11964 O  O   . LEU   E 80  ? 1.1369 1.0815 1.0774 -0.0698 -0.1134 -0.0347 80   LEU   E O   
11965 C  CB  . LEU   E 80  ? 1.0926 1.0141 1.0197 -0.0730 -0.1236 -0.0388 80   LEU   E CB  
11966 C  CG  . LEU   E 80  ? 1.1293 1.0567 1.0682 -0.0757 -0.1206 -0.0372 80   LEU   E CG  
11967 C  CD1 . LEU   E 80  ? 1.1579 1.0878 1.1087 -0.0811 -0.1263 -0.0367 80   LEU   E CD1 
11968 C  CD2 . LEU   E 80  ? 1.1757 1.0940 1.1059 -0.0742 -0.1187 -0.0385 80   LEU   E CD2 
11969 N  N   . THR   E 81  ? 1.1405 1.0934 1.1012 -0.0772 -0.1206 -0.0332 81   THR   E N   
11970 C  CA  . THR   E 81  ? 1.1003 1.0657 1.0706 -0.0765 -0.1149 -0.0307 81   THR   E CA  
11971 C  C   . THR   E 81  ? 1.1213 1.0900 1.0959 -0.0761 -0.1089 -0.0296 81   THR   E C   
11972 O  O   . THR   E 81  ? 1.1274 1.0902 1.1005 -0.0774 -0.1097 -0.0302 81   THR   E O   
11973 C  CB  . THR   E 81  ? 1.1096 1.0842 1.0940 -0.0800 -0.1180 -0.0291 81   THR   E CB  
11974 O  OG1 . THR   E 81  ? 1.1192 1.0958 1.1142 -0.0839 -0.1190 -0.0282 81   THR   E OG1 
11975 C  CG2 . THR   E 81  ? 1.1108 1.0810 1.0916 -0.0809 -0.1255 -0.0305 81   THR   E CG2 
11976 N  N   . ALA   E 82  ? 1.1239 1.1019 1.1039 -0.0741 -0.1032 -0.0279 82   ALA   E N   
11977 C  CA  . ALA   E 82  ? 1.0913 1.0728 1.0753 -0.0732 -0.0976 -0.0267 82   ALA   E CA  
11978 C  C   . ALA   E 82  ? 1.1250 1.1081 1.1188 -0.0772 -0.0988 -0.0254 82   ALA   E C   
11979 O  O   . ALA   E 82  ? 1.1423 1.1221 1.1349 -0.0769 -0.0963 -0.0254 82   ALA   E O   
11980 C  CB  . ALA   E 82  ? 1.0650 1.0568 1.0545 -0.0708 -0.0924 -0.0251 82   ALA   E CB  
11981 N  N   . LYS   E 83  ? 1.1449 1.1329 1.1488 -0.0809 -0.1025 -0.0244 83   LYS   E N   
11982 C  CA  . LYS   E 83  ? 1.1170 1.1063 1.1313 -0.0851 -0.1038 -0.0230 83   LYS   E CA  
11983 C  C   . LYS   E 83  ? 1.1385 1.1173 1.1481 -0.0875 -0.1084 -0.0248 83   LYS   E C   
11984 O  O   . LYS   E 83  ? 1.1592 1.1386 1.1781 -0.0915 -0.1102 -0.0239 83   LYS   E O   
11985 C  CB  . LYS   E 83  ? 1.1217 1.1195 1.1486 -0.0882 -0.1065 -0.0215 83   LYS   E CB  
11986 C  CG  . LYS   E 83  ? 1.1583 1.1669 1.1915 -0.0863 -0.1021 -0.0195 83   LYS   E CG  
11987 C  CD  . LYS   E 83  ? 1.1070 1.1226 1.1523 -0.0881 -0.0981 -0.0168 83   LYS   E CD  
11988 C  CE  . LYS   E 83  ? 1.0498 1.0761 1.1020 -0.0866 -0.0950 -0.0149 83   LYS   E CE  
11989 N  NZ  . LYS   E 83  ? 1.0624 1.0958 1.1287 -0.0896 -0.0942 -0.0124 83   LYS   E NZ  
11990 N  N   . TYR   E 84  ? 1.1435 1.1127 1.1394 -0.0851 -0.1101 -0.0273 84   TYR   E N   
11991 C  CA  . TYR   E 84  ? 1.1863 1.1439 1.1754 -0.0869 -0.1150 -0.0294 84   TYR   E CA  
11992 C  C   . TYR   E 84  ? 1.2020 1.1575 1.1943 -0.0902 -0.1230 -0.0305 84   TYR   E C   
11993 O  O   . TYR   E 84  ? 1.2464 1.1942 1.2382 -0.0931 -0.1278 -0.0318 84   TYR   E O   
11994 C  CB  . TYR   E 84  ? 1.2640 1.2191 1.2573 -0.0891 -0.1128 -0.0285 84   TYR   E CB  
11995 C  CG  . TYR   E 84  ? 1.2966 1.2506 1.2836 -0.0852 -0.1061 -0.0281 84   TYR   E CG  
11996 C  CD1 . TYR   E 84  ? 1.3196 1.2643 1.2923 -0.0817 -0.1057 -0.0304 84   TYR   E CD1 
11997 C  CD2 . TYR   E 84  ? 1.3652 1.3271 1.3601 -0.0846 -0.1003 -0.0257 84   TYR   E CD2 
11998 C  CE1 . TYR   E 84  ? 1.3159 1.2598 1.2833 -0.0779 -0.0999 -0.0302 84   TYR   E CE1 
11999 C  CE2 . TYR   E 84  ? 1.3779 1.3385 1.3668 -0.0807 -0.0948 -0.0256 84   TYR   E CE2 
12000 C  CZ  . TYR   E 84  ? 1.3057 1.2575 1.2813 -0.0774 -0.0948 -0.0280 84   TYR   E CZ  
12001 O  OH  . TYR   E 84  ? 1.2181 1.1686 1.1883 -0.0734 -0.0898 -0.0281 84   TYR   E OH  
12002 N  N   . ASN   E 85  ? 1.1766 1.1384 1.1722 -0.0898 -0.1248 -0.0301 85   ASN   E N   
12003 C  CA  . ASN   E 85  ? 1.1671 1.1260 1.1640 -0.0922 -0.1330 -0.0315 85   ASN   E CA  
12004 C  C   . ASN   E 85  ? 1.1670 1.1139 1.1463 -0.0891 -0.1367 -0.0344 85   ASN   E C   
12005 O  O   . ASN   E 85  ? 1.1555 1.1018 1.1250 -0.0848 -0.1329 -0.0347 85   ASN   E O   
12006 C  CB  . ASN   E 85  ? 1.1177 1.0872 1.1242 -0.0927 -0.1338 -0.0300 85   ASN   E CB  
12007 C  CG  . ASN   E 85  ? 1.1233 1.1052 1.1449 -0.0942 -0.1282 -0.0269 85   ASN   E CG  
12008 O  OD1 . ASN   E 85  ? 1.1276 1.1177 1.1516 -0.0920 -0.1239 -0.0253 85   ASN   E OD1 
12009 N  ND2 . ASN   E 85  ? 1.0608 1.0432 1.0921 -0.0980 -0.1282 -0.0260 85   ASN   E ND2 
12010 N  N   . ALA   E 86  ? 1.2313 1.1685 1.2067 -0.0912 -0.1438 -0.0367 86   ALA   E N   
12011 C  CA  . ALA   E 86  ? 1.2088 1.1335 1.1670 -0.0883 -0.1480 -0.0396 86   ALA   E CA  
12012 C  C   . ALA   E 86  ? 1.2415 1.1643 1.2011 -0.0899 -0.1569 -0.0410 86   ALA   E C   
12013 O  O   . ALA   E 86  ? 1.2106 1.1390 1.1846 -0.0942 -0.1612 -0.0404 86   ALA   E O   
12014 C  CB  . ALA   E 86  ? 1.2269 1.1394 1.1763 -0.0886 -0.1497 -0.0415 86   ALA   E CB  
12015 N  N   . CYS   E 87  ? 1.2530 1.1676 1.1974 -0.0861 -0.1594 -0.0428 87   CYS   E N   
12016 C  CA  . CYS   E 87  ? 1.3242 1.2355 1.2670 -0.0867 -0.1681 -0.0444 87   CYS   E CA  
12017 C  C   . CYS   E 87  ? 1.3252 1.2220 1.2465 -0.0822 -0.1708 -0.0470 87   CYS   E C   
12018 O  O   . CYS   E 87  ? 1.3212 1.2142 1.2305 -0.0781 -0.1642 -0.0469 87   CYS   E O   
12019 C  CB  . CYS   E 87  ? 1.3087 1.2322 1.2611 -0.0865 -0.1668 -0.0423 87   CYS   E CB  
12020 S  SG  . CYS   E 87  ? 1.3055 1.2324 1.2479 -0.0809 -0.1576 -0.0408 87   CYS   E SG  
12021 N  N   . ILE   E 88  ? 1.3061 1.1945 1.2225 -0.0828 -0.1805 -0.0494 88   ILE   E N   
12022 C  CA  . ILE   E 88  ? 1.3361 1.2102 1.2314 -0.0783 -0.1840 -0.0519 88   ILE   E CA  
12023 C  C   . ILE   E 88  ? 1.3796 1.2550 1.2752 -0.0776 -0.1901 -0.0523 88   ILE   E C   
12024 O  O   . ILE   E 88  ? 1.3829 1.2612 1.2901 -0.0814 -0.1981 -0.0530 88   ILE   E O   
12025 C  CB  . ILE   E 88  ? 1.3269 1.1859 1.2119 -0.0788 -0.1909 -0.0551 88   ILE   E CB  
12026 C  CG1 . ILE   E 88  ? 1.3098 1.1675 1.1944 -0.0793 -0.1846 -0.0546 88   ILE   E CG1 
12027 C  CG2 . ILE   E 88  ? 1.3165 1.1601 1.1784 -0.0735 -0.1940 -0.0575 88   ILE   E CG2 
12028 C  CD1 . ILE   E 88  ? 1.3257 1.1697 1.2029 -0.0806 -0.1913 -0.0576 88   ILE   E CD1 
12029 N  N   . LEU   E 89  ? 1.4173 1.2900 1.3000 -0.0727 -0.1864 -0.0519 89   LEU   E N   
12030 C  CA  . LEU   E 89  ? 1.4218 1.2977 1.3049 -0.0715 -0.1896 -0.0514 89   LEU   E CA  
12031 C  C   . LEU   E 89  ? 1.4639 1.3234 1.3249 -0.0668 -0.1948 -0.0539 89   LEU   E C   
12032 O  O   . LEU   E 89  ? 1.4403 1.2889 1.2839 -0.0629 -0.1908 -0.0548 89   LEU   E O   
12033 C  CB  . LEU   E 89  ? 1.3521 1.2399 1.2401 -0.0697 -0.1797 -0.0482 89   LEU   E CB  
12034 C  CG  . LEU   E 89  ? 1.2824 1.1848 1.1878 -0.0727 -0.1722 -0.0455 89   LEU   E CG  
12035 C  CD1 . LEU   E 89  ? 1.2303 1.1406 1.1354 -0.0697 -0.1634 -0.0431 89   LEU   E CD1 
12036 C  CD2 . LEU   E 89  ? 1.3297 1.2429 1.2557 -0.0779 -0.1770 -0.0447 89   LEU   E CD2 
12037 N  N   . GLU   E 90  ? 1.5243 1.3820 1.3859 -0.0670 -0.2036 -0.0551 90   GLU   E N   
12038 C  CA  . GLU   E 90  ? 1.5919 1.4342 1.4324 -0.0623 -0.2090 -0.0573 90   GLU   E CA  
12039 C  C   . GLU   E 90  ? 1.5830 1.4307 1.4240 -0.0602 -0.2087 -0.0558 90   GLU   E C   
12040 O  O   . GLU   E 90  ? 1.5507 1.4122 1.4101 -0.0636 -0.2098 -0.0542 90   GLU   E O   
12041 C  CB  . GLU   E 90  ? 1.6639 1.4950 1.5010 -0.0638 -0.2222 -0.0610 90   GLU   E CB  
12042 C  CG  . GLU   E 90  ? 1.7353 1.5488 1.5491 -0.0586 -0.2285 -0.0635 90   GLU   E CG  
12043 C  CD  . GLU   E 90  ? 1.8058 1.6110 1.6202 -0.0605 -0.2429 -0.0671 90   GLU   E CD  
12044 O  OE1 . GLU   E 90  ? 1.7919 1.6057 1.6260 -0.0662 -0.2472 -0.0674 90   GLU   E OE1 
12045 O  OE2 . GLU   E 90  ? 1.8783 1.6683 1.6739 -0.0563 -0.2499 -0.0695 90   GLU   E OE2 
12046 N  N   . TYR   E 91  ? 1.7968 1.6328 1.6169 -0.0546 -0.2070 -0.0562 91   TYR   E N   
12047 C  CA  . TYR   E 91  ? 1.8313 1.6693 1.6481 -0.0519 -0.2070 -0.0550 91   TYR   E CA  
12048 C  C   . TYR   E 91  ? 1.9299 1.7593 1.7422 -0.0516 -0.2204 -0.0578 91   TYR   E C   
12049 O  O   . TYR   E 91  ? 1.9462 1.7586 1.7411 -0.0491 -0.2270 -0.0608 91   TYR   E O   
12050 C  CB  . TYR   E 91  ? 1.7981 1.6268 1.5944 -0.0459 -0.1985 -0.0541 91   TYR   E CB  
12051 C  CG  . TYR   E 91  ? 1.8066 1.6379 1.5994 -0.0431 -0.1960 -0.0523 91   TYR   E CG  
12052 C  CD1 . TYR   E 91  ? 1.8470 1.6664 1.6257 -0.0398 -0.2040 -0.0539 91   TYR   E CD1 
12053 C  CD2 . TYR   E 91  ? 1.7971 1.6422 1.6003 -0.0435 -0.1857 -0.0489 91   TYR   E CD2 
12054 C  CE1 . TYR   E 91  ? 1.8719 1.6930 1.6469 -0.0371 -0.2016 -0.0522 91   TYR   E CE1 
12055 C  CE2 . TYR   E 91  ? 1.8199 1.6671 1.6200 -0.0410 -0.1833 -0.0472 91   TYR   E CE2 
12056 C  CZ  . TYR   E 91  ? 1.8774 1.7126 1.6633 -0.0378 -0.1910 -0.0488 91   TYR   E CZ  
12057 O  OH  . TYR   E 91  ? 1.9118 1.7486 1.6942 -0.0353 -0.1885 -0.0469 91   TYR   E OH  
12058 N  N   . LYS   E 92  ? 1.8938 1.7342 1.7212 -0.0539 -0.2246 -0.0569 92   LYS   E N   
12059 C  CA  . LYS   E 92  ? 1.8436 1.6777 1.6692 -0.0537 -0.2376 -0.0594 92   LYS   E CA  
12060 C  C   . LYS   E 92  ? 1.8299 1.6677 1.6537 -0.0509 -0.2366 -0.0577 92   LYS   E C   
12061 O  O   . LYS   E 92  ? 1.8235 1.6777 1.6650 -0.0534 -0.2321 -0.0550 92   LYS   E O   
12062 C  CB  . LYS   E 92  ? 1.7472 1.5912 1.5959 -0.0599 -0.2457 -0.0604 92   LYS   E CB  
12063 N  N   . GLN   E 93  ? 1.8990 1.7211 1.7010 -0.0456 -0.2411 -0.0593 93   GLN   E N   
12064 C  CA  . GLN   E 93  ? 1.9581 1.7807 1.7543 -0.0421 -0.2399 -0.0578 93   GLN   E CA  
12065 C  C   . GLN   E 93  ? 2.0289 1.8427 1.8203 -0.0408 -0.2543 -0.0608 93   GLN   E C   
12066 O  O   . GLN   E 93  ? 2.0545 1.8501 1.8264 -0.0375 -0.2616 -0.0639 93   GLN   E O   
12067 C  CB  . GLN   E 93  ? 1.9377 1.7490 1.7108 -0.0363 -0.2305 -0.0565 93   GLN   E CB  
12068 C  CG  . GLN   E 93  ? 1.9100 1.7303 1.6858 -0.0346 -0.2219 -0.0530 93   GLN   E CG  
12069 C  CD  . GLN   E 93  ? 1.9619 1.7795 1.7348 -0.0326 -0.2301 -0.0536 93   GLN   E CD  
12070 O  OE1 . GLN   E 93  ? 1.9378 1.7700 1.7289 -0.0354 -0.2309 -0.0520 93   GLN   E OE1 
12071 N  NE2 . GLN   E 93  ? 2.0105 1.8088 1.7600 -0.0276 -0.2365 -0.0559 93   GLN   E NE2 
12072 N  N   . SER   E 94  ? 2.0423 1.8687 1.8513 -0.0433 -0.2587 -0.0600 94   SER   E N   
12073 C  CA  . SER   E 94  ? 2.0269 1.8474 1.8350 -0.0423 -0.2727 -0.0628 94   SER   E CA  
12074 C  C   . SER   E 94  ? 2.0977 1.9162 1.8964 -0.0378 -0.2718 -0.0613 94   SER   E C   
12075 O  O   . SER   E 94  ? 2.1061 1.9344 1.9189 -0.0392 -0.2768 -0.0609 94   SER   E O   
12076 C  CB  . SER   E 94  ? 1.9514 1.7872 1.7879 -0.0486 -0.2796 -0.0634 94   SER   E CB  
12077 O  OG  . SER   E 94  ? 1.9575 1.8073 1.8086 -0.0495 -0.2783 -0.0611 94   SER   E OG  
12078 N  N   . GLY   E 95  ? 2.0719 1.8773 1.8463 -0.0323 -0.2650 -0.0605 95   GLY   E N   
12079 C  CA  . GLY   E 95  ? 2.0289 1.8299 1.7911 -0.0275 -0.2629 -0.0590 95   GLY   E CA  
12080 C  C   . GLY   E 95  ? 1.9527 1.7695 1.7266 -0.0287 -0.2502 -0.0546 95   GLY   E C   
12081 O  O   . GLY   E 95  ? 1.9469 1.7586 1.7066 -0.0252 -0.2397 -0.0524 95   GLY   E O   
12082 N  N   . GLU   E 96  ? 2.0436 1.8794 1.8432 -0.0335 -0.2509 -0.0532 96   GLU   E N   
12083 C  CA  . GLU   E 96  ? 1.9846 1.8363 1.7972 -0.0351 -0.2393 -0.0492 96   GLU   E CA  
12084 C  C   . GLU   E 96  ? 2.0268 1.8965 1.8646 -0.0413 -0.2350 -0.0479 96   GLU   E C   
12085 O  O   . GLU   E 96  ? 1.9516 1.8342 1.7999 -0.0427 -0.2249 -0.0447 96   GLU   E O   
12086 C  CB  . GLU   E 96  ? 1.8529 1.7106 1.6711 -0.0339 -0.2425 -0.0480 96   GLU   E CB  
12087 N  N   . SER   E 97  ? 2.1908 2.0613 2.0382 -0.0449 -0.2425 -0.0503 97   SER   E N   
12088 C  CA  . SER   E 97  ? 2.1751 2.0614 2.0461 -0.0509 -0.2392 -0.0492 97   SER   E CA  
12089 C  C   . SER   E 97  ? 2.1412 2.0220 2.0047 -0.0513 -0.2328 -0.0495 97   SER   E C   
12090 O  O   . SER   E 97  ? 2.1410 2.0133 2.0008 -0.0524 -0.2392 -0.0523 97   SER   E O   
12091 C  CB  . SER   E 97  ? 2.1995 2.0905 2.0873 -0.0549 -0.2512 -0.0515 97   SER   E CB  
12092 O  OG  . SER   E 97  ? 2.2243 2.1261 2.1306 -0.0603 -0.2483 -0.0509 97   SER   E OG  
12093 N  N   . ILE   E 98  ? 1.9016 1.7873 1.7633 -0.0504 -0.2203 -0.0467 98   ILE   E N   
12094 C  CA  . ILE   E 98  ? 1.8048 1.6881 1.6627 -0.0511 -0.2132 -0.0466 98   ILE   E CA  
12095 C  C   . ILE   E 98  ? 1.7802 1.6785 1.6617 -0.0570 -0.2119 -0.0457 98   ILE   E C   
12096 O  O   . ILE   E 98  ? 1.8338 1.7475 1.7328 -0.0594 -0.2079 -0.0433 98   ILE   E O   
12097 C  CB  . ILE   E 98  ? 1.7518 1.6351 1.6001 -0.0479 -0.2004 -0.0440 98   ILE   E CB  
12098 C  CG1 . ILE   E 98  ? 1.8014 1.6759 1.6334 -0.0429 -0.2005 -0.0436 98   ILE   E CG1 
12099 C  CG2 . ILE   E 98  ? 1.7489 1.6222 1.5841 -0.0464 -0.1957 -0.0450 98   ILE   E CG2 
12100 C  CD1 . ILE   E 98  ? 1.7449 1.6229 1.5726 -0.0405 -0.1877 -0.0406 98   ILE   E CD1 
12101 N  N   . ASP   E 99  ? 1.7200 1.6133 1.6015 -0.0591 -0.2148 -0.0477 99   ASP   E N   
12102 C  CA  . ASP   E 99  ? 1.6894 1.5953 1.5918 -0.0645 -0.2128 -0.0468 99   ASP   E CA  
12103 C  C   . ASP   E 99  ? 1.6550 1.5531 1.5496 -0.0648 -0.2098 -0.0479 99   ASP   E C   
12104 O  O   . ASP   E 99  ? 1.6397 1.5220 1.5161 -0.0620 -0.2140 -0.0505 99   ASP   E O   
12105 C  CB  . ASP   E 99  ? 1.7100 1.6211 1.6291 -0.0686 -0.2235 -0.0482 99   ASP   E CB  
12106 C  CG  . ASP   E 99  ? 1.8101 1.7353 1.7451 -0.0698 -0.2235 -0.0461 99   ASP   E CG  
12107 O  OD1 . ASP   E 99  ? 1.8584 1.7961 1.8035 -0.0708 -0.2140 -0.0430 99   ASP   E OD1 
12108 O  OD2 . ASP   E 99  ? 1.8411 1.7643 1.7779 -0.0695 -0.2332 -0.0477 99   ASP   E OD2 
12109 N  N   . ILE   E 100 ? 1.6133 1.5223 1.5214 -0.0679 -0.2025 -0.0460 100  ILE   E N   
12110 C  CA  . ILE   E 100 ? 1.5170 1.4203 1.4201 -0.0686 -0.1991 -0.0469 100  ILE   E CA  
12111 C  C   . ILE   E 100 ? 1.4572 1.3648 1.3765 -0.0740 -0.2049 -0.0479 100  ILE   E C   
12112 O  O   . ILE   E 100 ? 1.4415 1.3631 1.3801 -0.0778 -0.2014 -0.0457 100  ILE   E O   
12113 C  CB  . ILE   E 100 ? 1.4626 1.3732 1.3673 -0.0677 -0.1864 -0.0442 100  ILE   E CB  
12114 C  CG1 . ILE   E 100 ? 1.4916 1.3988 1.3821 -0.0626 -0.1804 -0.0430 100  ILE   E CG1 
12115 C  CG2 . ILE   E 100 ? 1.4455 1.3486 1.3432 -0.0677 -0.1838 -0.0454 100  ILE   E CG2 
12116 C  CD1 . ILE   E 100 ? 1.5844 1.4737 1.4510 -0.0581 -0.1811 -0.0452 100  ILE   E CD1 
12117 N  N   . ILE   E 101 ? 1.4423 1.3374 1.3535 -0.0744 -0.2134 -0.0510 101  ILE   E N   
12118 C  CA  . ILE   E 101 ? 1.4221 1.3199 1.3485 -0.0796 -0.2199 -0.0523 101  ILE   E CA  
12119 C  C   . ILE   E 101 ? 1.4438 1.3415 1.3719 -0.0815 -0.2137 -0.0518 101  ILE   E C   
12120 O  O   . ILE   E 101 ? 1.4383 1.3292 1.3517 -0.0782 -0.2071 -0.0517 101  ILE   E O   
12121 C  CB  . ILE   E 101 ? 1.4296 1.3138 1.3474 -0.0793 -0.2329 -0.0562 101  ILE   E CB  
12122 C  CG1 . ILE   E 101 ? 1.5363 1.4031 1.4324 -0.0763 -0.2336 -0.0586 101  ILE   E CG1 
12123 C  CG2 . ILE   E 101 ? 1.4489 1.3307 1.3592 -0.0757 -0.2376 -0.0566 101  ILE   E CG2 
12124 C  CD1 . ILE   E 101 ? 1.5413 1.4041 1.4430 -0.0803 -0.2369 -0.0604 101  ILE   E CD1 
12125 N  N   . THR   E 102 ? 1.4303 1.3355 1.3769 -0.0869 -0.2156 -0.0514 102  THR   E N   
12126 C  CA  . THR   E 102 ? 1.3858 1.2923 1.3368 -0.0892 -0.2096 -0.0506 102  THR   E CA  
12127 C  C   . THR   E 102 ? 1.3907 1.2856 1.3389 -0.0916 -0.2184 -0.0538 102  THR   E C   
12128 O  O   . THR   E 102 ? 1.4106 1.3103 1.3755 -0.0965 -0.2238 -0.0542 102  THR   E O   
12129 C  CB  . THR   E 102 ? 1.3597 1.2831 1.3335 -0.0934 -0.2038 -0.0474 102  THR   E CB  
12130 O  OG1 . THR   E 102 ? 1.3535 1.2879 1.3330 -0.0918 -0.1999 -0.0450 102  THR   E OG1 
12131 C  CG2 . THR   E 102 ? 1.3106 1.2355 1.2836 -0.0935 -0.1942 -0.0458 102  THR   E CG2 
12132 N  N   . ARG   E 103 ? 1.3608 1.2403 1.2879 -0.0880 -0.2196 -0.0561 103  ARG   E N   
12133 C  CA  . ARG   E 103 ? 1.3635 1.2304 1.2857 -0.0897 -0.2280 -0.0594 103  ARG   E CA  
12134 C  C   . ARG   E 103 ? 1.4298 1.3009 1.3647 -0.0944 -0.2245 -0.0585 103  ARG   E C   
12135 O  O   . ARG   E 103 ? 1.4889 1.3553 1.4302 -0.0982 -0.2321 -0.0606 103  ARG   E O   
12136 C  CB  . ARG   E 103 ? 1.3669 1.2163 1.2625 -0.0843 -0.2287 -0.0618 103  ARG   E CB  
12137 N  N   . ALA   E 104 ? 1.4014 1.2807 1.3399 -0.0940 -0.2132 -0.0556 104  ALA   E N   
12138 C  CA  . ALA   E 104 ? 1.3974 1.2811 1.3479 -0.0981 -0.2091 -0.0543 104  ALA   E CA  
12139 C  C   . ALA   E 104 ? 1.3915 1.2891 1.3513 -0.0979 -0.1977 -0.0504 104  ALA   E C   
12140 O  O   . ALA   E 104 ? 1.4061 1.3061 1.3574 -0.0937 -0.1918 -0.0492 104  ALA   E O   
12141 C  CB  . ALA   E 104 ? 1.4546 1.3241 1.3897 -0.0967 -0.2087 -0.0563 104  ALA   E CB  
12142 N  N   . HIS   E 105 ? 1.3672 1.2737 1.3444 -0.1024 -0.1945 -0.0485 105  HIS   E N   
12143 C  CA  . HIS   E 105 ? 1.3128 1.2324 1.2997 -0.1023 -0.1842 -0.0448 105  HIS   E CA  
12144 C  C   . HIS   E 105 ? 1.3264 1.2493 1.3259 -0.1066 -0.1808 -0.0434 105  HIS   E C   
12145 O  O   . HIS   E 105 ? 1.3584 1.2798 1.3683 -0.1112 -0.1868 -0.0443 105  HIS   E O   
12146 C  CB  . HIS   E 105 ? 1.2958 1.2287 1.2959 -0.1030 -0.1839 -0.0428 105  HIS   E CB  
12147 C  CG  . HIS   E 105 ? 1.2221 1.1619 1.2422 -0.1084 -0.1895 -0.0424 105  HIS   E CG  
12148 N  ND1 . HIS   E 105 ? 1.1975 1.1513 1.2361 -0.1111 -0.1844 -0.0393 105  HIS   E ND1 
12149 C  CD2 . HIS   E 105 ? 1.2689 1.2034 1.2935 -0.1114 -0.1998 -0.0449 105  HIS   E CD2 
12150 C  CE1 . HIS   E 105 ? 1.2091 1.1664 1.2634 -0.1156 -0.1908 -0.0397 105  HIS   E CE1 
12151 N  NE2 . HIS   E 105 ? 1.2375 1.1835 1.2842 -0.1160 -0.2005 -0.0432 105  HIS   E NE2 
12152 N  N   . GLY   E 106 ? 1.4294 1.3569 1.4283 -0.1050 -0.1712 -0.0411 106  GLY   E N   
12153 C  CA  . GLY   E 106 ? 1.4431 1.3742 1.4533 -0.1085 -0.1667 -0.0392 106  GLY   E CA  
12154 C  C   . GLY   E 106 ? 1.3816 1.3182 1.3893 -0.1055 -0.1562 -0.0368 106  GLY   E C   
12155 O  O   . GLY   E 106 ? 1.3711 1.3084 1.3685 -0.1009 -0.1525 -0.0367 106  GLY   E O   
12156 N  N   . ASN   E 107 ? 1.2384 1.1784 1.2556 -0.1080 -0.1514 -0.0348 107  ASN   E N   
12157 C  CA  . ASN   E 107 ? 1.2719 1.2166 1.2876 -0.1054 -0.1420 -0.0325 107  ASN   E CA  
12158 C  C   . ASN   E 107 ? 1.2798 1.2144 1.2868 -0.1050 -0.1397 -0.0334 107  ASN   E C   
12159 O  O   . ASN   E 107 ? 1.3129 1.2440 1.3266 -0.1090 -0.1415 -0.0333 107  ASN   E O   
12160 C  CB  . ASN   E 107 ? 1.2818 1.2391 1.3150 -0.1079 -0.1373 -0.0292 107  ASN   E CB  
12161 C  CG  . ASN   E 107 ? 1.2653 1.2284 1.2963 -0.1044 -0.1284 -0.0270 107  ASN   E CG  
12162 O  OD1 . ASN   E 107 ? 1.3033 1.2603 1.3227 -0.1012 -0.1247 -0.0277 107  ASN   E OD1 
12163 N  ND2 . ASN   E 107 ? 1.2468 1.2216 1.2891 -0.1047 -0.1249 -0.0245 107  ASN   E ND2 
12164 N  N   . VAL   E 108 ? 1.2882 1.2185 1.2811 -0.1001 -0.1356 -0.0341 108  VAL   E N   
12165 C  CA  . VAL   E 108 ? 1.3840 1.3041 1.3666 -0.0988 -0.1337 -0.0352 108  VAL   E CA  
12166 C  C   . VAL   E 108 ? 1.4862 1.4112 1.4728 -0.0979 -0.1253 -0.0327 108  VAL   E C   
12167 O  O   . VAL   E 108 ? 1.4938 1.4118 1.4704 -0.0952 -0.1221 -0.0334 108  VAL   E O   
12168 C  CB  . VAL   E 108 ? 1.3741 1.2852 1.3381 -0.0939 -0.1344 -0.0378 108  VAL   E CB  
12169 C  CG1 . VAL   E 108 ? 1.2955 1.1985 1.2533 -0.0948 -0.1432 -0.0405 108  VAL   E CG1 
12170 C  CG2 . VAL   E 108 ? 1.3697 1.2889 1.3313 -0.0895 -0.1288 -0.0366 108  VAL   E CG2 
12171 N  N   . GLN   E 109 ? 1.7411 1.6773 1.7417 -0.0997 -0.1218 -0.0299 109  GLN   E N   
12172 C  CA  . GLN   E 109 ? 1.7552 1.6953 1.7590 -0.0985 -0.1142 -0.0275 109  GLN   E CA  
12173 C  C   . GLN   E 109 ? 1.8003 1.7328 1.8055 -0.1015 -0.1139 -0.0272 109  GLN   E C   
12174 O  O   . GLN   E 109 ? 1.8374 1.7688 1.8519 -0.1065 -0.1180 -0.0271 109  GLN   E O   
12175 C  CB  . GLN   E 109 ? 1.7376 1.6909 1.7557 -0.0998 -0.1108 -0.0245 109  GLN   E CB  
12176 C  CG  . GLN   E 109 ? 1.8137 1.7702 1.8362 -0.0992 -0.1036 -0.0219 109  GLN   E CG  
12177 C  CD  . GLN   E 109 ? 1.8456 1.8033 1.8589 -0.0935 -0.0981 -0.0219 109  GLN   E CD  
12178 O  OE1 . GLN   E 109 ? 1.8743 1.8242 1.8774 -0.0910 -0.0962 -0.0230 109  GLN   E OE1 
12179 N  NE2 . GLN   E 109 ? 1.8046 1.7723 1.8220 -0.0914 -0.0957 -0.0208 109  GLN   E NE2 
12180 N  N   . ASP   E 110 ? 1.6868 1.6137 1.6830 -0.0985 -0.1093 -0.0273 110  ASP   E N   
12181 C  CA  . ASP   E 110 ? 1.6559 1.5756 1.6531 -0.1009 -0.1079 -0.0266 110  ASP   E CA  
12182 C  C   . ASP   E 110 ? 1.7007 1.6278 1.7072 -0.1011 -0.1009 -0.0232 110  ASP   E C   
12183 O  O   . ASP   E 110 ? 1.6961 1.6308 1.7024 -0.0974 -0.0964 -0.0220 110  ASP   E O   
12184 C  CB  . ASP   E 110 ? 1.6008 1.5091 1.5822 -0.0973 -0.1071 -0.0287 110  ASP   E CB  
12185 C  CG  . ASP   E 110 ? 1.5580 1.4571 1.5290 -0.0970 -0.1138 -0.0321 110  ASP   E CG  
12186 O  OD1 . ASP   E 110 ? 1.5700 1.4680 1.5468 -0.1012 -0.1201 -0.0329 110  ASP   E OD1 
12187 O  OD2 . ASP   E 110 ? 1.5280 1.4206 1.4850 -0.0925 -0.1130 -0.0340 110  ASP   E OD2 
12188 N  N   . ARG   E 111 ? 1.7225 1.6472 1.7372 -0.1053 -0.1001 -0.0215 111  ARG   E N   
12189 C  CA  . ARG   E 111 ? 1.6929 1.6237 1.7164 -0.1056 -0.0933 -0.0180 111  ARG   E CA  
12190 C  C   . ARG   E 111 ? 1.6992 1.6274 1.7122 -0.1002 -0.0873 -0.0176 111  ARG   E C   
12191 O  O   . ARG   E 111 ? 1.7293 1.6655 1.7437 -0.0969 -0.0830 -0.0162 111  ARG   E O   
12192 C  CB  . ARG   E 111 ? 1.7016 1.6280 1.7342 -0.1110 -0.0931 -0.0164 111  ARG   E CB  
12193 C  CG  . ARG   E 111 ? 1.7639 1.6879 1.8034 -0.1163 -0.1007 -0.0181 111  ARG   E CG  
12194 C  CD  . ARG   E 111 ? 1.8400 1.7575 1.8865 -0.1212 -0.1002 -0.0169 111  ARG   E CD  
12195 N  NE  . ARG   E 111 ? 1.9020 1.8088 1.9364 -0.1189 -0.0966 -0.0170 111  ARG   E NE  
12196 C  CZ  . ARG   E 111 ? 1.9328 1.8277 1.9566 -0.1189 -0.1006 -0.0197 111  ARG   E CZ  
12197 N  NH1 . ARG   E 111 ? 1.9960 1.8871 2.0194 -0.1214 -0.1086 -0.0226 111  ARG   E NH1 
12198 N  NH2 . ARG   E 111 ? 1.8850 1.7710 1.8979 -0.1162 -0.0966 -0.0196 111  ARG   E NH2 
12199 N  N   . ILE   E 112 ? 1.7249 1.6420 1.7277 -0.0991 -0.0873 -0.0189 112  ILE   E N   
12200 C  CA  . ILE   E 112 ? 1.7257 1.6392 1.7174 -0.0936 -0.0826 -0.0191 112  ILE   E CA  
12201 C  C   . ILE   E 112 ? 1.7667 1.6769 1.7460 -0.0895 -0.0855 -0.0224 112  ILE   E C   
12202 O  O   . ILE   E 112 ? 1.7592 1.6645 1.7350 -0.0912 -0.0912 -0.0247 112  ILE   E O   
12203 C  CB  . ILE   E 112 ? 1.7816 1.6844 1.7691 -0.0944 -0.0802 -0.0184 112  ILE   E CB  
12204 C  CG1 . ILE   E 112 ? 1.8250 1.7159 1.8022 -0.0949 -0.0851 -0.0215 112  ILE   E CG1 
12205 C  CG2 . ILE   E 112 ? 1.8049 1.7093 1.8056 -0.1000 -0.0787 -0.0155 112  ILE   E CG2 
12206 C  CD1 . ILE   E 112 ? 1.7811 1.6603 1.7496 -0.0937 -0.0824 -0.0214 112  ILE   E CD1 
12207 N  N   . GLY   E 113 ? 1.7116 1.6240 1.6843 -0.0839 -0.0816 -0.0227 113  GLY   E N   
12208 C  CA  . GLY   E 113 ? 1.6142 1.5232 1.5752 -0.0796 -0.0831 -0.0256 113  GLY   E CA  
12209 C  C   . GLY   E 113 ? 1.5319 1.4490 1.4917 -0.0744 -0.0792 -0.0254 113  GLY   E C   
12210 O  O   . GLY   E 113 ? 1.4651 1.3925 1.4341 -0.0750 -0.0776 -0.0236 113  GLY   E O   
12211 N  N   . ARG   E 114 ? 1.5171 1.4296 1.4662 -0.0694 -0.0778 -0.0274 114  ARG   E N   
12212 C  CA  . ARG   E 114 ? 1.4766 1.3960 1.4247 -0.0642 -0.0742 -0.0275 114  ARG   E CA  
12213 C  C   . ARG   E 114 ? 1.4616 1.3849 1.4075 -0.0628 -0.0762 -0.0293 114  ARG   E C   
12214 O  O   . ARG   E 114 ? 1.4540 1.3699 1.3904 -0.0613 -0.0782 -0.0316 114  ARG   E O   
12215 C  CB  . ARG   E 114 ? 1.4978 1.4105 1.4365 -0.0593 -0.0714 -0.0287 114  ARG   E CB  
12216 N  N   . PRO   E 115 ? 1.4060 1.3402 1.3600 -0.0632 -0.0756 -0.0281 115  PRO   E N   
12217 C  CA  . PRO   E 115 ? 1.3747 1.3122 1.3261 -0.0615 -0.0769 -0.0296 115  PRO   E CA  
12218 C  C   . PRO   E 115 ? 1.3897 1.3245 1.3322 -0.0559 -0.0742 -0.0316 115  PRO   E C   
12219 O  O   . PRO   E 115 ? 1.4371 1.3763 1.3814 -0.0525 -0.0704 -0.0312 115  PRO   E O   
12220 C  CB  . PRO   E 115 ? 1.3491 1.2990 1.3112 -0.0622 -0.0754 -0.0276 115  PRO   E CB  
12221 C  CG  . PRO   E 115 ? 1.3845 1.3361 1.3554 -0.0664 -0.0757 -0.0253 115  PRO   E CG  
12222 C  CD  . PRO   E 115 ? 1.4040 1.3468 1.3697 -0.0658 -0.0741 -0.0253 115  PRO   E CD  
12223 N  N   . SER   E 116 ? 1.3665 1.2940 1.2996 -0.0548 -0.0763 -0.0338 116  SER   E N   
12224 C  CA  . SER   E 116 ? 1.4222 1.3451 1.3463 -0.0496 -0.0737 -0.0358 116  SER   E CA  
12225 C  C   . SER   E 116 ? 1.4993 1.4317 1.4271 -0.0457 -0.0699 -0.0358 116  SER   E C   
12226 O  O   . SER   E 116 ? 1.4759 1.4164 1.4100 -0.0469 -0.0701 -0.0348 116  SER   E O   
12227 C  CB  . SER   E 116 ? 1.4781 1.3910 1.3910 -0.0492 -0.0766 -0.0381 116  SER   E CB  
12228 O  OG  . SER   E 116 ? 1.5211 1.4282 1.4249 -0.0442 -0.0740 -0.0400 116  SER   E OG  
12229 N  N   . GLU   E 117 ? 1.5120 1.4429 1.4360 -0.0410 -0.0666 -0.0369 117  GLU   E N   
12230 C  CA  . GLU   E 117 ? 1.5137 1.4534 1.4422 -0.0371 -0.0629 -0.0371 117  GLU   E CA  
12231 C  C   . GLU   E 117 ? 1.5464 1.4882 1.4729 -0.0361 -0.0625 -0.0380 117  GLU   E C   
12232 O  O   . GLU   E 117 ? 1.5916 1.5427 1.5254 -0.0362 -0.0613 -0.0370 117  GLU   E O   
12233 C  CB  . GLU   E 117 ? 1.5314 1.4680 1.4560 -0.0321 -0.0601 -0.0385 117  GLU   E CB  
12234 N  N   . THR   E 118 ? 1.7155 1.6483 1.6317 -0.0349 -0.0634 -0.0398 118  THR   E N   
12235 C  CA  . THR   E 118 ? 1.7432 1.6761 1.6555 -0.0336 -0.0626 -0.0406 118  THR   E CA  
12236 C  C   . THR   E 118 ? 1.7279 1.6625 1.6421 -0.0378 -0.0661 -0.0395 118  THR   E C   
12237 O  O   . THR   E 118 ? 1.7411 1.6754 1.6515 -0.0366 -0.0655 -0.0400 118  THR   E O   
12238 C  CB  . THR   E 118 ? 1.7436 1.6650 1.6429 -0.0306 -0.0623 -0.0428 118  THR   E CB  
12239 O  OG1 . THR   E 118 ? 1.7617 1.6731 1.6544 -0.0334 -0.0666 -0.0433 118  THR   E OG1 
12240 C  CG2 . THR   E 118 ? 1.7131 1.6344 1.6113 -0.0255 -0.0581 -0.0441 118  THR   E CG2 
12241 N  N   . GLY   E 119 ? 1.5285 1.4649 1.4484 -0.0423 -0.0696 -0.0380 119  GLY   E N   
12242 C  CA  . GLY   E 119 ? 1.4357 1.3758 1.3597 -0.0460 -0.0728 -0.0369 119  GLY   E CA  
12243 C  C   . GLY   E 119 ? 1.3375 1.2676 1.2538 -0.0488 -0.0782 -0.0379 119  GLY   E C   
12244 O  O   . GLY   E 119 ? 1.3441 1.2639 1.2514 -0.0480 -0.0795 -0.0395 119  GLY   E O   
12245 N  N   . ILE   E 120 ? 1.2987 1.2318 1.2186 -0.0519 -0.0816 -0.0371 120  ILE   E N   
12246 C  CA  . ILE   E 120 ? 1.2487 1.1733 1.1631 -0.0549 -0.0878 -0.0381 120  ILE   E CA  
12247 C  C   . ILE   E 120 ? 1.2210 1.1361 1.1214 -0.0518 -0.0883 -0.0402 120  ILE   E C   
12248 O  O   . ILE   E 120 ? 1.2423 1.1607 1.1410 -0.0495 -0.0862 -0.0400 120  ILE   E O   
12249 C  CB  . ILE   E 120 ? 1.1433 1.0745 1.0667 -0.0590 -0.0916 -0.0366 120  ILE   E CB  
12250 C  CG1 . ILE   E 120 ? 1.1422 1.0822 1.0793 -0.0622 -0.0908 -0.0344 120  ILE   E CG1 
12251 C  CG2 . ILE   E 120 ? 1.0860 1.0081 1.0038 -0.0618 -0.0985 -0.0380 120  ILE   E CG2 
12252 C  CD1 . ILE   E 120 ? 1.0924 1.0384 1.0387 -0.0662 -0.0949 -0.0331 120  ILE   E CD1 
12253 N  N   . ILE   E 121 ? 1.1838 1.0868 1.0738 -0.0515 -0.0911 -0.0420 121  ILE   E N   
12254 C  CA  . ILE   E 121 ? 1.1588 1.0510 1.0340 -0.0486 -0.0922 -0.0441 121  ILE   E CA  
12255 C  C   . ILE   E 121 ? 1.1410 1.0251 1.0120 -0.0521 -0.1001 -0.0451 121  ILE   E C   
12256 O  O   . ILE   E 121 ? 1.2328 1.1109 1.1036 -0.0548 -0.1040 -0.0458 121  ILE   E O   
12257 C  CB  . ILE   E 121 ? 1.1720 1.0554 1.0370 -0.0447 -0.0892 -0.0458 121  ILE   E CB  
12258 C  CG1 . ILE   E 121 ? 1.2224 1.1143 1.0933 -0.0413 -0.0820 -0.0449 121  ILE   E CG1 
12259 C  CG2 . ILE   E 121 ? 1.1651 1.0372 1.0142 -0.0410 -0.0895 -0.0477 121  ILE   E CG2 
12260 C  CD1 . ILE   E 121 ? 1.2840 1.1683 1.1442 -0.0361 -0.0779 -0.0467 121  ILE   E CD1 
12261 N  N   . GLY   E 122 ? 1.1121 0.9959 0.9801 -0.0520 -0.1027 -0.0452 122  GLY   E N   
12262 C  CA  . GLY   E 122 ? 1.1126 0.9870 0.9738 -0.0542 -0.1106 -0.0467 122  GLY   E CA  
12263 C  C   . GLY   E 122 ? 1.1481 1.0092 0.9909 -0.0498 -0.1107 -0.0489 122  GLY   E C   
12264 O  O   . GLY   E 122 ? 1.2399 1.1022 1.0774 -0.0457 -0.1055 -0.0486 122  GLY   E O   
12265 N  N   . ILE   E 123 ? 1.1778 1.0260 1.0109 -0.0506 -0.1164 -0.0511 123  ILE   E N   
12266 C  CA  . ILE   E 123 ? 1.2783 1.1118 1.0924 -0.0464 -0.1174 -0.0534 123  ILE   E CA  
12267 C  C   . ILE   E 123 ? 1.3752 1.1978 1.1832 -0.0492 -0.1274 -0.0554 123  ILE   E C   
12268 O  O   . ILE   E 123 ? 1.3661 1.1907 1.1840 -0.0542 -0.1324 -0.0553 123  ILE   E O   
12269 C  CB  . ILE   E 123 ? 1.3573 1.1838 1.1628 -0.0427 -0.1125 -0.0544 123  ILE   E CB  
12270 C  CG1 . ILE   E 123 ? 1.3142 1.1431 1.1290 -0.0462 -0.1135 -0.0541 123  ILE   E CG1 
12271 C  CG2 . ILE   E 123 ? 1.3307 1.1637 1.1361 -0.0380 -0.1032 -0.0534 123  ILE   E CG2 
12272 C  CD1 . ILE   E 123 ? 1.3482 1.1712 1.1556 -0.0425 -0.1086 -0.0551 123  ILE   E CD1 
12273 N  N   . ILE   E 124 ? 1.4557 1.2665 1.2477 -0.0460 -0.1302 -0.0571 124  ILE   E N   
12274 C  CA  . ILE   E 124 ? 1.5368 1.3352 1.3205 -0.0478 -0.1402 -0.0595 124  ILE   E CA  
12275 C  C   . ILE   E 124 ? 1.6461 1.4270 1.4091 -0.0433 -0.1406 -0.0621 124  ILE   E C   
12276 O  O   . ILE   E 124 ? 1.5974 1.3751 1.3497 -0.0379 -0.1337 -0.0620 124  ILE   E O   
12277 C  CB  . ILE   E 124 ? 1.4700 1.2698 1.2535 -0.0484 -0.1451 -0.0594 124  ILE   E CB  
12278 C  CG1 . ILE   E 124 ? 1.3500 1.1657 1.1547 -0.0536 -0.1465 -0.0572 124  ILE   E CG1 
12279 C  CG2 . ILE   E 124 ? 1.5614 1.3468 1.3341 -0.0492 -0.1556 -0.0623 124  ILE   E CG2 
12280 C  CD1 . ILE   E 124 ? 1.3440 1.1601 1.1502 -0.0552 -0.1537 -0.0575 124  ILE   E CD1 
12281 N  N   . ASP   E 125 ? 1.9601 1.7299 1.7181 -0.0455 -0.1485 -0.0644 125  ASP   E N   
12282 C  CA  . ASP   E 125 ? 1.9866 1.7383 1.7242 -0.0415 -0.1502 -0.0671 125  ASP   E CA  
12283 C  C   . ASP   E 125 ? 1.9979 1.7396 1.7181 -0.0366 -0.1510 -0.0682 125  ASP   E C   
12284 O  O   . ASP   E 125 ? 2.0006 1.7439 1.7228 -0.0380 -0.1563 -0.0682 125  ASP   E O   
12285 C  CB  . ASP   E 125 ? 2.0066 1.7487 1.7436 -0.0455 -0.1601 -0.0695 125  ASP   E CB  
12286 C  CG  . ASP   E 125 ? 2.0579 1.7801 1.7732 -0.0415 -0.1630 -0.0726 125  ASP   E CG  
12287 O  OD1 . ASP   E 125 ? 2.0549 1.7731 1.7630 -0.0380 -0.1565 -0.0727 125  ASP   E OD1 
12288 O  OD2 . ASP   E 125 ? 2.0617 1.7719 1.7668 -0.0416 -0.1720 -0.0750 125  ASP   E OD2 
12289 N  N   . PRO   E 126 ? 1.8203 1.5515 1.5232 -0.0304 -0.1455 -0.0691 126  PRO   E N   
12290 C  CA  . PRO   E 126 ? 1.7693 1.4896 1.4541 -0.0253 -0.1455 -0.0700 126  PRO   E CA  
12291 C  C   . PRO   E 126 ? 1.7918 1.4981 1.4655 -0.0262 -0.1573 -0.0727 126  PRO   E C   
12292 O  O   . PRO   E 126 ? 1.7536 1.4556 1.4190 -0.0240 -0.1597 -0.0728 126  PRO   E O   
12293 C  CB  . PRO   E 126 ? 1.6973 1.4077 1.3664 -0.0191 -0.1379 -0.0707 126  PRO   E CB  
12294 C  CG  . PRO   E 126 ? 1.7193 1.4421 1.4029 -0.0205 -0.1309 -0.0691 126  PRO   E CG  
12295 C  CD  . PRO   E 126 ? 1.7962 1.5266 1.4965 -0.0276 -0.1377 -0.0689 126  PRO   E CD  
12296 N  N   . GLU   E 127 ? 1.8259 1.5242 1.4988 -0.0291 -0.1649 -0.0749 127  GLU   E N   
12297 C  CA  . GLU   E 127 ? 1.7870 1.4732 1.4525 -0.0308 -0.1774 -0.0777 127  GLU   E CA  
12298 C  C   . GLU   E 127 ? 1.8113 1.5098 1.4984 -0.0382 -0.1845 -0.0771 127  GLU   E C   
12299 O  O   . GLU   E 127 ? 1.8055 1.4976 1.4946 -0.0419 -0.1942 -0.0793 127  GLU   E O   
12300 C  CB  . GLU   E 127 ? 1.6683 1.3368 1.3190 -0.0295 -0.1822 -0.0809 127  GLU   E CB  
12301 N  N   . CYS   E 128 ? 1.7572 1.4734 1.4610 -0.0404 -0.1799 -0.0741 128  CYS   E N   
12302 C  CA  . CYS   E 128 ? 1.7189 1.4490 1.4447 -0.0470 -0.1848 -0.0729 128  CYS   E CA  
12303 C  C   . CYS   E 128 ? 1.7589 1.4872 1.4947 -0.0528 -0.1928 -0.0744 128  CYS   E C   
12304 O  O   . CYS   E 128 ? 1.7252 1.4551 1.4698 -0.0570 -0.2019 -0.0753 128  CYS   E O   
12305 C  CB  . CYS   E 128 ? 1.6688 1.3985 1.3932 -0.0469 -0.1915 -0.0733 128  CYS   E CB  
12306 S  SG  . CYS   E 128 ? 1.7039 1.4439 1.4280 -0.0430 -0.1818 -0.0702 128  CYS   E SG  
12307 N  N   . ARG   E 129 ? 1.7729 1.4985 1.5085 -0.0533 -0.1893 -0.0746 129  ARG   E N   
12308 C  CA  . ARG   E 129 ? 1.7451 1.4697 1.4913 -0.0590 -0.1956 -0.0756 129  ARG   E CA  
12309 C  C   . ARG   E 129 ? 1.7386 1.4814 1.5088 -0.0643 -0.1909 -0.0725 129  ARG   E C   
12310 O  O   . ARG   E 129 ? 1.6886 1.4333 1.4717 -0.0701 -0.1965 -0.0729 129  ARG   E O   
12311 C  CB  . ARG   E 129 ? 1.6572 1.3667 1.3889 -0.0567 -0.1954 -0.0778 129  ARG   E CB  
12312 N  N   . MET   E 130 ? 1.7261 1.4817 1.5025 -0.0625 -0.1809 -0.0695 130  MET   E N   
12313 C  CA  . MET   E 130 ? 1.6340 1.4057 1.4311 -0.0667 -0.1758 -0.0666 130  MET   E CA  
12314 C  C   . MET   E 130 ? 1.5258 1.3112 1.3284 -0.0641 -0.1666 -0.0637 130  MET   E C   
12315 O  O   . MET   E 130 ? 1.5520 1.3337 1.3414 -0.0586 -0.1619 -0.0639 130  MET   E O   
12316 C  CB  . MET   E 130 ? 1.6151 1.3829 1.4115 -0.0671 -0.1720 -0.0667 130  MET   E CB  
12317 C  CG  . MET   E 130 ? 1.6566 1.4143 1.4340 -0.0605 -0.1666 -0.0678 130  MET   E CG  
12318 S  SD  . MET   E 130 ? 1.6260 1.3784 1.4024 -0.0610 -0.1633 -0.0681 130  MET   E SD  
12319 C  CE  . MET   E 130 ? 1.5944 1.3671 1.3914 -0.0632 -0.1545 -0.0641 130  MET   E CE  
12320 N  N   . ILE   E 131 ? 1.4711 1.2721 1.2933 -0.0681 -0.1639 -0.0610 131  ILE   E N   
12321 C  CA  . ILE   E 131 ? 1.4296 1.2448 1.2598 -0.0664 -0.1550 -0.0581 131  ILE   E CA  
12322 C  C   . ILE   E 131 ? 1.4359 1.2564 1.2732 -0.0670 -0.1482 -0.0566 131  ILE   E C   
12323 O  O   . ILE   E 131 ? 1.4565 1.2794 1.3050 -0.0717 -0.1504 -0.0560 131  ILE   E O   
12324 C  CB  . ILE   E 131 ? 1.3785 1.2072 1.2251 -0.0701 -0.1570 -0.0561 131  ILE   E CB  
12325 C  CG1 . ILE   E 131 ? 1.4013 1.2244 1.2405 -0.0692 -0.1642 -0.0577 131  ILE   E CG1 
12326 C  CG2 . ILE   E 131 ? 1.3084 1.1512 1.1632 -0.0684 -0.1480 -0.0532 131  ILE   E CG2 
12327 C  CD1 . ILE   E 131 ? 1.3489 1.1852 1.2031 -0.0720 -0.1656 -0.0559 131  ILE   E CD1 
12328 N  N   . GLY   E 132 ? 1.3555 1.1774 1.1865 -0.0622 -0.1399 -0.0559 132  GLY   E N   
12329 C  CA  . GLY   E 132 ? 1.3090 1.1352 1.1451 -0.0619 -0.1335 -0.0546 132  GLY   E CA  
12330 C  C   . GLY   E 132 ? 1.2838 1.1263 1.1335 -0.0619 -0.1267 -0.0517 132  GLY   E C   
12331 O  O   . GLY   E 132 ? 1.3316 1.1788 1.1786 -0.0584 -0.1225 -0.0511 132  GLY   E O   
12332 N  N   . LEU   E 133 ? 1.2815 1.1321 1.1453 -0.0657 -0.1255 -0.0499 133  LEU   E N   
12333 C  CA  . LEU   E 133 ? 1.2029 1.0686 1.0804 -0.0660 -0.1197 -0.0471 133  LEU   E CA  
12334 C  C   . LEU   E 133 ? 1.2488 1.1160 1.1286 -0.0649 -0.1140 -0.0462 133  LEU   E C   
12335 O  O   . LEU   E 133 ? 1.3823 1.2438 1.2630 -0.0674 -0.1160 -0.0465 133  LEU   E O   
12336 C  CB  . LEU   E 133 ? 1.1932 1.0678 1.0864 -0.0716 -0.1234 -0.0454 133  LEU   E CB  
12337 C  CG  . LEU   E 133 ? 1.2123 1.0874 1.1066 -0.0733 -0.1297 -0.0460 133  LEU   E CG  
12338 C  CD1 . LEU   E 133 ? 1.1805 1.0666 1.0928 -0.0785 -0.1318 -0.0439 133  LEU   E CD1 
12339 C  CD2 . LEU   E 133 ? 1.1970 1.0747 1.0844 -0.0689 -0.1266 -0.0460 133  LEU   E CD2 
12340 N  N   . ARG   E 134 ? 1.2090 1.0836 1.0900 -0.0611 -0.1070 -0.0452 134  ARG   E N   
12341 C  CA  . ARG   E 134 ? 1.2666 1.1443 1.1516 -0.0599 -0.1018 -0.0441 134  ARG   E CA  
12342 C  C   . ARG   E 134 ? 1.3253 1.2170 1.2257 -0.0619 -0.0990 -0.0414 134  ARG   E C   
12343 O  O   . ARG   E 134 ? 1.3232 1.2237 1.2268 -0.0592 -0.0947 -0.0405 134  ARG   E O   
12344 C  CB  . ARG   E 134 ? 1.2176 1.0932 1.0937 -0.0538 -0.0961 -0.0451 134  ARG   E CB  
12345 C  CG  . ARG   E 134 ? 1.3157 1.1895 1.1920 -0.0524 -0.0926 -0.0450 134  ARG   E CG  
12346 C  CD  . ARG   E 134 ? 1.3375 1.2235 1.2265 -0.0527 -0.0883 -0.0426 134  ARG   E CD  
12347 N  NE  . ARG   E 134 ? 1.3427 1.2376 1.2340 -0.0491 -0.0840 -0.0422 134  ARG   E NE  
12348 C  CZ  . ARG   E 134 ? 1.3643 1.2595 1.2515 -0.0440 -0.0792 -0.0430 134  ARG   E CZ  
12349 N  NH1 . ARG   E 134 ? 1.3625 1.2502 1.2431 -0.0416 -0.0779 -0.0442 134  ARG   E NH1 
12350 N  NH2 . ARG   E 134 ? 1.4307 1.3341 1.3211 -0.0413 -0.0756 -0.0427 134  ARG   E NH2 
12351 N  N   . LEU   E 135 ? 1.3111 1.2047 1.2209 -0.0666 -0.1010 -0.0400 135  LEU   E N   
12352 C  CA  . LEU   E 135 ? 1.3245 1.2307 1.2484 -0.0684 -0.0983 -0.0373 135  LEU   E CA  
12353 C  C   . LEU   E 135 ? 1.4003 1.3087 1.3268 -0.0667 -0.0929 -0.0361 135  LEU   E C   
12354 O  O   . LEU   E 135 ? 1.4076 1.3259 1.3412 -0.0652 -0.0887 -0.0344 135  LEU   E O   
12355 C  CB  . LEU   E 135 ? 1.3327 1.2410 1.2671 -0.0744 -0.1029 -0.0361 135  LEU   E CB  
12356 C  CG  . LEU   E 135 ? 1.2885 1.1959 1.2221 -0.0763 -0.1089 -0.0372 135  LEU   E CG  
12357 C  CD1 . LEU   E 135 ? 1.2671 1.1803 1.2148 -0.0819 -0.1126 -0.0357 135  LEU   E CD1 
12358 C  CD2 . LEU   E 135 ? 1.2517 1.1650 1.1823 -0.0725 -0.1066 -0.0373 135  LEU   E CD2 
12359 N  N   . TYR   E 136 ? 1.4488 1.3475 1.3692 -0.0666 -0.0931 -0.0370 136  TYR   E N   
12360 C  CA  . TYR   E 136 ? 1.4457 1.3453 1.3686 -0.0655 -0.0887 -0.0357 136  TYR   E CA  
12361 C  C   . TYR   E 136 ? 1.4375 1.3271 1.3481 -0.0613 -0.0872 -0.0376 136  TYR   E C   
12362 O  O   . TYR   E 136 ? 1.4237 1.3042 1.3240 -0.0603 -0.0900 -0.0399 136  TYR   E O   
12363 C  CB  . TYR   E 136 ? 1.4386 1.3374 1.3701 -0.0707 -0.0902 -0.0338 136  TYR   E CB  
12364 C  CG  . TYR   E 136 ? 1.4405 1.3483 1.3846 -0.0752 -0.0925 -0.0321 136  TYR   E CG  
12365 C  CD1 . TYR   E 136 ? 1.4054 1.3252 1.3588 -0.0746 -0.0890 -0.0299 136  TYR   E CD1 
12366 C  CD2 . TYR   E 136 ? 1.4672 1.3712 1.4137 -0.0798 -0.0984 -0.0327 136  TYR   E CD2 
12367 C  CE1 . TYR   E 136 ? 1.3849 1.3128 1.3495 -0.0783 -0.0909 -0.0284 136  TYR   E CE1 
12368 C  CE2 . TYR   E 136 ? 1.4462 1.3587 1.4047 -0.0836 -0.1007 -0.0312 136  TYR   E CE2 
12369 C  CZ  . TYR   E 136 ? 1.3897 1.3141 1.3571 -0.0828 -0.0967 -0.0290 136  TYR   E CZ  
12370 O  OH  . TYR   E 136 ? 1.4604 1.3933 1.4397 -0.0863 -0.0987 -0.0275 136  TYR   E OH  
12371 N  N   . ASP   E 137 ? 1.4285 1.3196 1.3398 -0.0585 -0.0827 -0.0368 137  ASP   E N   
12372 C  CA  . ASP   E 137 ? 1.4261 1.3085 1.3266 -0.0542 -0.0809 -0.0386 137  ASP   E CA  
12373 C  C   . ASP   E 137 ? 1.4928 1.3632 1.3881 -0.0570 -0.0838 -0.0391 137  ASP   E C   
12374 O  O   . ASP   E 137 ? 1.4919 1.3623 1.3940 -0.0611 -0.0843 -0.0373 137  ASP   E O   
12375 C  CB  . ASP   E 137 ? 1.4996 1.3870 1.4029 -0.0504 -0.0758 -0.0376 137  ASP   E CB  
12376 C  CG  . ASP   E 137 ? 1.5540 1.4502 1.4588 -0.0459 -0.0727 -0.0381 137  ASP   E CG  
12377 O  OD1 . ASP   E 137 ? 1.5773 1.4715 1.4759 -0.0438 -0.0733 -0.0399 137  ASP   E OD1 
12378 O  OD2 . ASP   E 137 ? 1.5240 1.4286 1.4359 -0.0444 -0.0696 -0.0367 137  ASP   E OD2 
12379 N  N   . GLY   E 138 ? 1.5534 1.4131 1.4365 -0.0549 -0.0857 -0.0417 138  GLY   E N   
12380 C  CA  . GLY   E 138 ? 1.5203 1.3675 1.3973 -0.0574 -0.0890 -0.0426 138  GLY   E CA  
12381 C  C   . GLY   E 138 ? 1.5546 1.3976 1.4325 -0.0625 -0.0952 -0.0432 138  GLY   E C   
12382 O  O   . GLY   E 138 ? 1.6001 1.4319 1.4725 -0.0647 -0.0986 -0.0443 138  GLY   E O   
12383 N  N   . LEU   E 139 ? 1.5552 1.4064 1.4396 -0.0644 -0.0970 -0.0427 139  LEU   E N   
12384 C  CA  . LEU   E 139 ? 1.5317 1.3803 1.4190 -0.0694 -0.1034 -0.0432 139  LEU   E CA  
12385 C  C   . LEU   E 139 ? 1.4523 1.3003 1.3329 -0.0675 -0.1062 -0.0450 139  LEU   E C   
12386 O  O   . LEU   E 139 ? 1.4507 1.3052 1.3300 -0.0635 -0.1025 -0.0449 139  LEU   E O   
12387 C  CB  . LEU   E 139 ? 1.5223 1.3814 1.4258 -0.0745 -0.1037 -0.0404 139  LEU   E CB  
12388 C  CG  . LEU   E 139 ? 1.5067 1.3635 1.4177 -0.0787 -0.1033 -0.0387 139  LEU   E CG  
12389 C  CD1 . LEU   E 139 ? 1.4767 1.3442 1.4035 -0.0834 -0.1037 -0.0361 139  LEU   E CD1 
12390 C  CD2 . LEU   E 139 ? 1.5226 1.3661 1.4272 -0.0815 -0.1087 -0.0406 139  LEU   E CD2 
12391 N  N   . PHE   E 140 ? 1.4283 1.2682 1.3051 -0.0704 -0.1129 -0.0467 140  PHE   E N   
12392 C  CA  . PHE   E 140 ? 1.4195 1.2566 1.2884 -0.0687 -0.1164 -0.0486 140  PHE   E CA  
12393 C  C   . PHE   E 140 ? 1.4222 1.2582 1.2970 -0.0741 -0.1240 -0.0490 140  PHE   E C   
12394 O  O   . PHE   E 140 ? 1.4809 1.3056 1.3503 -0.0763 -0.1296 -0.0508 140  PHE   E O   
12395 C  CB  . PHE   E 140 ? 1.4213 1.2450 1.2726 -0.0642 -0.1169 -0.0514 140  PHE   E CB  
12396 C  CG  . PHE   E 140 ? 1.4114 1.2318 1.2527 -0.0613 -0.1189 -0.0531 140  PHE   E CG  
12397 C  CD1 . PHE   E 140 ? 1.3644 1.1942 1.2073 -0.0580 -0.1143 -0.0521 140  PHE   E CD1 
12398 C  CD2 . PHE   E 140 ? 1.4832 1.2906 1.3132 -0.0617 -0.1255 -0.0557 140  PHE   E CD2 
12399 C  CE1 . PHE   E 140 ? 1.3548 1.1809 1.1881 -0.0551 -0.1155 -0.0535 140  PHE   E CE1 
12400 C  CE2 . PHE   E 140 ? 1.4658 1.2690 1.2853 -0.0585 -0.1271 -0.0571 140  PHE   E CE2 
12401 C  CZ  . PHE   E 140 ? 1.3992 1.2118 1.2203 -0.0553 -0.1219 -0.0559 140  PHE   E CZ  
12402 N  N   . LYS   E 141 ? 1.4046 1.2518 1.2902 -0.0761 -0.1245 -0.0474 141  LYS   E N   
12403 C  CA  . LYS   E 141 ? 1.3826 1.2298 1.2749 -0.0809 -0.1319 -0.0478 141  LYS   E CA  
12404 C  C   . LYS   E 141 ? 1.3901 1.2269 1.2686 -0.0789 -0.1378 -0.0508 141  LYS   E C   
12405 O  O   . LYS   E 141 ? 1.3454 1.1798 1.2123 -0.0738 -0.1350 -0.0517 141  LYS   E O   
12406 C  CB  . LYS   E 141 ? 1.3971 1.2593 1.3039 -0.0828 -0.1304 -0.0454 141  LYS   E CB  
12407 C  CG  . LYS   E 141 ? 1.4395 1.3053 1.3600 -0.0890 -0.1363 -0.0447 141  LYS   E CG  
12408 C  CD  . LYS   E 141 ? 1.4288 1.3082 1.3666 -0.0918 -0.1317 -0.0413 141  LYS   E CD  
12409 C  CE  . LYS   E 141 ? 1.4428 1.3274 1.3950 -0.0974 -0.1373 -0.0406 141  LYS   E CE  
12410 N  NZ  . LYS   E 141 ? 1.4771 1.3682 1.4451 -0.1018 -0.1345 -0.0379 141  LYS   E NZ  
12411 N  N   . VAL   E 142 ? 1.4657 1.2954 1.3451 -0.0829 -0.1460 -0.0524 142  VAL   E N   
12412 C  CA  . VAL   E 142 ? 1.4723 1.2905 1.3383 -0.0813 -0.1529 -0.0554 142  VAL   E CA  
12413 C  C   . VAL   E 142 ? 1.5076 1.3294 1.3842 -0.0861 -0.1607 -0.0556 142  VAL   E C   
12414 O  O   . VAL   E 142 ? 1.5173 1.3396 1.4054 -0.0915 -0.1645 -0.0554 142  VAL   E O   
12415 C  CB  . VAL   E 142 ? 1.4484 1.2503 1.3013 -0.0807 -0.1563 -0.0581 142  VAL   E CB  
12416 C  CG1 . VAL   E 142 ? 1.5597 1.3492 1.3993 -0.0795 -0.1645 -0.0613 142  VAL   E CG1 
12417 C  CG2 . VAL   E 142 ? 1.4120 1.2100 1.2538 -0.0755 -0.1489 -0.0581 142  VAL   E CG2 
12418 N  N   . ILE   E 143 ? 1.4815 1.3063 1.3552 -0.0841 -0.1626 -0.0560 143  ILE   E N   
12419 C  CA  . ILE   E 143 ? 1.4451 1.2715 1.3268 -0.0879 -0.1710 -0.0567 143  ILE   E CA  
12420 C  C   . ILE   E 143 ? 1.5258 1.3361 1.3912 -0.0862 -0.1792 -0.0604 143  ILE   E C   
12421 O  O   . ILE   E 143 ? 1.5816 1.3864 1.4320 -0.0811 -0.1786 -0.0615 143  ILE   E O   
12422 C  CB  . ILE   E 143 ? 1.4041 1.2424 1.2921 -0.0869 -0.1694 -0.0550 143  ILE   E CB  
12423 C  CG1 . ILE   E 143 ? 1.3829 1.2366 1.2854 -0.0878 -0.1610 -0.0515 143  ILE   E CG1 
12424 C  CG2 . ILE   E 143 ? 1.4595 1.2988 1.3558 -0.0907 -0.1787 -0.0560 143  ILE   E CG2 
12425 C  CD1 . ILE   E 143 ? 1.4126 1.2690 1.3065 -0.0824 -0.1526 -0.0505 143  ILE   E CD1 
12426 N  N   . PRO   E 144 ? 1.5310 1.3325 1.3979 -0.0900 -0.1868 -0.0624 144  PRO   E N   
12427 C  CA  . PRO   E 144 ? 1.5986 1.3837 1.4491 -0.0882 -0.1954 -0.0662 144  PRO   E CA  
12428 C  C   . PRO   E 144 ? 1.6257 1.4118 1.4747 -0.0873 -0.2016 -0.0672 144  PRO   E C   
12429 O  O   . PRO   E 144 ? 1.5954 1.3909 1.4607 -0.0916 -0.2057 -0.0663 144  PRO   E O   
12430 C  CB  . PRO   E 144 ? 1.6114 1.3901 1.4693 -0.0937 -0.2022 -0.0677 144  PRO   E CB  
12431 C  CG  . PRO   E 144 ? 1.5516 1.3399 1.4233 -0.0966 -0.1942 -0.0646 144  PRO   E CG  
12432 C  CD  . PRO   E 144 ? 1.5223 1.3273 1.4049 -0.0959 -0.1873 -0.0613 144  PRO   E CD  
12433 N  N   . LEU   E 145 ? 1.6554 1.4315 1.4844 -0.0814 -0.2020 -0.0689 145  LEU   E N   
12434 C  CA  . LEU   E 145 ? 1.7179 1.4928 1.5417 -0.0795 -0.2074 -0.0699 145  LEU   E CA  
12435 C  C   . LEU   E 145 ? 1.8263 1.5880 1.6449 -0.0813 -0.2204 -0.0736 145  LEU   E C   
12436 O  O   . LEU   E 145 ? 1.8758 1.6217 1.6739 -0.0770 -0.2247 -0.0765 145  LEU   E O   
12437 C  CB  . LEU   E 145 ? 1.7021 1.4715 1.5066 -0.0723 -0.2015 -0.0699 145  LEU   E CB  
12438 C  CG  . LEU   E 145 ? 1.6320 1.4156 1.4421 -0.0700 -0.1904 -0.0665 145  LEU   E CG  
12439 C  CD1 . LEU   E 145 ? 1.5877 1.3633 1.3775 -0.0628 -0.1848 -0.0669 145  LEU   E CD1 
12440 C  CD2 . LEU   E 145 ? 1.5365 1.3339 1.3619 -0.0726 -0.1920 -0.0646 145  LEU   E CD2 
12441 N  N   . ASP   E 146 ? 1.9760 1.7441 1.8134 -0.0877 -0.2266 -0.0736 146  ASP   E N   
12442 C  CA  . ASP   E 146 ? 1.9755 1.7338 1.8125 -0.0902 -0.2398 -0.0771 146  ASP   E CA  
12443 C  C   . ASP   E 146 ? 1.9927 1.7620 1.8446 -0.0927 -0.2450 -0.0764 146  ASP   E C   
12444 O  O   . ASP   E 146 ? 1.9712 1.7572 1.8417 -0.0957 -0.2394 -0.0732 146  ASP   E O   
12445 C  CB  . ASP   E 146 ? 1.9066 1.6612 1.7536 -0.0957 -0.2439 -0.0782 146  ASP   E CB  
12446 C  CG  . ASP   E 146 ? 2.0102 1.7513 1.8528 -0.0975 -0.2579 -0.0824 146  ASP   E CG  
12447 O  OD1 . ASP   E 146 ? 2.0068 1.7514 1.8572 -0.0990 -0.2658 -0.0834 146  ASP   E OD1 
12448 O  OD2 . ASP   E 146 ? 2.0826 1.8089 1.9132 -0.0969 -0.2612 -0.0850 146  ASP   E OD2 
12449 N  N   . ARG   E 147 ? 2.0184 1.7777 1.8615 -0.0914 -0.2560 -0.0797 147  ARG   E N   
12450 C  CA  . ARG   E 147 ? 1.9988 1.7669 1.8531 -0.0927 -0.2615 -0.0794 147  ARG   E CA  
12451 C  C   . ARG   E 147 ? 1.9919 1.7752 1.8751 -0.1000 -0.2629 -0.0777 147  ARG   E C   
12452 O  O   . ARG   E 147 ? 2.0086 1.8049 1.9055 -0.1014 -0.2630 -0.0759 147  ARG   E O   
12453 C  CB  . ARG   E 147 ? 1.9814 1.7343 1.8223 -0.0906 -0.2749 -0.0837 147  ARG   E CB  
12454 N  N   . ASP   E 148 ? 2.0746 1.8563 1.9672 -0.1048 -0.2639 -0.0781 148  ASP   E N   
12455 C  CA  . ASP   E 148 ? 2.0655 1.8613 1.9856 -0.1118 -0.2642 -0.0762 148  ASP   E CA  
12456 C  C   . ASP   E 148 ? 2.0300 1.8430 1.9624 -0.1123 -0.2514 -0.0714 148  ASP   E C   
12457 O  O   . ASP   E 148 ? 2.0482 1.8756 2.0006 -0.1157 -0.2510 -0.0693 148  ASP   E O   
12458 C  CB  . ASP   E 148 ? 2.0934 1.8821 2.0196 -0.1166 -0.2678 -0.0777 148  ASP   E CB  
12459 C  CG  . ASP   E 148 ? 2.1005 1.8949 2.0500 -0.1234 -0.2768 -0.0786 148  ASP   E CG  
12460 O  OD1 . ASP   E 148 ? 2.0790 1.8900 2.0500 -0.1270 -0.2727 -0.0755 148  ASP   E OD1 
12461 O  OD2 . ASP   E 148 ? 2.0928 1.8749 2.0389 -0.1250 -0.2881 -0.0825 148  ASP   E OD2 
12462 N  N   . ASN   E 149 ? 1.9218 1.7336 1.8427 -0.1088 -0.2410 -0.0697 149  ASN   E N   
12463 C  CA  . ASN   E 149 ? 1.7548 1.5818 1.6866 -0.1091 -0.2291 -0.0653 149  ASN   E CA  
12464 C  C   . ASN   E 149 ? 1.6678 1.5071 1.6056 -0.1074 -0.2270 -0.0634 149  ASN   E C   
12465 O  O   . ASN   E 149 ? 1.5992 1.4367 1.5223 -0.1020 -0.2234 -0.0632 149  ASN   E O   
12466 C  CB  . ASN   E 149 ? 1.6672 1.4892 1.5832 -0.1046 -0.2195 -0.0644 149  ASN   E CB  
12467 C  CG  . ASN   E 149 ? 1.5479 1.3806 1.4769 -0.1071 -0.2094 -0.0609 149  ASN   E CG  
12468 O  OD1 . ASN   E 149 ? 1.5047 1.3485 1.4541 -0.1120 -0.2087 -0.0588 149  ASN   E OD1 
12469 N  ND2 . ASN   E 149 ? 1.5202 1.3488 1.4369 -0.1033 -0.2015 -0.0602 149  ASN   E ND2 
12470 N  N   . LYS   E 150 ? 1.6120 1.4634 1.5713 -0.1121 -0.2295 -0.0620 150  LYS   E N   
12471 C  CA  . LYS   E 150 ? 1.5431 1.4076 1.5108 -0.1111 -0.2271 -0.0598 150  LYS   E CA  
12472 C  C   . LYS   E 150 ? 1.4772 1.3570 1.4596 -0.1128 -0.2160 -0.0556 150  LYS   E C   
12473 O  O   . LYS   E 150 ? 1.4555 1.3437 1.4366 -0.1097 -0.2096 -0.0534 150  LYS   E O   
12474 C  CB  . LYS   E 150 ? 1.5281 1.3962 1.5098 -0.1146 -0.2376 -0.0613 150  LYS   E CB  
12475 N  N   . GLU   E 151 ? 1.4235 1.3063 1.4188 -0.1173 -0.2134 -0.0543 151  GLU   E N   
12476 C  CA  . GLU   E 151 ? 1.4308 1.3257 1.4369 -0.1182 -0.2025 -0.0503 151  GLU   E CA  
12477 C  C   . GLU   E 151 ? 1.4318 1.3215 1.4227 -0.1142 -0.1939 -0.0496 151  GLU   E C   
12478 O  O   . GLU   E 151 ? 1.4532 1.3508 1.4511 -0.1147 -0.1851 -0.0467 151  GLU   E O   
12479 C  CB  . GLU   E 151 ? 1.4852 1.3854 1.5118 -0.1247 -0.2025 -0.0489 151  GLU   E CB  
12480 C  CG  . GLU   E 151 ? 1.5841 1.4957 1.6313 -0.1285 -0.2069 -0.0481 151  GLU   E CG  
12481 C  CD  . GLU   E 151 ? 1.6897 1.5998 1.7531 -0.1348 -0.2132 -0.0491 151  GLU   E CD  
12482 O  OE1 . GLU   E 151 ? 1.6158 1.5145 1.6727 -0.1362 -0.2154 -0.0508 151  GLU   E OE1 
12483 O  OE2 . GLU   E 151 ? 1.7535 1.6736 1.8363 -0.1385 -0.2160 -0.0481 151  GLU   E OE2 
12484 N  N   . LEU   E 152 ? 1.4586 1.3351 1.4288 -0.1101 -0.1964 -0.0523 152  LEU   E N   
12485 C  CA  . LEU   E 152 ? 1.4490 1.3200 1.4040 -0.1057 -0.1888 -0.0520 152  LEU   E CA  
12486 C  C   . LEU   E 152 ? 1.4626 1.3334 1.4239 -0.1085 -0.1838 -0.0507 152  LEU   E C   
12487 O  O   . LEU   E 152 ? 1.4092 1.2863 1.3720 -0.1070 -0.1745 -0.0481 152  LEU   E O   
12488 C  CB  . LEU   E 152 ? 1.4001 1.2805 1.3523 -0.1015 -0.1806 -0.0497 152  LEU   E CB  
12489 C  CG  . LEU   E 152 ? 1.3725 1.2521 1.3160 -0.0979 -0.1840 -0.0508 152  LEU   E CG  
12490 C  CD1 . LEU   E 152 ? 1.3667 1.2600 1.3165 -0.0960 -0.1766 -0.0478 152  LEU   E CD1 
12491 C  CD2 . LEU   E 152 ? 1.2317 1.0967 1.1521 -0.0928 -0.1848 -0.0533 152  LEU   E CD2 
12492 N  N   . LYS   E 153 ? 1.4578 1.3207 1.4226 -0.1126 -0.1903 -0.0525 153  LYS   E N   
12493 C  CA  . LYS   E 153 ? 1.4446 1.3040 1.4122 -0.1150 -0.1863 -0.0516 153  LYS   E CA  
12494 C  C   . LYS   E 153 ? 1.4950 1.3455 1.4434 -0.1097 -0.1808 -0.0523 153  LYS   E C   
12495 O  O   . LYS   E 153 ? 1.5120 1.3531 1.4431 -0.1054 -0.1837 -0.0548 153  LYS   E O   
12496 C  CB  . LYS   E 153 ? 1.3951 1.2455 1.3677 -0.1199 -0.1953 -0.0540 153  LYS   E CB  
12497 N  N   . ALA   E 154 ? 1.5237 1.3770 1.4748 -0.1097 -0.1726 -0.0501 154  ALA   E N   
12498 C  CA  . ALA   E 154 ? 1.5523 1.3988 1.4872 -0.1046 -0.1667 -0.0504 154  ALA   E CA  
12499 C  C   . ALA   E 154 ? 1.5994 1.4411 1.5358 -0.1065 -0.1631 -0.0497 154  ALA   E C   
12500 O  O   . ALA   E 154 ? 1.6152 1.4622 1.5670 -0.1114 -0.1621 -0.0477 154  ALA   E O   
12501 C  CB  . ALA   E 154 ? 1.5006 1.3577 1.4346 -0.1003 -0.1582 -0.0482 154  ALA   E CB  
12502 N  N   . PHE   E 155 ? 1.6537 1.4851 1.5736 -0.1023 -0.1605 -0.0511 155  PHE   E N   
12503 C  CA  . PHE   E 155 ? 1.6111 1.4364 1.5292 -0.1030 -0.1568 -0.0505 155  PHE   E CA  
12504 C  C   . PHE   E 155 ? 1.5554 1.3801 1.4616 -0.0969 -0.1488 -0.0500 155  PHE   E C   
12505 O  O   . PHE   E 155 ? 1.5726 1.3933 1.4650 -0.0919 -0.1487 -0.0517 155  PHE   E O   
12506 C  CB  . PHE   E 155 ? 1.6553 1.4648 1.5654 -0.1051 -0.1642 -0.0536 155  PHE   E CB  
12507 C  CG  . PHE   E 155 ? 1.6839 1.4809 1.5734 -0.1001 -0.1678 -0.0570 155  PHE   E CG  
12508 C  CD1 . PHE   E 155 ? 1.6870 1.4756 1.5614 -0.0953 -0.1631 -0.0578 155  PHE   E CD1 
12509 C  CD2 . PHE   E 155 ? 1.6600 1.4527 1.5448 -0.1000 -0.1760 -0.0595 155  PHE   E CD2 
12510 C  CE1 . PHE   E 155 ? 1.7099 1.4867 1.5653 -0.0906 -0.1659 -0.0608 155  PHE   E CE1 
12511 C  CE2 . PHE   E 155 ? 1.6672 1.4473 1.5320 -0.0952 -0.1789 -0.0625 155  PHE   E CE2 
12512 C  CZ  . PHE   E 155 ? 1.7077 1.4799 1.5579 -0.0905 -0.1737 -0.0631 155  PHE   E CZ  
12513 N  N   . ASN   E 156 ? 1.5016 1.3302 1.4132 -0.0971 -0.1420 -0.0477 156  ASN   E N   
12514 C  CA  . ASN   E 156 ? 1.4996 1.3280 1.4018 -0.0915 -0.1345 -0.0471 156  ASN   E CA  
12515 C  C   . ASN   E 156 ? 1.5542 1.3678 1.4425 -0.0896 -0.1351 -0.0492 156  ASN   E C   
12516 O  O   . ASN   E 156 ? 1.5847 1.3906 1.4752 -0.0936 -0.1384 -0.0497 156  ASN   E O   
12517 C  CB  . ASN   E 156 ? 1.4958 1.3351 1.4098 -0.0922 -0.1272 -0.0437 156  ASN   E CB  
12518 C  CG  . ASN   E 156 ? 1.5117 1.3656 1.4347 -0.0913 -0.1242 -0.0417 156  ASN   E CG  
12519 O  OD1 . ASN   E 156 ? 1.5621 1.4186 1.4781 -0.0870 -0.1230 -0.0426 156  ASN   E OD1 
12520 N  ND2 . ASN   E 156 ? 1.5123 1.3756 1.4511 -0.0954 -0.1228 -0.0390 156  ASN   E ND2 
12521 N  N   . ILE   E 157 ? 1.5714 1.3811 1.4457 -0.0835 -0.1317 -0.0505 157  ILE   E N   
12522 C  CA  . ILE   E 157 ? 1.6240 1.4214 1.4851 -0.0804 -0.1302 -0.0520 157  ILE   E CA  
12523 C  C   . ILE   E 157 ? 1.6086 1.4121 1.4710 -0.0768 -0.1218 -0.0500 157  ILE   E C   
12524 O  O   . ILE   E 157 ? 1.5962 1.4097 1.4606 -0.0735 -0.1172 -0.0490 157  ILE   E O   
12525 C  CB  . ILE   E 157 ? 1.6056 1.3928 1.4490 -0.0755 -0.1327 -0.0552 157  ILE   E CB  
12526 C  CG1 . ILE   E 157 ? 1.5899 1.3751 1.4327 -0.0778 -0.1403 -0.0568 157  ILE   E CG1 
12527 C  CG2 . ILE   E 157 ? 1.6558 1.4274 1.4862 -0.0741 -0.1341 -0.0573 157  ILE   E CG2 
12528 C  CD1 . ILE   E 157 ? 1.5862 1.3636 1.4121 -0.0723 -0.1414 -0.0593 157  ILE   E CD1 
12529 N  N   . ARG   E 158 ? 1.6327 1.4300 1.4942 -0.0776 -0.1198 -0.0495 158  ARG   E N   
12530 C  CA  . ARG   E 158 ? 1.6163 1.4173 1.4766 -0.0734 -0.1124 -0.0481 158  ARG   E CA  
12531 C  C   . ARG   E 158 ? 1.6384 1.4357 1.4848 -0.0665 -0.1102 -0.0502 158  ARG   E C   
12532 O  O   . ARG   E 158 ? 1.6465 1.4326 1.4805 -0.0650 -0.1139 -0.0529 158  ARG   E O   
12533 C  CB  . ARG   E 158 ? 1.6816 1.4745 1.5410 -0.0749 -0.1110 -0.0474 158  ARG   E CB  
12534 C  CG  . ARG   E 158 ? 1.7771 1.5692 1.6479 -0.0821 -0.1140 -0.0459 158  ARG   E CG  
12535 C  CD  . ARG   E 158 ? 1.7617 1.5686 1.6493 -0.0853 -0.1118 -0.0428 158  ARG   E CD  
12536 N  NE  . ARG   E 158 ? 1.8003 1.6071 1.7002 -0.0921 -0.1138 -0.0411 158  ARG   E NE  
12537 C  CZ  . ARG   E 158 ? 1.8027 1.6073 1.7081 -0.0972 -0.1205 -0.0421 158  ARG   E CZ  
12538 N  NH1 . ARG   E 158 ? 1.7244 1.5249 1.6222 -0.0962 -0.1265 -0.0451 158  ARG   E NH1 
12539 N  NH2 . ARG   E 158 ? 1.8317 1.6380 1.7507 -0.1034 -0.1213 -0.0402 158  ARG   E NH2 
12540 N  N   . LEU   E 159 ? 1.6507 1.4575 1.4994 -0.0624 -0.1041 -0.0490 159  LEU   E N   
12541 C  CA  . LEU   E 159 ? 1.6960 1.5014 1.5341 -0.0557 -0.1009 -0.0507 159  LEU   E CA  
12542 C  C   . LEU   E 159 ? 1.7191 1.5248 1.5560 -0.0518 -0.0953 -0.0500 159  LEU   E C   
12543 O  O   . LEU   E 159 ? 1.6866 1.5028 1.5332 -0.0517 -0.0914 -0.0478 159  LEU   E O   
12544 C  CB  . LEU   E 159 ? 1.6602 1.4769 1.5025 -0.0538 -0.0992 -0.0502 159  LEU   E CB  
12545 C  CG  . LEU   E 159 ? 1.7062 1.5197 1.5368 -0.0479 -0.0972 -0.0523 159  LEU   E CG  
12546 C  CD1 . LEU   E 159 ? 1.5986 1.4211 1.4334 -0.0478 -0.0972 -0.0519 159  LEU   E CD1 
12547 C  CD2 . LEU   E 159 ? 1.8299 1.6456 1.6581 -0.0422 -0.0910 -0.0524 159  LEU   E CD2 
12548 N  N   . GLU   E 160 ? 1.9318 1.7255 1.7562 -0.0485 -0.0952 -0.0519 160  GLU   E N   
12549 C  CA  . GLU   E 160 ? 1.9533 1.7457 1.7756 -0.0447 -0.0906 -0.0515 160  GLU   E CA  
12550 C  C   . GLU   E 160 ? 1.9349 1.7386 1.7608 -0.0395 -0.0852 -0.0511 160  GLU   E C   
12551 O  O   . GLU   E 160 ? 1.9492 1.7588 1.7813 -0.0383 -0.0816 -0.0495 160  GLU   E O   
12552 C  CB  . GLU   E 160 ? 2.0090 1.7864 1.8165 -0.0415 -0.0916 -0.0540 160  GLU   E CB  
12553 C  CG  . GLU   E 160 ? 2.0960 1.8611 1.8997 -0.0465 -0.0970 -0.0546 160  GLU   E CG  
12554 C  CD  . GLU   E 160 ? 2.1380 1.8982 1.9435 -0.0482 -0.0957 -0.0532 160  GLU   E CD  
12555 O  OE1 . GLU   E 160 ? 2.1052 1.8735 1.9178 -0.0469 -0.0912 -0.0512 160  GLU   E OE1 
12556 O  OE2 . GLU   E 160 ? 2.1350 1.8825 1.9341 -0.0506 -0.0992 -0.0542 160  GLU   E OE2 
12557 N  N   . GLU   E 161 ? 1.7580 1.5645 1.5803 -0.0364 -0.0846 -0.0525 161  GLU   E N   
12558 C  CA  . GLU   E 161 ? 1.7078 1.5259 1.5353 -0.0322 -0.0798 -0.0520 161  GLU   E CA  
12559 C  C   . GLU   E 161 ? 1.6891 1.5202 1.5303 -0.0362 -0.0799 -0.0496 161  GLU   E C   
12560 O  O   . GLU   E 161 ? 1.7278 1.5594 1.5716 -0.0406 -0.0836 -0.0492 161  GLU   E O   
12561 C  CB  . GLU   E 161 ? 1.6539 1.4703 1.4734 -0.0282 -0.0789 -0.0540 161  GLU   E CB  
12562 C  CG  . GLU   E 161 ? 1.6409 1.4446 1.4463 -0.0235 -0.0783 -0.0565 161  GLU   E CG  
12563 C  CD  . GLU   E 161 ? 1.7186 1.5082 1.5128 -0.0259 -0.0836 -0.0581 161  GLU   E CD  
12564 O  OE1 . GLU   E 161 ? 1.7544 1.5422 1.5525 -0.0318 -0.0882 -0.0572 161  GLU   E OE1 
12565 O  OE2 . GLU   E 161 ? 1.6767 1.4569 1.4582 -0.0218 -0.0833 -0.0604 161  GLU   E OE2 
12566 N  N   . LEU   E 162 ? 1.6713 1.5123 1.5210 -0.0344 -0.0759 -0.0481 162  LEU   E N   
12567 C  CA  . LEU   E 162 ? 1.6299 1.4832 1.4926 -0.0378 -0.0756 -0.0457 162  LEU   E CA  
12568 C  C   . LEU   E 162 ? 1.5937 1.4585 1.4617 -0.0344 -0.0722 -0.0456 162  LEU   E C   
12569 O  O   . LEU   E 162 ? 1.6177 1.4931 1.4964 -0.0364 -0.0713 -0.0436 162  LEU   E O   
12570 C  CB  . LEU   E 162 ? 1.6361 1.4912 1.5053 -0.0395 -0.0742 -0.0436 162  LEU   E CB  
12571 C  CG  . LEU   E 162 ? 1.6078 1.4515 1.4729 -0.0432 -0.0771 -0.0433 162  LEU   E CG  
12572 C  CD1 . LEU   E 162 ? 1.6066 1.4412 1.4633 -0.0393 -0.0751 -0.0442 162  LEU   E CD1 
12573 C  CD2 . LEU   E 162 ? 1.5425 1.3908 1.4184 -0.0489 -0.0778 -0.0406 162  LEU   E CD2 
12574 N  N   . HIS   E 163 ? 1.5495 1.4124 1.4106 -0.0296 -0.0702 -0.0476 163  HIS   E N   
12575 C  CA  . HIS   E 163 ? 1.5679 1.4414 1.4344 -0.0260 -0.0665 -0.0476 163  HIS   E CA  
12576 C  C   . HIS   E 163 ? 1.5500 1.4209 1.4098 -0.0244 -0.0664 -0.0491 163  HIS   E C   
12577 O  O   . HIS   E 163 ? 1.5461 1.4150 1.4005 -0.0194 -0.0633 -0.0507 163  HIS   E O   
12578 C  CB  . HIS   E 163 ? 1.6077 1.4829 1.4746 -0.0206 -0.0626 -0.0483 163  HIS   E CB  
12579 C  CG  . HIS   E 163 ? 1.6567 1.5358 1.5307 -0.0217 -0.0622 -0.0466 163  HIS   E CG  
12580 N  ND1 . HIS   E 163 ? 1.6827 1.5708 1.5670 -0.0255 -0.0627 -0.0443 163  HIS   E ND1 
12581 C  CD2 . HIS   E 163 ? 1.7157 1.5902 1.5872 -0.0194 -0.0614 -0.0467 163  HIS   E CD2 
12582 C  CE1 . HIS   E 163 ? 1.7359 1.6246 1.6235 -0.0254 -0.0619 -0.0430 163  HIS   E CE1 
12583 N  NE2 . HIS   E 163 ? 1.7749 1.6553 1.6547 -0.0218 -0.0612 -0.0445 163  HIS   E NE2 
12584 N  N   . VAL   E 164 ? 1.5475 1.4186 1.4080 -0.0285 -0.0697 -0.0485 164  VAL   E N   
12585 C  CA  . VAL   E 164 ? 1.4658 1.3327 1.3185 -0.0275 -0.0704 -0.0497 164  VAL   E CA  
12586 C  C   . VAL   E 164 ? 1.4700 1.3483 1.3297 -0.0258 -0.0668 -0.0490 164  VAL   E C   
12587 O  O   . VAL   E 164 ? 1.5034 1.3910 1.3730 -0.0290 -0.0677 -0.0471 164  VAL   E O   
12588 C  CB  . VAL   E 164 ? 1.3659 1.2268 1.2155 -0.0325 -0.0764 -0.0497 164  VAL   E CB  
12589 C  CG1 . VAL   E 164 ? 1.3828 1.2387 1.2232 -0.0308 -0.0770 -0.0510 164  VAL   E CG1 
12590 C  CG2 . VAL   E 164 ? 1.4295 1.2787 1.2726 -0.0344 -0.0799 -0.0505 164  VAL   E CG2 
12591 N  N   . ILE   E 165 ? 1.4920 1.3691 1.3464 -0.0208 -0.0628 -0.0503 165  ILE   E N   
12592 C  CA  . ILE   E 165 ? 1.4419 1.3284 1.3019 -0.0191 -0.0591 -0.0497 165  ILE   E CA  
12593 C  C   . ILE   E 165 ? 1.4089 1.2935 1.2653 -0.0218 -0.0618 -0.0493 165  ILE   E C   
12594 O  O   . ILE   E 165 ? 1.4412 1.3347 1.3065 -0.0247 -0.0627 -0.0476 165  ILE   E O   
12595 C  CB  . ILE   E 165 ? 1.3868 1.2719 1.2425 -0.0130 -0.0536 -0.0512 165  ILE   E CB  
12596 C  CG1 . ILE   E 165 ? 1.4445 1.3293 1.3020 -0.0101 -0.0519 -0.0520 165  ILE   E CG1 
12597 C  CG2 . ILE   E 165 ? 1.4450 1.3412 1.3093 -0.0113 -0.0492 -0.0504 165  ILE   E CG2 
12598 C  CD1 . ILE   E 165 ? 1.4998 1.3953 1.3703 -0.0118 -0.0520 -0.0505 165  ILE   E CD1 
12599 N  N   . ASP   E 166 ? 1.3550 1.2275 1.1978 -0.0206 -0.0635 -0.0508 166  ASP   E N   
12600 C  CA  . ASP   E 166 ? 1.3361 1.2043 1.1725 -0.0221 -0.0662 -0.0509 166  ASP   E CA  
12601 C  C   . ASP   E 166 ? 1.3634 1.2163 1.1858 -0.0227 -0.0712 -0.0526 166  ASP   E C   
12602 O  O   . ASP   E 166 ? 1.4291 1.2732 1.2421 -0.0191 -0.0694 -0.0543 166  ASP   E O   
12603 C  CB  . ASP   E 166 ? 1.3441 1.2138 1.1769 -0.0176 -0.0606 -0.0511 166  ASP   E CB  
12604 C  CG  . ASP   E 166 ? 1.3673 1.2372 1.1977 -0.0193 -0.0624 -0.0503 166  ASP   E CG  
12605 O  OD1 . ASP   E 166 ? 1.3447 1.2119 1.1745 -0.0236 -0.0688 -0.0500 166  ASP   E OD1 
12606 O  OD2 . ASP   E 166 ? 1.3464 1.2191 1.1759 -0.0163 -0.0574 -0.0500 166  ASP   E OD2 
12607 N  N   . VAL   E 167 ? 1.3464 1.1959 1.1676 -0.0271 -0.0775 -0.0524 167  VAL   E N   
12608 C  CA  . VAL   E 167 ? 1.3621 1.1967 1.1700 -0.0278 -0.0831 -0.0543 167  VAL   E CA  
12609 C  C   . VAL   E 167 ? 1.4123 1.2427 1.2132 -0.0283 -0.0863 -0.0546 167  VAL   E C   
12610 O  O   . VAL   E 167 ? 1.4643 1.3034 1.2739 -0.0310 -0.0876 -0.0531 167  VAL   E O   
12611 C  CB  . VAL   E 167 ? 1.2949 1.1273 1.1076 -0.0330 -0.0891 -0.0542 167  VAL   E CB  
12612 C  CG1 . VAL   E 167 ? 1.2325 1.0767 1.0599 -0.0380 -0.0913 -0.0520 167  VAL   E CG1 
12613 C  CG2 . VAL   E 167 ? 1.3511 1.1682 1.1507 -0.0342 -0.0958 -0.0563 167  VAL   E CG2 
12614 N  N   . LYS   E 168 ? 1.3705 1.1867 1.1548 -0.0253 -0.0877 -0.0566 168  LYS   E N   
12615 C  CA  . LYS   E 168 ? 1.4288 1.2383 1.2034 -0.0248 -0.0909 -0.0572 168  LYS   E CA  
12616 C  C   . LYS   E 168 ? 1.4905 1.2825 1.2490 -0.0243 -0.0968 -0.0598 168  LYS   E C   
12617 O  O   . LYS   E 168 ? 1.5339 1.3175 1.2831 -0.0208 -0.0942 -0.0612 168  LYS   E O   
12618 C  CB  . LYS   E 168 ? 1.4225 1.2334 1.1918 -0.0196 -0.0835 -0.0568 168  LYS   E CB  
12619 C  CG  . LYS   E 168 ? 1.3785 1.2001 1.1563 -0.0209 -0.0822 -0.0549 168  LYS   E CG  
12620 C  CD  . LYS   E 168 ? 1.4025 1.2410 1.1985 -0.0223 -0.0776 -0.0528 168  LYS   E CD  
12621 C  CE  . LYS   E 168 ? 1.4495 1.2978 1.2526 -0.0229 -0.0756 -0.0510 168  LYS   E CE  
12622 N  NZ  . LYS   E 168 ? 1.5063 1.3710 1.3275 -0.0248 -0.0723 -0.0490 168  LYS   E NZ  
12623 N  N   . PHE   E 169 ? 1.4528 1.2392 1.2082 -0.0277 -0.1049 -0.0605 169  PHE   E N   
12624 C  CA  . PHE   E 169 ? 1.4730 1.2419 1.2124 -0.0270 -0.1113 -0.0632 169  PHE   E CA  
12625 C  C   . PHE   E 169 ? 1.5418 1.2988 1.2624 -0.0203 -0.1071 -0.0645 169  PHE   E C   
12626 O  O   . PHE   E 169 ? 1.5323 1.2932 1.2511 -0.0171 -0.1017 -0.0635 169  PHE   E O   
12627 C  CB  . PHE   E 169 ? 1.5430 1.3085 1.2821 -0.0310 -0.1205 -0.0638 169  PHE   E CB  
12628 C  CG  . PHE   E 169 ? 1.5611 1.3318 1.3142 -0.0376 -0.1268 -0.0634 169  PHE   E CG  
12629 C  CD1 . PHE   E 169 ? 1.6221 1.3838 1.3721 -0.0394 -0.1309 -0.0650 169  PHE   E CD1 
12630 C  CD2 . PHE   E 169 ? 1.5427 1.3264 1.3115 -0.0419 -0.1288 -0.0615 169  PHE   E CD2 
12631 C  CE1 . PHE   E 169 ? 1.6346 1.4007 1.3978 -0.0456 -0.1364 -0.0645 169  PHE   E CE1 
12632 C  CE2 . PHE   E 169 ? 1.5130 1.3013 1.2950 -0.0480 -0.1342 -0.0611 169  PHE   E CE2 
12633 C  CZ  . PHE   E 169 ? 1.5601 1.3396 1.3396 -0.0499 -0.1378 -0.0625 169  PHE   E CZ  
12634 N  N   . LEU   E 170 ? 1.6059 1.3474 1.3118 -0.0182 -0.1098 -0.0669 170  LEU   E N   
12635 C  CA  . LEU   E 170 ? 1.5951 1.3244 1.2825 -0.0114 -0.1052 -0.0683 170  LEU   E CA  
12636 C  C   . LEU   E 170 ? 1.6522 1.3660 1.3218 -0.0098 -0.1114 -0.0701 170  LEU   E C   
12637 O  O   . LEU   E 170 ? 1.6159 1.3226 1.2832 -0.0135 -0.1210 -0.0716 170  LEU   E O   
12638 C  CB  . LEU   E 170 ? 1.5689 1.2901 1.2497 -0.0090 -0.1033 -0.0698 170  LEU   E CB  
12639 C  CG  . LEU   E 170 ? 1.5559 1.2896 1.2482 -0.0070 -0.0941 -0.0682 170  LEU   E CG  
12640 C  CD1 . LEU   E 170 ? 1.5803 1.3053 1.2648 -0.0037 -0.0918 -0.0697 170  LEU   E CD1 
12641 C  CD2 . LEU   E 170 ? 1.6133 1.3530 1.3052 -0.0027 -0.0859 -0.0668 170  LEU   E CD2 
12642 N  N   . TYR   E 171 ? 1.6298 1.3384 1.2872 -0.0042 -0.1057 -0.0700 171  TYR   E N   
12643 C  CA  . TYR   E 171 ? 1.6213 1.3128 1.2583 -0.0012 -0.1104 -0.0718 171  TYR   E CA  
12644 C  C   . TYR   E 171 ? 1.7650 1.4388 1.3839 0.0028  -0.1112 -0.0744 171  TYR   E C   
12645 O  O   . TYR   E 171 ? 1.7989 1.4741 1.4185 0.0055  -0.1046 -0.0743 171  TYR   E O   
12646 C  CB  . TYR   E 171 ? 1.6108 1.3026 1.2407 0.0036  -0.1031 -0.0704 171  TYR   E CB  
12647 C  CG  . TYR   E 171 ? 1.5882 1.2929 1.2303 0.0006  -0.1034 -0.0682 171  TYR   E CG  
12648 C  CD1 . TYR   E 171 ? 1.5901 1.2913 1.2305 -0.0026 -0.1129 -0.0689 171  TYR   E CD1 
12649 C  CD2 . TYR   E 171 ? 1.6206 1.3404 1.2754 0.0014  -0.0940 -0.0656 171  TYR   E CD2 
12650 C  CE1 . TYR   E 171 ? 1.5845 1.2972 1.2355 -0.0050 -0.1130 -0.0669 171  TYR   E CE1 
12651 C  CE2 . TYR   E 171 ? 1.5914 1.3225 1.2566 -0.0010 -0.0940 -0.0636 171  TYR   E CE2 
12652 C  CZ  . TYR   E 171 ? 1.6022 1.3297 1.2653 -0.0042 -0.1033 -0.0641 171  TYR   E CZ  
12653 O  OH  . TYR   E 171 ? 1.5599 1.2986 1.2334 -0.0064 -0.1031 -0.0621 171  TYR   E OH  
12654 N  N   . GLY   E 172 ? 1.7735 1.4303 1.3756 0.0035  -0.1197 -0.0769 172  GLY   E N   
12655 C  CA  . GLY   E 172 ? 1.8709 1.5090 1.4533 0.0079  -0.1207 -0.0795 172  GLY   E CA  
12656 C  C   . GLY   E 172 ? 1.9843 1.6186 1.5701 0.0043  -0.1267 -0.0813 172  GLY   E C   
12657 O  O   . GLY   E 172 ? 2.0153 1.6329 1.5842 0.0077  -0.1287 -0.0837 172  GLY   E O   
12658 N  N   . CYS   E 173 ? 2.0531 1.7017 1.6598 -0.0022 -0.1294 -0.0800 173  CYS   E N   
12659 C  CA  . CYS   E 173 ? 2.0034 1.6489 1.6147 -0.0061 -0.1347 -0.0813 173  CYS   E CA  
12660 C  C   . CYS   E 173 ? 2.0191 1.6499 1.6207 -0.0087 -0.1471 -0.0842 173  CYS   E C   
12661 O  O   . CYS   E 173 ? 2.0483 1.6776 1.6481 -0.0100 -0.1529 -0.0845 173  CYS   E O   
12662 C  CB  . CYS   E 173 ? 2.0270 1.6918 1.6632 -0.0124 -0.1340 -0.0789 173  CYS   E CB  
12663 S  SG  . CYS   E 173 ? 2.1536 1.8304 1.8040 -0.0179 -0.1396 -0.0774 173  CYS   E SG  
12664 N  N   . GLN   E 174 ? 1.9025 1.5221 1.4979 -0.0094 -0.1514 -0.0863 174  GLN   E N   
12665 C  CA  . GLN   E 174 ? 1.8827 1.4889 1.4712 -0.0126 -0.1637 -0.0892 174  GLN   E CA  
12666 C  C   . GLN   E 174 ? 1.8656 1.4842 1.4755 -0.0209 -0.1706 -0.0882 174  GLN   E C   
12667 O  O   . GLN   E 174 ? 1.8091 1.4256 1.4193 -0.0234 -0.1787 -0.0891 174  GLN   E O   
12668 C  CB  . GLN   E 174 ? 1.9159 1.5071 1.4930 -0.0113 -0.1660 -0.0916 174  GLN   E CB  
12669 C  CG  . GLN   E 174 ? 1.8915 1.4932 1.4834 -0.0139 -0.1607 -0.0900 174  GLN   E CG  
12670 C  CD  . GLN   E 174 ? 1.8965 1.4834 1.4752 -0.0111 -0.1609 -0.0922 174  GLN   E CD  
12671 O  OE1 . GLN   E 174 ? 1.9379 1.5065 1.4951 -0.0064 -0.1638 -0.0948 174  GLN   E OE1 
12672 N  NE2 . GLN   E 174 ? 1.7940 1.3878 1.3843 -0.0137 -0.1578 -0.0911 174  GLN   E NE2 
12673 N  N   . ALA   E 175 ? 1.8560 1.4872 1.4839 -0.0252 -0.1673 -0.0863 175  ALA   E N   
12674 C  CA  . ALA   E 175 ? 1.7891 1.4345 1.4394 -0.0328 -0.1710 -0.0847 175  ALA   E CA  
12675 C  C   . ALA   E 175 ? 1.7825 1.4479 1.4485 -0.0329 -0.1618 -0.0810 175  ALA   E C   
12676 O  O   . ALA   E 175 ? 1.8682 1.5361 1.5291 -0.0277 -0.1525 -0.0800 175  ALA   E O   
12677 C  CB  . ALA   E 175 ? 1.7780 1.4212 1.4356 -0.0371 -0.1737 -0.0852 175  ALA   E CB  
12678 N  N   . PRO   E 176 ? 1.7088 1.3887 1.3941 -0.0386 -0.1639 -0.0791 176  PRO   E N   
12679 C  CA  . PRO   E 176 ? 1.7329 1.4313 1.4322 -0.0385 -0.1556 -0.0758 176  PRO   E CA  
12680 C  C   . PRO   E 176 ? 1.7356 1.4409 1.4402 -0.0367 -0.1463 -0.0742 176  PRO   E C   
12681 O  O   . PRO   E 176 ? 1.7505 1.4545 1.4603 -0.0395 -0.1473 -0.0743 176  PRO   E O   
12682 C  CB  . PRO   E 176 ? 1.6874 1.3978 1.4065 -0.0456 -0.1609 -0.0744 176  PRO   E CB  
12683 C  CG  . PRO   E 176 ? 1.7304 1.4280 1.4428 -0.0481 -0.1724 -0.0772 176  PRO   E CG  
12684 C  CD  . PRO   E 176 ? 1.6863 1.3660 1.3813 -0.0452 -0.1743 -0.0800 176  PRO   E CD  
12685 N  N   . THR   E 177 ? 1.6947 1.4074 1.3984 -0.0320 -0.1373 -0.0727 177  THR   E N   
12686 C  CA  . THR   E 177 ? 1.6805 1.3987 1.3872 -0.0290 -0.1285 -0.0715 177  THR   E CA  
12687 C  C   . THR   E 177 ? 1.6590 1.3946 1.3785 -0.0281 -0.1206 -0.0687 177  THR   E C   
12688 O  O   . THR   E 177 ? 1.6378 1.3760 1.3542 -0.0257 -0.1185 -0.0682 177  THR   E O   
12689 C  CB  . THR   E 177 ? 1.7030 1.4071 1.3900 -0.0222 -0.1248 -0.0735 177  THR   E CB  
12690 O  OG1 . THR   E 177 ? 1.7374 1.4241 1.4109 -0.0227 -0.1327 -0.0763 177  THR   E OG1 
12691 C  CG2 . THR   E 177 ? 1.7481 1.4568 1.4388 -0.0195 -0.1170 -0.0727 177  THR   E CG2 
12692 N  N   . ILE   E 178 ? 1.6453 1.3920 1.3785 -0.0297 -0.1162 -0.0670 178  ILE   E N   
12693 C  CA  . ILE   E 178 ? 1.5719 1.3353 1.3185 -0.0291 -0.1091 -0.0644 178  ILE   E CA  
12694 C  C   . ILE   E 178 ? 1.5772 1.3417 1.3210 -0.0238 -0.1010 -0.0644 178  ILE   E C   
12695 O  O   . ILE   E 178 ? 1.6266 1.3851 1.3673 -0.0231 -0.1008 -0.0653 178  ILE   E O   
12696 C  CB  . ILE   E 178 ? 1.5296 1.3062 1.2954 -0.0350 -0.1106 -0.0623 178  ILE   E CB  
12697 C  CG1 . ILE   E 178 ? 1.5331 1.3052 1.3011 -0.0374 -0.1125 -0.0627 178  ILE   E CG1 
12698 C  CG2 . ILE   E 178 ? 1.5268 1.3061 1.2984 -0.0398 -0.1174 -0.0619 178  ILE   E CG2 
12699 C  CD1 . ILE   E 178 ? 1.4929 1.2783 1.2783 -0.0409 -0.1101 -0.0602 178  ILE   E CD1 
12700 N  N   . CYS   E 179 ? 1.5429 1.3158 1.2893 -0.0202 -0.0942 -0.0633 179  CYS   E N   
12701 C  CA  . CYS   E 179 ? 1.5207 1.2970 1.2671 -0.0151 -0.0860 -0.0632 179  CYS   E CA  
12702 C  C   . CYS   E 179 ? 1.4694 1.2636 1.2343 -0.0167 -0.0819 -0.0608 179  CYS   E C   
12703 O  O   . CYS   E 179 ? 1.4195 1.2230 1.1915 -0.0178 -0.0807 -0.0593 179  CYS   E O   
12704 C  CB  . CYS   E 179 ? 1.5219 1.2923 1.2558 -0.0093 -0.0814 -0.0640 179  CYS   E CB  
12705 S  SG  . CYS   E 179 ? 1.6356 1.4096 1.3695 -0.0026 -0.0713 -0.0641 179  CYS   E SG  
12706 N  N   . PHE   E 180 ? 1.5267 1.3251 1.2989 -0.0169 -0.0800 -0.0604 180  PHE   E N   
12707 C  CA  . PHE   E 180 ? 1.4953 1.3095 1.2842 -0.0184 -0.0767 -0.0583 180  PHE   E CA  
12708 C  C   . PHE   E 180 ? 1.5328 1.3503 1.3233 -0.0133 -0.0701 -0.0586 180  PHE   E C   
12709 O  O   . PHE   E 180 ? 1.6121 1.4200 1.3936 -0.0105 -0.0696 -0.0602 180  PHE   E O   
12710 C  CB  . PHE   E 180 ? 1.4949 1.3121 1.2933 -0.0243 -0.0815 -0.0571 180  PHE   E CB  
12711 C  CG  . PHE   E 180 ? 1.5614 1.3680 1.3535 -0.0245 -0.0839 -0.0584 180  PHE   E CG  
12712 C  CD1 . PHE   E 180 ? 1.6152 1.4073 1.3948 -0.0255 -0.0892 -0.0602 180  PHE   E CD1 
12713 C  CD2 . PHE   E 180 ? 1.5768 1.3873 1.3750 -0.0236 -0.0809 -0.0578 180  PHE   E CD2 
12714 C  CE1 . PHE   E 180 ? 1.6764 1.4583 1.4500 -0.0258 -0.0914 -0.0614 180  PHE   E CE1 
12715 C  CE2 . PHE   E 180 ? 1.6385 1.4388 1.4304 -0.0238 -0.0829 -0.0588 180  PHE   E CE2 
12716 C  CZ  . PHE   E 180 ? 1.6853 1.4714 1.4652 -0.0250 -0.0880 -0.0606 180  PHE   E CZ  
12717 N  N   . VAL   E 181 ? 1.4634 1.2945 1.2655 -0.0121 -0.0652 -0.0572 181  VAL   E N   
12718 C  CA  . VAL   E 181 ? 1.5124 1.3498 1.3203 -0.0079 -0.0595 -0.0573 181  VAL   E CA  
12719 C  C   . VAL   E 181 ? 1.5109 1.3555 1.3302 -0.0110 -0.0611 -0.0560 181  VAL   E C   
12720 O  O   . VAL   E 181 ? 1.5334 1.3859 1.3622 -0.0155 -0.0634 -0.0542 181  VAL   E O   
12721 C  CB  . VAL   E 181 ? 1.4417 1.2895 1.2564 -0.0049 -0.0536 -0.0566 181  VAL   E CB  
12722 C  CG1 . VAL   E 181 ? 1.4314 1.2881 1.2558 -0.0015 -0.0488 -0.0566 181  VAL   E CG1 
12723 C  CG2 . VAL   E 181 ? 1.4478 1.2873 1.2502 -0.0009 -0.0506 -0.0579 181  VAL   E CG2 
12724 N  N   . TYR   E 182 ? 1.5380 1.3796 1.3562 -0.0084 -0.0598 -0.0568 182  TYR   E N   
12725 C  CA  . TYR   E 182 ? 1.5320 1.3787 1.3591 -0.0106 -0.0608 -0.0556 182  TYR   E CA  
12726 C  C   . TYR   E 182 ? 1.5374 1.3886 1.3683 -0.0053 -0.0562 -0.0563 182  TYR   E C   
12727 O  O   . TYR   E 182 ? 1.6275 1.4752 1.4526 -0.0003 -0.0529 -0.0579 182  TYR   E O   
12728 C  CB  . TYR   E 182 ? 1.5520 1.3878 1.3728 -0.0140 -0.0658 -0.0559 182  TYR   E CB  
12729 C  CG  . TYR   E 182 ? 1.5960 1.4183 1.4035 -0.0104 -0.0658 -0.0581 182  TYR   E CG  
12730 C  CD1 . TYR   E 182 ? 1.5835 1.3957 1.3784 -0.0086 -0.0666 -0.0598 182  TYR   E CD1 
12731 C  CD2 . TYR   E 182 ? 1.6396 1.4585 1.4464 -0.0086 -0.0652 -0.0584 182  TYR   E CD2 
12732 C  CE1 . TYR   E 182 ? 1.6354 1.4350 1.4179 -0.0051 -0.0666 -0.0618 182  TYR   E CE1 
12733 C  CE2 . TYR   E 182 ? 1.6482 1.4547 1.4428 -0.0053 -0.0652 -0.0604 182  TYR   E CE2 
12734 C  CZ  . TYR   E 182 ? 1.6482 1.4452 1.4308 -0.0036 -0.0659 -0.0621 182  TYR   E CZ  
12735 O  OH  . TYR   E 182 ? 1.7277 1.5121 1.4980 0.0000  -0.0659 -0.0641 182  TYR   E OH  
12736 N  N   . GLN   E 183 ? 1.5011 1.3602 1.3421 -0.0064 -0.0561 -0.0550 183  GLN   E N   
12737 C  CA  . GLN   E 183 ? 1.6027 1.4665 1.4483 -0.0016 -0.0526 -0.0556 183  GLN   E CA  
12738 C  C   . GLN   E 183 ? 1.6896 1.5495 1.5353 -0.0029 -0.0549 -0.0550 183  GLN   E C   
12739 O  O   . GLN   E 183 ? 1.7222 1.5864 1.5745 -0.0073 -0.0569 -0.0530 183  GLN   E O   
12740 C  CB  . GLN   E 183 ? 1.6532 1.5316 1.5119 -0.0009 -0.0497 -0.0546 183  GLN   E CB  
12741 N  N   . ASP   E 184 ? 1.6910 1.5420 1.5287 0.0008  -0.0544 -0.0566 184  ASP   E N   
12742 C  CA  . ASP   E 184 ? 1.7598 1.6069 1.5971 0.0004  -0.0559 -0.0560 184  ASP   E CA  
12743 C  C   . ASP   E 184 ? 1.8149 1.6652 1.6546 0.0068  -0.0529 -0.0573 184  ASP   E C   
12744 O  O   . ASP   E 184 ? 1.8550 1.7109 1.6976 0.0107  -0.0498 -0.0585 184  ASP   E O   
12745 C  CB  . ASP   E 184 ? 1.7605 1.5927 1.5858 -0.0014 -0.0589 -0.0567 184  ASP   E CB  
12746 C  CG  . ASP   E 184 ? 1.8725 1.6954 1.6866 0.0037  -0.0576 -0.0593 184  ASP   E CG  
12747 O  OD1 . ASP   E 184 ? 1.9143 1.7424 1.7303 0.0084  -0.0541 -0.0605 184  ASP   E OD1 
12748 O  OD2 . ASP   E 184 ? 1.9282 1.7384 1.7320 0.0031  -0.0600 -0.0601 184  ASP   E OD2 
12749 N  N   . PRO   E 185 ? 1.8630 1.7102 1.7023 0.0080  -0.0535 -0.0570 185  PRO   E N   
12750 C  CA  . PRO   E 185 ? 1.9115 1.7610 1.7525 0.0146  -0.0513 -0.0586 185  PRO   E CA  
12751 C  C   . PRO   E 185 ? 1.9636 1.8105 1.7998 0.0201  -0.0488 -0.0612 185  PRO   E C   
12752 O  O   . PRO   E 185 ? 1.9254 1.7800 1.7685 0.0249  -0.0463 -0.0623 185  PRO   E O   
12753 C  CB  . PRO   E 185 ? 1.9103 1.7501 1.7450 0.0147  -0.0531 -0.0582 185  PRO   E CB  
12754 C  CG  . PRO   E 185 ? 1.8764 1.7169 1.7142 0.0079  -0.0553 -0.0554 185  PRO   E CG  
12755 C  CD  . PRO   E 185 ? 1.8672 1.7108 1.7067 0.0034  -0.0560 -0.0549 185  PRO   E CD  
12756 N  N   . GLN   E 186 ? 2.0876 1.9237 1.9127 0.0196  -0.0495 -0.0622 186  GLN   E N   
12757 C  CA  . GLN   E 186 ? 2.1100 1.9414 1.9285 0.0251  -0.0469 -0.0646 186  GLN   E CA  
12758 C  C   . GLN   E 186 ? 2.0834 1.9242 1.9084 0.0268  -0.0433 -0.0650 186  GLN   E C   
12759 O  O   . GLN   E 186 ? 2.0846 1.9265 1.9098 0.0324  -0.0399 -0.0669 186  GLN   E O   
12760 C  CB  . GLN   E 186 ? 2.0971 1.9136 1.9010 0.0238  -0.0489 -0.0654 186  GLN   E CB  
12761 C  CG  . GLN   E 186 ? 2.1394 1.9441 1.9348 0.0239  -0.0516 -0.0657 186  GLN   E CG  
12762 C  CD  . GLN   E 186 ? 2.1792 1.9856 1.9795 0.0187  -0.0543 -0.0633 186  GLN   E CD  
12763 O  OE1 . GLN   E 186 ? 2.1279 1.9403 1.9344 0.0133  -0.0556 -0.0615 186  GLN   E OE1 
12764 N  NE2 . GLN   E 186 ? 2.2201 2.0209 2.0175 0.0204  -0.0551 -0.0633 186  GLN   E NE2 
12765 N  N   . GLY   E 187 ? 1.9729 1.8199 1.8029 0.0220  -0.0438 -0.0634 187  GLY   E N   
12766 C  CA  . GLY   E 187 ? 1.8763 1.7314 1.7117 0.0232  -0.0403 -0.0635 187  GLY   E CA  
12767 C  C   . GLY   E 187 ? 1.8263 1.6820 1.6608 0.0175  -0.0421 -0.0618 187  GLY   E C   
12768 O  O   . GLY   E 187 ? 1.7931 1.6473 1.6277 0.0123  -0.0460 -0.0603 187  GLY   E O   
12769 N  N   . ARG   E 188 ? 1.7588 1.6167 1.5928 0.0186  -0.0391 -0.0622 188  ARG   E N   
12770 C  CA  . ARG   E 188 ? 1.7265 1.5831 1.5573 0.0142  -0.0407 -0.0610 188  ARG   E CA  
12771 C  C   . ARG   E 188 ? 1.8125 1.6555 1.6279 0.0160  -0.0406 -0.0625 188  ARG   E C   
12772 O  O   . ARG   E 188 ? 1.7959 1.6367 1.6076 0.0212  -0.0362 -0.0639 188  ARG   E O   
12773 C  CB  . ARG   E 188 ? 1.6086 1.4772 1.4495 0.0143  -0.0372 -0.0601 188  ARG   E CB  
12774 N  N   . HIS   E 189 ? 1.9096 1.7430 1.7161 0.0118  -0.0456 -0.0622 189  HIS   E N   
12775 C  CA  . HIS   E 189 ? 1.9027 1.7215 1.6933 0.0129  -0.0469 -0.0637 189  HIS   E CA  
12776 C  C   . HIS   E 189 ? 1.8765 1.6920 1.6627 0.0082  -0.0507 -0.0629 189  HIS   E C   
12777 O  O   . HIS   E 189 ? 1.8719 1.6965 1.6678 0.0038  -0.0525 -0.0611 189  HIS   E O   
12778 C  CB  . HIS   E 189 ? 1.9172 1.7244 1.6993 0.0129  -0.0504 -0.0648 189  HIS   E CB  
12779 C  CG  . HIS   E 189 ? 1.9425 1.7539 1.7309 0.0159  -0.0485 -0.0651 189  HIS   E CG  
12780 N  ND1 . HIS   E 189 ? 1.9949 1.8113 1.7869 0.0219  -0.0433 -0.0662 189  HIS   E ND1 
12781 C  CD2 . HIS   E 189 ? 1.9572 1.7680 1.7486 0.0139  -0.0513 -0.0645 189  HIS   E CD2 
12782 C  CE1 . HIS   E 189 ? 2.0077 1.8264 1.8045 0.0237  -0.0434 -0.0664 189  HIS   E CE1 
12783 N  NE2 . HIS   E 189 ? 2.0123 1.8273 1.8082 0.0190  -0.0480 -0.0653 189  HIS   E NE2 
12784 N  N   . VAL   E 190 ? 1.8087 1.6106 1.5799 0.0093  -0.0523 -0.0643 190  VAL   E N   
12785 C  CA  . VAL   E 190 ? 1.7164 1.5124 1.4809 0.0054  -0.0569 -0.0641 190  VAL   E CA  
12786 C  C   . VAL   E 190 ? 1.7501 1.5313 1.5028 0.0034  -0.0629 -0.0654 190  VAL   E C   
12787 O  O   . VAL   E 190 ? 1.8114 1.5824 1.5538 0.0073  -0.0618 -0.0672 190  VAL   E O   
12788 C  CB  . VAL   E 190 ? 1.6835 1.4763 1.4399 0.0090  -0.0532 -0.0646 190  VAL   E CB  
12789 C  CG1 . VAL   E 190 ? 1.6487 1.4378 1.4005 0.0048  -0.0581 -0.0641 190  VAL   E CG1 
12790 C  CG2 . VAL   E 190 ? 1.6832 1.4895 1.4509 0.0120  -0.0461 -0.0636 190  VAL   E CG2 
12791 N  N   . LYS   E 191 ? 1.7032 1.4832 1.4577 -0.0027 -0.0692 -0.0646 191  LYS   E N   
12792 C  CA  . LYS   E 191 ? 1.6994 1.4650 1.4432 -0.0053 -0.0756 -0.0660 191  LYS   E CA  
12793 C  C   . LYS   E 191 ? 1.6807 1.4432 1.4219 -0.0096 -0.0814 -0.0659 191  LYS   E C   
12794 O  O   . LYS   E 191 ? 1.6476 1.4204 1.3975 -0.0117 -0.0809 -0.0643 191  LYS   E O   
12795 C  CB  . LYS   E 191 ? 1.6112 1.3774 1.3618 -0.0089 -0.0784 -0.0653 191  LYS   E CB  
12796 N  N   . THR   E 192 ? 1.7744 1.5221 1.5031 -0.0108 -0.0872 -0.0676 192  THR   E N   
12797 C  CA  . THR   E 192 ? 1.7811 1.5233 1.5054 -0.0145 -0.0937 -0.0681 192  THR   E CA  
12798 C  C   . THR   E 192 ? 1.7962 1.5298 1.5194 -0.0196 -0.1013 -0.0689 192  THR   E C   
12799 O  O   . THR   E 192 ? 1.7963 1.5190 1.5110 -0.0181 -0.1022 -0.0704 192  THR   E O   
12800 C  CB  . THR   E 192 ? 1.8017 1.5313 1.5081 -0.0099 -0.0937 -0.0700 192  THR   E CB  
12801 O  OG1 . THR   E 192 ? 1.8297 1.5443 1.5217 -0.0066 -0.0945 -0.0723 192  THR   E OG1 
12802 C  CG2 . THR   E 192 ? 1.8219 1.5590 1.5289 -0.0049 -0.0858 -0.0692 192  THR   E CG2 
12803 N  N   . TYR   E 193 ? 1.7387 1.4771 1.4710 -0.0255 -0.1068 -0.0679 193  TYR   E N   
12804 C  CA  . TYR   E 193 ? 1.7184 1.4491 1.4511 -0.0310 -0.1146 -0.0686 193  TYR   E CA  
12805 C  C   . TYR   E 193 ? 1.6854 1.4095 1.4120 -0.0331 -0.1217 -0.0699 193  TYR   E C   
12806 O  O   . TYR   E 193 ? 1.6536 1.3840 1.3818 -0.0322 -0.1207 -0.0692 193  TYR   E O   
12807 C  CB  . TYR   E 193 ? 1.7008 1.4433 1.4519 -0.0368 -0.1151 -0.0662 193  TYR   E CB  
12808 C  CG  . TYR   E 193 ? 1.6497 1.3968 1.4060 -0.0351 -0.1093 -0.0650 193  TYR   E CG  
12809 C  CD1 . TYR   E 193 ? 1.6772 1.4166 1.4222 -0.0294 -0.1053 -0.0665 193  TYR   E CD1 
12810 C  CD2 . TYR   E 193 ? 1.6876 1.4463 1.4598 -0.0391 -0.1079 -0.0626 193  TYR   E CD2 
12811 C  CE1 . TYR   E 193 ? 1.7369 1.4800 1.4863 -0.0275 -0.1005 -0.0656 193  TYR   E CE1 
12812 C  CE2 . TYR   E 193 ? 1.7284 1.4903 1.5044 -0.0371 -0.1029 -0.0616 193  TYR   E CE2 
12813 C  CZ  . TYR   E 193 ? 1.7433 1.4974 1.5078 -0.0313 -0.0995 -0.0632 193  TYR   E CZ  
12814 O  OH  . TYR   E 193 ? 1.6837 1.4403 1.4511 -0.0289 -0.0949 -0.0625 193  TYR   E OH  
12815 N  N   . GLU   E 194 ? 1.7828 1.4939 1.5027 -0.0359 -0.1292 -0.0718 194  GLU   E N   
12816 C  CA  . GLU   E 194 ? 1.8037 1.5079 1.5194 -0.0388 -0.1377 -0.0733 194  GLU   E CA  
12817 C  C   . GLU   E 194 ? 1.7991 1.5107 1.5317 -0.0465 -0.1432 -0.0720 194  GLU   E C   
12818 O  O   . GLU   E 194 ? 1.8241 1.5406 1.5674 -0.0497 -0.1416 -0.0706 194  GLU   E O   
12819 C  CB  . GLU   E 194 ? 1.8391 1.5230 1.5357 -0.0366 -0.1432 -0.0767 194  GLU   E CB  
12820 C  CG  . GLU   E 194 ? 1.8463 1.5206 1.5240 -0.0287 -0.1384 -0.0782 194  GLU   E CG  
12821 C  CD  . GLU   E 194 ? 1.8871 1.5427 1.5456 -0.0268 -0.1457 -0.0814 194  GLU   E CD  
12822 O  OE1 . GLU   E 194 ? 1.8816 1.5245 1.5339 -0.0287 -0.1520 -0.0835 194  GLU   E OE1 
12823 O  OE2 . GLU   E 194 ? 1.9184 1.5714 1.5677 -0.0232 -0.1452 -0.0818 194  GLU   E OE2 
12824 N  N   . VAL   E 195 ? 1.7531 1.4650 1.4878 -0.0494 -0.1498 -0.0726 195  VAL   E N   
12825 C  CA  . VAL   E 195 ? 1.7477 1.4688 1.5002 -0.0565 -0.1546 -0.0712 195  VAL   E CA  
12826 C  C   . VAL   E 195 ? 1.8078 1.5166 1.5561 -0.0602 -0.1654 -0.0738 195  VAL   E C   
12827 O  O   . VAL   E 195 ? 1.7738 1.4750 1.5115 -0.0584 -0.1707 -0.0758 195  VAL   E O   
12828 C  CB  . VAL   E 195 ? 1.6967 1.4325 1.4596 -0.0571 -0.1526 -0.0691 195  VAL   E CB  
12829 C  CG1 . VAL   E 195 ? 1.6677 1.4120 1.4485 -0.0642 -0.1580 -0.0679 195  VAL   E CG1 
12830 C  CG2 . VAL   E 195 ? 1.6970 1.4453 1.4658 -0.0539 -0.1424 -0.0666 195  VAL   E CG2 
12831 N  N   . SER   E 196 ? 1.7890 1.4955 1.5457 -0.0654 -0.1689 -0.0738 196  SER   E N   
12832 C  CA  . SER   E 196 ? 1.8611 1.5573 1.6174 -0.0700 -0.1795 -0.0762 196  SER   E CA  
12833 C  C   . SER   E 196 ? 1.8327 1.5418 1.6107 -0.0769 -0.1828 -0.0743 196  SER   E C   
12834 O  O   . SER   E 196 ? 1.8105 1.5283 1.6034 -0.0808 -0.1791 -0.0719 196  SER   E O   
12835 C  CB  . SER   E 196 ? 1.9412 1.6243 1.6913 -0.0710 -0.1813 -0.0777 196  SER   E CB  
12836 O  OG  . SER   E 196 ? 1.9439 1.6145 1.6907 -0.0746 -0.1921 -0.0806 196  SER   E OG  
12837 N  N   . LEU   E 197 ? 1.8275 1.5377 1.6071 -0.0782 -0.1894 -0.0753 197  LEU   E N   
12838 C  CA  . LEU   E 197 ? 1.8149 1.5363 1.6151 -0.0848 -0.1935 -0.0738 197  LEU   E CA  
12839 C  C   . LEU   E 197 ? 1.8975 1.6115 1.7049 -0.0908 -0.2008 -0.0752 197  LEU   E C   
12840 O  O   . LEU   E 197 ? 1.8913 1.6152 1.7180 -0.0965 -0.1999 -0.0730 197  LEU   E O   
12841 C  CB  . LEU   E 197 ? 1.7281 1.4518 1.5274 -0.0841 -0.1993 -0.0748 197  LEU   E CB  
12842 C  CG  . LEU   E 197 ? 1.7213 1.4508 1.5125 -0.0781 -0.1928 -0.0737 197  LEU   E CG  
12843 C  CD1 . LEU   E 197 ? 1.7902 1.5039 1.5568 -0.0715 -0.1932 -0.0764 197  LEU   E CD1 
12844 C  CD2 . LEU   E 197 ? 1.6707 1.4093 1.4708 -0.0797 -0.1968 -0.0731 197  LEU   E CD2 
12845 N  N   . ARG   E 198 ? 1.9165 1.6129 1.7087 -0.0896 -0.2076 -0.0788 198  ARG   E N   
12846 C  CA  . ARG   E 198 ? 1.9316 1.6199 1.7303 -0.0954 -0.2150 -0.0803 198  ARG   E CA  
12847 C  C   . ARG   E 198 ? 1.9077 1.5970 1.7121 -0.0974 -0.2082 -0.0783 198  ARG   E C   
12848 O  O   . ARG   E 198 ? 1.8726 1.5660 1.6937 -0.1038 -0.2097 -0.0771 198  ARG   E O   
12849 C  CB  . ARG   E 198 ? 2.0026 1.6709 1.7820 -0.0931 -0.2242 -0.0848 198  ARG   E CB  
12850 C  CG  . ARG   E 198 ? 2.0787 1.7354 1.8345 -0.0854 -0.2193 -0.0861 198  ARG   E CG  
12851 C  CD  . ARG   E 198 ? 2.1538 1.7900 1.8946 -0.0850 -0.2265 -0.0899 198  ARG   E CD  
12852 N  NE  . ARG   E 198 ? 2.1273 1.7623 1.8792 -0.0905 -0.2266 -0.0892 198  ARG   E NE  
12853 C  CZ  . ARG   E 198 ? 2.1293 1.7633 1.8784 -0.0890 -0.2186 -0.0877 198  ARG   E CZ  
12854 N  NH1 . ARG   E 198 ? 2.1510 1.7856 1.8875 -0.0821 -0.2100 -0.0868 198  ARG   E NH1 
12855 N  NH2 . ARG   E 198 ? 2.1069 1.7391 1.8663 -0.0943 -0.2191 -0.0870 198  ARG   E NH2 
12856 N  N   . GLU   E 199 ? 2.0130 1.6985 1.8039 -0.0917 -0.2005 -0.0779 199  GLU   E N   
12857 C  CA  . GLU   E 199 ? 2.0744 1.7622 1.8707 -0.0928 -0.1932 -0.0756 199  GLU   E CA  
12858 C  C   . GLU   E 199 ? 2.0777 1.7846 1.8911 -0.0942 -0.1848 -0.0714 199  GLU   E C   
12859 O  O   . GLU   E 199 ? 2.1222 1.8323 1.9428 -0.0959 -0.1791 -0.0692 199  GLU   E O   
12860 C  CB  . GLU   E 199 ? 2.1204 1.7974 1.8964 -0.0859 -0.1882 -0.0768 199  GLU   E CB  
12861 C  CG  . GLU   E 199 ? 2.1682 1.8422 1.9451 -0.0865 -0.1825 -0.0755 199  GLU   E CG  
12862 C  CD  . GLU   E 199 ? 2.1785 1.8547 1.9453 -0.0794 -0.1728 -0.0744 199  GLU   E CD  
12863 O  OE1 . GLU   E 199 ? 2.2137 1.8914 1.9709 -0.0740 -0.1708 -0.0751 199  GLU   E OE1 
12864 O  OE2 . GLU   E 199 ? 2.1578 1.8342 1.9265 -0.0792 -0.1671 -0.0728 199  GLU   E OE2 
12865 N  N   . LYS   E 200 ? 1.9329 1.6517 1.7525 -0.0935 -0.1841 -0.0703 200  LYS   E N   
12866 C  CA  . LYS   E 200 ? 1.8111 1.5479 1.6463 -0.0945 -0.1766 -0.0664 200  LYS   E CA  
12867 C  C   . LYS   E 200 ? 1.7883 1.5280 1.6198 -0.0906 -0.1665 -0.0644 200  LYS   E C   
12868 O  O   . LYS   E 200 ? 1.7976 1.5486 1.6424 -0.0926 -0.1607 -0.0613 200  LYS   E O   
12869 C  CB  . LYS   E 200 ? 1.7926 1.5377 1.6495 -0.1021 -0.1787 -0.0645 200  LYS   E CB  
12870 C  CG  . LYS   E 200 ? 1.8468 1.5903 1.7108 -0.1067 -0.1892 -0.0664 200  LYS   E CG  
12871 C  CD  . LYS   E 200 ? 1.7843 1.5439 1.6635 -0.1085 -0.1888 -0.0643 200  LYS   E CD  
12872 C  CE  . LYS   E 200 ? 1.8305 1.5880 1.7174 -0.1131 -0.1999 -0.0665 200  LYS   E CE  
12873 N  NZ  . LYS   E 200 ? 1.7510 1.5199 1.6449 -0.1127 -0.2017 -0.0659 200  LYS   E NZ  
12874 N  N   . GLU   E 201 ? 1.8839 1.6132 1.6972 -0.0848 -0.1645 -0.0663 201  GLU   E N   
12875 C  CA  . GLU   E 201 ? 1.8797 1.6118 1.6891 -0.0804 -0.1553 -0.0647 201  GLU   E CA  
12876 C  C   . GLU   E 201 ? 1.8908 1.6184 1.6831 -0.0730 -0.1526 -0.0664 201  GLU   E C   
12877 O  O   . GLU   E 201 ? 1.8293 1.5541 1.6146 -0.0714 -0.1568 -0.0681 201  GLU   E O   
12878 C  CB  . GLU   E 201 ? 1.8982 1.6206 1.7056 -0.0821 -0.1547 -0.0648 201  GLU   E CB  
12879 N  N   . PHE   E 202 ? 1.8381 1.5646 1.6235 -0.0682 -0.1456 -0.0659 202  PHE   E N   
12880 C  CA  . PHE   E 202 ? 1.8590 1.5816 1.6293 -0.0609 -0.1418 -0.0673 202  PHE   E CA  
12881 C  C   . PHE   E 202 ? 1.9093 1.6136 1.6617 -0.0579 -0.1444 -0.0703 202  PHE   E C   
12882 O  O   . PHE   E 202 ? 1.9851 1.6808 1.7372 -0.0610 -0.1476 -0.0710 202  PHE   E O   
12883 C  CB  . PHE   E 202 ? 1.8540 1.5875 1.6286 -0.0569 -0.1323 -0.0651 202  PHE   E CB  
12884 C  CG  . PHE   E 202 ? 1.8179 1.5670 1.6024 -0.0564 -0.1288 -0.0631 202  PHE   E CG  
12885 C  CD1 . PHE   E 202 ? 1.8185 1.5676 1.5969 -0.0543 -0.1306 -0.0642 202  PHE   E CD1 
12886 C  CD2 . PHE   E 202 ? 1.7466 1.5096 1.5459 -0.0581 -0.1238 -0.0602 202  PHE   E CD2 
12887 C  CE1 . PHE   E 202 ? 1.7930 1.5559 1.5804 -0.0539 -0.1275 -0.0624 202  PHE   E CE1 
12888 C  CE2 . PHE   E 202 ? 1.7345 1.5114 1.5428 -0.0577 -0.1209 -0.0585 202  PHE   E CE2 
12889 C  CZ  . PHE   E 202 ? 1.7580 1.5349 1.5605 -0.0557 -0.1227 -0.0596 202  PHE   E CZ  
12890 N  N   . ASN   E 203 ? 1.9403 1.6385 1.6774 -0.0516 -0.1428 -0.0721 203  ASN   E N   
12891 C  CA  . ASN   E 203 ? 1.9624 1.6439 1.6809 -0.0471 -0.1435 -0.0748 203  ASN   E CA  
12892 C  C   . ASN   E 203 ? 1.9448 1.6288 1.6548 -0.0395 -0.1352 -0.0747 203  ASN   E C   
12893 O  O   . ASN   E 203 ? 1.9195 1.6136 1.6330 -0.0375 -0.1315 -0.0736 203  ASN   E O   
12894 C  CB  . ASN   E 203 ? 1.9613 1.6285 1.6667 -0.0474 -0.1522 -0.0779 203  ASN   E CB  
12895 C  CG  . ASN   E 203 ? 2.0250 1.6849 1.7356 -0.0542 -0.1611 -0.0790 203  ASN   E CG  
12896 O  OD1 . ASN   E 203 ? 2.0622 1.7219 1.7801 -0.0576 -0.1604 -0.0780 203  ASN   E OD1 
12897 N  ND2 . ASN   E 203 ? 2.0066 1.6597 1.7130 -0.0562 -0.1696 -0.0810 203  ASN   E ND2 
12898 N  N   . LYS   E 204 ? 1.8283 1.5030 1.5277 -0.0353 -0.1321 -0.0759 204  LYS   E N   
12899 C  CA  . LYS   E 204 ? 1.8015 1.4791 1.4949 -0.0282 -0.1238 -0.0757 204  LYS   E CA  
12900 C  C   . LYS   E 204 ? 1.7904 1.4646 1.4720 -0.0233 -0.1229 -0.0770 204  LYS   E C   
12901 O  O   . LYS   E 204 ? 1.8123 1.4720 1.4794 -0.0223 -0.1281 -0.0794 204  LYS   E O   
12902 C  CB  . LYS   E 204 ? 1.7456 1.4116 1.4282 -0.0246 -0.1219 -0.0771 204  LYS   E CB  
12903 N  N   . GLY   E 205 ? 1.7158 1.4026 1.4032 -0.0202 -0.1160 -0.0754 205  GLY   E N   
12904 C  CA  . GLY   E 205 ? 1.7295 1.4147 1.4079 -0.0161 -0.1144 -0.0760 205  GLY   E CA  
12905 C  C   . GLY   E 205 ? 1.7306 1.4038 1.3912 -0.0087 -0.1102 -0.0780 205  GLY   E C   
12906 O  O   . GLY   E 205 ? 1.7480 1.4149 1.4036 -0.0062 -0.1082 -0.0789 205  GLY   E O   
12907 N  N   . PRO   E 206 ? 1.7100 1.3794 1.3603 -0.0047 -0.1086 -0.0786 206  PRO   E N   
12908 C  CA  . PRO   E 206 ? 1.7300 1.3880 1.3631 0.0029  -0.1038 -0.0803 206  PRO   E CA  
12909 C  C   . PRO   E 206 ? 1.8158 1.4822 1.4541 0.0077  -0.0942 -0.0794 206  PRO   E C   
12910 O  O   . PRO   E 206 ? 1.9383 1.5966 1.5697 0.0106  -0.0929 -0.0807 206  PRO   E O   
12911 C  CB  . PRO   E 206 ? 1.7125 1.3678 1.3368 0.0054  -0.1034 -0.0805 206  PRO   E CB  
12912 C  CG  . PRO   E 206 ? 1.6969 1.3654 1.3364 -0.0003 -0.1063 -0.0785 206  PRO   E CG  
12913 C  CD  . PRO   E 206 ? 1.7096 1.3812 1.3606 -0.0071 -0.1126 -0.0783 206  PRO   E CD  
12914 N  N   . TRP   E 207 ? 1.7813 1.4632 1.4316 0.0087  -0.0878 -0.0773 207  TRP   E N   
12915 C  CA  . TRP   E 207 ? 1.8207 1.5101 1.4753 0.0140  -0.0787 -0.0767 207  TRP   E CA  
12916 C  C   . TRP   E 207 ? 1.8177 1.5254 1.4932 0.0110  -0.0760 -0.0744 207  TRP   E C   
12917 O  O   . TRP   E 207 ? 1.8081 1.5249 1.4953 0.0053  -0.0796 -0.0728 207  TRP   E O   
12918 C  CB  . TRP   E 207 ? 1.8922 1.5821 1.5405 0.0194  -0.0721 -0.0765 207  TRP   E CB  
12919 C  CG  . TRP   E 207 ? 1.8311 1.5269 1.4832 0.0164  -0.0739 -0.0751 207  TRP   E CG  
12920 C  CD1 . TRP   E 207 ? 1.7860 1.4711 1.4266 0.0148  -0.0801 -0.0761 207  TRP   E CD1 
12921 C  CD2 . TRP   E 207 ? 1.8005 1.5137 1.4687 0.0150  -0.0695 -0.0727 207  TRP   E CD2 
12922 N  NE1 . TRP   E 207 ? 1.7921 1.4870 1.4406 0.0125  -0.0798 -0.0743 207  TRP   E NE1 
12923 C  CE2 . TRP   E 207 ? 1.7759 1.4882 1.4413 0.0125  -0.0733 -0.0722 207  TRP   E CE2 
12924 C  CE3 . TRP   E 207 ? 1.7593 1.4886 1.4437 0.0157  -0.0631 -0.0711 207  TRP   E CE3 
12925 C  CZ2 . TRP   E 207 ? 1.6853 1.4120 1.3636 0.0106  -0.0705 -0.0700 207  TRP   E CZ2 
12926 C  CZ3 . TRP   E 207 ? 1.6483 1.3919 1.3457 0.0137  -0.0606 -0.0690 207  TRP   E CZ3 
12927 C  CH2 . TRP   E 207 ? 1.6389 1.3811 1.3330 0.0112  -0.0641 -0.0684 207  TRP   E CH2 
12928 N  N   . LYS   E 208 ? 1.8609 1.5735 1.5406 0.0152  -0.0698 -0.0744 208  LYS   E N   
12929 C  CA  . LYS   E 208 ? 1.8522 1.5812 1.5502 0.0136  -0.0667 -0.0725 208  LYS   E CA  
12930 C  C   . LYS   E 208 ? 1.9046 1.6395 1.6051 0.0202  -0.0582 -0.0727 208  LYS   E C   
12931 O  O   . LYS   E 208 ? 1.9072 1.6322 1.5953 0.0258  -0.0550 -0.0743 208  LYS   E O   
12932 C  CB  . LYS   E 208 ? 1.7155 1.4434 1.4183 0.0100  -0.0709 -0.0724 208  LYS   E CB  
12933 C  CG  . LYS   E 208 ? 1.7842 1.5097 1.4854 0.0146  -0.0672 -0.0733 208  LYS   E CG  
12934 C  CD  . LYS   E 208 ? 1.7609 1.4777 1.4593 0.0115  -0.0724 -0.0738 208  LYS   E CD  
12935 C  CE  . LYS   E 208 ? 1.7616 1.4610 1.4442 0.0100  -0.0784 -0.0757 208  LYS   E CE  
12936 N  NZ  . LYS   E 208 ? 1.7927 1.4818 1.4707 0.0080  -0.0826 -0.0765 208  LYS   E NZ  
12937 N  N   . GLN   E 209 ? 2.0448 1.7959 1.7619 0.0197  -0.0545 -0.0710 209  GLN   E N   
12938 C  CA  . GLN   E 209 ? 2.0592 1.8180 1.7819 0.0255  -0.0468 -0.0711 209  GLN   E CA  
12939 C  C   . GLN   E 209 ? 2.0540 1.8233 1.7905 0.0250  -0.0461 -0.0704 209  GLN   E C   
12940 O  O   . GLN   E 209 ? 2.0347 1.8149 1.7839 0.0204  -0.0480 -0.0687 209  GLN   E O   
12941 C  CB  . GLN   E 209 ? 2.0883 1.8568 1.8172 0.0263  -0.0421 -0.0699 209  GLN   E CB  
12942 C  CG  . GLN   E 209 ? 2.0828 1.8632 1.8231 0.0309  -0.0345 -0.0696 209  GLN   E CG  
12943 C  CD  . GLN   E 209 ? 2.1074 1.8795 1.8381 0.0380  -0.0292 -0.0715 209  GLN   E CD  
12944 O  OE1 . GLN   E 209 ? 2.1210 1.8932 1.8540 0.0410  -0.0282 -0.0726 209  GLN   E OE1 
12945 N  NE2 . GLN   E 209 ? 2.0653 1.8302 1.7852 0.0411  -0.0257 -0.0719 209  GLN   E NE2 
12946 N  N   . GLU   E 210 ? 2.0672 1.8328 1.8008 0.0299  -0.0434 -0.0719 210  GLU   E N   
12947 C  CA  . GLU   E 210 ? 2.0920 1.8634 1.8350 0.0296  -0.0442 -0.0716 210  GLU   E CA  
12948 C  C   . GLU   E 210 ? 2.0290 1.8178 1.7894 0.0301  -0.0405 -0.0702 210  GLU   E C   
12949 O  O   . GLU   E 210 ? 1.9865 1.7822 1.7566 0.0277  -0.0425 -0.0692 210  GLU   E O   
12950 C  CB  . GLU   E 210 ? 2.1082 1.8704 1.8427 0.0354  -0.0424 -0.0736 210  GLU   E CB  
12951 C  CG  . GLU   E 210 ? 2.1143 1.8582 1.8298 0.0365  -0.0449 -0.0754 210  GLU   E CG  
12952 C  CD  . GLU   E 210 ? 2.0804 1.8148 1.7902 0.0313  -0.0520 -0.0753 210  GLU   E CD  
12953 O  OE1 . GLU   E 210 ? 2.0350 1.7764 1.7551 0.0275  -0.0543 -0.0739 210  GLU   E OE1 
12954 O  OE2 . GLU   E 210 ? 2.1412 1.8609 1.8362 0.0310  -0.0552 -0.0766 210  GLU   E OE2 
12955 N  N   . ASN   E 211 ? 1.9315 1.7271 1.6961 0.0332  -0.0350 -0.0702 211  ASN   E N   
12956 C  CA  . ASN   E 211 ? 1.8683 1.6799 1.6496 0.0344  -0.0313 -0.0694 211  ASN   E CA  
12957 C  C   . ASN   E 211 ? 1.8228 1.6407 1.6075 0.0357  -0.0263 -0.0688 211  ASN   E C   
12958 O  O   . ASN   E 211 ? 1.8534 1.6658 1.6309 0.0405  -0.0217 -0.0700 211  ASN   E O   
12959 C  CB  . ASN   E 211 ? 1.8533 1.6663 1.6379 0.0402  -0.0283 -0.0709 211  ASN   E CB  
12960 C  CG  . ASN   E 211 ? 1.8831 1.7069 1.6813 0.0390  -0.0299 -0.0701 211  ASN   E CG  
12961 O  OD1 . ASN   E 211 ? 1.9409 1.7706 1.7457 0.0337  -0.0331 -0.0683 211  ASN   E OD1 
12962 N  ND2 . ASN   E 211 ? 1.8812 1.7073 1.6836 0.0442  -0.0278 -0.0715 211  ASN   E ND2 
12963 N  N   . VAL   E 212 ? 1.8001 1.6290 1.5957 0.0316  -0.0269 -0.0669 212  VAL   E N   
12964 C  CA  . VAL   E 212 ? 1.7149 1.5499 1.5142 0.0319  -0.0226 -0.0660 212  VAL   E CA  
12965 C  C   . VAL   E 212 ? 1.6407 1.4926 1.4588 0.0314  -0.0204 -0.0649 212  VAL   E C   
12966 O  O   . VAL   E 212 ? 1.6566 1.5141 1.4830 0.0310  -0.0225 -0.0650 212  VAL   E O   
12967 C  CB  . VAL   E 212 ? 1.6197 1.4491 1.4109 0.0270  -0.0265 -0.0649 212  VAL   E CB  
12968 C  CG1 . VAL   E 212 ? 1.6159 1.4540 1.4173 0.0208  -0.0312 -0.0630 212  VAL   E CG1 
12969 C  CG2 . VAL   E 212 ? 1.5852 1.4134 1.3718 0.0292  -0.0215 -0.0645 212  VAL   E CG2 
12970 N  N   . GLU   E 213 ? 1.5785 1.4378 1.4027 0.0319  -0.0159 -0.0640 213  GLU   E N   
12971 C  CA  . GLU   E 213 ? 1.5395 1.4143 1.3814 0.0322  -0.0130 -0.0633 213  GLU   E CA  
12972 C  C   . GLU   E 213 ? 1.5311 1.4135 1.3823 0.0275  -0.0183 -0.0621 213  GLU   E C   
12973 O  O   . GLU   E 213 ? 1.5311 1.4099 1.3776 0.0226  -0.0232 -0.0610 213  GLU   E O   
12974 C  CB  . GLU   E 213 ? 1.5658 1.4461 1.4115 0.0316  -0.0086 -0.0620 213  GLU   E CB  
12975 C  CG  . GLU   E 213 ? 1.5407 1.4371 1.4049 0.0304  -0.0068 -0.0610 213  GLU   E CG  
12976 C  CD  . GLU   E 213 ? 1.5598 1.4613 1.4285 0.0318  -0.0003 -0.0602 213  GLU   E CD  
12977 O  OE1 . GLU   E 213 ? 1.5736 1.4664 1.4304 0.0319  0.0015  -0.0597 213  GLU   E OE1 
12978 O  OE2 . GLU   E 213 ? 1.5592 1.4728 1.4432 0.0330  0.0029  -0.0601 213  GLU   E OE2 
12979 N  N   . ALA   E 214 ? 1.6213 1.5137 1.4855 0.0294  -0.0174 -0.0625 214  ALA   E N   
12980 C  CA  . ALA   E 214 ? 1.6401 1.5392 1.5127 0.0259  -0.0220 -0.0615 214  ALA   E CA  
12981 C  C   . ALA   E 214 ? 1.6233 1.5307 1.5031 0.0209  -0.0232 -0.0593 214  ALA   E C   
12982 O  O   . ALA   E 214 ? 1.6120 1.5224 1.4956 0.0171  -0.0274 -0.0581 214  ALA   E O   
12983 C  CB  . ALA   E 214 ? 1.6726 1.5801 1.5569 0.0298  -0.0207 -0.0626 214  ALA   E CB  
12984 N  N   . GLU   E 215 ? 1.6023 1.5132 1.4841 0.0211  -0.0193 -0.0587 215  GLU   E N   
12985 C  CA  . GLU   E 215 ? 1.6134 1.5308 1.5004 0.0166  -0.0203 -0.0567 215  GLU   E CA  
12986 C  C   . GLU   E 215 ? 1.6112 1.5194 1.4856 0.0146  -0.0209 -0.0561 215  GLU   E C   
12987 O  O   . GLU   E 215 ? 1.6016 1.5134 1.4780 0.0133  -0.0188 -0.0549 215  GLU   E O   
12988 C  CB  . GLU   E 215 ? 1.6790 1.6089 1.5799 0.0181  -0.0157 -0.0564 215  GLU   E CB  
12989 C  CG  . GLU   E 215 ? 1.6923 1.6313 1.6061 0.0206  -0.0155 -0.0573 215  GLU   E CG  
12990 C  CD  . GLU   E 215 ? 1.6835 1.6272 1.6028 0.0169  -0.0208 -0.0562 215  GLU   E CD  
12991 O  OE1 . GLU   E 215 ? 1.7074 1.6499 1.6235 0.0121  -0.0240 -0.0544 215  GLU   E OE1 
12992 O  OE2 . GLU   E 215 ? 1.6839 1.6324 1.6107 0.0191  -0.0217 -0.0571 215  GLU   E OE2 
12993 N  N   . ALA   E 216 ? 1.5823 1.4779 1.4431 0.0145  -0.0238 -0.0570 216  ALA   E N   
12994 C  CA  . ALA   E 216 ? 1.4760 1.3618 1.3243 0.0117  -0.0266 -0.0565 216  ALA   E CA  
12995 C  C   . ALA   E 216 ? 1.4592 1.3499 1.3127 0.0057  -0.0317 -0.0547 216  ALA   E C   
12996 O  O   . ALA   E 216 ? 1.4816 1.3750 1.3402 0.0031  -0.0356 -0.0542 216  ALA   E O   
12997 C  CB  . ALA   E 216 ? 1.5084 1.3799 1.3424 0.0127  -0.0295 -0.0580 216  ALA   E CB  
12998 N  N   . SER   E 217 ? 1.4316 1.3231 1.2835 0.0037  -0.0317 -0.0535 217  SER   E N   
12999 C  CA  . SER   E 217 ? 1.4286 1.3264 1.2872 -0.0017 -0.0359 -0.0517 217  SER   E CA  
13000 C  C   . SER   E 217 ? 1.4289 1.3194 1.2779 -0.0045 -0.0394 -0.0512 217  SER   E C   
13001 O  O   . SER   E 217 ? 1.4843 1.3780 1.3376 -0.0092 -0.0442 -0.0500 217  SER   E O   
13002 C  CB  . SER   E 217 ? 1.5327 1.4447 1.4058 -0.0016 -0.0323 -0.0504 217  SER   E CB  
13003 O  OG  . SER   E 217 ? 1.4604 1.3731 1.3326 0.0023  -0.0260 -0.0508 217  SER   E OG  
13004 N  N   . MET   E 218 ? 1.3848 1.2653 1.2209 -0.0017 -0.0374 -0.0521 218  MET   E N   
13005 C  CA  . MET   E 218 ? 1.3236 1.1977 1.1508 -0.0037 -0.0403 -0.0516 218  MET   E CA  
13006 C  C   . MET   E 218 ? 1.3992 1.2568 1.2084 -0.0019 -0.0426 -0.0534 218  MET   E C   
13007 O  O   . MET   E 218 ? 1.4265 1.2778 1.2284 0.0028  -0.0382 -0.0547 218  MET   E O   
13008 C  CB  . MET   E 218 ? 1.3440 1.2230 1.1734 -0.0016 -0.0345 -0.0506 218  MET   E CB  
13009 C  CG  . MET   E 218 ? 1.4189 1.2948 1.2426 -0.0040 -0.0374 -0.0496 218  MET   E CG  
13010 S  SD  . MET   E 218 ? 1.4292 1.3098 1.2548 -0.0009 -0.0292 -0.0484 218  MET   E SD  
13011 C  CE  . MET   E 218 ? 1.3689 1.2690 1.2171 -0.0037 -0.0280 -0.0467 218  MET   E CE  
13012 N  N   . VAL   E 219 ? 1.4292 1.2797 1.2317 -0.0056 -0.0496 -0.0535 219  VAL   E N   
13013 C  CA  . VAL   E 219 ? 1.3913 1.2253 1.1764 -0.0044 -0.0532 -0.0553 219  VAL   E CA  
13014 C  C   . VAL   E 219 ? 1.4081 1.2356 1.1834 -0.0048 -0.0554 -0.0551 219  VAL   E C   
13015 O  O   . VAL   E 219 ? 1.4034 1.2355 1.1842 -0.0091 -0.0601 -0.0540 219  VAL   E O   
13016 C  CB  . VAL   E 219 ? 1.3881 1.2173 1.1726 -0.0084 -0.0605 -0.0561 219  VAL   E CB  
13017 C  CG1 . VAL   E 219 ? 1.4505 1.2624 1.2169 -0.0076 -0.0652 -0.0580 219  VAL   E CG1 
13018 C  CG2 . VAL   E 219 ? 1.4256 1.2581 1.2161 -0.0071 -0.0581 -0.0565 219  VAL   E CG2 
13019 N  N   . ILE   E 220 ? 1.4382 1.2542 1.1984 -0.0001 -0.0521 -0.0562 220  ILE   E N   
13020 C  CA  . ILE   E 220 ? 1.4406 1.2483 1.1889 0.0006  -0.0536 -0.0561 220  ILE   E CA  
13021 C  C   . ILE   E 220 ? 1.5027 1.2920 1.2317 0.0023  -0.0582 -0.0584 220  ILE   E C   
13022 O  O   . ILE   E 220 ? 1.5379 1.3193 1.2582 0.0065  -0.0546 -0.0597 220  ILE   E O   
13023 C  CB  . ILE   E 220 ? 1.4089 1.2188 1.1555 0.0052  -0.0445 -0.0552 220  ILE   E CB  
13024 C  CG1 . ILE   E 220 ? 1.3903 1.2183 1.1564 0.0033  -0.0405 -0.0531 220  ILE   E CG1 
13025 C  CG2 . ILE   E 220 ? 1.4418 1.2412 1.1738 0.0064  -0.0459 -0.0551 220  ILE   E CG2 
13026 C  CD1 . ILE   E 220 ? 1.4080 1.2391 1.1748 0.0076  -0.0310 -0.0521 220  ILE   E CD1 
13027 N  N   . ALA   E 221 ? 1.4729 1.2553 1.1955 -0.0008 -0.0664 -0.0589 221  ALA   E N   
13028 C  CA  . ALA   E 221 ? 1.5050 1.2692 1.2088 0.0007  -0.0718 -0.0612 221  ALA   E CA  
13029 C  C   . ALA   E 221 ? 1.5406 1.2930 1.2268 0.0059  -0.0682 -0.0616 221  ALA   E C   
13030 O  O   . ALA   E 221 ? 1.5663 1.3201 1.2515 0.0053  -0.0690 -0.0605 221  ALA   E O   
13031 C  CB  . ALA   E 221 ? 1.4911 1.2529 1.1965 -0.0050 -0.0826 -0.0618 221  ALA   E CB  
13032 N  N   . VAL   E 222 ? 1.5945 1.3351 1.2666 0.0113  -0.0639 -0.0630 222  VAL   E N   
13033 C  CA  . VAL   E 222 ? 1.6298 1.3577 1.2836 0.0169  -0.0598 -0.0633 222  VAL   E CA  
13034 C  C   . VAL   E 222 ? 1.6508 1.3623 1.2873 0.0162  -0.0694 -0.0651 222  VAL   E C   
13035 O  O   . VAL   E 222 ? 1.6289 1.3327 1.2612 0.0143  -0.0767 -0.0671 222  VAL   E O   
13036 C  CB  . VAL   E 222 ? 1.6564 1.3774 1.3013 0.0231  -0.0517 -0.0641 222  VAL   E CB  
13037 C  CG1 . VAL   E 222 ? 1.6637 1.3755 1.2939 0.0290  -0.0444 -0.0636 222  VAL   E CG1 
13038 C  CG2 . VAL   E 222 ? 1.6343 1.3716 1.2982 0.0228  -0.0448 -0.0629 222  VAL   E CG2 
13039 N  N   . PRO   E 223 ? 1.6778 1.3833 1.3043 0.0177  -0.0700 -0.0646 223  PRO   E N   
13040 C  CA  . PRO   E 223 ? 1.6851 1.3758 1.2965 0.0169  -0.0803 -0.0664 223  PRO   E CA  
13041 C  C   . PRO   E 223 ? 1.7608 1.4306 1.3494 0.0217  -0.0817 -0.0691 223  PRO   E C   
13042 O  O   . PRO   E 223 ? 1.7515 1.4173 1.3343 0.0264  -0.0741 -0.0693 223  PRO   E O   
13043 C  CB  . PRO   E 223 ? 1.6609 1.3506 1.2668 0.0185  -0.0785 -0.0649 223  PRO   E CB  
13044 C  CG  . PRO   E 223 ? 1.6765 1.3838 1.2996 0.0180  -0.0692 -0.0621 223  PRO   E CG  
13045 C  CD  . PRO   E 223 ? 1.6822 1.3954 1.3128 0.0197  -0.0619 -0.0622 223  PRO   E CD  
13046 N  N   . GLU   E 224 ? 1.7449 1.4011 1.3204 0.0208  -0.0921 -0.0711 224  GLU   E N   
13047 C  CA  . GLU   E 224 ? 1.7452 1.3809 1.2999 0.0237  -0.0976 -0.0741 224  GLU   E CA  
13048 C  C   . GLU   E 224 ? 1.8180 1.4404 1.3538 0.0317  -0.0887 -0.0746 224  GLU   E C   
13049 O  O   . GLU   E 224 ? 1.8398 1.4506 1.3649 0.0340  -0.0902 -0.0767 224  GLU   E O   
13050 C  CB  . GLU   E 224 ? 1.8100 1.4336 1.3526 0.0226  -0.1087 -0.0757 224  GLU   E CB  
13051 C  CG  . GLU   E 224 ? 1.8809 1.5058 1.4324 0.0161  -0.1210 -0.0775 224  GLU   E CG  
13052 C  CD  . GLU   E 224 ? 2.0196 1.6284 1.5573 0.0177  -0.1258 -0.0806 224  GLU   E CD  
13053 O  OE1 . GLU   E 224 ? 2.0252 1.6393 1.5710 0.0169  -0.1219 -0.0805 224  GLU   E OE1 
13054 O  OE2 . GLU   E 224 ? 2.0297 1.6200 1.5481 0.0199  -0.1336 -0.0832 224  GLU   E OE2 
13055 N  N   . PRO   E 225 ? 1.8806 1.5035 1.4113 0.0363  -0.0792 -0.0726 225  PRO   E N   
13056 C  CA  . PRO   E 225 ? 1.8724 1.4845 1.3878 0.0438  -0.0692 -0.0728 225  PRO   E CA  
13057 C  C   . PRO   E 225 ? 1.8026 1.4214 1.3276 0.0444  -0.0637 -0.0731 225  PRO   E C   
13058 O  O   . PRO   E 225 ? 1.7129 1.3183 1.2250 0.0468  -0.0664 -0.0754 225  PRO   E O   
13059 C  CB  . PRO   E 225 ? 1.9130 1.5318 1.4308 0.0466  -0.0589 -0.0699 225  PRO   E CB  
13060 C  CG  . PRO   E 225 ? 1.8872 1.5081 1.4068 0.0427  -0.0668 -0.0693 225  PRO   E CG  
13061 C  CD  . PRO   E 225 ? 1.8771 1.5064 1.4116 0.0354  -0.0781 -0.0705 225  PRO   E CD  
13062 N  N   . PHE   E 226 ? 1.8670 1.5058 1.4141 0.0423  -0.0566 -0.0709 226  PHE   E N   
13063 C  CA  . PHE   E 226 ? 1.7950 1.4404 1.3511 0.0437  -0.0504 -0.0710 226  PHE   E CA  
13064 C  C   . PHE   E 226 ? 1.7791 1.4287 1.3454 0.0383  -0.0589 -0.0725 226  PHE   E C   
13065 O  O   . PHE   E 226 ? 1.7683 1.4099 1.3279 0.0404  -0.0593 -0.0743 226  PHE   E O   
13066 C  CB  . PHE   E 226 ? 1.7790 1.4440 1.3553 0.0435  -0.0401 -0.0683 226  PHE   E CB  
13067 C  CG  . PHE   E 226 ? 1.8007 1.4645 1.3712 0.0480  -0.0307 -0.0664 226  PHE   E CG  
13068 C  CD1 . PHE   E 226 ? 1.8657 1.5348 1.4401 0.0453  -0.0323 -0.0647 226  PHE   E CD1 
13069 C  CD2 . PHE   E 226 ? 1.8074 1.4658 1.3702 0.0547  -0.0198 -0.0662 226  PHE   E CD2 
13070 C  CE1 . PHE   E 226 ? 1.8389 1.5068 1.4082 0.0493  -0.0234 -0.0627 226  PHE   E CE1 
13071 C  CE2 . PHE   E 226 ? 1.8744 1.5318 1.4327 0.0587  -0.0105 -0.0642 226  PHE   E CE2 
13072 C  CZ  . PHE   E 226 ? 1.8621 1.5240 1.4234 0.0559  -0.0123 -0.0624 226  PHE   E CZ  
13073 N  N   . GLY   E 227 ? 1.7809 1.4436 1.3640 0.0314  -0.0651 -0.0715 227  GLY   E N   
13074 C  CA  . GLY   E 227 ? 1.7430 1.4118 1.3384 0.0259  -0.0722 -0.0723 227  GLY   E CA  
13075 C  C   . GLY   E 227 ? 1.7099 1.3962 1.3255 0.0247  -0.0656 -0.0708 227  GLY   E C   
13076 O  O   . GLY   E 227 ? 1.6996 1.3923 1.3191 0.0288  -0.0556 -0.0696 227  GLY   E O   
13077 N  N   . GLY   E 228 ? 1.7214 1.4154 1.3503 0.0192  -0.0714 -0.0709 228  GLY   E N   
13078 C  CA  . GLY   E 228 ? 1.7346 1.4430 1.3805 0.0186  -0.0659 -0.0699 228  GLY   E CA  
13079 C  C   . GLY   E 228 ? 1.7204 1.4481 1.3863 0.0151  -0.0632 -0.0673 228  GLY   E C   
13080 O  O   . GLY   E 228 ? 1.7168 1.4474 1.3850 0.0120  -0.0672 -0.0663 228  GLY   E O   
13081 N  N   . ALA   E 229 ? 1.6752 1.4159 1.3555 0.0160  -0.0567 -0.0662 229  ALA   E N   
13082 C  CA  . ALA   E 229 ? 1.6152 1.3746 1.3152 0.0129  -0.0541 -0.0639 229  ALA   E CA  
13083 C  C   . ALA   E 229 ? 1.6148 1.3831 1.3222 0.0174  -0.0437 -0.0630 229  ALA   E C   
13084 O  O   . ALA   E 229 ? 1.5917 1.3559 1.2952 0.0216  -0.0394 -0.0642 229  ALA   E O   
13085 C  CB  . ALA   E 229 ? 1.5669 1.3357 1.2818 0.0071  -0.0595 -0.0634 229  ALA   E CB  
13086 N  N   . ILE   E 230 ? 1.5806 1.3611 1.2992 0.0165  -0.0397 -0.0610 230  ILE   E N   
13087 C  CA  . ILE   E 230 ? 1.5665 1.3585 1.2965 0.0197  -0.0304 -0.0600 230  ILE   E CA  
13088 C  C   . ILE   E 230 ? 1.5572 1.3658 1.3078 0.0158  -0.0316 -0.0589 230  ILE   E C   
13089 O  O   . ILE   E 230 ? 1.4813 1.2967 1.2398 0.0106  -0.0367 -0.0577 230  ILE   E O   
13090 C  CB  . ILE   E 230 ? 1.4881 1.2822 1.2168 0.0215  -0.0247 -0.0584 230  ILE   E CB  
13091 C  CG1 . ILE   E 230 ? 1.5738 1.3504 1.2808 0.0241  -0.0261 -0.0592 230  ILE   E CG1 
13092 C  CG2 . ILE   E 230 ? 1.4738 1.2746 1.2094 0.0263  -0.0143 -0.0579 230  ILE   E CG2 
13093 C  CD1 . ILE   E 230 ? 1.5485 1.3251 1.2520 0.0265  -0.0198 -0.0576 230  ILE   E CD1 
13094 N  N   . ILE   E 231 ? 1.5969 1.4117 1.3558 0.0184  -0.0271 -0.0593 231  ILE   E N   
13095 C  CA  . ILE   E 231 ? 1.5619 1.3914 1.3392 0.0157  -0.0277 -0.0585 231  ILE   E CA  
13096 C  C   . ILE   E 231 ? 1.5395 1.3815 1.3294 0.0183  -0.0198 -0.0575 231  ILE   E C   
13097 O  O   . ILE   E 231 ? 1.5444 1.3862 1.3346 0.0232  -0.0135 -0.0584 231  ILE   E O   
13098 C  CB  . ILE   E 231 ? 1.5629 1.3895 1.3402 0.0167  -0.0295 -0.0600 231  ILE   E CB  
13099 C  CG1 . ILE   E 231 ? 1.5318 1.3448 1.2959 0.0143  -0.0370 -0.0612 231  ILE   E CG1 
13100 C  CG2 . ILE   E 231 ? 1.5157 1.3562 1.3104 0.0138  -0.0309 -0.0591 231  ILE   E CG2 
13101 C  CD1 . ILE   E 231 ? 1.4896 1.3066 1.2596 0.0078  -0.0441 -0.0600 231  ILE   E CD1 
13102 N  N   . ILE   E 232 ? 1.5492 1.4020 1.3500 0.0150  -0.0200 -0.0557 232  ILE   E N   
13103 C  CA  . ILE   E 232 ? 1.5048 1.3701 1.3190 0.0167  -0.0131 -0.0546 232  ILE   E CA  
13104 C  C   . ILE   E 232 ? 1.4109 1.2893 1.2422 0.0152  -0.0141 -0.0545 232  ILE   E C   
13105 O  O   . ILE   E 232 ? 1.3869 1.2702 1.2242 0.0106  -0.0199 -0.0537 232  ILE   E O   
13106 C  CB  . ILE   E 232 ? 1.4421 1.3117 1.2586 0.0143  -0.0125 -0.0527 232  ILE   E CB  
13107 C  CG1 . ILE   E 232 ? 1.4175 1.2729 1.2157 0.0159  -0.0121 -0.0529 232  ILE   E CG1 
13108 C  CG2 . ILE   E 232 ? 1.4087 1.2903 1.2388 0.0162  -0.0050 -0.0518 232  ILE   E CG2 
13109 C  CD1 . ILE   E 232 ? 1.3281 1.1867 1.1274 0.0140  -0.0114 -0.0510 232  ILE   E CD1 
13110 N  N   . GLY   E 233 ? 1.3990 1.2828 1.2379 0.0193  -0.0086 -0.0553 233  GLY   E N   
13111 C  CA  . GLY   E 233 ? 1.4886 1.3839 1.3427 0.0186  -0.0097 -0.0554 233  GLY   E CA  
13112 C  C   . GLY   E 233 ? 1.4891 1.3986 1.3595 0.0189  -0.0053 -0.0545 233  GLY   E C   
13113 O  O   . GLY   E 233 ? 1.4616 1.3757 1.3354 0.0164  -0.0047 -0.0528 233  GLY   E O   
13114 N  N   . GLN   E 234 ? 1.5074 1.4239 1.3884 0.0220  -0.0025 -0.0556 234  GLN   E N   
13115 C  CA  . GLN   E 234 ? 1.5228 1.4528 1.4204 0.0228  0.0017  -0.0551 234  GLN   E CA  
13116 C  C   . GLN   E 234 ? 1.5165 1.4452 1.4132 0.0268  0.0098  -0.0553 234  GLN   E C   
13117 O  O   . GLN   E 234 ? 1.5210 1.4528 1.4201 0.0257  0.0132  -0.0538 234  GLN   E O   
13118 C  CB  . GLN   E 234 ? 1.5523 1.4899 1.4617 0.0245  0.0002  -0.0564 234  GLN   E CB  
13119 C  CG  . GLN   E 234 ? 1.5748 1.5263 1.5022 0.0254  0.0034  -0.0563 234  GLN   E CG  
13120 C  CD  . GLN   E 234 ? 1.5942 1.5540 1.5292 0.0207  0.0008  -0.0544 234  GLN   E CD  
13121 O  OE1 . GLN   E 234 ? 1.6052 1.5693 1.5447 0.0200  0.0046  -0.0532 234  GLN   E OE1 
13122 N  NE2 . GLN   E 234 ? 1.5751 1.5369 1.5119 0.0176  -0.0055 -0.0539 234  GLN   E NE2 
13123 N  N   . GLU   E 235 ? 1.5101 1.4332 1.4026 0.0317  0.0132  -0.0570 235  GLU   E N   
13124 C  CA  . GLU   E 235 ? 1.5487 1.4712 1.4422 0.0363  0.0218  -0.0574 235  GLU   E CA  
13125 C  C   . GLU   E 235 ? 1.5202 1.4271 1.3946 0.0393  0.0241  -0.0580 235  GLU   E C   
13126 O  O   . GLU   E 235 ? 1.5300 1.4346 1.4033 0.0437  0.0317  -0.0584 235  GLU   E O   
13127 C  CB  . GLU   E 235 ? 1.5090 1.4405 1.4173 0.0401  0.0247  -0.0591 235  GLU   E CB  
13128 N  N   . SER   E 236 ? 1.5383 1.4344 1.3978 0.0371  0.0178  -0.0582 236  SER   E N   
13129 C  CA  . SER   E 236 ? 1.5752 1.4555 1.4157 0.0401  0.0189  -0.0592 236  SER   E CA  
13130 C  C   . SER   E 236 ? 1.5322 1.4022 1.3578 0.0362  0.0124  -0.0584 236  SER   E C   
13131 O  O   . SER   E 236 ? 1.4994 1.3699 1.3255 0.0322  0.0049  -0.0585 236  SER   E O   
13132 C  CB  . SER   E 236 ? 1.5898 1.4661 1.4282 0.0435  0.0176  -0.0613 236  SER   E CB  
13133 O  OG  . SER   E 236 ? 1.5002 1.3729 1.3341 0.0399  0.0091  -0.0617 236  SER   E OG  
13134 N  N   . ILE   E 237 ? 1.5255 1.3856 1.3376 0.0375  0.0155  -0.0578 237  ILE   E N   
13135 C  CA  . ILE   E 237 ? 1.5836 1.4312 1.3789 0.0349  0.0096  -0.0576 237  ILE   E CA  
13136 C  C   . ILE   E 237 ? 1.6319 1.4637 1.4096 0.0386  0.0091  -0.0595 237  ILE   E C   
13137 O  O   . ILE   E 237 ? 1.6295 1.4559 1.4016 0.0440  0.0162  -0.0602 237  ILE   E O   
13138 C  CB  . ILE   E 237 ? 1.5255 1.3706 1.3153 0.0344  0.0128  -0.0559 237  ILE   E CB  
13139 C  CG1 . ILE   E 237 ? 1.5087 1.3699 1.3167 0.0315  0.0146  -0.0541 237  ILE   E CG1 
13140 C  CG2 . ILE   E 237 ? 1.4904 1.3240 1.2647 0.0313  0.0055  -0.0557 237  ILE   E CG2 
13141 C  CD1 . ILE   E 237 ? 1.4886 1.3509 1.2974 0.0342  0.0234  -0.0527 237  ILE   E CD1 
13142 N  N   . THR   E 238 ? 1.7481 1.5724 1.5176 0.0357  0.0008  -0.0604 238  THR   E N   
13143 C  CA  . THR   E 238 ? 1.7444 1.5538 1.4979 0.0386  -0.0010 -0.0623 238  THR   E CA  
13144 C  C   . THR   E 238 ? 1.7746 1.5706 1.5117 0.0357  -0.0083 -0.0626 238  THR   E C   
13145 O  O   . THR   E 238 ? 1.7803 1.5803 1.5221 0.0301  -0.0153 -0.0618 238  THR   E O   
13146 C  CB  . THR   E 238 ? 1.7714 1.5842 1.5320 0.0385  -0.0040 -0.0636 238  THR   E CB  
13147 O  OG1 . THR   E 238 ? 1.7872 1.6096 1.5594 0.0327  -0.0104 -0.0627 238  THR   E OG1 
13148 C  CG2 . THR   E 238 ? 1.7429 1.5652 1.5159 0.0430  0.0034  -0.0640 238  THR   E CG2 
13149 N  N   . TYR   E 239 ? 1.7004 1.4805 1.4185 0.0397  -0.0067 -0.0637 239  TYR   E N   
13150 C  CA  . TYR   E 239 ? 1.6888 1.4540 1.3894 0.0379  -0.0140 -0.0644 239  TYR   E CA  
13151 C  C   . TYR   E 239 ? 1.7657 1.5194 1.4561 0.0388  -0.0187 -0.0666 239  TYR   E C   
13152 O  O   . TYR   E 239 ? 1.8027 1.5523 1.4893 0.0438  -0.0138 -0.0678 239  TYR   E O   
13153 C  CB  . TYR   E 239 ? 1.6573 1.4105 1.3413 0.0419  -0.0095 -0.0643 239  TYR   E CB  
13154 C  CG  . TYR   E 239 ? 1.6735 1.4087 1.3368 0.0414  -0.0168 -0.0656 239  TYR   E CG  
13155 C  CD1 . TYR   E 239 ? 1.7144 1.4490 1.3766 0.0363  -0.0246 -0.0650 239  TYR   E CD1 
13156 C  CD2 . TYR   E 239 ? 1.6840 1.4025 1.3289 0.0462  -0.0162 -0.0676 239  TYR   E CD2 
13157 C  CE1 . TYR   E 239 ? 1.6942 1.4124 1.3380 0.0359  -0.0320 -0.0665 239  TYR   E CE1 
13158 C  CE2 . TYR   E 239 ? 1.7029 1.4042 1.3284 0.0458  -0.0235 -0.0690 239  TYR   E CE2 
13159 C  CZ  . TYR   E 239 ? 1.6721 1.3735 1.2975 0.0406  -0.0316 -0.0685 239  TYR   E CZ  
13160 O  OH  . TYR   E 239 ? 1.7189 1.4037 1.3263 0.0401  -0.0396 -0.0701 239  TYR   E OH  
13161 N  N   . HIS   E 240 ? 1.7654 1.5138 1.4517 0.0339  -0.0282 -0.0672 240  HIS   E N   
13162 C  CA  . HIS   E 240 ? 1.7545 1.4915 1.4312 0.0340  -0.0335 -0.0692 240  HIS   E CA  
13163 C  C   . HIS   E 240 ? 1.7810 1.5029 1.4414 0.0318  -0.0415 -0.0703 240  HIS   E C   
13164 O  O   . HIS   E 240 ? 1.7455 1.4707 1.4087 0.0276  -0.0458 -0.0692 240  HIS   E O   
13165 C  CB  . HIS   E 240 ? 1.7533 1.5001 1.4448 0.0297  -0.0378 -0.0690 240  HIS   E CB  
13166 C  CG  . HIS   E 240 ? 1.7561 1.5196 1.4660 0.0307  -0.0316 -0.0679 240  HIS   E CG  
13167 N  ND1 . HIS   E 240 ? 1.7890 1.5540 1.5023 0.0344  -0.0280 -0.0689 240  HIS   E ND1 
13168 C  CD2 . HIS   E 240 ? 1.7441 1.5234 1.4702 0.0285  -0.0291 -0.0659 240  HIS   E CD2 
13169 C  CE1 . HIS   E 240 ? 1.7905 1.5714 1.5213 0.0345  -0.0237 -0.0677 240  HIS   E CE1 
13170 N  NE2 . HIS   E 240 ? 1.7414 1.5311 1.4802 0.0309  -0.0242 -0.0659 240  HIS   E NE2 
13171 N  N   . ASN   E 241 ? 1.8795 1.5848 1.5227 0.0349  -0.0436 -0.0724 241  ASN   E N   
13172 C  CA  . ASN   E 241 ? 1.9181 1.6077 1.5454 0.0329  -0.0524 -0.0739 241  ASN   E CA  
13173 C  C   . ASN   E 241 ? 2.0040 1.6778 1.6164 0.0359  -0.0547 -0.0764 241  ASN   E C   
13174 O  O   . ASN   E 241 ? 2.0429 1.7025 1.6374 0.0416  -0.0518 -0.0777 241  ASN   E O   
13175 C  CB  . ASN   E 241 ? 1.8464 1.5277 1.4602 0.0354  -0.0511 -0.0737 241  ASN   E CB  
13176 C  CG  . ASN   E 241 ? 1.8364 1.5052 1.4382 0.0320  -0.0617 -0.0750 241  ASN   E CG  
13177 O  OD1 . ASN   E 241 ? 1.8144 1.4823 1.4201 0.0270  -0.0701 -0.0758 241  ASN   E OD1 
13178 N  ND2 . ASN   E 241 ? 1.8259 1.4847 1.4131 0.0348  -0.0613 -0.0751 241  ASN   E ND2 
13179 N  N   . GLY   E 242 ? 2.2371 1.9122 1.8559 0.0323  -0.0599 -0.0771 242  GLY   E N   
13180 C  CA  . GLY   E 242 ? 2.2983 1.9588 1.9039 0.0352  -0.0618 -0.0794 242  GLY   E CA  
13181 C  C   . GLY   E 242 ? 2.3753 2.0379 1.9813 0.0417  -0.0525 -0.0796 242  GLY   E C   
13182 O  O   . GLY   E 242 ? 2.3776 2.0558 2.0007 0.0415  -0.0477 -0.0783 242  GLY   E O   
13183 N  N   . ASP   E 243 ? 2.2901 1.9369 1.8774 0.0478  -0.0499 -0.0814 243  ASP   E N   
13184 C  CA  . ASP   E 243 ? 2.3049 1.9530 1.8919 0.0546  -0.0405 -0.0817 243  ASP   E CA  
13185 C  C   . ASP   E 243 ? 2.2957 1.9569 1.8929 0.0571  -0.0313 -0.0797 243  ASP   E C   
13186 O  O   . ASP   E 243 ? 2.3459 2.0174 1.9543 0.0603  -0.0239 -0.0792 243  ASP   E O   
13187 C  CB  . ASP   E 243 ? 2.3480 1.9756 1.9116 0.0608  -0.0396 -0.0840 243  ASP   E CB  
13188 N  N   . LYS   E 244 ? 2.2272 1.8882 1.8213 0.0555  -0.0319 -0.0786 244  LYS   E N   
13189 C  CA  . LYS   E 244 ? 2.1299 1.8016 1.7320 0.0578  -0.0232 -0.0766 244  LYS   E CA  
13190 C  C   . LYS   E 244 ? 2.0384 1.7320 1.6658 0.0542  -0.0210 -0.0748 244  LYS   E C   
13191 O  O   . LYS   E 244 ? 2.0131 1.7144 1.6511 0.0479  -0.0278 -0.0742 244  LYS   E O   
13192 C  CB  . LYS   E 244 ? 1.9772 1.6432 1.5701 0.0563  -0.0256 -0.0758 244  LYS   E CB  
13193 N  N   . TYR   E 245 ? 1.9696 1.6729 1.6066 0.0584  -0.0113 -0.0739 245  TYR   E N   
13194 C  CA  . TYR   E 245 ? 1.9070 1.6307 1.5676 0.0559  -0.0086 -0.0723 245  TYR   E CA  
13195 C  C   . TYR   E 245 ? 1.9123 1.6435 1.5794 0.0605  0.0023  -0.0712 245  TYR   E C   
13196 O  O   . TYR   E 245 ? 1.9344 1.6617 1.5977 0.0666  0.0090  -0.0721 245  TYR   E O   
13197 C  CB  . TYR   E 245 ? 1.9276 1.6562 1.5973 0.0559  -0.0102 -0.0734 245  TYR   E CB  
13198 C  CG  . TYR   E 245 ? 1.8755 1.6236 1.5677 0.0555  -0.0057 -0.0722 245  TYR   E CG  
13199 C  CD1 . TYR   E 245 ? 1.8324 1.5942 1.5393 0.0502  -0.0078 -0.0703 245  TYR   E CD1 
13200 C  CD2 . TYR   E 245 ? 1.9244 1.6767 1.6230 0.0607  0.0004  -0.0731 245  TYR   E CD2 
13201 C  CE1 . TYR   E 245 ? 1.8470 1.6259 1.5740 0.0499  -0.0041 -0.0694 245  TYR   E CE1 
13202 C  CE2 . TYR   E 245 ? 1.9163 1.6861 1.6357 0.0605  0.0039  -0.0723 245  TYR   E CE2 
13203 C  CZ  . TYR   E 245 ? 1.9146 1.6974 1.6478 0.0550  0.0015  -0.0705 245  TYR   E CZ  
13204 O  OH  . TYR   E 245 ? 1.9462 1.7459 1.6996 0.0548  0.0044  -0.0697 245  TYR   E OH  
13205 N  N   . LEU   E 246 ? 1.8530 1.5948 1.5302 0.0576  0.0041  -0.0691 246  LEU   E N   
13206 C  CA  . LEU   E 246 ? 1.7636 1.5140 1.4492 0.0610  0.0142  -0.0677 246  LEU   E CA  
13207 C  C   . LEU   E 246 ? 1.7964 1.5674 1.5063 0.0570  0.0146  -0.0662 246  LEU   E C   
13208 O  O   . LEU   E 246 ? 1.8079 1.5848 1.5243 0.0511  0.0074  -0.0655 246  LEU   E O   
13209 C  CB  . LEU   E 246 ? 1.7642 1.5053 1.4359 0.0618  0.0163  -0.0666 246  LEU   E CB  
13210 C  CG  . LEU   E 246 ? 1.8009 1.5453 1.4750 0.0658  0.0273  -0.0650 246  LEU   E CG  
13211 C  CD1 . LEU   E 246 ? 1.8144 1.5552 1.4863 0.0729  0.0366  -0.0659 246  LEU   E CD1 
13212 C  CD2 . LEU   E 246 ? 1.7248 1.4565 1.3811 0.0662  0.0271  -0.0640 246  LEU   E CD2 
13213 N  N   . ALA   E 247 ? 1.7631 1.5451 1.4868 0.0605  0.0231  -0.0658 247  ALA   E N   
13214 C  CA  . ALA   E 247 ? 1.7355 1.5367 1.4826 0.0575  0.0238  -0.0648 247  ALA   E CA  
13215 C  C   . ALA   E 247 ? 1.7851 1.5951 1.5427 0.0605  0.0339  -0.0635 247  ALA   E C   
13216 O  O   . ALA   E 247 ? 1.8264 1.6337 1.5826 0.0663  0.0415  -0.0643 247  ALA   E O   
13217 C  CB  . ALA   E 247 ? 1.6314 1.4388 1.3887 0.0584  0.0216  -0.0663 247  ALA   E CB  
13218 N  N   . ILE   E 248 ? 1.7392 1.5599 1.5079 0.0568  0.0344  -0.0616 248  ILE   E N   
13219 C  CA  . ILE   E 248 ? 1.6844 1.5163 1.4675 0.0588  0.0434  -0.0604 248  ILE   E CA  
13220 C  C   . ILE   E 248 ? 1.6456 1.4958 1.4519 0.0557  0.0413  -0.0602 248  ILE   E C   
13221 O  O   . ILE   E 248 ? 1.5943 1.4489 1.4046 0.0508  0.0331  -0.0601 248  ILE   E O   
13222 C  CB  . ILE   E 248 ? 1.6372 1.4666 1.4149 0.0578  0.0473  -0.0582 248  ILE   E CB  
13223 C  CG1 . ILE   E 248 ? 1.6028 1.4303 1.3750 0.0519  0.0384  -0.0573 248  ILE   E CG1 
13224 C  CG2 . ILE   E 248 ? 1.6967 1.5104 1.4555 0.0632  0.0540  -0.0583 248  ILE   E CG2 
13225 C  CD1 . ILE   E 248 ? 1.6001 1.4253 1.3672 0.0510  0.0417  -0.0552 248  ILE   E CD1 
13226 N  N   . ALA   E 249 ? 1.6405 1.5014 1.4625 0.0586  0.0488  -0.0601 249  ALA   E N   
13227 C  CA  . ALA   E 249 ? 1.6352 1.5137 1.4798 0.0560  0.0476  -0.0599 249  ALA   E CA  
13228 C  C   . ALA   E 249 ? 1.6785 1.5654 1.5341 0.0561  0.0553  -0.0581 249  ALA   E C   
13229 O  O   . ALA   E 249 ? 1.6891 1.5853 1.5599 0.0591  0.0616  -0.0586 249  ALA   E O   
13230 C  CB  . ALA   E 249 ? 1.6361 1.5207 1.4918 0.0595  0.0481  -0.0620 249  ALA   E CB  
13231 N  N   . PRO   E 250 ? 1.7365 1.6201 1.5850 0.0530  0.0549  -0.0562 250  PRO   E N   
13232 C  CA  . PRO   E 250 ? 1.7147 1.6044 1.5715 0.0532  0.0627  -0.0543 250  PRO   E CA  
13233 C  C   . PRO   E 250 ? 1.6968 1.6047 1.5783 0.0512  0.0629  -0.0542 250  PRO   E C   
13234 O  O   . PRO   E 250 ? 1.7010 1.6164 1.5902 0.0474  0.0551  -0.0546 250  PRO   E O   
13235 C  CB  . PRO   E 250 ? 1.7371 1.6200 1.5813 0.0494  0.0591  -0.0524 250  PRO   E CB  
13236 C  CG  . PRO   E 250 ? 1.7480 1.6182 1.5743 0.0485  0.0511  -0.0535 250  PRO   E CG  
13237 C  CD  . PRO   E 250 ? 1.7423 1.6177 1.5767 0.0487  0.0466  -0.0555 250  PRO   E CD  
13238 N  N   . PRO   E 251 ? 1.5807 1.4959 1.4751 0.0538  0.0719  -0.0537 251  PRO   E N   
13239 C  CA  . PRO   E 251 ? 1.5756 1.5081 1.4942 0.0521  0.0719  -0.0539 251  PRO   E CA  
13240 C  C   . PRO   E 251 ? 1.5636 1.5032 1.4885 0.0468  0.0691  -0.0519 251  PRO   E C   
13241 O  O   . PRO   E 251 ? 1.5689 1.5214 1.5106 0.0442  0.0652  -0.0523 251  PRO   E O   
13242 C  CB  . PRO   E 251 ? 1.5396 1.4759 1.4689 0.0568  0.0829  -0.0541 251  PRO   E CB  
13243 C  CG  . PRO   E 251 ? 1.5274 1.4489 1.4374 0.0596  0.0896  -0.0529 251  PRO   E CG  
13244 C  CD  . PRO   E 251 ? 1.5500 1.4577 1.4382 0.0591  0.0823  -0.0535 251  PRO   E CD  
13245 N  N   . ILE   E 252 ? 1.5388 1.4699 1.4503 0.0453  0.0708  -0.0499 252  ILE   E N   
13246 C  CA  . ILE   E 252 ? 1.5024 1.4401 1.4199 0.0407  0.0690  -0.0479 252  ILE   E CA  
13247 C  C   . ILE   E 252 ? 1.5518 1.4930 1.4697 0.0359  0.0579  -0.0482 252  ILE   E C   
13248 O  O   . ILE   E 252 ? 1.5566 1.5101 1.4897 0.0327  0.0549  -0.0478 252  ILE   E O   
13249 C  CB  . ILE   E 252 ? 1.4503 1.3767 1.3517 0.0409  0.0736  -0.0457 252  ILE   E CB  
13250 C  CG1 . ILE   E 252 ? 1.5023 1.4331 1.4061 0.0359  0.0700  -0.0437 252  ILE   E CG1 
13251 C  CG2 . ILE   E 252 ? 1.5545 1.4642 1.4324 0.0428  0.0709  -0.0464 252  ILE   E CG2 
13252 C  CD1 . ILE   E 252 ? 1.5521 1.4985 1.4784 0.0341  0.0732  -0.0429 252  ILE   E CD1 
13253 N  N   . ILE   E 253 ? 1.5464 1.4771 1.4482 0.0355  0.0517  -0.0489 253  ILE   E N   
13254 C  CA  . ILE   E 253 ? 1.5853 1.5185 1.4872 0.0310  0.0416  -0.0491 253  ILE   E CA  
13255 C  C   . ILE   E 253 ? 1.6123 1.5557 1.5288 0.0310  0.0377  -0.0507 253  ILE   E C   
13256 O  O   . ILE   E 253 ? 1.6013 1.5482 1.5200 0.0273  0.0300  -0.0507 253  ILE   E O   
13257 C  CB  . ILE   E 253 ? 1.6121 1.5307 1.4933 0.0307  0.0361  -0.0496 253  ILE   E CB  
13258 C  CG1 . ILE   E 253 ? 1.6341 1.5479 1.5119 0.0345  0.0360  -0.0519 253  ILE   E CG1 
13259 C  CG2 . ILE   E 253 ? 1.5677 1.4738 1.4320 0.0319  0.0399  -0.0484 253  ILE   E CG2 
13260 C  CD1 . ILE   E 253 ? 1.6357 1.5391 1.4990 0.0329  0.0281  -0.0528 253  ILE   E CD1 
13261 N  N   . LYS   E 254 ? 1.6524 1.6003 1.5785 0.0351  0.0429  -0.0522 254  LYS   E N   
13262 C  CA  . LYS   E 254 ? 1.6780 1.6352 1.6181 0.0358  0.0395  -0.0540 254  LYS   E CA  
13263 C  C   . LYS   E 254 ? 1.6832 1.6554 1.6431 0.0334  0.0393  -0.0534 254  LYS   E C   
13264 O  O   . LYS   E 254 ? 1.7001 1.6817 1.6756 0.0356  0.0407  -0.0549 254  LYS   E O   
13265 C  CB  . LYS   E 254 ? 1.6156 1.5713 1.5583 0.0415  0.0448  -0.0560 254  LYS   E CB  
13266 N  N   . GLN   E 255 ? 1.5672 1.5417 1.5268 0.0292  0.0374  -0.0514 255  GLN   E N   
13267 C  CA  . GLN   E 255 ? 1.5383 1.5260 1.5153 0.0268  0.0372  -0.0506 255  GLN   E CA  
13268 C  C   . GLN   E 255 ? 1.5861 1.5763 1.5620 0.0216  0.0298  -0.0493 255  GLN   E C   
13269 O  O   . GLN   E 255 ? 1.5542 1.5554 1.5443 0.0196  0.0281  -0.0490 255  GLN   E O   
13270 C  CB  . GLN   E 255 ? 1.4962 1.4862 1.4783 0.0274  0.0456  -0.0492 255  GLN   E CB  
13271 N  N   . SER   E 256 ? 1.5752 1.5557 1.5350 0.0194  0.0253  -0.0485 256  SER   E N   
13272 C  CA  . SER   E 256 ? 1.5068 1.4887 1.4648 0.0149  0.0176  -0.0475 256  SER   E CA  
13273 C  C   . SER   E 256 ? 1.4753 1.4441 1.4151 0.0142  0.0135  -0.0477 256  SER   E C   
13274 O  O   . SER   E 256 ? 1.4599 1.4188 1.3880 0.0171  0.0170  -0.0482 256  SER   E O   
13275 C  CB  . SER   E 256 ? 1.4410 1.4276 1.4028 0.0114  0.0178  -0.0453 256  SER   E CB  
13276 O  OG  . SER   E 256 ? 1.3693 1.3577 1.3301 0.0071  0.0104  -0.0444 256  SER   E OG  
13277 N  N   . THR   E 257 ? 1.4037 1.3725 1.3413 0.0106  0.0062  -0.0473 257  THR   E N   
13278 C  CA  . THR   E 257 ? 1.3540 1.3110 1.2760 0.0096  0.0015  -0.0476 257  THR   E CA  
13279 C  C   . THR   E 257 ? 1.3020 1.2525 1.2132 0.0068  0.0000  -0.0460 257  THR   E C   
13280 O  O   . THR   E 257 ? 1.2593 1.2162 1.1765 0.0038  -0.0012 -0.0444 257  THR   E O   
13281 C  CB  . THR   E 257 ? 1.2780 1.2374 1.2029 0.0070  -0.0055 -0.0479 257  THR   E CB  
13282 O  OG1 . THR   E 257 ? 1.2940 1.2603 1.2253 0.0027  -0.0090 -0.0462 257  THR   E OG1 
13283 C  CG2 . THR   E 257 ? 1.3146 1.2810 1.2508 0.0096  -0.0047 -0.0494 257  THR   E CG2 
13284 N  N   . ILE   E 258 ? 1.3098 1.2471 1.2046 0.0081  -0.0004 -0.0466 258  ILE   E N   
13285 C  CA  . ILE   E 258 ? 1.2531 1.1820 1.1353 0.0058  -0.0033 -0.0455 258  ILE   E CA  
13286 C  C   . ILE   E 258 ? 1.2416 1.1718 1.1247 0.0010  -0.0118 -0.0451 258  ILE   E C   
13287 O  O   . ILE   E 258 ? 1.2525 1.1793 1.1330 0.0004  -0.0160 -0.0462 258  ILE   E O   
13288 C  CB  . ILE   E 258 ? 1.2486 1.1622 1.1127 0.0090  -0.0019 -0.0466 258  ILE   E CB  
13289 C  CG1 . ILE   E 258 ? 1.2626 1.1754 1.1277 0.0143  0.0066  -0.0475 258  ILE   E CG1 
13290 C  CG2 . ILE   E 258 ? 1.3192 1.2240 1.1703 0.0080  -0.0028 -0.0456 258  ILE   E CG2 
13291 C  CD1 . ILE   E 258 ? 1.2590 1.1744 1.1267 0.0159  0.0141  -0.0461 258  ILE   E CD1 
13292 N  N   . VAL   E 259 ? 1.2591 1.1942 1.1461 -0.0025 -0.0142 -0.0434 259  VAL   E N   
13293 C  CA  . VAL   E 259 ? 1.2942 1.2315 1.1836 -0.0071 -0.0217 -0.0428 259  VAL   E CA  
13294 C  C   . VAL   E 259 ? 1.3344 1.2620 1.2110 -0.0094 -0.0265 -0.0424 259  VAL   E C   
13295 O  O   . VAL   E 259 ? 1.3915 1.3163 1.2659 -0.0125 -0.0331 -0.0426 259  VAL   E O   
13296 C  CB  . VAL   E 259 ? 1.2654 1.2167 1.1707 -0.0097 -0.0220 -0.0413 259  VAL   E CB  
13297 C  CG1 . VAL   E 259 ? 1.2489 1.2083 1.1659 -0.0080 -0.0200 -0.0422 259  VAL   E CG1 
13298 C  CG2 . VAL   E 259 ? 1.2330 1.1882 1.1411 -0.0092 -0.0175 -0.0400 259  VAL   E CG2 
13299 N  N   . CYS   E 260 ? 1.2735 1.1954 1.1415 -0.0078 -0.0236 -0.0419 260  CYS   E N   
13300 C  CA  . CYS   E 260 ? 1.3154 1.2274 1.1706 -0.0095 -0.0288 -0.0417 260  CYS   E CA  
13301 C  C   . CYS   E 260 ? 1.3397 1.2378 1.1779 -0.0054 -0.0253 -0.0426 260  CYS   E C   
13302 O  O   . CYS   E 260 ? 1.3116 1.2100 1.1496 -0.0016 -0.0176 -0.0425 260  CYS   E O   
13303 C  CB  . CYS   E 260 ? 1.2992 1.2175 1.1597 -0.0124 -0.0303 -0.0399 260  CYS   E CB  
13304 S  SG  . CYS   E 260 ? 1.2710 1.1971 1.1391 -0.0099 -0.0214 -0.0384 260  CYS   E SG  
13305 N  N   . HIS   E 261 ? 1.3500 1.2359 1.1741 -0.0061 -0.0312 -0.0436 261  HIS   E N   
13306 C  CA  . HIS   E 261 ? 1.3366 1.2072 1.1421 -0.0022 -0.0291 -0.0446 261  HIS   E CA  
13307 C  C   . HIS   E 261 ? 1.3621 1.2242 1.1564 -0.0039 -0.0353 -0.0444 261  HIS   E C   
13308 O  O   . HIS   E 261 ? 1.3462 1.2139 1.1475 -0.0084 -0.0418 -0.0437 261  HIS   E O   
13309 C  CB  . HIS   E 261 ? 1.3467 1.2077 1.1433 -0.0001 -0.0303 -0.0467 261  HIS   E CB  
13310 C  CG  . HIS   E 261 ? 1.3512 1.2058 1.1425 -0.0035 -0.0399 -0.0478 261  HIS   E CG  
13311 N  ND1 . HIS   E 261 ? 1.3547 1.2185 1.1589 -0.0080 -0.0449 -0.0476 261  HIS   E ND1 
13312 C  CD2 . HIS   E 261 ? 1.3062 1.1460 1.0810 -0.0032 -0.0453 -0.0492 261  HIS   E CD2 
13313 C  CE1 . HIS   E 261 ? 1.3481 1.2034 1.1449 -0.0105 -0.0527 -0.0487 261  HIS   E CE1 
13314 N  NE2 . HIS   E 261 ? 1.3199 1.1606 1.0990 -0.0077 -0.0535 -0.0498 261  HIS   E NE2 
13315 N  N   . ASN   E 262 ? 1.3451 1.1932 1.1217 -0.0001 -0.0332 -0.0449 262  ASN   E N   
13316 C  CA  . ASN   E 262 ? 1.3642 1.2015 1.1270 -0.0006 -0.0388 -0.0450 262  ASN   E CA  
13317 C  C   . ASN   E 262 ? 1.4743 1.2942 1.2160 0.0047  -0.0358 -0.0463 262  ASN   E C   
13318 O  O   . ASN   E 262 ? 1.4493 1.2682 1.1889 0.0089  -0.0266 -0.0458 262  ASN   E O   
13319 C  CB  . ASN   E 262 ? 1.3153 1.1593 1.0833 -0.0017 -0.0370 -0.0429 262  ASN   E CB  
13320 C  CG  . ASN   E 262 ? 1.3958 1.2271 1.1475 -0.0011 -0.0420 -0.0431 262  ASN   E CG  
13321 O  OD1 . ASN   E 262 ? 1.4251 1.2480 1.1648 0.0028  -0.0368 -0.0424 262  ASN   E OD1 
13322 N  ND2 . ASN   E 262 ? 1.3686 1.1978 1.1196 -0.0048 -0.0522 -0.0440 262  ASN   E ND2 
13323 N  N   . ARG   E 263 ? 1.5158 1.3218 1.2421 0.0045  -0.0435 -0.0478 263  ARG   E N   
13324 C  CA  . ARG   E 263 ? 1.5633 1.3510 1.2676 0.0097  -0.0417 -0.0492 263  ARG   E CA  
13325 C  C   . ARG   E 263 ? 1.6048 1.3848 1.2970 0.0121  -0.0399 -0.0480 263  ARG   E C   
13326 O  O   . ARG   E 263 ? 1.5623 1.3421 1.2539 0.0092  -0.0471 -0.0477 263  ARG   E O   
13327 C  CB  . ARG   E 263 ? 1.6349 1.4102 1.3276 0.0087  -0.0513 -0.0517 263  ARG   E CB  
13328 C  CG  . ARG   E 263 ? 1.6972 1.4538 1.3678 0.0145  -0.0487 -0.0533 263  ARG   E CG  
13329 C  CD  . ARG   E 263 ? 1.6832 1.4266 1.3414 0.0134  -0.0590 -0.0559 263  ARG   E CD  
13330 N  NE  . ARG   E 263 ? 1.7381 1.4767 1.3909 0.0110  -0.0678 -0.0561 263  ARG   E NE  
13331 C  CZ  . ARG   E 263 ? 1.7522 1.4945 1.4130 0.0056  -0.0780 -0.0569 263  ARG   E CZ  
13332 N  NH1 . ARG   E 263 ? 1.5995 1.3497 1.2732 0.0019  -0.0807 -0.0575 263  ARG   E NH1 
13333 N  NH2 . ARG   E 263 ? 1.7749 1.5128 1.4306 0.0040  -0.0857 -0.0571 263  ARG   E NH2 
13334 N  N   . VAL   E 264 ? 1.6906 1.4640 1.3731 0.0174  -0.0303 -0.0473 264  VAL   E N   
13335 C  CA  . VAL   E 264 ? 1.7670 1.5320 1.4369 0.0203  -0.0273 -0.0460 264  VAL   E CA  
13336 C  C   . VAL   E 264 ? 1.9442 1.6894 1.5909 0.0223  -0.0351 -0.0479 264  VAL   E C   
13337 O  O   . VAL   E 264 ? 1.9306 1.6743 1.5759 0.0190  -0.0448 -0.0484 264  VAL   E O   
13338 C  CB  . VAL   E 264 ? 1.7341 1.4973 1.4006 0.0255  -0.0139 -0.0445 264  VAL   E CB  
13339 C  CG1 . VAL   E 264 ? 1.7026 1.4593 1.3589 0.0277  -0.0105 -0.0427 264  VAL   E CG1 
13340 C  CG2 . VAL   E 264 ? 1.6664 1.4487 1.3565 0.0237  -0.0069 -0.0432 264  VAL   E CG2 
13341 N  N   . ASP   E 265 ? 2.3183 2.0479 1.9467 0.0277  -0.0311 -0.0490 265  ASP   E N   
13342 C  CA  . ASP   E 265 ? 2.3303 2.0401 1.9357 0.0299  -0.0390 -0.0512 265  ASP   E CA  
13343 C  C   . ASP   E 265 ? 2.3252 2.0349 1.9342 0.0260  -0.0498 -0.0537 265  ASP   E C   
13344 O  O   . ASP   E 265 ? 2.3194 2.0376 1.9404 0.0245  -0.0478 -0.0541 265  ASP   E O   
13345 C  CB  . ASP   E 265 ? 2.3529 2.0451 1.9366 0.0372  -0.0315 -0.0517 265  ASP   E CB  
13346 C  CG  . ASP   E 265 ? 2.3670 2.0647 1.9584 0.0392  -0.0228 -0.0518 265  ASP   E CG  
13347 O  OD1 . ASP   E 265 ? 2.3647 2.0622 1.9586 0.0377  -0.0278 -0.0539 265  ASP   E OD1 
13348 O  OD2 . ASP   E 265 ? 2.3685 2.0705 1.9637 0.0423  -0.0109 -0.0499 265  ASP   E OD2 
13349 N  N   . PRO   E 266 ? 2.0312 1.7315 1.6307 0.0242  -0.0612 -0.0553 266  PRO   E N   
13350 C  CA  . PRO   E 266 ? 1.9932 1.6915 1.5949 0.0207  -0.0713 -0.0578 266  PRO   E CA  
13351 C  C   . PRO   E 266 ? 1.9351 1.6189 1.5214 0.0249  -0.0701 -0.0600 266  PRO   E C   
13352 O  O   . PRO   E 266 ? 1.8443 1.5229 1.4287 0.0226  -0.0787 -0.0624 266  PRO   E O   
13353 C  CB  . PRO   E 266 ? 1.9649 1.6549 1.5582 0.0187  -0.0832 -0.0591 266  PRO   E CB  
13354 C  CG  . PRO   E 266 ? 1.9226 1.6212 1.5223 0.0182  -0.0799 -0.0565 266  PRO   E CG  
13355 C  CD  . PRO   E 266 ? 1.9894 1.6870 1.5840 0.0234  -0.0661 -0.0545 266  PRO   E CD  
13356 N  N   . ASN   E 267 ? 1.9354 1.6127 1.5113 0.0309  -0.0592 -0.0593 267  ASN   E N   
13357 C  CA  . ASN   E 267 ? 1.9539 1.6183 1.5159 0.0353  -0.0565 -0.0611 267  ASN   E CA  
13358 C  C   . ASN   E 267 ? 1.9069 1.5850 1.4867 0.0337  -0.0514 -0.0609 267  ASN   E C   
13359 O  O   . ASN   E 267 ? 1.8486 1.5206 1.4244 0.0340  -0.0547 -0.0630 267  ASN   E O   
13360 C  CB  . ASN   E 267 ? 2.0091 1.6597 1.5514 0.0429  -0.0468 -0.0603 267  ASN   E CB  
13361 C  CG  . ASN   E 267 ? 2.0209 1.6543 1.5443 0.0483  -0.0451 -0.0625 267  ASN   E CG  
13362 O  OD1 . ASN   E 267 ? 2.0195 1.6331 1.5199 0.0514  -0.0509 -0.0644 267  ASN   E OD1 
13363 N  ND2 . ASN   E 267 ? 2.0302 1.6705 1.5624 0.0497  -0.0371 -0.0623 267  ASN   E ND2 
13364 N  N   . GLY   E 268 ? 1.9530 1.6490 1.5521 0.0322  -0.0436 -0.0585 268  GLY   E N   
13365 C  CA  . GLY   E 268 ? 1.8729 1.5823 1.4892 0.0312  -0.0384 -0.0582 268  GLY   E CA  
13366 C  C   . GLY   E 268 ? 1.8892 1.6011 1.5065 0.0364  -0.0250 -0.0569 268  GLY   E C   
13367 O  O   . GLY   E 268 ? 1.8277 1.5508 1.4595 0.0360  -0.0204 -0.0568 268  GLY   E O   
13368 N  N   . SER   E 269 ? 1.9679 1.6698 1.5708 0.0412  -0.0185 -0.0559 269  SER   E N   
13369 C  CA  . SER   E 269 ? 1.9766 1.6794 1.5797 0.0465  -0.0053 -0.0547 269  SER   E CA  
13370 C  C   . SER   E 269 ? 1.9777 1.7006 1.6038 0.0443  0.0019  -0.0522 269  SER   E C   
13371 O  O   . SER   E 269 ? 1.9749 1.7069 1.6130 0.0459  0.0099  -0.0519 269  SER   E O   
13372 C  CB  . SER   E 269 ? 2.0563 1.7403 1.6352 0.0527  -0.0002 -0.0544 269  SER   E CB  
13373 O  OG  . SER   E 269 ? 2.1785 1.8667 1.7599 0.0526  0.0044  -0.0519 269  SER   E OG  
13374 N  N   . ARG   E 270 ? 1.8869 1.6168 1.5196 0.0406  -0.0010 -0.0506 270  ARG   E N   
13375 C  CA  . ARG   E 270 ? 1.7783 1.5264 1.4319 0.0384  0.0054  -0.0482 270  ARG   E CA  
13376 C  C   . ARG   E 270 ? 1.7216 1.4850 1.3939 0.0315  -0.0032 -0.0481 270  ARG   E C   
13377 O  O   . ARG   E 270 ? 1.7612 1.5205 1.4281 0.0283  -0.0129 -0.0486 270  ARG   E O   
13378 C  CB  . ARG   E 270 ? 1.8485 1.5919 1.4943 0.0407  0.0113  -0.0460 270  ARG   E CB  
13379 C  CG  . ARG   E 270 ? 1.9307 1.6571 1.5559 0.0480  0.0203  -0.0459 270  ARG   E CG  
13380 C  CD  . ARG   E 270 ? 1.9070 1.6380 1.5374 0.0507  0.0331  -0.0432 270  ARG   E CD  
13381 N  NE  . ARG   E 270 ? 1.9235 1.6626 1.5619 0.0470  0.0313  -0.0412 270  ARG   E NE  
13382 C  CZ  . ARG   E 270 ? 2.0708 1.7983 1.6931 0.0476  0.0276  -0.0405 270  ARG   E CZ  
13383 N  NH1 . ARG   E 270 ? 2.1373 1.8439 1.7339 0.0520  0.0253  -0.0417 270  ARG   E NH1 
13384 N  NH2 . ARG   E 270 ? 2.0662 1.8028 1.6981 0.0440  0.0257  -0.0387 270  ARG   E NH2 
13385 N  N   . TYR   E 271 ? 1.6382 1.4187 1.3320 0.0293  0.0002  -0.0475 271  TYR   E N   
13386 C  CA  . TYR   E 271 ? 1.5030 1.2991 1.2161 0.0233  -0.0063 -0.0473 271  TYR   E CA  
13387 C  C   . TYR   E 271 ? 1.4804 1.2934 1.2129 0.0220  0.0005  -0.0452 271  TYR   E C   
13388 O  O   . TYR   E 271 ? 1.5313 1.3463 1.2666 0.0257  0.0105  -0.0444 271  TYR   E O   
13389 C  CB  . TYR   E 271 ? 1.4832 1.2826 1.2028 0.0223  -0.0095 -0.0491 271  TYR   E CB  
13390 C  CG  . TYR   E 271 ? 1.5222 1.3109 1.2306 0.0203  -0.0200 -0.0511 271  TYR   E CG  
13391 C  CD1 . TYR   E 271 ? 1.5029 1.2981 1.2199 0.0145  -0.0291 -0.0510 271  TYR   E CD1 
13392 C  CD2 . TYR   E 271 ? 1.5558 1.3280 1.2457 0.0241  -0.0206 -0.0531 271  TYR   E CD2 
13393 C  CE1 . TYR   E 271 ? 1.5061 1.2922 1.2146 0.0123  -0.0386 -0.0528 271  TYR   E CE1 
13394 C  CE2 . TYR   E 271 ? 1.5329 1.2953 1.2134 0.0221  -0.0304 -0.0550 271  TYR   E CE2 
13395 C  CZ  . TYR   E 271 ? 1.5332 1.3029 1.2236 0.0160  -0.0394 -0.0548 271  TYR   E CZ  
13396 O  OH  . TYR   E 271 ? 1.5659 1.3266 1.2488 0.0136  -0.0493 -0.0567 271  TYR   E OH  
13397 N  N   . LEU   E 272 ? 1.4442 1.2694 1.1907 0.0168  -0.0049 -0.0442 272  LEU   E N   
13398 C  CA  . LEU   E 272 ? 1.3813 1.2222 1.1461 0.0152  0.0004  -0.0422 272  LEU   E CA  
13399 C  C   . LEU   E 272 ? 1.2948 1.1513 1.0798 0.0119  -0.0019 -0.0426 272  LEU   E C   
13400 O  O   . LEU   E 272 ? 1.3023 1.1605 1.0898 0.0082  -0.0103 -0.0434 272  LEU   E O   
13401 C  CB  . LEU   E 272 ? 1.3947 1.2371 1.1590 0.0124  -0.0032 -0.0406 272  LEU   E CB  
13402 C  CG  . LEU   E 272 ? 1.3700 1.2042 1.1230 0.0159  0.0037  -0.0391 272  LEU   E CG  
13403 C  CD1 . LEU   E 272 ? 1.3272 1.1619 1.0785 0.0131  -0.0013 -0.0377 272  LEU   E CD1 
13404 C  CD2 . LEU   E 272 ? 1.3765 1.2205 1.1424 0.0180  0.0148  -0.0378 272  LEU   E CD2 
13405 N  N   . LEU   E 273 ? 1.3114 1.1791 1.1109 0.0132  0.0057  -0.0420 273  LEU   E N   
13406 C  CA  . LEU   E 273 ? 1.3315 1.2131 1.1493 0.0111  0.0044  -0.0425 273  LEU   E CA  
13407 C  C   . LEU   E 273 ? 1.2694 1.1665 1.1055 0.0089  0.0072  -0.0408 273  LEU   E C   
13408 O  O   . LEU   E 273 ? 1.2904 1.1890 1.1283 0.0107  0.0143  -0.0395 273  LEU   E O   
13409 C  CB  . LEU   E 273 ? 1.3230 1.2041 1.1427 0.0151  0.0100  -0.0439 273  LEU   E CB  
13410 C  CG  . LEU   E 273 ? 1.3238 1.1907 1.1272 0.0173  0.0069  -0.0458 273  LEU   E CG  
13411 C  CD1 . LEU   E 273 ? 1.3176 1.1851 1.1243 0.0215  0.0126  -0.0472 273  LEU   E CD1 
13412 C  CD2 . LEU   E 273 ? 1.2910 1.1572 1.0936 0.0128  -0.0037 -0.0466 273  LEU   E CD2 
13413 N  N   . GLY   E 274 ? 1.2493 1.1575 1.0989 0.0051  0.0019  -0.0408 274  GLY   E N   
13414 C  CA  . GLY   E 274 ? 1.2850 1.2077 1.1521 0.0032  0.0042  -0.0394 274  GLY   E CA  
13415 C  C   . GLY   E 274 ? 1.2420 1.1761 1.1247 0.0021  0.0026  -0.0403 274  GLY   E C   
13416 O  O   . GLY   E 274 ? 1.2231 1.1558 1.1044 0.0004  -0.0036 -0.0412 274  GLY   E O   
13417 N  N   . ASP   E 275 ? 1.2174 1.1624 1.1149 0.0032  0.0081  -0.0399 275  ASP   E N   
13418 C  CA  . ASP   E 275 ? 1.2662 1.2220 1.1786 0.0027  0.0066  -0.0409 275  ASP   E CA  
13419 C  C   . ASP   E 275 ? 1.2611 1.2292 1.1874 -0.0010 0.0038  -0.0396 275  ASP   E C   
13420 O  O   . ASP   E 275 ? 1.2662 1.2343 1.1904 -0.0034 0.0024  -0.0379 275  ASP   E O   
13421 C  CB  . ASP   E 275 ? 1.2738 1.2326 1.1932 0.0071  0.0138  -0.0420 275  ASP   E CB  
13422 C  CG  . ASP   E 275 ? 1.2808 1.2470 1.2108 0.0080  0.0210  -0.0409 275  ASP   E CG  
13423 O  OD1 . ASP   E 275 ? 1.3195 1.2897 1.2526 0.0053  0.0204  -0.0392 275  ASP   E OD1 
13424 O  OD2 . ASP   E 275 ? 1.2907 1.2589 1.2263 0.0116  0.0274  -0.0418 275  ASP   E OD2 
13425 N  N   . MET   E 276 ? 1.1897 1.1677 1.1297 -0.0012 0.0027  -0.0403 276  MET   E N   
13426 C  CA  . MET   E 276 ? 1.2129 1.2016 1.1651 -0.0045 -0.0007 -0.0392 276  MET   E CA  
13427 C  C   . MET   E 276 ? 1.2719 1.2696 1.2362 -0.0039 0.0045  -0.0384 276  MET   E C   
13428 O  O   . MET   E 276 ? 1.2871 1.2947 1.2634 -0.0060 0.0024  -0.0378 276  MET   E O   
13429 C  CB  . MET   E 276 ? 1.2324 1.2265 1.1924 -0.0048 -0.0048 -0.0404 276  MET   E CB  
13430 C  CG  . MET   E 276 ? 1.2730 1.2578 1.2219 -0.0043 -0.0084 -0.0415 276  MET   E CG  
13431 S  SD  . MET   E 276 ? 1.2501 1.2396 1.2071 -0.0032 -0.0113 -0.0431 276  MET   E SD  
13432 C  CE  . MET   E 276 ? 1.1874 1.1787 1.1450 -0.0081 -0.0189 -0.0418 276  MET   E CE  
13433 N  N   . GLU   E 277 ? 1.2737 1.2681 1.2355 -0.0011 0.0116  -0.0383 277  GLU   E N   
13434 C  CA  . GLU   E 277 ? 1.2732 1.2752 1.2462 -0.0009 0.0172  -0.0374 277  GLU   E CA  
13435 C  C   . GLU   E 277 ? 1.2816 1.2760 1.2442 -0.0006 0.0216  -0.0357 277  GLU   E C   
13436 O  O   . GLU   E 277 ? 1.2952 1.2927 1.2640 0.0007  0.0284  -0.0350 277  GLU   E O   
13437 C  CB  . GLU   E 277 ? 1.3185 1.3261 1.3031 0.0027  0.0229  -0.0389 277  GLU   E CB  
13438 C  CG  . GLU   E 277 ? 1.3302 1.3400 1.3188 0.0040  0.0191  -0.0410 277  GLU   E CG  
13439 C  CD  . GLU   E 277 ? 1.4533 1.4685 1.4537 0.0078  0.0243  -0.0427 277  GLU   E CD  
13440 O  OE1 . GLU   E 277 ? 1.5187 1.5396 1.5292 0.0084  0.0300  -0.0422 277  GLU   E OE1 
13441 O  OE2 . GLU   E 277 ? 1.4435 1.4572 1.4435 0.0102  0.0227  -0.0446 277  GLU   E OE2 
13442 N  N   . GLY   E 278 ? 1.4453 1.4294 1.3919 -0.0017 0.0178  -0.0352 278  GLY   E N   
13443 C  CA  . GLY   E 278 ? 1.4772 1.4535 1.4126 -0.0017 0.0205  -0.0335 278  GLY   E CA  
13444 C  C   . GLY   E 278 ? 1.4910 1.4555 1.4131 0.0023  0.0267  -0.0338 278  GLY   E C   
13445 O  O   . GLY   E 278 ? 1.5026 1.4588 1.4133 0.0028  0.0292  -0.0325 278  GLY   E O   
13446 N  N   . ARG   E 279 ? 1.3410 1.3038 1.2635 0.0054  0.0294  -0.0356 279  ARG   E N   
13447 C  CA  . ARG   E 279 ? 1.2854 1.2369 1.1954 0.0095  0.0361  -0.0358 279  ARG   E CA  
13448 C  C   . ARG   E 279 ? 1.3383 1.2752 1.2273 0.0097  0.0313  -0.0361 279  ARG   E C   
13449 O  O   . ARG   E 279 ? 1.3422 1.2775 1.2279 0.0081  0.0237  -0.0373 279  ARG   E O   
13450 C  CB  . ARG   E 279 ? 1.2226 1.1771 1.1401 0.0130  0.0403  -0.0376 279  ARG   E CB  
13451 C  CG  . ARG   E 279 ? 1.2515 1.2192 1.1892 0.0133  0.0455  -0.0375 279  ARG   E CG  
13452 C  CD  . ARG   E 279 ? 1.3001 1.2693 1.2441 0.0174  0.0511  -0.0392 279  ARG   E CD  
13453 N  NE  . ARG   E 279 ? 1.3784 1.3542 1.3310 0.0171  0.0454  -0.0412 279  ARG   E NE  
13454 C  CZ  . ARG   E 279 ? 1.3974 1.3862 1.3689 0.0165  0.0446  -0.0420 279  ARG   E CZ  
13455 N  NH1 . ARG   E 279 ? 1.3998 1.3975 1.3850 0.0158  0.0491  -0.0410 279  ARG   E NH1 
13456 N  NH2 . ARG   E 279 ? 1.4524 1.4452 1.4289 0.0166  0.0391  -0.0438 279  ARG   E NH2 
13457 N  N   . LEU   E 280 ? 1.3579 1.2836 1.2326 0.0119  0.0357  -0.0350 280  LEU   E N   
13458 C  CA  . LEU   E 280 ? 1.3466 1.2568 1.1998 0.0127  0.0317  -0.0354 280  LEU   E CA  
13459 C  C   . LEU   E 280 ? 1.3715 1.2707 1.2133 0.0179  0.0382  -0.0364 280  LEU   E C   
13460 O  O   . LEU   E 280 ? 1.3745 1.2692 1.2121 0.0211  0.0469  -0.0353 280  LEU   E O   
13461 C  CB  . LEU   E 280 ? 1.2652 1.1695 1.1088 0.0116  0.0312  -0.0335 280  LEU   E CB  
13462 C  CG  . LEU   E 280 ? 1.1743 1.0624 0.9956 0.0123  0.0261  -0.0337 280  LEU   E CG  
13463 C  CD1 . LEU   E 280 ? 1.2028 1.0909 1.0226 0.0088  0.0150  -0.0351 280  LEU   E CD1 
13464 C  CD2 . LEU   E 280 ? 1.2252 1.1097 1.0402 0.0116  0.0270  -0.0316 280  LEU   E CD2 
13465 N  N   . PHE   E 281 ? 1.4326 1.3273 1.2693 0.0189  0.0342  -0.0384 281  PHE   E N   
13466 C  CA  . PHE   E 281 ? 1.4415 1.3242 1.2651 0.0239  0.0394  -0.0395 281  PHE   E CA  
13467 C  C   . PHE   E 281 ? 1.4583 1.3235 1.2582 0.0249  0.0345  -0.0401 281  PHE   E C   
13468 O  O   . PHE   E 281 ? 1.4519 1.3150 1.2471 0.0213  0.0253  -0.0402 281  PHE   E O   
13469 C  CB  . PHE   E 281 ? 1.4052 1.2920 1.2361 0.0254  0.0389  -0.0416 281  PHE   E CB  
13470 C  CG  . PHE   E 281 ? 1.3863 1.2903 1.2402 0.0237  0.0399  -0.0417 281  PHE   E CG  
13471 C  CD1 . PHE   E 281 ? 1.4200 1.3310 1.2860 0.0265  0.0490  -0.0414 281  PHE   E CD1 
13472 C  CD2 . PHE   E 281 ? 1.3944 1.3069 1.2577 0.0196  0.0317  -0.0422 281  PHE   E CD2 
13473 C  CE1 . PHE   E 281 ? 1.4363 1.3627 1.3235 0.0251  0.0492  -0.0418 281  PHE   E CE1 
13474 C  CE2 . PHE   E 281 ? 1.4456 1.3729 1.3289 0.0184  0.0322  -0.0424 281  PHE   E CE2 
13475 C  CZ  . PHE   E 281 ? 1.4767 1.4110 1.3720 0.0212  0.0406  -0.0424 281  PHE   E CZ  
13476 N  N   . MET   E 282 ? 1.4769 1.3294 1.2623 0.0299  0.0406  -0.0405 282  MET   E N   
13477 C  CA  . MET   E 282 ? 1.5128 1.3469 1.2741 0.0318  0.0368  -0.0412 282  MET   E CA  
13478 C  C   . MET   E 282 ? 1.5323 1.3590 1.2865 0.0351  0.0369  -0.0435 282  MET   E C   
13479 O  O   . MET   E 282 ? 1.5244 1.3502 1.2799 0.0395  0.0457  -0.0437 282  MET   E O   
13480 C  CB  . MET   E 282 ? 1.5510 1.3740 1.2982 0.0354  0.0442  -0.0396 282  MET   E CB  
13481 C  CG  . MET   E 282 ? 1.6036 1.4055 1.3240 0.0388  0.0420  -0.0404 282  MET   E CG  
13482 S  SD  . MET   E 282 ? 1.6913 1.4841 1.3976 0.0351  0.0281  -0.0411 282  MET   E SD  
13483 C  CE  . MET   E 282 ? 1.6213 1.4244 1.3381 0.0312  0.0276  -0.0385 282  MET   E CE  
13484 N  N   . LEU   E 283 ? 1.5039 1.3258 1.2518 0.0329  0.0271  -0.0452 283  LEU   E N   
13485 C  CA  . LEU   E 283 ? 1.4878 1.3002 1.2258 0.0359  0.0260  -0.0474 283  LEU   E CA  
13486 C  C   . LEU   E 283 ? 1.6114 1.4033 1.3235 0.0396  0.0259  -0.0479 283  LEU   E C   
13487 O  O   . LEU   E 283 ? 1.6405 1.4245 1.3414 0.0374  0.0182  -0.0480 283  LEU   E O   
13488 C  CB  . LEU   E 283 ? 1.3945 1.2108 1.1378 0.0318  0.0158  -0.0489 283  LEU   E CB  
13489 C  CG  . LEU   E 283 ? 1.3894 1.1970 1.1243 0.0346  0.0145  -0.0513 283  LEU   E CG  
13490 C  CD1 . LEU   E 283 ? 1.3723 1.1889 1.1204 0.0376  0.0220  -0.0517 283  LEU   E CD1 
13491 C  CD2 . LEU   E 283 ? 1.3854 1.1925 1.1206 0.0302  0.0035  -0.0526 283  LEU   E CD2 
13492 N  N   . LEU   E 284 ? 1.6386 1.4215 1.3411 0.0455  0.0344  -0.0483 284  LEU   E N   
13493 C  CA  . LEU   E 284 ? 1.6277 1.3896 1.3042 0.0499  0.0346  -0.0490 284  LEU   E CA  
13494 C  C   . LEU   E 284 ? 1.6446 1.3978 1.3124 0.0522  0.0314  -0.0516 284  LEU   E C   
13495 O  O   . LEU   E 284 ? 1.5970 1.3578 1.2762 0.0537  0.0358  -0.0523 284  LEU   E O   
13496 C  CB  . LEU   E 284 ? 1.6065 1.3622 1.2757 0.0554  0.0471  -0.0474 284  LEU   E CB  
13497 C  CG  . LEU   E 284 ? 1.5949 1.3586 1.2727 0.0538  0.0522  -0.0446 284  LEU   E CG  
13498 C  CD1 . LEU   E 284 ? 1.5874 1.3661 1.2860 0.0549  0.0627  -0.0435 284  LEU   E CD1 
13499 C  CD2 . LEU   E 284 ? 1.7178 1.4647 1.3736 0.0577  0.0562  -0.0433 284  LEU   E CD2 
13500 N  N   . LEU   E 285 ? 1.6906 1.4279 1.3387 0.0523  0.0234  -0.0531 285  LEU   E N   
13501 C  CA  . LEU   E 285 ? 1.6963 1.4216 1.3318 0.0551  0.0206  -0.0556 285  LEU   E CA  
13502 C  C   . LEU   E 285 ? 1.7604 1.4668 1.3727 0.0621  0.0274  -0.0557 285  LEU   E C   
13503 O  O   . LEU   E 285 ? 1.8554 1.5462 1.4477 0.0631  0.0227  -0.0562 285  LEU   E O   
13504 C  CB  . LEU   E 285 ? 1.7082 1.4277 1.3374 0.0507  0.0071  -0.0574 285  LEU   E CB  
13505 C  CG  . LEU   E 285 ? 1.7013 1.4366 1.3508 0.0443  -0.0001 -0.0576 285  LEU   E CG  
13506 C  CD1 . LEU   E 285 ? 1.6965 1.4463 1.3615 0.0395  -0.0014 -0.0555 285  LEU   E CD1 
13507 C  CD2 . LEU   E 285 ? 1.6707 1.3969 1.3115 0.0414  -0.0118 -0.0598 285  LEU   E CD2 
13508 N  N   . GLU   E 286 ? 1.7686 1.4764 1.3839 0.0671  0.0386  -0.0553 286  GLU   E N   
13509 C  CA  . GLU   E 286 ? 1.8704 1.5609 1.4648 0.0743  0.0467  -0.0553 286  GLU   E CA  
13510 C  C   . GLU   E 286 ? 1.9868 1.6579 1.5585 0.0769  0.0398  -0.0579 286  GLU   E C   
13511 O  O   . GLU   E 286 ? 1.9793 1.6514 1.5543 0.0773  0.0377  -0.0598 286  GLU   E O   
13512 C  CB  . GLU   E 286 ? 1.7629 1.4608 1.3684 0.0788  0.0598  -0.0545 286  GLU   E CB  
13513 N  N   . LYS   E 287 ? 2.0638 1.7172 1.6125 0.0784  0.0356  -0.0582 287  LYS   E N   
13514 C  CA  . LYS   E 287 ? 2.1212 1.7561 1.6485 0.0798  0.0266  -0.0610 287  LYS   E CA  
13515 C  C   . LYS   E 287 ? 2.3401 1.9554 1.8442 0.0883  0.0346  -0.0615 287  LYS   E C   
13516 O  O   . LYS   E 287 ? 2.3541 1.9702 1.8586 0.0928  0.0471  -0.0596 287  LYS   E O   
13517 C  CB  . LYS   E 287 ? 2.0483 1.6760 1.5657 0.0760  0.0151  -0.0613 287  LYS   E CB  
13518 N  N   . GLU   E 288 ? 2.6172 2.2145 2.1007 0.0904  0.0273  -0.0642 288  GLU   E N   
13519 C  CA  . GLU   E 288 ? 2.6838 2.2623 2.1454 0.0986  0.0341  -0.0652 288  GLU   E CA  
13520 C  C   . GLU   E 288 ? 2.7141 2.2689 2.1475 0.1004  0.0241  -0.0676 288  GLU   E C   
13521 O  O   . GLU   E 288 ? 2.7008 2.2524 2.1327 0.0975  0.0133  -0.0702 288  GLU   E O   
13522 C  CB  . GLU   E 288 ? 2.7090 2.2937 2.1807 0.1003  0.0380  -0.0665 288  GLU   E CB  
13523 C  CG  . GLU   E 288 ? 2.7929 2.3595 2.2439 0.1089  0.0457  -0.0675 288  GLU   E CG  
13524 C  CD  . GLU   E 288 ? 2.8192 2.3951 2.2840 0.1109  0.0516  -0.0683 288  GLU   E CD  
13525 O  OE1 . GLU   E 288 ? 2.8398 2.4262 2.3189 0.1060  0.0440  -0.0697 288  GLU   E OE1 
13526 O  OE2 . GLU   E 288 ? 2.7887 2.3609 2.2497 0.1175  0.0639  -0.0675 288  GLU   E OE2 
13527 N  N   . GLU   E 289 ? 2.6213 2.1587 2.0318 0.1057  0.0279  -0.0669 289  GLU   E N   
13528 C  CA  . GLU   E 289 ? 2.5914 2.1050 1.9734 0.1081  0.0184  -0.0691 289  GLU   E CA  
13529 C  C   . GLU   E 289 ? 2.6098 2.1042 1.9704 0.1154  0.0217  -0.0712 289  GLU   E C   
13530 O  O   . GLU   E 289 ? 2.6056 2.0874 1.9498 0.1228  0.0325  -0.0701 289  GLU   E O   
13531 C  CB  . GLU   E 289 ? 2.5081 2.0114 1.8747 0.1107  0.0208  -0.0673 289  GLU   E CB  
13532 C  CG  . GLU   E 289 ? 2.4653 1.9843 1.8491 0.1039  0.0162  -0.0655 289  GLU   E CG  
13533 C  CD  . GLU   E 289 ? 2.4604 1.9737 1.8344 0.1073  0.0242  -0.0627 289  GLU   E CD  
13534 O  OE1 . GLU   E 289 ? 2.4288 1.9226 1.7785 0.1151  0.0314  -0.0625 289  GLU   E OE1 
13535 O  OE2 . GLU   E 289 ? 2.4793 2.0073 1.8695 0.1024  0.0234  -0.0607 289  GLU   E OE2 
13536 N  N   . GLN   E 290 ? 2.5542 2.0451 1.9136 0.1134  0.0124  -0.0742 290  GLN   E N   
13537 C  CA  . GLN   E 290 ? 2.4955 1.9677 1.8342 0.1201  0.0144  -0.0764 290  GLN   E CA  
13538 C  C   . GLN   E 290 ? 2.4932 1.9379 1.7985 0.1251  0.0093  -0.0779 290  GLN   E C   
13539 O  O   . GLN   E 290 ? 2.4936 1.9341 1.7928 0.1221  0.0004  -0.0781 290  GLN   E O   
13540 C  CB  . GLN   E 290 ? 2.4766 1.9524 1.8236 0.1163  0.0054  -0.0791 290  GLN   E CB  
13541 C  CG  . GLN   E 290 ? 2.5345 2.0375 1.9149 0.1098  0.0064  -0.0779 290  GLN   E CG  
13542 C  CD  . GLN   E 290 ? 2.6324 2.1469 2.0261 0.1138  0.0210  -0.0762 290  GLN   E CD  
13543 O  OE1 . GLN   E 290 ? 2.6564 2.1669 2.0433 0.1195  0.0329  -0.0743 290  GLN   E OE1 
13544 N  NE2 . GLN   E 290 ? 2.5968 2.1254 2.0098 0.1108  0.0202  -0.0769 290  GLN   E NE2 
13545 N  N   . MET   E 291 ? 2.5434 1.9692 1.8266 0.1332  0.0150  -0.0791 291  MET   E N   
13546 C  CA  . MET   E 291 ? 2.4779 1.8755 1.7268 0.1390  0.0104  -0.0809 291  MET   E CA  
13547 C  C   . MET   E 291 ? 2.4212 1.8091 1.6619 0.1347  -0.0076 -0.0846 291  MET   E C   
13548 O  O   . MET   E 291 ? 2.4179 1.7904 1.6400 0.1352  -0.0166 -0.0858 291  MET   E O   
13549 C  CB  . MET   E 291 ? 2.3224 1.7023 1.5502 0.1488  0.0213  -0.0813 291  MET   E CB  
13550 C  CG  . MET   E 291 ? 2.2994 1.6828 1.5286 0.1545  0.0395  -0.0776 291  MET   E CG  
13551 S  SD  . MET   E 291 ? 2.1566 1.5425 1.3850 0.1531  0.0419  -0.0743 291  MET   E SD  
13552 C  CE  . MET   E 291 ? 2.2865 1.7088 1.5583 0.1442  0.0457  -0.0716 291  MET   E CE  
13553 N  N   . ASP   E 292 ? 2.3810 1.7779 1.6362 0.1304  -0.0132 -0.0864 292  ASP   E N   
13554 C  CA  . ASP   E 292 ? 2.3522 1.7408 1.6019 0.1260  -0.0297 -0.0899 292  ASP   E CA  
13555 C  C   . ASP   E 292 ? 2.4483 1.8505 1.7151 0.1168  -0.0412 -0.0897 292  ASP   E C   
13556 O  O   . ASP   E 292 ? 2.4395 1.8465 1.7164 0.1106  -0.0527 -0.0917 292  ASP   E O   
13557 C  CB  . ASP   E 292 ? 2.2943 1.6881 1.5540 0.1247  -0.0304 -0.0916 292  ASP   E CB  
13558 C  CG  . ASP   E 292 ? 2.3155 1.7377 1.6097 0.1169  -0.0298 -0.0900 292  ASP   E CG  
13559 O  OD1 . ASP   E 292 ? 2.3526 1.7923 1.6643 0.1162  -0.0198 -0.0868 292  ASP   E OD1 
13560 O  OD2 . ASP   E 292 ? 2.2700 1.6965 1.5738 0.1112  -0.0400 -0.0919 292  ASP   E OD2 
13561 N  N   . GLY   E 293 ? 2.7447 2.1527 2.0147 0.1159  -0.0387 -0.0873 293  GLY   E N   
13562 C  CA  . GLY   E 293 ? 2.7258 2.1477 2.0133 0.1074  -0.0489 -0.0869 293  GLY   E CA  
13563 C  C   . GLY   E 293 ? 2.7242 2.1751 2.0462 0.1005  -0.0454 -0.0848 293  GLY   E C   
13564 O  O   . GLY   E 293 ? 2.7009 2.1673 2.0396 0.0955  -0.0462 -0.0827 293  GLY   E O   
13565 N  N   . THR   E 294 ? 2.4672 1.9249 1.7994 0.1006  -0.0413 -0.0853 294  THR   E N   
13566 C  CA  . THR   E 294 ? 2.4407 1.9243 1.8042 0.0944  -0.0388 -0.0837 294  THR   E CA  
13567 C  C   . THR   E 294 ? 2.4571 1.9576 1.8363 0.0943  -0.0276 -0.0800 294  THR   E C   
13568 O  O   . THR   E 294 ? 2.4495 1.9422 1.8161 0.1004  -0.0178 -0.0784 294  THR   E O   
13569 C  CB  . THR   E 294 ? 2.4561 1.9415 1.8240 0.0966  -0.0338 -0.0846 294  THR   E CB  
13570 O  OG1 . THR   E 294 ? 2.4641 1.9303 1.8135 0.0980  -0.0431 -0.0881 294  THR   E OG1 
13571 C  CG2 . THR   E 294 ? 2.3522 1.8624 1.7513 0.0899  -0.0338 -0.0836 294  THR   E CG2 
13572 N  N   . VAL   E 295 ? 2.5171 2.0405 1.9238 0.0871  -0.0293 -0.0785 295  VAL   E N   
13573 C  CA  . VAL   E 295 ? 2.4547 1.9977 1.8815 0.0861  -0.0189 -0.0752 295  VAL   E CA  
13574 C  C   . VAL   E 295 ? 2.3747 1.9383 1.8281 0.0814  -0.0181 -0.0748 295  VAL   E C   
13575 O  O   . VAL   E 295 ? 2.3141 1.8818 1.7756 0.0757  -0.0285 -0.0763 295  VAL   E O   
13576 C  CB  . VAL   E 295 ? 2.3865 1.9358 1.8185 0.0819  -0.0229 -0.0735 295  VAL   E CB  
13577 C  CG1 . VAL   E 295 ? 2.3921 1.9560 1.8380 0.0829  -0.0104 -0.0700 295  VAL   E CG1 
13578 C  CG2 . VAL   E 295 ? 2.3425 1.8690 1.7465 0.0854  -0.0289 -0.0747 295  VAL   E CG2 
13579 N  N   . THR   E 296 ? 2.3366 1.9125 1.8032 0.0839  -0.0058 -0.0730 296  THR   E N   
13580 C  CA  . THR   E 296 ? 2.3115 1.9062 1.8023 0.0805  -0.0042 -0.0727 296  THR   E CA  
13581 C  C   . THR   E 296 ? 2.2626 1.8781 1.7759 0.0787  0.0043  -0.0697 296  THR   E C   
13582 O  O   . THR   E 296 ? 2.2563 1.8713 1.7662 0.0800  0.0091  -0.0678 296  THR   E O   
13583 C  CB  . THR   E 296 ? 2.3790 1.9673 1.8641 0.0861  0.0017  -0.0742 296  THR   E CB  
13584 O  OG1 . THR   E 296 ? 2.4453 2.0268 1.9203 0.0936  0.0143  -0.0730 296  THR   E OG1 
13585 C  CG2 . THR   E 296 ? 2.4086 1.9775 1.8736 0.0871  -0.0077 -0.0773 296  THR   E CG2 
13586 N  N   . LEU   E 297 ? 2.1900 1.8235 1.7263 0.0758  0.0060  -0.0694 297  LEU   E N   
13587 C  CA  . LEU   E 297 ? 2.0707 1.7254 1.6307 0.0734  0.0127  -0.0669 297  LEU   E CA  
13588 C  C   . LEU   E 297 ? 1.9955 1.6551 1.5621 0.0790  0.0252  -0.0664 297  LEU   E C   
13589 O  O   . LEU   E 297 ? 1.8502 1.5134 1.4235 0.0799  0.0255  -0.0678 297  LEU   E O   
13590 C  CB  . LEU   E 297 ? 1.9658 1.6377 1.5477 0.0661  0.0052  -0.0668 297  LEU   E CB  
13591 C  CG  . LEU   E 297 ? 1.8464 1.5391 1.4515 0.0626  0.0096  -0.0643 297  LEU   E CG  
13592 C  CD1 . LEU   E 297 ? 1.8631 1.5532 1.4622 0.0617  0.0098  -0.0626 297  LEU   E CD1 
13593 C  CD2 . LEU   E 297 ? 1.7637 1.4708 1.3875 0.0559  0.0018  -0.0645 297  LEU   E CD2 
13594 N  N   . LYS   E 298 ? 2.0557 1.7152 1.6204 0.0828  0.0356  -0.0644 298  LYS   E N   
13595 C  CA  . LYS   E 298 ? 2.0298 1.6956 1.6033 0.0880  0.0484  -0.0636 298  LYS   E CA  
13596 C  C   . LYS   E 298 ? 1.9775 1.6668 1.5805 0.0841  0.0500  -0.0628 298  LYS   E C   
13597 O  O   . LYS   E 298 ? 1.9563 1.6515 1.5689 0.0854  0.0514  -0.0641 298  LYS   E O   
13598 C  CB  . LYS   E 298 ? 2.0942 1.7545 1.6596 0.0923  0.0591  -0.0614 298  LYS   E CB  
13599 C  CG  . LYS   E 298 ? 2.2904 1.9283 1.8289 0.1001  0.0649  -0.0621 298  LYS   E CG  
13600 C  CD  . LYS   E 298 ? 2.3939 2.0256 1.9234 0.1037  0.0748  -0.0595 298  LYS   E CD  
13601 C  CE  . LYS   E 298 ? 2.4949 2.1038 1.9971 0.1121  0.0815  -0.0600 298  LYS   E CE  
13602 N  NZ  . LYS   E 298 ? 2.4255 2.0211 1.9095 0.1149  0.0859  -0.0581 298  LYS   E NZ  
13603 N  N   . ASP   E 299 ? 1.8786 1.5813 1.4961 0.0794  0.0496  -0.0608 299  ASP   E N   
13604 C  CA  . ASP   E 299 ? 1.7742 1.4987 1.4192 0.0766  0.0528  -0.0599 299  ASP   E CA  
13605 C  C   . ASP   E 299 ? 1.6774 1.4133 1.3341 0.0694  0.0455  -0.0586 299  ASP   E C   
13606 O  O   . ASP   E 299 ? 1.6735 1.4010 1.3183 0.0664  0.0370  -0.0588 299  ASP   E O   
13607 C  CB  . ASP   E 299 ? 1.7313 1.4615 1.3844 0.0812  0.0666  -0.0582 299  ASP   E CB  
13608 C  CG  . ASP   E 299 ? 1.6935 1.4411 1.3707 0.0815  0.0711  -0.0586 299  ASP   E CG  
13609 O  OD1 . ASP   E 299 ? 1.7365 1.4843 1.4156 0.0821  0.0670  -0.0607 299  ASP   E OD1 
13610 O  OD2 . ASP   E 299 ? 1.6469 1.4074 1.3409 0.0815  0.0787  -0.0569 299  ASP   E OD2 
13611 N  N   . LEU   E 300 ? 1.6550 1.4101 1.3356 0.0668  0.0487  -0.0574 300  LEU   E N   
13612 C  CA  . LEU   E 300 ? 1.6101 1.3785 1.3050 0.0605  0.0434  -0.0560 300  LEU   E CA  
13613 C  C   . LEU   E 300 ? 1.5948 1.3779 1.3082 0.0609  0.0528  -0.0541 300  LEU   E C   
13614 O  O   . LEU   E 300 ? 1.6127 1.4056 1.3407 0.0630  0.0583  -0.0545 300  LEU   E O   
13615 C  CB  . LEU   E 300 ? 1.6014 1.3793 1.3086 0.0556  0.0342  -0.0572 300  LEU   E CB  
13616 C  CG  . LEU   E 300 ? 1.5554 1.3231 1.2498 0.0523  0.0227  -0.0586 300  LEU   E CG  
13617 C  CD1 . LEU   E 300 ? 1.5179 1.2961 1.2268 0.0486  0.0165  -0.0595 300  LEU   E CD1 
13618 C  CD2 . LEU   E 300 ? 1.5603 1.3270 1.2510 0.0482  0.0177  -0.0571 300  LEU   E CD2 
13619 N  N   . ARG   E 301 ? 1.5151 1.2995 1.2281 0.0590  0.0544  -0.0520 301  ARG   E N   
13620 C  CA  . ARG   E 301 ? 1.5278 1.3252 1.2576 0.0592  0.0632  -0.0500 301  ARG   E CA  
13621 C  C   . ARG   E 301 ? 1.5743 1.3852 1.3188 0.0528  0.0575  -0.0487 301  ARG   E C   
13622 O  O   . ARG   E 301 ? 1.5674 1.3747 1.3049 0.0488  0.0480  -0.0488 301  ARG   E O   
13623 C  CB  . ARG   E 301 ? 1.5766 1.3629 1.2927 0.0635  0.0726  -0.0483 301  ARG   E CB  
13624 C  CG  . ARG   E 301 ? 1.6093 1.4067 1.3420 0.0653  0.0845  -0.0465 301  ARG   E CG  
13625 C  CD  . ARG   E 301 ? 1.6294 1.4128 1.3464 0.0717  0.0957  -0.0455 301  ARG   E CD  
13626 N  NE  . ARG   E 301 ? 1.5964 1.3643 1.2912 0.0720  0.0937  -0.0443 301  ARG   E NE  
13627 C  CZ  . ARG   E 301 ? 1.6546 1.4251 1.3513 0.0698  0.0957  -0.0420 301  ARG   E CZ  
13628 N  NH1 . ARG   E 301 ? 1.6431 1.4308 1.3628 0.0671  0.1002  -0.0405 301  ARG   E NH1 
13629 N  NH2 . ARG   E 301 ? 1.6814 1.4365 1.3564 0.0705  0.0929  -0.0412 301  ARG   E NH2 
13630 N  N   . VAL   E 302 ? 1.6392 1.4660 1.4048 0.0519  0.0633  -0.0475 302  VAL   E N   
13631 C  CA  . VAL   E 302 ? 1.6019 1.4428 1.3834 0.0463  0.0591  -0.0462 302  VAL   E CA  
13632 C  C   . VAL   E 302 ? 1.5999 1.4474 1.3908 0.0471  0.0686  -0.0440 302  VAL   E C   
13633 O  O   . VAL   E 302 ? 1.5690 1.4216 1.3699 0.0505  0.0777  -0.0439 302  VAL   E O   
13634 C  CB  . VAL   E 302 ? 1.5036 1.3596 1.3048 0.0434  0.0542  -0.0475 302  VAL   E CB  
13635 C  CG1 . VAL   E 302 ? 1.5345 1.4061 1.3543 0.0389  0.0530  -0.0459 302  VAL   E CG1 
13636 C  CG2 . VAL   E 302 ? 1.4724 1.3223 1.2648 0.0412  0.0436  -0.0492 302  VAL   E CG2 
13637 N  N   . GLU   E 303 ? 1.7068 1.5542 1.4950 0.0440  0.0665  -0.0421 303  GLU   E N   
13638 C  CA  . GLU   E 303 ? 1.7101 1.5625 1.5057 0.0442  0.0748  -0.0398 303  GLU   E CA  
13639 C  C   . GLU   E 303 ? 1.6667 1.5336 1.4786 0.0385  0.0696  -0.0387 303  GLU   E C   
13640 O  O   . GLU   E 303 ? 1.6656 1.5311 1.4725 0.0347  0.0599  -0.0389 303  GLU   E O   
13641 C  CB  . GLU   E 303 ? 1.7718 1.6075 1.5453 0.0468  0.0785  -0.0382 303  GLU   E CB  
13642 C  CG  . GLU   E 303 ? 1.8562 1.6804 1.6182 0.0533  0.0891  -0.0382 303  GLU   E CG  
13643 C  CD  . GLU   E 303 ? 1.8764 1.7103 1.6551 0.0552  0.1014  -0.0367 303  GLU   E CD  
13644 O  OE1 . GLU   E 303 ? 1.8529 1.6966 1.6441 0.0521  0.1032  -0.0348 303  GLU   E OE1 
13645 O  OE2 . GLU   E 303 ? 1.8972 1.7290 1.6769 0.0599  0.1093  -0.0374 303  GLU   E OE2 
13646 N  N   . LEU   E 304 ? 1.5212 1.4013 1.3525 0.0380  0.0762  -0.0376 304  LEU   E N   
13647 C  CA  . LEU   E 304 ? 1.4390 1.3330 1.2866 0.0330  0.0724  -0.0366 304  LEU   E CA  
13648 C  C   . LEU   E 304 ? 1.4174 1.3072 1.2589 0.0324  0.0765  -0.0340 304  LEU   E C   
13649 O  O   . LEU   E 304 ? 1.3917 1.2825 1.2379 0.0347  0.0867  -0.0326 304  LEU   E O   
13650 C  CB  . LEU   E 304 ? 1.3880 1.2987 1.2605 0.0328  0.0764  -0.0371 304  LEU   E CB  
13651 C  CG  . LEU   E 304 ? 1.3348 1.2598 1.2250 0.0283  0.0742  -0.0359 304  LEU   E CG  
13652 C  CD1 . LEU   E 304 ? 1.3760 1.3030 1.2638 0.0236  0.0625  -0.0362 304  LEU   E CD1 
13653 C  CD2 . LEU   E 304 ? 1.2685 1.2090 1.1827 0.0285  0.0775  -0.0369 304  LEU   E CD2 
13654 N  N   . LEU   E 305 ? 1.4223 1.3076 1.2538 0.0293  0.0685  -0.0333 305  LEU   E N   
13655 C  CA  . LEU   E 305 ? 1.4139 1.2931 1.2366 0.0290  0.0713  -0.0310 305  LEU   E CA  
13656 C  C   . LEU   E 305 ? 1.4190 1.3128 1.2614 0.0259  0.0742  -0.0293 305  LEU   E C   
13657 O  O   . LEU   E 305 ? 1.4510 1.3437 1.2946 0.0275  0.0833  -0.0274 305  LEU   E O   
13658 C  CB  . LEU   E 305 ? 1.3846 1.2544 1.1909 0.0268  0.0612  -0.0311 305  LEU   E CB  
13659 C  CG  . LEU   E 305 ? 1.4061 1.2619 1.1938 0.0289  0.0560  -0.0331 305  LEU   E CG  
13660 C  CD1 . LEU   E 305 ? 1.3529 1.1991 1.1251 0.0269  0.0466  -0.0331 305  LEU   E CD1 
13661 C  CD2 . LEU   E 305 ? 1.5578 1.4006 1.3316 0.0349  0.0656  -0.0330 305  LEU   E CD2 
13662 N  N   . GLY   E 306 ? 1.4095 1.3167 1.2671 0.0216  0.0667  -0.0300 306  GLY   E N   
13663 C  CA  . GLY   E 306 ? 1.4055 1.3267 1.2822 0.0186  0.0686  -0.0287 306  GLY   E CA  
13664 C  C   . GLY   E 306 ? 1.3562 1.2908 1.2480 0.0144  0.0598  -0.0298 306  GLY   E C   
13665 O  O   . GLY   E 306 ? 1.3319 1.2680 1.2251 0.0144  0.0548  -0.0317 306  GLY   E O   
13666 N  N   . GLU   E 307 ? 1.3864 1.3304 1.2892 0.0110  0.0582  -0.0284 307  GLU   E N   
13667 C  CA  . GLU   E 307 ? 1.3299 1.2856 1.2455 0.0070  0.0498  -0.0290 307  GLU   E CA  
13668 C  C   . GLU   E 307 ? 1.3180 1.2709 1.2259 0.0037  0.0434  -0.0276 307  GLU   E C   
13669 O  O   . GLU   E 307 ? 1.3349 1.2836 1.2374 0.0039  0.0471  -0.0257 307  GLU   E O   
13670 C  CB  . GLU   E 307 ? 1.3504 1.3213 1.2888 0.0059  0.0533  -0.0290 307  GLU   E CB  
13671 C  CG  . GLU   E 307 ? 1.4109 1.3926 1.3624 0.0041  0.0466  -0.0308 307  GLU   E CG  
13672 C  CD  . GLU   E 307 ? 1.4241 1.4200 1.3976 0.0036  0.0496  -0.0311 307  GLU   E CD  
13673 O  OE1 . GLU   E 307 ? 1.4365 1.4350 1.4162 0.0037  0.0562  -0.0297 307  GLU   E OE1 
13674 O  OE2 . GLU   E 307 ? 1.3914 1.3955 1.3758 0.0032  0.0454  -0.0328 307  GLU   E OE2 
13675 N  N   . THR   E 308 ? 1.2709 1.2256 1.1779 0.0010  0.0338  -0.0285 308  THR   E N   
13676 C  CA  . THR   E 308 ? 1.2754 1.2290 1.1774 -0.0023 0.0269  -0.0274 308  THR   E CA  
13677 C  C   . THR   E 308 ? 1.2535 1.2214 1.1726 -0.0060 0.0215  -0.0275 308  THR   E C   
13678 O  O   . THR   E 308 ? 1.3137 1.2925 1.2490 -0.0060 0.0251  -0.0277 308  THR   E O   
13679 C  CB  . THR   E 308 ? 1.2493 1.1907 1.1334 -0.0023 0.0200  -0.0282 308  THR   E CB  
13680 O  OG1 . THR   E 308 ? 1.1962 1.1405 1.0841 -0.0033 0.0145  -0.0301 308  THR   E OG1 
13681 C  CG2 . THR   E 308 ? 1.2548 1.1809 1.1206 0.0019  0.0252  -0.0283 308  THR   E CG2 
13682 N  N   . SER   E 309 ? 1.1986 1.1665 1.1147 -0.0091 0.0129  -0.0274 309  SER   E N   
13683 C  CA  . SER   E 309 ? 1.2103 1.1904 1.1410 -0.0122 0.0076  -0.0277 309  SER   E CA  
13684 C  C   . SER   E 309 ? 1.2261 1.2054 1.1564 -0.0120 0.0036  -0.0297 309  SER   E C   
13685 O  O   . SER   E 309 ? 1.2589 1.2276 1.1759 -0.0104 0.0026  -0.0306 309  SER   E O   
13686 C  CB  . SER   E 309 ? 1.1834 1.1650 1.1130 -0.0157 0.0008  -0.0265 309  SER   E CB  
13687 O  OG  . SER   E 309 ? 1.1861 1.1704 1.1187 -0.0161 0.0043  -0.0247 309  SER   E OG  
13688 N  N   . ILE   E 310 ? 1.2520 1.2424 1.1968 -0.0135 0.0013  -0.0302 310  ILE   E N   
13689 C  CA  . ILE   E 310 ? 1.2587 1.2495 1.2047 -0.0136 -0.0027 -0.0319 310  ILE   E CA  
13690 C  C   . ILE   E 310 ? 1.2486 1.2315 1.1828 -0.0157 -0.0099 -0.0319 310  ILE   E C   
13691 O  O   . ILE   E 310 ? 1.2375 1.2248 1.1757 -0.0191 -0.0156 -0.0311 310  ILE   E O   
13692 C  CB  . ILE   E 310 ? 1.2306 1.2342 1.1933 -0.0149 -0.0045 -0.0321 310  ILE   E CB  
13693 C  CG1 . ILE   E 310 ? 1.2183 1.2297 1.1930 -0.0131 0.0022  -0.0320 310  ILE   E CG1 
13694 C  CG2 . ILE   E 310 ? 1.2663 1.2696 1.2300 -0.0140 -0.0071 -0.0339 310  ILE   E CG2 
13695 C  CD1 . ILE   E 310 ? 1.2181 1.2411 1.2088 -0.0136 0.0007  -0.0327 310  ILE   E CD1 
13696 N  N   . ALA   E 311 ? 1.1985 1.1695 1.1184 -0.0138 -0.0097 -0.0329 311  ALA   E N   
13697 C  CA  . ALA   E 311 ? 1.1667 1.1281 1.0735 -0.0154 -0.0158 -0.0329 311  ALA   E CA  
13698 C  C   . ALA   E 311 ? 1.1886 1.1503 1.0966 -0.0176 -0.0225 -0.0339 311  ALA   E C   
13699 O  O   . ALA   E 311 ? 1.2066 1.1682 1.1164 -0.0160 -0.0214 -0.0352 311  ALA   E O   
13700 C  CB  . ALA   E 311 ? 1.2096 1.1569 1.0993 -0.0121 -0.0129 -0.0335 311  ALA   E CB  
13701 N  N   . GLU   E 312 ? 1.2038 1.1662 1.1118 -0.0212 -0.0292 -0.0332 312  GLU   E N   
13702 C  CA  . GLU   E 312 ? 1.1979 1.1588 1.1057 -0.0236 -0.0357 -0.0339 312  GLU   E CA  
13703 C  C   . GLU   E 312 ? 1.2023 1.1491 1.0937 -0.0230 -0.0391 -0.0351 312  GLU   E C   
13704 O  O   . GLU   E 312 ? 1.2662 1.2073 1.1528 -0.0220 -0.0399 -0.0366 312  GLU   E O   
13705 C  CB  . GLU   E 312 ? 1.1871 1.1559 1.1038 -0.0278 -0.0410 -0.0326 312  GLU   E CB  
13706 C  CG  . GLU   E 312 ? 1.1909 1.1597 1.1100 -0.0307 -0.0470 -0.0330 312  GLU   E CG  
13707 C  CD  . GLU   E 312 ? 1.3091 1.2818 1.2346 -0.0297 -0.0451 -0.0339 312  GLU   E CD  
13708 O  OE1 . GLU   E 312 ? 1.3255 1.3023 1.2555 -0.0268 -0.0395 -0.0342 312  GLU   E OE1 
13709 O  OE2 . GLU   E 312 ? 1.4103 1.3817 1.3366 -0.0318 -0.0494 -0.0342 312  GLU   E OE2 
13710 N  N   . CYS   E 313 ? 1.2021 1.1425 1.0844 -0.0234 -0.0413 -0.0346 313  CYS   E N   
13711 C  CA  . CYS   E 313 ? 1.2461 1.1720 1.1116 -0.0224 -0.0449 -0.0359 313  CYS   E CA  
13712 C  C   . CYS   E 313 ? 1.2816 1.1994 1.1354 -0.0187 -0.0396 -0.0356 313  CYS   E C   
13713 O  O   . CYS   E 313 ? 1.2721 1.1955 1.1306 -0.0185 -0.0361 -0.0340 313  CYS   E O   
13714 C  CB  . CYS   E 313 ? 1.2888 1.2129 1.1530 -0.0263 -0.0538 -0.0357 313  CYS   E CB  
13715 S  SG  . CYS   E 313 ? 1.4081 1.3341 1.2718 -0.0272 -0.0551 -0.0340 313  CYS   E SG  
13716 N  N   . LEU   E 314 ? 1.2664 1.1708 1.1047 -0.0156 -0.0388 -0.0370 314  LEU   E N   
13717 C  CA  . LEU   E 314 ? 1.2274 1.1219 1.0521 -0.0117 -0.0338 -0.0367 314  LEU   E CA  
13718 C  C   . LEU   E 314 ? 1.2851 1.1641 1.0913 -0.0111 -0.0400 -0.0378 314  LEU   E C   
13719 O  O   . LEU   E 314 ? 1.3366 1.2099 1.1382 -0.0122 -0.0459 -0.0395 314  LEU   E O   
13720 C  CB  . LEU   E 314 ? 1.2109 1.1023 1.0325 -0.0073 -0.0253 -0.0373 314  LEU   E CB  
13721 C  CG  . LEU   E 314 ? 1.2014 1.1045 1.0368 -0.0062 -0.0169 -0.0360 314  LEU   E CG  
13722 C  CD1 . LEU   E 314 ? 1.1910 1.0892 1.0217 -0.0014 -0.0087 -0.0368 314  LEU   E CD1 
13723 C  CD2 . LEU   E 314 ? 1.1916 1.0969 1.0276 -0.0067 -0.0148 -0.0340 314  LEU   E CD2 
13724 N  N   . THR   E 315 ? 1.3185 1.1899 1.1136 -0.0091 -0.0385 -0.0370 315  THR   E N   
13725 C  CA  . THR   E 315 ? 1.3450 1.2003 1.1210 -0.0078 -0.0444 -0.0383 315  THR   E CA  
13726 C  C   . THR   E 315 ? 1.3547 1.2000 1.1163 -0.0034 -0.0384 -0.0374 315  THR   E C   
13727 O  O   . THR   E 315 ? 1.3622 1.2137 1.1294 -0.0036 -0.0346 -0.0354 315  THR   E O   
13728 C  CB  . THR   E 315 ? 1.3239 1.1816 1.1036 -0.0123 -0.0550 -0.0384 315  THR   E CB  
13729 O  OG1 . THR   E 315 ? 1.3701 1.2119 1.1312 -0.0108 -0.0612 -0.0397 315  THR   E OG1 
13730 C  CG2 . THR   E 315 ? 1.2980 1.1679 1.0903 -0.0147 -0.0544 -0.0363 315  THR   E CG2 
13731 N  N   . TYR   E 316 ? 1.3476 1.1773 1.0908 0.0009  -0.0366 -0.0387 316  TYR   E N   
13732 C  CA  . TYR   E 316 ? 1.3603 1.1781 1.0873 0.0055  -0.0309 -0.0378 316  TYR   E CA  
13733 C  C   . TYR   E 316 ? 1.3972 1.2042 1.1105 0.0051  -0.0396 -0.0382 316  TYR   E C   
13734 O  O   . TYR   E 316 ? 1.4235 1.2239 1.1307 0.0036  -0.0490 -0.0402 316  TYR   E O   
13735 C  CB  . TYR   E 316 ? 1.4495 1.2543 1.1617 0.0106  -0.0249 -0.0389 316  TYR   E CB  
13736 C  CG  . TYR   E 316 ? 1.5125 1.3010 1.2035 0.0158  -0.0202 -0.0382 316  TYR   E CG  
13737 C  CD1 . TYR   E 316 ? 1.5120 1.3034 1.2050 0.0177  -0.0110 -0.0358 316  TYR   E CD1 
13738 C  CD2 . TYR   E 316 ? 1.5499 1.3193 1.2182 0.0191  -0.0248 -0.0401 316  TYR   E CD2 
13739 C  CE1 . TYR   E 316 ? 1.5833 1.3588 1.2560 0.0227  -0.0061 -0.0350 316  TYR   E CE1 
13740 C  CE2 . TYR   E 316 ? 1.5591 1.3123 1.2065 0.0243  -0.0203 -0.0395 316  TYR   E CE2 
13741 C  CZ  . TYR   E 316 ? 1.6047 1.3610 1.2543 0.0261  -0.0107 -0.0368 316  TYR   E CZ  
13742 O  OH  . TYR   E 316 ? 1.7031 1.4428 1.3314 0.0314  -0.0058 -0.0360 316  TYR   E OH  
13743 N  N   . LEU   E 317 ? 1.4060 1.2112 1.1150 0.0064  -0.0366 -0.0364 317  LEU   E N   
13744 C  CA  . LEU   E 317 ? 1.4406 1.2355 1.1364 0.0065  -0.0448 -0.0368 317  LEU   E CA  
13745 C  C   . LEU   E 317 ? 1.5719 1.3452 1.2411 0.0123  -0.0431 -0.0376 317  LEU   E C   
13746 O  O   . LEU   E 317 ? 1.5865 1.3476 1.2427 0.0134  -0.0497 -0.0400 317  LEU   E O   
13747 C  CB  . LEU   E 317 ? 1.4026 1.2066 1.1073 0.0047  -0.0435 -0.0344 317  LEU   E CB  
13748 C  CG  . LEU   E 317 ? 1.3732 1.1979 1.1033 -0.0008 -0.0453 -0.0335 317  LEU   E CG  
13749 C  CD1 . LEU   E 317 ? 1.3362 1.1681 1.0730 -0.0022 -0.0448 -0.0313 317  LEU   E CD1 
13750 C  CD2 . LEU   E 317 ? 1.3435 1.1716 1.0800 -0.0050 -0.0564 -0.0354 317  LEU   E CD2 
13751 N  N   . ASP   E 318 ? 1.7004 1.4683 1.3611 0.0162  -0.0341 -0.0356 318  ASP   E N   
13752 C  CA  . ASP   E 318 ? 1.7054 1.4522 1.3400 0.0223  -0.0310 -0.0360 318  ASP   E CA  
13753 C  C   . ASP   E 318 ? 1.7110 1.4570 1.3430 0.0256  -0.0189 -0.0331 318  ASP   E C   
13754 O  O   . ASP   E 318 ? 1.7010 1.4611 1.3493 0.0228  -0.0154 -0.0310 318  ASP   E O   
13755 C  CB  . ASP   E 318 ? 1.7276 1.4598 1.3444 0.0231  -0.0423 -0.0375 318  ASP   E CB  
13756 C  CG  . ASP   E 318 ? 1.8283 1.5385 1.4190 0.0287  -0.0426 -0.0393 318  ASP   E CG  
13757 O  OD1 . ASP   E 318 ? 1.8474 1.5555 1.4365 0.0310  -0.0357 -0.0398 318  ASP   E OD1 
13758 O  OD2 . ASP   E 318 ? 1.9426 1.6373 1.5143 0.0311  -0.0495 -0.0403 318  ASP   E OD2 
13759 N  N   . ASN   E 319 ? 1.6940 1.4225 1.3046 0.0316  -0.0124 -0.0330 319  ASN   E N   
13760 C  CA  . ASN   E 319 ? 1.7194 1.4440 1.3244 0.0353  -0.0004 -0.0302 319  ASN   E CA  
13761 C  C   . ASN   E 319 ? 1.6763 1.4194 1.3049 0.0333  0.0100  -0.0283 319  ASN   E C   
13762 O  O   . ASN   E 319 ? 1.6316 1.3790 1.2651 0.0337  0.0180  -0.0256 319  ASN   E O   
13763 C  CB  . ASN   E 319 ? 1.7622 1.4826 1.3602 0.0351  -0.0045 -0.0288 319  ASN   E CB  
13764 C  CG  . ASN   E 319 ? 1.7907 1.4946 1.3682 0.0366  -0.0167 -0.0311 319  ASN   E CG  
13765 O  OD1 . ASN   E 319 ? 1.8144 1.5032 1.3743 0.0402  -0.0184 -0.0330 319  ASN   E OD1 
13766 N  ND2 . ASN   E 319 ? 1.7957 1.5024 1.3756 0.0338  -0.0256 -0.0310 319  ASN   E ND2 
13767 N  N   . GLY   E 320 ? 1.6735 1.4278 1.3171 0.0309  0.0095  -0.0296 320  GLY   E N   
13768 C  CA  . GLY   E 320 ? 1.6396 1.4104 1.3048 0.0294  0.0186  -0.0284 320  GLY   E CA  
13769 C  C   . GLY   E 320 ? 1.5365 1.3282 1.2270 0.0232  0.0139  -0.0281 320  GLY   E C   
13770 O  O   . GLY   E 320 ? 1.5424 1.3482 1.2517 0.0218  0.0199  -0.0277 320  GLY   E O   
13771 N  N   . VAL   E 321 ? 1.5297 1.3238 1.2215 0.0196  0.0034  -0.0284 321  VAL   E N   
13772 C  CA  . VAL   E 321 ? 1.4634 1.2766 1.1782 0.0142  0.0002  -0.0276 321  VAL   E CA  
13773 C  C   . VAL   E 321 ? 1.4282 1.2509 1.1554 0.0103  -0.0078 -0.0296 321  VAL   E C   
13774 O  O   . VAL   E 321 ? 1.4140 1.2297 1.1327 0.0092  -0.0177 -0.0315 321  VAL   E O   
13775 C  CB  . VAL   E 321 ? 1.4390 1.2510 1.1503 0.0125  -0.0057 -0.0265 321  VAL   E CB  
13776 C  CG1 . VAL   E 321 ? 1.4168 1.2479 1.1512 0.0081  -0.0051 -0.0249 321  VAL   E CG1 
13777 C  CG2 . VAL   E 321 ? 1.5858 1.3834 1.2789 0.0172  0.0010  -0.0248 321  VAL   E CG2 
13778 N  N   . VAL   E 322 ? 1.3736 1.2122 1.1212 0.0081  -0.0036 -0.0293 322  VAL   E N   
13779 C  CA  . VAL   E 322 ? 1.3168 1.1656 1.0780 0.0046  -0.0095 -0.0309 322  VAL   E CA  
13780 C  C   . VAL   E 322 ? 1.2649 1.1292 1.0442 -0.0004 -0.0143 -0.0299 322  VAL   E C   
13781 O  O   . VAL   E 322 ? 1.3049 1.1783 1.0948 -0.0010 -0.0088 -0.0280 322  VAL   E O   
13782 C  CB  . VAL   E 322 ? 1.2914 1.1469 1.0627 0.0061  -0.0016 -0.0313 322  VAL   E CB  
13783 C  CG1 . VAL   E 322 ? 1.2792 1.1407 1.0590 0.0034  -0.0079 -0.0332 322  VAL   E CG1 
13784 C  CG2 . VAL   E 322 ? 1.3373 1.1788 1.0924 0.0117  0.0062  -0.0316 322  VAL   E CG2 
13785 N  N   . PHE   E 323 ? 1.2191 1.0866 1.0026 -0.0041 -0.0242 -0.0311 323  PHE   E N   
13786 C  CA  . PHE   E 323 ? 1.2132 1.0961 1.0150 -0.0088 -0.0283 -0.0302 323  PHE   E CA  
13787 C  C   . PHE   E 323 ? 1.2115 1.1072 1.0303 -0.0104 -0.0261 -0.0307 323  PHE   E C   
13788 O  O   . PHE   E 323 ? 1.2465 1.1389 1.0630 -0.0102 -0.0283 -0.0324 323  PHE   E O   
13789 C  CB  . PHE   E 323 ? 1.1881 1.0692 0.9878 -0.0120 -0.0397 -0.0310 323  PHE   E CB  
13790 C  CG  . PHE   E 323 ? 1.2200 1.1173 1.0394 -0.0168 -0.0435 -0.0301 323  PHE   E CG  
13791 C  CD1 . PHE   E 323 ? 1.2064 1.1136 1.0362 -0.0176 -0.0397 -0.0281 323  PHE   E CD1 
13792 C  CD2 . PHE   E 323 ? 1.2167 1.1191 1.0442 -0.0202 -0.0506 -0.0313 323  PHE   E CD2 
13793 C  CE1 . PHE   E 323 ? 1.1140 1.0355 0.9611 -0.0216 -0.0430 -0.0273 323  PHE   E CE1 
13794 C  CE2 . PHE   E 323 ? 1.1787 1.0954 1.0237 -0.0242 -0.0534 -0.0303 323  PHE   E CE2 
13795 C  CZ  . PHE   E 323 ? 1.0858 1.0119 0.9401 -0.0248 -0.0496 -0.0283 323  PHE   E CZ  
13796 N  N   . VAL   E 324 ? 1.1842 1.0937 1.0195 -0.0119 -0.0219 -0.0293 324  VAL   E N   
13797 C  CA  . VAL   E 324 ? 1.1502 1.0724 1.0024 -0.0134 -0.0201 -0.0296 324  VAL   E CA  
13798 C  C   . VAL   E 324 ? 1.1367 1.0699 1.0018 -0.0180 -0.0271 -0.0291 324  VAL   E C   
13799 O  O   . VAL   E 324 ? 1.1728 1.1128 1.0448 -0.0195 -0.0271 -0.0276 324  VAL   E O   
13800 C  CB  . VAL   E 324 ? 1.0878 1.0174 0.9497 -0.0114 -0.0103 -0.0286 324  VAL   E CB  
13801 C  CG1 . VAL   E 324 ? 1.0868 1.0266 0.9631 -0.0118 -0.0085 -0.0296 324  VAL   E CG1 
13802 C  CG2 . VAL   E 324 ? 1.1446 1.0623 0.9925 -0.0069 -0.0030 -0.0285 324  VAL   E CG2 
13803 N  N   . GLY   E 325 ? 1.1370 1.0714 1.0049 -0.0201 -0.0331 -0.0304 325  GLY   E N   
13804 C  CA  . GLY   E 325 ? 1.1292 1.0745 1.0105 -0.0243 -0.0387 -0.0299 325  GLY   E CA  
13805 C  C   . GLY   E 325 ? 1.1409 1.0985 1.0380 -0.0246 -0.0347 -0.0298 325  GLY   E C   
13806 O  O   . GLY   E 325 ? 1.1690 1.1253 1.0661 -0.0230 -0.0326 -0.0311 325  GLY   E O   
13807 N  N   . SER   E 326 ? 1.1171 1.0862 1.0272 -0.0264 -0.0339 -0.0283 326  SER   E N   
13808 C  CA  . SER   E 326 ? 1.1179 1.0983 1.0426 -0.0261 -0.0297 -0.0282 326  SER   E CA  
13809 C  C   . SER   E 326 ? 1.1312 1.1222 1.0687 -0.0296 -0.0344 -0.0275 326  SER   E C   
13810 O  O   . SER   E 326 ? 1.0578 1.0512 0.9968 -0.0318 -0.0377 -0.0262 326  SER   E O   
13811 C  CB  . SER   E 326 ? 1.1275 1.1118 1.0566 -0.0241 -0.0223 -0.0272 326  SER   E CB  
13812 O  OG  . SER   E 326 ? 1.1205 1.1142 1.0627 -0.0233 -0.0183 -0.0276 326  SER   E OG  
13813 N  N   . ARG   E 327 ? 1.1352 1.1319 1.0812 -0.0298 -0.0345 -0.0282 327  ARG   E N   
13814 C  CA  . ARG   E 327 ? 1.1017 1.1083 1.0600 -0.0325 -0.0378 -0.0275 327  ARG   E CA  
13815 C  C   . ARG   E 327 ? 1.0641 1.0815 1.0353 -0.0317 -0.0336 -0.0270 327  ARG   E C   
13816 O  O   . ARG   E 327 ? 1.0265 1.0521 1.0073 -0.0337 -0.0359 -0.0260 327  ARG   E O   
13817 C  CB  . ARG   E 327 ? 1.1249 1.1302 1.0837 -0.0330 -0.0407 -0.0287 327  ARG   E CB  
13818 C  CG  . ARG   E 327 ? 1.1916 1.1905 1.1436 -0.0357 -0.0471 -0.0288 327  ARG   E CG  
13819 C  CD  . ARG   E 327 ? 1.2190 1.2255 1.1804 -0.0393 -0.0516 -0.0274 327  ARG   E CD  
13820 N  NE  . ARG   E 327 ? 1.2569 1.2711 1.2288 -0.0396 -0.0508 -0.0272 327  ARG   E NE  
13821 C  CZ  . ARG   E 327 ? 1.3320 1.3436 1.3032 -0.0397 -0.0522 -0.0281 327  ARG   E CZ  
13822 N  NH1 . ARG   E 327 ? 1.3394 1.3412 1.3007 -0.0400 -0.0546 -0.0292 327  ARG   E NH1 
13823 N  NH2 . ARG   E 327 ? 1.3097 1.3280 1.2898 -0.0395 -0.0512 -0.0279 327  ARG   E NH2 
13824 N  N   . LEU   E 328 ? 1.0718 1.0892 1.0438 -0.0287 -0.0275 -0.0276 328  LEU   E N   
13825 C  CA  . LEU   E 328 ? 1.0584 1.0855 1.0430 -0.0277 -0.0235 -0.0274 328  LEU   E CA  
13826 C  C   . LEU   E 328 ? 1.0726 1.1014 1.0585 -0.0276 -0.0199 -0.0260 328  LEU   E C   
13827 O  O   . LEU   E 328 ? 1.0858 1.1234 1.0823 -0.0286 -0.0197 -0.0252 328  LEU   E O   
13828 C  CB  . LEU   E 328 ? 1.0441 1.0711 1.0312 -0.0245 -0.0190 -0.0290 328  LEU   E CB  
13829 C  CG  . LEU   E 328 ? 0.9560 0.9821 0.9431 -0.0243 -0.0222 -0.0304 328  LEU   E CG  
13830 C  CD1 . LEU   E 328 ? 0.9796 1.0079 0.9721 -0.0210 -0.0180 -0.0320 328  LEU   E CD1 
13831 C  CD2 . LEU   E 328 ? 0.9412 0.9744 0.9362 -0.0269 -0.0269 -0.0295 328  LEU   E CD2 
13832 N  N   . GLY   E 329 ? 1.0908 1.1110 1.0657 -0.0262 -0.0171 -0.0258 329  GLY   E N   
13833 C  CA  . GLY   E 329 ? 1.1030 1.1237 1.0779 -0.0261 -0.0136 -0.0243 329  GLY   E CA  
13834 C  C   . GLY   E 329 ? 1.1062 1.1187 1.0687 -0.0272 -0.0169 -0.0233 329  GLY   E C   
13835 O  O   . GLY   E 329 ? 1.0896 1.0988 1.0468 -0.0290 -0.0232 -0.0236 329  GLY   E O   
13836 N  N   . ASP   E 330 ? 1.2090 1.2179 1.1667 -0.0262 -0.0129 -0.0221 330  ASP   E N   
13837 C  CA  . ASP   E 330 ? 1.2122 1.2120 1.1566 -0.0266 -0.0161 -0.0213 330  ASP   E CA  
13838 C  C   . ASP   E 330 ? 1.2317 1.2191 1.1610 -0.0248 -0.0171 -0.0226 330  ASP   E C   
13839 O  O   . ASP   E 330 ? 1.2472 1.2309 1.1736 -0.0222 -0.0118 -0.0235 330  ASP   E O   
13840 C  CB  . ASP   E 330 ? 1.2553 1.2529 1.1968 -0.0255 -0.0110 -0.0197 330  ASP   E CB  
13841 C  CG  . ASP   E 330 ? 1.2683 1.2766 1.2226 -0.0276 -0.0114 -0.0184 330  ASP   E CG  
13842 O  OD1 . ASP   E 330 ? 1.2729 1.2890 1.2359 -0.0300 -0.0169 -0.0185 330  ASP   E OD1 
13843 O  OD2 . ASP   E 330 ? 1.2907 1.2994 1.2464 -0.0267 -0.0060 -0.0171 330  ASP   E OD2 
13844 N  N   . SER   E 331 ? 1.1997 1.1809 1.1200 -0.0263 -0.0240 -0.0228 331  SER   E N   
13845 C  CA  . SER   E 331 ? 1.0270 0.9943 0.9303 -0.0243 -0.0252 -0.0238 331  SER   E CA  
13846 C  C   . SER   E 331 ? 1.0947 1.0534 0.9868 -0.0216 -0.0200 -0.0228 331  SER   E C   
13847 O  O   . SER   E 331 ? 1.1903 1.1532 1.0867 -0.0220 -0.0177 -0.0212 331  SER   E O   
13848 C  CB  . SER   E 331 ? 1.0417 1.0048 0.9393 -0.0267 -0.0345 -0.0243 331  SER   E CB  
13849 O  OG  . SER   E 331 ? 1.1291 1.1026 1.0400 -0.0300 -0.0390 -0.0244 331  SER   E OG  
13850 N  N   . GLN   E 332 ? 1.1359 1.0818 1.0128 -0.0185 -0.0179 -0.0237 332  GLN   E N   
13851 C  CA  . GLN   E 332 ? 1.1727 1.1101 1.0390 -0.0154 -0.0114 -0.0225 332  GLN   E CA  
13852 C  C   . GLN   E 332 ? 1.2276 1.1482 1.0733 -0.0122 -0.0116 -0.0236 332  GLN   E C   
13853 O  O   . GLN   E 332 ? 1.2202 1.1370 1.0621 -0.0117 -0.0139 -0.0254 332  GLN   E O   
13854 C  CB  . GLN   E 332 ? 1.1263 1.0706 1.0030 -0.0138 -0.0016 -0.0219 332  GLN   E CB  
13855 C  CG  . GLN   E 332 ? 1.1239 1.0707 1.0057 -0.0128 0.0007  -0.0235 332  GLN   E CG  
13856 C  CD  . GLN   E 332 ? 1.1800 1.1286 1.0667 -0.0100 0.0110  -0.0231 332  GLN   E CD  
13857 O  OE1 . GLN   E 332 ? 1.2302 1.1812 1.1221 -0.0085 0.0141  -0.0244 332  GLN   E OE1 
13858 N  NE2 . GLN   E 332 ? 1.2255 1.1728 1.1111 -0.0091 0.0165  -0.0213 332  GLN   E NE2 
13859 N  N   . LEU   E 333 ? 1.3150 1.2251 1.1469 -0.0099 -0.0091 -0.0225 333  LEU   E N   
13860 C  CA  . LEU   E 333 ? 1.2652 1.1582 1.0763 -0.0058 -0.0069 -0.0231 333  LEU   E CA  
13861 C  C   . LEU   E 333 ? 1.2897 1.1810 1.1005 -0.0023 0.0050  -0.0223 333  LEU   E C   
13862 O  O   . LEU   E 333 ? 1.3753 1.2739 1.1958 -0.0025 0.0113  -0.0205 333  LEU   E O   
13863 C  CB  . LEU   E 333 ? 1.3184 1.2000 1.1137 -0.0047 -0.0105 -0.0223 333  LEU   E CB  
13864 C  CG  . LEU   E 333 ? 1.2655 1.1431 1.0549 -0.0068 -0.0227 -0.0236 333  LEU   E CG  
13865 C  CD1 . LEU   E 333 ? 1.2083 1.0742 0.9819 -0.0051 -0.0257 -0.0229 333  LEU   E CD1 
13866 C  CD2 . LEU   E 333 ? 1.2689 1.1382 1.0493 -0.0059 -0.0266 -0.0260 333  LEU   E CD2 
13867 N  N   . VAL   E 334 ? 1.2807 1.1624 1.0809 0.0010  0.0081  -0.0235 334  VAL   E N   
13868 C  CA  . VAL   E 334 ? 1.3536 1.2320 1.1520 0.0049  0.0198  -0.0228 334  VAL   E CA  
13869 C  C   . VAL   E 334 ? 1.3992 1.2578 1.1730 0.0095  0.0218  -0.0231 334  VAL   E C   
13870 O  O   . VAL   E 334 ? 1.4130 1.2626 1.1750 0.0101  0.0150  -0.0250 334  VAL   E O   
13871 C  CB  . VAL   E 334 ? 1.2889 1.1773 1.1021 0.0049  0.0238  -0.0239 334  VAL   E CB  
13872 C  CG1 . VAL   E 334 ? 1.2825 1.1891 1.1190 0.0014  0.0244  -0.0232 334  VAL   E CG1 
13873 C  CG2 . VAL   E 334 ? 1.3130 1.1989 1.1227 0.0042  0.0164  -0.0264 334  VAL   E CG2 
13874 N  N   . LYS   E 335 ? 1.4251 1.2765 1.1910 0.0128  0.0310  -0.0213 335  LYS   E N   
13875 C  CA  . LYS   E 335 ? 1.4797 1.3123 1.2229 0.0181  0.0356  -0.0214 335  LYS   E CA  
13876 C  C   . LYS   E 335 ? 1.5175 1.3513 1.2652 0.0209  0.0446  -0.0220 335  LYS   E C   
13877 O  O   . LYS   E 335 ? 1.5379 1.3841 1.3036 0.0201  0.0520  -0.0211 335  LYS   E O   
13878 C  CB  . LYS   E 335 ? 1.5585 1.3822 1.2907 0.0206  0.0419  -0.0189 335  LYS   E CB  
13879 C  CG  . LYS   E 335 ? 1.5811 1.3854 1.2904 0.0266  0.0492  -0.0185 335  LYS   E CG  
13880 C  CD  . LYS   E 335 ? 1.6092 1.3969 1.2955 0.0284  0.0396  -0.0202 335  LYS   E CD  
13881 C  CE  . LYS   E 335 ? 1.6758 1.4438 1.3387 0.0347  0.0465  -0.0201 335  LYS   E CE  
13882 N  NZ  . LYS   E 335 ? 1.7787 1.5503 1.4489 0.0366  0.0548  -0.0207 335  LYS   E NZ  
13883 N  N   . LEU   E 336 ? 1.5674 1.3881 1.2991 0.0243  0.0437  -0.0237 336  LEU   E N   
13884 C  CA  . LEU   E 336 ? 1.6105 1.4301 1.3436 0.0277  0.0523  -0.0244 336  LEU   E CA  
13885 C  C   . LEU   E 336 ? 1.7597 1.5628 1.4737 0.0334  0.0623  -0.0229 336  LEU   E C   
13886 O  O   . LEU   E 336 ? 1.8332 1.6185 1.5239 0.0367  0.0594  -0.0236 336  LEU   E O   
13887 C  CB  . LEU   E 336 ? 1.5895 1.4055 1.3178 0.0280  0.0455  -0.0272 336  LEU   E CB  
13888 C  CG  . LEU   E 336 ? 1.4645 1.2936 1.2079 0.0227  0.0350  -0.0288 336  LEU   E CG  
13889 C  CD1 . LEU   E 336 ? 1.3703 1.1967 1.1115 0.0236  0.0319  -0.0313 336  LEU   E CD1 
13890 C  CD2 . LEU   E 336 ? 1.4714 1.3201 1.2400 0.0193  0.0380  -0.0277 336  LEU   E CD2 
13891 N  N   . ASN   E 337 ? 1.8698 1.6783 1.5936 0.0347  0.0740  -0.0208 337  ASN   E N   
13892 C  CA  . ASN   E 337 ? 1.9137 1.7072 1.6211 0.0403  0.0852  -0.0192 337  ASN   E CA  
13893 C  C   . ASN   E 337 ? 1.9789 1.7679 1.6834 0.0443  0.0915  -0.0206 337  ASN   E C   
13894 O  O   . ASN   E 337 ? 1.9892 1.7908 1.7106 0.0426  0.0902  -0.0222 337  ASN   E O   
13895 C  CB  . ASN   E 337 ? 1.9281 1.7289 1.6478 0.0399  0.0958  -0.0163 337  ASN   E CB  
13896 C  CG  . ASN   E 337 ? 1.9354 1.7386 1.6556 0.0366  0.0905  -0.0147 337  ASN   E CG  
13897 O  OD1 . ASN   E 337 ? 1.9643 1.7550 1.6655 0.0372  0.0830  -0.0149 337  ASN   E OD1 
13898 N  ND2 . ASN   E 337 ? 1.8907 1.7096 1.6325 0.0331  0.0939  -0.0133 337  ASN   E ND2 
13899 N  N   . VAL   E 338 ? 2.0938 1.8640 1.7757 0.0501  0.0981  -0.0199 338  VAL   E N   
13900 C  CA  . VAL   E 338 ? 2.1014 1.8657 1.7788 0.0546  0.1050  -0.0211 338  VAL   E CA  
13901 C  C   . VAL   E 338 ? 2.1304 1.9017 1.8218 0.0566  0.1201  -0.0190 338  VAL   E C   
13902 O  O   . VAL   E 338 ? 2.1435 1.9090 1.8309 0.0611  0.1288  -0.0192 338  VAL   E O   
13903 C  CB  . VAL   E 338 ? 2.0725 1.8124 1.7182 0.0604  0.1050  -0.0216 338  VAL   E CB  
13904 C  CG1 . VAL   E 338 ? 2.1114 1.8446 1.7444 0.0584  0.0898  -0.0240 338  VAL   E CG1 
13905 C  CG2 . VAL   E 338 ? 2.0547 1.7809 1.6840 0.0640  0.1133  -0.0187 338  VAL   E CG2 
13906 N  N   . ASP   E 339 ? 2.1675 1.9511 1.8756 0.0532  0.1232  -0.0169 339  ASP   E N   
13907 C  CA  . ASP   E 339 ? 2.1897 1.9808 1.9132 0.0544  0.1371  -0.0149 339  ASP   E CA  
13908 C  C   . ASP   E 339 ? 2.1838 1.9982 1.9382 0.0488  0.1351  -0.0151 339  ASP   E C   
13909 O  O   . ASP   E 339 ? 2.1455 1.9674 1.9063 0.0443  0.1272  -0.0147 339  ASP   E O   
13910 C  CB  . ASP   E 339 ? 2.2484 2.0278 1.9588 0.0567  0.1456  -0.0116 339  ASP   E CB  
13911 C  CG  . ASP   E 339 ? 2.3271 2.0838 2.0098 0.0636  0.1528  -0.0110 339  ASP   E CG  
13912 O  OD1 . ASP   E 339 ? 2.3371 2.0789 1.9964 0.0653  0.1443  -0.0123 339  ASP   E OD1 
13913 O  OD2 . ASP   E 339 ? 2.3675 2.1213 2.0520 0.0673  0.1669  -0.0092 339  ASP   E OD2 
13914 N  N   . SER   E 340 ? 2.1253 1.9509 1.8987 0.0495  0.1419  -0.0158 340  SER   E N   
13915 C  CA  . SER   E 340 ? 2.0770 1.9242 1.8801 0.0450  0.1409  -0.0161 340  SER   E CA  
13916 C  C   . SER   E 340 ? 2.1038 1.9559 1.9157 0.0427  0.1462  -0.0133 340  SER   E C   
13917 O  O   . SER   E 340 ? 2.1321 1.9743 1.9350 0.0458  0.1570  -0.0108 340  SER   E O   
13918 C  CB  . SER   E 340 ? 2.0836 1.9397 1.9039 0.0471  0.1487  -0.0173 340  SER   E CB  
13919 O  OG  . SER   E 340 ? 2.0915 1.9381 1.9051 0.0520  0.1629  -0.0154 340  SER   E OG  
13920 N  N   . ASN   E 341 ? 2.0970 1.9640 1.9262 0.0374  0.1389  -0.0136 341  ASN   E N   
13921 C  CA  . ASN   E 341 ? 2.1279 2.0005 1.9666 0.0348  0.1430  -0.0111 341  ASN   E CA  
13922 C  C   . ASN   E 341 ? 2.1850 2.0733 2.0513 0.0339  0.1516  -0.0109 341  ASN   E C   
13923 O  O   . ASN   E 341 ? 2.1627 2.0533 2.0361 0.0366  0.1572  -0.0121 341  ASN   E O   
13924 C  CB  . ASN   E 341 ? 2.0469 1.9253 1.8871 0.0299  0.1305  -0.0113 341  ASN   E CB  
13925 C  CG  . ASN   E 341 ? 2.0262 1.9218 1.8866 0.0259  0.1214  -0.0138 341  ASN   E CG  
13926 O  OD1 . ASN   E 341 ? 2.1109 2.0177 1.9898 0.0260  0.1251  -0.0150 341  ASN   E OD1 
13927 N  ND2 . ASN   E 341 ? 1.8913 1.7889 1.7481 0.0226  0.1093  -0.0146 341  ASN   E ND2 
13928 N  N   . GLU   E 342 ? 2.3236 2.2223 2.2054 0.0302  0.1524  -0.0094 342  GLU   E N   
13929 C  CA  . GLU   E 342 ? 2.3449 2.2590 2.2541 0.0289  0.1594  -0.0094 342  GLU   E CA  
13930 C  C   . GLU   E 342 ? 2.3792 2.3074 2.3063 0.0275  0.1527  -0.0127 342  GLU   E C   
13931 O  O   . GLU   E 342 ? 2.4018 2.3362 2.3428 0.0295  0.1593  -0.0138 342  GLU   E O   
13932 C  CB  . GLU   E 342 ? 2.2892 2.2114 2.2107 0.0247  0.1593  -0.0076 342  GLU   E CB  
13933 N  N   . GLN   E 343 ? 2.1927 2.1260 2.1194 0.0243  0.1397  -0.0144 343  GLN   E N   
13934 C  CA  . GLN   E 343 ? 2.1246 2.0695 2.0650 0.0231  0.1322  -0.0174 343  GLN   E CA  
13935 C  C   . GLN   E 343 ? 2.0964 2.0323 2.0229 0.0268  0.1305  -0.0193 343  GLN   E C   
13936 O  O   . GLN   E 343 ? 2.0854 2.0284 2.0187 0.0258  0.1227  -0.0218 343  GLN   E O   
13937 C  CB  . GLN   E 343 ? 2.0270 1.9797 1.9711 0.0184  0.1194  -0.0181 343  GLN   E CB  
13938 N  N   . GLY   E 344 ? 2.1063 2.0265 2.0134 0.0310  0.1377  -0.0182 344  GLY   E N   
13939 C  CA  . GLY   E 344 ? 2.0734 1.9834 1.9651 0.0347  0.1360  -0.0200 344  GLY   E CA  
13940 C  C   . GLY   E 344 ? 2.0402 1.9463 1.9193 0.0327  0.1225  -0.0216 344  GLY   E C   
13941 O  O   . GLY   E 344 ? 2.0091 1.9134 1.8845 0.0343  0.1185  -0.0239 344  GLY   E O   
13942 N  N   . SER   E 345 ? 1.9495 1.8545 1.8226 0.0293  0.1155  -0.0205 345  SER   E N   
13943 C  CA  . SER   E 345 ? 1.7782 1.6816 1.6428 0.0266  0.1024  -0.0219 345  SER   E CA  
13944 C  C   . SER   E 345 ? 1.7508 1.6359 1.5883 0.0284  0.1005  -0.0209 345  SER   E C   
13945 O  O   . SER   E 345 ? 1.7836 1.6654 1.6156 0.0271  0.1005  -0.0189 345  SER   E O   
13946 C  CB  . SER   E 345 ? 1.7397 1.6577 1.6208 0.0213  0.0952  -0.0217 345  SER   E CB  
13947 O  OG  . SER   E 345 ? 1.5645 1.4819 1.4390 0.0184  0.0829  -0.0228 345  SER   E OG  
13948 N  N   . TYR   E 346 ? 1.6977 1.5703 1.5179 0.0316  0.0987  -0.0224 346  TYR   E N   
13949 C  CA  . TYR   E 346 ? 1.7353 1.5902 1.5293 0.0332  0.0944  -0.0220 346  TYR   E CA  
13950 C  C   . TYR   E 346 ? 1.6483 1.5060 1.4410 0.0286  0.0822  -0.0221 346  TYR   E C   
13951 O  O   . TYR   E 346 ? 1.6485 1.4935 1.4225 0.0292  0.0788  -0.0213 346  TYR   E O   
13952 C  CB  . TYR   E 346 ? 1.7133 1.5562 1.4916 0.0369  0.0926  -0.0241 346  TYR   E CB  
13953 C  CG  . TYR   E 346 ? 1.8321 1.6704 1.6093 0.0420  0.1050  -0.0238 346  TYR   E CG  
13954 C  CD1 . TYR   E 346 ? 1.8452 1.6970 1.6435 0.0421  0.1097  -0.0248 346  TYR   E CD1 
13955 C  CD2 . TYR   E 346 ? 1.9903 1.8104 1.7455 0.0470  0.1122  -0.0226 346  TYR   E CD2 
13956 C  CE1 . TYR   E 346 ? 1.9472 1.7954 1.7459 0.0468  0.1213  -0.0245 346  TYR   E CE1 
13957 C  CE2 . TYR   E 346 ? 2.0623 1.8782 1.8169 0.0519  0.1243  -0.0222 346  TYR   E CE2 
13958 C  CZ  . TYR   E 346 ? 2.0315 1.8619 1.8086 0.0517  0.1289  -0.0232 346  TYR   E CZ  
13959 O  OH  . TYR   E 346 ? 2.0766 1.9032 1.8541 0.0566  0.1410  -0.0228 346  TYR   E OH  
13960 N  N   . VAL   E 347 ? 1.6051 1.4789 1.4171 0.0241  0.0756  -0.0231 347  VAL   E N   
13961 C  CA  . VAL   E 347 ? 1.5150 1.3936 1.3291 0.0196  0.0653  -0.0229 347  VAL   E CA  
13962 C  C   . VAL   E 347 ? 1.4973 1.3825 1.3206 0.0177  0.0694  -0.0205 347  VAL   E C   
13963 O  O   . VAL   E 347 ? 1.5141 1.4096 1.3541 0.0175  0.0770  -0.0197 347  VAL   E O   
13964 C  CB  . VAL   E 347 ? 1.4498 1.3422 1.2802 0.0158  0.0571  -0.0248 347  VAL   E CB  
13965 C  CG1 . VAL   E 347 ? 1.3904 1.2854 1.2200 0.0116  0.0462  -0.0247 347  VAL   E CG1 
13966 C  CG2 . VAL   E 347 ? 1.4357 1.3229 1.2599 0.0179  0.0549  -0.0271 347  VAL   E CG2 
13967 N  N   . VAL   E 348 ? 1.4579 1.3371 1.2704 0.0163  0.0640  -0.0194 348  VAL   E N   
13968 C  CA  . VAL   E 348 ? 1.4007 1.2856 1.2205 0.0141  0.0660  -0.0171 348  VAL   E CA  
13969 C  C   . VAL   E 348 ? 1.4011 1.2900 1.2216 0.0100  0.0539  -0.0175 348  VAL   E C   
13970 O  O   . VAL   E 348 ? 1.4449 1.3239 1.2499 0.0104  0.0462  -0.0186 348  VAL   E O   
13971 C  CB  . VAL   E 348 ? 1.4138 1.2837 1.2158 0.0177  0.0735  -0.0149 348  VAL   E CB  
13972 C  CG1 . VAL   E 348 ? 1.4312 1.3080 1.2431 0.0155  0.0771  -0.0125 348  VAL   E CG1 
13973 C  CG2 . VAL   E 348 ? 1.5426 1.4048 1.3391 0.0225  0.0848  -0.0148 348  VAL   E CG2 
13974 N  N   . ALA   E 349 ? 1.3895 1.2928 1.2280 0.0062  0.0521  -0.0167 349  ALA   E N   
13975 C  CA  . ALA   E 349 ? 1.4089 1.3166 1.2489 0.0025  0.0411  -0.0171 349  ALA   E CA  
13976 C  C   . ALA   E 349 ? 1.4657 1.3628 1.2905 0.0030  0.0393  -0.0154 349  ALA   E C   
13977 O  O   . ALA   E 349 ? 1.4741 1.3665 1.2949 0.0049  0.0473  -0.0134 349  ALA   E O   
13978 C  CB  . ALA   E 349 ? 1.4233 1.3494 1.2868 -0.0015 0.0391  -0.0169 349  ALA   E CB  
13979 N  N   . MET   E 350 ? 1.6139 1.5070 1.4302 0.0015  0.0288  -0.0163 350  MET   E N   
13980 C  CA  . MET   E 350 ? 1.6432 1.5237 1.4416 0.0027  0.0254  -0.0153 350  MET   E CA  
13981 C  C   . MET   E 350 ? 1.6342 1.5230 1.4405 -0.0013 0.0166  -0.0149 350  MET   E C   
13982 O  O   . MET   E 350 ? 1.6872 1.5701 1.4851 -0.0009 0.0158  -0.0134 350  MET   E O   
13983 C  CB  . MET   E 350 ? 1.6645 1.5291 1.4420 0.0053  0.0205  -0.0170 350  MET   E CB  
13984 C  CG  . MET   E 350 ? 1.7477 1.5957 1.5031 0.0080  0.0183  -0.0162 350  MET   E CG  
13985 S  SD  . MET   E 350 ? 1.8933 1.7227 1.6246 0.0111  0.0112  -0.0187 350  MET   E SD  
13986 C  CE  . MET   E 350 ? 1.8171 1.6264 1.5224 0.0154  0.0119  -0.0172 350  MET   E CE  
13987 N  N   . GLU   E 351 ? 1.6066 1.5083 1.4283 -0.0050 0.0103  -0.0161 351  GLU   E N   
13988 C  CA  . GLU   E 351 ? 1.5561 1.4680 1.3886 -0.0090 0.0029  -0.0157 351  GLU   E CA  
13989 C  C   . GLU   E 351 ? 1.5236 1.4514 1.3765 -0.0121 0.0012  -0.0167 351  GLU   E C   
13990 O  O   . GLU   E 351 ? 1.5403 1.4697 1.3969 -0.0111 0.0045  -0.0179 351  GLU   E O   
13991 C  CB  . GLU   E 351 ? 1.5621 1.4656 1.3819 -0.0096 -0.0077 -0.0166 351  GLU   E CB  
13992 C  CG  . GLU   E 351 ? 1.6204 1.5265 1.4416 -0.0113 -0.0122 -0.0152 351  GLU   E CG  
13993 C  CD  . GLU   E 351 ? 1.7101 1.6053 1.5163 -0.0110 -0.0220 -0.0162 351  GLU   E CD  
13994 O  OE1 . GLU   E 351 ? 1.7742 1.6546 1.5625 -0.0078 -0.0222 -0.0173 351  GLU   E OE1 
13995 O  OE2 . GLU   E 351 ? 1.7491 1.6504 1.5618 -0.0138 -0.0296 -0.0161 351  GLU   E OE2 
13996 N  N   . THR   E 352 ? 1.3077 1.2468 1.1734 -0.0156 -0.0038 -0.0161 352  THR   E N   
13997 C  CA  . THR   E 352 ? 1.2412 1.1946 1.1252 -0.0184 -0.0060 -0.0170 352  THR   E CA  
13998 C  C   . THR   E 352 ? 1.1975 1.1570 1.0870 -0.0219 -0.0154 -0.0169 352  THR   E C   
13999 O  O   . THR   E 352 ? 1.2650 1.2255 1.1544 -0.0227 -0.0168 -0.0155 352  THR   E O   
14000 C  CB  . THR   E 352 ? 1.2481 1.2126 1.1480 -0.0187 0.0015  -0.0160 352  THR   E CB  
14001 O  OG1 . THR   E 352 ? 1.4205 1.3833 1.3183 -0.0183 0.0051  -0.0140 352  THR   E OG1 
14002 C  CG2 . THR   E 352 ? 1.2720 1.2346 1.1726 -0.0159 0.0098  -0.0167 352  THR   E CG2 
14003 N  N   . PHE   E 353 ? 1.1518 1.1152 1.0461 -0.0238 -0.0213 -0.0184 353  PHE   E N   
14004 C  CA  . PHE   E 353 ? 1.1615 1.1303 1.0611 -0.0271 -0.0301 -0.0184 353  PHE   E CA  
14005 C  C   . PHE   E 353 ? 1.1475 1.1313 1.0661 -0.0297 -0.0304 -0.0184 353  PHE   E C   
14006 O  O   . PHE   E 353 ? 1.1506 1.1374 1.0743 -0.0296 -0.0292 -0.0196 353  PHE   E O   
14007 C  CB  . PHE   E 353 ? 1.1663 1.1265 1.0555 -0.0275 -0.0374 -0.0200 353  PHE   E CB  
14008 C  CG  . PHE   E 353 ? 1.1734 1.1176 1.0427 -0.0243 -0.0368 -0.0205 353  PHE   E CG  
14009 C  CD1 . PHE   E 353 ? 1.2286 1.1655 1.0876 -0.0238 -0.0405 -0.0198 353  PHE   E CD1 
14010 C  CD2 . PHE   E 353 ? 1.2164 1.1524 1.0768 -0.0215 -0.0325 -0.0216 353  PHE   E CD2 
14011 C  CE1 . PHE   E 353 ? 1.2475 1.1685 1.0869 -0.0204 -0.0401 -0.0202 353  PHE   E CE1 
14012 C  CE2 . PHE   E 353 ? 1.2706 1.1909 1.1115 -0.0182 -0.0316 -0.0220 353  PHE   E CE2 
14013 C  CZ  . PHE   E 353 ? 1.2907 1.2031 1.1206 -0.0176 -0.0355 -0.0213 353  PHE   E CZ  
14014 N  N   . THR   E 354 ? 1.1570 1.1494 1.0851 -0.0317 -0.0322 -0.0170 354  THR   E N   
14015 C  CA  . THR   E 354 ? 1.0941 1.1000 1.0395 -0.0335 -0.0313 -0.0167 354  THR   E CA  
14016 C  C   . THR   E 354 ? 1.0859 1.0958 1.0369 -0.0353 -0.0360 -0.0180 354  THR   E C   
14017 O  O   . THR   E 354 ? 1.0983 1.1040 1.0439 -0.0366 -0.0424 -0.0185 354  THR   E O   
14018 C  CB  . THR   E 354 ? 1.0417 1.0546 0.9943 -0.0354 -0.0338 -0.0151 354  THR   E CB  
14019 O  OG1 . THR   E 354 ? 1.0663 1.0725 1.0099 -0.0339 -0.0312 -0.0139 354  THR   E OG1 
14020 C  CG2 . THR   E 354 ? 1.0708 1.0958 1.0391 -0.0361 -0.0302 -0.0146 354  THR   E CG2 
14021 N  N   . ASN   E 355 ? 1.0705 1.0884 1.0326 -0.0351 -0.0328 -0.0185 355  ASN   E N   
14022 C  CA  . ASN   E 355 ? 1.0512 1.0740 1.0202 -0.0367 -0.0366 -0.0194 355  ASN   E CA  
14023 C  C   . ASN   E 355 ? 1.0321 1.0670 1.0164 -0.0374 -0.0348 -0.0190 355  ASN   E C   
14024 O  O   . ASN   E 355 ? 1.0155 1.0537 1.0052 -0.0357 -0.0293 -0.0193 355  ASN   E O   
14025 C  CB  . ASN   E 355 ? 1.1110 1.1278 1.0742 -0.0350 -0.0350 -0.0212 355  ASN   E CB  
14026 C  CG  . ASN   E 355 ? 1.1165 1.1383 1.0871 -0.0364 -0.0382 -0.0220 355  ASN   E CG  
14027 O  OD1 . ASN   E 355 ? 1.0555 1.0815 1.0310 -0.0391 -0.0434 -0.0215 355  ASN   E OD1 
14028 N  ND2 . ASN   E 355 ? 1.1471 1.1685 1.1188 -0.0346 -0.0349 -0.0233 355  ASN   E ND2 
14029 N  N   . LEU   E 356 ? 1.0366 1.0779 1.0280 -0.0399 -0.0395 -0.0182 356  LEU   E N   
14030 C  CA  . LEU   E 356 ? 1.0084 1.0605 1.0133 -0.0404 -0.0387 -0.0177 356  LEU   E CA  
14031 C  C   . LEU   E 356 ? 1.0763 1.1314 1.0865 -0.0400 -0.0386 -0.0190 356  LEU   E C   
14032 O  O   . LEU   E 356 ? 1.1027 1.1648 1.1224 -0.0391 -0.0361 -0.0192 356  LEU   E O   
14033 C  CB  . LEU   E 356 ? 0.9725 1.0295 0.9821 -0.0429 -0.0436 -0.0163 356  LEU   E CB  
14034 C  CG  . LEU   E 356 ? 0.9360 0.9909 0.9414 -0.0431 -0.0438 -0.0151 356  LEU   E CG  
14035 C  CD1 . LEU   E 356 ? 0.9135 0.9745 0.9252 -0.0453 -0.0482 -0.0137 356  LEU   E CD1 
14036 C  CD2 . LEU   E 356 ? 0.9970 1.0533 1.0044 -0.0412 -0.0376 -0.0147 356  LEU   E CD2 
14037 N  N   . GLY   E 357 ? 1.0981 1.1475 1.1021 -0.0404 -0.0413 -0.0200 357  GLY   E N   
14038 C  CA  . GLY   E 357 ? 1.0867 1.1380 1.0948 -0.0400 -0.0416 -0.0210 357  GLY   E CA  
14039 C  C   . GLY   E 357 ? 1.0962 1.1460 1.1039 -0.0370 -0.0366 -0.0225 357  GLY   E C   
14040 O  O   . GLY   E 357 ? 1.1186 1.1638 1.1207 -0.0353 -0.0328 -0.0228 357  GLY   E O   
14041 N  N   . PRO   E 358 ? 1.0353 1.0892 1.0496 -0.0361 -0.0362 -0.0234 358  PRO   E N   
14042 C  CA  . PRO   E 358 ? 1.0079 1.0681 1.0300 -0.0375 -0.0394 -0.0229 358  PRO   E CA  
14043 C  C   . PRO   E 358 ? 1.0027 1.0712 1.0341 -0.0377 -0.0383 -0.0218 358  PRO   E C   
14044 O  O   . PRO   E 358 ? 0.9616 1.0324 0.9965 -0.0360 -0.0344 -0.0222 358  PRO   E O   
14045 C  CB  . PRO   E 358 ? 0.9571 1.0173 0.9813 -0.0354 -0.0382 -0.0245 358  PRO   E CB  
14046 C  CG  . PRO   E 358 ? 0.9357 0.9947 0.9594 -0.0326 -0.0333 -0.0257 358  PRO   E CG  
14047 C  CD  . PRO   E 358 ? 1.0069 1.0590 1.0209 -0.0332 -0.0325 -0.0252 358  PRO   E CD  
14048 N  N   . ILE   E 359 ? 0.9963 1.0691 1.0319 -0.0398 -0.0416 -0.0205 359  ILE   E N   
14049 C  CA  . ILE   E 359 ? 0.9512 1.0320 0.9960 -0.0398 -0.0411 -0.0195 359  ILE   E CA  
14050 C  C   . ILE   E 359 ? 0.9647 1.0500 1.0163 -0.0388 -0.0418 -0.0201 359  ILE   E C   
14051 O  O   . ILE   E 359 ? 0.9582 1.0435 1.0099 -0.0401 -0.0447 -0.0194 359  ILE   E O   
14052 C  CB  . ILE   E 359 ? 0.9296 1.0122 0.9748 -0.0423 -0.0440 -0.0177 359  ILE   E CB  
14053 C  CG1 . ILE   E 359 ? 0.9280 1.0055 0.9657 -0.0427 -0.0433 -0.0173 359  ILE   E CG1 
14054 C  CG2 . ILE   E 359 ? 0.9529 1.0436 1.0075 -0.0420 -0.0436 -0.0168 359  ILE   E CG2 
14055 C  CD1 . ILE   E 359 ? 0.8979 0.9759 0.9345 -0.0449 -0.0468 -0.0156 359  ILE   E CD1 
14056 N  N   . VAL   E 360 ? 0.9347 1.0233 0.9919 -0.0363 -0.0390 -0.0213 360  VAL   E N   
14057 C  CA  . VAL   E 360 ? 0.9272 1.0191 0.9899 -0.0346 -0.0397 -0.0222 360  VAL   E CA  
14058 C  C   . VAL   E 360 ? 1.0007 1.0997 1.0718 -0.0344 -0.0404 -0.0215 360  VAL   E C   
14059 O  O   . VAL   E 360 ? 1.0078 1.1089 1.0822 -0.0334 -0.0420 -0.0217 360  VAL   E O   
14060 C  CB  . VAL   E 360 ? 0.8801 0.9707 0.9437 -0.0316 -0.0369 -0.0245 360  VAL   E CB  
14061 C  CG1 . VAL   E 360 ? 0.8824 0.9654 0.9369 -0.0316 -0.0361 -0.0251 360  VAL   E CG1 
14062 C  CG2 . VAL   E 360 ? 0.9493 1.0440 1.0192 -0.0304 -0.0336 -0.0250 360  VAL   E CG2 
14063 N  N   . ASP   E 361 ? 1.0095 1.1116 1.0835 -0.0352 -0.0393 -0.0206 361  ASP   E N   
14064 C  CA  . ASP   E 361 ? 1.0212 1.1294 1.1023 -0.0353 -0.0403 -0.0198 361  ASP   E CA  
14065 C  C   . ASP   E 361 ? 1.0013 1.1104 1.0815 -0.0373 -0.0400 -0.0181 361  ASP   E C   
14066 O  O   . ASP   E 361 ? 0.9903 1.0952 1.0649 -0.0381 -0.0385 -0.0179 361  ASP   E O   
14067 C  CB  . ASP   E 361 ? 1.0098 1.1223 1.0989 -0.0326 -0.0387 -0.0214 361  ASP   E CB  
14068 C  CG  . ASP   E 361 ? 1.0402 1.1576 1.1354 -0.0319 -0.0409 -0.0211 361  ASP   E CG  
14069 O  OD1 . ASP   E 361 ? 1.0272 1.1449 1.1205 -0.0333 -0.0432 -0.0194 361  ASP   E OD1 
14070 O  OD2 . ASP   E 361 ? 1.0397 1.1605 1.1416 -0.0297 -0.0405 -0.0226 361  ASP   E OD2 
14071 N  N   . MET   E 362 ? 0.9640 1.0778 1.0491 -0.0379 -0.0415 -0.0169 362  MET   E N   
14072 C  CA  . MET   E 362 ? 0.9149 1.0296 0.9995 -0.0395 -0.0413 -0.0154 362  MET   E CA  
14073 C  C   . MET   E 362 ? 0.9719 1.0925 1.0634 -0.0393 -0.0425 -0.0145 362  MET   E C   
14074 O  O   . MET   E 362 ? 1.0830 1.2060 1.1779 -0.0383 -0.0441 -0.0147 362  MET   E O   
14075 C  CB  . MET   E 362 ? 0.9348 1.0456 1.0124 -0.0417 -0.0435 -0.0140 362  MET   E CB  
14076 C  CG  . MET   E 362 ? 0.9423 1.0548 1.0212 -0.0428 -0.0468 -0.0130 362  MET   E CG  
14077 S  SD  . MET   E 362 ? 1.0506 1.1597 1.1237 -0.0458 -0.0499 -0.0114 362  MET   E SD  
14078 C  CE  . MET   E 362 ? 0.9352 1.0364 0.9990 -0.0456 -0.0485 -0.0127 362  MET   E CE  
14079 N  N   . CYS   E 363 ? 0.9533 1.0756 1.0463 -0.0400 -0.0417 -0.0135 363  CYS   E N   
14080 C  CA  . CYS   E 363 ? 0.9755 1.1027 1.0740 -0.0400 -0.0430 -0.0125 363  CYS   E CA  
14081 C  C   . CYS   E 363 ? 1.0057 1.1323 1.1017 -0.0416 -0.0430 -0.0108 363  CYS   E C   
14082 O  O   . CYS   E 363 ? 0.9847 1.1073 1.0757 -0.0422 -0.0413 -0.0107 363  CYS   E O   
14083 C  CB  . CYS   E 363 ? 1.0156 1.1468 1.1218 -0.0380 -0.0417 -0.0139 363  CYS   E CB  
14084 S  SG  . CYS   E 363 ? 0.9972 1.1276 1.1059 -0.0374 -0.0373 -0.0150 363  CYS   E SG  
14085 N  N   . VAL   E 364 ? 0.9867 1.1170 1.0859 -0.0420 -0.0450 -0.0094 364  VAL   E N   
14086 C  CA  . VAL   E 364 ? 0.9769 1.1071 1.0743 -0.0433 -0.0456 -0.0078 364  VAL   E CA  
14087 C  C   . VAL   E 364 ? 1.0513 1.1846 1.1540 -0.0424 -0.0439 -0.0078 364  VAL   E C   
14088 O  O   . VAL   E 364 ? 1.1140 1.2515 1.2227 -0.0413 -0.0447 -0.0080 364  VAL   E O   
14089 C  CB  . VAL   E 364 ? 0.9932 1.1253 1.0907 -0.0444 -0.0490 -0.0062 364  VAL   E CB  
14090 C  CG1 . VAL   E 364 ? 1.1553 1.2862 1.2496 -0.0456 -0.0502 -0.0047 364  VAL   E CG1 
14091 C  CG2 . VAL   E 364 ? 0.9962 1.1262 1.0908 -0.0451 -0.0506 -0.0064 364  VAL   E CG2 
14092 N  N   . VAL   E 365 ? 1.1089 1.2396 1.2092 -0.0428 -0.0414 -0.0076 365  VAL   E N   
14093 C  CA  . VAL   E 365 ? 1.1533 1.2862 1.2587 -0.0422 -0.0393 -0.0076 365  VAL   E CA  
14094 C  C   . VAL   E 365 ? 1.2877 1.4181 1.3884 -0.0433 -0.0392 -0.0058 365  VAL   E C   
14095 O  O   . VAL   E 365 ? 1.3741 1.4991 1.4674 -0.0438 -0.0379 -0.0054 365  VAL   E O   
14096 C  CB  . VAL   E 365 ? 1.0838 1.2158 1.1922 -0.0413 -0.0353 -0.0092 365  VAL   E CB  
14097 C  CG1 . VAL   E 365 ? 1.1205 1.2556 1.2362 -0.0408 -0.0335 -0.0094 365  VAL   E CG1 
14098 C  CG2 . VAL   E 365 ? 1.0809 1.2143 1.1924 -0.0400 -0.0358 -0.0111 365  VAL   E CG2 
14099 N  N   . ASP   E 366 ? 1.4047 1.5382 1.5087 -0.0433 -0.0406 -0.0047 366  ASP   E N   
14100 C  CA  . ASP   E 366 ? 1.4704 1.6016 1.5704 -0.0440 -0.0406 -0.0030 366  ASP   E CA  
14101 C  C   . ASP   E 366 ? 1.4528 1.5820 1.5539 -0.0437 -0.0362 -0.0032 366  ASP   E C   
14102 O  O   . ASP   E 366 ? 1.5082 1.6396 1.6140 -0.0435 -0.0355 -0.0028 366  ASP   E O   
14103 C  CB  . ASP   E 366 ? 1.5049 1.6403 1.6083 -0.0439 -0.0437 -0.0018 366  ASP   E CB  
14104 C  CG  . ASP   E 366 ? 1.5568 1.6896 1.6553 -0.0444 -0.0446 -0.0001 366  ASP   E CG  
14105 O  OD1 . ASP   E 366 ? 1.6034 1.7305 1.6948 -0.0449 -0.0432 0.0002  366  ASP   E OD1 
14106 O  OD2 . ASP   E 366 ? 1.5299 1.6659 1.6313 -0.0442 -0.0467 0.0010  366  ASP   E OD2 
14107 N  N   . LEU   E 367 ? 1.3932 1.5177 1.4898 -0.0437 -0.0329 -0.0038 367  LEU   E N   
14108 C  CA  . LEU   E 367 ? 1.3382 1.4615 1.4381 -0.0433 -0.0278 -0.0044 367  LEU   E CA  
14109 C  C   . LEU   E 367 ? 1.3935 1.5143 1.4916 -0.0437 -0.0259 -0.0028 367  LEU   E C   
14110 O  O   . LEU   E 367 ? 1.3606 1.4827 1.4650 -0.0435 -0.0225 -0.0031 367  LEU   E O   
14111 C  CB  . LEU   E 367 ? 1.3069 1.4249 1.4012 -0.0430 -0.0244 -0.0051 367  LEU   E CB  
14112 C  CG  . LEU   E 367 ? 1.2024 1.3228 1.3017 -0.0423 -0.0237 -0.0072 367  LEU   E CG  
14113 C  CD1 . LEU   E 367 ? 1.2054 1.3197 1.2969 -0.0419 -0.0211 -0.0077 367  LEU   E CD1 
14114 C  CD2 . LEU   E 367 ? 1.1562 1.2813 1.2669 -0.0416 -0.0211 -0.0086 367  LEU   E CD2 
14115 N  N   . GLU   E 368 ? 1.4457 1.5629 1.5355 -0.0441 -0.0282 -0.0012 368  GLU   E N   
14116 C  CA  . GLU   E 368 ? 1.4540 1.5683 1.5409 -0.0442 -0.0269 0.0005  368  GLU   E CA  
14117 C  C   . GLU   E 368 ? 1.5284 1.6476 1.6196 -0.0443 -0.0309 0.0013  368  GLU   E C   
14118 O  O   . GLU   E 368 ? 1.5572 1.6745 1.6466 -0.0443 -0.0304 0.0027  368  GLU   E O   
14119 C  CB  . GLU   E 368 ? 1.4022 1.5083 1.4762 -0.0441 -0.0269 0.0017  368  GLU   E CB  
14120 C  CG  . GLU   E 368 ? 1.3849 1.4859 1.4535 -0.0438 -0.0236 0.0008  368  GLU   E CG  
14121 C  CD  . GLU   E 368 ? 1.4020 1.4932 1.4574 -0.0433 -0.0220 0.0020  368  GLU   E CD  
14122 O  OE1 . GLU   E 368 ? 1.4012 1.4897 1.4507 -0.0432 -0.0250 0.0034  368  GLU   E OE1 
14123 O  OE2 . GLU   E 368 ? 1.4071 1.4931 1.4578 -0.0426 -0.0178 0.0015  368  GLU   E OE2 
14124 N  N   . ARG   E 369 ? 1.5480 1.6730 1.6447 -0.0442 -0.0346 0.0005  369  ARG   E N   
14125 C  CA  . ARG   E 369 ? 1.5618 1.6919 1.6636 -0.0439 -0.0379 0.0011  369  ARG   E CA  
14126 C  C   . ARG   E 369 ? 1.5821 1.7101 1.6777 -0.0441 -0.0409 0.0030  369  ARG   E C   
14127 O  O   . ARG   E 369 ? 1.5703 1.7005 1.6686 -0.0437 -0.0423 0.0039  369  ARG   E O   
14128 C  CB  . ARG   E 369 ? 1.5320 1.6645 1.6414 -0.0435 -0.0356 0.0008  369  ARG   E CB  
14129 N  N   . GLN   E 370 ? 1.6169 1.7403 1.7042 -0.0445 -0.0422 0.0034  370  GLN   E N   
14130 C  CA  . GLN   E 370 ? 1.6237 1.7449 1.7051 -0.0446 -0.0458 0.0048  370  GLN   E CA  
14131 C  C   . GLN   E 370 ? 1.6476 1.7733 1.7317 -0.0449 -0.0505 0.0049  370  GLN   E C   
14132 O  O   . GLN   E 370 ? 1.6129 1.7362 1.6917 -0.0452 -0.0539 0.0056  370  GLN   E O   
14133 C  CB  . GLN   E 370 ? 1.6055 1.7183 1.6758 -0.0446 -0.0449 0.0052  370  GLN   E CB  
14134 C  CG  . GLN   E 370 ? 1.6092 1.7164 1.6759 -0.0442 -0.0391 0.0052  370  GLN   E CG  
14135 C  CD  . GLN   E 370 ? 1.6342 1.7422 1.7045 -0.0439 -0.0368 0.0062  370  GLN   E CD  
14136 O  OE1 . GLN   E 370 ? 1.6328 1.7366 1.6972 -0.0435 -0.0374 0.0076  370  GLN   E OE1 
14137 N  NE2 . GLN   E 370 ? 1.6608 1.7739 1.7409 -0.0441 -0.0343 0.0053  370  GLN   E NE2 
14138 N  N   . GLY   E 371 ? 1.6692 1.8010 1.7612 -0.0447 -0.0509 0.0041  371  GLY   E N   
14139 C  CA  . GLY   E 371 ? 1.6835 1.8193 1.7785 -0.0450 -0.0545 0.0043  371  GLY   E CA  
14140 C  C   . GLY   E 371 ? 1.7285 1.8619 1.8196 -0.0460 -0.0559 0.0037  371  GLY   E C   
14141 O  O   . GLY   E 371 ? 1.6803 1.8171 1.7748 -0.0464 -0.0582 0.0037  371  GLY   E O   
14142 N  N   . GLN   E 372 ? 1.9482 2.0753 2.0319 -0.0463 -0.0545 0.0032  372  GLN   E N   
14143 C  CA  . GLN   E 372 ? 1.9073 2.0306 1.9857 -0.0472 -0.0560 0.0025  372  GLN   E CA  
14144 C  C   . GLN   E 372 ? 1.8811 2.0067 1.9635 -0.0473 -0.0546 0.0012  372  GLN   E C   
14145 O  O   . GLN   E 372 ? 1.8836 2.0126 1.9697 -0.0478 -0.0570 0.0012  372  GLN   E O   
14146 C  CB  . GLN   E 372 ? 1.9282 2.0433 1.9967 -0.0469 -0.0542 0.0024  372  GLN   E CB  
14147 C  CG  . GLN   E 372 ? 1.9203 2.0300 1.9817 -0.0475 -0.0558 0.0015  372  GLN   E CG  
14148 C  CD  . GLN   E 372 ? 1.9290 2.0370 1.9868 -0.0482 -0.0614 0.0021  372  GLN   E CD  
14149 O  OE1 . GLN   E 372 ? 1.9283 2.0419 1.9924 -0.0486 -0.0645 0.0029  372  GLN   E OE1 
14150 N  NE2 . GLN   E 372 ? 1.9157 2.0159 1.9637 -0.0482 -0.0628 0.0016  372  GLN   E NE2 
14151 N  N   . GLY   E 373 ? 1.6318 1.7553 1.7134 -0.0467 -0.0506 0.0001  373  GLY   E N   
14152 C  CA  . GLY   E 373 ? 1.5094 1.6342 1.5938 -0.0465 -0.0493 -0.0014 373  GLY   E CA  
14153 C  C   . GLY   E 373 ? 1.4261 1.5445 1.5029 -0.0468 -0.0484 -0.0023 373  GLY   E C   
14154 O  O   . GLY   E 373 ? 1.4058 1.5208 1.4769 -0.0477 -0.0513 -0.0021 373  GLY   E O   
14155 N  N   . GLN   E 374 ? 1.3850 1.5019 1.4620 -0.0460 -0.0443 -0.0034 374  GLN   E N   
14156 C  CA  . GLN   E 374 ? 1.3567 1.4677 1.4271 -0.0458 -0.0426 -0.0045 374  GLN   E CA  
14157 C  C   . GLN   E 374 ? 1.2846 1.3982 1.3589 -0.0457 -0.0431 -0.0059 374  GLN   E C   
14158 O  O   . GLN   E 374 ? 1.2714 1.3908 1.3532 -0.0455 -0.0443 -0.0060 374  GLN   E O   
14159 C  CB  . GLN   E 374 ? 1.3620 1.4698 1.4307 -0.0448 -0.0373 -0.0048 374  GLN   E CB  
14160 C  CG  . GLN   E 374 ? 1.4109 1.5181 1.4790 -0.0448 -0.0363 -0.0033 374  GLN   E CG  
14161 C  CD  . GLN   E 374 ? 1.4511 1.5529 1.5151 -0.0441 -0.0309 -0.0032 374  GLN   E CD  
14162 O  OE1 . GLN   E 374 ? 1.5025 1.5993 1.5596 -0.0440 -0.0302 -0.0019 374  GLN   E OE1 
14163 N  NE2 . GLN   E 374 ? 1.4121 1.5149 1.4804 -0.0434 -0.0268 -0.0045 374  GLN   E NE2 
14164 N  N   . LEU   E 375 ? 1.1172 1.2258 1.1857 -0.0455 -0.0423 -0.0069 375  LEU   E N   
14165 C  CA  . LEU   E 375 ? 1.0733 1.1832 1.1445 -0.0451 -0.0423 -0.0083 375  LEU   E CA  
14166 C  C   . LEU   E 375 ? 1.0188 1.1256 1.0885 -0.0437 -0.0379 -0.0097 375  LEU   E C   
14167 O  O   . LEU   E 375 ? 1.0549 1.1553 1.1167 -0.0436 -0.0361 -0.0097 375  LEU   E O   
14168 C  CB  . LEU   E 375 ? 1.1080 1.2147 1.1740 -0.0463 -0.0461 -0.0083 375  LEU   E CB  
14169 C  CG  . LEU   E 375 ? 1.0460 1.1537 1.1142 -0.0462 -0.0471 -0.0093 375  LEU   E CG  
14170 C  CD1 . LEU   E 375 ? 0.9817 1.0963 1.0587 -0.0459 -0.0480 -0.0091 375  LEU   E CD1 
14171 C  CD2 . LEU   E 375 ? 1.0026 1.1061 1.0650 -0.0478 -0.0507 -0.0091 375  LEU   E CD2 
14172 N  N   . VAL   E 376 ? 0.9138 1.0247 0.9909 -0.0425 -0.0361 -0.0110 376  VAL   E N   
14173 C  CA  . VAL   E 376 ? 0.9613 1.0701 1.0385 -0.0410 -0.0320 -0.0125 376  VAL   E CA  
14174 C  C   . VAL   E 376 ? 1.0317 1.1402 1.1091 -0.0403 -0.0333 -0.0140 376  VAL   E C   
14175 O  O   . VAL   E 376 ? 1.0724 1.1853 1.1549 -0.0402 -0.0359 -0.0142 376  VAL   E O   
14176 C  CB  . VAL   E 376 ? 0.9974 1.1108 1.0838 -0.0400 -0.0287 -0.0131 376  VAL   E CB  
14177 C  CG1 . VAL   E 376 ? 0.9439 1.0550 1.0311 -0.0385 -0.0240 -0.0146 376  VAL   E CG1 
14178 C  CG2 . VAL   E 376 ? 1.0323 1.1458 1.1186 -0.0408 -0.0276 -0.0115 376  VAL   E CG2 
14179 N  N   . THR   E 377 ? 1.0280 1.1309 1.0993 -0.0396 -0.0312 -0.0150 377  THR   E N   
14180 C  CA  . THR   E 377 ? 0.9773 1.0782 1.0462 -0.0391 -0.0326 -0.0163 377  THR   E CA  
14181 C  C   . THR   E 377 ? 0.9486 1.0479 1.0187 -0.0369 -0.0286 -0.0181 377  THR   E C   
14182 O  O   . THR   E 377 ? 0.9115 1.0079 0.9793 -0.0363 -0.0245 -0.0181 377  THR   E O   
14183 C  CB  . THR   E 377 ? 0.9447 1.0388 1.0032 -0.0404 -0.0351 -0.0157 377  THR   E CB  
14184 O  OG1 . THR   E 377 ? 0.9522 1.0401 1.0031 -0.0399 -0.0321 -0.0156 377  THR   E OG1 
14185 C  CG2 . THR   E 377 ? 0.9565 1.0523 1.0146 -0.0425 -0.0394 -0.0140 377  THR   E CG2 
14186 N  N   . CYS   E 378 ? 0.9600 1.0612 1.0337 -0.0357 -0.0296 -0.0195 378  CYS   E N   
14187 C  CA  . CYS   E 378 ? 0.9347 1.0337 1.0084 -0.0336 -0.0267 -0.0214 378  CYS   E CA  
14188 C  C   . CYS   E 378 ? 0.9488 1.0400 1.0114 -0.0339 -0.0274 -0.0216 378  CYS   E C   
14189 O  O   . CYS   E 378 ? 0.9621 1.0519 1.0223 -0.0342 -0.0306 -0.0219 378  CYS   E O   
14190 C  CB  . CYS   E 378 ? 0.9300 1.0334 1.0112 -0.0318 -0.0281 -0.0230 378  CYS   E CB  
14191 S  SG  . CYS   E 378 ? 0.9881 1.0999 1.0824 -0.0309 -0.0279 -0.0235 378  CYS   E SG  
14192 N  N   . SER   E 379 ? 0.9409 1.0265 0.9965 -0.0339 -0.0245 -0.0212 379  SER   E N   
14193 C  CA  . SER   E 379 ? 0.9330 1.0102 0.9767 -0.0343 -0.0256 -0.0212 379  SER   E CA  
14194 C  C   . SER   E 379 ? 0.9816 1.0539 1.0214 -0.0319 -0.0217 -0.0228 379  SER   E C   
14195 O  O   . SER   E 379 ? 0.9737 1.0478 1.0184 -0.0302 -0.0169 -0.0234 379  SER   E O   
14196 C  CB  . SER   E 379 ? 0.9429 1.0156 0.9790 -0.0356 -0.0257 -0.0196 379  SER   E CB  
14197 O  OG  . SER   E 379 ? 0.9737 1.0492 1.0110 -0.0379 -0.0305 -0.0183 379  SER   E OG  
14198 N  N   . GLY   E 380 ? 0.9897 1.0556 1.0209 -0.0319 -0.0239 -0.0234 380  GLY   E N   
14199 C  CA  . GLY   E 380 ? 0.9404 1.0002 0.9659 -0.0296 -0.0206 -0.0249 380  GLY   E CA  
14200 C  C   . GLY   E 380 ? 0.9500 1.0141 0.9834 -0.0275 -0.0193 -0.0266 380  GLY   E C   
14201 O  O   . GLY   E 380 ? 0.9284 0.9995 0.9711 -0.0277 -0.0213 -0.0269 380  GLY   E O   
14202 N  N   . ALA   E 381 ? 1.0061 1.0652 1.0353 -0.0251 -0.0159 -0.0280 381  ALA   E N   
14203 C  CA  . ALA   E 381 ? 0.9707 1.0327 1.0065 -0.0226 -0.0145 -0.0299 381  ALA   E CA  
14204 C  C   . ALA   E 381 ? 0.9277 0.9866 0.9623 -0.0199 -0.0083 -0.0309 381  ALA   E C   
14205 O  O   . ALA   E 381 ? 0.9295 0.9812 0.9543 -0.0198 -0.0058 -0.0301 381  ALA   E O   
14206 C  CB  . ALA   E 381 ? 0.9235 0.9817 0.9541 -0.0224 -0.0185 -0.0309 381  ALA   E CB  
14207 N  N   . PHE   E 382 ? 0.9760 1.0402 1.0209 -0.0175 -0.0059 -0.0325 382  PHE   E N   
14208 C  CA  . PHE   E 382 ? 0.9982 1.0601 1.0439 -0.0144 0.0001  -0.0337 382  PHE   E CA  
14209 C  C   . PHE   E 382 ? 1.0248 1.0856 1.0699 -0.0148 0.0057  -0.0322 382  PHE   E C   
14210 O  O   . PHE   E 382 ? 1.0205 1.0867 1.0722 -0.0166 0.0054  -0.0310 382  PHE   E O   
14211 C  CB  . PHE   E 382 ? 1.0278 1.0807 1.0615 -0.0130 -0.0002 -0.0346 382  PHE   E CB  
14212 C  CG  . PHE   E 382 ? 1.0492 1.1023 1.0825 -0.0129 -0.0056 -0.0357 382  PHE   E CG  
14213 C  CD1 . PHE   E 382 ? 1.0330 1.0940 1.0782 -0.0119 -0.0076 -0.0369 382  PHE   E CD1 
14214 C  CD2 . PHE   E 382 ? 1.0440 1.0888 1.0648 -0.0136 -0.0089 -0.0357 382  PHE   E CD2 
14215 C  CE1 . PHE   E 382 ? 1.0413 1.1016 1.0851 -0.0116 -0.0122 -0.0378 382  PHE   E CE1 
14216 C  CE2 . PHE   E 382 ? 1.0616 1.1060 1.0819 -0.0136 -0.0134 -0.0365 382  PHE   E CE2 
14217 C  CZ  . PHE   E 382 ? 1.0457 1.0977 1.0771 -0.0125 -0.0148 -0.0375 382  PHE   E CZ  
14218 N  N   . LYS   E 383 ? 0.9904 1.0438 1.0273 -0.0129 0.0108  -0.0323 383  LYS   E N   
14219 C  CA  . LYS   E 383 ? 0.9939 1.0451 1.0293 -0.0130 0.0168  -0.0307 383  LYS   E CA  
14220 C  C   . LYS   E 383 ? 1.0129 1.0617 1.0411 -0.0159 0.0139  -0.0286 383  LYS   E C   
14221 O  O   . LYS   E 383 ? 1.0310 1.0811 1.0619 -0.0166 0.0175  -0.0271 383  LYS   E O   
14222 C  CB  . LYS   E 383 ? 1.0778 1.1196 1.1029 -0.0102 0.0226  -0.0310 383  LYS   E CB  
14223 C  CG  . LYS   E 383 ? 1.1586 1.1887 1.1650 -0.0104 0.0197  -0.0306 383  LYS   E CG  
14224 C  CD  . LYS   E 383 ? 1.2194 1.2401 1.2159 -0.0070 0.0260  -0.0311 383  LYS   E CD  
14225 C  CE  . LYS   E 383 ? 1.2319 1.2397 1.2089 -0.0071 0.0248  -0.0300 383  LYS   E CE  
14226 N  NZ  . LYS   E 383 ? 1.2247 1.2310 1.1983 -0.0088 0.0262  -0.0278 383  LYS   E NZ  
14227 N  N   . GLU   E 384 ? 0.9982 1.0439 1.0184 -0.0177 0.0073  -0.0283 384  GLU   E N   
14228 C  CA  . GLU   E 384 ? 0.9988 1.0426 1.0129 -0.0205 0.0036  -0.0265 384  GLU   E CA  
14229 C  C   . GLU   E 384 ? 0.9859 1.0396 1.0116 -0.0228 -0.0002 -0.0258 384  GLU   E C   
14230 O  O   . GLU   E 384 ? 0.9981 1.0513 1.0200 -0.0252 -0.0043 -0.0245 384  GLU   E O   
14231 C  CB  . GLU   E 384 ? 1.0332 1.0688 1.0340 -0.0214 -0.0018 -0.0267 384  GLU   E CB  
14232 C  CG  . GLU   E 384 ? 1.0893 1.1149 1.0785 -0.0188 0.0011  -0.0277 384  GLU   E CG  
14233 C  CD  . GLU   E 384 ? 1.1750 1.1921 1.1538 -0.0173 0.0066  -0.0267 384  GLU   E CD  
14234 O  OE1 . GLU   E 384 ? 1.2146 1.2323 1.1932 -0.0186 0.0073  -0.0250 384  GLU   E OE1 
14235 O  OE2 . GLU   E 384 ? 1.1925 1.2014 1.1625 -0.0146 0.0103  -0.0275 384  GLU   E OE2 
14236 N  N   . GLY   E 385 ? 0.9333 0.9958 0.9730 -0.0220 0.0009  -0.0269 385  GLY   E N   
14237 C  CA  . GLY   E 385 ? 0.9428 1.0139 0.9926 -0.0239 -0.0028 -0.0264 385  GLY   E CA  
14238 C  C   . GLY   E 385 ? 0.9452 1.0180 0.9970 -0.0254 -0.0007 -0.0245 385  GLY   E C   
14239 O  O   . GLY   E 385 ? 1.0096 1.0818 1.0638 -0.0243 0.0053  -0.0243 385  GLY   E O   
14240 N  N   . SER   E 386 ? 0.9201 0.9949 0.9710 -0.0278 -0.0053 -0.0232 386  SER   E N   
14241 C  CA  . SER   E 386 ? 0.9152 0.9901 0.9655 -0.0291 -0.0039 -0.0213 386  SER   E CA  
14242 C  C   . SER   E 386 ? 0.9687 1.0512 1.0269 -0.0311 -0.0085 -0.0206 386  SER   E C   
14243 O  O   . SER   E 386 ? 1.0150 1.1013 1.0770 -0.0314 -0.0129 -0.0213 386  SER   E O   
14244 C  CB  . SER   E 386 ? 0.9178 0.9832 0.9530 -0.0298 -0.0047 -0.0200 386  SER   E CB  
14245 O  OG  . SER   E 386 ? 0.9152 0.9795 0.9453 -0.0316 -0.0114 -0.0197 386  SER   E OG  
14246 N  N   . LEU   E 387 ? 0.9639 1.0479 1.0241 -0.0321 -0.0070 -0.0190 387  LEU   E N   
14247 C  CA  . LEU   E 387 ? 0.9562 1.0454 1.0206 -0.0340 -0.0114 -0.0179 387  LEU   E CA  
14248 C  C   . LEU   E 387 ? 0.9789 1.0624 1.0328 -0.0354 -0.0129 -0.0160 387  LEU   E C   
14249 O  O   . LEU   E 387 ? 1.0012 1.0795 1.0496 -0.0349 -0.0087 -0.0151 387  LEU   E O   
14250 C  CB  . LEU   E 387 ? 0.9166 1.0129 0.9934 -0.0339 -0.0090 -0.0179 387  LEU   E CB  
14251 C  CG  . LEU   E 387 ? 0.8742 0.9775 0.9629 -0.0327 -0.0097 -0.0198 387  LEU   E CG  
14252 C  CD1 . LEU   E 387 ? 0.9052 1.0151 1.0051 -0.0332 -0.0092 -0.0196 387  LEU   E CD1 
14253 C  CD2 . LEU   E 387 ? 0.9071 1.0116 0.9942 -0.0330 -0.0155 -0.0204 387  LEU   E CD2 
14254 N  N   . ARG   E 388 ? 0.9481 1.0320 0.9990 -0.0370 -0.0187 -0.0154 388  ARG   E N   
14255 C  CA  . ARG   E 388 ? 0.9803 1.0591 1.0217 -0.0383 -0.0212 -0.0138 388  ARG   E CA  
14256 C  C   . ARG   E 388 ? 1.0521 1.1370 1.0998 -0.0398 -0.0241 -0.0125 388  ARG   E C   
14257 O  O   . ARG   E 388 ? 1.1022 1.1938 1.1579 -0.0403 -0.0271 -0.0128 388  ARG   E O   
14258 C  CB  . ARG   E 388 ? 0.9960 1.0696 1.0288 -0.0389 -0.0257 -0.0143 388  ARG   E CB  
14259 C  CG  . ARG   E 388 ? 0.9870 1.0545 1.0136 -0.0373 -0.0235 -0.0158 388  ARG   E CG  
14260 C  CD  . ARG   E 388 ? 0.9919 1.0516 1.0098 -0.0356 -0.0181 -0.0155 388  ARG   E CD  
14261 N  NE  . ARG   E 388 ? 1.0136 1.0672 1.0253 -0.0339 -0.0158 -0.0170 388  ARG   E NE  
14262 C  CZ  . ARG   E 388 ? 1.0488 1.0920 1.0468 -0.0329 -0.0153 -0.0170 388  ARG   E CZ  
14263 N  NH1 . ARG   E 388 ? 1.0657 1.1028 1.0541 -0.0334 -0.0171 -0.0158 388  ARG   E NH1 
14264 N  NH2 . ARG   E 388 ? 1.0720 1.1102 1.0653 -0.0311 -0.0130 -0.0185 388  ARG   E NH2 
14265 N  N   . ILE   E 389 ? 1.0413 1.1236 1.0851 -0.0401 -0.0232 -0.0110 389  ILE   E N   
14266 C  CA  . ILE   E 389 ? 1.0637 1.1512 1.1126 -0.0414 -0.0258 -0.0096 389  ILE   E CA  
14267 C  C   . ILE   E 389 ? 1.1297 1.2120 1.1690 -0.0423 -0.0300 -0.0084 389  ILE   E C   
14268 O  O   . ILE   E 389 ? 1.1892 1.2641 1.2190 -0.0417 -0.0282 -0.0077 389  ILE   E O   
14269 C  CB  . ILE   E 389 ? 1.0671 1.1571 1.1217 -0.0409 -0.0213 -0.0089 389  ILE   E CB  
14270 C  CG1 . ILE   E 389 ? 1.0388 1.1333 1.1032 -0.0398 -0.0172 -0.0104 389  ILE   E CG1 
14271 C  CG2 . ILE   E 389 ? 1.1078 1.2041 1.1690 -0.0420 -0.0245 -0.0079 389  ILE   E CG2 
14272 C  CD1 . ILE   E 389 ? 1.0229 1.1120 1.0837 -0.0384 -0.0110 -0.0108 389  ILE   E CD1 
14273 N  N   . ILE   E 390 ? 1.1683 1.2545 1.2104 -0.0437 -0.0355 -0.0081 390  ILE   E N   
14274 C  CA  . ILE   E 390 ? 1.2195 1.3014 1.2539 -0.0448 -0.0406 -0.0075 390  ILE   E CA  
14275 C  C   . ILE   E 390 ? 1.2875 1.3738 1.3259 -0.0457 -0.0436 -0.0060 390  ILE   E C   
14276 O  O   . ILE   E 390 ? 1.3460 1.4401 1.3940 -0.0463 -0.0448 -0.0058 390  ILE   E O   
14277 C  CB  . ILE   E 390 ? 1.2088 1.2914 1.2438 -0.0457 -0.0444 -0.0085 390  ILE   E CB  
14278 C  CG1 . ILE   E 390 ? 1.1346 1.2127 1.1656 -0.0446 -0.0415 -0.0101 390  ILE   E CG1 
14279 C  CG2 . ILE   E 390 ? 1.2686 1.3477 1.2979 -0.0471 -0.0502 -0.0079 390  ILE   E CG2 
14280 C  CD1 . ILE   E 390 ? 1.0477 1.1303 1.0852 -0.0449 -0.0427 -0.0111 390  ILE   E CD1 
14281 N  N   . ARG   E 391 ? 1.5169 1.5978 1.5473 -0.0457 -0.0451 -0.0050 391  ARG   E N   
14282 C  CA  . ARG   E 391 ? 1.5243 1.6090 1.5582 -0.0463 -0.0479 -0.0036 391  ARG   E CA  
14283 C  C   . ARG   E 391 ? 1.5523 1.6312 1.5774 -0.0467 -0.0531 -0.0031 391  ARG   E C   
14284 O  O   . ARG   E 391 ? 1.5778 1.6481 1.5923 -0.0460 -0.0536 -0.0038 391  ARG   E O   
14285 C  CB  . ARG   E 391 ? 1.5744 1.6595 1.6096 -0.0453 -0.0433 -0.0027 391  ARG   E CB  
14286 C  CG  . ARG   E 391 ? 1.6328 1.7080 1.6562 -0.0440 -0.0404 -0.0022 391  ARG   E CG  
14287 C  CD  . ARG   E 391 ? 1.6885 1.7647 1.7145 -0.0434 -0.0359 -0.0011 391  ARG   E CD  
14288 N  NE  . ARG   E 391 ? 1.7277 1.8128 1.7645 -0.0442 -0.0379 -0.0004 391  ARG   E NE  
14289 C  CZ  . ARG   E 391 ? 1.7686 1.8546 1.8048 -0.0445 -0.0415 0.0008  391  ARG   E CZ  
14290 N  NH1 . ARG   E 391 ? 1.8097 1.8883 1.8352 -0.0440 -0.0440 0.0015  391  ARG   E NH1 
14291 N  NH2 . ARG   E 391 ? 1.7472 1.8414 1.7935 -0.0451 -0.0429 0.0013  391  ARG   E NH2 
14292 N  N   . ASN   E 392 ? 1.5148 1.5983 1.5446 -0.0475 -0.0571 -0.0021 392  ASN   E N   
14293 C  CA  . ASN   E 392 ? 1.5060 1.5848 1.5290 -0.0477 -0.0624 -0.0017 392  ASN   E CA  
14294 C  C   . ASN   E 392 ? 1.5433 1.6166 1.5587 -0.0462 -0.0610 -0.0006 392  ASN   E C   
14295 O  O   . ASN   E 392 ? 1.4810 1.5481 1.4880 -0.0457 -0.0650 -0.0004 392  ASN   E O   
14296 C  CB  . ASN   E 392 ? 1.4902 1.5767 1.5223 -0.0492 -0.0675 -0.0011 392  ASN   E CB  
14297 C  CG  . ASN   E 392 ? 1.4394 1.5271 1.4742 -0.0507 -0.0709 -0.0021 392  ASN   E CG  
14298 O  OD1 . ASN   E 392 ? 1.4990 1.5806 1.5268 -0.0511 -0.0749 -0.0028 392  ASN   E OD1 
14299 N  ND2 . ASN   E 392 ? 1.3838 1.4790 1.4284 -0.0515 -0.0696 -0.0021 392  ASN   E ND2 
14300 N  N   . LEU   E 406 ? 1.5765 1.6267 1.5658 -0.0467 -0.0690 -0.0057 710  LEU   E N   
14301 C  CA  . LEU   E 406 ? 1.6047 1.6592 1.5999 -0.0465 -0.0629 -0.0060 710  LEU   E CA  
14302 C  C   . LEU   E 406 ? 1.7308 1.7777 1.7168 -0.0443 -0.0566 -0.0062 710  LEU   E C   
14303 O  O   . LEU   E 406 ? 1.7934 1.8298 1.7665 -0.0430 -0.0574 -0.0068 710  LEU   E O   
14304 C  CB  . LEU   E 406 ? 1.4674 1.5234 1.4659 -0.0478 -0.0647 -0.0073 710  LEU   E CB  
14305 C  CG  . LEU   E 406 ? 1.3983 1.4650 1.4106 -0.0498 -0.0667 -0.0070 710  LEU   E CG  
14306 C  CD1 . LEU   E 406 ? 1.1469 1.2148 1.1622 -0.0504 -0.0658 -0.0082 710  LEU   E CD1 
14307 C  CD2 . LEU   E 406 ? 1.5144 1.5894 1.5359 -0.0495 -0.0632 -0.0057 710  LEU   E CD2 
14308 N  N   . HIS   E 407 ? 1.8372 1.8890 1.8299 -0.0437 -0.0504 -0.0057 711  HIS   E N   
14309 C  CA  . HIS   E 407 ? 1.8868 1.9326 1.8731 -0.0417 -0.0436 -0.0055 711  HIS   E CA  
14310 C  C   . HIS   E 407 ? 1.8261 1.8780 1.8218 -0.0417 -0.0383 -0.0063 711  HIS   E C   
14311 O  O   . HIS   E 407 ? 1.7961 1.8578 1.8042 -0.0427 -0.0382 -0.0060 711  HIS   E O   
14312 C  CB  . HIS   E 407 ? 1.9678 2.0126 1.9526 -0.0410 -0.0412 -0.0038 711  HIS   E CB  
14313 C  CG  . HIS   E 407 ? 2.0192 2.0625 2.0002 -0.0414 -0.0475 -0.0030 711  HIS   E CG  
14314 N  ND1 . HIS   E 407 ? 2.0297 2.0807 2.0195 -0.0424 -0.0495 -0.0019 711  HIS   E ND1 
14315 C  CD2 . HIS   E 407 ? 2.0161 2.0507 1.9854 -0.0408 -0.0526 -0.0033 711  HIS   E CD2 
14316 C  CE1 . HIS   E 407 ? 2.0254 2.0730 2.0096 -0.0424 -0.0553 -0.0015 711  HIS   E CE1 
14317 N  NE2 . HIS   E 407 ? 2.0305 2.0683 2.0025 -0.0414 -0.0576 -0.0024 711  HIS   E NE2 
14318 N  N   . ILE   E 408 ? 1.4973 1.5432 1.4869 -0.0402 -0.0341 -0.0072 712  ILE   E N   
14319 C  CA  . ILE   E 408 ? 1.2881 1.3387 1.2855 -0.0399 -0.0303 -0.0084 712  ILE   E CA  
14320 C  C   . ILE   E 408 ? 1.1947 1.2420 1.1906 -0.0380 -0.0222 -0.0083 712  ILE   E C   
14321 O  O   . ILE   E 408 ? 1.2235 1.2608 1.2072 -0.0363 -0.0195 -0.0083 712  ILE   E O   
14322 C  CB  . ILE   E 408 ? 1.2659 1.3127 1.2585 -0.0399 -0.0330 -0.0100 712  ILE   E CB  
14323 C  CG1 . ILE   E 408 ? 1.3252 1.3761 1.3215 -0.0421 -0.0404 -0.0102 712  ILE   E CG1 
14324 C  CG2 . ILE   E 408 ? 1.1581 1.2082 1.1570 -0.0390 -0.0285 -0.0113 712  ILE   E CG2 
14325 C  CD1 . ILE   E 408 ? 1.4047 1.4467 1.3891 -0.0424 -0.0457 -0.0106 712  ILE   E CD1 
14326 N  N   . ARG   E 409 ? 1.1117 1.1671 1.1200 -0.0381 -0.0184 -0.0082 713  ARG   E N   
14327 C  CA  . ARG   E 409 ? 1.0523 1.1067 1.0630 -0.0366 -0.0106 -0.0083 713  ARG   E CA  
14328 C  C   . ARG   E 409 ? 1.0053 1.0634 1.0227 -0.0359 -0.0088 -0.0101 713  ARG   E C   
14329 O  O   . ARG   E 409 ? 1.0349 1.1005 1.0611 -0.0370 -0.0125 -0.0110 713  ARG   E O   
14330 C  CB  . ARG   E 409 ? 1.1128 1.1739 1.1339 -0.0372 -0.0079 -0.0072 713  ARG   E CB  
14331 C  CG  . ARG   E 409 ? 1.1211 1.1831 1.1485 -0.0361 0.0002  -0.0073 713  ARG   E CG  
14332 C  CD  . ARG   E 409 ? 1.1132 1.1817 1.1510 -0.0371 0.0015  -0.0062 713  ARG   E CD  
14333 N  NE  . ARG   E 409 ? 1.2067 1.2764 1.2520 -0.0364 0.0091  -0.0062 713  ARG   E NE  
14334 C  CZ  . ARG   E 409 ? 1.2783 1.3535 1.3339 -0.0372 0.0110  -0.0056 713  ARG   E CZ  
14335 N  NH1 . ARG   E 409 ? 1.3100 1.3900 1.3694 -0.0386 0.0061  -0.0050 713  ARG   E NH1 
14336 N  NH2 . ARG   E 409 ? 1.2467 1.3225 1.3094 -0.0366 0.0182  -0.0056 713  ARG   E NH2 
14337 N  N   . THR   E 410 ? 0.9601 1.0125 0.9728 -0.0340 -0.0031 -0.0107 714  THR   E N   
14338 C  CA  . THR   E 410 ? 0.9447 0.9992 0.9619 -0.0330 -0.0016 -0.0126 714  THR   E CA  
14339 C  C   . THR   E 410 ? 0.9250 0.9841 0.9530 -0.0319 0.0053  -0.0130 714  THR   E C   
14340 O  O   . THR   E 410 ? 0.9902 1.0445 1.0148 -0.0308 0.0116  -0.0120 714  THR   E O   
14341 C  CB  . THR   E 410 ? 1.0171 1.0611 1.0204 -0.0314 -0.0008 -0.0133 714  THR   E CB  
14342 O  OG1 . THR   E 410 ? 1.0872 1.1278 1.0824 -0.0326 -0.0081 -0.0134 714  THR   E OG1 
14343 C  CG2 . THR   E 410 ? 0.9760 1.0219 0.9845 -0.0299 0.0025  -0.0151 714  THR   E CG2 
14344 N  N   . VAL   E 411 ? 0.9142 0.9822 0.9552 -0.0321 0.0042  -0.0145 715  VAL   E N   
14345 C  CA  . VAL   E 411 ? 0.9103 0.9834 0.9633 -0.0310 0.0099  -0.0154 715  VAL   E CA  
14346 C  C   . VAL   E 411 ? 0.9191 0.9912 0.9721 -0.0292 0.0108  -0.0174 715  VAL   E C   
14347 O  O   . VAL   E 411 ? 0.9513 1.0286 1.0100 -0.0293 0.0064  -0.0188 715  VAL   E O   
14348 C  CB  . VAL   E 411 ? 0.8971 0.9810 0.9654 -0.0321 0.0075  -0.0158 715  VAL   E CB  
14349 C  CG1 . VAL   E 411 ? 0.8943 0.9829 0.9752 -0.0311 0.0133  -0.0167 715  VAL   E CG1 
14350 C  CG2 . VAL   E 411 ? 0.8949 0.9798 0.9623 -0.0339 0.0053  -0.0139 715  VAL   E CG2 
14351 N  N   . PRO   E 412 ? 0.9478 1.0127 0.9937 -0.0273 0.0165  -0.0175 716  PRO   E N   
14352 C  CA  . PRO   E 412 ? 0.9946 1.0592 1.0422 -0.0252 0.0181  -0.0194 716  PRO   E CA  
14353 C  C   . PRO   E 412 ? 1.0083 1.0828 1.0735 -0.0247 0.0199  -0.0210 716  PRO   E C   
14354 O  O   . PRO   E 412 ? 1.0045 1.0833 1.0794 -0.0250 0.0238  -0.0204 716  PRO   E O   
14355 C  CB  . PRO   E 412 ? 1.0669 1.1217 1.1041 -0.0232 0.0252  -0.0188 716  PRO   E CB  
14356 C  CG  . PRO   E 412 ? 1.0523 1.1061 1.0898 -0.0240 0.0293  -0.0167 716  PRO   E CG  
14357 C  CD  . PRO   E 412 ? 0.9920 1.0488 1.0289 -0.0266 0.0223  -0.0157 716  PRO   E CD  
14358 N  N   . LEU   E 413 ? 1.0164 1.0941 1.0857 -0.0237 0.0166  -0.0230 717  LEU   E N   
14359 C  CA  . LEU   E 413 ? 0.9827 1.0689 1.0676 -0.0226 0.0174  -0.0250 717  LEU   E CA  
14360 C  C   . LEU   E 413 ? 0.9800 1.0640 1.0651 -0.0198 0.0206  -0.0268 717  LEU   E C   
14361 O  O   . LEU   E 413 ? 0.9888 1.0791 1.0873 -0.0183 0.0228  -0.0285 717  LEU   E O   
14362 C  CB  . LEU   E 413 ? 0.9076 1.0005 0.9987 -0.0236 0.0100  -0.0258 717  LEU   E CB  
14363 C  CG  . LEU   E 413 ? 0.8852 0.9815 0.9783 -0.0261 0.0072  -0.0241 717  LEU   E CG  
14364 C  CD1 . LEU   E 413 ? 0.8808 0.9778 0.9694 -0.0276 -0.0001 -0.0237 717  LEU   E CD1 
14365 C  CD2 . LEU   E 413 ? 0.8771 0.9818 0.9861 -0.0261 0.0085  -0.0248 717  LEU   E CD2 
14366 N  N   . TYR   E 414 ? 1.0137 1.0891 1.0847 -0.0189 0.0204  -0.0268 718  TYR   E N   
14367 C  CA  . TYR   E 414 ? 1.0253 1.0971 1.0943 -0.0160 0.0238  -0.0284 718  TYR   E CA  
14368 C  C   . TYR   E 414 ? 1.0051 1.0828 1.0830 -0.0147 0.0199  -0.0308 718  TYR   E C   
14369 O  O   . TYR   E 414 ? 0.9801 1.0568 1.0600 -0.0120 0.0229  -0.0325 718  TYR   E O   
14370 C  CB  . TYR   E 414 ? 1.0570 1.1285 1.1317 -0.0143 0.0327  -0.0281 718  TYR   E CB  
14371 C  CG  . TYR   E 414 ? 1.0210 1.0849 1.0847 -0.0151 0.0371  -0.0256 718  TYR   E CG  
14372 C  CD1 . TYR   E 414 ? 1.0725 1.1259 1.1178 -0.0152 0.0353  -0.0246 718  TYR   E CD1 
14373 C  CD2 . TYR   E 414 ? 0.9685 1.0351 1.0400 -0.0157 0.0428  -0.0243 718  TYR   E CD2 
14374 C  CE1 . TYR   E 414 ? 1.0444 1.0899 1.0786 -0.0155 0.0389  -0.0225 718  TYR   E CE1 
14375 C  CE2 . TYR   E 414 ? 1.0248 1.0835 1.0853 -0.0161 0.0469  -0.0220 718  TYR   E CE2 
14376 C  CZ  . TYR   E 414 ? 1.0336 1.0816 1.0750 -0.0158 0.0448  -0.0211 718  TYR   E CZ  
14377 O  OH  . TYR   E 414 ? 1.0621 1.1013 1.0913 -0.0159 0.0486  -0.0188 718  TYR   E OH  
14378 N  N   . GLU   E 415 ? 0.9939 1.0773 1.0767 -0.0164 0.0134  -0.0310 719  GLU   E N   
14379 C  CA  . GLU   E 415 ? 0.9817 1.0695 1.0702 -0.0153 0.0084  -0.0330 719  GLU   E CA  
14380 C  C   . GLU   E 415 ? 0.9504 1.0390 1.0348 -0.0178 0.0015  -0.0320 719  GLU   E C   
14381 O  O   . GLU   E 415 ? 0.9359 1.0235 1.0161 -0.0202 0.0007  -0.0300 719  GLU   E O   
14382 C  CB  . GLU   E 415 ? 0.9718 1.0687 1.0778 -0.0139 0.0095  -0.0347 719  GLU   E CB  
14383 C  CG  . GLU   E 415 ? 0.9602 1.0639 1.0754 -0.0160 0.0077  -0.0339 719  GLU   E CG  
14384 C  CD  . GLU   E 415 ? 1.0163 1.1282 1.1488 -0.0144 0.0090  -0.0358 719  GLU   E CD  
14385 O  OE1 . GLU   E 415 ? 1.0683 1.1807 1.2069 -0.0133 0.0153  -0.0362 719  GLU   E OE1 
14386 O  OE2 . GLU   E 415 ? 1.0490 1.1664 1.1890 -0.0142 0.0038  -0.0370 719  GLU   E OE2 
14387 N  N   . SER   E 416 ? 0.9553 1.0454 1.0409 -0.0170 -0.0033 -0.0333 720  SER   E N   
14388 C  CA  . SER   E 416 ? 0.9332 1.0227 1.0133 -0.0192 -0.0093 -0.0323 720  SER   E CA  
14389 C  C   . SER   E 416 ? 0.9178 1.0151 1.0078 -0.0204 -0.0121 -0.0318 720  SER   E C   
14390 O  O   . SER   E 416 ? 0.9264 1.0294 1.0269 -0.0186 -0.0129 -0.0334 720  SER   E O   
14391 C  CB  . SER   E 416 ? 0.9299 1.0168 1.0062 -0.0178 -0.0128 -0.0337 720  SER   E CB  
14392 O  OG  . SER   E 416 ? 0.9559 1.0354 1.0233 -0.0164 -0.0103 -0.0343 720  SER   E OG  
14393 N  N   . PRO   E 417 ? 0.8830 0.9805 0.9699 -0.0231 -0.0136 -0.0297 721  PRO   E N   
14394 C  CA  . PRO   E 417 ? 0.8664 0.9703 0.9607 -0.0241 -0.0172 -0.0292 721  PRO   E CA  
14395 C  C   . PRO   E 417 ? 0.9048 1.0081 0.9955 -0.0245 -0.0225 -0.0291 721  PRO   E C   
14396 O  O   . PRO   E 417 ? 0.9255 1.0232 1.0062 -0.0257 -0.0241 -0.0282 721  PRO   E O   
14397 C  CB  . PRO   E 417 ? 0.8668 0.9701 0.9580 -0.0267 -0.0164 -0.0269 721  PRO   E CB  
14398 C  CG  . PRO   E 417 ? 0.8812 0.9766 0.9598 -0.0274 -0.0154 -0.0260 721  PRO   E CG  
14399 C  CD  . PRO   E 417 ? 0.8929 0.9848 0.9701 -0.0250 -0.0119 -0.0277 721  PRO   E CD  
14400 N  N   . ARG   E 418 ? 0.8701 0.9786 0.9687 -0.0233 -0.0252 -0.0301 722  ARG   E N   
14401 C  CA  . ARG   E 418 ? 0.8610 0.9689 0.9569 -0.0231 -0.0297 -0.0300 722  ARG   E CA  
14402 C  C   . ARG   E 418 ? 0.9349 1.0466 1.0333 -0.0247 -0.0327 -0.0284 722  ARG   E C   
14403 O  O   . ARG   E 418 ? 0.9458 1.0551 1.0380 -0.0265 -0.0351 -0.0269 722  ARG   E O   
14404 C  CB  . ARG   E 418 ? 0.8975 1.0070 0.9988 -0.0198 -0.0307 -0.0325 722  ARG   E CB  
14405 C  CG  . ARG   E 418 ? 0.9587 1.0646 1.0580 -0.0178 -0.0279 -0.0342 722  ARG   E CG  
14406 C  CD  . ARG   E 418 ? 1.0131 1.1115 1.1003 -0.0188 -0.0282 -0.0335 722  ARG   E CD  
14407 N  NE  . ARG   E 418 ? 1.0335 1.1298 1.1162 -0.0191 -0.0323 -0.0330 722  ARG   E NE  
14408 C  CZ  . ARG   E 418 ? 0.9570 1.0476 1.0301 -0.0209 -0.0337 -0.0318 722  ARG   E CZ  
14409 N  NH1 . ARG   E 418 ? 0.9689 1.0548 1.0349 -0.0225 -0.0318 -0.0311 722  ARG   E NH1 
14410 N  NH2 . ARG   E 418 ? 0.9463 1.0354 1.0168 -0.0211 -0.0369 -0.0314 722  ARG   E NH2 
14411 N  N   . LYS   E 419 ? 0.8804 0.9978 0.9879 -0.0242 -0.0326 -0.0287 723  LYS   E N   
14412 C  CA  . LYS   E 419 ? 0.9093 1.0299 1.0186 -0.0255 -0.0353 -0.0272 723  LYS   E CA  
14413 C  C   . LYS   E 419 ? 0.9444 1.0690 1.0600 -0.0265 -0.0334 -0.0266 723  LYS   E C   
14414 O  O   . LYS   E 419 ? 0.9709 1.0973 1.0925 -0.0255 -0.0305 -0.0279 723  LYS   E O   
14415 C  CB  . LYS   E 419 ? 0.9411 1.0639 1.0544 -0.0232 -0.0387 -0.0284 723  LYS   E CB  
14416 C  CG  . LYS   E 419 ? 0.9236 1.0421 1.0311 -0.0217 -0.0404 -0.0291 723  LYS   E CG  
14417 C  CD  . LYS   E 419 ? 0.9348 1.0505 1.0349 -0.0237 -0.0423 -0.0269 723  LYS   E CD  
14418 C  CE  . LYS   E 419 ? 0.9683 1.0789 1.0624 -0.0225 -0.0435 -0.0275 723  LYS   E CE  
14419 N  NZ  . LYS   E 419 ? 1.1055 1.2144 1.1953 -0.0237 -0.0457 -0.0256 723  LYS   E NZ  
14420 N  N   . ILE   E 420 ? 0.9882 1.1144 1.1028 -0.0284 -0.0350 -0.0246 724  ILE   E N   
14421 C  CA  . ILE   E 420 ? 0.9951 1.1239 1.1135 -0.0298 -0.0333 -0.0235 724  ILE   E CA  
14422 C  C   . ILE   E 420 ? 1.0536 1.1862 1.1753 -0.0302 -0.0363 -0.0225 724  ILE   E C   
14423 O  O   . ILE   E 420 ? 1.0548 1.1868 1.1727 -0.0305 -0.0392 -0.0215 724  ILE   E O   
14424 C  CB  . ILE   E 420 ? 1.0069 1.1316 1.1173 -0.0321 -0.0312 -0.0216 724  ILE   E CB  
14425 C  CG1 . ILE   E 420 ? 1.0048 1.1311 1.1190 -0.0330 -0.0282 -0.0209 724  ILE   E CG1 
14426 C  CG2 . ILE   E 420 ? 0.9874 1.1108 1.0916 -0.0341 -0.0345 -0.0196 724  ILE   E CG2 
14427 C  CD1 . ILE   E 420 ? 0.9677 1.0891 1.0732 -0.0348 -0.0262 -0.0191 724  ILE   E CD1 
14428 N  N   . CYS   E 421 ? 1.1606 1.2967 1.2893 -0.0302 -0.0352 -0.0226 725  CYS   E N   
14429 C  CA  . CYS   E 421 ? 1.1583 1.2978 1.2904 -0.0304 -0.0377 -0.0217 725  CYS   E CA  
14430 C  C   . CYS   E 421 ? 1.1755 1.3171 1.3127 -0.0315 -0.0352 -0.0212 725  CYS   E C   
14431 O  O   . CYS   E 421 ? 1.1523 1.2936 1.2928 -0.0314 -0.0316 -0.0221 725  CYS   E O   
14432 C  CB  . CYS   E 421 ? 1.1170 1.2591 1.2546 -0.0278 -0.0407 -0.0235 725  CYS   E CB  
14433 S  SG  . CYS   E 421 ? 1.1769 1.3221 1.3258 -0.0260 -0.0388 -0.0264 725  CYS   E SG  
14434 N  N   . TYR   E 422 ? 1.1126 1.2562 1.2507 -0.0323 -0.0369 -0.0198 726  TYR   E N   
14435 C  CA  . TYR   E 422 ? 1.0886 1.2335 1.2302 -0.0335 -0.0348 -0.0189 726  TYR   E CA  
14436 C  C   . TYR   E 422 ? 1.1421 1.2911 1.2918 -0.0324 -0.0369 -0.0197 726  TYR   E C   
14437 O  O   . TYR   E 422 ? 1.1720 1.3222 1.3210 -0.0314 -0.0405 -0.0195 726  TYR   E O   
14438 C  CB  . TYR   E 422 ? 1.0725 1.2152 1.2066 -0.0356 -0.0348 -0.0162 726  TYR   E CB  
14439 C  CG  . TYR   E 422 ? 1.0946 1.2378 1.2309 -0.0368 -0.0328 -0.0150 726  TYR   E CG  
14440 C  CD1 . TYR   E 422 ? 1.1155 1.2570 1.2536 -0.0372 -0.0283 -0.0153 726  TYR   E CD1 
14441 C  CD2 . TYR   E 422 ? 1.1414 1.2863 1.2778 -0.0373 -0.0351 -0.0136 726  TYR   E CD2 
14442 C  CE1 . TYR   E 422 ? 1.1518 1.2931 1.2915 -0.0383 -0.0260 -0.0141 726  TYR   E CE1 
14443 C  CE2 . TYR   E 422 ? 1.1386 1.2834 1.2765 -0.0383 -0.0332 -0.0124 726  TYR   E CE2 
14444 C  CZ  . TYR   E 422 ? 1.1470 1.2899 1.2865 -0.0388 -0.0286 -0.0127 726  TYR   E CZ  
14445 O  OH  . TYR   E 422 ? 1.1790 1.3211 1.3197 -0.0398 -0.0264 -0.0115 726  TYR   E OH  
14446 N  N   . GLN   E 423 ? 1.1447 1.2955 1.3021 -0.0325 -0.0345 -0.0206 727  GLN   E N   
14447 C  CA  . GLN   E 423 ? 1.1541 1.3085 1.3206 -0.0314 -0.0364 -0.0219 727  GLN   E CA  
14448 C  C   . GLN   E 423 ? 1.2164 1.3708 1.3843 -0.0334 -0.0342 -0.0202 727  GLN   E C   
14449 O  O   . GLN   E 423 ? 1.2243 1.3786 1.3969 -0.0342 -0.0301 -0.0205 727  GLN   E O   
14450 C  CB  . GLN   E 423 ? 1.1594 1.3158 1.3355 -0.0298 -0.0358 -0.0249 727  GLN   E CB  
14451 C  CG  . GLN   E 423 ? 1.1969 1.3568 1.3829 -0.0284 -0.0386 -0.0267 727  GLN   E CG  
14452 C  CD  . GLN   E 423 ? 1.2081 1.3698 1.4016 -0.0257 -0.0408 -0.0301 727  GLN   E CD  
14453 O  OE1 . GLN   E 423 ? 1.2521 1.4162 1.4562 -0.0255 -0.0394 -0.0320 727  GLN   E OE1 
14454 N  NE2 . GLN   E 423 ? 1.2147 1.3751 1.4029 -0.0236 -0.0444 -0.0307 727  GLN   E NE2 
14455 N  N   . GLU   E 424 ? 1.2411 1.3955 1.4048 -0.0339 -0.0365 -0.0183 728  GLU   E N   
14456 C  CA  . GLU   E 424 ? 1.2255 1.3795 1.3895 -0.0356 -0.0347 -0.0166 728  GLU   E CA  
14457 C  C   . GLU   E 424 ? 1.2432 1.3998 1.4182 -0.0353 -0.0338 -0.0182 728  GLU   E C   
14458 O  O   . GLU   E 424 ? 1.2435 1.3991 1.4214 -0.0367 -0.0297 -0.0176 728  GLU   E O   
14459 C  CB  . GLU   E 424 ? 1.1553 1.3094 1.3140 -0.0358 -0.0378 -0.0146 728  GLU   E CB  
14460 N  N   . VAL   E 425 ? 1.2331 1.3924 1.4143 -0.0333 -0.0377 -0.0202 729  VAL   E N   
14461 C  CA  . VAL   E 425 ? 1.2533 1.4152 1.4460 -0.0327 -0.0381 -0.0223 729  VAL   E CA  
14462 C  C   . VAL   E 425 ? 1.2883 1.4505 1.4882 -0.0337 -0.0333 -0.0234 729  VAL   E C   
14463 O  O   . VAL   E 425 ? 1.3692 1.5326 1.5775 -0.0347 -0.0313 -0.0238 729  VAL   E O   
14464 C  CB  . VAL   E 425 ? 1.3016 1.4654 1.4985 -0.0298 -0.0432 -0.0250 729  VAL   E CB  
14465 C  CG1 . VAL   E 425 ? 1.3156 1.4821 1.5257 -0.0290 -0.0434 -0.0281 729  VAL   E CG1 
14466 C  CG2 . VAL   E 425 ? 1.2847 1.4484 1.4782 -0.0288 -0.0474 -0.0242 729  VAL   E CG2 
14467 N  N   . SER   E 426 ? 1.2932 1.4544 1.4905 -0.0334 -0.0312 -0.0239 730  SER   E N   
14468 C  CA  . SER   E 426 ? 1.2771 1.4384 1.4807 -0.0341 -0.0261 -0.0247 730  SER   E CA  
14469 C  C   . SER   E 426 ? 1.2678 1.4249 1.4630 -0.0360 -0.0206 -0.0221 730  SER   E C   
14470 O  O   . SER   E 426 ? 1.2816 1.4379 1.4809 -0.0367 -0.0154 -0.0223 730  SER   E O   
14471 C  CB  . SER   E 426 ? 1.3378 1.5004 1.5446 -0.0321 -0.0270 -0.0273 730  SER   E CB  
14472 O  OG  . SER   E 426 ? 1.4346 1.6003 1.6489 -0.0298 -0.0323 -0.0299 730  SER   E OG  
14473 N  N   . GLN   E 427 ? 1.3463 1.5004 1.5297 -0.0368 -0.0218 -0.0197 731  GLN   E N   
14474 C  CA  . GLN   E 427 ? 1.3836 1.5328 1.5575 -0.0384 -0.0175 -0.0172 731  GLN   E CA  
14475 C  C   . GLN   E 427 ? 1.3799 1.5267 1.5504 -0.0379 -0.0143 -0.0179 731  GLN   E C   
14476 O  O   . GLN   E 427 ? 1.3593 1.5021 1.5261 -0.0387 -0.0090 -0.0167 731  GLN   E O   
14477 C  CB  . GLN   E 427 ? 1.4029 1.5506 1.5800 -0.0399 -0.0129 -0.0159 731  GLN   E CB  
14478 C  CG  . GLN   E 427 ? 1.4256 1.5738 1.6021 -0.0407 -0.0154 -0.0145 731  GLN   E CG  
14479 C  CD  . GLN   E 427 ? 1.4815 1.6267 1.6454 -0.0410 -0.0179 -0.0122 731  GLN   E CD  
14480 O  OE1 . GLN   E 427 ? 1.5122 1.6526 1.6676 -0.0420 -0.0150 -0.0102 731  GLN   E OE1 
14481 N  NE2 . GLN   E 427 ? 1.4982 1.6460 1.6608 -0.0401 -0.0234 -0.0126 731  GLN   E NE2 
14482 N  N   . CYS   E 428 ? 1.2513 1.3997 1.4223 -0.0363 -0.0174 -0.0197 732  CYS   E N   
14483 C  CA  . CYS   E 428 ? 1.1467 1.2929 1.3150 -0.0355 -0.0148 -0.0205 732  CYS   E CA  
14484 C  C   . CYS   E 428 ? 1.0892 1.2350 1.2512 -0.0344 -0.0193 -0.0211 732  CYS   E C   
14485 O  O   . CYS   E 428 ? 1.0732 1.2208 1.2344 -0.0340 -0.0242 -0.0210 732  CYS   E O   
14486 C  CB  . CYS   E 428 ? 1.1333 1.2828 1.3142 -0.0344 -0.0122 -0.0230 732  CYS   E CB  
14487 S  SG  . CYS   E 428 ? 1.3715 1.5264 1.5618 -0.0321 -0.0185 -0.0262 732  CYS   E SG  
14488 N  N   . PHE   E 429 ? 1.0913 1.2340 1.2484 -0.0338 -0.0174 -0.0216 733  PHE   E N   
14489 C  CA  . PHE   E 429 ? 1.0637 1.2051 1.2145 -0.0329 -0.0208 -0.0221 733  PHE   E CA  
14490 C  C   . PHE   E 429 ? 1.1184 1.2619 1.2762 -0.0306 -0.0211 -0.0250 733  PHE   E C   
14491 O  O   . PHE   E 429 ? 1.0919 1.2362 1.2563 -0.0300 -0.0171 -0.0262 733  PHE   E O   
14492 C  CB  . PHE   E 429 ? 1.0442 1.1797 1.1830 -0.0338 -0.0190 -0.0206 733  PHE   E CB  
14493 C  CG  . PHE   E 429 ? 1.0890 1.2219 1.2195 -0.0357 -0.0203 -0.0181 733  PHE   E CG  
14494 C  CD1 . PHE   E 429 ? 1.1261 1.2563 1.2539 -0.0369 -0.0166 -0.0165 733  PHE   E CD1 
14495 C  CD2 . PHE   E 429 ? 1.0734 1.2063 1.1987 -0.0361 -0.0249 -0.0173 733  PHE   E CD2 
14496 C  CE1 . PHE   E 429 ? 1.0531 1.1806 1.1729 -0.0384 -0.0183 -0.0142 733  PHE   E CE1 
14497 C  CE2 . PHE   E 429 ? 1.0538 1.1848 1.1724 -0.0377 -0.0264 -0.0151 733  PHE   E CE2 
14498 C  CZ  . PHE   E 429 ? 1.0582 1.1865 1.1739 -0.0388 -0.0233 -0.0136 733  PHE   E CZ  
14499 N  N   . GLY   E 430 ? 1.1289 1.2732 1.2853 -0.0291 -0.0257 -0.0260 734  GLY   E N   
14500 C  CA  . GLY   E 430 ? 1.1029 1.2479 1.2632 -0.0267 -0.0265 -0.0286 734  GLY   E CA  
14501 C  C   . GLY   E 430 ? 1.1037 1.2440 1.2539 -0.0265 -0.0262 -0.0282 734  GLY   E C   
14502 O  O   . GLY   E 430 ? 1.1055 1.2436 1.2477 -0.0271 -0.0292 -0.0270 734  GLY   E O   
14503 N  N   . VAL   E 431 ? 0.9731 1.1116 1.1239 -0.0255 -0.0228 -0.0294 735  VAL   E N   
14504 C  CA  . VAL   E 431 ? 0.9623 1.0956 1.1031 -0.0253 -0.0224 -0.0292 735  VAL   E CA  
14505 C  C   . VAL   E 431 ? 0.9377 1.0716 1.0829 -0.0224 -0.0226 -0.0320 735  VAL   E C   
14506 O  O   . VAL   E 431 ? 0.9656 1.1024 1.1204 -0.0212 -0.0199 -0.0336 735  VAL   E O   
14507 C  CB  . VAL   E 431 ? 0.9841 1.1127 1.1176 -0.0269 -0.0176 -0.0276 735  VAL   E CB  
14508 C  CG1 . VAL   E 431 ? 0.9930 1.1160 1.1172 -0.0261 -0.0171 -0.0280 735  VAL   E CG1 
14509 C  CG2 . VAL   E 431 ? 0.9615 1.0884 1.0884 -0.0294 -0.0184 -0.0250 735  VAL   E CG2 
14510 N  N   . LEU   E 432 ? 0.9163 1.0473 1.0548 -0.0214 -0.0257 -0.0324 736  LEU   E N   
14511 C  CA  . LEU   E 432 ? 0.8982 1.0285 1.0387 -0.0185 -0.0261 -0.0348 736  LEU   E CA  
14512 C  C   . LEU   E 432 ? 0.9078 1.0325 1.0401 -0.0187 -0.0226 -0.0345 736  LEU   E C   
14513 O  O   . LEU   E 432 ? 0.9519 1.0719 1.0735 -0.0206 -0.0228 -0.0326 736  LEU   E O   
14514 C  CB  . LEU   E 432 ? 0.8977 1.0270 1.0348 -0.0170 -0.0314 -0.0355 736  LEU   E CB  
14515 C  CG  . LEU   E 432 ? 0.8766 1.0101 1.0210 -0.0153 -0.0356 -0.0366 736  LEU   E CG  
14516 C  CD1 . LEU   E 432 ? 0.8805 1.0112 1.0192 -0.0134 -0.0399 -0.0372 736  LEU   E CD1 
14517 C  CD2 . LEU   E 432 ? 0.9086 1.0468 1.0660 -0.0132 -0.0348 -0.0393 736  LEU   E CD2 
14518 N  N   . SER   E 433 ? 0.9145 1.0396 1.0520 -0.0165 -0.0196 -0.0365 737  SER   E N   
14519 C  CA  . SER   E 433 ? 0.9212 1.0409 1.0515 -0.0163 -0.0155 -0.0363 737  SER   E CA  
14520 C  C   . SER   E 433 ? 0.9617 1.0807 1.0942 -0.0130 -0.0159 -0.0389 737  SER   E C   
14521 O  O   . SER   E 433 ? 0.9806 1.1040 1.1222 -0.0108 -0.0187 -0.0410 737  SER   E O   
14522 C  CB  . SER   E 433 ? 0.9453 1.0656 1.0795 -0.0171 -0.0093 -0.0357 737  SER   E CB  
14523 O  OG  . SER   E 433 ? 0.9449 1.0706 1.0931 -0.0151 -0.0073 -0.0378 737  SER   E OG  
14524 N  N   . SER   E 434 ? 0.9479 1.0608 1.0714 -0.0125 -0.0134 -0.0388 738  SER   E N   
14525 C  CA  . SER   E 434 ? 0.9597 1.0712 1.0847 -0.0092 -0.0128 -0.0412 738  SER   E CA  
14526 C  C   . SER   E 434 ? 0.9756 1.0826 1.0961 -0.0088 -0.0067 -0.0409 738  SER   E C   
14527 O  O   . SER   E 434 ? 0.9896 1.0908 1.0987 -0.0108 -0.0051 -0.0390 738  SER   E O   
14528 C  CB  . SER   E 434 ? 1.0134 1.1205 1.1295 -0.0083 -0.0175 -0.0416 738  SER   E CB  
14529 O  OG  . SER   E 434 ? 1.0865 1.1868 1.1890 -0.0106 -0.0176 -0.0396 738  SER   E OG  
14530 N  N   . ARG   E 435 ? 0.9988 1.1085 1.1285 -0.0061 -0.0033 -0.0430 739  ARG   E N   
14531 C  CA  . ARG   E 435 ? 1.0230 1.1290 1.1504 -0.0051 0.0033  -0.0429 739  ARG   E CA  
14532 C  C   . ARG   E 435 ? 1.0405 1.1437 1.1664 -0.0016 0.0031  -0.0452 739  ARG   E C   
14533 O  O   . ARG   E 435 ? 1.0702 1.1772 1.2030 0.0005  -0.0010 -0.0473 739  ARG   E O   
14534 C  CB  . ARG   E 435 ? 1.0119 1.1238 1.1532 -0.0049 0.0086  -0.0432 739  ARG   E CB  
14535 C  CG  . ARG   E 435 ? 1.1115 1.2206 1.2535 -0.0032 0.0163  -0.0434 739  ARG   E CG  
14536 C  CD  . ARG   E 435 ? 1.1514 1.2682 1.3111 -0.0028 0.0206  -0.0442 739  ARG   E CD  
14537 N  NE  . ARG   E 435 ? 1.1447 1.2690 1.3194 -0.0004 0.0169  -0.0473 739  ARG   E NE  
14538 C  CZ  . ARG   E 435 ? 1.0948 1.2270 1.2848 -0.0010 0.0155  -0.0483 739  ARG   E CZ  
14539 N  NH1 . ARG   E 435 ? 1.1679 1.3020 1.3602 -0.0040 0.0169  -0.0463 739  ARG   E NH1 
14540 N  NH2 . ARG   E 435 ? 1.0947 1.2328 1.2980 0.0017  0.0123  -0.0514 739  ARG   E NH2 
14541 N  N   . ILE   E 436 ? 1.0728 1.1689 1.1886 -0.0008 0.0070  -0.0447 740  ILE   E N   
14542 C  CA  . ILE   E 436 ? 1.1203 1.2130 1.2332 0.0025  0.0069  -0.0468 740  ILE   E CA  
14543 C  C   . ILE   E 436 ? 1.1879 1.2825 1.3097 0.0052  0.0138  -0.0480 740  ILE   E C   
14544 O  O   . ILE   E 436 ? 1.1711 1.2630 1.2901 0.0044  0.0201  -0.0465 740  ILE   E O   
14545 C  CB  . ILE   E 436 ? 1.1383 1.2208 1.2331 0.0019  0.0060  -0.0457 740  ILE   E CB  
14546 C  CG1 . ILE   E 436 ? 1.1333 1.2146 1.2210 -0.0011 -0.0005 -0.0443 740  ILE   E CG1 
14547 C  CG2 . ILE   E 436 ? 1.2035 1.2821 1.2954 0.0056  0.0059  -0.0479 740  ILE   E CG2 
14548 C  CD1 . ILE   E 436 ? 1.1044 1.1857 1.1886 -0.0050 -0.0001 -0.0415 740  ILE   E CD1 
14549 N  N   . GLU   E 437 ? 1.2593 1.3587 1.3923 0.0084  0.0126  -0.0508 741  GLU   E N   
14550 C  CA  . GLU   E 437 ? 1.3002 1.4021 1.4434 0.0115  0.0186  -0.0524 741  GLU   E CA  
14551 C  C   . GLU   E 437 ? 1.3207 1.4185 1.4593 0.0153  0.0173  -0.0545 741  GLU   E C   
14552 O  O   . GLU   E 437 ? 1.3445 1.4395 1.4759 0.0157  0.0111  -0.0552 741  GLU   E O   
14553 C  CB  . GLU   E 437 ? 1.3159 1.4285 1.4797 0.0122  0.0181  -0.0542 741  GLU   E CB  
14554 C  CG  . GLU   E 437 ? 1.2873 1.4042 1.4567 0.0086  0.0190  -0.0522 741  GLU   E CG  
14555 C  CD  . GLU   E 437 ? 1.3093 1.4357 1.4997 0.0093  0.0212  -0.0538 741  GLU   E CD  
14556 O  OE1 . GLU   E 437 ? 1.3203 1.4509 1.5221 0.0127  0.0203  -0.0568 741  GLU   E OE1 
14557 O  OE2 . GLU   E 437 ? 1.3096 1.4391 1.5054 0.0065  0.0237  -0.0522 741  GLU   E OE2 
14558 N  N   . VAL   E 438 ? 1.3293 1.4264 1.4719 0.0181  0.0237  -0.0555 742  VAL   E N   
14559 C  CA  . VAL   E 438 ? 1.4245 1.5182 1.5645 0.0222  0.0234  -0.0577 742  VAL   E CA  
14560 C  C   . VAL   E 438 ? 1.4861 1.5887 1.6461 0.0256  0.0245  -0.0606 742  VAL   E C   
14561 O  O   . VAL   E 438 ? 1.5179 1.6264 1.6911 0.0251  0.0298  -0.0604 742  VAL   E O   
14562 C  CB  . VAL   E 438 ? 1.4688 1.5531 1.5954 0.0233  0.0298  -0.0566 742  VAL   E CB  
14563 C  CG1 . VAL   E 438 ? 1.5537 1.6360 1.6816 0.0281  0.0311  -0.0591 742  VAL   E CG1 
14564 C  CG2 . VAL   E 438 ? 1.4729 1.5479 1.5795 0.0206  0.0267  -0.0545 742  VAL   E CG2 
14565 N  N   . GLN   E 439 ? 1.5672 1.6706 1.7298 0.0289  0.0193  -0.0633 743  GLN   E N   
14566 C  CA  . GLN   E 439 ? 1.6105 1.7219 1.7918 0.0326  0.0192  -0.0665 743  GLN   E CA  
14567 C  C   . GLN   E 439 ? 1.6121 1.7247 1.8015 0.0347  0.0284  -0.0669 743  GLN   E C   
14568 O  O   . GLN   E 439 ? 1.6242 1.7298 1.8037 0.0370  0.0322  -0.0668 743  GLN   E O   
14569 C  CB  . GLN   E 439 ? 1.6931 1.8020 1.8710 0.0364  0.0129  -0.0691 743  GLN   E CB  
14570 C  CG  . GLN   E 439 ? 1.8054 1.9220 2.0020 0.0408  0.0119  -0.0728 743  GLN   E CG  
14571 C  CD  . GLN   E 439 ? 1.7945 1.9191 2.0042 0.0403  0.0051  -0.0743 743  GLN   E CD  
14572 O  OE1 . GLN   E 439 ? 1.6537 1.7816 1.8659 0.0364  0.0047  -0.0726 743  GLN   E OE1 
14573 N  NE2 . GLN   E 439 ? 1.9152 2.0425 2.1328 0.0445  -0.0006 -0.0778 743  GLN   E NE2 
14574 N  N   . THR   E 441 ? 1.6661 1.7913 1.8943 0.0417  0.0459  -0.0703 745  THR   E N   
14575 C  CA  . THR   E 441 ? 1.7375 1.8653 1.9759 0.0470  0.0469  -0.0735 745  THR   E CA  
14576 C  C   . THR   E 441 ? 1.7523 1.8924 2.0161 0.0485  0.0433  -0.0768 745  THR   E C   
14577 O  O   . THR   E 441 ? 1.7873 1.9296 2.0567 0.0524  0.0374  -0.0800 745  THR   E O   
14578 C  CB  . THR   E 441 ? 1.7310 1.8557 1.9697 0.0491  0.0584  -0.0726 745  THR   E CB  
14579 O  OG1 . THR   E 441 ? 1.7414 1.8705 1.9905 0.0463  0.0660  -0.0706 745  THR   E OG1 
14580 C  CG2 . THR   E 441 ? 1.7880 1.8995 2.0011 0.0491  0.0608  -0.0704 745  THR   E CG2 
14581 N  N   . SER   E 442 ? 1.7254 1.8730 2.0043 0.0456  0.0466  -0.0759 746  SER   E N   
14582 C  CA  . SER   E 442 ? 1.7042 1.8635 2.0091 0.0470  0.0441  -0.0791 746  SER   E CA  
14583 C  C   . SER   E 442 ? 1.6864 1.8490 1.9931 0.0461  0.0324  -0.0808 746  SER   E C   
14584 O  O   . SER   E 442 ? 1.6943 1.8635 2.0128 0.0433  0.0300  -0.0809 746  SER   E O   
14585 C  CB  . SER   E 442 ? 1.6434 1.8090 1.9641 0.0441  0.0525  -0.0775 746  SER   E CB  
14586 O  OG  . SER   E 442 ? 1.6871 1.8512 2.0004 0.0390  0.0516  -0.0746 746  SER   E OG  
14587 N  N   . GLY   E 443 ? 1.6871 1.8443 1.9811 0.0487  0.0251  -0.0822 747  GLY   E N   
14588 C  CA  . GLY   E 443 ? 1.7069 1.8648 1.9983 0.0485  0.0142  -0.0836 747  GLY   E CA  
14589 C  C   . GLY   E 443 ? 1.6762 1.8335 1.9608 0.0432  0.0127  -0.0807 747  GLY   E C   
14590 O  O   . GLY   E 443 ? 1.6530 1.8153 1.9459 0.0423  0.0060  -0.0819 747  GLY   E O   
14591 N  N   . GLY   E 444 ? 1.6776 1.8286 1.9475 0.0398  0.0187  -0.0769 748  GLY   E N   
14592 C  CA  . GLY   E 444 ? 1.5734 1.7244 1.8383 0.0348  0.0181  -0.0740 748  GLY   E CA  
14593 C  C   . GLY   E 444 ? 1.5619 1.7034 1.8053 0.0320  0.0223  -0.0703 748  GLY   E C   
14594 O  O   . GLY   E 444 ? 1.5736 1.7093 1.8086 0.0334  0.0283  -0.0695 748  GLY   E O   
14595 N  N   . THR   E 445 ? 1.5395 1.6794 1.7745 0.0280  0.0189  -0.0680 749  THR   E N   
14596 C  CA  . THR   E 445 ? 1.4563 1.5877 1.6717 0.0248  0.0216  -0.0644 749  THR   E CA  
14597 C  C   . THR   E 445 ? 1.4043 1.5369 1.6232 0.0218  0.0297  -0.0619 749  THR   E C   
14598 O  O   . THR   E 445 ? 1.3846 1.5247 1.6185 0.0202  0.0303  -0.0620 749  THR   E O   
14599 C  CB  . THR   E 445 ? 1.4090 1.5382 1.6138 0.0223  0.0138  -0.0633 749  THR   E CB  
14600 O  OG1 . THR   E 445 ? 1.3569 1.4933 1.5733 0.0197  0.0118  -0.0630 749  THR   E OG1 
14601 C  CG2 . THR   E 445 ? 1.4711 1.5989 1.6726 0.0254  0.0060  -0.0657 749  THR   E CG2 
14602 N  N   . THR   E 446 ? 1.4037 1.5281 1.6080 0.0212  0.0357  -0.0595 750  THR   E N   
14603 C  CA  . THR   E 446 ? 1.3877 1.5106 1.5909 0.0186  0.0437  -0.0567 750  THR   E CA  
14604 C  C   . THR   E 446 ? 1.3851 1.4999 1.5681 0.0153  0.0419  -0.0536 750  THR   E C   
14605 O  O   . THR   E 446 ? 1.4081 1.5158 1.5755 0.0159  0.0382  -0.0535 750  THR   E O   
14606 C  CB  . THR   E 446 ? 1.4321 1.5515 1.6355 0.0213  0.0532  -0.0566 750  THR   E CB  
14607 O  OG1 . THR   E 446 ? 1.5610 1.6788 1.7640 0.0191  0.0614  -0.0538 750  THR   E OG1 
14608 C  CG2 . THR   E 446 ? 1.3846 1.4933 1.5679 0.0234  0.0531  -0.0563 750  THR   E CG2 
14609 N  N   . ALA   E 447 ? 1.3359 1.4518 1.5196 0.0118  0.0441  -0.0512 751  ALA   E N   
14610 C  CA  . ALA   E 447 ? 1.3118 1.4204 1.4774 0.0087  0.0422  -0.0484 751  ALA   E CA  
14611 C  C   . ALA   E 447 ? 1.3088 1.4065 1.4572 0.0097  0.0478  -0.0469 751  ALA   E C   
14612 O  O   . ALA   E 447 ? 1.2626 1.3585 1.4136 0.0126  0.0546  -0.0475 751  ALA   E O   
14613 C  CB  . ALA   E 447 ? 1.3052 1.4173 1.4757 0.0051  0.0436  -0.0463 751  ALA   E CB  
14614 N  N   . LEU   E 448 ? 1.3066 1.3965 1.4370 0.0075  0.0449  -0.0448 752  LEU   E N   
14615 C  CA  . LEU   E 448 ? 1.2254 1.3039 1.3375 0.0083  0.0488  -0.0434 752  LEU   E CA  
14616 C  C   . LEU   E 448 ? 1.1795 1.2528 1.2833 0.0061  0.0539  -0.0405 752  LEU   E C   
14617 O  O   . LEU   E 448 ? 1.1436 1.2077 1.2351 0.0076  0.0594  -0.0394 752  LEU   E O   
14618 C  CB  . LEU   E 448 ? 1.2485 1.3204 1.3448 0.0077  0.0414  -0.0435 752  LEU   E CB  
14619 C  CG  . LEU   E 448 ? 1.2931 1.3679 1.3929 0.0093  0.0346  -0.0461 752  LEU   E CG  
14620 C  CD1 . LEU   E 448 ? 1.2689 1.3353 1.3511 0.0083  0.0290  -0.0455 752  LEU   E CD1 
14621 C  CD2 . LEU   E 448 ? 1.3128 1.3890 1.4203 0.0137  0.0382  -0.0485 752  LEU   E CD2 
14622 N  N   . ARG   E 449 ? 1.2111 1.2894 1.3207 0.0029  0.0520  -0.0391 753  ARG   E N   
14623 C  CA  . ARG   E 449 ? 1.2113 1.2847 1.3122 0.0005  0.0551  -0.0362 753  ARG   E CA  
14624 C  C   . ARG   E 449 ? 1.2137 1.2964 1.3291 -0.0022 0.0540  -0.0356 753  ARG   E C   
14625 O  O   . ARG   E 449 ? 1.2372 1.3277 1.3625 -0.0030 0.0474  -0.0371 753  ARG   E O   
14626 C  CB  . ARG   E 449 ? 1.2320 1.2968 1.3134 -0.0013 0.0496  -0.0348 753  ARG   E CB  
14627 C  CG  . ARG   E 449 ? 1.2313 1.3013 1.3149 -0.0037 0.0400  -0.0354 753  ARG   E CG  
14628 C  CD  . ARG   E 449 ? 1.1943 1.2561 1.2602 -0.0052 0.0346  -0.0344 753  ARG   E CD  
14629 N  NE  . ARG   E 449 ? 1.2048 1.2614 1.2626 -0.0031 0.0321  -0.0360 753  ARG   E NE  
14630 C  CZ  . ARG   E 449 ? 1.2170 1.2635 1.2612 -0.0012 0.0355  -0.0358 753  ARG   E CZ  
14631 N  NH1 . ARG   E 449 ? 1.2127 1.2531 1.2500 -0.0008 0.0420  -0.0342 753  ARG   E NH1 
14632 N  NH2 . ARG   E 449 ? 1.2420 1.2837 1.2786 0.0003  0.0323  -0.0373 753  ARG   E NH2 
14633 N  N   . PRO   E 450 ? 1.2052 1.2867 1.3216 -0.0035 0.0601  -0.0335 754  PRO   E N   
14634 C  CA  . PRO   E 450 ? 1.1581 1.2480 1.2884 -0.0060 0.0593  -0.0329 754  PRO   E CA  
14635 C  C   . PRO   E 450 ? 1.1234 1.2139 1.2475 -0.0090 0.0512  -0.0319 754  PRO   E C   
14636 O  O   . PRO   E 450 ? 1.1534 1.2393 1.2687 -0.0110 0.0525  -0.0295 754  PRO   E O   
14637 C  CB  . PRO   E 450 ? 1.2326 1.3181 1.3612 -0.0063 0.0687  -0.0305 754  PRO   E CB  
14638 C  CG  . PRO   E 450 ? 1.2482 1.3207 1.3543 -0.0052 0.0706  -0.0290 754  PRO   E CG  
14639 C  CD  . PRO   E 450 ? 1.2281 1.2991 1.3307 -0.0026 0.0677  -0.0313 754  PRO   E CD  
14640 N  N   . SER   E 451 ? 1.1051 1.2009 1.2334 -0.0093 0.0432  -0.0337 755  SER   E N   
14641 C  CA  . SER   E 451 ? 1.0738 1.1699 1.1960 -0.0120 0.0359  -0.0326 755  SER   E CA  
14642 C  C   . SER   E 451 ? 1.0908 1.1945 1.2257 -0.0142 0.0353  -0.0320 755  SER   E C   
14643 O  O   . SER   E 451 ? 1.1704 1.2776 1.3167 -0.0140 0.0411  -0.0320 755  SER   E O   
14644 C  CB  . SER   E 451 ? 1.1070 1.2044 1.2272 -0.0113 0.0283  -0.0345 755  SER   E CB  
14645 O  OG  . SER   E 451 ? 1.1569 1.2625 1.2929 -0.0095 0.0268  -0.0371 755  SER   E OG  
14646 N  N   . ALA   E 452 ? 1.0839 1.1899 1.2169 -0.0164 0.0284  -0.0314 756  ALA   E N   
14647 C  CA  . ALA   E 452 ? 1.0962 1.2081 1.2388 -0.0186 0.0277  -0.0305 756  ALA   E CA  
14648 C  C   . ALA   E 452 ? 1.1193 1.2407 1.2809 -0.0177 0.0261  -0.0330 756  ALA   E C   
14649 O  O   . ALA   E 452 ? 1.1593 1.2855 1.3322 -0.0188 0.0284  -0.0327 756  ALA   E O   
14650 C  CB  . ALA   E 452 ? 1.0233 1.1348 1.1582 -0.0209 0.0208  -0.0292 756  ALA   E CB  
14651 N  N   . SER   E 453 ? 1.1337 1.2578 1.2988 -0.0156 0.0219  -0.0354 757  SER   E N   
14652 C  CA  . SER   E 453 ? 1.1187 1.2513 1.3012 -0.0143 0.0194  -0.0381 757  SER   E CA  
14653 C  C   . SER   E 453 ? 1.1563 1.2917 1.3516 -0.0127 0.0263  -0.0393 757  SER   E C   
14654 O  O   . SER   E 453 ? 1.2067 1.3491 1.4183 -0.0129 0.0267  -0.0406 757  SER   E O   
14655 C  CB  . SER   E 453 ? 1.0947 1.2284 1.2759 -0.0123 0.0124  -0.0403 757  SER   E CB  
14656 O  OG  . SER   E 453 ? 1.0760 1.2036 1.2468 -0.0105 0.0138  -0.0406 757  SER   E OG  
14657 N  N   . THR   E 454 ? 1.1472 1.2770 1.3355 -0.0112 0.0320  -0.0390 758  THR   E N   
14658 C  CA  . THR   E 454 ? 1.2519 1.3843 1.4528 -0.0096 0.0395  -0.0399 758  THR   E CA  
14659 C  C   . THR   E 454 ? 1.3323 1.4658 1.5394 -0.0119 0.0457  -0.0378 758  THR   E C   
14660 O  O   . THR   E 454 ? 1.3374 1.4779 1.5625 -0.0119 0.0481  -0.0391 758  THR   E O   
14661 C  CB  . THR   E 454 ? 1.2490 1.3745 1.4401 -0.0071 0.0446  -0.0399 758  THR   E CB  
14662 O  OG1 . THR   E 454 ? 1.2738 1.3905 1.4496 -0.0083 0.0499  -0.0368 758  THR   E OG1 
14663 C  CG2 . THR   E 454 ? 1.2222 1.3451 1.4037 -0.0054 0.0380  -0.0414 758  THR   E CG2 
14664 N  N   . GLN   E 455 ? 1.4507 1.5773 1.6433 -0.0139 0.0479  -0.0348 759  GLN   E N   
14665 C  CA  . GLN   E 455 ? 1.4801 1.6062 1.6763 -0.0160 0.0542  -0.0325 759  GLN   E CA  
14666 C  C   . GLN   E 455 ? 1.4704 1.6003 1.6698 -0.0188 0.0487  -0.0317 759  GLN   E C   
14667 O  O   . GLN   E 455 ? 1.5004 1.6256 1.6894 -0.0208 0.0496  -0.0290 759  GLN   E O   
14668 C  CB  . GLN   E 455 ? 1.5137 1.6289 1.6919 -0.0161 0.0604  -0.0296 759  GLN   E CB  
14669 C  CG  . GLN   E 455 ? 1.5400 1.6486 1.7069 -0.0133 0.0626  -0.0301 759  GLN   E CG  
14670 C  CD  . GLN   E 455 ? 1.6216 1.7324 1.8005 -0.0108 0.0702  -0.0315 759  GLN   E CD  
14671 O  OE1 . GLN   E 455 ? 1.6626 1.7730 1.8477 -0.0110 0.0786  -0.0301 759  GLN   E OE1 
14672 N  NE2 . GLN   E 455 ? 1.6193 1.7328 1.8021 -0.0082 0.0673  -0.0342 759  GLN   E NE2 
14673 N  N   . ALA   E 456 ? 1.3473 1.4858 1.5612 -0.0188 0.0430  -0.0341 760  ALA   E N   
14674 C  CA  . ALA   E 456 ? 1.2483 1.3908 1.4667 -0.0211 0.0382  -0.0336 760  ALA   E CA  
14675 C  C   . ALA   E 456 ? 1.2998 1.4476 1.5359 -0.0222 0.0431  -0.0338 760  ALA   E C   
14676 O  O   . ALA   E 456 ? 1.3434 1.4931 1.5902 -0.0210 0.0493  -0.0347 760  ALA   E O   
14677 C  CB  . ALA   E 456 ? 1.1423 1.2898 1.3643 -0.0203 0.0285  -0.0359 760  ALA   E CB  
14678 N  N   . LEU   E 457 ? 1.2977 1.4478 1.5369 -0.0246 0.0403  -0.0328 761  LEU   E N   
14679 C  CA  . LEU   E 457 ? 1.2138 1.3688 1.4700 -0.0261 0.0441  -0.0330 761  LEU   E CA  
14680 C  C   . LEU   E 457 ? 1.1825 1.3466 1.4578 -0.0250 0.0387  -0.0367 761  LEU   E C   
14681 O  O   . LEU   E 457 ? 1.2201 1.3885 1.5106 -0.0238 0.0425  -0.0386 761  LEU   E O   
14682 C  CB  . LEU   E 457 ? 1.1575 1.3105 1.4085 -0.0289 0.0435  -0.0304 761  LEU   E CB  
14683 C  CG  . LEU   E 457 ? 1.1901 1.3336 1.4214 -0.0300 0.0476  -0.0267 761  LEU   E CG  
14684 C  CD1 . LEU   E 457 ? 1.1995 1.3416 1.4283 -0.0326 0.0472  -0.0244 761  LEU   E CD1 
14685 C  CD2 . LEU   E 457 ? 1.2054 1.3436 1.4340 -0.0291 0.0577  -0.0254 761  LEU   E CD2 
14686 N  N   . SER   E 458 ? 1.2072 1.3742 1.4820 -0.0251 0.0296  -0.0379 762  SER   E N   
14687 C  CA  . SER   E 458 ? 1.1972 1.3712 1.4862 -0.0232 0.0231  -0.0417 762  SER   E CA  
14688 C  C   . SER   E 458 ? 1.1816 1.3541 1.4631 -0.0202 0.0198  -0.0434 762  SER   E C   
14689 O  O   . SER   E 458 ? 1.1975 1.3638 1.4614 -0.0201 0.0198  -0.0415 762  SER   E O   
14690 C  CB  . SER   E 458 ? 1.2091 1.3859 1.4995 -0.0240 0.0147  -0.0424 762  SER   E CB  
14691 O  OG  . SER   E 458 ? 1.2057 1.3815 1.4958 -0.0270 0.0169  -0.0400 762  SER   E OG  
14692 N  N   . SER   E 459 ? 1.0696 1.2474 1.3645 -0.0177 0.0167  -0.0470 763  SER   E N   
14693 C  CA  . SER   E 459 ? 1.0726 1.2490 1.3605 -0.0146 0.0122  -0.0488 763  SER   E CA  
14694 C  C   . SER   E 459 ? 1.0930 1.2756 1.3952 -0.0121 0.0050  -0.0529 763  SER   E C   
14695 O  O   . SER   E 459 ? 1.1519 1.3399 1.4719 -0.0111 0.0071  -0.0552 763  SER   E O   
14696 C  CB  . SER   E 459 ? 1.1201 1.2931 1.4042 -0.0131 0.0192  -0.0484 763  SER   E CB  
14697 O  OG  . SER   E 459 ? 1.1477 1.3261 1.4483 -0.0106 0.0201  -0.0516 763  SER   E OG  
14698 N  N   . SER   E 460 ? 1.1079 1.2894 1.4023 -0.0109 -0.0035 -0.0538 764  SER   E N   
14699 C  CA  . SER   E 460 ? 1.0827 1.2683 1.3866 -0.0078 -0.0114 -0.0577 764  SER   E CA  
14700 C  C   . SER   E 460 ? 1.1217 1.3042 1.4167 -0.0044 -0.0145 -0.0591 764  SER   E C   
14701 O  O   . SER   E 460 ? 1.1366 1.3131 1.4147 -0.0049 -0.0132 -0.0568 764  SER   E O   
14702 C  CB  . SER   E 460 ? 1.0794 1.2652 1.3805 -0.0085 -0.0188 -0.0577 764  SER   E CB  
14703 O  OG  . SER   E 460 ? 1.0789 1.2591 1.3610 -0.0098 -0.0198 -0.0546 764  SER   E OG  
14704 N  N   . VAL   E 461 ? 1.1273 1.3136 1.4340 -0.0010 -0.0187 -0.0630 765  VAL   E N   
14705 C  CA  . VAL   E 461 ? 1.1341 1.3174 1.4337 0.0027  -0.0223 -0.0648 765  VAL   E CA  
14706 C  C   . VAL   E 461 ? 1.1431 1.3277 1.4455 0.0057  -0.0321 -0.0678 765  VAL   E C   
14707 O  O   . VAL   E 461 ? 1.1573 1.3473 1.4761 0.0068  -0.0355 -0.0708 765  VAL   E O   
14708 C  CB  . VAL   E 461 ? 1.1169 1.3025 1.4265 0.0050  -0.0176 -0.0667 765  VAL   E CB  
14709 C  CG1 . VAL   E 461 ? 1.1634 1.3474 1.4700 0.0095  -0.0234 -0.0696 765  VAL   E CG1 
14710 C  CG2 . VAL   E 461 ? 1.1362 1.3175 1.4360 0.0030  -0.0084 -0.0635 765  VAL   E CG2 
14711 N  N   . SER   E 462 ? 1.1979 1.3768 1.4842 0.0070  -0.0367 -0.0671 766  SER   E N   
14712 C  CA  . SER   E 462 ? 1.1972 1.3755 1.4823 0.0096  -0.0457 -0.0692 766  SER   E CA  
14713 C  C   . SER   E 462 ? 1.3038 1.4848 1.6005 0.0143  -0.0506 -0.0738 766  SER   E C   
14714 O  O   . SER   E 462 ? 1.2565 1.4378 1.5562 0.0162  -0.0480 -0.0751 766  SER   E O   
14715 C  CB  . SER   E 462 ? 1.1637 1.3349 1.4287 0.0101  -0.0486 -0.0672 766  SER   E CB  
14716 O  OG  . SER   E 462 ? 1.1399 1.3103 1.4022 0.0109  -0.0553 -0.0677 766  SER   E OG  
14717 N  N   . SER   E 463 ? 1.4300 1.6125 1.7326 0.0163  -0.0583 -0.0763 767  SER   E N   
14718 C  CA  . SER   E 463 ? 1.4893 1.6746 1.8046 0.0209  -0.0644 -0.0811 767  SER   E CA  
14719 C  C   . SER   E 463 ? 1.5107 1.6920 1.8184 0.0239  -0.0738 -0.0827 767  SER   E C   
14720 O  O   . SER   E 463 ? 1.5051 1.6880 1.8172 0.0229  -0.0772 -0.0829 767  SER   E O   
14721 C  CB  . SER   E 463 ? 1.5144 1.7077 1.8523 0.0198  -0.0630 -0.0833 767  SER   E CB  
14722 O  OG  . SER   E 463 ? 1.5434 1.7390 1.8924 0.0236  -0.0717 -0.0878 767  SER   E OG  
14723 N  N   . SER   E 464 ? 1.5668 1.7424 1.8627 0.0278  -0.0776 -0.0836 768  SER   E N   
14724 C  CA  . SER   E 464 ? 1.6260 1.7965 1.9131 0.0315  -0.0862 -0.0851 768  SER   E CA  
14725 C  C   . SER   E 464 ? 1.7606 1.9300 2.0528 0.0375  -0.0930 -0.0897 768  SER   E C   
14726 O  O   . SER   E 464 ? 1.7522 1.9206 2.0474 0.0409  -0.1010 -0.0927 768  SER   E O   
14727 C  CB  . SER   E 464 ? 1.5461 1.7085 1.8109 0.0309  -0.0852 -0.0815 768  SER   E CB  
14728 O  OG  . SER   E 464 ? 1.4939 1.6568 1.7531 0.0258  -0.0805 -0.0774 768  SER   E OG  
14729 N  N   . LYS   E 465 ? 1.8805 2.0495 2.1727 0.0392  -0.0902 -0.0905 769  LYS   E N   
14730 C  CA  . LYS   E 465 ? 1.9275 2.0941 2.2212 0.0453  -0.0964 -0.0946 769  LYS   E CA  
14731 C  C   . LYS   E 465 ? 2.0029 2.1608 2.2798 0.0490  -0.1036 -0.0948 769  LYS   E C   
14732 O  O   . LYS   E 465 ? 2.0365 2.1924 2.3164 0.0541  -0.1118 -0.0987 769  LYS   E O   
14733 C  CB  . LYS   E 465 ? 1.8604 2.0344 2.1768 0.0476  -0.1007 -0.0993 769  LYS   E CB  
14734 N  N   . LEU   E 466 ? 1.9035 2.0557 2.1626 0.0464  -0.1006 -0.0905 770  LEU   E N   
14735 C  CA  . LEU   E 466 ? 1.8659 2.0092 2.1078 0.0494  -0.1059 -0.0899 770  LEU   E CA  
14736 C  C   . LEU   E 466 ? 1.8747 2.0107 2.1032 0.0527  -0.1060 -0.0899 770  LEU   E C   
14737 O  O   . LEU   E 466 ? 1.8285 1.9564 2.0436 0.0563  -0.1109 -0.0900 770  LEU   E O   
14738 C  CB  . LEU   E 466 ? 1.7782 1.9193 2.0086 0.0449  -0.1025 -0.0853 770  LEU   E CB  
14739 N  N   . PHE   E 467 ? 1.8613 1.9994 2.0929 0.0517  -0.1007 -0.0896 771  PHE   E N   
14740 C  CA  . PHE   E 467 ? 1.8674 1.9984 2.0862 0.0544  -0.1001 -0.0893 771  PHE   E CA  
14741 C  C   . PHE   E 467 ? 1.8537 1.9888 2.0838 0.0562  -0.0980 -0.0919 771  PHE   E C   
14742 O  O   . PHE   E 467 ? 1.8732 2.0130 2.1184 0.0596  -0.1023 -0.0961 771  PHE   E O   
14743 C  CB  . PHE   E 467 ? 1.8284 1.9549 2.0314 0.0499  -0.0937 -0.0843 771  PHE   E CB  
14744 C  CG  . PHE   E 467 ? 1.8073 1.9328 2.0034 0.0465  -0.0935 -0.0811 771  PHE   E CG  
14745 C  CD1 . PHE   E 467 ? 1.7720 1.8898 1.9542 0.0488  -0.0978 -0.0803 771  PHE   E CD1 
14746 C  CD2 . PHE   E 467 ? 1.7583 1.8902 1.9617 0.0412  -0.0887 -0.0790 771  PHE   E CD2 
14747 C  CE1 . PHE   E 467 ? 1.7259 1.8428 1.9021 0.0459  -0.0973 -0.0774 771  PHE   E CE1 
14748 C  CE2 . PHE   E 467 ? 1.7323 1.8633 1.9296 0.0382  -0.0886 -0.0761 771  PHE   E CE2 
14749 C  CZ  . PHE   E 467 ? 1.7169 1.8407 1.9010 0.0406  -0.0928 -0.0753 771  PHE   E CZ  
14750 N  N   . THR   E 476 ? 2.3307 2.4461 2.5292 0.0574  -0.0352 -0.0861 780  THR   E N   
14751 C  CA  . THR   E 476 ? 2.3454 2.4501 2.5239 0.0581  -0.0377 -0.0850 780  THR   E CA  
14752 C  C   . THR   E 476 ? 2.4222 2.5211 2.5874 0.0543  -0.0309 -0.0816 780  THR   E C   
14753 O  O   . THR   E 476 ? 2.4266 2.5163 2.5760 0.0549  -0.0313 -0.0807 780  THR   E O   
14754 C  CB  . THR   E 476 ? 2.3132 2.4148 2.4832 0.0570  -0.0446 -0.0841 780  THR   E CB  
14755 O  OG1 . THR   E 476 ? 2.2002 2.3080 2.3839 0.0600  -0.0505 -0.0871 780  THR   E OG1 
14756 C  CG2 . THR   E 476 ? 2.3100 2.4008 2.4623 0.0592  -0.0481 -0.0838 780  THR   E CG2 
14757 N  N   . SER   E 477 ? 2.5127 2.6163 2.6841 0.0506  -0.0248 -0.0797 781  SER   E N   
14758 C  CA  . SER   E 477 ? 2.5036 2.6017 2.6631 0.0472  -0.0183 -0.0767 781  SER   E CA  
14759 C  C   . SER   E 477 ? 2.4548 2.5554 2.6226 0.0491  -0.0108 -0.0776 781  SER   E C   
14760 O  O   . SER   E 477 ? 2.4502 2.5596 2.6361 0.0502  -0.0088 -0.0792 781  SER   E O   
14761 C  CB  . SER   E 477 ? 2.4642 2.5642 2.6216 0.0415  -0.0167 -0.0735 781  SER   E CB  
14762 O  OG  . SER   E 477 ? 2.4367 2.5329 2.5864 0.0389  -0.0098 -0.0710 781  SER   E OG  
14763 N  N   . PHE   E 478 ? 2.1757 2.2682 2.3302 0.0494  -0.0066 -0.0764 782  PHE   E N   
14764 C  CA  . PHE   E 478 ? 2.0327 2.1256 2.1924 0.0521  0.0005  -0.0774 782  PHE   E CA  
14765 C  C   . PHE   E 478 ? 1.8983 1.9850 2.0459 0.0490  0.0076  -0.0743 782  PHE   E C   
14766 O  O   . PHE   E 478 ? 1.8082 1.8873 1.9451 0.0510  0.0110  -0.0742 782  PHE   E O   
14767 C  CB  . PHE   E 478 ? 1.9138 2.0019 2.0697 0.0575  -0.0016 -0.0800 782  PHE   E CB  
14768 N  N   . GLY   E 479 ? 1.8666 1.9561 2.0155 0.0444  0.0099  -0.0718 783  GLY   E N   
14769 C  CA  . GLY   E 479 ? 1.7855 1.8696 1.9243 0.0417  0.0167  -0.0690 783  GLY   E CA  
14770 C  C   . GLY   E 479 ? 1.7278 1.8057 1.8505 0.0370  0.0141  -0.0660 783  GLY   E C   
14771 O  O   . GLY   E 479 ? 1.5605 1.6333 1.6737 0.0347  0.0191  -0.0637 783  GLY   E O   
14772 N  N   . GLU   E 480 ? 1.7139 1.7920 1.8334 0.0355  0.0065  -0.0660 784  GLU   E N   
14773 C  CA  . GLU   E 480 ? 1.6133 1.6854 1.7180 0.0313  0.0035  -0.0633 784  GLU   E CA  
14774 C  C   . GLU   E 480 ? 1.5515 1.6289 1.6612 0.0270  0.0047  -0.0611 784  GLU   E C   
14775 O  O   . GLU   E 480 ? 1.5400 1.6242 1.6627 0.0271  0.0092  -0.0613 784  GLU   E O   
14776 C  CB  . GLU   E 480 ? 1.6227 1.6926 1.7222 0.0318  -0.0044 -0.0641 784  GLU   E CB  
14777 N  N   . GLU   E 481 ? 1.4681 1.5425 1.5682 0.0231  0.0010  -0.0590 785  GLU   E N   
14778 C  CA  . GLU   E 481 ? 1.3582 1.4372 1.4621 0.0191  0.0013  -0.0568 785  GLU   E CA  
14779 C  C   . GLU   E 481 ? 1.2717 1.3577 1.3850 0.0186  -0.0046 -0.0576 785  GLU   E C   
14780 O  O   . GLU   E 481 ? 1.2750 1.3597 1.3863 0.0205  -0.0100 -0.0589 785  GLU   E O   
14781 C  CB  . GLU   E 481 ? 1.3997 1.4714 1.4878 0.0152  0.0008  -0.0540 785  GLU   E CB  
14782 C  CG  . GLU   E 481 ? 1.5279 1.5892 1.6010 0.0160  0.0035  -0.0536 785  GLU   E CG  
14783 C  CD  . GLU   E 481 ? 1.5736 1.6280 1.6322 0.0120  0.0020  -0.0510 785  GLU   E CD  
14784 O  OE1 . GLU   E 481 ? 1.6094 1.6644 1.6656 0.0094  -0.0035 -0.0501 785  GLU   E OE1 
14785 O  OE2 . GLU   E 481 ? 1.5891 1.6374 1.6388 0.0114  0.0062  -0.0499 785  GLU   E OE2 
14786 N  N   . VAL   E 482 ? 1.3006 1.3934 1.4232 0.0162  -0.0037 -0.0566 786  VAL   E N   
14787 C  CA  . VAL   E 482 ? 1.1792 1.2785 1.3110 0.0158  -0.0091 -0.0573 786  VAL   E CA  
14788 C  C   . VAL   E 482 ? 1.1102 1.2124 1.2426 0.0115  -0.0086 -0.0547 786  VAL   E C   
14789 O  O   . VAL   E 482 ? 1.1256 1.2266 1.2558 0.0094  -0.0034 -0.0529 786  VAL   E O   
14790 C  CB  . VAL   E 482 ? 1.1563 1.2637 1.3060 0.0193  -0.0092 -0.0603 786  VAL   E CB  
14791 C  CG1 . VAL   E 482 ? 1.1623 1.2760 1.3242 0.0177  -0.0037 -0.0597 786  VAL   E CG1 
14792 C  CG2 . VAL   E 482 ? 1.2374 1.3484 1.3923 0.0203  -0.0164 -0.0617 786  VAL   E CG2 
14793 N  N   . GLU   E 483 ? 1.0526 1.1577 1.1870 0.0104  -0.0141 -0.0545 787  GLU   E N   
14794 C  CA  . GLU   E 483 ? 1.0696 1.1773 1.2043 0.0065  -0.0144 -0.0521 787  GLU   E CA  
14795 C  C   . GLU   E 483 ? 1.0612 1.1779 1.2125 0.0069  -0.0147 -0.0534 787  GLU   E C   
14796 O  O   . GLU   E 483 ? 1.0520 1.1726 1.2134 0.0101  -0.0174 -0.0561 787  GLU   E O   
14797 C  CB  . GLU   E 483 ? 1.0685 1.1732 1.1937 0.0047  -0.0199 -0.0507 787  GLU   E CB  
14798 C  CG  . GLU   E 483 ? 1.1256 1.2236 1.2365 0.0014  -0.0187 -0.0479 787  GLU   E CG  
14799 C  CD  . GLU   E 483 ? 1.1728 1.2678 1.2752 -0.0003 -0.0238 -0.0465 787  GLU   E CD  
14800 O  OE1 . GLU   E 483 ? 1.1665 1.2614 1.2697 0.0020  -0.0279 -0.0479 787  GLU   E OE1 
14801 O  OE2 . GLU   E 483 ? 1.2161 1.3084 1.3109 -0.0038 -0.0237 -0.0440 787  GLU   E OE2 
14802 N  N   . VAL   E 484 ? 1.0606 1.1800 1.2146 0.0036  -0.0121 -0.0513 788  VAL   E N   
14803 C  CA  . VAL   E 484 ? 1.0407 1.1681 1.2101 0.0033  -0.0119 -0.0521 788  VAL   E CA  
14804 C  C   . VAL   E 484 ? 1.0147 1.1431 1.1811 -0.0003 -0.0138 -0.0497 788  VAL   E C   
14805 O  O   . VAL   E 484 ? 1.0385 1.1661 1.2023 -0.0031 -0.0097 -0.0474 788  VAL   E O   
14806 C  CB  . VAL   E 484 ? 1.0499 1.1800 1.2286 0.0034  -0.0046 -0.0523 788  VAL   E CB  
14807 C  CG1 . VAL   E 484 ? 1.1442 1.2827 1.3402 0.0032  -0.0049 -0.0535 788  VAL   E CG1 
14808 C  CG2 . VAL   E 484 ? 0.9885 1.1165 1.1681 0.0069  -0.0016 -0.0543 788  VAL   E CG2 
14809 N  N   . HIS   E 485 ? 1.0242 1.1544 1.1914 0.0001  -0.0201 -0.0502 789  HIS   E N   
14810 C  CA  . HIS   E 485 ? 1.0030 1.1338 1.1665 -0.0031 -0.0222 -0.0479 789  HIS   E CA  
14811 C  C   . HIS   E 485 ? 1.0133 1.1510 1.1902 -0.0041 -0.0212 -0.0481 789  HIS   E C   
14812 O  O   . HIS   E 485 ? 1.0947 1.2374 1.2841 -0.0018 -0.0232 -0.0507 789  HIS   E O   
14813 C  CB  . HIS   E 485 ? 0.9824 1.1115 1.1402 -0.0021 -0.0287 -0.0481 789  HIS   E CB  
14814 C  CG  . HIS   E 485 ? 0.9958 1.1177 1.1393 -0.0022 -0.0295 -0.0471 789  HIS   E CG  
14815 N  ND1 . HIS   E 485 ? 1.0529 1.1713 1.1936 0.0004  -0.0285 -0.0487 789  HIS   E ND1 
14816 C  CD2 . HIS   E 485 ? 1.0299 1.1475 1.1619 -0.0046 -0.0310 -0.0446 789  HIS   E CD2 
14817 C  CE1 . HIS   E 485 ? 1.0606 1.1723 1.1880 -0.0005 -0.0295 -0.0473 789  HIS   E CE1 
14818 N  NE2 . HIS   E 485 ? 1.0756 1.1869 1.1980 -0.0036 -0.0310 -0.0448 789  HIS   E NE2 
14819 N  N   . ASN   E 486 ? 0.9528 1.0904 1.1272 -0.0075 -0.0181 -0.0455 790  ASN   E N   
14820 C  CA  . ASN   E 486 ? 0.9992 1.1425 1.1850 -0.0088 -0.0175 -0.0454 790  ASN   E CA  
14821 C  C   . ASN   E 486 ? 1.0076 1.1502 1.1868 -0.0116 -0.0201 -0.0429 790  ASN   E C   
14822 O  O   . ASN   E 486 ? 0.9974 1.1352 1.1637 -0.0131 -0.0207 -0.0408 790  ASN   E O   
14823 C  CB  . ASN   E 486 ? 1.0031 1.1476 1.1950 -0.0100 -0.0102 -0.0448 790  ASN   E CB  
14824 C  CG  . ASN   E 486 ? 1.0780 1.2212 1.2723 -0.0076 -0.0061 -0.0464 790  ASN   E CG  
14825 O  OD1 . ASN   E 486 ? 1.0833 1.2314 1.2916 -0.0055 -0.0052 -0.0489 790  ASN   E OD1 
14826 N  ND2 . ASN   E 486 ? 1.0843 1.2208 1.2651 -0.0078 -0.0035 -0.0450 790  ASN   E ND2 
14827 N  N   . LEU   E 487 ? 1.0431 1.1907 1.2318 -0.0121 -0.0222 -0.0433 791  LEU   E N   
14828 C  CA  . LEU   E 487 ? 0.9622 1.1102 1.1475 -0.0149 -0.0230 -0.0409 791  LEU   E CA  
14829 C  C   . LEU   E 487 ? 0.9991 1.1479 1.1884 -0.0172 -0.0169 -0.0394 791  LEU   E C   
14830 O  O   . LEU   E 487 ? 0.9963 1.1488 1.1979 -0.0164 -0.0139 -0.0410 791  LEU   E O   
14831 C  CB  . LEU   E 487 ? 0.9222 1.0742 1.1148 -0.0140 -0.0285 -0.0421 791  LEU   E CB  
14832 C  CG  . LEU   E 487 ? 0.9209 1.0746 1.1139 -0.0165 -0.0292 -0.0401 791  LEU   E CG  
14833 C  CD1 . LEU   E 487 ? 0.9443 1.0939 1.1234 -0.0185 -0.0300 -0.0371 791  LEU   E CD1 
14834 C  CD2 . LEU   E 487 ? 0.9585 1.1159 1.1595 -0.0148 -0.0346 -0.0420 791  LEU   E CD2 
14835 N  N   . LEU   E 488 ? 1.0056 1.1506 1.1844 -0.0198 -0.0148 -0.0365 792  LEU   E N   
14836 C  CA  . LEU   E 488 ? 1.0021 1.1464 1.1820 -0.0219 -0.0090 -0.0347 792  LEU   E CA  
14837 C  C   . LEU   E 488 ? 1.0179 1.1643 1.1992 -0.0240 -0.0108 -0.0330 792  LEU   E C   
14838 O  O   . LEU   E 488 ? 1.0315 1.1766 1.2049 -0.0248 -0.0150 -0.0318 792  LEU   E O   
14839 C  CB  . LEU   E 488 ? 0.9622 1.0994 1.1281 -0.0229 -0.0053 -0.0326 792  LEU   E CB  
14840 C  CG  . LEU   E 488 ? 0.9505 1.0839 1.1118 -0.0210 -0.0027 -0.0337 792  LEU   E CG  
14841 C  CD1 . LEU   E 488 ? 0.9487 1.0750 1.0977 -0.0223 0.0019  -0.0314 792  LEU   E CD1 
14842 C  CD2 . LEU   E 488 ? 1.0582 1.1956 1.2330 -0.0188 0.0005  -0.0362 792  LEU   E CD2 
14843 N  N   . ILE   E 489 ? 1.0847 1.2343 1.2764 -0.0248 -0.0076 -0.0331 793  ILE   E N   
14844 C  CA  . ILE   E 489 ? 1.1121 1.2629 1.3046 -0.0270 -0.0083 -0.0313 793  ILE   E CA  
14845 C  C   . ILE   E 489 ? 1.1249 1.2708 1.3095 -0.0290 -0.0023 -0.0286 793  ILE   E C   
14846 O  O   . ILE   E 489 ? 1.1354 1.2808 1.3252 -0.0291 0.0038  -0.0286 793  ILE   E O   
14847 C  CB  . ILE   E 489 ? 1.1254 1.2821 1.3339 -0.0268 -0.0088 -0.0331 793  ILE   E CB  
14848 C  CG1 . ILE   E 489 ? 1.0933 1.2539 1.3094 -0.0241 -0.0147 -0.0363 793  ILE   E CG1 
14849 C  CG2 . ILE   E 489 ? 1.1811 1.3384 1.3891 -0.0288 -0.0103 -0.0313 793  ILE   E CG2 
14850 C  CD1 . ILE   E 489 ? 1.0970 1.2574 1.3068 -0.0237 -0.0214 -0.0360 793  ILE   E CD1 
14851 N  N   . ILE   E 490 ? 1.0972 1.2391 1.2692 -0.0304 -0.0040 -0.0262 794  ILE   E N   
14852 C  CA  . ILE   E 490 ? 1.1129 1.2488 1.2747 -0.0319 0.0006  -0.0237 794  ILE   E CA  
14853 C  C   . ILE   E 490 ? 1.1475 1.2836 1.3081 -0.0338 -0.0002 -0.0216 794  ILE   E C   
14854 O  O   . ILE   E 490 ? 1.1733 1.3116 1.3329 -0.0342 -0.0057 -0.0214 794  ILE   E O   
14855 C  CB  . ILE   E 490 ? 1.0926 1.2227 1.2399 -0.0317 -0.0008 -0.0229 794  ILE   E CB  
14856 C  CG1 . ILE   E 490 ? 1.0746 1.2041 1.2234 -0.0296 0.0006  -0.0250 794  ILE   E CG1 
14857 C  CG2 . ILE   E 490 ? 1.0723 1.1954 1.2080 -0.0330 0.0031  -0.0204 794  ILE   E CG2 
14858 C  CD1 . ILE   E 490 ? 1.0285 1.1521 1.1639 -0.0292 -0.0009 -0.0246 794  ILE   E CD1 
14859 N  N   . ASP   E 491 ? 1.1514 1.2847 1.3117 -0.0349 0.0055  -0.0201 795  ASP   E N   
14860 C  CA  . ASP   E 491 ? 1.1091 1.2429 1.2709 -0.0365 0.0057  -0.0184 795  ASP   E CA  
14861 C  C   . ASP   E 491 ? 1.0937 1.2218 1.2406 -0.0376 0.0043  -0.0158 795  ASP   E C   
14862 O  O   . ASP   E 491 ? 1.1013 1.2228 1.2382 -0.0376 0.0081  -0.0145 795  ASP   E O   
14863 C  CB  . ASP   E 491 ? 1.1026 1.2359 1.2719 -0.0371 0.0128  -0.0179 795  ASP   E CB  
14864 C  CG  . ASP   E 491 ? 1.1632 1.2944 1.3298 -0.0388 0.0141  -0.0156 795  ASP   E CG  
14865 O  OD1 . ASP   E 491 ? 1.1880 1.3240 1.3639 -0.0395 0.0114  -0.0161 795  ASP   E OD1 
14866 O  OD2 . ASP   E 491 ? 1.1771 1.3012 1.3317 -0.0393 0.0174  -0.0133 795  ASP   E OD2 
14867 N  N   . GLN   E 492 ? 1.1514 1.2818 1.2971 -0.0384 -0.0011 -0.0151 796  GLN   E N   
14868 C  CA  . GLN   E 492 ? 1.1733 1.2992 1.3059 -0.0392 -0.0038 -0.0131 796  GLN   E CA  
14869 C  C   . GLN   E 492 ? 1.0996 1.2185 1.2232 -0.0399 0.0009  -0.0109 796  GLN   E C   
14870 O  O   . GLN   E 492 ? 1.0259 1.1392 1.1370 -0.0401 -0.0005 -0.0096 796  GLN   E O   
14871 C  CB  . GLN   E 492 ? 1.2266 1.3565 1.3612 -0.0398 -0.0095 -0.0126 796  GLN   E CB  
14872 C  CG  . GLN   E 492 ? 1.2112 1.3418 1.3493 -0.0408 -0.0083 -0.0112 796  GLN   E CG  
14873 C  CD  . GLN   E 492 ? 1.2265 1.3605 1.3653 -0.0411 -0.0140 -0.0107 796  GLN   E CD  
14874 O  OE1 . GLN   E 492 ? 1.1856 1.3246 1.3311 -0.0402 -0.0177 -0.0123 796  GLN   E OE1 
14875 N  NE2 . GLN   E 492 ? 1.2362 1.3673 1.3677 -0.0420 -0.0148 -0.0085 796  GLN   E NE2 
14876 N  N   . HIS   E 493 ? 1.1244 1.2428 1.2537 -0.0402 0.0064  -0.0104 797  HIS   E N   
14877 C  CA  . HIS   E 493 ? 1.1415 1.2522 1.2606 -0.0406 0.0108  -0.0081 797  HIS   E CA  
14878 C  C   . HIS   E 493 ? 1.1330 1.2374 1.2456 -0.0396 0.0166  -0.0081 797  HIS   E C   
14879 O  O   . HIS   E 493 ? 1.1759 1.2727 1.2743 -0.0392 0.0168  -0.0068 797  HIS   E O   
14880 C  CB  . HIS   E 493 ? 1.1676 1.2793 1.2942 -0.0416 0.0145  -0.0071 797  HIS   E CB  
14881 C  CG  . HIS   E 493 ? 1.1677 1.2847 1.3000 -0.0425 0.0092  -0.0070 797  HIS   E CG  
14882 N  ND1 . HIS   E 493 ? 1.1972 1.3219 1.3441 -0.0426 0.0075  -0.0088 797  HIS   E ND1 
14883 C  CD2 . HIS   E 493 ? 1.2079 1.3235 1.3332 -0.0431 0.0052  -0.0054 797  HIS   E CD2 
14884 C  CE1 . HIS   E 493 ? 1.2787 1.4059 1.4266 -0.0431 0.0028  -0.0083 797  HIS   E CE1 
14885 N  NE2 . HIS   E 493 ? 1.2567 1.3789 1.3920 -0.0435 0.0015  -0.0061 797  HIS   E NE2 
14886 N  N   . THR   E 494 ? 1.1264 1.2337 1.2495 -0.0389 0.0211  -0.0096 798  THR   E N   
14887 C  CA  . THR   E 494 ? 1.1860 1.2877 1.3043 -0.0376 0.0275  -0.0096 798  THR   E CA  
14888 C  C   . THR   E 494 ? 1.1302 1.2309 1.2425 -0.0363 0.0243  -0.0111 798  THR   E C   
14889 O  O   . THR   E 494 ? 1.1048 1.1981 1.2066 -0.0352 0.0278  -0.0106 798  THR   E O   
14890 C  CB  . THR   E 494 ? 1.1855 1.2913 1.3188 -0.0373 0.0338  -0.0107 798  THR   E CB  
14891 O  OG1 . THR   E 494 ? 1.2181 1.3320 1.3638 -0.0367 0.0302  -0.0135 798  THR   E OG1 
14892 C  CG2 . THR   E 494 ? 1.1513 1.2594 1.2932 -0.0388 0.0360  -0.0096 798  THR   E CG2 
14893 N  N   . PHE   E 495 ? 1.1220 1.2291 1.2399 -0.0364 0.0178  -0.0128 799  PHE   E N   
14894 C  CA  . PHE   E 495 ? 1.0553 1.1627 1.1710 -0.0351 0.0151  -0.0146 799  PHE   E CA  
14895 C  C   . PHE   E 495 ? 1.1517 1.2591 1.2735 -0.0335 0.0211  -0.0161 799  PHE   E C   
14896 O  O   . PHE   E 495 ? 1.2215 1.3235 1.3351 -0.0321 0.0233  -0.0163 799  PHE   E O   
14897 C  CB  . PHE   E 495 ? 0.9829 1.0829 1.0820 -0.0351 0.0124  -0.0135 799  PHE   E CB  
14898 C  CG  . PHE   E 495 ? 1.0228 1.1250 1.1190 -0.0365 0.0053  -0.0128 799  PHE   E CG  
14899 C  CD1 . PHE   E 495 ? 1.0581 1.1672 1.1620 -0.0365 0.0000  -0.0142 799  PHE   E CD1 
14900 C  CD2 . PHE   E 495 ? 1.0629 1.1600 1.1488 -0.0374 0.0040  -0.0107 799  PHE   E CD2 
14901 C  CE1 . PHE   E 495 ? 1.0528 1.1640 1.1544 -0.0376 -0.0060 -0.0135 799  PHE   E CE1 
14902 C  CE2 . PHE   E 495 ? 1.0766 1.1763 1.1610 -0.0386 -0.0024 -0.0101 799  PHE   E CE2 
14903 C  CZ  . PHE   E 495 ? 1.0395 1.1464 1.1319 -0.0388 -0.0072 -0.0114 799  PHE   E CZ  
14904 N  N   . GLU   E 496 ? 1.1500 1.2638 1.2871 -0.0335 0.0235  -0.0171 800  GLU   E N   
14905 C  CA  . GLU   E 496 ? 1.1529 1.2686 1.2998 -0.0321 0.0291  -0.0187 800  GLU   E CA  
14906 C  C   . GLU   E 496 ? 1.1759 1.3003 1.3366 -0.0313 0.0243  -0.0216 800  GLU   E C   
14907 O  O   . GLU   E 496 ? 1.1666 1.2960 1.3328 -0.0321 0.0188  -0.0220 800  GLU   E O   
14908 C  CB  . GLU   E 496 ? 1.2160 1.3313 1.3700 -0.0329 0.0364  -0.0174 800  GLU   E CB  
14909 C  CG  . GLU   E 496 ? 1.3108 1.4288 1.4775 -0.0316 0.0429  -0.0189 800  GLU   E CG  
14910 C  CD  . GLU   E 496 ? 1.3776 1.4960 1.5531 -0.0329 0.0497  -0.0175 800  GLU   E CD  
14911 O  OE1 . GLU   E 496 ? 1.3408 1.4635 1.5236 -0.0346 0.0467  -0.0173 800  GLU   E OE1 
14912 O  OE2 . GLU   E 496 ? 1.4275 1.5413 1.6019 -0.0321 0.0582  -0.0166 800  GLU   E OE2 
14913 N  N   . VAL   E 497 ? 1.2193 1.3447 1.3848 -0.0293 0.0264  -0.0235 801  VAL   E N   
14914 C  CA  . VAL   E 497 ? 1.1707 1.3032 1.3477 -0.0279 0.0217  -0.0265 801  VAL   E CA  
14915 C  C   . VAL   E 497 ? 1.1361 1.2756 1.3315 -0.0282 0.0234  -0.0278 801  VAL   E C   
14916 O  O   . VAL   E 497 ? 1.1026 1.2430 1.3068 -0.0276 0.0299  -0.0284 801  VAL   E O   
14917 C  CB  . VAL   E 497 ? 1.1495 1.2800 1.3243 -0.0255 0.0232  -0.0282 801  VAL   E CB  
14918 C  CG1 . VAL   E 497 ? 1.1329 1.2693 1.3160 -0.0238 0.0170  -0.0311 801  VAL   E CG1 
14919 C  CG2 . VAL   E 497 ? 1.0549 1.1770 1.2108 -0.0254 0.0230  -0.0266 801  VAL   E CG2 
14920 N  N   . LEU   E 498 ? 1.1259 1.2705 1.3278 -0.0291 0.0177  -0.0284 802  LEU   E N   
14921 C  CA  . LEU   E 498 ? 1.1110 1.2617 1.3300 -0.0297 0.0184  -0.0297 802  LEU   E CA  
14922 C  C   . LEU   E 498 ? 1.1579 1.3148 1.3912 -0.0274 0.0161  -0.0333 802  LEU   E C   
14923 O  O   . LEU   E 498 ? 1.1724 1.3330 1.4203 -0.0273 0.0202  -0.0345 802  LEU   E O   
14924 C  CB  . LEU   E 498 ? 1.1509 1.3041 1.3708 -0.0312 0.0128  -0.0291 802  LEU   E CB  
14925 C  CG  . LEU   E 498 ? 1.1831 1.3316 1.3900 -0.0332 0.0126  -0.0259 802  LEU   E CG  
14926 C  CD1 . LEU   E 498 ? 1.2013 1.3535 1.4121 -0.0340 0.0064  -0.0260 802  LEU   E CD1 
14927 C  CD2 . LEU   E 498 ? 1.1516 1.2958 1.3569 -0.0346 0.0207  -0.0236 802  LEU   E CD2 
14928 N  N   . HIS   E 499 ? 1.1468 1.3047 1.3764 -0.0257 0.0092  -0.0349 803  HIS   E N   
14929 C  CA  . HIS   E 499 ? 1.1049 1.2676 1.3455 -0.0231 0.0056  -0.0385 803  HIS   E CA  
14930 C  C   . HIS   E 499 ? 1.0920 1.2510 1.3215 -0.0211 0.0039  -0.0390 803  HIS   E C   
14931 O  O   . HIS   E 499 ? 1.0857 1.2391 1.2996 -0.0220 0.0036  -0.0368 803  HIS   E O   
14932 C  CB  . HIS   E 499 ? 1.1323 1.2996 1.3797 -0.0226 -0.0023 -0.0403 803  HIS   E CB  
14933 C  CG  . HIS   E 499 ? 1.1672 1.3407 1.4327 -0.0207 -0.0043 -0.0439 803  HIS   E CG  
14934 N  ND1 . HIS   E 499 ? 1.1179 1.2929 1.3886 -0.0179 -0.0047 -0.0465 803  HIS   E ND1 
14935 C  CD2 . HIS   E 499 ? 1.2213 1.3999 1.5012 -0.0212 -0.0065 -0.0454 803  HIS   E CD2 
14936 C  CE1 . HIS   E 499 ? 1.1194 1.3003 1.4073 -0.0167 -0.0071 -0.0496 803  HIS   E CE1 
14937 N  NE2 . HIS   E 499 ? 1.1795 1.3626 1.4734 -0.0187 -0.0084 -0.0490 803  HIS   E NE2 
14938 N  N   . ALA   E 500 ? 1.0637 1.2255 1.3014 -0.0183 0.0025  -0.0420 804  ALA   E N   
14939 C  CA  . ALA   E 500 ? 1.0673 1.2254 1.2948 -0.0162 0.0006  -0.0427 804  ALA   E CA  
14940 C  C   . ALA   E 500 ? 1.1048 1.2673 1.3426 -0.0130 -0.0046 -0.0464 804  ALA   E C   
14941 O  O   . ALA   E 500 ? 1.1064 1.2715 1.3546 -0.0111 -0.0018 -0.0485 804  ALA   E O   
14942 C  CB  . ALA   E 500 ? 1.0720 1.2256 1.2939 -0.0159 0.0080  -0.0417 804  ALA   E CB  
14943 N  N   . HIS   E 501 ? 1.0810 1.2438 1.3150 -0.0122 -0.0121 -0.0472 805  HIS   E N   
14944 C  CA  . HIS   E 501 ? 1.0738 1.2400 1.3164 -0.0089 -0.0180 -0.0507 805  HIS   E CA  
14945 C  C   . HIS   E 501 ? 1.0838 1.2460 1.3175 -0.0062 -0.0195 -0.0517 805  HIS   E C   
14946 O  O   . HIS   E 501 ? 1.1248 1.2825 1.3447 -0.0064 -0.0225 -0.0503 805  HIS   E O   
14947 C  CB  . HIS   E 501 ? 1.0682 1.2356 1.3103 -0.0087 -0.0252 -0.0511 805  HIS   E CB  
14948 C  CG  . HIS   E 501 ? 1.0826 1.2523 1.3319 -0.0049 -0.0316 -0.0548 805  HIS   E CG  
14949 N  ND1 . HIS   E 501 ? 1.1112 1.2865 1.3780 -0.0034 -0.0326 -0.0579 805  HIS   E ND1 
14950 C  CD2 . HIS   E 501 ? 1.0875 1.2542 1.3289 -0.0022 -0.0374 -0.0559 805  HIS   E CD2 
14951 C  CE1 . HIS   E 501 ? 1.1278 1.3033 1.3968 0.0003  -0.0393 -0.0610 805  HIS   E CE1 
14952 N  NE2 . HIS   E 501 ? 1.1195 1.2895 1.3726 0.0012  -0.0420 -0.0597 805  HIS   E NE2 
14953 N  N   . GLN   E 502 ? 1.2529 1.4169 1.4950 -0.0037 -0.0176 -0.0541 806  GLN   E N   
14954 C  CA  . GLN   E 502 ? 1.2532 1.4132 1.4874 -0.0009 -0.0189 -0.0553 806  GLN   E CA  
14955 C  C   . GLN   E 502 ? 1.2244 1.3852 1.4600 0.0023  -0.0270 -0.0580 806  GLN   E C   
14956 O  O   . GLN   E 502 ? 1.2174 1.3831 1.4671 0.0047  -0.0300 -0.0611 806  GLN   E O   
14957 C  CB  . GLN   E 502 ? 1.2669 1.4283 1.5092 0.0009  -0.0134 -0.0568 806  GLN   E CB  
14958 C  CG  . GLN   E 502 ? 1.2574 1.4139 1.4900 0.0037  -0.0144 -0.0578 806  GLN   E CG  
14959 C  CD  . GLN   E 502 ? 1.2950 1.4544 1.5395 0.0071  -0.0123 -0.0608 806  GLN   E CD  
14960 O  OE1 . GLN   E 502 ? 1.2989 1.4601 1.5507 0.0065  -0.0053 -0.0604 806  GLN   E OE1 
14961 N  NE2 . GLN   E 502 ? 1.2896 1.4494 1.5362 0.0108  -0.0183 -0.0637 806  GLN   E NE2 
14962 N  N   . PHE   E 503 ? 1.1480 1.3034 1.3689 0.0026  -0.0307 -0.0568 807  PHE   E N   
14963 C  CA  . PHE   E 503 ? 1.1259 1.2804 1.3454 0.0058  -0.0381 -0.0589 807  PHE   E CA  
14964 C  C   . PHE   E 503 ? 1.1669 1.3214 1.3911 0.0100  -0.0393 -0.0622 807  PHE   E C   
14965 O  O   . PHE   E 503 ? 1.2014 1.3562 1.4288 0.0103  -0.0342 -0.0626 807  PHE   E O   
14966 C  CB  . PHE   E 503 ? 1.0486 1.1969 1.2510 0.0050  -0.0406 -0.0566 807  PHE   E CB  
14967 C  CG  . PHE   E 503 ? 0.9925 1.1412 1.1911 0.0019  -0.0414 -0.0540 807  PHE   E CG  
14968 C  CD1 . PHE   E 503 ? 1.0231 1.1735 1.2249 0.0031  -0.0470 -0.0550 807  PHE   E CD1 
14969 C  CD2 . PHE   E 503 ? 0.9690 1.1159 1.1604 -0.0020 -0.0369 -0.0507 807  PHE   E CD2 
14970 C  CE1 . PHE   E 503 ? 0.9838 1.1344 1.1820 0.0005  -0.0477 -0.0526 807  PHE   E CE1 
14971 C  CE2 . PHE   E 503 ? 1.0199 1.1673 1.2081 -0.0046 -0.0379 -0.0484 807  PHE   E CE2 
14972 C  CZ  . PHE   E 503 ? 1.0005 1.1499 1.1923 -0.0034 -0.0431 -0.0493 807  PHE   E CZ  
14973 N  N   . LEU   E 504 ? 1.1389 1.2921 1.3623 0.0135  -0.0462 -0.0644 808  LEU   E N   
14974 C  CA  . LEU   E 504 ? 1.1903 1.3438 1.4196 0.0181  -0.0488 -0.0680 808  LEU   E CA  
14975 C  C   . LEU   E 504 ? 1.2466 1.3950 1.4659 0.0190  -0.0454 -0.0674 808  LEU   E C   
14976 O  O   . LEU   E 504 ? 1.2284 1.3713 1.4331 0.0167  -0.0432 -0.0644 808  LEU   E O   
14977 C  CB  . LEU   E 504 ? 1.1579 1.3092 1.3846 0.0218  -0.0571 -0.0702 808  LEU   E CB  
14978 C  CG  . LEU   E 504 ? 1.1292 1.2855 1.3673 0.0219  -0.0613 -0.0717 808  LEU   E CG  
14979 C  CD1 . LEU   E 504 ? 1.1675 1.3193 1.3977 0.0251  -0.0690 -0.0728 808  LEU   E CD1 
14980 C  CD2 . LEU   E 504 ? 1.1856 1.3487 1.4432 0.0238  -0.0615 -0.0753 808  LEU   E CD2 
14981 N  N   . GLN   E 505 ? 1.3195 1.4696 1.5473 0.0224  -0.0450 -0.0704 809  GLN   E N   
14982 C  CA  . GLN   E 505 ? 1.3491 1.4943 1.5684 0.0237  -0.0417 -0.0702 809  GLN   E CA  
14983 C  C   . GLN   E 505 ? 1.3351 1.4727 1.5387 0.0257  -0.0466 -0.0699 809  GLN   E C   
14984 O  O   . GLN   E 505 ? 1.3234 1.4604 1.5280 0.0288  -0.0532 -0.0719 809  GLN   E O   
14985 C  CB  . GLN   E 505 ? 1.3955 1.5446 1.6283 0.0274  -0.0406 -0.0736 809  GLN   E CB  
14986 C  CG  . GLN   E 505 ? 1.4176 1.5640 1.6462 0.0272  -0.0335 -0.0726 809  GLN   E CG  
14987 C  CD  . GLN   E 505 ? 1.4978 1.6379 1.7164 0.0310  -0.0357 -0.0739 809  GLN   E CD  
14988 O  OE1 . GLN   E 505 ? 1.5519 1.6931 1.7769 0.0354  -0.0406 -0.0773 809  GLN   E OE1 
14989 N  NE2 . GLN   E 505 ? 1.4960 1.6289 1.6986 0.0293  -0.0323 -0.0714 809  GLN   E NE2 
14990 N  N   . ASN   E 506 ? 1.2522 1.3835 1.4413 0.0238  -0.0434 -0.0673 810  ASN   E N   
14991 C  CA  . ASN   E 506 ? 1.2189 1.3424 1.3919 0.0243  -0.0467 -0.0661 810  ASN   E CA  
14992 C  C   . ASN   E 506 ? 1.1742 1.2969 1.3415 0.0220  -0.0500 -0.0640 810  ASN   E C   
14993 O  O   . ASN   E 506 ? 1.1271 1.2437 1.2824 0.0227  -0.0530 -0.0630 810  ASN   E O   
14994 C  CB  . ASN   E 506 ? 1.2026 1.3230 1.3746 0.0297  -0.0518 -0.0691 810  ASN   E CB  
14995 C  CG  . ASN   E 506 ? 1.2331 1.3492 1.3999 0.0315  -0.0489 -0.0698 810  ASN   E CG  
14996 O  OD1 . ASN   E 506 ? 1.2613 1.3800 1.4374 0.0350  -0.0489 -0.0727 810  ASN   E OD1 
14997 N  ND2 . ASN   E 506 ? 1.2298 1.3391 1.3818 0.0291  -0.0464 -0.0670 810  ASN   E ND2 
14998 N  N   . GLU   E 507 ? 1.1625 1.2911 1.3384 0.0196  -0.0495 -0.0633 811  GLU   E N   
14999 C  CA  . GLU   E 507 ? 1.1037 1.2313 1.2735 0.0172  -0.0518 -0.0610 811  GLU   E CA  
15000 C  C   . GLU   E 507 ? 1.0521 1.1770 1.2120 0.0126  -0.0473 -0.0572 811  GLU   E C   
15001 O  O   . GLU   E 507 ? 1.0516 1.1778 1.2137 0.0104  -0.0420 -0.0563 811  GLU   E O   
15002 C  CB  . GLU   E 507 ? 1.1281 1.2625 1.3106 0.0167  -0.0535 -0.0619 811  GLU   E CB  
15003 C  CG  . GLU   E 507 ? 1.0940 1.2274 1.2707 0.0148  -0.0563 -0.0597 811  GLU   E CG  
15004 C  CD  . GLU   E 507 ? 1.1090 1.2487 1.2984 0.0147  -0.0586 -0.0610 811  GLU   E CD  
15005 O  OE1 . GLU   E 507 ? 1.1338 1.2791 1.3357 0.0138  -0.0555 -0.0620 811  GLU   E OE1 
15006 O  OE2 . GLU   E 507 ? 1.1078 1.2464 1.2947 0.0158  -0.0632 -0.0610 811  GLU   E OE2 
15007 N  N   . TYR   E 508 ? 1.0533 1.1739 1.2022 0.0112  -0.0494 -0.0550 812  TYR   E N   
15008 C  CA  . TYR   E 508 ? 1.0521 1.1695 1.1909 0.0070  -0.0463 -0.0515 812  TYR   E CA  
15009 C  C   . TYR   E 508 ? 1.0393 1.1591 1.1782 0.0044  -0.0477 -0.0494 812  TYR   E C   
15010 O  O   . TYR   E 508 ? 1.0242 1.1434 1.1620 0.0062  -0.0520 -0.0498 812  TYR   E O   
15011 C  CB  . TYR   E 508 ? 1.0870 1.1966 1.2124 0.0077  -0.0474 -0.0507 812  TYR   E CB  
15012 C  CG  . TYR   E 508 ? 1.0744 1.1801 1.1906 0.0039  -0.0438 -0.0481 812  TYR   E CG  
15013 C  CD1 . TYR   E 508 ? 1.0709 1.1769 1.1830 0.0000  -0.0434 -0.0451 812  TYR   E CD1 
15014 C  CD2 . TYR   E 508 ? 1.0622 1.1639 1.1738 0.0045  -0.0411 -0.0486 812  TYR   E CD2 
15015 C  CE1 . TYR   E 508 ? 1.0695 1.1718 1.1734 -0.0034 -0.0407 -0.0429 812  TYR   E CE1 
15016 C  CE2 . TYR   E 508 ? 1.1230 1.2205 1.2256 0.0012  -0.0382 -0.0464 812  TYR   E CE2 
15017 C  CZ  . TYR   E 508 ? 1.1145 1.2124 1.2134 -0.0028 -0.0383 -0.0436 812  TYR   E CZ  
15018 O  OH  . TYR   E 508 ? 1.1776 1.2712 1.2678 -0.0060 -0.0362 -0.0415 812  TYR   E OH  
15019 N  N   . ALA   E 509 ? 1.1036 1.2259 1.2436 0.0006  -0.0442 -0.0473 813  ALA   E N   
15020 C  CA  . ALA   E 509 ? 1.1164 1.2412 1.2571 -0.0019 -0.0452 -0.0453 813  ALA   E CA  
15021 C  C   . ALA   E 509 ? 1.1261 1.2464 1.2548 -0.0047 -0.0452 -0.0422 813  ALA   E C   
15022 O  O   . ALA   E 509 ? 1.1636 1.2810 1.2861 -0.0071 -0.0422 -0.0407 813  ALA   E O   
15023 C  CB  . ALA   E 509 ? 1.0535 1.1834 1.2026 -0.0044 -0.0415 -0.0447 813  ALA   E CB  
15024 N  N   . LEU   E 510 ? 1.0141 1.1337 1.1396 -0.0045 -0.0486 -0.0412 814  LEU   E N   
15025 C  CA  . LEU   E 510 ? 0.9777 1.0931 1.0929 -0.0068 -0.0489 -0.0384 814  LEU   E CA  
15026 C  C   . LEU   E 510 ? 1.0157 1.1340 1.1316 -0.0097 -0.0490 -0.0360 814  LEU   E C   
15027 O  O   . LEU   E 510 ? 1.0914 1.2084 1.2022 -0.0131 -0.0473 -0.0336 814  LEU   E O   
15028 C  CB  . LEU   E 510 ? 0.9517 1.0623 1.0606 -0.0041 -0.0520 -0.0388 814  LEU   E CB  
15029 C  CG  . LEU   E 510 ? 1.0271 1.1343 1.1350 -0.0005 -0.0527 -0.0414 814  LEU   E CG  
15030 C  CD1 . LEU   E 510 ? 1.0437 1.1461 1.1459 0.0029  -0.0562 -0.0420 814  LEU   E CD1 
15031 C  CD2 . LEU   E 510 ? 1.0259 1.1292 1.1275 -0.0023 -0.0498 -0.0407 814  LEU   E CD2 
15032 N  N   . SER   E 511 ? 0.9950 1.1166 1.1164 -0.0082 -0.0514 -0.0366 815  SER   E N   
15033 C  CA  . SER   E 511 ? 0.9743 1.0983 1.0958 -0.0105 -0.0517 -0.0342 815  SER   E CA  
15034 C  C   . SER   E 511 ? 1.0052 1.1348 1.1361 -0.0113 -0.0508 -0.0348 815  SER   E C   
15035 O  O   . SER   E 511 ? 1.0217 1.1540 1.1608 -0.0092 -0.0511 -0.0374 815  SER   E O   
15036 C  CB  . SER   E 511 ? 1.0148 1.1370 1.1332 -0.0083 -0.0551 -0.0339 815  SER   E CB  
15037 O  OG  . SER   E 511 ? 1.0442 1.1665 1.1668 -0.0041 -0.0579 -0.0368 815  SER   E OG  
15038 N  N   . LEU   E 512 ? 1.0431 1.1745 1.1733 -0.0144 -0.0495 -0.0324 816  LEU   E N   
15039 C  CA  . LEU   E 512 ? 1.0005 1.1367 1.1387 -0.0156 -0.0484 -0.0324 816  LEU   E CA  
15040 C  C   . LEU   E 512 ? 1.0474 1.1848 1.1840 -0.0171 -0.0497 -0.0302 816  LEU   E C   
15041 O  O   . LEU   E 512 ? 1.0090 1.1440 1.1382 -0.0185 -0.0500 -0.0279 816  LEU   E O   
15042 C  CB  . LEU   E 512 ? 0.9178 1.0544 1.0568 -0.0181 -0.0441 -0.0318 816  LEU   E CB  
15043 C  CG  . LEU   E 512 ? 0.9206 1.0614 1.0687 -0.0190 -0.0420 -0.0323 816  LEU   E CG  
15044 C  CD1 . LEU   E 512 ? 0.9547 1.0982 1.1126 -0.0162 -0.0426 -0.0355 816  LEU   E CD1 
15045 C  CD2 . LEU   E 512 ? 0.9481 1.0875 1.0935 -0.0215 -0.0374 -0.0310 816  LEU   E CD2 
15046 N  N   . VAL   E 513 ? 1.0751 1.2163 1.2190 -0.0167 -0.0505 -0.0308 817  VAL   E N   
15047 C  CA  . VAL   E 513 ? 1.1415 1.2841 1.2847 -0.0177 -0.0518 -0.0289 817  VAL   E CA  
15048 C  C   . VAL   E 513 ? 1.1539 1.3007 1.3063 -0.0180 -0.0515 -0.0298 817  VAL   E C   
15049 O  O   . VAL   E 513 ? 1.1179 1.2666 1.2780 -0.0167 -0.0513 -0.0323 817  VAL   E O   
15050 C  CB  . VAL   E 513 ? 1.1107 1.2512 1.2501 -0.0149 -0.0554 -0.0290 817  VAL   E CB  
15051 C  CG1 . VAL   E 513 ? 1.0696 1.2100 1.2137 -0.0110 -0.0582 -0.0323 817  VAL   E CG1 
15052 C  CG2 . VAL   E 513 ? 1.1405 1.2823 1.2790 -0.0155 -0.0566 -0.0270 817  VAL   E CG2 
15053 N  N   . SER   E 514 ? 1.1895 1.3378 1.3414 -0.0199 -0.0512 -0.0277 818  SER   E N   
15054 C  CA  . SER   E 514 ? 1.1828 1.3344 1.3424 -0.0203 -0.0512 -0.0281 818  SER   E CA  
15055 C  C   . SER   E 514 ? 1.1723 1.3242 1.3301 -0.0195 -0.0541 -0.0270 818  SER   E C   
15056 O  O   . SER   E 514 ? 1.1836 1.3343 1.3347 -0.0209 -0.0539 -0.0244 818  SER   E O   
15057 C  CB  . SER   E 514 ? 1.2001 1.3525 1.3603 -0.0237 -0.0471 -0.0265 818  SER   E CB  
15058 O  OG  . SER   E 514 ? 1.1831 1.3385 1.3511 -0.0242 -0.0467 -0.0269 818  SER   E OG  
15059 N  N   . CYS   E 515 ? 1.2569 1.4102 1.4206 -0.0171 -0.0571 -0.0290 819  CYS   E N   
15060 C  CA  . CYS   E 515 ? 1.3079 1.4610 1.4698 -0.0159 -0.0598 -0.0281 819  CYS   E CA  
15061 C  C   . CYS   E 515 ? 1.2920 1.4468 1.4624 -0.0139 -0.0627 -0.0308 819  CYS   E C   
15062 O  O   . CYS   E 515 ? 1.2075 1.3638 1.3856 -0.0130 -0.0630 -0.0335 819  CYS   E O   
15063 C  CB  . CYS   E 515 ? 1.2579 1.4074 1.4116 -0.0136 -0.0619 -0.0275 819  CYS   E CB  
15064 S  SG  . CYS   E 515 ? 1.1913 1.3382 1.3455 -0.0096 -0.0647 -0.0309 819  CYS   E SG  
15065 N  N   . LYS   E 516 ? 1.3287 1.4834 1.4982 -0.0131 -0.0648 -0.0300 820  LYS   E N   
15066 C  CA  . LYS   E 516 ? 1.3219 1.4769 1.4972 -0.0104 -0.0687 -0.0324 820  LYS   E CA  
15067 C  C   . LYS   E 516 ? 1.3372 1.4882 1.5054 -0.0064 -0.0724 -0.0330 820  LYS   E C   
15068 O  O   . LYS   E 516 ? 1.3153 1.4643 1.4754 -0.0063 -0.0719 -0.0304 820  LYS   E O   
15069 C  CB  . LYS   E 516 ? 1.2539 1.4108 1.4325 -0.0121 -0.0684 -0.0312 820  LYS   E CB  
15070 N  N   . LEU   E 517 ? 1.3330 1.4825 1.5041 -0.0029 -0.0761 -0.0363 821  LEU   E N   
15071 C  CA  . LEU   E 517 ? 1.3256 1.4701 1.4891 0.0015  -0.0796 -0.0371 821  LEU   E CA  
15072 C  C   . LEU   E 517 ? 1.3397 1.4824 1.5052 0.0049  -0.0845 -0.0392 821  LEU   E C   
15073 O  O   . LEU   E 517 ? 1.3713 1.5169 1.5468 0.0046  -0.0864 -0.0415 821  LEU   E O   
15074 C  CB  . LEU   E 517 ? 1.3144 1.4571 1.4782 0.0036  -0.0808 -0.0396 821  LEU   E CB  
15075 C  CG  . LEU   E 517 ? 1.2921 1.4350 1.4523 0.0013  -0.0767 -0.0380 821  LEU   E CG  
15076 C  CD1 . LEU   E 517 ? 1.2930 1.4341 1.4548 0.0041  -0.0787 -0.0411 821  LEU   E CD1 
15077 C  CD2 . LEU   E 517 ? 1.3191 1.4585 1.4680 0.0010  -0.0750 -0.0347 821  LEU   E CD2 
15078 N  N   . GLY   E 518 ? 1.3074 1.4451 1.4634 0.0082  -0.0866 -0.0384 822  GLY   E N   
15079 C  CA  . GLY   E 518 ? 1.3711 1.5060 1.5270 0.0119  -0.0914 -0.0402 822  GLY   E CA  
15080 C  C   . GLY   E 518 ? 1.3925 1.5305 1.5528 0.0095  -0.0906 -0.0390 822  GLY   E C   
15081 O  O   . GLY   E 518 ? 1.3868 1.5273 1.5455 0.0059  -0.0864 -0.0356 822  GLY   E O   
15082 N  N   . LYS   E 519 ? 1.4130 1.5503 1.5787 0.0116  -0.0952 -0.0418 823  LYS   E N   
15083 C  CA  . LYS   E 519 ? 1.4372 1.5775 1.6087 0.0092  -0.0948 -0.0411 823  LYS   E CA  
15084 C  C   . LYS   E 519 ? 1.4447 1.5906 1.6295 0.0055  -0.0933 -0.0425 823  LYS   E C   
15085 O  O   . LYS   E 519 ? 1.4327 1.5813 1.6227 0.0028  -0.0920 -0.0416 823  LYS   E O   
15086 C  CB  . LYS   E 519 ? 1.3832 1.5191 1.5529 0.0134  -0.1003 -0.0431 823  LYS   E CB  
15087 C  CG  . LYS   E 519 ? 1.4273 1.5570 1.5831 0.0171  -0.1008 -0.0412 823  LYS   E CG  
15088 C  CD  . LYS   E 519 ? 1.4961 1.6280 1.6461 0.0137  -0.0947 -0.0364 823  LYS   E CD  
15089 C  CE  . LYS   E 519 ? 1.4980 1.6253 1.6374 0.0164  -0.0944 -0.0339 823  LYS   E CE  
15090 N  NZ  . LYS   E 519 ? 1.2258 1.3568 1.3650 0.0127  -0.0901 -0.0301 823  LYS   E NZ  
15091 N  N   . ASP   E 520 ? 1.4659 1.6135 1.6560 0.0054  -0.0932 -0.0446 824  ASP   E N   
15092 C  CA  . ASP   E 520 ? 1.4417 1.5945 1.6443 0.0020  -0.0908 -0.0458 824  ASP   E CA  
15093 C  C   . ASP   E 520 ? 1.4731 1.6292 1.6758 -0.0029 -0.0848 -0.0421 824  ASP   E C   
15094 O  O   . ASP   E 520 ? 1.5061 1.6614 1.6999 -0.0043 -0.0814 -0.0390 824  ASP   E O   
15095 C  CB  . ASP   E 520 ? 1.4379 1.5914 1.6424 0.0026  -0.0901 -0.0474 824  ASP   E CB  
15096 C  CG  . ASP   E 520 ? 1.4606 1.6188 1.6795 0.0007  -0.0891 -0.0498 824  ASP   E CG  
15097 O  OD1 . ASP   E 520 ? 1.4503 1.6122 1.6752 -0.0033 -0.0847 -0.0482 824  ASP   E OD1 
15098 O  OD2 . ASP   E 520 ? 1.5289 1.6869 1.7531 0.0035  -0.0925 -0.0532 824  ASP   E OD2 
15099 N  N   . PRO   E 521 ? 1.4302 1.5895 1.6425 -0.0057 -0.0834 -0.0424 825  PRO   E N   
15100 C  CA  . PRO   E 521 ? 1.4133 1.5746 1.6242 -0.0099 -0.0780 -0.0389 825  PRO   E CA  
15101 C  C   . PRO   E 521 ? 1.4372 1.6009 1.6501 -0.0129 -0.0727 -0.0379 825  PRO   E C   
15102 O  O   . PRO   E 521 ? 1.4255 1.5894 1.6327 -0.0157 -0.0684 -0.0346 825  PRO   E O   
15103 C  CB  . PRO   E 521 ? 1.4605 1.6234 1.6810 -0.0112 -0.0789 -0.0399 825  PRO   E CB  
15104 C  CG  . PRO   E 521 ? 1.4616 1.6256 1.6933 -0.0094 -0.0825 -0.0442 825  PRO   E CG  
15105 C  CD  . PRO   E 521 ? 1.4497 1.6105 1.6746 -0.0050 -0.0869 -0.0460 825  PRO   E CD  
15106 N  N   . ASN   E 522 ? 1.4175 1.5827 1.6383 -0.0122 -0.0732 -0.0407 826  ASN   E N   
15107 C  CA  . ASN   E 522 ? 1.4180 1.5853 1.6415 -0.0147 -0.0680 -0.0401 826  ASN   E CA  
15108 C  C   . ASN   E 522 ? 1.4229 1.5880 1.6350 -0.0144 -0.0664 -0.0382 826  ASN   E C   
15109 O  O   . ASN   E 522 ? 1.3954 1.5576 1.6000 -0.0115 -0.0698 -0.0385 826  ASN   E O   
15110 C  CB  . ASN   E 522 ? 1.3792 1.5488 1.6151 -0.0136 -0.0692 -0.0438 826  ASN   E CB  
15111 C  CG  . ASN   E 522 ? 1.4090 1.5798 1.6553 -0.0121 -0.0739 -0.0468 826  ASN   E CG  
15112 O  OD1 . ASN   E 522 ? 1.4736 1.6454 1.7245 -0.0143 -0.0728 -0.0459 826  ASN   E OD1 
15113 N  ND2 . ASN   E 522 ? 1.4190 1.5891 1.6687 -0.0083 -0.0794 -0.0503 826  ASN   E ND2 
15114 N  N   . THR   E 523 ? 1.4545 1.6203 1.6649 -0.0174 -0.0610 -0.0363 827  THR   E N   
15115 C  CA  . THR   E 523 ? 1.4185 1.5821 1.6191 -0.0176 -0.0592 -0.0346 827  THR   E CA  
15116 C  C   . THR   E 523 ? 1.3805 1.5449 1.5857 -0.0168 -0.0578 -0.0368 827  THR   E C   
15117 O  O   . THR   E 523 ? 1.4132 1.5800 1.6277 -0.0181 -0.0551 -0.0379 827  THR   E O   
15118 C  CB  . THR   E 523 ? 1.3895 1.5526 1.5838 -0.0211 -0.0547 -0.0310 827  THR   E CB  
15119 O  OG1 . THR   E 523 ? 1.4152 1.5783 1.6078 -0.0218 -0.0557 -0.0293 827  THR   E OG1 
15120 C  CG2 . THR   E 523 ? 1.3610 1.5215 1.5445 -0.0210 -0.0542 -0.0293 827  THR   E CG2 
15121 N  N   . TYR   E 524 ? 1.3022 1.4641 1.5009 -0.0146 -0.0597 -0.0374 828  TYR   E N   
15122 C  CA  . TYR   E 524 ? 1.3095 1.4717 1.5122 -0.0131 -0.0593 -0.0398 828  TYR   E CA  
15123 C  C   . TYR   E 524 ? 1.3194 1.4789 1.5126 -0.0139 -0.0565 -0.0381 828  TYR   E C   
15124 O  O   . TYR   E 524 ? 1.3252 1.4820 1.5082 -0.0142 -0.0570 -0.0359 828  TYR   E O   
15125 C  CB  . TYR   E 524 ? 1.2922 1.4535 1.4972 -0.0088 -0.0651 -0.0430 828  TYR   E CB  
15126 C  CG  . TYR   E 524 ? 1.3628 1.5261 1.5772 -0.0075 -0.0689 -0.0452 828  TYR   E CG  
15127 C  CD1 . TYR   E 524 ? 1.3475 1.5147 1.5759 -0.0081 -0.0682 -0.0476 828  TYR   E CD1 
15128 C  CD2 . TYR   E 524 ? 1.4128 1.5738 1.6224 -0.0057 -0.0731 -0.0450 828  TYR   E CD2 
15129 C  CE1 . TYR   E 524 ? 1.3932 1.5620 1.6310 -0.0070 -0.0722 -0.0499 828  TYR   E CE1 
15130 C  CE2 . TYR   E 524 ? 1.4478 1.6100 1.6656 -0.0043 -0.0771 -0.0472 828  TYR   E CE2 
15131 C  CZ  . TYR   E 524 ? 1.4377 1.6039 1.6698 -0.0051 -0.0768 -0.0498 828  TYR   E CZ  
15132 O  OH  . TYR   E 524 ? 1.4103 1.5775 1.6512 -0.0039 -0.0811 -0.0522 828  TYR   E OH  
15133 N  N   . PHE   E 525 ? 1.2684 1.4287 1.4655 -0.0143 -0.0534 -0.0392 829  PHE   E N   
15134 C  CA  . PHE   E 525 ? 1.1532 1.3106 1.3422 -0.0147 -0.0510 -0.0383 829  PHE   E CA  
15135 C  C   . PHE   E 525 ? 1.1438 1.2992 1.3313 -0.0109 -0.0548 -0.0407 829  PHE   E C   
15136 O  O   . PHE   E 525 ? 1.1331 1.2903 1.3292 -0.0089 -0.0557 -0.0437 829  PHE   E O   
15137 C  CB  . PHE   E 525 ? 1.1288 1.2874 1.3224 -0.0164 -0.0457 -0.0384 829  PHE   E CB  
15138 C  CG  . PHE   E 525 ? 1.1404 1.2987 1.3309 -0.0201 -0.0411 -0.0354 829  PHE   E CG  
15139 C  CD1 . PHE   E 525 ? 1.1651 1.3204 1.3443 -0.0219 -0.0408 -0.0325 829  PHE   E CD1 
15140 C  CD2 . PHE   E 525 ? 1.1153 1.2759 1.3144 -0.0216 -0.0369 -0.0356 829  PHE   E CD2 
15141 C  CE1 . PHE   E 525 ? 1.1239 1.2784 1.2999 -0.0249 -0.0370 -0.0299 829  PHE   E CE1 
15142 C  CE2 . PHE   E 525 ? 1.1061 1.2653 1.3012 -0.0246 -0.0326 -0.0329 829  PHE   E CE2 
15143 C  CZ  . PHE   E 525 ? 1.0835 1.2396 1.2668 -0.0261 -0.0329 -0.0301 829  PHE   E CZ  
15144 N  N   . ILE   E 526 ? 1.1488 1.3004 1.3259 -0.0099 -0.0570 -0.0395 830  ILE   E N   
15145 C  CA  . ILE   E 526 ? 1.1220 1.2707 1.2959 -0.0061 -0.0604 -0.0415 830  ILE   E CA  
15146 C  C   . ILE   E 526 ? 1.0786 1.2240 1.2451 -0.0067 -0.0578 -0.0407 830  ILE   E C   
15147 O  O   . ILE   E 526 ? 1.0264 1.1698 1.1847 -0.0094 -0.0554 -0.0378 830  ILE   E O   
15148 C  CB  . ILE   E 526 ? 1.0635 1.2092 1.2308 -0.0039 -0.0646 -0.0410 830  ILE   E CB  
15149 C  CG1 . ILE   E 526 ? 1.0268 1.1752 1.2006 -0.0035 -0.0670 -0.0416 830  ILE   E CG1 
15150 C  CG2 . ILE   E 526 ? 1.0260 1.1681 1.1908 0.0006  -0.0684 -0.0435 830  ILE   E CG2 
15151 C  CD1 . ILE   E 526 ? 1.0473 1.1949 1.2146 -0.0053 -0.0666 -0.0384 830  ILE   E CD1 
15152 N  N   . VAL   E 527 ? 1.0370 1.1818 1.2067 -0.0042 -0.0584 -0.0433 831  VAL   E N   
15153 C  CA  . VAL   E 527 ? 0.9925 1.1342 1.1563 -0.0042 -0.0561 -0.0432 831  VAL   E CA  
15154 C  C   . VAL   E 527 ? 1.0406 1.1778 1.1983 -0.0004 -0.0600 -0.0445 831  VAL   E C   
15155 O  O   . VAL   E 527 ? 1.0544 1.1917 1.2159 0.0031  -0.0643 -0.0469 831  VAL   E O   
15156 C  CB  . VAL   E 527 ? 0.9876 1.1322 1.1605 -0.0042 -0.0531 -0.0451 831  VAL   E CB  
15157 C  CG1 . VAL   E 527 ? 1.0144 1.1552 1.1810 -0.0037 -0.0509 -0.0453 831  VAL   E CG1 
15158 C  CG2 . VAL   E 527 ? 0.9498 1.0980 1.1280 -0.0078 -0.0488 -0.0436 831  VAL   E CG2 
15159 N  N   . GLY   E 528 ? 1.0567 1.1892 1.2044 -0.0009 -0.0587 -0.0431 832  GLY   E N   
15160 C  CA  . GLY   E 528 ? 1.0378 1.1652 1.1790 0.0026  -0.0615 -0.0443 832  GLY   E CA  
15161 C  C   . GLY   E 528 ? 1.0064 1.1317 1.1461 0.0031  -0.0594 -0.0454 832  GLY   E C   
15162 O  O   . GLY   E 528 ? 1.0027 1.1280 1.1402 0.0000  -0.0554 -0.0438 832  GLY   E O   
15163 N  N   . THR   E 529 ? 1.0842 1.2074 1.2250 0.0074  -0.0622 -0.0483 833  THR   E N   
15164 C  CA  . THR   E 529 ? 1.1088 1.2309 1.2504 0.0084  -0.0603 -0.0499 833  THR   E CA  
15165 C  C   . THR   E 529 ? 1.1310 1.2466 1.2644 0.0121  -0.0631 -0.0510 833  THR   E C   
15166 O  O   . THR   E 529 ? 1.1198 1.2315 1.2469 0.0141  -0.0664 -0.0506 833  THR   E O   
15167 C  CB  . THR   E 529 ? 1.1223 1.2502 1.2780 0.0099  -0.0602 -0.0529 833  THR   E CB  
15168 O  OG1 . THR   E 529 ? 1.1742 1.3014 1.3337 0.0147  -0.0654 -0.0562 833  THR   E OG1 
15169 C  CG2 . THR   E 529 ? 1.0845 1.2185 1.2490 0.0070  -0.0589 -0.0521 833  THR   E CG2 
15170 N  N   . ALA   E 530 ? 1.1095 1.2232 1.2422 0.0133  -0.0615 -0.0524 834  ALA   E N   
15171 C  CA  . ALA   E 530 ? 1.1067 1.2142 1.2325 0.0172  -0.0641 -0.0539 834  ALA   E CA  
15172 C  C   . ALA   E 530 ? 1.1346 1.2436 1.2671 0.0196  -0.0632 -0.0569 834  ALA   E C   
15173 O  O   . ALA   E 530 ? 1.1034 1.2138 1.2373 0.0172  -0.0587 -0.0562 834  ALA   E O   
15174 C  CB  . ALA   E 530 ? 1.1096 1.2104 1.2219 0.0152  -0.0623 -0.0510 834  ALA   E CB  
15175 N  N   . MET   E 531 ? 1.2021 1.3107 1.3389 0.0246  -0.0675 -0.0602 835  MET   E N   
15176 C  CA  . MET   E 531 ? 1.2014 1.3105 1.3435 0.0275  -0.0670 -0.0631 835  MET   E CA  
15177 C  C   . MET   E 531 ? 1.2221 1.3233 1.3513 0.0282  -0.0659 -0.0622 835  MET   E C   
15178 O  O   . MET   E 531 ? 1.2910 1.3856 1.4103 0.0305  -0.0690 -0.0619 835  MET   E O   
15179 C  CB  . MET   E 531 ? 1.2064 1.3170 1.3569 0.0328  -0.0726 -0.0671 835  MET   E CB  
15180 C  CG  . MET   E 531 ? 1.2714 1.3888 1.4342 0.0326  -0.0750 -0.0683 835  MET   E CG  
15181 S  SD  . MET   E 531 ? 1.2301 1.3567 1.4072 0.0281  -0.0690 -0.0678 835  MET   E SD  
15182 C  CE  . MET   E 531 ? 1.1963 1.3240 1.3802 0.0308  -0.0667 -0.0706 835  MET   E CE  
15183 N  N   . VAL   E 532 ? 1.1949 1.2961 1.3237 0.0264  -0.0612 -0.0617 836  VAL   E N   
15184 C  CA  . VAL   E 532 ? 1.2250 1.3184 1.3412 0.0265  -0.0598 -0.0607 836  VAL   E CA  
15185 C  C   . VAL   E 532 ? 1.2336 1.3269 1.3539 0.0296  -0.0585 -0.0634 836  VAL   E C   
15186 O  O   . VAL   E 532 ? 1.2278 1.3272 1.3591 0.0291  -0.0556 -0.0646 836  VAL   E O   
15187 C  CB  . VAL   E 532 ? 1.1950 1.2866 1.3034 0.0210  -0.0555 -0.0570 836  VAL   E CB  
15188 C  CG1 . VAL   E 532 ? 1.1602 1.2515 1.2642 0.0183  -0.0569 -0.0543 836  VAL   E CG1 
15189 C  CG2 . VAL   E 532 ? 1.1817 1.2789 1.2980 0.0182  -0.0507 -0.0567 836  VAL   E CG2 
15190 N  N   . TYR   E 533 ? 1.2984 1.3844 1.4097 0.0328  -0.0603 -0.0643 837  TYR   E N   
15191 C  CA  . TYR   E 533 ? 1.3211 1.4058 1.4347 0.0364  -0.0596 -0.0670 837  TYR   E CA  
15192 C  C   . TYR   E 533 ? 1.4182 1.4936 1.5170 0.0361  -0.0583 -0.0656 837  TYR   E C   
15193 O  O   . TYR   E 533 ? 1.4750 1.5444 1.5627 0.0349  -0.0598 -0.0634 837  TYR   E O   
15194 C  CB  . TYR   E 533 ? 1.3052 1.3908 1.4255 0.0424  -0.0651 -0.0708 837  TYR   E CB  
15195 C  CG  . TYR   E 533 ? 1.2503 1.3441 1.3844 0.0428  -0.0677 -0.0723 837  TYR   E CG  
15196 C  CD1 . TYR   E 533 ? 1.2236 1.3259 1.3736 0.0427  -0.0655 -0.0741 837  TYR   E CD1 
15197 C  CD2 . TYR   E 533 ? 1.2768 1.3695 1.4082 0.0432  -0.0721 -0.0717 837  TYR   E CD2 
15198 C  CE1 . TYR   E 533 ? 1.1990 1.3087 1.3623 0.0428  -0.0680 -0.0756 837  TYR   E CE1 
15199 C  CE2 . TYR   E 533 ? 1.2629 1.3625 1.4065 0.0436  -0.0748 -0.0732 837  TYR   E CE2 
15200 C  CZ  . TYR   E 533 ? 1.2417 1.3498 1.4014 0.0433  -0.0729 -0.0752 837  TYR   E CZ  
15201 O  OH  . TYR   E 533 ? 1.2987 1.4134 1.4710 0.0435  -0.0758 -0.0767 837  TYR   E OH  
15202 N  N   . PRO   E 534 ? 1.4126 1.4864 1.5111 0.0373  -0.0553 -0.0667 838  PRO   E N   
15203 C  CA  . PRO   E 534 ? 1.4793 1.5442 1.5636 0.0360  -0.0534 -0.0650 838  PRO   E CA  
15204 C  C   . PRO   E 534 ? 1.5618 1.6182 1.6355 0.0392  -0.0574 -0.0655 838  PRO   E C   
15205 O  O   . PRO   E 534 ? 1.5649 1.6137 1.6261 0.0372  -0.0565 -0.0633 838  PRO   E O   
15206 C  CB  . PRO   E 534 ? 1.5074 1.5732 1.5957 0.0377  -0.0496 -0.0668 838  PRO   E CB  
15207 C  CG  . PRO   E 534 ? 1.4700 1.5458 1.5746 0.0381  -0.0482 -0.0684 838  PRO   E CG  
15208 C  CD  . PRO   E 534 ? 1.3914 1.4710 1.5025 0.0399  -0.0534 -0.0695 838  PRO   E CD  
15209 N  N   . GLU   E 535 ? 1.6198 1.6769 1.6982 0.0444  -0.0619 -0.0682 839  GLU   E N   
15210 C  CA  . GLU   E 535 ? 1.6624 1.7109 1.7304 0.0481  -0.0659 -0.0687 839  GLU   E CA  
15211 C  C   . GLU   E 535 ? 1.6286 1.6750 1.6910 0.0464  -0.0683 -0.0664 839  GLU   E C   
15212 O  O   . GLU   E 535 ? 1.6197 1.6576 1.6693 0.0457  -0.0685 -0.0644 839  GLU   E O   
15213 C  CB  . GLU   E 535 ? 1.6928 1.7425 1.7679 0.0548  -0.0702 -0.0729 839  GLU   E CB  
15214 C  CG  . GLU   E 535 ? 1.7324 1.7862 1.8167 0.0569  -0.0677 -0.0756 839  GLU   E CG  
15215 C  CD  . GLU   E 535 ? 1.6868 1.7523 1.7881 0.0550  -0.0652 -0.0764 839  GLU   E CD  
15216 O  OE1 . GLU   E 535 ? 1.6581 1.7283 1.7633 0.0514  -0.0651 -0.0747 839  GLU   E OE1 
15217 O  OE2 . GLU   E 535 ? 1.6926 1.7623 1.8035 0.0571  -0.0632 -0.0788 839  GLU   E OE2 
15218 N  N   . GLU   E 536 ? 1.8359 1.8898 1.9081 0.0458  -0.0698 -0.0668 840  GLU   E N   
15219 C  CA  . GLU   E 536 ? 1.8356 1.8884 1.9036 0.0443  -0.0717 -0.0646 840  GLU   E CA  
15220 C  C   . GLU   E 536 ? 1.8190 1.8692 1.8787 0.0384  -0.0678 -0.0605 840  GLU   E C   
15221 O  O   . GLU   E 536 ? 1.8004 1.8562 1.8652 0.0339  -0.0643 -0.0591 840  GLU   E O   
15222 C  CB  . GLU   E 536 ? 1.8644 1.9263 1.9452 0.0441  -0.0734 -0.0656 840  GLU   E CB  
15223 C  CG  . GLU   E 536 ? 1.8670 1.9272 1.9438 0.0442  -0.0764 -0.0641 840  GLU   E CG  
15224 C  CD  . GLU   E 536 ? 1.8899 1.9589 1.9762 0.0403  -0.0753 -0.0629 840  GLU   E CD  
15225 O  OE1 . GLU   E 536 ? 1.8957 1.9699 1.9869 0.0357  -0.0709 -0.0615 840  GLU   E OE1 
15226 O  OE2 . GLU   E 536 ? 1.8549 1.9248 1.9429 0.0420  -0.0788 -0.0633 840  GLU   E OE2 
15227 N  N   . ALA   E 537 ? 1.5361 1.5776 1.5833 0.0384  -0.0684 -0.0585 841  ALA   E N   
15228 C  CA  . ALA   E 537 ? 1.4183 1.4568 1.4579 0.0330  -0.0652 -0.0547 841  ALA   E CA  
15229 C  C   . ALA   E 537 ? 1.3461 1.3899 1.3897 0.0298  -0.0652 -0.0526 841  ALA   E C   
15230 O  O   . ALA   E 537 ? 1.3130 1.3635 1.3628 0.0256  -0.0627 -0.0514 841  ALA   E O   
15231 C  CB  . ALA   E 537 ? 1.3739 1.4012 1.3997 0.0342  -0.0657 -0.0534 841  ALA   E CB  
15232 N  N   . GLU   E 538 ? 1.3038 1.3442 1.3432 0.0323  -0.0679 -0.0520 842  GLU   E N   
15233 C  CA  . GLU   E 538 ? 1.2086 1.2532 1.2510 0.0302  -0.0682 -0.0502 842  GLU   E CA  
15234 C  C   . GLU   E 538 ? 1.2913 1.3443 1.3460 0.0322  -0.0706 -0.0528 842  GLU   E C   
15235 O  O   . GLU   E 538 ? 1.3744 1.4271 1.4324 0.0372  -0.0738 -0.0561 842  GLU   E O   
15236 C  CB  . GLU   E 538 ? 1.1635 1.2005 1.1963 0.0327  -0.0700 -0.0488 842  GLU   E CB  
15237 C  CG  . GLU   E 538 ? 1.2404 1.2728 1.2649 0.0283  -0.0667 -0.0448 842  GLU   E CG  
15238 C  CD  . GLU   E 538 ? 1.4308 1.4517 1.4428 0.0313  -0.0671 -0.0440 842  GLU   E CD  
15239 O  OE1 . GLU   E 538 ? 1.5073 1.5241 1.5166 0.0372  -0.0705 -0.0465 842  GLU   E OE1 
15240 O  OE2 . GLU   E 538 ? 1.3302 1.3458 1.3350 0.0280  -0.0642 -0.0411 842  GLU   E OE2 
15241 N  N   . PRO   E 539 ? 1.2430 1.3033 1.3048 0.0286  -0.0693 -0.0514 843  PRO   E N   
15242 C  CA  . PRO   E 539 ? 1.2685 1.3369 1.3428 0.0301  -0.0714 -0.0538 843  PRO   E CA  
15243 C  C   . PRO   E 539 ? 1.3141 1.3805 1.3876 0.0346  -0.0762 -0.0551 843  PRO   E C   
15244 O  O   . PRO   E 539 ? 1.2807 1.3436 1.3474 0.0340  -0.0763 -0.0528 843  PRO   E O   
15245 C  CB  . PRO   E 539 ? 1.2070 1.2822 1.2867 0.0245  -0.0683 -0.0514 843  PRO   E CB  
15246 C  CG  . PRO   E 539 ? 1.1677 1.2379 1.2371 0.0215  -0.0665 -0.0477 843  PRO   E CG  
15247 C  CD  . PRO   E 539 ? 1.1748 1.2362 1.2338 0.0230  -0.0662 -0.0476 843  PRO   E CD  
15248 N  N   . LYS   E 540 ? 1.3388 1.4072 1.4195 0.0393  -0.0801 -0.0590 844  LYS   E N   
15249 C  CA  . LYS   E 540 ? 1.2547 1.3203 1.3343 0.0443  -0.0854 -0.0608 844  LYS   E CA  
15250 C  C   . LYS   E 540 ? 1.2522 1.3260 1.3454 0.0452  -0.0884 -0.0633 844  LYS   E C   
15251 O  O   . LYS   E 540 ? 1.2556 1.3271 1.3483 0.0494  -0.0934 -0.0651 844  LYS   E O   
15252 C  CB  . LYS   E 540 ? 1.2265 1.2845 1.3000 0.0504  -0.0890 -0.0635 844  LYS   E CB  
15253 C  CG  . LYS   E 540 ? 1.2898 1.3376 1.3475 0.0503  -0.0870 -0.0608 844  LYS   E CG  
15254 C  CD  . LYS   E 540 ? 1.4308 1.4714 1.4826 0.0554  -0.0893 -0.0633 844  LYS   E CD  
15255 C  CE  . LYS   E 540 ? 1.5564 1.5871 1.5934 0.0544  -0.0864 -0.0603 844  LYS   E CE  
15256 N  NZ  . LYS   E 540 ? 1.8304 1.8521 1.8592 0.0601  -0.0891 -0.0625 844  LYS   E NZ  
15257 N  N   . GLN   E 541 ? 1.2500 1.3327 1.3551 0.0414  -0.0856 -0.0634 845  GLN   E N   
15258 C  CA  . GLN   E 541 ? 1.2236 1.3138 1.3414 0.0413  -0.0878 -0.0651 845  GLN   E CA  
15259 C  C   . GLN   E 541 ? 1.2127 1.3105 1.3379 0.0352  -0.0825 -0.0629 845  GLN   E C   
15260 O  O   . GLN   E 541 ? 1.2615 1.3599 1.3858 0.0324  -0.0780 -0.0618 845  GLN   E O   
15261 C  CB  . GLN   E 541 ? 1.2853 1.3787 1.4145 0.0458  -0.0920 -0.0698 845  GLN   E CB  
15262 C  CG  . GLN   E 541 ? 1.4122 1.5081 1.5467 0.0454  -0.0888 -0.0711 845  GLN   E CG  
15263 C  CD  . GLN   E 541 ? 1.5126 1.6124 1.6599 0.0498  -0.0928 -0.0758 845  GLN   E CD  
15264 O  OE1 . GLN   E 541 ? 1.5562 1.6540 1.7048 0.0545  -0.0992 -0.0785 845  GLN   E OE1 
15265 N  NE2 . GLN   E 541 ? 1.5270 1.6323 1.6842 0.0484  -0.0891 -0.0768 845  GLN   E NE2 
15266 N  N   . GLY   E 542 ? 1.2314 1.3341 1.3626 0.0333  -0.0831 -0.0623 846  GLY   E N   
15267 C  CA  . GLY   E 542 ? 1.1944 1.3035 1.3317 0.0278  -0.0784 -0.0601 846  GLY   E CA  
15268 C  C   . GLY   E 542 ? 1.1924 1.3074 1.3401 0.0277  -0.0809 -0.0612 846  GLY   E C   
15269 O  O   . GLY   E 542 ? 1.2494 1.3642 1.4017 0.0320  -0.0862 -0.0643 846  GLY   E O   
15270 N  N   . ARG   E 543 ? 1.1100 1.2295 1.2608 0.0229  -0.0773 -0.0587 847  ARG   E N   
15271 C  CA  . ARG   E 543 ? 1.1072 1.2329 1.2700 0.0224  -0.0789 -0.0599 847  ARG   E CA  
15272 C  C   . ARG   E 543 ? 1.1144 1.2423 1.2753 0.0178  -0.0760 -0.0564 847  ARG   E C   
15273 O  O   . ARG   E 543 ? 1.1433 1.2722 1.3014 0.0137  -0.0710 -0.0538 847  ARG   E O   
15274 C  CB  . ARG   E 543 ? 1.0869 1.2190 1.2640 0.0219  -0.0770 -0.0623 847  ARG   E CB  
15275 C  CG  . ARG   E 543 ? 1.0770 1.2157 1.2685 0.0216  -0.0787 -0.0642 847  ARG   E CG  
15276 C  CD  . ARG   E 543 ? 1.1076 1.2512 1.3134 0.0230  -0.0784 -0.0676 847  ARG   E CD  
15277 N  NE  . ARG   E 543 ? 1.1032 1.2497 1.3119 0.0194  -0.0713 -0.0659 847  ARG   E NE  
15278 C  CZ  . ARG   E 543 ? 1.1337 1.2865 1.3546 0.0165  -0.0676 -0.0659 847  ARG   E CZ  
15279 N  NH1 . ARG   E 543 ? 1.1603 1.3176 1.3928 0.0166  -0.0704 -0.0675 847  ARG   E NH1 
15280 N  NH2 . ARG   E 543 ? 1.1498 1.3037 1.3710 0.0136  -0.0609 -0.0642 847  ARG   E NH2 
15281 N  N   . ILE   E 544 ? 1.0894 1.2179 1.2517 0.0188  -0.0795 -0.0566 848  ILE   E N   
15282 C  CA  . ILE   E 544 ? 1.0391 1.1712 1.2032 0.0149  -0.0773 -0.0541 848  ILE   E CA  
15283 C  C   . ILE   E 544 ? 1.0813 1.2199 1.2605 0.0144  -0.0782 -0.0564 848  ILE   E C   
15284 O  O   . ILE   E 544 ? 1.1085 1.2476 1.2941 0.0181  -0.0832 -0.0597 848  ILE   E O   
15285 C  CB  . ILE   E 544 ? 1.0063 1.1343 1.1617 0.0161  -0.0801 -0.0525 848  ILE   E CB  
15286 C  CG1 . ILE   E 544 ? 1.0598 1.1810 1.2012 0.0169  -0.0792 -0.0504 848  ILE   E CG1 
15287 C  CG2 . ILE   E 544 ? 0.9946 1.1263 1.1517 0.0120  -0.0776 -0.0497 848  ILE   E CG2 
15288 C  CD1 . ILE   E 544 ? 1.0501 1.1662 1.1825 0.0192  -0.0818 -0.0491 848  ILE   E CD1 
15289 N  N   . VAL   E 545 ? 1.0666 1.2100 1.2516 0.0100  -0.0733 -0.0547 849  VAL   E N   
15290 C  CA  . VAL   E 545 ? 1.0503 1.2000 1.2501 0.0089  -0.0728 -0.0565 849  VAL   E CA  
15291 C  C   . VAL   E 545 ? 1.0815 1.2336 1.2814 0.0050  -0.0703 -0.0536 849  VAL   E C   
15292 O  O   . VAL   E 545 ? 1.0832 1.2340 1.2751 0.0017  -0.0662 -0.0502 849  VAL   E O   
15293 C  CB  . VAL   E 545 ? 1.0246 1.1777 1.2327 0.0077  -0.0684 -0.0575 849  VAL   E CB  
15294 C  CG1 . VAL   E 545 ? 1.0742 1.2270 1.2878 0.0121  -0.0719 -0.0613 849  VAL   E CG1 
15295 C  CG2 . VAL   E 545 ? 1.1025 1.2527 1.3003 0.0052  -0.0633 -0.0545 849  VAL   E CG2 
15296 N  N   . VAL   E 546 ? 1.1088 1.2641 1.3181 0.0053  -0.0729 -0.0551 850  VAL   E N   
15297 C  CA  . VAL   E 546 ? 1.1116 1.2692 1.3224 0.0018  -0.0710 -0.0527 850  VAL   E CA  
15298 C  C   . VAL   E 546 ? 1.1474 1.3106 1.3719 -0.0007 -0.0673 -0.0535 850  VAL   E C   
15299 O  O   . VAL   E 546 ? 1.1801 1.3462 1.4168 0.0012  -0.0695 -0.0569 850  VAL   E O   
15300 C  CB  . VAL   E 546 ? 1.0818 1.2383 1.2923 0.0040  -0.0765 -0.0536 850  VAL   E CB  
15301 C  CG1 . VAL   E 546 ? 1.1040 1.2618 1.3128 0.0006  -0.0742 -0.0506 850  VAL   E CG1 
15302 C  CG2 . VAL   E 546 ? 1.0781 1.2285 1.2762 0.0076  -0.0802 -0.0535 850  VAL   E CG2 
15303 N  N   . PHE   E 547 ? 1.1758 1.3401 1.3984 -0.0048 -0.0616 -0.0504 851  PHE   E N   
15304 C  CA  . PHE   E 547 ? 1.1609 1.3294 1.3946 -0.0075 -0.0570 -0.0504 851  PHE   E CA  
15305 C  C   . PHE   E 547 ? 1.2132 1.3831 1.4486 -0.0103 -0.0562 -0.0485 851  PHE   E C   
15306 O  O   . PHE   E 547 ? 1.2047 1.3725 1.4323 -0.0101 -0.0591 -0.0471 851  PHE   E O   
15307 C  CB  . PHE   E 547 ? 1.1667 1.3342 1.3961 -0.0097 -0.0504 -0.0485 851  PHE   E CB  
15308 C  CG  . PHE   E 547 ? 1.1743 1.3407 1.4034 -0.0071 -0.0505 -0.0506 851  PHE   E CG  
15309 C  CD1 . PHE   E 547 ? 1.1268 1.2885 1.3433 -0.0055 -0.0525 -0.0499 851  PHE   E CD1 
15310 C  CD2 . PHE   E 547 ? 1.1782 1.3480 1.4199 -0.0063 -0.0483 -0.0530 851  PHE   E CD2 
15311 C  CE1 . PHE   E 547 ? 1.1132 1.2734 1.3290 -0.0030 -0.0526 -0.0518 851  PHE   E CE1 
15312 C  CE2 . PHE   E 547 ? 1.0988 1.2675 1.3401 -0.0037 -0.0484 -0.0549 851  PHE   E CE2 
15313 C  CZ  . PHE   E 547 ? 1.0747 1.2384 1.3026 -0.0020 -0.0507 -0.0543 851  PHE   E CZ  
15314 N  N   . GLN   E 548 ? 1.3390 1.5123 1.5846 -0.0127 -0.0518 -0.0484 852  GLN   E N   
15315 C  CA  . GLN   E 548 ? 1.3892 1.5633 1.6357 -0.0158 -0.0496 -0.0461 852  GLN   E CA  
15316 C  C   . GLN   E 548 ? 1.4301 1.6060 1.6831 -0.0188 -0.0423 -0.0450 852  GLN   E C   
15317 O  O   . GLN   E 548 ? 1.3914 1.5707 1.6578 -0.0183 -0.0409 -0.0473 852  GLN   E O   
15318 C  CB  . GLN   E 548 ? 1.3664 1.5426 1.6219 -0.0147 -0.0547 -0.0482 852  GLN   E CB  
15319 C  CG  . GLN   E 548 ? 1.4700 1.6470 1.7272 -0.0177 -0.0525 -0.0460 852  GLN   E CG  
15320 C  CD  . GLN   E 548 ? 1.4391 1.6172 1.7035 -0.0164 -0.0582 -0.0481 852  GLN   E CD  
15321 O  OE1 . GLN   E 548 ? 1.4250 1.6008 1.6814 -0.0158 -0.0614 -0.0469 852  GLN   E OE1 
15322 N  NE2 . GLN   E 548 ? 1.4386 1.6201 1.7183 -0.0157 -0.0596 -0.0514 852  GLN   E NE2 
15323 N  N   . TYR   E 549 ? 1.4783 1.6517 1.7219 -0.0216 -0.0376 -0.0414 853  TYR   E N   
15324 C  CA  . TYR   E 549 ? 1.4607 1.6349 1.7099 -0.0242 -0.0307 -0.0402 853  TYR   E CA  
15325 C  C   . TYR   E 549 ? 1.5072 1.6828 1.7626 -0.0262 -0.0302 -0.0393 853  TYR   E C   
15326 O  O   . TYR   E 549 ? 1.5136 1.6917 1.7811 -0.0274 -0.0265 -0.0401 853  TYR   E O   
15327 C  CB  . TYR   E 549 ? 1.3477 1.5177 1.5842 -0.0261 -0.0254 -0.0370 853  TYR   E CB  
15328 C  CG  . TYR   E 549 ? 1.3434 1.5134 1.5856 -0.0278 -0.0178 -0.0362 853  TYR   E CG  
15329 C  CD1 . TYR   E 549 ? 1.3755 1.5476 1.6272 -0.0265 -0.0151 -0.0385 853  TYR   E CD1 
15330 C  CD2 . TYR   E 549 ? 1.2919 1.4595 1.5302 -0.0305 -0.0131 -0.0333 853  TYR   E CD2 
15331 C  CE1 . TYR   E 549 ? 1.3504 1.5223 1.6077 -0.0278 -0.0075 -0.0377 853  TYR   E CE1 
15332 C  CE2 . TYR   E 549 ? 1.2838 1.4506 1.5268 -0.0318 -0.0055 -0.0325 853  TYR   E CE2 
15333 C  CZ  . TYR   E 549 ? 1.3438 1.5128 1.5965 -0.0305 -0.0025 -0.0346 853  TYR   E CZ  
15334 O  OH  . TYR   E 549 ? 1.3413 1.5095 1.5991 -0.0315 0.0055  -0.0338 853  TYR   E OH  
15335 N  N   . SER   E 550 ? 1.6324 1.8065 1.8801 -0.0266 -0.0338 -0.0378 854  SER   E N   
15336 C  CA  . SER   E 550 ? 1.6833 1.8582 1.9351 -0.0283 -0.0340 -0.0369 854  SER   E CA  
15337 C  C   . SER   E 550 ? 1.7129 1.8917 1.9822 -0.0283 -0.0340 -0.0396 854  SER   E C   
15338 O  O   . SER   E 550 ? 1.7266 1.9072 2.0024 -0.0268 -0.0398 -0.0418 854  SER   E O   
15339 C  CB  . SER   E 550 ? 1.6600 1.8338 1.9048 -0.0270 -0.0403 -0.0365 854  SER   E CB  
15340 O  OG  . SER   E 550 ? 1.6494 1.8199 1.8793 -0.0274 -0.0400 -0.0338 854  SER   E OG  
15341 N  N   . ASP   E 551 ? 1.6233 1.8031 1.9003 -0.0300 -0.0275 -0.0394 855  ASP   E N   
15342 C  CA  . ASP   E 551 ? 1.6053 1.7894 1.9007 -0.0302 -0.0267 -0.0420 855  ASP   E CA  
15343 C  C   . ASP   E 551 ? 1.5795 1.7634 1.8800 -0.0325 -0.0176 -0.0405 855  ASP   E C   
15344 O  O   . ASP   E 551 ? 1.5881 1.7725 1.8963 -0.0349 -0.0137 -0.0396 855  ASP   E O   
15345 C  CB  . ASP   E 551 ? 1.5501 1.7374 1.8544 -0.0270 -0.0318 -0.0461 855  ASP   E CB  
15346 N  N   . GLY   E 552 ? 1.5186 1.7014 1.8144 -0.0317 -0.0141 -0.0402 856  GLY   E N   
15347 C  CA  . GLY   E 552 ? 1.4496 1.6322 1.7511 -0.0330 -0.0055 -0.0394 856  GLY   E CA  
15348 C  C   . GLY   E 552 ? 1.5007 1.6844 1.8033 -0.0305 -0.0053 -0.0414 856  GLY   E C   
15349 O  O   . GLY   E 552 ? 1.5096 1.6915 1.8104 -0.0309 0.0017  -0.0402 856  GLY   E O   
15350 N  N   . LYS   E 553 ? 1.4863 1.6723 1.7907 -0.0278 -0.0129 -0.0443 857  LYS   E N   
15351 C  CA  . LYS   E 553 ? 1.4803 1.6666 1.7838 -0.0251 -0.0134 -0.0462 857  LYS   E CA  
15352 C  C   . LYS   E 553 ? 1.4710 1.6558 1.7645 -0.0226 -0.0216 -0.0473 857  LYS   E C   
15353 O  O   . LYS   E 553 ? 1.4764 1.6604 1.7650 -0.0227 -0.0266 -0.0468 857  LYS   E O   
15354 C  CB  . LYS   E 553 ? 1.4892 1.6809 1.8124 -0.0239 -0.0126 -0.0496 857  LYS   E CB  
15355 N  N   . LEU   E 554 ? 1.3763 1.5605 1.6668 -0.0201 -0.0224 -0.0488 858  LEU   E N   
15356 C  CA  . LEU   E 554 ? 1.3309 1.5131 1.6118 -0.0173 -0.0293 -0.0499 858  LEU   E CA  
15357 C  C   . LEU   E 554 ? 1.3529 1.5389 1.6462 -0.0142 -0.0359 -0.0542 858  LEU   E C   
15358 O  O   . LEU   E 554 ? 1.3063 1.4959 1.6131 -0.0130 -0.0344 -0.0567 858  LEU   E O   
15359 C  CB  . LEU   E 554 ? 1.2647 1.4434 1.5348 -0.0163 -0.0266 -0.0491 858  LEU   E CB  
15360 C  CG  . LEU   E 554 ? 1.1749 1.3493 1.4292 -0.0151 -0.0311 -0.0481 858  LEU   E CG  
15361 C  CD1 . LEU   E 554 ? 1.2599 1.4328 1.5069 -0.0170 -0.0332 -0.0457 858  LEU   E CD1 
15362 C  CD2 . LEU   E 554 ? 1.1368 1.3068 1.3794 -0.0156 -0.0264 -0.0462 858  LEU   E CD2 
15363 N  N   . GLN   E 555 ? 1.3345 1.5194 1.6235 -0.0125 -0.0432 -0.0550 859  GLN   E N   
15364 C  CA  . GLN   E 555 ? 1.2882 1.4753 1.5866 -0.0090 -0.0505 -0.0592 859  GLN   E CA  
15365 C  C   . GLN   E 555 ? 1.2258 1.4085 1.5105 -0.0059 -0.0565 -0.0595 859  GLN   E C   
15366 O  O   . GLN   E 555 ? 1.2025 1.3816 1.4741 -0.0068 -0.0573 -0.0569 859  GLN   E O   
15367 C  CB  . GLN   E 555 ? 1.2437 1.4337 1.5534 -0.0097 -0.0539 -0.0605 859  GLN   E CB  
15368 N  N   . THR   E 556 ? 1.2179 1.4007 1.5058 -0.0021 -0.0604 -0.0628 860  THR   E N   
15369 C  CA  . THR   E 556 ? 1.1827 1.3607 1.4585 0.0015  -0.0663 -0.0635 860  THR   E CA  
15370 C  C   . THR   E 556 ? 1.1786 1.3558 1.4557 0.0037  -0.0739 -0.0653 860  THR   E C   
15371 O  O   . THR   E 556 ? 1.2260 1.4063 1.5166 0.0057  -0.0782 -0.0690 860  THR   E O   
15372 C  CB  . THR   E 556 ? 1.2218 1.3998 1.5008 0.0050  -0.0678 -0.0665 860  THR   E CB  
15373 O  OG1 . THR   E 556 ? 1.2410 1.4213 1.5246 0.0030  -0.0605 -0.0656 860  THR   E OG1 
15374 C  CG2 . THR   E 556 ? 1.2446 1.4163 1.5069 0.0077  -0.0708 -0.0658 860  THR   E CG2 
15375 N  N   . VAL   E 557 ? 1.2039 1.3770 1.4674 0.0035  -0.0756 -0.0629 861  VAL   E N   
15376 C  CA  . VAL   E 557 ? 1.1558 1.3273 1.4188 0.0056  -0.0822 -0.0642 861  VAL   E CA  
15377 C  C   . VAL   E 557 ? 1.1713 1.3376 1.4261 0.0109  -0.0891 -0.0665 861  VAL   E C   
15378 O  O   . VAL   E 557 ? 1.1898 1.3546 1.4464 0.0137  -0.0955 -0.0687 861  VAL   E O   
15379 C  CB  . VAL   E 557 ? 1.1352 1.3050 1.3889 0.0025  -0.0799 -0.0603 861  VAL   E CB  
15380 C  CG1 . VAL   E 557 ? 1.1613 1.3294 1.4145 0.0044  -0.0860 -0.0614 861  VAL   E CG1 
15381 C  CG2 . VAL   E 557 ? 1.1792 1.3533 1.4407 -0.0023 -0.0733 -0.0583 861  VAL   E CG2 
15382 N  N   . ALA   E 558 ? 1.1800 1.3431 1.4259 0.0125  -0.0880 -0.0661 862  ALA   E N   
15383 C  CA  . ALA   E 558 ? 1.1604 1.3178 1.3974 0.0176  -0.0938 -0.0679 862  ALA   E CA  
15384 C  C   . ALA   E 558 ? 1.1333 1.2882 1.3624 0.0180  -0.0905 -0.0670 862  ALA   E C   
15385 O  O   . ALA   E 558 ? 1.1283 1.2846 1.3547 0.0143  -0.0840 -0.0641 862  ALA   E O   
15386 C  CB  . ALA   E 558 ? 1.1582 1.3099 1.3815 0.0190  -0.0968 -0.0661 862  ALA   E CB  
15387 N  N   . GLU   E 559 ? 1.2134 1.3640 1.4380 0.0229  -0.0953 -0.0695 863  GLU   E N   
15388 C  CA  . GLU   E 559 ? 1.2088 1.3557 1.4241 0.0239  -0.0930 -0.0687 863  GLU   E CA  
15389 C  C   . GLU   E 559 ? 1.2337 1.3727 1.4369 0.0291  -0.0987 -0.0698 863  GLU   E C   
15390 O  O   . GLU   E 559 ? 1.2904 1.4283 1.4983 0.0337  -0.1045 -0.0737 863  GLU   E O   
15391 C  CB  . GLU   E 559 ? 1.2278 1.3785 1.4543 0.0246  -0.0915 -0.0713 863  GLU   E CB  
15392 C  CG  . GLU   E 559 ? 1.3296 1.4883 1.5723 0.0209  -0.0872 -0.0716 863  GLU   E CG  
15393 C  CD  . GLU   E 559 ? 1.3650 1.5274 1.6207 0.0230  -0.0873 -0.0751 863  GLU   E CD  
15394 O  OE1 . GLU   E 559 ? 1.3172 1.4757 1.5674 0.0269  -0.0900 -0.0768 863  GLU   E OE1 
15395 O  OE2 . GLU   E 559 ? 1.4469 1.6158 1.7180 0.0208  -0.0843 -0.0761 863  GLU   E OE2 
15396 N  N   . LYS   E 560 ? 1.1837 1.3173 1.3717 0.0284  -0.0971 -0.0663 864  LYS   E N   
15397 C  CA  . LYS   E 560 ? 1.1429 1.2682 1.3180 0.0332  -0.1013 -0.0668 864  LYS   E CA  
15398 C  C   . LYS   E 560 ? 1.1581 1.2802 1.3265 0.0338  -0.0987 -0.0664 864  LYS   E C   
15399 O  O   . LYS   E 560 ? 1.1637 1.2859 1.3266 0.0298  -0.0929 -0.0630 864  LYS   E O   
15400 C  CB  . LYS   E 560 ? 1.1541 1.2747 1.3165 0.0325  -0.1007 -0.0634 864  LYS   E CB  
15401 C  CG  . LYS   E 560 ? 1.2205 1.3319 1.3701 0.0380  -0.1052 -0.0641 864  LYS   E CG  
15402 C  CD  . LYS   E 560 ? 1.3191 1.4285 1.4706 0.0421  -0.1118 -0.0668 864  LYS   E CD  
15403 C  CE  . LYS   E 560 ? 1.3508 1.4510 1.4923 0.0489  -0.1174 -0.0691 864  LYS   E CE  
15404 N  NZ  . LYS   E 560 ? 1.2746 1.3765 1.4257 0.0521  -0.1217 -0.0737 864  LYS   E NZ  
15405 N  N   . GLU   E 561 ? 1.1697 1.2888 1.3392 0.0387  -0.1031 -0.0699 865  GLU   E N   
15406 C  CA  . GLU   E 561 ? 1.1337 1.2486 1.2959 0.0402  -0.1015 -0.0699 865  GLU   E CA  
15407 C  C   . GLU   E 561 ? 1.1864 1.2923 1.3306 0.0415  -0.1013 -0.0671 865  GLU   E C   
15408 O  O   . GLU   E 561 ? 1.2341 1.3348 1.3718 0.0450  -0.1057 -0.0676 865  GLU   E O   
15409 C  CB  . GLU   E 561 ? 1.2488 1.3629 1.4174 0.0456  -0.1069 -0.0747 865  GLU   E CB  
15410 C  CG  . GLU   E 561 ? 1.3833 1.4910 1.5422 0.0485  -0.1067 -0.0750 865  GLU   E CG  
15411 C  CD  . GLU   E 561 ? 1.4841 1.5902 1.6484 0.0547  -0.1132 -0.0799 865  GLU   E CD  
15412 O  OE1 . GLU   E 561 ? 1.4102 1.5183 1.5832 0.0574  -0.1190 -0.0831 865  GLU   E OE1 
15413 O  OE2 . GLU   E 561 ? 1.5815 1.6839 1.7412 0.0569  -0.1127 -0.0807 865  GLU   E OE2 
15414 N  N   . VAL   E 562 ? 1.1908 1.2946 1.3270 0.0386  -0.0961 -0.0640 866  VAL   E N   
15415 C  CA  . VAL   E 562 ? 1.1678 1.2631 1.2878 0.0393  -0.0950 -0.0612 866  VAL   E CA  
15416 C  C   . VAL   E 562 ? 1.1527 1.2431 1.2667 0.0411  -0.0942 -0.0618 866  VAL   E C   
15417 O  O   . VAL   E 562 ? 1.2046 1.2993 1.3260 0.0397  -0.0920 -0.0630 866  VAL   E O   
15418 C  CB  . VAL   E 562 ? 1.1294 1.2264 1.2451 0.0335  -0.0895 -0.0565 866  VAL   E CB  
15419 C  CG1 . VAL   E 562 ? 1.0775 1.1776 1.1966 0.0325  -0.0907 -0.0556 866  VAL   E CG1 
15420 C  CG2 . VAL   E 562 ? 1.1645 1.2675 1.2868 0.0286  -0.0844 -0.0555 866  VAL   E CG2 
15421 N  N   . LYS   E 563 ? 1.1652 1.2463 1.2656 0.0446  -0.0957 -0.0611 867  LYS   E N   
15422 C  CA  . LYS   E 563 ? 1.1829 1.2579 1.2766 0.0473  -0.0958 -0.0621 867  LYS   E CA  
15423 C  C   . LYS   E 563 ? 1.1734 1.2458 1.2585 0.0429  -0.0899 -0.0582 867  LYS   E C   
15424 O  O   . LYS   E 563 ? 1.1721 1.2361 1.2447 0.0444  -0.0893 -0.0566 867  LYS   E O   
15425 C  CB  . LYS   E 563 ? 1.1300 1.1954 1.2134 0.0540  -0.1011 -0.0638 867  LYS   E CB  
15426 N  N   . GLY   E 564 ? 1.2211 1.3007 1.3135 0.0374  -0.0856 -0.0567 868  GLY   E N   
15427 C  CA  . GLY   E 564 ? 1.2223 1.3002 1.3082 0.0329  -0.0804 -0.0534 868  GLY   E CA  
15428 C  C   . GLY   E 564 ? 1.1998 1.2860 1.2944 0.0272  -0.0765 -0.0519 868  GLY   E C   
15429 O  O   . GLY   E 564 ? 1.2052 1.2984 1.3112 0.0269  -0.0773 -0.0537 868  GLY   E O   
15430 N  N   . ALA   E 565 ? 1.1244 1.2092 1.2130 0.0228  -0.0723 -0.0487 869  ALA   E N   
15431 C  CA  . ALA   E 565 ? 1.0473 1.1384 1.1416 0.0175  -0.0685 -0.0470 869  ALA   E CA  
15432 C  C   . ALA   E 565 ? 1.0146 1.1086 1.1097 0.0149  -0.0682 -0.0445 869  ALA   E C   
15433 O  O   . ALA   E 565 ? 1.0593 1.1487 1.1465 0.0154  -0.0687 -0.0425 869  ALA   E O   
15434 C  CB  . ALA   E 565 ? 1.0245 1.1122 1.1119 0.0141  -0.0647 -0.0449 869  ALA   E CB  
15435 N  N   . VAL   E 566 ? 0.9890 1.0902 1.0934 0.0124  -0.0670 -0.0446 870  VAL   E N   
15436 C  CA  . VAL   E 566 ? 1.0121 1.1163 1.1174 0.0096  -0.0664 -0.0421 870  VAL   E CA  
15437 C  C   . VAL   E 566 ? 1.0299 1.1350 1.1323 0.0044  -0.0623 -0.0391 870  VAL   E C   
15438 O  O   . VAL   E 566 ? 1.0320 1.1417 1.1402 0.0016  -0.0600 -0.0390 870  VAL   E O   
15439 C  CB  . VAL   E 566 ? 1.0177 1.1286 1.1342 0.0100  -0.0679 -0.0438 870  VAL   E CB  
15440 C  CG1 . VAL   E 566 ? 1.0457 1.1586 1.1617 0.0077  -0.0676 -0.0412 870  VAL   E CG1 
15441 C  CG2 . VAL   E 566 ? 1.0007 1.1103 1.1203 0.0153  -0.0726 -0.0472 870  VAL   E CG2 
15442 N  N   . TYR   E 567 ? 1.0067 1.1068 1.0999 0.0031  -0.0613 -0.0365 871  TYR   E N   
15443 C  CA  . TYR   E 567 ? 0.9406 1.0406 1.0306 -0.0016 -0.0581 -0.0340 871  TYR   E CA  
15444 C  C   . TYR   E 567 ? 0.9485 1.0536 1.0423 -0.0052 -0.0569 -0.0318 871  TYR   E C   
15445 O  O   . TYR   E 567 ? 1.0518 1.1587 1.1462 -0.0089 -0.0546 -0.0306 871  TYR   E O   
15446 C  CB  . TYR   E 567 ? 0.9670 1.0602 1.0472 -0.0020 -0.0576 -0.0320 871  TYR   E CB  
15447 C  CG  . TYR   E 567 ? 0.9699 1.0574 1.0452 0.0007  -0.0581 -0.0338 871  TYR   E CG  
15448 C  CD1 . TYR   E 567 ? 0.9976 1.0848 1.0734 -0.0004 -0.0566 -0.0349 871  TYR   E CD1 
15449 C  CD2 . TYR   E 567 ? 1.0030 1.0847 1.0726 0.0047  -0.0601 -0.0343 871  TYR   E CD2 
15450 C  CE1 . TYR   E 567 ? 0.9946 1.0763 1.0656 0.0023  -0.0571 -0.0366 871  TYR   E CE1 
15451 C  CE2 . TYR   E 567 ? 1.0327 1.1088 1.0975 0.0074  -0.0607 -0.0360 871  TYR   E CE2 
15452 C  CZ  . TYR   E 567 ? 1.0019 1.0782 1.0676 0.0062  -0.0593 -0.0371 871  TYR   E CZ  
15453 O  OH  . TYR   E 567 ? 1.0390 1.1094 1.0997 0.0092  -0.0600 -0.0388 871  TYR   E OH  
15454 N  N   . SER   E 568 ? 1.0063 1.1132 1.1019 -0.0041 -0.0585 -0.0312 872  SER   E N   
15455 C  CA  . SER   E 568 ? 1.0375 1.1486 1.1357 -0.0075 -0.0573 -0.0289 872  SER   E CA  
15456 C  C   . SER   E 568 ? 1.0932 1.2075 1.1966 -0.0052 -0.0595 -0.0298 872  SER   E C   
15457 O  O   . SER   E 568 ? 1.1007 1.2129 1.2040 -0.0010 -0.0622 -0.0318 872  SER   E O   
15458 C  CB  . SER   E 568 ? 1.0448 1.1529 1.1364 -0.0098 -0.0561 -0.0257 872  SER   E CB  
15459 O  OG  . SER   E 568 ? 1.0711 1.1830 1.1649 -0.0138 -0.0547 -0.0235 872  SER   E OG  
15460 N  N   . MET   E 569 ? 1.0935 1.2126 1.2014 -0.0078 -0.0587 -0.0284 873  MET   E N   
15461 C  CA  . MET   E 569 ? 1.1035 1.2252 1.2153 -0.0063 -0.0607 -0.0286 873  MET   E CA  
15462 C  C   . MET   E 569 ? 1.1305 1.2550 1.2423 -0.0096 -0.0592 -0.0256 873  MET   E C   
15463 O  O   . MET   E 569 ? 1.1676 1.2942 1.2803 -0.0133 -0.0569 -0.0243 873  MET   E O   
15464 C  CB  . MET   E 569 ? 1.0601 1.1861 1.1812 -0.0051 -0.0618 -0.0314 873  MET   E CB  
15465 C  CG  . MET   E 569 ? 1.0284 1.1526 1.1515 -0.0009 -0.0645 -0.0348 873  MET   E CG  
15466 S  SD  . MET   E 569 ? 0.9662 1.0959 1.1010 -0.0017 -0.0636 -0.0375 873  MET   E SD  
15467 C  CE  . MET   E 569 ? 1.0548 1.1817 1.1913 0.0037  -0.0673 -0.0415 873  MET   E CE  
15468 N  N   . VAL   E 570 ? 1.1319 1.2561 1.2424 -0.0081 -0.0605 -0.0246 874  VAL   E N   
15469 C  CA  . VAL   E 570 ? 1.1927 1.3200 1.3045 -0.0106 -0.0595 -0.0221 874  VAL   E CA  
15470 C  C   . VAL   E 570 ? 1.2584 1.3871 1.3735 -0.0078 -0.0619 -0.0231 874  VAL   E C   
15471 O  O   . VAL   E 570 ? 1.2379 1.3630 1.3500 -0.0038 -0.0641 -0.0243 874  VAL   E O   
15472 C  CB  . VAL   E 570 ? 1.1673 1.2922 1.2730 -0.0120 -0.0580 -0.0190 874  VAL   E CB  
15473 C  CG1 . VAL   E 570 ? 1.1516 1.2749 1.2544 -0.0150 -0.0561 -0.0181 874  VAL   E CG1 
15474 C  CG2 . VAL   E 570 ? 1.1983 1.3181 1.2983 -0.0083 -0.0590 -0.0189 874  VAL   E CG2 
15475 N  N   . GLU   E 571 ? 1.3651 1.4985 1.4861 -0.0097 -0.0616 -0.0229 875  GLU   E N   
15476 C  CA  . GLU   E 571 ? 1.3424 1.4771 1.4662 -0.0076 -0.0638 -0.0234 875  GLU   E CA  
15477 C  C   . GLU   E 571 ? 1.3684 1.5008 1.4862 -0.0068 -0.0635 -0.0208 875  GLU   E C   
15478 O  O   . GLU   E 571 ? 1.3636 1.4978 1.4805 -0.0098 -0.0614 -0.0180 875  GLU   E O   
15479 C  CB  . GLU   E 571 ? 1.3653 1.5050 1.4962 -0.0103 -0.0630 -0.0233 875  GLU   E CB  
15480 C  CG  . GLU   E 571 ? 1.3971 1.5382 1.5322 -0.0082 -0.0656 -0.0245 875  GLU   E CG  
15481 C  CD  . GLU   E 571 ? 1.4571 1.5997 1.5911 -0.0097 -0.0648 -0.0218 875  GLU   E CD  
15482 O  OE1 . GLU   E 571 ? 1.4941 1.6369 1.6242 -0.0122 -0.0625 -0.0190 875  GLU   E OE1 
15483 O  OE2 . GLU   E 571 ? 1.4806 1.6243 1.6179 -0.0084 -0.0667 -0.0225 875  GLU   E OE2 
15484 N  N   . PHE   E 572 ? 1.3343 1.4623 1.4478 -0.0025 -0.0656 -0.0217 876  PHE   E N   
15485 C  CA  . PHE   E 572 ? 1.3089 1.4334 1.4155 -0.0010 -0.0648 -0.0192 876  PHE   E CA  
15486 C  C   . PHE   E 572 ? 1.2996 1.4237 1.4066 0.0020  -0.0670 -0.0196 876  PHE   E C   
15487 O  O   . PHE   E 572 ? 1.3107 1.4305 1.4146 0.0065  -0.0698 -0.0216 876  PHE   E O   
15488 C  CB  . PHE   E 572 ? 1.2778 1.3960 1.3772 0.0018  -0.0648 -0.0195 876  PHE   E CB  
15489 C  CG  . PHE   E 572 ? 1.2636 1.3778 1.3560 0.0030  -0.0629 -0.0167 876  PHE   E CG  
15490 C  CD1 . PHE   E 572 ? 1.2530 1.3683 1.3444 -0.0006 -0.0595 -0.0135 876  PHE   E CD1 
15491 C  CD2 . PHE   E 572 ? 1.2521 1.3610 1.3389 0.0080  -0.0646 -0.0171 876  PHE   E CD2 
15492 C  CE1 . PHE   E 572 ? 1.2655 1.3774 1.3515 0.0004  -0.0573 -0.0108 876  PHE   E CE1 
15493 C  CE2 . PHE   E 572 ? 1.2696 1.3744 1.3498 0.0093  -0.0621 -0.0143 876  PHE   E CE2 
15494 C  CZ  . PHE   E 572 ? 1.2493 1.3558 1.3295 0.0054  -0.0582 -0.0110 876  PHE   E CZ  
15495 N  N   . ASN   E 573 ? 1.4103 1.5386 1.5207 -0.0003 -0.0660 -0.0179 877  ASN   E N   
15496 C  CA  . ASN   E 573 ? 1.4483 1.5763 1.5589 0.0021  -0.0678 -0.0180 877  ASN   E CA  
15497 C  C   . ASN   E 573 ? 1.4057 1.5337 1.5209 0.0046  -0.0718 -0.0217 877  ASN   E C   
15498 O  O   . ASN   E 573 ? 1.3846 1.5081 1.4964 0.0092  -0.0749 -0.0235 877  ASN   E O   
15499 C  CB  . ASN   E 573 ? 1.4478 1.5701 1.5499 0.0059  -0.0674 -0.0164 877  ASN   E CB  
15500 C  CG  . ASN   E 573 ? 1.4475 1.5700 1.5464 0.0034  -0.0634 -0.0126 877  ASN   E CG  
15501 O  OD1 . ASN   E 573 ? 1.4632 1.5907 1.5664 -0.0011 -0.0614 -0.0110 877  ASN   E OD1 
15502 N  ND2 . ASN   E 573 ? 1.4267 1.5434 1.5179 0.0064  -0.0621 -0.0113 877  ASN   E ND2 
15503 N  N   . GLY   E 574 ? 1.3586 1.4916 1.4819 0.0016  -0.0717 -0.0229 878  GLY   E N   
15504 C  CA  . GLY   E 574 ? 1.3301 1.4642 1.4602 0.0031  -0.0751 -0.0264 878  GLY   E CA  
15505 C  C   . GLY   E 574 ? 1.2986 1.4298 1.4287 0.0062  -0.0777 -0.0296 878  GLY   E C   
15506 O  O   . GLY   E 574 ? 1.2823 1.4152 1.4198 0.0070  -0.0803 -0.0327 878  GLY   E O   
15507 N  N   . LYS   E 575 ? 1.2941 1.4207 1.4164 0.0079  -0.0770 -0.0290 879  LYS   E N   
15508 C  CA  . LYS   E 575 ? 1.2789 1.4022 1.4002 0.0108  -0.0792 -0.0317 879  LYS   E CA  
15509 C  C   . LYS   E 575 ? 1.2695 1.3943 1.3908 0.0075  -0.0758 -0.0308 879  LYS   E C   
15510 O  O   . LYS   E 575 ? 1.2982 1.4252 1.4183 0.0036  -0.0721 -0.0278 879  LYS   E O   
15511 C  CB  . LYS   E 575 ? 1.2451 1.3607 1.3562 0.0158  -0.0811 -0.0318 879  LYS   E CB  
15512 C  CG  . LYS   E 575 ? 1.2725 1.3857 1.3790 0.0178  -0.0817 -0.0302 879  LYS   E CG  
15513 C  CD  . LYS   E 575 ? 1.2498 1.3543 1.3455 0.0235  -0.0836 -0.0305 879  LYS   E CD  
15514 C  CE  . LYS   E 575 ? 1.2210 1.3228 1.3106 0.0250  -0.0825 -0.0280 879  LYS   E CE  
15515 N  NZ  . LYS   E 575 ? 1.2133 1.3056 1.2914 0.0309  -0.0839 -0.0282 879  LYS   E NZ  
15516 N  N   . LEU   E 576 ? 1.2345 1.3577 1.3570 0.0093  -0.0773 -0.0335 880  LEU   E N   
15517 C  CA  . LEU   E 576 ? 1.2290 1.3528 1.3512 0.0068  -0.0745 -0.0331 880  LEU   E CA  
15518 C  C   . LEU   E 576 ? 1.2331 1.3503 1.3451 0.0092  -0.0742 -0.0322 880  LEU   E C   
15519 O  O   . LEU   E 576 ? 1.2373 1.3493 1.3449 0.0140  -0.0774 -0.0340 880  LEU   E O   
15520 C  CB  . LEU   E 576 ? 1.1998 1.3264 1.3306 0.0073  -0.0759 -0.0365 880  LEU   E CB  
15521 C  CG  . LEU   E 576 ? 1.1613 1.2887 1.2933 0.0053  -0.0734 -0.0370 880  LEU   E CG  
15522 C  CD1 . LEU   E 576 ? 1.1629 1.2965 1.3050 0.0020  -0.0713 -0.0376 880  LEU   E CD1 
15523 C  CD2 . LEU   E 576 ? 1.1078 1.2315 1.2387 0.0096  -0.0763 -0.0401 880  LEU   E CD2 
15524 N  N   . LEU   E 577 ? 1.2079 1.3248 1.3158 0.0059  -0.0704 -0.0294 881  LEU   E N   
15525 C  CA  . LEU   E 577 ? 1.1519 1.2625 1.2507 0.0073  -0.0694 -0.0283 881  LEU   E CA  
15526 C  C   . LEU   E 577 ? 1.1632 1.2740 1.2629 0.0055  -0.0680 -0.0292 881  LEU   E C   
15527 O  O   . LEU   E 577 ? 1.1908 1.3048 1.2924 0.0011  -0.0651 -0.0276 881  LEU   E O   
15528 C  CB  . LEU   E 577 ? 1.1389 1.2486 1.2325 0.0050  -0.0662 -0.0243 881  LEU   E CB  
15529 C  CG  . LEU   E 577 ? 1.0944 1.1976 1.1791 0.0057  -0.0644 -0.0227 881  LEU   E CG  
15530 C  CD1 . LEU   E 577 ? 1.1664 1.2628 1.2450 0.0116  -0.0671 -0.0245 881  LEU   E CD1 
15531 C  CD2 . LEU   E 577 ? 1.0949 1.1983 1.1769 0.0034  -0.0613 -0.0188 881  LEU   E CD2 
15532 N  N   . ALA   E 578 ? 1.1354 1.2425 1.2335 0.0092  -0.0703 -0.0320 882  ALA   E N   
15533 C  CA  . ALA   E 578 ? 1.0909 1.1977 1.1898 0.0082  -0.0693 -0.0332 882  ALA   E CA  
15534 C  C   . ALA   E 578 ? 1.1060 1.2053 1.1950 0.0102  -0.0688 -0.0325 882  ALA   E C   
15535 O  O   . ALA   E 578 ? 1.1386 1.2323 1.2207 0.0137  -0.0702 -0.0321 882  ALA   E O   
15536 C  CB  . ALA   E 578 ? 1.0802 1.1892 1.1867 0.0109  -0.0723 -0.0373 882  ALA   E CB  
15537 N  N   . SER   E 579 ? 1.0854 1.1838 1.1729 0.0079  -0.0666 -0.0322 883  SER   E N   
15538 C  CA  . SER   E 579 ? 1.0981 1.1891 1.1768 0.0100  -0.0664 -0.0321 883  SER   E CA  
15539 C  C   . SER   E 579 ? 1.0938 1.1839 1.1748 0.0127  -0.0684 -0.0356 883  SER   E C   
15540 O  O   . SER   E 579 ? 1.0127 1.1081 1.1014 0.0109  -0.0678 -0.0371 883  SER   E O   
15541 C  CB  . SER   E 579 ? 1.0530 1.1423 1.1271 0.0057  -0.0627 -0.0290 883  SER   E CB  
15542 O  OG  . SER   E 579 ? 1.0291 1.1236 1.1086 0.0013  -0.0608 -0.0287 883  SER   E OG  
15543 N  N   . ILE   E 580 ? 1.1384 1.2215 1.2127 0.0174  -0.0706 -0.0370 884  ILE   E N   
15544 C  CA  . ILE   E 580 ? 1.0947 1.1757 1.1698 0.0207  -0.0727 -0.0403 884  ILE   E CA  
15545 C  C   . ILE   E 580 ? 1.0865 1.1588 1.1503 0.0218  -0.0715 -0.0391 884  ILE   E C   
15546 O  O   . ILE   E 580 ? 1.1538 1.2191 1.2093 0.0256  -0.0729 -0.0387 884  ILE   E O   
15547 C  CB  . ILE   E 580 ? 0.9939 1.0744 1.0723 0.0262  -0.0778 -0.0439 884  ILE   E CB  
15548 C  CG1 . ILE   E 580 ? 1.0000 1.0884 1.0892 0.0249  -0.0790 -0.0448 884  ILE   E CG1 
15549 C  CG2 . ILE   E 580 ? 0.9937 1.0730 1.0745 0.0293  -0.0799 -0.0474 884  ILE   E CG2 
15550 C  CD1 . ILE   E 580 ? 1.0383 1.1256 1.1242 0.0255  -0.0798 -0.0430 884  ILE   E CD1 
15551 N  N   . ASN   E 581 ? 1.0390 1.1112 1.1019 0.0186  -0.0686 -0.0383 885  ASN   E N   
15552 C  CA  . ASN   E 581 ? 1.0545 1.1185 1.1073 0.0193  -0.0673 -0.0372 885  ASN   E CA  
15553 C  C   . ASN   E 581 ? 1.0806 1.1396 1.1253 0.0182  -0.0653 -0.0336 885  ASN   E C   
15554 O  O   . ASN   E 581 ? 1.0911 1.1521 1.1361 0.0132  -0.0621 -0.0307 885  ASN   E O   
15555 C  CB  . ASN   E 581 ? 1.1029 1.1610 1.1519 0.0253  -0.0707 -0.0404 885  ASN   E CB  
15556 C  CG  . ASN   E 581 ? 1.1299 1.1926 1.1871 0.0263  -0.0722 -0.0439 885  ASN   E CG  
15557 O  OD1 . ASN   E 581 ? 1.1284 1.1977 1.1930 0.0223  -0.0700 -0.0437 885  ASN   E OD1 
15558 N  ND2 . ASN   E 581 ? 1.1495 1.2084 1.2055 0.0318  -0.0758 -0.0470 885  ASN   E ND2 
15559 N  N   . SER   E 582 ? 1.1204 1.1726 1.1579 0.0228  -0.0670 -0.0337 886  SER   E N   
15560 C  CA  . SER   E 582 ? 1.1265 1.1739 1.1567 0.0221  -0.0645 -0.0301 886  SER   E CA  
15561 C  C   . SER   E 582 ? 1.1778 1.2278 1.2101 0.0234  -0.0655 -0.0294 886  SER   E C   
15562 O  O   . SER   E 582 ? 1.2323 1.2796 1.2600 0.0225  -0.0629 -0.0263 886  SER   E O   
15563 C  CB  . SER   E 582 ? 1.1751 1.2112 1.1935 0.0265  -0.0646 -0.0300 886  SER   E CB  
15564 O  OG  . SER   E 582 ? 1.2851 1.3185 1.3014 0.0249  -0.0635 -0.0304 886  SER   E OG  
15565 N  N   . THR   E 583 ? 1.1658 1.2212 1.2054 0.0254  -0.0690 -0.0323 887  THR   E N   
15566 C  CA  . THR   E 583 ? 1.1880 1.2441 1.2283 0.0281  -0.0712 -0.0325 887  THR   E CA  
15567 C  C   . THR   E 583 ? 1.2024 1.2680 1.2522 0.0235  -0.0698 -0.0313 887  THR   E C   
15568 O  O   . THR   E 583 ? 1.1631 1.2359 1.2223 0.0214  -0.0708 -0.0331 887  THR   E O   
15569 C  CB  . THR   E 583 ? 1.1626 1.2177 1.2050 0.0337  -0.0767 -0.0369 887  THR   E CB  
15570 O  OG1 . THR   E 583 ? 1.1334 1.1800 1.1675 0.0380  -0.0782 -0.0384 887  THR   E OG1 
15571 C  CG2 . THR   E 583 ? 1.2195 1.2732 1.2602 0.0373  -0.0793 -0.0371 887  THR   E CG2 
15572 N  N   . VAL   E 584 ? 1.2376 1.3029 1.2847 0.0222  -0.0676 -0.0281 888  VAL   E N   
15573 C  CA  . VAL   E 584 ? 1.2195 1.2928 1.2746 0.0190  -0.0670 -0.0271 888  VAL   E CA  
15574 C  C   . VAL   E 584 ? 1.2059 1.2788 1.2616 0.0235  -0.0708 -0.0290 888  VAL   E C   
15575 O  O   . VAL   E 584 ? 1.2621 1.3280 1.3094 0.0275  -0.0713 -0.0282 888  VAL   E O   
15576 C  CB  . VAL   E 584 ? 1.1878 1.2617 1.2408 0.0150  -0.0627 -0.0228 888  VAL   E CB  
15577 C  CG1 . VAL   E 584 ? 1.1250 1.2051 1.1839 0.0135  -0.0628 -0.0218 888  VAL   E CG1 
15578 C  CG2 . VAL   E 584 ? 1.1177 1.1940 1.1729 0.0098  -0.0598 -0.0215 888  VAL   E CG2 
15579 N  N   . ARG   E 585 ? 1.1841 1.2639 1.2496 0.0229  -0.0734 -0.0314 889  ARG   E N   
15580 C  CA  . ARG   E 585 ? 1.2210 1.3006 1.2888 0.0272  -0.0780 -0.0342 889  ARG   E CA  
15581 C  C   . ARG   E 585 ? 1.2366 1.3239 1.3130 0.0243  -0.0779 -0.0336 889  ARG   E C   
15582 O  O   . ARG   E 585 ? 1.2315 1.3260 1.3161 0.0197  -0.0761 -0.0334 889  ARG   E O   
15583 C  CB  . ARG   E 585 ? 1.1518 1.2317 1.2242 0.0301  -0.0821 -0.0386 889  ARG   E CB  
15584 C  CG  . ARG   E 585 ? 1.0841 1.1672 1.1643 0.0328  -0.0870 -0.0419 889  ARG   E CG  
15585 C  CD  . ARG   E 585 ? 1.0740 1.1557 1.1571 0.0363  -0.0909 -0.0460 889  ARG   E CD  
15586 N  NE  . ARG   E 585 ? 1.1520 1.2237 1.2228 0.0410  -0.0921 -0.0462 889  ARG   E NE  
15587 C  CZ  . ARG   E 585 ? 1.1639 1.2321 1.2336 0.0443  -0.0947 -0.0490 889  ARG   E CZ  
15588 N  NH1 . ARG   E 585 ? 1.1006 1.1750 1.1812 0.0432  -0.0959 -0.0518 889  ARG   E NH1 
15589 N  NH2 . ARG   E 585 ? 1.2237 1.2818 1.2808 0.0489  -0.0958 -0.0489 889  ARG   E NH2 
15590 N  N   . LEU   E 586 ? 1.2227 1.3079 1.2964 0.0271  -0.0797 -0.0334 890  LEU   E N   
15591 C  CA  . LEU   E 586 ? 1.1749 1.2663 1.2559 0.0251  -0.0801 -0.0331 890  LEU   E CA  
15592 C  C   . LEU   E 586 ? 1.2020 1.2948 1.2896 0.0283  -0.0856 -0.0374 890  LEU   E C   
15593 O  O   . LEU   E 586 ? 1.2337 1.3202 1.3159 0.0338  -0.0897 -0.0394 890  LEU   E O   
15594 C  CB  . LEU   E 586 ? 1.1904 1.2786 1.2646 0.0261  -0.0785 -0.0301 890  LEU   E CB  
15595 C  CG  . LEU   E 586 ? 1.2254 1.3195 1.3056 0.0237  -0.0781 -0.0289 890  LEU   E CG  
15596 C  CD1 . LEU   E 586 ? 1.2250 1.3281 1.3157 0.0179  -0.0762 -0.0286 890  LEU   E CD1 
15597 C  CD2 . LEU   E 586 ? 1.2310 1.3224 1.3042 0.0234  -0.0745 -0.0249 890  LEU   E CD2 
15598 N  N   . TYR   E 587 ? 1.1836 1.2841 1.2827 0.0251  -0.0857 -0.0389 891  TYR   E N   
15599 C  CA  . TYR   E 587 ? 1.1659 1.2690 1.2737 0.0273  -0.0905 -0.0428 891  TYR   E CA  
15600 C  C   . TYR   E 587 ? 1.1573 1.2639 1.2696 0.0262  -0.0913 -0.0422 891  TYR   E C   
15601 O  O   . TYR   E 587 ? 1.1301 1.2390 1.2410 0.0227  -0.0875 -0.0388 891  TYR   E O   
15602 C  CB  . TYR   E 587 ? 1.1269 1.2361 1.2454 0.0245  -0.0897 -0.0447 891  TYR   E CB  
15603 C  CG  . TYR   E 587 ? 1.1276 1.2335 1.2446 0.0273  -0.0914 -0.0472 891  TYR   E CG  
15604 C  CD1 . TYR   E 587 ? 1.2155 1.3172 1.3320 0.0330  -0.0972 -0.0509 891  TYR   E CD1 
15605 C  CD2 . TYR   E 587 ? 1.1473 1.2541 1.2633 0.0244  -0.0875 -0.0459 891  TYR   E CD2 
15606 C  CE1 . TYR   E 587 ? 1.2543 1.3529 1.3696 0.0357  -0.0988 -0.0532 891  TYR   E CE1 
15607 C  CE2 . TYR   E 587 ? 1.1548 1.2586 1.2694 0.0270  -0.0888 -0.0482 891  TYR   E CE2 
15608 C  CZ  . TYR   E 587 ? 1.2144 1.3143 1.3289 0.0327  -0.0944 -0.0518 891  TYR   E CZ  
15609 O  OH  . TYR   E 587 ? 1.2095 1.3063 1.3225 0.0354  -0.0958 -0.0540 891  TYR   E OH  
15610 N  N   . GLU   E 588 ? 1.1741 1.2812 1.2925 0.0291  -0.0964 -0.0457 892  GLU   E N   
15611 C  CA  . GLU   E 588 ? 1.1536 1.2634 1.2766 0.0285  -0.0979 -0.0457 892  GLU   E CA  
15612 C  C   . GLU   E 588 ? 1.2103 1.3258 1.3474 0.0278  -0.1010 -0.0493 892  GLU   E C   
15613 O  O   . GLU   E 588 ? 1.2114 1.3263 1.3529 0.0303  -0.1044 -0.0528 892  GLU   E O   
15614 C  CB  . GLU   E 588 ? 1.2074 1.3097 1.3213 0.0340  -0.1018 -0.0462 892  GLU   E CB  
15615 C  CG  . GLU   E 588 ? 1.2569 1.3572 1.3624 0.0330  -0.0982 -0.0421 892  GLU   E CG  
15616 C  CD  . GLU   E 588 ? 1.3250 1.4159 1.4187 0.0391  -0.1013 -0.0424 892  GLU   E CD  
15617 O  OE1 . GLU   E 588 ? 1.2933 1.3784 1.3838 0.0443  -0.1063 -0.0457 892  GLU   E OE1 
15618 O  OE2 . GLU   E 588 ? 1.3486 1.4375 1.4359 0.0390  -0.0986 -0.0392 892  GLU   E OE2 
15619 N  N   . TRP   E 589 ? 1.3002 1.4211 1.4446 0.0244  -0.0997 -0.0484 893  TRP   E N   
15620 C  CA  . TRP   E 589 ? 1.3139 1.4408 1.4727 0.0227  -0.1015 -0.0511 893  TRP   E CA  
15621 C  C   . TRP   E 589 ? 1.3567 1.4810 1.5177 0.0266  -0.1078 -0.0540 893  TRP   E C   
15622 O  O   . TRP   E 589 ? 1.3791 1.5023 1.5367 0.0265  -0.1079 -0.0524 893  TRP   E O   
15623 C  CB  . TRP   E 589 ? 1.2721 1.4056 1.4369 0.0167  -0.0962 -0.0483 893  TRP   E CB  
15624 C  CG  . TRP   E 589 ? 1.2689 1.4087 1.4484 0.0141  -0.0958 -0.0505 893  TRP   E CG  
15625 C  CD1 . TRP   E 589 ? 1.3306 1.4747 1.5186 0.0112  -0.0949 -0.0502 893  TRP   E CD1 
15626 C  CD2 . TRP   E 589 ? 1.2960 1.4382 1.4835 0.0142  -0.0959 -0.0532 893  TRP   E CD2 
15627 N  NE1 . TRP   E 589 ? 1.3375 1.4867 1.5387 0.0093  -0.0941 -0.0524 893  TRP   E NE1 
15628 C  CE2 . TRP   E 589 ? 1.3279 1.4763 1.5293 0.0112  -0.0947 -0.0543 893  TRP   E CE2 
15629 C  CE3 . TRP   E 589 ? 1.3012 1.4410 1.4858 0.0167  -0.0967 -0.0546 893  TRP   E CE3 
15630 C  CZ2 . TRP   E 589 ? 1.3216 1.4739 1.5343 0.0106  -0.0940 -0.0568 893  TRP   E CZ2 
15631 C  CZ3 . TRP   E 589 ? 1.3062 1.4500 1.5017 0.0162  -0.0964 -0.0573 893  TRP   E CZ3 
15632 C  CH2 . TRP   E 589 ? 1.2911 1.4411 1.5007 0.0132  -0.0949 -0.0583 893  TRP   E CH2 
15633 N  N   . THR   E 590 ? 1.4133 1.5364 1.5800 0.0302  -0.1133 -0.0584 894  THR   E N   
15634 C  CA  . THR   E 590 ? 1.4532 1.5731 1.6221 0.0343  -0.1203 -0.0618 894  THR   E CA  
15635 C  C   . THR   E 590 ? 1.4761 1.6025 1.6588 0.0308  -0.1204 -0.0626 894  THR   E C   
15636 O  O   . THR   E 590 ? 1.3954 1.5289 1.5886 0.0260  -0.1162 -0.0620 894  THR   E O   
15637 C  CB  . THR   E 590 ? 1.4797 1.5962 1.6511 0.0394  -0.1268 -0.0665 894  THR   E CB  
15638 O  OG1 . THR   E 590 ? 1.5096 1.6334 1.6975 0.0370  -0.1270 -0.0692 894  THR   E OG1 
15639 C  CG2 . THR   E 590 ? 1.4299 1.5402 1.5886 0.0425  -0.1260 -0.0657 894  THR   E CG2 
15640 N  N   . THR   E 591 ? 1.5787 1.7018 1.7604 0.0334  -0.1253 -0.0640 895  THR   E N   
15641 C  CA  . THR   E 591 ? 1.5658 1.6937 1.7611 0.0312  -0.1273 -0.0659 895  THR   E CA  
15642 C  C   . THR   E 591 ? 1.5520 1.6850 1.7633 0.0306  -0.1295 -0.0699 895  THR   E C   
15643 O  O   . THR   E 591 ? 1.5223 1.6616 1.7475 0.0268  -0.1281 -0.0705 895  THR   E O   
15644 C  CB  . THR   E 591 ? 1.5161 1.6377 1.7064 0.0355  -0.1337 -0.0677 895  THR   E CB  
15645 O  OG1 . THR   E 591 ? 1.5768 1.6915 1.7612 0.0418  -0.1403 -0.0712 895  THR   E OG1 
15646 C  CG2 . THR   E 591 ? 1.4103 1.5278 1.5861 0.0357  -0.1304 -0.0634 895  THR   E CG2 
15647 N  N   . GLU   E 592 ? 1.6140 1.7443 1.8236 0.0343  -0.1325 -0.0724 896  GLU   E N   
15648 C  CA  . GLU   E 592 ? 1.6101 1.7452 1.8343 0.0343  -0.1345 -0.0761 896  GLU   E CA  
15649 C  C   . GLU   E 592 ? 1.6145 1.7557 1.8434 0.0298  -0.1269 -0.0739 896  GLU   E C   
15650 O  O   . GLU   E 592 ? 1.5868 1.7309 1.8250 0.0304  -0.1278 -0.0767 896  GLU   E O   
15651 C  CB  . GLU   E 592 ? 1.5948 1.7234 1.8138 0.0409  -0.1417 -0.0799 896  GLU   E CB  
15652 C  CG  . GLU   E 592 ? 1.6148 1.7352 1.8247 0.0462  -0.1490 -0.0818 896  GLU   E CG  
15653 C  CD  . GLU   E 592 ? 1.7531 1.8760 1.9767 0.0462  -0.1547 -0.0853 896  GLU   E CD  
15654 O  OE1 . GLU   E 592 ? 1.8757 1.9953 2.1036 0.0510  -0.1631 -0.0902 896  GLU   E OE1 
15655 O  OE2 . GLU   E 592 ? 1.7639 1.8916 1.9939 0.0415  -0.1511 -0.0833 896  GLU   E OE2 
15656 N  N   . LYS   E 593 ? 1.4833 1.6259 1.7056 0.0255  -0.1198 -0.0692 897  LYS   E N   
15657 C  CA  . LYS   E 593 ? 1.3928 1.5402 1.6176 0.0211  -0.1124 -0.0667 897  LYS   E CA  
15658 C  C   . LYS   E 593 ? 1.4366 1.5820 1.6577 0.0237  -0.1128 -0.0680 897  LYS   E C   
15659 O  O   . LYS   E 593 ? 1.4015 1.5513 1.6323 0.0224  -0.1107 -0.0694 897  LYS   E O   
15660 C  CB  . LYS   E 593 ? 1.2591 1.4141 1.5012 0.0169  -0.1097 -0.0676 897  LYS   E CB  
15661 N  N   . GLU   E 594 ? 1.4239 1.5619 1.6302 0.0277  -0.1153 -0.0674 898  GLU   E N   
15662 C  CA  . GLU   E 594 ? 1.3914 1.5258 1.5913 0.0306  -0.1158 -0.0683 898  GLU   E CA  
15663 C  C   . GLU   E 594 ? 1.3721 1.5011 1.5548 0.0306  -0.1122 -0.0642 898  GLU   E C   
15664 O  O   . GLU   E 594 ? 1.3624 1.4902 1.5384 0.0290  -0.1103 -0.0611 898  GLU   E O   
15665 C  CB  . GLU   E 594 ? 1.3627 1.4925 1.5634 0.0370  -0.1242 -0.0730 898  GLU   E CB  
15666 N  N   . LEU   E 595 ? 1.3454 1.4709 1.5211 0.0324  -0.1114 -0.0641 899  LEU   E N   
15667 C  CA  . LEU   E 595 ? 1.3069 1.4271 1.4673 0.0322  -0.1078 -0.0604 899  LEU   E CA  
15668 C  C   . LEU   E 595 ? 1.3494 1.4604 1.4980 0.0385  -0.1127 -0.0619 899  LEU   E C   
15669 O  O   . LEU   E 595 ? 1.3715 1.4800 1.5207 0.0420  -0.1159 -0.0648 899  LEU   E O   
15670 C  CB  . LEU   E 595 ? 1.2659 1.3885 1.4260 0.0289  -0.1022 -0.0587 899  LEU   E CB  
15671 C  CG  . LEU   E 595 ? 1.1750 1.3039 1.3395 0.0225  -0.0957 -0.0554 899  LEU   E CG  
15672 C  CD1 . LEU   E 595 ? 1.1088 1.2398 1.2754 0.0203  -0.0916 -0.0552 899  LEU   E CD1 
15673 C  CD2 . LEU   E 595 ? 1.1289 1.2555 1.2828 0.0203  -0.0925 -0.0511 899  LEU   E CD2 
15674 N  N   . ARG   E 596 ? 1.3289 1.4344 1.4665 0.0402  -0.1132 -0.0598 900  ARG   E N   
15675 C  CA  . ARG   E 596 ? 1.3552 1.4505 1.4788 0.0462  -0.1167 -0.0603 900  ARG   E CA  
15676 C  C   . ARG   E 596 ? 1.3083 1.3994 1.4187 0.0447  -0.1110 -0.0556 900  ARG   E C   
15677 O  O   . ARG   E 596 ? 1.2586 1.3531 1.3686 0.0404  -0.1063 -0.0520 900  ARG   E O   
15678 C  CB  . ARG   E 596 ? 1.3143 1.4056 1.4355 0.0500  -0.1221 -0.0618 900  ARG   E CB  
15679 N  N   . THR   E 597 ? 1.3169 1.4005 1.4167 0.0483  -0.1114 -0.0557 901  THR   E N   
15680 C  CA  . THR   E 597 ? 1.2897 1.3690 1.3777 0.0469  -0.1059 -0.0514 901  THR   E CA  
15681 C  C   . THR   E 597 ? 1.3220 1.3942 1.3984 0.0500  -0.1061 -0.0493 901  THR   E C   
15682 O  O   . THR   E 597 ? 1.3207 1.3850 1.3899 0.0561  -0.1111 -0.0515 901  THR   E O   
15683 C  CB  . THR   E 597 ? 1.3163 1.3898 1.3973 0.0494  -0.1059 -0.0521 901  THR   E CB  
15684 O  OG1 . THR   E 597 ? 1.3665 1.4345 1.4353 0.0486  -0.1009 -0.0479 901  THR   E OG1 
15685 C  CG2 . THR   E 597 ? 1.3798 1.4453 1.4554 0.0568  -0.1128 -0.0560 901  THR   E CG2 
15686 N  N   . GLU   E 598 ? 1.2990 1.3735 1.3731 0.0459  -0.1006 -0.0450 902  GLU   E N   
15687 C  CA  . GLU   E 598 ? 1.3132 1.3812 1.3766 0.0487  -0.0999 -0.0427 902  GLU   E CA  
15688 C  C   . GLU   E 598 ? 1.3451 1.4034 1.3941 0.0519  -0.0975 -0.0406 902  GLU   E C   
15689 O  O   . GLU   E 598 ? 1.4194 1.4681 1.4583 0.0582  -0.1011 -0.0422 902  GLU   E O   
15690 C  CB  . GLU   E 598 ? 1.2927 1.3669 1.3597 0.0436  -0.0952 -0.0389 902  GLU   E CB  
15691 C  CG  . GLU   E 598 ? 1.3457 1.4127 1.4012 0.0470  -0.0940 -0.0364 902  GLU   E CG  
15692 C  CD  . GLU   E 598 ? 1.3423 1.4146 1.4005 0.0428  -0.0896 -0.0327 902  GLU   E CD  
15693 O  OE1 . GLU   E 598 ? 1.2999 1.3815 1.3691 0.0375  -0.0883 -0.0323 902  GLU   E OE1 
15694 O  OE2 . GLU   E 598 ? 1.3544 1.4210 1.4031 0.0452  -0.0873 -0.0301 902  GLU   E OE2 
15695 N  N   . CYS   E 599 ? 1.3643 1.4243 1.4117 0.0475  -0.0915 -0.0372 903  CYS   E N   
15696 C  CA  . CYS   E 599 ? 1.3875 1.4385 1.4220 0.0496  -0.0883 -0.0347 903  CYS   E CA  
15697 C  C   . CYS   E 599 ? 1.3866 1.4400 1.4234 0.0458  -0.0852 -0.0340 903  CYS   E C   
15698 O  O   . CYS   E 599 ? 1.3191 1.3816 1.3667 0.0406  -0.0839 -0.0341 903  CYS   E O   
15699 C  CB  . CYS   E 599 ? 1.3691 1.4183 1.3977 0.0484  -0.0832 -0.0302 903  CYS   E CB  
15700 S  SG  . CYS   E 599 ? 1.2506 1.3125 1.2918 0.0404  -0.0793 -0.0277 903  CYS   E SG  
15701 N  N   . ASN   E 600 ? 1.3997 1.4442 1.4257 0.0486  -0.0838 -0.0331 904  ASN   E N   
15702 C  CA  . ASN   E 600 ? 1.3912 1.4363 1.4178 0.0457  -0.0813 -0.0327 904  ASN   E CA  
15703 C  C   . ASN   E 600 ? 1.3875 1.4278 1.4058 0.0437  -0.0752 -0.0282 904  ASN   E C   
15704 O  O   . ASN   E 600 ? 1.4128 1.4468 1.4223 0.0462  -0.0731 -0.0258 904  ASN   E O   
15705 C  CB  . ASN   E 600 ? 1.3625 1.4014 1.3850 0.0507  -0.0857 -0.0363 904  ASN   E CB  
15706 C  CG  . ASN   E 600 ? 1.3599 1.4068 1.3949 0.0493  -0.0893 -0.0401 904  ASN   E CG  
15707 O  OD1 . ASN   E 600 ? 1.3633 1.4199 1.4092 0.0440  -0.0876 -0.0396 904  ASN   E OD1 
15708 N  ND2 . ASN   E 600 ? 1.3892 1.4317 1.4226 0.0543  -0.0944 -0.0440 904  ASN   E ND2 
15709 N  N   . HIS   E 601 ? 1.3711 1.4145 1.3926 0.0391  -0.0722 -0.0272 905  HIS   E N   
15710 C  CA  . HIS   E 601 ? 1.3402 1.3787 1.3547 0.0370  -0.0669 -0.0235 905  HIS   E CA  
15711 C  C   . HIS   E 601 ? 1.3058 1.3431 1.3203 0.0357  -0.0668 -0.0247 905  HIS   E C   
15712 O  O   . HIS   E 601 ? 1.2517 1.2969 1.2756 0.0317  -0.0672 -0.0260 905  HIS   E O   
15713 C  CB  . HIS   E 601 ? 1.2239 1.2692 1.2441 0.0309  -0.0622 -0.0198 905  HIS   E CB  
15714 C  CG  . HIS   E 601 ? 1.2290 1.2682 1.2416 0.0299  -0.0569 -0.0157 905  HIS   E CG  
15715 N  ND1 . HIS   E 601 ? 1.2742 1.3100 1.2838 0.0277  -0.0543 -0.0146 905  HIS   E ND1 
15716 C  CD2 . HIS   E 601 ? 1.2801 1.3157 1.2877 0.0311  -0.0535 -0.0125 905  HIS   E CD2 
15717 C  CE1 . HIS   E 601 ? 1.3026 1.3332 1.3065 0.0272  -0.0495 -0.0109 905  HIS   E CE1 
15718 N  NE2 . HIS   E 601 ? 1.3127 1.3431 1.3152 0.0292  -0.0487 -0.0095 905  HIS   E NE2 
15719 N  N   . TYR   E 602 ? 1.3035 1.3305 1.3069 0.0392  -0.0660 -0.0243 906  TYR   E N   
15720 C  CA  . TYR   E 602 ? 1.2823 1.3066 1.2840 0.0386  -0.0660 -0.0255 906  TYR   E CA  
15721 C  C   . TYR   E 602 ? 1.2911 1.3125 1.2889 0.0343  -0.0602 -0.0215 906  TYR   E C   
15722 O  O   . TYR   E 602 ? 1.3214 1.3358 1.3110 0.0357  -0.0569 -0.0185 906  TYR   E O   
15723 C  CB  . TYR   E 602 ? 1.3405 1.3548 1.3327 0.0457  -0.0698 -0.0282 906  TYR   E CB  
15724 C  CG  . TYR   E 602 ? 1.3136 1.3306 1.3103 0.0499  -0.0760 -0.0324 906  TYR   E CG  
15725 C  CD1 . TYR   E 602 ? 1.3273 1.3433 1.3224 0.0530  -0.0779 -0.0324 906  TYR   E CD1 
15726 C  CD2 . TYR   E 602 ? 1.3213 1.3419 1.3246 0.0508  -0.0801 -0.0363 906  TYR   E CD2 
15727 C  CE1 . TYR   E 602 ? 1.3292 1.3476 1.3290 0.0566  -0.0839 -0.0363 906  TYR   E CE1 
15728 C  CE2 . TYR   E 602 ? 1.3201 1.3436 1.3291 0.0545  -0.0859 -0.0402 906  TYR   E CE2 
15729 C  CZ  . TYR   E 602 ? 1.3402 1.3626 1.3476 0.0572  -0.0880 -0.0402 906  TYR   E CZ  
15730 O  OH  . TYR   E 602 ? 1.4644 1.4895 1.4780 0.0607  -0.0941 -0.0443 906  TYR   E OH  
15731 N  N   . ASN   E 603 ? 1.2764 1.3029 1.2802 0.0293  -0.0589 -0.0215 907  ASN   E N   
15732 C  CA  . ASN   E 603 ? 1.2559 1.2816 1.2589 0.0242  -0.0540 -0.0180 907  ASN   E CA  
15733 C  C   . ASN   E 603 ? 1.2683 1.2867 1.2649 0.0249  -0.0536 -0.0187 907  ASN   E C   
15734 O  O   . ASN   E 603 ? 1.2928 1.3083 1.2870 0.0289  -0.0572 -0.0220 907  ASN   E O   
15735 C  CB  . ASN   E 603 ? 1.2258 1.2625 1.2402 0.0176  -0.0530 -0.0173 907  ASN   E CB  
15736 C  CG  . ASN   E 603 ? 1.2673 1.3114 1.2884 0.0172  -0.0539 -0.0170 907  ASN   E CG  
15737 O  OD1 . ASN   E 603 ? 1.2762 1.3187 1.2948 0.0177  -0.0517 -0.0144 907  ASN   E OD1 
15738 N  ND2 . ASN   E 603 ? 1.2439 1.2958 1.2735 0.0163  -0.0569 -0.0197 907  ASN   E ND2 
15739 N  N   . ASN   E 604 ? 1.2362 1.2515 1.2301 0.0211  -0.0492 -0.0155 908  ASN   E N   
15740 C  CA  . ASN   E 604 ? 1.2288 1.2380 1.2178 0.0203  -0.0483 -0.0157 908  ASN   E CA  
15741 C  C   . ASN   E 604 ? 1.2073 1.2235 1.2042 0.0143  -0.0479 -0.0160 908  ASN   E C   
15742 O  O   . ASN   E 604 ? 1.2210 1.2327 1.2145 0.0133  -0.0474 -0.0164 908  ASN   E O   
15743 C  CB  . ASN   E 604 ? 1.2622 1.2620 1.2425 0.0201  -0.0437 -0.0121 908  ASN   E CB  
15744 C  CG  . ASN   E 604 ? 1.2979 1.3027 1.2844 0.0139  -0.0395 -0.0083 908  ASN   E CG  
15745 O  OD1 . ASN   E 604 ? 1.3265 1.3401 1.3210 0.0118  -0.0399 -0.0080 908  ASN   E OD1 
15746 N  ND2 . ASN   E 604 ? 1.2764 1.2756 1.2594 0.0110  -0.0355 -0.0056 908  ASN   E ND2 
15747 N  N   . ILE   E 605 ? 1.1960 1.2222 1.2026 0.0105  -0.0482 -0.0157 909  ILE   E N   
15748 C  CA  . ILE   E 605 ? 1.1703 1.2032 1.1842 0.0057  -0.0487 -0.0167 909  ILE   E CA  
15749 C  C   . ILE   E 605 ? 1.1799 1.2195 1.2001 0.0077  -0.0523 -0.0202 909  ILE   E C   
15750 O  O   . ILE   E 605 ? 1.2086 1.2492 1.2294 0.0117  -0.0544 -0.0215 909  ILE   E O   
15751 C  CB  . ILE   E 605 ? 1.1287 1.1676 1.1489 -0.0003 -0.0461 -0.0137 909  ILE   E CB  
15752 C  CG1 . ILE   E 605 ? 1.1132 1.1593 1.1394 0.0000  -0.0468 -0.0132 909  ILE   E CG1 
15753 C  CG2 . ILE   E 605 ? 1.1745 1.2070 1.1898 -0.0021 -0.0424 -0.0103 909  ILE   E CG2 
15754 C  CD1 . ILE   E 605 ? 1.1136 1.1657 1.1461 -0.0054 -0.0446 -0.0104 909  ILE   E CD1 
15755 N  N   . MET   E 606 ? 1.1072 1.1509 1.1320 0.0049  -0.0528 -0.0217 910  MET   E N   
15756 C  CA  . MET   E 606 ? 1.0379 1.0887 1.0702 0.0059  -0.0554 -0.0246 910  MET   E CA  
15757 C  C   . MET   E 606 ? 1.0881 1.1475 1.1283 0.0019  -0.0546 -0.0232 910  MET   E C   
15758 O  O   . MET   E 606 ? 1.1640 1.2253 1.2057 -0.0030 -0.0525 -0.0210 910  MET   E O   
15759 C  CB  . MET   E 606 ? 1.0233 1.0738 1.0562 0.0049  -0.0556 -0.0267 910  MET   E CB  
15760 C  CG  . MET   E 606 ? 1.0440 1.1009 1.0844 0.0061  -0.0576 -0.0297 910  MET   E CG  
15761 S  SD  . MET   E 606 ? 1.0847 1.1400 1.1242 0.0044  -0.0566 -0.0312 910  MET   E SD  
15762 C  CE  . MET   E 606 ? 1.2143 1.2615 1.2472 0.0109  -0.0589 -0.0340 910  MET   E CE  
15763 N  N   . ALA   E 607 ? 1.0743 1.1385 1.1195 0.0041  -0.0565 -0.0244 911  ALA   E N   
15764 C  CA  . ALA   E 607 ? 1.0208 1.0927 1.0730 0.0008  -0.0558 -0.0230 911  ALA   E CA  
15765 C  C   . ALA   E 607 ? 1.0314 1.1095 1.0905 -0.0024 -0.0558 -0.0243 911  ALA   E C   
15766 O  O   . ALA   E 607 ? 1.0031 1.0863 1.0686 -0.0012 -0.0573 -0.0264 911  ALA   E O   
15767 C  CB  . ALA   E 607 ? 1.0630 1.1370 1.1176 0.0043  -0.0579 -0.0238 911  ALA   E CB  
15768 N  N   . LEU   E 608 ? 1.0215 1.0986 1.0790 -0.0064 -0.0539 -0.0230 912  LEU   E N   
15769 C  CA  . LEU   E 608 ? 0.9783 1.0599 1.0404 -0.0097 -0.0533 -0.0237 912  LEU   E CA  
15770 C  C   . LEU   E 608 ? 0.9684 1.0567 1.0363 -0.0129 -0.0528 -0.0220 912  LEU   E C   
15771 O  O   . LEU   E 608 ? 1.0084 1.1019 1.0820 -0.0134 -0.0530 -0.0233 912  LEU   E O   
15772 C  CB  . LEU   E 608 ? 1.0033 1.0806 1.0606 -0.0127 -0.0519 -0.0228 912  LEU   E CB  
15773 C  CG  . LEU   E 608 ? 1.0002 1.0725 1.0535 -0.0106 -0.0522 -0.0251 912  LEU   E CG  
15774 C  CD1 . LEU   E 608 ? 0.9281 1.0045 0.9863 -0.0098 -0.0525 -0.0277 912  LEU   E CD1 
15775 C  CD2 . LEU   E 608 ? 1.0894 1.1570 1.1386 -0.0058 -0.0535 -0.0260 912  LEU   E CD2 
15776 N  N   . TYR   E 609 ? 0.9597 1.0477 1.0262 -0.0153 -0.0517 -0.0191 913  TYR   E N   
15777 C  CA  . TYR   E 609 ? 0.9903 1.0842 1.0619 -0.0183 -0.0513 -0.0174 913  TYR   E CA  
15778 C  C   . TYR   E 609 ? 1.0478 1.1435 1.1210 -0.0159 -0.0519 -0.0166 913  TYR   E C   
15779 O  O   . TYR   E 609 ? 1.0156 1.1068 1.0844 -0.0133 -0.0517 -0.0159 913  TYR   E O   
15780 C  CB  . TYR   E 609 ? 0.9288 1.0219 0.9991 -0.0228 -0.0501 -0.0148 913  TYR   E CB  
15781 C  CG  . TYR   E 609 ? 0.9562 1.0462 1.0236 -0.0248 -0.0499 -0.0157 913  TYR   E CG  
15782 C  CD1 . TYR   E 609 ? 0.9337 1.0268 1.0036 -0.0267 -0.0501 -0.0167 913  TYR   E CD1 
15783 C  CD2 . TYR   E 609 ? 1.0373 1.1207 1.0989 -0.0245 -0.0495 -0.0157 913  TYR   E CD2 
15784 C  CE1 . TYR   E 609 ? 0.9349 1.0244 1.0012 -0.0282 -0.0499 -0.0176 913  TYR   E CE1 
15785 C  CE2 . TYR   E 609 ? 1.0082 1.0882 1.0667 -0.0261 -0.0495 -0.0167 913  TYR   E CE2 
15786 C  CZ  . TYR   E 609 ? 0.9598 1.0429 1.0205 -0.0279 -0.0497 -0.0177 913  TYR   E CZ  
15787 O  OH  . TYR   E 609 ? 1.0005 1.0795 1.0571 -0.0292 -0.0497 -0.0187 913  TYR   E OH  
15788 N  N   . LEU   E 610 ? 1.0537 1.1555 1.1328 -0.0165 -0.0524 -0.0167 914  LEU   E N   
15789 C  CA  . LEU   E 610 ? 1.0110 1.1151 1.0923 -0.0142 -0.0533 -0.0163 914  LEU   E CA  
15790 C  C   . LEU   E 610 ? 0.9767 1.0868 1.0632 -0.0175 -0.0528 -0.0147 914  LEU   E C   
15791 O  O   . LEU   E 610 ? 1.0415 1.1553 1.1320 -0.0191 -0.0530 -0.0158 914  LEU   E O   
15792 C  CB  . LEU   E 610 ? 1.0592 1.1640 1.1430 -0.0102 -0.0555 -0.0194 914  LEU   E CB  
15793 C  CG  . LEU   E 610 ? 1.0808 1.1849 1.1641 -0.0063 -0.0571 -0.0198 914  LEU   E CG  
15794 C  CD1 . LEU   E 610 ? 1.0497 1.1468 1.1250 -0.0038 -0.0565 -0.0185 914  LEU   E CD1 
15795 C  CD2 . LEU   E 610 ? 1.0466 1.1516 1.1335 -0.0028 -0.0599 -0.0234 914  LEU   E CD2 
15796 N  N   . LYS   E 611 ? 1.0108 1.1214 1.0970 -0.0183 -0.0519 -0.0121 915  LYS   E N   
15797 C  CA  . LYS   E 611 ? 1.0983 1.2144 1.1892 -0.0209 -0.0517 -0.0105 915  LYS   E CA  
15798 C  C   . LYS   E 611 ? 1.1499 1.2662 1.2406 -0.0189 -0.0513 -0.0087 915  LYS   E C   
15799 O  O   . LYS   E 611 ? 1.1394 1.2514 1.2258 -0.0174 -0.0501 -0.0074 915  LYS   E O   
15800 C  CB  . LYS   E 611 ? 1.0375 1.1546 1.1290 -0.0255 -0.0506 -0.0085 915  LYS   E CB  
15801 C  CG  . LYS   E 611 ? 0.9895 1.1061 1.0805 -0.0277 -0.0509 -0.0101 915  LYS   E CG  
15802 C  CD  . LYS   E 611 ? 1.0411 1.1623 1.1360 -0.0303 -0.0512 -0.0099 915  LYS   E CD  
15803 C  CE  . LYS   E 611 ? 1.0389 1.1591 1.1328 -0.0311 -0.0511 -0.0119 915  LYS   E CE  
15804 N  NZ  . LYS   E 611 ? 1.0017 1.1176 1.0912 -0.0331 -0.0509 -0.0118 915  LYS   E NZ  
15805 N  N   . THR   E 612 ? 1.3330 1.4540 1.4280 -0.0188 -0.0521 -0.0086 916  THR   E N   
15806 C  CA  . THR   E 612 ? 1.3108 1.4322 1.4057 -0.0165 -0.0519 -0.0072 916  THR   E CA  
15807 C  C   . THR   E 612 ? 1.3152 1.4418 1.4147 -0.0194 -0.0513 -0.0051 916  THR   E C   
15808 O  O   . THR   E 612 ? 1.3190 1.4496 1.4223 -0.0218 -0.0521 -0.0057 916  THR   E O   
15809 C  CB  . THR   E 612 ? 1.3160 1.4370 1.4113 -0.0124 -0.0541 -0.0096 916  THR   E CB  
15810 O  OG1 . THR   E 612 ? 1.3301 1.4557 1.4310 -0.0138 -0.0554 -0.0114 916  THR   E OG1 
15811 C  CG2 . THR   E 612 ? 1.3351 1.4504 1.4256 -0.0089 -0.0551 -0.0116 916  THR   E CG2 
15812 N  N   . LYS   E 613 ? 1.2001 1.3263 1.2987 -0.0189 -0.0498 -0.0026 917  LYS   E N   
15813 C  CA  . LYS   E 613 ? 1.1990 1.3300 1.3018 -0.0203 -0.0495 -0.0007 917  LYS   E CA  
15814 C  C   . LYS   E 613 ? 1.2718 1.4012 1.3727 -0.0160 -0.0496 -0.0006 917  LYS   E C   
15815 O  O   . LYS   E 613 ? 1.2557 1.3817 1.3531 -0.0141 -0.0476 0.0011  917  LYS   E O   
15816 C  CB  . LYS   E 613 ? 1.0625 1.1948 1.1672 -0.0237 -0.0476 0.0022  917  LYS   E CB  
15817 N  N   . GLY   E 614 ? 1.2933 1.4243 1.3958 -0.0142 -0.0518 -0.0026 918  GLY   E N   
15818 C  CA  . GLY   E 614 ? 1.1975 1.3271 1.2984 -0.0101 -0.0526 -0.0028 918  GLY   E CA  
15819 C  C   . GLY   E 614 ? 1.2369 1.3597 1.3311 -0.0056 -0.0527 -0.0037 918  GLY   E C   
15820 O  O   . GLY   E 614 ? 1.2752 1.3959 1.3683 -0.0030 -0.0553 -0.0067 918  GLY   E O   
15821 N  N   . ASP   E 615 ? 1.2389 1.3580 1.3286 -0.0045 -0.0500 -0.0013 919  ASP   E N   
15822 C  CA  . ASP   E 615 ? 1.2493 1.3607 1.3311 0.0002  -0.0495 -0.0015 919  ASP   E CA  
15823 C  C   . ASP   E 615 ? 1.2068 1.3138 1.2846 -0.0004 -0.0479 -0.0013 919  ASP   E C   
15824 O  O   . ASP   E 615 ? 1.1770 1.2772 1.2479 0.0036  -0.0485 -0.0025 919  ASP   E O   
15825 C  CB  . ASP   E 615 ? 1.3387 1.4480 1.4174 0.0024  -0.0466 0.0014  919  ASP   E CB  
15826 C  CG  . ASP   E 615 ? 1.3601 1.4729 1.4428 -0.0018 -0.0427 0.0049  919  ASP   E CG  
15827 O  OD1 . ASP   E 615 ? 1.3431 1.4614 1.4320 -0.0065 -0.0432 0.0050  919  ASP   E OD1 
15828 O  OD2 . ASP   E 615 ? 1.3550 1.4647 1.4346 -0.0002 -0.0392 0.0077  919  ASP   E OD2 
15829 N  N   . PHE   E 616 ? 1.2475 1.3577 1.3292 -0.0053 -0.0462 0.0001  920  PHE   E N   
15830 C  CA  . PHE   E 616 ? 1.2632 1.3694 1.3417 -0.0066 -0.0446 0.0006  920  PHE   E CA  
15831 C  C   . PHE   E 616 ? 1.2472 1.3543 1.3270 -0.0080 -0.0471 -0.0024 920  PHE   E C   
15832 O  O   . PHE   E 616 ? 1.2440 1.3564 1.3292 -0.0100 -0.0490 -0.0038 920  PHE   E O   
15833 C  CB  . PHE   E 616 ? 1.2911 1.4000 1.3734 -0.0111 -0.0415 0.0037  920  PHE   E CB  
15834 C  CG  . PHE   E 616 ? 1.3411 1.4486 1.4223 -0.0097 -0.0381 0.0069  920  PHE   E CG  
15835 C  CD1 . PHE   E 616 ? 1.3313 1.4319 1.4049 -0.0044 -0.0368 0.0071  920  PHE   E CD1 
15836 C  CD2 . PHE   E 616 ? 1.4118 1.5245 1.4995 -0.0133 -0.0361 0.0095  920  PHE   E CD2 
15837 C  CE1 . PHE   E 616 ? 1.2884 1.3872 1.3606 -0.0029 -0.0330 0.0102  920  PHE   E CE1 
15838 C  CE2 . PHE   E 616 ? 1.4040 1.5156 1.4915 -0.0119 -0.0325 0.0126  920  PHE   E CE2 
15839 C  CZ  . PHE   E 616 ? 1.3646 1.4693 1.4442 -0.0067 -0.0307 0.0130  920  PHE   E CZ  
15840 N  N   . ILE   E 617 ? 1.1888 1.2900 1.2633 -0.0067 -0.0468 -0.0032 921  ILE   E N   
15841 C  CA  . ILE   E 617 ? 1.1623 1.2632 1.2370 -0.0075 -0.0487 -0.0059 921  ILE   E CA  
15842 C  C   . ILE   E 617 ? 1.1618 1.2593 1.2339 -0.0102 -0.0465 -0.0046 921  ILE   E C   
15843 O  O   . ILE   E 617 ? 1.1877 1.2793 1.2543 -0.0085 -0.0443 -0.0029 921  ILE   E O   
15844 C  CB  . ILE   E 617 ? 1.1496 1.2459 1.2200 -0.0023 -0.0513 -0.0089 921  ILE   E CB  
15845 C  CG1 . ILE   E 617 ? 1.1274 1.2257 1.1995 0.0008  -0.0535 -0.0099 921  ILE   E CG1 
15846 C  CG2 . ILE   E 617 ? 1.1741 1.2716 1.2467 -0.0031 -0.0534 -0.0118 921  ILE   E CG2 
15847 C  CD1 . ILE   E 617 ? 1.2175 1.3088 1.2819 0.0062  -0.0537 -0.0098 921  ILE   E CD1 
15848 N  N   . LEU   E 618 ? 1.1131 1.2136 1.1887 -0.0141 -0.0471 -0.0052 922  LEU   E N   
15849 C  CA  . LEU   E 618 ? 1.0902 1.1874 1.1636 -0.0169 -0.0456 -0.0044 922  LEU   E CA  
15850 C  C   . LEU   E 618 ? 1.0862 1.1804 1.1567 -0.0158 -0.0473 -0.0073 922  LEU   E C   
15851 O  O   . LEU   E 618 ? 1.0984 1.1965 1.1726 -0.0168 -0.0489 -0.0092 922  LEU   E O   
15852 C  CB  . LEU   E 618 ? 1.0501 1.1523 1.1290 -0.0223 -0.0451 -0.0028 922  LEU   E CB  
15853 C  CG  . LEU   E 618 ? 1.0098 1.1083 1.0865 -0.0251 -0.0442 -0.0023 922  LEU   E CG  
15854 C  CD1 . LEU   E 618 ? 1.0836 1.1761 1.1560 -0.0240 -0.0415 -0.0002 922  LEU   E CD1 
15855 C  CD2 . LEU   E 618 ? 0.9841 1.0869 1.0660 -0.0301 -0.0446 -0.0011 922  LEU   E CD2 
15856 N  N   . VAL   E 619 ? 1.0544 1.1415 1.1184 -0.0136 -0.0465 -0.0074 923  VAL   E N   
15857 C  CA  . VAL   E 619 ? 1.0456 1.1291 1.1063 -0.0119 -0.0480 -0.0102 923  VAL   E CA  
15858 C  C   . VAL   E 619 ? 1.1025 1.1823 1.1606 -0.0151 -0.0466 -0.0094 923  VAL   E C   
15859 O  O   . VAL   E 619 ? 1.1391 1.2156 1.1950 -0.0166 -0.0443 -0.0069 923  VAL   E O   
15860 C  CB  . VAL   E 619 ? 1.0862 1.1634 1.1406 -0.0061 -0.0489 -0.0115 923  VAL   E CB  
15861 C  CG1 . VAL   E 619 ? 1.1397 1.2140 1.1918 -0.0040 -0.0509 -0.0147 923  VAL   E CG1 
15862 C  CG2 . VAL   E 619 ? 1.1142 1.1942 1.1706 -0.0029 -0.0505 -0.0122 923  VAL   E CG2 
15863 N  N   . GLY   E 620 ? 1.0835 1.1635 1.1419 -0.0159 -0.0480 -0.0117 924  GLY   E N   
15864 C  CA  . GLY   E 620 ? 1.0343 1.1111 1.0904 -0.0191 -0.0471 -0.0112 924  GLY   E CA  
15865 C  C   . GLY   E 620 ? 1.0750 1.1474 1.1270 -0.0168 -0.0482 -0.0140 924  GLY   E C   
15866 O  O   . GLY   E 620 ? 1.0687 1.1427 1.1219 -0.0136 -0.0499 -0.0166 924  GLY   E O   
15867 N  N   . ASP   E 621 ? 1.2307 1.2980 1.2786 -0.0188 -0.0474 -0.0135 925  ASP   E N   
15868 C  CA  . ASP   E 621 ? 1.2232 1.2842 1.2653 -0.0164 -0.0479 -0.0155 925  ASP   E CA  
15869 C  C   . ASP   E 621 ? 1.2268 1.2861 1.2679 -0.0205 -0.0476 -0.0154 925  ASP   E C   
15870 O  O   . ASP   E 621 ? 1.2456 1.3054 1.2883 -0.0246 -0.0466 -0.0131 925  ASP   E O   
15871 C  CB  . ASP   E 621 ? 1.2530 1.3064 1.2883 -0.0133 -0.0468 -0.0145 925  ASP   E CB  
15872 C  CG  . ASP   E 621 ? 1.3218 1.3674 1.3501 -0.0112 -0.0471 -0.0161 925  ASP   E CG  
15873 O  OD1 . ASP   E 621 ? 1.3614 1.4064 1.3885 -0.0071 -0.0490 -0.0190 925  ASP   E OD1 
15874 O  OD2 . ASP   E 621 ? 1.3263 1.3662 1.3504 -0.0133 -0.0455 -0.0144 925  ASP   E OD2 
15875 N  N   . LEU   E 622 ? 1.1081 1.1653 1.1469 -0.0194 -0.0485 -0.0179 926  LEU   E N   
15876 C  CA  . LEU   E 622 ? 1.0654 1.1214 1.1033 -0.0231 -0.0485 -0.0181 926  LEU   E CA  
15877 C  C   . LEU   E 622 ? 1.0857 1.1364 1.1202 -0.0265 -0.0477 -0.0159 926  LEU   E C   
15878 O  O   . LEU   E 622 ? 1.0474 1.0967 1.0811 -0.0299 -0.0482 -0.0160 926  LEU   E O   
15879 C  CB  . LEU   E 622 ? 1.0092 1.0619 1.0436 -0.0206 -0.0492 -0.0210 926  LEU   E CB  
15880 C  CG  . LEU   E 622 ? 0.9868 1.0455 1.0261 -0.0207 -0.0496 -0.0228 926  LEU   E CG  
15881 C  CD1 . LEU   E 622 ? 1.1556 1.2203 1.2006 -0.0180 -0.0501 -0.0232 926  LEU   E CD1 
15882 C  CD2 . LEU   E 622 ? 0.9313 0.9868 0.9676 -0.0184 -0.0497 -0.0254 926  LEU   E CD2 
15883 N  N   . MET   E 623 ? 1.1431 1.1900 1.1753 -0.0256 -0.0464 -0.0141 927  MET   E N   
15884 C  CA  . MET   E 623 ? 1.0842 1.1259 1.1141 -0.0289 -0.0451 -0.0119 927  MET   E CA  
15885 C  C   . MET   E 623 ? 1.0630 1.1080 1.0977 -0.0310 -0.0435 -0.0088 927  MET   E C   
15886 O  O   . MET   E 623 ? 1.0637 1.1041 1.0959 -0.0304 -0.0413 -0.0068 927  MET   E O   
15887 C  CB  . MET   E 623 ? 1.0848 1.1172 1.1067 -0.0260 -0.0442 -0.0124 927  MET   E CB  
15888 C  CG  . MET   E 623 ? 1.0816 1.1111 1.0990 -0.0228 -0.0458 -0.0157 927  MET   E CG  
15889 S  SD  . MET   E 623 ? 1.1400 1.1578 1.1473 -0.0200 -0.0454 -0.0167 927  MET   E SD  
15890 C  CE  . MET   E 623 ? 1.0148 1.0271 1.0205 -0.0256 -0.0440 -0.0141 927  MET   E CE  
15891 N  N   . ARG   E 624 ? 1.0722 1.1251 1.1138 -0.0334 -0.0444 -0.0083 928  ARG   E N   
15892 C  CA  . ARG   E 624 ? 1.0801 1.1377 1.1278 -0.0358 -0.0432 -0.0055 928  ARG   E CA  
15893 C  C   . ARG   E 624 ? 1.1471 1.2025 1.1929 -0.0325 -0.0408 -0.0039 928  ARG   E C   
15894 O  O   . ARG   E 624 ? 1.1559 1.2116 1.2046 -0.0343 -0.0386 -0.0011 928  ARG   E O   
15895 C  CB  . ARG   E 624 ? 1.0902 1.1466 1.1405 -0.0410 -0.0431 -0.0038 928  ARG   E CB  
15896 C  CG  . ARG   E 624 ? 1.1157 1.1790 1.1744 -0.0444 -0.0431 -0.0016 928  ARG   E CG  
15897 C  CD  . ARG   E 624 ? 1.1753 1.2357 1.2367 -0.0489 -0.0424 0.0005  928  ARG   E CD  
15898 N  NE  . ARG   E 624 ? 1.2221 1.2880 1.2919 -0.0516 -0.0414 0.0031  928  ARG   E NE  
15899 C  CZ  . ARG   E 624 ? 1.2838 1.3514 1.3560 -0.0499 -0.0383 0.0053  928  ARG   E CZ  
15900 N  NH1 . ARG   E 624 ? 1.2537 1.3183 1.3201 -0.0451 -0.0363 0.0051  928  ARG   E NH1 
15901 N  NH2 . ARG   E 624 ? 1.3151 1.3870 1.3954 -0.0528 -0.0372 0.0078  928  ARG   E NH2 
15902 N  N   . SER   E 625 ? 1.1799 1.2330 1.2210 -0.0274 -0.0412 -0.0057 929  SER   E N   
15903 C  CA  . SER   E 625 ? 1.1545 1.2052 1.1929 -0.0235 -0.0394 -0.0045 929  SER   E CA  
15904 C  C   . SER   E 625 ? 1.1299 1.1886 1.1743 -0.0230 -0.0401 -0.0042 929  SER   E C   
15905 O  O   . SER   E 625 ? 1.1505 1.2127 1.1961 -0.0205 -0.0423 -0.0065 929  SER   E O   
15906 C  CB  . SER   E 625 ? 1.1989 1.2435 1.2297 -0.0180 -0.0404 -0.0069 929  SER   E CB  
15907 O  OG  . SER   E 625 ? 1.1936 1.2314 1.2190 -0.0185 -0.0404 -0.0077 929  SER   E OG  
15908 N  N   . VAL   E 626 ? 1.1884 1.2501 1.2373 -0.0254 -0.0381 -0.0013 930  VAL   E N   
15909 C  CA  . VAL   E 626 ? 1.2126 1.2810 1.2664 -0.0244 -0.0383 -0.0007 930  VAL   E CA  
15910 C  C   . VAL   E 626 ? 1.2875 1.3518 1.3370 -0.0201 -0.0361 0.0007  930  VAL   E C   
15911 O  O   . VAL   E 626 ? 1.2529 1.3094 1.2962 -0.0185 -0.0338 0.0019  930  VAL   E O   
15912 C  CB  . VAL   E 626 ? 1.1055 1.1807 1.1676 -0.0293 -0.0380 0.0014  930  VAL   E CB  
15913 C  CG1 . VAL   E 626 ? 1.0589 1.1377 1.1242 -0.0328 -0.0406 -0.0003 930  VAL   E CG1 
15914 C  CG2 . VAL   E 626 ? 1.2115 1.2840 1.2750 -0.0319 -0.0347 0.0046  930  VAL   E CG2 
15915 N  N   . LEU   E 627 ? 1.3201 1.3892 1.3724 -0.0181 -0.0368 0.0007  931  LEU   E N   
15916 C  CA  . LEU   E 627 ? 1.3135 1.3785 1.3604 -0.0126 -0.0361 0.0008  931  LEU   E CA  
15917 C  C   . LEU   E 627 ? 1.2992 1.3712 1.3512 -0.0117 -0.0374 0.0006  931  LEU   E C   
15918 O  O   . LEU   E 627 ? 1.2775 1.3543 1.3328 -0.0115 -0.0406 -0.0020 931  LEU   E O   
15919 C  CB  . LEU   E 627 ? 1.2914 1.3507 1.3312 -0.0081 -0.0384 -0.0023 931  LEU   E CB  
15920 C  CG  . LEU   E 627 ? 1.3411 1.3970 1.3757 -0.0020 -0.0393 -0.0032 931  LEU   E CG  
15921 C  CD1 . LEU   E 627 ? 1.3911 1.4412 1.4207 -0.0004 -0.0352 0.0002  931  LEU   E CD1 
15922 C  CD2 . LEU   E 627 ? 1.3627 1.4127 1.3909 0.0023  -0.0421 -0.0064 931  LEU   E CD2 
15923 N  N   . LEU   E 628 ? 1.2890 1.3614 1.3417 -0.0112 -0.0348 0.0033  932  LEU   E N   
15924 C  CA  . LEU   E 628 ? 1.2170 1.2956 1.2744 -0.0104 -0.0357 0.0035  932  LEU   E CA  
15925 C  C   . LEU   E 628 ? 1.2622 1.3356 1.3127 -0.0041 -0.0358 0.0029  932  LEU   E C   
15926 O  O   . LEU   E 628 ? 1.2602 1.3261 1.3037 -0.0015 -0.0329 0.0047  932  LEU   E O   
15927 C  CB  . LEU   E 628 ? 1.1367 1.2200 1.2006 -0.0142 -0.0328 0.0068  932  LEU   E CB  
15928 C  CG  . LEU   E 628 ? 1.1406 1.2312 1.2104 -0.0143 -0.0337 0.0072  932  LEU   E CG  
15929 C  CD1 . LEU   E 628 ? 1.1841 1.2811 1.2589 -0.0164 -0.0376 0.0047  932  LEU   E CD1 
15930 C  CD2 . LEU   E 628 ? 1.1430 1.2371 1.2187 -0.0176 -0.0306 0.0107  932  LEU   E CD2 
15931 N  N   . LEU   E 629 ? 1.2821 1.3589 1.3341 -0.0017 -0.0394 0.0004  933  LEU   E N   
15932 C  CA  . LEU   E 629 ? 1.2628 1.3352 1.3089 0.0043  -0.0408 -0.0007 933  LEU   E CA  
15933 C  C   . LEU   E 629 ? 1.2796 1.3581 1.3309 0.0044  -0.0414 -0.0002 933  LEU   E C   
15934 O  O   . LEU   E 629 ? 1.2520 1.3386 1.3116 0.0002  -0.0420 0.0001  933  LEU   E O   
15935 C  CB  . LEU   E 629 ? 1.2108 1.2810 1.2543 0.0077  -0.0452 -0.0048 933  LEU   E CB  
15936 C  CG  . LEU   E 629 ? 1.1934 1.2581 1.2322 0.0081  -0.0456 -0.0062 933  LEU   E CG  
15937 C  CD1 . LEU   E 629 ? 1.2067 1.2723 1.2466 0.0106  -0.0503 -0.0104 933  LEU   E CD1 
15938 C  CD2 . LEU   E 629 ? 1.2738 1.3279 1.3020 0.0120  -0.0431 -0.0047 933  LEU   E CD2 
15939 N  N   . ALA   E 630 ? 1.3730 1.4466 1.4182 0.0096  -0.0416 -0.0001 934  ALA   E N   
15940 C  CA  . ALA   E 630 ? 1.3845 1.4621 1.4327 0.0108  -0.0422 0.0003  934  ALA   E CA  
15941 C  C   . ALA   E 630 ? 1.4398 1.5127 1.4824 0.0169  -0.0462 -0.0026 934  ALA   E C   
15942 O  O   . ALA   E 630 ? 1.4554 1.5191 1.4881 0.0218  -0.0457 -0.0027 934  ALA   E O   
15943 C  CB  . ALA   E 630 ? 1.3814 1.4573 1.4279 0.0110  -0.0373 0.0043  934  ALA   E CB  
15944 N  N   . TYR   E 631 ? 1.3894 1.4682 1.4381 0.0166  -0.0501 -0.0051 935  TYR   E N   
15945 C  CA  . TYR   E 631 ? 1.3723 1.4479 1.4177 0.0219  -0.0545 -0.0081 935  TYR   E CA  
15946 C  C   . TYR   E 631 ? 1.3921 1.4646 1.4329 0.0252  -0.0528 -0.0060 935  TYR   E C   
15947 O  O   . TYR   E 631 ? 1.3729 1.4514 1.4194 0.0230  -0.0521 -0.0047 935  TYR   E O   
15948 C  CB  . TYR   E 631 ? 1.3090 1.3924 1.3639 0.0198  -0.0585 -0.0110 935  TYR   E CB  
15949 C  CG  . TYR   E 631 ? 1.3363 1.4178 1.3902 0.0246  -0.0633 -0.0141 935  TYR   E CG  
15950 C  CD1 . TYR   E 631 ? 1.3900 1.4631 1.4359 0.0304  -0.0664 -0.0165 935  TYR   E CD1 
15951 C  CD2 . TYR   E 631 ? 1.3479 1.4357 1.4090 0.0233  -0.0652 -0.0148 935  TYR   E CD2 
15952 C  CE1 . TYR   E 631 ? 1.4500 1.5211 1.4954 0.0348  -0.0715 -0.0196 935  TYR   E CE1 
15953 C  CE2 . TYR   E 631 ? 1.3146 1.4005 1.3754 0.0274  -0.0699 -0.0177 935  TYR   E CE2 
15954 C  CZ  . TYR   E 631 ? 1.3876 1.4652 1.4408 0.0332  -0.0732 -0.0202 935  TYR   E CZ  
15955 O  OH  . TYR   E 631 ? 1.3696 1.4450 1.4227 0.0374  -0.0785 -0.0234 935  TYR   E OH  
15956 N  N   . LYS   E 632 ? 1.3994 1.4618 1.4290 0.0307  -0.0520 -0.0056 936  LYS   E N   
15957 C  CA  . LYS   E 632 ? 1.4018 1.4600 1.4256 0.0345  -0.0504 -0.0038 936  LYS   E CA  
15958 C  C   . LYS   E 632 ? 1.4749 1.5333 1.4993 0.0381  -0.0562 -0.0073 936  LYS   E C   
15959 O  O   . LYS   E 632 ? 1.5427 1.5950 1.5615 0.0426  -0.0606 -0.0105 936  LYS   E O   
15960 C  CB  . LYS   E 632 ? 1.4272 1.4734 1.4377 0.0396  -0.0473 -0.0022 936  LYS   E CB  
15961 C  CG  . LYS   E 632 ? 1.3886 1.4330 1.3980 0.0365  -0.0425 0.0003  936  LYS   E CG  
15962 C  CD  . LYS   E 632 ? 1.3610 1.4128 1.3788 0.0305  -0.0373 0.0042  936  LYS   E CD  
15963 C  CE  . LYS   E 632 ? 1.3939 1.4395 1.4051 0.0327  -0.0311 0.0082  936  LYS   E CE  
15964 N  NZ  . LYS   E 632 ? 1.4425 1.4946 1.4622 0.0267  -0.0258 0.0119  936  LYS   E NZ  
15965 N  N   . PRO   E 633 ? 1.4712 1.5365 1.5026 0.0362  -0.0569 -0.0069 937  PRO   E N   
15966 C  CA  . PRO   E 633 ? 1.4792 1.5455 1.5129 0.0388  -0.0628 -0.0105 937  PRO   E CA  
15967 C  C   . PRO   E 633 ? 1.5997 1.6550 1.6214 0.0464  -0.0653 -0.0118 937  PRO   E C   
15968 O  O   . PRO   E 633 ? 1.5859 1.6371 1.6051 0.0500  -0.0707 -0.0157 937  PRO   E O   
15969 C  CB  . PRO   E 633 ? 1.2893 1.3637 1.3309 0.0354  -0.0616 -0.0088 937  PRO   E CB  
15970 C  CG  . PRO   E 633 ? 1.2744 1.3531 1.3192 0.0307  -0.0556 -0.0048 937  PRO   E CG  
15971 C  CD  . PRO   E 633 ? 1.3887 1.4597 1.4249 0.0325  -0.0522 -0.0031 937  PRO   E CD  
15972 N  N   . MET   E 634 ? 1.5624 1.6127 1.5766 0.0491  -0.0612 -0.0087 938  MET   E N   
15973 C  CA  . MET   E 634 ? 1.5928 1.6314 1.5937 0.0568  -0.0627 -0.0094 938  MET   E CA  
15974 C  C   . MET   E 634 ? 1.5829 1.6123 1.5750 0.0610  -0.0655 -0.0118 938  MET   E C   
15975 O  O   . MET   E 634 ? 1.6228 1.6478 1.6118 0.0654  -0.0720 -0.0158 938  MET   E O   
15976 C  CB  . MET   E 634 ? 1.5962 1.6304 1.5901 0.0582  -0.0558 -0.0047 938  MET   E CB  
15977 N  N   . GLU   E 635 ? 1.6003 1.6269 1.5887 0.0596  -0.0609 -0.0096 939  GLU   E N   
15978 C  CA  . GLU   E 635 ? 1.6419 1.6594 1.6215 0.0636  -0.0632 -0.0116 939  GLU   E CA  
15979 C  C   . GLU   E 635 ? 1.7008 1.7232 1.6882 0.0625  -0.0701 -0.0164 939  GLU   E C   
15980 O  O   . GLU   E 635 ? 1.6800 1.6948 1.6606 0.0679  -0.0752 -0.0198 939  GLU   E O   
15981 C  CB  . GLU   E 635 ? 1.6356 1.6507 1.6120 0.0611  -0.0568 -0.0082 939  GLU   E CB  
15982 N  N   . GLY   E 636 ? 1.9099 1.9445 1.9114 0.0559  -0.0702 -0.0167 940  GLY   E N   
15983 C  CA  . GLY   E 636 ? 1.8843 1.9239 1.8942 0.0546  -0.0758 -0.0209 940  GLY   E CA  
15984 C  C   . GLY   E 636 ? 1.8984 1.9367 1.9078 0.0534  -0.0752 -0.0217 940  GLY   E C   
15985 O  O   . GLY   E 636 ? 1.9044 1.9420 1.9157 0.0553  -0.0805 -0.0256 940  GLY   E O   
15986 N  N   . ASN   E 637 ? 1.6067 1.6442 1.6134 0.0503  -0.0691 -0.0180 941  ASN   E N   
15987 C  CA  . ASN   E 637 ? 1.4973 1.5343 1.5042 0.0483  -0.0682 -0.0184 941  ASN   E CA  
15988 C  C   . ASN   E 637 ? 1.4838 1.5265 1.4956 0.0418  -0.0618 -0.0143 941  ASN   E C   
15989 O  O   . ASN   E 637 ? 1.5005 1.5442 1.5120 0.0404  -0.0577 -0.0110 941  ASN   E O   
15990 C  CB  . ASN   E 637 ? 1.5126 1.5364 1.5052 0.0544  -0.0684 -0.0187 941  ASN   E CB  
15991 C  CG  . ASN   E 637 ? 1.5273 1.5498 1.5197 0.0529  -0.0681 -0.0196 941  ASN   E CG  
15992 O  OD1 . ASN   E 637 ? 1.4624 1.4822 1.4510 0.0506  -0.0628 -0.0164 941  ASN   E OD1 
15993 N  ND2 . ASN   E 637 ? 1.5086 1.5331 1.5054 0.0541  -0.0737 -0.0239 941  ASN   E ND2 
15994 N  N   . PHE   E 638 ? 1.4716 1.5176 1.4880 0.0379  -0.0613 -0.0149 942  PHE   E N   
15995 C  CA  . PHE   E 638 ? 1.4170 1.4675 1.4375 0.0318  -0.0560 -0.0114 942  PHE   E CA  
15996 C  C   . PHE   E 638 ? 1.3977 1.4392 1.4081 0.0335  -0.0509 -0.0081 942  PHE   E C   
15997 O  O   . PHE   E 638 ? 1.3790 1.4106 1.3792 0.0383  -0.0517 -0.0090 942  PHE   E O   
15998 C  CB  . PHE   E 638 ? 1.3594 1.4145 1.3862 0.0279  -0.0570 -0.0131 942  PHE   E CB  
15999 C  CG  . PHE   E 638 ? 1.2468 1.3095 1.2830 0.0267  -0.0616 -0.0166 942  PHE   E CG  
16000 C  CD1 . PHE   E 638 ? 1.2533 1.3257 1.2996 0.0218  -0.0609 -0.0159 942  PHE   E CD1 
16001 C  CD2 . PHE   E 638 ? 1.2690 1.3289 1.3041 0.0307  -0.0664 -0.0206 942  PHE   E CD2 
16002 C  CE1 . PHE   E 638 ? 1.2794 1.3583 1.3343 0.0207  -0.0645 -0.0189 942  PHE   E CE1 
16003 C  CE2 . PHE   E 638 ? 1.2961 1.3631 1.3409 0.0295  -0.0701 -0.0238 942  PHE   E CE2 
16004 C  CZ  . PHE   E 638 ? 1.2703 1.3468 1.3250 0.0244  -0.0689 -0.0228 942  PHE   E CZ  
16005 N  N   . GLU   E 639 ? 1.3383 1.3830 1.3518 0.0294  -0.0457 -0.0041 943  GLU   E N   
16006 C  CA  . GLU   E 639 ? 1.3165 1.3539 1.3227 0.0298  -0.0400 -0.0005 943  GLU   E CA  
16007 C  C   . GLU   E 639 ? 1.3379 1.3807 1.3513 0.0230  -0.0365 0.0017  943  GLU   E C   
16008 O  O   . GLU   E 639 ? 1.3664 1.4187 1.3899 0.0181  -0.0360 0.0027  943  GLU   E O   
16009 C  CB  . GLU   E 639 ? 1.3219 1.3573 1.3250 0.0319  -0.0363 0.0026  943  GLU   E CB  
16010 N  N   . GLU   E 640 ? 1.3225 1.3587 1.3304 0.0228  -0.0344 0.0024  944  GLU   E N   
16011 C  CA  . GLU   E 640 ? 1.3123 1.3524 1.3263 0.0165  -0.0315 0.0042  944  GLU   E CA  
16012 C  C   . GLU   E 640 ? 1.2913 1.3337 1.3093 0.0134  -0.0259 0.0086  944  GLU   E C   
16013 O  O   . GLU   E 640 ? 1.3090 1.3453 1.3206 0.0168  -0.0222 0.0110  944  GLU   E O   
16014 C  CB  . GLU   E 640 ? 1.3146 1.3459 1.3209 0.0175  -0.0304 0.0040  944  GLU   E CB  
16015 C  CG  . GLU   E 640 ? 1.3729 1.4086 1.3860 0.0110  -0.0293 0.0046  944  GLU   E CG  
16016 C  CD  . GLU   E 640 ? 1.4380 1.4654 1.4453 0.0102  -0.0249 0.0071  944  GLU   E CD  
16017 O  OE1 . GLU   E 640 ? 1.4178 1.4444 1.4265 0.0081  -0.0197 0.0108  944  GLU   E OE1 
16018 O  OE2 . GLU   E 640 ? 1.4374 1.4592 1.4392 0.0114  -0.0265 0.0052  944  GLU   E OE2 
16019 N  N   . ILE   E 641 ? 1.2828 1.3339 1.3113 0.0070  -0.0253 0.0096  945  ILE   E N   
16020 C  CA  . ILE   E 641 ? 1.2531 1.3081 1.2877 0.0036  -0.0207 0.0134  945  ILE   E CA  
16021 C  C   . ILE   E 641 ? 1.3884 1.4409 1.4245 -0.0006 -0.0171 0.0155  945  ILE   E C   
16022 O  O   . ILE   E 641 ? 1.4553 1.5025 1.4885 0.0000  -0.0118 0.0187  945  ILE   E O   
16023 C  CB  . ILE   E 641 ? 1.2388 1.3053 1.2847 -0.0004 -0.0230 0.0130  945  ILE   E CB  
16024 C  CG1 . ILE   E 641 ? 1.2803 1.3495 1.3256 0.0030  -0.0277 0.0100  945  ILE   E CG1 
16025 C  CG2 . ILE   E 641 ? 1.3031 1.3731 1.3545 -0.0023 -0.0186 0.0167  945  ILE   E CG2 
16026 C  CD1 . ILE   E 641 ? 1.3060 1.3859 1.3617 -0.0009 -0.0301 0.0094  945  ILE   E CD1 
16027 N  N   . ALA   E 642 ? 1.3941 1.4504 1.4349 -0.0048 -0.0199 0.0137  946  ALA   E N   
16028 C  CA  . ALA   E 642 ? 1.3839 1.4385 1.4270 -0.0093 -0.0174 0.0153  946  ALA   E CA  
16029 C  C   . ALA   E 642 ? 1.3532 1.4083 1.3960 -0.0111 -0.0216 0.0121  946  ALA   E C   
16030 O  O   . ALA   E 642 ? 1.3124 1.3698 1.3543 -0.0091 -0.0260 0.0089  946  ALA   E O   
16031 C  CB  . ALA   E 642 ? 1.3667 1.4291 1.4210 -0.0148 -0.0153 0.0180  946  ALA   E CB  
16032 N  N   . ARG   E 643 ? 1.3924 1.4452 1.4364 -0.0150 -0.0201 0.0131  947  ARG   E N   
16033 C  CA  . ARG   E 643 ? 1.3533 1.4060 1.3971 -0.0172 -0.0235 0.0104  947  ARG   E CA  
16034 C  C   . ARG   E 643 ? 1.3657 1.4171 1.4132 -0.0225 -0.0214 0.0123  947  ARG   E C   
16035 O  O   . ARG   E 643 ? 1.3947 1.4444 1.4443 -0.0241 -0.0170 0.0155  947  ARG   E O   
16036 C  CB  . ARG   E 643 ? 1.3139 1.3584 1.3472 -0.0121 -0.0250 0.0080  947  ARG   E CB  
16037 C  CG  . ARG   E 643 ? 1.3450 1.3790 1.3693 -0.0087 -0.0209 0.0101  947  ARG   E CG  
16038 C  CD  . ARG   E 643 ? 1.4041 1.4297 1.4184 -0.0047 -0.0228 0.0076  947  ARG   E CD  
16039 N  NE  . ARG   E 643 ? 1.4110 1.4387 1.4235 -0.0004 -0.0275 0.0041  947  ARG   E NE  
16040 C  CZ  . ARG   E 643 ? 1.4313 1.4534 1.4367 0.0037  -0.0303 0.0012  947  ARG   E CZ  
16041 N  NH1 . ARG   E 643 ? 1.4479 1.4613 1.4462 0.0044  -0.0291 0.0013  947  ARG   E NH1 
16042 N  NH2 . ARG   E 643 ? 1.4424 1.4676 1.4483 0.0072  -0.0347 -0.0020 947  ARG   E NH2 
16043 N  N   . ASP   E 644 ? 1.3148 1.3670 1.3632 -0.0253 -0.0244 0.0101  948  ASP   E N   
16044 C  CA  . ASP   E 644 ? 1.3057 1.3549 1.3557 -0.0298 -0.0233 0.0111  948  ASP   E CA  
16045 C  C   . ASP   E 644 ? 1.3078 1.3540 1.3531 -0.0296 -0.0267 0.0079  948  ASP   E C   
16046 O  O   . ASP   E 644 ? 1.2848 1.3361 1.3320 -0.0295 -0.0304 0.0053  948  ASP   E O   
16047 C  CB  . ASP   E 644 ? 1.3267 1.3836 1.3878 -0.0357 -0.0237 0.0126  948  ASP   E CB  
16048 C  CG  . ASP   E 644 ? 1.3677 1.4211 1.4310 -0.0405 -0.0229 0.0135  948  ASP   E CG  
16049 O  OD1 . ASP   E 644 ? 1.3786 1.4248 1.4386 -0.0402 -0.0189 0.0156  948  ASP   E OD1 
16050 O  OD2 . ASP   E 644 ? 1.3723 1.4298 1.4407 -0.0446 -0.0262 0.0123  948  ASP   E OD2 
16051 N  N   . PHE   E 645 ? 1.3478 1.3851 1.3866 -0.0294 -0.0252 0.0082  949  PHE   E N   
16052 C  CA  . PHE   E 645 ? 1.3457 1.3789 1.3797 -0.0293 -0.0279 0.0054  949  PHE   E CA  
16053 C  C   . PHE   E 645 ? 1.3005 1.3320 1.3378 -0.0350 -0.0275 0.0064  949  PHE   E C   
16054 O  O   . PHE   E 645 ? 1.3028 1.3282 1.3386 -0.0362 -0.0240 0.0088  949  PHE   E O   
16055 C  CB  . PHE   E 645 ? 1.3499 1.3734 1.3728 -0.0239 -0.0270 0.0045  949  PHE   E CB  
16056 C  CG  . PHE   E 645 ? 1.3665 1.3910 1.3857 -0.0181 -0.0286 0.0027  949  PHE   E CG  
16057 C  CD1 . PHE   E 645 ? 1.3346 1.3683 1.3602 -0.0181 -0.0313 0.0013  949  PHE   E CD1 
16058 C  CD2 . PHE   E 645 ? 1.4021 1.4178 1.4113 -0.0125 -0.0277 0.0023  949  PHE   E CD2 
16059 C  CE1 . PHE   E 645 ? 1.3485 1.3831 1.3714 -0.0129 -0.0331 -0.0005 949  PHE   E CE1 
16060 C  CE2 . PHE   E 645 ? 1.3859 1.4023 1.3920 -0.0069 -0.0299 0.0004  949  PHE   E CE2 
16061 C  CZ  . PHE   E 645 ? 1.3378 1.3638 1.3512 -0.0073 -0.0326 -0.0011 949  PHE   E CZ  
16062 N  N   . ASN   E 646 ? 1.2525 1.2889 1.2941 -0.0383 -0.0310 0.0046  950  ASN   E N   
16063 C  CA  . ASN   E 646 ? 1.2013 1.2354 1.2451 -0.0433 -0.0318 0.0048  950  ASN   E CA  
16064 C  C   . ASN   E 646 ? 1.1419 1.1751 1.1815 -0.0427 -0.0356 0.0013  950  ASN   E C   
16065 O  O   . ASN   E 646 ? 1.1356 1.1752 1.1792 -0.0441 -0.0385 -0.0002 950  ASN   E O   
16066 C  CB  . ASN   E 646 ? 1.2144 1.2556 1.2687 -0.0485 -0.0324 0.0064  950  ASN   E CB  
16067 C  CG  . ASN   E 646 ? 1.2358 1.2734 1.2924 -0.0534 -0.0329 0.0070  950  ASN   E CG  
16068 O  OD1 . ASN   E 646 ? 1.2921 1.3288 1.3473 -0.0553 -0.0364 0.0048  950  ASN   E OD1 
16069 N  ND2 . ASN   E 646 ? 1.2534 1.2882 1.3134 -0.0555 -0.0293 0.0099  950  ASN   E ND2 
16070 N  N   . PRO   E 647 ? 1.1253 1.1501 1.1566 -0.0406 -0.0354 0.0001  951  PRO   E N   
16071 C  CA  . PRO   E 647 ? 1.1240 1.1478 1.1504 -0.0382 -0.0383 -0.0034 951  PRO   E CA  
16072 C  C   . PRO   E 647 ? 1.1296 1.1555 1.1588 -0.0425 -0.0412 -0.0046 951  PRO   E C   
16073 O  O   . PRO   E 647 ? 1.1543 1.1760 1.1837 -0.0463 -0.0413 -0.0039 951  PRO   E O   
16074 C  CB  . PRO   E 647 ? 1.0659 1.0794 1.0829 -0.0352 -0.0370 -0.0039 951  PRO   E CB  
16075 C  CG  . PRO   E 647 ? 1.1266 1.1354 1.1434 -0.0362 -0.0332 -0.0005 951  PRO   E CG  
16076 C  CD  . PRO   E 647 ? 1.1260 1.1416 1.1527 -0.0410 -0.0325 0.0018  951  PRO   E CD  
16077 N  N   . ASN   E 648 ? 1.0426 1.0743 1.0736 -0.0416 -0.0435 -0.0067 952  ASN   E N   
16078 C  CA  . ASN   E 648 ? 1.0391 1.0730 1.0720 -0.0449 -0.0462 -0.0080 952  ASN   E CA  
16079 C  C   . ASN   E 648 ? 1.0444 1.0843 1.0784 -0.0423 -0.0475 -0.0101 952  ASN   E C   
16080 O  O   . ASN   E 648 ? 1.0847 1.1297 1.1217 -0.0400 -0.0467 -0.0097 952  ASN   E O   
16081 C  CB  . ASN   E 648 ? 1.0726 1.1105 1.1130 -0.0500 -0.0469 -0.0059 952  ASN   E CB  
16082 C  CG  . ASN   E 648 ? 1.0800 1.1193 1.1213 -0.0531 -0.0502 -0.0074 952  ASN   E CG  
16083 O  OD1 . ASN   E 648 ? 1.1006 1.1466 1.1474 -0.0547 -0.0515 -0.0070 952  ASN   E OD1 
16084 N  ND2 . ASN   E 648 ? 1.1345 1.1669 1.1697 -0.0537 -0.0515 -0.0090 952  ASN   E ND2 
16085 N  N   . TRP   E 649 ? 1.0300 1.0689 1.0612 -0.0427 -0.0494 -0.0123 953  TRP   E N   
16086 C  CA  . TRP   E 649 ? 1.0078 1.0518 1.0402 -0.0402 -0.0500 -0.0142 953  TRP   E CA  
16087 C  C   . TRP   E 649 ? 1.0155 1.0678 1.0552 -0.0421 -0.0505 -0.0129 953  TRP   E C   
16088 O  O   . TRP   E 649 ? 1.0425 1.0960 1.0851 -0.0462 -0.0516 -0.0116 953  TRP   E O   
16089 C  CB  . TRP   E 649 ? 1.0392 1.0797 1.0668 -0.0404 -0.0513 -0.0165 953  TRP   E CB  
16090 C  CG  . TRP   E 649 ? 0.9848 1.0168 1.0049 -0.0384 -0.0510 -0.0179 953  TRP   E CG  
16091 C  CD1 . TRP   E 649 ? 1.0553 1.0805 1.0701 -0.0404 -0.0521 -0.0186 953  TRP   E CD1 
16092 C  CD2 . TRP   E 649 ? 0.9891 1.0180 1.0057 -0.0338 -0.0498 -0.0189 953  TRP   E CD2 
16093 N  NE1 . TRP   E 649 ? 1.0394 1.0577 1.0478 -0.0375 -0.0514 -0.0199 953  TRP   E NE1 
16094 C  CE2 . TRP   E 649 ? 0.9829 1.0034 0.9924 -0.0333 -0.0500 -0.0201 953  TRP   E CE2 
16095 C  CE3 . TRP   E 649 ? 1.0689 1.1011 1.0876 -0.0299 -0.0489 -0.0191 953  TRP   E CE3 
16096 C  CZ2 . TRP   E 649 ? 1.0334 1.0488 1.0378 -0.0291 -0.0493 -0.0213 953  TRP   E CZ2 
16097 C  CZ3 . TRP   E 649 ? 1.0125 1.0394 1.0260 -0.0256 -0.0485 -0.0205 953  TRP   E CZ3 
16098 C  CH2 . TRP   E 649 ? 0.9994 1.0181 1.0059 -0.0252 -0.0487 -0.0215 953  TRP   E CH2 
16099 N  N   . MET   E 650 ? 0.9846 1.0424 1.0273 -0.0392 -0.0499 -0.0134 954  MET   E N   
16100 C  CA  . MET   E 650 ? 0.9819 1.0475 1.0312 -0.0403 -0.0501 -0.0122 954  MET   E CA  
16101 C  C   . MET   E 650 ? 0.9749 1.0448 1.0256 -0.0381 -0.0504 -0.0142 954  MET   E C   
16102 O  O   . MET   E 650 ? 1.0006 1.0710 1.0509 -0.0342 -0.0498 -0.0156 954  MET   E O   
16103 C  CB  . MET   E 650 ? 0.9756 1.0436 1.0282 -0.0390 -0.0487 -0.0103 954  MET   E CB  
16104 C  CG  . MET   E 650 ? 0.9126 0.9883 0.9718 -0.0401 -0.0489 -0.0090 954  MET   E CG  
16105 S  SD  . MET   E 650 ? 0.9742 1.0518 1.0358 -0.0374 -0.0470 -0.0071 954  MET   E SD  
16106 C  CE  . MET   E 650 ? 1.0278 1.1031 1.0850 -0.0317 -0.0470 -0.0097 954  MET   E CE  
16107 N  N   . SER   E 651 ? 0.9980 1.0709 1.0505 -0.0404 -0.0514 -0.0144 955  SER   E N   
16108 C  CA  . SER   E 651 ? 0.9777 1.0533 1.0307 -0.0387 -0.0512 -0.0162 955  SER   E CA  
16109 C  C   . SER   E 651 ? 0.9374 1.0204 0.9966 -0.0381 -0.0510 -0.0157 955  SER   E C   
16110 O  O   . SER   E 651 ? 0.9332 1.0187 0.9938 -0.0363 -0.0504 -0.0172 955  SER   E O   
16111 C  CB  . SER   E 651 ? 0.9964 1.0693 1.0458 -0.0411 -0.0521 -0.0169 955  SER   E CB  
16112 O  OG  . SER   E 651 ? 1.0077 1.0826 1.0594 -0.0447 -0.0537 -0.0152 955  SER   E OG  
16113 N  N   . ALA   E 652 ? 0.9023 0.9887 0.9655 -0.0397 -0.0513 -0.0135 956  ALA   E N   
16114 C  CA  . ALA   E 652 ? 0.8908 0.9839 0.9595 -0.0393 -0.0512 -0.0128 956  ALA   E CA  
16115 C  C   . ALA   E 652 ? 0.8587 0.9542 0.9310 -0.0408 -0.0513 -0.0103 956  ALA   E C   
16116 O  O   . ALA   E 652 ? 0.8871 0.9805 0.9589 -0.0436 -0.0519 -0.0089 956  ALA   E O   
16117 C  CB  . ALA   E 652 ? 0.9505 1.0456 1.0197 -0.0413 -0.0519 -0.0131 956  ALA   E CB  
16118 N  N   . VAL   E 653 ? 0.8903 0.9902 0.9664 -0.0388 -0.0508 -0.0097 957  VAL   E N   
16119 C  CA  . VAL   E 653 ? 0.9468 1.0489 1.0262 -0.0393 -0.0503 -0.0073 957  VAL   E CA  
16120 C  C   . VAL   E 653 ? 0.9078 1.0162 0.9920 -0.0385 -0.0505 -0.0069 957  VAL   E C   
16121 O  O   . VAL   E 653 ? 0.9051 1.0156 0.9902 -0.0370 -0.0508 -0.0086 957  VAL   E O   
16122 C  CB  . VAL   E 653 ? 0.9264 1.0247 1.0031 -0.0364 -0.0489 -0.0070 957  VAL   E CB  
16123 C  CG1 . VAL   E 653 ? 0.9014 1.0012 0.9783 -0.0320 -0.0488 -0.0085 957  VAL   E CG1 
16124 C  CG2 . VAL   E 653 ? 0.8793 0.9780 0.9583 -0.0380 -0.0477 -0.0041 957  VAL   E CG2 
16125 N  N   . GLU   E 654 ? 0.8762 0.9874 0.9640 -0.0396 -0.0502 -0.0046 958  GLU   E N   
16126 C  CA  . GLU   E 654 ? 0.9557 1.0727 1.0482 -0.0393 -0.0505 -0.0039 958  GLU   E CA  
16127 C  C   . GLU   E 654 ? 0.9502 1.0689 1.0457 -0.0395 -0.0494 -0.0013 958  GLU   E C   
16128 O  O   . GLU   E 654 ? 0.9394 1.0566 1.0355 -0.0418 -0.0489 0.0003  958  GLU   E O   
16129 C  CB  . GLU   E 654 ? 1.0216 1.1411 1.1157 -0.0423 -0.0520 -0.0040 958  GLU   E CB  
16130 C  CG  . GLU   E 654 ? 0.9696 1.0947 1.0681 -0.0423 -0.0525 -0.0031 958  GLU   E CG  
16131 C  CD  . GLU   E 654 ? 0.9838 1.1107 1.0830 -0.0393 -0.0521 -0.0047 958  GLU   E CD  
16132 O  OE1 . GLU   E 654 ? 1.0017 1.1287 1.1001 -0.0396 -0.0524 -0.0062 958  GLU   E OE1 
16133 O  OE2 . GLU   E 654 ? 0.9564 1.0841 1.0566 -0.0367 -0.0515 -0.0045 958  GLU   E OE2 
16134 N  N   . ILE   E 655 ? 0.9765 1.0985 1.0743 -0.0371 -0.0490 -0.0008 959  ILE   E N   
16135 C  CA  . ILE   E 655 ? 1.0319 1.1560 1.1328 -0.0370 -0.0477 0.0017  959  ILE   E CA  
16136 C  C   . ILE   E 655 ? 1.0073 1.1363 1.1134 -0.0402 -0.0489 0.0030  959  ILE   E C   
16137 O  O   . ILE   E 655 ? 0.9697 1.1015 1.0768 -0.0407 -0.0505 0.0019  959  ILE   E O   
16138 C  CB  . ILE   E 655 ? 1.0441 1.1689 1.1444 -0.0328 -0.0471 0.0015  959  ILE   E CB  
16139 C  CG1 . ILE   E 655 ? 1.0144 1.1341 1.1094 -0.0292 -0.0469 -0.0004 959  ILE   E CG1 
16140 C  CG2 . ILE   E 655 ? 0.9998 1.1259 1.1024 -0.0322 -0.0452 0.0042  959  ILE   E CG2 
16141 C  CD1 . ILE   E 655 ? 0.9811 1.1009 1.0752 -0.0249 -0.0471 -0.0010 959  ILE   E CD1 
16142 N  N   . LEU   E 656 ? 1.0420 1.1719 1.1514 -0.0424 -0.0481 0.0053  960  LEU   E N   
16143 C  CA  . LEU   E 656 ? 1.0469 1.1816 1.1619 -0.0452 -0.0495 0.0066  960  LEU   E CA  
16144 C  C   . LEU   E 656 ? 1.1390 1.2780 1.2580 -0.0435 -0.0485 0.0083  960  LEU   E C   
16145 O  O   . LEU   E 656 ? 1.1078 1.2509 1.2296 -0.0440 -0.0500 0.0083  960  LEU   E O   
16146 C  CB  . LEU   E 656 ? 1.0045 1.1383 1.1225 -0.0488 -0.0497 0.0080  960  LEU   E CB  
16147 C  CG  . LEU   E 656 ? 0.9769 1.1079 1.0927 -0.0517 -0.0521 0.0065  960  LEU   E CG  
16148 C  CD1 . LEU   E 656 ? 0.9930 1.1230 1.1127 -0.0551 -0.0523 0.0080  960  LEU   E CD1 
16149 C  CD2 . LEU   E 656 ? 0.9682 1.1018 1.0841 -0.0527 -0.0550 0.0054  960  LEU   E CD2 
16150 N  N   . ASP   E 657 ? 1.2240 1.3614 1.3427 -0.0414 -0.0457 0.0097  961  ASP   E N   
16151 C  CA  . ASP   E 657 ? 1.2202 1.3603 1.3413 -0.0389 -0.0440 0.0114  961  ASP   E CA  
16152 C  C   . ASP   E 657 ? 1.2557 1.3908 1.3724 -0.0358 -0.0408 0.0121  961  ASP   E C   
16153 O  O   . ASP   E 657 ? 1.2572 1.3873 1.3695 -0.0357 -0.0403 0.0113  961  ASP   E O   
16154 C  CB  . ASP   E 657 ? 1.2213 1.3662 1.3498 -0.0414 -0.0438 0.0138  961  ASP   E CB  
16155 C  CG  . ASP   E 657 ? 1.2839 1.4273 1.4155 -0.0432 -0.0412 0.0159  961  ASP   E CG  
16156 O  OD1 . ASP   E 657 ? 1.3281 1.4691 1.4585 -0.0407 -0.0375 0.0175  961  ASP   E OD1 
16157 O  OD2 . ASP   E 657 ? 1.3060 1.4502 1.4414 -0.0470 -0.0427 0.0161  961  ASP   E OD2 
16158 N  N   . ASP   E 658 ? 1.3240 1.4599 1.4413 -0.0329 -0.0387 0.0137  962  ASP   E N   
16159 C  CA  . ASP   E 658 ? 1.3240 1.4543 1.4357 -0.0291 -0.0357 0.0144  962  ASP   E CA  
16160 C  C   . ASP   E 658 ? 1.3336 1.4595 1.4443 -0.0306 -0.0329 0.0158  962  ASP   E C   
16161 O  O   . ASP   E 658 ? 1.3243 1.4437 1.4283 -0.0275 -0.0309 0.0158  962  ASP   E O   
16162 C  CB  . ASP   E 658 ? 1.3747 1.5068 1.4881 -0.0264 -0.0334 0.0165  962  ASP   E CB  
16163 C  CG  . ASP   E 658 ? 1.4621 1.5966 1.5745 -0.0238 -0.0358 0.0149  962  ASP   E CG  
16164 O  OD1 . ASP   E 658 ? 1.5198 1.6504 1.6262 -0.0205 -0.0371 0.0128  962  ASP   E OD1 
16165 O  OD2 . ASP   E 658 ? 1.5096 1.6496 1.6274 -0.0249 -0.0366 0.0158  962  ASP   E OD2 
16166 N  N   . ASP   E 659 ? 1.3624 1.4911 1.4795 -0.0351 -0.0329 0.0171  963  ASP   E N   
16167 C  CA  . ASP   E 659 ? 1.3754 1.5002 1.4928 -0.0368 -0.0300 0.0188  963  ASP   E CA  
16168 C  C   . ASP   E 659 ? 1.3444 1.4674 1.4616 -0.0405 -0.0323 0.0173  963  ASP   E C   
16169 O  O   . ASP   E 659 ? 1.3852 1.5025 1.4990 -0.0408 -0.0304 0.0176  963  ASP   E O   
16170 C  CB  . ASP   E 659 ? 1.3919 1.5206 1.5180 -0.0389 -0.0272 0.0220  963  ASP   E CB  
16171 C  CG  . ASP   E 659 ? 1.4258 1.5556 1.5517 -0.0350 -0.0244 0.0237  963  ASP   E CG  
16172 O  OD1 . ASP   E 659 ? 1.4153 1.5513 1.5461 -0.0352 -0.0261 0.0238  963  ASP   E OD1 
16173 O  OD2 . ASP   E 659 ? 1.4187 1.5427 1.5388 -0.0315 -0.0205 0.0249  963  ASP   E OD2 
16174 N  N   . ASN   E 660 ? 1.2374 1.3644 1.3574 -0.0432 -0.0363 0.0157  964  ASN   E N   
16175 C  CA  . ASN   E 660 ? 1.1547 1.2797 1.2741 -0.0466 -0.0386 0.0143  964  ASN   E CA  
16176 C  C   . ASN   E 660 ? 1.1350 1.2580 1.2480 -0.0451 -0.0412 0.0112  964  ASN   E C   
16177 O  O   . ASN   E 660 ? 1.1446 1.2708 1.2572 -0.0433 -0.0428 0.0100  964  ASN   E O   
16178 C  CB  . ASN   E 660 ? 1.1294 1.2594 1.2567 -0.0510 -0.0412 0.0148  964  ASN   E CB  
16179 C  CG  . ASN   E 660 ? 1.1893 1.3228 1.3249 -0.0522 -0.0386 0.0178  964  ASN   E CG  
16180 O  OD1 . ASN   E 660 ? 1.2329 1.3637 1.3709 -0.0539 -0.0362 0.0194  964  ASN   E OD1 
16181 N  ND2 . ASN   E 660 ? 1.2709 1.4100 1.4111 -0.0514 -0.0390 0.0187  964  ASN   E ND2 
16182 N  N   . PHE   E 661 ? 1.0971 1.2146 1.2052 -0.0456 -0.0415 0.0098  965  PHE   E N   
16183 C  CA  . PHE   E 661 ? 1.0545 1.1696 1.1567 -0.0442 -0.0436 0.0069  965  PHE   E CA  
16184 C  C   . PHE   E 661 ? 1.0250 1.1379 1.1264 -0.0478 -0.0458 0.0058  965  PHE   E C   
16185 O  O   . PHE   E 661 ? 1.0708 1.1805 1.1728 -0.0500 -0.0450 0.0068  965  PHE   E O   
16186 C  CB  . PHE   E 661 ? 1.0520 1.1612 1.1473 -0.0402 -0.0418 0.0060  965  PHE   E CB  
16187 C  CG  . PHE   E 661 ? 1.0837 1.1929 1.1785 -0.0368 -0.0393 0.0076  965  PHE   E CG  
16188 C  CD1 . PHE   E 661 ? 1.0524 1.1640 1.1465 -0.0335 -0.0402 0.0065  965  PHE   E CD1 
16189 C  CD2 . PHE   E 661 ? 1.1236 1.2299 1.2187 -0.0368 -0.0359 0.0102  965  PHE   E CD2 
16190 C  CE1 . PHE   E 661 ? 1.0827 1.1935 1.1755 -0.0300 -0.0382 0.0078  965  PHE   E CE1 
16191 C  CE2 . PHE   E 661 ? 1.1436 1.2490 1.2372 -0.0332 -0.0333 0.0117  965  PHE   E CE2 
16192 C  CZ  . PHE   E 661 ? 1.1168 1.2243 1.2089 -0.0297 -0.0346 0.0104  965  PHE   E CZ  
16193 N  N   . LEU   E 662 ? 0.9771 1.0914 1.0771 -0.0482 -0.0484 0.0037  966  LEU   E N   
16194 C  CA  . LEU   E 662 ? 0.9449 1.0568 1.0432 -0.0512 -0.0507 0.0024  966  LEU   E CA  
16195 C  C   . LEU   E 662 ? 0.9592 1.0663 1.0505 -0.0492 -0.0508 -0.0001 966  LEU   E C   
16196 O  O   . LEU   E 662 ? 0.9598 1.0679 1.0493 -0.0461 -0.0505 -0.0014 966  LEU   E O   
16197 C  CB  . LEU   E 662 ? 0.9464 1.0626 1.0476 -0.0531 -0.0535 0.0021  966  LEU   E CB  
16198 C  CG  . LEU   E 662 ? 0.8955 1.0089 0.9938 -0.0557 -0.0563 0.0006  966  LEU   E CG  
16199 C  CD1 . LEU   E 662 ? 0.9563 1.0672 1.0567 -0.0592 -0.0575 0.0015  966  LEU   E CD1 
16200 C  CD2 . LEU   E 662 ? 0.8449 0.9617 0.9442 -0.0565 -0.0586 0.0001  966  LEU   E CD2 
16201 N  N   . GLY   E 663 ? 0.9603 1.0621 1.0482 -0.0511 -0.0515 -0.0007 967  GLY   E N   
16202 C  CA  . GLY   E 663 ? 0.9348 1.0316 1.0161 -0.0493 -0.0515 -0.0030 967  GLY   E CA  
16203 C  C   . GLY   E 663 ? 0.9581 1.0507 1.0364 -0.0522 -0.0535 -0.0040 967  GLY   E C   
16204 O  O   . GLY   E 663 ? 0.9622 1.0549 1.0436 -0.0557 -0.0550 -0.0028 967  GLY   E O   
16205 N  N   . ALA   E 664 ? 0.9514 1.0400 1.0238 -0.0505 -0.0537 -0.0062 968  ALA   E N   
16206 C  CA  . ALA   E 664 ? 0.9132 0.9968 0.9810 -0.0525 -0.0555 -0.0076 968  ALA   E CA  
16207 C  C   . ALA   E 664 ? 0.9716 1.0483 1.0337 -0.0513 -0.0545 -0.0085 968  ALA   E C   
16208 O  O   . ALA   E 664 ? 0.9787 1.0543 1.0379 -0.0477 -0.0530 -0.0098 968  ALA   E O   
16209 C  CB  . ALA   E 664 ? 0.8824 0.9670 0.9476 -0.0515 -0.0563 -0.0095 968  ALA   E CB  
16210 N  N   . GLU   E 665 ? 0.9715 1.0435 1.0324 -0.0541 -0.0555 -0.0080 969  GLU   E N   
16211 C  CA  . GLU   E 665 ? 0.9952 1.0599 1.0506 -0.0533 -0.0546 -0.0086 969  GLU   E CA  
16212 C  C   . GLU   E 665 ? 1.0338 1.0927 1.0849 -0.0560 -0.0570 -0.0098 969  GLU   E C   
16213 O  O   . GLU   E 665 ? 1.0523 1.1126 1.1043 -0.0582 -0.0595 -0.0102 969  GLU   E O   
16214 C  CB  . GLU   E 665 ? 1.0341 1.0976 1.0921 -0.0538 -0.0525 -0.0064 969  GLU   E CB  
16215 C  CG  . GLU   E 665 ? 1.0727 1.1375 1.1370 -0.0583 -0.0534 -0.0042 969  GLU   E CG  
16216 C  CD  . GLU   E 665 ? 1.1664 1.2292 1.2330 -0.0585 -0.0503 -0.0018 969  GLU   E CD  
16217 O  OE1 . GLU   E 665 ? 1.1705 1.2265 1.2315 -0.0572 -0.0488 -0.0021 969  GLU   E OE1 
16218 O  OE2 . GLU   E 665 ? 1.1705 1.2383 1.2443 -0.0597 -0.0491 0.0005  969  GLU   E OE2 
16219 N  N   . ASN   E 666 ? 1.0576 1.1092 1.1033 -0.0555 -0.0565 -0.0105 970  ASN   E N   
16220 C  CA  . ASN   E 666 ? 1.0736 1.1182 1.1137 -0.0575 -0.0588 -0.0119 970  ASN   E CA  
16221 C  C   . ASN   E 666 ? 1.0755 1.1190 1.1199 -0.0623 -0.0610 -0.0104 970  ASN   E C   
16222 O  O   . ASN   E 666 ? 1.1097 1.1552 1.1600 -0.0638 -0.0596 -0.0083 970  ASN   E O   
16223 C  CB  . ASN   E 666 ? 1.0938 1.1310 1.1269 -0.0551 -0.0572 -0.0130 970  ASN   E CB  
16224 C  CG  . ASN   E 666 ? 1.1393 1.1691 1.1648 -0.0556 -0.0592 -0.0152 970  ASN   E CG  
16225 O  OD1 . ASN   E 666 ? 1.1517 1.1755 1.1753 -0.0584 -0.0607 -0.0150 970  ASN   E OD1 
16226 N  ND2 . ASN   E 666 ? 1.2082 1.2380 1.2293 -0.0528 -0.0591 -0.0172 970  ASN   E ND2 
16227 N  N   . ALA   E 667 ? 1.0613 1.1014 1.1030 -0.0647 -0.0645 -0.0117 971  ALA   E N   
16228 C  CA  . ALA   E 667 ? 1.0617 1.1000 1.0967 -0.0629 -0.0658 -0.0140 971  ALA   E CA  
16229 C  C   . ALA   E 667 ? 1.0892 1.1319 1.1276 -0.0648 -0.0686 -0.0138 971  ALA   E C   
16230 O  O   . ALA   E 667 ? 1.0745 1.1158 1.1152 -0.0684 -0.0720 -0.0134 971  ALA   E O   
16231 C  CB  . ALA   E 667 ? 1.0219 1.0507 1.0486 -0.0634 -0.0675 -0.0158 971  ALA   E CB  
16232 N  N   . PHE   E 668 ? 1.0693 1.1174 1.1082 -0.0624 -0.0672 -0.0140 972  PHE   E N   
16233 C  CA  . PHE   E 668 ? 0.9673 1.0202 1.0094 -0.0636 -0.0693 -0.0136 972  PHE   E CA  
16234 C  C   . PHE   E 668 ? 0.9640 1.0228 1.0159 -0.0663 -0.0702 -0.0113 972  PHE   E C   
16235 O  O   . PHE   E 668 ? 0.9864 1.0461 1.0414 -0.0692 -0.0737 -0.0109 972  PHE   E O   
16236 C  CB  . PHE   E 668 ? 0.9709 1.0175 1.0064 -0.0650 -0.0731 -0.0152 972  PHE   E CB  
16237 C  CG  . PHE   E 668 ? 1.0364 1.0754 1.0615 -0.0626 -0.0721 -0.0174 972  PHE   E CG  
16238 C  CD1 . PHE   E 668 ? 1.0601 1.1000 1.0811 -0.0592 -0.0695 -0.0185 972  PHE   E CD1 
16239 C  CD2 . PHE   E 668 ? 0.9945 1.0253 1.0142 -0.0637 -0.0737 -0.0184 972  PHE   E CD2 
16240 C  CE1 . PHE   E 668 ? 1.0310 1.0642 1.0431 -0.0568 -0.0683 -0.0204 972  PHE   E CE1 
16241 C  CE2 . PHE   E 668 ? 1.0100 1.0337 1.0201 -0.0612 -0.0727 -0.0205 972  PHE   E CE2 
16242 C  CZ  . PHE   E 668 ? 1.0027 1.0278 1.0092 -0.0577 -0.0699 -0.0214 972  PHE   E CZ  
16243 N  N   . ASN   E 669 ? 1.0056 1.0685 1.0626 -0.0652 -0.0669 -0.0098 973  ASN   E N   
16244 C  CA  . ASN   E 669 ? 0.9775 1.0451 1.0435 -0.0674 -0.0665 -0.0074 973  ASN   E CA  
16245 C  C   . ASN   E 669 ? 0.9803 1.0553 1.0512 -0.0650 -0.0638 -0.0060 973  ASN   E C   
16246 O  O   . ASN   E 669 ? 0.9896 1.0650 1.0572 -0.0615 -0.0612 -0.0068 973  ASN   E O   
16247 C  CB  . ASN   E 669 ? 0.9854 1.0485 1.0518 -0.0683 -0.0648 -0.0065 973  ASN   E CB  
16248 C  CG  . ASN   E 669 ? 1.0267 1.0835 1.0916 -0.0717 -0.0680 -0.0071 973  ASN   E CG  
16249 O  OD1 . ASN   E 669 ? 1.0180 1.0754 1.0848 -0.0742 -0.0719 -0.0076 973  ASN   E OD1 
16250 N  ND2 . ASN   E 669 ? 1.0914 1.1417 1.1527 -0.0718 -0.0666 -0.0073 973  ASN   E ND2 
16251 N  N   . LEU   E 670 ? 0.9644 1.0453 1.0433 -0.0669 -0.0645 -0.0042 974  LEU   E N   
16252 C  CA  . LEU   E 670 ? 0.9517 1.0393 1.0356 -0.0649 -0.0619 -0.0027 974  LEU   E CA  
16253 C  C   . LEU   E 670 ? 0.9977 1.0865 1.0876 -0.0658 -0.0595 -0.0003 974  LEU   E C   
16254 O  O   . LEU   E 670 ? 0.9898 1.0762 1.0829 -0.0690 -0.0604 0.0005  974  LEU   E O   
16255 C  CB  . LEU   E 670 ? 0.9144 1.0081 1.0030 -0.0658 -0.0641 -0.0022 974  LEU   E CB  
16256 C  CG  . LEU   E 670 ? 0.8709 0.9648 0.9548 -0.0647 -0.0659 -0.0039 974  LEU   E CG  
16257 C  CD1 . LEU   E 670 ? 0.8663 0.9665 0.9563 -0.0657 -0.0675 -0.0027 974  LEU   E CD1 
16258 C  CD2 . LEU   E 670 ? 0.8683 0.9621 0.9479 -0.0609 -0.0630 -0.0050 974  LEU   E CD2 
16259 N  N   . PHE   E 671 ? 1.0365 1.1288 1.1282 -0.0630 -0.0563 0.0009  975  PHE   E N   
16260 C  CA  . PHE   E 671 ? 1.0150 1.1083 1.1117 -0.0633 -0.0533 0.0034  975  PHE   E CA  
16261 C  C   . PHE   E 671 ? 0.9517 1.0511 1.0519 -0.0607 -0.0513 0.0046  975  PHE   E C   
16262 O  O   . PHE   E 671 ? 0.9393 1.0403 1.0361 -0.0577 -0.0514 0.0033  975  PHE   E O   
16263 C  CB  . PHE   E 671 ? 1.0259 1.1124 1.1170 -0.0616 -0.0504 0.0034  975  PHE   E CB  
16264 C  CG  . PHE   E 671 ? 1.0313 1.1167 1.1162 -0.0568 -0.0486 0.0021  975  PHE   E CG  
16265 C  CD1 . PHE   E 671 ? 1.0695 1.1570 1.1556 -0.0538 -0.0457 0.0036  975  PHE   E CD1 
16266 C  CD2 . PHE   E 671 ? 1.0520 1.1341 1.1301 -0.0551 -0.0501 -0.0005 975  PHE   E CD2 
16267 C  CE1 . PHE   E 671 ? 1.0865 1.1728 1.1672 -0.0493 -0.0448 0.0022  975  PHE   E CE1 
16268 C  CE2 . PHE   E 671 ? 1.0587 1.1402 1.1324 -0.0508 -0.0488 -0.0018 975  PHE   E CE2 
16269 C  CZ  . PHE   E 671 ? 1.0818 1.1654 1.1569 -0.0479 -0.0465 -0.0006 975  PHE   E CZ  
16270 N  N   . VAL   E 672 ? 0.9749 1.0775 1.0822 -0.0618 -0.0494 0.0072  976  VAL   E N   
16271 C  CA  . VAL   E 672 ? 1.0231 1.1305 1.1335 -0.0591 -0.0469 0.0087  976  VAL   E CA  
16272 C  C   . VAL   E 672 ? 1.0855 1.1901 1.1969 -0.0583 -0.0425 0.0111  976  VAL   E C   
16273 O  O   . VAL   E 672 ? 1.1527 1.2552 1.2679 -0.0614 -0.0417 0.0124  976  VAL   E O   
16274 C  CB  . VAL   E 672 ? 1.0371 1.1518 1.1557 -0.0610 -0.0487 0.0098  976  VAL   E CB  
16275 C  CG1 . VAL   E 672 ? 1.0629 1.1819 1.1844 -0.0581 -0.0458 0.0116  976  VAL   E CG1 
16276 C  CG2 . VAL   E 672 ? 1.0277 1.1444 1.1445 -0.0617 -0.0529 0.0077  976  VAL   E CG2 
16277 N  N   . CYS   E 673 ? 1.0927 1.1967 1.2004 -0.0540 -0.0396 0.0115  977  CYS   E N   
16278 C  CA  . CYS   E 673 ? 1.1698 1.2704 1.2769 -0.0524 -0.0350 0.0139  977  CYS   E CA  
16279 C  C   . CYS   E 673 ? 1.1757 1.2804 1.2846 -0.0492 -0.0329 0.0153  977  CYS   E C   
16280 O  O   . CYS   E 673 ? 1.1736 1.2817 1.2810 -0.0470 -0.0350 0.0138  977  CYS   E O   
16281 C  CB  . CYS   E 673 ? 1.2046 1.2970 1.3021 -0.0495 -0.0335 0.0128  977  CYS   E CB  
16282 S  SG  . CYS   E 673 ? 1.2049 1.2972 1.2950 -0.0449 -0.0358 0.0096  977  CYS   E SG  
16283 N  N   . GLN   E 674 ? 1.2285 1.3326 1.3407 -0.0489 -0.0287 0.0182  978  GLN   E N   
16284 C  CA  . GLN   E 674 ? 1.2795 1.3885 1.3958 -0.0470 -0.0267 0.0200  978  GLN   E CA  
16285 C  C   . GLN   E 674 ? 1.3868 1.4902 1.4972 -0.0426 -0.0218 0.0217  978  GLN   E C   
16286 O  O   . GLN   E 674 ? 1.4210 1.5175 1.5272 -0.0423 -0.0189 0.0226  978  GLN   E O   
16287 C  CB  . GLN   E 674 ? 1.2520 1.3668 1.3799 -0.0511 -0.0263 0.0222  978  GLN   E CB  
16288 C  CG  . GLN   E 674 ? 1.3080 1.4282 1.4408 -0.0493 -0.0243 0.0241  978  GLN   E CG  
16289 C  CD  . GLN   E 674 ? 1.3949 1.5162 1.5362 -0.0513 -0.0200 0.0274  978  GLN   E CD  
16290 O  OE1 . GLN   E 674 ? 1.2644 1.3850 1.4109 -0.0555 -0.0203 0.0279  978  GLN   E OE1 
16291 N  NE2 . GLN   E 674 ? 1.5698 1.6926 1.7126 -0.0484 -0.0160 0.0297  978  GLN   E NE2 
16292 N  N   . LYS   E 675 ? 1.4463 1.5521 1.5557 -0.0389 -0.0209 0.0222  979  LYS   E N   
16293 C  CA  . LYS   E 675 ? 1.5401 1.6402 1.6427 -0.0340 -0.0166 0.0236  979  LYS   E CA  
16294 C  C   . LYS   E 675 ? 1.7056 1.8061 1.8143 -0.0352 -0.0112 0.0275  979  LYS   E C   
16295 O  O   . LYS   E 675 ? 1.7276 1.8345 1.8436 -0.0357 -0.0105 0.0290  979  LYS   E O   
16296 C  CB  . LYS   E 675 ? 1.4911 1.5933 1.5902 -0.0296 -0.0183 0.0224  979  LYS   E CB  
16297 N  N   . ASP   E 676 ? 1.9916 2.0853 2.0978 -0.0357 -0.0072 0.0292  980  ASP   E N   
16298 C  CA  . ASP   E 676 ? 2.0544 2.1478 2.1667 -0.0369 -0.0012 0.0330  980  ASP   E CA  
16299 C  C   . ASP   E 676 ? 2.1614 2.2534 2.2696 -0.0316 0.0027  0.0348  980  ASP   E C   
16300 O  O   . ASP   E 676 ? 2.2378 2.3212 2.3369 -0.0275 0.0071  0.0361  980  ASP   E O   
16301 C  CB  . ASP   E 676 ? 2.0696 2.1547 2.1786 -0.0381 0.0025  0.0344  980  ASP   E CB  
16302 N  N   . SER   E 677 ? 1.9725 2.0724 2.0868 -0.0313 0.0011  0.0349  981  SER   E N   
16303 C  CA  . SER   E 677 ? 2.0551 2.1540 2.1650 -0.0260 0.0038  0.0360  981  SER   E CA  
16304 C  C   . SER   E 677 ? 2.1149 2.2086 2.2243 -0.0242 0.0118  0.0400  981  SER   E C   
16305 O  O   . SER   E 677 ? 2.0803 2.1684 2.1809 -0.0186 0.0150  0.0410  981  SER   E O   
16306 C  CB  . SER   E 677 ? 2.0308 2.1395 2.1491 -0.0269 0.0009  0.0357  981  SER   E CB  
16307 O  OG  . SER   E 677 ? 2.0885 2.2034 2.2196 -0.0309 0.0035  0.0384  981  SER   E OG  
16308 N  N   . ALA   E 678 ? 2.1298 2.2252 2.2487 -0.0289 0.0151  0.0424  982  ALA   E N   
16309 C  CA  . ALA   E 678 ? 2.0724 2.1627 2.1918 -0.0277 0.0234  0.0464  982  ALA   E CA  
16310 C  C   . ALA   E 678 ? 2.0854 2.1628 2.1892 -0.0231 0.0265  0.0465  982  ALA   E C   
16311 O  O   . ALA   E 678 ? 2.0925 2.1647 2.1931 -0.0250 0.0260  0.0457  982  ALA   E O   
16312 C  CB  . ALA   E 678 ? 2.0102 2.1040 2.1428 -0.0341 0.0255  0.0483  982  ALA   E CB  
16313 N  N   . ALA   E 679 ? 2.1309 2.2027 2.2245 -0.0166 0.0293  0.0472  983  ALA   E N   
16314 C  CA  . ALA   E 679 ? 2.1348 2.1935 2.2123 -0.0113 0.0319  0.0472  983  ALA   E CA  
16315 C  C   . ALA   E 679 ? 2.1375 2.1883 2.2141 -0.0116 0.0406  0.0513  983  ALA   E C   
16316 O  O   . ALA   E 679 ? 2.1168 2.1558 2.1790 -0.0063 0.0438  0.0518  983  ALA   E O   
16317 C  CB  . ALA   E 679 ? 2.0275 2.0819 2.0938 -0.0040 0.0317  0.0466  983  ALA   E CB  
16318 N  N   . THR   E 680 ? 2.1123 2.1697 2.2039 -0.0174 0.0438  0.0538  984  THR   E N   
16319 C  CA  . THR   E 680 ? 2.1272 2.1794 2.2222 -0.0196 0.0516  0.0575  984  THR   E CA  
16320 C  C   . THR   E 680 ? 2.1943 2.2325 2.2738 -0.0164 0.0538  0.0574  984  THR   E C   
16321 O  O   . THR   E 680 ? 2.2295 2.2577 2.2994 -0.0117 0.0610  0.0602  984  THR   E O   
16322 C  CB  . THR   E 680 ? 2.0814 2.1420 2.1930 -0.0278 0.0496  0.0575  984  THR   E CB  
16323 O  OG1 . THR   E 680 ? 2.0248 2.0982 2.1507 -0.0306 0.0469  0.0574  984  THR   E OG1 
16324 C  CG2 . THR   E 680 ? 2.0587 2.1143 2.1756 -0.0305 0.0578  0.0614  984  THR   E CG2 
16325 N  N   . THR   E 681 ? 2.2139 2.2513 2.2906 -0.0187 0.0477  0.0541  985  THR   E N   
16326 C  CA  . THR   E 681 ? 2.2461 2.2712 2.3067 -0.0149 0.0472  0.0528  985  THR   E CA  
16327 C  C   . THR   E 681 ? 2.2455 2.2718 2.2978 -0.0113 0.0391  0.0483  985  THR   E C   
16328 O  O   . THR   E 681 ? 2.1917 2.2275 2.2519 -0.0149 0.0323  0.0454  985  THR   E O   
16329 C  CB  . THR   E 681 ? 2.2333 2.2557 2.2969 -0.0200 0.0466  0.0524  985  THR   E CB  
16330 O  OG1 . THR   E 681 ? 2.2433 2.2702 2.3215 -0.0257 0.0518  0.0558  985  THR   E OG1 
16331 C  CG2 . THR   E 681 ? 2.2097 2.2170 2.2570 -0.0157 0.0499  0.0529  985  THR   E CG2 
16332 N  N   . ASP   E 682 ? 2.3872 2.4040 2.4240 -0.0040 0.0397  0.0477  986  ASP   E N   
16333 C  CA  . ASP   E 682 ? 2.3601 2.3764 2.3885 -0.0004 0.0319  0.0432  986  ASP   E CA  
16334 C  C   . ASP   E 682 ? 2.3464 2.3637 2.3761 -0.0043 0.0266  0.0402  986  ASP   E C   
16335 O  O   . ASP   E 682 ? 2.3256 2.3485 2.3563 -0.0046 0.0194  0.0364  986  ASP   E O   
16336 C  CB  . ASP   E 682 ? 2.3582 2.3616 2.3687 0.0079  0.0335  0.0431  986  ASP   E CB  
16337 C  CG  . ASP   E 682 ? 2.3901 2.3940 2.3936 0.0120  0.0255  0.0385  986  ASP   E CG  
16338 O  OD1 . ASP   E 682 ? 2.4088 2.4105 2.4084 0.0117  0.0206  0.0354  986  ASP   E OD1 
16339 O  OD2 . ASP   E 682 ? 2.3674 2.3742 2.3701 0.0154  0.0241  0.0380  986  ASP   E OD2 
16340 N  N   . GLU   E 683 ? 2.3596 2.3715 2.3897 -0.0074 0.0302  0.0420  987  GLU   E N   
16341 C  CA  . GLU   E 683 ? 2.2106 2.2239 2.2433 -0.0117 0.0256  0.0395  987  GLU   E CA  
16342 C  C   . GLU   E 683 ? 2.1598 2.1869 2.2072 -0.0177 0.0205  0.0378  987  GLU   E C   
16343 O  O   . GLU   E 683 ? 2.0692 2.0996 2.1164 -0.0188 0.0140  0.0342  987  GLU   E O   
16344 C  CB  . GLU   E 683 ? 2.0954 2.1012 2.1279 -0.0146 0.0312  0.0422  987  GLU   E CB  
16345 N  N   . GLU   E 684 ? 2.3073 2.3421 2.3672 -0.0213 0.0235  0.0404  988  GLU   E N   
16346 C  CA  . GLU   E 684 ? 2.2575 2.3049 2.3310 -0.0267 0.0185  0.0390  988  GLU   E CA  
16347 C  C   . GLU   E 684 ? 2.2113 2.2649 2.2834 -0.0239 0.0128  0.0360  988  GLU   E C   
16348 O  O   . GLU   E 684 ? 2.1463 2.2065 2.2230 -0.0268 0.0067  0.0331  988  GLU   E O   
16349 C  CB  . GLU   E 684 ? 2.2533 2.3072 2.3408 -0.0308 0.0230  0.0425  988  GLU   E CB  
16350 N  N   . ARG   E 685 ? 2.1026 2.1537 2.1682 -0.0183 0.0148  0.0367  989  ARG   E N   
16351 C  CA  . ARG   E 685 ? 1.9695 2.0259 2.0337 -0.0155 0.0096  0.0340  989  ARG   E CA  
16352 C  C   . ARG   E 685 ? 1.8362 1.8903 1.8933 -0.0141 0.0034  0.0298  989  ARG   E C   
16353 O  O   . ARG   E 685 ? 1.7679 1.8295 1.8295 -0.0156 -0.0021 0.0271  989  ARG   E O   
16354 C  CB  . ARG   E 685 ? 1.9220 1.9739 1.9787 -0.0092 0.0130  0.0355  989  ARG   E CB  
16355 N  N   . GLN   E 686 ? 1.7572 1.8010 1.8033 -0.0112 0.0044  0.0292  990  GLN   E N   
16356 C  CA  . GLN   E 686 ? 1.6485 1.6896 1.6880 -0.0095 -0.0011 0.0253  990  GLN   E CA  
16357 C  C   . GLN   E 686 ? 1.6137 1.6563 1.6577 -0.0150 -0.0031 0.0242  990  GLN   E C   
16358 O  O   . GLN   E 686 ? 1.5554 1.5916 1.5919 -0.0135 -0.0051 0.0222  990  GLN   E O   
16359 C  CB  . GLN   E 686 ? 1.7308 1.7595 1.7554 -0.0030 0.0002  0.0248  990  GLN   E CB  
16360 N  N   . HIS   E 687 ? 1.6048 1.6551 1.6607 -0.0210 -0.0029 0.0255  991  HIS   E N   
16361 C  CA  . HIS   E 687 ? 1.5172 1.5695 1.5778 -0.0262 -0.0057 0.0241  991  HIS   E CA  
16362 C  C   . HIS   E 687 ? 1.4522 1.5158 1.5246 -0.0308 -0.0091 0.0235  991  HIS   E C   
16363 O  O   . HIS   E 687 ? 1.4683 1.5376 1.5488 -0.0323 -0.0069 0.0258  991  HIS   E O   
16364 C  CB  . HIS   E 687 ? 1.5573 1.6038 1.6190 -0.0294 -0.0012 0.0268  991  HIS   E CB  
16365 C  CG  . HIS   E 687 ? 1.5268 1.5774 1.5968 -0.0358 -0.0040 0.0259  991  HIS   E CG  
16366 N  ND1 . HIS   E 687 ? 1.4797 1.5276 1.5453 -0.0367 -0.0080 0.0230  991  HIS   E ND1 
16367 C  CD2 . HIS   E 687 ? 1.4933 1.5503 1.5755 -0.0414 -0.0035 0.0276  991  HIS   E CD2 
16368 C  CE1 . HIS   E 687 ? 1.4298 1.4815 1.5036 -0.0425 -0.0099 0.0229  991  HIS   E CE1 
16369 N  NE2 . HIS   E 687 ? 1.4308 1.4882 1.5150 -0.0455 -0.0075 0.0255  991  HIS   E NE2 
16370 N  N   . LEU   E 688 ? 1.4009 1.4675 1.4739 -0.0326 -0.0143 0.0204  992  LEU   E N   
16371 C  CA  . LEU   E 688 ? 1.3928 1.4688 1.4754 -0.0368 -0.0180 0.0195  992  LEU   E CA  
16372 C  C   . LEU   E 688 ? 1.4079 1.4843 1.4969 -0.0426 -0.0181 0.0203  992  LEU   E C   
16373 O  O   . LEU   E 688 ? 1.4178 1.4898 1.5030 -0.0440 -0.0200 0.0186  992  LEU   E O   
16374 C  CB  . LEU   E 688 ? 1.3424 1.4205 1.4215 -0.0354 -0.0232 0.0157  992  LEU   E CB  
16375 C  CG  . LEU   E 688 ? 1.3293 1.4070 1.4030 -0.0297 -0.0236 0.0147  992  LEU   E CG  
16376 C  CD1 . LEU   E 688 ? 1.2924 1.3693 1.3611 -0.0277 -0.0277 0.0109  992  LEU   E CD1 
16377 C  CD2 . LEU   E 688 ? 1.3063 1.3922 1.3873 -0.0303 -0.0238 0.0157  992  LEU   E CD2 
16378 N  N   . GLN   E 689 ? 1.4007 1.4820 1.4998 -0.0460 -0.0161 0.0229  993  GLN   E N   
16379 C  CA  . GLN   E 689 ? 1.3735 1.4556 1.4802 -0.0517 -0.0165 0.0237  993  GLN   E CA  
16380 C  C   . GLN   E 689 ? 1.3240 1.4121 1.4351 -0.0549 -0.0226 0.0212  993  GLN   E C   
16381 O  O   . GLN   E 689 ? 1.2864 1.3816 1.4015 -0.0546 -0.0249 0.0207  993  GLN   E O   
16382 C  CB  . GLN   E 689 ? 1.3044 1.3900 1.4214 -0.0539 -0.0123 0.0273  993  GLN   E CB  
16383 N  N   . GLU   E 690 ? 1.3838 1.4683 1.4931 -0.0578 -0.0253 0.0195  994  GLU   E N   
16384 C  CA  . GLU   E 690 ? 1.3459 1.4348 1.4589 -0.0611 -0.0308 0.0174  994  GLU   E CA  
16385 C  C   . GLU   E 690 ? 1.3543 1.4498 1.4799 -0.0653 -0.0315 0.0191  994  GLU   E C   
16386 O  O   . GLU   E 690 ? 1.3794 1.4741 1.5112 -0.0673 -0.0280 0.0217  994  GLU   E O   
16387 C  CB  . GLU   E 690 ? 1.4118 1.4942 1.5198 -0.0631 -0.0331 0.0155  994  GLU   E CB  
16388 C  CG  . GLU   E 690 ? 1.4872 1.5608 1.5850 -0.0597 -0.0301 0.0153  994  GLU   E CG  
16389 C  CD  . GLU   E 690 ? 1.5462 1.6130 1.6391 -0.0618 -0.0321 0.0136  994  GLU   E CD  
16390 O  OE1 . GLU   E 690 ? 1.5142 1.5817 1.6129 -0.0665 -0.0345 0.0135  994  GLU   E OE1 
16391 O  OE2 . GLU   E 690 ? 1.5358 1.5962 1.6189 -0.0584 -0.0315 0.0122  994  GLU   E OE2 
16392 N  N   . VAL   E 691 ? 1.2224 1.3245 1.3519 -0.0665 -0.0359 0.0178  995  VAL   E N   
16393 C  CA  . VAL   E 691 ? 1.2421 1.3510 1.3836 -0.0700 -0.0373 0.0191  995  VAL   E CA  
16394 C  C   . VAL   E 691 ? 1.1466 1.2580 1.2891 -0.0725 -0.0438 0.0166  995  VAL   E C   
16395 O  O   . VAL   E 691 ? 1.1839 1.3015 1.3351 -0.0747 -0.0464 0.0170  995  VAL   E O   
16396 C  CB  . VAL   E 691 ? 1.2665 1.3817 1.4127 -0.0675 -0.0347 0.0211  995  VAL   E CB  
16397 C  CG1 . VAL   E 691 ? 1.2293 1.3421 1.3770 -0.0660 -0.0280 0.0242  995  VAL   E CG1 
16398 C  CG2 . VAL   E 691 ? 1.1499 1.2667 1.2887 -0.0633 -0.0360 0.0194  995  VAL   E CG2 
16399 N  N   . GLY   E 692 ? 1.0666 1.1730 1.2001 -0.0720 -0.0464 0.0140  996  GLY   E N   
16400 C  CA  . GLY   E 692 ? 1.0780 1.1855 1.2108 -0.0740 -0.0521 0.0117  996  GLY   E CA  
16401 C  C   . GLY   E 692 ? 1.0656 1.1659 1.1889 -0.0740 -0.0544 0.0090  996  GLY   E C   
16402 O  O   . GLY   E 692 ? 1.0329 1.1302 1.1475 -0.0706 -0.0531 0.0078  996  GLY   E O   
16403 N  N   . LEU   E 693 ? 1.0586 1.1562 1.1836 -0.0777 -0.0581 0.0081  997  LEU   E N   
16404 C  CA  . LEU   E 693 ? 1.0277 1.1182 1.1438 -0.0780 -0.0606 0.0056  997  LEU   E CA  
16405 C  C   . LEU   E 693 ? 1.0219 1.1130 1.1379 -0.0801 -0.0665 0.0037  997  LEU   E C   
16406 O  O   . LEU   E 693 ? 1.0566 1.1518 1.1812 -0.0829 -0.0693 0.0044  997  LEU   E O   
16407 C  CB  . LEU   E 693 ? 1.0199 1.1039 1.1361 -0.0803 -0.0594 0.0061  997  LEU   E CB  
16408 C  CG  . LEU   E 693 ? 1.0074 1.0876 1.1187 -0.0773 -0.0539 0.0072  997  LEU   E CG  
16409 C  CD1 . LEU   E 693 ? 1.0786 1.1502 1.1857 -0.0789 -0.0535 0.0068  997  LEU   E CD1 
16410 C  CD2 . LEU   E 693 ? 1.0005 1.0806 1.1029 -0.0726 -0.0531 0.0057  997  LEU   E CD2 
16411 N  N   . PHE   E 694 ? 0.9789 1.0656 1.0850 -0.0784 -0.0684 0.0012  998  PHE   E N   
16412 C  CA  . PHE   E 694 ? 0.9763 1.0624 1.0800 -0.0796 -0.0736 -0.0006 998  PHE   E CA  
16413 C  C   . PHE   E 694 ? 0.9655 1.0445 1.0571 -0.0777 -0.0744 -0.0032 998  PHE   E C   
16414 O  O   . PHE   E 694 ? 0.9433 1.0219 1.0294 -0.0743 -0.0711 -0.0036 998  PHE   E O   
16415 C  CB  . PHE   E 694 ? 0.9986 1.0919 1.1053 -0.0781 -0.0742 -0.0002 998  PHE   E CB  
16416 C  CG  . PHE   E 694 ? 0.9269 1.0193 1.0309 -0.0791 -0.0795 -0.0018 998  PHE   E CG  
16417 C  CD1 . PHE   E 694 ? 0.9885 1.0823 1.0994 -0.0823 -0.0840 -0.0016 998  PHE   E CD1 
16418 C  CD2 . PHE   E 694 ? 0.9262 1.0162 1.0210 -0.0765 -0.0799 -0.0036 998  PHE   E CD2 
16419 C  CE1 . PHE   E 694 ? 1.0237 1.1160 1.1314 -0.0828 -0.0892 -0.0032 998  PHE   E CE1 
16420 C  CE2 . PHE   E 694 ? 0.9933 1.0816 1.0845 -0.0770 -0.0844 -0.0049 998  PHE   E CE2 
16421 C  CZ  . PHE   E 694 ? 1.0277 1.1168 1.1248 -0.0801 -0.0893 -0.0048 998  PHE   E CZ  
16422 N  N   . HIS   E 695 ? 0.9627 1.0362 1.0508 -0.0798 -0.0788 -0.0049 999  HIS   E N   
16423 C  CA  . HIS   E 695 ? 0.9130 0.9793 0.9894 -0.0781 -0.0798 -0.0073 999  HIS   E CA  
16424 C  C   . HIS   E 695 ? 0.9650 1.0333 1.0379 -0.0767 -0.0820 -0.0083 999  HIS   E C   
16425 O  O   . HIS   E 695 ? 0.9557 1.0237 1.0300 -0.0787 -0.0867 -0.0088 999  HIS   E O   
16426 C  CB  . HIS   E 695 ? 0.9575 1.0160 1.0312 -0.0810 -0.0834 -0.0086 999  HIS   E CB  
16427 C  CG  . HIS   E 695 ? 1.0065 1.0567 1.0678 -0.0791 -0.0841 -0.0110 999  HIS   E CG  
16428 N  ND1 . HIS   E 695 ? 1.0257 1.0713 1.0811 -0.0771 -0.0806 -0.0115 999  HIS   E ND1 
16429 C  CD2 . HIS   E 695 ? 1.0201 1.0652 1.0732 -0.0786 -0.0878 -0.0131 999  HIS   E CD2 
16430 C  CE1 . HIS   E 695 ? 1.0208 1.0595 1.0658 -0.0755 -0.0819 -0.0138 999  HIS   E CE1 
16431 N  NE2 . HIS   E 695 ? 0.9731 1.0111 1.0161 -0.0764 -0.0861 -0.0147 999  HIS   E NE2 
16432 N  N   . LEU   E 696 ? 0.9725 1.0433 1.0417 -0.0732 -0.0787 -0.0085 1000 LEU   E N   
16433 C  CA  . LEU   E 696 ? 0.9189 0.9907 0.9841 -0.0717 -0.0801 -0.0094 1000 LEU   E CA  
16434 C  C   . LEU   E 696 ? 0.9086 0.9719 0.9633 -0.0715 -0.0828 -0.0117 1000 LEU   E C   
16435 O  O   . LEU   E 696 ? 0.9571 1.0188 1.0088 -0.0720 -0.0864 -0.0124 1000 LEU   E O   
16436 C  CB  . LEU   E 696 ? 0.8932 0.9693 0.9575 -0.0682 -0.0756 -0.0091 1000 LEU   E CB  
16437 C  CG  . LEU   E 696 ? 0.8902 0.9687 0.9521 -0.0665 -0.0758 -0.0095 1000 LEU   E CG  
16438 C  CD1 . LEU   E 696 ? 0.8846 0.9701 0.9548 -0.0677 -0.0772 -0.0078 1000 LEU   E CD1 
16439 C  CD2 . LEU   E 696 ? 0.8862 0.9662 0.9453 -0.0630 -0.0715 -0.0101 1000 LEU   E CD2 
16440 N  N   . GLY   E 697 ? 0.9505 1.0075 0.9990 -0.0707 -0.0814 -0.0129 1001 GLY   E N   
16441 C  CA  . GLY   E 697 ? 0.9799 1.0281 1.0172 -0.0697 -0.0831 -0.0151 1001 GLY   E CA  
16442 C  C   . GLY   E 697 ? 1.0213 1.0686 1.0518 -0.0659 -0.0792 -0.0161 1001 GLY   E C   
16443 O  O   . GLY   E 697 ? 1.0663 1.1061 1.0871 -0.0645 -0.0795 -0.0179 1001 GLY   E O   
16444 N  N   . GLU   E 698 ? 0.9629 1.0175 0.9984 -0.0639 -0.0754 -0.0150 1002 GLU   E N   
16445 C  CA  . GLU   E 698 ? 0.9597 1.0150 0.9912 -0.0605 -0.0718 -0.0159 1002 GLU   E CA  
16446 C  C   . GLU   E 698 ? 0.9429 1.0025 0.9788 -0.0584 -0.0677 -0.0155 1002 GLU   E C   
16447 O  O   . GLU   E 698 ? 0.9239 0.9879 0.9669 -0.0595 -0.0674 -0.0140 1002 GLU   E O   
16448 C  CB  . GLU   E 698 ? 0.9776 1.0376 1.0110 -0.0602 -0.0722 -0.0151 1002 GLU   E CB  
16449 C  CG  . GLU   E 698 ? 1.0451 1.1023 1.0715 -0.0576 -0.0700 -0.0163 1002 GLU   E CG  
16450 C  CD  . GLU   E 698 ? 1.0845 1.1319 1.1000 -0.0574 -0.0718 -0.0179 1002 GLU   E CD  
16451 O  OE1 . GLU   E 698 ? 0.9881 1.0320 1.0005 -0.0592 -0.0762 -0.0180 1002 GLU   E OE1 
16452 O  OE2 . GLU   E 698 ? 1.1405 1.1835 1.1504 -0.0553 -0.0691 -0.0193 1002 GLU   E OE2 
16453 N  N   . PHE   E 699 ? 0.9312 0.9894 0.9629 -0.0553 -0.0646 -0.0168 1003 PHE   E N   
16454 C  CA  . PHE   E 699 ? 0.9438 1.0047 0.9786 -0.0529 -0.0613 -0.0169 1003 PHE   E CA  
16455 C  C   . PHE   E 699 ? 0.9397 1.0082 0.9802 -0.0511 -0.0590 -0.0163 1003 PHE   E C   
16456 O  O   . PHE   E 699 ? 0.9328 1.0015 0.9710 -0.0493 -0.0574 -0.0173 1003 PHE   E O   
16457 C  CB  . PHE   E 699 ? 0.9968 1.0514 1.0245 -0.0505 -0.0596 -0.0189 1003 PHE   E CB  
16458 C  CG  . PHE   E 699 ? 0.9810 1.0378 1.0112 -0.0475 -0.0567 -0.0194 1003 PHE   E CG  
16459 C  CD1 . PHE   E 699 ? 0.9726 1.0341 1.0058 -0.0446 -0.0540 -0.0201 1003 PHE   E CD1 
16460 C  CD2 . PHE   E 699 ? 0.9826 1.0361 1.0119 -0.0474 -0.0568 -0.0194 1003 PHE   E CD2 
16461 C  CE1 . PHE   E 699 ? 0.9178 0.9810 0.9534 -0.0416 -0.0520 -0.0209 1003 PHE   E CE1 
16462 C  CE2 . PHE   E 699 ? 0.9996 1.0542 1.0303 -0.0442 -0.0546 -0.0201 1003 PHE   E CE2 
16463 C  CZ  . PHE   E 699 ? 0.9450 1.0046 0.9790 -0.0413 -0.0525 -0.0209 1003 PHE   E CZ  
16464 N  N   . VAL   E 700 ? 0.9210 0.9954 0.9688 -0.0515 -0.0588 -0.0147 1004 VAL   E N   
16465 C  CA  . VAL   E 700 ? 0.8956 0.9771 0.9491 -0.0501 -0.0573 -0.0141 1004 VAL   E CA  
16466 C  C   . VAL   E 700 ? 0.8753 0.9581 0.9297 -0.0465 -0.0544 -0.0153 1004 VAL   E C   
16467 O  O   . VAL   E 700 ? 0.8880 0.9690 0.9420 -0.0453 -0.0538 -0.0157 1004 VAL   E O   
16468 C  CB  . VAL   E 700 ? 0.8712 0.9581 0.9318 -0.0516 -0.0582 -0.0119 1004 VAL   E CB  
16469 C  CG1 . VAL   E 700 ? 0.8795 0.9729 0.9449 -0.0503 -0.0570 -0.0114 1004 VAL   E CG1 
16470 C  CG2 . VAL   E 700 ? 0.8742 0.9600 0.9352 -0.0551 -0.0614 -0.0108 1004 VAL   E CG2 
16471 N  N   . ASN   E 701 ? 0.8798 0.9656 0.9356 -0.0448 -0.0527 -0.0161 1005 ASN   E N   
16472 C  CA  . ASN   E 701 ? 0.8678 0.9559 0.9262 -0.0415 -0.0504 -0.0174 1005 ASN   E CA  
16473 C  C   . ASN   E 701 ? 0.8990 0.9940 0.9646 -0.0405 -0.0499 -0.0166 1005 ASN   E C   
16474 O  O   . ASN   E 701 ? 0.8716 0.9685 0.9402 -0.0378 -0.0490 -0.0175 1005 ASN   E O   
16475 C  CB  . ASN   E 701 ? 0.8711 0.9569 0.9264 -0.0398 -0.0484 -0.0192 1005 ASN   E CB  
16476 C  CG  . ASN   E 701 ? 0.9318 1.0117 0.9818 -0.0385 -0.0478 -0.0208 1005 ASN   E CG  
16477 O  OD1 . ASN   E 701 ? 0.9837 1.0587 1.0278 -0.0385 -0.0471 -0.0216 1005 ASN   E OD1 
16478 N  ND2 . ASN   E 701 ? 0.9552 1.0347 1.0063 -0.0370 -0.0481 -0.0211 1005 ASN   E ND2 
16479 N  N   . VAL   E 702 ? 0.9020 1.0003 0.9701 -0.0424 -0.0509 -0.0151 1006 VAL   E N   
16480 C  CA  . VAL   E 702 ? 0.8914 0.9960 0.9658 -0.0415 -0.0503 -0.0144 1006 VAL   E CA  
16481 C  C   . VAL   E 702 ? 0.8956 1.0030 0.9723 -0.0439 -0.0521 -0.0122 1006 VAL   E C   
16482 O  O   . VAL   E 702 ? 0.9257 1.0315 0.9998 -0.0461 -0.0534 -0.0116 1006 VAL   E O   
16483 C  CB  . VAL   E 702 ? 0.8876 0.9937 0.9630 -0.0404 -0.0484 -0.0155 1006 VAL   E CB  
16484 C  CG1 . VAL   E 702 ? 0.9076 1.0107 0.9782 -0.0424 -0.0486 -0.0150 1006 VAL   E CG1 
16485 C  CG2 . VAL   E 702 ? 0.9421 1.0541 1.0241 -0.0393 -0.0479 -0.0150 1006 VAL   E CG2 
16486 N  N   . PHE   E 703 ? 0.9308 1.0417 1.0120 -0.0434 -0.0524 -0.0110 1007 PHE   E N   
16487 C  CA  . PHE   E 703 ? 0.9420 1.0570 1.0271 -0.0449 -0.0536 -0.0090 1007 PHE   E CA  
16488 C  C   . PHE   E 703 ? 1.0159 1.1359 1.1055 -0.0432 -0.0527 -0.0091 1007 PHE   E C   
16489 O  O   . PHE   E 703 ? 1.0762 1.1971 1.1675 -0.0405 -0.0516 -0.0102 1007 PHE   E O   
16490 C  CB  . PHE   E 703 ? 0.9236 1.0395 1.0112 -0.0453 -0.0540 -0.0074 1007 PHE   E CB  
16491 C  CG  . PHE   E 703 ? 0.9098 1.0215 0.9947 -0.0476 -0.0550 -0.0069 1007 PHE   E CG  
16492 C  CD1 . PHE   E 703 ? 0.9024 1.0145 0.9884 -0.0507 -0.0570 -0.0056 1007 PHE   E CD1 
16493 C  CD2 . PHE   E 703 ? 0.9284 1.0357 1.0100 -0.0465 -0.0541 -0.0077 1007 PHE   E CD2 
16494 C  CE1 . PHE   E 703 ? 0.9358 1.0439 1.0201 -0.0530 -0.0582 -0.0053 1007 PHE   E CE1 
16495 C  CE2 . PHE   E 703 ? 0.9136 1.0166 0.9928 -0.0488 -0.0550 -0.0072 1007 PHE   E CE2 
16496 C  CZ  . PHE   E 703 ? 0.9274 1.0310 1.0084 -0.0521 -0.0570 -0.0060 1007 PHE   E CZ  
16497 N  N   . CYS   E 704 ? 1.0438 1.1666 1.1353 -0.0445 -0.0534 -0.0079 1008 CYS   E N   
16498 C  CA  . CYS   E 704 ? 1.0724 1.1999 1.1685 -0.0431 -0.0529 -0.0076 1008 CYS   E CA  
16499 C  C   . CYS   E 704 ? 1.0343 1.1648 1.1327 -0.0448 -0.0543 -0.0056 1008 CYS   E C   
16500 O  O   . CYS   E 704 ? 1.0189 1.1478 1.1149 -0.0471 -0.0557 -0.0050 1008 CYS   E O   
16501 C  CB  . CYS   E 704 ? 1.0380 1.1655 1.1340 -0.0419 -0.0513 -0.0092 1008 CYS   E CB  
16502 S  SG  . CYS   E 704 ? 1.0385 1.1652 1.1320 -0.0439 -0.0513 -0.0085 1008 CYS   E SG  
16503 N  N   . HIS   E 705 ? 0.9586 1.0932 1.0615 -0.0436 -0.0542 -0.0046 1009 HIS   E N   
16504 C  CA  . HIS   E 705 ? 0.9446 1.0825 1.0503 -0.0448 -0.0554 -0.0028 1009 HIS   E CA  
16505 C  C   . HIS   E 705 ? 0.9861 1.1246 1.0911 -0.0450 -0.0553 -0.0031 1009 HIS   E C   
16506 O  O   . HIS   E 705 ? 1.0257 1.1637 1.1304 -0.0437 -0.0538 -0.0045 1009 HIS   E O   
16507 C  CB  . HIS   E 705 ? 0.9457 1.0871 1.0555 -0.0429 -0.0550 -0.0017 1009 HIS   E CB  
16508 C  CG  . HIS   E 705 ? 0.9772 1.1177 1.0874 -0.0428 -0.0547 -0.0007 1009 HIS   E CG  
16509 N  ND1 . HIS   E 705 ? 1.0279 1.1702 1.1408 -0.0445 -0.0553 0.0013  1009 HIS   E ND1 
16510 C  CD2 . HIS   E 705 ? 0.9823 1.1201 1.0907 -0.0412 -0.0536 -0.0015 1009 HIS   E CD2 
16511 C  CE1 . HIS   E 705 ? 0.9781 1.1187 1.0909 -0.0440 -0.0543 0.0020  1009 HIS   E CE1 
16512 N  NE2 . HIS   E 705 ? 1.0026 1.1402 1.1122 -0.0420 -0.0533 0.0003  1009 HIS   E NE2 
16513 N  N   . GLY   E 706 ? 1.0107 1.1501 1.1158 -0.0467 -0.0570 -0.0017 1010 GLY   E N   
16514 C  CA  . GLY   E 706 ? 1.0000 1.1389 1.1032 -0.0471 -0.0570 -0.0018 1010 GLY   E CA  
16515 C  C   . GLY   E 706 ? 0.9586 1.0952 1.0584 -0.0493 -0.0595 -0.0010 1010 GLY   E C   
16516 O  O   . GLY   E 706 ? 0.9711 1.1060 1.0699 -0.0507 -0.0611 -0.0009 1010 GLY   E O   
16517 N  N   . SER   E 707 ? 0.9914 1.1275 1.0894 -0.0495 -0.0600 -0.0005 1011 SER   E N   
16518 C  CA  . SER   E 707 ? 1.0936 1.2268 1.1875 -0.0511 -0.0628 0.0000  1011 SER   E CA  
16519 C  C   . SER   E 707 ? 1.1571 1.2864 1.2453 -0.0505 -0.0615 -0.0005 1011 SER   E C   
16520 O  O   . SER   E 707 ? 1.2329 1.3638 1.3228 -0.0492 -0.0589 -0.0006 1011 SER   E O   
16521 C  CB  . SER   E 707 ? 1.1448 1.2819 1.2431 -0.0518 -0.0656 0.0017  1011 SER   E CB  
16522 O  OG  . SER   E 707 ? 1.1360 1.2705 1.2317 -0.0536 -0.0693 0.0019  1011 SER   E OG  
16523 N  N   . LEU   E 708 ? 1.2127 1.3364 1.2939 -0.0514 -0.0633 -0.0008 1012 LEU   E N   
16524 C  CA  . LEU   E 708 ? 1.3076 1.4264 1.3820 -0.0507 -0.0618 -0.0010 1012 LEU   E CA  
16525 C  C   . LEU   E 708 ? 1.3408 1.4592 1.4134 -0.0509 -0.0646 0.0002  1012 LEU   E C   
16526 O  O   . LEU   E 708 ? 1.3718 1.4844 1.4368 -0.0504 -0.0642 0.0002  1012 LEU   E O   
16527 C  CB  . LEU   E 708 ? 1.3309 1.4424 1.3969 -0.0509 -0.0615 -0.0023 1012 LEU   E CB  
16528 C  CG  . LEU   E 708 ? 1.2069 1.3182 1.2740 -0.0506 -0.0591 -0.0037 1012 LEU   E CG  
16529 C  CD1 . LEU   E 708 ? 1.1317 1.2351 1.1896 -0.0504 -0.0583 -0.0049 1012 LEU   E CD1 
16530 C  CD2 . LEU   E 708 ? 1.1539 1.2695 1.2269 -0.0492 -0.0550 -0.0041 1012 LEU   E CD2 
16531 N  N   . VAL   E 709 ? 1.3296 1.4535 1.4087 -0.0514 -0.0673 0.0013  1013 VAL   E N   
16532 C  CA  . VAL   E 709 ? 1.3605 1.4850 1.4394 -0.0514 -0.0702 0.0026  1013 VAL   E CA  
16533 C  C   . VAL   E 709 ? 1.4253 1.5563 1.5116 -0.0504 -0.0687 0.0036  1013 VAL   E C   
16534 O  O   . VAL   E 709 ? 1.4512 1.5861 1.5429 -0.0499 -0.0663 0.0034  1013 VAL   E O   
16535 C  CB  . VAL   E 709 ? 1.2736 1.3986 1.3541 -0.0528 -0.0754 0.0029  1013 VAL   E CB  
16536 C  CG1 . VAL   E 709 ? 1.2538 1.3712 1.3256 -0.0536 -0.0778 0.0017  1013 VAL   E CG1 
16537 C  CG2 . VAL   E 709 ? 1.2832 1.4140 1.3723 -0.0538 -0.0754 0.0031  1013 VAL   E CG2 
16538 N  N   . MET   E 710 ? 1.4132 1.5448 1.4993 -0.0499 -0.0706 0.0048  1014 MET   E N   
16539 C  CA  . MET   E 710 ? 1.4025 1.5395 1.4947 -0.0488 -0.0694 0.0058  1014 MET   E CA  
16540 C  C   . MET   E 710 ? 1.2807 1.4241 1.3810 -0.0490 -0.0717 0.0069  1014 MET   E C   
16541 O  O   . MET   E 710 ? 1.1649 1.3129 1.2704 -0.0479 -0.0705 0.0077  1014 MET   E O   
16542 C  CB  . MET   E 710 ? 1.4893 1.6233 1.5769 -0.0479 -0.0697 0.0066  1014 MET   E CB  
16543 C  CG  . MET   E 710 ? 1.6185 1.7474 1.7002 -0.0473 -0.0657 0.0059  1014 MET   E CG  
16544 S  SD  . MET   E 710 ? 1.7572 1.8814 1.8327 -0.0461 -0.0653 0.0069  1014 MET   E SD  
16545 C  CE  . MET   E 710 ? 1.7661 1.8808 1.8306 -0.0461 -0.0626 0.0060  1014 MET   E CE  
16546 N  N   . PRO   E 719 ? 1.5765 1.7583 1.7550 -0.0613 -0.0825 0.0161  1023 PRO   E N   
16547 C  CA  . PRO   E 719 ? 1.5109 1.6892 1.6894 -0.0643 -0.0854 0.0148  1023 PRO   E CA  
16548 C  C   . PRO   E 719 ? 1.4756 1.6495 1.6484 -0.0646 -0.0816 0.0142  1023 PRO   E C   
16549 O  O   . PRO   E 719 ? 1.4017 1.5768 1.5796 -0.0653 -0.0783 0.0154  1023 PRO   E O   
16550 C  CB  . PRO   E 719 ? 1.4765 1.6504 1.6474 -0.0646 -0.0908 0.0129  1023 PRO   E CB  
16551 C  CG  . PRO   E 719 ? 1.5268 1.7001 1.6906 -0.0616 -0.0889 0.0129  1023 PRO   E CG  
16552 C  CD  . PRO   E 719 ? 1.5749 1.7542 1.7454 -0.0597 -0.0848 0.0150  1023 PRO   E CD  
16553 N  N   . THR   E 720 ? 1.4795 1.6481 1.6415 -0.0638 -0.0820 0.0125  1024 THR   E N   
16554 C  CA  . THR   E 720 ? 1.4785 1.6431 1.6342 -0.0631 -0.0783 0.0118  1024 THR   E CA  
16555 C  C   . THR   E 720 ? 1.4630 1.6299 1.6180 -0.0601 -0.0736 0.0128  1024 THR   E C   
16556 O  O   . THR   E 720 ? 1.4880 1.6580 1.6441 -0.0583 -0.0737 0.0135  1024 THR   E O   
16557 C  CB  . THR   E 720 ? 1.4972 1.6555 1.6422 -0.0631 -0.0801 0.0096  1024 THR   E CB  
16558 O  OG1 . THR   E 720 ? 1.5327 1.6911 1.6733 -0.0613 -0.0808 0.0094  1024 THR   E OG1 
16559 C  CG2 . THR   E 720 ? 1.4506 1.6050 1.5946 -0.0659 -0.0848 0.0084  1024 THR   E CG2 
16560 N  N   . GLN   E 721 ? 1.4839 1.6488 1.6367 -0.0594 -0.0698 0.0128  1025 GLN   E N   
16561 C  CA  . GLN   E 721 ? 1.4869 1.6524 1.6372 -0.0563 -0.0659 0.0131  1025 GLN   E CA  
16562 C  C   . GLN   E 721 ? 1.4747 1.6348 1.6172 -0.0557 -0.0645 0.0114  1025 GLN   E C   
16563 O  O   . GLN   E 721 ? 1.4630 1.6202 1.6048 -0.0570 -0.0639 0.0111  1025 GLN   E O   
16564 C  CB  . GLN   E 721 ? 1.5339 1.7023 1.6904 -0.0553 -0.0623 0.0153  1025 GLN   E CB  
16565 C  CG  . GLN   E 721 ? 1.6845 1.8585 1.8504 -0.0561 -0.0633 0.0171  1025 GLN   E CG  
16566 C  CD  . GLN   E 721 ? 1.7361 1.9122 1.9084 -0.0556 -0.0591 0.0194  1025 GLN   E CD  
16567 O  OE1 . GLN   E 721 ? 1.6684 1.8415 1.8404 -0.0566 -0.0570 0.0196  1025 GLN   E OE1 
16568 N  NE2 . GLN   E 721 ? 1.7980 1.9787 1.9758 -0.0539 -0.0577 0.0211  1025 GLN   E NE2 
16569 N  N   . GLY   E 722 ? 1.3434 1.5023 1.4805 -0.0537 -0.0640 0.0102  1026 GLY   E N   
16570 C  CA  . GLY   E 722 ? 1.2511 1.4056 1.3817 -0.0528 -0.0626 0.0084  1026 GLY   E CA  
16571 C  C   . GLY   E 722 ? 1.1535 1.3039 1.2784 -0.0543 -0.0648 0.0066  1026 GLY   E C   
16572 O  O   . GLY   E 722 ? 1.1805 1.3305 1.3056 -0.0563 -0.0680 0.0066  1026 GLY   E O   
16573 N  N   . SER   E 723 ? 1.0874 1.2343 1.2069 -0.0531 -0.0632 0.0050  1027 SER   E N   
16574 C  CA  . SER   E 723 ? 1.0128 1.1555 1.1261 -0.0538 -0.0644 0.0033  1027 SER   E CA  
16575 C  C   . SER   E 723 ? 1.0033 1.1426 1.1123 -0.0524 -0.0621 0.0017  1027 SER   E C   
16576 O  O   . SER   E 723 ? 1.0200 1.1600 1.1283 -0.0502 -0.0602 0.0009  1027 SER   E O   
16577 C  CB  . SER   E 723 ? 1.0099 1.1538 1.1219 -0.0529 -0.0650 0.0032  1027 SER   E CB  
16578 O  OG  . SER   E 723 ? 0.9732 1.1126 1.0788 -0.0536 -0.0661 0.0020  1027 SER   E OG  
16579 N  N   . VAL   E 724 ? 0.9642 1.0996 1.0707 -0.0536 -0.0623 0.0010  1028 VAL   E N   
16580 C  CA  . VAL   E 724 ? 0.9209 1.0527 1.0230 -0.0522 -0.0604 -0.0007 1028 VAL   E CA  
16581 C  C   . VAL   E 724 ? 0.9401 1.0668 1.0361 -0.0534 -0.0617 -0.0021 1028 VAL   E C   
16582 O  O   . VAL   E 724 ? 0.9594 1.0836 1.0541 -0.0556 -0.0641 -0.0020 1028 VAL   E O   
16583 C  CB  . VAL   E 724 ? 0.9416 1.0720 1.0445 -0.0519 -0.0592 -0.0005 1028 VAL   E CB  
16584 C  CG1 . VAL   E 724 ? 0.9693 1.0968 1.0684 -0.0495 -0.0572 -0.0023 1028 VAL   E CG1 
16585 C  CG2 . VAL   E 724 ? 1.0538 1.1883 1.1622 -0.0509 -0.0580 0.0013  1028 VAL   E CG2 
16586 N  N   . LEU   E 725 ? 0.9318 1.0568 1.0241 -0.0518 -0.0600 -0.0036 1029 LEU   E N   
16587 C  CA  . LEU   E 725 ? 0.9434 1.0629 1.0290 -0.0523 -0.0604 -0.0050 1029 LEU   E CA  
16588 C  C   . LEU   E 725 ? 0.9586 1.0743 1.0411 -0.0514 -0.0588 -0.0065 1029 LEU   E C   
16589 O  O   . LEU   E 725 ? 0.9607 1.0781 1.0458 -0.0496 -0.0570 -0.0068 1029 LEU   E O   
16590 C  CB  . LEU   E 725 ? 0.9120 1.0314 0.9954 -0.0511 -0.0589 -0.0056 1029 LEU   E CB  
16591 C  CG  . LEU   E 725 ? 0.8564 0.9776 0.9405 -0.0519 -0.0605 -0.0043 1029 LEU   E CG  
16592 C  CD1 . LEU   E 725 ? 0.9396 1.0606 1.0220 -0.0504 -0.0580 -0.0048 1029 LEU   E CD1 
16593 C  CD2 . LEU   E 725 ? 0.8595 0.9766 0.9389 -0.0539 -0.0639 -0.0041 1029 LEU   E CD2 
16594 N  N   . PHE   E 726 ? 0.9286 1.0385 1.0048 -0.0524 -0.0598 -0.0075 1030 PHE   E N   
16595 C  CA  . PHE   E 726 ? 0.9115 1.0172 0.9840 -0.0514 -0.0583 -0.0090 1030 PHE   E CA  
16596 C  C   . PHE   E 726 ? 0.8784 0.9781 0.9432 -0.0512 -0.0581 -0.0104 1030 PHE   E C   
16597 O  O   . PHE   E 726 ? 0.8963 0.9925 0.9569 -0.0529 -0.0605 -0.0102 1030 PHE   E O   
16598 C  CB  . PHE   E 726 ? 0.8954 0.9994 0.9686 -0.0527 -0.0597 -0.0086 1030 PHE   E CB  
16599 C  CG  . PHE   E 726 ? 0.8623 0.9636 0.9340 -0.0557 -0.0631 -0.0079 1030 PHE   E CG  
16600 C  CD1 . PHE   E 726 ? 0.9022 0.9968 0.9667 -0.0566 -0.0646 -0.0092 1030 PHE   E CD1 
16601 C  CD2 . PHE   E 726 ? 0.8908 0.9961 0.9686 -0.0576 -0.0649 -0.0062 1030 PHE   E CD2 
16602 C  CE1 . PHE   E 726 ? 0.9117 1.0035 0.9751 -0.0593 -0.0684 -0.0089 1030 PHE   E CE1 
16603 C  CE2 . PHE   E 726 ? 0.9050 1.0081 0.9828 -0.0604 -0.0685 -0.0058 1030 PHE   E CE2 
16604 C  CZ  . PHE   E 726 ? 0.8763 0.9726 0.9469 -0.0613 -0.0706 -0.0072 1030 PHE   E CZ  
16605 N  N   . GLY   E 727 ? 0.8750 0.9732 0.9380 -0.0490 -0.0551 -0.0119 1031 GLY   E N   
16606 C  CA  . GLY   E 727 ? 0.8936 0.9853 0.9489 -0.0484 -0.0541 -0.0134 1031 GLY   E CA  
16607 C  C   . GLY   E 727 ? 0.9093 0.9962 0.9610 -0.0485 -0.0547 -0.0144 1031 GLY   E C   
16608 O  O   . GLY   E 727 ? 0.8995 0.9884 0.9550 -0.0483 -0.0549 -0.0142 1031 GLY   E O   
16609 N  N   . THR   E 728 ? 0.9365 1.0163 0.9801 -0.0485 -0.0549 -0.0155 1032 THR   E N   
16610 C  CA  . THR   E 728 ? 0.9444 1.0186 0.9834 -0.0488 -0.0560 -0.0165 1032 THR   E CA  
16611 C  C   . THR   E 728 ? 1.0114 1.0795 1.0430 -0.0468 -0.0536 -0.0183 1032 THR   E C   
16612 O  O   . THR   E 728 ? 1.0048 1.0732 1.0352 -0.0451 -0.0507 -0.0187 1032 THR   E O   
16613 C  CB  . THR   E 728 ? 0.9400 1.0105 0.9762 -0.0519 -0.0603 -0.0158 1032 THR   E CB  
16614 O  OG1 . THR   E 728 ? 0.9941 1.0596 1.0231 -0.0522 -0.0616 -0.0162 1032 THR   E OG1 
16615 C  CG2 . THR   E 728 ? 0.8866 0.9635 0.9308 -0.0539 -0.0624 -0.0139 1032 THR   E CG2 
16616 N  N   . VAL   E 729 ? 1.0382 1.1002 1.0644 -0.0469 -0.0545 -0.0193 1033 VAL   E N   
16617 C  CA  . VAL   E 729 ? 1.0560 1.1126 1.0759 -0.0444 -0.0518 -0.0211 1033 VAL   E CA  
16618 C  C   . VAL   E 729 ? 1.1197 1.1688 1.1299 -0.0447 -0.0524 -0.0215 1033 VAL   E C   
16619 O  O   . VAL   E 729 ? 1.1395 1.1853 1.1450 -0.0423 -0.0490 -0.0225 1033 VAL   E O   
16620 C  CB  . VAL   E 729 ? 1.0821 1.1351 1.1002 -0.0438 -0.0522 -0.0221 1033 VAL   E CB  
16621 C  CG1 . VAL   E 729 ? 1.1729 1.2174 1.1816 -0.0422 -0.0510 -0.0238 1033 VAL   E CG1 
16622 C  CG2 . VAL   E 729 ? 1.0862 1.1449 1.1115 -0.0416 -0.0497 -0.0224 1033 VAL   E CG2 
16623 N  N   . ASN   E 730 ? 1.1700 1.2162 1.1771 -0.0473 -0.0568 -0.0208 1034 ASN   E N   
16624 C  CA  . ASN   E 730 ? 1.1871 1.2261 1.1847 -0.0474 -0.0581 -0.0212 1034 ASN   E CA  
16625 C  C   . ASN   E 730 ? 1.1790 1.2216 1.1783 -0.0474 -0.0575 -0.0200 1034 ASN   E C   
16626 O  O   . ASN   E 730 ? 1.1839 1.2209 1.1757 -0.0479 -0.0599 -0.0199 1034 ASN   E O   
16627 C  CB  . ASN   E 730 ? 1.1832 1.2165 1.1762 -0.0500 -0.0638 -0.0213 1034 ASN   E CB  
16628 C  CG  . ASN   E 730 ? 1.2165 1.2437 1.2050 -0.0499 -0.0644 -0.0227 1034 ASN   E CG  
16629 O  OD1 . ASN   E 730 ? 1.2622 1.2806 1.2405 -0.0484 -0.0641 -0.0241 1034 ASN   E OD1 
16630 N  ND2 . ASN   E 730 ? 1.2007 1.2319 1.1964 -0.0511 -0.0650 -0.0223 1034 ASN   E ND2 
16631 N  N   . GLY   E 731 ? 1.0930 1.1440 1.1013 -0.0468 -0.0548 -0.0191 1035 GLY   E N   
16632 C  CA  . GLY   E 731 ? 1.0995 1.1536 1.1093 -0.0467 -0.0538 -0.0179 1035 GLY   E CA  
16633 C  C   . GLY   E 731 ? 1.1148 1.1722 1.1281 -0.0492 -0.0583 -0.0165 1035 GLY   E C   
16634 O  O   . GLY   E 731 ? 1.0919 1.1526 1.1074 -0.0491 -0.0575 -0.0154 1035 GLY   E O   
16635 N  N   . MET   E 732 ? 1.0386 1.0952 1.0529 -0.0515 -0.0628 -0.0164 1036 MET   E N   
16636 C  CA  . MET   E 732 ? 0.9741 1.0350 0.9940 -0.0539 -0.0669 -0.0150 1036 MET   E CA  
16637 C  C   . MET   E 732 ? 0.9521 1.0230 0.9829 -0.0538 -0.0649 -0.0136 1036 MET   E C   
16638 O  O   . MET   E 732 ? 0.9811 1.0556 1.0168 -0.0529 -0.0622 -0.0138 1036 MET   E O   
16639 C  CB  . MET   E 732 ? 0.9884 1.0472 1.0092 -0.0564 -0.0713 -0.0152 1036 MET   E CB  
16640 C  CG  . MET   E 732 ? 1.0011 1.0642 1.0288 -0.0591 -0.0758 -0.0139 1036 MET   E CG  
16641 S  SD  . MET   E 732 ? 1.0161 1.0903 1.0577 -0.0600 -0.0741 -0.0120 1036 MET   E SD  
16642 C  CE  . MET   E 732 ? 0.9648 1.0425 1.0128 -0.0630 -0.0795 -0.0106 1036 MET   E CE  
16643 N  N   . ILE   E 733 ? 0.9350 1.0097 0.9690 -0.0545 -0.0663 -0.0123 1037 ILE   E N   
16644 C  CA  . ILE   E 733 ? 0.8897 0.9733 0.9335 -0.0544 -0.0650 -0.0109 1037 ILE   E CA  
16645 C  C   . ILE   E 733 ? 0.9554 1.0424 1.0046 -0.0568 -0.0693 -0.0097 1037 ILE   E C   
16646 O  O   . ILE   E 733 ? 1.0251 1.1090 1.0709 -0.0580 -0.0730 -0.0095 1037 ILE   E O   
16647 C  CB  . ILE   E 733 ? 0.9200 1.0055 0.9635 -0.0529 -0.0624 -0.0104 1037 ILE   E CB  
16648 C  CG1 . ILE   E 733 ? 0.9648 1.0469 1.0037 -0.0506 -0.0578 -0.0117 1037 ILE   E CG1 
16649 C  CG2 . ILE   E 733 ? 0.8727 0.9669 0.9259 -0.0529 -0.0617 -0.0091 1037 ILE   E CG2 
16650 C  CD1 . ILE   E 733 ? 0.8877 0.9688 0.9238 -0.0492 -0.0549 -0.0114 1037 ILE   E CD1 
16651 N  N   . GLY   E 734 ? 0.9481 1.0412 1.0059 -0.0574 -0.0688 -0.0087 1038 GLY   E N   
16652 C  CA  . GLY   E 734 ? 0.9577 1.0543 1.0217 -0.0597 -0.0722 -0.0074 1038 GLY   E CA  
16653 C  C   . GLY   E 734 ? 0.9315 1.0363 1.0042 -0.0591 -0.0707 -0.0058 1038 GLY   E C   
16654 O  O   . GLY   E 734 ? 0.9019 1.0095 0.9759 -0.0571 -0.0673 -0.0058 1038 GLY   E O   
16655 N  N   . LEU   E 735 ? 0.9401 1.0484 1.0189 -0.0610 -0.0735 -0.0044 1039 LEU   E N   
16656 C  CA  . LEU   E 735 ? 0.9382 1.0540 1.0251 -0.0605 -0.0723 -0.0027 1039 LEU   E CA  
16657 C  C   . LEU   E 735 ? 0.9596 1.0784 1.0539 -0.0622 -0.0729 -0.0015 1039 LEU   E C   
16658 O  O   . LEU   E 735 ? 0.9825 1.0989 1.0775 -0.0645 -0.0760 -0.0016 1039 LEU   E O   
16659 C  CB  . LEU   E 735 ? 0.9410 1.0588 1.0286 -0.0607 -0.0747 -0.0020 1039 LEU   E CB  
16660 C  CG  . LEU   E 735 ? 0.9423 1.0670 1.0366 -0.0596 -0.0735 -0.0004 1039 LEU   E CG  
16661 C  CD1 . LEU   E 735 ? 0.9350 1.0616 1.0290 -0.0571 -0.0693 -0.0007 1039 LEU   E CD1 
16662 C  CD2 . LEU   E 735 ? 1.0406 1.1655 1.1337 -0.0598 -0.0765 0.0000  1039 LEU   E CD2 
16663 N  N   . VAL   E 736 ? 0.9647 1.0880 1.0641 -0.0608 -0.0698 -0.0004 1040 VAL   E N   
16664 C  CA  . VAL   E 736 ? 1.0092 1.1359 1.1161 -0.0620 -0.0695 0.0013  1040 VAL   E CA  
16665 C  C   . VAL   E 736 ? 1.1019 1.2352 1.2152 -0.0609 -0.0686 0.0030  1040 VAL   E C   
16666 O  O   . VAL   E 736 ? 1.0523 1.1874 1.1646 -0.0584 -0.0661 0.0029  1040 VAL   E O   
16667 C  CB  . VAL   E 736 ? 0.9414 1.0661 1.0476 -0.0612 -0.0665 0.0012  1040 VAL   E CB  
16668 C  CG1 . VAL   E 736 ? 0.9851 1.1123 1.0987 -0.0628 -0.0660 0.0031  1040 VAL   E CG1 
16669 C  CG2 . VAL   E 736 ? 0.9928 1.1107 1.0921 -0.0618 -0.0672 -0.0006 1040 VAL   E CG2 
16670 N  N   . THR   E 737 ? 1.1931 1.3298 1.3132 -0.0628 -0.0706 0.0044  1041 THR   E N   
16671 C  CA  . THR   E 737 ? 1.2427 1.3856 1.3697 -0.0619 -0.0696 0.0063  1041 THR   E CA  
16672 C  C   . THR   E 737 ? 1.2613 1.4068 1.3965 -0.0636 -0.0690 0.0081  1041 THR   E C   
16673 O  O   . THR   E 737 ? 1.2401 1.3830 1.3765 -0.0662 -0.0709 0.0078  1041 THR   E O   
16674 C  CB  . THR   E 737 ? 1.2624 1.4077 1.3904 -0.0622 -0.0729 0.0064  1041 THR   E CB  
16675 O  OG1 . THR   E 737 ? 1.3098 1.4611 1.4445 -0.0610 -0.0717 0.0082  1041 THR   E OG1 
16676 C  CG2 . THR   E 737 ? 1.2402 1.3839 1.3699 -0.0651 -0.0776 0.0060  1041 THR   E CG2 
16677 N  N   . SER   E 738 ? 1.2591 1.4093 1.3997 -0.0621 -0.0663 0.0099  1042 SER   E N   
16678 C  CA  . SER   E 738 ? 1.2581 1.4105 1.4064 -0.0632 -0.0644 0.0119  1042 SER   E CA  
16679 C  C   . SER   E 738 ? 1.2607 1.4182 1.4180 -0.0650 -0.0671 0.0131  1042 SER   E C   
16680 O  O   . SER   E 738 ? 1.3168 1.4766 1.4740 -0.0645 -0.0698 0.0127  1042 SER   E O   
16681 C  CB  . SER   E 738 ? 1.3126 1.4665 1.4616 -0.0602 -0.0596 0.0133  1042 SER   E CB  
16682 O  OG  . SER   E 738 ? 1.2953 1.4442 1.4369 -0.0585 -0.0573 0.0122  1042 SER   E OG  
16683 N  N   . LEU   E 739 ? 1.2681 1.4271 1.4334 -0.0671 -0.0663 0.0146  1043 LEU   E N   
16684 C  CA  . LEU   E 739 ? 1.2937 1.4578 1.4694 -0.0691 -0.0688 0.0157  1043 LEU   E CA  
16685 C  C   . LEU   E 739 ? 1.3128 1.4807 1.4973 -0.0688 -0.0642 0.0184  1043 LEU   E C   
16686 O  O   . LEU   E 739 ? 1.3024 1.4680 1.4839 -0.0671 -0.0593 0.0193  1043 LEU   E O   
16687 C  CB  . LEU   E 739 ? 1.2184 1.3801 1.3964 -0.0728 -0.0737 0.0145  1043 LEU   E CB  
16688 C  CG  . LEU   E 739 ? 1.2270 1.3827 1.3942 -0.0730 -0.0774 0.0118  1043 LEU   E CG  
16689 C  CD1 . LEU   E 739 ? 1.2067 1.3591 1.3760 -0.0765 -0.0818 0.0107  1043 LEU   E CD1 
16690 C  CD2 . LEU   E 739 ? 1.2938 1.4510 1.4576 -0.0714 -0.0805 0.0110  1043 LEU   E CD2 
16691 N  N   . SER   E 740 ? 1.3253 1.4987 1.5208 -0.0703 -0.0657 0.0197  1044 SER   E N   
16692 C  CA  . SER   E 740 ? 1.3730 1.5504 1.5786 -0.0703 -0.0611 0.0224  1044 SER   E CA  
16693 C  C   . SER   E 740 ? 1.3887 1.5650 1.6020 -0.0743 -0.0615 0.0229  1044 SER   E C   
16694 O  O   . SER   E 740 ? 1.4079 1.5812 1.6198 -0.0770 -0.0663 0.0209  1044 SER   E O   
16695 C  CB  . SER   E 740 ? 1.3522 1.5367 1.5665 -0.0695 -0.0622 0.0237  1044 SER   E CB  
16696 O  OG  . SER   E 740 ? 1.3598 1.5461 1.5780 -0.0719 -0.0689 0.0223  1044 SER   E OG  
16697 N  N   . GLU   E 741 ? 1.3540 1.5321 1.5751 -0.0744 -0.0560 0.0255  1045 GLU   E N   
16698 C  CA  . GLU   E 741 ? 1.2472 1.4256 1.4786 -0.0784 -0.0560 0.0263  1045 GLU   E CA  
16699 C  C   . GLU   E 741 ? 1.2256 1.4087 1.4672 -0.0813 -0.0627 0.0253  1045 GLU   E C   
16700 O  O   . GLU   E 741 ? 1.2454 1.4260 1.4892 -0.0848 -0.0670 0.0238  1045 GLU   E O   
16701 C  CB  . GLU   E 741 ? 1.2456 1.4264 1.4853 -0.0777 -0.0486 0.0297  1045 GLU   E CB  
16702 C  CG  . GLU   E 741 ? 1.3006 1.4817 1.5525 -0.0819 -0.0475 0.0309  1045 GLU   E CG  
16703 C  CD  . GLU   E 741 ? 1.3475 1.5208 1.5929 -0.0828 -0.0438 0.0311  1045 GLU   E CD  
16704 O  OE1 . GLU   E 741 ? 1.3470 1.5168 1.5851 -0.0796 -0.0375 0.0326  1045 GLU   E OE1 
16705 O  OE2 . GLU   E 741 ? 1.2960 1.4661 1.5429 -0.0866 -0.0474 0.0296  1045 GLU   E OE2 
16706 N  N   . SER   E 742 ? 1.2407 1.4301 1.4877 -0.0797 -0.0639 0.0260  1046 SER   E N   
16707 C  CA  . SER   E 742 ? 1.2835 1.4774 1.5395 -0.0819 -0.0708 0.0249  1046 SER   E CA  
16708 C  C   . SER   E 742 ? 1.2832 1.4721 1.5297 -0.0830 -0.0781 0.0216  1046 SER   E C   
16709 O  O   . SER   E 742 ? 1.2535 1.4417 1.5054 -0.0863 -0.0837 0.0202  1046 SER   E O   
16710 C  CB  . SER   E 742 ? 1.3353 1.5358 1.5955 -0.0791 -0.0709 0.0259  1046 SER   E CB  
16711 O  OG  . SER   E 742 ? 1.3597 1.5625 1.6228 -0.0801 -0.0787 0.0241  1046 SER   E OG  
16712 N  N   . TRP   E 743 ? 1.2996 1.4844 1.5318 -0.0802 -0.0781 0.0203  1047 TRP   E N   
16713 C  CA  . TRP   E 743 ? 1.3202 1.5000 1.5427 -0.0808 -0.0844 0.0174  1047 TRP   E CA  
16714 C  C   . TRP   E 743 ? 1.3177 1.4903 1.5344 -0.0831 -0.0851 0.0159  1047 TRP   E C   
16715 O  O   . TRP   E 743 ? 1.3364 1.5048 1.5485 -0.0846 -0.0911 0.0136  1047 TRP   E O   
16716 C  CB  . TRP   E 743 ? 1.3481 1.5263 1.5585 -0.0771 -0.0837 0.0167  1047 TRP   E CB  
16717 C  CG  . TRP   E 743 ? 1.4054 1.5885 1.6191 -0.0756 -0.0868 0.0169  1047 TRP   E CG  
16718 C  CD1 . TRP   E 743 ? 1.4391 1.6293 1.6634 -0.0746 -0.0849 0.0190  1047 TRP   E CD1 
16719 C  CD2 . TRP   E 743 ? 1.4208 1.6015 1.6270 -0.0747 -0.0923 0.0150  1047 TRP   E CD2 
16720 N  NE1 . TRP   E 743 ? 1.4695 1.6621 1.6934 -0.0732 -0.0891 0.0184  1047 TRP   E NE1 
16721 C  CE2 . TRP   E 743 ? 1.4246 1.6112 1.6372 -0.0733 -0.0937 0.0160  1047 TRP   E CE2 
16722 C  CE3 . TRP   E 743 ? 1.4918 1.6655 1.6860 -0.0748 -0.0959 0.0126  1047 TRP   E CE3 
16723 C  CZ2 . TRP   E 743 ? 1.4730 1.6586 1.6803 -0.0719 -0.0986 0.0147  1047 TRP   E CZ2 
16724 C  CZ3 . TRP   E 743 ? 1.4445 1.6170 1.6332 -0.0735 -0.1004 0.0114  1047 TRP   E CZ3 
16725 C  CH2 . TRP   E 743 ? 1.4620 1.6402 1.6570 -0.0721 -0.1018 0.0125  1047 TRP   E CH2 
16726 N  N   . TYR   E 744 ? 1.2916 1.4621 1.5075 -0.0831 -0.0792 0.0172  1048 TYR   E N   
16727 C  CA  . TYR   E 744 ? 1.2144 1.3779 1.4252 -0.0853 -0.0796 0.0159  1048 TYR   E CA  
16728 C  C   . TYR   E 744 ? 1.1939 1.3582 1.4161 -0.0896 -0.0834 0.0158  1048 TYR   E C   
16729 O  O   . TYR   E 744 ? 1.2380 1.3971 1.4564 -0.0917 -0.0885 0.0135  1048 TYR   E O   
16730 C  CB  . TYR   E 744 ? 1.2069 1.3676 1.4137 -0.0838 -0.0723 0.0174  1048 TYR   E CB  
16731 C  CG  . TYR   E 744 ? 1.1775 1.3314 1.3809 -0.0862 -0.0720 0.0166  1048 TYR   E CG  
16732 C  CD1 . TYR   E 744 ? 1.1722 1.3192 1.3631 -0.0857 -0.0745 0.0141  1048 TYR   E CD1 
16733 C  CD2 . TYR   E 744 ? 1.2186 1.3727 1.4313 -0.0887 -0.0688 0.0184  1048 TYR   E CD2 
16734 C  CE1 . TYR   E 744 ? 1.2546 1.3950 1.4419 -0.0877 -0.0742 0.0133  1048 TYR   E CE1 
16735 C  CE2 . TYR   E 744 ? 1.1800 1.3273 1.3893 -0.0908 -0.0684 0.0177  1048 TYR   E CE2 
16736 C  CZ  . TYR   E 744 ? 1.2415 1.3819 1.4379 -0.0903 -0.0713 0.0151  1048 TYR   E CZ  
16737 O  OH  . TYR   E 744 ? 1.2361 1.3695 1.4287 -0.0922 -0.0709 0.0143  1048 TYR   E OH  
16738 N  N   . ASN   E 745 ? 1.1945 1.3651 1.4313 -0.0908 -0.0808 0.0181  1049 ASN   E N   
16739 C  CA  . ASN   E 745 ? 1.2027 1.3749 1.4528 -0.0951 -0.0842 0.0180  1049 ASN   E CA  
16740 C  C   . ASN   E 745 ? 1.2184 1.3913 1.4704 -0.0964 -0.0935 0.0155  1049 ASN   E C   
16741 O  O   . ASN   E 745 ? 1.2329 1.4023 1.4874 -0.0997 -0.0988 0.0137  1049 ASN   E O   
16742 C  CB  . ASN   E 745 ? 1.1859 1.3657 1.4521 -0.0957 -0.0792 0.0212  1049 ASN   E CB  
16743 C  CG  . ASN   E 745 ? 1.2240 1.4017 1.4888 -0.0948 -0.0700 0.0238  1049 ASN   E CG  
16744 O  OD1 . ASN   E 745 ? 1.1710 1.3415 1.4242 -0.0942 -0.0678 0.0231  1049 ASN   E OD1 
16745 N  ND2 . ASN   E 745 ? 1.2639 1.4476 1.5404 -0.0943 -0.0645 0.0268  1049 ASN   E ND2 
16746 N  N   . LEU   E 746 ? 1.2000 1.3770 1.4505 -0.0938 -0.0958 0.0153  1050 LEU   E N   
16747 C  CA  . LEU   E 746 ? 1.1678 1.3448 1.4187 -0.0944 -0.1046 0.0130  1050 LEU   E CA  
16748 C  C   . LEU   E 746 ? 1.2306 1.3983 1.4673 -0.0948 -0.1095 0.0100  1050 LEU   E C   
16749 O  O   . LEU   E 746 ? 1.2968 1.4616 1.5358 -0.0972 -0.1168 0.0079  1050 LEU   E O   
16750 C  CB  . LEU   E 746 ? 1.1607 1.3422 1.4093 -0.0909 -0.1050 0.0135  1050 LEU   E CB  
16751 C  CG  . LEU   E 746 ? 1.1656 1.3497 1.4192 -0.0911 -0.1133 0.0120  1050 LEU   E CG  
16752 C  CD1 . LEU   E 746 ? 1.1272 1.3031 1.3661 -0.0905 -0.1199 0.0089  1050 LEU   E CD1 
16753 C  CD2 . LEU   E 746 ? 1.2570 1.4453 1.5283 -0.0948 -0.1168 0.0121  1050 LEU   E CD2 
16754 N  N   . LEU   E 747 ? 1.2471 1.4097 1.4690 -0.0923 -0.1058 0.0097  1051 LEU   E N   
16755 C  CA  . LEU   E 747 ? 1.2539 1.4075 1.4614 -0.0922 -0.1095 0.0070  1051 LEU   E CA  
16756 C  C   . LEU   E 747 ? 1.2546 1.4025 1.4618 -0.0951 -0.1089 0.0064  1051 LEU   E C   
16757 O  O   . LEU   E 747 ? 1.2791 1.4196 1.4777 -0.0960 -0.1137 0.0039  1051 LEU   E O   
16758 C  CB  . LEU   E 747 ? 1.2153 1.3660 1.4084 -0.0885 -0.1055 0.0069  1051 LEU   E CB  
16759 C  CG  . LEU   E 747 ? 1.1387 1.2922 1.3280 -0.0856 -0.1072 0.0068  1051 LEU   E CG  
16760 C  CD1 . LEU   E 747 ? 1.1618 1.3121 1.3377 -0.0822 -0.1030 0.0066  1051 LEU   E CD1 
16761 C  CD2 . LEU   E 747 ? 1.1441 1.2939 1.3307 -0.0864 -0.1157 0.0045  1051 LEU   E CD2 
16762 N  N   . LEU   E 748 ? 1.2388 1.3895 1.4544 -0.0964 -0.1030 0.0086  1052 LEU   E N   
16763 C  CA  . LEU   E 748 ? 1.2438 1.3895 1.4613 -0.0996 -0.1027 0.0082  1052 LEU   E CA  
16764 C  C   . LEU   E 748 ? 1.3271 1.4734 1.5556 -0.1034 -0.1101 0.0068  1052 LEU   E C   
16765 O  O   . LEU   E 748 ? 1.4020 1.5412 1.6257 -0.1055 -0.1147 0.0046  1052 LEU   E O   
16766 C  CB  . LEU   E 748 ? 1.2161 1.3645 1.4404 -0.0999 -0.0944 0.0111  1052 LEU   E CB  
16767 C  CG  . LEU   E 748 ? 1.1926 1.3333 1.4085 -0.1005 -0.0909 0.0108  1052 LEU   E CG  
16768 C  CD1 . LEU   E 748 ? 1.2632 1.3985 1.4616 -0.0969 -0.0902 0.0093  1052 LEU   E CD1 
16769 C  CD2 . LEU   E 748 ? 1.1658 1.3086 1.3882 -0.1005 -0.0826 0.0140  1052 LEU   E CD2 
16770 N  N   . ASP   E 749 ? 1.2879 1.4425 1.5312 -0.1043 -0.1115 0.0081  1053 ASP   E N   
16771 C  CA  . ASP   E 749 ? 1.3186 1.4744 1.5731 -0.1076 -0.1196 0.0065  1053 ASP   E CA  
16772 C  C   . ASP   E 749 ? 1.3649 1.5146 1.6077 -0.1065 -0.1283 0.0031  1053 ASP   E C   
16773 O  O   . ASP   E 749 ? 1.4271 1.5709 1.6687 -0.1090 -0.1348 0.0007  1053 ASP   E O   
16774 C  CB  . ASP   E 749 ? 1.2514 1.4178 1.5232 -0.1079 -0.1194 0.0084  1053 ASP   E CB  
16775 N  N   . MET   E 750 ? 1.3494 1.4999 1.5825 -0.1027 -0.1283 0.0030  1054 MET   E N   
16776 C  CA  . MET   E 750 ? 1.3254 1.4697 1.5460 -0.1011 -0.1356 0.0002  1054 MET   E CA  
16777 C  C   . MET   E 750 ? 1.3851 1.5184 1.5903 -0.1012 -0.1368 -0.0020 1054 MET   E C   
16778 O  O   . MET   E 750 ? 1.3706 1.4971 1.5686 -0.1014 -0.1444 -0.0048 1054 MET   E O   
16779 C  CB  . MET   E 750 ? 1.2442 1.3915 1.4575 -0.0969 -0.1332 0.0010  1054 MET   E CB  
16780 C  CG  . MET   E 750 ? 1.3626 1.5031 1.5613 -0.0946 -0.1389 -0.0014 1054 MET   E CG  
16781 S  SD  . MET   E 750 ? 1.4827 1.6267 1.6896 -0.0945 -0.1484 -0.0026 1054 MET   E SD  
16782 C  CE  . MET   E 750 ? 1.5217 1.6577 1.7288 -0.0978 -0.1580 -0.0059 1054 MET   E CE  
16783 N  N   . GLN   E 751 ? 1.4396 1.5706 1.6390 -0.1008 -0.1296 -0.0009 1055 GLN   E N   
16784 C  CA  . GLN   E 751 ? 1.4053 1.5260 1.5904 -0.1007 -0.1302 -0.0029 1055 GLN   E CA  
16785 C  C   . GLN   E 751 ? 1.4597 1.5756 1.6499 -0.1046 -0.1358 -0.0046 1055 GLN   E C   
16786 O  O   . GLN   E 751 ? 1.4785 1.5853 1.6576 -0.1046 -0.1413 -0.0073 1055 GLN   E O   
16787 C  CB  . GLN   E 751 ? 1.3327 1.4525 1.5120 -0.0993 -0.1214 -0.0013 1055 GLN   E CB  
16788 C  CG  . GLN   E 751 ? 1.3367 1.4535 1.5008 -0.0952 -0.1184 -0.0018 1055 GLN   E CG  
16789 C  CD  . GLN   E 751 ? 1.3238 1.4394 1.4827 -0.0938 -0.1104 -0.0006 1055 GLN   E CD  
16790 O  OE1 . GLN   E 751 ? 1.2969 1.4049 1.4448 -0.0933 -0.1098 -0.0020 1055 GLN   E OE1 
16791 N  NE2 . GLN   E 751 ? 1.3374 1.4601 1.5038 -0.0929 -0.1045 0.0020  1055 GLN   E NE2 
16792 N  N   . ASN   E 752 ? 1.5897 1.7109 1.7963 -0.1080 -0.1343 -0.0031 1056 ASN   E N   
16793 C  CA  . ASN   E 752 ? 1.5950 1.7120 1.8083 -0.1121 -0.1397 -0.0046 1056 ASN   E CA  
16794 C  C   . ASN   E 752 ? 1.5941 1.7088 1.8082 -0.1127 -0.1504 -0.0075 1056 ASN   E C   
16795 O  O   . ASN   E 752 ? 1.5966 1.7025 1.8036 -0.1139 -0.1566 -0.0102 1056 ASN   E O   
16796 C  CB  . ASN   E 752 ? 1.5974 1.7215 1.8302 -0.1157 -0.1359 -0.0022 1056 ASN   E CB  
16797 C  CG  . ASN   E 752 ? 1.6867 1.8132 1.9190 -0.1146 -0.1252 0.0009  1056 ASN   E CG  
16798 O  OD1 . ASN   E 752 ? 1.7313 1.8663 1.9756 -0.1146 -0.1201 0.0037  1056 ASN   E OD1 
16799 N  ND2 . ASN   E 752 ? 1.7161 1.8348 1.9344 -0.1134 -0.1219 0.0003  1056 ASN   E ND2 
16800 N  N   . ARG   E 753 ? 1.4832 1.6057 1.7057 -0.1117 -0.1528 -0.0068 1057 ARG   E N   
16801 C  CA  . ARG   E 753 ? 1.4554 1.5759 1.6788 -0.1118 -0.1633 -0.0095 1057 ARG   E CA  
16802 C  C   . ARG   E 753 ? 1.4735 1.5828 1.6754 -0.1089 -0.1678 -0.0123 1057 ARG   E C   
16803 O  O   . ARG   E 753 ? 1.4887 1.5904 1.6867 -0.1100 -0.1764 -0.0153 1057 ARG   E O   
16804 C  CB  . ARG   E 753 ? 1.4389 1.5691 1.6719 -0.1101 -0.1640 -0.0082 1057 ARG   E CB  
16805 N  N   . LEU   E 754 ? 1.4231 1.5306 1.6108 -0.1053 -0.1617 -0.0114 1058 LEU   E N   
16806 C  CA  . LEU   E 754 ? 1.3994 1.4964 1.5666 -0.1023 -0.1645 -0.0136 1058 LEU   E CA  
16807 C  C   . LEU   E 754 ? 1.4314 1.5179 1.5895 -0.1038 -0.1659 -0.0156 1058 LEU   E C   
16808 O  O   . LEU   E 754 ? 1.4502 1.5271 1.5970 -0.1030 -0.1729 -0.0185 1058 LEU   E O   
16809 C  CB  . LEU   E 754 ? 1.3689 1.4672 1.5253 -0.0984 -0.1569 -0.0120 1058 LEU   E CB  
16810 C  CG  . LEU   E 754 ? 1.3881 1.4930 1.5471 -0.0959 -0.1571 -0.0109 1058 LEU   E CG  
16811 C  CD1 . LEU   E 754 ? 1.3412 1.4460 1.4887 -0.0924 -0.1496 -0.0095 1058 LEU   E CD1 
16812 C  CD2 . LEU   E 754 ? 1.4682 1.5672 1.6206 -0.0947 -0.1667 -0.0134 1058 LEU   E CD2 
16813 N  N   . ASN   E 755 ? 1.4496 1.5373 1.6116 -0.1056 -0.1593 -0.0141 1059 ASN   E N   
16814 C  CA  . ASN   E 755 ? 1.4005 1.4783 1.5541 -0.1070 -0.1602 -0.0159 1059 ASN   E CA  
16815 C  C   . ASN   E 755 ? 1.4653 1.5379 1.6236 -0.1101 -0.1701 -0.0186 1059 ASN   E C   
16816 O  O   . ASN   E 755 ? 1.4306 1.4920 1.5762 -0.1098 -0.1744 -0.0212 1059 ASN   E O   
16817 C  CB  . ASN   E 755 ? 1.3878 1.4684 1.5478 -0.1089 -0.1522 -0.0137 1059 ASN   E CB  
16818 C  CG  . ASN   E 755 ? 1.4253 1.5051 1.5735 -0.1055 -0.1437 -0.0124 1059 ASN   E CG  
16819 O  OD1 . ASN   E 755 ? 1.4255 1.5008 1.5593 -0.1020 -0.1441 -0.0135 1059 ASN   E OD1 
16820 N  ND2 . ASN   E 755 ? 1.4032 1.4871 1.5575 -0.1063 -0.1360 -0.0100 1059 ASN   E ND2 
16821 N  N   . LYS   E 756 ? 1.4433 1.5236 1.6198 -0.1129 -0.1739 -0.0180 1060 LYS   E N   
16822 C  CA  . LYS   E 756 ? 1.3825 1.4589 1.5661 -0.1160 -0.1840 -0.0207 1060 LYS   E CA  
16823 C  C   . LYS   E 756 ? 1.4035 1.4710 1.5727 -0.1132 -0.1931 -0.0240 1060 LYS   E C   
16824 O  O   . LYS   E 756 ? 1.4229 1.4817 1.5888 -0.1147 -0.2013 -0.0270 1060 LYS   E O   
16825 C  CB  . LYS   E 756 ? 1.3587 1.4466 1.5658 -0.1190 -0.1856 -0.0193 1060 LYS   E CB  
16826 N  N   . VAL   E 757 ? 1.4329 1.5014 1.5921 -0.1090 -0.1917 -0.0235 1061 VAL   E N   
16827 C  CA  . VAL   E 757 ? 1.4167 1.4779 1.5642 -0.1061 -0.2004 -0.0261 1061 VAL   E CA  
16828 C  C   . VAL   E 757 ? 1.4767 1.5269 1.5997 -0.1019 -0.1983 -0.0272 1061 VAL   E C   
16829 O  O   . VAL   E 757 ? 1.4709 1.5109 1.5809 -0.0997 -0.2060 -0.0299 1061 VAL   E O   
16830 C  CB  . VAL   E 757 ? 1.3563 1.4266 1.5124 -0.1045 -0.2021 -0.0250 1061 VAL   E CB  
16831 C  CG1 . VAL   E 757 ? 1.4343 1.5155 1.6152 -0.1086 -0.2042 -0.0240 1061 VAL   E CG1 
16832 C  CG2 . VAL   E 757 ? 1.4714 1.5477 1.6227 -0.1015 -0.1923 -0.0220 1061 VAL   E CG2 
16833 N  N   . ILE   E 758 ? 1.5502 1.6014 1.6664 -0.1004 -0.1882 -0.0252 1062 ILE   E N   
16834 C  CA  . ILE   E 758 ? 1.5671 1.6089 1.6618 -0.0964 -0.1850 -0.0259 1062 ILE   E CA  
16835 C  C   . ILE   E 758 ? 1.5646 1.5957 1.6499 -0.0975 -0.1860 -0.0279 1062 ILE   E C   
16836 O  O   . ILE   E 758 ? 1.5550 1.5885 1.6499 -0.1009 -0.1836 -0.0272 1062 ILE   E O   
16837 C  CB  . ILE   E 758 ? 1.5683 1.6173 1.6619 -0.0943 -0.1741 -0.0229 1062 ILE   E CB  
16838 C  CG1 . ILE   E 758 ? 1.5409 1.5979 1.6394 -0.0924 -0.1740 -0.0214 1062 ILE   E CG1 
16839 C  CG2 . ILE   E 758 ? 1.5922 1.6321 1.6662 -0.0910 -0.1692 -0.0235 1062 ILE   E CG2 
16840 C  CD1 . ILE   E 758 ? 1.4505 1.5171 1.5539 -0.0914 -0.1642 -0.0183 1062 ILE   E CD1 
16841 N  N   . LYS   E 759 ? 1.4502 1.4687 1.5161 -0.0944 -0.1895 -0.0302 1063 LYS   E N   
16842 C  CA  . LYS   E 759 ? 1.4228 1.4298 1.4778 -0.0948 -0.1909 -0.0323 1063 LYS   E CA  
16843 C  C   . LYS   E 759 ? 1.4708 1.4765 1.5161 -0.0928 -0.1807 -0.0309 1063 LYS   E C   
16844 O  O   . LYS   E 759 ? 1.5294 1.5376 1.5682 -0.0895 -0.1749 -0.0295 1063 LYS   E O   
16845 C  CB  . LYS   E 759 ? 1.3103 1.3035 1.3486 -0.0922 -0.1996 -0.0356 1063 LYS   E CB  
16846 N  N   . SER   E 760 ? 1.4058 1.4078 1.4513 -0.0948 -0.1787 -0.0313 1064 SER   E N   
16847 C  CA  . SER   E 760 ? 1.3487 1.3486 1.3853 -0.0929 -0.1699 -0.0304 1064 SER   E CA  
16848 C  C   . SER   E 760 ? 1.3486 1.3336 1.3669 -0.0910 -0.1728 -0.0332 1064 SER   E C   
16849 O  O   . SER   E 760 ? 1.3599 1.3375 1.3777 -0.0931 -0.1803 -0.0355 1064 SER   E O   
16850 C  CB  . SER   E 760 ? 1.3379 1.3447 1.3877 -0.0962 -0.1645 -0.0285 1064 SER   E CB  
16851 O  OG  . SER   E 760 ? 1.3303 1.3328 1.3702 -0.0944 -0.1576 -0.0283 1064 SER   E OG  
16852 N  N   . VAL   E 761 ? 1.3098 1.2903 1.3134 -0.0869 -0.1668 -0.0330 1065 VAL   E N   
16853 C  CA  . VAL   E 761 ? 1.3133 1.2789 1.2975 -0.0841 -0.1693 -0.0356 1065 VAL   E CA  
16854 C  C   . VAL   E 761 ? 1.3117 1.2707 1.2949 -0.0864 -0.1704 -0.0370 1065 VAL   E C   
16855 O  O   . VAL   E 761 ? 1.3383 1.2849 1.3105 -0.0859 -0.1768 -0.0397 1065 VAL   E O   
16856 C  CB  . VAL   E 761 ? 1.2637 1.2270 1.2342 -0.0794 -0.1615 -0.0348 1065 VAL   E CB  
16857 C  CG1 . VAL   E 761 ? 1.1776 1.1252 1.1276 -0.0761 -0.1638 -0.0373 1065 VAL   E CG1 
16858 C  CG2 . VAL   E 761 ? 1.2979 1.2678 1.2702 -0.0775 -0.1604 -0.0333 1065 VAL   E CG2 
16859 N  N   . GLY   E 762 ? 1.2620 1.2283 1.2560 -0.0887 -0.1645 -0.0352 1066 GLY   E N   
16860 C  CA  . GLY   E 762 ? 1.2597 1.2182 1.2517 -0.0907 -0.1664 -0.0367 1066 GLY   E CA  
16861 C  C   . GLY   E 762 ? 1.2128 1.1756 1.2216 -0.0961 -0.1713 -0.0366 1066 GLY   E C   
16862 O  O   . GLY   E 762 ? 1.1972 1.1548 1.2068 -0.0984 -0.1721 -0.0374 1066 GLY   E O   
16863 N  N   . LYS   E 763 ? 1.2138 1.1858 1.2363 -0.0981 -0.1745 -0.0355 1067 LYS   E N   
16864 C  CA  . LYS   E 763 ? 1.2254 1.2052 1.2680 -0.1032 -0.1766 -0.0345 1067 LYS   E CA  
16865 C  C   . LYS   E 763 ? 1.2428 1.2302 1.2941 -0.1045 -0.1672 -0.0316 1067 LYS   E C   
16866 O  O   . LYS   E 763 ? 1.2172 1.2036 1.2762 -0.1080 -0.1669 -0.0314 1067 LYS   E O   
16867 C  CB  . LYS   E 763 ? 1.1933 1.1641 1.2370 -0.1065 -0.1856 -0.0373 1067 LYS   E CB  
16868 C  CG  . LYS   E 763 ? 1.1854 1.1493 1.2234 -0.1057 -0.1965 -0.0403 1067 LYS   E CG  
16869 C  CD  . LYS   E 763 ? 1.2419 1.1964 1.2812 -0.1090 -0.2053 -0.0432 1067 LYS   E CD  
16870 C  CE  . LYS   E 763 ? 1.2856 1.2324 1.3194 -0.1082 -0.2173 -0.0465 1067 LYS   E CE  
16871 N  NZ  . LYS   E 763 ? 1.3101 1.2463 1.3438 -0.1112 -0.2263 -0.0497 1067 LYS   E NZ  
16872 N  N   . ILE   E 764 ? 1.2424 1.2366 1.2919 -0.1015 -0.1594 -0.0295 1068 ILE   E N   
16873 C  CA  . ILE   E 764 ? 1.1989 1.2008 1.2560 -0.1020 -0.1505 -0.0267 1068 ILE   E CA  
16874 C  C   . ILE   E 764 ? 1.2087 1.2237 1.2831 -0.1039 -0.1491 -0.0242 1068 ILE   E C   
16875 O  O   . ILE   E 764 ? 1.2182 1.2383 1.2926 -0.1018 -0.1496 -0.0237 1068 ILE   E O   
16876 C  CB  . ILE   E 764 ? 1.1579 1.1590 1.2025 -0.0973 -0.1431 -0.0261 1068 ILE   E CB  
16877 C  CG1 . ILE   E 764 ? 1.1675 1.1556 1.1931 -0.0944 -0.1455 -0.0289 1068 ILE   E CG1 
16878 C  CG2 . ILE   E 764 ? 1.1095 1.1146 1.1587 -0.0976 -0.1350 -0.0240 1068 ILE   E CG2 
16879 C  CD1 . ILE   E 764 ? 1.1839 1.1713 1.1973 -0.0895 -0.1394 -0.0286 1068 ILE   E CD1 
16880 N  N   . GLU   E 765 ? 1.1632 1.1833 1.2522 -0.1076 -0.1472 -0.0225 1069 GLU   E N   
16881 C  CA  . GLU   E 765 ? 1.1975 1.2300 1.3030 -0.1092 -0.1452 -0.0199 1069 GLU   E CA  
16882 C  C   . GLU   E 765 ? 1.2285 1.2677 1.3310 -0.1055 -0.1372 -0.0177 1069 GLU   E C   
16883 O  O   . GLU   E 765 ? 1.2141 1.2509 1.3090 -0.1035 -0.1310 -0.0171 1069 GLU   E O   
16884 C  CB  . GLU   E 765 ? 1.2048 1.2408 1.3255 -0.1135 -0.1431 -0.0182 1069 GLU   E CB  
16885 C  CG  . GLU   E 765 ? 1.2441 1.2730 1.3682 -0.1174 -0.1505 -0.0204 1069 GLU   E CG  
16886 C  CD  . GLU   E 765 ? 1.4410 1.4711 1.5766 -0.1212 -0.1467 -0.0187 1069 GLU   E CD  
16887 O  OE1 . GLU   E 765 ? 1.4599 1.4898 1.5914 -0.1198 -0.1386 -0.0169 1069 GLU   E OE1 
16888 O  OE2 . GLU   E 765 ? 1.5268 1.5579 1.6760 -0.1256 -0.1516 -0.0191 1069 GLU   E OE2 
16889 N  N   . HIS   E 766 ? 1.2433 1.2905 1.3514 -0.1045 -0.1378 -0.0167 1070 HIS   E N   
16890 C  CA  . HIS   E 766 ? 1.2328 1.2870 1.3398 -0.1013 -0.1307 -0.0146 1070 HIS   E CA  
16891 C  C   . HIS   E 766 ? 1.1950 1.2538 1.3093 -0.1021 -0.1231 -0.0121 1070 HIS   E C   
16892 O  O   . HIS   E 766 ? 1.2004 1.2590 1.3075 -0.0992 -0.1168 -0.0113 1070 HIS   E O   
16893 C  CB  . HIS   E 766 ? 1.2821 1.3447 1.3974 -0.1009 -0.1330 -0.0137 1070 HIS   E CB  
16894 C  CG  . HIS   E 766 ? 1.2591 1.3297 1.3753 -0.0980 -0.1262 -0.0114 1070 HIS   E CG  
16895 N  ND1 . HIS   E 766 ? 1.2458 1.3246 1.3735 -0.0988 -0.1204 -0.0087 1070 HIS   E ND1 
16896 C  CD2 . HIS   E 766 ? 1.2077 1.2789 1.3150 -0.0943 -0.1247 -0.0115 1070 HIS   E CD2 
16897 C  CE1 . HIS   E 766 ? 1.2102 1.2942 1.3356 -0.0957 -0.1158 -0.0073 1070 HIS   E CE1 
16898 N  NE2 . HIS   E 766 ? 1.1830 1.2628 1.2966 -0.0931 -0.1183 -0.0090 1070 HIS   E NE2 
16899 N  N   . SER   E 767 ? 1.1599 1.2223 1.2885 -0.1059 -0.1235 -0.0108 1071 SER   E N   
16900 C  CA  . SER   E 767 ? 1.1707 1.2369 1.3065 -0.1067 -0.1161 -0.0082 1071 SER   E CA  
16901 C  C   . SER   E 767 ? 1.1257 1.1839 1.2502 -0.1054 -0.1122 -0.0087 1071 SER   E C   
16902 O  O   . SER   E 767 ? 1.0913 1.1514 1.2132 -0.1030 -0.1052 -0.0071 1071 SER   E O   
16903 C  CB  . SER   E 767 ? 1.2568 1.3266 1.4094 -0.1114 -0.1178 -0.0070 1071 SER   E CB  
16904 O  OG  . SER   E 767 ? 1.3776 1.4548 1.5405 -0.1122 -0.1220 -0.0068 1071 SER   E OG  
16905 N  N   . PHE   E 768 ? 1.1644 1.2130 1.2817 -0.1068 -0.1169 -0.0112 1072 PHE   E N   
16906 C  CA  . PHE   E 768 ? 1.1339 1.1740 1.2391 -0.1052 -0.1138 -0.0121 1072 PHE   E CA  
16907 C  C   . PHE   E 768 ? 1.0830 1.1230 1.1759 -0.1002 -0.1099 -0.0124 1072 PHE   E C   
16908 O  O   . PHE   E 768 ? 1.0648 1.1036 1.1529 -0.0980 -0.1040 -0.0116 1072 PHE   E O   
16909 C  CB  . PHE   E 768 ? 1.1314 1.1608 1.2297 -0.1070 -0.1205 -0.0150 1072 PHE   E CB  
16910 C  CG  . PHE   E 768 ? 1.0622 1.0821 1.1469 -0.1051 -0.1180 -0.0163 1072 PHE   E CG  
16911 C  CD1 . PHE   E 768 ? 1.0210 1.0366 1.1084 -0.1074 -0.1158 -0.0156 1072 PHE   E CD1 
16912 C  CD2 . PHE   E 768 ? 1.0681 1.0832 1.1378 -0.1010 -0.1178 -0.0180 1072 PHE   E CD2 
16913 C  CE1 . PHE   E 768 ? 0.9981 1.0047 1.0730 -0.1055 -0.1136 -0.0168 1072 PHE   E CE1 
16914 C  CE2 . PHE   E 768 ? 1.0565 1.0631 1.1144 -0.0990 -0.1155 -0.0192 1072 PHE   E CE2 
16915 C  CZ  . PHE   E 768 ? 1.0453 1.0477 1.1056 -0.1012 -0.1136 -0.0187 1072 PHE   E CZ  
16916 N  N   . TRP   E 769 ? 1.1115 1.1528 1.1997 -0.0982 -0.1131 -0.0135 1073 TRP   E N   
16917 C  CA  . TRP   E 769 ? 1.1320 1.1720 1.2079 -0.0937 -0.1101 -0.0142 1073 TRP   E CA  
16918 C  C   . TRP   E 769 ? 1.0587 1.1071 1.1388 -0.0913 -0.1031 -0.0119 1073 TRP   E C   
16919 O  O   . TRP   E 769 ? 1.0487 1.0953 1.1216 -0.0884 -0.0983 -0.0119 1073 TRP   E O   
16920 C  CB  . TRP   E 769 ? 1.1143 1.1531 1.1845 -0.0924 -0.1153 -0.0159 1073 TRP   E CB  
16921 C  CG  . TRP   E 769 ? 1.0384 1.0794 1.1008 -0.0882 -0.1119 -0.0158 1073 TRP   E CG  
16922 C  CD1 . TRP   E 769 ? 1.0266 1.0735 1.0918 -0.0872 -0.1130 -0.0152 1073 TRP   E CD1 
16923 C  CD2 . TRP   E 769 ? 1.0642 1.1013 1.1153 -0.0846 -0.1073 -0.0165 1073 TRP   E CD2 
16924 N  NE1 . TRP   E 769 ? 1.0452 1.0920 1.1017 -0.0834 -0.1091 -0.0153 1073 TRP   E NE1 
16925 C  CE2 . TRP   E 769 ? 1.0276 1.0687 1.0758 -0.0818 -0.1055 -0.0162 1073 TRP   E CE2 
16926 C  CE3 . TRP   E 769 ? 1.0948 1.1254 1.1384 -0.0835 -0.1044 -0.0174 1073 TRP   E CE3 
16927 C  CZ2 . TRP   E 769 ? 0.9861 1.0255 1.0252 -0.0780 -0.1009 -0.0167 1073 TRP   E CZ2 
16928 C  CZ3 . TRP   E 769 ? 1.1001 1.1292 1.1344 -0.0794 -0.0999 -0.0180 1073 TRP   E CZ3 
16929 C  CH2 . TRP   E 769 ? 1.0085 1.0421 1.0412 -0.0769 -0.0982 -0.0176 1073 TRP   E CH2 
16930 N  N   . ARG   E 770 ? 1.0410 1.0985 1.1324 -0.0923 -0.1029 -0.0100 1074 ARG   E N   
16931 C  CA  . ARG   E 770 ? 1.0418 1.1073 1.1374 -0.0901 -0.0970 -0.0078 1074 ARG   E CA  
16932 C  C   . ARG   E 770 ? 1.0560 1.1233 1.1579 -0.0908 -0.0916 -0.0057 1074 ARG   E C   
16933 O  O   . ARG   E 770 ? 1.0105 1.0834 1.1149 -0.0886 -0.0866 -0.0040 1074 ARG   E O   
16934 C  CB  . ARG   E 770 ? 1.0647 1.1385 1.1694 -0.0906 -0.0991 -0.0067 1074 ARG   E CB  
16935 C  CG  . ARG   E 770 ? 1.0706 1.1427 1.1679 -0.0891 -0.1034 -0.0084 1074 ARG   E CG  
16936 C  CD  . ARG   E 770 ? 1.0360 1.1070 1.1229 -0.0850 -0.0993 -0.0089 1074 ARG   E CD  
16937 N  NE  . ARG   E 770 ? 1.0599 1.1298 1.1401 -0.0832 -0.1023 -0.0101 1074 ARG   E NE  
16938 C  CZ  . ARG   E 770 ? 1.0499 1.1183 1.1209 -0.0798 -0.0993 -0.0107 1074 ARG   E CZ  
16939 N  NH1 . ARG   E 770 ? 0.9783 1.0468 1.0466 -0.0777 -0.0937 -0.0104 1074 ARG   E NH1 
16940 N  NH2 . ARG   E 770 ? 1.0949 1.1612 1.1595 -0.0783 -0.1019 -0.0117 1074 ARG   E NH2 
16941 N  N   . SER   E 771 ? 1.1184 1.1806 1.2226 -0.0937 -0.0926 -0.0058 1075 SER   E N   
16942 C  CA  . SER   E 771 ? 1.1202 1.1823 1.2283 -0.0942 -0.0871 -0.0039 1075 SER   E CA  
16943 C  C   . SER   E 771 ? 1.1046 1.1624 1.2014 -0.0903 -0.0826 -0.0044 1075 SER   E C   
16944 O  O   . SER   E 771 ? 1.0980 1.1500 1.1839 -0.0885 -0.0844 -0.0067 1075 SER   E O   
16945 C  CB  . SER   E 771 ? 1.1827 1.2393 1.2953 -0.0984 -0.0895 -0.0040 1075 SER   E CB  
16946 O  OG  . SER   E 771 ? 1.2181 1.2791 1.3428 -0.1021 -0.0939 -0.0036 1075 SER   E OG  
16947 N  N   . PHE   E 772 ? 1.1111 1.1716 1.2107 -0.0888 -0.0768 -0.0023 1076 PHE   E N   
16948 C  CA  . PHE   E 772 ? 1.1516 1.2098 1.2420 -0.0845 -0.0725 -0.0026 1076 PHE   E CA  
16949 C  C   . PHE   E 772 ? 1.2334 1.2818 1.3152 -0.0844 -0.0724 -0.0041 1076 PHE   E C   
16950 O  O   . PHE   E 772 ? 1.3133 1.3582 1.3976 -0.0861 -0.0703 -0.0028 1076 PHE   E O   
16951 C  CB  . PHE   E 772 ? 1.1320 1.1951 1.2279 -0.0829 -0.0669 0.0001  1076 PHE   E CB  
16952 C  CG  . PHE   E 772 ? 1.1241 1.1846 1.2116 -0.0784 -0.0628 -0.0002 1076 PHE   E CG  
16953 C  CD1 . PHE   E 772 ? 1.1751 1.2281 1.2568 -0.0778 -0.0606 -0.0004 1076 PHE   E CD1 
16954 C  CD2 . PHE   E 772 ? 1.0926 1.1583 1.1784 -0.0748 -0.0613 -0.0004 1076 PHE   E CD2 
16955 C  CE1 . PHE   E 772 ? 1.1516 1.2022 1.2259 -0.0735 -0.0573 -0.0008 1076 PHE   E CE1 
16956 C  CE2 . PHE   E 772 ? 1.0636 1.1272 1.1427 -0.0707 -0.0580 -0.0008 1076 PHE   E CE2 
16957 C  CZ  . PHE   E 772 ? 1.0693 1.1254 1.1426 -0.0699 -0.0562 -0.0011 1076 PHE   E CZ  
16958 N  N   . HIS   E 773 ? 1.2857 1.3295 1.3571 -0.0823 -0.0743 -0.0066 1077 HIS   E N   
16959 C  CA  . HIS   E 773 ? 1.3421 1.3761 1.4049 -0.0824 -0.0752 -0.0083 1077 HIS   E CA  
16960 C  C   . HIS   E 773 ? 1.4232 1.4540 1.4774 -0.0780 -0.0711 -0.0090 1077 HIS   E C   
16961 O  O   . HIS   E 773 ? 1.3354 1.3699 1.3866 -0.0745 -0.0695 -0.0095 1077 HIS   E O   
16962 C  CB  . HIS   E 773 ? 1.3528 1.3822 1.4094 -0.0832 -0.0806 -0.0109 1077 HIS   E CB  
16963 C  CG  . HIS   E 773 ? 1.4064 1.4256 1.4521 -0.0822 -0.0812 -0.0130 1077 HIS   E CG  
16964 N  ND1 . HIS   E 773 ? 1.4527 1.4653 1.4985 -0.0846 -0.0815 -0.0128 1077 HIS   E ND1 
16965 C  CD2 . HIS   E 773 ? 1.4117 1.4262 1.4463 -0.0790 -0.0815 -0.0152 1077 HIS   E CD2 
16966 C  CE1 . HIS   E 773 ? 1.5444 1.5483 1.5790 -0.0828 -0.0822 -0.0150 1077 HIS   E CE1 
16967 N  NE2 . HIS   E 773 ? 1.5246 1.5297 1.5525 -0.0794 -0.0820 -0.0165 1077 HIS   E NE2 
16968 N  N   . THR   E 774 ? 1.5950 1.6184 1.6455 -0.0784 -0.0697 -0.0090 1078 THR   E N   
16969 C  CA  . THR   E 774 ? 1.6682 1.6861 1.7094 -0.0745 -0.0669 -0.0100 1078 THR   E CA  
16970 C  C   . THR   E 774 ? 1.7483 1.7562 1.7845 -0.0766 -0.0684 -0.0110 1078 THR   E C   
16971 O  O   . THR   E 774 ? 1.7363 1.7425 1.7783 -0.0809 -0.0702 -0.0100 1078 THR   E O   
16972 C  CB  . THR   E 774 ? 1.6143 1.6354 1.6579 -0.0719 -0.0617 -0.0080 1078 THR   E CB  
16973 O  OG1 . THR   E 774 ? 1.5088 1.5390 1.5573 -0.0703 -0.0609 -0.0073 1078 THR   E OG1 
16974 C  CG2 . THR   E 774 ? 1.6255 1.6411 1.6597 -0.0674 -0.0593 -0.0093 1078 THR   E CG2 
16975 N  N   . GLU   E 775 ? 1.7065 1.7075 1.7321 -0.0734 -0.0680 -0.0130 1079 GLU   E N   
16976 C  CA  . GLU   E 775 ? 1.6948 1.6855 1.7143 -0.0748 -0.0693 -0.0140 1079 GLU   E CA  
16977 C  C   . GLU   E 775 ? 1.7627 1.7505 1.7864 -0.0768 -0.0665 -0.0117 1079 GLU   E C   
16978 O  O   . GLU   E 775 ? 1.7250 1.7052 1.7472 -0.0797 -0.0681 -0.0120 1079 GLU   E O   
16979 C  CB  . GLU   E 775 ? 1.6581 1.6428 1.6659 -0.0703 -0.0684 -0.0164 1079 GLU   E CB  
16980 C  CG  . GLU   E 775 ? 1.7104 1.6952 1.7156 -0.0660 -0.0637 -0.0157 1079 GLU   E CG  
16981 C  CD  . GLU   E 775 ? 1.6527 1.6474 1.6633 -0.0635 -0.0613 -0.0147 1079 GLU   E CD  
16982 O  OE1 . GLU   E 775 ? 1.5982 1.5990 1.6112 -0.0634 -0.0629 -0.0153 1079 GLU   E OE1 
16983 O  OE2 . GLU   E 775 ? 1.6049 1.6008 1.6169 -0.0614 -0.0578 -0.0132 1079 GLU   E OE2 
16984 N  N   . ARG   E 776 ? 1.8899 1.8832 1.9185 -0.0752 -0.0622 -0.0094 1080 ARG   E N   
16985 C  CA  . ARG   E 776 ? 1.8755 1.8662 1.9079 -0.0766 -0.0586 -0.0068 1080 ARG   E CA  
16986 C  C   . ARG   E 776 ? 1.9156 1.9125 1.9608 -0.0811 -0.0586 -0.0043 1080 ARG   E C   
16987 O  O   . ARG   E 776 ? 1.9437 1.9366 1.9934 -0.0848 -0.0580 -0.0029 1080 ARG   E O   
16988 C  CB  . ARG   E 776 ? 1.8142 1.8060 1.8430 -0.0716 -0.0538 -0.0058 1080 ARG   E CB  
16989 N  N   . LYS   E 777 ? 1.9427 1.9493 1.9945 -0.0809 -0.0592 -0.0038 1081 LYS   E N   
16990 C  CA  . LYS   E 777 ? 1.9274 1.9407 1.9921 -0.0848 -0.0592 -0.0015 1081 LYS   E CA  
16991 C  C   . LYS   E 777 ? 1.8750 1.8946 1.9440 -0.0864 -0.0642 -0.0028 1081 LYS   E C   
16992 O  O   . LYS   E 777 ? 1.8682 1.8906 1.9320 -0.0833 -0.0654 -0.0044 1081 LYS   E O   
16993 C  CB  . LYS   E 777 ? 1.9185 1.9376 1.9877 -0.0825 -0.0538 0.0013  1081 LYS   E CB  
16994 C  CG  . LYS   E 777 ? 1.9820 1.9944 2.0463 -0.0804 -0.0487 0.0028  1081 LYS   E CG  
16995 C  CD  . LYS   E 777 ? 1.9818 1.9987 2.0482 -0.0772 -0.0436 0.0052  1081 LYS   E CD  
16996 C  CE  . LYS   E 777 ? 1.9967 2.0050 2.0561 -0.0748 -0.0388 0.0066  1081 LYS   E CE  
16997 N  NZ  . LYS   E 777 ? 2.0039 2.0148 2.0648 -0.0718 -0.0336 0.0092  1081 LYS   E NZ  
16998 N  N   . THR   E 778 ? 1.6517 1.6734 1.7304 -0.0912 -0.0672 -0.0021 1082 THR   E N   
16999 C  CA  . THR   E 778 ? 1.4967 1.5254 1.5816 -0.0928 -0.0716 -0.0028 1082 THR   E CA  
17000 C  C   . THR   E 778 ? 1.4454 1.4810 1.5448 -0.0960 -0.0702 0.0000  1082 THR   E C   
17001 O  O   . THR   E 778 ? 1.4142 1.4470 1.5206 -0.1001 -0.0706 0.0010  1082 THR   E O   
17002 C  CB  . THR   E 778 ? 1.4734 1.4970 1.5548 -0.0952 -0.0783 -0.0055 1082 THR   E CB  
17003 O  OG1 . THR   E 778 ? 1.4799 1.5015 1.5704 -0.1003 -0.0807 -0.0048 1082 THR   E OG1 
17004 C  CG2 . THR   E 778 ? 1.5285 1.5427 1.5957 -0.0926 -0.0788 -0.0080 1082 THR   E CG2 
17005 N  N   . GLU   E 779 ? 1.3587 1.4032 1.4631 -0.0942 -0.0684 0.0014  1083 GLU   E N   
17006 C  CA  . GLU   E 779 ? 1.3044 1.3569 1.4221 -0.0961 -0.0663 0.0041  1083 GLU   E CA  
17007 C  C   . GLU   E 779 ? 1.2633 1.3236 1.3864 -0.0966 -0.0707 0.0034  1083 GLU   E C   
17008 O  O   . GLU   E 779 ? 1.2772 1.3381 1.3925 -0.0939 -0.0730 0.0015  1083 GLU   E O   
17009 C  CB  . GLU   E 779 ? 1.3191 1.3742 1.4358 -0.0924 -0.0593 0.0065  1083 GLU   E CB  
17010 C  CG  . GLU   E 779 ? 1.5239 1.5708 1.6354 -0.0917 -0.0546 0.0076  1083 GLU   E CG  
17011 C  CD  . GLU   E 779 ? 1.6183 1.6649 1.7233 -0.0866 -0.0487 0.0089  1083 GLU   E CD  
17012 O  OE1 . GLU   E 779 ? 1.5950 1.6484 1.7055 -0.0851 -0.0459 0.0108  1083 GLU   E OE1 
17013 O  OE2 . GLU   E 779 ? 1.6672 1.7063 1.7615 -0.0839 -0.0472 0.0079  1083 GLU   E OE2 
17014 N  N   . PRO   E 780 ? 1.2708 1.3370 1.4075 -0.1000 -0.0720 0.0049  1084 PRO   E N   
17015 C  CA  . PRO   E 780 ? 1.2266 1.2996 1.3684 -0.1006 -0.0770 0.0040  1084 PRO   E CA  
17016 C  C   . PRO   E 780 ? 1.1877 1.2671 1.3269 -0.0964 -0.0743 0.0047  1084 PRO   E C   
17017 O  O   . PRO   E 780 ? 1.2164 1.2963 1.3525 -0.0934 -0.0685 0.0062  1084 PRO   E O   
17018 C  CB  . PRO   E 780 ? 1.2384 1.3167 1.3968 -0.1047 -0.0774 0.0060  1084 PRO   E CB  
17019 C  CG  . PRO   E 780 ? 1.2534 1.3313 1.4147 -0.1042 -0.0695 0.0090  1084 PRO   E CG  
17020 C  CD  . PRO   E 780 ? 1.2808 1.3488 1.4292 -0.1028 -0.0679 0.0078  1084 PRO   E CD  
17021 N  N   . ALA   E 781 ? 1.1195 1.2035 1.2601 -0.0962 -0.0787 0.0036  1085 ALA   E N   
17022 C  CA  . ALA   E 781 ? 1.0931 1.1833 1.2322 -0.0926 -0.0763 0.0043  1085 ALA   E CA  
17023 C  C   . ALA   E 781 ? 1.0965 1.1948 1.2483 -0.0932 -0.0731 0.0073  1085 ALA   E C   
17024 O  O   . ALA   E 781 ? 1.1250 1.2251 1.2880 -0.0967 -0.0734 0.0086  1085 ALA   E O   
17025 C  CB  . ALA   E 781 ? 1.0548 1.1461 1.1891 -0.0916 -0.0816 0.0022  1085 ALA   E CB  
17026 N  N   . THR   E 782 ? 1.0957 1.1991 1.2461 -0.0897 -0.0701 0.0082  1086 THR   E N   
17027 C  CA  . THR   E 782 ? 1.1353 1.2460 1.2959 -0.0894 -0.0664 0.0110  1086 THR   E CA  
17028 C  C   . THR   E 782 ? 1.1371 1.2523 1.2934 -0.0853 -0.0650 0.0111  1086 THR   E C   
17029 O  O   . THR   E 782 ? 1.1481 1.2600 1.2936 -0.0823 -0.0643 0.0096  1086 THR   E O   
17030 C  CB  . THR   E 782 ? 1.1205 1.2289 1.2832 -0.0893 -0.0599 0.0134  1086 THR   E CB  
17031 O  OG1 . THR   E 782 ? 1.1623 1.2774 1.3334 -0.0881 -0.0558 0.0162  1086 THR   E OG1 
17032 C  CG2 . THR   E 782 ? 1.0114 1.1134 1.1608 -0.0856 -0.0567 0.0126  1086 THR   E CG2 
17033 N  N   . GLY   E 783 ? 1.2051 1.3280 1.3704 -0.0853 -0.0647 0.0127  1087 GLY   E N   
17034 C  CA  . GLY   E 783 ? 1.2498 1.3768 1.4118 -0.0814 -0.0628 0.0131  1087 GLY   E CA  
17035 C  C   . GLY   E 783 ? 1.2805 1.4070 1.4347 -0.0800 -0.0671 0.0106  1087 GLY   E C   
17036 O  O   . GLY   E 783 ? 1.2704 1.3996 1.4209 -0.0768 -0.0657 0.0106  1087 GLY   E O   
17037 N  N   . PHE   E 784 ? 1.2146 1.3373 1.3661 -0.0823 -0.0723 0.0085  1088 PHE   E N   
17038 C  CA  . PHE   E 784 ? 1.1686 1.2895 1.3119 -0.0811 -0.0763 0.0062  1088 PHE   E CA  
17039 C  C   . PHE   E 784 ? 1.1932 1.3148 1.3410 -0.0840 -0.0827 0.0052  1088 PHE   E C   
17040 O  O   . PHE   E 784 ? 1.2143 1.3351 1.3690 -0.0873 -0.0849 0.0055  1088 PHE   E O   
17041 C  CB  . PHE   E 784 ? 1.0978 1.2110 1.2292 -0.0800 -0.0760 0.0042  1088 PHE   E CB  
17042 C  CG  . PHE   E 784 ? 1.0875 1.2002 1.2125 -0.0762 -0.0711 0.0043  1088 PHE   E CG  
17043 C  CD1 . PHE   E 784 ? 1.0615 1.1751 1.1802 -0.0733 -0.0713 0.0031  1088 PHE   E CD1 
17044 C  CD2 . PHE   E 784 ? 1.0548 1.1658 1.1799 -0.0753 -0.0665 0.0055  1088 PHE   E CD2 
17045 C  CE1 . PHE   E 784 ? 1.0408 1.1541 1.1546 -0.0699 -0.0673 0.0030  1088 PHE   E CE1 
17046 C  CE2 . PHE   E 784 ? 1.0384 1.1486 1.1574 -0.0715 -0.0628 0.0053  1088 PHE   E CE2 
17047 C  CZ  . PHE   E 784 ? 1.0201 1.1318 1.1341 -0.0689 -0.0634 0.0040  1088 PHE   E CZ  
17048 N  N   . ILE   E 785 ? 1.2652 1.3879 1.4088 -0.0826 -0.0859 0.0041  1089 ILE   E N   
17049 C  CA  . ILE   E 785 ? 1.2559 1.3788 1.4023 -0.0845 -0.0925 0.0030  1089 ILE   E CA  
17050 C  C   . ILE   E 785 ? 1.2721 1.3888 1.4058 -0.0830 -0.0957 0.0006  1089 ILE   E C   
17051 O  O   . ILE   E 785 ? 1.2551 1.3728 1.3829 -0.0802 -0.0942 0.0005  1089 ILE   E O   
17052 C  CB  . ILE   E 785 ? 1.2440 1.3751 1.3996 -0.0841 -0.0933 0.0046  1089 ILE   E CB  
17053 C  CG1 . ILE   E 785 ? 1.2604 1.3968 1.4298 -0.0863 -0.0910 0.0068  1089 ILE   E CG1 
17054 C  CG2 . ILE   E 785 ? 1.2336 1.3637 1.3881 -0.0848 -0.1004 0.0030  1089 ILE   E CG2 
17055 C  CD1 . ILE   E 785 ? 1.3146 1.4592 1.4926 -0.0850 -0.0890 0.0089  1089 ILE   E CD1 
17056 N  N   . ASP   E 786 ? 1.2047 1.3145 1.3340 -0.0850 -0.1001 -0.0013 1090 ASP   E N   
17057 C  CA  . ASP   E 786 ? 1.2263 1.3287 1.3424 -0.0835 -0.1030 -0.0037 1090 ASP   E CA  
17058 C  C   . ASP   E 786 ? 1.2168 1.3212 1.3314 -0.0822 -0.1065 -0.0039 1090 ASP   E C   
17059 O  O   . ASP   E 786 ? 1.2397 1.3420 1.3552 -0.0836 -0.1128 -0.0050 1090 ASP   E O   
17060 C  CB  . ASP   E 786 ? 1.2164 1.3109 1.3291 -0.0860 -0.1077 -0.0056 1090 ASP   E CB  
17061 C  CG  . ASP   E 786 ? 1.2055 1.2909 1.3029 -0.0841 -0.1095 -0.0079 1090 ASP   E CG  
17062 O  OD1 . ASP   E 786 ? 1.2019 1.2872 1.2918 -0.0811 -0.1073 -0.0081 1090 ASP   E OD1 
17063 O  OD2 . ASP   E 786 ? 1.1671 1.2452 1.2601 -0.0857 -0.1129 -0.0096 1090 ASP   E OD2 
17064 N  N   . GLY   E 787 ? 1.1269 1.2351 1.2392 -0.0793 -0.1025 -0.0030 1091 GLY   E N   
17065 C  CA  . GLY   E 787 ? 1.1285 1.2388 1.2396 -0.0779 -0.1051 -0.0030 1091 GLY   E CA  
17066 C  C   . GLY   E 787 ? 1.1138 1.2160 1.2139 -0.0774 -0.1102 -0.0051 1091 GLY   E C   
17067 O  O   . GLY   E 787 ? 1.1154 1.2181 1.2154 -0.0769 -0.1144 -0.0053 1091 GLY   E O   
17068 N  N   . ASP   E 788 ? 1.1171 1.2112 1.2072 -0.0771 -0.1099 -0.0068 1092 ASP   E N   
17069 C  CA  . ASP   E 788 ? 1.0733 1.1583 1.1522 -0.0766 -0.1149 -0.0089 1092 ASP   E CA  
17070 C  C   . ASP   E 788 ? 1.1226 1.2062 1.2071 -0.0794 -0.1224 -0.0098 1092 ASP   E C   
17071 O  O   . ASP   E 788 ? 1.1931 1.2730 1.2732 -0.0789 -0.1281 -0.0109 1092 ASP   E O   
17072 C  CB  . ASP   E 788 ? 1.0853 1.1620 1.1530 -0.0757 -0.1126 -0.0104 1092 ASP   E CB  
17073 C  CG  . ASP   E 788 ? 1.1180 1.1954 1.1798 -0.0727 -0.1059 -0.0099 1092 ASP   E CG  
17074 O  OD1 . ASP   E 788 ? 1.1068 1.1846 1.1643 -0.0706 -0.1051 -0.0097 1092 ASP   E OD1 
17075 O  OD2 . ASP   E 788 ? 1.1165 1.1940 1.1783 -0.0725 -0.1014 -0.0099 1092 ASP   E OD2 
17076 N  N   . LEU   E 789 ? 1.1422 1.2283 1.2363 -0.0824 -0.1225 -0.0094 1093 LEU   E N   
17077 C  CA  . LEU   E 789 ? 1.1768 1.2628 1.2790 -0.0854 -0.1294 -0.0101 1093 LEU   E CA  
17078 C  C   . LEU   E 789 ? 1.1757 1.2689 1.2871 -0.0854 -0.1326 -0.0091 1093 LEU   E C   
17079 O  O   . LEU   E 789 ? 1.2071 1.2976 1.3187 -0.0861 -0.1401 -0.0106 1093 LEU   E O   
17080 C  CB  . LEU   E 789 ? 1.2130 1.3019 1.3259 -0.0886 -0.1274 -0.0092 1093 LEU   E CB  
17081 C  CG  . LEU   E 789 ? 1.2600 1.3481 1.3820 -0.0922 -0.1344 -0.0102 1093 LEU   E CG  
17082 C  CD1 . LEU   E 789 ? 1.2763 1.3528 1.3861 -0.0922 -0.1406 -0.0132 1093 LEU   E CD1 
17083 C  CD2 . LEU   E 789 ? 1.2858 1.3776 1.4192 -0.0951 -0.1307 -0.0088 1093 LEU   E CD2 
17084 N  N   . ILE   E 790 ? 1.1843 1.2862 1.3025 -0.0843 -0.1273 -0.0068 1094 ILE   E N   
17085 C  CA  . ILE   E 790 ? 1.1870 1.2963 1.3147 -0.0841 -0.1295 -0.0057 1094 ILE   E CA  
17086 C  C   . ILE   E 790 ? 1.2294 1.3345 1.3467 -0.0815 -0.1334 -0.0068 1094 ILE   E C   
17087 O  O   . ILE   E 790 ? 1.2763 1.3828 1.3980 -0.0818 -0.1395 -0.0073 1094 ILE   E O   
17088 C  CB  . ILE   E 790 ? 1.1689 1.2874 1.3046 -0.0832 -0.1223 -0.0030 1094 ILE   E CB  
17089 C  CG1 . ILE   E 790 ? 1.1305 1.2519 1.2747 -0.0854 -0.1180 -0.0017 1094 ILE   E CG1 
17090 C  CG2 . ILE   E 790 ? 1.1957 1.3220 1.3415 -0.0829 -0.1246 -0.0017 1094 ILE   E CG2 
17091 C  CD1 . ILE   E 790 ? 1.1838 1.3101 1.3433 -0.0886 -0.1211 -0.0010 1094 ILE   E CD1 
17092 N  N   . GLU   E 791 ? 1.2732 1.3734 1.3771 -0.0787 -0.1296 -0.0071 1095 GLU   E N   
17093 C  CA  . GLU   E 791 ? 1.2810 1.3763 1.3739 -0.0759 -0.1323 -0.0079 1095 GLU   E CA  
17094 C  C   . GLU   E 791 ? 1.3232 1.4085 1.4071 -0.0761 -0.1400 -0.0104 1095 GLU   E C   
17095 O  O   . GLU   E 791 ? 1.3840 1.4653 1.4608 -0.0742 -0.1441 -0.0112 1095 GLU   E O   
17096 C  CB  . GLU   E 791 ? 1.2574 1.3496 1.3388 -0.0731 -0.1257 -0.0076 1095 GLU   E CB  
17097 C  CG  . GLU   E 791 ? 1.3067 1.4077 1.3946 -0.0718 -0.1195 -0.0054 1095 GLU   E CG  
17098 C  CD  . GLU   E 791 ? 1.3418 1.4398 1.4196 -0.0692 -0.1133 -0.0053 1095 GLU   E CD  
17099 O  OE1 . GLU   E 791 ? 1.3290 1.4180 1.3939 -0.0678 -0.1140 -0.0068 1095 GLU   E OE1 
17100 O  OE2 . GLU   E 791 ? 1.3328 1.4373 1.4158 -0.0683 -0.1078 -0.0038 1095 GLU   E OE2 
17101 N  N   . SER   E 792 ? 1.3090 1.3896 1.3924 -0.0783 -0.1421 -0.0118 1096 SER   E N   
17102 C  CA  . SER   E 792 ? 1.3091 1.3800 1.3846 -0.0786 -0.1502 -0.0144 1096 SER   E CA  
17103 C  C   . SER   E 792 ? 1.3692 1.4439 1.4560 -0.0803 -0.1582 -0.0149 1096 SER   E C   
17104 O  O   . SER   E 792 ? 1.4594 1.5262 1.5392 -0.0798 -0.1660 -0.0171 1096 SER   E O   
17105 C  CB  . SER   E 792 ? 1.2689 1.3335 1.3410 -0.0804 -0.1503 -0.0158 1096 SER   E CB  
17106 O  OG  . SER   E 792 ? 1.3012 1.3738 1.3887 -0.0837 -0.1481 -0.0146 1096 SER   E OG  
17107 N  N   . PHE   E 793 ? 1.3913 1.4774 1.4952 -0.0822 -0.1565 -0.0130 1097 PHE   E N   
17108 C  CA  . PHE   E 793 ? 1.4391 1.5301 1.5552 -0.0836 -0.1636 -0.0132 1097 PHE   E CA  
17109 C  C   . PHE   E 793 ? 1.5172 1.6051 1.6249 -0.0803 -0.1681 -0.0139 1097 PHE   E C   
17110 O  O   . PHE   E 793 ? 1.5791 1.6640 1.6881 -0.0806 -0.1769 -0.0156 1097 PHE   E O   
17111 C  CB  . PHE   E 793 ? 1.4592 1.5635 1.5940 -0.0854 -0.1591 -0.0106 1097 PHE   E CB  
17112 C  CG  . PHE   E 793 ? 1.5285 1.6399 1.6751 -0.0853 -0.1640 -0.0101 1097 PHE   E CG  
17113 C  CD1 . PHE   E 793 ? 1.5358 1.6511 1.6802 -0.0823 -0.1618 -0.0087 1097 PHE   E CD1 
17114 C  CD2 . PHE   E 793 ? 1.5674 1.6820 1.7282 -0.0883 -0.1707 -0.0110 1097 PHE   E CD2 
17115 C  CE1 . PHE   E 793 ? 1.5522 1.6740 1.7074 -0.0820 -0.1663 -0.0083 1097 PHE   E CE1 
17116 C  CE2 . PHE   E 793 ? 1.5693 1.6909 1.7418 -0.0880 -0.1752 -0.0106 1097 PHE   E CE2 
17117 C  CZ  . PHE   E 793 ? 1.5522 1.6773 1.7215 -0.0848 -0.1730 -0.0092 1097 PHE   E CZ  
17118 N  N   . LEU   E 794 ? 1.4457 1.5338 1.5449 -0.0773 -0.1623 -0.0125 1098 LEU   E N   
17119 C  CA  . LEU   E 794 ? 1.4645 1.5492 1.5550 -0.0741 -0.1657 -0.0128 1098 LEU   E CA  
17120 C  C   . LEU   E 794 ? 1.5315 1.6030 1.6069 -0.0726 -0.1731 -0.0156 1098 LEU   E C   
17121 O  O   . LEU   E 794 ? 1.6176 1.6859 1.6894 -0.0707 -0.1796 -0.0165 1098 LEU   E O   
17122 C  CB  . LEU   E 794 ? 1.4254 1.5107 1.5075 -0.0712 -0.1575 -0.0111 1098 LEU   E CB  
17123 C  CG  . LEU   E 794 ? 1.4216 1.5194 1.5173 -0.0718 -0.1513 -0.0084 1098 LEU   E CG  
17124 C  CD1 . LEU   E 794 ? 1.3844 1.4823 1.4719 -0.0689 -0.1442 -0.0069 1098 LEU   E CD1 
17125 C  CD2 . LEU   E 794 ? 1.4346 1.5396 1.5433 -0.0723 -0.1567 -0.0079 1098 LEU   E CD2 
17126 N  N   . ASP   E 795 ? 1.5160 1.5790 1.5819 -0.0731 -0.1725 -0.0171 1099 ASP   E N   
17127 C  CA  . ASP   E 795 ? 1.5702 1.6192 1.6191 -0.0711 -0.1787 -0.0197 1099 ASP   E CA  
17128 C  C   . ASP   E 795 ? 1.6294 1.6743 1.6828 -0.0738 -0.1874 -0.0222 1099 ASP   E C   
17129 O  O   . ASP   E 795 ? 1.6888 1.7233 1.7306 -0.0736 -0.1890 -0.0241 1099 ASP   E O   
17130 C  CB  . ASP   E 795 ? 1.5934 1.6340 1.6258 -0.0690 -0.1720 -0.0198 1099 ASP   E CB  
17131 C  CG  . ASP   E 795 ? 1.6902 1.7171 1.7022 -0.0652 -0.1753 -0.0213 1099 ASP   E CG  
17132 O  OD1 . ASP   E 795 ? 1.6243 1.6415 1.6289 -0.0650 -0.1832 -0.0239 1099 ASP   E OD1 
17133 O  OD2 . ASP   E 795 ? 1.7568 1.7824 1.7601 -0.0622 -0.1700 -0.0199 1099 ASP   E OD2 
17134 N  N   . ILE   E 796 ? 1.6406 1.6934 1.7109 -0.0763 -0.1932 -0.0223 1100 ILE   E N   
17135 C  CA  . ILE   E 796 ? 1.7343 1.7830 1.8094 -0.0788 -0.2025 -0.0249 1100 ILE   E CA  
17136 C  C   . ILE   E 796 ? 1.8466 1.8940 1.9240 -0.0775 -0.2127 -0.0265 1100 ILE   E C   
17137 O  O   . ILE   E 796 ? 1.8573 1.9073 1.9325 -0.0747 -0.2121 -0.0254 1100 ILE   E O   
17138 C  CB  . ILE   E 796 ? 1.7078 1.7663 1.8029 -0.0836 -0.2004 -0.0240 1100 ILE   E CB  
17139 C  CG1 . ILE   E 796 ? 1.7467 1.8199 1.8612 -0.0848 -0.1980 -0.0215 1100 ILE   E CG1 
17140 C  CG2 . ILE   E 796 ? 1.6245 1.6827 1.7158 -0.0844 -0.1911 -0.0228 1100 ILE   E CG2 
17141 C  CD1 . ILE   E 796 ? 1.7107 1.7938 1.8445 -0.0892 -0.1941 -0.0200 1100 ILE   E CD1 
17142 N  N   . SER   E 797 ? 2.0440 2.0872 2.1259 -0.0794 -0.2226 -0.0292 1101 SER   E N   
17143 C  CA  . SER   E 797 ? 2.0352 2.0761 2.1188 -0.0780 -0.2336 -0.0313 1101 SER   E CA  
17144 C  C   . SER   E 797 ? 2.0272 2.0833 2.1342 -0.0801 -0.2344 -0.0297 1101 SER   E C   
17145 O  O   . SER   E 797 ? 2.0492 2.1157 2.1741 -0.0840 -0.2303 -0.0282 1101 SER   E O   
17146 C  CB  . SER   E 797 ? 2.0424 2.0733 2.1233 -0.0794 -0.2444 -0.0350 1101 SER   E CB  
17147 O  OG  . SER   E 797 ? 2.0581 2.0982 2.1615 -0.0844 -0.2473 -0.0353 1101 SER   E OG  
17148 N  N   . ARG   E 798 ? 1.9201 1.9769 2.0264 -0.0772 -0.2398 -0.0300 1102 ARG   E N   
17149 C  CA  . ARG   E 798 ? 1.8893 1.9604 2.0168 -0.0785 -0.2401 -0.0283 1102 ARG   E CA  
17150 C  C   . ARG   E 798 ? 1.8974 1.9763 2.0478 -0.0832 -0.2455 -0.0293 1102 ARG   E C   
17151 O  O   . ARG   E 798 ? 1.8936 1.9863 2.0636 -0.0854 -0.2407 -0.0269 1102 ARG   E O   
17152 C  CB  . ARG   E 798 ? 1.8466 1.9150 1.9679 -0.0743 -0.2466 -0.0290 1102 ARG   E CB  
17153 N  N   . PRO   E 799 ? 1.8537 1.9247 2.0032 -0.0848 -0.2548 -0.0326 1103 PRO   E N   
17154 C  CA  . PRO   E 799 ? 1.8405 1.9194 2.0129 -0.0900 -0.2577 -0.0331 1103 PRO   E CA  
17155 C  C   . PRO   E 799 ? 1.8421 1.9266 2.0211 -0.0935 -0.2467 -0.0306 1103 PRO   E C   
17156 O  O   . PRO   E 799 ? 1.8302 1.9275 2.0307 -0.0968 -0.2427 -0.0285 1103 PRO   E O   
17157 C  CB  . PRO   E 799 ? 1.8656 1.9319 2.0307 -0.0904 -0.2698 -0.0375 1103 PRO   E CB  
17158 C  CG  . PRO   E 799 ? 1.9231 1.9780 2.0671 -0.0849 -0.2760 -0.0393 1103 PRO   E CG  
17159 C  CD  . PRO   E 799 ? 1.8883 1.9434 2.0181 -0.0817 -0.2646 -0.0362 1103 PRO   E CD  
17160 N  N   . LYS   E 800 ? 1.9182 1.9934 2.0793 -0.0927 -0.2414 -0.0306 1104 LYS   E N   
17161 C  CA  . LYS   E 800 ? 1.8538 1.9336 2.0198 -0.0955 -0.2310 -0.0283 1104 LYS   E CA  
17162 C  C   . LYS   E 800 ? 1.8345 1.9273 2.0104 -0.0952 -0.2207 -0.0244 1104 LYS   E C   
17163 O  O   . LYS   E 800 ? 1.8364 1.9383 2.0284 -0.0986 -0.2149 -0.0223 1104 LYS   E O   
17164 C  CB  . LYS   E 800 ? 1.8116 1.8791 1.9550 -0.0937 -0.2271 -0.0290 1104 LYS   E CB  
17165 N  N   . MET   E 801 ? 1.8267 1.9198 1.9931 -0.0911 -0.2184 -0.0233 1105 MET   E N   
17166 C  CA  . MET   E 801 ? 1.8144 1.9196 1.9906 -0.0905 -0.2100 -0.0198 1105 MET   E CA  
17167 C  C   . MET   E 801 ? 1.8659 1.9835 2.0668 -0.0931 -0.2128 -0.0190 1105 MET   E C   
17168 O  O   . MET   E 801 ? 1.8561 1.9837 2.0716 -0.0954 -0.2053 -0.0163 1105 MET   E O   
17169 C  CB  . MET   E 801 ? 1.7535 1.8561 1.9157 -0.0857 -0.2091 -0.0192 1105 MET   E CB  
17170 C  CG  . MET   E 801 ? 1.7662 1.8554 1.9035 -0.0826 -0.2082 -0.0205 1105 MET   E CG  
17171 S  SD  . MET   E 801 ? 1.7102 1.7989 1.8336 -0.0777 -0.2017 -0.0184 1105 MET   E SD  
17172 C  CE  . MET   E 801 ? 1.6085 1.7140 1.7521 -0.0795 -0.1929 -0.0148 1105 MET   E CE  
17173 N  N   . GLN   E 802 ? 1.8341 1.9509 2.0401 -0.0926 -0.2235 -0.0212 1106 GLN   E N   
17174 C  CA  . GLN   E 802 ? 1.8232 1.9515 2.0536 -0.0950 -0.2269 -0.0207 1106 GLN   E CA  
17175 C  C   . GLN   E 802 ? 1.8079 1.9407 2.0553 -0.1003 -0.2254 -0.0205 1106 GLN   E C   
17176 O  O   . GLN   E 802 ? 1.8075 1.9521 2.0764 -0.1026 -0.2228 -0.0186 1106 GLN   E O   
17177 C  CB  . GLN   E 802 ? 1.7829 1.9076 2.0142 -0.0934 -0.2401 -0.0239 1106 GLN   E CB  
17178 N  N   . GLU   E 803 ? 1.8852 2.0084 2.1232 -0.1021 -0.2265 -0.0222 1107 GLU   E N   
17179 C  CA  . GLU   E 803 ? 1.8833 2.0091 2.1356 -0.1072 -0.2250 -0.0221 1107 GLU   E CA  
17180 C  C   . GLU   E 803 ? 1.8977 2.0283 2.1517 -0.1084 -0.2119 -0.0186 1107 GLU   E C   
17181 O  O   . GLU   E 803 ? 1.8560 1.9952 2.1288 -0.1119 -0.2076 -0.0167 1107 GLU   E O   
17182 C  CB  . GLU   E 803 ? 1.8659 1.9784 2.1067 -0.1084 -0.2324 -0.0256 1107 GLU   E CB  
17183 N  N   . VAL   E 804 ? 1.8798 2.0045 2.1142 -0.1055 -0.2055 -0.0178 1108 VAL   E N   
17184 C  CA  . VAL   E 804 ? 1.8783 2.0067 2.1125 -0.1061 -0.1936 -0.0147 1108 VAL   E CA  
17185 C  C   . VAL   E 804 ? 1.9008 2.0418 2.1477 -0.1053 -0.1863 -0.0113 1108 VAL   E C   
17186 O  O   . VAL   E 804 ? 1.8701 2.0150 2.1191 -0.1058 -0.1765 -0.0086 1108 VAL   E O   
17187 C  CB  . VAL   E 804 ? 1.8704 1.9897 2.0809 -0.1028 -0.1889 -0.0149 1108 VAL   E CB  
17188 C  CG1 . VAL   E 804 ? 1.8293 1.9355 2.0259 -0.1032 -0.1953 -0.0182 1108 VAL   E CG1 
17189 C  CG2 . VAL   E 804 ? 1.8490 1.9687 2.0492 -0.0982 -0.1886 -0.0144 1108 VAL   E CG2 
17190 N  N   . VAL   E 805 ? 2.1166 2.2635 2.3715 -0.1038 -0.1909 -0.0113 1109 VAL   E N   
17191 C  CA  . VAL   E 805 ? 2.1130 2.2717 2.3801 -0.1027 -0.1845 -0.0081 1109 VAL   E CA  
17192 C  C   . VAL   E 805 ? 2.1168 2.2856 2.4093 -0.1060 -0.1865 -0.0074 1109 VAL   E C   
17193 O  O   . VAL   E 805 ? 2.1097 2.2886 2.4143 -0.1055 -0.1804 -0.0045 1109 VAL   E O   
17194 C  CB  . VAL   E 805 ? 2.1108 2.2697 2.3685 -0.0982 -0.1865 -0.0082 1109 VAL   E CB  
17195 C  CG1 . VAL   E 805 ? 2.0964 2.2458 2.3302 -0.0951 -0.1834 -0.0086 1109 VAL   E CG1 
17196 C  CG2 . VAL   E 805 ? 2.1122 2.2695 2.3737 -0.0977 -0.1986 -0.0110 1109 VAL   E CG2 
17197 N  N   . ALA   E 806 ? 1.8902 2.0564 2.1913 -0.1093 -0.1947 -0.0098 1110 ALA   E N   
17198 C  CA  . ALA   E 806 ? 1.7650 1.9409 2.0917 -0.1127 -0.1968 -0.0093 1110 ALA   E CA  
17199 C  C   . ALA   E 806 ? 1.7344 1.9175 2.0735 -0.1152 -0.1854 -0.0056 1110 ALA   E C   
17200 O  O   . ALA   E 806 ? 1.7922 1.9708 2.1206 -0.1153 -0.1779 -0.0044 1110 ALA   E O   
17201 C  CB  . ALA   E 806 ? 1.6803 1.8506 2.0128 -0.1162 -0.2073 -0.0128 1110 ALA   E CB  
17202 N  N   . ASN   E 807 ? 1.6576 1.8519 2.0195 -0.1168 -0.1840 -0.0039 1111 ASN   E N   
17203 C  CA  . ASN   E 807 ? 1.6136 1.8153 1.9900 -0.1192 -0.1733 -0.0002 1111 ASN   E CA  
17204 C  C   . ASN   E 807 ? 1.6187 1.8202 1.9820 -0.1161 -0.1618 0.0029  1111 ASN   E C   
17205 O  O   . ASN   E 807 ? 1.5757 1.7751 1.9366 -0.1176 -0.1537 0.0047  1111 ASN   E O   
17206 C  CB  . ASN   E 807 ? 1.5333 1.7309 1.9167 -0.1242 -0.1737 -0.0010 1111 ASN   E CB  
17207 C  CG  . ASN   E 807 ? 1.5033 1.7051 1.9083 -0.1280 -0.1826 -0.0029 1111 ASN   E CG  
17208 O  OD1 . ASN   E 807 ? 1.5331 1.7375 1.9426 -0.1266 -0.1915 -0.0050 1111 ASN   E OD1 
17209 N  ND2 . ASN   E 807 ? 1.4430 1.6453 1.8617 -0.1329 -0.1803 -0.0023 1111 ASN   E ND2 
17210 N  N   . LEU   E 808 ? 1.6265 1.8303 1.9816 -0.1118 -0.1612 0.0034  1112 LEU   E N   
17211 C  CA  . LEU   E 808 ? 1.6275 1.8314 1.9708 -0.1086 -0.1512 0.0061  1112 LEU   E CA  
17212 C  C   . LEU   E 808 ? 1.7282 1.9381 2.0713 -0.1045 -0.1512 0.0070  1112 LEU   E C   
17213 O  O   . LEU   E 808 ? 1.7305 1.9396 2.0720 -0.1031 -0.1600 0.0048  1112 LEU   E O   
17214 C  CB  . LEU   E 808 ? 1.6041 1.7968 1.9240 -0.1073 -0.1507 0.0046  1112 LEU   E CB  
17215 C  CG  . LEU   E 808 ? 1.5706 1.7624 1.8805 -0.1053 -0.1397 0.0072  1112 LEU   E CG  
17216 C  CD1 . LEU   E 808 ? 1.5749 1.7698 1.8972 -0.1084 -0.1323 0.0096  1112 LEU   E CD1 
17217 C  CD2 . LEU   E 808 ? 1.4653 1.6465 1.7530 -0.1038 -0.1400 0.0055  1112 LEU   E CD2 
17218 N  N   . GLN   E 809 ? 1.7392 1.9543 2.0835 -0.1025 -0.1415 0.0103  1113 GLN   E N   
17219 C  CA  . GLN   E 809 ? 1.7314 1.9524 2.0762 -0.0986 -0.1406 0.0115  1113 GLN   E CA  
17220 C  C   . GLN   E 809 ? 1.7608 1.9833 2.0983 -0.0957 -0.1297 0.0146  1113 GLN   E C   
17221 O  O   . GLN   E 809 ? 1.7040 1.9246 2.0400 -0.0969 -0.1223 0.0162  1113 GLN   E O   
17222 C  CB  . GLN   E 809 ? 1.7239 1.9552 2.0919 -0.0997 -0.1432 0.0123  1113 GLN   E CB  
17223 C  CG  . GLN   E 809 ? 1.7150 1.9489 2.0834 -0.0969 -0.1510 0.0108  1113 GLN   E CG  
17224 C  CD  . GLN   E 809 ? 1.7553 1.9955 2.1240 -0.0929 -0.1448 0.0134  1113 GLN   E CD  
17225 O  OE1 . GLN   E 809 ? 1.7740 2.0179 2.1460 -0.0925 -0.1349 0.0165  1113 GLN   E OE1 
17226 N  NE2 . GLN   E 809 ? 1.7813 2.0221 2.1458 -0.0897 -0.1508 0.0122  1113 GLN   E NE2 
17227 N  N   . ALA   E 820 ? 1.7558 1.9654 2.0886 -0.0973 -0.1710 0.0025  1124 ALA   E N   
17228 C  CA  . ALA   E 820 ? 1.8063 2.0088 2.1168 -0.0933 -0.1706 0.0020  1124 ALA   E CA  
17229 C  C   . ALA   E 820 ? 1.8858 2.0775 2.1822 -0.0930 -0.1806 -0.0018 1124 ALA   E C   
17230 O  O   . ALA   E 820 ? 1.9283 2.1139 2.2224 -0.0958 -0.1835 -0.0035 1124 ALA   E O   
17231 C  CB  . ALA   E 820 ? 1.7221 1.9215 2.0211 -0.0929 -0.1605 0.0039  1124 ALA   E CB  
17232 N  N   . THR   E 821 ? 1.8952 2.0840 2.1817 -0.0893 -0.1857 -0.0029 1125 THR   E N   
17233 C  CA  . THR   E 821 ? 1.9088 2.0869 2.1812 -0.0883 -0.1955 -0.0064 1125 THR   E CA  
17234 C  C   . THR   E 821 ? 1.9430 2.1104 2.1919 -0.0865 -0.1917 -0.0068 1125 THR   E C   
17235 O  O   . THR   E 821 ? 1.9308 2.0997 2.1733 -0.0852 -0.1825 -0.0045 1125 THR   E O   
17236 C  CB  . THR   E 821 ? 1.9435 2.1222 2.2148 -0.0848 -0.2028 -0.0074 1125 THR   E CB  
17237 O  OG1 . THR   E 821 ? 1.9735 2.1402 2.2294 -0.0835 -0.2123 -0.0108 1125 THR   E OG1 
17238 C  CG2 . THR   E 821 ? 1.9347 2.1150 2.1962 -0.0809 -0.1960 -0.0051 1125 THR   E CG2 
17239 N  N   . ALA   E 822 ? 2.0232 2.1795 2.2591 -0.0864 -0.1992 -0.0098 1126 ALA   E N   
17240 C  CA  . ALA   E 822 ? 1.9861 2.1315 2.1995 -0.0846 -0.1961 -0.0104 1126 ALA   E CA  
17241 C  C   . ALA   E 822 ? 1.9804 2.1256 2.1819 -0.0805 -0.1911 -0.0088 1126 ALA   E C   
17242 O  O   . ALA   E 822 ? 1.8978 2.0390 2.0866 -0.0794 -0.1839 -0.0078 1126 ALA   E O   
17243 C  CB  . ALA   E 822 ? 1.9494 2.0825 2.1501 -0.0842 -0.2059 -0.0140 1126 ALA   E CB  
17244 N  N   . ASP   E 823 ? 2.2078 2.3574 2.4141 -0.0781 -0.1947 -0.0085 1127 ASP   E N   
17245 C  CA  . ASP   E 823 ? 2.2123 2.3602 2.4062 -0.0741 -0.1910 -0.0072 1127 ASP   E CA  
17246 C  C   . ASP   E 823 ? 2.1655 2.3216 2.3643 -0.0740 -0.1800 -0.0040 1127 ASP   E C   
17247 O  O   . ASP   E 823 ? 2.1951 2.3480 2.3809 -0.0715 -0.1747 -0.0030 1127 ASP   E O   
17248 C  CB  . ASP   E 823 ? 2.2598 2.4096 2.4572 -0.0716 -0.1984 -0.0079 1127 ASP   E CB  
17249 C  CG  . ASP   E 823 ? 2.3348 2.4758 2.5269 -0.0713 -0.2103 -0.0114 1127 ASP   E CG  
17250 O  OD1 . ASP   E 823 ? 2.3451 2.4896 2.5519 -0.0743 -0.2161 -0.0128 1127 ASP   E OD1 
17251 O  OD2 . ASP   E 823 ? 2.3229 2.4529 2.4959 -0.0681 -0.2137 -0.0127 1127 ASP   E OD2 
17252 N  N   . ASP   E 824 ? 1.8612 2.0273 2.0782 -0.0766 -0.1762 -0.0023 1128 ASP   E N   
17253 C  CA  . ASP   E 824 ? 1.7799 1.9527 2.0003 -0.0762 -0.1658 0.0007  1128 ASP   E CA  
17254 C  C   . ASP   E 824 ? 1.7235 1.8922 1.9363 -0.0777 -0.1590 0.0011  1128 ASP   E C   
17255 O  O   . ASP   E 824 ? 1.6321 1.8032 1.8417 -0.0765 -0.1508 0.0031  1128 ASP   E O   
17256 C  CB  . ASP   E 824 ? 1.7880 1.9728 2.0301 -0.0777 -0.1636 0.0026  1128 ASP   E CB  
17257 C  CG  . ASP   E 824 ? 1.7827 1.9698 2.0382 -0.0820 -0.1650 0.0021  1128 ASP   E CG  
17258 O  OD1 . ASP   E 824 ? 1.7524 1.9377 2.0056 -0.0839 -0.1591 0.0028  1128 ASP   E OD1 
17259 O  OD2 . ASP   E 824 ? 1.7970 1.9876 2.0656 -0.0834 -0.1721 0.0010  1128 ASP   E OD2 
17260 N  N   . LEU   E 825 ? 1.7643 1.9265 1.9738 -0.0802 -0.1626 -0.0009 1129 LEU   E N   
17261 C  CA  . LEU   E 825 ? 1.6400 1.7969 1.8401 -0.0812 -0.1570 -0.0009 1129 LEU   E CA  
17262 C  C   . LEU   E 825 ? 1.5378 1.6844 1.7169 -0.0785 -0.1571 -0.0023 1129 LEU   E C   
17263 O  O   . LEU   E 825 ? 1.4667 1.6107 1.6372 -0.0780 -0.1504 -0.0016 1129 LEU   E O   
17264 C  CB  . LEU   E 825 ? 1.6445 1.7988 1.8505 -0.0850 -0.1603 -0.0024 1129 LEU   E CB  
17265 C  CG  . LEU   E 825 ? 1.6331 1.7967 1.8590 -0.0881 -0.1570 -0.0006 1129 LEU   E CG  
17266 C  CD1 . LEU   E 825 ? 1.7812 1.9507 2.0236 -0.0897 -0.1642 -0.0012 1129 LEU   E CD1 
17267 C  CD2 . LEU   E 825 ? 1.5799 1.7389 1.8048 -0.0912 -0.1554 -0.0012 1129 LEU   E CD2 
17268 N  N   . ILE   E 826 ? 1.6310 1.7714 1.8016 -0.0767 -0.1646 -0.0042 1130 ILE   E N   
17269 C  CA  . ILE   E 826 ? 1.6109 1.7422 1.7619 -0.0736 -0.1638 -0.0049 1130 ILE   E CA  
17270 C  C   . ILE   E 826 ? 1.5533 1.6892 1.7021 -0.0713 -0.1557 -0.0025 1130 ILE   E C   
17271 O  O   . ILE   E 826 ? 1.5034 1.6339 1.6391 -0.0697 -0.1509 -0.0024 1130 ILE   E O   
17272 C  CB  . ILE   E 826 ? 1.6332 1.7583 1.7769 -0.0714 -0.1728 -0.0068 1130 ILE   E CB  
17273 C  CG1 . ILE   E 826 ? 1.6567 1.7753 1.7999 -0.0733 -0.1814 -0.0096 1130 ILE   E CG1 
17274 C  CG2 . ILE   E 826 ? 1.5241 1.6403 1.6480 -0.0679 -0.1705 -0.0069 1130 ILE   E CG2 
17275 C  CD1 . ILE   E 826 ? 1.7824 1.8980 1.9251 -0.0717 -0.1916 -0.0114 1130 ILE   E CD1 
17276 N  N   . LYS   E 827 ? 1.5372 1.6830 1.6992 -0.0710 -0.1544 -0.0007 1131 LYS   E N   
17277 C  CA  . LYS   E 827 ? 1.4691 1.6194 1.6299 -0.0688 -0.1474 0.0015  1131 LYS   E CA  
17278 C  C   . LYS   E 827 ? 1.4905 1.6426 1.6513 -0.0698 -0.1388 0.0028  1131 LYS   E C   
17279 O  O   . LYS   E 827 ? 1.4928 1.6413 1.6427 -0.0680 -0.1339 0.0031  1131 LYS   E O   
17280 C  CB  . LYS   E 827 ? 1.4428 1.6031 1.6184 -0.0683 -0.1481 0.0031  1131 LYS   E CB  
17281 N  N   . VAL   E 828 ? 1.4712 1.6285 1.6443 -0.0725 -0.1371 0.0034  1132 VAL   E N   
17282 C  CA  . VAL   E 828 ? 1.4427 1.6020 1.6164 -0.0731 -0.1290 0.0048  1132 VAL   E CA  
17283 C  C   . VAL   E 828 ? 1.4279 1.5781 1.5875 -0.0732 -0.1277 0.0032  1132 VAL   E C   
17284 O  O   . VAL   E 828 ? 1.4420 1.5909 1.5945 -0.0718 -0.1216 0.0039  1132 VAL   E O   
17285 C  CB  . VAL   E 828 ? 1.4214 1.5873 1.6108 -0.0759 -0.1273 0.0060  1132 VAL   E CB  
17286 C  CG1 . VAL   E 828 ? 1.4259 1.5892 1.6202 -0.0788 -0.1342 0.0042  1132 VAL   E CG1 
17287 C  CG2 . VAL   E 828 ? 1.3718 1.5372 1.5590 -0.0765 -0.1198 0.0069  1132 VAL   E CG2 
17288 N  N   . VAL   E 829 ? 1.4231 1.5667 1.5786 -0.0748 -0.1334 0.0011  1133 VAL   E N   
17289 C  CA  . VAL   E 829 ? 1.4008 1.5355 1.5429 -0.0748 -0.1320 -0.0003 1133 VAL   E CA  
17290 C  C   . VAL   E 829 ? 1.4436 1.5725 1.5707 -0.0716 -0.1306 -0.0008 1133 VAL   E C   
17291 O  O   . VAL   E 829 ? 1.4785 1.6029 1.5962 -0.0707 -0.1259 -0.0010 1133 VAL   E O   
17292 C  CB  . VAL   E 829 ? 1.3715 1.4996 1.5117 -0.0770 -0.1388 -0.0026 1133 VAL   E CB  
17293 C  CG1 . VAL   E 829 ? 1.3162 1.4355 1.4431 -0.0768 -0.1365 -0.0040 1133 VAL   E CG1 
17294 C  CG2 . VAL   E 829 ? 1.3859 1.5201 1.5421 -0.0804 -0.1397 -0.0021 1133 VAL   E CG2 
17295 N  N   . GLU   E 830 ? 1.5026 1.6312 1.6274 -0.0697 -0.1345 -0.0008 1134 GLU   E N   
17296 C  CA  . GLU   E 830 ? 1.5002 1.6238 1.6119 -0.0667 -0.1321 -0.0008 1134 GLU   E CA  
17297 C  C   . GLU   E 830 ? 1.5149 1.6438 1.6283 -0.0655 -0.1239 0.0010  1134 GLU   E C   
17298 O  O   . GLU   E 830 ? 1.5254 1.6497 1.6287 -0.0642 -0.1195 0.0008  1134 GLU   E O   
17299 C  CB  . GLU   E 830 ? 1.5188 1.6419 1.6290 -0.0648 -0.1374 -0.0009 1134 GLU   E CB  
17300 C  CG  . GLU   E 830 ? 1.5269 1.6387 1.6230 -0.0634 -0.1433 -0.0029 1134 GLU   E CG  
17301 C  CD  . GLU   E 830 ? 1.5894 1.7011 1.6864 -0.0619 -0.1500 -0.0032 1134 GLU   E CD  
17302 O  OE1 . GLU   E 830 ? 1.6182 1.7375 1.7229 -0.0609 -0.1482 -0.0015 1134 GLU   E OE1 
17303 O  OE2 . GLU   E 830 ? 1.6202 1.7241 1.7100 -0.0614 -0.1573 -0.0051 1134 GLU   E OE2 
17304 N  N   . GLU   E 831 ? 1.4081 1.5465 1.5346 -0.0660 -0.1218 0.0028  1135 GLU   E N   
17305 C  CA  . GLU   E 831 ? 1.3948 1.5381 1.5234 -0.0647 -0.1146 0.0045  1135 GLU   E CA  
17306 C  C   . GLU   E 831 ? 1.3970 1.5382 1.5223 -0.0655 -0.1095 0.0042  1135 GLU   E C   
17307 O  O   . GLU   E 831 ? 1.3662 1.5073 1.4871 -0.0639 -0.1042 0.0046  1135 GLU   E O   
17308 C  CB  . GLU   E 831 ? 1.3797 1.5328 1.5229 -0.0651 -0.1134 0.0064  1135 GLU   E CB  
17309 C  CG  . GLU   E 831 ? 1.4395 1.5973 1.5841 -0.0632 -0.1069 0.0081  1135 GLU   E CG  
17310 C  CD  . GLU   E 831 ? 1.5690 1.7241 1.7048 -0.0605 -0.1064 0.0081  1135 GLU   E CD  
17311 O  OE1 . GLU   E 831 ? 1.5002 1.6502 1.6291 -0.0599 -0.1111 0.0071  1135 GLU   E OE1 
17312 O  OE2 . GLU   E 831 ? 1.6617 1.8192 1.7970 -0.0589 -0.1013 0.0091  1135 GLU   E OE2 
17313 N  N   . LEU   E 832 ? 1.3726 1.5117 1.5001 -0.0679 -0.1113 0.0033  1136 LEU   E N   
17314 C  CA  . LEU   E 832 ? 1.3425 1.4785 1.4657 -0.0684 -0.1070 0.0028  1136 LEU   E CA  
17315 C  C   . LEU   E 832 ? 1.3834 1.5111 1.4920 -0.0668 -0.1061 0.0013  1136 LEU   E C   
17316 O  O   . LEU   E 832 ? 1.3928 1.5196 1.4973 -0.0657 -0.1008 0.0013  1136 LEU   E O   
17317 C  CB  . LEU   E 832 ? 1.2615 1.3968 1.3904 -0.0714 -0.1094 0.0022  1136 LEU   E CB  
17318 C  CG  . LEU   E 832 ? 1.2063 1.3499 1.3508 -0.0731 -0.1096 0.0038  1136 LEU   E CG  
17319 C  CD1 . LEU   E 832 ? 1.2044 1.3468 1.3548 -0.0764 -0.1116 0.0033  1136 LEU   E CD1 
17320 C  CD2 . LEU   E 832 ? 1.1816 1.3317 1.3317 -0.0719 -0.1029 0.0059  1136 LEU   E CD2 
17321 N  N   . THR   E 833 ? 1.3719 1.4933 1.4725 -0.0663 -0.1111 0.0000  1137 THR   E N   
17322 C  CA  . THR   E 833 ? 1.3756 1.4884 1.4618 -0.0644 -0.1098 -0.0012 1137 THR   E CA  
17323 C  C   . THR   E 833 ? 1.3853 1.4997 1.4682 -0.0620 -0.1048 -0.0001 1137 THR   E C   
17324 O  O   . THR   E 833 ? 1.3353 1.4432 1.4072 -0.0604 -0.1026 -0.0008 1137 THR   E O   
17325 C  CB  . THR   E 833 ? 1.3444 1.4492 1.4218 -0.0641 -0.1164 -0.0026 1137 THR   E CB  
17326 O  OG1 . THR   E 833 ? 1.4071 1.5138 1.4849 -0.0625 -0.1187 -0.0018 1137 THR   E OG1 
17327 C  CG2 . THR   E 833 ? 1.3710 1.4753 1.4540 -0.0666 -0.1225 -0.0037 1137 THR   E CG2 
17328 N  N   . ARG   E 834 ? 1.3218 1.4445 1.4139 -0.0616 -0.1027 0.0015  1138 ARG   E N   
17329 C  CA  . ARG   E 834 ? 1.2850 1.4092 1.3747 -0.0594 -0.0985 0.0025  1138 ARG   E CA  
17330 C  C   . ARG   E 834 ? 1.2904 1.4187 1.3838 -0.0590 -0.0923 0.0030  1138 ARG   E C   
17331 O  O   . ARG   E 834 ? 1.3078 1.4383 1.4011 -0.0573 -0.0887 0.0037  1138 ARG   E O   
17332 C  CB  . ARG   E 834 ? 1.3768 1.5063 1.4726 -0.0586 -0.1007 0.0038  1138 ARG   E CB  
17333 C  CG  . ARG   E 834 ? 1.3954 1.5191 1.4836 -0.0576 -0.1059 0.0032  1138 ARG   E CG  
17334 C  CD  . ARG   E 834 ? 1.3980 1.5258 1.4944 -0.0584 -0.1119 0.0036  1138 ARG   E CD  
17335 N  NE  . ARG   E 834 ? 1.4709 1.5922 1.5592 -0.0572 -0.1175 0.0028  1138 ARG   E NE  
17336 C  CZ  . ARG   E 834 ? 1.5282 1.6417 1.6089 -0.0577 -0.1223 0.0010  1138 ARG   E CZ  
17337 N  NH1 . ARG   E 834 ? 1.5065 1.6171 1.5857 -0.0594 -0.1218 -0.0001 1138 ARG   E NH1 
17338 N  NH2 . ARG   E 834 ? 1.5011 1.6090 1.5750 -0.0562 -0.1279 0.0004  1138 ARG   E NH2 
17339 N  N   . ILE   E 835 ? 1.2820 1.4109 1.3786 -0.0604 -0.0912 0.0025  1139 ILE   E N   
17340 C  CA  . ILE   E 835 ? 1.2381 1.3689 1.3359 -0.0597 -0.0857 0.0026  1139 ILE   E CA  
17341 C  C   . ILE   E 835 ? 1.1992 1.3233 1.2872 -0.0589 -0.0832 0.0011  1139 ILE   E C   
17342 O  O   . ILE   E 835 ? 1.1802 1.3054 1.2683 -0.0577 -0.0788 0.0010  1139 ILE   E O   
17343 C  CB  . ILE   E 835 ? 1.2014 1.3359 1.3070 -0.0612 -0.0849 0.0031  1139 ILE   E CB  
17344 C  CG1 . ILE   E 835 ? 1.1712 1.3008 1.2743 -0.0633 -0.0881 0.0019  1139 ILE   E CG1 
17345 C  CG2 . ILE   E 835 ? 1.2307 1.3723 1.3468 -0.0618 -0.0862 0.0048  1139 ILE   E CG2 
17346 C  CD1 . ILE   E 835 ? 1.1995 1.3322 1.3104 -0.0650 -0.0872 0.0025  1139 ILE   E CD1 
17347 N  N   . HIS   E 836 ? 1.2083 1.3252 1.2878 -0.0592 -0.0861 0.0000  1140 HIS   E N   
17348 C  CA  . HIS   E 836 ? 1.1830 1.2930 1.2525 -0.0580 -0.0835 -0.0013 1140 HIS   E CA  
17349 C  C   . HIS   E 836 ? 1.2730 1.3762 1.3327 -0.0570 -0.0859 -0.0016 1140 HIS   E C   
17350 O  O   . HIS   E 836 ? 1.3288 1.4240 1.3787 -0.0566 -0.0859 -0.0029 1140 HIS   E O   
17351 C  CB  . HIS   E 836 ? 1.1480 1.2539 1.2147 -0.0591 -0.0837 -0.0026 1140 HIS   E CB  
17352 C  CG  . HIS   E 836 ? 1.1652 1.2664 1.2290 -0.0608 -0.0895 -0.0034 1140 HIS   E CG  
17353 N  ND1 . HIS   E 836 ? 1.1469 1.2389 1.1995 -0.0604 -0.0913 -0.0049 1140 HIS   E ND1 
17354 C  CD2 . HIS   E 836 ? 1.1716 1.2760 1.2427 -0.0628 -0.0940 -0.0030 1140 HIS   E CD2 
17355 C  CE1 . HIS   E 836 ? 1.1647 1.2540 1.2174 -0.0621 -0.0971 -0.0055 1140 HIS   E CE1 
17356 N  NE2 . HIS   E 836 ? 1.1699 1.2671 1.2345 -0.0637 -0.0988 -0.0044 1140 HIS   E NE2 
17357 N  N   . SER   F 3   ? 1.9530 1.2134 1.1897 0.2587  0.0129  0.0221  868  SER   F N   
17358 C  CA  . SER   F 3   ? 2.0371 1.2922 1.2760 0.2493  0.0273  0.0291  868  SER   F CA  
17359 C  C   . SER   F 3   ? 2.0460 1.3102 1.2970 0.2410  0.0390  0.0350  868  SER   F C   
17360 O  O   . SER   F 3   ? 1.9550 1.2419 1.2332 0.2289  0.0419  0.0358  868  SER   F O   
17361 C  CB  . SER   F 3   ? 2.1292 1.3511 1.3358 0.2574  0.0335  0.0328  868  SER   F CB  
17362 O  OG  . SER   F 3   ? 2.1759 1.3877 1.3691 0.2664  0.0221  0.0272  868  SER   F OG  
17363 N  N   . LEU   F 4   ? 2.1815 1.4274 1.4119 0.2478  0.0459  0.0390  869  LEU   F N   
17364 C  CA  . LEU   F 4   ? 2.1484 1.4012 1.3880 0.2415  0.0570  0.0446  869  LEU   F CA  
17365 C  C   . LEU   F 4   ? 2.1449 1.4149 1.3958 0.2434  0.0494  0.0409  869  LEU   F C   
17366 O  O   . LEU   F 4   ? 2.1506 1.4251 1.4069 0.2400  0.0576  0.0450  869  LEU   F O   
17367 C  CB  . LEU   F 4   ? 2.1746 1.3983 1.3862 0.2476  0.0697  0.0514  869  LEU   F CB  
17368 C  CG  . LEU   F 4   ? 2.2349 1.4486 1.4460 0.2397  0.0839  0.0581  869  LEU   F CG  
17369 C  CD1 . LEU   F 4   ? 2.2516 1.4432 1.4425 0.2432  0.0985  0.0656  869  LEU   F CD1 
17370 C  CD2 . LEU   F 4   ? 2.2195 1.4610 1.4657 0.2239  0.0873  0.0592  869  LEU   F CD2 
17371 N  N   . THR   F 5   ? 2.0354 1.3151 1.2905 0.2487  0.0341  0.0332  870  THR   F N   
17372 C  CA  . THR   F 5   ? 1.9188 1.2147 1.1848 0.2509  0.0256  0.0291  870  THR   F CA  
17373 C  C   . THR   F 5   ? 1.9093 1.2330 1.2029 0.2451  0.0140  0.0227  870  THR   F C   
17374 O  O   . THR   F 5   ? 1.8463 1.1803 1.1453 0.2496  0.0032  0.0174  870  THR   F O   
17375 C  CB  . THR   F 5   ? 1.9919 1.2685 1.2312 0.2661  0.0173  0.0258  870  THR   F CB  
17376 O  OG1 . THR   F 5   ? 2.0416 1.3067 1.2679 0.2735  0.0080  0.0212  870  THR   F OG1 
17377 C  CG2 . THR   F 5   ? 2.0850 1.3358 1.2976 0.2722  0.0290  0.0322  870  THR   F CG2 
17378 N  N   . THR   F 6   ? 1.9387 1.2733 1.2486 0.2357  0.0157  0.0228  871  THR   F N   
17379 C  CA  . THR   F 6   ? 1.8096 1.1721 1.1482 0.2283  0.0072  0.0178  871  THR   F CA  
17380 C  C   . THR   F 6   ? 1.7642 1.1476 1.1281 0.2150  0.0155  0.0216  871  THR   F C   
17381 O  O   . THR   F 6   ? 1.7625 1.1392 1.1247 0.2094  0.0284  0.0282  871  THR   F O   
17382 C  CB  . THR   F 6   ? 1.8177 1.1800 1.1589 0.2265  0.0030  0.0151  871  THR   F CB  
17383 O  OG1 . THR   F 6   ? 1.8185 1.1815 1.1677 0.2160  0.0142  0.0204  871  THR   F OG1 
17384 C  CG2 . THR   F 6   ? 1.8554 1.1916 1.1676 0.2392  -0.0017 0.0132  871  THR   F CG2 
17385 N  N   . CYS   F 7   ? 1.7640 1.1728 1.1520 0.2102  0.0080  0.0174  872  CYS   F N   
17386 C  CA  . CYS   F 7   ? 1.6930 1.1229 1.1052 0.1989  0.0140  0.0202  872  CYS   F CA  
17387 C  C   . CYS   F 7   ? 1.7001 1.1453 1.1336 0.1872  0.0159  0.0204  872  CYS   F C   
17388 O  O   . CYS   F 7   ? 1.6747 1.1271 1.1149 0.1873  0.0072  0.0155  872  CYS   F O   
17389 C  CB  . CYS   F 7   ? 1.6375 1.0862 1.0637 0.2001  0.0050  0.0156  872  CYS   F CB  
17390 S  SG  . CYS   F 7   ? 1.5715 1.0479 1.0288 0.1864  0.0107  0.0182  872  CYS   F SG  
17391 N  N   . GLU   F 8   ? 1.7653 1.2156 1.2097 0.1773  0.0271  0.0261  873  GLU   F N   
17392 C  CA  . GLU   F 8   ? 1.7281 1.1901 1.1906 0.1664  0.0297  0.0269  873  GLU   F CA  
17393 C  C   . GLU   F 8   ? 1.6816 1.1715 1.1711 0.1595  0.0221  0.0225  873  GLU   F C   
17394 O  O   . GLU   F 8   ? 1.6776 1.1770 1.1800 0.1530  0.0201  0.0208  873  GLU   F O   
17395 C  CB  . GLU   F 8   ? 1.7669 1.2255 1.2334 0.1579  0.0438  0.0342  873  GLU   F CB  
17396 C  CG  . GLU   F 8   ? 1.8600 1.2914 1.2999 0.1651  0.0525  0.0391  873  GLU   F CG  
17397 C  CD  . GLU   F 8   ? 1.9090 1.3300 1.3475 0.1583  0.0641  0.0449  873  GLU   F CD  
17398 O  OE1 . GLU   F 8   ? 1.9479 1.3845 1.4084 0.1467  0.0695  0.0474  873  GLU   F OE1 
17399 O  OE2 . GLU   F 8   ? 1.8823 1.2794 1.2978 0.1645  0.0676  0.0468  873  GLU   F OE2 
17400 N  N   . VAL   F 9   ? 1.5952 1.0978 1.0930 0.1609  0.0180  0.0205  874  VAL   F N   
17401 C  CA  . VAL   F 9   ? 1.5504 1.0797 1.0747 0.1535  0.0124  0.0172  874  VAL   F CA  
17402 C  C   . VAL   F 9   ? 1.5558 1.0925 1.0830 0.1588  -0.0009 0.0098  874  VAL   F C   
17403 O  O   . VAL   F 9   ? 1.5413 1.0932 1.0853 0.1530  -0.0052 0.0069  874  VAL   F O   
17404 C  CB  . VAL   F 9   ? 1.5083 1.0493 1.0426 0.1512  0.0151  0.0190  874  VAL   F CB  
17405 C  CG1 . VAL   F 9   ? 1.4682 1.0362 1.0292 0.1438  0.0090  0.0154  874  VAL   F CG1 
17406 C  CG2 . VAL   F 9   ? 1.5144 1.0493 1.0480 0.1454  0.0285  0.0262  874  VAL   F CG2 
17407 N  N   . CYS   F 10  ? 1.5838 1.1099 1.0950 0.1701  -0.0077 0.0066  875  CYS   F N   
17408 C  CA  . CYS   F 10  ? 1.4968 1.0308 1.0125 0.1753  -0.0204 -0.0005 875  CYS   F CA  
17409 C  C   . CYS   F 10  ? 1.5618 1.0762 1.0563 0.1853  -0.0256 -0.0031 875  CYS   F C   
17410 O  O   . CYS   F 10  ? 1.5983 1.1192 1.0980 0.1884  -0.0354 -0.0088 875  CYS   F O   
17411 C  CB  . CYS   F 10  ? 1.5124 1.0552 1.0321 0.1800  -0.0271 -0.0036 875  CYS   F CB  
17412 S  SG  . CYS   F 10  ? 1.4979 1.0144 0.9869 0.1931  -0.0262 -0.0020 875  CYS   F SG  
17413 N  N   . GLY   F 11  ? 1.6630 1.1535 1.1338 0.1906  -0.0192 0.0009  876  GLY   F N   
17414 C  CA  . GLY   F 11  ? 1.7210 1.1914 1.1703 0.2002  -0.0237 -0.0013 876  GLY   F CA  
17415 C  C   . GLY   F 11  ? 1.7445 1.2004 1.1738 0.2134  -0.0306 -0.0041 876  GLY   F C   
17416 O  O   . GLY   F 11  ? 1.7656 1.2047 1.1767 0.2223  -0.0356 -0.0065 876  GLY   F O   
17417 N  N   . ALA   F 12  ? 1.6676 1.1291 1.0995 0.2150  -0.0313 -0.0040 877  ALA   F N   
17418 C  CA  . ALA   F 12  ? 1.6788 1.1261 1.0913 0.2275  -0.0379 -0.0066 877  ALA   F CA  
17419 C  C   . ALA   F 12  ? 1.7229 1.1404 1.1048 0.2351  -0.0311 -0.0023 877  ALA   F C   
17420 O  O   . ALA   F 12  ? 1.7485 1.1585 1.1254 0.2304  -0.0185 0.0044  877  ALA   F O   
17421 C  CB  . ALA   F 12  ? 1.6591 1.1180 1.0808 0.2265  -0.0381 -0.0064 877  ALA   F CB  
17422 N  N   . CYS   F 13  ? 1.7480 1.1482 1.1096 0.2469  -0.0392 -0.0060 878  CYS   F N   
17423 C  CA  . CYS   F 13  ? 1.8101 1.1803 1.1408 0.2551  -0.0338 -0.0025 878  CYS   F CA  
17424 C  C   . CYS   F 13  ? 1.8462 1.2020 1.1570 0.2661  -0.0370 -0.0031 878  CYS   F C   
17425 O  O   . CYS   F 13  ? 1.8744 1.2320 1.1835 0.2742  -0.0498 -0.0094 878  CYS   F O   
17426 C  CB  . CYS   F 13  ? 1.8237 1.1820 1.1429 0.2611  -0.0403 -0.0060 878  CYS   F CB  
17427 S  SG  . CYS   F 13  ? 2.0297 1.3516 1.3126 0.2688  -0.0315 -0.0007 878  CYS   F SG  
17428 N  N   . PHE   F 14  ? 1.8844 1.2256 1.1804 0.2665  -0.0254 0.0033  879  PHE   F N   
17429 C  CA  . PHE   F 14  ? 1.9396 1.2663 1.2160 0.2767  -0.0271 0.0034  879  PHE   F CA  
17430 C  C   . PHE   F 14  ? 2.0409 1.3343 1.2818 0.2884  -0.0250 0.0052  879  PHE   F C   
17431 O  O   . PHE   F 14  ? 2.0455 1.3264 1.2771 0.2868  -0.0183 0.0085  879  PHE   F O   
17432 C  CB  . PHE   F 14  ? 1.8991 1.2321 1.1825 0.2702  -0.0158 0.0091  879  PHE   F CB  
17433 C  CG  . PHE   F 14  ? 1.8269 1.1902 1.1412 0.2615  -0.0197 0.0066  879  PHE   F CG  
17434 C  CD1 . PHE   F 14  ? 1.8139 1.1843 1.1310 0.2667  -0.0289 0.0023  879  PHE   F CD1 
17435 C  CD2 . PHE   F 14  ? 1.8321 1.2164 1.1726 0.2483  -0.0151 0.0081  879  PHE   F CD2 
17436 C  CE1 . PHE   F 14  ? 1.8352 1.2329 1.1805 0.2588  -0.0327 -0.0001 879  PHE   F CE1 
17437 C  CE2 . PHE   F 14  ? 1.8184 1.2301 1.1868 0.2405  -0.0190 0.0057  879  PHE   F CE2 
17438 C  CZ  . PHE   F 14  ? 1.8297 1.2483 1.2007 0.2457  -0.0276 0.0016  879  PHE   F CZ  
17439 N  N   . GLU   F 15  ? 2.0346 1.3134 1.2553 0.3004  -0.0314 0.0029  880  GLU   F N   
17440 C  CA  . GLU   F 15  ? 1.9909 1.2367 1.1759 0.3126  -0.0300 0.0045  880  GLU   F CA  
17441 C  C   . GLU   F 15  ? 2.0242 1.2525 1.1921 0.3122  -0.0139 0.0128  880  GLU   F C   
17442 O  O   . GLU   F 15  ? 2.1908 1.3926 1.3323 0.3180  -0.0072 0.0166  880  GLU   F O   
17443 C  CB  . GLU   F 15  ? 2.0568 1.2926 1.2259 0.3265  -0.0445 -0.0020 880  GLU   F CB  
17444 C  CG  . GLU   F 15  ? 2.0991 1.3477 1.2810 0.3292  -0.0609 -0.0105 880  GLU   F CG  
17445 C  CD  . GLU   F 15  ? 2.2004 1.4394 1.3677 0.3428  -0.0754 -0.0169 880  GLU   F CD  
17446 O  OE1 . GLU   F 15  ? 2.2710 1.4823 1.4067 0.3539  -0.0739 -0.0151 880  GLU   F OE1 
17447 O  OE2 . GLU   F 15  ? 2.2203 1.4792 1.4077 0.3425  -0.0882 -0.0237 880  GLU   F OE2 
17448 N  N   . THR   F 16  ? 2.0882 1.3300 1.2698 0.3059  -0.0076 0.0158  881  THR   F N   
17449 C  CA  . THR   F 16  ? 2.1166 1.3433 1.2837 0.3056  0.0078  0.0237  881  THR   F CA  
17450 C  C   . THR   F 16  ? 2.0538 1.3007 1.2475 0.2902  0.0202  0.0290  881  THR   F C   
17451 O  O   . THR   F 16  ? 2.0256 1.3005 1.2492 0.2810  0.0154  0.0261  881  THR   F O   
17452 C  CB  . THR   F 16  ? 2.1147 1.3356 1.2703 0.3135  0.0054  0.0230  881  THR   F CB  
17453 O  OG1 . THR   F 16  ? 2.1558 1.3652 1.3014 0.3115  0.0218  0.0312  881  THR   F OG1 
17454 C  CG2 . THR   F 16  ? 2.0323 1.2841 1.2182 0.3071  -0.0032 0.0184  881  THR   F CG2 
17455 N  N   . ARG   F 17  ? 1.9883 1.2207 1.1712 0.2875  0.0361  0.0369  882  ARG   F N   
17456 C  CA  . ARG   F 17  ? 1.8923 1.1433 1.1004 0.2733  0.0480  0.0421  882  ARG   F CA  
17457 C  C   . ARG   F 17  ? 1.9603 1.2310 1.1861 0.2696  0.0473  0.0417  882  ARG   F C   
17458 O  O   . ARG   F 17  ? 1.9235 1.2168 1.1768 0.2572  0.0526  0.0438  882  ARG   F O   
17459 C  CB  . ARG   F 17  ? 1.8456 1.0757 1.0379 0.2719  0.0655  0.0507  882  ARG   F CB  
17460 N  N   . LYS   F 18  ? 1.9579 1.2208 1.1689 0.2801  0.0405  0.0388  883  LYS   F N   
17461 C  CA  . LYS   F 18  ? 1.9461 1.2292 1.1754 0.2765  0.0383  0.0376  883  LYS   F CA  
17462 C  C   . LYS   F 18  ? 1.9502 1.2615 1.2072 0.2711  0.0244  0.0305  883  LYS   F C   
17463 O  O   . LYS   F 18  ? 1.9015 1.2370 1.1844 0.2621  0.0252  0.0304  883  LYS   F O   
17464 C  CB  . LYS   F 18  ? 2.0298 1.2961 1.2352 0.2891  0.0349  0.0366  883  LYS   F CB  
17465 N  N   . GLY   F 19  ? 2.0242 1.3323 1.2760 0.2769  0.0118  0.0243  884  GLY   F N   
17466 C  CA  . GLY   F 19  ? 1.9672 1.3013 1.2457 0.2714  -0.0004 0.0178  884  GLY   F CA  
17467 C  C   . GLY   F 19  ? 1.8842 1.2407 1.1915 0.2564  0.0066  0.0205  884  GLY   F C   
17468 O  O   . GLY   F 19  ? 1.9095 1.2917 1.2432 0.2487  0.0027  0.0181  884  GLY   F O   
17469 N  N   . LEU   F 20  ? 1.7935 1.1397 1.0953 0.2519  0.0176  0.0258  885  LEU   F N   
17470 C  CA  . LEU   F 20  ? 1.7220 1.0875 1.0497 0.2377  0.0251  0.0289  885  LEU   F CA  
17471 C  C   . LEU   F 20  ? 1.7692 1.1474 1.1115 0.2303  0.0343  0.0334  885  LEU   F C   
17472 O  O   . LEU   F 20  ? 1.8244 1.2281 1.1946 0.2203  0.0329  0.0322  885  LEU   F O   
17473 C  CB  . LEU   F 20  ? 1.7440 1.0939 1.0616 0.2349  0.0352  0.0337  885  LEU   F CB  
17474 C  CG  . LEU   F 20  ? 1.8088 1.1671 1.1377 0.2305  0.0288  0.0301  885  LEU   F CG  
17475 C  CD1 . LEU   F 20  ? 1.9360 1.2861 1.2639 0.2234  0.0412  0.0360  885  LEU   F CD1 
17476 C  CD2 . LEU   F 20  ? 1.7026 1.0921 1.0634 0.2215  0.0217  0.0259  885  LEU   F CD2 
17477 N  N   . SER   F 21  ? 1.7504 1.1109 1.0741 0.2352  0.0440  0.0386  886  SER   F N   
17478 C  CA  . SER   F 21  ? 1.7380 1.1102 1.0756 0.2282  0.0535  0.0431  886  SER   F CA  
17479 C  C   . SER   F 21  ? 1.7071 1.1034 1.0652 0.2261  0.0437  0.0382  886  SER   F C   
17480 O  O   . SER   F 21  ? 1.7091 1.1279 1.0933 0.2152  0.0468  0.0395  886  SER   F O   
17481 C  CB  . SER   F 21  ? 1.8138 1.1623 1.1258 0.2362  0.0635  0.0485  886  SER   F CB  
17482 O  OG  . SER   F 21  ? 1.8895 1.2344 1.1903 0.2460  0.0545  0.0445  886  SER   F OG  
17483 N  N   . SER   F 22  ? 1.7037 1.0952 1.0503 0.2363  0.0314  0.0325  887  SER   F N   
17484 C  CA  . SER   F 22  ? 1.6811 1.0946 1.0467 0.2346  0.0217  0.0276  887  SER   F CA  
17485 C  C   . SER   F 22  ? 1.7219 1.1619 1.1173 0.2243  0.0155  0.0239  887  SER   F C   
17486 O  O   . SER   F 22  ? 1.7199 1.1824 1.1395 0.2155  0.0165  0.0242  887  SER   F O   
17487 C  CB  . SER   F 22  ? 1.6422 1.0449 0.9902 0.2476  0.0086  0.0216  887  SER   F CB  
17488 O  OG  . SER   F 22  ? 1.6927 1.0943 1.0392 0.2510  -0.0023 0.0161  887  SER   F OG  
17489 N  N   . HIS   F 23  ? 1.6985 1.1357 1.0920 0.2254  0.0092  0.0205  888  HIS   F N   
17490 C  CA  . HIS   F 23  ? 1.6561 1.1166 1.0759 0.2164  0.0032  0.0169  888  HIS   F CA  
17491 C  C   . HIS   F 23  ? 1.6477 1.1235 1.0890 0.2028  0.0139  0.0218  888  HIS   F C   
17492 O  O   . HIS   F 23  ? 1.6330 1.1323 1.0997 0.1942  0.0099  0.0194  888  HIS   F O   
17493 C  CB  . HIS   F 23  ? 1.6422 1.0932 1.0531 0.2203  -0.0029 0.0136  888  HIS   F CB  
17494 C  CG  . HIS   F 23  ? 1.6276 1.1006 1.0631 0.2123  -0.0094 0.0095  888  HIS   F CG  
17495 N  ND1 . HIS   F 23  ? 1.6231 1.1202 1.0819 0.2079  -0.0169 0.0053  888  HIS   F ND1 
17496 C  CD2 . HIS   F 23  ? 1.6148 1.0885 1.0547 0.2082  -0.0095 0.0090  888  HIS   F CD2 
17497 C  CE1 . HIS   F 23  ? 1.5643 1.0759 1.0404 0.2016  -0.0210 0.0025  888  HIS   F CE1 
17498 N  NE2 . HIS   F 23  ? 1.5559 1.0538 1.0209 0.2017  -0.0167 0.0046  888  HIS   F NE2 
17499 N  N   . ALA   F 24  ? 1.6423 1.1047 1.0738 0.2007  0.0273  0.0287  889  ALA   F N   
17500 C  CA  . ALA   F 24  ? 1.6492 1.1254 1.1011 0.1880  0.0375  0.0336  889  ALA   F CA  
17501 C  C   . ALA   F 24  ? 1.6755 1.1725 1.1476 0.1824  0.0379  0.0338  889  ALA   F C   
17502 O  O   . ALA   F 24  ? 1.7435 1.2594 1.2392 0.1712  0.0415  0.0353  889  ALA   F O   
17503 C  CB  . ALA   F 24  ? 1.6530 1.1091 1.0893 0.1879  0.0520  0.0410  889  ALA   F CB  
17504 N  N   . ARG   F 25  ? 1.6252 1.1191 1.0885 0.1900  0.0338  0.0321  890  ARG   F N   
17505 C  CA  . ARG   F 25  ? 1.6141 1.1291 1.0976 0.1849  0.0322  0.0313  890  ARG   F CA  
17506 C  C   . ARG   F 25  ? 1.6514 1.1891 1.1566 0.1806  0.0202  0.0249  890  ARG   F C   
17507 O  O   . ARG   F 25  ? 1.7138 1.2730 1.2433 0.1708  0.0214  0.0252  890  ARG   F O   
17508 C  CB  . ARG   F 25  ? 1.6624 1.1677 1.1304 0.1944  0.0305  0.0309  890  ARG   F CB  
17509 N  N   . SER   F 26  ? 1.6279 1.1608 1.1248 0.1879  0.0086  0.0190  891  SER   F N   
17510 C  CA  . SER   F 26  ? 1.6507 1.2038 1.1673 0.1846  -0.0028 0.0127  891  SER   F CA  
17511 C  C   . SER   F 26  ? 1.6975 1.2687 1.2376 0.1720  0.0010  0.0140  891  SER   F C   
17512 O  O   . SER   F 26  ? 1.7212 1.3144 1.2837 0.1657  -0.0039 0.0112  891  SER   F O   
17513 C  CB  . SER   F 26  ? 1.5791 1.1214 1.0822 0.1936  -0.0134 0.0072  891  SER   F CB  
17514 O  OG  . SER   F 26  ? 1.5083 1.0680 1.0305 0.1886  -0.0212 0.0025  891  SER   F OG  
17515 N  N   . HIS   F 27  ? 1.7206 1.2822 1.2556 0.1682  0.0099  0.0185  892  HIS   F N   
17516 C  CA  . HIS   F 27  ? 1.7227 1.2981 1.2770 0.1571  0.0128  0.0194  892  HIS   F CA  
17517 C  C   . HIS   F 27  ? 1.7440 1.3314 1.3148 0.1470  0.0226  0.0246  892  HIS   F C   
17518 O  O   . HIS   F 27  ? 1.8647 1.4650 1.4531 0.1373  0.0247  0.0253  892  HIS   F O   
17519 C  CB  . HIS   F 27  ? 1.6298 1.1886 1.1709 0.1578  0.0168  0.0213  892  HIS   F CB  
17520 C  CG  . HIS   F 27  ? 1.5508 1.1062 1.0861 0.1633  0.0063  0.0156  892  HIS   F CG  
17521 N  ND1 . HIS   F 27  ? 1.6136 1.1881 1.1676 0.1596  -0.0028 0.0103  892  HIS   F ND1 
17522 C  CD2 . HIS   F 27  ? 1.5431 1.0780 1.0562 0.1724  0.0036  0.0143  892  HIS   F CD2 
17523 C  CE1 . HIS   F 27  ? 1.6202 1.1867 1.1644 0.1662  -0.0106 0.0060  892  HIS   F CE1 
17524 N  NE2 . HIS   F 27  ? 1.5794 1.1219 1.0988 0.1740  -0.0073 0.0082  892  HIS   F NE2 
17525 N  N   . LEU   F 28  ? 1.6921 1.2750 1.2572 0.1492  0.0287  0.0281  893  LEU   F N   
17526 C  CA  . LEU   F 28  ? 1.8145 1.4104 1.3972 0.1396  0.0374  0.0326  893  LEU   F CA  
17527 C  C   . LEU   F 28  ? 2.0110 1.6312 1.6158 0.1350  0.0301  0.0289  893  LEU   F C   
17528 O  O   . LEU   F 28  ? 1.9395 1.5648 1.5466 0.1367  0.0303  0.0293  893  LEU   F O   
17529 C  CB  . LEU   F 28  ? 1.7856 1.3673 1.3544 0.1433  0.0478  0.0383  893  LEU   F CB  
17530 C  CG  . LEU   F 28  ? 1.7556 1.3117 1.3011 0.1483  0.0554  0.0422  893  LEU   F CG  
17531 C  CD1 . LEU   F 28  ? 1.6765 1.2172 1.2071 0.1524  0.0668  0.0482  893  LEU   F CD1 
17532 C  CD2 . LEU   F 28  ? 1.6327 1.1894 1.1862 0.1400  0.0603  0.0443  893  LEU   F CD2 
17533 N  N   . ARG   F 29  ? 2.3340 1.9684 1.9542 0.1296  0.0233  0.0250  894  ARG   F N   
17534 C  CA  . ARG   F 29  ? 2.2956 1.9545 1.9399 0.1228  0.0177  0.0219  894  ARG   F CA  
17535 C  C   . ARG   F 29  ? 2.2975 1.9679 1.9599 0.1110  0.0241  0.0251  894  ARG   F C   
17536 O  O   . ARG   F 29  ? 2.2632 1.9316 1.9269 0.1077  0.0240  0.0247  894  ARG   F O   
17537 C  CB  . ARG   F 29  ? 2.2265 1.8927 1.8749 0.1256  0.0054  0.0151  894  ARG   F CB  
17538 C  CG  . ARG   F 29  ? 2.2403 1.8963 1.8727 0.1371  -0.0028 0.0109  894  ARG   F CG  
17539 C  CD  . ARG   F 29  ? 2.2374 1.8994 1.8744 0.1392  -0.0136 0.0047  894  ARG   F CD  
17540 N  NE  . ARG   F 29  ? 2.2517 1.9078 1.8862 0.1365  -0.0117 0.0052  894  ARG   F NE  
17541 C  CZ  . ARG   F 29  ? 2.2708 1.9083 1.8860 0.1438  -0.0131 0.0044  894  ARG   F CZ  
17542 N  NH1 . ARG   F 29  ? 2.2776 1.9001 1.8738 0.1545  -0.0167 0.0030  894  ARG   F NH1 
17543 N  NH2 . ARG   F 29  ? 2.2743 1.9077 1.8889 0.1405  -0.0112 0.0049  894  ARG   F NH2 
17544 ZN ZN  . ZN    G .   ? 1.2978 1.0857 0.9808 0.0303  -0.0475 0.0478  501  ZN    A ZN  
17545 S  S   . SO4   H .   ? 1.6141 1.7197 1.6746 -0.0051 -0.0853 0.0316  502  SO4   A S   
17546 O  O1  . SO4   H .   ? 1.3025 1.4008 1.3545 -0.0070 -0.0841 0.0317  502  SO4   A O1  
17547 O  O2  . SO4   H .   ? 1.3595 1.4645 1.4234 -0.0066 -0.0810 0.0310  502  SO4   A O2  
17548 O  O3  . SO4   H .   ? 1.4666 1.5695 1.5235 -0.0014 -0.0885 0.0328  502  SO4   A O3  
17549 O  O4  . SO4   H .   ? 1.4777 1.5933 1.5470 -0.0053 -0.0874 0.0309  502  SO4   A O4  
17550 C  C1  . A1A5I I .   ? 1.3847 1.2153 1.0958 0.0108  -0.0715 0.0130  503  A1A5I A C1  
17551 C  C2  . A1A5I I .   ? 1.4539 1.2832 1.1622 0.0114  -0.0837 0.0100  503  A1A5I A C2  
17552 C  C3  . A1A5I I .   ? 1.4383 1.2812 1.1626 0.0089  -0.0940 0.0085  503  A1A5I A C3  
17553 C  C12 . A1A5I I .   ? 1.2751 1.1745 1.0683 -0.0013 -0.0968 0.0119  503  A1A5I A C12 
17554 C  C13 . A1A5I I .   ? 1.2800 1.1767 1.0693 0.0011  -0.1087 0.0108  503  A1A5I A C13 
17555 C  C14 . A1A5I I .   ? 1.3357 1.2503 1.1468 -0.0018 -0.1128 0.0109  503  A1A5I A C14 
17556 C  C15 . A1A5I I .   ? 1.3475 1.2786 1.1790 -0.0065 -0.1127 0.0097  503  A1A5I A C15 
17557 C  C17 . A1A5I I .   ? 1.4196 1.3371 1.2350 -0.0061 -0.0966 0.0108  503  A1A5I A C17 
17558 C  C20 . A1A5I I .   ? 1.4871 1.3119 1.1897 0.0110  -0.0895 0.0058  503  A1A5I A C20 
17559 C  C21 . A1A5I I .   ? 1.4815 1.3067 1.1855 0.0099  -0.0765 0.0071  503  A1A5I A C21 
17560 C  C22 . A1A5I I .   ? 1.5730 1.3760 1.2503 0.0151  -0.0701 0.0082  503  A1A5I A C22 
17561 C  C23 . A1A5I I .   ? 1.6142 1.4013 1.2713 0.0191  -0.0800 0.0056  503  A1A5I A C23 
17562 C  C25 . A1A5I I .   ? 1.5473 1.3581 1.2327 0.0142  -0.0993 0.0030  503  A1A5I A C25 
17563 C  C26 . A1A5I I .   ? 1.7193 1.4924 1.3586 0.0235  -0.1041 0.0012  503  A1A5I A C26 
17564 C  C27 . A1A5I I .   ? 1.7123 1.4693 1.3315 0.0288  -0.1107 0.0014  503  A1A5I A C27 
17565 C  C28 . A1A5I I .   ? 1.6713 1.4349 1.2999 0.0249  -0.0737 0.0069  503  A1A5I A C28 
17566 C  C4  . A1A5I I .   ? 1.3450 1.2027 1.0875 0.0061  -0.0919 0.0101  503  A1A5I A C4  
17567 C  C5  . A1A5I I .   ? 1.3707 1.2295 1.1155 0.0054  -0.0803 0.0129  503  A1A5I A C5  
17568 C  C6  . A1A5I I .   ? 1.3297 1.1749 1.0591 0.0077  -0.0700 0.0144  503  A1A5I A C6  
17569 C  C7  . A1A5I I .   ? 1.3210 1.1949 1.0828 0.0033  -0.1006 0.0092  503  A1A5I A C7  
17570 C  C9  . A1A5I I .   ? 1.4122 1.2878 1.1776 0.0023  -0.0810 0.0138  503  A1A5I A C9  
17571 N  N16 . A1A5I I .   ? 1.4148 1.3459 1.2465 -0.0082 -0.1047 0.0098  503  A1A5I A N16 
17572 N  N24 . A1A5I I .   ? 1.6248 1.4134 1.2830 0.0196  -0.0937 0.0040  503  A1A5I A N24 
17573 N  N8  . A1A5I I .   ? 1.3347 1.2182 1.1087 0.0013  -0.0927 0.0117  503  A1A5I A N8  
17574 O  O10 . A1A5I I .   ? 1.4819 1.2978 1.1736 0.0141  -0.0867 0.0081  503  A1A5I A O10 
17575 O  O11 . A1A5I I .   ? 1.3957 1.2770 1.1692 0.0008  -0.0731 0.0160  503  A1A5I A O11 
17576 O  O18 . A1A5I I .   ? 1.4764 1.3964 1.2954 -0.0080 -0.0890 0.0110  503  A1A5I A O18 
17577 O  O19 . A1A5I I .   ? 1.2716 1.2155 1.1189 -0.0086 -0.1193 0.0087  503  A1A5I A O19 
17578 ZN ZN  . ZN    J .   ? 1.2666 1.0673 0.9495 0.0198  -0.0446 0.0289  900  ZN    C ZN  
17579 ZN ZN  . ZN    K .   ? 1.3621 1.0353 0.9898 0.1835  -0.0725 -0.0247 501  ZN    D ZN  
17580 S  S   . SO4   L .   ? 2.0307 2.0259 2.0246 0.0515  -0.0747 -0.0564 502  SO4   D S   
17581 O  O1  . SO4   L .   ? 1.8608 1.8611 1.8577 0.0440  -0.0703 -0.0534 502  SO4   D O1  
17582 O  O2  . SO4   L .   ? 1.9855 1.9899 1.9921 0.0545  -0.0781 -0.0596 502  SO4   D O2  
17583 O  O3  . SO4   L .   ? 1.8802 1.8667 1.8631 0.0531  -0.0755 -0.0542 502  SO4   D O3  
17584 O  O4  . SO4   L .   ? 1.8842 1.8732 1.8730 0.0545  -0.0750 -0.0584 502  SO4   D O4  
17585 C  C1  . A1A5I M .   ? 1.6985 1.1458 1.1397 0.1840  0.0004  0.0106  503  A1A5I D C1  
17586 C  C2  . A1A5I M .   ? 1.7334 1.1677 1.1602 0.1917  -0.0063 0.0070  503  A1A5I D C2  
17587 C  C3  . A1A5I M .   ? 1.7449 1.1929 1.1834 0.1928  -0.0174 0.0004  503  A1A5I D C3  
17588 C  C12 . A1A5I M .   ? 1.5759 1.1150 1.1030 0.1738  -0.0391 -0.0136 503  A1A5I D C12 
17589 C  C13 . A1A5I M .   ? 1.5862 1.1270 1.1106 0.1839  -0.0509 -0.0200 503  A1A5I D C13 
17590 C  C14 . A1A5I M .   ? 1.5661 1.1307 1.1145 0.1797  -0.0581 -0.0250 503  A1A5I D C14 
17591 C  C15 . A1A5I M .   ? 1.5949 1.1644 1.1517 0.1737  -0.0570 -0.0256 503  A1A5I D C15 
17592 C  C17 . A1A5I M .   ? 1.6416 1.1872 1.1790 0.1671  -0.0387 -0.0145 503  A1A5I D C17 
17593 C  C20 . A1A5I M .   ? 1.7546 1.1526 1.1507 0.1953  0.0018  0.0113  503  A1A5I D C20 
17594 C  C21 . A1A5I M .   ? 1.7732 1.1658 1.1705 0.1865  0.0160  0.0188  503  A1A5I D C21 
17595 C  C22 . A1A5I M .   ? 1.7952 1.1652 1.1689 0.1932  0.0239  0.0238  503  A1A5I D C22 
17596 C  C23 . A1A5I M .   ? 1.8803 1.2252 1.2251 0.2061  0.0195  0.0219  503  A1A5I D C23 
17597 C  C25 . A1A5I M .   ? 1.8504 1.2232 1.2184 0.2076  -0.0019 0.0098  503  A1A5I D C25 
17598 C  C26 . A1A5I M .   ? 2.0405 1.3707 1.3596 0.2277  -0.0010 0.0119  503  A1A5I D C26 
17599 C  C27 . A1A5I M .   ? 1.9802 1.3144 1.2962 0.2372  -0.0118 0.0067  503  A1A5I D C27 
17600 C  C28 . A1A5I M .   ? 1.8457 1.1666 1.1652 0.2135  0.0274  0.0268  503  A1A5I D C28 
17601 C  C4  . A1A5I M .   ? 1.6696 1.1437 1.1338 0.1861  -0.0216 -0.0023 503  A1A5I D C4  
17602 C  C5  . A1A5I M .   ? 1.6585 1.1453 1.1367 0.1782  -0.0150 0.0013  503  A1A5I D C5  
17603 C  C6  . A1A5I M .   ? 1.6814 1.1549 1.1483 0.1772  -0.0042 0.0077  503  A1A5I D C6  
17604 C  C7  . A1A5I M .   ? 1.6450 1.1374 1.1258 0.1862  -0.0326 -0.0090 503  A1A5I D C7  
17605 C  C9  . A1A5I M .   ? 1.6146 1.1279 1.1187 0.1722  -0.0212 -0.0026 503  A1A5I D C9  
17606 N  N16 . A1A5I M .   ? 1.6417 1.2011 1.1919 0.1680  -0.0477 -0.0204 503  A1A5I D N16 
17607 N  N24 . A1A5I M .   ? 1.9498 1.3031 1.2966 0.2138  0.0049  0.0143  503  A1A5I D N24 
17608 N  N8  . A1A5I M .   ? 1.6046 1.1207 1.1096 0.1771  -0.0313 -0.0086 503  A1A5I D N8  
17609 O  O10 . A1A5I M .   ? 1.7695 1.1772 1.1703 0.1984  -0.0018 0.0098  503  A1A5I D O10 
17610 O  O11 . A1A5I M .   ? 1.6108 1.1410 1.1326 0.1645  -0.0183 -0.0011 503  A1A5I D O11 
17611 O  O18 . A1A5I M .   ? 1.6728 1.2112 1.2073 0.1611  -0.0305 -0.0101 503  A1A5I D O18 
17612 O  O19 . A1A5I M .   ? 1.5933 1.1748 1.1623 0.1739  -0.0640 -0.0304 503  A1A5I D O19 
17613 S  S   . SO4   N .   ? 1.7821 1.8629 1.8927 0.0573  -0.1234 -0.0662 1201 SO4   E S   
17614 O  O1  . SO4   N .   ? 1.6847 1.7582 1.7859 0.0611  -0.1242 -0.0670 1201 SO4   E O1  
17615 O  O2  . SO4   N .   ? 1.6430 1.7305 1.7702 0.0577  -0.1283 -0.0707 1201 SO4   E O2  
17616 O  O3  . SO4   N .   ? 1.5868 1.6742 1.7001 0.0501  -0.1155 -0.0619 1201 SO4   E O3  
17617 O  O4  . SO4   N .   ? 1.6270 1.7010 1.7274 0.0605  -0.1257 -0.0652 1201 SO4   E O4  
17618 ZN ZN  . ZN    O .   ? 1.4833 0.9904 0.9652 0.1876  -0.0074 0.0086  900  ZN    F ZN  
17619 O  O   . HOH   P .   ? 1.3307 1.4685 1.5389 -0.0504 -0.0042 -0.0059 601  HOH   A O   
17620 O  O   . HOH   P .   ? 0.9804 0.9996 0.9409 -0.0128 -0.0662 0.0339  602  HOH   A O   
17621 O  O   . HOH   P .   ? 0.8376 0.9841 0.9441 -0.0051 -0.0809 0.0275  603  HOH   A O   
17622 O  O   . HOH   P .   ? 0.8254 0.9601 0.9564 -0.0434 -0.0291 0.0014  604  HOH   A O   
17623 O  O   . HOH   Q .   ? 0.9051 1.0083 1.1413 0.0261  -0.1665 -0.0747 1201 HOH   B O   
17624 O  O   . HOH   Q .   ? 1.1577 1.1817 1.1711 0.0891  -0.1168 -0.0170 1202 HOH   B O   
17625 O  O   . HOH   Q .   ? 1.4675 1.6550 1.6161 0.0315  -0.0811 0.0385  1203 HOH   B O   
17626 O  O   . HOH   Q .   ? 1.0092 0.9940 0.9402 0.1156  -0.0735 -0.0048 1204 HOH   B O   
17627 O  O   . HOH   Q .   ? 0.8937 0.9745 0.9539 -0.0147 -0.0633 0.0301  1205 HOH   B O   
17629 O  O   . HOH   R .   ? 1.5812 1.1142 0.9265 0.0913  -0.0936 0.0111  1002 HOH   C O   
17632 O  O   . HOH   S .   ? 1.2288 1.0884 1.1090 -0.0107 -0.0461 -0.0274 602  HOH   D O   
17633 O  O   . HOH   S .   ? 1.0853 0.9626 0.9468 0.0866  -0.0735 -0.0392 603  HOH   D O   
17634 O  O   . HOH   S .   ? 1.0935 0.9818 1.0226 -0.0403 -0.0375 -0.0108 604  HOH   D O   
17635 O  O   . HOH   T .   ? 0.9989 1.0077 1.0169 -0.0824 -0.1513 -0.0262 1301 HOH   E O   
17636 O  O   . HOH   T .   ? 1.4614 1.2324 1.1477 -0.0120 -0.1733 -0.0478 1302 HOH   E O   
17637 O  O   . HOH   T .   ? 1.0291 1.1803 1.2704 0.0138  0.0076  -0.0622 1303 HOH   E O   
17638 O  O   . HOH   T .   ? 1.3541 1.1083 1.0425 -0.0176 -0.1361 -0.0584 1304 HOH   E O   
17639 O  O   . HOH   T .   ? 1.1423 1.2772 1.2526 -0.0125 -0.0576 -0.0099 1305 HOH   E O   
17640 O  O   . HOH   T .   ? 0.8696 0.9837 1.0158 0.0135  -0.0342 -0.0574 1306 HOH   E O   
# 
