data_8RHH
# 
_entry.id   8RHH 
# 
_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   8RHH         pdb_00008rhh 10.2210/pdb8rhh/pdb 
WWPDB D_1292135414 ?            ?                   
EMDB  EMD-19176    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RHH 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB 'Microtubule-associated kinesin-1 tail complex bound to AMPPNP, single-headed state' EMD-19174 'other EM volume'      
PDB  'Microtubule-associated kinesin-1 tail complex bound to AMPPNP, single-headed state' 8RHB      unspecified            
EMDB 'Microtubule-associated kinesin-1 tail complex bound to AMPPNP, two-headed state'    EMD-19176 'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 roberto.steiner@kcl.ac.uk Steiner Roberto  ? 'principal investigator/group leader' 0000-0001-7084-9745 
4 joseph.atherton@kcl.ac.uk Joseph  Atherton ? 'principal investigator/group leader' 0000-0002-6362-2347 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Atherton, J.'   1 0000-0002-6362-2347 
'Chegkazi, M.S.' 2 0000-0002-0855-2681 
'Steiner, R.A.'  3 0000-0001-7084-9745 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.11.11.622991 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Atherton, J.'   1 ? 
primary 'Chegkazi, M.S.' 2 ? 
primary 'Peirano, E.'    3 ? 
primary 'Pozzer, L.S.'   4 ? 
primary 'Foran, T.'      5 ? 
primary 'Steiner, R.A.'  6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Tubulin beta chain'                          49907.770  1 ? ? ? ? 
2 polymer     man 'Kinesin-1 heavy chain'                       109856.102 4 ? ? ? ? 
3 polymer     nat 'Tubulin alpha-1B chain'                      50204.445  1 ? ? ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                    443.201    1 ? ? ? ? 
5 non-polymer syn TAXOL                                         853.906    1 ? ? ? ? 
6 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196    2 ? ? ? ? 
7 non-polymer syn 'MAGNESIUM ION'                               24.305     3 ? ? ? ? 
8 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                   523.180    1 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 Beta-tubulin                                                                
2 'Conventional kinesin heavy chain,Ubiquitous kinesin heavy chain,UKHC'      
3 'Alpha-tubulin ubiquitous,Tubulin K-alpha-1,Tubulin alpha-ubiquitous chain' 
# 
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 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
;
B       ? 
2 'polypeptide(L)' no no 
;MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT
IFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN
RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ
RAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTN
DKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAE
NDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLK
DLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHE
AKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLR
DEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLR
KLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESA
LKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPSAIRGGGAFVQNSQPVAVRGGGG
KQV
;
;MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT
IFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN
RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ
RAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTN
DKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAE
NDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLK
DLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHE
AKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLR
DEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLR
KLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESA
LKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPSAIRGGGAFVQNSQPVAVRGGGG
KQV
;
K,L,T,t ? 
3 'polypeptide(L)' no no 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
A       ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "GUANOSINE-5'-DIPHOSPHATE"                    GDP 
5 TAXOL                                         TA1 
6 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
7 'MAGNESIUM ION'                               MG  
8 "GUANOSINE-5'-TRIPHOSPHATE"                   GTP 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   GLU n 
1 4   ILE n 
1 5   VAL n 
1 6   HIS n 
1 7   ILE n 
1 8   GLN n 
1 9   ALA n 
1 10  GLY n 
1 11  GLN n 
1 12  CYS n 
1 13  GLY n 
1 14  ASN n 
1 15  GLN n 
1 16  ILE n 
1 17  GLY n 
1 18  ALA n 
1 19  LYS n 
1 20  PHE n 
1 21  TRP n 
1 22  GLU n 
1 23  VAL n 
1 24  ILE n 
1 25  SER n 
1 26  ASP n 
1 27  GLU n 
1 28  HIS n 
1 29  GLY n 
1 30  ILE n 
1 31  ASP n 
1 32  PRO n 
1 33  THR n 
1 34  GLY n 
1 35  SER n 
1 36  TYR n 
1 37  HIS n 
1 38  GLY n 
1 39  ASP n 
1 40  SER n 
1 41  ASP n 
1 42  LEU n 
1 43  GLN n 
1 44  LEU n 
1 45  GLU n 
1 46  ARG n 
1 47  ILE n 
1 48  ASN n 
1 49  VAL n 
1 50  TYR n 
1 51  TYR n 
1 52  ASN n 
1 53  GLU n 
1 54  ALA n 
1 55  ALA n 
1 56  GLY n 
1 57  ASN n 
1 58  LYS n 
1 59  TYR n 
1 60  VAL n 
1 61  PRO n 
1 62  ARG n 
1 63  ALA n 
1 64  ILE n 
1 65  LEU n 
1 66  VAL n 
1 67  ASP n 
1 68  LEU n 
1 69  GLU n 
1 70  PRO n 
1 71  GLY n 
1 72  THR n 
1 73  MET n 
1 74  ASP n 
1 75  SER n 
1 76  VAL n 
1 77  ARG n 
1 78  SER n 
1 79  GLY n 
1 80  PRO n 
1 81  PHE n 
1 82  GLY n 
1 83  GLN n 
1 84  ILE n 
1 85  PHE n 
1 86  ARG n 
1 87  PRO n 
1 88  ASP n 
1 89  ASN n 
1 90  PHE n 
1 91  VAL n 
1 92  PHE n 
1 93  GLY n 
1 94  GLN n 
1 95  SER n 
1 96  GLY n 
1 97  ALA n 
1 98  GLY n 
1 99  ASN n 
1 100 ASN n 
1 101 TRP n 
1 102 ALA n 
1 103 LYS n 
1 104 GLY n 
1 105 HIS n 
1 106 TYR n 
1 107 THR n 
1 108 GLU n 
1 109 GLY n 
1 110 ALA n 
1 111 GLU n 
1 112 LEU n 
1 113 VAL n 
1 114 ASP n 
1 115 SER n 
1 116 VAL n 
1 117 LEU n 
1 118 ASP n 
1 119 VAL n 
1 120 VAL n 
1 121 ARG n 
1 122 LYS n 
1 123 GLU n 
1 124 SER n 
1 125 GLU n 
1 126 SER n 
1 127 CYS n 
1 128 ASP n 
1 129 CYS n 
1 130 LEU n 
1 131 GLN n 
1 132 GLY n 
1 133 PHE n 
1 134 GLN n 
1 135 LEU n 
1 136 THR n 
1 137 HIS n 
1 138 SER n 
1 139 LEU n 
1 140 GLY n 
1 141 GLY n 
1 142 GLY n 
1 143 THR n 
1 144 GLY n 
1 145 SER n 
1 146 GLY n 
1 147 MET n 
1 148 GLY n 
1 149 THR n 
1 150 LEU n 
1 151 LEU n 
1 152 ILE n 
1 153 SER n 
1 154 LYS n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 GLU n 
1 159 TYR n 
1 160 PRO n 
1 161 ASP n 
1 162 ARG n 
1 163 ILE n 
1 164 MET n 
1 165 ASN n 
1 166 THR n 
1 167 PHE n 
1 168 SER n 
1 169 VAL n 
1 170 VAL n 
1 171 PRO n 
1 172 SER n 
1 173 PRO n 
1 174 LYS n 
1 175 VAL n 
1 176 SER n 
1 177 ASP n 
1 178 THR n 
1 179 VAL n 
1 180 VAL n 
1 181 GLU n 
1 182 PRO n 
1 183 TYR n 
1 184 ASN n 
1 185 ALA n 
1 186 THR n 
1 187 LEU n 
1 188 SER n 
1 189 VAL n 
1 190 HIS n 
1 191 GLN n 
1 192 LEU n 
1 193 VAL n 
1 194 GLU n 
1 195 ASN n 
1 196 THR n 
1 197 ASP n 
1 198 GLU n 
1 199 THR n 
1 200 TYR n 
1 201 CYS n 
1 202 ILE n 
1 203 ASP n 
1 204 ASN n 
1 205 GLU n 
1 206 ALA n 
1 207 LEU n 
1 208 TYR n 
1 209 ASP n 
1 210 ILE n 
1 211 CYS n 
1 212 PHE n 
1 213 ARG n 
1 214 THR n 
1 215 LEU n 
1 216 LYS n 
1 217 LEU n 
1 218 THR n 
1 219 THR n 
1 220 PRO n 
1 221 THR n 
1 222 TYR n 
1 223 GLY n 
1 224 ASP n 
1 225 LEU n 
1 226 ASN n 
1 227 HIS n 
1 228 LEU n 
1 229 VAL n 
1 230 SER n 
1 231 ALA n 
1 232 THR n 
1 233 MET n 
1 234 SER n 
1 235 GLY n 
1 236 VAL n 
1 237 THR n 
1 238 THR n 
1 239 CYS n 
1 240 LEU n 
1 241 ARG n 
1 242 PHE n 
1 243 PRO n 
1 244 GLY n 
1 245 GLN n 
1 246 LEU n 
1 247 ASN n 
1 248 ALA n 
1 249 ASP n 
1 250 LEU n 
1 251 ARG n 
1 252 LYS n 
1 253 LEU n 
1 254 ALA n 
1 255 VAL n 
1 256 ASN n 
1 257 MET n 
1 258 VAL n 
1 259 PRO n 
1 260 PHE n 
1 261 PRO n 
1 262 ARG n 
1 263 LEU n 
1 264 HIS n 
1 265 PHE n 
1 266 PHE n 
1 267 MET n 
1 268 PRO n 
1 269 GLY n 
1 270 PHE n 
1 271 ALA n 
1 272 PRO n 
1 273 LEU n 
1 274 THR n 
1 275 SER n 
1 276 ARG n 
1 277 GLY n 
1 278 SER n 
1 279 GLN n 
1 280 GLN n 
1 281 TYR n 
1 282 ARG n 
1 283 ALA n 
1 284 LEU n 
1 285 THR n 
1 286 VAL n 
1 287 PRO n 
1 288 GLU n 
1 289 LEU n 
1 290 THR n 
1 291 GLN n 
1 292 GLN n 
1 293 MET n 
1 294 PHE n 
1 295 ASP n 
1 296 ALA n 
1 297 LYS n 
1 298 ASN n 
1 299 MET n 
1 300 MET n 
1 301 ALA n 
1 302 ALA n 
1 303 CYS n 
1 304 ASP n 
1 305 PRO n 
1 306 ARG n 
1 307 HIS n 
1 308 GLY n 
1 309 ARG n 
1 310 TYR n 
1 311 LEU n 
1 312 THR n 
1 313 VAL n 
1 314 ALA n 
1 315 ALA n 
1 316 VAL n 
1 317 PHE n 
1 318 ARG n 
1 319 GLY n 
1 320 ARG n 
1 321 MET n 
1 322 SER n 
1 323 MET n 
1 324 LYS n 
1 325 GLU n 
1 326 VAL n 
1 327 ASP n 
1 328 GLU n 
1 329 GLN n 
1 330 MET n 
1 331 LEU n 
1 332 ASN n 
1 333 VAL n 
1 334 GLN n 
1 335 ASN n 
1 336 LYS n 
1 337 ASN n 
1 338 SER n 
1 339 SER n 
1 340 TYR n 
1 341 PHE n 
1 342 VAL n 
1 343 GLU n 
1 344 TRP n 
1 345 ILE n 
1 346 PRO n 
1 347 ASN n 
1 348 ASN n 
1 349 VAL n 
1 350 LYS n 
1 351 THR n 
1 352 ALA n 
1 353 VAL n 
1 354 CYS n 
1 355 ASP n 
1 356 ILE n 
1 357 PRO n 
1 358 PRO n 
1 359 ARG n 
1 360 GLY n 
1 361 LEU n 
1 362 LYS n 
1 363 MET n 
1 364 SER n 
1 365 ALA n 
1 366 THR n 
1 367 PHE n 
1 368 ILE n 
1 369 GLY n 
1 370 ASN n 
1 371 SER n 
1 372 THR n 
1 373 ALA n 
1 374 ILE n 
1 375 GLN n 
1 376 GLU n 
1 377 LEU n 
1 378 PHE n 
1 379 LYS n 
1 380 ARG n 
1 381 ILE n 
1 382 SER n 
1 383 GLU n 
1 384 GLN n 
1 385 PHE n 
1 386 THR n 
1 387 ALA n 
1 388 MET n 
1 389 PHE n 
1 390 ARG n 
1 391 ARG n 
1 392 LYS n 
1 393 ALA n 
1 394 PHE n 
1 395 LEU n 
1 396 HIS n 
1 397 TRP n 
1 398 TYR n 
1 399 THR n 
1 400 GLY n 
1 401 GLU n 
1 402 GLY n 
1 403 MET n 
1 404 ASP n 
1 405 GLU n 
1 406 MET n 
1 407 GLU n 
1 408 PHE n 
1 409 THR n 
1 410 GLU n 
1 411 ALA n 
1 412 GLU n 
1 413 SER n 
1 414 ASN n 
1 415 MET n 
1 416 ASN n 
1 417 ASP n 
1 418 LEU n 
1 419 VAL n 
1 420 SER n 
1 421 GLU n 
1 422 TYR n 
1 423 GLN n 
1 424 GLN n 
1 425 TYR n 
1 426 GLN n 
1 427 ASP n 
1 428 ALA n 
1 429 THR n 
1 430 ALA n 
1 431 ASP n 
1 432 GLU n 
1 433 GLN n 
1 434 GLY n 
1 435 GLU n 
1 436 PHE n 
1 437 GLU n 
1 438 GLU n 
1 439 GLU n 
1 440 GLY n 
1 441 GLU n 
1 442 GLU n 
1 443 ASP n 
1 444 GLU n 
1 445 ALA n 
2 1   MET n 
2 2   ALA n 
2 3   ASP n 
2 4   LEU n 
2 5   ALA n 
2 6   GLU n 
2 7   CYS n 
2 8   ASN n 
2 9   ILE n 
2 10  LYS n 
2 11  VAL n 
2 12  MET n 
2 13  CYS n 
2 14  ARG n 
2 15  PHE n 
2 16  ARG n 
2 17  PRO n 
2 18  LEU n 
2 19  ASN n 
2 20  GLU n 
2 21  SER n 
2 22  GLU n 
2 23  VAL n 
2 24  ASN n 
2 25  ARG n 
2 26  GLY n 
2 27  ASP n 
2 28  LYS n 
2 29  TYR n 
2 30  ILE n 
2 31  ALA n 
2 32  LYS n 
2 33  PHE n 
2 34  GLN n 
2 35  GLY n 
2 36  GLU n 
2 37  ASP n 
2 38  THR n 
2 39  VAL n 
2 40  VAL n 
2 41  ILE n 
2 42  ALA n 
2 43  SER n 
2 44  LYS n 
2 45  PRO n 
2 46  TYR n 
2 47  ALA n 
2 48  PHE n 
2 49  ASP n 
2 50  ARG n 
2 51  VAL n 
2 52  PHE n 
2 53  GLN n 
2 54  SER n 
2 55  SER n 
2 56  THR n 
2 57  SER n 
2 58  GLN n 
2 59  GLU n 
2 60  GLN n 
2 61  VAL n 
2 62  TYR n 
2 63  ASN n 
2 64  ASP n 
2 65  CYS n 
2 66  ALA n 
2 67  LYS n 
2 68  LYS n 
2 69  ILE n 
2 70  VAL n 
2 71  LYS n 
2 72  ASP n 
2 73  VAL n 
2 74  LEU n 
2 75  GLU n 
2 76  GLY n 
2 77  TYR n 
2 78  ASN n 
2 79  GLY n 
2 80  THR n 
2 81  ILE n 
2 82  PHE n 
2 83  ALA n 
2 84  TYR n 
2 85  GLY n 
2 86  GLN n 
2 87  THR n 
2 88  SER n 
2 89  SER n 
2 90  GLY n 
2 91  LYS n 
2 92  THR n 
2 93  HIS n 
2 94  THR n 
2 95  MET n 
2 96  GLU n 
2 97  GLY n 
2 98  LYS n 
2 99  LEU n 
2 100 HIS n 
2 101 ASP n 
2 102 PRO n 
2 103 GLU n 
2 104 GLY n 
2 105 MET n 
2 106 GLY n 
2 107 ILE n 
2 108 ILE n 
2 109 PRO n 
2 110 ARG n 
2 111 ILE n 
2 112 VAL n 
2 113 GLN n 
2 114 ASP n 
2 115 ILE n 
2 116 PHE n 
2 117 ASN n 
2 118 TYR n 
2 119 ILE n 
2 120 TYR n 
2 121 SER n 
2 122 MET n 
2 123 ASP n 
2 124 GLU n 
2 125 ASN n 
2 126 LEU n 
2 127 GLU n 
2 128 PHE n 
2 129 HIS n 
2 130 ILE n 
2 131 LYS n 
2 132 VAL n 
2 133 SER n 
2 134 TYR n 
2 135 PHE n 
2 136 GLU n 
2 137 ILE n 
2 138 TYR n 
2 139 LEU n 
2 140 ASP n 
2 141 LYS n 
2 142 ILE n 
2 143 ARG n 
2 144 ASP n 
2 145 LEU n 
2 146 LEU n 
2 147 ASP n 
2 148 VAL n 
2 149 SER n 
2 150 LYS n 
2 151 THR n 
2 152 ASN n 
2 153 LEU n 
2 154 SER n 
2 155 VAL n 
2 156 HIS n 
2 157 GLU n 
2 158 ASP n 
2 159 LYS n 
2 160 ASN n 
2 161 ARG n 
2 162 VAL n 
2 163 PRO n 
2 164 TYR n 
2 165 VAL n 
2 166 LYS n 
2 167 GLY n 
2 168 CYS n 
2 169 THR n 
2 170 GLU n 
2 171 ARG n 
2 172 PHE n 
2 173 VAL n 
2 174 CYS n 
2 175 SER n 
2 176 PRO n 
2 177 ASP n 
2 178 GLU n 
2 179 VAL n 
2 180 MET n 
2 181 ASP n 
2 182 THR n 
2 183 ILE n 
2 184 ASP n 
2 185 GLU n 
2 186 GLY n 
2 187 LYS n 
2 188 SER n 
2 189 ASN n 
2 190 ARG n 
2 191 HIS n 
2 192 VAL n 
2 193 ALA n 
2 194 VAL n 
2 195 THR n 
2 196 ASN n 
2 197 MET n 
2 198 ASN n 
2 199 GLU n 
2 200 HIS n 
2 201 SER n 
2 202 SER n 
2 203 ARG n 
2 204 SER n 
2 205 HIS n 
2 206 SER n 
2 207 ILE n 
2 208 PHE n 
2 209 LEU n 
2 210 ILE n 
2 211 ASN n 
2 212 VAL n 
2 213 LYS n 
2 214 GLN n 
2 215 GLU n 
2 216 ASN n 
2 217 THR n 
2 218 GLN n 
2 219 THR n 
2 220 GLU n 
2 221 GLN n 
2 222 LYS n 
2 223 LEU n 
2 224 SER n 
2 225 GLY n 
2 226 LYS n 
2 227 LEU n 
2 228 TYR n 
2 229 LEU n 
2 230 VAL n 
2 231 ASP n 
2 232 LEU n 
2 233 ALA n 
2 234 GLY n 
2 235 SER n 
2 236 GLU n 
2 237 LYS n 
2 238 VAL n 
2 239 SER n 
2 240 LYS n 
2 241 THR n 
2 242 GLY n 
2 243 ALA n 
2 244 GLU n 
2 245 GLY n 
2 246 ALA n 
2 247 VAL n 
2 248 LEU n 
2 249 ASP n 
2 250 GLU n 
2 251 ALA n 
2 252 LYS n 
2 253 ASN n 
2 254 ILE n 
2 255 ASN n 
2 256 LYS n 
2 257 SER n 
2 258 LEU n 
2 259 SER n 
2 260 ALA n 
2 261 LEU n 
2 262 GLY n 
2 263 ASN n 
2 264 VAL n 
2 265 ILE n 
2 266 SER n 
2 267 ALA n 
2 268 LEU n 
2 269 ALA n 
2 270 GLU n 
2 271 GLY n 
2 272 SER n 
2 273 THR n 
2 274 TYR n 
2 275 VAL n 
2 276 PRO n 
2 277 TYR n 
2 278 ARG n 
2 279 ASP n 
2 280 SER n 
2 281 LYS n 
2 282 MET n 
2 283 THR n 
2 284 ARG n 
2 285 ILE n 
2 286 LEU n 
2 287 GLN n 
2 288 ASP n 
2 289 SER n 
2 290 LEU n 
2 291 GLY n 
2 292 GLY n 
2 293 ASN n 
2 294 CYS n 
2 295 ARG n 
2 296 THR n 
2 297 THR n 
2 298 ILE n 
2 299 VAL n 
2 300 ILE n 
2 301 CYS n 
2 302 CYS n 
2 303 SER n 
2 304 PRO n 
2 305 SER n 
2 306 SER n 
2 307 TYR n 
2 308 ASN n 
2 309 GLU n 
2 310 SER n 
2 311 GLU n 
2 312 THR n 
2 313 LYS n 
2 314 SER n 
2 315 THR n 
2 316 LEU n 
2 317 LEU n 
2 318 PHE n 
2 319 GLY n 
2 320 GLN n 
2 321 ARG n 
2 322 ALA n 
2 323 LYS n 
2 324 THR n 
2 325 ILE n 
2 326 LYS n 
2 327 ASN n 
2 328 THR n 
2 329 VAL n 
2 330 CYS n 
2 331 VAL n 
2 332 ASN n 
2 333 VAL n 
2 334 GLU n 
2 335 LEU n 
2 336 THR n 
2 337 ALA n 
2 338 GLU n 
2 339 GLN n 
2 340 TRP n 
2 341 LYS n 
2 342 LYS n 
2 343 LYS n 
2 344 TYR n 
2 345 GLU n 
2 346 LYS n 
2 347 GLU n 
2 348 LYS n 
2 349 GLU n 
2 350 LYS n 
2 351 ASN n 
2 352 LYS n 
2 353 ILE n 
2 354 LEU n 
2 355 ARG n 
2 356 ASN n 
2 357 THR n 
2 358 ILE n 
2 359 GLN n 
2 360 TRP n 
2 361 LEU n 
2 362 GLU n 
2 363 ASN n 
2 364 GLU n 
2 365 LEU n 
2 366 ASN n 
2 367 ARG n 
2 368 TRP n 
2 369 ARG n 
2 370 ASN n 
2 371 GLY n 
2 372 GLU n 
2 373 THR n 
2 374 VAL n 
2 375 PRO n 
2 376 ILE n 
2 377 ASP n 
2 378 GLU n 
2 379 GLN n 
2 380 PHE n 
2 381 ASP n 
2 382 LYS n 
2 383 GLU n 
2 384 LYS n 
2 385 ALA n 
2 386 ASN n 
2 387 LEU n 
2 388 GLU n 
2 389 ALA n 
2 390 PHE n 
2 391 THR n 
2 392 VAL n 
2 393 ASP n 
2 394 LYS n 
2 395 ASP n 
2 396 ILE n 
2 397 THR n 
2 398 LEU n 
2 399 THR n 
2 400 ASN n 
2 401 ASP n 
2 402 LYS n 
2 403 PRO n 
2 404 ALA n 
2 405 THR n 
2 406 ALA n 
2 407 ILE n 
2 408 GLY n 
2 409 VAL n 
2 410 ILE n 
2 411 GLY n 
2 412 ASN n 
2 413 PHE n 
2 414 THR n 
2 415 ASP n 
2 416 ALA n 
2 417 GLU n 
2 418 ARG n 
2 419 ARG n 
2 420 LYS n 
2 421 CYS n 
2 422 GLU n 
2 423 GLU n 
2 424 GLU n 
2 425 ILE n 
2 426 ALA n 
2 427 LYS n 
2 428 LEU n 
2 429 TYR n 
2 430 LYS n 
2 431 GLN n 
2 432 LEU n 
2 433 ASP n 
2 434 ASP n 
2 435 LYS n 
2 436 ASP n 
2 437 GLU n 
2 438 GLU n 
2 439 ILE n 
2 440 ASN n 
2 441 GLN n 
2 442 GLN n 
2 443 SER n 
2 444 GLN n 
2 445 LEU n 
2 446 VAL n 
2 447 GLU n 
2 448 LYS n 
2 449 LEU n 
2 450 LYS n 
2 451 THR n 
2 452 GLN n 
2 453 MET n 
2 454 LEU n 
2 455 ASP n 
2 456 GLN n 
2 457 GLU n 
2 458 GLU n 
2 459 LEU n 
2 460 LEU n 
2 461 ALA n 
2 462 SER n 
2 463 THR n 
2 464 ARG n 
2 465 ARG n 
2 466 ASP n 
2 467 GLN n 
2 468 ASP n 
2 469 ASN n 
2 470 MET n 
2 471 GLN n 
2 472 ALA n 
2 473 GLU n 
2 474 LEU n 
2 475 ASN n 
2 476 ARG n 
2 477 LEU n 
2 478 GLN n 
2 479 ALA n 
2 480 GLU n 
2 481 ASN n 
2 482 ASP n 
2 483 ALA n 
2 484 SER n 
2 485 LYS n 
2 486 GLU n 
2 487 GLU n 
2 488 VAL n 
2 489 LYS n 
2 490 GLU n 
2 491 VAL n 
2 492 LEU n 
2 493 GLN n 
2 494 ALA n 
2 495 LEU n 
2 496 GLU n 
2 497 GLU n 
2 498 LEU n 
2 499 ALA n 
2 500 VAL n 
2 501 ASN n 
2 502 TYR n 
2 503 ASP n 
2 504 GLN n 
2 505 LYS n 
2 506 SER n 
2 507 GLN n 
2 508 GLU n 
2 509 VAL n 
2 510 GLU n 
2 511 ASP n 
2 512 LYS n 
2 513 THR n 
2 514 LYS n 
2 515 GLU n 
2 516 TYR n 
2 517 GLU n 
2 518 LEU n 
2 519 LEU n 
2 520 SER n 
2 521 ASP n 
2 522 GLU n 
2 523 LEU n 
2 524 ASN n 
2 525 GLN n 
2 526 LYS n 
2 527 SER n 
2 528 ALA n 
2 529 THR n 
2 530 LEU n 
2 531 ALA n 
2 532 SER n 
2 533 ILE n 
2 534 ASP n 
2 535 ALA n 
2 536 GLU n 
2 537 LEU n 
2 538 GLN n 
2 539 LYS n 
2 540 LEU n 
2 541 LYS n 
2 542 GLU n 
2 543 MET n 
2 544 THR n 
2 545 ASN n 
2 546 HIS n 
2 547 GLN n 
2 548 LYS n 
2 549 LYS n 
2 550 ARG n 
2 551 ALA n 
2 552 ALA n 
2 553 GLU n 
2 554 MET n 
2 555 MET n 
2 556 ALA n 
2 557 SER n 
2 558 LEU n 
2 559 LEU n 
2 560 LYS n 
2 561 ASP n 
2 562 LEU n 
2 563 ALA n 
2 564 GLU n 
2 565 ILE n 
2 566 GLY n 
2 567 ILE n 
2 568 ALA n 
2 569 VAL n 
2 570 GLY n 
2 571 ASN n 
2 572 ASN n 
2 573 ASP n 
2 574 VAL n 
2 575 LYS n 
2 576 GLN n 
2 577 PRO n 
2 578 GLU n 
2 579 GLY n 
2 580 THR n 
2 581 GLY n 
2 582 MET n 
2 583 ILE n 
2 584 ASP n 
2 585 GLU n 
2 586 GLU n 
2 587 PHE n 
2 588 THR n 
2 589 VAL n 
2 590 ALA n 
2 591 ARG n 
2 592 LEU n 
2 593 TYR n 
2 594 ILE n 
2 595 SER n 
2 596 LYS n 
2 597 MET n 
2 598 LYS n 
2 599 SER n 
2 600 GLU n 
2 601 VAL n 
2 602 LYS n 
2 603 THR n 
2 604 MET n 
2 605 VAL n 
2 606 LYS n 
2 607 ARG n 
2 608 CYS n 
2 609 LYS n 
2 610 GLN n 
2 611 LEU n 
2 612 GLU n 
2 613 SER n 
2 614 THR n 
2 615 GLN n 
2 616 THR n 
2 617 GLU n 
2 618 SER n 
2 619 ASN n 
2 620 LYS n 
2 621 LYS n 
2 622 MET n 
2 623 GLU n 
2 624 GLU n 
2 625 ASN n 
2 626 GLU n 
2 627 LYS n 
2 628 GLU n 
2 629 LEU n 
2 630 ALA n 
2 631 ALA n 
2 632 CYS n 
2 633 GLN n 
2 634 LEU n 
2 635 ARG n 
2 636 ILE n 
2 637 SER n 
2 638 GLN n 
2 639 HIS n 
2 640 GLU n 
2 641 ALA n 
2 642 LYS n 
2 643 ILE n 
2 644 LYS n 
2 645 SER n 
2 646 LEU n 
2 647 THR n 
2 648 GLU n 
2 649 TYR n 
2 650 LEU n 
2 651 GLN n 
2 652 ASN n 
2 653 VAL n 
2 654 GLU n 
2 655 GLN n 
2 656 LYS n 
2 657 LYS n 
2 658 ARG n 
2 659 GLN n 
2 660 LEU n 
2 661 GLU n 
2 662 GLU n 
2 663 SER n 
2 664 VAL n 
2 665 ASP n 
2 666 ALA n 
2 667 LEU n 
2 668 SER n 
2 669 GLU n 
2 670 GLU n 
2 671 LEU n 
2 672 VAL n 
2 673 GLN n 
2 674 LEU n 
2 675 ARG n 
2 676 ALA n 
2 677 GLN n 
2 678 GLU n 
2 679 LYS n 
2 680 VAL n 
2 681 HIS n 
2 682 GLU n 
2 683 MET n 
2 684 GLU n 
2 685 LYS n 
2 686 GLU n 
2 687 HIS n 
2 688 LEU n 
2 689 ASN n 
2 690 LYS n 
2 691 VAL n 
2 692 GLN n 
2 693 THR n 
2 694 ALA n 
2 695 ASN n 
2 696 GLU n 
2 697 VAL n 
2 698 LYS n 
2 699 GLN n 
2 700 ALA n 
2 701 VAL n 
2 702 GLU n 
2 703 GLN n 
2 704 GLN n 
2 705 ILE n 
2 706 GLN n 
2 707 SER n 
2 708 HIS n 
2 709 ARG n 
2 710 GLU n 
2 711 THR n 
2 712 HIS n 
2 713 GLN n 
2 714 LYS n 
2 715 GLN n 
2 716 ILE n 
2 717 SER n 
2 718 SER n 
2 719 LEU n 
2 720 ARG n 
2 721 ASP n 
2 722 GLU n 
2 723 VAL n 
2 724 GLU n 
2 725 ALA n 
2 726 LYS n 
2 727 ALA n 
2 728 LYS n 
2 729 LEU n 
2 730 ILE n 
2 731 THR n 
2 732 ASP n 
2 733 LEU n 
2 734 GLN n 
2 735 ASP n 
2 736 GLN n 
2 737 ASN n 
2 738 GLN n 
2 739 LYS n 
2 740 MET n 
2 741 MET n 
2 742 LEU n 
2 743 GLU n 
2 744 GLN n 
2 745 GLU n 
2 746 ARG n 
2 747 LEU n 
2 748 ARG n 
2 749 VAL n 
2 750 GLU n 
2 751 HIS n 
2 752 GLU n 
2 753 LYS n 
2 754 LEU n 
2 755 LYS n 
2 756 ALA n 
2 757 THR n 
2 758 ASP n 
2 759 GLN n 
2 760 GLU n 
2 761 LYS n 
2 762 SER n 
2 763 ARG n 
2 764 LYS n 
2 765 LEU n 
2 766 HIS n 
2 767 GLU n 
2 768 LEU n 
2 769 THR n 
2 770 VAL n 
2 771 MET n 
2 772 GLN n 
2 773 ASP n 
2 774 ARG n 
2 775 ARG n 
2 776 GLU n 
2 777 GLN n 
2 778 ALA n 
2 779 ARG n 
2 780 GLN n 
2 781 ASP n 
2 782 LEU n 
2 783 LYS n 
2 784 GLY n 
2 785 LEU n 
2 786 GLU n 
2 787 GLU n 
2 788 THR n 
2 789 VAL n 
2 790 ALA n 
2 791 LYS n 
2 792 GLU n 
2 793 LEU n 
2 794 GLN n 
2 795 THR n 
2 796 LEU n 
2 797 HIS n 
2 798 ASN n 
2 799 LEU n 
2 800 ARG n 
2 801 LYS n 
2 802 LEU n 
2 803 PHE n 
2 804 VAL n 
2 805 GLN n 
2 806 ASP n 
2 807 LEU n 
2 808 ALA n 
2 809 THR n 
2 810 ARG n 
2 811 VAL n 
2 812 LYS n 
2 813 LYS n 
2 814 SER n 
2 815 ALA n 
2 816 GLU n 
2 817 ILE n 
2 818 ASP n 
2 819 SER n 
2 820 ASP n 
2 821 ASP n 
2 822 THR n 
2 823 GLY n 
2 824 GLY n 
2 825 SER n 
2 826 ALA n 
2 827 ALA n 
2 828 GLN n 
2 829 LYS n 
2 830 GLN n 
2 831 LYS n 
2 832 ILE n 
2 833 SER n 
2 834 PHE n 
2 835 LEU n 
2 836 GLU n 
2 837 ASN n 
2 838 ASN n 
2 839 LEU n 
2 840 GLU n 
2 841 GLN n 
2 842 LEU n 
2 843 THR n 
2 844 LYS n 
2 845 VAL n 
2 846 HIS n 
2 847 LYS n 
2 848 GLN n 
2 849 LEU n 
2 850 VAL n 
2 851 ARG n 
2 852 ASP n 
2 853 ASN n 
2 854 ALA n 
2 855 ASP n 
2 856 LEU n 
2 857 ARG n 
2 858 CYS n 
2 859 GLU n 
2 860 LEU n 
2 861 PRO n 
2 862 LYS n 
2 863 LEU n 
2 864 GLU n 
2 865 LYS n 
2 866 ARG n 
2 867 LEU n 
2 868 ARG n 
2 869 ALA n 
2 870 THR n 
2 871 ALA n 
2 872 GLU n 
2 873 ARG n 
2 874 VAL n 
2 875 LYS n 
2 876 ALA n 
2 877 LEU n 
2 878 GLU n 
2 879 SER n 
2 880 ALA n 
2 881 LEU n 
2 882 LYS n 
2 883 GLU n 
2 884 ALA n 
2 885 LYS n 
2 886 GLU n 
2 887 ASN n 
2 888 ALA n 
2 889 SER n 
2 890 ARG n 
2 891 ASP n 
2 892 ARG n 
2 893 LYS n 
2 894 ARG n 
2 895 TYR n 
2 896 GLN n 
2 897 GLN n 
2 898 GLU n 
2 899 VAL n 
2 900 ASP n 
2 901 ARG n 
2 902 ILE n 
2 903 LYS n 
2 904 GLU n 
2 905 ALA n 
2 906 VAL n 
2 907 ARG n 
2 908 SER n 
2 909 LYS n 
2 910 ASN n 
2 911 MET n 
2 912 ALA n 
2 913 ARG n 
2 914 ARG n 
2 915 GLY n 
2 916 HIS n 
2 917 SER n 
2 918 ALA n 
2 919 GLN n 
2 920 ILE n 
2 921 ALA n 
2 922 LYS n 
2 923 PRO n 
2 924 ILE n 
2 925 ARG n 
2 926 PRO n 
2 927 GLY n 
2 928 GLN n 
2 929 HIS n 
2 930 PRO n 
2 931 ALA n 
2 932 ALA n 
2 933 SER n 
2 934 PRO n 
2 935 THR n 
2 936 HIS n 
2 937 PRO n 
2 938 SER n 
2 939 ALA n 
2 940 ILE n 
2 941 ARG n 
2 942 GLY n 
2 943 GLY n 
2 944 GLY n 
2 945 ALA n 
2 946 PHE n 
2 947 VAL n 
2 948 GLN n 
2 949 ASN n 
2 950 SER n 
2 951 GLN n 
2 952 PRO n 
2 953 VAL n 
2 954 ALA n 
2 955 VAL n 
2 956 ARG n 
2 957 GLY n 
2 958 GLY n 
2 959 GLY n 
2 960 GLY n 
2 961 LYS n 
2 962 GLN n 
2 963 VAL n 
3 1   MET n 
3 2   ARG n 
3 3   GLU n 
3 4   CYS n 
3 5   ILE n 
3 6   SER n 
3 7   ILE n 
3 8   HIS n 
3 9   VAL n 
3 10  GLY n 
3 11  GLN n 
3 12  ALA n 
3 13  GLY n 
3 14  VAL n 
3 15  GLN n 
3 16  ILE n 
3 17  GLY n 
3 18  ASN n 
3 19  ALA n 
3 20  CYS n 
3 21  TRP n 
3 22  GLU n 
3 23  LEU n 
3 24  TYR n 
3 25  CYS n 
3 26  LEU n 
3 27  GLU n 
3 28  HIS n 
3 29  GLY n 
3 30  ILE n 
3 31  GLN n 
3 32  PRO n 
3 33  ASP n 
3 34  GLY n 
3 35  GLN n 
3 36  MET n 
3 37  PRO n 
3 38  SER n 
3 39  ASP n 
3 40  LYS n 
3 41  THR n 
3 42  ILE n 
3 43  GLY n 
3 44  GLY n 
3 45  GLY n 
3 46  ASP n 
3 47  ASP n 
3 48  SER n 
3 49  PHE n 
3 50  ASN n 
3 51  THR n 
3 52  PHE n 
3 53  PHE n 
3 54  SER n 
3 55  GLU n 
3 56  THR n 
3 57  GLY n 
3 58  ALA n 
3 59  GLY n 
3 60  LYS n 
3 61  HIS n 
3 62  VAL n 
3 63  PRO n 
3 64  ARG n 
3 65  ALA n 
3 66  VAL n 
3 67  PHE n 
3 68  VAL n 
3 69  ASP n 
3 70  LEU n 
3 71  GLU n 
3 72  PRO n 
3 73  THR n 
3 74  VAL n 
3 75  ILE n 
3 76  ASP n 
3 77  GLU n 
3 78  VAL n 
3 79  ARG n 
3 80  THR n 
3 81  GLY n 
3 82  THR n 
3 83  TYR n 
3 84  ARG n 
3 85  GLN n 
3 86  LEU n 
3 87  PHE n 
3 88  HIS n 
3 89  PRO n 
3 90  GLU n 
3 91  GLN n 
3 92  LEU n 
3 93  ILE n 
3 94  THR n 
3 95  GLY n 
3 96  LYS n 
3 97  GLU n 
3 98  ASP n 
3 99  ALA n 
3 100 ALA n 
3 101 ASN n 
3 102 ASN n 
3 103 TYR n 
3 104 ALA n 
3 105 ARG n 
3 106 GLY n 
3 107 HIS n 
3 108 TYR n 
3 109 THR n 
3 110 ILE n 
3 111 GLY n 
3 112 LYS n 
3 113 GLU n 
3 114 ILE n 
3 115 ILE n 
3 116 ASP n 
3 117 LEU n 
3 118 VAL n 
3 119 LEU n 
3 120 ASP n 
3 121 ARG n 
3 122 ILE n 
3 123 ARG n 
3 124 LYS n 
3 125 LEU n 
3 126 ALA n 
3 127 ASP n 
3 128 GLN n 
3 129 CYS n 
3 130 THR n 
3 131 GLY n 
3 132 LEU n 
3 133 GLN n 
3 134 GLY n 
3 135 PHE n 
3 136 LEU n 
3 137 VAL n 
3 138 PHE n 
3 139 HIS n 
3 140 SER n 
3 141 PHE n 
3 142 GLY n 
3 143 GLY n 
3 144 GLY n 
3 145 THR n 
3 146 GLY n 
3 147 SER n 
3 148 GLY n 
3 149 PHE n 
3 150 THR n 
3 151 SER n 
3 152 LEU n 
3 153 LEU n 
3 154 MET n 
3 155 GLU n 
3 156 ARG n 
3 157 LEU n 
3 158 SER n 
3 159 VAL n 
3 160 ASP n 
3 161 TYR n 
3 162 GLY n 
3 163 LYS n 
3 164 LYS n 
3 165 SER n 
3 166 LYS n 
3 167 LEU n 
3 168 GLU n 
3 169 PHE n 
3 170 SER n 
3 171 ILE n 
3 172 TYR n 
3 173 PRO n 
3 174 ALA n 
3 175 PRO n 
3 176 GLN n 
3 177 VAL n 
3 178 SER n 
3 179 THR n 
3 180 ALA n 
3 181 VAL n 
3 182 VAL n 
3 183 GLU n 
3 184 PRO n 
3 185 TYR n 
3 186 ASN n 
3 187 SER n 
3 188 ILE n 
3 189 LEU n 
3 190 THR n 
3 191 THR n 
3 192 HIS n 
3 193 THR n 
3 194 THR n 
3 195 LEU n 
3 196 GLU n 
3 197 HIS n 
3 198 SER n 
3 199 ASP n 
3 200 CYS n 
3 201 ALA n 
3 202 PHE n 
3 203 MET n 
3 204 VAL n 
3 205 ASP n 
3 206 ASN n 
3 207 GLU n 
3 208 ALA n 
3 209 ILE n 
3 210 TYR n 
3 211 ASP n 
3 212 ILE n 
3 213 CYS n 
3 214 ARG n 
3 215 ARG n 
3 216 ASN n 
3 217 LEU n 
3 218 ASP n 
3 219 ILE n 
3 220 GLU n 
3 221 ARG n 
3 222 PRO n 
3 223 THR n 
3 224 TYR n 
3 225 THR n 
3 226 ASN n 
3 227 LEU n 
3 228 ASN n 
3 229 ARG n 
3 230 LEU n 
3 231 ILE n 
3 232 SER n 
3 233 GLN n 
3 234 ILE n 
3 235 VAL n 
3 236 SER n 
3 237 SER n 
3 238 ILE n 
3 239 THR n 
3 240 ALA n 
3 241 SER n 
3 242 LEU n 
3 243 ARG n 
3 244 PHE n 
3 245 ASP n 
3 246 GLY n 
3 247 ALA n 
3 248 LEU n 
3 249 ASN n 
3 250 VAL n 
3 251 ASP n 
3 252 LEU n 
3 253 THR n 
3 254 GLU n 
3 255 PHE n 
3 256 GLN n 
3 257 THR n 
3 258 ASN n 
3 259 LEU n 
3 260 VAL n 
3 261 PRO n 
3 262 TYR n 
3 263 PRO n 
3 264 ARG n 
3 265 ILE n 
3 266 HIS n 
3 267 PHE n 
3 268 PRO n 
3 269 LEU n 
3 270 ALA n 
3 271 THR n 
3 272 TYR n 
3 273 ALA n 
3 274 PRO n 
3 275 VAL n 
3 276 ILE n 
3 277 SER n 
3 278 ALA n 
3 279 GLU n 
3 280 LYS n 
3 281 ALA n 
3 282 TYR n 
3 283 HIS n 
3 284 GLU n 
3 285 GLN n 
3 286 LEU n 
3 287 SER n 
3 288 VAL n 
3 289 ALA n 
3 290 GLU n 
3 291 ILE n 
3 292 THR n 
3 293 ASN n 
3 294 ALA n 
3 295 CYS n 
3 296 PHE n 
3 297 GLU n 
3 298 PRO n 
3 299 ALA n 
3 300 ASN n 
3 301 GLN n 
3 302 MET n 
3 303 VAL n 
3 304 LYS n 
3 305 CYS n 
3 306 ASP n 
3 307 PRO n 
3 308 ARG n 
3 309 HIS n 
3 310 GLY n 
3 311 LYS n 
3 312 TYR n 
3 313 MET n 
3 314 ALA n 
3 315 CYS n 
3 316 CYS n 
3 317 LEU n 
3 318 LEU n 
3 319 TYR n 
3 320 ARG n 
3 321 GLY n 
3 322 ASP n 
3 323 VAL n 
3 324 VAL n 
3 325 PRO n 
3 326 LYS n 
3 327 ASP n 
3 328 VAL n 
3 329 ASN n 
3 330 ALA n 
3 331 ALA n 
3 332 ILE n 
3 333 ALA n 
3 334 THR n 
3 335 ILE n 
3 336 LYS n 
3 337 THR n 
3 338 LYS n 
3 339 ARG n 
3 340 SER n 
3 341 ILE n 
3 342 GLN n 
3 343 PHE n 
3 344 VAL n 
3 345 ASP n 
3 346 TRP n 
3 347 CYS n 
3 348 PRO n 
3 349 THR n 
3 350 GLY n 
3 351 PHE n 
3 352 LYS n 
3 353 VAL n 
3 354 GLY n 
3 355 ILE n 
3 356 ASN n 
3 357 TYR n 
3 358 GLN n 
3 359 PRO n 
3 360 PRO n 
3 361 THR n 
3 362 VAL n 
3 363 VAL n 
3 364 PRO n 
3 365 GLY n 
3 366 GLY n 
3 367 ASP n 
3 368 LEU n 
3 369 ALA n 
3 370 LYS n 
3 371 VAL n 
3 372 GLN n 
3 373 ARG n 
3 374 ALA n 
3 375 VAL n 
3 376 CYS n 
3 377 MET n 
3 378 LEU n 
3 379 SER n 
3 380 ASN n 
3 381 THR n 
3 382 THR n 
3 383 ALA n 
3 384 ILE n 
3 385 ALA n 
3 386 GLU n 
3 387 ALA n 
3 388 TRP n 
3 389 ALA n 
3 390 ARG n 
3 391 LEU n 
3 392 ASP n 
3 393 HIS n 
3 394 LYS n 
3 395 PHE n 
3 396 ASP n 
3 397 LEU n 
3 398 MET n 
3 399 TYR n 
3 400 ALA n 
3 401 LYS n 
3 402 ARG n 
3 403 ALA n 
3 404 PHE n 
3 405 VAL n 
3 406 HIS n 
3 407 TRP n 
3 408 TYR n 
3 409 VAL n 
3 410 GLY n 
3 411 GLU n 
3 412 GLY n 
3 413 MET n 
3 414 GLU n 
3 415 GLU n 
3 416 GLY n 
3 417 GLU n 
3 418 PHE n 
3 419 SER n 
3 420 GLU n 
3 421 ALA n 
3 422 ARG n 
3 423 GLU n 
3 424 ASP n 
3 425 MET n 
3 426 ALA n 
3 427 ALA n 
3 428 LEU n 
3 429 GLU n 
3 430 LYS n 
3 431 ASP n 
3 432 TYR n 
3 433 GLU n 
3 434 GLU n 
3 435 VAL n 
3 436 GLY n 
3 437 VAL n 
3 438 ASP n 
3 439 SER n 
3 440 VAL n 
3 441 GLU n 
3 442 GLY n 
3 443 GLU n 
3 444 GLY n 
3 445 GLU n 
3 446 GLU n 
3 447 GLU n 
3 448 GLY n 
3 449 GLU n 
3 450 GLU n 
3 451 TYR n 
# 
_entity_src_gen.entity_id                          2 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   963 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KIF5B, KNS, KNS1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1 445 pig 'Sus scrofa' 9823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 1 451 pig 'Sus scrofa' 9823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
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 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"                    ? 'C10 H15 N5 O11 P2' 443.201 
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  
GTP non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE"                   ? 'C10 H16 N5 O14 P3' 523.180 
HIS 'L-peptide linking' y HISTIDINE                                     ? 'C6 H10 N3 O2 1'    156.162 
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 
MG  non-polymer         . 'MAGNESIUM ION'                               ? 'Mg 2'              24.305  
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 
TA1 non-polymer         . TAXOL                                         ? 'C47 H51 N O14'     853.906 
THR 'L-peptide linking' y THREONINE                                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET B . n 
A 1 2   ARG 2   2   2   ARG ARG B . n 
A 1 3   GLU 3   3   3   GLU GLU B . n 
A 1 4   ILE 4   4   4   ILE ILE B . n 
A 1 5   VAL 5   5   5   VAL VAL B . n 
A 1 6   HIS 6   6   6   HIS HIS B . n 
A 1 7   ILE 7   7   7   ILE ILE B . n 
A 1 8   GLN 8   8   8   GLN GLN B . n 
A 1 9   ALA 9   9   9   ALA ALA B . n 
A 1 10  GLY 10  10  10  GLY GLY B . n 
A 1 11  GLN 11  11  11  GLN GLN B . n 
A 1 12  CYS 12  12  12  CYS CYS B . n 
A 1 13  GLY 13  13  13  GLY GLY B . n 
A 1 14  ASN 14  14  14  ASN ASN B . n 
A 1 15  GLN 15  15  15  GLN GLN B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  GLY 17  17  17  GLY GLY B . n 
A 1 18  ALA 18  18  18  ALA ALA B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  PHE 20  20  20  PHE PHE B . n 
A 1 21  TRP 21  21  21  TRP TRP B . n 
A 1 22  GLU 22  22  22  GLU GLU B . n 
A 1 23  VAL 23  23  23  VAL VAL B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  SER 25  25  25  SER SER B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLU 27  27  27  GLU GLU B . n 
A 1 28  HIS 28  28  28  HIS HIS B . n 
A 1 29  GLY 29  29  29  GLY GLY B . n 
A 1 30  ILE 30  30  30  ILE ILE B . n 
A 1 31  ASP 31  31  31  ASP ASP B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  THR 33  33  33  THR THR B . n 
A 1 34  GLY 34  34  34  GLY GLY B . n 
A 1 35  SER 35  35  35  SER SER B . n 
A 1 36  TYR 36  36  36  TYR TYR B . n 
A 1 37  HIS 37  37  37  HIS HIS B . n 
A 1 38  GLY 38  38  38  GLY GLY B . n 
A 1 39  ASP 39  39  39  ASP ASP B . n 
A 1 40  SER 40  40  40  SER SER B . n 
A 1 41  ASP 41  41  41  ASP ASP B . n 
A 1 42  LEU 42  42  42  LEU LEU B . n 
A 1 43  GLN 43  43  43  GLN GLN B . n 
A 1 44  LEU 44  44  44  LEU LEU B . n 
A 1 45  GLU 45  47  47  GLU GLU B . n 
A 1 46  ARG 46  48  48  ARG ARG B . n 
A 1 47  ILE 47  49  49  ILE ILE B . n 
A 1 48  ASN 48  50  50  ASN ASN B . n 
A 1 49  VAL 49  51  51  VAL VAL B . n 
A 1 50  TYR 50  52  52  TYR TYR B . n 
A 1 51  TYR 51  53  53  TYR TYR B . n 
A 1 52  ASN 52  54  54  ASN ASN B . n 
A 1 53  GLU 53  55  55  GLU GLU B . n 
A 1 54  ALA 54  56  56  ALA ALA B . n 
A 1 55  ALA 55  57  57  ALA ALA B . n 
A 1 56  GLY 56  58  58  GLY GLY B . n 
A 1 57  ASN 57  59  59  ASN ASN B . n 
A 1 58  LYS 58  60  60  LYS LYS B . n 
A 1 59  TYR 59  61  61  TYR TYR B . n 
A 1 60  VAL 60  62  62  VAL VAL B . n 
A 1 61  PRO 61  63  63  PRO PRO B . n 
A 1 62  ARG 62  64  64  ARG ARG B . n 
A 1 63  ALA 63  65  65  ALA ALA B . n 
A 1 64  ILE 64  66  66  ILE ILE B . n 
A 1 65  LEU 65  67  67  LEU LEU B . n 
A 1 66  VAL 66  68  68  VAL VAL B . n 
A 1 67  ASP 67  69  69  ASP ASP B . n 
A 1 68  LEU 68  70  70  LEU LEU B . n 
A 1 69  GLU 69  71  71  GLU GLU B . n 
A 1 70  PRO 70  72  72  PRO PRO B . n 
A 1 71  GLY 71  73  73  GLY GLY B . n 
A 1 72  THR 72  74  74  THR THR B . n 
A 1 73  MET 73  75  75  MET MET B . n 
A 1 74  ASP 74  76  76  ASP ASP B . n 
A 1 75  SER 75  77  77  SER SER B . n 
A 1 76  VAL 76  78  78  VAL VAL B . n 
A 1 77  ARG 77  79  79  ARG ARG B . n 
A 1 78  SER 78  80  80  SER SER B . n 
A 1 79  GLY 79  81  81  GLY GLY B . n 
A 1 80  PRO 80  82  82  PRO PRO B . n 
A 1 81  PHE 81  83  83  PHE PHE B . n 
A 1 82  GLY 82  84  84  GLY GLY B . n 
A 1 83  GLN 83  85  85  GLN GLN B . n 
A 1 84  ILE 84  86  86  ILE ILE B . n 
A 1 85  PHE 85  87  87  PHE PHE B . n 
A 1 86  ARG 86  88  88  ARG ARG B . n 
A 1 87  PRO 87  89  89  PRO PRO B . n 
A 1 88  ASP 88  90  90  ASP ASP B . n 
A 1 89  ASN 89  91  91  ASN ASN B . n 
A 1 90  PHE 90  92  92  PHE PHE B . n 
A 1 91  VAL 91  93  93  VAL VAL B . n 
A 1 92  PHE 92  94  94  PHE PHE B . n 
A 1 93  GLY 93  95  95  GLY GLY B . n 
A 1 94  GLN 94  96  96  GLN GLN B . n 
A 1 95  SER 95  97  97  SER SER B . n 
A 1 96  GLY 96  98  98  GLY GLY B . n 
A 1 97  ALA 97  99  99  ALA ALA B . n 
A 1 98  GLY 98  100 100 GLY GLY B . n 
A 1 99  ASN 99  101 101 ASN ASN B . n 
A 1 100 ASN 100 102 102 ASN ASN B . n 
A 1 101 TRP 101 103 103 TRP TRP B . n 
A 1 102 ALA 102 104 104 ALA ALA B . n 
A 1 103 LYS 103 105 105 LYS LYS B . n 
A 1 104 GLY 104 106 106 GLY GLY B . n 
A 1 105 HIS 105 107 107 HIS HIS B . n 
A 1 106 TYR 106 108 108 TYR TYR B . n 
A 1 107 THR 107 109 109 THR THR B . n 
A 1 108 GLU 108 110 110 GLU GLU B . n 
A 1 109 GLY 109 111 111 GLY GLY B . n 
A 1 110 ALA 110 112 112 ALA ALA B . n 
A 1 111 GLU 111 113 113 GLU GLU B . n 
A 1 112 LEU 112 114 114 LEU LEU B . n 
A 1 113 VAL 113 115 115 VAL VAL B . n 
A 1 114 ASP 114 116 116 ASP ASP B . n 
A 1 115 SER 115 117 117 SER SER B . n 
A 1 116 VAL 116 118 118 VAL VAL B . n 
A 1 117 LEU 117 119 119 LEU LEU B . n 
A 1 118 ASP 118 120 120 ASP ASP B . n 
A 1 119 VAL 119 121 121 VAL VAL B . n 
A 1 120 VAL 120 122 122 VAL VAL B . n 
A 1 121 ARG 121 123 123 ARG ARG B . n 
A 1 122 LYS 122 124 124 LYS LYS B . n 
A 1 123 GLU 123 125 125 GLU GLU B . n 
A 1 124 SER 124 126 126 SER SER B . n 
A 1 125 GLU 125 127 127 GLU GLU B . n 
A 1 126 SER 126 128 128 SER SER B . n 
A 1 127 CYS 127 129 129 CYS CYS B . n 
A 1 128 ASP 128 130 130 ASP ASP B . n 
A 1 129 CYS 129 131 131 CYS CYS B . n 
A 1 130 LEU 130 132 132 LEU LEU B . n 
A 1 131 GLN 131 133 133 GLN GLN B . n 
A 1 132 GLY 132 134 134 GLY GLY B . n 
A 1 133 PHE 133 135 135 PHE PHE B . n 
A 1 134 GLN 134 136 136 GLN GLN B . n 
A 1 135 LEU 135 137 137 LEU LEU B . n 
A 1 136 THR 136 138 138 THR THR B . n 
A 1 137 HIS 137 139 139 HIS HIS B . n 
A 1 138 SER 138 140 140 SER SER B . n 
A 1 139 LEU 139 141 141 LEU LEU B . n 
A 1 140 GLY 140 142 142 GLY GLY B . n 
A 1 141 GLY 141 143 143 GLY GLY B . n 
A 1 142 GLY 142 144 144 GLY GLY B . n 
A 1 143 THR 143 145 145 THR THR B . n 
A 1 144 GLY 144 146 146 GLY GLY B . n 
A 1 145 SER 145 147 147 SER SER B . n 
A 1 146 GLY 146 148 148 GLY GLY B . n 
A 1 147 MET 147 149 149 MET MET B . n 
A 1 148 GLY 148 150 150 GLY GLY B . n 
A 1 149 THR 149 151 151 THR THR B . n 
A 1 150 LEU 150 152 152 LEU LEU B . n 
A 1 151 LEU 151 153 153 LEU LEU B . n 
A 1 152 ILE 152 154 154 ILE ILE B . n 
A 1 153 SER 153 155 155 SER SER B . n 
A 1 154 LYS 154 156 156 LYS LYS B . n 
A 1 155 ILE 155 157 157 ILE ILE B . n 
A 1 156 ARG 156 158 158 ARG ARG B . n 
A 1 157 GLU 157 159 159 GLU GLU B . n 
A 1 158 GLU 158 160 160 GLU GLU B . n 
A 1 159 TYR 159 161 161 TYR TYR B . n 
A 1 160 PRO 160 162 162 PRO PRO B . n 
A 1 161 ASP 161 163 163 ASP ASP B . n 
A 1 162 ARG 162 164 164 ARG ARG B . n 
A 1 163 ILE 163 165 165 ILE ILE B . n 
A 1 164 MET 164 166 166 MET MET B . n 
A 1 165 ASN 165 167 167 ASN ASN B . n 
A 1 166 THR 166 168 168 THR THR B . n 
A 1 167 PHE 167 169 169 PHE PHE B . n 
A 1 168 SER 168 170 170 SER SER B . n 
A 1 169 VAL 169 171 171 VAL VAL B . n 
A 1 170 VAL 170 172 172 VAL VAL B . n 
A 1 171 PRO 171 173 173 PRO PRO B . n 
A 1 172 SER 172 174 174 SER SER B . n 
A 1 173 PRO 173 175 175 PRO PRO B . n 
A 1 174 LYS 174 176 176 LYS LYS B . n 
A 1 175 VAL 175 177 177 VAL VAL B . n 
A 1 176 SER 176 178 178 SER SER B . n 
A 1 177 ASP 177 179 179 ASP ASP B . n 
A 1 178 THR 178 180 180 THR THR B . n 
A 1 179 VAL 179 181 181 VAL VAL B . n 
A 1 180 VAL 180 182 182 VAL VAL B . n 
A 1 181 GLU 181 183 183 GLU GLU B . n 
A 1 182 PRO 182 184 184 PRO PRO B . n 
A 1 183 TYR 183 185 185 TYR TYR B . n 
A 1 184 ASN 184 186 186 ASN ASN B . n 
A 1 185 ALA 185 187 187 ALA ALA B . n 
A 1 186 THR 186 188 188 THR THR B . n 
A 1 187 LEU 187 189 189 LEU LEU B . n 
A 1 188 SER 188 190 190 SER SER B . n 
A 1 189 VAL 189 191 191 VAL VAL B . n 
A 1 190 HIS 190 192 192 HIS HIS B . n 
A 1 191 GLN 191 193 193 GLN GLN B . n 
A 1 192 LEU 192 194 194 LEU LEU B . n 
A 1 193 VAL 193 195 195 VAL VAL B . n 
A 1 194 GLU 194 196 196 GLU GLU B . n 
A 1 195 ASN 195 197 197 ASN ASN B . n 
A 1 196 THR 196 198 198 THR THR B . n 
A 1 197 ASP 197 199 199 ASP ASP B . n 
A 1 198 GLU 198 200 200 GLU GLU B . n 
A 1 199 THR 199 201 201 THR THR B . n 
A 1 200 TYR 200 202 202 TYR TYR B . n 
A 1 201 CYS 201 203 203 CYS CYS B . n 
A 1 202 ILE 202 204 204 ILE ILE B . n 
A 1 203 ASP 203 205 205 ASP ASP B . n 
A 1 204 ASN 204 206 206 ASN ASN B . n 
A 1 205 GLU 205 207 207 GLU GLU B . n 
A 1 206 ALA 206 208 208 ALA ALA B . n 
A 1 207 LEU 207 209 209 LEU LEU B . n 
A 1 208 TYR 208 210 210 TYR TYR B . n 
A 1 209 ASP 209 211 211 ASP ASP B . n 
A 1 210 ILE 210 212 212 ILE ILE B . n 
A 1 211 CYS 211 213 213 CYS CYS B . n 
A 1 212 PHE 212 214 214 PHE PHE B . n 
A 1 213 ARG 213 215 215 ARG ARG B . n 
A 1 214 THR 214 216 216 THR THR B . n 
A 1 215 LEU 215 217 217 LEU LEU B . n 
A 1 216 LYS 216 218 218 LYS LYS B . n 
A 1 217 LEU 217 219 219 LEU LEU B . n 
A 1 218 THR 218 220 220 THR THR B . n 
A 1 219 THR 219 221 221 THR THR B . n 
A 1 220 PRO 220 222 222 PRO PRO B . n 
A 1 221 THR 221 223 223 THR THR B . n 
A 1 222 TYR 222 224 224 TYR TYR B . n 
A 1 223 GLY 223 225 225 GLY GLY B . n 
A 1 224 ASP 224 226 226 ASP ASP B . n 
A 1 225 LEU 225 227 227 LEU LEU B . n 
A 1 226 ASN 226 228 228 ASN ASN B . n 
A 1 227 HIS 227 229 229 HIS HIS B . n 
A 1 228 LEU 228 230 230 LEU LEU B . n 
A 1 229 VAL 229 231 231 VAL VAL B . n 
A 1 230 SER 230 232 232 SER SER B . n 
A 1 231 ALA 231 233 233 ALA ALA B . n 
A 1 232 THR 232 234 234 THR THR B . n 
A 1 233 MET 233 235 235 MET MET B . n 
A 1 234 SER 234 236 236 SER SER B . n 
A 1 235 GLY 235 237 237 GLY GLY B . n 
A 1 236 VAL 236 238 238 VAL VAL B . n 
A 1 237 THR 237 239 239 THR THR B . n 
A 1 238 THR 238 240 240 THR THR B . n 
A 1 239 CYS 239 241 241 CYS CYS B . n 
A 1 240 LEU 240 242 242 LEU LEU B . n 
A 1 241 ARG 241 243 243 ARG ARG B . n 
A 1 242 PHE 242 244 244 PHE PHE B . n 
A 1 243 PRO 243 245 245 PRO PRO B . n 
A 1 244 GLY 244 246 246 GLY GLY B . n 
A 1 245 GLN 245 247 247 GLN GLN B . n 
A 1 246 LEU 246 248 248 LEU LEU B . n 
A 1 247 ASN 247 249 249 ASN ASN B . n 
A 1 248 ALA 248 250 250 ALA ALA B . n 
A 1 249 ASP 249 251 251 ASP ASP B . n 
A 1 250 LEU 250 252 252 LEU LEU B . n 
A 1 251 ARG 251 253 253 ARG ARG B . n 
A 1 252 LYS 252 254 254 LYS LYS B . n 
A 1 253 LEU 253 255 255 LEU LEU B . n 
A 1 254 ALA 254 256 256 ALA ALA B . n 
A 1 255 VAL 255 257 257 VAL VAL B . n 
A 1 256 ASN 256 258 258 ASN ASN B . n 
A 1 257 MET 257 259 259 MET MET B . n 
A 1 258 VAL 258 260 260 VAL VAL B . n 
A 1 259 PRO 259 261 261 PRO PRO B . n 
A 1 260 PHE 260 262 262 PHE PHE B . n 
A 1 261 PRO 261 263 263 PRO PRO B . n 
A 1 262 ARG 262 264 264 ARG ARG B . n 
A 1 263 LEU 263 265 265 LEU LEU B . n 
A 1 264 HIS 264 266 266 HIS HIS B . n 
A 1 265 PHE 265 267 267 PHE PHE B . n 
A 1 266 PHE 266 268 268 PHE PHE B . n 
A 1 267 MET 267 269 269 MET MET B . n 
A 1 268 PRO 268 270 270 PRO PRO B . n 
A 1 269 GLY 269 271 271 GLY GLY B . n 
A 1 270 PHE 270 272 272 PHE PHE B . n 
A 1 271 ALA 271 273 273 ALA ALA B . n 
A 1 272 PRO 272 274 274 PRO PRO B . n 
A 1 273 LEU 273 275 275 LEU LEU B . n 
A 1 274 THR 274 276 276 THR THR B . n 
A 1 275 SER 275 277 277 SER SER B . n 
A 1 276 ARG 276 278 278 ARG ARG B . n 
A 1 277 GLY 277 279 279 GLY GLY B . n 
A 1 278 SER 278 280 280 SER SER B . n 
A 1 279 GLN 279 281 281 GLN GLN B . n 
A 1 280 GLN 280 282 282 GLN GLN B . n 
A 1 281 TYR 281 283 283 TYR TYR B . n 
A 1 282 ARG 282 284 284 ARG ARG B . n 
A 1 283 ALA 283 285 285 ALA ALA B . n 
A 1 284 LEU 284 286 286 LEU LEU B . n 
A 1 285 THR 285 287 287 THR THR B . n 
A 1 286 VAL 286 288 288 VAL VAL B . n 
A 1 287 PRO 287 289 289 PRO PRO B . n 
A 1 288 GLU 288 290 290 GLU GLU B . n 
A 1 289 LEU 289 291 291 LEU LEU B . n 
A 1 290 THR 290 292 292 THR THR B . n 
A 1 291 GLN 291 293 293 GLN GLN B . n 
A 1 292 GLN 292 294 294 GLN GLN B . n 
A 1 293 MET 293 295 295 MET MET B . n 
A 1 294 PHE 294 296 296 PHE PHE B . n 
A 1 295 ASP 295 297 297 ASP ASP B . n 
A 1 296 ALA 296 298 298 ALA ALA B . n 
A 1 297 LYS 297 299 299 LYS LYS B . n 
A 1 298 ASN 298 300 300 ASN ASN B . n 
A 1 299 MET 299 301 301 MET MET B . n 
A 1 300 MET 300 302 302 MET MET B . n 
A 1 301 ALA 301 303 303 ALA ALA B . n 
A 1 302 ALA 302 304 304 ALA ALA B . n 
A 1 303 CYS 303 305 305 CYS CYS B . n 
A 1 304 ASP 304 306 306 ASP ASP B . n 
A 1 305 PRO 305 307 307 PRO PRO B . n 
A 1 306 ARG 306 308 308 ARG ARG B . n 
A 1 307 HIS 307 309 309 HIS HIS B . n 
A 1 308 GLY 308 310 310 GLY GLY B . n 
A 1 309 ARG 309 311 311 ARG ARG B . n 
A 1 310 TYR 310 312 312 TYR TYR B . n 
A 1 311 LEU 311 313 313 LEU LEU B . n 
A 1 312 THR 312 314 314 THR THR B . n 
A 1 313 VAL 313 315 315 VAL VAL B . n 
A 1 314 ALA 314 316 316 ALA ALA B . n 
A 1 315 ALA 315 317 317 ALA ALA B . n 
A 1 316 VAL 316 318 318 VAL VAL B . n 
A 1 317 PHE 317 319 319 PHE PHE B . n 
A 1 318 ARG 318 320 320 ARG ARG B . n 
A 1 319 GLY 319 321 321 GLY GLY B . n 
A 1 320 ARG 320 322 322 ARG ARG B . n 
A 1 321 MET 321 323 323 MET MET B . n 
A 1 322 SER 322 324 324 SER SER B . n 
A 1 323 MET 323 325 325 MET MET B . n 
A 1 324 LYS 324 326 326 LYS LYS B . n 
A 1 325 GLU 325 327 327 GLU GLU B . n 
A 1 326 VAL 326 328 328 VAL VAL B . n 
A 1 327 ASP 327 329 329 ASP ASP B . n 
A 1 328 GLU 328 330 330 GLU GLU B . n 
A 1 329 GLN 329 331 331 GLN GLN B . n 
A 1 330 MET 330 332 332 MET MET B . n 
A 1 331 LEU 331 333 333 LEU LEU B . n 
A 1 332 ASN 332 334 334 ASN ASN B . n 
A 1 333 VAL 333 335 335 VAL VAL B . n 
A 1 334 GLN 334 336 336 GLN GLN B . n 
A 1 335 ASN 335 337 337 ASN ASN B . n 
A 1 336 LYS 336 338 338 LYS LYS B . n 
A 1 337 ASN 337 339 339 ASN ASN B . n 
A 1 338 SER 338 340 340 SER SER B . n 
A 1 339 SER 339 341 341 SER SER B . n 
A 1 340 TYR 340 342 342 TYR TYR B . n 
A 1 341 PHE 341 343 343 PHE PHE B . n 
A 1 342 VAL 342 344 344 VAL VAL B . n 
A 1 343 GLU 343 345 345 GLU GLU B . n 
A 1 344 TRP 344 346 346 TRP TRP B . n 
A 1 345 ILE 345 347 347 ILE ILE B . n 
A 1 346 PRO 346 348 348 PRO PRO B . n 
A 1 347 ASN 347 349 349 ASN ASN B . n 
A 1 348 ASN 348 350 350 ASN ASN B . n 
A 1 349 VAL 349 351 351 VAL VAL B . n 
A 1 350 LYS 350 352 352 LYS LYS B . n 
A 1 351 THR 351 353 353 THR THR B . n 
A 1 352 ALA 352 354 354 ALA ALA B . n 
A 1 353 VAL 353 355 355 VAL VAL B . n 
A 1 354 CYS 354 356 356 CYS CYS B . n 
A 1 355 ASP 355 357 357 ASP ASP B . n 
A 1 356 ILE 356 358 358 ILE ILE B . n 
A 1 357 PRO 357 359 359 PRO PRO B . n 
A 1 358 PRO 358 360 360 PRO PRO B . n 
A 1 359 ARG 359 369 369 ARG ARG B . n 
A 1 360 GLY 360 370 370 GLY GLY B . n 
A 1 361 LEU 361 371 371 LEU LEU B . n 
A 1 362 LYS 362 372 372 LYS LYS B . n 
A 1 363 MET 363 373 373 MET MET B . n 
A 1 364 SER 364 374 374 SER SER B . n 
A 1 365 ALA 365 375 375 ALA ALA B . n 
A 1 366 THR 366 376 376 THR THR B . n 
A 1 367 PHE 367 377 377 PHE PHE B . n 
A 1 368 ILE 368 378 378 ILE ILE B . n 
A 1 369 GLY 369 379 379 GLY GLY B . n 
A 1 370 ASN 370 380 380 ASN ASN B . n 
A 1 371 SER 371 381 381 SER SER B . n 
A 1 372 THR 372 382 382 THR THR B . n 
A 1 373 ALA 373 383 383 ALA ALA B . n 
A 1 374 ILE 374 384 384 ILE ILE B . n 
A 1 375 GLN 375 385 385 GLN GLN B . n 
A 1 376 GLU 376 386 386 GLU GLU B . n 
A 1 377 LEU 377 387 387 LEU LEU B . n 
A 1 378 PHE 378 388 388 PHE PHE B . n 
A 1 379 LYS 379 389 389 LYS LYS B . n 
A 1 380 ARG 380 390 390 ARG ARG B . n 
A 1 381 ILE 381 391 391 ILE ILE B . n 
A 1 382 SER 382 392 392 SER SER B . n 
A 1 383 GLU 383 393 393 GLU GLU B . n 
A 1 384 GLN 384 394 394 GLN GLN B . n 
A 1 385 PHE 385 395 395 PHE PHE B . n 
A 1 386 THR 386 396 396 THR THR B . n 
A 1 387 ALA 387 397 397 ALA ALA B . n 
A 1 388 MET 388 398 398 MET MET B . n 
A 1 389 PHE 389 399 399 PHE PHE B . n 
A 1 390 ARG 390 400 400 ARG ARG B . n 
A 1 391 ARG 391 401 401 ARG ARG B . n 
A 1 392 LYS 392 402 402 LYS LYS B . n 
A 1 393 ALA 393 403 403 ALA ALA B . n 
A 1 394 PHE 394 404 404 PHE PHE B . n 
A 1 395 LEU 395 405 405 LEU LEU B . n 
A 1 396 HIS 396 406 406 HIS HIS B . n 
A 1 397 TRP 397 407 407 TRP TRP B . n 
A 1 398 TYR 398 408 408 TYR TYR B . n 
A 1 399 THR 399 409 409 THR THR B . n 
A 1 400 GLY 400 410 410 GLY GLY B . n 
A 1 401 GLU 401 411 411 GLU GLU B . n 
A 1 402 GLY 402 412 412 GLY GLY B . n 
A 1 403 MET 403 413 413 MET MET B . n 
A 1 404 ASP 404 414 414 ASP ASP B . n 
A 1 405 GLU 405 415 415 GLU GLU B . n 
A 1 406 MET 406 416 416 MET MET B . n 
A 1 407 GLU 407 417 417 GLU GLU B . n 
A 1 408 PHE 408 418 418 PHE PHE B . n 
A 1 409 THR 409 419 419 THR THR B . n 
A 1 410 GLU 410 420 420 GLU GLU B . n 
A 1 411 ALA 411 421 421 ALA ALA B . n 
A 1 412 GLU 412 422 422 GLU GLU B . n 
A 1 413 SER 413 423 423 SER SER B . n 
A 1 414 ASN 414 424 424 ASN ASN B . n 
A 1 415 MET 415 425 425 MET MET B . n 
A 1 416 ASN 416 426 426 ASN ASN B . n 
A 1 417 ASP 417 427 427 ASP ASP B . n 
A 1 418 LEU 418 428 428 LEU LEU B . n 
A 1 419 VAL 419 429 429 VAL VAL B . n 
A 1 420 SER 420 430 430 SER SER B . n 
A 1 421 GLU 421 431 431 GLU GLU B . n 
A 1 422 TYR 422 432 432 TYR TYR B . n 
A 1 423 GLN 423 433 433 GLN GLN B . n 
A 1 424 GLN 424 434 434 GLN GLN B . n 
A 1 425 TYR 425 435 435 TYR TYR B . n 
A 1 426 GLN 426 436 436 GLN GLN B . n 
A 1 427 ASP 427 437 ?   ?   ?   B . n 
A 1 428 ALA 428 438 ?   ?   ?   B . n 
A 1 429 THR 429 439 ?   ?   ?   B . n 
A 1 430 ALA 430 440 ?   ?   ?   B . n 
A 1 431 ASP 431 441 ?   ?   ?   B . n 
A 1 432 GLU 432 442 ?   ?   ?   B . n 
A 1 433 GLN 433 443 ?   ?   ?   B . n 
A 1 434 GLY 434 444 ?   ?   ?   B . n 
A 1 435 GLU 435 445 ?   ?   ?   B . n 
A 1 436 PHE 436 446 ?   ?   ?   B . n 
A 1 437 GLU 437 447 ?   ?   ?   B . n 
A 1 438 GLU 438 448 ?   ?   ?   B . n 
A 1 439 GLU 439 449 ?   ?   ?   B . n 
A 1 440 GLY 440 450 ?   ?   ?   B . n 
A 1 441 GLU 441 451 ?   ?   ?   B . n 
A 1 442 GLU 442 452 ?   ?   ?   B . n 
A 1 443 ASP 443 453 ?   ?   ?   B . n 
A 1 444 GLU 444 454 ?   ?   ?   B . n 
A 1 445 ALA 445 455 ?   ?   ?   B . n 
B 2 1   MET 1   1   ?   ?   ?   K . n 
B 2 2   ALA 2   2   ?   ?   ?   K . n 
B 2 3   ASP 3   3   3   ASP ASP K . n 
B 2 4   LEU 4   4   4   LEU LEU K . n 
B 2 5   ALA 5   5   5   ALA ALA K . n 
B 2 6   GLU 6   6   6   GLU GLU K . n 
B 2 7   CYS 7   7   7   CYS CYS K . n 
B 2 8   ASN 8   8   8   ASN ASN K . n 
B 2 9   ILE 9   9   9   ILE ILE K . n 
B 2 10  LYS 10  10  10  LYS LYS K . n 
B 2 11  VAL 11  11  11  VAL VAL K . n 
B 2 12  MET 12  12  12  MET MET K . n 
B 2 13  CYS 13  13  13  CYS CYS K . n 
B 2 14  ARG 14  14  14  ARG ARG K . n 
B 2 15  PHE 15  15  15  PHE PHE K . n 
B 2 16  ARG 16  16  16  ARG ARG K . n 
B 2 17  PRO 17  17  17  PRO PRO K . n 
B 2 18  LEU 18  18  18  LEU LEU K . n 
B 2 19  ASN 19  19  19  ASN ASN K . n 
B 2 20  GLU 20  20  20  GLU GLU K . n 
B 2 21  SER 21  21  21  SER SER K . n 
B 2 22  GLU 22  22  22  GLU GLU K . n 
B 2 23  VAL 23  23  23  VAL VAL K . n 
B 2 24  ASN 24  24  24  ASN ASN K . n 
B 2 25  ARG 25  25  25  ARG ARG K . n 
B 2 26  GLY 26  26  26  GLY GLY K . n 
B 2 27  ASP 27  27  27  ASP ASP K . n 
B 2 28  LYS 28  28  28  LYS LYS K . n 
B 2 29  TYR 29  29  29  TYR TYR K . n 
B 2 30  ILE 30  30  30  ILE ILE K . n 
B 2 31  ALA 31  31  31  ALA ALA K . n 
B 2 32  LYS 32  32  32  LYS LYS K . n 
B 2 33  PHE 33  33  33  PHE PHE K . n 
B 2 34  GLN 34  34  34  GLN GLN K . n 
B 2 35  GLY 35  35  35  GLY GLY K . n 
B 2 36  GLU 36  36  36  GLU GLU K . n 
B 2 37  ASP 37  37  37  ASP ASP K . n 
B 2 38  THR 38  38  38  THR THR K . n 
B 2 39  VAL 39  39  39  VAL VAL K . n 
B 2 40  VAL 40  40  40  VAL VAL K . n 
B 2 41  ILE 41  41  41  ILE ILE K . n 
B 2 42  ALA 42  42  42  ALA ALA K . n 
B 2 43  SER 43  43  43  SER SER K . n 
B 2 44  LYS 44  44  44  LYS LYS K . n 
B 2 45  PRO 45  45  45  PRO PRO K . n 
B 2 46  TYR 46  46  46  TYR TYR K . n 
B 2 47  ALA 47  47  47  ALA ALA K . n 
B 2 48  PHE 48  48  48  PHE PHE K . n 
B 2 49  ASP 49  49  49  ASP ASP K . n 
B 2 50  ARG 50  50  50  ARG ARG K . n 
B 2 51  VAL 51  51  51  VAL VAL K . n 
B 2 52  PHE 52  52  52  PHE PHE K . n 
B 2 53  GLN 53  53  53  GLN GLN K . n 
B 2 54  SER 54  54  54  SER SER K . n 
B 2 55  SER 55  55  55  SER SER K . n 
B 2 56  THR 56  56  56  THR THR K . n 
B 2 57  SER 57  57  57  SER SER K . n 
B 2 58  GLN 58  58  58  GLN GLN K . n 
B 2 59  GLU 59  59  59  GLU GLU K . n 
B 2 60  GLN 60  60  60  GLN GLN K . n 
B 2 61  VAL 61  61  61  VAL VAL K . n 
B 2 62  TYR 62  62  62  TYR TYR K . n 
B 2 63  ASN 63  63  63  ASN ASN K . n 
B 2 64  ASP 64  64  64  ASP ASP K . n 
B 2 65  CYS 65  65  65  CYS CYS K . n 
B 2 66  ALA 66  66  66  ALA ALA K . n 
B 2 67  LYS 67  67  67  LYS LYS K . n 
B 2 68  LYS 68  68  68  LYS LYS K . n 
B 2 69  ILE 69  69  69  ILE ILE K . n 
B 2 70  VAL 70  70  70  VAL VAL K . n 
B 2 71  LYS 71  71  71  LYS LYS K . n 
B 2 72  ASP 72  72  72  ASP ASP K . n 
B 2 73  VAL 73  73  73  VAL VAL K . n 
B 2 74  LEU 74  74  74  LEU LEU K . n 
B 2 75  GLU 75  75  75  GLU GLU K . n 
B 2 76  GLY 76  76  76  GLY GLY K . n 
B 2 77  TYR 77  77  77  TYR TYR K . n 
B 2 78  ASN 78  78  78  ASN ASN K . n 
B 2 79  GLY 79  79  79  GLY GLY K . n 
B 2 80  THR 80  80  80  THR THR K . n 
B 2 81  ILE 81  81  81  ILE ILE K . n 
B 2 82  PHE 82  82  82  PHE PHE K . n 
B 2 83  ALA 83  83  83  ALA ALA K . n 
B 2 84  TYR 84  84  84  TYR TYR K . n 
B 2 85  GLY 85  85  85  GLY GLY K . n 
B 2 86  GLN 86  86  86  GLN GLN K . n 
B 2 87  THR 87  87  87  THR THR K . n 
B 2 88  SER 88  88  88  SER SER K . n 
B 2 89  SER 89  89  89  SER SER K . n 
B 2 90  GLY 90  90  90  GLY GLY K . n 
B 2 91  LYS 91  91  91  LYS LYS K . n 
B 2 92  THR 92  92  92  THR THR K . n 
B 2 93  HIS 93  93  93  HIS HIS K . n 
B 2 94  THR 94  94  94  THR THR K . n 
B 2 95  MET 95  95  95  MET MET K . n 
B 2 96  GLU 96  96  96  GLU GLU K . n 
B 2 97  GLY 97  97  97  GLY GLY K . n 
B 2 98  LYS 98  98  98  LYS LYS K . n 
B 2 99  LEU 99  99  99  LEU LEU K . n 
B 2 100 HIS 100 100 100 HIS HIS K . n 
B 2 101 ASP 101 101 101 ASP ASP K . n 
B 2 102 PRO 102 102 102 PRO PRO K . n 
B 2 103 GLU 103 103 103 GLU GLU K . n 
B 2 104 GLY 104 104 104 GLY GLY K . n 
B 2 105 MET 105 105 105 MET MET K . n 
B 2 106 GLY 106 106 106 GLY GLY K . n 
B 2 107 ILE 107 107 107 ILE ILE K . n 
B 2 108 ILE 108 108 108 ILE ILE K . n 
B 2 109 PRO 109 109 109 PRO PRO K . n 
B 2 110 ARG 110 110 110 ARG ARG K . n 
B 2 111 ILE 111 111 111 ILE ILE K . n 
B 2 112 VAL 112 112 112 VAL VAL K . n 
B 2 113 GLN 113 113 113 GLN GLN K . n 
B 2 114 ASP 114 114 114 ASP ASP K . n 
B 2 115 ILE 115 115 115 ILE ILE K . n 
B 2 116 PHE 116 116 116 PHE PHE K . n 
B 2 117 ASN 117 117 117 ASN ASN K . n 
B 2 118 TYR 118 118 118 TYR TYR K . n 
B 2 119 ILE 119 119 119 ILE ILE K . n 
B 2 120 TYR 120 120 120 TYR TYR K . n 
B 2 121 SER 121 121 121 SER SER K . n 
B 2 122 MET 122 122 122 MET MET K . n 
B 2 123 ASP 123 123 123 ASP ASP K . n 
B 2 124 GLU 124 124 124 GLU GLU K . n 
B 2 125 ASN 125 125 125 ASN ASN K . n 
B 2 126 LEU 126 126 126 LEU LEU K . n 
B 2 127 GLU 127 127 127 GLU GLU K . n 
B 2 128 PHE 128 128 128 PHE PHE K . n 
B 2 129 HIS 129 129 129 HIS HIS K . n 
B 2 130 ILE 130 130 130 ILE ILE K . n 
B 2 131 LYS 131 131 131 LYS LYS K . n 
B 2 132 VAL 132 132 132 VAL VAL K . n 
B 2 133 SER 133 133 133 SER SER K . n 
B 2 134 TYR 134 134 134 TYR TYR K . n 
B 2 135 PHE 135 135 135 PHE PHE K . n 
B 2 136 GLU 136 136 136 GLU GLU K . n 
B 2 137 ILE 137 137 137 ILE ILE K . n 
B 2 138 TYR 138 138 138 TYR TYR K . n 
B 2 139 LEU 139 139 139 LEU LEU K . n 
B 2 140 ASP 140 140 140 ASP ASP K . n 
B 2 141 LYS 141 141 141 LYS LYS K . n 
B 2 142 ILE 142 142 142 ILE ILE K . n 
B 2 143 ARG 143 143 143 ARG ARG K . n 
B 2 144 ASP 144 144 144 ASP ASP K . n 
B 2 145 LEU 145 145 145 LEU LEU K . n 
B 2 146 LEU 146 146 146 LEU LEU K . n 
B 2 147 ASP 147 147 147 ASP ASP K . n 
B 2 148 VAL 148 148 148 VAL VAL K . n 
B 2 149 SER 149 149 149 SER SER K . n 
B 2 150 LYS 150 150 150 LYS LYS K . n 
B 2 151 THR 151 151 151 THR THR K . n 
B 2 152 ASN 152 152 152 ASN ASN K . n 
B 2 153 LEU 153 153 153 LEU LEU K . n 
B 2 154 SER 154 154 154 SER SER K . n 
B 2 155 VAL 155 155 155 VAL VAL K . n 
B 2 156 HIS 156 156 156 HIS HIS K . n 
B 2 157 GLU 157 157 157 GLU GLU K . n 
B 2 158 ASP 158 158 158 ASP ASP K . n 
B 2 159 LYS 159 159 159 LYS LYS K . n 
B 2 160 ASN 160 160 160 ASN ASN K . n 
B 2 161 ARG 161 161 161 ARG ARG K . n 
B 2 162 VAL 162 162 162 VAL VAL K . n 
B 2 163 PRO 163 163 163 PRO PRO K . n 
B 2 164 TYR 164 164 164 TYR TYR K . n 
B 2 165 VAL 165 165 165 VAL VAL K . n 
B 2 166 LYS 166 166 166 LYS LYS K . n 
B 2 167 GLY 167 167 167 GLY GLY K . n 
B 2 168 CYS 168 168 168 CYS CYS K . n 
B 2 169 THR 169 169 169 THR THR K . n 
B 2 170 GLU 170 170 170 GLU GLU K . n 
B 2 171 ARG 171 171 171 ARG ARG K . n 
B 2 172 PHE 172 172 172 PHE PHE K . n 
B 2 173 VAL 173 173 173 VAL VAL K . n 
B 2 174 CYS 174 174 174 CYS CYS K . n 
B 2 175 SER 175 175 175 SER SER K . n 
B 2 176 PRO 176 176 176 PRO PRO K . n 
B 2 177 ASP 177 177 177 ASP ASP K . n 
B 2 178 GLU 178 178 178 GLU GLU K . n 
B 2 179 VAL 179 179 179 VAL VAL K . n 
B 2 180 MET 180 180 180 MET MET K . n 
B 2 181 ASP 181 181 181 ASP ASP K . n 
B 2 182 THR 182 182 182 THR THR K . n 
B 2 183 ILE 183 183 183 ILE ILE K . n 
B 2 184 ASP 184 184 184 ASP ASP K . n 
B 2 185 GLU 185 185 185 GLU GLU K . n 
B 2 186 GLY 186 186 186 GLY GLY K . n 
B 2 187 LYS 187 187 187 LYS LYS K . n 
B 2 188 SER 188 188 188 SER SER K . n 
B 2 189 ASN 189 189 189 ASN ASN K . n 
B 2 190 ARG 190 190 190 ARG ARG K . n 
B 2 191 HIS 191 191 191 HIS HIS K . n 
B 2 192 VAL 192 192 192 VAL VAL K . n 
B 2 193 ALA 193 193 193 ALA ALA K . n 
B 2 194 VAL 194 194 194 VAL VAL K . n 
B 2 195 THR 195 195 195 THR THR K . n 
B 2 196 ASN 196 196 196 ASN ASN K . n 
B 2 197 MET 197 197 197 MET MET K . n 
B 2 198 ASN 198 198 198 ASN ASN K . n 
B 2 199 GLU 199 199 199 GLU GLU K . n 
B 2 200 HIS 200 200 200 HIS HIS K . n 
B 2 201 SER 201 201 201 SER SER K . n 
B 2 202 SER 202 202 202 SER SER K . n 
B 2 203 ARG 203 203 203 ARG ARG K . n 
B 2 204 SER 204 204 204 SER SER K . n 
B 2 205 HIS 205 205 205 HIS HIS K . n 
B 2 206 SER 206 206 206 SER SER K . n 
B 2 207 ILE 207 207 207 ILE ILE K . n 
B 2 208 PHE 208 208 208 PHE PHE K . n 
B 2 209 LEU 209 209 209 LEU LEU K . n 
B 2 210 ILE 210 210 210 ILE ILE K . n 
B 2 211 ASN 211 211 211 ASN ASN K . n 
B 2 212 VAL 212 212 212 VAL VAL K . n 
B 2 213 LYS 213 213 213 LYS LYS K . n 
B 2 214 GLN 214 214 214 GLN GLN K . n 
B 2 215 GLU 215 215 215 GLU GLU K . n 
B 2 216 ASN 216 216 216 ASN ASN K . n 
B 2 217 THR 217 217 217 THR THR K . n 
B 2 218 GLN 218 218 218 GLN GLN K . n 
B 2 219 THR 219 219 219 THR THR K . n 
B 2 220 GLU 220 220 220 GLU GLU K . n 
B 2 221 GLN 221 221 221 GLN GLN K . n 
B 2 222 LYS 222 222 222 LYS LYS K . n 
B 2 223 LEU 223 223 223 LEU LEU K . n 
B 2 224 SER 224 224 224 SER SER K . n 
B 2 225 GLY 225 225 225 GLY GLY K . n 
B 2 226 LYS 226 226 226 LYS LYS K . n 
B 2 227 LEU 227 227 227 LEU LEU K . n 
B 2 228 TYR 228 228 228 TYR TYR K . n 
B 2 229 LEU 229 229 229 LEU LEU K . n 
B 2 230 VAL 230 230 230 VAL VAL K . n 
B 2 231 ASP 231 231 231 ASP ASP K . n 
B 2 232 LEU 232 232 232 LEU LEU K . n 
B 2 233 ALA 233 233 233 ALA ALA K . n 
B 2 234 GLY 234 234 234 GLY GLY K . n 
B 2 235 SER 235 235 235 SER SER K . n 
B 2 236 GLU 236 236 236 GLU GLU K . n 
B 2 237 LYS 237 237 237 LYS LYS K . n 
B 2 238 VAL 238 238 238 VAL VAL K . n 
B 2 239 SER 239 239 239 SER SER K . n 
B 2 240 LYS 240 240 240 LYS LYS K . n 
B 2 241 THR 241 241 241 THR THR K . n 
B 2 242 GLY 242 242 242 GLY GLY K . n 
B 2 243 ALA 243 243 243 ALA ALA K . n 
B 2 244 GLU 244 244 244 GLU GLU K . n 
B 2 245 GLY 245 245 245 GLY GLY K . n 
B 2 246 ALA 246 246 246 ALA ALA K . n 
B 2 247 VAL 247 247 247 VAL VAL K . n 
B 2 248 LEU 248 248 248 LEU LEU K . n 
B 2 249 ASP 249 249 249 ASP ASP K . n 
B 2 250 GLU 250 250 250 GLU GLU K . n 
B 2 251 ALA 251 251 251 ALA ALA K . n 
B 2 252 LYS 252 252 252 LYS LYS K . n 
B 2 253 ASN 253 253 253 ASN ASN K . n 
B 2 254 ILE 254 254 254 ILE ILE K . n 
B 2 255 ASN 255 255 255 ASN ASN K . n 
B 2 256 LYS 256 256 256 LYS LYS K . n 
B 2 257 SER 257 257 257 SER SER K . n 
B 2 258 LEU 258 258 258 LEU LEU K . n 
B 2 259 SER 259 259 259 SER SER K . n 
B 2 260 ALA 260 260 260 ALA ALA K . n 
B 2 261 LEU 261 261 261 LEU LEU K . n 
B 2 262 GLY 262 262 262 GLY GLY K . n 
B 2 263 ASN 263 263 263 ASN ASN K . n 
B 2 264 VAL 264 264 264 VAL VAL K . n 
B 2 265 ILE 265 265 265 ILE ILE K . n 
B 2 266 SER 266 266 266 SER SER K . n 
B 2 267 ALA 267 267 267 ALA ALA K . n 
B 2 268 LEU 268 268 268 LEU LEU K . n 
B 2 269 ALA 269 269 269 ALA ALA K . n 
B 2 270 GLU 270 270 270 GLU GLU K . n 
B 2 271 GLY 271 271 271 GLY GLY K . n 
B 2 272 SER 272 272 272 SER SER K . n 
B 2 273 THR 273 273 273 THR THR K . n 
B 2 274 TYR 274 274 274 TYR TYR K . n 
B 2 275 VAL 275 275 275 VAL VAL K . n 
B 2 276 PRO 276 276 276 PRO PRO K . n 
B 2 277 TYR 277 277 277 TYR TYR K . n 
B 2 278 ARG 278 278 278 ARG ARG K . n 
B 2 279 ASP 279 279 279 ASP ASP K . n 
B 2 280 SER 280 280 280 SER SER K . n 
B 2 281 LYS 281 281 281 LYS LYS K . n 
B 2 282 MET 282 282 282 MET MET K . n 
B 2 283 THR 283 283 283 THR THR K . n 
B 2 284 ARG 284 284 284 ARG ARG K . n 
B 2 285 ILE 285 285 285 ILE ILE K . n 
B 2 286 LEU 286 286 286 LEU LEU K . n 
B 2 287 GLN 287 287 287 GLN GLN K . n 
B 2 288 ASP 288 288 288 ASP ASP K . n 
B 2 289 SER 289 289 289 SER SER K . n 
B 2 290 LEU 290 290 290 LEU LEU K . n 
B 2 291 GLY 291 291 291 GLY GLY K . n 
B 2 292 GLY 292 292 292 GLY GLY K . n 
B 2 293 ASN 293 293 293 ASN ASN K . n 
B 2 294 CYS 294 294 294 CYS CYS K . n 
B 2 295 ARG 295 295 295 ARG ARG K . n 
B 2 296 THR 296 296 296 THR THR K . n 
B 2 297 THR 297 297 297 THR THR K . n 
B 2 298 ILE 298 298 298 ILE ILE K . n 
B 2 299 VAL 299 299 299 VAL VAL K . n 
B 2 300 ILE 300 300 300 ILE ILE K . n 
B 2 301 CYS 301 301 301 CYS CYS K . n 
B 2 302 CYS 302 302 302 CYS CYS K . n 
B 2 303 SER 303 303 303 SER SER K . n 
B 2 304 PRO 304 304 304 PRO PRO K . n 
B 2 305 SER 305 305 305 SER SER K . n 
B 2 306 SER 306 306 306 SER SER K . n 
B 2 307 TYR 307 307 307 TYR TYR K . n 
B 2 308 ASN 308 308 308 ASN ASN K . n 
B 2 309 GLU 309 309 309 GLU GLU K . n 
B 2 310 SER 310 310 310 SER SER K . n 
B 2 311 GLU 311 311 311 GLU GLU K . n 
B 2 312 THR 312 312 312 THR THR K . n 
B 2 313 LYS 313 313 313 LYS LYS K . n 
B 2 314 SER 314 314 314 SER SER K . n 
B 2 315 THR 315 315 315 THR THR K . n 
B 2 316 LEU 316 316 316 LEU LEU K . n 
B 2 317 LEU 317 317 317 LEU LEU K . n 
B 2 318 PHE 318 318 318 PHE PHE K . n 
B 2 319 GLY 319 319 319 GLY GLY K . n 
B 2 320 GLN 320 320 320 GLN GLN K . n 
B 2 321 ARG 321 321 321 ARG ARG K . n 
B 2 322 ALA 322 322 322 ALA ALA K . n 
B 2 323 LYS 323 323 323 LYS LYS K . n 
B 2 324 THR 324 324 324 THR THR K . n 
B 2 325 ILE 325 325 325 ILE ILE K . n 
B 2 326 LYS 326 326 326 LYS LYS K . n 
B 2 327 ASN 327 327 327 ASN ASN K . n 
B 2 328 THR 328 328 328 THR THR K . n 
B 2 329 VAL 329 329 329 VAL VAL K . n 
B 2 330 CYS 330 330 330 CYS CYS K . n 
B 2 331 VAL 331 331 331 VAL VAL K . n 
B 2 332 ASN 332 332 332 ASN ASN K . n 
B 2 333 VAL 333 333 333 VAL VAL K . n 
B 2 334 GLU 334 334 334 GLU GLU K . n 
B 2 335 LEU 335 335 335 LEU LEU K . n 
B 2 336 THR 336 336 336 THR THR K . n 
B 2 337 ALA 337 337 337 ALA ALA K . n 
B 2 338 GLU 338 338 338 GLU GLU K . n 
B 2 339 GLN 339 339 339 GLN GLN K . n 
B 2 340 TRP 340 340 340 TRP TRP K . n 
B 2 341 LYS 341 341 341 LYS LYS K . n 
B 2 342 LYS 342 342 342 LYS LYS K . n 
B 2 343 LYS 343 343 343 LYS LYS K . n 
B 2 344 TYR 344 344 344 TYR TYR K . n 
B 2 345 GLU 345 345 345 GLU GLU K . n 
B 2 346 LYS 346 346 346 LYS LYS K . n 
B 2 347 GLU 347 347 ?   ?   ?   K . n 
B 2 348 LYS 348 348 ?   ?   ?   K . n 
B 2 349 GLU 349 349 ?   ?   ?   K . n 
B 2 350 LYS 350 350 ?   ?   ?   K . n 
B 2 351 ASN 351 351 ?   ?   ?   K . n 
B 2 352 LYS 352 352 ?   ?   ?   K . n 
B 2 353 ILE 353 353 ?   ?   ?   K . n 
B 2 354 LEU 354 354 ?   ?   ?   K . n 
B 2 355 ARG 355 355 ?   ?   ?   K . n 
B 2 356 ASN 356 356 ?   ?   ?   K . n 
B 2 357 THR 357 357 ?   ?   ?   K . n 
B 2 358 ILE 358 358 ?   ?   ?   K . n 
B 2 359 GLN 359 359 ?   ?   ?   K . n 
B 2 360 TRP 360 360 ?   ?   ?   K . n 
B 2 361 LEU 361 361 ?   ?   ?   K . n 
B 2 362 GLU 362 362 ?   ?   ?   K . n 
B 2 363 ASN 363 363 ?   ?   ?   K . n 
B 2 364 GLU 364 364 ?   ?   ?   K . n 
B 2 365 LEU 365 365 ?   ?   ?   K . n 
B 2 366 ASN 366 366 ?   ?   ?   K . n 
B 2 367 ARG 367 367 ?   ?   ?   K . n 
B 2 368 TRP 368 368 ?   ?   ?   K . n 
B 2 369 ARG 369 369 ?   ?   ?   K . n 
B 2 370 ASN 370 370 ?   ?   ?   K . n 
B 2 371 GLY 371 371 ?   ?   ?   K . n 
B 2 372 GLU 372 372 ?   ?   ?   K . n 
B 2 373 THR 373 373 ?   ?   ?   K . n 
B 2 374 VAL 374 374 ?   ?   ?   K . n 
B 2 375 PRO 375 375 ?   ?   ?   K . n 
B 2 376 ILE 376 376 ?   ?   ?   K . n 
B 2 377 ASP 377 377 ?   ?   ?   K . n 
B 2 378 GLU 378 378 ?   ?   ?   K . n 
B 2 379 GLN 379 379 ?   ?   ?   K . n 
B 2 380 PHE 380 380 ?   ?   ?   K . n 
B 2 381 ASP 381 381 ?   ?   ?   K . n 
B 2 382 LYS 382 382 ?   ?   ?   K . n 
B 2 383 GLU 383 383 ?   ?   ?   K . n 
B 2 384 LYS 384 384 ?   ?   ?   K . n 
B 2 385 ALA 385 385 ?   ?   ?   K . n 
B 2 386 ASN 386 386 ?   ?   ?   K . n 
B 2 387 LEU 387 387 ?   ?   ?   K . n 
B 2 388 GLU 388 388 ?   ?   ?   K . n 
B 2 389 ALA 389 389 ?   ?   ?   K . n 
B 2 390 PHE 390 390 ?   ?   ?   K . n 
B 2 391 THR 391 391 ?   ?   ?   K . n 
B 2 392 VAL 392 392 ?   ?   ?   K . n 
B 2 393 ASP 393 393 ?   ?   ?   K . n 
B 2 394 LYS 394 394 ?   ?   ?   K . n 
B 2 395 ASP 395 395 ?   ?   ?   K . n 
B 2 396 ILE 396 396 ?   ?   ?   K . n 
B 2 397 THR 397 397 ?   ?   ?   K . n 
B 2 398 LEU 398 398 ?   ?   ?   K . n 
B 2 399 THR 399 399 ?   ?   ?   K . n 
B 2 400 ASN 400 400 ?   ?   ?   K . n 
B 2 401 ASP 401 401 ?   ?   ?   K . n 
B 2 402 LYS 402 402 ?   ?   ?   K . n 
B 2 403 PRO 403 403 ?   ?   ?   K . n 
B 2 404 ALA 404 404 ?   ?   ?   K . n 
B 2 405 THR 405 405 ?   ?   ?   K . n 
B 2 406 ALA 406 406 ?   ?   ?   K . n 
B 2 407 ILE 407 407 ?   ?   ?   K . n 
B 2 408 GLY 408 408 ?   ?   ?   K . n 
B 2 409 VAL 409 409 ?   ?   ?   K . n 
B 2 410 ILE 410 410 ?   ?   ?   K . n 
B 2 411 GLY 411 411 ?   ?   ?   K . n 
B 2 412 ASN 412 412 ?   ?   ?   K . n 
B 2 413 PHE 413 413 ?   ?   ?   K . n 
B 2 414 THR 414 414 ?   ?   ?   K . n 
B 2 415 ASP 415 415 ?   ?   ?   K . n 
B 2 416 ALA 416 416 ?   ?   ?   K . n 
B 2 417 GLU 417 417 ?   ?   ?   K . n 
B 2 418 ARG 418 418 ?   ?   ?   K . n 
B 2 419 ARG 419 419 ?   ?   ?   K . n 
B 2 420 LYS 420 420 ?   ?   ?   K . n 
B 2 421 CYS 421 421 ?   ?   ?   K . n 
B 2 422 GLU 422 422 ?   ?   ?   K . n 
B 2 423 GLU 423 423 ?   ?   ?   K . n 
B 2 424 GLU 424 424 ?   ?   ?   K . n 
B 2 425 ILE 425 425 ?   ?   ?   K . n 
B 2 426 ALA 426 426 ?   ?   ?   K . n 
B 2 427 LYS 427 427 ?   ?   ?   K . n 
B 2 428 LEU 428 428 ?   ?   ?   K . n 
B 2 429 TYR 429 429 ?   ?   ?   K . n 
B 2 430 LYS 430 430 ?   ?   ?   K . n 
B 2 431 GLN 431 431 ?   ?   ?   K . n 
B 2 432 LEU 432 432 ?   ?   ?   K . n 
B 2 433 ASP 433 433 ?   ?   ?   K . n 
B 2 434 ASP 434 434 ?   ?   ?   K . n 
B 2 435 LYS 435 435 ?   ?   ?   K . n 
B 2 436 ASP 436 436 ?   ?   ?   K . n 
B 2 437 GLU 437 437 ?   ?   ?   K . n 
B 2 438 GLU 438 438 ?   ?   ?   K . n 
B 2 439 ILE 439 439 ?   ?   ?   K . n 
B 2 440 ASN 440 440 ?   ?   ?   K . n 
B 2 441 GLN 441 441 ?   ?   ?   K . n 
B 2 442 GLN 442 442 ?   ?   ?   K . n 
B 2 443 SER 443 443 ?   ?   ?   K . n 
B 2 444 GLN 444 444 ?   ?   ?   K . n 
B 2 445 LEU 445 445 ?   ?   ?   K . n 
B 2 446 VAL 446 446 ?   ?   ?   K . n 
B 2 447 GLU 447 447 ?   ?   ?   K . n 
B 2 448 LYS 448 448 ?   ?   ?   K . n 
B 2 449 LEU 449 449 ?   ?   ?   K . n 
B 2 450 LYS 450 450 ?   ?   ?   K . n 
B 2 451 THR 451 451 ?   ?   ?   K . n 
B 2 452 GLN 452 452 ?   ?   ?   K . n 
B 2 453 MET 453 453 ?   ?   ?   K . n 
B 2 454 LEU 454 454 ?   ?   ?   K . n 
B 2 455 ASP 455 455 ?   ?   ?   K . n 
B 2 456 GLN 456 456 ?   ?   ?   K . n 
B 2 457 GLU 457 457 ?   ?   ?   K . n 
B 2 458 GLU 458 458 ?   ?   ?   K . n 
B 2 459 LEU 459 459 ?   ?   ?   K . n 
B 2 460 LEU 460 460 ?   ?   ?   K . n 
B 2 461 ALA 461 461 ?   ?   ?   K . n 
B 2 462 SER 462 462 ?   ?   ?   K . n 
B 2 463 THR 463 463 ?   ?   ?   K . n 
B 2 464 ARG 464 464 ?   ?   ?   K . n 
B 2 465 ARG 465 465 ?   ?   ?   K . n 
B 2 466 ASP 466 466 ?   ?   ?   K . n 
B 2 467 GLN 467 467 ?   ?   ?   K . n 
B 2 468 ASP 468 468 ?   ?   ?   K . n 
B 2 469 ASN 469 469 ?   ?   ?   K . n 
B 2 470 MET 470 470 ?   ?   ?   K . n 
B 2 471 GLN 471 471 ?   ?   ?   K . n 
B 2 472 ALA 472 472 ?   ?   ?   K . n 
B 2 473 GLU 473 473 ?   ?   ?   K . n 
B 2 474 LEU 474 474 ?   ?   ?   K . n 
B 2 475 ASN 475 475 ?   ?   ?   K . n 
B 2 476 ARG 476 476 ?   ?   ?   K . n 
B 2 477 LEU 477 477 ?   ?   ?   K . n 
B 2 478 GLN 478 478 ?   ?   ?   K . n 
B 2 479 ALA 479 479 ?   ?   ?   K . n 
B 2 480 GLU 480 480 ?   ?   ?   K . n 
B 2 481 ASN 481 481 ?   ?   ?   K . n 
B 2 482 ASP 482 482 ?   ?   ?   K . n 
B 2 483 ALA 483 483 ?   ?   ?   K . n 
B 2 484 SER 484 484 ?   ?   ?   K . n 
B 2 485 LYS 485 485 ?   ?   ?   K . n 
B 2 486 GLU 486 486 ?   ?   ?   K . n 
B 2 487 GLU 487 487 ?   ?   ?   K . n 
B 2 488 VAL 488 488 ?   ?   ?   K . n 
B 2 489 LYS 489 489 ?   ?   ?   K . n 
B 2 490 GLU 490 490 ?   ?   ?   K . n 
B 2 491 VAL 491 491 ?   ?   ?   K . n 
B 2 492 LEU 492 492 ?   ?   ?   K . n 
B 2 493 GLN 493 493 ?   ?   ?   K . n 
B 2 494 ALA 494 494 ?   ?   ?   K . n 
B 2 495 LEU 495 495 ?   ?   ?   K . n 
B 2 496 GLU 496 496 ?   ?   ?   K . n 
B 2 497 GLU 497 497 ?   ?   ?   K . n 
B 2 498 LEU 498 498 ?   ?   ?   K . n 
B 2 499 ALA 499 499 ?   ?   ?   K . n 
B 2 500 VAL 500 500 ?   ?   ?   K . n 
B 2 501 ASN 501 501 ?   ?   ?   K . n 
B 2 502 TYR 502 502 ?   ?   ?   K . n 
B 2 503 ASP 503 503 ?   ?   ?   K . n 
B 2 504 GLN 504 504 ?   ?   ?   K . n 
B 2 505 LYS 505 505 ?   ?   ?   K . n 
B 2 506 SER 506 506 ?   ?   ?   K . n 
B 2 507 GLN 507 507 ?   ?   ?   K . n 
B 2 508 GLU 508 508 ?   ?   ?   K . n 
B 2 509 VAL 509 509 ?   ?   ?   K . n 
B 2 510 GLU 510 510 ?   ?   ?   K . n 
B 2 511 ASP 511 511 ?   ?   ?   K . n 
B 2 512 LYS 512 512 ?   ?   ?   K . n 
B 2 513 THR 513 513 ?   ?   ?   K . n 
B 2 514 LYS 514 514 ?   ?   ?   K . n 
B 2 515 GLU 515 515 ?   ?   ?   K . n 
B 2 516 TYR 516 516 ?   ?   ?   K . n 
B 2 517 GLU 517 517 ?   ?   ?   K . n 
B 2 518 LEU 518 518 ?   ?   ?   K . n 
B 2 519 LEU 519 519 ?   ?   ?   K . n 
B 2 520 SER 520 520 ?   ?   ?   K . n 
B 2 521 ASP 521 521 ?   ?   ?   K . n 
B 2 522 GLU 522 522 ?   ?   ?   K . n 
B 2 523 LEU 523 523 ?   ?   ?   K . n 
B 2 524 ASN 524 524 ?   ?   ?   K . n 
B 2 525 GLN 525 525 ?   ?   ?   K . n 
B 2 526 LYS 526 526 ?   ?   ?   K . n 
B 2 527 SER 527 527 ?   ?   ?   K . n 
B 2 528 ALA 528 528 ?   ?   ?   K . n 
B 2 529 THR 529 529 ?   ?   ?   K . n 
B 2 530 LEU 530 530 ?   ?   ?   K . n 
B 2 531 ALA 531 531 ?   ?   ?   K . n 
B 2 532 SER 532 532 ?   ?   ?   K . n 
B 2 533 ILE 533 533 ?   ?   ?   K . n 
B 2 534 ASP 534 534 ?   ?   ?   K . n 
B 2 535 ALA 535 535 ?   ?   ?   K . n 
B 2 536 GLU 536 536 ?   ?   ?   K . n 
B 2 537 LEU 537 537 ?   ?   ?   K . n 
B 2 538 GLN 538 538 ?   ?   ?   K . n 
B 2 539 LYS 539 539 ?   ?   ?   K . n 
B 2 540 LEU 540 540 ?   ?   ?   K . n 
B 2 541 LYS 541 541 ?   ?   ?   K . n 
B 2 542 GLU 542 542 ?   ?   ?   K . n 
B 2 543 MET 543 543 ?   ?   ?   K . n 
B 2 544 THR 544 544 ?   ?   ?   K . n 
B 2 545 ASN 545 545 ?   ?   ?   K . n 
B 2 546 HIS 546 546 ?   ?   ?   K . n 
B 2 547 GLN 547 547 ?   ?   ?   K . n 
B 2 548 LYS 548 548 ?   ?   ?   K . n 
B 2 549 LYS 549 549 ?   ?   ?   K . n 
B 2 550 ARG 550 550 ?   ?   ?   K . n 
B 2 551 ALA 551 551 ?   ?   ?   K . n 
B 2 552 ALA 552 552 ?   ?   ?   K . n 
B 2 553 GLU 553 553 ?   ?   ?   K . n 
B 2 554 MET 554 554 ?   ?   ?   K . n 
B 2 555 MET 555 555 ?   ?   ?   K . n 
B 2 556 ALA 556 556 ?   ?   ?   K . n 
B 2 557 SER 557 557 ?   ?   ?   K . n 
B 2 558 LEU 558 558 ?   ?   ?   K . n 
B 2 559 LEU 559 559 ?   ?   ?   K . n 
B 2 560 LYS 560 560 ?   ?   ?   K . n 
B 2 561 ASP 561 561 ?   ?   ?   K . n 
B 2 562 LEU 562 562 ?   ?   ?   K . n 
B 2 563 ALA 563 563 ?   ?   ?   K . n 
B 2 564 GLU 564 564 ?   ?   ?   K . n 
B 2 565 ILE 565 565 ?   ?   ?   K . n 
B 2 566 GLY 566 566 ?   ?   ?   K . n 
B 2 567 ILE 567 567 ?   ?   ?   K . n 
B 2 568 ALA 568 568 ?   ?   ?   K . n 
B 2 569 VAL 569 569 ?   ?   ?   K . n 
B 2 570 GLY 570 570 ?   ?   ?   K . n 
B 2 571 ASN 571 571 ?   ?   ?   K . n 
B 2 572 ASN 572 572 ?   ?   ?   K . n 
B 2 573 ASP 573 573 ?   ?   ?   K . n 
B 2 574 VAL 574 574 ?   ?   ?   K . n 
B 2 575 LYS 575 575 ?   ?   ?   K . n 
B 2 576 GLN 576 576 ?   ?   ?   K . n 
B 2 577 PRO 577 577 ?   ?   ?   K . n 
B 2 578 GLU 578 578 ?   ?   ?   K . n 
B 2 579 GLY 579 579 ?   ?   ?   K . n 
B 2 580 THR 580 580 ?   ?   ?   K . n 
B 2 581 GLY 581 581 ?   ?   ?   K . n 
B 2 582 MET 582 582 ?   ?   ?   K . n 
B 2 583 ILE 583 583 ?   ?   ?   K . n 
B 2 584 ASP 584 584 ?   ?   ?   K . n 
B 2 585 GLU 585 585 ?   ?   ?   K . n 
B 2 586 GLU 586 586 ?   ?   ?   K . n 
B 2 587 PHE 587 587 ?   ?   ?   K . n 
B 2 588 THR 588 588 ?   ?   ?   K . n 
B 2 589 VAL 589 589 ?   ?   ?   K . n 
B 2 590 ALA 590 590 ?   ?   ?   K . n 
B 2 591 ARG 591 591 ?   ?   ?   K . n 
B 2 592 LEU 592 592 ?   ?   ?   K . n 
B 2 593 TYR 593 593 ?   ?   ?   K . n 
B 2 594 ILE 594 594 ?   ?   ?   K . n 
B 2 595 SER 595 595 ?   ?   ?   K . n 
B 2 596 LYS 596 596 ?   ?   ?   K . n 
B 2 597 MET 597 597 ?   ?   ?   K . n 
B 2 598 LYS 598 598 ?   ?   ?   K . n 
B 2 599 SER 599 599 ?   ?   ?   K . n 
B 2 600 GLU 600 600 ?   ?   ?   K . n 
B 2 601 VAL 601 601 ?   ?   ?   K . n 
B 2 602 LYS 602 602 ?   ?   ?   K . n 
B 2 603 THR 603 603 ?   ?   ?   K . n 
B 2 604 MET 604 604 ?   ?   ?   K . n 
B 2 605 VAL 605 605 ?   ?   ?   K . n 
B 2 606 LYS 606 606 ?   ?   ?   K . n 
B 2 607 ARG 607 607 ?   ?   ?   K . n 
B 2 608 CYS 608 608 ?   ?   ?   K . n 
B 2 609 LYS 609 609 ?   ?   ?   K . n 
B 2 610 GLN 610 610 ?   ?   ?   K . n 
B 2 611 LEU 611 611 ?   ?   ?   K . n 
B 2 612 GLU 612 612 ?   ?   ?   K . n 
B 2 613 SER 613 613 ?   ?   ?   K . n 
B 2 614 THR 614 614 ?   ?   ?   K . n 
B 2 615 GLN 615 615 ?   ?   ?   K . n 
B 2 616 THR 616 616 ?   ?   ?   K . n 
B 2 617 GLU 617 617 ?   ?   ?   K . n 
B 2 618 SER 618 618 ?   ?   ?   K . n 
B 2 619 ASN 619 619 ?   ?   ?   K . n 
B 2 620 LYS 620 620 ?   ?   ?   K . n 
B 2 621 LYS 621 621 ?   ?   ?   K . n 
B 2 622 MET 622 622 ?   ?   ?   K . n 
B 2 623 GLU 623 623 ?   ?   ?   K . n 
B 2 624 GLU 624 624 ?   ?   ?   K . n 
B 2 625 ASN 625 625 ?   ?   ?   K . n 
B 2 626 GLU 626 626 ?   ?   ?   K . n 
B 2 627 LYS 627 627 ?   ?   ?   K . n 
B 2 628 GLU 628 628 ?   ?   ?   K . n 
B 2 629 LEU 629 629 ?   ?   ?   K . n 
B 2 630 ALA 630 630 ?   ?   ?   K . n 
B 2 631 ALA 631 631 ?   ?   ?   K . n 
B 2 632 CYS 632 632 ?   ?   ?   K . n 
B 2 633 GLN 633 633 ?   ?   ?   K . n 
B 2 634 LEU 634 634 ?   ?   ?   K . n 
B 2 635 ARG 635 635 ?   ?   ?   K . n 
B 2 636 ILE 636 636 ?   ?   ?   K . n 
B 2 637 SER 637 637 ?   ?   ?   K . n 
B 2 638 GLN 638 638 ?   ?   ?   K . n 
B 2 639 HIS 639 639 ?   ?   ?   K . n 
B 2 640 GLU 640 640 ?   ?   ?   K . n 
B 2 641 ALA 641 641 ?   ?   ?   K . n 
B 2 642 LYS 642 642 ?   ?   ?   K . n 
B 2 643 ILE 643 643 ?   ?   ?   K . n 
B 2 644 LYS 644 644 ?   ?   ?   K . n 
B 2 645 SER 645 645 ?   ?   ?   K . n 
B 2 646 LEU 646 646 ?   ?   ?   K . n 
B 2 647 THR 647 647 ?   ?   ?   K . n 
B 2 648 GLU 648 648 ?   ?   ?   K . n 
B 2 649 TYR 649 649 ?   ?   ?   K . n 
B 2 650 LEU 650 650 ?   ?   ?   K . n 
B 2 651 GLN 651 651 ?   ?   ?   K . n 
B 2 652 ASN 652 652 ?   ?   ?   K . n 
B 2 653 VAL 653 653 ?   ?   ?   K . n 
B 2 654 GLU 654 654 ?   ?   ?   K . n 
B 2 655 GLN 655 655 ?   ?   ?   K . n 
B 2 656 LYS 656 656 ?   ?   ?   K . n 
B 2 657 LYS 657 657 ?   ?   ?   K . n 
B 2 658 ARG 658 658 ?   ?   ?   K . n 
B 2 659 GLN 659 659 ?   ?   ?   K . n 
B 2 660 LEU 660 660 ?   ?   ?   K . n 
B 2 661 GLU 661 661 ?   ?   ?   K . n 
B 2 662 GLU 662 662 ?   ?   ?   K . n 
B 2 663 SER 663 663 ?   ?   ?   K . n 
B 2 664 VAL 664 664 ?   ?   ?   K . n 
B 2 665 ASP 665 665 ?   ?   ?   K . n 
B 2 666 ALA 666 666 ?   ?   ?   K . n 
B 2 667 LEU 667 667 ?   ?   ?   K . n 
B 2 668 SER 668 668 ?   ?   ?   K . n 
B 2 669 GLU 669 669 ?   ?   ?   K . n 
B 2 670 GLU 670 670 ?   ?   ?   K . n 
B 2 671 LEU 671 671 ?   ?   ?   K . n 
B 2 672 VAL 672 672 ?   ?   ?   K . n 
B 2 673 GLN 673 673 ?   ?   ?   K . n 
B 2 674 LEU 674 674 ?   ?   ?   K . n 
B 2 675 ARG 675 675 ?   ?   ?   K . n 
B 2 676 ALA 676 676 ?   ?   ?   K . n 
B 2 677 GLN 677 677 ?   ?   ?   K . n 
B 2 678 GLU 678 678 ?   ?   ?   K . n 
B 2 679 LYS 679 679 ?   ?   ?   K . n 
B 2 680 VAL 680 680 ?   ?   ?   K . n 
B 2 681 HIS 681 681 ?   ?   ?   K . n 
B 2 682 GLU 682 682 ?   ?   ?   K . n 
B 2 683 MET 683 683 ?   ?   ?   K . n 
B 2 684 GLU 684 684 ?   ?   ?   K . n 
B 2 685 LYS 685 685 ?   ?   ?   K . n 
B 2 686 GLU 686 686 ?   ?   ?   K . n 
B 2 687 HIS 687 687 ?   ?   ?   K . n 
B 2 688 LEU 688 688 ?   ?   ?   K . n 
B 2 689 ASN 689 689 ?   ?   ?   K . n 
B 2 690 LYS 690 690 ?   ?   ?   K . n 
B 2 691 VAL 691 691 ?   ?   ?   K . n 
B 2 692 GLN 692 692 ?   ?   ?   K . n 
B 2 693 THR 693 693 ?   ?   ?   K . n 
B 2 694 ALA 694 694 ?   ?   ?   K . n 
B 2 695 ASN 695 695 ?   ?   ?   K . n 
B 2 696 GLU 696 696 ?   ?   ?   K . n 
B 2 697 VAL 697 697 ?   ?   ?   K . n 
B 2 698 LYS 698 698 ?   ?   ?   K . n 
B 2 699 GLN 699 699 ?   ?   ?   K . n 
B 2 700 ALA 700 700 ?   ?   ?   K . n 
B 2 701 VAL 701 701 ?   ?   ?   K . n 
B 2 702 GLU 702 702 ?   ?   ?   K . n 
B 2 703 GLN 703 703 ?   ?   ?   K . n 
B 2 704 GLN 704 704 ?   ?   ?   K . n 
B 2 705 ILE 705 705 ?   ?   ?   K . n 
B 2 706 GLN 706 706 ?   ?   ?   K . n 
B 2 707 SER 707 707 ?   ?   ?   K . n 
B 2 708 HIS 708 708 ?   ?   ?   K . n 
B 2 709 ARG 709 709 ?   ?   ?   K . n 
B 2 710 GLU 710 710 ?   ?   ?   K . n 
B 2 711 THR 711 711 ?   ?   ?   K . n 
B 2 712 HIS 712 712 ?   ?   ?   K . n 
B 2 713 GLN 713 713 ?   ?   ?   K . n 
B 2 714 LYS 714 714 ?   ?   ?   K . n 
B 2 715 GLN 715 715 ?   ?   ?   K . n 
B 2 716 ILE 716 716 ?   ?   ?   K . n 
B 2 717 SER 717 717 ?   ?   ?   K . n 
B 2 718 SER 718 718 ?   ?   ?   K . n 
B 2 719 LEU 719 719 ?   ?   ?   K . n 
B 2 720 ARG 720 720 ?   ?   ?   K . n 
B 2 721 ASP 721 721 ?   ?   ?   K . n 
B 2 722 GLU 722 722 ?   ?   ?   K . n 
B 2 723 VAL 723 723 ?   ?   ?   K . n 
B 2 724 GLU 724 724 ?   ?   ?   K . n 
B 2 725 ALA 725 725 ?   ?   ?   K . n 
B 2 726 LYS 726 726 ?   ?   ?   K . n 
B 2 727 ALA 727 727 ?   ?   ?   K . n 
B 2 728 LYS 728 728 ?   ?   ?   K . n 
B 2 729 LEU 729 729 ?   ?   ?   K . n 
B 2 730 ILE 730 730 ?   ?   ?   K . n 
B 2 731 THR 731 731 ?   ?   ?   K . n 
B 2 732 ASP 732 732 ?   ?   ?   K . n 
B 2 733 LEU 733 733 ?   ?   ?   K . n 
B 2 734 GLN 734 734 ?   ?   ?   K . n 
B 2 735 ASP 735 735 ?   ?   ?   K . n 
B 2 736 GLN 736 736 ?   ?   ?   K . n 
B 2 737 ASN 737 737 ?   ?   ?   K . n 
B 2 738 GLN 738 738 ?   ?   ?   K . n 
B 2 739 LYS 739 739 ?   ?   ?   K . n 
B 2 740 MET 740 740 ?   ?   ?   K . n 
B 2 741 MET 741 741 ?   ?   ?   K . n 
B 2 742 LEU 742 742 ?   ?   ?   K . n 
B 2 743 GLU 743 743 ?   ?   ?   K . n 
B 2 744 GLN 744 744 ?   ?   ?   K . n 
B 2 745 GLU 745 745 ?   ?   ?   K . n 
B 2 746 ARG 746 746 ?   ?   ?   K . n 
B 2 747 LEU 747 747 ?   ?   ?   K . n 
B 2 748 ARG 748 748 ?   ?   ?   K . n 
B 2 749 VAL 749 749 ?   ?   ?   K . n 
B 2 750 GLU 750 750 ?   ?   ?   K . n 
B 2 751 HIS 751 751 ?   ?   ?   K . n 
B 2 752 GLU 752 752 ?   ?   ?   K . n 
B 2 753 LYS 753 753 ?   ?   ?   K . n 
B 2 754 LEU 754 754 ?   ?   ?   K . n 
B 2 755 LYS 755 755 ?   ?   ?   K . n 
B 2 756 ALA 756 756 ?   ?   ?   K . n 
B 2 757 THR 757 757 ?   ?   ?   K . n 
B 2 758 ASP 758 758 ?   ?   ?   K . n 
B 2 759 GLN 759 759 ?   ?   ?   K . n 
B 2 760 GLU 760 760 ?   ?   ?   K . n 
B 2 761 LYS 761 761 ?   ?   ?   K . n 
B 2 762 SER 762 762 ?   ?   ?   K . n 
B 2 763 ARG 763 763 ?   ?   ?   K . n 
B 2 764 LYS 764 764 ?   ?   ?   K . n 
B 2 765 LEU 765 765 ?   ?   ?   K . n 
B 2 766 HIS 766 766 ?   ?   ?   K . n 
B 2 767 GLU 767 767 ?   ?   ?   K . n 
B 2 768 LEU 768 768 ?   ?   ?   K . n 
B 2 769 THR 769 769 ?   ?   ?   K . n 
B 2 770 VAL 770 770 ?   ?   ?   K . n 
B 2 771 MET 771 771 ?   ?   ?   K . n 
B 2 772 GLN 772 772 ?   ?   ?   K . n 
B 2 773 ASP 773 773 ?   ?   ?   K . n 
B 2 774 ARG 774 774 ?   ?   ?   K . n 
B 2 775 ARG 775 775 ?   ?   ?   K . n 
B 2 776 GLU 776 776 ?   ?   ?   K . n 
B 2 777 GLN 777 777 ?   ?   ?   K . n 
B 2 778 ALA 778 778 ?   ?   ?   K . n 
B 2 779 ARG 779 779 ?   ?   ?   K . n 
B 2 780 GLN 780 780 ?   ?   ?   K . n 
B 2 781 ASP 781 781 ?   ?   ?   K . n 
B 2 782 LEU 782 782 ?   ?   ?   K . n 
B 2 783 LYS 783 783 ?   ?   ?   K . n 
B 2 784 GLY 784 784 ?   ?   ?   K . n 
B 2 785 LEU 785 785 ?   ?   ?   K . n 
B 2 786 GLU 786 786 ?   ?   ?   K . n 
B 2 787 GLU 787 787 ?   ?   ?   K . n 
B 2 788 THR 788 788 ?   ?   ?   K . n 
B 2 789 VAL 789 789 ?   ?   ?   K . n 
B 2 790 ALA 790 790 ?   ?   ?   K . n 
B 2 791 LYS 791 791 ?   ?   ?   K . n 
B 2 792 GLU 792 792 ?   ?   ?   K . n 
B 2 793 LEU 793 793 ?   ?   ?   K . n 
B 2 794 GLN 794 794 ?   ?   ?   K . n 
B 2 795 THR 795 795 ?   ?   ?   K . n 
B 2 796 LEU 796 796 ?   ?   ?   K . n 
B 2 797 HIS 797 797 ?   ?   ?   K . n 
B 2 798 ASN 798 798 ?   ?   ?   K . n 
B 2 799 LEU 799 799 ?   ?   ?   K . n 
B 2 800 ARG 800 800 ?   ?   ?   K . n 
B 2 801 LYS 801 801 ?   ?   ?   K . n 
B 2 802 LEU 802 802 ?   ?   ?   K . n 
B 2 803 PHE 803 803 ?   ?   ?   K . n 
B 2 804 VAL 804 804 ?   ?   ?   K . n 
B 2 805 GLN 805 805 ?   ?   ?   K . n 
B 2 806 ASP 806 806 ?   ?   ?   K . n 
B 2 807 LEU 807 807 ?   ?   ?   K . n 
B 2 808 ALA 808 808 ?   ?   ?   K . n 
B 2 809 THR 809 809 ?   ?   ?   K . n 
B 2 810 ARG 810 810 ?   ?   ?   K . n 
B 2 811 VAL 811 811 ?   ?   ?   K . n 
B 2 812 LYS 812 812 ?   ?   ?   K . n 
B 2 813 LYS 813 813 ?   ?   ?   K . n 
B 2 814 SER 814 814 ?   ?   ?   K . n 
B 2 815 ALA 815 815 ?   ?   ?   K . n 
B 2 816 GLU 816 816 ?   ?   ?   K . n 
B 2 817 ILE 817 817 ?   ?   ?   K . n 
B 2 818 ASP 818 818 ?   ?   ?   K . n 
B 2 819 SER 819 819 ?   ?   ?   K . n 
B 2 820 ASP 820 820 ?   ?   ?   K . n 
B 2 821 ASP 821 821 ?   ?   ?   K . n 
B 2 822 THR 822 822 ?   ?   ?   K . n 
B 2 823 GLY 823 823 ?   ?   ?   K . n 
B 2 824 GLY 824 824 ?   ?   ?   K . n 
B 2 825 SER 825 825 ?   ?   ?   K . n 
B 2 826 ALA 826 826 ?   ?   ?   K . n 
B 2 827 ALA 827 827 ?   ?   ?   K . n 
B 2 828 GLN 828 828 ?   ?   ?   K . n 
B 2 829 LYS 829 829 ?   ?   ?   K . n 
B 2 830 GLN 830 830 ?   ?   ?   K . n 
B 2 831 LYS 831 831 ?   ?   ?   K . n 
B 2 832 ILE 832 832 ?   ?   ?   K . n 
B 2 833 SER 833 833 ?   ?   ?   K . n 
B 2 834 PHE 834 834 ?   ?   ?   K . n 
B 2 835 LEU 835 835 ?   ?   ?   K . n 
B 2 836 GLU 836 836 ?   ?   ?   K . n 
B 2 837 ASN 837 837 ?   ?   ?   K . n 
B 2 838 ASN 838 838 ?   ?   ?   K . n 
B 2 839 LEU 839 839 ?   ?   ?   K . n 
B 2 840 GLU 840 840 ?   ?   ?   K . n 
B 2 841 GLN 841 841 ?   ?   ?   K . n 
B 2 842 LEU 842 842 ?   ?   ?   K . n 
B 2 843 THR 843 843 ?   ?   ?   K . n 
B 2 844 LYS 844 844 ?   ?   ?   K . n 
B 2 845 VAL 845 845 ?   ?   ?   K . n 
B 2 846 HIS 846 846 ?   ?   ?   K . n 
B 2 847 LYS 847 847 ?   ?   ?   K . n 
B 2 848 GLN 848 848 ?   ?   ?   K . n 
B 2 849 LEU 849 849 ?   ?   ?   K . n 
B 2 850 VAL 850 850 ?   ?   ?   K . n 
B 2 851 ARG 851 851 ?   ?   ?   K . n 
B 2 852 ASP 852 852 ?   ?   ?   K . n 
B 2 853 ASN 853 853 ?   ?   ?   K . n 
B 2 854 ALA 854 854 ?   ?   ?   K . n 
B 2 855 ASP 855 855 ?   ?   ?   K . n 
B 2 856 LEU 856 856 ?   ?   ?   K . n 
B 2 857 ARG 857 857 ?   ?   ?   K . n 
B 2 858 CYS 858 858 ?   ?   ?   K . n 
B 2 859 GLU 859 859 ?   ?   ?   K . n 
B 2 860 LEU 860 860 ?   ?   ?   K . n 
B 2 861 PRO 861 861 ?   ?   ?   K . n 
B 2 862 LYS 862 862 ?   ?   ?   K . n 
B 2 863 LEU 863 863 ?   ?   ?   K . n 
B 2 864 GLU 864 864 ?   ?   ?   K . n 
B 2 865 LYS 865 865 ?   ?   ?   K . n 
B 2 866 ARG 866 866 ?   ?   ?   K . n 
B 2 867 LEU 867 867 ?   ?   ?   K . n 
B 2 868 ARG 868 868 ?   ?   ?   K . n 
B 2 869 ALA 869 869 ?   ?   ?   K . n 
B 2 870 THR 870 870 ?   ?   ?   K . n 
B 2 871 ALA 871 871 ?   ?   ?   K . n 
B 2 872 GLU 872 872 ?   ?   ?   K . n 
B 2 873 ARG 873 873 ?   ?   ?   K . n 
B 2 874 VAL 874 874 ?   ?   ?   K . n 
B 2 875 LYS 875 875 ?   ?   ?   K . n 
B 2 876 ALA 876 876 ?   ?   ?   K . n 
B 2 877 LEU 877 877 ?   ?   ?   K . n 
B 2 878 GLU 878 878 ?   ?   ?   K . n 
B 2 879 SER 879 879 ?   ?   ?   K . n 
B 2 880 ALA 880 880 ?   ?   ?   K . n 
B 2 881 LEU 881 881 ?   ?   ?   K . n 
B 2 882 LYS 882 882 ?   ?   ?   K . n 
B 2 883 GLU 883 883 ?   ?   ?   K . n 
B 2 884 ALA 884 884 ?   ?   ?   K . n 
B 2 885 LYS 885 885 ?   ?   ?   K . n 
B 2 886 GLU 886 886 ?   ?   ?   K . n 
B 2 887 ASN 887 887 ?   ?   ?   K . n 
B 2 888 ALA 888 888 ?   ?   ?   K . n 
B 2 889 SER 889 889 ?   ?   ?   K . n 
B 2 890 ARG 890 890 ?   ?   ?   K . n 
B 2 891 ASP 891 891 ?   ?   ?   K . n 
B 2 892 ARG 892 892 ?   ?   ?   K . n 
B 2 893 LYS 893 893 ?   ?   ?   K . n 
B 2 894 ARG 894 894 ?   ?   ?   K . n 
B 2 895 TYR 895 895 ?   ?   ?   K . n 
B 2 896 GLN 896 896 ?   ?   ?   K . n 
B 2 897 GLN 897 897 ?   ?   ?   K . n 
B 2 898 GLU 898 898 ?   ?   ?   K . n 
B 2 899 VAL 899 899 ?   ?   ?   K . n 
B 2 900 ASP 900 900 ?   ?   ?   K . n 
B 2 901 ARG 901 901 ?   ?   ?   K . n 
B 2 902 ILE 902 902 ?   ?   ?   K . n 
B 2 903 LYS 903 903 ?   ?   ?   K . n 
B 2 904 GLU 904 904 ?   ?   ?   K . n 
B 2 905 ALA 905 905 ?   ?   ?   K . n 
B 2 906 VAL 906 906 ?   ?   ?   K . n 
B 2 907 ARG 907 907 ?   ?   ?   K . n 
B 2 908 SER 908 908 ?   ?   ?   K . n 
B 2 909 LYS 909 909 ?   ?   ?   K . n 
B 2 910 ASN 910 910 ?   ?   ?   K . n 
B 2 911 MET 911 911 ?   ?   ?   K . n 
B 2 912 ALA 912 912 ?   ?   ?   K . n 
B 2 913 ARG 913 913 ?   ?   ?   K . n 
B 2 914 ARG 914 914 ?   ?   ?   K . n 
B 2 915 GLY 915 915 ?   ?   ?   K . n 
B 2 916 HIS 916 916 ?   ?   ?   K . n 
B 2 917 SER 917 917 ?   ?   ?   K . n 
B 2 918 ALA 918 918 ?   ?   ?   K . n 
B 2 919 GLN 919 919 ?   ?   ?   K . n 
B 2 920 ILE 920 920 ?   ?   ?   K . n 
B 2 921 ALA 921 921 ?   ?   ?   K . n 
B 2 922 LYS 922 922 ?   ?   ?   K . n 
B 2 923 PRO 923 923 ?   ?   ?   K . n 
B 2 924 ILE 924 924 ?   ?   ?   K . n 
B 2 925 ARG 925 925 ?   ?   ?   K . n 
B 2 926 PRO 926 926 ?   ?   ?   K . n 
B 2 927 GLY 927 927 ?   ?   ?   K . n 
B 2 928 GLN 928 928 ?   ?   ?   K . n 
B 2 929 HIS 929 929 ?   ?   ?   K . n 
B 2 930 PRO 930 930 ?   ?   ?   K . n 
B 2 931 ALA 931 931 ?   ?   ?   K . n 
B 2 932 ALA 932 932 ?   ?   ?   K . n 
B 2 933 SER 933 933 ?   ?   ?   K . n 
B 2 934 PRO 934 934 ?   ?   ?   K . n 
B 2 935 THR 935 935 ?   ?   ?   K . n 
B 2 936 HIS 936 936 ?   ?   ?   K . n 
B 2 937 PRO 937 937 ?   ?   ?   K . n 
B 2 938 SER 938 938 ?   ?   ?   K . n 
B 2 939 ALA 939 939 ?   ?   ?   K . n 
B 2 940 ILE 940 940 ?   ?   ?   K . n 
B 2 941 ARG 941 941 ?   ?   ?   K . n 
B 2 942 GLY 942 942 ?   ?   ?   K . n 
B 2 943 GLY 943 943 ?   ?   ?   K . n 
B 2 944 GLY 944 944 ?   ?   ?   K . n 
B 2 945 ALA 945 945 ?   ?   ?   K . n 
B 2 946 PHE 946 946 ?   ?   ?   K . n 
B 2 947 VAL 947 947 ?   ?   ?   K . n 
B 2 948 GLN 948 948 ?   ?   ?   K . n 
B 2 949 ASN 949 949 ?   ?   ?   K . n 
B 2 950 SER 950 950 ?   ?   ?   K . n 
B 2 951 GLN 951 951 ?   ?   ?   K . n 
B 2 952 PRO 952 952 ?   ?   ?   K . n 
B 2 953 VAL 953 953 ?   ?   ?   K . n 
B 2 954 ALA 954 954 ?   ?   ?   K . n 
B 2 955 VAL 955 955 ?   ?   ?   K . n 
B 2 956 ARG 956 956 ?   ?   ?   K . n 
B 2 957 GLY 957 957 ?   ?   ?   K . n 
B 2 958 GLY 958 958 ?   ?   ?   K . n 
B 2 959 GLY 959 959 ?   ?   ?   K . n 
B 2 960 GLY 960 960 ?   ?   ?   K . n 
B 2 961 LYS 961 961 ?   ?   ?   K . n 
B 2 962 GLN 962 962 ?   ?   ?   K . n 
B 2 963 VAL 963 963 ?   ?   ?   K . n 
C 2 1   MET 1   1   ?   ?   ?   L . n 
C 2 2   ALA 2   2   ?   ?   ?   L . n 
C 2 3   ASP 3   3   ?   ?   ?   L . n 
C 2 4   LEU 4   4   4   LEU LEU L . n 
C 2 5   ALA 5   5   5   ALA ALA L . n 
C 2 6   GLU 6   6   6   GLU GLU L . n 
C 2 7   CYS 7   7   7   CYS CYS L . n 
C 2 8   ASN 8   8   8   ASN ASN L . n 
C 2 9   ILE 9   9   9   ILE ILE L . n 
C 2 10  LYS 10  10  10  LYS LYS L . n 
C 2 11  VAL 11  11  11  VAL VAL L . n 
C 2 12  MET 12  12  12  MET MET L . n 
C 2 13  CYS 13  13  13  CYS CYS L . n 
C 2 14  ARG 14  14  14  ARG ARG L . n 
C 2 15  PHE 15  15  15  PHE PHE L . n 
C 2 16  ARG 16  16  16  ARG ARG L . n 
C 2 17  PRO 17  17  17  PRO PRO L . n 
C 2 18  LEU 18  18  18  LEU LEU L . n 
C 2 19  ASN 19  19  19  ASN ASN L . n 
C 2 20  GLU 20  20  20  GLU GLU L . n 
C 2 21  SER 21  21  21  SER SER L . n 
C 2 22  GLU 22  22  22  GLU GLU L . n 
C 2 23  VAL 23  23  23  VAL VAL L . n 
C 2 24  ASN 24  24  24  ASN ASN L . n 
C 2 25  ARG 25  25  25  ARG ARG L . n 
C 2 26  GLY 26  26  26  GLY GLY L . n 
C 2 27  ASP 27  27  27  ASP ASP L . n 
C 2 28  LYS 28  28  28  LYS LYS L . n 
C 2 29  TYR 29  29  29  TYR TYR L . n 
C 2 30  ILE 30  30  30  ILE ILE L . n 
C 2 31  ALA 31  31  31  ALA ALA L . n 
C 2 32  LYS 32  32  32  LYS LYS L . n 
C 2 33  PHE 33  33  33  PHE PHE L . n 
C 2 34  GLN 34  34  34  GLN GLN L . n 
C 2 35  GLY 35  35  35  GLY GLY L . n 
C 2 36  GLU 36  36  36  GLU GLU L . n 
C 2 37  ASP 37  37  37  ASP ASP L . n 
C 2 38  THR 38  38  38  THR THR L . n 
C 2 39  VAL 39  39  39  VAL VAL L . n 
C 2 40  VAL 40  40  40  VAL VAL L . n 
C 2 41  ILE 41  41  41  ILE ILE L . n 
C 2 42  ALA 42  42  42  ALA ALA L . n 
C 2 43  SER 43  43  43  SER SER L . n 
C 2 44  LYS 44  44  44  LYS LYS L . n 
C 2 45  PRO 45  45  45  PRO PRO L . n 
C 2 46  TYR 46  46  46  TYR TYR L . n 
C 2 47  ALA 47  47  47  ALA ALA L . n 
C 2 48  PHE 48  48  48  PHE PHE L . n 
C 2 49  ASP 49  49  49  ASP ASP L . n 
C 2 50  ARG 50  50  50  ARG ARG L . n 
C 2 51  VAL 51  51  51  VAL VAL L . n 
C 2 52  PHE 52  52  52  PHE PHE L . n 
C 2 53  GLN 53  53  53  GLN GLN L . n 
C 2 54  SER 54  54  54  SER SER L . n 
C 2 55  SER 55  55  55  SER SER L . n 
C 2 56  THR 56  56  56  THR THR L . n 
C 2 57  SER 57  57  57  SER SER L . n 
C 2 58  GLN 58  58  58  GLN GLN L . n 
C 2 59  GLU 59  59  59  GLU GLU L . n 
C 2 60  GLN 60  60  60  GLN GLN L . n 
C 2 61  VAL 61  61  61  VAL VAL L . n 
C 2 62  TYR 62  62  62  TYR TYR L . n 
C 2 63  ASN 63  63  63  ASN ASN L . n 
C 2 64  ASP 64  64  64  ASP ASP L . n 
C 2 65  CYS 65  65  65  CYS CYS L . n 
C 2 66  ALA 66  66  66  ALA ALA L . n 
C 2 67  LYS 67  67  67  LYS LYS L . n 
C 2 68  LYS 68  68  68  LYS LYS L . n 
C 2 69  ILE 69  69  69  ILE ILE L . n 
C 2 70  VAL 70  70  70  VAL VAL L . n 
C 2 71  LYS 71  71  71  LYS LYS L . n 
C 2 72  ASP 72  72  72  ASP ASP L . n 
C 2 73  VAL 73  73  73  VAL VAL L . n 
C 2 74  LEU 74  74  74  LEU LEU L . n 
C 2 75  GLU 75  75  75  GLU GLU L . n 
C 2 76  GLY 76  76  76  GLY GLY L . n 
C 2 77  TYR 77  77  77  TYR TYR L . n 
C 2 78  ASN 78  78  78  ASN ASN L . n 
C 2 79  GLY 79  79  79  GLY GLY L . n 
C 2 80  THR 80  80  80  THR THR L . n 
C 2 81  ILE 81  81  81  ILE ILE L . n 
C 2 82  PHE 82  82  82  PHE PHE L . n 
C 2 83  ALA 83  83  83  ALA ALA L . n 
C 2 84  TYR 84  84  84  TYR TYR L . n 
C 2 85  GLY 85  85  85  GLY GLY L . n 
C 2 86  GLN 86  86  86  GLN GLN L . n 
C 2 87  THR 87  87  87  THR THR L . n 
C 2 88  SER 88  88  88  SER SER L . n 
C 2 89  SER 89  89  89  SER SER L . n 
C 2 90  GLY 90  90  90  GLY GLY L . n 
C 2 91  LYS 91  91  91  LYS LYS L . n 
C 2 92  THR 92  92  92  THR THR L . n 
C 2 93  HIS 93  93  93  HIS HIS L . n 
C 2 94  THR 94  94  94  THR THR L . n 
C 2 95  MET 95  95  95  MET MET L . n 
C 2 96  GLU 96  96  96  GLU GLU L . n 
C 2 97  GLY 97  97  97  GLY GLY L . n 
C 2 98  LYS 98  98  98  LYS LYS L . n 
C 2 99  LEU 99  99  99  LEU LEU L . n 
C 2 100 HIS 100 100 100 HIS HIS L . n 
C 2 101 ASP 101 101 101 ASP ASP L . n 
C 2 102 PRO 102 102 102 PRO PRO L . n 
C 2 103 GLU 103 103 103 GLU GLU L . n 
C 2 104 GLY 104 104 104 GLY GLY L . n 
C 2 105 MET 105 105 105 MET MET L . n 
C 2 106 GLY 106 106 106 GLY GLY L . n 
C 2 107 ILE 107 107 107 ILE ILE L . n 
C 2 108 ILE 108 108 108 ILE ILE L . n 
C 2 109 PRO 109 109 109 PRO PRO L . n 
C 2 110 ARG 110 110 110 ARG ARG L . n 
C 2 111 ILE 111 111 111 ILE ILE L . n 
C 2 112 VAL 112 112 112 VAL VAL L . n 
C 2 113 GLN 113 113 113 GLN GLN L . n 
C 2 114 ASP 114 114 114 ASP ASP L . n 
C 2 115 ILE 115 115 115 ILE ILE L . n 
C 2 116 PHE 116 116 116 PHE PHE L . n 
C 2 117 ASN 117 117 117 ASN ASN L . n 
C 2 118 TYR 118 118 118 TYR TYR L . n 
C 2 119 ILE 119 119 119 ILE ILE L . n 
C 2 120 TYR 120 120 120 TYR TYR L . n 
C 2 121 SER 121 121 121 SER SER L . n 
C 2 122 MET 122 122 122 MET MET L . n 
C 2 123 ASP 123 123 123 ASP ASP L . n 
C 2 124 GLU 124 124 124 GLU GLU L . n 
C 2 125 ASN 125 125 125 ASN ASN L . n 
C 2 126 LEU 126 126 126 LEU LEU L . n 
C 2 127 GLU 127 127 127 GLU GLU L . n 
C 2 128 PHE 128 128 128 PHE PHE L . n 
C 2 129 HIS 129 129 129 HIS HIS L . n 
C 2 130 ILE 130 130 130 ILE ILE L . n 
C 2 131 LYS 131 131 131 LYS LYS L . n 
C 2 132 VAL 132 132 132 VAL VAL L . n 
C 2 133 SER 133 133 133 SER SER L . n 
C 2 134 TYR 134 134 134 TYR TYR L . n 
C 2 135 PHE 135 135 135 PHE PHE L . n 
C 2 136 GLU 136 136 136 GLU GLU L . n 
C 2 137 ILE 137 137 137 ILE ILE L . n 
C 2 138 TYR 138 138 138 TYR TYR L . n 
C 2 139 LEU 139 139 139 LEU LEU L . n 
C 2 140 ASP 140 140 140 ASP ASP L . n 
C 2 141 LYS 141 141 141 LYS LYS L . n 
C 2 142 ILE 142 142 142 ILE ILE L . n 
C 2 143 ARG 143 143 143 ARG ARG L . n 
C 2 144 ASP 144 144 144 ASP ASP L . n 
C 2 145 LEU 145 145 145 LEU LEU L . n 
C 2 146 LEU 146 146 146 LEU LEU L . n 
C 2 147 ASP 147 147 147 ASP ASP L . n 
C 2 148 VAL 148 148 148 VAL VAL L . n 
C 2 149 SER 149 149 149 SER SER L . n 
C 2 150 LYS 150 150 150 LYS LYS L . n 
C 2 151 THR 151 151 151 THR THR L . n 
C 2 152 ASN 152 152 152 ASN ASN L . n 
C 2 153 LEU 153 153 153 LEU LEU L . n 
C 2 154 SER 154 154 154 SER SER L . n 
C 2 155 VAL 155 155 155 VAL VAL L . n 
C 2 156 HIS 156 156 156 HIS HIS L . n 
C 2 157 GLU 157 157 157 GLU GLU L . n 
C 2 158 ASP 158 158 158 ASP ASP L . n 
C 2 159 LYS 159 159 159 LYS LYS L . n 
C 2 160 ASN 160 160 160 ASN ASN L . n 
C 2 161 ARG 161 161 161 ARG ARG L . n 
C 2 162 VAL 162 162 162 VAL VAL L . n 
C 2 163 PRO 163 163 163 PRO PRO L . n 
C 2 164 TYR 164 164 164 TYR TYR L . n 
C 2 165 VAL 165 165 165 VAL VAL L . n 
C 2 166 LYS 166 166 166 LYS LYS L . n 
C 2 167 GLY 167 167 167 GLY GLY L . n 
C 2 168 CYS 168 168 168 CYS CYS L . n 
C 2 169 THR 169 169 169 THR THR L . n 
C 2 170 GLU 170 170 170 GLU GLU L . n 
C 2 171 ARG 171 171 171 ARG ARG L . n 
C 2 172 PHE 172 172 172 PHE PHE L . n 
C 2 173 VAL 173 173 173 VAL VAL L . n 
C 2 174 CYS 174 174 174 CYS CYS L . n 
C 2 175 SER 175 175 175 SER SER L . n 
C 2 176 PRO 176 176 176 PRO PRO L . n 
C 2 177 ASP 177 177 177 ASP ASP L . n 
C 2 178 GLU 178 178 178 GLU GLU L . n 
C 2 179 VAL 179 179 179 VAL VAL L . n 
C 2 180 MET 180 180 180 MET MET L . n 
C 2 181 ASP 181 181 181 ASP ASP L . n 
C 2 182 THR 182 182 182 THR THR L . n 
C 2 183 ILE 183 183 183 ILE ILE L . n 
C 2 184 ASP 184 184 184 ASP ASP L . n 
C 2 185 GLU 185 185 185 GLU GLU L . n 
C 2 186 GLY 186 186 186 GLY GLY L . n 
C 2 187 LYS 187 187 187 LYS LYS L . n 
C 2 188 SER 188 188 188 SER SER L . n 
C 2 189 ASN 189 189 189 ASN ASN L . n 
C 2 190 ARG 190 190 190 ARG ARG L . n 
C 2 191 HIS 191 191 191 HIS HIS L . n 
C 2 192 VAL 192 192 ?   ?   ?   L . n 
C 2 193 ALA 193 193 ?   ?   ?   L . n 
C 2 194 VAL 194 194 ?   ?   ?   L . n 
C 2 195 THR 195 195 ?   ?   ?   L . n 
C 2 196 ASN 196 196 ?   ?   ?   L . n 
C 2 197 MET 197 197 ?   ?   ?   L . n 
C 2 198 ASN 198 198 ?   ?   ?   L . n 
C 2 199 GLU 199 199 ?   ?   ?   L . n 
C 2 200 HIS 200 200 ?   ?   ?   L . n 
C 2 201 SER 201 201 ?   ?   ?   L . n 
C 2 202 SER 202 202 202 SER SER L . n 
C 2 203 ARG 203 203 203 ARG ARG L . n 
C 2 204 SER 204 204 204 SER SER L . n 
C 2 205 HIS 205 205 205 HIS HIS L . n 
C 2 206 SER 206 206 206 SER SER L . n 
C 2 207 ILE 207 207 207 ILE ILE L . n 
C 2 208 PHE 208 208 208 PHE PHE L . n 
C 2 209 LEU 209 209 209 LEU LEU L . n 
C 2 210 ILE 210 210 210 ILE ILE L . n 
C 2 211 ASN 211 211 211 ASN ASN L . n 
C 2 212 VAL 212 212 212 VAL VAL L . n 
C 2 213 LYS 213 213 213 LYS LYS L . n 
C 2 214 GLN 214 214 214 GLN GLN L . n 
C 2 215 GLU 215 215 215 GLU GLU L . n 
C 2 216 ASN 216 216 216 ASN ASN L . n 
C 2 217 THR 217 217 217 THR THR L . n 
C 2 218 GLN 218 218 218 GLN GLN L . n 
C 2 219 THR 219 219 219 THR THR L . n 
C 2 220 GLU 220 220 220 GLU GLU L . n 
C 2 221 GLN 221 221 221 GLN GLN L . n 
C 2 222 LYS 222 222 222 LYS LYS L . n 
C 2 223 LEU 223 223 223 LEU LEU L . n 
C 2 224 SER 224 224 224 SER SER L . n 
C 2 225 GLY 225 225 225 GLY GLY L . n 
C 2 226 LYS 226 226 226 LYS LYS L . n 
C 2 227 LEU 227 227 227 LEU LEU L . n 
C 2 228 TYR 228 228 228 TYR TYR L . n 
C 2 229 LEU 229 229 229 LEU LEU L . n 
C 2 230 VAL 230 230 230 VAL VAL L . n 
C 2 231 ASP 231 231 231 ASP ASP L . n 
C 2 232 LEU 232 232 232 LEU LEU L . n 
C 2 233 ALA 233 233 233 ALA ALA L . n 
C 2 234 GLY 234 234 234 GLY GLY L . n 
C 2 235 SER 235 235 235 SER SER L . n 
C 2 236 GLU 236 236 236 GLU GLU L . n 
C 2 237 LYS 237 237 237 LYS LYS L . n 
C 2 238 VAL 238 238 ?   ?   ?   L . n 
C 2 239 SER 239 239 ?   ?   ?   L . n 
C 2 240 LYS 240 240 ?   ?   ?   L . n 
C 2 241 THR 241 241 ?   ?   ?   L . n 
C 2 242 GLY 242 242 ?   ?   ?   L . n 
C 2 243 ALA 243 243 ?   ?   ?   L . n 
C 2 244 GLU 244 244 ?   ?   ?   L . n 
C 2 245 GLY 245 245 ?   ?   ?   L . n 
C 2 246 ALA 246 246 ?   ?   ?   L . n 
C 2 247 VAL 247 247 ?   ?   ?   L . n 
C 2 248 LEU 248 248 ?   ?   ?   L . n 
C 2 249 ASP 249 249 ?   ?   ?   L . n 
C 2 250 GLU 250 250 ?   ?   ?   L . n 
C 2 251 ALA 251 251 ?   ?   ?   L . n 
C 2 252 LYS 252 252 ?   ?   ?   L . n 
C 2 253 ASN 253 253 ?   ?   ?   L . n 
C 2 254 ILE 254 254 254 ILE ILE L . n 
C 2 255 ASN 255 255 255 ASN ASN L . n 
C 2 256 LYS 256 256 256 LYS LYS L . n 
C 2 257 SER 257 257 257 SER SER L . n 
C 2 258 LEU 258 258 258 LEU LEU L . n 
C 2 259 SER 259 259 259 SER SER L . n 
C 2 260 ALA 260 260 260 ALA ALA L . n 
C 2 261 LEU 261 261 261 LEU LEU L . n 
C 2 262 GLY 262 262 262 GLY GLY L . n 
C 2 263 ASN 263 263 263 ASN ASN L . n 
C 2 264 VAL 264 264 264 VAL VAL L . n 
C 2 265 ILE 265 265 265 ILE ILE L . n 
C 2 266 SER 266 266 266 SER SER L . n 
C 2 267 ALA 267 267 267 ALA ALA L . n 
C 2 268 LEU 268 268 268 LEU LEU L . n 
C 2 269 ALA 269 269 269 ALA ALA L . n 
C 2 270 GLU 270 270 270 GLU GLU L . n 
C 2 271 GLY 271 271 271 GLY GLY L . n 
C 2 272 SER 272 272 272 SER SER L . n 
C 2 273 THR 273 273 273 THR THR L . n 
C 2 274 TYR 274 274 274 TYR TYR L . n 
C 2 275 VAL 275 275 275 VAL VAL L . n 
C 2 276 PRO 276 276 276 PRO PRO L . n 
C 2 277 TYR 277 277 277 TYR TYR L . n 
C 2 278 ARG 278 278 278 ARG ARG L . n 
C 2 279 ASP 279 279 279 ASP ASP L . n 
C 2 280 SER 280 280 280 SER SER L . n 
C 2 281 LYS 281 281 281 LYS LYS L . n 
C 2 282 MET 282 282 282 MET MET L . n 
C 2 283 THR 283 283 283 THR THR L . n 
C 2 284 ARG 284 284 284 ARG ARG L . n 
C 2 285 ILE 285 285 285 ILE ILE L . n 
C 2 286 LEU 286 286 286 LEU LEU L . n 
C 2 287 GLN 287 287 287 GLN GLN L . n 
C 2 288 ASP 288 288 288 ASP ASP L . n 
C 2 289 SER 289 289 289 SER SER L . n 
C 2 290 LEU 290 290 290 LEU LEU L . n 
C 2 291 GLY 291 291 291 GLY GLY L . n 
C 2 292 GLY 292 292 292 GLY GLY L . n 
C 2 293 ASN 293 293 293 ASN ASN L . n 
C 2 294 CYS 294 294 294 CYS CYS L . n 
C 2 295 ARG 295 295 295 ARG ARG L . n 
C 2 296 THR 296 296 296 THR THR L . n 
C 2 297 THR 297 297 297 THR THR L . n 
C 2 298 ILE 298 298 298 ILE ILE L . n 
C 2 299 VAL 299 299 299 VAL VAL L . n 
C 2 300 ILE 300 300 300 ILE ILE L . n 
C 2 301 CYS 301 301 301 CYS CYS L . n 
C 2 302 CYS 302 302 302 CYS CYS L . n 
C 2 303 SER 303 303 303 SER SER L . n 
C 2 304 PRO 304 304 304 PRO PRO L . n 
C 2 305 SER 305 305 305 SER SER L . n 
C 2 306 SER 306 306 306 SER SER L . n 
C 2 307 TYR 307 307 307 TYR TYR L . n 
C 2 308 ASN 308 308 308 ASN ASN L . n 
C 2 309 GLU 309 309 309 GLU GLU L . n 
C 2 310 SER 310 310 310 SER SER L . n 
C 2 311 GLU 311 311 311 GLU GLU L . n 
C 2 312 THR 312 312 312 THR THR L . n 
C 2 313 LYS 313 313 313 LYS LYS L . n 
C 2 314 SER 314 314 314 SER SER L . n 
C 2 315 THR 315 315 315 THR THR L . n 
C 2 316 LEU 316 316 316 LEU LEU L . n 
C 2 317 LEU 317 317 317 LEU LEU L . n 
C 2 318 PHE 318 318 318 PHE PHE L . n 
C 2 319 GLY 319 319 319 GLY GLY L . n 
C 2 320 GLN 320 320 320 GLN GLN L . n 
C 2 321 ARG 321 321 321 ARG ARG L . n 
C 2 322 ALA 322 322 322 ALA ALA L . n 
C 2 323 LYS 323 323 323 LYS LYS L . n 
C 2 324 THR 324 324 324 THR THR L . n 
C 2 325 ILE 325 325 325 ILE ILE L . n 
C 2 326 LYS 326 326 326 LYS LYS L . n 
C 2 327 ASN 327 327 327 ASN ASN L . n 
C 2 328 THR 328 328 328 THR THR L . n 
C 2 329 VAL 329 329 329 VAL VAL L . n 
C 2 330 CYS 330 330 330 CYS CYS L . n 
C 2 331 VAL 331 331 331 VAL VAL L . n 
C 2 332 ASN 332 332 332 ASN ASN L . n 
C 2 333 VAL 333 333 333 VAL VAL L . n 
C 2 334 GLU 334 334 334 GLU GLU L . n 
C 2 335 LEU 335 335 335 LEU LEU L . n 
C 2 336 THR 336 336 336 THR THR L . n 
C 2 337 ALA 337 337 337 ALA ALA L . n 
C 2 338 GLU 338 338 338 GLU GLU L . n 
C 2 339 GLN 339 339 339 GLN GLN L . n 
C 2 340 TRP 340 340 340 TRP TRP L . n 
C 2 341 LYS 341 341 341 LYS LYS L . n 
C 2 342 LYS 342 342 342 LYS LYS L . n 
C 2 343 LYS 343 343 343 LYS LYS L . n 
C 2 344 TYR 344 344 344 TYR TYR L . n 
C 2 345 GLU 345 345 345 GLU GLU L . n 
C 2 346 LYS 346 346 346 LYS LYS L . n 
C 2 347 GLU 347 347 ?   ?   ?   L . n 
C 2 348 LYS 348 348 ?   ?   ?   L . n 
C 2 349 GLU 349 349 ?   ?   ?   L . n 
C 2 350 LYS 350 350 ?   ?   ?   L . n 
C 2 351 ASN 351 351 ?   ?   ?   L . n 
C 2 352 LYS 352 352 ?   ?   ?   L . n 
C 2 353 ILE 353 353 ?   ?   ?   L . n 
C 2 354 LEU 354 354 ?   ?   ?   L . n 
C 2 355 ARG 355 355 ?   ?   ?   L . n 
C 2 356 ASN 356 356 ?   ?   ?   L . n 
C 2 357 THR 357 357 ?   ?   ?   L . n 
C 2 358 ILE 358 358 ?   ?   ?   L . n 
C 2 359 GLN 359 359 ?   ?   ?   L . n 
C 2 360 TRP 360 360 ?   ?   ?   L . n 
C 2 361 LEU 361 361 ?   ?   ?   L . n 
C 2 362 GLU 362 362 ?   ?   ?   L . n 
C 2 363 ASN 363 363 ?   ?   ?   L . n 
C 2 364 GLU 364 364 ?   ?   ?   L . n 
C 2 365 LEU 365 365 ?   ?   ?   L . n 
C 2 366 ASN 366 366 ?   ?   ?   L . n 
C 2 367 ARG 367 367 ?   ?   ?   L . n 
C 2 368 TRP 368 368 ?   ?   ?   L . n 
C 2 369 ARG 369 369 ?   ?   ?   L . n 
C 2 370 ASN 370 370 ?   ?   ?   L . n 
C 2 371 GLY 371 371 ?   ?   ?   L . n 
C 2 372 GLU 372 372 ?   ?   ?   L . n 
C 2 373 THR 373 373 ?   ?   ?   L . n 
C 2 374 VAL 374 374 ?   ?   ?   L . n 
C 2 375 PRO 375 375 ?   ?   ?   L . n 
C 2 376 ILE 376 376 ?   ?   ?   L . n 
C 2 377 ASP 377 377 ?   ?   ?   L . n 
C 2 378 GLU 378 378 ?   ?   ?   L . n 
C 2 379 GLN 379 379 ?   ?   ?   L . n 
C 2 380 PHE 380 380 ?   ?   ?   L . n 
C 2 381 ASP 381 381 ?   ?   ?   L . n 
C 2 382 LYS 382 382 ?   ?   ?   L . n 
C 2 383 GLU 383 383 ?   ?   ?   L . n 
C 2 384 LYS 384 384 ?   ?   ?   L . n 
C 2 385 ALA 385 385 ?   ?   ?   L . n 
C 2 386 ASN 386 386 ?   ?   ?   L . n 
C 2 387 LEU 387 387 ?   ?   ?   L . n 
C 2 388 GLU 388 388 ?   ?   ?   L . n 
C 2 389 ALA 389 389 ?   ?   ?   L . n 
C 2 390 PHE 390 390 ?   ?   ?   L . n 
C 2 391 THR 391 391 ?   ?   ?   L . n 
C 2 392 VAL 392 392 ?   ?   ?   L . n 
C 2 393 ASP 393 393 ?   ?   ?   L . n 
C 2 394 LYS 394 394 ?   ?   ?   L . n 
C 2 395 ASP 395 395 ?   ?   ?   L . n 
C 2 396 ILE 396 396 ?   ?   ?   L . n 
C 2 397 THR 397 397 ?   ?   ?   L . n 
C 2 398 LEU 398 398 ?   ?   ?   L . n 
C 2 399 THR 399 399 ?   ?   ?   L . n 
C 2 400 ASN 400 400 ?   ?   ?   L . n 
C 2 401 ASP 401 401 ?   ?   ?   L . n 
C 2 402 LYS 402 402 ?   ?   ?   L . n 
C 2 403 PRO 403 403 ?   ?   ?   L . n 
C 2 404 ALA 404 404 ?   ?   ?   L . n 
C 2 405 THR 405 405 ?   ?   ?   L . n 
C 2 406 ALA 406 406 ?   ?   ?   L . n 
C 2 407 ILE 407 407 ?   ?   ?   L . n 
C 2 408 GLY 408 408 ?   ?   ?   L . n 
C 2 409 VAL 409 409 ?   ?   ?   L . n 
C 2 410 ILE 410 410 ?   ?   ?   L . n 
C 2 411 GLY 411 411 ?   ?   ?   L . n 
C 2 412 ASN 412 412 ?   ?   ?   L . n 
C 2 413 PHE 413 413 ?   ?   ?   L . n 
C 2 414 THR 414 414 ?   ?   ?   L . n 
C 2 415 ASP 415 415 ?   ?   ?   L . n 
C 2 416 ALA 416 416 ?   ?   ?   L . n 
C 2 417 GLU 417 417 ?   ?   ?   L . n 
C 2 418 ARG 418 418 ?   ?   ?   L . n 
C 2 419 ARG 419 419 ?   ?   ?   L . n 
C 2 420 LYS 420 420 ?   ?   ?   L . n 
C 2 421 CYS 421 421 ?   ?   ?   L . n 
C 2 422 GLU 422 422 ?   ?   ?   L . n 
C 2 423 GLU 423 423 ?   ?   ?   L . n 
C 2 424 GLU 424 424 ?   ?   ?   L . n 
C 2 425 ILE 425 425 ?   ?   ?   L . n 
C 2 426 ALA 426 426 ?   ?   ?   L . n 
C 2 427 LYS 427 427 ?   ?   ?   L . n 
C 2 428 LEU 428 428 ?   ?   ?   L . n 
C 2 429 TYR 429 429 ?   ?   ?   L . n 
C 2 430 LYS 430 430 ?   ?   ?   L . n 
C 2 431 GLN 431 431 ?   ?   ?   L . n 
C 2 432 LEU 432 432 ?   ?   ?   L . n 
C 2 433 ASP 433 433 ?   ?   ?   L . n 
C 2 434 ASP 434 434 ?   ?   ?   L . n 
C 2 435 LYS 435 435 ?   ?   ?   L . n 
C 2 436 ASP 436 436 ?   ?   ?   L . n 
C 2 437 GLU 437 437 ?   ?   ?   L . n 
C 2 438 GLU 438 438 ?   ?   ?   L . n 
C 2 439 ILE 439 439 ?   ?   ?   L . n 
C 2 440 ASN 440 440 ?   ?   ?   L . n 
C 2 441 GLN 441 441 ?   ?   ?   L . n 
C 2 442 GLN 442 442 ?   ?   ?   L . n 
C 2 443 SER 443 443 ?   ?   ?   L . n 
C 2 444 GLN 444 444 ?   ?   ?   L . n 
C 2 445 LEU 445 445 ?   ?   ?   L . n 
C 2 446 VAL 446 446 ?   ?   ?   L . n 
C 2 447 GLU 447 447 ?   ?   ?   L . n 
C 2 448 LYS 448 448 ?   ?   ?   L . n 
C 2 449 LEU 449 449 ?   ?   ?   L . n 
C 2 450 LYS 450 450 ?   ?   ?   L . n 
C 2 451 THR 451 451 ?   ?   ?   L . n 
C 2 452 GLN 452 452 ?   ?   ?   L . n 
C 2 453 MET 453 453 ?   ?   ?   L . n 
C 2 454 LEU 454 454 ?   ?   ?   L . n 
C 2 455 ASP 455 455 ?   ?   ?   L . n 
C 2 456 GLN 456 456 ?   ?   ?   L . n 
C 2 457 GLU 457 457 ?   ?   ?   L . n 
C 2 458 GLU 458 458 ?   ?   ?   L . n 
C 2 459 LEU 459 459 ?   ?   ?   L . n 
C 2 460 LEU 460 460 ?   ?   ?   L . n 
C 2 461 ALA 461 461 ?   ?   ?   L . n 
C 2 462 SER 462 462 ?   ?   ?   L . n 
C 2 463 THR 463 463 ?   ?   ?   L . n 
C 2 464 ARG 464 464 ?   ?   ?   L . n 
C 2 465 ARG 465 465 ?   ?   ?   L . n 
C 2 466 ASP 466 466 ?   ?   ?   L . n 
C 2 467 GLN 467 467 ?   ?   ?   L . n 
C 2 468 ASP 468 468 ?   ?   ?   L . n 
C 2 469 ASN 469 469 ?   ?   ?   L . n 
C 2 470 MET 470 470 ?   ?   ?   L . n 
C 2 471 GLN 471 471 ?   ?   ?   L . n 
C 2 472 ALA 472 472 ?   ?   ?   L . n 
C 2 473 GLU 473 473 ?   ?   ?   L . n 
C 2 474 LEU 474 474 ?   ?   ?   L . n 
C 2 475 ASN 475 475 ?   ?   ?   L . n 
C 2 476 ARG 476 476 ?   ?   ?   L . n 
C 2 477 LEU 477 477 ?   ?   ?   L . n 
C 2 478 GLN 478 478 ?   ?   ?   L . n 
C 2 479 ALA 479 479 ?   ?   ?   L . n 
C 2 480 GLU 480 480 ?   ?   ?   L . n 
C 2 481 ASN 481 481 ?   ?   ?   L . n 
C 2 482 ASP 482 482 ?   ?   ?   L . n 
C 2 483 ALA 483 483 ?   ?   ?   L . n 
C 2 484 SER 484 484 ?   ?   ?   L . n 
C 2 485 LYS 485 485 ?   ?   ?   L . n 
C 2 486 GLU 486 486 ?   ?   ?   L . n 
C 2 487 GLU 487 487 ?   ?   ?   L . n 
C 2 488 VAL 488 488 ?   ?   ?   L . n 
C 2 489 LYS 489 489 ?   ?   ?   L . n 
C 2 490 GLU 490 490 ?   ?   ?   L . n 
C 2 491 VAL 491 491 ?   ?   ?   L . n 
C 2 492 LEU 492 492 ?   ?   ?   L . n 
C 2 493 GLN 493 493 ?   ?   ?   L . n 
C 2 494 ALA 494 494 ?   ?   ?   L . n 
C 2 495 LEU 495 495 ?   ?   ?   L . n 
C 2 496 GLU 496 496 ?   ?   ?   L . n 
C 2 497 GLU 497 497 ?   ?   ?   L . n 
C 2 498 LEU 498 498 ?   ?   ?   L . n 
C 2 499 ALA 499 499 ?   ?   ?   L . n 
C 2 500 VAL 500 500 ?   ?   ?   L . n 
C 2 501 ASN 501 501 ?   ?   ?   L . n 
C 2 502 TYR 502 502 ?   ?   ?   L . n 
C 2 503 ASP 503 503 ?   ?   ?   L . n 
C 2 504 GLN 504 504 ?   ?   ?   L . n 
C 2 505 LYS 505 505 ?   ?   ?   L . n 
C 2 506 SER 506 506 ?   ?   ?   L . n 
C 2 507 GLN 507 507 ?   ?   ?   L . n 
C 2 508 GLU 508 508 ?   ?   ?   L . n 
C 2 509 VAL 509 509 ?   ?   ?   L . n 
C 2 510 GLU 510 510 ?   ?   ?   L . n 
C 2 511 ASP 511 511 ?   ?   ?   L . n 
C 2 512 LYS 512 512 ?   ?   ?   L . n 
C 2 513 THR 513 513 ?   ?   ?   L . n 
C 2 514 LYS 514 514 ?   ?   ?   L . n 
C 2 515 GLU 515 515 ?   ?   ?   L . n 
C 2 516 TYR 516 516 ?   ?   ?   L . n 
C 2 517 GLU 517 517 ?   ?   ?   L . n 
C 2 518 LEU 518 518 ?   ?   ?   L . n 
C 2 519 LEU 519 519 ?   ?   ?   L . n 
C 2 520 SER 520 520 ?   ?   ?   L . n 
C 2 521 ASP 521 521 ?   ?   ?   L . n 
C 2 522 GLU 522 522 ?   ?   ?   L . n 
C 2 523 LEU 523 523 ?   ?   ?   L . n 
C 2 524 ASN 524 524 ?   ?   ?   L . n 
C 2 525 GLN 525 525 ?   ?   ?   L . n 
C 2 526 LYS 526 526 ?   ?   ?   L . n 
C 2 527 SER 527 527 ?   ?   ?   L . n 
C 2 528 ALA 528 528 ?   ?   ?   L . n 
C 2 529 THR 529 529 ?   ?   ?   L . n 
C 2 530 LEU 530 530 ?   ?   ?   L . n 
C 2 531 ALA 531 531 ?   ?   ?   L . n 
C 2 532 SER 532 532 ?   ?   ?   L . n 
C 2 533 ILE 533 533 ?   ?   ?   L . n 
C 2 534 ASP 534 534 ?   ?   ?   L . n 
C 2 535 ALA 535 535 ?   ?   ?   L . n 
C 2 536 GLU 536 536 ?   ?   ?   L . n 
C 2 537 LEU 537 537 ?   ?   ?   L . n 
C 2 538 GLN 538 538 ?   ?   ?   L . n 
C 2 539 LYS 539 539 ?   ?   ?   L . n 
C 2 540 LEU 540 540 ?   ?   ?   L . n 
C 2 541 LYS 541 541 ?   ?   ?   L . n 
C 2 542 GLU 542 542 ?   ?   ?   L . n 
C 2 543 MET 543 543 ?   ?   ?   L . n 
C 2 544 THR 544 544 ?   ?   ?   L . n 
C 2 545 ASN 545 545 ?   ?   ?   L . n 
C 2 546 HIS 546 546 ?   ?   ?   L . n 
C 2 547 GLN 547 547 ?   ?   ?   L . n 
C 2 548 LYS 548 548 ?   ?   ?   L . n 
C 2 549 LYS 549 549 ?   ?   ?   L . n 
C 2 550 ARG 550 550 ?   ?   ?   L . n 
C 2 551 ALA 551 551 ?   ?   ?   L . n 
C 2 552 ALA 552 552 ?   ?   ?   L . n 
C 2 553 GLU 553 553 ?   ?   ?   L . n 
C 2 554 MET 554 554 ?   ?   ?   L . n 
C 2 555 MET 555 555 ?   ?   ?   L . n 
C 2 556 ALA 556 556 ?   ?   ?   L . n 
C 2 557 SER 557 557 ?   ?   ?   L . n 
C 2 558 LEU 558 558 ?   ?   ?   L . n 
C 2 559 LEU 559 559 ?   ?   ?   L . n 
C 2 560 LYS 560 560 ?   ?   ?   L . n 
C 2 561 ASP 561 561 ?   ?   ?   L . n 
C 2 562 LEU 562 562 ?   ?   ?   L . n 
C 2 563 ALA 563 563 ?   ?   ?   L . n 
C 2 564 GLU 564 564 ?   ?   ?   L . n 
C 2 565 ILE 565 565 ?   ?   ?   L . n 
C 2 566 GLY 566 566 ?   ?   ?   L . n 
C 2 567 ILE 567 567 ?   ?   ?   L . n 
C 2 568 ALA 568 568 ?   ?   ?   L . n 
C 2 569 VAL 569 569 ?   ?   ?   L . n 
C 2 570 GLY 570 570 ?   ?   ?   L . n 
C 2 571 ASN 571 571 ?   ?   ?   L . n 
C 2 572 ASN 572 572 ?   ?   ?   L . n 
C 2 573 ASP 573 573 ?   ?   ?   L . n 
C 2 574 VAL 574 574 ?   ?   ?   L . n 
C 2 575 LYS 575 575 ?   ?   ?   L . n 
C 2 576 GLN 576 576 ?   ?   ?   L . n 
C 2 577 PRO 577 577 ?   ?   ?   L . n 
C 2 578 GLU 578 578 ?   ?   ?   L . n 
C 2 579 GLY 579 579 ?   ?   ?   L . n 
C 2 580 THR 580 580 ?   ?   ?   L . n 
C 2 581 GLY 581 581 ?   ?   ?   L . n 
C 2 582 MET 582 582 ?   ?   ?   L . n 
C 2 583 ILE 583 583 ?   ?   ?   L . n 
C 2 584 ASP 584 584 ?   ?   ?   L . n 
C 2 585 GLU 585 585 ?   ?   ?   L . n 
C 2 586 GLU 586 586 ?   ?   ?   L . n 
C 2 587 PHE 587 587 ?   ?   ?   L . n 
C 2 588 THR 588 588 ?   ?   ?   L . n 
C 2 589 VAL 589 589 ?   ?   ?   L . n 
C 2 590 ALA 590 590 ?   ?   ?   L . n 
C 2 591 ARG 591 591 ?   ?   ?   L . n 
C 2 592 LEU 592 592 ?   ?   ?   L . n 
C 2 593 TYR 593 593 ?   ?   ?   L . n 
C 2 594 ILE 594 594 ?   ?   ?   L . n 
C 2 595 SER 595 595 ?   ?   ?   L . n 
C 2 596 LYS 596 596 ?   ?   ?   L . n 
C 2 597 MET 597 597 ?   ?   ?   L . n 
C 2 598 LYS 598 598 ?   ?   ?   L . n 
C 2 599 SER 599 599 ?   ?   ?   L . n 
C 2 600 GLU 600 600 ?   ?   ?   L . n 
C 2 601 VAL 601 601 ?   ?   ?   L . n 
C 2 602 LYS 602 602 ?   ?   ?   L . n 
C 2 603 THR 603 603 ?   ?   ?   L . n 
C 2 604 MET 604 604 ?   ?   ?   L . n 
C 2 605 VAL 605 605 ?   ?   ?   L . n 
C 2 606 LYS 606 606 ?   ?   ?   L . n 
C 2 607 ARG 607 607 ?   ?   ?   L . n 
C 2 608 CYS 608 608 ?   ?   ?   L . n 
C 2 609 LYS 609 609 ?   ?   ?   L . n 
C 2 610 GLN 610 610 ?   ?   ?   L . n 
C 2 611 LEU 611 611 ?   ?   ?   L . n 
C 2 612 GLU 612 612 ?   ?   ?   L . n 
C 2 613 SER 613 613 ?   ?   ?   L . n 
C 2 614 THR 614 614 ?   ?   ?   L . n 
C 2 615 GLN 615 615 ?   ?   ?   L . n 
C 2 616 THR 616 616 ?   ?   ?   L . n 
C 2 617 GLU 617 617 ?   ?   ?   L . n 
C 2 618 SER 618 618 ?   ?   ?   L . n 
C 2 619 ASN 619 619 ?   ?   ?   L . n 
C 2 620 LYS 620 620 ?   ?   ?   L . n 
C 2 621 LYS 621 621 ?   ?   ?   L . n 
C 2 622 MET 622 622 ?   ?   ?   L . n 
C 2 623 GLU 623 623 ?   ?   ?   L . n 
C 2 624 GLU 624 624 ?   ?   ?   L . n 
C 2 625 ASN 625 625 ?   ?   ?   L . n 
C 2 626 GLU 626 626 ?   ?   ?   L . n 
C 2 627 LYS 627 627 ?   ?   ?   L . n 
C 2 628 GLU 628 628 ?   ?   ?   L . n 
C 2 629 LEU 629 629 ?   ?   ?   L . n 
C 2 630 ALA 630 630 ?   ?   ?   L . n 
C 2 631 ALA 631 631 ?   ?   ?   L . n 
C 2 632 CYS 632 632 ?   ?   ?   L . n 
C 2 633 GLN 633 633 ?   ?   ?   L . n 
C 2 634 LEU 634 634 ?   ?   ?   L . n 
C 2 635 ARG 635 635 ?   ?   ?   L . n 
C 2 636 ILE 636 636 ?   ?   ?   L . n 
C 2 637 SER 637 637 ?   ?   ?   L . n 
C 2 638 GLN 638 638 ?   ?   ?   L . n 
C 2 639 HIS 639 639 ?   ?   ?   L . n 
C 2 640 GLU 640 640 ?   ?   ?   L . n 
C 2 641 ALA 641 641 ?   ?   ?   L . n 
C 2 642 LYS 642 642 ?   ?   ?   L . n 
C 2 643 ILE 643 643 ?   ?   ?   L . n 
C 2 644 LYS 644 644 ?   ?   ?   L . n 
C 2 645 SER 645 645 ?   ?   ?   L . n 
C 2 646 LEU 646 646 ?   ?   ?   L . n 
C 2 647 THR 647 647 ?   ?   ?   L . n 
C 2 648 GLU 648 648 ?   ?   ?   L . n 
C 2 649 TYR 649 649 ?   ?   ?   L . n 
C 2 650 LEU 650 650 ?   ?   ?   L . n 
C 2 651 GLN 651 651 ?   ?   ?   L . n 
C 2 652 ASN 652 652 ?   ?   ?   L . n 
C 2 653 VAL 653 653 ?   ?   ?   L . n 
C 2 654 GLU 654 654 ?   ?   ?   L . n 
C 2 655 GLN 655 655 ?   ?   ?   L . n 
C 2 656 LYS 656 656 ?   ?   ?   L . n 
C 2 657 LYS 657 657 ?   ?   ?   L . n 
C 2 658 ARG 658 658 ?   ?   ?   L . n 
C 2 659 GLN 659 659 ?   ?   ?   L . n 
C 2 660 LEU 660 660 ?   ?   ?   L . n 
C 2 661 GLU 661 661 ?   ?   ?   L . n 
C 2 662 GLU 662 662 ?   ?   ?   L . n 
C 2 663 SER 663 663 ?   ?   ?   L . n 
C 2 664 VAL 664 664 ?   ?   ?   L . n 
C 2 665 ASP 665 665 ?   ?   ?   L . n 
C 2 666 ALA 666 666 ?   ?   ?   L . n 
C 2 667 LEU 667 667 ?   ?   ?   L . n 
C 2 668 SER 668 668 ?   ?   ?   L . n 
C 2 669 GLU 669 669 ?   ?   ?   L . n 
C 2 670 GLU 670 670 ?   ?   ?   L . n 
C 2 671 LEU 671 671 ?   ?   ?   L . n 
C 2 672 VAL 672 672 ?   ?   ?   L . n 
C 2 673 GLN 673 673 ?   ?   ?   L . n 
C 2 674 LEU 674 674 ?   ?   ?   L . n 
C 2 675 ARG 675 675 ?   ?   ?   L . n 
C 2 676 ALA 676 676 ?   ?   ?   L . n 
C 2 677 GLN 677 677 ?   ?   ?   L . n 
C 2 678 GLU 678 678 ?   ?   ?   L . n 
C 2 679 LYS 679 679 ?   ?   ?   L . n 
C 2 680 VAL 680 680 ?   ?   ?   L . n 
C 2 681 HIS 681 681 ?   ?   ?   L . n 
C 2 682 GLU 682 682 ?   ?   ?   L . n 
C 2 683 MET 683 683 ?   ?   ?   L . n 
C 2 684 GLU 684 684 ?   ?   ?   L . n 
C 2 685 LYS 685 685 ?   ?   ?   L . n 
C 2 686 GLU 686 686 ?   ?   ?   L . n 
C 2 687 HIS 687 687 ?   ?   ?   L . n 
C 2 688 LEU 688 688 ?   ?   ?   L . n 
C 2 689 ASN 689 689 ?   ?   ?   L . n 
C 2 690 LYS 690 690 ?   ?   ?   L . n 
C 2 691 VAL 691 691 ?   ?   ?   L . n 
C 2 692 GLN 692 692 ?   ?   ?   L . n 
C 2 693 THR 693 693 ?   ?   ?   L . n 
C 2 694 ALA 694 694 ?   ?   ?   L . n 
C 2 695 ASN 695 695 ?   ?   ?   L . n 
C 2 696 GLU 696 696 ?   ?   ?   L . n 
C 2 697 VAL 697 697 ?   ?   ?   L . n 
C 2 698 LYS 698 698 ?   ?   ?   L . n 
C 2 699 GLN 699 699 ?   ?   ?   L . n 
C 2 700 ALA 700 700 ?   ?   ?   L . n 
C 2 701 VAL 701 701 ?   ?   ?   L . n 
C 2 702 GLU 702 702 ?   ?   ?   L . n 
C 2 703 GLN 703 703 ?   ?   ?   L . n 
C 2 704 GLN 704 704 ?   ?   ?   L . n 
C 2 705 ILE 705 705 ?   ?   ?   L . n 
C 2 706 GLN 706 706 ?   ?   ?   L . n 
C 2 707 SER 707 707 ?   ?   ?   L . n 
C 2 708 HIS 708 708 ?   ?   ?   L . n 
C 2 709 ARG 709 709 ?   ?   ?   L . n 
C 2 710 GLU 710 710 ?   ?   ?   L . n 
C 2 711 THR 711 711 ?   ?   ?   L . n 
C 2 712 HIS 712 712 ?   ?   ?   L . n 
C 2 713 GLN 713 713 ?   ?   ?   L . n 
C 2 714 LYS 714 714 ?   ?   ?   L . n 
C 2 715 GLN 715 715 ?   ?   ?   L . n 
C 2 716 ILE 716 716 ?   ?   ?   L . n 
C 2 717 SER 717 717 ?   ?   ?   L . n 
C 2 718 SER 718 718 ?   ?   ?   L . n 
C 2 719 LEU 719 719 ?   ?   ?   L . n 
C 2 720 ARG 720 720 ?   ?   ?   L . n 
C 2 721 ASP 721 721 ?   ?   ?   L . n 
C 2 722 GLU 722 722 ?   ?   ?   L . n 
C 2 723 VAL 723 723 ?   ?   ?   L . n 
C 2 724 GLU 724 724 ?   ?   ?   L . n 
C 2 725 ALA 725 725 ?   ?   ?   L . n 
C 2 726 LYS 726 726 ?   ?   ?   L . n 
C 2 727 ALA 727 727 ?   ?   ?   L . n 
C 2 728 LYS 728 728 ?   ?   ?   L . n 
C 2 729 LEU 729 729 ?   ?   ?   L . n 
C 2 730 ILE 730 730 ?   ?   ?   L . n 
C 2 731 THR 731 731 ?   ?   ?   L . n 
C 2 732 ASP 732 732 ?   ?   ?   L . n 
C 2 733 LEU 733 733 ?   ?   ?   L . n 
C 2 734 GLN 734 734 ?   ?   ?   L . n 
C 2 735 ASP 735 735 ?   ?   ?   L . n 
C 2 736 GLN 736 736 ?   ?   ?   L . n 
C 2 737 ASN 737 737 ?   ?   ?   L . n 
C 2 738 GLN 738 738 ?   ?   ?   L . n 
C 2 739 LYS 739 739 ?   ?   ?   L . n 
C 2 740 MET 740 740 ?   ?   ?   L . n 
C 2 741 MET 741 741 ?   ?   ?   L . n 
C 2 742 LEU 742 742 ?   ?   ?   L . n 
C 2 743 GLU 743 743 ?   ?   ?   L . n 
C 2 744 GLN 744 744 ?   ?   ?   L . n 
C 2 745 GLU 745 745 ?   ?   ?   L . n 
C 2 746 ARG 746 746 ?   ?   ?   L . n 
C 2 747 LEU 747 747 ?   ?   ?   L . n 
C 2 748 ARG 748 748 ?   ?   ?   L . n 
C 2 749 VAL 749 749 ?   ?   ?   L . n 
C 2 750 GLU 750 750 ?   ?   ?   L . n 
C 2 751 HIS 751 751 ?   ?   ?   L . n 
C 2 752 GLU 752 752 ?   ?   ?   L . n 
C 2 753 LYS 753 753 ?   ?   ?   L . n 
C 2 754 LEU 754 754 ?   ?   ?   L . n 
C 2 755 LYS 755 755 ?   ?   ?   L . n 
C 2 756 ALA 756 756 ?   ?   ?   L . n 
C 2 757 THR 757 757 ?   ?   ?   L . n 
C 2 758 ASP 758 758 ?   ?   ?   L . n 
C 2 759 GLN 759 759 ?   ?   ?   L . n 
C 2 760 GLU 760 760 ?   ?   ?   L . n 
C 2 761 LYS 761 761 ?   ?   ?   L . n 
C 2 762 SER 762 762 ?   ?   ?   L . n 
C 2 763 ARG 763 763 ?   ?   ?   L . n 
C 2 764 LYS 764 764 ?   ?   ?   L . n 
C 2 765 LEU 765 765 ?   ?   ?   L . n 
C 2 766 HIS 766 766 ?   ?   ?   L . n 
C 2 767 GLU 767 767 ?   ?   ?   L . n 
C 2 768 LEU 768 768 ?   ?   ?   L . n 
C 2 769 THR 769 769 ?   ?   ?   L . n 
C 2 770 VAL 770 770 ?   ?   ?   L . n 
C 2 771 MET 771 771 ?   ?   ?   L . n 
C 2 772 GLN 772 772 ?   ?   ?   L . n 
C 2 773 ASP 773 773 ?   ?   ?   L . n 
C 2 774 ARG 774 774 ?   ?   ?   L . n 
C 2 775 ARG 775 775 ?   ?   ?   L . n 
C 2 776 GLU 776 776 ?   ?   ?   L . n 
C 2 777 GLN 777 777 ?   ?   ?   L . n 
C 2 778 ALA 778 778 ?   ?   ?   L . n 
C 2 779 ARG 779 779 ?   ?   ?   L . n 
C 2 780 GLN 780 780 ?   ?   ?   L . n 
C 2 781 ASP 781 781 ?   ?   ?   L . n 
C 2 782 LEU 782 782 ?   ?   ?   L . n 
C 2 783 LYS 783 783 ?   ?   ?   L . n 
C 2 784 GLY 784 784 ?   ?   ?   L . n 
C 2 785 LEU 785 785 ?   ?   ?   L . n 
C 2 786 GLU 786 786 ?   ?   ?   L . n 
C 2 787 GLU 787 787 ?   ?   ?   L . n 
C 2 788 THR 788 788 ?   ?   ?   L . n 
C 2 789 VAL 789 789 ?   ?   ?   L . n 
C 2 790 ALA 790 790 ?   ?   ?   L . n 
C 2 791 LYS 791 791 ?   ?   ?   L . n 
C 2 792 GLU 792 792 ?   ?   ?   L . n 
C 2 793 LEU 793 793 ?   ?   ?   L . n 
C 2 794 GLN 794 794 ?   ?   ?   L . n 
C 2 795 THR 795 795 ?   ?   ?   L . n 
C 2 796 LEU 796 796 ?   ?   ?   L . n 
C 2 797 HIS 797 797 ?   ?   ?   L . n 
C 2 798 ASN 798 798 ?   ?   ?   L . n 
C 2 799 LEU 799 799 ?   ?   ?   L . n 
C 2 800 ARG 800 800 ?   ?   ?   L . n 
C 2 801 LYS 801 801 ?   ?   ?   L . n 
C 2 802 LEU 802 802 ?   ?   ?   L . n 
C 2 803 PHE 803 803 ?   ?   ?   L . n 
C 2 804 VAL 804 804 ?   ?   ?   L . n 
C 2 805 GLN 805 805 ?   ?   ?   L . n 
C 2 806 ASP 806 806 ?   ?   ?   L . n 
C 2 807 LEU 807 807 ?   ?   ?   L . n 
C 2 808 ALA 808 808 ?   ?   ?   L . n 
C 2 809 THR 809 809 ?   ?   ?   L . n 
C 2 810 ARG 810 810 ?   ?   ?   L . n 
C 2 811 VAL 811 811 ?   ?   ?   L . n 
C 2 812 LYS 812 812 ?   ?   ?   L . n 
C 2 813 LYS 813 813 ?   ?   ?   L . n 
C 2 814 SER 814 814 ?   ?   ?   L . n 
C 2 815 ALA 815 815 ?   ?   ?   L . n 
C 2 816 GLU 816 816 ?   ?   ?   L . n 
C 2 817 ILE 817 817 ?   ?   ?   L . n 
C 2 818 ASP 818 818 ?   ?   ?   L . n 
C 2 819 SER 819 819 ?   ?   ?   L . n 
C 2 820 ASP 820 820 ?   ?   ?   L . n 
C 2 821 ASP 821 821 ?   ?   ?   L . n 
C 2 822 THR 822 822 ?   ?   ?   L . n 
C 2 823 GLY 823 823 ?   ?   ?   L . n 
C 2 824 GLY 824 824 ?   ?   ?   L . n 
C 2 825 SER 825 825 ?   ?   ?   L . n 
C 2 826 ALA 826 826 ?   ?   ?   L . n 
C 2 827 ALA 827 827 ?   ?   ?   L . n 
C 2 828 GLN 828 828 ?   ?   ?   L . n 
C 2 829 LYS 829 829 ?   ?   ?   L . n 
C 2 830 GLN 830 830 ?   ?   ?   L . n 
C 2 831 LYS 831 831 ?   ?   ?   L . n 
C 2 832 ILE 832 832 ?   ?   ?   L . n 
C 2 833 SER 833 833 ?   ?   ?   L . n 
C 2 834 PHE 834 834 ?   ?   ?   L . n 
C 2 835 LEU 835 835 ?   ?   ?   L . n 
C 2 836 GLU 836 836 ?   ?   ?   L . n 
C 2 837 ASN 837 837 ?   ?   ?   L . n 
C 2 838 ASN 838 838 ?   ?   ?   L . n 
C 2 839 LEU 839 839 ?   ?   ?   L . n 
C 2 840 GLU 840 840 ?   ?   ?   L . n 
C 2 841 GLN 841 841 ?   ?   ?   L . n 
C 2 842 LEU 842 842 ?   ?   ?   L . n 
C 2 843 THR 843 843 ?   ?   ?   L . n 
C 2 844 LYS 844 844 ?   ?   ?   L . n 
C 2 845 VAL 845 845 ?   ?   ?   L . n 
C 2 846 HIS 846 846 ?   ?   ?   L . n 
C 2 847 LYS 847 847 ?   ?   ?   L . n 
C 2 848 GLN 848 848 ?   ?   ?   L . n 
C 2 849 LEU 849 849 ?   ?   ?   L . n 
C 2 850 VAL 850 850 ?   ?   ?   L . n 
C 2 851 ARG 851 851 ?   ?   ?   L . n 
C 2 852 ASP 852 852 ?   ?   ?   L . n 
C 2 853 ASN 853 853 ?   ?   ?   L . n 
C 2 854 ALA 854 854 ?   ?   ?   L . n 
C 2 855 ASP 855 855 ?   ?   ?   L . n 
C 2 856 LEU 856 856 ?   ?   ?   L . n 
C 2 857 ARG 857 857 ?   ?   ?   L . n 
C 2 858 CYS 858 858 ?   ?   ?   L . n 
C 2 859 GLU 859 859 ?   ?   ?   L . n 
C 2 860 LEU 860 860 ?   ?   ?   L . n 
C 2 861 PRO 861 861 ?   ?   ?   L . n 
C 2 862 LYS 862 862 ?   ?   ?   L . n 
C 2 863 LEU 863 863 ?   ?   ?   L . n 
C 2 864 GLU 864 864 ?   ?   ?   L . n 
C 2 865 LYS 865 865 ?   ?   ?   L . n 
C 2 866 ARG 866 866 ?   ?   ?   L . n 
C 2 867 LEU 867 867 ?   ?   ?   L . n 
C 2 868 ARG 868 868 ?   ?   ?   L . n 
C 2 869 ALA 869 869 ?   ?   ?   L . n 
C 2 870 THR 870 870 ?   ?   ?   L . n 
C 2 871 ALA 871 871 ?   ?   ?   L . n 
C 2 872 GLU 872 872 ?   ?   ?   L . n 
C 2 873 ARG 873 873 ?   ?   ?   L . n 
C 2 874 VAL 874 874 ?   ?   ?   L . n 
C 2 875 LYS 875 875 ?   ?   ?   L . n 
C 2 876 ALA 876 876 ?   ?   ?   L . n 
C 2 877 LEU 877 877 ?   ?   ?   L . n 
C 2 878 GLU 878 878 ?   ?   ?   L . n 
C 2 879 SER 879 879 ?   ?   ?   L . n 
C 2 880 ALA 880 880 ?   ?   ?   L . n 
C 2 881 LEU 881 881 ?   ?   ?   L . n 
C 2 882 LYS 882 882 ?   ?   ?   L . n 
C 2 883 GLU 883 883 ?   ?   ?   L . n 
C 2 884 ALA 884 884 ?   ?   ?   L . n 
C 2 885 LYS 885 885 ?   ?   ?   L . n 
C 2 886 GLU 886 886 ?   ?   ?   L . n 
C 2 887 ASN 887 887 ?   ?   ?   L . n 
C 2 888 ALA 888 888 ?   ?   ?   L . n 
C 2 889 SER 889 889 ?   ?   ?   L . n 
C 2 890 ARG 890 890 ?   ?   ?   L . n 
C 2 891 ASP 891 891 ?   ?   ?   L . n 
C 2 892 ARG 892 892 ?   ?   ?   L . n 
C 2 893 LYS 893 893 ?   ?   ?   L . n 
C 2 894 ARG 894 894 ?   ?   ?   L . n 
C 2 895 TYR 895 895 ?   ?   ?   L . n 
C 2 896 GLN 896 896 ?   ?   ?   L . n 
C 2 897 GLN 897 897 ?   ?   ?   L . n 
C 2 898 GLU 898 898 ?   ?   ?   L . n 
C 2 899 VAL 899 899 ?   ?   ?   L . n 
C 2 900 ASP 900 900 ?   ?   ?   L . n 
C 2 901 ARG 901 901 ?   ?   ?   L . n 
C 2 902 ILE 902 902 ?   ?   ?   L . n 
C 2 903 LYS 903 903 ?   ?   ?   L . n 
C 2 904 GLU 904 904 ?   ?   ?   L . n 
C 2 905 ALA 905 905 ?   ?   ?   L . n 
C 2 906 VAL 906 906 ?   ?   ?   L . n 
C 2 907 ARG 907 907 ?   ?   ?   L . n 
C 2 908 SER 908 908 ?   ?   ?   L . n 
C 2 909 LYS 909 909 ?   ?   ?   L . n 
C 2 910 ASN 910 910 ?   ?   ?   L . n 
C 2 911 MET 911 911 ?   ?   ?   L . n 
C 2 912 ALA 912 912 ?   ?   ?   L . n 
C 2 913 ARG 913 913 ?   ?   ?   L . n 
C 2 914 ARG 914 914 ?   ?   ?   L . n 
C 2 915 GLY 915 915 ?   ?   ?   L . n 
C 2 916 HIS 916 916 ?   ?   ?   L . n 
C 2 917 SER 917 917 ?   ?   ?   L . n 
C 2 918 ALA 918 918 ?   ?   ?   L . n 
C 2 919 GLN 919 919 ?   ?   ?   L . n 
C 2 920 ILE 920 920 ?   ?   ?   L . n 
C 2 921 ALA 921 921 ?   ?   ?   L . n 
C 2 922 LYS 922 922 ?   ?   ?   L . n 
C 2 923 PRO 923 923 ?   ?   ?   L . n 
C 2 924 ILE 924 924 ?   ?   ?   L . n 
C 2 925 ARG 925 925 ?   ?   ?   L . n 
C 2 926 PRO 926 926 ?   ?   ?   L . n 
C 2 927 GLY 927 927 ?   ?   ?   L . n 
C 2 928 GLN 928 928 ?   ?   ?   L . n 
C 2 929 HIS 929 929 ?   ?   ?   L . n 
C 2 930 PRO 930 930 ?   ?   ?   L . n 
C 2 931 ALA 931 931 ?   ?   ?   L . n 
C 2 932 ALA 932 932 ?   ?   ?   L . n 
C 2 933 SER 933 933 ?   ?   ?   L . n 
C 2 934 PRO 934 934 ?   ?   ?   L . n 
C 2 935 THR 935 935 ?   ?   ?   L . n 
C 2 936 HIS 936 936 ?   ?   ?   L . n 
C 2 937 PRO 937 937 ?   ?   ?   L . n 
C 2 938 SER 938 938 ?   ?   ?   L . n 
C 2 939 ALA 939 939 ?   ?   ?   L . n 
C 2 940 ILE 940 940 ?   ?   ?   L . n 
C 2 941 ARG 941 941 ?   ?   ?   L . n 
C 2 942 GLY 942 942 ?   ?   ?   L . n 
C 2 943 GLY 943 943 ?   ?   ?   L . n 
C 2 944 GLY 944 944 ?   ?   ?   L . n 
C 2 945 ALA 945 945 ?   ?   ?   L . n 
C 2 946 PHE 946 946 ?   ?   ?   L . n 
C 2 947 VAL 947 947 ?   ?   ?   L . n 
C 2 948 GLN 948 948 ?   ?   ?   L . n 
C 2 949 ASN 949 949 ?   ?   ?   L . n 
C 2 950 SER 950 950 ?   ?   ?   L . n 
C 2 951 GLN 951 951 ?   ?   ?   L . n 
C 2 952 PRO 952 952 ?   ?   ?   L . n 
C 2 953 VAL 953 953 ?   ?   ?   L . n 
C 2 954 ALA 954 954 ?   ?   ?   L . n 
C 2 955 VAL 955 955 ?   ?   ?   L . n 
C 2 956 ARG 956 956 ?   ?   ?   L . n 
C 2 957 GLY 957 957 ?   ?   ?   L . n 
C 2 958 GLY 958 958 ?   ?   ?   L . n 
C 2 959 GLY 959 959 ?   ?   ?   L . n 
C 2 960 GLY 960 960 ?   ?   ?   L . n 
C 2 961 LYS 961 961 ?   ?   ?   L . n 
C 2 962 GLN 962 962 ?   ?   ?   L . n 
C 2 963 VAL 963 963 ?   ?   ?   L . n 
D 3 1   MET 1   1   1   MET MET A . n 
D 3 2   ARG 2   2   2   ARG ARG A . n 
D 3 3   GLU 3   3   3   GLU GLU A . n 
D 3 4   CYS 4   4   4   CYS CYS A . n 
D 3 5   ILE 5   5   5   ILE ILE A . n 
D 3 6   SER 6   6   6   SER SER A . n 
D 3 7   ILE 7   7   7   ILE ILE A . n 
D 3 8   HIS 8   8   8   HIS HIS A . n 
D 3 9   VAL 9   9   9   VAL VAL A . n 
D 3 10  GLY 10  10  10  GLY GLY A . n 
D 3 11  GLN 11  11  11  GLN GLN A . n 
D 3 12  ALA 12  12  12  ALA ALA A . n 
D 3 13  GLY 13  13  13  GLY GLY A . n 
D 3 14  VAL 14  14  14  VAL VAL A . n 
D 3 15  GLN 15  15  15  GLN GLN A . n 
D 3 16  ILE 16  16  16  ILE ILE A . n 
D 3 17  GLY 17  17  17  GLY GLY A . n 
D 3 18  ASN 18  18  18  ASN ASN A . n 
D 3 19  ALA 19  19  19  ALA ALA A . n 
D 3 20  CYS 20  20  20  CYS CYS A . n 
D 3 21  TRP 21  21  21  TRP TRP A . n 
D 3 22  GLU 22  22  22  GLU GLU A . n 
D 3 23  LEU 23  23  23  LEU LEU A . n 
D 3 24  TYR 24  24  24  TYR TYR A . n 
D 3 25  CYS 25  25  25  CYS CYS A . n 
D 3 26  LEU 26  26  26  LEU LEU A . n 
D 3 27  GLU 27  27  27  GLU GLU A . n 
D 3 28  HIS 28  28  28  HIS HIS A . n 
D 3 29  GLY 29  29  29  GLY GLY A . n 
D 3 30  ILE 30  30  30  ILE ILE A . n 
D 3 31  GLN 31  31  31  GLN GLN A . n 
D 3 32  PRO 32  32  32  PRO PRO A . n 
D 3 33  ASP 33  33  33  ASP ASP A . n 
D 3 34  GLY 34  34  34  GLY GLY A . n 
D 3 35  GLN 35  35  35  GLN GLN A . n 
D 3 36  MET 36  36  36  MET MET A . n 
D 3 37  PRO 37  37  37  PRO PRO A . n 
D 3 38  SER 38  38  ?   ?   ?   A . n 
D 3 39  ASP 39  39  ?   ?   ?   A . n 
D 3 40  LYS 40  40  ?   ?   ?   A . n 
D 3 41  THR 41  41  ?   ?   ?   A . n 
D 3 42  ILE 42  42  ?   ?   ?   A . n 
D 3 43  GLY 43  43  ?   ?   ?   A . n 
D 3 44  GLY 44  44  ?   ?   ?   A . n 
D 3 45  GLY 45  45  ?   ?   ?   A . n 
D 3 46  ASP 46  46  ?   ?   ?   A . n 
D 3 47  ASP 47  47  47  ASP ASP A . n 
D 3 48  SER 48  48  48  SER SER A . n 
D 3 49  PHE 49  49  49  PHE PHE A . n 
D 3 50  ASN 50  50  50  ASN ASN A . n 
D 3 51  THR 51  51  51  THR THR A . n 
D 3 52  PHE 52  52  52  PHE PHE A . n 
D 3 53  PHE 53  53  53  PHE PHE A . n 
D 3 54  SER 54  54  54  SER SER A . n 
D 3 55  GLU 55  55  55  GLU GLU A . n 
D 3 56  THR 56  56  56  THR THR A . n 
D 3 57  GLY 57  57  57  GLY GLY A . n 
D 3 58  ALA 58  58  58  ALA ALA A . n 
D 3 59  GLY 59  59  59  GLY GLY A . n 
D 3 60  LYS 60  60  60  LYS LYS A . n 
D 3 61  HIS 61  61  61  HIS HIS A . n 
D 3 62  VAL 62  62  62  VAL VAL A . n 
D 3 63  PRO 63  63  63  PRO PRO A . n 
D 3 64  ARG 64  64  64  ARG ARG A . n 
D 3 65  ALA 65  65  65  ALA ALA A . n 
D 3 66  VAL 66  66  66  VAL VAL A . n 
D 3 67  PHE 67  67  67  PHE PHE A . n 
D 3 68  VAL 68  68  68  VAL VAL A . n 
D 3 69  ASP 69  69  69  ASP ASP A . n 
D 3 70  LEU 70  70  70  LEU LEU A . n 
D 3 71  GLU 71  71  71  GLU GLU A . n 
D 3 72  PRO 72  72  72  PRO PRO A . n 
D 3 73  THR 73  73  73  THR THR A . n 
D 3 74  VAL 74  74  74  VAL VAL A . n 
D 3 75  ILE 75  75  75  ILE ILE A . n 
D 3 76  ASP 76  76  76  ASP ASP A . n 
D 3 77  GLU 77  77  77  GLU GLU A . n 
D 3 78  VAL 78  78  78  VAL VAL A . n 
D 3 79  ARG 79  79  79  ARG ARG A . n 
D 3 80  THR 80  80  80  THR THR A . n 
D 3 81  GLY 81  81  81  GLY GLY A . n 
D 3 82  THR 82  82  82  THR THR A . n 
D 3 83  TYR 83  83  83  TYR TYR A . n 
D 3 84  ARG 84  84  84  ARG ARG A . n 
D 3 85  GLN 85  85  85  GLN GLN A . n 
D 3 86  LEU 86  86  86  LEU LEU A . n 
D 3 87  PHE 87  87  87  PHE PHE A . n 
D 3 88  HIS 88  88  88  HIS HIS A . n 
D 3 89  PRO 89  89  89  PRO PRO A . n 
D 3 90  GLU 90  90  90  GLU GLU A . n 
D 3 91  GLN 91  91  91  GLN GLN A . n 
D 3 92  LEU 92  92  92  LEU LEU A . n 
D 3 93  ILE 93  93  93  ILE ILE A . n 
D 3 94  THR 94  94  94  THR THR A . n 
D 3 95  GLY 95  95  95  GLY GLY A . n 
D 3 96  LYS 96  96  96  LYS LYS A . n 
D 3 97  GLU 97  97  97  GLU GLU A . n 
D 3 98  ASP 98  98  98  ASP ASP A . n 
D 3 99  ALA 99  99  99  ALA ALA A . n 
D 3 100 ALA 100 100 100 ALA ALA A . n 
D 3 101 ASN 101 101 101 ASN ASN A . n 
D 3 102 ASN 102 102 102 ASN ASN A . n 
D 3 103 TYR 103 103 103 TYR TYR A . n 
D 3 104 ALA 104 104 104 ALA ALA A . n 
D 3 105 ARG 105 105 105 ARG ARG A . n 
D 3 106 GLY 106 106 106 GLY GLY A . n 
D 3 107 HIS 107 107 107 HIS HIS A . n 
D 3 108 TYR 108 108 108 TYR TYR A . n 
D 3 109 THR 109 109 109 THR THR A . n 
D 3 110 ILE 110 110 110 ILE ILE A . n 
D 3 111 GLY 111 111 111 GLY GLY A . n 
D 3 112 LYS 112 112 112 LYS LYS A . n 
D 3 113 GLU 113 113 113 GLU GLU A . n 
D 3 114 ILE 114 114 114 ILE ILE A . n 
D 3 115 ILE 115 115 115 ILE ILE A . n 
D 3 116 ASP 116 116 116 ASP ASP A . n 
D 3 117 LEU 117 117 117 LEU LEU A . n 
D 3 118 VAL 118 118 118 VAL VAL A . n 
D 3 119 LEU 119 119 119 LEU LEU A . n 
D 3 120 ASP 120 120 120 ASP ASP A . n 
D 3 121 ARG 121 121 121 ARG ARG A . n 
D 3 122 ILE 122 122 122 ILE ILE A . n 
D 3 123 ARG 123 123 123 ARG ARG A . n 
D 3 124 LYS 124 124 124 LYS LYS A . n 
D 3 125 LEU 125 125 125 LEU LEU A . n 
D 3 126 ALA 126 126 126 ALA ALA A . n 
D 3 127 ASP 127 127 127 ASP ASP A . n 
D 3 128 GLN 128 128 128 GLN GLN A . n 
D 3 129 CYS 129 129 129 CYS CYS A . n 
D 3 130 THR 130 130 130 THR THR A . n 
D 3 131 GLY 131 131 131 GLY GLY A . n 
D 3 132 LEU 132 132 132 LEU LEU A . n 
D 3 133 GLN 133 133 133 GLN GLN A . n 
D 3 134 GLY 134 134 134 GLY GLY A . n 
D 3 135 PHE 135 135 135 PHE PHE A . n 
D 3 136 LEU 136 136 136 LEU LEU A . n 
D 3 137 VAL 137 137 137 VAL VAL A . n 
D 3 138 PHE 138 138 138 PHE PHE A . n 
D 3 139 HIS 139 139 139 HIS HIS A . n 
D 3 140 SER 140 140 140 SER SER A . n 
D 3 141 PHE 141 141 141 PHE PHE A . n 
D 3 142 GLY 142 142 142 GLY GLY A . n 
D 3 143 GLY 143 143 143 GLY GLY A . n 
D 3 144 GLY 144 144 144 GLY GLY A . n 
D 3 145 THR 145 145 145 THR THR A . n 
D 3 146 GLY 146 146 146 GLY GLY A . n 
D 3 147 SER 147 147 147 SER SER A . n 
D 3 148 GLY 148 148 148 GLY GLY A . n 
D 3 149 PHE 149 149 149 PHE PHE A . n 
D 3 150 THR 150 150 150 THR THR A . n 
D 3 151 SER 151 151 151 SER SER A . n 
D 3 152 LEU 152 152 152 LEU LEU A . n 
D 3 153 LEU 153 153 153 LEU LEU A . n 
D 3 154 MET 154 154 154 MET MET A . n 
D 3 155 GLU 155 155 155 GLU GLU A . n 
D 3 156 ARG 156 156 156 ARG ARG A . n 
D 3 157 LEU 157 157 157 LEU LEU A . n 
D 3 158 SER 158 158 158 SER SER A . n 
D 3 159 VAL 159 159 159 VAL VAL A . n 
D 3 160 ASP 160 160 160 ASP ASP A . n 
D 3 161 TYR 161 161 161 TYR TYR A . n 
D 3 162 GLY 162 162 162 GLY GLY A . n 
D 3 163 LYS 163 163 163 LYS LYS A . n 
D 3 164 LYS 164 164 164 LYS LYS A . n 
D 3 165 SER 165 165 165 SER SER A . n 
D 3 166 LYS 166 166 166 LYS LYS A . n 
D 3 167 LEU 167 167 167 LEU LEU A . n 
D 3 168 GLU 168 168 168 GLU GLU A . n 
D 3 169 PHE 169 169 169 PHE PHE A . n 
D 3 170 SER 170 170 170 SER SER A . n 
D 3 171 ILE 171 171 171 ILE ILE A . n 
D 3 172 TYR 172 172 172 TYR TYR A . n 
D 3 173 PRO 173 173 173 PRO PRO A . n 
D 3 174 ALA 174 174 174 ALA ALA A . n 
D 3 175 PRO 175 175 175 PRO PRO A . n 
D 3 176 GLN 176 176 176 GLN GLN A . n 
D 3 177 VAL 177 177 177 VAL VAL A . n 
D 3 178 SER 178 178 178 SER SER A . n 
D 3 179 THR 179 179 179 THR THR A . n 
D 3 180 ALA 180 180 180 ALA ALA A . n 
D 3 181 VAL 181 181 181 VAL VAL A . n 
D 3 182 VAL 182 182 182 VAL VAL A . n 
D 3 183 GLU 183 183 183 GLU GLU A . n 
D 3 184 PRO 184 184 184 PRO PRO A . n 
D 3 185 TYR 185 185 185 TYR TYR A . n 
D 3 186 ASN 186 186 186 ASN ASN A . n 
D 3 187 SER 187 187 187 SER SER A . n 
D 3 188 ILE 188 188 188 ILE ILE A . n 
D 3 189 LEU 189 189 189 LEU LEU A . n 
D 3 190 THR 190 190 190 THR THR A . n 
D 3 191 THR 191 191 191 THR THR A . n 
D 3 192 HIS 192 192 192 HIS HIS A . n 
D 3 193 THR 193 193 193 THR THR A . n 
D 3 194 THR 194 194 194 THR THR A . n 
D 3 195 LEU 195 195 195 LEU LEU A . n 
D 3 196 GLU 196 196 196 GLU GLU A . n 
D 3 197 HIS 197 197 197 HIS HIS A . n 
D 3 198 SER 198 198 198 SER SER A . n 
D 3 199 ASP 199 199 199 ASP ASP A . n 
D 3 200 CYS 200 200 200 CYS CYS A . n 
D 3 201 ALA 201 201 201 ALA ALA A . n 
D 3 202 PHE 202 202 202 PHE PHE A . n 
D 3 203 MET 203 203 203 MET MET A . n 
D 3 204 VAL 204 204 204 VAL VAL A . n 
D 3 205 ASP 205 205 205 ASP ASP A . n 
D 3 206 ASN 206 206 206 ASN ASN A . n 
D 3 207 GLU 207 207 207 GLU GLU A . n 
D 3 208 ALA 208 208 208 ALA ALA A . n 
D 3 209 ILE 209 209 209 ILE ILE A . n 
D 3 210 TYR 210 210 210 TYR TYR A . n 
D 3 211 ASP 211 211 211 ASP ASP A . n 
D 3 212 ILE 212 212 212 ILE ILE A . n 
D 3 213 CYS 213 213 213 CYS CYS A . n 
D 3 214 ARG 214 214 214 ARG ARG A . n 
D 3 215 ARG 215 215 215 ARG ARG A . n 
D 3 216 ASN 216 216 216 ASN ASN A . n 
D 3 217 LEU 217 217 217 LEU LEU A . n 
D 3 218 ASP 218 218 218 ASP ASP A . n 
D 3 219 ILE 219 219 219 ILE ILE A . n 
D 3 220 GLU 220 220 220 GLU GLU A . n 
D 3 221 ARG 221 221 221 ARG ARG A . n 
D 3 222 PRO 222 222 222 PRO PRO A . n 
D 3 223 THR 223 223 223 THR THR A . n 
D 3 224 TYR 224 224 224 TYR TYR A . n 
D 3 225 THR 225 225 225 THR THR A . n 
D 3 226 ASN 226 226 226 ASN ASN A . n 
D 3 227 LEU 227 227 227 LEU LEU A . n 
D 3 228 ASN 228 228 228 ASN ASN A . n 
D 3 229 ARG 229 229 229 ARG ARG A . n 
D 3 230 LEU 230 230 230 LEU LEU A . n 
D 3 231 ILE 231 231 231 ILE ILE A . n 
D 3 232 SER 232 232 232 SER SER A . n 
D 3 233 GLN 233 233 233 GLN GLN A . n 
D 3 234 ILE 234 234 234 ILE ILE A . n 
D 3 235 VAL 235 235 235 VAL VAL A . n 
D 3 236 SER 236 236 236 SER SER A . n 
D 3 237 SER 237 237 237 SER SER A . n 
D 3 238 ILE 238 238 238 ILE ILE A . n 
D 3 239 THR 239 239 239 THR THR A . n 
D 3 240 ALA 240 240 240 ALA ALA A . n 
D 3 241 SER 241 241 241 SER SER A . n 
D 3 242 LEU 242 242 242 LEU LEU A . n 
D 3 243 ARG 243 243 243 ARG ARG A . n 
D 3 244 PHE 244 244 244 PHE PHE A . n 
D 3 245 ASP 245 245 245 ASP ASP A . n 
D 3 246 GLY 246 246 246 GLY GLY A . n 
D 3 247 ALA 247 247 247 ALA ALA A . n 
D 3 248 LEU 248 248 248 LEU LEU A . n 
D 3 249 ASN 249 249 249 ASN ASN A . n 
D 3 250 VAL 250 250 250 VAL VAL A . n 
D 3 251 ASP 251 251 251 ASP ASP A . n 
D 3 252 LEU 252 252 252 LEU LEU A . n 
D 3 253 THR 253 253 253 THR THR A . n 
D 3 254 GLU 254 254 254 GLU GLU A . n 
D 3 255 PHE 255 255 255 PHE PHE A . n 
D 3 256 GLN 256 256 256 GLN GLN A . n 
D 3 257 THR 257 257 257 THR THR A . n 
D 3 258 ASN 258 258 258 ASN ASN A . n 
D 3 259 LEU 259 259 259 LEU LEU A . n 
D 3 260 VAL 260 260 260 VAL VAL A . n 
D 3 261 PRO 261 261 261 PRO PRO A . n 
D 3 262 TYR 262 262 262 TYR TYR A . n 
D 3 263 PRO 263 263 263 PRO PRO A . n 
D 3 264 ARG 264 264 264 ARG ARG A . n 
D 3 265 ILE 265 265 265 ILE ILE A . n 
D 3 266 HIS 266 266 266 HIS HIS A . n 
D 3 267 PHE 267 267 267 PHE PHE A . n 
D 3 268 PRO 268 268 268 PRO PRO A . n 
D 3 269 LEU 269 269 269 LEU LEU A . n 
D 3 270 ALA 270 270 270 ALA ALA A . n 
D 3 271 THR 271 271 271 THR THR A . n 
D 3 272 TYR 272 272 272 TYR TYR A . n 
D 3 273 ALA 273 273 273 ALA ALA A . n 
D 3 274 PRO 274 274 274 PRO PRO A . n 
D 3 275 VAL 275 275 275 VAL VAL A . n 
D 3 276 ILE 276 276 276 ILE ILE A . n 
D 3 277 SER 277 277 277 SER SER A . n 
D 3 278 ALA 278 278 278 ALA ALA A . n 
D 3 279 GLU 279 279 279 GLU GLU A . n 
D 3 280 LYS 280 280 280 LYS LYS A . n 
D 3 281 ALA 281 281 281 ALA ALA A . n 
D 3 282 TYR 282 282 282 TYR TYR A . n 
D 3 283 HIS 283 283 283 HIS HIS A . n 
D 3 284 GLU 284 284 284 GLU GLU A . n 
D 3 285 GLN 285 285 285 GLN GLN A . n 
D 3 286 LEU 286 286 286 LEU LEU A . n 
D 3 287 SER 287 287 287 SER SER A . n 
D 3 288 VAL 288 288 288 VAL VAL A . n 
D 3 289 ALA 289 289 289 ALA ALA A . n 
D 3 290 GLU 290 290 290 GLU GLU A . n 
D 3 291 ILE 291 291 291 ILE ILE A . n 
D 3 292 THR 292 292 292 THR THR A . n 
D 3 293 ASN 293 293 293 ASN ASN A . n 
D 3 294 ALA 294 294 294 ALA ALA A . n 
D 3 295 CYS 295 295 295 CYS CYS A . n 
D 3 296 PHE 296 296 296 PHE PHE A . n 
D 3 297 GLU 297 297 297 GLU GLU A . n 
D 3 298 PRO 298 298 298 PRO PRO A . n 
D 3 299 ALA 299 299 299 ALA ALA A . n 
D 3 300 ASN 300 300 300 ASN ASN A . n 
D 3 301 GLN 301 301 301 GLN GLN A . n 
D 3 302 MET 302 302 302 MET MET A . n 
D 3 303 VAL 303 303 303 VAL VAL A . n 
D 3 304 LYS 304 304 304 LYS LYS A . n 
D 3 305 CYS 305 305 305 CYS CYS A . n 
D 3 306 ASP 306 306 306 ASP ASP A . n 
D 3 307 PRO 307 307 307 PRO PRO A . n 
D 3 308 ARG 308 308 308 ARG ARG A . n 
D 3 309 HIS 309 309 309 HIS HIS A . n 
D 3 310 GLY 310 310 310 GLY GLY A . n 
D 3 311 LYS 311 311 311 LYS LYS A . n 
D 3 312 TYR 312 312 312 TYR TYR A . n 
D 3 313 MET 313 313 313 MET MET A . n 
D 3 314 ALA 314 314 314 ALA ALA A . n 
D 3 315 CYS 315 315 315 CYS CYS A . n 
D 3 316 CYS 316 316 316 CYS CYS A . n 
D 3 317 LEU 317 317 317 LEU LEU A . n 
D 3 318 LEU 318 318 318 LEU LEU A . n 
D 3 319 TYR 319 319 319 TYR TYR A . n 
D 3 320 ARG 320 320 320 ARG ARG A . n 
D 3 321 GLY 321 321 321 GLY GLY A . n 
D 3 322 ASP 322 322 322 ASP ASP A . n 
D 3 323 VAL 323 323 323 VAL VAL A . n 
D 3 324 VAL 324 324 324 VAL VAL A . n 
D 3 325 PRO 325 325 325 PRO PRO A . n 
D 3 326 LYS 326 326 326 LYS LYS A . n 
D 3 327 ASP 327 327 327 ASP ASP A . n 
D 3 328 VAL 328 328 328 VAL VAL A . n 
D 3 329 ASN 329 329 329 ASN ASN A . n 
D 3 330 ALA 330 330 330 ALA ALA A . n 
D 3 331 ALA 331 331 331 ALA ALA A . n 
D 3 332 ILE 332 332 332 ILE ILE A . n 
D 3 333 ALA 333 333 333 ALA ALA A . n 
D 3 334 THR 334 334 334 THR THR A . n 
D 3 335 ILE 335 335 335 ILE ILE A . n 
D 3 336 LYS 336 336 336 LYS LYS A . n 
D 3 337 THR 337 337 337 THR THR A . n 
D 3 338 LYS 338 338 338 LYS LYS A . n 
D 3 339 ARG 339 339 339 ARG ARG A . n 
D 3 340 SER 340 340 340 SER SER A . n 
D 3 341 ILE 341 341 341 ILE ILE A . n 
D 3 342 GLN 342 342 342 GLN GLN A . n 
D 3 343 PHE 343 343 343 PHE PHE A . n 
D 3 344 VAL 344 344 344 VAL VAL A . n 
D 3 345 ASP 345 345 345 ASP ASP A . n 
D 3 346 TRP 346 346 346 TRP TRP A . n 
D 3 347 CYS 347 347 347 CYS CYS A . n 
D 3 348 PRO 348 348 348 PRO PRO A . n 
D 3 349 THR 349 349 349 THR THR A . n 
D 3 350 GLY 350 350 350 GLY GLY A . n 
D 3 351 PHE 351 351 351 PHE PHE A . n 
D 3 352 LYS 352 352 352 LYS LYS A . n 
D 3 353 VAL 353 353 353 VAL VAL A . n 
D 3 354 GLY 354 354 354 GLY GLY A . n 
D 3 355 ILE 355 355 355 ILE ILE A . n 
D 3 356 ASN 356 356 356 ASN ASN A . n 
D 3 357 TYR 357 357 357 TYR TYR A . n 
D 3 358 GLN 358 358 358 GLN GLN A . n 
D 3 359 PRO 359 359 359 PRO PRO A . n 
D 3 360 PRO 360 360 360 PRO PRO A . n 
D 3 361 THR 361 361 361 THR THR A . n 
D 3 362 VAL 362 362 362 VAL VAL A . n 
D 3 363 VAL 363 363 363 VAL VAL A . n 
D 3 364 PRO 364 364 364 PRO PRO A . n 
D 3 365 GLY 365 365 365 GLY GLY A . n 
D 3 366 GLY 366 366 366 GLY GLY A . n 
D 3 367 ASP 367 367 367 ASP ASP A . n 
D 3 368 LEU 368 368 368 LEU LEU A . n 
D 3 369 ALA 369 369 369 ALA ALA A . n 
D 3 370 LYS 370 370 370 LYS LYS A . n 
D 3 371 VAL 371 371 371 VAL VAL A . n 
D 3 372 GLN 372 372 372 GLN GLN A . n 
D 3 373 ARG 373 373 373 ARG ARG A . n 
D 3 374 ALA 374 374 374 ALA ALA A . n 
D 3 375 VAL 375 375 375 VAL VAL A . n 
D 3 376 CYS 376 376 376 CYS CYS A . n 
D 3 377 MET 377 377 377 MET MET A . n 
D 3 378 LEU 378 378 378 LEU LEU A . n 
D 3 379 SER 379 379 379 SER SER A . n 
D 3 380 ASN 380 380 380 ASN ASN A . n 
D 3 381 THR 381 381 381 THR THR A . n 
D 3 382 THR 382 382 382 THR THR A . n 
D 3 383 ALA 383 383 383 ALA ALA A . n 
D 3 384 ILE 384 384 384 ILE ILE A . n 
D 3 385 ALA 385 385 385 ALA ALA A . n 
D 3 386 GLU 386 386 386 GLU GLU A . n 
D 3 387 ALA 387 387 387 ALA ALA A . n 
D 3 388 TRP 388 388 388 TRP TRP A . n 
D 3 389 ALA 389 389 389 ALA ALA A . n 
D 3 390 ARG 390 390 390 ARG ARG A . n 
D 3 391 LEU 391 391 391 LEU LEU A . n 
D 3 392 ASP 392 392 392 ASP ASP A . n 
D 3 393 HIS 393 393 393 HIS HIS A . n 
D 3 394 LYS 394 394 394 LYS LYS A . n 
D 3 395 PHE 395 395 395 PHE PHE A . n 
D 3 396 ASP 396 396 396 ASP ASP A . n 
D 3 397 LEU 397 397 397 LEU LEU A . n 
D 3 398 MET 398 398 398 MET MET A . n 
D 3 399 TYR 399 399 399 TYR TYR A . n 
D 3 400 ALA 400 400 400 ALA ALA A . n 
D 3 401 LYS 401 401 401 LYS LYS A . n 
D 3 402 ARG 402 402 402 ARG ARG A . n 
D 3 403 ALA 403 403 403 ALA ALA A . n 
D 3 404 PHE 404 404 404 PHE PHE A . n 
D 3 405 VAL 405 405 405 VAL VAL A . n 
D 3 406 HIS 406 406 406 HIS HIS A . n 
D 3 407 TRP 407 407 407 TRP TRP A . n 
D 3 408 TYR 408 408 408 TYR TYR A . n 
D 3 409 VAL 409 409 409 VAL VAL A . n 
D 3 410 GLY 410 410 410 GLY GLY A . n 
D 3 411 GLU 411 411 411 GLU GLU A . n 
D 3 412 GLY 412 412 412 GLY GLY A . n 
D 3 413 MET 413 413 413 MET MET A . n 
D 3 414 GLU 414 414 414 GLU GLU A . n 
D 3 415 GLU 415 415 415 GLU GLU A . n 
D 3 416 GLY 416 416 416 GLY GLY A . n 
D 3 417 GLU 417 417 417 GLU GLU A . n 
D 3 418 PHE 418 418 418 PHE PHE A . n 
D 3 419 SER 419 419 419 SER SER A . n 
D 3 420 GLU 420 420 420 GLU GLU A . n 
D 3 421 ALA 421 421 421 ALA ALA A . n 
D 3 422 ARG 422 422 422 ARG ARG A . n 
D 3 423 GLU 423 423 423 GLU GLU A . n 
D 3 424 ASP 424 424 424 ASP ASP A . n 
D 3 425 MET 425 425 425 MET MET A . n 
D 3 426 ALA 426 426 426 ALA ALA A . n 
D 3 427 ALA 427 427 427 ALA ALA A . n 
D 3 428 LEU 428 428 428 LEU LEU A . n 
D 3 429 GLU 429 429 429 GLU GLU A . n 
D 3 430 LYS 430 430 430 LYS LYS A . n 
D 3 431 ASP 431 431 431 ASP ASP A . n 
D 3 432 TYR 432 432 432 TYR TYR A . n 
D 3 433 GLU 433 433 433 GLU GLU A . n 
D 3 434 GLU 434 434 434 GLU GLU A . n 
D 3 435 VAL 435 435 435 VAL VAL A . n 
D 3 436 GLY 436 436 436 GLY GLY A . n 
D 3 437 VAL 437 437 437 VAL VAL A . n 
D 3 438 ASP 438 438 ?   ?   ?   A . n 
D 3 439 SER 439 439 ?   ?   ?   A . n 
D 3 440 VAL 440 440 ?   ?   ?   A . n 
D 3 441 GLU 441 441 ?   ?   ?   A . n 
D 3 442 GLY 442 442 ?   ?   ?   A . n 
D 3 443 GLU 443 443 ?   ?   ?   A . n 
D 3 444 GLY 444 444 ?   ?   ?   A . n 
D 3 445 GLU 445 445 ?   ?   ?   A . n 
D 3 446 GLU 446 446 ?   ?   ?   A . n 
D 3 447 GLU 447 447 ?   ?   ?   A . n 
D 3 448 GLY 448 448 ?   ?   ?   A . n 
D 3 449 GLU 449 449 ?   ?   ?   A . n 
D 3 450 GLU 450 450 ?   ?   ?   A . n 
D 3 451 TYR 451 451 ?   ?   ?   A . n 
E 2 1   MET 1   1   ?   ?   ?   T . n 
E 2 2   ALA 2   2   ?   ?   ?   T . n 
E 2 3   ASP 3   3   ?   ?   ?   T . n 
E 2 4   LEU 4   4   ?   ?   ?   T . n 
E 2 5   ALA 5   5   ?   ?   ?   T . n 
E 2 6   GLU 6   6   ?   ?   ?   T . n 
E 2 7   CYS 7   7   ?   ?   ?   T . n 
E 2 8   ASN 8   8   ?   ?   ?   T . n 
E 2 9   ILE 9   9   ?   ?   ?   T . n 
E 2 10  LYS 10  10  ?   ?   ?   T . n 
E 2 11  VAL 11  11  ?   ?   ?   T . n 
E 2 12  MET 12  12  ?   ?   ?   T . n 
E 2 13  CYS 13  13  ?   ?   ?   T . n 
E 2 14  ARG 14  14  ?   ?   ?   T . n 
E 2 15  PHE 15  15  ?   ?   ?   T . n 
E 2 16  ARG 16  16  ?   ?   ?   T . n 
E 2 17  PRO 17  17  ?   ?   ?   T . n 
E 2 18  LEU 18  18  ?   ?   ?   T . n 
E 2 19  ASN 19  19  ?   ?   ?   T . n 
E 2 20  GLU 20  20  ?   ?   ?   T . n 
E 2 21  SER 21  21  ?   ?   ?   T . n 
E 2 22  GLU 22  22  ?   ?   ?   T . n 
E 2 23  VAL 23  23  ?   ?   ?   T . n 
E 2 24  ASN 24  24  ?   ?   ?   T . n 
E 2 25  ARG 25  25  ?   ?   ?   T . n 
E 2 26  GLY 26  26  ?   ?   ?   T . n 
E 2 27  ASP 27  27  ?   ?   ?   T . n 
E 2 28  LYS 28  28  ?   ?   ?   T . n 
E 2 29  TYR 29  29  ?   ?   ?   T . n 
E 2 30  ILE 30  30  ?   ?   ?   T . n 
E 2 31  ALA 31  31  ?   ?   ?   T . n 
E 2 32  LYS 32  32  ?   ?   ?   T . n 
E 2 33  PHE 33  33  ?   ?   ?   T . n 
E 2 34  GLN 34  34  ?   ?   ?   T . n 
E 2 35  GLY 35  35  ?   ?   ?   T . n 
E 2 36  GLU 36  36  ?   ?   ?   T . n 
E 2 37  ASP 37  37  ?   ?   ?   T . n 
E 2 38  THR 38  38  ?   ?   ?   T . n 
E 2 39  VAL 39  39  ?   ?   ?   T . n 
E 2 40  VAL 40  40  ?   ?   ?   T . n 
E 2 41  ILE 41  41  ?   ?   ?   T . n 
E 2 42  ALA 42  42  ?   ?   ?   T . n 
E 2 43  SER 43  43  ?   ?   ?   T . n 
E 2 44  LYS 44  44  ?   ?   ?   T . n 
E 2 45  PRO 45  45  ?   ?   ?   T . n 
E 2 46  TYR 46  46  ?   ?   ?   T . n 
E 2 47  ALA 47  47  ?   ?   ?   T . n 
E 2 48  PHE 48  48  ?   ?   ?   T . n 
E 2 49  ASP 49  49  ?   ?   ?   T . n 
E 2 50  ARG 50  50  ?   ?   ?   T . n 
E 2 51  VAL 51  51  ?   ?   ?   T . n 
E 2 52  PHE 52  52  ?   ?   ?   T . n 
E 2 53  GLN 53  53  ?   ?   ?   T . n 
E 2 54  SER 54  54  ?   ?   ?   T . n 
E 2 55  SER 55  55  ?   ?   ?   T . n 
E 2 56  THR 56  56  ?   ?   ?   T . n 
E 2 57  SER 57  57  ?   ?   ?   T . n 
E 2 58  GLN 58  58  ?   ?   ?   T . n 
E 2 59  GLU 59  59  ?   ?   ?   T . n 
E 2 60  GLN 60  60  ?   ?   ?   T . n 
E 2 61  VAL 61  61  ?   ?   ?   T . n 
E 2 62  TYR 62  62  ?   ?   ?   T . n 
E 2 63  ASN 63  63  ?   ?   ?   T . n 
E 2 64  ASP 64  64  ?   ?   ?   T . n 
E 2 65  CYS 65  65  ?   ?   ?   T . n 
E 2 66  ALA 66  66  ?   ?   ?   T . n 
E 2 67  LYS 67  67  ?   ?   ?   T . n 
E 2 68  LYS 68  68  ?   ?   ?   T . n 
E 2 69  ILE 69  69  ?   ?   ?   T . n 
E 2 70  VAL 70  70  ?   ?   ?   T . n 
E 2 71  LYS 71  71  ?   ?   ?   T . n 
E 2 72  ASP 72  72  ?   ?   ?   T . n 
E 2 73  VAL 73  73  ?   ?   ?   T . n 
E 2 74  LEU 74  74  ?   ?   ?   T . n 
E 2 75  GLU 75  75  ?   ?   ?   T . n 
E 2 76  GLY 76  76  ?   ?   ?   T . n 
E 2 77  TYR 77  77  ?   ?   ?   T . n 
E 2 78  ASN 78  78  ?   ?   ?   T . n 
E 2 79  GLY 79  79  ?   ?   ?   T . n 
E 2 80  THR 80  80  ?   ?   ?   T . n 
E 2 81  ILE 81  81  ?   ?   ?   T . n 
E 2 82  PHE 82  82  ?   ?   ?   T . n 
E 2 83  ALA 83  83  ?   ?   ?   T . n 
E 2 84  TYR 84  84  ?   ?   ?   T . n 
E 2 85  GLY 85  85  ?   ?   ?   T . n 
E 2 86  GLN 86  86  ?   ?   ?   T . n 
E 2 87  THR 87  87  ?   ?   ?   T . n 
E 2 88  SER 88  88  ?   ?   ?   T . n 
E 2 89  SER 89  89  ?   ?   ?   T . n 
E 2 90  GLY 90  90  ?   ?   ?   T . n 
E 2 91  LYS 91  91  ?   ?   ?   T . n 
E 2 92  THR 92  92  ?   ?   ?   T . n 
E 2 93  HIS 93  93  ?   ?   ?   T . n 
E 2 94  THR 94  94  ?   ?   ?   T . n 
E 2 95  MET 95  95  ?   ?   ?   T . n 
E 2 96  GLU 96  96  ?   ?   ?   T . n 
E 2 97  GLY 97  97  ?   ?   ?   T . n 
E 2 98  LYS 98  98  ?   ?   ?   T . n 
E 2 99  LEU 99  99  ?   ?   ?   T . n 
E 2 100 HIS 100 100 ?   ?   ?   T . n 
E 2 101 ASP 101 101 ?   ?   ?   T . n 
E 2 102 PRO 102 102 ?   ?   ?   T . n 
E 2 103 GLU 103 103 ?   ?   ?   T . n 
E 2 104 GLY 104 104 ?   ?   ?   T . n 
E 2 105 MET 105 105 ?   ?   ?   T . n 
E 2 106 GLY 106 106 ?   ?   ?   T . n 
E 2 107 ILE 107 107 ?   ?   ?   T . n 
E 2 108 ILE 108 108 ?   ?   ?   T . n 
E 2 109 PRO 109 109 ?   ?   ?   T . n 
E 2 110 ARG 110 110 ?   ?   ?   T . n 
E 2 111 ILE 111 111 ?   ?   ?   T . n 
E 2 112 VAL 112 112 ?   ?   ?   T . n 
E 2 113 GLN 113 113 ?   ?   ?   T . n 
E 2 114 ASP 114 114 ?   ?   ?   T . n 
E 2 115 ILE 115 115 ?   ?   ?   T . n 
E 2 116 PHE 116 116 ?   ?   ?   T . n 
E 2 117 ASN 117 117 ?   ?   ?   T . n 
E 2 118 TYR 118 118 ?   ?   ?   T . n 
E 2 119 ILE 119 119 ?   ?   ?   T . n 
E 2 120 TYR 120 120 ?   ?   ?   T . n 
E 2 121 SER 121 121 ?   ?   ?   T . n 
E 2 122 MET 122 122 ?   ?   ?   T . n 
E 2 123 ASP 123 123 ?   ?   ?   T . n 
E 2 124 GLU 124 124 ?   ?   ?   T . n 
E 2 125 ASN 125 125 ?   ?   ?   T . n 
E 2 126 LEU 126 126 ?   ?   ?   T . n 
E 2 127 GLU 127 127 ?   ?   ?   T . n 
E 2 128 PHE 128 128 ?   ?   ?   T . n 
E 2 129 HIS 129 129 ?   ?   ?   T . n 
E 2 130 ILE 130 130 ?   ?   ?   T . n 
E 2 131 LYS 131 131 ?   ?   ?   T . n 
E 2 132 VAL 132 132 ?   ?   ?   T . n 
E 2 133 SER 133 133 ?   ?   ?   T . n 
E 2 134 TYR 134 134 ?   ?   ?   T . n 
E 2 135 PHE 135 135 ?   ?   ?   T . n 
E 2 136 GLU 136 136 ?   ?   ?   T . n 
E 2 137 ILE 137 137 ?   ?   ?   T . n 
E 2 138 TYR 138 138 ?   ?   ?   T . n 
E 2 139 LEU 139 139 ?   ?   ?   T . n 
E 2 140 ASP 140 140 ?   ?   ?   T . n 
E 2 141 LYS 141 141 ?   ?   ?   T . n 
E 2 142 ILE 142 142 ?   ?   ?   T . n 
E 2 143 ARG 143 143 ?   ?   ?   T . n 
E 2 144 ASP 144 144 ?   ?   ?   T . n 
E 2 145 LEU 145 145 ?   ?   ?   T . n 
E 2 146 LEU 146 146 ?   ?   ?   T . n 
E 2 147 ASP 147 147 ?   ?   ?   T . n 
E 2 148 VAL 148 148 ?   ?   ?   T . n 
E 2 149 SER 149 149 ?   ?   ?   T . n 
E 2 150 LYS 150 150 ?   ?   ?   T . n 
E 2 151 THR 151 151 ?   ?   ?   T . n 
E 2 152 ASN 152 152 ?   ?   ?   T . n 
E 2 153 LEU 153 153 ?   ?   ?   T . n 
E 2 154 SER 154 154 ?   ?   ?   T . n 
E 2 155 VAL 155 155 ?   ?   ?   T . n 
E 2 156 HIS 156 156 ?   ?   ?   T . n 
E 2 157 GLU 157 157 ?   ?   ?   T . n 
E 2 158 ASP 158 158 ?   ?   ?   T . n 
E 2 159 LYS 159 159 ?   ?   ?   T . n 
E 2 160 ASN 160 160 ?   ?   ?   T . n 
E 2 161 ARG 161 161 ?   ?   ?   T . n 
E 2 162 VAL 162 162 ?   ?   ?   T . n 
E 2 163 PRO 163 163 ?   ?   ?   T . n 
E 2 164 TYR 164 164 ?   ?   ?   T . n 
E 2 165 VAL 165 165 ?   ?   ?   T . n 
E 2 166 LYS 166 166 ?   ?   ?   T . n 
E 2 167 GLY 167 167 ?   ?   ?   T . n 
E 2 168 CYS 168 168 ?   ?   ?   T . n 
E 2 169 THR 169 169 ?   ?   ?   T . n 
E 2 170 GLU 170 170 ?   ?   ?   T . n 
E 2 171 ARG 171 171 ?   ?   ?   T . n 
E 2 172 PHE 172 172 ?   ?   ?   T . n 
E 2 173 VAL 173 173 ?   ?   ?   T . n 
E 2 174 CYS 174 174 ?   ?   ?   T . n 
E 2 175 SER 175 175 ?   ?   ?   T . n 
E 2 176 PRO 176 176 ?   ?   ?   T . n 
E 2 177 ASP 177 177 ?   ?   ?   T . n 
E 2 178 GLU 178 178 ?   ?   ?   T . n 
E 2 179 VAL 179 179 ?   ?   ?   T . n 
E 2 180 MET 180 180 ?   ?   ?   T . n 
E 2 181 ASP 181 181 ?   ?   ?   T . n 
E 2 182 THR 182 182 ?   ?   ?   T . n 
E 2 183 ILE 183 183 ?   ?   ?   T . n 
E 2 184 ASP 184 184 ?   ?   ?   T . n 
E 2 185 GLU 185 185 ?   ?   ?   T . n 
E 2 186 GLY 186 186 ?   ?   ?   T . n 
E 2 187 LYS 187 187 ?   ?   ?   T . n 
E 2 188 SER 188 188 ?   ?   ?   T . n 
E 2 189 ASN 189 189 ?   ?   ?   T . n 
E 2 190 ARG 190 190 ?   ?   ?   T . n 
E 2 191 HIS 191 191 ?   ?   ?   T . n 
E 2 192 VAL 192 192 ?   ?   ?   T . n 
E 2 193 ALA 193 193 ?   ?   ?   T . n 
E 2 194 VAL 194 194 ?   ?   ?   T . n 
E 2 195 THR 195 195 ?   ?   ?   T . n 
E 2 196 ASN 196 196 ?   ?   ?   T . n 
E 2 197 MET 197 197 ?   ?   ?   T . n 
E 2 198 ASN 198 198 ?   ?   ?   T . n 
E 2 199 GLU 199 199 ?   ?   ?   T . n 
E 2 200 HIS 200 200 ?   ?   ?   T . n 
E 2 201 SER 201 201 ?   ?   ?   T . n 
E 2 202 SER 202 202 ?   ?   ?   T . n 
E 2 203 ARG 203 203 ?   ?   ?   T . n 
E 2 204 SER 204 204 ?   ?   ?   T . n 
E 2 205 HIS 205 205 ?   ?   ?   T . n 
E 2 206 SER 206 206 ?   ?   ?   T . n 
E 2 207 ILE 207 207 ?   ?   ?   T . n 
E 2 208 PHE 208 208 ?   ?   ?   T . n 
E 2 209 LEU 209 209 ?   ?   ?   T . n 
E 2 210 ILE 210 210 ?   ?   ?   T . n 
E 2 211 ASN 211 211 ?   ?   ?   T . n 
E 2 212 VAL 212 212 ?   ?   ?   T . n 
E 2 213 LYS 213 213 ?   ?   ?   T . n 
E 2 214 GLN 214 214 ?   ?   ?   T . n 
E 2 215 GLU 215 215 ?   ?   ?   T . n 
E 2 216 ASN 216 216 ?   ?   ?   T . n 
E 2 217 THR 217 217 ?   ?   ?   T . n 
E 2 218 GLN 218 218 ?   ?   ?   T . n 
E 2 219 THR 219 219 ?   ?   ?   T . n 
E 2 220 GLU 220 220 ?   ?   ?   T . n 
E 2 221 GLN 221 221 ?   ?   ?   T . n 
E 2 222 LYS 222 222 ?   ?   ?   T . n 
E 2 223 LEU 223 223 ?   ?   ?   T . n 
E 2 224 SER 224 224 ?   ?   ?   T . n 
E 2 225 GLY 225 225 ?   ?   ?   T . n 
E 2 226 LYS 226 226 ?   ?   ?   T . n 
E 2 227 LEU 227 227 ?   ?   ?   T . n 
E 2 228 TYR 228 228 ?   ?   ?   T . n 
E 2 229 LEU 229 229 ?   ?   ?   T . n 
E 2 230 VAL 230 230 ?   ?   ?   T . n 
E 2 231 ASP 231 231 ?   ?   ?   T . n 
E 2 232 LEU 232 232 ?   ?   ?   T . n 
E 2 233 ALA 233 233 ?   ?   ?   T . n 
E 2 234 GLY 234 234 ?   ?   ?   T . n 
E 2 235 SER 235 235 ?   ?   ?   T . n 
E 2 236 GLU 236 236 ?   ?   ?   T . n 
E 2 237 LYS 237 237 ?   ?   ?   T . n 
E 2 238 VAL 238 238 ?   ?   ?   T . n 
E 2 239 SER 239 239 ?   ?   ?   T . n 
E 2 240 LYS 240 240 ?   ?   ?   T . n 
E 2 241 THR 241 241 ?   ?   ?   T . n 
E 2 242 GLY 242 242 ?   ?   ?   T . n 
E 2 243 ALA 243 243 ?   ?   ?   T . n 
E 2 244 GLU 244 244 ?   ?   ?   T . n 
E 2 245 GLY 245 245 ?   ?   ?   T . n 
E 2 246 ALA 246 246 ?   ?   ?   T . n 
E 2 247 VAL 247 247 ?   ?   ?   T . n 
E 2 248 LEU 248 248 ?   ?   ?   T . n 
E 2 249 ASP 249 249 ?   ?   ?   T . n 
E 2 250 GLU 250 250 ?   ?   ?   T . n 
E 2 251 ALA 251 251 ?   ?   ?   T . n 
E 2 252 LYS 252 252 ?   ?   ?   T . n 
E 2 253 ASN 253 253 ?   ?   ?   T . n 
E 2 254 ILE 254 254 ?   ?   ?   T . n 
E 2 255 ASN 255 255 ?   ?   ?   T . n 
E 2 256 LYS 256 256 ?   ?   ?   T . n 
E 2 257 SER 257 257 ?   ?   ?   T . n 
E 2 258 LEU 258 258 ?   ?   ?   T . n 
E 2 259 SER 259 259 ?   ?   ?   T . n 
E 2 260 ALA 260 260 ?   ?   ?   T . n 
E 2 261 LEU 261 261 ?   ?   ?   T . n 
E 2 262 GLY 262 262 ?   ?   ?   T . n 
E 2 263 ASN 263 263 ?   ?   ?   T . n 
E 2 264 VAL 264 264 ?   ?   ?   T . n 
E 2 265 ILE 265 265 ?   ?   ?   T . n 
E 2 266 SER 266 266 ?   ?   ?   T . n 
E 2 267 ALA 267 267 ?   ?   ?   T . n 
E 2 268 LEU 268 268 ?   ?   ?   T . n 
E 2 269 ALA 269 269 ?   ?   ?   T . n 
E 2 270 GLU 270 270 ?   ?   ?   T . n 
E 2 271 GLY 271 271 ?   ?   ?   T . n 
E 2 272 SER 272 272 ?   ?   ?   T . n 
E 2 273 THR 273 273 ?   ?   ?   T . n 
E 2 274 TYR 274 274 ?   ?   ?   T . n 
E 2 275 VAL 275 275 ?   ?   ?   T . n 
E 2 276 PRO 276 276 ?   ?   ?   T . n 
E 2 277 TYR 277 277 ?   ?   ?   T . n 
E 2 278 ARG 278 278 ?   ?   ?   T . n 
E 2 279 ASP 279 279 ?   ?   ?   T . n 
E 2 280 SER 280 280 ?   ?   ?   T . n 
E 2 281 LYS 281 281 ?   ?   ?   T . n 
E 2 282 MET 282 282 ?   ?   ?   T . n 
E 2 283 THR 283 283 ?   ?   ?   T . n 
E 2 284 ARG 284 284 ?   ?   ?   T . n 
E 2 285 ILE 285 285 ?   ?   ?   T . n 
E 2 286 LEU 286 286 ?   ?   ?   T . n 
E 2 287 GLN 287 287 ?   ?   ?   T . n 
E 2 288 ASP 288 288 ?   ?   ?   T . n 
E 2 289 SER 289 289 ?   ?   ?   T . n 
E 2 290 LEU 290 290 ?   ?   ?   T . n 
E 2 291 GLY 291 291 ?   ?   ?   T . n 
E 2 292 GLY 292 292 ?   ?   ?   T . n 
E 2 293 ASN 293 293 ?   ?   ?   T . n 
E 2 294 CYS 294 294 ?   ?   ?   T . n 
E 2 295 ARG 295 295 ?   ?   ?   T . n 
E 2 296 THR 296 296 ?   ?   ?   T . n 
E 2 297 THR 297 297 ?   ?   ?   T . n 
E 2 298 ILE 298 298 ?   ?   ?   T . n 
E 2 299 VAL 299 299 ?   ?   ?   T . n 
E 2 300 ILE 300 300 ?   ?   ?   T . n 
E 2 301 CYS 301 301 ?   ?   ?   T . n 
E 2 302 CYS 302 302 ?   ?   ?   T . n 
E 2 303 SER 303 303 ?   ?   ?   T . n 
E 2 304 PRO 304 304 ?   ?   ?   T . n 
E 2 305 SER 305 305 ?   ?   ?   T . n 
E 2 306 SER 306 306 ?   ?   ?   T . n 
E 2 307 TYR 307 307 ?   ?   ?   T . n 
E 2 308 ASN 308 308 ?   ?   ?   T . n 
E 2 309 GLU 309 309 ?   ?   ?   T . n 
E 2 310 SER 310 310 ?   ?   ?   T . n 
E 2 311 GLU 311 311 ?   ?   ?   T . n 
E 2 312 THR 312 312 ?   ?   ?   T . n 
E 2 313 LYS 313 313 ?   ?   ?   T . n 
E 2 314 SER 314 314 ?   ?   ?   T . n 
E 2 315 THR 315 315 ?   ?   ?   T . n 
E 2 316 LEU 316 316 ?   ?   ?   T . n 
E 2 317 LEU 317 317 ?   ?   ?   T . n 
E 2 318 PHE 318 318 ?   ?   ?   T . n 
E 2 319 GLY 319 319 ?   ?   ?   T . n 
E 2 320 GLN 320 320 ?   ?   ?   T . n 
E 2 321 ARG 321 321 ?   ?   ?   T . n 
E 2 322 ALA 322 322 ?   ?   ?   T . n 
E 2 323 LYS 323 323 ?   ?   ?   T . n 
E 2 324 THR 324 324 ?   ?   ?   T . n 
E 2 325 ILE 325 325 ?   ?   ?   T . n 
E 2 326 LYS 326 326 ?   ?   ?   T . n 
E 2 327 ASN 327 327 ?   ?   ?   T . n 
E 2 328 THR 328 328 ?   ?   ?   T . n 
E 2 329 VAL 329 329 ?   ?   ?   T . n 
E 2 330 CYS 330 330 ?   ?   ?   T . n 
E 2 331 VAL 331 331 ?   ?   ?   T . n 
E 2 332 ASN 332 332 ?   ?   ?   T . n 
E 2 333 VAL 333 333 ?   ?   ?   T . n 
E 2 334 GLU 334 334 ?   ?   ?   T . n 
E 2 335 LEU 335 335 ?   ?   ?   T . n 
E 2 336 THR 336 336 ?   ?   ?   T . n 
E 2 337 ALA 337 337 ?   ?   ?   T . n 
E 2 338 GLU 338 338 ?   ?   ?   T . n 
E 2 339 GLN 339 339 ?   ?   ?   T . n 
E 2 340 TRP 340 340 ?   ?   ?   T . n 
E 2 341 LYS 341 341 ?   ?   ?   T . n 
E 2 342 LYS 342 342 ?   ?   ?   T . n 
E 2 343 LYS 343 343 ?   ?   ?   T . n 
E 2 344 TYR 344 344 ?   ?   ?   T . n 
E 2 345 GLU 345 345 ?   ?   ?   T . n 
E 2 346 LYS 346 346 ?   ?   ?   T . n 
E 2 347 GLU 347 347 ?   ?   ?   T . n 
E 2 348 LYS 348 348 ?   ?   ?   T . n 
E 2 349 GLU 349 349 ?   ?   ?   T . n 
E 2 350 LYS 350 350 ?   ?   ?   T . n 
E 2 351 ASN 351 351 ?   ?   ?   T . n 
E 2 352 LYS 352 352 ?   ?   ?   T . n 
E 2 353 ILE 353 353 ?   ?   ?   T . n 
E 2 354 LEU 354 354 ?   ?   ?   T . n 
E 2 355 ARG 355 355 ?   ?   ?   T . n 
E 2 356 ASN 356 356 ?   ?   ?   T . n 
E 2 357 THR 357 357 ?   ?   ?   T . n 
E 2 358 ILE 358 358 ?   ?   ?   T . n 
E 2 359 GLN 359 359 ?   ?   ?   T . n 
E 2 360 TRP 360 360 ?   ?   ?   T . n 
E 2 361 LEU 361 361 ?   ?   ?   T . n 
E 2 362 GLU 362 362 ?   ?   ?   T . n 
E 2 363 ASN 363 363 ?   ?   ?   T . n 
E 2 364 GLU 364 364 ?   ?   ?   T . n 
E 2 365 LEU 365 365 ?   ?   ?   T . n 
E 2 366 ASN 366 366 ?   ?   ?   T . n 
E 2 367 ARG 367 367 ?   ?   ?   T . n 
E 2 368 TRP 368 368 ?   ?   ?   T . n 
E 2 369 ARG 369 369 ?   ?   ?   T . n 
E 2 370 ASN 370 370 ?   ?   ?   T . n 
E 2 371 GLY 371 371 ?   ?   ?   T . n 
E 2 372 GLU 372 372 ?   ?   ?   T . n 
E 2 373 THR 373 373 ?   ?   ?   T . n 
E 2 374 VAL 374 374 ?   ?   ?   T . n 
E 2 375 PRO 375 375 ?   ?   ?   T . n 
E 2 376 ILE 376 376 ?   ?   ?   T . n 
E 2 377 ASP 377 377 ?   ?   ?   T . n 
E 2 378 GLU 378 378 ?   ?   ?   T . n 
E 2 379 GLN 379 379 ?   ?   ?   T . n 
E 2 380 PHE 380 380 ?   ?   ?   T . n 
E 2 381 ASP 381 381 ?   ?   ?   T . n 
E 2 382 LYS 382 382 ?   ?   ?   T . n 
E 2 383 GLU 383 383 ?   ?   ?   T . n 
E 2 384 LYS 384 384 ?   ?   ?   T . n 
E 2 385 ALA 385 385 ?   ?   ?   T . n 
E 2 386 ASN 386 386 ?   ?   ?   T . n 
E 2 387 LEU 387 387 ?   ?   ?   T . n 
E 2 388 GLU 388 388 ?   ?   ?   T . n 
E 2 389 ALA 389 389 ?   ?   ?   T . n 
E 2 390 PHE 390 390 ?   ?   ?   T . n 
E 2 391 THR 391 391 ?   ?   ?   T . n 
E 2 392 VAL 392 392 ?   ?   ?   T . n 
E 2 393 ASP 393 393 ?   ?   ?   T . n 
E 2 394 LYS 394 394 ?   ?   ?   T . n 
E 2 395 ASP 395 395 ?   ?   ?   T . n 
E 2 396 ILE 396 396 ?   ?   ?   T . n 
E 2 397 THR 397 397 ?   ?   ?   T . n 
E 2 398 LEU 398 398 ?   ?   ?   T . n 
E 2 399 THR 399 399 ?   ?   ?   T . n 
E 2 400 ASN 400 400 ?   ?   ?   T . n 
E 2 401 ASP 401 401 ?   ?   ?   T . n 
E 2 402 LYS 402 402 ?   ?   ?   T . n 
E 2 403 PRO 403 403 ?   ?   ?   T . n 
E 2 404 ALA 404 404 ?   ?   ?   T . n 
E 2 405 THR 405 405 ?   ?   ?   T . n 
E 2 406 ALA 406 406 ?   ?   ?   T . n 
E 2 407 ILE 407 407 ?   ?   ?   T . n 
E 2 408 GLY 408 408 ?   ?   ?   T . n 
E 2 409 VAL 409 409 ?   ?   ?   T . n 
E 2 410 ILE 410 410 ?   ?   ?   T . n 
E 2 411 GLY 411 411 ?   ?   ?   T . n 
E 2 412 ASN 412 412 ?   ?   ?   T . n 
E 2 413 PHE 413 413 ?   ?   ?   T . n 
E 2 414 THR 414 414 ?   ?   ?   T . n 
E 2 415 ASP 415 415 ?   ?   ?   T . n 
E 2 416 ALA 416 416 ?   ?   ?   T . n 
E 2 417 GLU 417 417 ?   ?   ?   T . n 
E 2 418 ARG 418 418 ?   ?   ?   T . n 
E 2 419 ARG 419 419 ?   ?   ?   T . n 
E 2 420 LYS 420 420 ?   ?   ?   T . n 
E 2 421 CYS 421 421 ?   ?   ?   T . n 
E 2 422 GLU 422 422 ?   ?   ?   T . n 
E 2 423 GLU 423 423 ?   ?   ?   T . n 
E 2 424 GLU 424 424 ?   ?   ?   T . n 
E 2 425 ILE 425 425 ?   ?   ?   T . n 
E 2 426 ALA 426 426 ?   ?   ?   T . n 
E 2 427 LYS 427 427 ?   ?   ?   T . n 
E 2 428 LEU 428 428 ?   ?   ?   T . n 
E 2 429 TYR 429 429 ?   ?   ?   T . n 
E 2 430 LYS 430 430 ?   ?   ?   T . n 
E 2 431 GLN 431 431 ?   ?   ?   T . n 
E 2 432 LEU 432 432 ?   ?   ?   T . n 
E 2 433 ASP 433 433 ?   ?   ?   T . n 
E 2 434 ASP 434 434 ?   ?   ?   T . n 
E 2 435 LYS 435 435 ?   ?   ?   T . n 
E 2 436 ASP 436 436 ?   ?   ?   T . n 
E 2 437 GLU 437 437 ?   ?   ?   T . n 
E 2 438 GLU 438 438 ?   ?   ?   T . n 
E 2 439 ILE 439 439 ?   ?   ?   T . n 
E 2 440 ASN 440 440 ?   ?   ?   T . n 
E 2 441 GLN 441 441 ?   ?   ?   T . n 
E 2 442 GLN 442 442 ?   ?   ?   T . n 
E 2 443 SER 443 443 ?   ?   ?   T . n 
E 2 444 GLN 444 444 ?   ?   ?   T . n 
E 2 445 LEU 445 445 ?   ?   ?   T . n 
E 2 446 VAL 446 446 ?   ?   ?   T . n 
E 2 447 GLU 447 447 ?   ?   ?   T . n 
E 2 448 LYS 448 448 ?   ?   ?   T . n 
E 2 449 LEU 449 449 ?   ?   ?   T . n 
E 2 450 LYS 450 450 ?   ?   ?   T . n 
E 2 451 THR 451 451 ?   ?   ?   T . n 
E 2 452 GLN 452 452 ?   ?   ?   T . n 
E 2 453 MET 453 453 ?   ?   ?   T . n 
E 2 454 LEU 454 454 ?   ?   ?   T . n 
E 2 455 ASP 455 455 ?   ?   ?   T . n 
E 2 456 GLN 456 456 ?   ?   ?   T . n 
E 2 457 GLU 457 457 ?   ?   ?   T . n 
E 2 458 GLU 458 458 ?   ?   ?   T . n 
E 2 459 LEU 459 459 ?   ?   ?   T . n 
E 2 460 LEU 460 460 ?   ?   ?   T . n 
E 2 461 ALA 461 461 ?   ?   ?   T . n 
E 2 462 SER 462 462 ?   ?   ?   T . n 
E 2 463 THR 463 463 ?   ?   ?   T . n 
E 2 464 ARG 464 464 ?   ?   ?   T . n 
E 2 465 ARG 465 465 ?   ?   ?   T . n 
E 2 466 ASP 466 466 ?   ?   ?   T . n 
E 2 467 GLN 467 467 ?   ?   ?   T . n 
E 2 468 ASP 468 468 ?   ?   ?   T . n 
E 2 469 ASN 469 469 ?   ?   ?   T . n 
E 2 470 MET 470 470 ?   ?   ?   T . n 
E 2 471 GLN 471 471 ?   ?   ?   T . n 
E 2 472 ALA 472 472 ?   ?   ?   T . n 
E 2 473 GLU 473 473 ?   ?   ?   T . n 
E 2 474 LEU 474 474 ?   ?   ?   T . n 
E 2 475 ASN 475 475 ?   ?   ?   T . n 
E 2 476 ARG 476 476 ?   ?   ?   T . n 
E 2 477 LEU 477 477 ?   ?   ?   T . n 
E 2 478 GLN 478 478 ?   ?   ?   T . n 
E 2 479 ALA 479 479 ?   ?   ?   T . n 
E 2 480 GLU 480 480 ?   ?   ?   T . n 
E 2 481 ASN 481 481 ?   ?   ?   T . n 
E 2 482 ASP 482 482 ?   ?   ?   T . n 
E 2 483 ALA 483 483 ?   ?   ?   T . n 
E 2 484 SER 484 484 ?   ?   ?   T . n 
E 2 485 LYS 485 485 ?   ?   ?   T . n 
E 2 486 GLU 486 486 ?   ?   ?   T . n 
E 2 487 GLU 487 487 ?   ?   ?   T . n 
E 2 488 VAL 488 488 ?   ?   ?   T . n 
E 2 489 LYS 489 489 ?   ?   ?   T . n 
E 2 490 GLU 490 490 ?   ?   ?   T . n 
E 2 491 VAL 491 491 ?   ?   ?   T . n 
E 2 492 LEU 492 492 ?   ?   ?   T . n 
E 2 493 GLN 493 493 ?   ?   ?   T . n 
E 2 494 ALA 494 494 ?   ?   ?   T . n 
E 2 495 LEU 495 495 ?   ?   ?   T . n 
E 2 496 GLU 496 496 ?   ?   ?   T . n 
E 2 497 GLU 497 497 ?   ?   ?   T . n 
E 2 498 LEU 498 498 ?   ?   ?   T . n 
E 2 499 ALA 499 499 ?   ?   ?   T . n 
E 2 500 VAL 500 500 ?   ?   ?   T . n 
E 2 501 ASN 501 501 ?   ?   ?   T . n 
E 2 502 TYR 502 502 ?   ?   ?   T . n 
E 2 503 ASP 503 503 ?   ?   ?   T . n 
E 2 504 GLN 504 504 ?   ?   ?   T . n 
E 2 505 LYS 505 505 ?   ?   ?   T . n 
E 2 506 SER 506 506 ?   ?   ?   T . n 
E 2 507 GLN 507 507 ?   ?   ?   T . n 
E 2 508 GLU 508 508 ?   ?   ?   T . n 
E 2 509 VAL 509 509 ?   ?   ?   T . n 
E 2 510 GLU 510 510 ?   ?   ?   T . n 
E 2 511 ASP 511 511 ?   ?   ?   T . n 
E 2 512 LYS 512 512 ?   ?   ?   T . n 
E 2 513 THR 513 513 ?   ?   ?   T . n 
E 2 514 LYS 514 514 ?   ?   ?   T . n 
E 2 515 GLU 515 515 ?   ?   ?   T . n 
E 2 516 TYR 516 516 ?   ?   ?   T . n 
E 2 517 GLU 517 517 ?   ?   ?   T . n 
E 2 518 LEU 518 518 ?   ?   ?   T . n 
E 2 519 LEU 519 519 ?   ?   ?   T . n 
E 2 520 SER 520 520 ?   ?   ?   T . n 
E 2 521 ASP 521 521 ?   ?   ?   T . n 
E 2 522 GLU 522 522 ?   ?   ?   T . n 
E 2 523 LEU 523 523 ?   ?   ?   T . n 
E 2 524 ASN 524 524 ?   ?   ?   T . n 
E 2 525 GLN 525 525 ?   ?   ?   T . n 
E 2 526 LYS 526 526 ?   ?   ?   T . n 
E 2 527 SER 527 527 ?   ?   ?   T . n 
E 2 528 ALA 528 528 ?   ?   ?   T . n 
E 2 529 THR 529 529 ?   ?   ?   T . n 
E 2 530 LEU 530 530 ?   ?   ?   T . n 
E 2 531 ALA 531 531 ?   ?   ?   T . n 
E 2 532 SER 532 532 ?   ?   ?   T . n 
E 2 533 ILE 533 533 ?   ?   ?   T . n 
E 2 534 ASP 534 534 ?   ?   ?   T . n 
E 2 535 ALA 535 535 ?   ?   ?   T . n 
E 2 536 GLU 536 536 ?   ?   ?   T . n 
E 2 537 LEU 537 537 ?   ?   ?   T . n 
E 2 538 GLN 538 538 ?   ?   ?   T . n 
E 2 539 LYS 539 539 ?   ?   ?   T . n 
E 2 540 LEU 540 540 ?   ?   ?   T . n 
E 2 541 LYS 541 541 ?   ?   ?   T . n 
E 2 542 GLU 542 542 ?   ?   ?   T . n 
E 2 543 MET 543 543 ?   ?   ?   T . n 
E 2 544 THR 544 544 ?   ?   ?   T . n 
E 2 545 ASN 545 545 ?   ?   ?   T . n 
E 2 546 HIS 546 546 ?   ?   ?   T . n 
E 2 547 GLN 547 547 ?   ?   ?   T . n 
E 2 548 LYS 548 548 ?   ?   ?   T . n 
E 2 549 LYS 549 549 ?   ?   ?   T . n 
E 2 550 ARG 550 550 ?   ?   ?   T . n 
E 2 551 ALA 551 551 ?   ?   ?   T . n 
E 2 552 ALA 552 552 ?   ?   ?   T . n 
E 2 553 GLU 553 553 ?   ?   ?   T . n 
E 2 554 MET 554 554 ?   ?   ?   T . n 
E 2 555 MET 555 555 ?   ?   ?   T . n 
E 2 556 ALA 556 556 ?   ?   ?   T . n 
E 2 557 SER 557 557 ?   ?   ?   T . n 
E 2 558 LEU 558 558 ?   ?   ?   T . n 
E 2 559 LEU 559 559 ?   ?   ?   T . n 
E 2 560 LYS 560 560 ?   ?   ?   T . n 
E 2 561 ASP 561 561 ?   ?   ?   T . n 
E 2 562 LEU 562 562 ?   ?   ?   T . n 
E 2 563 ALA 563 563 ?   ?   ?   T . n 
E 2 564 GLU 564 564 ?   ?   ?   T . n 
E 2 565 ILE 565 565 ?   ?   ?   T . n 
E 2 566 GLY 566 566 ?   ?   ?   T . n 
E 2 567 ILE 567 567 ?   ?   ?   T . n 
E 2 568 ALA 568 568 ?   ?   ?   T . n 
E 2 569 VAL 569 569 ?   ?   ?   T . n 
E 2 570 GLY 570 570 ?   ?   ?   T . n 
E 2 571 ASN 571 571 ?   ?   ?   T . n 
E 2 572 ASN 572 572 ?   ?   ?   T . n 
E 2 573 ASP 573 573 ?   ?   ?   T . n 
E 2 574 VAL 574 574 ?   ?   ?   T . n 
E 2 575 LYS 575 575 ?   ?   ?   T . n 
E 2 576 GLN 576 576 ?   ?   ?   T . n 
E 2 577 PRO 577 577 ?   ?   ?   T . n 
E 2 578 GLU 578 578 ?   ?   ?   T . n 
E 2 579 GLY 579 579 ?   ?   ?   T . n 
E 2 580 THR 580 580 ?   ?   ?   T . n 
E 2 581 GLY 581 581 ?   ?   ?   T . n 
E 2 582 MET 582 582 ?   ?   ?   T . n 
E 2 583 ILE 583 583 ?   ?   ?   T . n 
E 2 584 ASP 584 584 ?   ?   ?   T . n 
E 2 585 GLU 585 585 ?   ?   ?   T . n 
E 2 586 GLU 586 586 ?   ?   ?   T . n 
E 2 587 PHE 587 587 ?   ?   ?   T . n 
E 2 588 THR 588 588 ?   ?   ?   T . n 
E 2 589 VAL 589 589 ?   ?   ?   T . n 
E 2 590 ALA 590 590 ?   ?   ?   T . n 
E 2 591 ARG 591 591 ?   ?   ?   T . n 
E 2 592 LEU 592 592 ?   ?   ?   T . n 
E 2 593 TYR 593 593 ?   ?   ?   T . n 
E 2 594 ILE 594 594 ?   ?   ?   T . n 
E 2 595 SER 595 595 ?   ?   ?   T . n 
E 2 596 LYS 596 596 ?   ?   ?   T . n 
E 2 597 MET 597 597 ?   ?   ?   T . n 
E 2 598 LYS 598 598 ?   ?   ?   T . n 
E 2 599 SER 599 599 ?   ?   ?   T . n 
E 2 600 GLU 600 600 ?   ?   ?   T . n 
E 2 601 VAL 601 601 ?   ?   ?   T . n 
E 2 602 LYS 602 602 ?   ?   ?   T . n 
E 2 603 THR 603 603 ?   ?   ?   T . n 
E 2 604 MET 604 604 ?   ?   ?   T . n 
E 2 605 VAL 605 605 ?   ?   ?   T . n 
E 2 606 LYS 606 606 ?   ?   ?   T . n 
E 2 607 ARG 607 607 ?   ?   ?   T . n 
E 2 608 CYS 608 608 ?   ?   ?   T . n 
E 2 609 LYS 609 609 ?   ?   ?   T . n 
E 2 610 GLN 610 610 ?   ?   ?   T . n 
E 2 611 LEU 611 611 ?   ?   ?   T . n 
E 2 612 GLU 612 612 ?   ?   ?   T . n 
E 2 613 SER 613 613 ?   ?   ?   T . n 
E 2 614 THR 614 614 ?   ?   ?   T . n 
E 2 615 GLN 615 615 ?   ?   ?   T . n 
E 2 616 THR 616 616 ?   ?   ?   T . n 
E 2 617 GLU 617 617 ?   ?   ?   T . n 
E 2 618 SER 618 618 ?   ?   ?   T . n 
E 2 619 ASN 619 619 ?   ?   ?   T . n 
E 2 620 LYS 620 620 ?   ?   ?   T . n 
E 2 621 LYS 621 621 ?   ?   ?   T . n 
E 2 622 MET 622 622 ?   ?   ?   T . n 
E 2 623 GLU 623 623 ?   ?   ?   T . n 
E 2 624 GLU 624 624 ?   ?   ?   T . n 
E 2 625 ASN 625 625 ?   ?   ?   T . n 
E 2 626 GLU 626 626 ?   ?   ?   T . n 
E 2 627 LYS 627 627 ?   ?   ?   T . n 
E 2 628 GLU 628 628 ?   ?   ?   T . n 
E 2 629 LEU 629 629 ?   ?   ?   T . n 
E 2 630 ALA 630 630 ?   ?   ?   T . n 
E 2 631 ALA 631 631 ?   ?   ?   T . n 
E 2 632 CYS 632 632 ?   ?   ?   T . n 
E 2 633 GLN 633 633 ?   ?   ?   T . n 
E 2 634 LEU 634 634 ?   ?   ?   T . n 
E 2 635 ARG 635 635 ?   ?   ?   T . n 
E 2 636 ILE 636 636 ?   ?   ?   T . n 
E 2 637 SER 637 637 ?   ?   ?   T . n 
E 2 638 GLN 638 638 ?   ?   ?   T . n 
E 2 639 HIS 639 639 ?   ?   ?   T . n 
E 2 640 GLU 640 640 ?   ?   ?   T . n 
E 2 641 ALA 641 641 ?   ?   ?   T . n 
E 2 642 LYS 642 642 ?   ?   ?   T . n 
E 2 643 ILE 643 643 ?   ?   ?   T . n 
E 2 644 LYS 644 644 ?   ?   ?   T . n 
E 2 645 SER 645 645 ?   ?   ?   T . n 
E 2 646 LEU 646 646 ?   ?   ?   T . n 
E 2 647 THR 647 647 ?   ?   ?   T . n 
E 2 648 GLU 648 648 ?   ?   ?   T . n 
E 2 649 TYR 649 649 ?   ?   ?   T . n 
E 2 650 LEU 650 650 ?   ?   ?   T . n 
E 2 651 GLN 651 651 ?   ?   ?   T . n 
E 2 652 ASN 652 652 ?   ?   ?   T . n 
E 2 653 VAL 653 653 ?   ?   ?   T . n 
E 2 654 GLU 654 654 ?   ?   ?   T . n 
E 2 655 GLN 655 655 ?   ?   ?   T . n 
E 2 656 LYS 656 656 ?   ?   ?   T . n 
E 2 657 LYS 657 657 ?   ?   ?   T . n 
E 2 658 ARG 658 658 ?   ?   ?   T . n 
E 2 659 GLN 659 659 ?   ?   ?   T . n 
E 2 660 LEU 660 660 ?   ?   ?   T . n 
E 2 661 GLU 661 661 ?   ?   ?   T . n 
E 2 662 GLU 662 662 ?   ?   ?   T . n 
E 2 663 SER 663 663 ?   ?   ?   T . n 
E 2 664 VAL 664 664 ?   ?   ?   T . n 
E 2 665 ASP 665 665 ?   ?   ?   T . n 
E 2 666 ALA 666 666 ?   ?   ?   T . n 
E 2 667 LEU 667 667 ?   ?   ?   T . n 
E 2 668 SER 668 668 ?   ?   ?   T . n 
E 2 669 GLU 669 669 ?   ?   ?   T . n 
E 2 670 GLU 670 670 ?   ?   ?   T . n 
E 2 671 LEU 671 671 ?   ?   ?   T . n 
E 2 672 VAL 672 672 ?   ?   ?   T . n 
E 2 673 GLN 673 673 ?   ?   ?   T . n 
E 2 674 LEU 674 674 ?   ?   ?   T . n 
E 2 675 ARG 675 675 ?   ?   ?   T . n 
E 2 676 ALA 676 676 ?   ?   ?   T . n 
E 2 677 GLN 677 677 ?   ?   ?   T . n 
E 2 678 GLU 678 678 ?   ?   ?   T . n 
E 2 679 LYS 679 679 ?   ?   ?   T . n 
E 2 680 VAL 680 680 ?   ?   ?   T . n 
E 2 681 HIS 681 681 ?   ?   ?   T . n 
E 2 682 GLU 682 682 ?   ?   ?   T . n 
E 2 683 MET 683 683 ?   ?   ?   T . n 
E 2 684 GLU 684 684 ?   ?   ?   T . n 
E 2 685 LYS 685 685 ?   ?   ?   T . n 
E 2 686 GLU 686 686 ?   ?   ?   T . n 
E 2 687 HIS 687 687 ?   ?   ?   T . n 
E 2 688 LEU 688 688 ?   ?   ?   T . n 
E 2 689 ASN 689 689 ?   ?   ?   T . n 
E 2 690 LYS 690 690 ?   ?   ?   T . n 
E 2 691 VAL 691 691 ?   ?   ?   T . n 
E 2 692 GLN 692 692 ?   ?   ?   T . n 
E 2 693 THR 693 693 ?   ?   ?   T . n 
E 2 694 ALA 694 694 ?   ?   ?   T . n 
E 2 695 ASN 695 695 ?   ?   ?   T . n 
E 2 696 GLU 696 696 ?   ?   ?   T . n 
E 2 697 VAL 697 697 ?   ?   ?   T . n 
E 2 698 LYS 698 698 ?   ?   ?   T . n 
E 2 699 GLN 699 699 ?   ?   ?   T . n 
E 2 700 ALA 700 700 ?   ?   ?   T . n 
E 2 701 VAL 701 701 ?   ?   ?   T . n 
E 2 702 GLU 702 702 ?   ?   ?   T . n 
E 2 703 GLN 703 703 ?   ?   ?   T . n 
E 2 704 GLN 704 704 ?   ?   ?   T . n 
E 2 705 ILE 705 705 ?   ?   ?   T . n 
E 2 706 GLN 706 706 ?   ?   ?   T . n 
E 2 707 SER 707 707 ?   ?   ?   T . n 
E 2 708 HIS 708 708 ?   ?   ?   T . n 
E 2 709 ARG 709 709 ?   ?   ?   T . n 
E 2 710 GLU 710 710 ?   ?   ?   T . n 
E 2 711 THR 711 711 ?   ?   ?   T . n 
E 2 712 HIS 712 712 ?   ?   ?   T . n 
E 2 713 GLN 713 713 ?   ?   ?   T . n 
E 2 714 LYS 714 714 ?   ?   ?   T . n 
E 2 715 GLN 715 715 ?   ?   ?   T . n 
E 2 716 ILE 716 716 ?   ?   ?   T . n 
E 2 717 SER 717 717 ?   ?   ?   T . n 
E 2 718 SER 718 718 ?   ?   ?   T . n 
E 2 719 LEU 719 719 ?   ?   ?   T . n 
E 2 720 ARG 720 720 ?   ?   ?   T . n 
E 2 721 ASP 721 721 ?   ?   ?   T . n 
E 2 722 GLU 722 722 ?   ?   ?   T . n 
E 2 723 VAL 723 723 ?   ?   ?   T . n 
E 2 724 GLU 724 724 ?   ?   ?   T . n 
E 2 725 ALA 725 725 ?   ?   ?   T . n 
E 2 726 LYS 726 726 ?   ?   ?   T . n 
E 2 727 ALA 727 727 ?   ?   ?   T . n 
E 2 728 LYS 728 728 ?   ?   ?   T . n 
E 2 729 LEU 729 729 ?   ?   ?   T . n 
E 2 730 ILE 730 730 ?   ?   ?   T . n 
E 2 731 THR 731 731 ?   ?   ?   T . n 
E 2 732 ASP 732 732 ?   ?   ?   T . n 
E 2 733 LEU 733 733 ?   ?   ?   T . n 
E 2 734 GLN 734 734 ?   ?   ?   T . n 
E 2 735 ASP 735 735 ?   ?   ?   T . n 
E 2 736 GLN 736 736 ?   ?   ?   T . n 
E 2 737 ASN 737 737 ?   ?   ?   T . n 
E 2 738 GLN 738 738 ?   ?   ?   T . n 
E 2 739 LYS 739 739 ?   ?   ?   T . n 
E 2 740 MET 740 740 ?   ?   ?   T . n 
E 2 741 MET 741 741 ?   ?   ?   T . n 
E 2 742 LEU 742 742 ?   ?   ?   T . n 
E 2 743 GLU 743 743 ?   ?   ?   T . n 
E 2 744 GLN 744 744 ?   ?   ?   T . n 
E 2 745 GLU 745 745 ?   ?   ?   T . n 
E 2 746 ARG 746 746 ?   ?   ?   T . n 
E 2 747 LEU 747 747 ?   ?   ?   T . n 
E 2 748 ARG 748 748 ?   ?   ?   T . n 
E 2 749 VAL 749 749 ?   ?   ?   T . n 
E 2 750 GLU 750 750 ?   ?   ?   T . n 
E 2 751 HIS 751 751 ?   ?   ?   T . n 
E 2 752 GLU 752 752 ?   ?   ?   T . n 
E 2 753 LYS 753 753 ?   ?   ?   T . n 
E 2 754 LEU 754 754 ?   ?   ?   T . n 
E 2 755 LYS 755 755 ?   ?   ?   T . n 
E 2 756 ALA 756 756 ?   ?   ?   T . n 
E 2 757 THR 757 757 ?   ?   ?   T . n 
E 2 758 ASP 758 758 ?   ?   ?   T . n 
E 2 759 GLN 759 759 ?   ?   ?   T . n 
E 2 760 GLU 760 760 ?   ?   ?   T . n 
E 2 761 LYS 761 761 ?   ?   ?   T . n 
E 2 762 SER 762 762 ?   ?   ?   T . n 
E 2 763 ARG 763 763 ?   ?   ?   T . n 
E 2 764 LYS 764 764 ?   ?   ?   T . n 
E 2 765 LEU 765 765 ?   ?   ?   T . n 
E 2 766 HIS 766 766 ?   ?   ?   T . n 
E 2 767 GLU 767 767 ?   ?   ?   T . n 
E 2 768 LEU 768 768 ?   ?   ?   T . n 
E 2 769 THR 769 769 ?   ?   ?   T . n 
E 2 770 VAL 770 770 ?   ?   ?   T . n 
E 2 771 MET 771 771 ?   ?   ?   T . n 
E 2 772 GLN 772 772 ?   ?   ?   T . n 
E 2 773 ASP 773 773 ?   ?   ?   T . n 
E 2 774 ARG 774 774 ?   ?   ?   T . n 
E 2 775 ARG 775 775 ?   ?   ?   T . n 
E 2 776 GLU 776 776 ?   ?   ?   T . n 
E 2 777 GLN 777 777 ?   ?   ?   T . n 
E 2 778 ALA 778 778 ?   ?   ?   T . n 
E 2 779 ARG 779 779 ?   ?   ?   T . n 
E 2 780 GLN 780 780 ?   ?   ?   T . n 
E 2 781 ASP 781 781 ?   ?   ?   T . n 
E 2 782 LEU 782 782 ?   ?   ?   T . n 
E 2 783 LYS 783 783 ?   ?   ?   T . n 
E 2 784 GLY 784 784 ?   ?   ?   T . n 
E 2 785 LEU 785 785 ?   ?   ?   T . n 
E 2 786 GLU 786 786 ?   ?   ?   T . n 
E 2 787 GLU 787 787 ?   ?   ?   T . n 
E 2 788 THR 788 788 ?   ?   ?   T . n 
E 2 789 VAL 789 789 ?   ?   ?   T . n 
E 2 790 ALA 790 790 ?   ?   ?   T . n 
E 2 791 LYS 791 791 ?   ?   ?   T . n 
E 2 792 GLU 792 792 ?   ?   ?   T . n 
E 2 793 LEU 793 793 ?   ?   ?   T . n 
E 2 794 GLN 794 794 ?   ?   ?   T . n 
E 2 795 THR 795 795 ?   ?   ?   T . n 
E 2 796 LEU 796 796 ?   ?   ?   T . n 
E 2 797 HIS 797 797 ?   ?   ?   T . n 
E 2 798 ASN 798 798 ?   ?   ?   T . n 
E 2 799 LEU 799 799 ?   ?   ?   T . n 
E 2 800 ARG 800 800 ?   ?   ?   T . n 
E 2 801 LYS 801 801 ?   ?   ?   T . n 
E 2 802 LEU 802 802 ?   ?   ?   T . n 
E 2 803 PHE 803 803 ?   ?   ?   T . n 
E 2 804 VAL 804 804 ?   ?   ?   T . n 
E 2 805 GLN 805 805 ?   ?   ?   T . n 
E 2 806 ASP 806 806 ?   ?   ?   T . n 
E 2 807 LEU 807 807 ?   ?   ?   T . n 
E 2 808 ALA 808 808 ?   ?   ?   T . n 
E 2 809 THR 809 809 ?   ?   ?   T . n 
E 2 810 ARG 810 810 ?   ?   ?   T . n 
E 2 811 VAL 811 811 ?   ?   ?   T . n 
E 2 812 LYS 812 812 ?   ?   ?   T . n 
E 2 813 LYS 813 813 ?   ?   ?   T . n 
E 2 814 SER 814 814 ?   ?   ?   T . n 
E 2 815 ALA 815 815 ?   ?   ?   T . n 
E 2 816 GLU 816 816 ?   ?   ?   T . n 
E 2 817 ILE 817 817 ?   ?   ?   T . n 
E 2 818 ASP 818 818 ?   ?   ?   T . n 
E 2 819 SER 819 819 ?   ?   ?   T . n 
E 2 820 ASP 820 820 ?   ?   ?   T . n 
E 2 821 ASP 821 821 ?   ?   ?   T . n 
E 2 822 THR 822 822 ?   ?   ?   T . n 
E 2 823 GLY 823 823 ?   ?   ?   T . n 
E 2 824 GLY 824 824 ?   ?   ?   T . n 
E 2 825 SER 825 825 ?   ?   ?   T . n 
E 2 826 ALA 826 826 ?   ?   ?   T . n 
E 2 827 ALA 827 827 ?   ?   ?   T . n 
E 2 828 GLN 828 828 ?   ?   ?   T . n 
E 2 829 LYS 829 829 ?   ?   ?   T . n 
E 2 830 GLN 830 830 ?   ?   ?   T . n 
E 2 831 LYS 831 831 ?   ?   ?   T . n 
E 2 832 ILE 832 832 ?   ?   ?   T . n 
E 2 833 SER 833 833 ?   ?   ?   T . n 
E 2 834 PHE 834 834 ?   ?   ?   T . n 
E 2 835 LEU 835 835 ?   ?   ?   T . n 
E 2 836 GLU 836 836 ?   ?   ?   T . n 
E 2 837 ASN 837 837 ?   ?   ?   T . n 
E 2 838 ASN 838 838 ?   ?   ?   T . n 
E 2 839 LEU 839 839 ?   ?   ?   T . n 
E 2 840 GLU 840 840 ?   ?   ?   T . n 
E 2 841 GLN 841 841 ?   ?   ?   T . n 
E 2 842 LEU 842 842 ?   ?   ?   T . n 
E 2 843 THR 843 843 ?   ?   ?   T . n 
E 2 844 LYS 844 844 ?   ?   ?   T . n 
E 2 845 VAL 845 845 ?   ?   ?   T . n 
E 2 846 HIS 846 846 ?   ?   ?   T . n 
E 2 847 LYS 847 847 ?   ?   ?   T . n 
E 2 848 GLN 848 848 ?   ?   ?   T . n 
E 2 849 LEU 849 849 ?   ?   ?   T . n 
E 2 850 VAL 850 850 ?   ?   ?   T . n 
E 2 851 ARG 851 851 ?   ?   ?   T . n 
E 2 852 ASP 852 852 ?   ?   ?   T . n 
E 2 853 ASN 853 853 ?   ?   ?   T . n 
E 2 854 ALA 854 854 ?   ?   ?   T . n 
E 2 855 ASP 855 855 ?   ?   ?   T . n 
E 2 856 LEU 856 856 ?   ?   ?   T . n 
E 2 857 ARG 857 857 ?   ?   ?   T . n 
E 2 858 CYS 858 858 ?   ?   ?   T . n 
E 2 859 GLU 859 859 ?   ?   ?   T . n 
E 2 860 LEU 860 860 ?   ?   ?   T . n 
E 2 861 PRO 861 861 ?   ?   ?   T . n 
E 2 862 LYS 862 862 ?   ?   ?   T . n 
E 2 863 LEU 863 863 ?   ?   ?   T . n 
E 2 864 GLU 864 864 ?   ?   ?   T . n 
E 2 865 LYS 865 865 ?   ?   ?   T . n 
E 2 866 ARG 866 866 ?   ?   ?   T . n 
E 2 867 LEU 867 867 ?   ?   ?   T . n 
E 2 868 ARG 868 868 ?   ?   ?   T . n 
E 2 869 ALA 869 869 ?   ?   ?   T . n 
E 2 870 THR 870 870 ?   ?   ?   T . n 
E 2 871 ALA 871 871 ?   ?   ?   T . n 
E 2 872 GLU 872 872 ?   ?   ?   T . n 
E 2 873 ARG 873 873 ?   ?   ?   T . n 
E 2 874 VAL 874 874 ?   ?   ?   T . n 
E 2 875 LYS 875 875 ?   ?   ?   T . n 
E 2 876 ALA 876 876 ?   ?   ?   T . n 
E 2 877 LEU 877 877 ?   ?   ?   T . n 
E 2 878 GLU 878 878 ?   ?   ?   T . n 
E 2 879 SER 879 879 ?   ?   ?   T . n 
E 2 880 ALA 880 880 ?   ?   ?   T . n 
E 2 881 LEU 881 881 ?   ?   ?   T . n 
E 2 882 LYS 882 882 ?   ?   ?   T . n 
E 2 883 GLU 883 883 ?   ?   ?   T . n 
E 2 884 ALA 884 884 ?   ?   ?   T . n 
E 2 885 LYS 885 885 ?   ?   ?   T . n 
E 2 886 GLU 886 886 ?   ?   ?   T . n 
E 2 887 ASN 887 887 ?   ?   ?   T . n 
E 2 888 ALA 888 888 ?   ?   ?   T . n 
E 2 889 SER 889 889 ?   ?   ?   T . n 
E 2 890 ARG 890 890 ?   ?   ?   T . n 
E 2 891 ASP 891 891 ?   ?   ?   T . n 
E 2 892 ARG 892 892 ?   ?   ?   T . n 
E 2 893 LYS 893 893 ?   ?   ?   T . n 
E 2 894 ARG 894 894 ?   ?   ?   T . n 
E 2 895 TYR 895 895 ?   ?   ?   T . n 
E 2 896 GLN 896 896 ?   ?   ?   T . n 
E 2 897 GLN 897 897 ?   ?   ?   T . n 
E 2 898 GLU 898 898 ?   ?   ?   T . n 
E 2 899 VAL 899 899 ?   ?   ?   T . n 
E 2 900 ASP 900 900 ?   ?   ?   T . n 
E 2 901 ARG 901 901 ?   ?   ?   T . n 
E 2 902 ILE 902 902 ?   ?   ?   T . n 
E 2 903 LYS 903 903 ?   ?   ?   T . n 
E 2 904 GLU 904 904 ?   ?   ?   T . n 
E 2 905 ALA 905 905 ?   ?   ?   T . n 
E 2 906 VAL 906 906 ?   ?   ?   T . n 
E 2 907 ARG 907 907 ?   ?   ?   T . n 
E 2 908 SER 908 908 ?   ?   ?   T . n 
E 2 909 LYS 909 909 ?   ?   ?   T . n 
E 2 910 ASN 910 910 ?   ?   ?   T . n 
E 2 911 MET 911 911 ?   ?   ?   T . n 
E 2 912 ALA 912 912 ?   ?   ?   T . n 
E 2 913 ARG 913 913 ?   ?   ?   T . n 
E 2 914 ARG 914 914 ?   ?   ?   T . n 
E 2 915 GLY 915 915 ?   ?   ?   T . n 
E 2 916 HIS 916 916 ?   ?   ?   T . n 
E 2 917 SER 917 917 ?   ?   ?   T . n 
E 2 918 ALA 918 918 918 ALA ALA T . n 
E 2 919 GLN 919 919 919 GLN GLN T . n 
E 2 920 ILE 920 920 920 ILE ILE T . n 
E 2 921 ALA 921 921 921 ALA ALA T . n 
E 2 922 LYS 922 922 922 LYS LYS T . n 
E 2 923 PRO 923 923 923 PRO PRO T . n 
E 2 924 ILE 924 924 924 ILE ILE T . n 
E 2 925 ARG 925 925 925 ARG ARG T . n 
E 2 926 PRO 926 926 926 PRO PRO T . n 
E 2 927 GLY 927 927 ?   ?   ?   T . n 
E 2 928 GLN 928 928 ?   ?   ?   T . n 
E 2 929 HIS 929 929 ?   ?   ?   T . n 
E 2 930 PRO 930 930 ?   ?   ?   T . n 
E 2 931 ALA 931 931 ?   ?   ?   T . n 
E 2 932 ALA 932 932 ?   ?   ?   T . n 
E 2 933 SER 933 933 ?   ?   ?   T . n 
E 2 934 PRO 934 934 ?   ?   ?   T . n 
E 2 935 THR 935 935 ?   ?   ?   T . n 
E 2 936 HIS 936 936 ?   ?   ?   T . n 
E 2 937 PRO 937 937 ?   ?   ?   T . n 
E 2 938 SER 938 938 ?   ?   ?   T . n 
E 2 939 ALA 939 939 ?   ?   ?   T . n 
E 2 940 ILE 940 940 ?   ?   ?   T . n 
E 2 941 ARG 941 941 ?   ?   ?   T . n 
E 2 942 GLY 942 942 ?   ?   ?   T . n 
E 2 943 GLY 943 943 ?   ?   ?   T . n 
E 2 944 GLY 944 944 ?   ?   ?   T . n 
E 2 945 ALA 945 945 ?   ?   ?   T . n 
E 2 946 PHE 946 946 ?   ?   ?   T . n 
E 2 947 VAL 947 947 ?   ?   ?   T . n 
E 2 948 GLN 948 948 ?   ?   ?   T . n 
E 2 949 ASN 949 949 ?   ?   ?   T . n 
E 2 950 SER 950 950 ?   ?   ?   T . n 
E 2 951 GLN 951 951 ?   ?   ?   T . n 
E 2 952 PRO 952 952 ?   ?   ?   T . n 
E 2 953 VAL 953 953 ?   ?   ?   T . n 
E 2 954 ALA 954 954 ?   ?   ?   T . n 
E 2 955 VAL 955 955 ?   ?   ?   T . n 
E 2 956 ARG 956 956 ?   ?   ?   T . n 
E 2 957 GLY 957 957 ?   ?   ?   T . n 
E 2 958 GLY 958 958 ?   ?   ?   T . n 
E 2 959 GLY 959 959 ?   ?   ?   T . n 
E 2 960 GLY 960 960 ?   ?   ?   T . n 
E 2 961 LYS 961 961 ?   ?   ?   T . n 
E 2 962 GLN 962 962 ?   ?   ?   T . n 
E 2 963 VAL 963 963 ?   ?   ?   T . n 
F 2 1   MET 1   1   ?   ?   ?   t . n 
F 2 2   ALA 2   2   ?   ?   ?   t . n 
F 2 3   ASP 3   3   ?   ?   ?   t . n 
F 2 4   LEU 4   4   ?   ?   ?   t . n 
F 2 5   ALA 5   5   ?   ?   ?   t . n 
F 2 6   GLU 6   6   ?   ?   ?   t . n 
F 2 7   CYS 7   7   ?   ?   ?   t . n 
F 2 8   ASN 8   8   ?   ?   ?   t . n 
F 2 9   ILE 9   9   ?   ?   ?   t . n 
F 2 10  LYS 10  10  ?   ?   ?   t . n 
F 2 11  VAL 11  11  ?   ?   ?   t . n 
F 2 12  MET 12  12  ?   ?   ?   t . n 
F 2 13  CYS 13  13  ?   ?   ?   t . n 
F 2 14  ARG 14  14  ?   ?   ?   t . n 
F 2 15  PHE 15  15  ?   ?   ?   t . n 
F 2 16  ARG 16  16  ?   ?   ?   t . n 
F 2 17  PRO 17  17  ?   ?   ?   t . n 
F 2 18  LEU 18  18  ?   ?   ?   t . n 
F 2 19  ASN 19  19  ?   ?   ?   t . n 
F 2 20  GLU 20  20  ?   ?   ?   t . n 
F 2 21  SER 21  21  ?   ?   ?   t . n 
F 2 22  GLU 22  22  ?   ?   ?   t . n 
F 2 23  VAL 23  23  ?   ?   ?   t . n 
F 2 24  ASN 24  24  ?   ?   ?   t . n 
F 2 25  ARG 25  25  ?   ?   ?   t . n 
F 2 26  GLY 26  26  ?   ?   ?   t . n 
F 2 27  ASP 27  27  ?   ?   ?   t . n 
F 2 28  LYS 28  28  ?   ?   ?   t . n 
F 2 29  TYR 29  29  ?   ?   ?   t . n 
F 2 30  ILE 30  30  ?   ?   ?   t . n 
F 2 31  ALA 31  31  ?   ?   ?   t . n 
F 2 32  LYS 32  32  ?   ?   ?   t . n 
F 2 33  PHE 33  33  ?   ?   ?   t . n 
F 2 34  GLN 34  34  ?   ?   ?   t . n 
F 2 35  GLY 35  35  ?   ?   ?   t . n 
F 2 36  GLU 36  36  ?   ?   ?   t . n 
F 2 37  ASP 37  37  ?   ?   ?   t . n 
F 2 38  THR 38  38  ?   ?   ?   t . n 
F 2 39  VAL 39  39  ?   ?   ?   t . n 
F 2 40  VAL 40  40  ?   ?   ?   t . n 
F 2 41  ILE 41  41  ?   ?   ?   t . n 
F 2 42  ALA 42  42  ?   ?   ?   t . n 
F 2 43  SER 43  43  ?   ?   ?   t . n 
F 2 44  LYS 44  44  ?   ?   ?   t . n 
F 2 45  PRO 45  45  ?   ?   ?   t . n 
F 2 46  TYR 46  46  ?   ?   ?   t . n 
F 2 47  ALA 47  47  ?   ?   ?   t . n 
F 2 48  PHE 48  48  ?   ?   ?   t . n 
F 2 49  ASP 49  49  ?   ?   ?   t . n 
F 2 50  ARG 50  50  ?   ?   ?   t . n 
F 2 51  VAL 51  51  ?   ?   ?   t . n 
F 2 52  PHE 52  52  ?   ?   ?   t . n 
F 2 53  GLN 53  53  ?   ?   ?   t . n 
F 2 54  SER 54  54  ?   ?   ?   t . n 
F 2 55  SER 55  55  ?   ?   ?   t . n 
F 2 56  THR 56  56  ?   ?   ?   t . n 
F 2 57  SER 57  57  ?   ?   ?   t . n 
F 2 58  GLN 58  58  ?   ?   ?   t . n 
F 2 59  GLU 59  59  ?   ?   ?   t . n 
F 2 60  GLN 60  60  ?   ?   ?   t . n 
F 2 61  VAL 61  61  ?   ?   ?   t . n 
F 2 62  TYR 62  62  ?   ?   ?   t . n 
F 2 63  ASN 63  63  ?   ?   ?   t . n 
F 2 64  ASP 64  64  ?   ?   ?   t . n 
F 2 65  CYS 65  65  ?   ?   ?   t . n 
F 2 66  ALA 66  66  ?   ?   ?   t . n 
F 2 67  LYS 67  67  ?   ?   ?   t . n 
F 2 68  LYS 68  68  ?   ?   ?   t . n 
F 2 69  ILE 69  69  ?   ?   ?   t . n 
F 2 70  VAL 70  70  ?   ?   ?   t . n 
F 2 71  LYS 71  71  ?   ?   ?   t . n 
F 2 72  ASP 72  72  ?   ?   ?   t . n 
F 2 73  VAL 73  73  ?   ?   ?   t . n 
F 2 74  LEU 74  74  ?   ?   ?   t . n 
F 2 75  GLU 75  75  ?   ?   ?   t . n 
F 2 76  GLY 76  76  ?   ?   ?   t . n 
F 2 77  TYR 77  77  ?   ?   ?   t . n 
F 2 78  ASN 78  78  ?   ?   ?   t . n 
F 2 79  GLY 79  79  ?   ?   ?   t . n 
F 2 80  THR 80  80  ?   ?   ?   t . n 
F 2 81  ILE 81  81  ?   ?   ?   t . n 
F 2 82  PHE 82  82  ?   ?   ?   t . n 
F 2 83  ALA 83  83  ?   ?   ?   t . n 
F 2 84  TYR 84  84  ?   ?   ?   t . n 
F 2 85  GLY 85  85  ?   ?   ?   t . n 
F 2 86  GLN 86  86  ?   ?   ?   t . n 
F 2 87  THR 87  87  ?   ?   ?   t . n 
F 2 88  SER 88  88  ?   ?   ?   t . n 
F 2 89  SER 89  89  ?   ?   ?   t . n 
F 2 90  GLY 90  90  ?   ?   ?   t . n 
F 2 91  LYS 91  91  ?   ?   ?   t . n 
F 2 92  THR 92  92  ?   ?   ?   t . n 
F 2 93  HIS 93  93  ?   ?   ?   t . n 
F 2 94  THR 94  94  ?   ?   ?   t . n 
F 2 95  MET 95  95  ?   ?   ?   t . n 
F 2 96  GLU 96  96  ?   ?   ?   t . n 
F 2 97  GLY 97  97  ?   ?   ?   t . n 
F 2 98  LYS 98  98  ?   ?   ?   t . n 
F 2 99  LEU 99  99  ?   ?   ?   t . n 
F 2 100 HIS 100 100 ?   ?   ?   t . n 
F 2 101 ASP 101 101 ?   ?   ?   t . n 
F 2 102 PRO 102 102 ?   ?   ?   t . n 
F 2 103 GLU 103 103 ?   ?   ?   t . n 
F 2 104 GLY 104 104 ?   ?   ?   t . n 
F 2 105 MET 105 105 ?   ?   ?   t . n 
F 2 106 GLY 106 106 ?   ?   ?   t . n 
F 2 107 ILE 107 107 ?   ?   ?   t . n 
F 2 108 ILE 108 108 ?   ?   ?   t . n 
F 2 109 PRO 109 109 ?   ?   ?   t . n 
F 2 110 ARG 110 110 ?   ?   ?   t . n 
F 2 111 ILE 111 111 ?   ?   ?   t . n 
F 2 112 VAL 112 112 ?   ?   ?   t . n 
F 2 113 GLN 113 113 ?   ?   ?   t . n 
F 2 114 ASP 114 114 ?   ?   ?   t . n 
F 2 115 ILE 115 115 ?   ?   ?   t . n 
F 2 116 PHE 116 116 ?   ?   ?   t . n 
F 2 117 ASN 117 117 ?   ?   ?   t . n 
F 2 118 TYR 118 118 ?   ?   ?   t . n 
F 2 119 ILE 119 119 ?   ?   ?   t . n 
F 2 120 TYR 120 120 ?   ?   ?   t . n 
F 2 121 SER 121 121 ?   ?   ?   t . n 
F 2 122 MET 122 122 ?   ?   ?   t . n 
F 2 123 ASP 123 123 ?   ?   ?   t . n 
F 2 124 GLU 124 124 ?   ?   ?   t . n 
F 2 125 ASN 125 125 ?   ?   ?   t . n 
F 2 126 LEU 126 126 ?   ?   ?   t . n 
F 2 127 GLU 127 127 ?   ?   ?   t . n 
F 2 128 PHE 128 128 ?   ?   ?   t . n 
F 2 129 HIS 129 129 ?   ?   ?   t . n 
F 2 130 ILE 130 130 ?   ?   ?   t . n 
F 2 131 LYS 131 131 ?   ?   ?   t . n 
F 2 132 VAL 132 132 ?   ?   ?   t . n 
F 2 133 SER 133 133 ?   ?   ?   t . n 
F 2 134 TYR 134 134 ?   ?   ?   t . n 
F 2 135 PHE 135 135 ?   ?   ?   t . n 
F 2 136 GLU 136 136 ?   ?   ?   t . n 
F 2 137 ILE 137 137 ?   ?   ?   t . n 
F 2 138 TYR 138 138 ?   ?   ?   t . n 
F 2 139 LEU 139 139 ?   ?   ?   t . n 
F 2 140 ASP 140 140 ?   ?   ?   t . n 
F 2 141 LYS 141 141 ?   ?   ?   t . n 
F 2 142 ILE 142 142 ?   ?   ?   t . n 
F 2 143 ARG 143 143 ?   ?   ?   t . n 
F 2 144 ASP 144 144 ?   ?   ?   t . n 
F 2 145 LEU 145 145 ?   ?   ?   t . n 
F 2 146 LEU 146 146 ?   ?   ?   t . n 
F 2 147 ASP 147 147 ?   ?   ?   t . n 
F 2 148 VAL 148 148 ?   ?   ?   t . n 
F 2 149 SER 149 149 ?   ?   ?   t . n 
F 2 150 LYS 150 150 ?   ?   ?   t . n 
F 2 151 THR 151 151 ?   ?   ?   t . n 
F 2 152 ASN 152 152 ?   ?   ?   t . n 
F 2 153 LEU 153 153 ?   ?   ?   t . n 
F 2 154 SER 154 154 ?   ?   ?   t . n 
F 2 155 VAL 155 155 ?   ?   ?   t . n 
F 2 156 HIS 156 156 ?   ?   ?   t . n 
F 2 157 GLU 157 157 ?   ?   ?   t . n 
F 2 158 ASP 158 158 ?   ?   ?   t . n 
F 2 159 LYS 159 159 ?   ?   ?   t . n 
F 2 160 ASN 160 160 ?   ?   ?   t . n 
F 2 161 ARG 161 161 ?   ?   ?   t . n 
F 2 162 VAL 162 162 ?   ?   ?   t . n 
F 2 163 PRO 163 163 ?   ?   ?   t . n 
F 2 164 TYR 164 164 ?   ?   ?   t . n 
F 2 165 VAL 165 165 ?   ?   ?   t . n 
F 2 166 LYS 166 166 ?   ?   ?   t . n 
F 2 167 GLY 167 167 ?   ?   ?   t . n 
F 2 168 CYS 168 168 ?   ?   ?   t . n 
F 2 169 THR 169 169 ?   ?   ?   t . n 
F 2 170 GLU 170 170 ?   ?   ?   t . n 
F 2 171 ARG 171 171 ?   ?   ?   t . n 
F 2 172 PHE 172 172 ?   ?   ?   t . n 
F 2 173 VAL 173 173 ?   ?   ?   t . n 
F 2 174 CYS 174 174 ?   ?   ?   t . n 
F 2 175 SER 175 175 ?   ?   ?   t . n 
F 2 176 PRO 176 176 ?   ?   ?   t . n 
F 2 177 ASP 177 177 ?   ?   ?   t . n 
F 2 178 GLU 178 178 ?   ?   ?   t . n 
F 2 179 VAL 179 179 ?   ?   ?   t . n 
F 2 180 MET 180 180 ?   ?   ?   t . n 
F 2 181 ASP 181 181 ?   ?   ?   t . n 
F 2 182 THR 182 182 ?   ?   ?   t . n 
F 2 183 ILE 183 183 ?   ?   ?   t . n 
F 2 184 ASP 184 184 ?   ?   ?   t . n 
F 2 185 GLU 185 185 ?   ?   ?   t . n 
F 2 186 GLY 186 186 ?   ?   ?   t . n 
F 2 187 LYS 187 187 ?   ?   ?   t . n 
F 2 188 SER 188 188 ?   ?   ?   t . n 
F 2 189 ASN 189 189 ?   ?   ?   t . n 
F 2 190 ARG 190 190 ?   ?   ?   t . n 
F 2 191 HIS 191 191 ?   ?   ?   t . n 
F 2 192 VAL 192 192 ?   ?   ?   t . n 
F 2 193 ALA 193 193 ?   ?   ?   t . n 
F 2 194 VAL 194 194 ?   ?   ?   t . n 
F 2 195 THR 195 195 ?   ?   ?   t . n 
F 2 196 ASN 196 196 ?   ?   ?   t . n 
F 2 197 MET 197 197 ?   ?   ?   t . n 
F 2 198 ASN 198 198 ?   ?   ?   t . n 
F 2 199 GLU 199 199 ?   ?   ?   t . n 
F 2 200 HIS 200 200 ?   ?   ?   t . n 
F 2 201 SER 201 201 ?   ?   ?   t . n 
F 2 202 SER 202 202 ?   ?   ?   t . n 
F 2 203 ARG 203 203 ?   ?   ?   t . n 
F 2 204 SER 204 204 ?   ?   ?   t . n 
F 2 205 HIS 205 205 ?   ?   ?   t . n 
F 2 206 SER 206 206 ?   ?   ?   t . n 
F 2 207 ILE 207 207 ?   ?   ?   t . n 
F 2 208 PHE 208 208 ?   ?   ?   t . n 
F 2 209 LEU 209 209 ?   ?   ?   t . n 
F 2 210 ILE 210 210 ?   ?   ?   t . n 
F 2 211 ASN 211 211 ?   ?   ?   t . n 
F 2 212 VAL 212 212 ?   ?   ?   t . n 
F 2 213 LYS 213 213 ?   ?   ?   t . n 
F 2 214 GLN 214 214 ?   ?   ?   t . n 
F 2 215 GLU 215 215 ?   ?   ?   t . n 
F 2 216 ASN 216 216 ?   ?   ?   t . n 
F 2 217 THR 217 217 ?   ?   ?   t . n 
F 2 218 GLN 218 218 ?   ?   ?   t . n 
F 2 219 THR 219 219 ?   ?   ?   t . n 
F 2 220 GLU 220 220 ?   ?   ?   t . n 
F 2 221 GLN 221 221 ?   ?   ?   t . n 
F 2 222 LYS 222 222 ?   ?   ?   t . n 
F 2 223 LEU 223 223 ?   ?   ?   t . n 
F 2 224 SER 224 224 ?   ?   ?   t . n 
F 2 225 GLY 225 225 ?   ?   ?   t . n 
F 2 226 LYS 226 226 ?   ?   ?   t . n 
F 2 227 LEU 227 227 ?   ?   ?   t . n 
F 2 228 TYR 228 228 ?   ?   ?   t . n 
F 2 229 LEU 229 229 ?   ?   ?   t . n 
F 2 230 VAL 230 230 ?   ?   ?   t . n 
F 2 231 ASP 231 231 ?   ?   ?   t . n 
F 2 232 LEU 232 232 ?   ?   ?   t . n 
F 2 233 ALA 233 233 ?   ?   ?   t . n 
F 2 234 GLY 234 234 ?   ?   ?   t . n 
F 2 235 SER 235 235 ?   ?   ?   t . n 
F 2 236 GLU 236 236 ?   ?   ?   t . n 
F 2 237 LYS 237 237 ?   ?   ?   t . n 
F 2 238 VAL 238 238 ?   ?   ?   t . n 
F 2 239 SER 239 239 ?   ?   ?   t . n 
F 2 240 LYS 240 240 ?   ?   ?   t . n 
F 2 241 THR 241 241 ?   ?   ?   t . n 
F 2 242 GLY 242 242 ?   ?   ?   t . n 
F 2 243 ALA 243 243 ?   ?   ?   t . n 
F 2 244 GLU 244 244 ?   ?   ?   t . n 
F 2 245 GLY 245 245 ?   ?   ?   t . n 
F 2 246 ALA 246 246 ?   ?   ?   t . n 
F 2 247 VAL 247 247 ?   ?   ?   t . n 
F 2 248 LEU 248 248 ?   ?   ?   t . n 
F 2 249 ASP 249 249 ?   ?   ?   t . n 
F 2 250 GLU 250 250 ?   ?   ?   t . n 
F 2 251 ALA 251 251 ?   ?   ?   t . n 
F 2 252 LYS 252 252 ?   ?   ?   t . n 
F 2 253 ASN 253 253 ?   ?   ?   t . n 
F 2 254 ILE 254 254 ?   ?   ?   t . n 
F 2 255 ASN 255 255 ?   ?   ?   t . n 
F 2 256 LYS 256 256 ?   ?   ?   t . n 
F 2 257 SER 257 257 ?   ?   ?   t . n 
F 2 258 LEU 258 258 ?   ?   ?   t . n 
F 2 259 SER 259 259 ?   ?   ?   t . n 
F 2 260 ALA 260 260 ?   ?   ?   t . n 
F 2 261 LEU 261 261 ?   ?   ?   t . n 
F 2 262 GLY 262 262 ?   ?   ?   t . n 
F 2 263 ASN 263 263 ?   ?   ?   t . n 
F 2 264 VAL 264 264 ?   ?   ?   t . n 
F 2 265 ILE 265 265 ?   ?   ?   t . n 
F 2 266 SER 266 266 ?   ?   ?   t . n 
F 2 267 ALA 267 267 ?   ?   ?   t . n 
F 2 268 LEU 268 268 ?   ?   ?   t . n 
F 2 269 ALA 269 269 ?   ?   ?   t . n 
F 2 270 GLU 270 270 ?   ?   ?   t . n 
F 2 271 GLY 271 271 ?   ?   ?   t . n 
F 2 272 SER 272 272 ?   ?   ?   t . n 
F 2 273 THR 273 273 ?   ?   ?   t . n 
F 2 274 TYR 274 274 ?   ?   ?   t . n 
F 2 275 VAL 275 275 ?   ?   ?   t . n 
F 2 276 PRO 276 276 ?   ?   ?   t . n 
F 2 277 TYR 277 277 ?   ?   ?   t . n 
F 2 278 ARG 278 278 ?   ?   ?   t . n 
F 2 279 ASP 279 279 ?   ?   ?   t . n 
F 2 280 SER 280 280 ?   ?   ?   t . n 
F 2 281 LYS 281 281 ?   ?   ?   t . n 
F 2 282 MET 282 282 ?   ?   ?   t . n 
F 2 283 THR 283 283 ?   ?   ?   t . n 
F 2 284 ARG 284 284 ?   ?   ?   t . n 
F 2 285 ILE 285 285 ?   ?   ?   t . n 
F 2 286 LEU 286 286 ?   ?   ?   t . n 
F 2 287 GLN 287 287 ?   ?   ?   t . n 
F 2 288 ASP 288 288 ?   ?   ?   t . n 
F 2 289 SER 289 289 ?   ?   ?   t . n 
F 2 290 LEU 290 290 ?   ?   ?   t . n 
F 2 291 GLY 291 291 ?   ?   ?   t . n 
F 2 292 GLY 292 292 ?   ?   ?   t . n 
F 2 293 ASN 293 293 ?   ?   ?   t . n 
F 2 294 CYS 294 294 ?   ?   ?   t . n 
F 2 295 ARG 295 295 ?   ?   ?   t . n 
F 2 296 THR 296 296 ?   ?   ?   t . n 
F 2 297 THR 297 297 ?   ?   ?   t . n 
F 2 298 ILE 298 298 ?   ?   ?   t . n 
F 2 299 VAL 299 299 ?   ?   ?   t . n 
F 2 300 ILE 300 300 ?   ?   ?   t . n 
F 2 301 CYS 301 301 ?   ?   ?   t . n 
F 2 302 CYS 302 302 ?   ?   ?   t . n 
F 2 303 SER 303 303 ?   ?   ?   t . n 
F 2 304 PRO 304 304 ?   ?   ?   t . n 
F 2 305 SER 305 305 ?   ?   ?   t . n 
F 2 306 SER 306 306 ?   ?   ?   t . n 
F 2 307 TYR 307 307 ?   ?   ?   t . n 
F 2 308 ASN 308 308 ?   ?   ?   t . n 
F 2 309 GLU 309 309 ?   ?   ?   t . n 
F 2 310 SER 310 310 ?   ?   ?   t . n 
F 2 311 GLU 311 311 ?   ?   ?   t . n 
F 2 312 THR 312 312 ?   ?   ?   t . n 
F 2 313 LYS 313 313 ?   ?   ?   t . n 
F 2 314 SER 314 314 ?   ?   ?   t . n 
F 2 315 THR 315 315 ?   ?   ?   t . n 
F 2 316 LEU 316 316 ?   ?   ?   t . n 
F 2 317 LEU 317 317 ?   ?   ?   t . n 
F 2 318 PHE 318 318 ?   ?   ?   t . n 
F 2 319 GLY 319 319 ?   ?   ?   t . n 
F 2 320 GLN 320 320 ?   ?   ?   t . n 
F 2 321 ARG 321 321 ?   ?   ?   t . n 
F 2 322 ALA 322 322 ?   ?   ?   t . n 
F 2 323 LYS 323 323 ?   ?   ?   t . n 
F 2 324 THR 324 324 ?   ?   ?   t . n 
F 2 325 ILE 325 325 ?   ?   ?   t . n 
F 2 326 LYS 326 326 ?   ?   ?   t . n 
F 2 327 ASN 327 327 ?   ?   ?   t . n 
F 2 328 THR 328 328 ?   ?   ?   t . n 
F 2 329 VAL 329 329 ?   ?   ?   t . n 
F 2 330 CYS 330 330 ?   ?   ?   t . n 
F 2 331 VAL 331 331 ?   ?   ?   t . n 
F 2 332 ASN 332 332 ?   ?   ?   t . n 
F 2 333 VAL 333 333 ?   ?   ?   t . n 
F 2 334 GLU 334 334 ?   ?   ?   t . n 
F 2 335 LEU 335 335 ?   ?   ?   t . n 
F 2 336 THR 336 336 ?   ?   ?   t . n 
F 2 337 ALA 337 337 ?   ?   ?   t . n 
F 2 338 GLU 338 338 ?   ?   ?   t . n 
F 2 339 GLN 339 339 ?   ?   ?   t . n 
F 2 340 TRP 340 340 ?   ?   ?   t . n 
F 2 341 LYS 341 341 ?   ?   ?   t . n 
F 2 342 LYS 342 342 ?   ?   ?   t . n 
F 2 343 LYS 343 343 ?   ?   ?   t . n 
F 2 344 TYR 344 344 ?   ?   ?   t . n 
F 2 345 GLU 345 345 ?   ?   ?   t . n 
F 2 346 LYS 346 346 ?   ?   ?   t . n 
F 2 347 GLU 347 347 ?   ?   ?   t . n 
F 2 348 LYS 348 348 ?   ?   ?   t . n 
F 2 349 GLU 349 349 ?   ?   ?   t . n 
F 2 350 LYS 350 350 ?   ?   ?   t . n 
F 2 351 ASN 351 351 ?   ?   ?   t . n 
F 2 352 LYS 352 352 ?   ?   ?   t . n 
F 2 353 ILE 353 353 ?   ?   ?   t . n 
F 2 354 LEU 354 354 ?   ?   ?   t . n 
F 2 355 ARG 355 355 ?   ?   ?   t . n 
F 2 356 ASN 356 356 ?   ?   ?   t . n 
F 2 357 THR 357 357 ?   ?   ?   t . n 
F 2 358 ILE 358 358 ?   ?   ?   t . n 
F 2 359 GLN 359 359 ?   ?   ?   t . n 
F 2 360 TRP 360 360 ?   ?   ?   t . n 
F 2 361 LEU 361 361 ?   ?   ?   t . n 
F 2 362 GLU 362 362 ?   ?   ?   t . n 
F 2 363 ASN 363 363 ?   ?   ?   t . n 
F 2 364 GLU 364 364 ?   ?   ?   t . n 
F 2 365 LEU 365 365 ?   ?   ?   t . n 
F 2 366 ASN 366 366 ?   ?   ?   t . n 
F 2 367 ARG 367 367 ?   ?   ?   t . n 
F 2 368 TRP 368 368 ?   ?   ?   t . n 
F 2 369 ARG 369 369 ?   ?   ?   t . n 
F 2 370 ASN 370 370 ?   ?   ?   t . n 
F 2 371 GLY 371 371 ?   ?   ?   t . n 
F 2 372 GLU 372 372 ?   ?   ?   t . n 
F 2 373 THR 373 373 ?   ?   ?   t . n 
F 2 374 VAL 374 374 ?   ?   ?   t . n 
F 2 375 PRO 375 375 ?   ?   ?   t . n 
F 2 376 ILE 376 376 ?   ?   ?   t . n 
F 2 377 ASP 377 377 ?   ?   ?   t . n 
F 2 378 GLU 378 378 ?   ?   ?   t . n 
F 2 379 GLN 379 379 ?   ?   ?   t . n 
F 2 380 PHE 380 380 ?   ?   ?   t . n 
F 2 381 ASP 381 381 ?   ?   ?   t . n 
F 2 382 LYS 382 382 ?   ?   ?   t . n 
F 2 383 GLU 383 383 ?   ?   ?   t . n 
F 2 384 LYS 384 384 ?   ?   ?   t . n 
F 2 385 ALA 385 385 ?   ?   ?   t . n 
F 2 386 ASN 386 386 ?   ?   ?   t . n 
F 2 387 LEU 387 387 ?   ?   ?   t . n 
F 2 388 GLU 388 388 ?   ?   ?   t . n 
F 2 389 ALA 389 389 ?   ?   ?   t . n 
F 2 390 PHE 390 390 ?   ?   ?   t . n 
F 2 391 THR 391 391 ?   ?   ?   t . n 
F 2 392 VAL 392 392 ?   ?   ?   t . n 
F 2 393 ASP 393 393 ?   ?   ?   t . n 
F 2 394 LYS 394 394 ?   ?   ?   t . n 
F 2 395 ASP 395 395 ?   ?   ?   t . n 
F 2 396 ILE 396 396 ?   ?   ?   t . n 
F 2 397 THR 397 397 ?   ?   ?   t . n 
F 2 398 LEU 398 398 ?   ?   ?   t . n 
F 2 399 THR 399 399 ?   ?   ?   t . n 
F 2 400 ASN 400 400 ?   ?   ?   t . n 
F 2 401 ASP 401 401 ?   ?   ?   t . n 
F 2 402 LYS 402 402 ?   ?   ?   t . n 
F 2 403 PRO 403 403 ?   ?   ?   t . n 
F 2 404 ALA 404 404 ?   ?   ?   t . n 
F 2 405 THR 405 405 ?   ?   ?   t . n 
F 2 406 ALA 406 406 ?   ?   ?   t . n 
F 2 407 ILE 407 407 ?   ?   ?   t . n 
F 2 408 GLY 408 408 ?   ?   ?   t . n 
F 2 409 VAL 409 409 ?   ?   ?   t . n 
F 2 410 ILE 410 410 ?   ?   ?   t . n 
F 2 411 GLY 411 411 ?   ?   ?   t . n 
F 2 412 ASN 412 412 ?   ?   ?   t . n 
F 2 413 PHE 413 413 ?   ?   ?   t . n 
F 2 414 THR 414 414 ?   ?   ?   t . n 
F 2 415 ASP 415 415 ?   ?   ?   t . n 
F 2 416 ALA 416 416 ?   ?   ?   t . n 
F 2 417 GLU 417 417 ?   ?   ?   t . n 
F 2 418 ARG 418 418 ?   ?   ?   t . n 
F 2 419 ARG 419 419 ?   ?   ?   t . n 
F 2 420 LYS 420 420 ?   ?   ?   t . n 
F 2 421 CYS 421 421 ?   ?   ?   t . n 
F 2 422 GLU 422 422 ?   ?   ?   t . n 
F 2 423 GLU 423 423 ?   ?   ?   t . n 
F 2 424 GLU 424 424 ?   ?   ?   t . n 
F 2 425 ILE 425 425 ?   ?   ?   t . n 
F 2 426 ALA 426 426 ?   ?   ?   t . n 
F 2 427 LYS 427 427 ?   ?   ?   t . n 
F 2 428 LEU 428 428 ?   ?   ?   t . n 
F 2 429 TYR 429 429 ?   ?   ?   t . n 
F 2 430 LYS 430 430 ?   ?   ?   t . n 
F 2 431 GLN 431 431 ?   ?   ?   t . n 
F 2 432 LEU 432 432 ?   ?   ?   t . n 
F 2 433 ASP 433 433 ?   ?   ?   t . n 
F 2 434 ASP 434 434 ?   ?   ?   t . n 
F 2 435 LYS 435 435 ?   ?   ?   t . n 
F 2 436 ASP 436 436 ?   ?   ?   t . n 
F 2 437 GLU 437 437 ?   ?   ?   t . n 
F 2 438 GLU 438 438 ?   ?   ?   t . n 
F 2 439 ILE 439 439 ?   ?   ?   t . n 
F 2 440 ASN 440 440 ?   ?   ?   t . n 
F 2 441 GLN 441 441 ?   ?   ?   t . n 
F 2 442 GLN 442 442 ?   ?   ?   t . n 
F 2 443 SER 443 443 ?   ?   ?   t . n 
F 2 444 GLN 444 444 ?   ?   ?   t . n 
F 2 445 LEU 445 445 ?   ?   ?   t . n 
F 2 446 VAL 446 446 ?   ?   ?   t . n 
F 2 447 GLU 447 447 ?   ?   ?   t . n 
F 2 448 LYS 448 448 ?   ?   ?   t . n 
F 2 449 LEU 449 449 ?   ?   ?   t . n 
F 2 450 LYS 450 450 ?   ?   ?   t . n 
F 2 451 THR 451 451 ?   ?   ?   t . n 
F 2 452 GLN 452 452 ?   ?   ?   t . n 
F 2 453 MET 453 453 ?   ?   ?   t . n 
F 2 454 LEU 454 454 ?   ?   ?   t . n 
F 2 455 ASP 455 455 ?   ?   ?   t . n 
F 2 456 GLN 456 456 ?   ?   ?   t . n 
F 2 457 GLU 457 457 ?   ?   ?   t . n 
F 2 458 GLU 458 458 ?   ?   ?   t . n 
F 2 459 LEU 459 459 ?   ?   ?   t . n 
F 2 460 LEU 460 460 ?   ?   ?   t . n 
F 2 461 ALA 461 461 ?   ?   ?   t . n 
F 2 462 SER 462 462 ?   ?   ?   t . n 
F 2 463 THR 463 463 ?   ?   ?   t . n 
F 2 464 ARG 464 464 ?   ?   ?   t . n 
F 2 465 ARG 465 465 ?   ?   ?   t . n 
F 2 466 ASP 466 466 ?   ?   ?   t . n 
F 2 467 GLN 467 467 ?   ?   ?   t . n 
F 2 468 ASP 468 468 ?   ?   ?   t . n 
F 2 469 ASN 469 469 ?   ?   ?   t . n 
F 2 470 MET 470 470 ?   ?   ?   t . n 
F 2 471 GLN 471 471 ?   ?   ?   t . n 
F 2 472 ALA 472 472 ?   ?   ?   t . n 
F 2 473 GLU 473 473 ?   ?   ?   t . n 
F 2 474 LEU 474 474 ?   ?   ?   t . n 
F 2 475 ASN 475 475 ?   ?   ?   t . n 
F 2 476 ARG 476 476 ?   ?   ?   t . n 
F 2 477 LEU 477 477 ?   ?   ?   t . n 
F 2 478 GLN 478 478 ?   ?   ?   t . n 
F 2 479 ALA 479 479 ?   ?   ?   t . n 
F 2 480 GLU 480 480 ?   ?   ?   t . n 
F 2 481 ASN 481 481 ?   ?   ?   t . n 
F 2 482 ASP 482 482 ?   ?   ?   t . n 
F 2 483 ALA 483 483 ?   ?   ?   t . n 
F 2 484 SER 484 484 ?   ?   ?   t . n 
F 2 485 LYS 485 485 ?   ?   ?   t . n 
F 2 486 GLU 486 486 ?   ?   ?   t . n 
F 2 487 GLU 487 487 ?   ?   ?   t . n 
F 2 488 VAL 488 488 ?   ?   ?   t . n 
F 2 489 LYS 489 489 ?   ?   ?   t . n 
F 2 490 GLU 490 490 ?   ?   ?   t . n 
F 2 491 VAL 491 491 ?   ?   ?   t . n 
F 2 492 LEU 492 492 ?   ?   ?   t . n 
F 2 493 GLN 493 493 ?   ?   ?   t . n 
F 2 494 ALA 494 494 ?   ?   ?   t . n 
F 2 495 LEU 495 495 ?   ?   ?   t . n 
F 2 496 GLU 496 496 ?   ?   ?   t . n 
F 2 497 GLU 497 497 ?   ?   ?   t . n 
F 2 498 LEU 498 498 ?   ?   ?   t . n 
F 2 499 ALA 499 499 ?   ?   ?   t . n 
F 2 500 VAL 500 500 ?   ?   ?   t . n 
F 2 501 ASN 501 501 ?   ?   ?   t . n 
F 2 502 TYR 502 502 ?   ?   ?   t . n 
F 2 503 ASP 503 503 ?   ?   ?   t . n 
F 2 504 GLN 504 504 ?   ?   ?   t . n 
F 2 505 LYS 505 505 ?   ?   ?   t . n 
F 2 506 SER 506 506 ?   ?   ?   t . n 
F 2 507 GLN 507 507 ?   ?   ?   t . n 
F 2 508 GLU 508 508 ?   ?   ?   t . n 
F 2 509 VAL 509 509 ?   ?   ?   t . n 
F 2 510 GLU 510 510 ?   ?   ?   t . n 
F 2 511 ASP 511 511 ?   ?   ?   t . n 
F 2 512 LYS 512 512 ?   ?   ?   t . n 
F 2 513 THR 513 513 ?   ?   ?   t . n 
F 2 514 LYS 514 514 ?   ?   ?   t . n 
F 2 515 GLU 515 515 ?   ?   ?   t . n 
F 2 516 TYR 516 516 ?   ?   ?   t . n 
F 2 517 GLU 517 517 ?   ?   ?   t . n 
F 2 518 LEU 518 518 ?   ?   ?   t . n 
F 2 519 LEU 519 519 ?   ?   ?   t . n 
F 2 520 SER 520 520 ?   ?   ?   t . n 
F 2 521 ASP 521 521 ?   ?   ?   t . n 
F 2 522 GLU 522 522 ?   ?   ?   t . n 
F 2 523 LEU 523 523 ?   ?   ?   t . n 
F 2 524 ASN 524 524 ?   ?   ?   t . n 
F 2 525 GLN 525 525 ?   ?   ?   t . n 
F 2 526 LYS 526 526 ?   ?   ?   t . n 
F 2 527 SER 527 527 ?   ?   ?   t . n 
F 2 528 ALA 528 528 ?   ?   ?   t . n 
F 2 529 THR 529 529 ?   ?   ?   t . n 
F 2 530 LEU 530 530 ?   ?   ?   t . n 
F 2 531 ALA 531 531 ?   ?   ?   t . n 
F 2 532 SER 532 532 ?   ?   ?   t . n 
F 2 533 ILE 533 533 ?   ?   ?   t . n 
F 2 534 ASP 534 534 ?   ?   ?   t . n 
F 2 535 ALA 535 535 ?   ?   ?   t . n 
F 2 536 GLU 536 536 ?   ?   ?   t . n 
F 2 537 LEU 537 537 ?   ?   ?   t . n 
F 2 538 GLN 538 538 ?   ?   ?   t . n 
F 2 539 LYS 539 539 ?   ?   ?   t . n 
F 2 540 LEU 540 540 ?   ?   ?   t . n 
F 2 541 LYS 541 541 ?   ?   ?   t . n 
F 2 542 GLU 542 542 ?   ?   ?   t . n 
F 2 543 MET 543 543 ?   ?   ?   t . n 
F 2 544 THR 544 544 ?   ?   ?   t . n 
F 2 545 ASN 545 545 ?   ?   ?   t . n 
F 2 546 HIS 546 546 ?   ?   ?   t . n 
F 2 547 GLN 547 547 ?   ?   ?   t . n 
F 2 548 LYS 548 548 ?   ?   ?   t . n 
F 2 549 LYS 549 549 ?   ?   ?   t . n 
F 2 550 ARG 550 550 ?   ?   ?   t . n 
F 2 551 ALA 551 551 ?   ?   ?   t . n 
F 2 552 ALA 552 552 ?   ?   ?   t . n 
F 2 553 GLU 553 553 ?   ?   ?   t . n 
F 2 554 MET 554 554 ?   ?   ?   t . n 
F 2 555 MET 555 555 ?   ?   ?   t . n 
F 2 556 ALA 556 556 ?   ?   ?   t . n 
F 2 557 SER 557 557 ?   ?   ?   t . n 
F 2 558 LEU 558 558 ?   ?   ?   t . n 
F 2 559 LEU 559 559 ?   ?   ?   t . n 
F 2 560 LYS 560 560 ?   ?   ?   t . n 
F 2 561 ASP 561 561 ?   ?   ?   t . n 
F 2 562 LEU 562 562 ?   ?   ?   t . n 
F 2 563 ALA 563 563 ?   ?   ?   t . n 
F 2 564 GLU 564 564 ?   ?   ?   t . n 
F 2 565 ILE 565 565 ?   ?   ?   t . n 
F 2 566 GLY 566 566 ?   ?   ?   t . n 
F 2 567 ILE 567 567 ?   ?   ?   t . n 
F 2 568 ALA 568 568 ?   ?   ?   t . n 
F 2 569 VAL 569 569 ?   ?   ?   t . n 
F 2 570 GLY 570 570 ?   ?   ?   t . n 
F 2 571 ASN 571 571 ?   ?   ?   t . n 
F 2 572 ASN 572 572 ?   ?   ?   t . n 
F 2 573 ASP 573 573 ?   ?   ?   t . n 
F 2 574 VAL 574 574 ?   ?   ?   t . n 
F 2 575 LYS 575 575 ?   ?   ?   t . n 
F 2 576 GLN 576 576 ?   ?   ?   t . n 
F 2 577 PRO 577 577 ?   ?   ?   t . n 
F 2 578 GLU 578 578 ?   ?   ?   t . n 
F 2 579 GLY 579 579 ?   ?   ?   t . n 
F 2 580 THR 580 580 ?   ?   ?   t . n 
F 2 581 GLY 581 581 ?   ?   ?   t . n 
F 2 582 MET 582 582 ?   ?   ?   t . n 
F 2 583 ILE 583 583 ?   ?   ?   t . n 
F 2 584 ASP 584 584 ?   ?   ?   t . n 
F 2 585 GLU 585 585 ?   ?   ?   t . n 
F 2 586 GLU 586 586 ?   ?   ?   t . n 
F 2 587 PHE 587 587 ?   ?   ?   t . n 
F 2 588 THR 588 588 ?   ?   ?   t . n 
F 2 589 VAL 589 589 ?   ?   ?   t . n 
F 2 590 ALA 590 590 ?   ?   ?   t . n 
F 2 591 ARG 591 591 ?   ?   ?   t . n 
F 2 592 LEU 592 592 ?   ?   ?   t . n 
F 2 593 TYR 593 593 ?   ?   ?   t . n 
F 2 594 ILE 594 594 ?   ?   ?   t . n 
F 2 595 SER 595 595 ?   ?   ?   t . n 
F 2 596 LYS 596 596 ?   ?   ?   t . n 
F 2 597 MET 597 597 ?   ?   ?   t . n 
F 2 598 LYS 598 598 ?   ?   ?   t . n 
F 2 599 SER 599 599 ?   ?   ?   t . n 
F 2 600 GLU 600 600 ?   ?   ?   t . n 
F 2 601 VAL 601 601 ?   ?   ?   t . n 
F 2 602 LYS 602 602 ?   ?   ?   t . n 
F 2 603 THR 603 603 ?   ?   ?   t . n 
F 2 604 MET 604 604 ?   ?   ?   t . n 
F 2 605 VAL 605 605 ?   ?   ?   t . n 
F 2 606 LYS 606 606 ?   ?   ?   t . n 
F 2 607 ARG 607 607 ?   ?   ?   t . n 
F 2 608 CYS 608 608 ?   ?   ?   t . n 
F 2 609 LYS 609 609 ?   ?   ?   t . n 
F 2 610 GLN 610 610 ?   ?   ?   t . n 
F 2 611 LEU 611 611 ?   ?   ?   t . n 
F 2 612 GLU 612 612 ?   ?   ?   t . n 
F 2 613 SER 613 613 ?   ?   ?   t . n 
F 2 614 THR 614 614 ?   ?   ?   t . n 
F 2 615 GLN 615 615 ?   ?   ?   t . n 
F 2 616 THR 616 616 ?   ?   ?   t . n 
F 2 617 GLU 617 617 ?   ?   ?   t . n 
F 2 618 SER 618 618 ?   ?   ?   t . n 
F 2 619 ASN 619 619 ?   ?   ?   t . n 
F 2 620 LYS 620 620 ?   ?   ?   t . n 
F 2 621 LYS 621 621 ?   ?   ?   t . n 
F 2 622 MET 622 622 ?   ?   ?   t . n 
F 2 623 GLU 623 623 ?   ?   ?   t . n 
F 2 624 GLU 624 624 ?   ?   ?   t . n 
F 2 625 ASN 625 625 ?   ?   ?   t . n 
F 2 626 GLU 626 626 ?   ?   ?   t . n 
F 2 627 LYS 627 627 ?   ?   ?   t . n 
F 2 628 GLU 628 628 ?   ?   ?   t . n 
F 2 629 LEU 629 629 ?   ?   ?   t . n 
F 2 630 ALA 630 630 ?   ?   ?   t . n 
F 2 631 ALA 631 631 ?   ?   ?   t . n 
F 2 632 CYS 632 632 ?   ?   ?   t . n 
F 2 633 GLN 633 633 ?   ?   ?   t . n 
F 2 634 LEU 634 634 ?   ?   ?   t . n 
F 2 635 ARG 635 635 ?   ?   ?   t . n 
F 2 636 ILE 636 636 ?   ?   ?   t . n 
F 2 637 SER 637 637 ?   ?   ?   t . n 
F 2 638 GLN 638 638 ?   ?   ?   t . n 
F 2 639 HIS 639 639 ?   ?   ?   t . n 
F 2 640 GLU 640 640 ?   ?   ?   t . n 
F 2 641 ALA 641 641 ?   ?   ?   t . n 
F 2 642 LYS 642 642 ?   ?   ?   t . n 
F 2 643 ILE 643 643 ?   ?   ?   t . n 
F 2 644 LYS 644 644 ?   ?   ?   t . n 
F 2 645 SER 645 645 ?   ?   ?   t . n 
F 2 646 LEU 646 646 ?   ?   ?   t . n 
F 2 647 THR 647 647 ?   ?   ?   t . n 
F 2 648 GLU 648 648 ?   ?   ?   t . n 
F 2 649 TYR 649 649 ?   ?   ?   t . n 
F 2 650 LEU 650 650 ?   ?   ?   t . n 
F 2 651 GLN 651 651 ?   ?   ?   t . n 
F 2 652 ASN 652 652 ?   ?   ?   t . n 
F 2 653 VAL 653 653 ?   ?   ?   t . n 
F 2 654 GLU 654 654 ?   ?   ?   t . n 
F 2 655 GLN 655 655 ?   ?   ?   t . n 
F 2 656 LYS 656 656 ?   ?   ?   t . n 
F 2 657 LYS 657 657 ?   ?   ?   t . n 
F 2 658 ARG 658 658 ?   ?   ?   t . n 
F 2 659 GLN 659 659 ?   ?   ?   t . n 
F 2 660 LEU 660 660 ?   ?   ?   t . n 
F 2 661 GLU 661 661 ?   ?   ?   t . n 
F 2 662 GLU 662 662 ?   ?   ?   t . n 
F 2 663 SER 663 663 ?   ?   ?   t . n 
F 2 664 VAL 664 664 ?   ?   ?   t . n 
F 2 665 ASP 665 665 ?   ?   ?   t . n 
F 2 666 ALA 666 666 ?   ?   ?   t . n 
F 2 667 LEU 667 667 ?   ?   ?   t . n 
F 2 668 SER 668 668 ?   ?   ?   t . n 
F 2 669 GLU 669 669 ?   ?   ?   t . n 
F 2 670 GLU 670 670 ?   ?   ?   t . n 
F 2 671 LEU 671 671 ?   ?   ?   t . n 
F 2 672 VAL 672 672 ?   ?   ?   t . n 
F 2 673 GLN 673 673 ?   ?   ?   t . n 
F 2 674 LEU 674 674 ?   ?   ?   t . n 
F 2 675 ARG 675 675 ?   ?   ?   t . n 
F 2 676 ALA 676 676 ?   ?   ?   t . n 
F 2 677 GLN 677 677 ?   ?   ?   t . n 
F 2 678 GLU 678 678 ?   ?   ?   t . n 
F 2 679 LYS 679 679 ?   ?   ?   t . n 
F 2 680 VAL 680 680 ?   ?   ?   t . n 
F 2 681 HIS 681 681 ?   ?   ?   t . n 
F 2 682 GLU 682 682 ?   ?   ?   t . n 
F 2 683 MET 683 683 ?   ?   ?   t . n 
F 2 684 GLU 684 684 ?   ?   ?   t . n 
F 2 685 LYS 685 685 ?   ?   ?   t . n 
F 2 686 GLU 686 686 ?   ?   ?   t . n 
F 2 687 HIS 687 687 ?   ?   ?   t . n 
F 2 688 LEU 688 688 ?   ?   ?   t . n 
F 2 689 ASN 689 689 ?   ?   ?   t . n 
F 2 690 LYS 690 690 ?   ?   ?   t . n 
F 2 691 VAL 691 691 ?   ?   ?   t . n 
F 2 692 GLN 692 692 ?   ?   ?   t . n 
F 2 693 THR 693 693 ?   ?   ?   t . n 
F 2 694 ALA 694 694 ?   ?   ?   t . n 
F 2 695 ASN 695 695 ?   ?   ?   t . n 
F 2 696 GLU 696 696 ?   ?   ?   t . n 
F 2 697 VAL 697 697 ?   ?   ?   t . n 
F 2 698 LYS 698 698 ?   ?   ?   t . n 
F 2 699 GLN 699 699 ?   ?   ?   t . n 
F 2 700 ALA 700 700 ?   ?   ?   t . n 
F 2 701 VAL 701 701 ?   ?   ?   t . n 
F 2 702 GLU 702 702 ?   ?   ?   t . n 
F 2 703 GLN 703 703 ?   ?   ?   t . n 
F 2 704 GLN 704 704 ?   ?   ?   t . n 
F 2 705 ILE 705 705 ?   ?   ?   t . n 
F 2 706 GLN 706 706 ?   ?   ?   t . n 
F 2 707 SER 707 707 ?   ?   ?   t . n 
F 2 708 HIS 708 708 ?   ?   ?   t . n 
F 2 709 ARG 709 709 ?   ?   ?   t . n 
F 2 710 GLU 710 710 ?   ?   ?   t . n 
F 2 711 THR 711 711 ?   ?   ?   t . n 
F 2 712 HIS 712 712 ?   ?   ?   t . n 
F 2 713 GLN 713 713 ?   ?   ?   t . n 
F 2 714 LYS 714 714 ?   ?   ?   t . n 
F 2 715 GLN 715 715 ?   ?   ?   t . n 
F 2 716 ILE 716 716 ?   ?   ?   t . n 
F 2 717 SER 717 717 ?   ?   ?   t . n 
F 2 718 SER 718 718 ?   ?   ?   t . n 
F 2 719 LEU 719 719 ?   ?   ?   t . n 
F 2 720 ARG 720 720 ?   ?   ?   t . n 
F 2 721 ASP 721 721 ?   ?   ?   t . n 
F 2 722 GLU 722 722 ?   ?   ?   t . n 
F 2 723 VAL 723 723 ?   ?   ?   t . n 
F 2 724 GLU 724 724 ?   ?   ?   t . n 
F 2 725 ALA 725 725 ?   ?   ?   t . n 
F 2 726 LYS 726 726 ?   ?   ?   t . n 
F 2 727 ALA 727 727 ?   ?   ?   t . n 
F 2 728 LYS 728 728 ?   ?   ?   t . n 
F 2 729 LEU 729 729 ?   ?   ?   t . n 
F 2 730 ILE 730 730 ?   ?   ?   t . n 
F 2 731 THR 731 731 ?   ?   ?   t . n 
F 2 732 ASP 732 732 ?   ?   ?   t . n 
F 2 733 LEU 733 733 ?   ?   ?   t . n 
F 2 734 GLN 734 734 ?   ?   ?   t . n 
F 2 735 ASP 735 735 ?   ?   ?   t . n 
F 2 736 GLN 736 736 ?   ?   ?   t . n 
F 2 737 ASN 737 737 ?   ?   ?   t . n 
F 2 738 GLN 738 738 ?   ?   ?   t . n 
F 2 739 LYS 739 739 ?   ?   ?   t . n 
F 2 740 MET 740 740 ?   ?   ?   t . n 
F 2 741 MET 741 741 ?   ?   ?   t . n 
F 2 742 LEU 742 742 ?   ?   ?   t . n 
F 2 743 GLU 743 743 ?   ?   ?   t . n 
F 2 744 GLN 744 744 ?   ?   ?   t . n 
F 2 745 GLU 745 745 ?   ?   ?   t . n 
F 2 746 ARG 746 746 ?   ?   ?   t . n 
F 2 747 LEU 747 747 ?   ?   ?   t . n 
F 2 748 ARG 748 748 ?   ?   ?   t . n 
F 2 749 VAL 749 749 ?   ?   ?   t . n 
F 2 750 GLU 750 750 ?   ?   ?   t . n 
F 2 751 HIS 751 751 ?   ?   ?   t . n 
F 2 752 GLU 752 752 ?   ?   ?   t . n 
F 2 753 LYS 753 753 ?   ?   ?   t . n 
F 2 754 LEU 754 754 ?   ?   ?   t . n 
F 2 755 LYS 755 755 ?   ?   ?   t . n 
F 2 756 ALA 756 756 ?   ?   ?   t . n 
F 2 757 THR 757 757 ?   ?   ?   t . n 
F 2 758 ASP 758 758 ?   ?   ?   t . n 
F 2 759 GLN 759 759 ?   ?   ?   t . n 
F 2 760 GLU 760 760 ?   ?   ?   t . n 
F 2 761 LYS 761 761 ?   ?   ?   t . n 
F 2 762 SER 762 762 ?   ?   ?   t . n 
F 2 763 ARG 763 763 ?   ?   ?   t . n 
F 2 764 LYS 764 764 ?   ?   ?   t . n 
F 2 765 LEU 765 765 ?   ?   ?   t . n 
F 2 766 HIS 766 766 ?   ?   ?   t . n 
F 2 767 GLU 767 767 ?   ?   ?   t . n 
F 2 768 LEU 768 768 ?   ?   ?   t . n 
F 2 769 THR 769 769 ?   ?   ?   t . n 
F 2 770 VAL 770 770 ?   ?   ?   t . n 
F 2 771 MET 771 771 ?   ?   ?   t . n 
F 2 772 GLN 772 772 ?   ?   ?   t . n 
F 2 773 ASP 773 773 ?   ?   ?   t . n 
F 2 774 ARG 774 774 ?   ?   ?   t . n 
F 2 775 ARG 775 775 ?   ?   ?   t . n 
F 2 776 GLU 776 776 ?   ?   ?   t . n 
F 2 777 GLN 777 777 ?   ?   ?   t . n 
F 2 778 ALA 778 778 ?   ?   ?   t . n 
F 2 779 ARG 779 779 ?   ?   ?   t . n 
F 2 780 GLN 780 780 ?   ?   ?   t . n 
F 2 781 ASP 781 781 ?   ?   ?   t . n 
F 2 782 LEU 782 782 ?   ?   ?   t . n 
F 2 783 LYS 783 783 ?   ?   ?   t . n 
F 2 784 GLY 784 784 ?   ?   ?   t . n 
F 2 785 LEU 785 785 ?   ?   ?   t . n 
F 2 786 GLU 786 786 ?   ?   ?   t . n 
F 2 787 GLU 787 787 ?   ?   ?   t . n 
F 2 788 THR 788 788 ?   ?   ?   t . n 
F 2 789 VAL 789 789 ?   ?   ?   t . n 
F 2 790 ALA 790 790 ?   ?   ?   t . n 
F 2 791 LYS 791 791 ?   ?   ?   t . n 
F 2 792 GLU 792 792 ?   ?   ?   t . n 
F 2 793 LEU 793 793 ?   ?   ?   t . n 
F 2 794 GLN 794 794 ?   ?   ?   t . n 
F 2 795 THR 795 795 ?   ?   ?   t . n 
F 2 796 LEU 796 796 ?   ?   ?   t . n 
F 2 797 HIS 797 797 ?   ?   ?   t . n 
F 2 798 ASN 798 798 ?   ?   ?   t . n 
F 2 799 LEU 799 799 ?   ?   ?   t . n 
F 2 800 ARG 800 800 ?   ?   ?   t . n 
F 2 801 LYS 801 801 ?   ?   ?   t . n 
F 2 802 LEU 802 802 ?   ?   ?   t . n 
F 2 803 PHE 803 803 ?   ?   ?   t . n 
F 2 804 VAL 804 804 ?   ?   ?   t . n 
F 2 805 GLN 805 805 ?   ?   ?   t . n 
F 2 806 ASP 806 806 ?   ?   ?   t . n 
F 2 807 LEU 807 807 ?   ?   ?   t . n 
F 2 808 ALA 808 808 ?   ?   ?   t . n 
F 2 809 THR 809 809 ?   ?   ?   t . n 
F 2 810 ARG 810 810 ?   ?   ?   t . n 
F 2 811 VAL 811 811 ?   ?   ?   t . n 
F 2 812 LYS 812 812 ?   ?   ?   t . n 
F 2 813 LYS 813 813 ?   ?   ?   t . n 
F 2 814 SER 814 814 ?   ?   ?   t . n 
F 2 815 ALA 815 815 ?   ?   ?   t . n 
F 2 816 GLU 816 816 ?   ?   ?   t . n 
F 2 817 ILE 817 817 ?   ?   ?   t . n 
F 2 818 ASP 818 818 ?   ?   ?   t . n 
F 2 819 SER 819 819 ?   ?   ?   t . n 
F 2 820 ASP 820 820 ?   ?   ?   t . n 
F 2 821 ASP 821 821 ?   ?   ?   t . n 
F 2 822 THR 822 822 ?   ?   ?   t . n 
F 2 823 GLY 823 823 ?   ?   ?   t . n 
F 2 824 GLY 824 824 ?   ?   ?   t . n 
F 2 825 SER 825 825 ?   ?   ?   t . n 
F 2 826 ALA 826 826 ?   ?   ?   t . n 
F 2 827 ALA 827 827 ?   ?   ?   t . n 
F 2 828 GLN 828 828 ?   ?   ?   t . n 
F 2 829 LYS 829 829 ?   ?   ?   t . n 
F 2 830 GLN 830 830 ?   ?   ?   t . n 
F 2 831 LYS 831 831 ?   ?   ?   t . n 
F 2 832 ILE 832 832 ?   ?   ?   t . n 
F 2 833 SER 833 833 ?   ?   ?   t . n 
F 2 834 PHE 834 834 ?   ?   ?   t . n 
F 2 835 LEU 835 835 ?   ?   ?   t . n 
F 2 836 GLU 836 836 ?   ?   ?   t . n 
F 2 837 ASN 837 837 ?   ?   ?   t . n 
F 2 838 ASN 838 838 ?   ?   ?   t . n 
F 2 839 LEU 839 839 ?   ?   ?   t . n 
F 2 840 GLU 840 840 ?   ?   ?   t . n 
F 2 841 GLN 841 841 ?   ?   ?   t . n 
F 2 842 LEU 842 842 ?   ?   ?   t . n 
F 2 843 THR 843 843 ?   ?   ?   t . n 
F 2 844 LYS 844 844 ?   ?   ?   t . n 
F 2 845 VAL 845 845 ?   ?   ?   t . n 
F 2 846 HIS 846 846 ?   ?   ?   t . n 
F 2 847 LYS 847 847 ?   ?   ?   t . n 
F 2 848 GLN 848 848 ?   ?   ?   t . n 
F 2 849 LEU 849 849 ?   ?   ?   t . n 
F 2 850 VAL 850 850 ?   ?   ?   t . n 
F 2 851 ARG 851 851 ?   ?   ?   t . n 
F 2 852 ASP 852 852 ?   ?   ?   t . n 
F 2 853 ASN 853 853 ?   ?   ?   t . n 
F 2 854 ALA 854 854 ?   ?   ?   t . n 
F 2 855 ASP 855 855 ?   ?   ?   t . n 
F 2 856 LEU 856 856 ?   ?   ?   t . n 
F 2 857 ARG 857 857 ?   ?   ?   t . n 
F 2 858 CYS 858 858 ?   ?   ?   t . n 
F 2 859 GLU 859 859 ?   ?   ?   t . n 
F 2 860 LEU 860 860 ?   ?   ?   t . n 
F 2 861 PRO 861 861 ?   ?   ?   t . n 
F 2 862 LYS 862 862 ?   ?   ?   t . n 
F 2 863 LEU 863 863 ?   ?   ?   t . n 
F 2 864 GLU 864 864 ?   ?   ?   t . n 
F 2 865 LYS 865 865 ?   ?   ?   t . n 
F 2 866 ARG 866 866 ?   ?   ?   t . n 
F 2 867 LEU 867 867 ?   ?   ?   t . n 
F 2 868 ARG 868 868 ?   ?   ?   t . n 
F 2 869 ALA 869 869 ?   ?   ?   t . n 
F 2 870 THR 870 870 ?   ?   ?   t . n 
F 2 871 ALA 871 871 ?   ?   ?   t . n 
F 2 872 GLU 872 872 ?   ?   ?   t . n 
F 2 873 ARG 873 873 ?   ?   ?   t . n 
F 2 874 VAL 874 874 ?   ?   ?   t . n 
F 2 875 LYS 875 875 ?   ?   ?   t . n 
F 2 876 ALA 876 876 ?   ?   ?   t . n 
F 2 877 LEU 877 877 ?   ?   ?   t . n 
F 2 878 GLU 878 878 ?   ?   ?   t . n 
F 2 879 SER 879 879 ?   ?   ?   t . n 
F 2 880 ALA 880 880 ?   ?   ?   t . n 
F 2 881 LEU 881 881 ?   ?   ?   t . n 
F 2 882 LYS 882 882 ?   ?   ?   t . n 
F 2 883 GLU 883 883 ?   ?   ?   t . n 
F 2 884 ALA 884 884 ?   ?   ?   t . n 
F 2 885 LYS 885 885 ?   ?   ?   t . n 
F 2 886 GLU 886 886 ?   ?   ?   t . n 
F 2 887 ASN 887 887 ?   ?   ?   t . n 
F 2 888 ALA 888 888 ?   ?   ?   t . n 
F 2 889 SER 889 889 ?   ?   ?   t . n 
F 2 890 ARG 890 890 ?   ?   ?   t . n 
F 2 891 ASP 891 891 ?   ?   ?   t . n 
F 2 892 ARG 892 892 ?   ?   ?   t . n 
F 2 893 LYS 893 893 ?   ?   ?   t . n 
F 2 894 ARG 894 894 ?   ?   ?   t . n 
F 2 895 TYR 895 895 ?   ?   ?   t . n 
F 2 896 GLN 896 896 ?   ?   ?   t . n 
F 2 897 GLN 897 897 ?   ?   ?   t . n 
F 2 898 GLU 898 898 ?   ?   ?   t . n 
F 2 899 VAL 899 899 ?   ?   ?   t . n 
F 2 900 ASP 900 900 ?   ?   ?   t . n 
F 2 901 ARG 901 901 ?   ?   ?   t . n 
F 2 902 ILE 902 902 ?   ?   ?   t . n 
F 2 903 LYS 903 903 ?   ?   ?   t . n 
F 2 904 GLU 904 904 ?   ?   ?   t . n 
F 2 905 ALA 905 905 ?   ?   ?   t . n 
F 2 906 VAL 906 906 ?   ?   ?   t . n 
F 2 907 ARG 907 907 ?   ?   ?   t . n 
F 2 908 SER 908 908 ?   ?   ?   t . n 
F 2 909 LYS 909 909 ?   ?   ?   t . n 
F 2 910 ASN 910 910 ?   ?   ?   t . n 
F 2 911 MET 911 911 ?   ?   ?   t . n 
F 2 912 ALA 912 912 ?   ?   ?   t . n 
F 2 913 ARG 913 913 ?   ?   ?   t . n 
F 2 914 ARG 914 914 ?   ?   ?   t . n 
F 2 915 GLY 915 915 ?   ?   ?   t . n 
F 2 916 HIS 916 916 ?   ?   ?   t . n 
F 2 917 SER 917 917 ?   ?   ?   t . n 
F 2 918 ALA 918 918 918 ALA ALA t . n 
F 2 919 GLN 919 919 919 GLN GLN t . n 
F 2 920 ILE 920 920 920 ILE ILE t . n 
F 2 921 ALA 921 921 921 ALA ALA t . n 
F 2 922 LYS 922 922 922 LYS LYS t . n 
F 2 923 PRO 923 923 923 PRO PRO t . n 
F 2 924 ILE 924 924 924 ILE ILE t . n 
F 2 925 ARG 925 925 925 ARG ARG t . n 
F 2 926 PRO 926 926 926 PRO PRO t . n 
F 2 927 GLY 927 927 ?   ?   ?   t . n 
F 2 928 GLN 928 928 ?   ?   ?   t . n 
F 2 929 HIS 929 929 ?   ?   ?   t . n 
F 2 930 PRO 930 930 ?   ?   ?   t . n 
F 2 931 ALA 931 931 ?   ?   ?   t . n 
F 2 932 ALA 932 932 ?   ?   ?   t . n 
F 2 933 SER 933 933 ?   ?   ?   t . n 
F 2 934 PRO 934 934 ?   ?   ?   t . n 
F 2 935 THR 935 935 ?   ?   ?   t . n 
F 2 936 HIS 936 936 ?   ?   ?   t . n 
F 2 937 PRO 937 937 ?   ?   ?   t . n 
F 2 938 SER 938 938 ?   ?   ?   t . n 
F 2 939 ALA 939 939 ?   ?   ?   t . n 
F 2 940 ILE 940 940 ?   ?   ?   t . n 
F 2 941 ARG 941 941 ?   ?   ?   t . n 
F 2 942 GLY 942 942 ?   ?   ?   t . n 
F 2 943 GLY 943 943 ?   ?   ?   t . n 
F 2 944 GLY 944 944 ?   ?   ?   t . n 
F 2 945 ALA 945 945 ?   ?   ?   t . n 
F 2 946 PHE 946 946 ?   ?   ?   t . n 
F 2 947 VAL 947 947 ?   ?   ?   t . n 
F 2 948 GLN 948 948 ?   ?   ?   t . n 
F 2 949 ASN 949 949 ?   ?   ?   t . n 
F 2 950 SER 950 950 ?   ?   ?   t . n 
F 2 951 GLN 951 951 ?   ?   ?   t . n 
F 2 952 PRO 952 952 ?   ?   ?   t . n 
F 2 953 VAL 953 953 ?   ?   ?   t . n 
F 2 954 ALA 954 954 ?   ?   ?   t . n 
F 2 955 VAL 955 955 ?   ?   ?   t . n 
F 2 956 ARG 956 956 ?   ?   ?   t . n 
F 2 957 GLY 957 957 ?   ?   ?   t . n 
F 2 958 GLY 958 958 ?   ?   ?   t . n 
F 2 959 GLY 959 959 ?   ?   ?   t . n 
F 2 960 GLY 960 960 ?   ?   ?   t . n 
F 2 961 LYS 961 961 ?   ?   ?   t . n 
F 2 962 GLN 962 962 ?   ?   ?   t . n 
F 2 963 VAL 963 963 ?   ?   ?   t . n 
# 
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 GDP 1 501  501 GDP GDP B . 
H 5 TA1 1 502  502 TA1 TA1 B . 
I 6 ANP 1 1001 602 ANP ANP K . 
J 7 MG  1 1002 502 MG  MG  K . 
K 7 MG  1 1001 501 MG  MG  L . 
L 6 ANP 1 1002 500 ANP ANP L . 
M 8 GTP 1 501  501 GTP GTP A . 
N 7 MG  1 502  502 MG  MG  A . 
# 
_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                     8RHH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         8RHH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   8RHH 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8RHH 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.004  ? 12440 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.728  ? 16863 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 11.890 ? 1705  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.046  ? 1868  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 2169  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8RHH 
_struct.title                        'Microtubule-associated kinesin-1 tail complex bound to AMPPNP, two-headed state' 
_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        8RHH 
_struct_keywords.text            
'Kinesin autoinhibition motor microtubules mechanochemistry intracellular transport, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
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 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 2 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
K N N 7 ? 
L N N 6 ? 
M N N 8 ? 
N 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 TBB_PIG    P02554 ? 1 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
;
1 
2 UNP KINH_HUMAN P33176 ? 2 
;MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT
IFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN
RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ
RAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTN
DKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAE
NDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLK
DLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHE
AKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLR
DEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLR
KLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESA
LKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPSAIRGGGAFVQNSQPVAVRGGGG
KQV
;
0 
3 UNP TBA1B_PIG  Q2XVP4 ? 3 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8RHH B 1 ? 445 ? P02554 1 ? 445 ? 1 455 
2 2 8RHH K 1 ? 963 ? P33176 1 ? 963 ? 1 963 
3 2 8RHH L 1 ? 963 ? P33176 1 ? 963 ? 1 963 
4 3 8RHH A 1 ? 451 ? Q2XVP4 1 ? 451 ? 1 451 
5 2 8RHH T 1 ? 963 ? P33176 1 ? 963 ? 1 963 
6 2 8RHH t 1 ? 963 ? P33176 1 ? 963 ? 1 963 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 10  ? GLY A 29  ? GLY B 10  GLY B 29  1 ? 20 
HELX_P HELX_P2  AA2 SER A 40  ? ARG A 46  ? SER B 40  ARG B 48  1 ? 7  
HELX_P HELX_P3  AA3 PRO A 70  ? SER A 78  ? PRO B 72  SER B 80  1 ? 9  
HELX_P HELX_P4  AA4 ARG A 86  ? ASP A 88  ? ARG B 88  ASP B 90  5 ? 3  
HELX_P HELX_P5  AA5 ASN A 100 ? TYR A 106 ? ASN B 102 TYR B 108 1 ? 7  
HELX_P HELX_P6  AA6 THR A 107 ? SER A 126 ? THR B 109 SER B 128 1 ? 20 
HELX_P HELX_P7  AA7 GLY A 142 ? TYR A 159 ? GLY B 144 TYR B 161 1 ? 18 
HELX_P HELX_P8  AA8 VAL A 180 ? THR A 196 ? VAL B 182 THR B 198 1 ? 17 
HELX_P HELX_P9  AA9 ASP A 203 ? THR A 214 ? ASP B 205 THR B 216 1 ? 12 
HELX_P HELX_P10 AB1 THR A 221 ? THR A 237 ? THR B 223 THR B 239 1 ? 17 
HELX_P HELX_P11 AB2 ASP A 249 ? VAL A 258 ? ASP B 251 VAL B 260 1 ? 10 
HELX_P HELX_P12 AB3 SER A 278 ? ARG A 282 ? SER B 280 ARG B 284 5 ? 5  
HELX_P HELX_P13 AB4 THR A 285 ? ASP A 295 ? THR B 287 ASP B 297 1 ? 11 
HELX_P HELX_P14 AB5 ALA A 296 ? MET A 299 ? ALA B 298 MET B 301 5 ? 4  
HELX_P HELX_P15 AB6 SER A 322 ? ASN A 337 ? SER B 324 ASN B 339 1 ? 16 
HELX_P HELX_P16 AB7 SER A 338 ? PHE A 341 ? SER B 340 PHE B 343 5 ? 4  
HELX_P HELX_P17 AB8 ILE A 374 ? ARG A 391 ? ILE B 384 ARG B 401 1 ? 18 
HELX_P HELX_P18 AB9 LEU A 395 ? GLY A 400 ? LEU B 405 GLY B 410 1 ? 6  
HELX_P HELX_P19 AC1 ASP A 404 ? TYR A 425 ? ASP B 414 TYR B 435 1 ? 22 
HELX_P HELX_P20 AC2 ASN B 19  ? ASN B 24  ? ASN K 19  ASN K 24  1 ? 6  
HELX_P HELX_P21 AC3 SER B 57  ? ALA B 66  ? SER K 57  ALA K 66  1 ? 10 
HELX_P HELX_P22 AC4 ALA B 66  ? GLY B 76  ? ALA K 66  GLY K 76  1 ? 11 
HELX_P HELX_P23 AC5 GLY B 90  ? GLU B 96  ? GLY K 90  GLU K 96  1 ? 7  
HELX_P HELX_P24 AC6 GLY B 106 ? SER B 121 ? GLY K 106 SER K 121 1 ? 16 
HELX_P HELX_P25 AC7 SER B 175 ? ARG B 190 ? SER K 175 ARG K 190 1 ? 16 
HELX_P HELX_P26 AC8 LYS B 237 ? GLY B 242 ? LYS K 237 GLY K 242 1 ? 6  
HELX_P HELX_P27 AC9 GLY B 245 ? GLY B 271 ? GLY K 245 GLY K 271 1 ? 27 
HELX_P HELX_P28 AD1 PRO B 276 ? ASP B 279 ? PRO K 276 ASP K 279 5 ? 4  
HELX_P HELX_P29 AD2 SER B 280 ? LEU B 286 ? SER K 280 LEU K 286 1 ? 7  
HELX_P HELX_P30 AD3 LEU B 286 ? GLY B 292 ? LEU K 286 GLY K 292 1 ? 7  
HELX_P HELX_P31 AD4 SER B 305 ? TYR B 307 ? SER K 305 TYR K 307 5 ? 3  
HELX_P HELX_P32 AD5 ASN B 308 ? ILE B 325 ? ASN K 308 ILE K 325 1 ? 18 
HELX_P HELX_P33 AD6 THR B 336 ? LYS B 346 ? THR K 336 LYS K 346 1 ? 11 
HELX_P HELX_P34 AD7 ASN C 19  ? GLY C 26  ? ASN L 19  GLY L 26  1 ? 8  
HELX_P HELX_P35 AD8 SER C 57  ? GLY C 76  ? SER L 57  GLY L 76  1 ? 20 
HELX_P HELX_P36 AD9 ILE C 107 ? SER C 121 ? ILE L 107 SER L 121 1 ? 15 
HELX_P HELX_P37 AE1 SER C 175 ? ASN C 189 ? SER L 175 ASN L 189 1 ? 15 
HELX_P HELX_P38 AE2 LYS C 256 ? GLY C 271 ? LYS L 256 GLY L 271 1 ? 16 
HELX_P HELX_P39 AE3 LEU C 286 ? GLY C 292 ? LEU L 286 GLY L 292 1 ? 7  
HELX_P HELX_P40 AE4 ASN C 308 ? LYS C 323 ? ASN L 308 LYS L 323 1 ? 16 
HELX_P HELX_P41 AE5 THR C 336 ? LYS C 346 ? THR L 336 LYS L 346 1 ? 11 
HELX_P HELX_P42 AE6 GLY D 10  ? HIS D 28  ? GLY A 10  HIS A 28  1 ? 19 
HELX_P HELX_P43 AE7 GLU D 71  ? GLY D 81  ? GLU A 71  GLY A 81  1 ? 11 
HELX_P HELX_P44 AE8 ASN D 102 ? TYR D 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P45 AE9 ILE D 110 ? GLU D 113 ? ILE A 110 GLU A 113 5 ? 4  
HELX_P HELX_P46 AF1 ILE D 114 ? GLN D 128 ? ILE A 114 GLN A 128 1 ? 15 
HELX_P HELX_P47 AF2 GLY D 144 ? TYR D 161 ? GLY A 144 TYR A 161 1 ? 18 
HELX_P HELX_P48 AF3 VAL D 182 ? THR D 194 ? VAL A 182 THR A 194 1 ? 13 
HELX_P HELX_P49 AF4 ASP D 205 ? ASN D 216 ? ASP A 205 ASN A 216 1 ? 12 
HELX_P HELX_P50 AF5 THR D 223 ? PHE D 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P51 AF6 ASP D 251 ? VAL D 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P52 AF7 SER D 287 ? PHE D 296 ? SER A 287 PHE A 296 1 ? 10 
HELX_P HELX_P53 AF8 GLU D 297 ? GLN D 301 ? GLU A 297 GLN A 301 5 ? 5  
HELX_P HELX_P54 AF9 VAL D 324 ? LYS D 338 ? VAL A 324 LYS A 338 1 ? 15 
HELX_P HELX_P55 AG1 ILE D 384 ? LYS D 401 ? ILE A 384 LYS A 401 1 ? 18 
HELX_P HELX_P56 AG2 PHE D 404 ? GLY D 410 ? PHE A 404 GLY A 410 1 ? 7  
HELX_P HELX_P57 AG3 GLU D 415 ? VAL D 437 ? GLU A 415 VAL A 437 1 ? 23 
# 
_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 
metalc1  metalc ? ? B THR 92  OG1 ? ? ? 1_555 J MG  . MG  ? ? K THR 92   K MG  1002 1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc2  metalc ? ? B SER 202 OG  ? ? ? 1_555 J MG  . MG  ? ? K SER 202  K MG  1002 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc3  metalc ? ? I ANP .   O3G ? ? ? 1_555 J MG  . MG  ? ? K ANP 1001 K MG  1002 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc4  metalc ? ? I ANP .   O2B ? ? ? 1_555 J MG  . MG  ? ? K ANP 1001 K MG  1002 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc5  metalc ? ? K MG  .   MG  ? ? ? 1_555 L ANP . O2G ? ? L MG  1001 L ANP 1002 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc6  metalc ? ? K MG  .   MG  ? ? ? 1_555 L ANP . O1B ? ? L MG  1001 L ANP 1002 1_555 ? ? ? ? ? ? ? 1.967 ? ? 
metalc7  metalc ? ? D GLU 71  OE1 ? ? ? 1_555 N MG  . MG  ? ? A GLU 71   A MG  502  1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc8  metalc ? ? D GLU 71  OE2 ? ? ? 1_555 N MG  . MG  ? ? A GLU 71   A MG  502  1_555 ? ? ? ? ? ? ? 2.467 ? ? 
metalc9  metalc ? ? M GTP .   O3G ? ? ? 1_555 N MG  . MG  ? ? A GTP 501  A MG  502  1_555 ? ? ? ? ? ? ? 1.931 ? ? 
metalc10 metalc ? ? M GTP .   O1B ? ? ? 1_555 N MG  . MG  ? ? A GTP 501  A MG  502  1_555 ? ? ? ? ? ? ? 2.547 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  OG1 ? B THR 92  ? K THR 92   ? 1_555 MG ? J MG . ? K MG 1002 ? 1_555 OG  ? B SER 202 ? K SER 202  ? 1_555 126.1 ? 
2  OG1 ? B THR 92  ? K THR 92   ? 1_555 MG ? J MG . ? K MG 1002 ? 1_555 O3G ? I ANP .   ? K ANP 1001 ? 1_555 155.9 ? 
3  OG  ? B SER 202 ? K SER 202  ? 1_555 MG ? J MG . ? K MG 1002 ? 1_555 O3G ? I ANP .   ? K ANP 1001 ? 1_555 62.8  ? 
4  OG1 ? B THR 92  ? K THR 92   ? 1_555 MG ? J MG . ? K MG 1002 ? 1_555 O2B ? I ANP .   ? K ANP 1001 ? 1_555 74.1  ? 
5  OG  ? B SER 202 ? K SER 202  ? 1_555 MG ? J MG . ? K MG 1002 ? 1_555 O2B ? I ANP .   ? K ANP 1001 ? 1_555 148.8 ? 
6  O3G ? I ANP .   ? K ANP 1001 ? 1_555 MG ? J MG . ? K MG 1002 ? 1_555 O2B ? I ANP .   ? K ANP 1001 ? 1_555 89.6  ? 
7  O2G ? L ANP .   ? L ANP 1002 ? 1_555 MG ? K MG . ? L MG 1001 ? 1_555 O1B ? L ANP .   ? L ANP 1002 ? 1_555 106.3 ? 
8  OE1 ? D GLU 71  ? A GLU 71   ? 1_555 MG ? N MG . ? A MG 502  ? 1_555 OE2 ? D GLU 71  ? A GLU 71   ? 1_555 54.9  ? 
9  OE1 ? D GLU 71  ? A GLU 71   ? 1_555 MG ? N MG . ? A MG 502  ? 1_555 O3G ? M GTP .   ? A GTP 501  ? 1_555 134.9 ? 
10 OE2 ? D GLU 71  ? A GLU 71   ? 1_555 MG ? N MG . ? A MG 502  ? 1_555 O3G ? M GTP .   ? A GTP 501  ? 1_555 80.0  ? 
11 OE1 ? D GLU 71  ? A GLU 71   ? 1_555 MG ? N MG . ? A MG 502  ? 1_555 O1B ? M GTP .   ? A GTP 501  ? 1_555 150.0 ? 
12 OE2 ? D GLU 71  ? A GLU 71   ? 1_555 MG ? N MG . ? A MG 502  ? 1_555 O1B ? M GTP .   ? A GTP 501  ? 1_555 154.8 ? 
13 O3G ? M GTP .   ? A GTP 501  ? 1_555 MG ? N MG . ? A MG 502  ? 1_555 O1B ? M GTP .   ? A GTP 501  ? 1_555 74.9  ? 
# 
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 ALA 271 A . ? ALA 273 B PRO 272 A ? PRO 274 B 1 1.01  
2 ALA 273 D . ? ALA 273 A PRO 274 D ? PRO 274 A 1 -0.69 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 2  ? 
AA3 ? 2  ? 
AA4 ? 11 ? 
AA5 ? 3  ? 
AA6 ? 2  ? 
AA7 ? 2  ? 
AA8 ? 2  ? 
AA9 ? 11 ? 
AB1 ? 3  ? 
AB2 ? 2  ? 
AB3 ? 6  ? 
AB4 ? 2  ? 
AB5 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 1 9  ? parallel      
AA4 3 8  ? parallel      
AA4 3 9  ? parallel      
AA4 4 5  ? anti-parallel 
AA4 4 6  ? anti-parallel 
AA4 4 7  ? anti-parallel 
AA4 4 11 ? parallel      
AA4 7 8  ? anti-parallel 
AA4 8 10 ? anti-parallel 
AA5 1 2  ? anti-parallel 
AA5 2 3  ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA7 1 2  ? anti-parallel 
AA8 1 2  ? anti-parallel 
AA9 1 2  ? parallel      
AA9 1 9  ? parallel      
AA9 3 8  ? parallel      
AA9 3 9  ? parallel      
AA9 4 5  ? anti-parallel 
AA9 4 6  ? anti-parallel 
AA9 4 7  ? anti-parallel 
AA9 4 11 ? parallel      
AA9 7 8  ? anti-parallel 
AA9 8 10 ? anti-parallel 
AB1 1 2  ? anti-parallel 
AB1 2 3  ? anti-parallel 
AB2 1 2  ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? parallel      
AB3 5 6  ? parallel      
AB4 1 2  ? anti-parallel 
AB5 1 5  ? anti-parallel 
AB5 2 4  ? parallel      
AB5 2 5  ? anti-parallel 
AB5 3 5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 90  ? PHE A 92  ? PHE B 92  PHE B 94  
AA1 2  ALA A 63  ? ASP A 67  ? ALA B 65  ASP B 69  
AA1 3  GLU A 3   ? ALA A 9   ? GLU B 3   ALA B 9   
AA1 4  LEU A 130 ? SER A 138 ? LEU B 132 SER B 140 
AA1 5  ILE A 163 ? VAL A 169 ? ILE B 165 VAL B 171 
AA1 6  GLU A 198 ? ILE A 202 ? GLU B 200 ILE B 204 
AA1 7  PHE A 265 ? ALA A 271 ? PHE B 267 ALA B 273 
AA1 8  MET A 363 ? SER A 371 ? MET B 373 SER B 381 
AA1 9  TYR A 310 ? GLY A 319 ? TYR B 312 GLY B 321 
AA1 10 VAL A 349 ? CYS A 354 ? VAL B 351 CYS B 356 
AA2 1  TYR A 51  ? ALA A 54  ? TYR B 53  ALA B 56  
AA2 2  LYS A 58  ? PRO A 61  ? LYS B 60  PRO B 63  
AA3 1  ALA B 5   ? ASN B 8   ? ALA K 5   ASN K 8   
AA3 2  LYS B 326 ? VAL B 329 ? LYS K 326 VAL K 329 
AA4 1  MET B 12  ? PHE B 15  ? MET K 12  PHE K 15  
AA4 2  VAL B 51  ? PHE B 52  ? VAL K 51  PHE K 52  
AA4 3  GLY B 79  ? TYR B 84  ? GLY K 79  TYR K 84  
AA4 4  LEU B 126 ? TYR B 138 ? LEU K 126 TYR K 138 
AA4 5  LYS B 141 ? ASP B 144 ? LYS K 141 ASP K 144 
AA4 6  ARG B 171 ? VAL B 173 ? ARG K 171 VAL K 173 
AA4 7  SER B 206 ? ASN B 216 ? SER K 206 ASN K 216 
AA4 8  LYS B 222 ? ASP B 231 ? LYS K 222 ASP K 231 
AA4 9  ARG B 295 ? CYS B 302 ? ARG K 295 CYS K 302 
AA4 10 VAL B 333 ? GLU B 334 ? VAL K 333 GLU K 334 
AA4 11 GLN F 919 ? ILE F 920 ? GLN t 919 ILE t 920 
AA5 1  LYS B 32  ? GLN B 34  ? LYS K 32  GLN K 34  
AA5 2  THR B 38  ? ILE B 41  ? THR K 38  ILE K 41  
AA5 3  LYS B 44  ? ALA B 47  ? LYS K 44  ALA K 47  
AA6 1  SER B 154 ? GLU B 157 ? SER K 154 GLU K 157 
AA6 2  PRO B 163 ? LYS B 166 ? PRO K 163 LYS K 166 
AA7 1  VAL B 192 ? ALA B 193 ? VAL K 192 ALA K 193 
AA7 2  SER B 201 ? SER B 202 ? SER K 201 SER K 202 
AA8 1  GLU C 6   ? ASN C 8   ? GLU L 6   ASN L 8   
AA8 2  LYS C 326 ? THR C 328 ? LYS L 326 THR L 328 
AA9 1  LYS C 10  ? PHE C 15  ? LYS L 10  PHE L 15  
AA9 2  ARG C 50  ? VAL C 51  ? ARG L 50  VAL L 51  
AA9 3  GLY C 79  ? GLY C 85  ? GLY L 79  GLY L 85  
AA9 4  GLU C 127 ? TYR C 138 ? GLU L 127 TYR L 138 
AA9 5  LYS C 141 ? ASP C 144 ? LYS L 141 ASP L 144 
AA9 6  ARG C 171 ? PHE C 172 ? ARG L 171 PHE L 172 
AA9 7  HIS C 205 ? ASN C 216 ? HIS L 205 ASN L 216 
AA9 8  GLN C 221 ? LEU C 229 ? GLN L 221 LEU L 229 
AA9 9  ARG C 295 ? CYS C 302 ? ARG L 295 CYS L 302 
AA9 10 VAL C 333 ? LEU C 335 ? VAL L 333 LEU L 335 
AA9 11 GLN E 919 ? ILE E 920 ? GLN T 919 ILE T 920 
AB1 1  LYS C 32  ? PHE C 33  ? LYS L 32  PHE L 33  
AB1 2  THR C 38  ? ILE C 41  ? THR L 38  ILE L 41  
AB1 3  LYS C 44  ? ALA C 47  ? LYS L 44  ALA L 47  
AB2 1  VAL C 155 ? GLU C 157 ? VAL L 155 GLU L 157 
AB2 2  PRO C 163 ? VAL C 165 ? PRO L 163 VAL L 165 
AB3 1  ILE D 93  ? THR D 94  ? ILE A 93  THR A 94  
AB3 2  ALA D 65  ? ASP D 69  ? ALA A 65  ASP A 69  
AB3 3  ARG D 2   ? VAL D 9   ? ARG A 2   VAL A 9   
AB3 4  GLY D 131 ? PHE D 138 ? GLY A 131 PHE A 138 
AB3 5  SER D 165 ? ILE D 171 ? SER A 165 ILE A 171 
AB3 6  CYS D 200 ? VAL D 204 ? CYS A 200 VAL A 204 
AB4 1  PHE D 53  ? GLU D 55  ? PHE A 53  GLU A 55  
AB4 2  HIS D 61  ? PRO D 63  ? HIS A 61  PRO A 63  
AB5 1  LEU D 269 ? ALA D 273 ? LEU A 269 ALA A 273 
AB5 2  TYR D 312 ? LEU D 318 ? TYR A 312 LEU A 318 
AB5 3  ARG D 320 ? GLY D 321 ? ARG A 320 GLY A 321 
AB5 4  PHE D 351 ? GLY D 354 ? PHE A 351 GLY A 354 
AB5 5  ARG D 373 ? THR D 381 ? ARG A 373 THR A 381 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O VAL A 91  ? O VAL B 93  N LEU A 65  ? N LEU B 67  
AA1 2 3  O VAL A 66  ? O VAL B 68  N GLN A 8   ? N GLN B 8   
AA1 3 4  N VAL A 5   ? N VAL B 5   O GLN A 134 ? O GLN B 136 
AA1 4 5  N LEU A 135 ? N LEU B 137 O PHE A 167 ? O PHE B 169 
AA1 5 6  N THR A 166 ? N THR B 168 O TYR A 200 ? O TYR B 202 
AA1 6 7  N CYS A 201 ? N CYS B 203 O PHE A 266 ? O PHE B 268 
AA1 7 8  N ALA A 271 ? N ALA B 273 O ALA A 365 ? O ALA B 375 
AA1 8 9  O ASN A 370 ? O ASN B 380 N LEU A 311 ? N LEU B 313 
AA1 9 10 N GLY A 319 ? N GLY B 321 O CYS A 354 ? O CYS B 356 
AA2 1 2  N ASN A 52  ? N ASN B 54  O VAL A 60  ? O VAL B 62  
AA3 1 2  N CYS B 7   ? N CYS K 7   O ASN B 327 ? O ASN K 327 
AA4 1 2  N CYS B 13  ? N CYS K 13  O PHE B 52  ? O PHE K 52  
AA4 1 9  N MET B 12  ? N MET K 12  O ILE B 298 ? O ILE K 298 
AA4 3 8  N ILE B 81  ? N ILE K 81  O TYR B 228 ? O TYR K 228 
AA4 3 9  N TYR B 84  ? N TYR K 84  O CYS B 301 ? O CYS K 301 
AA4 4 5  N TYR B 138 ? N TYR K 138 O LYS B 141 ? O LYS K 141 
AA4 4 6  N VAL B 132 ? N VAL K 132 O ARG B 171 ? O ARG K 171 
AA4 4 7  N SER B 133 ? N SER K 133 O LEU B 209 ? O LEU K 209 
AA4 4 11 O PHE B 128 ? O PHE K 128 N GLN F 919 ? N GLN t 919 
AA4 7 8  N GLN B 214 ? N GLN K 214 O LEU B 223 ? O LEU K 223 
AA4 8 10 N LYS B 222 ? N LYS K 222 O GLU B 334 ? O GLU K 334 
AA5 1 2  N LYS B 32  ? N LYS K 32  O VAL B 40  ? O VAL K 40  
AA5 2 3  N VAL B 39  ? N VAL K 39  O TYR B 46  ? O TYR K 46  
AA6 1 2  N SER B 154 ? N SER K 154 O LYS B 166 ? O LYS K 166 
AA7 1 2  N ALA B 193 ? N ALA K 193 O SER B 201 ? O SER K 201 
AA8 1 2  N CYS C 7   ? N CYS L 7   O ASN C 327 ? O ASN L 327 
AA9 1 2  N CYS C 13  ? N CYS L 13  O ARG C 50  ? O ARG L 50  
AA9 1 9  N ARG C 14  ? N ARG L 14  O ILE C 300 ? O ILE L 300 
AA9 3 8  N GLY C 79  ? N GLY L 79  O TYR C 228 ? O TYR L 228 
AA9 3 9  N PHE C 82  ? N PHE L 82  O VAL C 299 ? O VAL L 299 
AA9 4 5  N GLU C 136 ? N GLU L 136 O ARG C 143 ? O ARG L 143 
AA9 4 6  N VAL C 132 ? N VAL L 132 O ARG C 171 ? O ARG L 171 
AA9 4 7  N PHE C 135 ? N PHE L 135 O ILE C 207 ? O ILE L 207 
AA9 4 11 N PHE C 128 ? N PHE L 128 O GLN E 919 ? O GLN T 919 
AA9 7 8  N GLN C 214 ? N GLN L 214 O LEU C 223 ? O LEU L 223 
AA9 8 10 N LYS C 222 ? N LYS L 222 O GLU C 334 ? O GLU L 334 
AB1 1 2  N LYS C 32  ? N LYS L 32  O VAL C 40  ? O VAL L 40  
AB1 2 3  N VAL C 39  ? N VAL L 39  O TYR C 46  ? O TYR L 46  
AB2 1 2  N HIS C 156 ? N HIS L 156 O TYR C 164 ? O TYR L 164 
AB3 1 2  O ILE D 93  ? O ILE A 93  N PHE D 67  ? N PHE A 67  
AB3 2 3  O VAL D 68  ? O VAL A 68  N HIS D 8   ? N HIS A 8   
AB3 3 4  N ILE D 7   ? N ILE A 7   O PHE D 138 ? O PHE A 138 
AB3 4 5  N PHE D 135 ? N PHE A 135 O LEU D 167 ? O LEU A 167 
AB3 5 6  N GLU D 168 ? N GLU A 168 O PHE D 202 ? O PHE A 202 
AB4 1 2  N SER D 54  ? N SER A 54  O VAL D 62  ? O VAL A 62  
AB5 1 5  N ALA D 273 ? N ALA A 273 O VAL D 375 ? O VAL A 375 
AB5 2 4  N LEU D 317 ? N LEU A 317 O LYS D 352 ? O LYS A 352 
AB5 2 5  N ALA D 314 ? N ALA A 314 O ASN D 380 ? O ASN A 380 
AB5 3 5  N ARG D 320 ? N ARG A 320 O ALA D 374 ? O ALA A 374 
# 
_pdbx_entry_details.entry_id                   8RHH 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  K SER 202 ? ? O3G K ANP 1001 ? ? 2.13 
2 1 NE2 B HIS 229 ? ? O14 B TA1 502  ? ? 2.14 
# 
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 ASP B 357 ? ? -90.78  48.12   
2  1 GLU K 220 ? ? 67.55   -6.39   
3  1 VAL K 275 ? ? 44.85   79.77   
4  1 PRO K 276 ? ? -69.07  82.02   
5  1 GLU L 75  ? ? -82.11  -71.32  
6  1 MET L 105 ? ? 34.46   58.99   
7  1 ILE L 107 ? ? -133.10 -50.60  
8  1 SER L 121 ? ? -79.33  -165.72 
9  1 MET L 122 ? ? 56.44   -171.98 
10 1 TYR A 83  ? ? -95.48  56.72   
11 1 THR A 109 ? ? -92.19  -64.76  
12 1 LEU A 248 ? ? 61.34   65.46   
13 1 HIS A 283 ? ? 66.58   -1.67   
14 1 HIS A 309 ? ? -91.78  51.59   
15 1 PHE A 404 ? ? 66.98   -0.13   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8RHH 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           'Phenix Real Space refine and Coot' 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_reconstruction.entry_id                    8RHH 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     'Relion noise-substitution test corrected FSC' 
_em_3d_reconstruction.resolution                  3.0 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               570836 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       'BRB80 + 5mM AMPPNP' 
_em_buffer.pH            6.8 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX '13pf microtubule bound to Kif5bMoNeIAK in the presence of AMPPNP (two-headed state)' ? ? ? 
'1, 2, 3' 
2 1 RECOMBINANT        COMPLEX 'Kinesin-1 heavy chain'                                                               ? ? ? 2 
3 1 NATURAL            COMPLEX '13pf microtubule'                                                                    ? ? ? '1, 3' 
# 
_em_imaging.entry_id                        8RHH 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             700 
_em_imaging.nominal_defocus_max             2500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    ? 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        C-flat-2/2 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8RHH 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              80 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            'LEICA EM GP' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8RHH 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       FILAMENT 
_em_experiment.entity_assembly_id      1 
# 
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 B ASP 437 ? A ASP 427 
2    1 Y 1 B ALA 438 ? A ALA 428 
3    1 Y 1 B THR 439 ? A THR 429 
4    1 Y 1 B ALA 440 ? A ALA 430 
5    1 Y 1 B ASP 441 ? A ASP 431 
6    1 Y 1 B GLU 442 ? A GLU 432 
7    1 Y 1 B GLN 443 ? A GLN 433 
8    1 Y 1 B GLY 444 ? A GLY 434 
9    1 Y 1 B GLU 445 ? A GLU 435 
10   1 Y 1 B PHE 446 ? A PHE 436 
11   1 Y 1 B GLU 447 ? A GLU 437 
12   1 Y 1 B GLU 448 ? A GLU 438 
13   1 Y 1 B GLU 449 ? A GLU 439 
14   1 Y 1 B GLY 450 ? A GLY 440 
15   1 Y 1 B GLU 451 ? A GLU 441 
16   1 Y 1 B GLU 452 ? A GLU 442 
17   1 Y 1 B ASP 453 ? A ASP 443 
18   1 Y 1 B GLU 454 ? A GLU 444 
19   1 Y 1 B ALA 455 ? A ALA 445 
20   1 Y 1 K MET 1   ? B MET 1   
21   1 Y 1 K ALA 2   ? B ALA 2   
22   1 Y 1 K GLU 347 ? B GLU 347 
23   1 Y 1 K LYS 348 ? B LYS 348 
24   1 Y 1 K GLU 349 ? B GLU 349 
25   1 Y 1 K LYS 350 ? B LYS 350 
26   1 Y 1 K ASN 351 ? B ASN 351 
27   1 Y 1 K LYS 352 ? B LYS 352 
28   1 Y 1 K ILE 353 ? B ILE 353 
29   1 Y 1 K LEU 354 ? B LEU 354 
30   1 Y 1 K ARG 355 ? B ARG 355 
31   1 Y 1 K ASN 356 ? B ASN 356 
32   1 Y 1 K THR 357 ? B THR 357 
33   1 Y 1 K ILE 358 ? B ILE 358 
34   1 Y 1 K GLN 359 ? B GLN 359 
35   1 Y 1 K TRP 360 ? B TRP 360 
36   1 Y 1 K LEU 361 ? B LEU 361 
37   1 Y 1 K GLU 362 ? B GLU 362 
38   1 Y 1 K ASN 363 ? B ASN 363 
39   1 Y 1 K GLU 364 ? B GLU 364 
40   1 Y 1 K LEU 365 ? B LEU 365 
41   1 Y 1 K ASN 366 ? B ASN 366 
42   1 Y 1 K ARG 367 ? B ARG 367 
43   1 Y 1 K TRP 368 ? B TRP 368 
44   1 Y 1 K ARG 369 ? B ARG 369 
45   1 Y 1 K ASN 370 ? B ASN 370 
46   1 Y 1 K GLY 371 ? B GLY 371 
47   1 Y 1 K GLU 372 ? B GLU 372 
48   1 Y 1 K THR 373 ? B THR 373 
49   1 Y 1 K VAL 374 ? B VAL 374 
50   1 Y 1 K PRO 375 ? B PRO 375 
51   1 Y 1 K ILE 376 ? B ILE 376 
52   1 Y 1 K ASP 377 ? B ASP 377 
53   1 Y 1 K GLU 378 ? B GLU 378 
54   1 Y 1 K GLN 379 ? B GLN 379 
55   1 Y 1 K PHE 380 ? B PHE 380 
56   1 Y 1 K ASP 381 ? B ASP 381 
57   1 Y 1 K LYS 382 ? B LYS 382 
58   1 Y 1 K GLU 383 ? B GLU 383 
59   1 Y 1 K LYS 384 ? B LYS 384 
60   1 Y 1 K ALA 385 ? B ALA 385 
61   1 Y 1 K ASN 386 ? B ASN 386 
62   1 Y 1 K LEU 387 ? B LEU 387 
63   1 Y 1 K GLU 388 ? B GLU 388 
64   1 Y 1 K ALA 389 ? B ALA 389 
65   1 Y 1 K PHE 390 ? B PHE 390 
66   1 Y 1 K THR 391 ? B THR 391 
67   1 Y 1 K VAL 392 ? B VAL 392 
68   1 Y 1 K ASP 393 ? B ASP 393 
69   1 Y 1 K LYS 394 ? B LYS 394 
70   1 Y 1 K ASP 395 ? B ASP 395 
71   1 Y 1 K ILE 396 ? B ILE 396 
72   1 Y 1 K THR 397 ? B THR 397 
73   1 Y 1 K LEU 398 ? B LEU 398 
74   1 Y 1 K THR 399 ? B THR 399 
75   1 Y 1 K ASN 400 ? B ASN 400 
76   1 Y 1 K ASP 401 ? B ASP 401 
77   1 Y 1 K LYS 402 ? B LYS 402 
78   1 Y 1 K PRO 403 ? B PRO 403 
79   1 Y 1 K ALA 404 ? B ALA 404 
80   1 Y 1 K THR 405 ? B THR 405 
81   1 Y 1 K ALA 406 ? B ALA 406 
82   1 Y 1 K ILE 407 ? B ILE 407 
83   1 Y 1 K GLY 408 ? B GLY 408 
84   1 Y 1 K VAL 409 ? B VAL 409 
85   1 Y 1 K ILE 410 ? B ILE 410 
86   1 Y 1 K GLY 411 ? B GLY 411 
87   1 Y 1 K ASN 412 ? B ASN 412 
88   1 Y 1 K PHE 413 ? B PHE 413 
89   1 Y 1 K THR 414 ? B THR 414 
90   1 Y 1 K ASP 415 ? B ASP 415 
91   1 Y 1 K ALA 416 ? B ALA 416 
92   1 Y 1 K GLU 417 ? B GLU 417 
93   1 Y 1 K ARG 418 ? B ARG 418 
94   1 Y 1 K ARG 419 ? B ARG 419 
95   1 Y 1 K LYS 420 ? B LYS 420 
96   1 Y 1 K CYS 421 ? B CYS 421 
97   1 Y 1 K GLU 422 ? B GLU 422 
98   1 Y 1 K GLU 423 ? B GLU 423 
99   1 Y 1 K GLU 424 ? B GLU 424 
100  1 Y 1 K ILE 425 ? B ILE 425 
101  1 Y 1 K ALA 426 ? B ALA 426 
102  1 Y 1 K LYS 427 ? B LYS 427 
103  1 Y 1 K LEU 428 ? B LEU 428 
104  1 Y 1 K TYR 429 ? B TYR 429 
105  1 Y 1 K LYS 430 ? B LYS 430 
106  1 Y 1 K GLN 431 ? B GLN 431 
107  1 Y 1 K LEU 432 ? B LEU 432 
108  1 Y 1 K ASP 433 ? B ASP 433 
109  1 Y 1 K ASP 434 ? B ASP 434 
110  1 Y 1 K LYS 435 ? B LYS 435 
111  1 Y 1 K ASP 436 ? B ASP 436 
112  1 Y 1 K GLU 437 ? B GLU 437 
113  1 Y 1 K GLU 438 ? B GLU 438 
114  1 Y 1 K ILE 439 ? B ILE 439 
115  1 Y 1 K ASN 440 ? B ASN 440 
116  1 Y 1 K GLN 441 ? B GLN 441 
117  1 Y 1 K GLN 442 ? B GLN 442 
118  1 Y 1 K SER 443 ? B SER 443 
119  1 Y 1 K GLN 444 ? B GLN 444 
120  1 Y 1 K LEU 445 ? B LEU 445 
121  1 Y 1 K VAL 446 ? B VAL 446 
122  1 Y 1 K GLU 447 ? B GLU 447 
123  1 Y 1 K LYS 448 ? B LYS 448 
124  1 Y 1 K LEU 449 ? B LEU 449 
125  1 Y 1 K LYS 450 ? B LYS 450 
126  1 Y 1 K THR 451 ? B THR 451 
127  1 Y 1 K GLN 452 ? B GLN 452 
128  1 Y 1 K MET 453 ? B MET 453 
129  1 Y 1 K LEU 454 ? B LEU 454 
130  1 Y 1 K ASP 455 ? B ASP 455 
131  1 Y 1 K GLN 456 ? B GLN 456 
132  1 Y 1 K GLU 457 ? B GLU 457 
133  1 Y 1 K GLU 458 ? B GLU 458 
134  1 Y 1 K LEU 459 ? B LEU 459 
135  1 Y 1 K LEU 460 ? B LEU 460 
136  1 Y 1 K ALA 461 ? B ALA 461 
137  1 Y 1 K SER 462 ? B SER 462 
138  1 Y 1 K THR 463 ? B THR 463 
139  1 Y 1 K ARG 464 ? B ARG 464 
140  1 Y 1 K ARG 465 ? B ARG 465 
141  1 Y 1 K ASP 466 ? B ASP 466 
142  1 Y 1 K GLN 467 ? B GLN 467 
143  1 Y 1 K ASP 468 ? B ASP 468 
144  1 Y 1 K ASN 469 ? B ASN 469 
145  1 Y 1 K MET 470 ? B MET 470 
146  1 Y 1 K GLN 471 ? B GLN 471 
147  1 Y 1 K ALA 472 ? B ALA 472 
148  1 Y 1 K GLU 473 ? B GLU 473 
149  1 Y 1 K LEU 474 ? B LEU 474 
150  1 Y 1 K ASN 475 ? B ASN 475 
151  1 Y 1 K ARG 476 ? B ARG 476 
152  1 Y 1 K LEU 477 ? B LEU 477 
153  1 Y 1 K GLN 478 ? B GLN 478 
154  1 Y 1 K ALA 479 ? B ALA 479 
155  1 Y 1 K GLU 480 ? B GLU 480 
156  1 Y 1 K ASN 481 ? B ASN 481 
157  1 Y 1 K ASP 482 ? B ASP 482 
158  1 Y 1 K ALA 483 ? B ALA 483 
159  1 Y 1 K SER 484 ? B SER 484 
160  1 Y 1 K LYS 485 ? B LYS 485 
161  1 Y 1 K GLU 486 ? B GLU 486 
162  1 Y 1 K GLU 487 ? B GLU 487 
163  1 Y 1 K VAL 488 ? B VAL 488 
164  1 Y 1 K LYS 489 ? B LYS 489 
165  1 Y 1 K GLU 490 ? B GLU 490 
166  1 Y 1 K VAL 491 ? B VAL 491 
167  1 Y 1 K LEU 492 ? B LEU 492 
168  1 Y 1 K GLN 493 ? B GLN 493 
169  1 Y 1 K ALA 494 ? B ALA 494 
170  1 Y 1 K LEU 495 ? B LEU 495 
171  1 Y 1 K GLU 496 ? B GLU 496 
172  1 Y 1 K GLU 497 ? B GLU 497 
173  1 Y 1 K LEU 498 ? B LEU 498 
174  1 Y 1 K ALA 499 ? B ALA 499 
175  1 Y 1 K VAL 500 ? B VAL 500 
176  1 Y 1 K ASN 501 ? B ASN 501 
177  1 Y 1 K TYR 502 ? B TYR 502 
178  1 Y 1 K ASP 503 ? B ASP 503 
179  1 Y 1 K GLN 504 ? B GLN 504 
180  1 Y 1 K LYS 505 ? B LYS 505 
181  1 Y 1 K SER 506 ? B SER 506 
182  1 Y 1 K GLN 507 ? B GLN 507 
183  1 Y 1 K GLU 508 ? B GLU 508 
184  1 Y 1 K VAL 509 ? B VAL 509 
185  1 Y 1 K GLU 510 ? B GLU 510 
186  1 Y 1 K ASP 511 ? B ASP 511 
187  1 Y 1 K LYS 512 ? B LYS 512 
188  1 Y 1 K THR 513 ? B THR 513 
189  1 Y 1 K LYS 514 ? B LYS 514 
190  1 Y 1 K GLU 515 ? B GLU 515 
191  1 Y 1 K TYR 516 ? B TYR 516 
192  1 Y 1 K GLU 517 ? B GLU 517 
193  1 Y 1 K LEU 518 ? B LEU 518 
194  1 Y 1 K LEU 519 ? B LEU 519 
195  1 Y 1 K SER 520 ? B SER 520 
196  1 Y 1 K ASP 521 ? B ASP 521 
197  1 Y 1 K GLU 522 ? B GLU 522 
198  1 Y 1 K LEU 523 ? B LEU 523 
199  1 Y 1 K ASN 524 ? B ASN 524 
200  1 Y 1 K GLN 525 ? B GLN 525 
201  1 Y 1 K LYS 526 ? B LYS 526 
202  1 Y 1 K SER 527 ? B SER 527 
203  1 Y 1 K ALA 528 ? B ALA 528 
204  1 Y 1 K THR 529 ? B THR 529 
205  1 Y 1 K LEU 530 ? B LEU 530 
206  1 Y 1 K ALA 531 ? B ALA 531 
207  1 Y 1 K SER 532 ? B SER 532 
208  1 Y 1 K ILE 533 ? B ILE 533 
209  1 Y 1 K ASP 534 ? B ASP 534 
210  1 Y 1 K ALA 535 ? B ALA 535 
211  1 Y 1 K GLU 536 ? B GLU 536 
212  1 Y 1 K LEU 537 ? B LEU 537 
213  1 Y 1 K GLN 538 ? B GLN 538 
214  1 Y 1 K LYS 539 ? B LYS 539 
215  1 Y 1 K LEU 540 ? B LEU 540 
216  1 Y 1 K LYS 541 ? B LYS 541 
217  1 Y 1 K GLU 542 ? B GLU 542 
218  1 Y 1 K MET 543 ? B MET 543 
219  1 Y 1 K THR 544 ? B THR 544 
220  1 Y 1 K ASN 545 ? B ASN 545 
221  1 Y 1 K HIS 546 ? B HIS 546 
222  1 Y 1 K GLN 547 ? B GLN 547 
223  1 Y 1 K LYS 548 ? B LYS 548 
224  1 Y 1 K LYS 549 ? B LYS 549 
225  1 Y 1 K ARG 550 ? B ARG 550 
226  1 Y 1 K ALA 551 ? B ALA 551 
227  1 Y 1 K ALA 552 ? B ALA 552 
228  1 Y 1 K GLU 553 ? B GLU 553 
229  1 Y 1 K MET 554 ? B MET 554 
230  1 Y 1 K MET 555 ? B MET 555 
231  1 Y 1 K ALA 556 ? B ALA 556 
232  1 Y 1 K SER 557 ? B SER 557 
233  1 Y 1 K LEU 558 ? B LEU 558 
234  1 Y 1 K LEU 559 ? B LEU 559 
235  1 Y 1 K LYS 560 ? B LYS 560 
236  1 Y 1 K ASP 561 ? B ASP 561 
237  1 Y 1 K LEU 562 ? B LEU 562 
238  1 Y 1 K ALA 563 ? B ALA 563 
239  1 Y 1 K GLU 564 ? B GLU 564 
240  1 Y 1 K ILE 565 ? B ILE 565 
241  1 Y 1 K GLY 566 ? B GLY 566 
242  1 Y 1 K ILE 567 ? B ILE 567 
243  1 Y 1 K ALA 568 ? B ALA 568 
244  1 Y 1 K VAL 569 ? B VAL 569 
245  1 Y 1 K GLY 570 ? B GLY 570 
246  1 Y 1 K ASN 571 ? B ASN 571 
247  1 Y 1 K ASN 572 ? B ASN 572 
248  1 Y 1 K ASP 573 ? B ASP 573 
249  1 Y 1 K VAL 574 ? B VAL 574 
250  1 Y 1 K LYS 575 ? B LYS 575 
251  1 Y 1 K GLN 576 ? B GLN 576 
252  1 Y 1 K PRO 577 ? B PRO 577 
253  1 Y 1 K GLU 578 ? B GLU 578 
254  1 Y 1 K GLY 579 ? B GLY 579 
255  1 Y 1 K THR 580 ? B THR 580 
256  1 Y 1 K GLY 581 ? B GLY 581 
257  1 Y 1 K MET 582 ? B MET 582 
258  1 Y 1 K ILE 583 ? B ILE 583 
259  1 Y 1 K ASP 584 ? B ASP 584 
260  1 Y 1 K GLU 585 ? B GLU 585 
261  1 Y 1 K GLU 586 ? B GLU 586 
262  1 Y 1 K PHE 587 ? B PHE 587 
263  1 Y 1 K THR 588 ? B THR 588 
264  1 Y 1 K VAL 589 ? B VAL 589 
265  1 Y 1 K ALA 590 ? B ALA 590 
266  1 Y 1 K ARG 591 ? B ARG 591 
267  1 Y 1 K LEU 592 ? B LEU 592 
268  1 Y 1 K TYR 593 ? B TYR 593 
269  1 Y 1 K ILE 594 ? B ILE 594 
270  1 Y 1 K SER 595 ? B SER 595 
271  1 Y 1 K LYS 596 ? B LYS 596 
272  1 Y 1 K MET 597 ? B MET 597 
273  1 Y 1 K LYS 598 ? B LYS 598 
274  1 Y 1 K SER 599 ? B SER 599 
275  1 Y 1 K GLU 600 ? B GLU 600 
276  1 Y 1 K VAL 601 ? B VAL 601 
277  1 Y 1 K LYS 602 ? B LYS 602 
278  1 Y 1 K THR 603 ? B THR 603 
279  1 Y 1 K MET 604 ? B MET 604 
280  1 Y 1 K VAL 605 ? B VAL 605 
281  1 Y 1 K LYS 606 ? B LYS 606 
282  1 Y 1 K ARG 607 ? B ARG 607 
283  1 Y 1 K CYS 608 ? B CYS 608 
284  1 Y 1 K LYS 609 ? B LYS 609 
285  1 Y 1 K GLN 610 ? B GLN 610 
286  1 Y 1 K LEU 611 ? B LEU 611 
287  1 Y 1 K GLU 612 ? B GLU 612 
288  1 Y 1 K SER 613 ? B SER 613 
289  1 Y 1 K THR 614 ? B THR 614 
290  1 Y 1 K GLN 615 ? B GLN 615 
291  1 Y 1 K THR 616 ? B THR 616 
292  1 Y 1 K GLU 617 ? B GLU 617 
293  1 Y 1 K SER 618 ? B SER 618 
294  1 Y 1 K ASN 619 ? B ASN 619 
295  1 Y 1 K LYS 620 ? B LYS 620 
296  1 Y 1 K LYS 621 ? B LYS 621 
297  1 Y 1 K MET 622 ? B MET 622 
298  1 Y 1 K GLU 623 ? B GLU 623 
299  1 Y 1 K GLU 624 ? B GLU 624 
300  1 Y 1 K ASN 625 ? B ASN 625 
301  1 Y 1 K GLU 626 ? B GLU 626 
302  1 Y 1 K LYS 627 ? B LYS 627 
303  1 Y 1 K GLU 628 ? B GLU 628 
304  1 Y 1 K LEU 629 ? B LEU 629 
305  1 Y 1 K ALA 630 ? B ALA 630 
306  1 Y 1 K ALA 631 ? B ALA 631 
307  1 Y 1 K CYS 632 ? B CYS 632 
308  1 Y 1 K GLN 633 ? B GLN 633 
309  1 Y 1 K LEU 634 ? B LEU 634 
310  1 Y 1 K ARG 635 ? B ARG 635 
311  1 Y 1 K ILE 636 ? B ILE 636 
312  1 Y 1 K SER 637 ? B SER 637 
313  1 Y 1 K GLN 638 ? B GLN 638 
314  1 Y 1 K HIS 639 ? B HIS 639 
315  1 Y 1 K GLU 640 ? B GLU 640 
316  1 Y 1 K ALA 641 ? B ALA 641 
317  1 Y 1 K LYS 642 ? B LYS 642 
318  1 Y 1 K ILE 643 ? B ILE 643 
319  1 Y 1 K LYS 644 ? B LYS 644 
320  1 Y 1 K SER 645 ? B SER 645 
321  1 Y 1 K LEU 646 ? B LEU 646 
322  1 Y 1 K THR 647 ? B THR 647 
323  1 Y 1 K GLU 648 ? B GLU 648 
324  1 Y 1 K TYR 649 ? B TYR 649 
325  1 Y 1 K LEU 650 ? B LEU 650 
326  1 Y 1 K GLN 651 ? B GLN 651 
327  1 Y 1 K ASN 652 ? B ASN 652 
328  1 Y 1 K VAL 653 ? B VAL 653 
329  1 Y 1 K GLU 654 ? B GLU 654 
330  1 Y 1 K GLN 655 ? B GLN 655 
331  1 Y 1 K LYS 656 ? B LYS 656 
332  1 Y 1 K LYS 657 ? B LYS 657 
333  1 Y 1 K ARG 658 ? B ARG 658 
334  1 Y 1 K GLN 659 ? B GLN 659 
335  1 Y 1 K LEU 660 ? B LEU 660 
336  1 Y 1 K GLU 661 ? B GLU 661 
337  1 Y 1 K GLU 662 ? B GLU 662 
338  1 Y 1 K SER 663 ? B SER 663 
339  1 Y 1 K VAL 664 ? B VAL 664 
340  1 Y 1 K ASP 665 ? B ASP 665 
341  1 Y 1 K ALA 666 ? B ALA 666 
342  1 Y 1 K LEU 667 ? B LEU 667 
343  1 Y 1 K SER 668 ? B SER 668 
344  1 Y 1 K GLU 669 ? B GLU 669 
345  1 Y 1 K GLU 670 ? B GLU 670 
346  1 Y 1 K LEU 671 ? B LEU 671 
347  1 Y 1 K VAL 672 ? B VAL 672 
348  1 Y 1 K GLN 673 ? B GLN 673 
349  1 Y 1 K LEU 674 ? B LEU 674 
350  1 Y 1 K ARG 675 ? B ARG 675 
351  1 Y 1 K ALA 676 ? B ALA 676 
352  1 Y 1 K GLN 677 ? B GLN 677 
353  1 Y 1 K GLU 678 ? B GLU 678 
354  1 Y 1 K LYS 679 ? B LYS 679 
355  1 Y 1 K VAL 680 ? B VAL 680 
356  1 Y 1 K HIS 681 ? B HIS 681 
357  1 Y 1 K GLU 682 ? B GLU 682 
358  1 Y 1 K MET 683 ? B MET 683 
359  1 Y 1 K GLU 684 ? B GLU 684 
360  1 Y 1 K LYS 685 ? B LYS 685 
361  1 Y 1 K GLU 686 ? B GLU 686 
362  1 Y 1 K HIS 687 ? B HIS 687 
363  1 Y 1 K LEU 688 ? B LEU 688 
364  1 Y 1 K ASN 689 ? B ASN 689 
365  1 Y 1 K LYS 690 ? B LYS 690 
366  1 Y 1 K VAL 691 ? B VAL 691 
367  1 Y 1 K GLN 692 ? B GLN 692 
368  1 Y 1 K THR 693 ? B THR 693 
369  1 Y 1 K ALA 694 ? B ALA 694 
370  1 Y 1 K ASN 695 ? B ASN 695 
371  1 Y 1 K GLU 696 ? B GLU 696 
372  1 Y 1 K VAL 697 ? B VAL 697 
373  1 Y 1 K LYS 698 ? B LYS 698 
374  1 Y 1 K GLN 699 ? B GLN 699 
375  1 Y 1 K ALA 700 ? B ALA 700 
376  1 Y 1 K VAL 701 ? B VAL 701 
377  1 Y 1 K GLU 702 ? B GLU 702 
378  1 Y 1 K GLN 703 ? B GLN 703 
379  1 Y 1 K GLN 704 ? B GLN 704 
380  1 Y 1 K ILE 705 ? B ILE 705 
381  1 Y 1 K GLN 706 ? B GLN 706 
382  1 Y 1 K SER 707 ? B SER 707 
383  1 Y 1 K HIS 708 ? B HIS 708 
384  1 Y 1 K ARG 709 ? B ARG 709 
385  1 Y 1 K GLU 710 ? B GLU 710 
386  1 Y 1 K THR 711 ? B THR 711 
387  1 Y 1 K HIS 712 ? B HIS 712 
388  1 Y 1 K GLN 713 ? B GLN 713 
389  1 Y 1 K LYS 714 ? B LYS 714 
390  1 Y 1 K GLN 715 ? B GLN 715 
391  1 Y 1 K ILE 716 ? B ILE 716 
392  1 Y 1 K SER 717 ? B SER 717 
393  1 Y 1 K SER 718 ? B SER 718 
394  1 Y 1 K LEU 719 ? B LEU 719 
395  1 Y 1 K ARG 720 ? B ARG 720 
396  1 Y 1 K ASP 721 ? B ASP 721 
397  1 Y 1 K GLU 722 ? B GLU 722 
398  1 Y 1 K VAL 723 ? B VAL 723 
399  1 Y 1 K GLU 724 ? B GLU 724 
400  1 Y 1 K ALA 725 ? B ALA 725 
401  1 Y 1 K LYS 726 ? B LYS 726 
402  1 Y 1 K ALA 727 ? B ALA 727 
403  1 Y 1 K LYS 728 ? B LYS 728 
404  1 Y 1 K LEU 729 ? B LEU 729 
405  1 Y 1 K ILE 730 ? B ILE 730 
406  1 Y 1 K THR 731 ? B THR 731 
407  1 Y 1 K ASP 732 ? B ASP 732 
408  1 Y 1 K LEU 733 ? B LEU 733 
409  1 Y 1 K GLN 734 ? B GLN 734 
410  1 Y 1 K ASP 735 ? B ASP 735 
411  1 Y 1 K GLN 736 ? B GLN 736 
412  1 Y 1 K ASN 737 ? B ASN 737 
413  1 Y 1 K GLN 738 ? B GLN 738 
414  1 Y 1 K LYS 739 ? B LYS 739 
415  1 Y 1 K MET 740 ? B MET 740 
416  1 Y 1 K MET 741 ? B MET 741 
417  1 Y 1 K LEU 742 ? B LEU 742 
418  1 Y 1 K GLU 743 ? B GLU 743 
419  1 Y 1 K GLN 744 ? B GLN 744 
420  1 Y 1 K GLU 745 ? B GLU 745 
421  1 Y 1 K ARG 746 ? B ARG 746 
422  1 Y 1 K LEU 747 ? B LEU 747 
423  1 Y 1 K ARG 748 ? B ARG 748 
424  1 Y 1 K VAL 749 ? B VAL 749 
425  1 Y 1 K GLU 750 ? B GLU 750 
426  1 Y 1 K HIS 751 ? B HIS 751 
427  1 Y 1 K GLU 752 ? B GLU 752 
428  1 Y 1 K LYS 753 ? B LYS 753 
429  1 Y 1 K LEU 754 ? B LEU 754 
430  1 Y 1 K LYS 755 ? B LYS 755 
431  1 Y 1 K ALA 756 ? B ALA 756 
432  1 Y 1 K THR 757 ? B THR 757 
433  1 Y 1 K ASP 758 ? B ASP 758 
434  1 Y 1 K GLN 759 ? B GLN 759 
435  1 Y 1 K GLU 760 ? B GLU 760 
436  1 Y 1 K LYS 761 ? B LYS 761 
437  1 Y 1 K SER 762 ? B SER 762 
438  1 Y 1 K ARG 763 ? B ARG 763 
439  1 Y 1 K LYS 764 ? B LYS 764 
440  1 Y 1 K LEU 765 ? B LEU 765 
441  1 Y 1 K HIS 766 ? B HIS 766 
442  1 Y 1 K GLU 767 ? B GLU 767 
443  1 Y 1 K LEU 768 ? B LEU 768 
444  1 Y 1 K THR 769 ? B THR 769 
445  1 Y 1 K VAL 770 ? B VAL 770 
446  1 Y 1 K MET 771 ? B MET 771 
447  1 Y 1 K GLN 772 ? B GLN 772 
448  1 Y 1 K ASP 773 ? B ASP 773 
449  1 Y 1 K ARG 774 ? B ARG 774 
450  1 Y 1 K ARG 775 ? B ARG 775 
451  1 Y 1 K GLU 776 ? B GLU 776 
452  1 Y 1 K GLN 777 ? B GLN 777 
453  1 Y 1 K ALA 778 ? B ALA 778 
454  1 Y 1 K ARG 779 ? B ARG 779 
455  1 Y 1 K GLN 780 ? B GLN 780 
456  1 Y 1 K ASP 781 ? B ASP 781 
457  1 Y 1 K LEU 782 ? B LEU 782 
458  1 Y 1 K LYS 783 ? B LYS 783 
459  1 Y 1 K GLY 784 ? B GLY 784 
460  1 Y 1 K LEU 785 ? B LEU 785 
461  1 Y 1 K GLU 786 ? B GLU 786 
462  1 Y 1 K GLU 787 ? B GLU 787 
463  1 Y 1 K THR 788 ? B THR 788 
464  1 Y 1 K VAL 789 ? B VAL 789 
465  1 Y 1 K ALA 790 ? B ALA 790 
466  1 Y 1 K LYS 791 ? B LYS 791 
467  1 Y 1 K GLU 792 ? B GLU 792 
468  1 Y 1 K LEU 793 ? B LEU 793 
469  1 Y 1 K GLN 794 ? B GLN 794 
470  1 Y 1 K THR 795 ? B THR 795 
471  1 Y 1 K LEU 796 ? B LEU 796 
472  1 Y 1 K HIS 797 ? B HIS 797 
473  1 Y 1 K ASN 798 ? B ASN 798 
474  1 Y 1 K LEU 799 ? B LEU 799 
475  1 Y 1 K ARG 800 ? B ARG 800 
476  1 Y 1 K LYS 801 ? B LYS 801 
477  1 Y 1 K LEU 802 ? B LEU 802 
478  1 Y 1 K PHE 803 ? B PHE 803 
479  1 Y 1 K VAL 804 ? B VAL 804 
480  1 Y 1 K GLN 805 ? B GLN 805 
481  1 Y 1 K ASP 806 ? B ASP 806 
482  1 Y 1 K LEU 807 ? B LEU 807 
483  1 Y 1 K ALA 808 ? B ALA 808 
484  1 Y 1 K THR 809 ? B THR 809 
485  1 Y 1 K ARG 810 ? B ARG 810 
486  1 Y 1 K VAL 811 ? B VAL 811 
487  1 Y 1 K LYS 812 ? B LYS 812 
488  1 Y 1 K LYS 813 ? B LYS 813 
489  1 Y 1 K SER 814 ? B SER 814 
490  1 Y 1 K ALA 815 ? B ALA 815 
491  1 Y 1 K GLU 816 ? B GLU 816 
492  1 Y 1 K ILE 817 ? B ILE 817 
493  1 Y 1 K ASP 818 ? B ASP 818 
494  1 Y 1 K SER 819 ? B SER 819 
495  1 Y 1 K ASP 820 ? B ASP 820 
496  1 Y 1 K ASP 821 ? B ASP 821 
497  1 Y 1 K THR 822 ? B THR 822 
498  1 Y 1 K GLY 823 ? B GLY 823 
499  1 Y 1 K GLY 824 ? B GLY 824 
500  1 Y 1 K SER 825 ? B SER 825 
501  1 Y 1 K ALA 826 ? B ALA 826 
502  1 Y 1 K ALA 827 ? B ALA 827 
503  1 Y 1 K GLN 828 ? B GLN 828 
504  1 Y 1 K LYS 829 ? B LYS 829 
505  1 Y 1 K GLN 830 ? B GLN 830 
506  1 Y 1 K LYS 831 ? B LYS 831 
507  1 Y 1 K ILE 832 ? B ILE 832 
508  1 Y 1 K SER 833 ? B SER 833 
509  1 Y 1 K PHE 834 ? B PHE 834 
510  1 Y 1 K LEU 835 ? B LEU 835 
511  1 Y 1 K GLU 836 ? B GLU 836 
512  1 Y 1 K ASN 837 ? B ASN 837 
513  1 Y 1 K ASN 838 ? B ASN 838 
514  1 Y 1 K LEU 839 ? B LEU 839 
515  1 Y 1 K GLU 840 ? B GLU 840 
516  1 Y 1 K GLN 841 ? B GLN 841 
517  1 Y 1 K LEU 842 ? B LEU 842 
518  1 Y 1 K THR 843 ? B THR 843 
519  1 Y 1 K LYS 844 ? B LYS 844 
520  1 Y 1 K VAL 845 ? B VAL 845 
521  1 Y 1 K HIS 846 ? B HIS 846 
522  1 Y 1 K LYS 847 ? B LYS 847 
523  1 Y 1 K GLN 848 ? B GLN 848 
524  1 Y 1 K LEU 849 ? B LEU 849 
525  1 Y 1 K VAL 850 ? B VAL 850 
526  1 Y 1 K ARG 851 ? B ARG 851 
527  1 Y 1 K ASP 852 ? B ASP 852 
528  1 Y 1 K ASN 853 ? B ASN 853 
529  1 Y 1 K ALA 854 ? B ALA 854 
530  1 Y 1 K ASP 855 ? B ASP 855 
531  1 Y 1 K LEU 856 ? B LEU 856 
532  1 Y 1 K ARG 857 ? B ARG 857 
533  1 Y 1 K CYS 858 ? B CYS 858 
534  1 Y 1 K GLU 859 ? B GLU 859 
535  1 Y 1 K LEU 860 ? B LEU 860 
536  1 Y 1 K PRO 861 ? B PRO 861 
537  1 Y 1 K LYS 862 ? B LYS 862 
538  1 Y 1 K LEU 863 ? B LEU 863 
539  1 Y 1 K GLU 864 ? B GLU 864 
540  1 Y 1 K LYS 865 ? B LYS 865 
541  1 Y 1 K ARG 866 ? B ARG 866 
542  1 Y 1 K LEU 867 ? B LEU 867 
543  1 Y 1 K ARG 868 ? B ARG 868 
544  1 Y 1 K ALA 869 ? B ALA 869 
545  1 Y 1 K THR 870 ? B THR 870 
546  1 Y 1 K ALA 871 ? B ALA 871 
547  1 Y 1 K GLU 872 ? B GLU 872 
548  1 Y 1 K ARG 873 ? B ARG 873 
549  1 Y 1 K VAL 874 ? B VAL 874 
550  1 Y 1 K LYS 875 ? B LYS 875 
551  1 Y 1 K ALA 876 ? B ALA 876 
552  1 Y 1 K LEU 877 ? B LEU 877 
553  1 Y 1 K GLU 878 ? B GLU 878 
554  1 Y 1 K SER 879 ? B SER 879 
555  1 Y 1 K ALA 880 ? B ALA 880 
556  1 Y 1 K LEU 881 ? B LEU 881 
557  1 Y 1 K LYS 882 ? B LYS 882 
558  1 Y 1 K GLU 883 ? B GLU 883 
559  1 Y 1 K ALA 884 ? B ALA 884 
560  1 Y 1 K LYS 885 ? B LYS 885 
561  1 Y 1 K GLU 886 ? B GLU 886 
562  1 Y 1 K ASN 887 ? B ASN 887 
563  1 Y 1 K ALA 888 ? B ALA 888 
564  1 Y 1 K SER 889 ? B SER 889 
565  1 Y 1 K ARG 890 ? B ARG 890 
566  1 Y 1 K ASP 891 ? B ASP 891 
567  1 Y 1 K ARG 892 ? B ARG 892 
568  1 Y 1 K LYS 893 ? B LYS 893 
569  1 Y 1 K ARG 894 ? B ARG 894 
570  1 Y 1 K TYR 895 ? B TYR 895 
571  1 Y 1 K GLN 896 ? B GLN 896 
572  1 Y 1 K GLN 897 ? B GLN 897 
573  1 Y 1 K GLU 898 ? B GLU 898 
574  1 Y 1 K VAL 899 ? B VAL 899 
575  1 Y 1 K ASP 900 ? B ASP 900 
576  1 Y 1 K ARG 901 ? B ARG 901 
577  1 Y 1 K ILE 902 ? B ILE 902 
578  1 Y 1 K LYS 903 ? B LYS 903 
579  1 Y 1 K GLU 904 ? B GLU 904 
580  1 Y 1 K ALA 905 ? B ALA 905 
581  1 Y 1 K VAL 906 ? B VAL 906 
582  1 Y 1 K ARG 907 ? B ARG 907 
583  1 Y 1 K SER 908 ? B SER 908 
584  1 Y 1 K LYS 909 ? B LYS 909 
585  1 Y 1 K ASN 910 ? B ASN 910 
586  1 Y 1 K MET 911 ? B MET 911 
587  1 Y 1 K ALA 912 ? B ALA 912 
588  1 Y 1 K ARG 913 ? B ARG 913 
589  1 Y 1 K ARG 914 ? B ARG 914 
590  1 Y 1 K GLY 915 ? B GLY 915 
591  1 Y 1 K HIS 916 ? B HIS 916 
592  1 Y 1 K SER 917 ? B SER 917 
593  1 Y 1 K ALA 918 ? B ALA 918 
594  1 Y 1 K GLN 919 ? B GLN 919 
595  1 Y 1 K ILE 920 ? B ILE 920 
596  1 Y 1 K ALA 921 ? B ALA 921 
597  1 Y 1 K LYS 922 ? B LYS 922 
598  1 Y 1 K PRO 923 ? B PRO 923 
599  1 Y 1 K ILE 924 ? B ILE 924 
600  1 Y 1 K ARG 925 ? B ARG 925 
601  1 Y 1 K PRO 926 ? B PRO 926 
602  1 Y 1 K GLY 927 ? B GLY 927 
603  1 Y 1 K GLN 928 ? B GLN 928 
604  1 Y 1 K HIS 929 ? B HIS 929 
605  1 Y 1 K PRO 930 ? B PRO 930 
606  1 Y 1 K ALA 931 ? B ALA 931 
607  1 Y 1 K ALA 932 ? B ALA 932 
608  1 Y 1 K SER 933 ? B SER 933 
609  1 Y 1 K PRO 934 ? B PRO 934 
610  1 Y 1 K THR 935 ? B THR 935 
611  1 Y 1 K HIS 936 ? B HIS 936 
612  1 Y 1 K PRO 937 ? B PRO 937 
613  1 Y 1 K SER 938 ? B SER 938 
614  1 Y 1 K ALA 939 ? B ALA 939 
615  1 Y 1 K ILE 940 ? B ILE 940 
616  1 Y 1 K ARG 941 ? B ARG 941 
617  1 Y 1 K GLY 942 ? B GLY 942 
618  1 Y 1 K GLY 943 ? B GLY 943 
619  1 Y 1 K GLY 944 ? B GLY 944 
620  1 Y 1 K ALA 945 ? B ALA 945 
621  1 Y 1 K PHE 946 ? B PHE 946 
622  1 Y 1 K VAL 947 ? B VAL 947 
623  1 Y 1 K GLN 948 ? B GLN 948 
624  1 Y 1 K ASN 949 ? B ASN 949 
625  1 Y 1 K SER 950 ? B SER 950 
626  1 Y 1 K GLN 951 ? B GLN 951 
627  1 Y 1 K PRO 952 ? B PRO 952 
628  1 Y 1 K VAL 953 ? B VAL 953 
629  1 Y 1 K ALA 954 ? B ALA 954 
630  1 Y 1 K VAL 955 ? B VAL 955 
631  1 Y 1 K ARG 956 ? B ARG 956 
632  1 Y 1 K GLY 957 ? B GLY 957 
633  1 Y 1 K GLY 958 ? B GLY 958 
634  1 Y 1 K GLY 959 ? B GLY 959 
635  1 Y 1 K GLY 960 ? B GLY 960 
636  1 Y 1 K LYS 961 ? B LYS 961 
637  1 Y 1 K GLN 962 ? B GLN 962 
638  1 Y 1 K VAL 963 ? B VAL 963 
639  1 Y 1 L MET 1   ? C MET 1   
640  1 Y 1 L ALA 2   ? C ALA 2   
641  1 Y 1 L ASP 3   ? C ASP 3   
642  1 Y 1 L VAL 192 ? C VAL 192 
643  1 Y 1 L ALA 193 ? C ALA 193 
644  1 Y 1 L VAL 194 ? C VAL 194 
645  1 Y 1 L THR 195 ? C THR 195 
646  1 Y 1 L ASN 196 ? C ASN 196 
647  1 Y 1 L MET 197 ? C MET 197 
648  1 Y 1 L ASN 198 ? C ASN 198 
649  1 Y 1 L GLU 199 ? C GLU 199 
650  1 Y 1 L HIS 200 ? C HIS 200 
651  1 Y 1 L SER 201 ? C SER 201 
652  1 Y 1 L VAL 238 ? C VAL 238 
653  1 Y 1 L SER 239 ? C SER 239 
654  1 Y 1 L LYS 240 ? C LYS 240 
655  1 Y 1 L THR 241 ? C THR 241 
656  1 Y 1 L GLY 242 ? C GLY 242 
657  1 Y 1 L ALA 243 ? C ALA 243 
658  1 Y 1 L GLU 244 ? C GLU 244 
659  1 Y 1 L GLY 245 ? C GLY 245 
660  1 Y 1 L ALA 246 ? C ALA 246 
661  1 Y 1 L VAL 247 ? C VAL 247 
662  1 Y 1 L LEU 248 ? C LEU 248 
663  1 Y 1 L ASP 249 ? C ASP 249 
664  1 Y 1 L GLU 250 ? C GLU 250 
665  1 Y 1 L ALA 251 ? C ALA 251 
666  1 Y 1 L LYS 252 ? C LYS 252 
667  1 Y 1 L ASN 253 ? C ASN 253 
668  1 Y 1 L GLU 347 ? C GLU 347 
669  1 Y 1 L LYS 348 ? C LYS 348 
670  1 Y 1 L GLU 349 ? C GLU 349 
671  1 Y 1 L LYS 350 ? C LYS 350 
672  1 Y 1 L ASN 351 ? C ASN 351 
673  1 Y 1 L LYS 352 ? C LYS 352 
674  1 Y 1 L ILE 353 ? C ILE 353 
675  1 Y 1 L LEU 354 ? C LEU 354 
676  1 Y 1 L ARG 355 ? C ARG 355 
677  1 Y 1 L ASN 356 ? C ASN 356 
678  1 Y 1 L THR 357 ? C THR 357 
679  1 Y 1 L ILE 358 ? C ILE 358 
680  1 Y 1 L GLN 359 ? C GLN 359 
681  1 Y 1 L TRP 360 ? C TRP 360 
682  1 Y 1 L LEU 361 ? C LEU 361 
683  1 Y 1 L GLU 362 ? C GLU 362 
684  1 Y 1 L ASN 363 ? C ASN 363 
685  1 Y 1 L GLU 364 ? C GLU 364 
686  1 Y 1 L LEU 365 ? C LEU 365 
687  1 Y 1 L ASN 366 ? C ASN 366 
688  1 Y 1 L ARG 367 ? C ARG 367 
689  1 Y 1 L TRP 368 ? C TRP 368 
690  1 Y 1 L ARG 369 ? C ARG 369 
691  1 Y 1 L ASN 370 ? C ASN 370 
692  1 Y 1 L GLY 371 ? C GLY 371 
693  1 Y 1 L GLU 372 ? C GLU 372 
694  1 Y 1 L THR 373 ? C THR 373 
695  1 Y 1 L VAL 374 ? C VAL 374 
696  1 Y 1 L PRO 375 ? C PRO 375 
697  1 Y 1 L ILE 376 ? C ILE 376 
698  1 Y 1 L ASP 377 ? C ASP 377 
699  1 Y 1 L GLU 378 ? C GLU 378 
700  1 Y 1 L GLN 379 ? C GLN 379 
701  1 Y 1 L PHE 380 ? C PHE 380 
702  1 Y 1 L ASP 381 ? C ASP 381 
703  1 Y 1 L LYS 382 ? C LYS 382 
704  1 Y 1 L GLU 383 ? C GLU 383 
705  1 Y 1 L LYS 384 ? C LYS 384 
706  1 Y 1 L ALA 385 ? C ALA 385 
707  1 Y 1 L ASN 386 ? C ASN 386 
708  1 Y 1 L LEU 387 ? C LEU 387 
709  1 Y 1 L GLU 388 ? C GLU 388 
710  1 Y 1 L ALA 389 ? C ALA 389 
711  1 Y 1 L PHE 390 ? C PHE 390 
712  1 Y 1 L THR 391 ? C THR 391 
713  1 Y 1 L VAL 392 ? C VAL 392 
714  1 Y 1 L ASP 393 ? C ASP 393 
715  1 Y 1 L LYS 394 ? C LYS 394 
716  1 Y 1 L ASP 395 ? C ASP 395 
717  1 Y 1 L ILE 396 ? C ILE 396 
718  1 Y 1 L THR 397 ? C THR 397 
719  1 Y 1 L LEU 398 ? C LEU 398 
720  1 Y 1 L THR 399 ? C THR 399 
721  1 Y 1 L ASN 400 ? C ASN 400 
722  1 Y 1 L ASP 401 ? C ASP 401 
723  1 Y 1 L LYS 402 ? C LYS 402 
724  1 Y 1 L PRO 403 ? C PRO 403 
725  1 Y 1 L ALA 404 ? C ALA 404 
726  1 Y 1 L THR 405 ? C THR 405 
727  1 Y 1 L ALA 406 ? C ALA 406 
728  1 Y 1 L ILE 407 ? C ILE 407 
729  1 Y 1 L GLY 408 ? C GLY 408 
730  1 Y 1 L VAL 409 ? C VAL 409 
731  1 Y 1 L ILE 410 ? C ILE 410 
732  1 Y 1 L GLY 411 ? C GLY 411 
733  1 Y 1 L ASN 412 ? C ASN 412 
734  1 Y 1 L PHE 413 ? C PHE 413 
735  1 Y 1 L THR 414 ? C THR 414 
736  1 Y 1 L ASP 415 ? C ASP 415 
737  1 Y 1 L ALA 416 ? C ALA 416 
738  1 Y 1 L GLU 417 ? C GLU 417 
739  1 Y 1 L ARG 418 ? C ARG 418 
740  1 Y 1 L ARG 419 ? C ARG 419 
741  1 Y 1 L LYS 420 ? C LYS 420 
742  1 Y 1 L CYS 421 ? C CYS 421 
743  1 Y 1 L GLU 422 ? C GLU 422 
744  1 Y 1 L GLU 423 ? C GLU 423 
745  1 Y 1 L GLU 424 ? C GLU 424 
746  1 Y 1 L ILE 425 ? C ILE 425 
747  1 Y 1 L ALA 426 ? C ALA 426 
748  1 Y 1 L LYS 427 ? C LYS 427 
749  1 Y 1 L LEU 428 ? C LEU 428 
750  1 Y 1 L TYR 429 ? C TYR 429 
751  1 Y 1 L LYS 430 ? C LYS 430 
752  1 Y 1 L GLN 431 ? C GLN 431 
753  1 Y 1 L LEU 432 ? C LEU 432 
754  1 Y 1 L ASP 433 ? C ASP 433 
755  1 Y 1 L ASP 434 ? C ASP 434 
756  1 Y 1 L LYS 435 ? C LYS 435 
757  1 Y 1 L ASP 436 ? C ASP 436 
758  1 Y 1 L GLU 437 ? C GLU 437 
759  1 Y 1 L GLU 438 ? C GLU 438 
760  1 Y 1 L ILE 439 ? C ILE 439 
761  1 Y 1 L ASN 440 ? C ASN 440 
762  1 Y 1 L GLN 441 ? C GLN 441 
763  1 Y 1 L GLN 442 ? C GLN 442 
764  1 Y 1 L SER 443 ? C SER 443 
765  1 Y 1 L GLN 444 ? C GLN 444 
766  1 Y 1 L LEU 445 ? C LEU 445 
767  1 Y 1 L VAL 446 ? C VAL 446 
768  1 Y 1 L GLU 447 ? C GLU 447 
769  1 Y 1 L LYS 448 ? C LYS 448 
770  1 Y 1 L LEU 449 ? C LEU 449 
771  1 Y 1 L LYS 450 ? C LYS 450 
772  1 Y 1 L THR 451 ? C THR 451 
773  1 Y 1 L GLN 452 ? C GLN 452 
774  1 Y 1 L MET 453 ? C MET 453 
775  1 Y 1 L LEU 454 ? C LEU 454 
776  1 Y 1 L ASP 455 ? C ASP 455 
777  1 Y 1 L GLN 456 ? C GLN 456 
778  1 Y 1 L GLU 457 ? C GLU 457 
779  1 Y 1 L GLU 458 ? C GLU 458 
780  1 Y 1 L LEU 459 ? C LEU 459 
781  1 Y 1 L LEU 460 ? C LEU 460 
782  1 Y 1 L ALA 461 ? C ALA 461 
783  1 Y 1 L SER 462 ? C SER 462 
784  1 Y 1 L THR 463 ? C THR 463 
785  1 Y 1 L ARG 464 ? C ARG 464 
786  1 Y 1 L ARG 465 ? C ARG 465 
787  1 Y 1 L ASP 466 ? C ASP 466 
788  1 Y 1 L GLN 467 ? C GLN 467 
789  1 Y 1 L ASP 468 ? C ASP 468 
790  1 Y 1 L ASN 469 ? C ASN 469 
791  1 Y 1 L MET 470 ? C MET 470 
792  1 Y 1 L GLN 471 ? C GLN 471 
793  1 Y 1 L ALA 472 ? C ALA 472 
794  1 Y 1 L GLU 473 ? C GLU 473 
795  1 Y 1 L LEU 474 ? C LEU 474 
796  1 Y 1 L ASN 475 ? C ASN 475 
797  1 Y 1 L ARG 476 ? C ARG 476 
798  1 Y 1 L LEU 477 ? C LEU 477 
799  1 Y 1 L GLN 478 ? C GLN 478 
800  1 Y 1 L ALA 479 ? C ALA 479 
801  1 Y 1 L GLU 480 ? C GLU 480 
802  1 Y 1 L ASN 481 ? C ASN 481 
803  1 Y 1 L ASP 482 ? C ASP 482 
804  1 Y 1 L ALA 483 ? C ALA 483 
805  1 Y 1 L SER 484 ? C SER 484 
806  1 Y 1 L LYS 485 ? C LYS 485 
807  1 Y 1 L GLU 486 ? C GLU 486 
808  1 Y 1 L GLU 487 ? C GLU 487 
809  1 Y 1 L VAL 488 ? C VAL 488 
810  1 Y 1 L LYS 489 ? C LYS 489 
811  1 Y 1 L GLU 490 ? C GLU 490 
812  1 Y 1 L VAL 491 ? C VAL 491 
813  1 Y 1 L LEU 492 ? C LEU 492 
814  1 Y 1 L GLN 493 ? C GLN 493 
815  1 Y 1 L ALA 494 ? C ALA 494 
816  1 Y 1 L LEU 495 ? C LEU 495 
817  1 Y 1 L GLU 496 ? C GLU 496 
818  1 Y 1 L GLU 497 ? C GLU 497 
819  1 Y 1 L LEU 498 ? C LEU 498 
820  1 Y 1 L ALA 499 ? C ALA 499 
821  1 Y 1 L VAL 500 ? C VAL 500 
822  1 Y 1 L ASN 501 ? C ASN 501 
823  1 Y 1 L TYR 502 ? C TYR 502 
824  1 Y 1 L ASP 503 ? C ASP 503 
825  1 Y 1 L GLN 504 ? C GLN 504 
826  1 Y 1 L LYS 505 ? C LYS 505 
827  1 Y 1 L SER 506 ? C SER 506 
828  1 Y 1 L GLN 507 ? C GLN 507 
829  1 Y 1 L GLU 508 ? C GLU 508 
830  1 Y 1 L VAL 509 ? C VAL 509 
831  1 Y 1 L GLU 510 ? C GLU 510 
832  1 Y 1 L ASP 511 ? C ASP 511 
833  1 Y 1 L LYS 512 ? C LYS 512 
834  1 Y 1 L THR 513 ? C THR 513 
835  1 Y 1 L LYS 514 ? C LYS 514 
836  1 Y 1 L GLU 515 ? C GLU 515 
837  1 Y 1 L TYR 516 ? C TYR 516 
838  1 Y 1 L GLU 517 ? C GLU 517 
839  1 Y 1 L LEU 518 ? C LEU 518 
840  1 Y 1 L LEU 519 ? C LEU 519 
841  1 Y 1 L SER 520 ? C SER 520 
842  1 Y 1 L ASP 521 ? C ASP 521 
843  1 Y 1 L GLU 522 ? C GLU 522 
844  1 Y 1 L LEU 523 ? C LEU 523 
845  1 Y 1 L ASN 524 ? C ASN 524 
846  1 Y 1 L GLN 525 ? C GLN 525 
847  1 Y 1 L LYS 526 ? C LYS 526 
848  1 Y 1 L SER 527 ? C SER 527 
849  1 Y 1 L ALA 528 ? C ALA 528 
850  1 Y 1 L THR 529 ? C THR 529 
851  1 Y 1 L LEU 530 ? C LEU 530 
852  1 Y 1 L ALA 531 ? C ALA 531 
853  1 Y 1 L SER 532 ? C SER 532 
854  1 Y 1 L ILE 533 ? C ILE 533 
855  1 Y 1 L ASP 534 ? C ASP 534 
856  1 Y 1 L ALA 535 ? C ALA 535 
857  1 Y 1 L GLU 536 ? C GLU 536 
858  1 Y 1 L LEU 537 ? C LEU 537 
859  1 Y 1 L GLN 538 ? C GLN 538 
860  1 Y 1 L LYS 539 ? C LYS 539 
861  1 Y 1 L LEU 540 ? C LEU 540 
862  1 Y 1 L LYS 541 ? C LYS 541 
863  1 Y 1 L GLU 542 ? C GLU 542 
864  1 Y 1 L MET 543 ? C MET 543 
865  1 Y 1 L THR 544 ? C THR 544 
866  1 Y 1 L ASN 545 ? C ASN 545 
867  1 Y 1 L HIS 546 ? C HIS 546 
868  1 Y 1 L GLN 547 ? C GLN 547 
869  1 Y 1 L LYS 548 ? C LYS 548 
870  1 Y 1 L LYS 549 ? C LYS 549 
871  1 Y 1 L ARG 550 ? C ARG 550 
872  1 Y 1 L ALA 551 ? C ALA 551 
873  1 Y 1 L ALA 552 ? C ALA 552 
874  1 Y 1 L GLU 553 ? C GLU 553 
875  1 Y 1 L MET 554 ? C MET 554 
876  1 Y 1 L MET 555 ? C MET 555 
877  1 Y 1 L ALA 556 ? C ALA 556 
878  1 Y 1 L SER 557 ? C SER 557 
879  1 Y 1 L LEU 558 ? C LEU 558 
880  1 Y 1 L LEU 559 ? C LEU 559 
881  1 Y 1 L LYS 560 ? C LYS 560 
882  1 Y 1 L ASP 561 ? C ASP 561 
883  1 Y 1 L LEU 562 ? C LEU 562 
884  1 Y 1 L ALA 563 ? C ALA 563 
885  1 Y 1 L GLU 564 ? C GLU 564 
886  1 Y 1 L ILE 565 ? C ILE 565 
887  1 Y 1 L GLY 566 ? C GLY 566 
888  1 Y 1 L ILE 567 ? C ILE 567 
889  1 Y 1 L ALA 568 ? C ALA 568 
890  1 Y 1 L VAL 569 ? C VAL 569 
891  1 Y 1 L GLY 570 ? C GLY 570 
892  1 Y 1 L ASN 571 ? C ASN 571 
893  1 Y 1 L ASN 572 ? C ASN 572 
894  1 Y 1 L ASP 573 ? C ASP 573 
895  1 Y 1 L VAL 574 ? C VAL 574 
896  1 Y 1 L LYS 575 ? C LYS 575 
897  1 Y 1 L GLN 576 ? C GLN 576 
898  1 Y 1 L PRO 577 ? C PRO 577 
899  1 Y 1 L GLU 578 ? C GLU 578 
900  1 Y 1 L GLY 579 ? C GLY 579 
901  1 Y 1 L THR 580 ? C THR 580 
902  1 Y 1 L GLY 581 ? C GLY 581 
903  1 Y 1 L MET 582 ? C MET 582 
904  1 Y 1 L ILE 583 ? C ILE 583 
905  1 Y 1 L ASP 584 ? C ASP 584 
906  1 Y 1 L GLU 585 ? C GLU 585 
907  1 Y 1 L GLU 586 ? C GLU 586 
908  1 Y 1 L PHE 587 ? C PHE 587 
909  1 Y 1 L THR 588 ? C THR 588 
910  1 Y 1 L VAL 589 ? C VAL 589 
911  1 Y 1 L ALA 590 ? C ALA 590 
912  1 Y 1 L ARG 591 ? C ARG 591 
913  1 Y 1 L LEU 592 ? C LEU 592 
914  1 Y 1 L TYR 593 ? C TYR 593 
915  1 Y 1 L ILE 594 ? C ILE 594 
916  1 Y 1 L SER 595 ? C SER 595 
917  1 Y 1 L LYS 596 ? C LYS 596 
918  1 Y 1 L MET 597 ? C MET 597 
919  1 Y 1 L LYS 598 ? C LYS 598 
920  1 Y 1 L SER 599 ? C SER 599 
921  1 Y 1 L GLU 600 ? C GLU 600 
922  1 Y 1 L VAL 601 ? C VAL 601 
923  1 Y 1 L LYS 602 ? C LYS 602 
924  1 Y 1 L THR 603 ? C THR 603 
925  1 Y 1 L MET 604 ? C MET 604 
926  1 Y 1 L VAL 605 ? C VAL 605 
927  1 Y 1 L LYS 606 ? C LYS 606 
928  1 Y 1 L ARG 607 ? C ARG 607 
929  1 Y 1 L CYS 608 ? C CYS 608 
930  1 Y 1 L LYS 609 ? C LYS 609 
931  1 Y 1 L GLN 610 ? C GLN 610 
932  1 Y 1 L LEU 611 ? C LEU 611 
933  1 Y 1 L GLU 612 ? C GLU 612 
934  1 Y 1 L SER 613 ? C SER 613 
935  1 Y 1 L THR 614 ? C THR 614 
936  1 Y 1 L GLN 615 ? C GLN 615 
937  1 Y 1 L THR 616 ? C THR 616 
938  1 Y 1 L GLU 617 ? C GLU 617 
939  1 Y 1 L SER 618 ? C SER 618 
940  1 Y 1 L ASN 619 ? C ASN 619 
941  1 Y 1 L LYS 620 ? C LYS 620 
942  1 Y 1 L LYS 621 ? C LYS 621 
943  1 Y 1 L MET 622 ? C MET 622 
944  1 Y 1 L GLU 623 ? C GLU 623 
945  1 Y 1 L GLU 624 ? C GLU 624 
946  1 Y 1 L ASN 625 ? C ASN 625 
947  1 Y 1 L GLU 626 ? C GLU 626 
948  1 Y 1 L LYS 627 ? C LYS 627 
949  1 Y 1 L GLU 628 ? C GLU 628 
950  1 Y 1 L LEU 629 ? C LEU 629 
951  1 Y 1 L ALA 630 ? C ALA 630 
952  1 Y 1 L ALA 631 ? C ALA 631 
953  1 Y 1 L CYS 632 ? C CYS 632 
954  1 Y 1 L GLN 633 ? C GLN 633 
955  1 Y 1 L LEU 634 ? C LEU 634 
956  1 Y 1 L ARG 635 ? C ARG 635 
957  1 Y 1 L ILE 636 ? C ILE 636 
958  1 Y 1 L SER 637 ? C SER 637 
959  1 Y 1 L GLN 638 ? C GLN 638 
960  1 Y 1 L HIS 639 ? C HIS 639 
961  1 Y 1 L GLU 640 ? C GLU 640 
962  1 Y 1 L ALA 641 ? C ALA 641 
963  1 Y 1 L LYS 642 ? C LYS 642 
964  1 Y 1 L ILE 643 ? C ILE 643 
965  1 Y 1 L LYS 644 ? C LYS 644 
966  1 Y 1 L SER 645 ? C SER 645 
967  1 Y 1 L LEU 646 ? C LEU 646 
968  1 Y 1 L THR 647 ? C THR 647 
969  1 Y 1 L GLU 648 ? C GLU 648 
970  1 Y 1 L TYR 649 ? C TYR 649 
971  1 Y 1 L LEU 650 ? C LEU 650 
972  1 Y 1 L GLN 651 ? C GLN 651 
973  1 Y 1 L ASN 652 ? C ASN 652 
974  1 Y 1 L VAL 653 ? C VAL 653 
975  1 Y 1 L GLU 654 ? C GLU 654 
976  1 Y 1 L GLN 655 ? C GLN 655 
977  1 Y 1 L LYS 656 ? C LYS 656 
978  1 Y 1 L LYS 657 ? C LYS 657 
979  1 Y 1 L ARG 658 ? C ARG 658 
980  1 Y 1 L GLN 659 ? C GLN 659 
981  1 Y 1 L LEU 660 ? C LEU 660 
982  1 Y 1 L GLU 661 ? C GLU 661 
983  1 Y 1 L GLU 662 ? C GLU 662 
984  1 Y 1 L SER 663 ? C SER 663 
985  1 Y 1 L VAL 664 ? C VAL 664 
986  1 Y 1 L ASP 665 ? C ASP 665 
987  1 Y 1 L ALA 666 ? C ALA 666 
988  1 Y 1 L LEU 667 ? C LEU 667 
989  1 Y 1 L SER 668 ? C SER 668 
990  1 Y 1 L GLU 669 ? C GLU 669 
991  1 Y 1 L GLU 670 ? C GLU 670 
992  1 Y 1 L LEU 671 ? C LEU 671 
993  1 Y 1 L VAL 672 ? C VAL 672 
994  1 Y 1 L GLN 673 ? C GLN 673 
995  1 Y 1 L LEU 674 ? C LEU 674 
996  1 Y 1 L ARG 675 ? C ARG 675 
997  1 Y 1 L ALA 676 ? C ALA 676 
998  1 Y 1 L GLN 677 ? C GLN 677 
999  1 Y 1 L GLU 678 ? C GLU 678 
1000 1 Y 1 L LYS 679 ? C LYS 679 
1001 1 Y 1 L VAL 680 ? C VAL 680 
1002 1 Y 1 L HIS 681 ? C HIS 681 
1003 1 Y 1 L GLU 682 ? C GLU 682 
1004 1 Y 1 L MET 683 ? C MET 683 
1005 1 Y 1 L GLU 684 ? C GLU 684 
1006 1 Y 1 L LYS 685 ? C LYS 685 
1007 1 Y 1 L GLU 686 ? C GLU 686 
1008 1 Y 1 L HIS 687 ? C HIS 687 
1009 1 Y 1 L LEU 688 ? C LEU 688 
1010 1 Y 1 L ASN 689 ? C ASN 689 
1011 1 Y 1 L LYS 690 ? C LYS 690 
1012 1 Y 1 L VAL 691 ? C VAL 691 
1013 1 Y 1 L GLN 692 ? C GLN 692 
1014 1 Y 1 L THR 693 ? C THR 693 
1015 1 Y 1 L ALA 694 ? C ALA 694 
1016 1 Y 1 L ASN 695 ? C ASN 695 
1017 1 Y 1 L GLU 696 ? C GLU 696 
1018 1 Y 1 L VAL 697 ? C VAL 697 
1019 1 Y 1 L LYS 698 ? C LYS 698 
1020 1 Y 1 L GLN 699 ? C GLN 699 
1021 1 Y 1 L ALA 700 ? C ALA 700 
1022 1 Y 1 L VAL 701 ? C VAL 701 
1023 1 Y 1 L GLU 702 ? C GLU 702 
1024 1 Y 1 L GLN 703 ? C GLN 703 
1025 1 Y 1 L GLN 704 ? C GLN 704 
1026 1 Y 1 L ILE 705 ? C ILE 705 
1027 1 Y 1 L GLN 706 ? C GLN 706 
1028 1 Y 1 L SER 707 ? C SER 707 
1029 1 Y 1 L HIS 708 ? C HIS 708 
1030 1 Y 1 L ARG 709 ? C ARG 709 
1031 1 Y 1 L GLU 710 ? C GLU 710 
1032 1 Y 1 L THR 711 ? C THR 711 
1033 1 Y 1 L HIS 712 ? C HIS 712 
1034 1 Y 1 L GLN 713 ? C GLN 713 
1035 1 Y 1 L LYS 714 ? C LYS 714 
1036 1 Y 1 L GLN 715 ? C GLN 715 
1037 1 Y 1 L ILE 716 ? C ILE 716 
1038 1 Y 1 L SER 717 ? C SER 717 
1039 1 Y 1 L SER 718 ? C SER 718 
1040 1 Y 1 L LEU 719 ? C LEU 719 
1041 1 Y 1 L ARG 720 ? C ARG 720 
1042 1 Y 1 L ASP 721 ? C ASP 721 
1043 1 Y 1 L GLU 722 ? C GLU 722 
1044 1 Y 1 L VAL 723 ? C VAL 723 
1045 1 Y 1 L GLU 724 ? C GLU 724 
1046 1 Y 1 L ALA 725 ? C ALA 725 
1047 1 Y 1 L LYS 726 ? C LYS 726 
1048 1 Y 1 L ALA 727 ? C ALA 727 
1049 1 Y 1 L LYS 728 ? C LYS 728 
1050 1 Y 1 L LEU 729 ? C LEU 729 
1051 1 Y 1 L ILE 730 ? C ILE 730 
1052 1 Y 1 L THR 731 ? C THR 731 
1053 1 Y 1 L ASP 732 ? C ASP 732 
1054 1 Y 1 L LEU 733 ? C LEU 733 
1055 1 Y 1 L GLN 734 ? C GLN 734 
1056 1 Y 1 L ASP 735 ? C ASP 735 
1057 1 Y 1 L GLN 736 ? C GLN 736 
1058 1 Y 1 L ASN 737 ? C ASN 737 
1059 1 Y 1 L GLN 738 ? C GLN 738 
1060 1 Y 1 L LYS 739 ? C LYS 739 
1061 1 Y 1 L MET 740 ? C MET 740 
1062 1 Y 1 L MET 741 ? C MET 741 
1063 1 Y 1 L LEU 742 ? C LEU 742 
1064 1 Y 1 L GLU 743 ? C GLU 743 
1065 1 Y 1 L GLN 744 ? C GLN 744 
1066 1 Y 1 L GLU 745 ? C GLU 745 
1067 1 Y 1 L ARG 746 ? C ARG 746 
1068 1 Y 1 L LEU 747 ? C LEU 747 
1069 1 Y 1 L ARG 748 ? C ARG 748 
1070 1 Y 1 L VAL 749 ? C VAL 749 
1071 1 Y 1 L GLU 750 ? C GLU 750 
1072 1 Y 1 L HIS 751 ? C HIS 751 
1073 1 Y 1 L GLU 752 ? C GLU 752 
1074 1 Y 1 L LYS 753 ? C LYS 753 
1075 1 Y 1 L LEU 754 ? C LEU 754 
1076 1 Y 1 L LYS 755 ? C LYS 755 
1077 1 Y 1 L ALA 756 ? C ALA 756 
1078 1 Y 1 L THR 757 ? C THR 757 
1079 1 Y 1 L ASP 758 ? C ASP 758 
1080 1 Y 1 L GLN 759 ? C GLN 759 
1081 1 Y 1 L GLU 760 ? C GLU 760 
1082 1 Y 1 L LYS 761 ? C LYS 761 
1083 1 Y 1 L SER 762 ? C SER 762 
1084 1 Y 1 L ARG 763 ? C ARG 763 
1085 1 Y 1 L LYS 764 ? C LYS 764 
1086 1 Y 1 L LEU 765 ? C LEU 765 
1087 1 Y 1 L HIS 766 ? C HIS 766 
1088 1 Y 1 L GLU 767 ? C GLU 767 
1089 1 Y 1 L LEU 768 ? C LEU 768 
1090 1 Y 1 L THR 769 ? C THR 769 
1091 1 Y 1 L VAL 770 ? C VAL 770 
1092 1 Y 1 L MET 771 ? C MET 771 
1093 1 Y 1 L GLN 772 ? C GLN 772 
1094 1 Y 1 L ASP 773 ? C ASP 773 
1095 1 Y 1 L ARG 774 ? C ARG 774 
1096 1 Y 1 L ARG 775 ? C ARG 775 
1097 1 Y 1 L GLU 776 ? C GLU 776 
1098 1 Y 1 L GLN 777 ? C GLN 777 
1099 1 Y 1 L ALA 778 ? C ALA 778 
1100 1 Y 1 L ARG 779 ? C ARG 779 
1101 1 Y 1 L GLN 780 ? C GLN 780 
1102 1 Y 1 L ASP 781 ? C ASP 781 
1103 1 Y 1 L LEU 782 ? C LEU 782 
1104 1 Y 1 L LYS 783 ? C LYS 783 
1105 1 Y 1 L GLY 784 ? C GLY 784 
1106 1 Y 1 L LEU 785 ? C LEU 785 
1107 1 Y 1 L GLU 786 ? C GLU 786 
1108 1 Y 1 L GLU 787 ? C GLU 787 
1109 1 Y 1 L THR 788 ? C THR 788 
1110 1 Y 1 L VAL 789 ? C VAL 789 
1111 1 Y 1 L ALA 790 ? C ALA 790 
1112 1 Y 1 L LYS 791 ? C LYS 791 
1113 1 Y 1 L GLU 792 ? C GLU 792 
1114 1 Y 1 L LEU 793 ? C LEU 793 
1115 1 Y 1 L GLN 794 ? C GLN 794 
1116 1 Y 1 L THR 795 ? C THR 795 
1117 1 Y 1 L LEU 796 ? C LEU 796 
1118 1 Y 1 L HIS 797 ? C HIS 797 
1119 1 Y 1 L ASN 798 ? C ASN 798 
1120 1 Y 1 L LEU 799 ? C LEU 799 
1121 1 Y 1 L ARG 800 ? C ARG 800 
1122 1 Y 1 L LYS 801 ? C LYS 801 
1123 1 Y 1 L LEU 802 ? C LEU 802 
1124 1 Y 1 L PHE 803 ? C PHE 803 
1125 1 Y 1 L VAL 804 ? C VAL 804 
1126 1 Y 1 L GLN 805 ? C GLN 805 
1127 1 Y 1 L ASP 806 ? C ASP 806 
1128 1 Y 1 L LEU 807 ? C LEU 807 
1129 1 Y 1 L ALA 808 ? C ALA 808 
1130 1 Y 1 L THR 809 ? C THR 809 
1131 1 Y 1 L ARG 810 ? C ARG 810 
1132 1 Y 1 L VAL 811 ? C VAL 811 
1133 1 Y 1 L LYS 812 ? C LYS 812 
1134 1 Y 1 L LYS 813 ? C LYS 813 
1135 1 Y 1 L SER 814 ? C SER 814 
1136 1 Y 1 L ALA 815 ? C ALA 815 
1137 1 Y 1 L GLU 816 ? C GLU 816 
1138 1 Y 1 L ILE 817 ? C ILE 817 
1139 1 Y 1 L ASP 818 ? C ASP 818 
1140 1 Y 1 L SER 819 ? C SER 819 
1141 1 Y 1 L ASP 820 ? C ASP 820 
1142 1 Y 1 L ASP 821 ? C ASP 821 
1143 1 Y 1 L THR 822 ? C THR 822 
1144 1 Y 1 L GLY 823 ? C GLY 823 
1145 1 Y 1 L GLY 824 ? C GLY 824 
1146 1 Y 1 L SER 825 ? C SER 825 
1147 1 Y 1 L ALA 826 ? C ALA 826 
1148 1 Y 1 L ALA 827 ? C ALA 827 
1149 1 Y 1 L GLN 828 ? C GLN 828 
1150 1 Y 1 L LYS 829 ? C LYS 829 
1151 1 Y 1 L GLN 830 ? C GLN 830 
1152 1 Y 1 L LYS 831 ? C LYS 831 
1153 1 Y 1 L ILE 832 ? C ILE 832 
1154 1 Y 1 L SER 833 ? C SER 833 
1155 1 Y 1 L PHE 834 ? C PHE 834 
1156 1 Y 1 L LEU 835 ? C LEU 835 
1157 1 Y 1 L GLU 836 ? C GLU 836 
1158 1 Y 1 L ASN 837 ? C ASN 837 
1159 1 Y 1 L ASN 838 ? C ASN 838 
1160 1 Y 1 L LEU 839 ? C LEU 839 
1161 1 Y 1 L GLU 840 ? C GLU 840 
1162 1 Y 1 L GLN 841 ? C GLN 841 
1163 1 Y 1 L LEU 842 ? C LEU 842 
1164 1 Y 1 L THR 843 ? C THR 843 
1165 1 Y 1 L LYS 844 ? C LYS 844 
1166 1 Y 1 L VAL 845 ? C VAL 845 
1167 1 Y 1 L HIS 846 ? C HIS 846 
1168 1 Y 1 L LYS 847 ? C LYS 847 
1169 1 Y 1 L GLN 848 ? C GLN 848 
1170 1 Y 1 L LEU 849 ? C LEU 849 
1171 1 Y 1 L VAL 850 ? C VAL 850 
1172 1 Y 1 L ARG 851 ? C ARG 851 
1173 1 Y 1 L ASP 852 ? C ASP 852 
1174 1 Y 1 L ASN 853 ? C ASN 853 
1175 1 Y 1 L ALA 854 ? C ALA 854 
1176 1 Y 1 L ASP 855 ? C ASP 855 
1177 1 Y 1 L LEU 856 ? C LEU 856 
1178 1 Y 1 L ARG 857 ? C ARG 857 
1179 1 Y 1 L CYS 858 ? C CYS 858 
1180 1 Y 1 L GLU 859 ? C GLU 859 
1181 1 Y 1 L LEU 860 ? C LEU 860 
1182 1 Y 1 L PRO 861 ? C PRO 861 
1183 1 Y 1 L LYS 862 ? C LYS 862 
1184 1 Y 1 L LEU 863 ? C LEU 863 
1185 1 Y 1 L GLU 864 ? C GLU 864 
1186 1 Y 1 L LYS 865 ? C LYS 865 
1187 1 Y 1 L ARG 866 ? C ARG 866 
1188 1 Y 1 L LEU 867 ? C LEU 867 
1189 1 Y 1 L ARG 868 ? C ARG 868 
1190 1 Y 1 L ALA 869 ? C ALA 869 
1191 1 Y 1 L THR 870 ? C THR 870 
1192 1 Y 1 L ALA 871 ? C ALA 871 
1193 1 Y 1 L GLU 872 ? C GLU 872 
1194 1 Y 1 L ARG 873 ? C ARG 873 
1195 1 Y 1 L VAL 874 ? C VAL 874 
1196 1 Y 1 L LYS 875 ? C LYS 875 
1197 1 Y 1 L ALA 876 ? C ALA 876 
1198 1 Y 1 L LEU 877 ? C LEU 877 
1199 1 Y 1 L GLU 878 ? C GLU 878 
1200 1 Y 1 L SER 879 ? C SER 879 
1201 1 Y 1 L ALA 880 ? C ALA 880 
1202 1 Y 1 L LEU 881 ? C LEU 881 
1203 1 Y 1 L LYS 882 ? C LYS 882 
1204 1 Y 1 L GLU 883 ? C GLU 883 
1205 1 Y 1 L ALA 884 ? C ALA 884 
1206 1 Y 1 L LYS 885 ? C LYS 885 
1207 1 Y 1 L GLU 886 ? C GLU 886 
1208 1 Y 1 L ASN 887 ? C ASN 887 
1209 1 Y 1 L ALA 888 ? C ALA 888 
1210 1 Y 1 L SER 889 ? C SER 889 
1211 1 Y 1 L ARG 890 ? C ARG 890 
1212 1 Y 1 L ASP 891 ? C ASP 891 
1213 1 Y 1 L ARG 892 ? C ARG 892 
1214 1 Y 1 L LYS 893 ? C LYS 893 
1215 1 Y 1 L ARG 894 ? C ARG 894 
1216 1 Y 1 L TYR 895 ? C TYR 895 
1217 1 Y 1 L GLN 896 ? C GLN 896 
1218 1 Y 1 L GLN 897 ? C GLN 897 
1219 1 Y 1 L GLU 898 ? C GLU 898 
1220 1 Y 1 L VAL 899 ? C VAL 899 
1221 1 Y 1 L ASP 900 ? C ASP 900 
1222 1 Y 1 L ARG 901 ? C ARG 901 
1223 1 Y 1 L ILE 902 ? C ILE 902 
1224 1 Y 1 L LYS 903 ? C LYS 903 
1225 1 Y 1 L GLU 904 ? C GLU 904 
1226 1 Y 1 L ALA 905 ? C ALA 905 
1227 1 Y 1 L VAL 906 ? C VAL 906 
1228 1 Y 1 L ARG 907 ? C ARG 907 
1229 1 Y 1 L SER 908 ? C SER 908 
1230 1 Y 1 L LYS 909 ? C LYS 909 
1231 1 Y 1 L ASN 910 ? C ASN 910 
1232 1 Y 1 L MET 911 ? C MET 911 
1233 1 Y 1 L ALA 912 ? C ALA 912 
1234 1 Y 1 L ARG 913 ? C ARG 913 
1235 1 Y 1 L ARG 914 ? C ARG 914 
1236 1 Y 1 L GLY 915 ? C GLY 915 
1237 1 Y 1 L HIS 916 ? C HIS 916 
1238 1 Y 1 L SER 917 ? C SER 917 
1239 1 Y 1 L ALA 918 ? C ALA 918 
1240 1 Y 1 L GLN 919 ? C GLN 919 
1241 1 Y 1 L ILE 920 ? C ILE 920 
1242 1 Y 1 L ALA 921 ? C ALA 921 
1243 1 Y 1 L LYS 922 ? C LYS 922 
1244 1 Y 1 L PRO 923 ? C PRO 923 
1245 1 Y 1 L ILE 924 ? C ILE 924 
1246 1 Y 1 L ARG 925 ? C ARG 925 
1247 1 Y 1 L PRO 926 ? C PRO 926 
1248 1 Y 1 L GLY 927 ? C GLY 927 
1249 1 Y 1 L GLN 928 ? C GLN 928 
1250 1 Y 1 L HIS 929 ? C HIS 929 
1251 1 Y 1 L PRO 930 ? C PRO 930 
1252 1 Y 1 L ALA 931 ? C ALA 931 
1253 1 Y 1 L ALA 932 ? C ALA 932 
1254 1 Y 1 L SER 933 ? C SER 933 
1255 1 Y 1 L PRO 934 ? C PRO 934 
1256 1 Y 1 L THR 935 ? C THR 935 
1257 1 Y 1 L HIS 936 ? C HIS 936 
1258 1 Y 1 L PRO 937 ? C PRO 937 
1259 1 Y 1 L SER 938 ? C SER 938 
1260 1 Y 1 L ALA 939 ? C ALA 939 
1261 1 Y 1 L ILE 940 ? C ILE 940 
1262 1 Y 1 L ARG 941 ? C ARG 941 
1263 1 Y 1 L GLY 942 ? C GLY 942 
1264 1 Y 1 L GLY 943 ? C GLY 943 
1265 1 Y 1 L GLY 944 ? C GLY 944 
1266 1 Y 1 L ALA 945 ? C ALA 945 
1267 1 Y 1 L PHE 946 ? C PHE 946 
1268 1 Y 1 L VAL 947 ? C VAL 947 
1269 1 Y 1 L GLN 948 ? C GLN 948 
1270 1 Y 1 L ASN 949 ? C ASN 949 
1271 1 Y 1 L SER 950 ? C SER 950 
1272 1 Y 1 L GLN 951 ? C GLN 951 
1273 1 Y 1 L PRO 952 ? C PRO 952 
1274 1 Y 1 L VAL 953 ? C VAL 953 
1275 1 Y 1 L ALA 954 ? C ALA 954 
1276 1 Y 1 L VAL 955 ? C VAL 955 
1277 1 Y 1 L ARG 956 ? C ARG 956 
1278 1 Y 1 L GLY 957 ? C GLY 957 
1279 1 Y 1 L GLY 958 ? C GLY 958 
1280 1 Y 1 L GLY 959 ? C GLY 959 
1281 1 Y 1 L GLY 960 ? C GLY 960 
1282 1 Y 1 L LYS 961 ? C LYS 961 
1283 1 Y 1 L GLN 962 ? C GLN 962 
1284 1 Y 1 L VAL 963 ? C VAL 963 
1285 1 Y 1 A SER 38  ? D SER 38  
1286 1 Y 1 A ASP 39  ? D ASP 39  
1287 1 Y 1 A LYS 40  ? D LYS 40  
1288 1 Y 1 A THR 41  ? D THR 41  
1289 1 Y 1 A ILE 42  ? D ILE 42  
1290 1 Y 1 A GLY 43  ? D GLY 43  
1291 1 Y 1 A GLY 44  ? D GLY 44  
1292 1 Y 1 A GLY 45  ? D GLY 45  
1293 1 Y 1 A ASP 46  ? D ASP 46  
1294 1 Y 1 A ASP 438 ? D ASP 438 
1295 1 Y 1 A SER 439 ? D SER 439 
1296 1 Y 1 A VAL 440 ? D VAL 440 
1297 1 Y 1 A GLU 441 ? D GLU 441 
1298 1 Y 1 A GLY 442 ? D GLY 442 
1299 1 Y 1 A GLU 443 ? D GLU 443 
1300 1 Y 1 A GLY 444 ? D GLY 444 
1301 1 Y 1 A GLU 445 ? D GLU 445 
1302 1 Y 1 A GLU 446 ? D GLU 446 
1303 1 Y 1 A GLU 447 ? D GLU 447 
1304 1 Y 1 A GLY 448 ? D GLY 448 
1305 1 Y 1 A GLU 449 ? D GLU 449 
1306 1 Y 1 A GLU 450 ? D GLU 450 
1307 1 Y 1 A TYR 451 ? D TYR 451 
1308 1 Y 1 T MET 1   ? E MET 1   
1309 1 Y 1 T ALA 2   ? E ALA 2   
1310 1 Y 1 T ASP 3   ? E ASP 3   
1311 1 Y 1 T LEU 4   ? E LEU 4   
1312 1 Y 1 T ALA 5   ? E ALA 5   
1313 1 Y 1 T GLU 6   ? E GLU 6   
1314 1 Y 1 T CYS 7   ? E CYS 7   
1315 1 Y 1 T ASN 8   ? E ASN 8   
1316 1 Y 1 T ILE 9   ? E ILE 9   
1317 1 Y 1 T LYS 10  ? E LYS 10  
1318 1 Y 1 T VAL 11  ? E VAL 11  
1319 1 Y 1 T MET 12  ? E MET 12  
1320 1 Y 1 T CYS 13  ? E CYS 13  
1321 1 Y 1 T ARG 14  ? E ARG 14  
1322 1 Y 1 T PHE 15  ? E PHE 15  
1323 1 Y 1 T ARG 16  ? E ARG 16  
1324 1 Y 1 T PRO 17  ? E PRO 17  
1325 1 Y 1 T LEU 18  ? E LEU 18  
1326 1 Y 1 T ASN 19  ? E ASN 19  
1327 1 Y 1 T GLU 20  ? E GLU 20  
1328 1 Y 1 T SER 21  ? E SER 21  
1329 1 Y 1 T GLU 22  ? E GLU 22  
1330 1 Y 1 T VAL 23  ? E VAL 23  
1331 1 Y 1 T ASN 24  ? E ASN 24  
1332 1 Y 1 T ARG 25  ? E ARG 25  
1333 1 Y 1 T GLY 26  ? E GLY 26  
1334 1 Y 1 T ASP 27  ? E ASP 27  
1335 1 Y 1 T LYS 28  ? E LYS 28  
1336 1 Y 1 T TYR 29  ? E TYR 29  
1337 1 Y 1 T ILE 30  ? E ILE 30  
1338 1 Y 1 T ALA 31  ? E ALA 31  
1339 1 Y 1 T LYS 32  ? E LYS 32  
1340 1 Y 1 T PHE 33  ? E PHE 33  
1341 1 Y 1 T GLN 34  ? E GLN 34  
1342 1 Y 1 T GLY 35  ? E GLY 35  
1343 1 Y 1 T GLU 36  ? E GLU 36  
1344 1 Y 1 T ASP 37  ? E ASP 37  
1345 1 Y 1 T THR 38  ? E THR 38  
1346 1 Y 1 T VAL 39  ? E VAL 39  
1347 1 Y 1 T VAL 40  ? E VAL 40  
1348 1 Y 1 T ILE 41  ? E ILE 41  
1349 1 Y 1 T ALA 42  ? E ALA 42  
1350 1 Y 1 T SER 43  ? E SER 43  
1351 1 Y 1 T LYS 44  ? E LYS 44  
1352 1 Y 1 T PRO 45  ? E PRO 45  
1353 1 Y 1 T TYR 46  ? E TYR 46  
1354 1 Y 1 T ALA 47  ? E ALA 47  
1355 1 Y 1 T PHE 48  ? E PHE 48  
1356 1 Y 1 T ASP 49  ? E ASP 49  
1357 1 Y 1 T ARG 50  ? E ARG 50  
1358 1 Y 1 T VAL 51  ? E VAL 51  
1359 1 Y 1 T PHE 52  ? E PHE 52  
1360 1 Y 1 T GLN 53  ? E GLN 53  
1361 1 Y 1 T SER 54  ? E SER 54  
1362 1 Y 1 T SER 55  ? E SER 55  
1363 1 Y 1 T THR 56  ? E THR 56  
1364 1 Y 1 T SER 57  ? E SER 57  
1365 1 Y 1 T GLN 58  ? E GLN 58  
1366 1 Y 1 T GLU 59  ? E GLU 59  
1367 1 Y 1 T GLN 60  ? E GLN 60  
1368 1 Y 1 T VAL 61  ? E VAL 61  
1369 1 Y 1 T TYR 62  ? E TYR 62  
1370 1 Y 1 T ASN 63  ? E ASN 63  
1371 1 Y 1 T ASP 64  ? E ASP 64  
1372 1 Y 1 T CYS 65  ? E CYS 65  
1373 1 Y 1 T ALA 66  ? E ALA 66  
1374 1 Y 1 T LYS 67  ? E LYS 67  
1375 1 Y 1 T LYS 68  ? E LYS 68  
1376 1 Y 1 T ILE 69  ? E ILE 69  
1377 1 Y 1 T VAL 70  ? E VAL 70  
1378 1 Y 1 T LYS 71  ? E LYS 71  
1379 1 Y 1 T ASP 72  ? E ASP 72  
1380 1 Y 1 T VAL 73  ? E VAL 73  
1381 1 Y 1 T LEU 74  ? E LEU 74  
1382 1 Y 1 T GLU 75  ? E GLU 75  
1383 1 Y 1 T GLY 76  ? E GLY 76  
1384 1 Y 1 T TYR 77  ? E TYR 77  
1385 1 Y 1 T ASN 78  ? E ASN 78  
1386 1 Y 1 T GLY 79  ? E GLY 79  
1387 1 Y 1 T THR 80  ? E THR 80  
1388 1 Y 1 T ILE 81  ? E ILE 81  
1389 1 Y 1 T PHE 82  ? E PHE 82  
1390 1 Y 1 T ALA 83  ? E ALA 83  
1391 1 Y 1 T TYR 84  ? E TYR 84  
1392 1 Y 1 T GLY 85  ? E GLY 85  
1393 1 Y 1 T GLN 86  ? E GLN 86  
1394 1 Y 1 T THR 87  ? E THR 87  
1395 1 Y 1 T SER 88  ? E SER 88  
1396 1 Y 1 T SER 89  ? E SER 89  
1397 1 Y 1 T GLY 90  ? E GLY 90  
1398 1 Y 1 T LYS 91  ? E LYS 91  
1399 1 Y 1 T THR 92  ? E THR 92  
1400 1 Y 1 T HIS 93  ? E HIS 93  
1401 1 Y 1 T THR 94  ? E THR 94  
1402 1 Y 1 T MET 95  ? E MET 95  
1403 1 Y 1 T GLU 96  ? E GLU 96  
1404 1 Y 1 T GLY 97  ? E GLY 97  
1405 1 Y 1 T LYS 98  ? E LYS 98  
1406 1 Y 1 T LEU 99  ? E LEU 99  
1407 1 Y 1 T HIS 100 ? E HIS 100 
1408 1 Y 1 T ASP 101 ? E ASP 101 
1409 1 Y 1 T PRO 102 ? E PRO 102 
1410 1 Y 1 T GLU 103 ? E GLU 103 
1411 1 Y 1 T GLY 104 ? E GLY 104 
1412 1 Y 1 T MET 105 ? E MET 105 
1413 1 Y 1 T GLY 106 ? E GLY 106 
1414 1 Y 1 T ILE 107 ? E ILE 107 
1415 1 Y 1 T ILE 108 ? E ILE 108 
1416 1 Y 1 T PRO 109 ? E PRO 109 
1417 1 Y 1 T ARG 110 ? E ARG 110 
1418 1 Y 1 T ILE 111 ? E ILE 111 
1419 1 Y 1 T VAL 112 ? E VAL 112 
1420 1 Y 1 T GLN 113 ? E GLN 113 
1421 1 Y 1 T ASP 114 ? E ASP 114 
1422 1 Y 1 T ILE 115 ? E ILE 115 
1423 1 Y 1 T PHE 116 ? E PHE 116 
1424 1 Y 1 T ASN 117 ? E ASN 117 
1425 1 Y 1 T TYR 118 ? E TYR 118 
1426 1 Y 1 T ILE 119 ? E ILE 119 
1427 1 Y 1 T TYR 120 ? E TYR 120 
1428 1 Y 1 T SER 121 ? E SER 121 
1429 1 Y 1 T MET 122 ? E MET 122 
1430 1 Y 1 T ASP 123 ? E ASP 123 
1431 1 Y 1 T GLU 124 ? E GLU 124 
1432 1 Y 1 T ASN 125 ? E ASN 125 
1433 1 Y 1 T LEU 126 ? E LEU 126 
1434 1 Y 1 T GLU 127 ? E GLU 127 
1435 1 Y 1 T PHE 128 ? E PHE 128 
1436 1 Y 1 T HIS 129 ? E HIS 129 
1437 1 Y 1 T ILE 130 ? E ILE 130 
1438 1 Y 1 T LYS 131 ? E LYS 131 
1439 1 Y 1 T VAL 132 ? E VAL 132 
1440 1 Y 1 T SER 133 ? E SER 133 
1441 1 Y 1 T TYR 134 ? E TYR 134 
1442 1 Y 1 T PHE 135 ? E PHE 135 
1443 1 Y 1 T GLU 136 ? E GLU 136 
1444 1 Y 1 T ILE 137 ? E ILE 137 
1445 1 Y 1 T TYR 138 ? E TYR 138 
1446 1 Y 1 T LEU 139 ? E LEU 139 
1447 1 Y 1 T ASP 140 ? E ASP 140 
1448 1 Y 1 T LYS 141 ? E LYS 141 
1449 1 Y 1 T ILE 142 ? E ILE 142 
1450 1 Y 1 T ARG 143 ? E ARG 143 
1451 1 Y 1 T ASP 144 ? E ASP 144 
1452 1 Y 1 T LEU 145 ? E LEU 145 
1453 1 Y 1 T LEU 146 ? E LEU 146 
1454 1 Y 1 T ASP 147 ? E ASP 147 
1455 1 Y 1 T VAL 148 ? E VAL 148 
1456 1 Y 1 T SER 149 ? E SER 149 
1457 1 Y 1 T LYS 150 ? E LYS 150 
1458 1 Y 1 T THR 151 ? E THR 151 
1459 1 Y 1 T ASN 152 ? E ASN 152 
1460 1 Y 1 T LEU 153 ? E LEU 153 
1461 1 Y 1 T SER 154 ? E SER 154 
1462 1 Y 1 T VAL 155 ? E VAL 155 
1463 1 Y 1 T HIS 156 ? E HIS 156 
1464 1 Y 1 T GLU 157 ? E GLU 157 
1465 1 Y 1 T ASP 158 ? E ASP 158 
1466 1 Y 1 T LYS 159 ? E LYS 159 
1467 1 Y 1 T ASN 160 ? E ASN 160 
1468 1 Y 1 T ARG 161 ? E ARG 161 
1469 1 Y 1 T VAL 162 ? E VAL 162 
1470 1 Y 1 T PRO 163 ? E PRO 163 
1471 1 Y 1 T TYR 164 ? E TYR 164 
1472 1 Y 1 T VAL 165 ? E VAL 165 
1473 1 Y 1 T LYS 166 ? E LYS 166 
1474 1 Y 1 T GLY 167 ? E GLY 167 
1475 1 Y 1 T CYS 168 ? E CYS 168 
1476 1 Y 1 T THR 169 ? E THR 169 
1477 1 Y 1 T GLU 170 ? E GLU 170 
1478 1 Y 1 T ARG 171 ? E ARG 171 
1479 1 Y 1 T PHE 172 ? E PHE 172 
1480 1 Y 1 T VAL 173 ? E VAL 173 
1481 1 Y 1 T CYS 174 ? E CYS 174 
1482 1 Y 1 T SER 175 ? E SER 175 
1483 1 Y 1 T PRO 176 ? E PRO 176 
1484 1 Y 1 T ASP 177 ? E ASP 177 
1485 1 Y 1 T GLU 178 ? E GLU 178 
1486 1 Y 1 T VAL 179 ? E VAL 179 
1487 1 Y 1 T MET 180 ? E MET 180 
1488 1 Y 1 T ASP 181 ? E ASP 181 
1489 1 Y 1 T THR 182 ? E THR 182 
1490 1 Y 1 T ILE 183 ? E ILE 183 
1491 1 Y 1 T ASP 184 ? E ASP 184 
1492 1 Y 1 T GLU 185 ? E GLU 185 
1493 1 Y 1 T GLY 186 ? E GLY 186 
1494 1 Y 1 T LYS 187 ? E LYS 187 
1495 1 Y 1 T SER 188 ? E SER 188 
1496 1 Y 1 T ASN 189 ? E ASN 189 
1497 1 Y 1 T ARG 190 ? E ARG 190 
1498 1 Y 1 T HIS 191 ? E HIS 191 
1499 1 Y 1 T VAL 192 ? E VAL 192 
1500 1 Y 1 T ALA 193 ? E ALA 193 
1501 1 Y 1 T VAL 194 ? E VAL 194 
1502 1 Y 1 T THR 195 ? E THR 195 
1503 1 Y 1 T ASN 196 ? E ASN 196 
1504 1 Y 1 T MET 197 ? E MET 197 
1505 1 Y 1 T ASN 198 ? E ASN 198 
1506 1 Y 1 T GLU 199 ? E GLU 199 
1507 1 Y 1 T HIS 200 ? E HIS 200 
1508 1 Y 1 T SER 201 ? E SER 201 
1509 1 Y 1 T SER 202 ? E SER 202 
1510 1 Y 1 T ARG 203 ? E ARG 203 
1511 1 Y 1 T SER 204 ? E SER 204 
1512 1 Y 1 T HIS 205 ? E HIS 205 
1513 1 Y 1 T SER 206 ? E SER 206 
1514 1 Y 1 T ILE 207 ? E ILE 207 
1515 1 Y 1 T PHE 208 ? E PHE 208 
1516 1 Y 1 T LEU 209 ? E LEU 209 
1517 1 Y 1 T ILE 210 ? E ILE 210 
1518 1 Y 1 T ASN 211 ? E ASN 211 
1519 1 Y 1 T VAL 212 ? E VAL 212 
1520 1 Y 1 T LYS 213 ? E LYS 213 
1521 1 Y 1 T GLN 214 ? E GLN 214 
1522 1 Y 1 T GLU 215 ? E GLU 215 
1523 1 Y 1 T ASN 216 ? E ASN 216 
1524 1 Y 1 T THR 217 ? E THR 217 
1525 1 Y 1 T GLN 218 ? E GLN 218 
1526 1 Y 1 T THR 219 ? E THR 219 
1527 1 Y 1 T GLU 220 ? E GLU 220 
1528 1 Y 1 T GLN 221 ? E GLN 221 
1529 1 Y 1 T LYS 222 ? E LYS 222 
1530 1 Y 1 T LEU 223 ? E LEU 223 
1531 1 Y 1 T SER 224 ? E SER 224 
1532 1 Y 1 T GLY 225 ? E GLY 225 
1533 1 Y 1 T LYS 226 ? E LYS 226 
1534 1 Y 1 T LEU 227 ? E LEU 227 
1535 1 Y 1 T TYR 228 ? E TYR 228 
1536 1 Y 1 T LEU 229 ? E LEU 229 
1537 1 Y 1 T VAL 230 ? E VAL 230 
1538 1 Y 1 T ASP 231 ? E ASP 231 
1539 1 Y 1 T LEU 232 ? E LEU 232 
1540 1 Y 1 T ALA 233 ? E ALA 233 
1541 1 Y 1 T GLY 234 ? E GLY 234 
1542 1 Y 1 T SER 235 ? E SER 235 
1543 1 Y 1 T GLU 236 ? E GLU 236 
1544 1 Y 1 T LYS 237 ? E LYS 237 
1545 1 Y 1 T VAL 238 ? E VAL 238 
1546 1 Y 1 T SER 239 ? E SER 239 
1547 1 Y 1 T LYS 240 ? E LYS 240 
1548 1 Y 1 T THR 241 ? E THR 241 
1549 1 Y 1 T GLY 242 ? E GLY 242 
1550 1 Y 1 T ALA 243 ? E ALA 243 
1551 1 Y 1 T GLU 244 ? E GLU 244 
1552 1 Y 1 T GLY 245 ? E GLY 245 
1553 1 Y 1 T ALA 246 ? E ALA 246 
1554 1 Y 1 T VAL 247 ? E VAL 247 
1555 1 Y 1 T LEU 248 ? E LEU 248 
1556 1 Y 1 T ASP 249 ? E ASP 249 
1557 1 Y 1 T GLU 250 ? E GLU 250 
1558 1 Y 1 T ALA 251 ? E ALA 251 
1559 1 Y 1 T LYS 252 ? E LYS 252 
1560 1 Y 1 T ASN 253 ? E ASN 253 
1561 1 Y 1 T ILE 254 ? E ILE 254 
1562 1 Y 1 T ASN 255 ? E ASN 255 
1563 1 Y 1 T LYS 256 ? E LYS 256 
1564 1 Y 1 T SER 257 ? E SER 257 
1565 1 Y 1 T LEU 258 ? E LEU 258 
1566 1 Y 1 T SER 259 ? E SER 259 
1567 1 Y 1 T ALA 260 ? E ALA 260 
1568 1 Y 1 T LEU 261 ? E LEU 261 
1569 1 Y 1 T GLY 262 ? E GLY 262 
1570 1 Y 1 T ASN 263 ? E ASN 263 
1571 1 Y 1 T VAL 264 ? E VAL 264 
1572 1 Y 1 T ILE 265 ? E ILE 265 
1573 1 Y 1 T SER 266 ? E SER 266 
1574 1 Y 1 T ALA 267 ? E ALA 267 
1575 1 Y 1 T LEU 268 ? E LEU 268 
1576 1 Y 1 T ALA 269 ? E ALA 269 
1577 1 Y 1 T GLU 270 ? E GLU 270 
1578 1 Y 1 T GLY 271 ? E GLY 271 
1579 1 Y 1 T SER 272 ? E SER 272 
1580 1 Y 1 T THR 273 ? E THR 273 
1581 1 Y 1 T TYR 274 ? E TYR 274 
1582 1 Y 1 T VAL 275 ? E VAL 275 
1583 1 Y 1 T PRO 276 ? E PRO 276 
1584 1 Y 1 T TYR 277 ? E TYR 277 
1585 1 Y 1 T ARG 278 ? E ARG 278 
1586 1 Y 1 T ASP 279 ? E ASP 279 
1587 1 Y 1 T SER 280 ? E SER 280 
1588 1 Y 1 T LYS 281 ? E LYS 281 
1589 1 Y 1 T MET 282 ? E MET 282 
1590 1 Y 1 T THR 283 ? E THR 283 
1591 1 Y 1 T ARG 284 ? E ARG 284 
1592 1 Y 1 T ILE 285 ? E ILE 285 
1593 1 Y 1 T LEU 286 ? E LEU 286 
1594 1 Y 1 T GLN 287 ? E GLN 287 
1595 1 Y 1 T ASP 288 ? E ASP 288 
1596 1 Y 1 T SER 289 ? E SER 289 
1597 1 Y 1 T LEU 290 ? E LEU 290 
1598 1 Y 1 T GLY 291 ? E GLY 291 
1599 1 Y 1 T GLY 292 ? E GLY 292 
1600 1 Y 1 T ASN 293 ? E ASN 293 
1601 1 Y 1 T CYS 294 ? E CYS 294 
1602 1 Y 1 T ARG 295 ? E ARG 295 
1603 1 Y 1 T THR 296 ? E THR 296 
1604 1 Y 1 T THR 297 ? E THR 297 
1605 1 Y 1 T ILE 298 ? E ILE 298 
1606 1 Y 1 T VAL 299 ? E VAL 299 
1607 1 Y 1 T ILE 300 ? E ILE 300 
1608 1 Y 1 T CYS 301 ? E CYS 301 
1609 1 Y 1 T CYS 302 ? E CYS 302 
1610 1 Y 1 T SER 303 ? E SER 303 
1611 1 Y 1 T PRO 304 ? E PRO 304 
1612 1 Y 1 T SER 305 ? E SER 305 
1613 1 Y 1 T SER 306 ? E SER 306 
1614 1 Y 1 T TYR 307 ? E TYR 307 
1615 1 Y 1 T ASN 308 ? E ASN 308 
1616 1 Y 1 T GLU 309 ? E GLU 309 
1617 1 Y 1 T SER 310 ? E SER 310 
1618 1 Y 1 T GLU 311 ? E GLU 311 
1619 1 Y 1 T THR 312 ? E THR 312 
1620 1 Y 1 T LYS 313 ? E LYS 313 
1621 1 Y 1 T SER 314 ? E SER 314 
1622 1 Y 1 T THR 315 ? E THR 315 
1623 1 Y 1 T LEU 316 ? E LEU 316 
1624 1 Y 1 T LEU 317 ? E LEU 317 
1625 1 Y 1 T PHE 318 ? E PHE 318 
1626 1 Y 1 T GLY 319 ? E GLY 319 
1627 1 Y 1 T GLN 320 ? E GLN 320 
1628 1 Y 1 T ARG 321 ? E ARG 321 
1629 1 Y 1 T ALA 322 ? E ALA 322 
1630 1 Y 1 T LYS 323 ? E LYS 323 
1631 1 Y 1 T THR 324 ? E THR 324 
1632 1 Y 1 T ILE 325 ? E ILE 325 
1633 1 Y 1 T LYS 326 ? E LYS 326 
1634 1 Y 1 T ASN 327 ? E ASN 327 
1635 1 Y 1 T THR 328 ? E THR 328 
1636 1 Y 1 T VAL 329 ? E VAL 329 
1637 1 Y 1 T CYS 330 ? E CYS 330 
1638 1 Y 1 T VAL 331 ? E VAL 331 
1639 1 Y 1 T ASN 332 ? E ASN 332 
1640 1 Y 1 T VAL 333 ? E VAL 333 
1641 1 Y 1 T GLU 334 ? E GLU 334 
1642 1 Y 1 T LEU 335 ? E LEU 335 
1643 1 Y 1 T THR 336 ? E THR 336 
1644 1 Y 1 T ALA 337 ? E ALA 337 
1645 1 Y 1 T GLU 338 ? E GLU 338 
1646 1 Y 1 T GLN 339 ? E GLN 339 
1647 1 Y 1 T TRP 340 ? E TRP 340 
1648 1 Y 1 T LYS 341 ? E LYS 341 
1649 1 Y 1 T LYS 342 ? E LYS 342 
1650 1 Y 1 T LYS 343 ? E LYS 343 
1651 1 Y 1 T TYR 344 ? E TYR 344 
1652 1 Y 1 T GLU 345 ? E GLU 345 
1653 1 Y 1 T LYS 346 ? E LYS 346 
1654 1 Y 1 T GLU 347 ? E GLU 347 
1655 1 Y 1 T LYS 348 ? E LYS 348 
1656 1 Y 1 T GLU 349 ? E GLU 349 
1657 1 Y 1 T LYS 350 ? E LYS 350 
1658 1 Y 1 T ASN 351 ? E ASN 351 
1659 1 Y 1 T LYS 352 ? E LYS 352 
1660 1 Y 1 T ILE 353 ? E ILE 353 
1661 1 Y 1 T LEU 354 ? E LEU 354 
1662 1 Y 1 T ARG 355 ? E ARG 355 
1663 1 Y 1 T ASN 356 ? E ASN 356 
1664 1 Y 1 T THR 357 ? E THR 357 
1665 1 Y 1 T ILE 358 ? E ILE 358 
1666 1 Y 1 T GLN 359 ? E GLN 359 
1667 1 Y 1 T TRP 360 ? E TRP 360 
1668 1 Y 1 T LEU 361 ? E LEU 361 
1669 1 Y 1 T GLU 362 ? E GLU 362 
1670 1 Y 1 T ASN 363 ? E ASN 363 
1671 1 Y 1 T GLU 364 ? E GLU 364 
1672 1 Y 1 T LEU 365 ? E LEU 365 
1673 1 Y 1 T ASN 366 ? E ASN 366 
1674 1 Y 1 T ARG 367 ? E ARG 367 
1675 1 Y 1 T TRP 368 ? E TRP 368 
1676 1 Y 1 T ARG 369 ? E ARG 369 
1677 1 Y 1 T ASN 370 ? E ASN 370 
1678 1 Y 1 T GLY 371 ? E GLY 371 
1679 1 Y 1 T GLU 372 ? E GLU 372 
1680 1 Y 1 T THR 373 ? E THR 373 
1681 1 Y 1 T VAL 374 ? E VAL 374 
1682 1 Y 1 T PRO 375 ? E PRO 375 
1683 1 Y 1 T ILE 376 ? E ILE 376 
1684 1 Y 1 T ASP 377 ? E ASP 377 
1685 1 Y 1 T GLU 378 ? E GLU 378 
1686 1 Y 1 T GLN 379 ? E GLN 379 
1687 1 Y 1 T PHE 380 ? E PHE 380 
1688 1 Y 1 T ASP 381 ? E ASP 381 
1689 1 Y 1 T LYS 382 ? E LYS 382 
1690 1 Y 1 T GLU 383 ? E GLU 383 
1691 1 Y 1 T LYS 384 ? E LYS 384 
1692 1 Y 1 T ALA 385 ? E ALA 385 
1693 1 Y 1 T ASN 386 ? E ASN 386 
1694 1 Y 1 T LEU 387 ? E LEU 387 
1695 1 Y 1 T GLU 388 ? E GLU 388 
1696 1 Y 1 T ALA 389 ? E ALA 389 
1697 1 Y 1 T PHE 390 ? E PHE 390 
1698 1 Y 1 T THR 391 ? E THR 391 
1699 1 Y 1 T VAL 392 ? E VAL 392 
1700 1 Y 1 T ASP 393 ? E ASP 393 
1701 1 Y 1 T LYS 394 ? E LYS 394 
1702 1 Y 1 T ASP 395 ? E ASP 395 
1703 1 Y 1 T ILE 396 ? E ILE 396 
1704 1 Y 1 T THR 397 ? E THR 397 
1705 1 Y 1 T LEU 398 ? E LEU 398 
1706 1 Y 1 T THR 399 ? E THR 399 
1707 1 Y 1 T ASN 400 ? E ASN 400 
1708 1 Y 1 T ASP 401 ? E ASP 401 
1709 1 Y 1 T LYS 402 ? E LYS 402 
1710 1 Y 1 T PRO 403 ? E PRO 403 
1711 1 Y 1 T ALA 404 ? E ALA 404 
1712 1 Y 1 T THR 405 ? E THR 405 
1713 1 Y 1 T ALA 406 ? E ALA 406 
1714 1 Y 1 T ILE 407 ? E ILE 407 
1715 1 Y 1 T GLY 408 ? E GLY 408 
1716 1 Y 1 T VAL 409 ? E VAL 409 
1717 1 Y 1 T ILE 410 ? E ILE 410 
1718 1 Y 1 T GLY 411 ? E GLY 411 
1719 1 Y 1 T ASN 412 ? E ASN 412 
1720 1 Y 1 T PHE 413 ? E PHE 413 
1721 1 Y 1 T THR 414 ? E THR 414 
1722 1 Y 1 T ASP 415 ? E ASP 415 
1723 1 Y 1 T ALA 416 ? E ALA 416 
1724 1 Y 1 T GLU 417 ? E GLU 417 
1725 1 Y 1 T ARG 418 ? E ARG 418 
1726 1 Y 1 T ARG 419 ? E ARG 419 
1727 1 Y 1 T LYS 420 ? E LYS 420 
1728 1 Y 1 T CYS 421 ? E CYS 421 
1729 1 Y 1 T GLU 422 ? E GLU 422 
1730 1 Y 1 T GLU 423 ? E GLU 423 
1731 1 Y 1 T GLU 424 ? E GLU 424 
1732 1 Y 1 T ILE 425 ? E ILE 425 
1733 1 Y 1 T ALA 426 ? E ALA 426 
1734 1 Y 1 T LYS 427 ? E LYS 427 
1735 1 Y 1 T LEU 428 ? E LEU 428 
1736 1 Y 1 T TYR 429 ? E TYR 429 
1737 1 Y 1 T LYS 430 ? E LYS 430 
1738 1 Y 1 T GLN 431 ? E GLN 431 
1739 1 Y 1 T LEU 432 ? E LEU 432 
1740 1 Y 1 T ASP 433 ? E ASP 433 
1741 1 Y 1 T ASP 434 ? E ASP 434 
1742 1 Y 1 T LYS 435 ? E LYS 435 
1743 1 Y 1 T ASP 436 ? E ASP 436 
1744 1 Y 1 T GLU 437 ? E GLU 437 
1745 1 Y 1 T GLU 438 ? E GLU 438 
1746 1 Y 1 T ILE 439 ? E ILE 439 
1747 1 Y 1 T ASN 440 ? E ASN 440 
1748 1 Y 1 T GLN 441 ? E GLN 441 
1749 1 Y 1 T GLN 442 ? E GLN 442 
1750 1 Y 1 T SER 443 ? E SER 443 
1751 1 Y 1 T GLN 444 ? E GLN 444 
1752 1 Y 1 T LEU 445 ? E LEU 445 
1753 1 Y 1 T VAL 446 ? E VAL 446 
1754 1 Y 1 T GLU 447 ? E GLU 447 
1755 1 Y 1 T LYS 448 ? E LYS 448 
1756 1 Y 1 T LEU 449 ? E LEU 449 
1757 1 Y 1 T LYS 450 ? E LYS 450 
1758 1 Y 1 T THR 451 ? E THR 451 
1759 1 Y 1 T GLN 452 ? E GLN 452 
1760 1 Y 1 T MET 453 ? E MET 453 
1761 1 Y 1 T LEU 454 ? E LEU 454 
1762 1 Y 1 T ASP 455 ? E ASP 455 
1763 1 Y 1 T GLN 456 ? E GLN 456 
1764 1 Y 1 T GLU 457 ? E GLU 457 
1765 1 Y 1 T GLU 458 ? E GLU 458 
1766 1 Y 1 T LEU 459 ? E LEU 459 
1767 1 Y 1 T LEU 460 ? E LEU 460 
1768 1 Y 1 T ALA 461 ? E ALA 461 
1769 1 Y 1 T SER 462 ? E SER 462 
1770 1 Y 1 T THR 463 ? E THR 463 
1771 1 Y 1 T ARG 464 ? E ARG 464 
1772 1 Y 1 T ARG 465 ? E ARG 465 
1773 1 Y 1 T ASP 466 ? E ASP 466 
1774 1 Y 1 T GLN 467 ? E GLN 467 
1775 1 Y 1 T ASP 468 ? E ASP 468 
1776 1 Y 1 T ASN 469 ? E ASN 469 
1777 1 Y 1 T MET 470 ? E MET 470 
1778 1 Y 1 T GLN 471 ? E GLN 471 
1779 1 Y 1 T ALA 472 ? E ALA 472 
1780 1 Y 1 T GLU 473 ? E GLU 473 
1781 1 Y 1 T LEU 474 ? E LEU 474 
1782 1 Y 1 T ASN 475 ? E ASN 475 
1783 1 Y 1 T ARG 476 ? E ARG 476 
1784 1 Y 1 T LEU 477 ? E LEU 477 
1785 1 Y 1 T GLN 478 ? E GLN 478 
1786 1 Y 1 T ALA 479 ? E ALA 479 
1787 1 Y 1 T GLU 480 ? E GLU 480 
1788 1 Y 1 T ASN 481 ? E ASN 481 
1789 1 Y 1 T ASP 482 ? E ASP 482 
1790 1 Y 1 T ALA 483 ? E ALA 483 
1791 1 Y 1 T SER 484 ? E SER 484 
1792 1 Y 1 T LYS 485 ? E LYS 485 
1793 1 Y 1 T GLU 486 ? E GLU 486 
1794 1 Y 1 T GLU 487 ? E GLU 487 
1795 1 Y 1 T VAL 488 ? E VAL 488 
1796 1 Y 1 T LYS 489 ? E LYS 489 
1797 1 Y 1 T GLU 490 ? E GLU 490 
1798 1 Y 1 T VAL 491 ? E VAL 491 
1799 1 Y 1 T LEU 492 ? E LEU 492 
1800 1 Y 1 T GLN 493 ? E GLN 493 
1801 1 Y 1 T ALA 494 ? E ALA 494 
1802 1 Y 1 T LEU 495 ? E LEU 495 
1803 1 Y 1 T GLU 496 ? E GLU 496 
1804 1 Y 1 T GLU 497 ? E GLU 497 
1805 1 Y 1 T LEU 498 ? E LEU 498 
1806 1 Y 1 T ALA 499 ? E ALA 499 
1807 1 Y 1 T VAL 500 ? E VAL 500 
1808 1 Y 1 T ASN 501 ? E ASN 501 
1809 1 Y 1 T TYR 502 ? E TYR 502 
1810 1 Y 1 T ASP 503 ? E ASP 503 
1811 1 Y 1 T GLN 504 ? E GLN 504 
1812 1 Y 1 T LYS 505 ? E LYS 505 
1813 1 Y 1 T SER 506 ? E SER 506 
1814 1 Y 1 T GLN 507 ? E GLN 507 
1815 1 Y 1 T GLU 508 ? E GLU 508 
1816 1 Y 1 T VAL 509 ? E VAL 509 
1817 1 Y 1 T GLU 510 ? E GLU 510 
1818 1 Y 1 T ASP 511 ? E ASP 511 
1819 1 Y 1 T LYS 512 ? E LYS 512 
1820 1 Y 1 T THR 513 ? E THR 513 
1821 1 Y 1 T LYS 514 ? E LYS 514 
1822 1 Y 1 T GLU 515 ? E GLU 515 
1823 1 Y 1 T TYR 516 ? E TYR 516 
1824 1 Y 1 T GLU 517 ? E GLU 517 
1825 1 Y 1 T LEU 518 ? E LEU 518 
1826 1 Y 1 T LEU 519 ? E LEU 519 
1827 1 Y 1 T SER 520 ? E SER 520 
1828 1 Y 1 T ASP 521 ? E ASP 521 
1829 1 Y 1 T GLU 522 ? E GLU 522 
1830 1 Y 1 T LEU 523 ? E LEU 523 
1831 1 Y 1 T ASN 524 ? E ASN 524 
1832 1 Y 1 T GLN 525 ? E GLN 525 
1833 1 Y 1 T LYS 526 ? E LYS 526 
1834 1 Y 1 T SER 527 ? E SER 527 
1835 1 Y 1 T ALA 528 ? E ALA 528 
1836 1 Y 1 T THR 529 ? E THR 529 
1837 1 Y 1 T LEU 530 ? E LEU 530 
1838 1 Y 1 T ALA 531 ? E ALA 531 
1839 1 Y 1 T SER 532 ? E SER 532 
1840 1 Y 1 T ILE 533 ? E ILE 533 
1841 1 Y 1 T ASP 534 ? E ASP 534 
1842 1 Y 1 T ALA 535 ? E ALA 535 
1843 1 Y 1 T GLU 536 ? E GLU 536 
1844 1 Y 1 T LEU 537 ? E LEU 537 
1845 1 Y 1 T GLN 538 ? E GLN 538 
1846 1 Y 1 T LYS 539 ? E LYS 539 
1847 1 Y 1 T LEU 540 ? E LEU 540 
1848 1 Y 1 T LYS 541 ? E LYS 541 
1849 1 Y 1 T GLU 542 ? E GLU 542 
1850 1 Y 1 T MET 543 ? E MET 543 
1851 1 Y 1 T THR 544 ? E THR 544 
1852 1 Y 1 T ASN 545 ? E ASN 545 
1853 1 Y 1 T HIS 546 ? E HIS 546 
1854 1 Y 1 T GLN 547 ? E GLN 547 
1855 1 Y 1 T LYS 548 ? E LYS 548 
1856 1 Y 1 T LYS 549 ? E LYS 549 
1857 1 Y 1 T ARG 550 ? E ARG 550 
1858 1 Y 1 T ALA 551 ? E ALA 551 
1859 1 Y 1 T ALA 552 ? E ALA 552 
1860 1 Y 1 T GLU 553 ? E GLU 553 
1861 1 Y 1 T MET 554 ? E MET 554 
1862 1 Y 1 T MET 555 ? E MET 555 
1863 1 Y 1 T ALA 556 ? E ALA 556 
1864 1 Y 1 T SER 557 ? E SER 557 
1865 1 Y 1 T LEU 558 ? E LEU 558 
1866 1 Y 1 T LEU 559 ? E LEU 559 
1867 1 Y 1 T LYS 560 ? E LYS 560 
1868 1 Y 1 T ASP 561 ? E ASP 561 
1869 1 Y 1 T LEU 562 ? E LEU 562 
1870 1 Y 1 T ALA 563 ? E ALA 563 
1871 1 Y 1 T GLU 564 ? E GLU 564 
1872 1 Y 1 T ILE 565 ? E ILE 565 
1873 1 Y 1 T GLY 566 ? E GLY 566 
1874 1 Y 1 T ILE 567 ? E ILE 567 
1875 1 Y 1 T ALA 568 ? E ALA 568 
1876 1 Y 1 T VAL 569 ? E VAL 569 
1877 1 Y 1 T GLY 570 ? E GLY 570 
1878 1 Y 1 T ASN 571 ? E ASN 571 
1879 1 Y 1 T ASN 572 ? E ASN 572 
1880 1 Y 1 T ASP 573 ? E ASP 573 
1881 1 Y 1 T VAL 574 ? E VAL 574 
1882 1 Y 1 T LYS 575 ? E LYS 575 
1883 1 Y 1 T GLN 576 ? E GLN 576 
1884 1 Y 1 T PRO 577 ? E PRO 577 
1885 1 Y 1 T GLU 578 ? E GLU 578 
1886 1 Y 1 T GLY 579 ? E GLY 579 
1887 1 Y 1 T THR 580 ? E THR 580 
1888 1 Y 1 T GLY 581 ? E GLY 581 
1889 1 Y 1 T MET 582 ? E MET 582 
1890 1 Y 1 T ILE 583 ? E ILE 583 
1891 1 Y 1 T ASP 584 ? E ASP 584 
1892 1 Y 1 T GLU 585 ? E GLU 585 
1893 1 Y 1 T GLU 586 ? E GLU 586 
1894 1 Y 1 T PHE 587 ? E PHE 587 
1895 1 Y 1 T THR 588 ? E THR 588 
1896 1 Y 1 T VAL 589 ? E VAL 589 
1897 1 Y 1 T ALA 590 ? E ALA 590 
1898 1 Y 1 T ARG 591 ? E ARG 591 
1899 1 Y 1 T LEU 592 ? E LEU 592 
1900 1 Y 1 T TYR 593 ? E TYR 593 
1901 1 Y 1 T ILE 594 ? E ILE 594 
1902 1 Y 1 T SER 595 ? E SER 595 
1903 1 Y 1 T LYS 596 ? E LYS 596 
1904 1 Y 1 T MET 597 ? E MET 597 
1905 1 Y 1 T LYS 598 ? E LYS 598 
1906 1 Y 1 T SER 599 ? E SER 599 
1907 1 Y 1 T GLU 600 ? E GLU 600 
1908 1 Y 1 T VAL 601 ? E VAL 601 
1909 1 Y 1 T LYS 602 ? E LYS 602 
1910 1 Y 1 T THR 603 ? E THR 603 
1911 1 Y 1 T MET 604 ? E MET 604 
1912 1 Y 1 T VAL 605 ? E VAL 605 
1913 1 Y 1 T LYS 606 ? E LYS 606 
1914 1 Y 1 T ARG 607 ? E ARG 607 
1915 1 Y 1 T CYS 608 ? E CYS 608 
1916 1 Y 1 T LYS 609 ? E LYS 609 
1917 1 Y 1 T GLN 610 ? E GLN 610 
1918 1 Y 1 T LEU 611 ? E LEU 611 
1919 1 Y 1 T GLU 612 ? E GLU 612 
1920 1 Y 1 T SER 613 ? E SER 613 
1921 1 Y 1 T THR 614 ? E THR 614 
1922 1 Y 1 T GLN 615 ? E GLN 615 
1923 1 Y 1 T THR 616 ? E THR 616 
1924 1 Y 1 T GLU 617 ? E GLU 617 
1925 1 Y 1 T SER 618 ? E SER 618 
1926 1 Y 1 T ASN 619 ? E ASN 619 
1927 1 Y 1 T LYS 620 ? E LYS 620 
1928 1 Y 1 T LYS 621 ? E LYS 621 
1929 1 Y 1 T MET 622 ? E MET 622 
1930 1 Y 1 T GLU 623 ? E GLU 623 
1931 1 Y 1 T GLU 624 ? E GLU 624 
1932 1 Y 1 T ASN 625 ? E ASN 625 
1933 1 Y 1 T GLU 626 ? E GLU 626 
1934 1 Y 1 T LYS 627 ? E LYS 627 
1935 1 Y 1 T GLU 628 ? E GLU 628 
1936 1 Y 1 T LEU 629 ? E LEU 629 
1937 1 Y 1 T ALA 630 ? E ALA 630 
1938 1 Y 1 T ALA 631 ? E ALA 631 
1939 1 Y 1 T CYS 632 ? E CYS 632 
1940 1 Y 1 T GLN 633 ? E GLN 633 
1941 1 Y 1 T LEU 634 ? E LEU 634 
1942 1 Y 1 T ARG 635 ? E ARG 635 
1943 1 Y 1 T ILE 636 ? E ILE 636 
1944 1 Y 1 T SER 637 ? E SER 637 
1945 1 Y 1 T GLN 638 ? E GLN 638 
1946 1 Y 1 T HIS 639 ? E HIS 639 
1947 1 Y 1 T GLU 640 ? E GLU 640 
1948 1 Y 1 T ALA 641 ? E ALA 641 
1949 1 Y 1 T LYS 642 ? E LYS 642 
1950 1 Y 1 T ILE 643 ? E ILE 643 
1951 1 Y 1 T LYS 644 ? E LYS 644 
1952 1 Y 1 T SER 645 ? E SER 645 
1953 1 Y 1 T LEU 646 ? E LEU 646 
1954 1 Y 1 T THR 647 ? E THR 647 
1955 1 Y 1 T GLU 648 ? E GLU 648 
1956 1 Y 1 T TYR 649 ? E TYR 649 
1957 1 Y 1 T LEU 650 ? E LEU 650 
1958 1 Y 1 T GLN 651 ? E GLN 651 
1959 1 Y 1 T ASN 652 ? E ASN 652 
1960 1 Y 1 T VAL 653 ? E VAL 653 
1961 1 Y 1 T GLU 654 ? E GLU 654 
1962 1 Y 1 T GLN 655 ? E GLN 655 
1963 1 Y 1 T LYS 656 ? E LYS 656 
1964 1 Y 1 T LYS 657 ? E LYS 657 
1965 1 Y 1 T ARG 658 ? E ARG 658 
1966 1 Y 1 T GLN 659 ? E GLN 659 
1967 1 Y 1 T LEU 660 ? E LEU 660 
1968 1 Y 1 T GLU 661 ? E GLU 661 
1969 1 Y 1 T GLU 662 ? E GLU 662 
1970 1 Y 1 T SER 663 ? E SER 663 
1971 1 Y 1 T VAL 664 ? E VAL 664 
1972 1 Y 1 T ASP 665 ? E ASP 665 
1973 1 Y 1 T ALA 666 ? E ALA 666 
1974 1 Y 1 T LEU 667 ? E LEU 667 
1975 1 Y 1 T SER 668 ? E SER 668 
1976 1 Y 1 T GLU 669 ? E GLU 669 
1977 1 Y 1 T GLU 670 ? E GLU 670 
1978 1 Y 1 T LEU 671 ? E LEU 671 
1979 1 Y 1 T VAL 672 ? E VAL 672 
1980 1 Y 1 T GLN 673 ? E GLN 673 
1981 1 Y 1 T LEU 674 ? E LEU 674 
1982 1 Y 1 T ARG 675 ? E ARG 675 
1983 1 Y 1 T ALA 676 ? E ALA 676 
1984 1 Y 1 T GLN 677 ? E GLN 677 
1985 1 Y 1 T GLU 678 ? E GLU 678 
1986 1 Y 1 T LYS 679 ? E LYS 679 
1987 1 Y 1 T VAL 680 ? E VAL 680 
1988 1 Y 1 T HIS 681 ? E HIS 681 
1989 1 Y 1 T GLU 682 ? E GLU 682 
1990 1 Y 1 T MET 683 ? E MET 683 
1991 1 Y 1 T GLU 684 ? E GLU 684 
1992 1 Y 1 T LYS 685 ? E LYS 685 
1993 1 Y 1 T GLU 686 ? E GLU 686 
1994 1 Y 1 T HIS 687 ? E HIS 687 
1995 1 Y 1 T LEU 688 ? E LEU 688 
1996 1 Y 1 T ASN 689 ? E ASN 689 
1997 1 Y 1 T LYS 690 ? E LYS 690 
1998 1 Y 1 T VAL 691 ? E VAL 691 
1999 1 Y 1 T GLN 692 ? E GLN 692 
2000 1 Y 1 T THR 693 ? E THR 693 
2001 1 Y 1 T ALA 694 ? E ALA 694 
2002 1 Y 1 T ASN 695 ? E ASN 695 
2003 1 Y 1 T GLU 696 ? E GLU 696 
2004 1 Y 1 T VAL 697 ? E VAL 697 
2005 1 Y 1 T LYS 698 ? E LYS 698 
2006 1 Y 1 T GLN 699 ? E GLN 699 
2007 1 Y 1 T ALA 700 ? E ALA 700 
2008 1 Y 1 T VAL 701 ? E VAL 701 
2009 1 Y 1 T GLU 702 ? E GLU 702 
2010 1 Y 1 T GLN 703 ? E GLN 703 
2011 1 Y 1 T GLN 704 ? E GLN 704 
2012 1 Y 1 T ILE 705 ? E ILE 705 
2013 1 Y 1 T GLN 706 ? E GLN 706 
2014 1 Y 1 T SER 707 ? E SER 707 
2015 1 Y 1 T HIS 708 ? E HIS 708 
2016 1 Y 1 T ARG 709 ? E ARG 709 
2017 1 Y 1 T GLU 710 ? E GLU 710 
2018 1 Y 1 T THR 711 ? E THR 711 
2019 1 Y 1 T HIS 712 ? E HIS 712 
2020 1 Y 1 T GLN 713 ? E GLN 713 
2021 1 Y 1 T LYS 714 ? E LYS 714 
2022 1 Y 1 T GLN 715 ? E GLN 715 
2023 1 Y 1 T ILE 716 ? E ILE 716 
2024 1 Y 1 T SER 717 ? E SER 717 
2025 1 Y 1 T SER 718 ? E SER 718 
2026 1 Y 1 T LEU 719 ? E LEU 719 
2027 1 Y 1 T ARG 720 ? E ARG 720 
2028 1 Y 1 T ASP 721 ? E ASP 721 
2029 1 Y 1 T GLU 722 ? E GLU 722 
2030 1 Y 1 T VAL 723 ? E VAL 723 
2031 1 Y 1 T GLU 724 ? E GLU 724 
2032 1 Y 1 T ALA 725 ? E ALA 725 
2033 1 Y 1 T LYS 726 ? E LYS 726 
2034 1 Y 1 T ALA 727 ? E ALA 727 
2035 1 Y 1 T LYS 728 ? E LYS 728 
2036 1 Y 1 T LEU 729 ? E LEU 729 
2037 1 Y 1 T ILE 730 ? E ILE 730 
2038 1 Y 1 T THR 731 ? E THR 731 
2039 1 Y 1 T ASP 732 ? E ASP 732 
2040 1 Y 1 T LEU 733 ? E LEU 733 
2041 1 Y 1 T GLN 734 ? E GLN 734 
2042 1 Y 1 T ASP 735 ? E ASP 735 
2043 1 Y 1 T GLN 736 ? E GLN 736 
2044 1 Y 1 T ASN 737 ? E ASN 737 
2045 1 Y 1 T GLN 738 ? E GLN 738 
2046 1 Y 1 T LYS 739 ? E LYS 739 
2047 1 Y 1 T MET 740 ? E MET 740 
2048 1 Y 1 T MET 741 ? E MET 741 
2049 1 Y 1 T LEU 742 ? E LEU 742 
2050 1 Y 1 T GLU 743 ? E GLU 743 
2051 1 Y 1 T GLN 744 ? E GLN 744 
2052 1 Y 1 T GLU 745 ? E GLU 745 
2053 1 Y 1 T ARG 746 ? E ARG 746 
2054 1 Y 1 T LEU 747 ? E LEU 747 
2055 1 Y 1 T ARG 748 ? E ARG 748 
2056 1 Y 1 T VAL 749 ? E VAL 749 
2057 1 Y 1 T GLU 750 ? E GLU 750 
2058 1 Y 1 T HIS 751 ? E HIS 751 
2059 1 Y 1 T GLU 752 ? E GLU 752 
2060 1 Y 1 T LYS 753 ? E LYS 753 
2061 1 Y 1 T LEU 754 ? E LEU 754 
2062 1 Y 1 T LYS 755 ? E LYS 755 
2063 1 Y 1 T ALA 756 ? E ALA 756 
2064 1 Y 1 T THR 757 ? E THR 757 
2065 1 Y 1 T ASP 758 ? E ASP 758 
2066 1 Y 1 T GLN 759 ? E GLN 759 
2067 1 Y 1 T GLU 760 ? E GLU 760 
2068 1 Y 1 T LYS 761 ? E LYS 761 
2069 1 Y 1 T SER 762 ? E SER 762 
2070 1 Y 1 T ARG 763 ? E ARG 763 
2071 1 Y 1 T LYS 764 ? E LYS 764 
2072 1 Y 1 T LEU 765 ? E LEU 765 
2073 1 Y 1 T HIS 766 ? E HIS 766 
2074 1 Y 1 T GLU 767 ? E GLU 767 
2075 1 Y 1 T LEU 768 ? E LEU 768 
2076 1 Y 1 T THR 769 ? E THR 769 
2077 1 Y 1 T VAL 770 ? E VAL 770 
2078 1 Y 1 T MET 771 ? E MET 771 
2079 1 Y 1 T GLN 772 ? E GLN 772 
2080 1 Y 1 T ASP 773 ? E ASP 773 
2081 1 Y 1 T ARG 774 ? E ARG 774 
2082 1 Y 1 T ARG 775 ? E ARG 775 
2083 1 Y 1 T GLU 776 ? E GLU 776 
2084 1 Y 1 T GLN 777 ? E GLN 777 
2085 1 Y 1 T ALA 778 ? E ALA 778 
2086 1 Y 1 T ARG 779 ? E ARG 779 
2087 1 Y 1 T GLN 780 ? E GLN 780 
2088 1 Y 1 T ASP 781 ? E ASP 781 
2089 1 Y 1 T LEU 782 ? E LEU 782 
2090 1 Y 1 T LYS 783 ? E LYS 783 
2091 1 Y 1 T GLY 784 ? E GLY 784 
2092 1 Y 1 T LEU 785 ? E LEU 785 
2093 1 Y 1 T GLU 786 ? E GLU 786 
2094 1 Y 1 T GLU 787 ? E GLU 787 
2095 1 Y 1 T THR 788 ? E THR 788 
2096 1 Y 1 T VAL 789 ? E VAL 789 
2097 1 Y 1 T ALA 790 ? E ALA 790 
2098 1 Y 1 T LYS 791 ? E LYS 791 
2099 1 Y 1 T GLU 792 ? E GLU 792 
2100 1 Y 1 T LEU 793 ? E LEU 793 
2101 1 Y 1 T GLN 794 ? E GLN 794 
2102 1 Y 1 T THR 795 ? E THR 795 
2103 1 Y 1 T LEU 796 ? E LEU 796 
2104 1 Y 1 T HIS 797 ? E HIS 797 
2105 1 Y 1 T ASN 798 ? E ASN 798 
2106 1 Y 1 T LEU 799 ? E LEU 799 
2107 1 Y 1 T ARG 800 ? E ARG 800 
2108 1 Y 1 T LYS 801 ? E LYS 801 
2109 1 Y 1 T LEU 802 ? E LEU 802 
2110 1 Y 1 T PHE 803 ? E PHE 803 
2111 1 Y 1 T VAL 804 ? E VAL 804 
2112 1 Y 1 T GLN 805 ? E GLN 805 
2113 1 Y 1 T ASP 806 ? E ASP 806 
2114 1 Y 1 T LEU 807 ? E LEU 807 
2115 1 Y 1 T ALA 808 ? E ALA 808 
2116 1 Y 1 T THR 809 ? E THR 809 
2117 1 Y 1 T ARG 810 ? E ARG 810 
2118 1 Y 1 T VAL 811 ? E VAL 811 
2119 1 Y 1 T LYS 812 ? E LYS 812 
2120 1 Y 1 T LYS 813 ? E LYS 813 
2121 1 Y 1 T SER 814 ? E SER 814 
2122 1 Y 1 T ALA 815 ? E ALA 815 
2123 1 Y 1 T GLU 816 ? E GLU 816 
2124 1 Y 1 T ILE 817 ? E ILE 817 
2125 1 Y 1 T ASP 818 ? E ASP 818 
2126 1 Y 1 T SER 819 ? E SER 819 
2127 1 Y 1 T ASP 820 ? E ASP 820 
2128 1 Y 1 T ASP 821 ? E ASP 821 
2129 1 Y 1 T THR 822 ? E THR 822 
2130 1 Y 1 T GLY 823 ? E GLY 823 
2131 1 Y 1 T GLY 824 ? E GLY 824 
2132 1 Y 1 T SER 825 ? E SER 825 
2133 1 Y 1 T ALA 826 ? E ALA 826 
2134 1 Y 1 T ALA 827 ? E ALA 827 
2135 1 Y 1 T GLN 828 ? E GLN 828 
2136 1 Y 1 T LYS 829 ? E LYS 829 
2137 1 Y 1 T GLN 830 ? E GLN 830 
2138 1 Y 1 T LYS 831 ? E LYS 831 
2139 1 Y 1 T ILE 832 ? E ILE 832 
2140 1 Y 1 T SER 833 ? E SER 833 
2141 1 Y 1 T PHE 834 ? E PHE 834 
2142 1 Y 1 T LEU 835 ? E LEU 835 
2143 1 Y 1 T GLU 836 ? E GLU 836 
2144 1 Y 1 T ASN 837 ? E ASN 837 
2145 1 Y 1 T ASN 838 ? E ASN 838 
2146 1 Y 1 T LEU 839 ? E LEU 839 
2147 1 Y 1 T GLU 840 ? E GLU 840 
2148 1 Y 1 T GLN 841 ? E GLN 841 
2149 1 Y 1 T LEU 842 ? E LEU 842 
2150 1 Y 1 T THR 843 ? E THR 843 
2151 1 Y 1 T LYS 844 ? E LYS 844 
2152 1 Y 1 T VAL 845 ? E VAL 845 
2153 1 Y 1 T HIS 846 ? E HIS 846 
2154 1 Y 1 T LYS 847 ? E LYS 847 
2155 1 Y 1 T GLN 848 ? E GLN 848 
2156 1 Y 1 T LEU 849 ? E LEU 849 
2157 1 Y 1 T VAL 850 ? E VAL 850 
2158 1 Y 1 T ARG 851 ? E ARG 851 
2159 1 Y 1 T ASP 852 ? E ASP 852 
2160 1 Y 1 T ASN 853 ? E ASN 853 
2161 1 Y 1 T ALA 854 ? E ALA 854 
2162 1 Y 1 T ASP 855 ? E ASP 855 
2163 1 Y 1 T LEU 856 ? E LEU 856 
2164 1 Y 1 T ARG 857 ? E ARG 857 
2165 1 Y 1 T CYS 858 ? E CYS 858 
2166 1 Y 1 T GLU 859 ? E GLU 859 
2167 1 Y 1 T LEU 860 ? E LEU 860 
2168 1 Y 1 T PRO 861 ? E PRO 861 
2169 1 Y 1 T LYS 862 ? E LYS 862 
2170 1 Y 1 T LEU 863 ? E LEU 863 
2171 1 Y 1 T GLU 864 ? E GLU 864 
2172 1 Y 1 T LYS 865 ? E LYS 865 
2173 1 Y 1 T ARG 866 ? E ARG 866 
2174 1 Y 1 T LEU 867 ? E LEU 867 
2175 1 Y 1 T ARG 868 ? E ARG 868 
2176 1 Y 1 T ALA 869 ? E ALA 869 
2177 1 Y 1 T THR 870 ? E THR 870 
2178 1 Y 1 T ALA 871 ? E ALA 871 
2179 1 Y 1 T GLU 872 ? E GLU 872 
2180 1 Y 1 T ARG 873 ? E ARG 873 
2181 1 Y 1 T VAL 874 ? E VAL 874 
2182 1 Y 1 T LYS 875 ? E LYS 875 
2183 1 Y 1 T ALA 876 ? E ALA 876 
2184 1 Y 1 T LEU 877 ? E LEU 877 
2185 1 Y 1 T GLU 878 ? E GLU 878 
2186 1 Y 1 T SER 879 ? E SER 879 
2187 1 Y 1 T ALA 880 ? E ALA 880 
2188 1 Y 1 T LEU 881 ? E LEU 881 
2189 1 Y 1 T LYS 882 ? E LYS 882 
2190 1 Y 1 T GLU 883 ? E GLU 883 
2191 1 Y 1 T ALA 884 ? E ALA 884 
2192 1 Y 1 T LYS 885 ? E LYS 885 
2193 1 Y 1 T GLU 886 ? E GLU 886 
2194 1 Y 1 T ASN 887 ? E ASN 887 
2195 1 Y 1 T ALA 888 ? E ALA 888 
2196 1 Y 1 T SER 889 ? E SER 889 
2197 1 Y 1 T ARG 890 ? E ARG 890 
2198 1 Y 1 T ASP 891 ? E ASP 891 
2199 1 Y 1 T ARG 892 ? E ARG 892 
2200 1 Y 1 T LYS 893 ? E LYS 893 
2201 1 Y 1 T ARG 894 ? E ARG 894 
2202 1 Y 1 T TYR 895 ? E TYR 895 
2203 1 Y 1 T GLN 896 ? E GLN 896 
2204 1 Y 1 T GLN 897 ? E GLN 897 
2205 1 Y 1 T GLU 898 ? E GLU 898 
2206 1 Y 1 T VAL 899 ? E VAL 899 
2207 1 Y 1 T ASP 900 ? E ASP 900 
2208 1 Y 1 T ARG 901 ? E ARG 901 
2209 1 Y 1 T ILE 902 ? E ILE 902 
2210 1 Y 1 T LYS 903 ? E LYS 903 
2211 1 Y 1 T GLU 904 ? E GLU 904 
2212 1 Y 1 T ALA 905 ? E ALA 905 
2213 1 Y 1 T VAL 906 ? E VAL 906 
2214 1 Y 1 T ARG 907 ? E ARG 907 
2215 1 Y 1 T SER 908 ? E SER 908 
2216 1 Y 1 T LYS 909 ? E LYS 909 
2217 1 Y 1 T ASN 910 ? E ASN 910 
2218 1 Y 1 T MET 911 ? E MET 911 
2219 1 Y 1 T ALA 912 ? E ALA 912 
2220 1 Y 1 T ARG 913 ? E ARG 913 
2221 1 Y 1 T ARG 914 ? E ARG 914 
2222 1 Y 1 T GLY 915 ? E GLY 915 
2223 1 Y 1 T HIS 916 ? E HIS 916 
2224 1 Y 1 T SER 917 ? E SER 917 
2225 1 Y 1 T GLY 927 ? E GLY 927 
2226 1 Y 1 T GLN 928 ? E GLN 928 
2227 1 Y 1 T HIS 929 ? E HIS 929 
2228 1 Y 1 T PRO 930 ? E PRO 930 
2229 1 Y 1 T ALA 931 ? E ALA 931 
2230 1 Y 1 T ALA 932 ? E ALA 932 
2231 1 Y 1 T SER 933 ? E SER 933 
2232 1 Y 1 T PRO 934 ? E PRO 934 
2233 1 Y 1 T THR 935 ? E THR 935 
2234 1 Y 1 T HIS 936 ? E HIS 936 
2235 1 Y 1 T PRO 937 ? E PRO 937 
2236 1 Y 1 T SER 938 ? E SER 938 
2237 1 Y 1 T ALA 939 ? E ALA 939 
2238 1 Y 1 T ILE 940 ? E ILE 940 
2239 1 Y 1 T ARG 941 ? E ARG 941 
2240 1 Y 1 T GLY 942 ? E GLY 942 
2241 1 Y 1 T GLY 943 ? E GLY 943 
2242 1 Y 1 T GLY 944 ? E GLY 944 
2243 1 Y 1 T ALA 945 ? E ALA 945 
2244 1 Y 1 T PHE 946 ? E PHE 946 
2245 1 Y 1 T VAL 947 ? E VAL 947 
2246 1 Y 1 T GLN 948 ? E GLN 948 
2247 1 Y 1 T ASN 949 ? E ASN 949 
2248 1 Y 1 T SER 950 ? E SER 950 
2249 1 Y 1 T GLN 951 ? E GLN 951 
2250 1 Y 1 T PRO 952 ? E PRO 952 
2251 1 Y 1 T VAL 953 ? E VAL 953 
2252 1 Y 1 T ALA 954 ? E ALA 954 
2253 1 Y 1 T VAL 955 ? E VAL 955 
2254 1 Y 1 T ARG 956 ? E ARG 956 
2255 1 Y 1 T GLY 957 ? E GLY 957 
2256 1 Y 1 T GLY 958 ? E GLY 958 
2257 1 Y 1 T GLY 959 ? E GLY 959 
2258 1 Y 1 T GLY 960 ? E GLY 960 
2259 1 Y 1 T LYS 961 ? E LYS 961 
2260 1 Y 1 T GLN 962 ? E GLN 962 
2261 1 Y 1 T VAL 963 ? E VAL 963 
2262 1 Y 1 t MET 1   ? F MET 1   
2263 1 Y 1 t ALA 2   ? F ALA 2   
2264 1 Y 1 t ASP 3   ? F ASP 3   
2265 1 Y 1 t LEU 4   ? F LEU 4   
2266 1 Y 1 t ALA 5   ? F ALA 5   
2267 1 Y 1 t GLU 6   ? F GLU 6   
2268 1 Y 1 t CYS 7   ? F CYS 7   
2269 1 Y 1 t ASN 8   ? F ASN 8   
2270 1 Y 1 t ILE 9   ? F ILE 9   
2271 1 Y 1 t LYS 10  ? F LYS 10  
2272 1 Y 1 t VAL 11  ? F VAL 11  
2273 1 Y 1 t MET 12  ? F MET 12  
2274 1 Y 1 t CYS 13  ? F CYS 13  
2275 1 Y 1 t ARG 14  ? F ARG 14  
2276 1 Y 1 t PHE 15  ? F PHE 15  
2277 1 Y 1 t ARG 16  ? F ARG 16  
2278 1 Y 1 t PRO 17  ? F PRO 17  
2279 1 Y 1 t LEU 18  ? F LEU 18  
2280 1 Y 1 t ASN 19  ? F ASN 19  
2281 1 Y 1 t GLU 20  ? F GLU 20  
2282 1 Y 1 t SER 21  ? F SER 21  
2283 1 Y 1 t GLU 22  ? F GLU 22  
2284 1 Y 1 t VAL 23  ? F VAL 23  
2285 1 Y 1 t ASN 24  ? F ASN 24  
2286 1 Y 1 t ARG 25  ? F ARG 25  
2287 1 Y 1 t GLY 26  ? F GLY 26  
2288 1 Y 1 t ASP 27  ? F ASP 27  
2289 1 Y 1 t LYS 28  ? F LYS 28  
2290 1 Y 1 t TYR 29  ? F TYR 29  
2291 1 Y 1 t ILE 30  ? F ILE 30  
2292 1 Y 1 t ALA 31  ? F ALA 31  
2293 1 Y 1 t LYS 32  ? F LYS 32  
2294 1 Y 1 t PHE 33  ? F PHE 33  
2295 1 Y 1 t GLN 34  ? F GLN 34  
2296 1 Y 1 t GLY 35  ? F GLY 35  
2297 1 Y 1 t GLU 36  ? F GLU 36  
2298 1 Y 1 t ASP 37  ? F ASP 37  
2299 1 Y 1 t THR 38  ? F THR 38  
2300 1 Y 1 t VAL 39  ? F VAL 39  
2301 1 Y 1 t VAL 40  ? F VAL 40  
2302 1 Y 1 t ILE 41  ? F ILE 41  
2303 1 Y 1 t ALA 42  ? F ALA 42  
2304 1 Y 1 t SER 43  ? F SER 43  
2305 1 Y 1 t LYS 44  ? F LYS 44  
2306 1 Y 1 t PRO 45  ? F PRO 45  
2307 1 Y 1 t TYR 46  ? F TYR 46  
2308 1 Y 1 t ALA 47  ? F ALA 47  
2309 1 Y 1 t PHE 48  ? F PHE 48  
2310 1 Y 1 t ASP 49  ? F ASP 49  
2311 1 Y 1 t ARG 50  ? F ARG 50  
2312 1 Y 1 t VAL 51  ? F VAL 51  
2313 1 Y 1 t PHE 52  ? F PHE 52  
2314 1 Y 1 t GLN 53  ? F GLN 53  
2315 1 Y 1 t SER 54  ? F SER 54  
2316 1 Y 1 t SER 55  ? F SER 55  
2317 1 Y 1 t THR 56  ? F THR 56  
2318 1 Y 1 t SER 57  ? F SER 57  
2319 1 Y 1 t GLN 58  ? F GLN 58  
2320 1 Y 1 t GLU 59  ? F GLU 59  
2321 1 Y 1 t GLN 60  ? F GLN 60  
2322 1 Y 1 t VAL 61  ? F VAL 61  
2323 1 Y 1 t TYR 62  ? F TYR 62  
2324 1 Y 1 t ASN 63  ? F ASN 63  
2325 1 Y 1 t ASP 64  ? F ASP 64  
2326 1 Y 1 t CYS 65  ? F CYS 65  
2327 1 Y 1 t ALA 66  ? F ALA 66  
2328 1 Y 1 t LYS 67  ? F LYS 67  
2329 1 Y 1 t LYS 68  ? F LYS 68  
2330 1 Y 1 t ILE 69  ? F ILE 69  
2331 1 Y 1 t VAL 70  ? F VAL 70  
2332 1 Y 1 t LYS 71  ? F LYS 71  
2333 1 Y 1 t ASP 72  ? F ASP 72  
2334 1 Y 1 t VAL 73  ? F VAL 73  
2335 1 Y 1 t LEU 74  ? F LEU 74  
2336 1 Y 1 t GLU 75  ? F GLU 75  
2337 1 Y 1 t GLY 76  ? F GLY 76  
2338 1 Y 1 t TYR 77  ? F TYR 77  
2339 1 Y 1 t ASN 78  ? F ASN 78  
2340 1 Y 1 t GLY 79  ? F GLY 79  
2341 1 Y 1 t THR 80  ? F THR 80  
2342 1 Y 1 t ILE 81  ? F ILE 81  
2343 1 Y 1 t PHE 82  ? F PHE 82  
2344 1 Y 1 t ALA 83  ? F ALA 83  
2345 1 Y 1 t TYR 84  ? F TYR 84  
2346 1 Y 1 t GLY 85  ? F GLY 85  
2347 1 Y 1 t GLN 86  ? F GLN 86  
2348 1 Y 1 t THR 87  ? F THR 87  
2349 1 Y 1 t SER 88  ? F SER 88  
2350 1 Y 1 t SER 89  ? F SER 89  
2351 1 Y 1 t GLY 90  ? F GLY 90  
2352 1 Y 1 t LYS 91  ? F LYS 91  
2353 1 Y 1 t THR 92  ? F THR 92  
2354 1 Y 1 t HIS 93  ? F HIS 93  
2355 1 Y 1 t THR 94  ? F THR 94  
2356 1 Y 1 t MET 95  ? F MET 95  
2357 1 Y 1 t GLU 96  ? F GLU 96  
2358 1 Y 1 t GLY 97  ? F GLY 97  
2359 1 Y 1 t LYS 98  ? F LYS 98  
2360 1 Y 1 t LEU 99  ? F LEU 99  
2361 1 Y 1 t HIS 100 ? F HIS 100 
2362 1 Y 1 t ASP 101 ? F ASP 101 
2363 1 Y 1 t PRO 102 ? F PRO 102 
2364 1 Y 1 t GLU 103 ? F GLU 103 
2365 1 Y 1 t GLY 104 ? F GLY 104 
2366 1 Y 1 t MET 105 ? F MET 105 
2367 1 Y 1 t GLY 106 ? F GLY 106 
2368 1 Y 1 t ILE 107 ? F ILE 107 
2369 1 Y 1 t ILE 108 ? F ILE 108 
2370 1 Y 1 t PRO 109 ? F PRO 109 
2371 1 Y 1 t ARG 110 ? F ARG 110 
2372 1 Y 1 t ILE 111 ? F ILE 111 
2373 1 Y 1 t VAL 112 ? F VAL 112 
2374 1 Y 1 t GLN 113 ? F GLN 113 
2375 1 Y 1 t ASP 114 ? F ASP 114 
2376 1 Y 1 t ILE 115 ? F ILE 115 
2377 1 Y 1 t PHE 116 ? F PHE 116 
2378 1 Y 1 t ASN 117 ? F ASN 117 
2379 1 Y 1 t TYR 118 ? F TYR 118 
2380 1 Y 1 t ILE 119 ? F ILE 119 
2381 1 Y 1 t TYR 120 ? F TYR 120 
2382 1 Y 1 t SER 121 ? F SER 121 
2383 1 Y 1 t MET 122 ? F MET 122 
2384 1 Y 1 t ASP 123 ? F ASP 123 
2385 1 Y 1 t GLU 124 ? F GLU 124 
2386 1 Y 1 t ASN 125 ? F ASN 125 
2387 1 Y 1 t LEU 126 ? F LEU 126 
2388 1 Y 1 t GLU 127 ? F GLU 127 
2389 1 Y 1 t PHE 128 ? F PHE 128 
2390 1 Y 1 t HIS 129 ? F HIS 129 
2391 1 Y 1 t ILE 130 ? F ILE 130 
2392 1 Y 1 t LYS 131 ? F LYS 131 
2393 1 Y 1 t VAL 132 ? F VAL 132 
2394 1 Y 1 t SER 133 ? F SER 133 
2395 1 Y 1 t TYR 134 ? F TYR 134 
2396 1 Y 1 t PHE 135 ? F PHE 135 
2397 1 Y 1 t GLU 136 ? F GLU 136 
2398 1 Y 1 t ILE 137 ? F ILE 137 
2399 1 Y 1 t TYR 138 ? F TYR 138 
2400 1 Y 1 t LEU 139 ? F LEU 139 
2401 1 Y 1 t ASP 140 ? F ASP 140 
2402 1 Y 1 t LYS 141 ? F LYS 141 
2403 1 Y 1 t ILE 142 ? F ILE 142 
2404 1 Y 1 t ARG 143 ? F ARG 143 
2405 1 Y 1 t ASP 144 ? F ASP 144 
2406 1 Y 1 t LEU 145 ? F LEU 145 
2407 1 Y 1 t LEU 146 ? F LEU 146 
2408 1 Y 1 t ASP 147 ? F ASP 147 
2409 1 Y 1 t VAL 148 ? F VAL 148 
2410 1 Y 1 t SER 149 ? F SER 149 
2411 1 Y 1 t LYS 150 ? F LYS 150 
2412 1 Y 1 t THR 151 ? F THR 151 
2413 1 Y 1 t ASN 152 ? F ASN 152 
2414 1 Y 1 t LEU 153 ? F LEU 153 
2415 1 Y 1 t SER 154 ? F SER 154 
2416 1 Y 1 t VAL 155 ? F VAL 155 
2417 1 Y 1 t HIS 156 ? F HIS 156 
2418 1 Y 1 t GLU 157 ? F GLU 157 
2419 1 Y 1 t ASP 158 ? F ASP 158 
2420 1 Y 1 t LYS 159 ? F LYS 159 
2421 1 Y 1 t ASN 160 ? F ASN 160 
2422 1 Y 1 t ARG 161 ? F ARG 161 
2423 1 Y 1 t VAL 162 ? F VAL 162 
2424 1 Y 1 t PRO 163 ? F PRO 163 
2425 1 Y 1 t TYR 164 ? F TYR 164 
2426 1 Y 1 t VAL 165 ? F VAL 165 
2427 1 Y 1 t LYS 166 ? F LYS 166 
2428 1 Y 1 t GLY 167 ? F GLY 167 
2429 1 Y 1 t CYS 168 ? F CYS 168 
2430 1 Y 1 t THR 169 ? F THR 169 
2431 1 Y 1 t GLU 170 ? F GLU 170 
2432 1 Y 1 t ARG 171 ? F ARG 171 
2433 1 Y 1 t PHE 172 ? F PHE 172 
2434 1 Y 1 t VAL 173 ? F VAL 173 
2435 1 Y 1 t CYS 174 ? F CYS 174 
2436 1 Y 1 t SER 175 ? F SER 175 
2437 1 Y 1 t PRO 176 ? F PRO 176 
2438 1 Y 1 t ASP 177 ? F ASP 177 
2439 1 Y 1 t GLU 178 ? F GLU 178 
2440 1 Y 1 t VAL 179 ? F VAL 179 
2441 1 Y 1 t MET 180 ? F MET 180 
2442 1 Y 1 t ASP 181 ? F ASP 181 
2443 1 Y 1 t THR 182 ? F THR 182 
2444 1 Y 1 t ILE 183 ? F ILE 183 
2445 1 Y 1 t ASP 184 ? F ASP 184 
2446 1 Y 1 t GLU 185 ? F GLU 185 
2447 1 Y 1 t GLY 186 ? F GLY 186 
2448 1 Y 1 t LYS 187 ? F LYS 187 
2449 1 Y 1 t SER 188 ? F SER 188 
2450 1 Y 1 t ASN 189 ? F ASN 189 
2451 1 Y 1 t ARG 190 ? F ARG 190 
2452 1 Y 1 t HIS 191 ? F HIS 191 
2453 1 Y 1 t VAL 192 ? F VAL 192 
2454 1 Y 1 t ALA 193 ? F ALA 193 
2455 1 Y 1 t VAL 194 ? F VAL 194 
2456 1 Y 1 t THR 195 ? F THR 195 
2457 1 Y 1 t ASN 196 ? F ASN 196 
2458 1 Y 1 t MET 197 ? F MET 197 
2459 1 Y 1 t ASN 198 ? F ASN 198 
2460 1 Y 1 t GLU 199 ? F GLU 199 
2461 1 Y 1 t HIS 200 ? F HIS 200 
2462 1 Y 1 t SER 201 ? F SER 201 
2463 1 Y 1 t SER 202 ? F SER 202 
2464 1 Y 1 t ARG 203 ? F ARG 203 
2465 1 Y 1 t SER 204 ? F SER 204 
2466 1 Y 1 t HIS 205 ? F HIS 205 
2467 1 Y 1 t SER 206 ? F SER 206 
2468 1 Y 1 t ILE 207 ? F ILE 207 
2469 1 Y 1 t PHE 208 ? F PHE 208 
2470 1 Y 1 t LEU 209 ? F LEU 209 
2471 1 Y 1 t ILE 210 ? F ILE 210 
2472 1 Y 1 t ASN 211 ? F ASN 211 
2473 1 Y 1 t VAL 212 ? F VAL 212 
2474 1 Y 1 t LYS 213 ? F LYS 213 
2475 1 Y 1 t GLN 214 ? F GLN 214 
2476 1 Y 1 t GLU 215 ? F GLU 215 
2477 1 Y 1 t ASN 216 ? F ASN 216 
2478 1 Y 1 t THR 217 ? F THR 217 
2479 1 Y 1 t GLN 218 ? F GLN 218 
2480 1 Y 1 t THR 219 ? F THR 219 
2481 1 Y 1 t GLU 220 ? F GLU 220 
2482 1 Y 1 t GLN 221 ? F GLN 221 
2483 1 Y 1 t LYS 222 ? F LYS 222 
2484 1 Y 1 t LEU 223 ? F LEU 223 
2485 1 Y 1 t SER 224 ? F SER 224 
2486 1 Y 1 t GLY 225 ? F GLY 225 
2487 1 Y 1 t LYS 226 ? F LYS 226 
2488 1 Y 1 t LEU 227 ? F LEU 227 
2489 1 Y 1 t TYR 228 ? F TYR 228 
2490 1 Y 1 t LEU 229 ? F LEU 229 
2491 1 Y 1 t VAL 230 ? F VAL 230 
2492 1 Y 1 t ASP 231 ? F ASP 231 
2493 1 Y 1 t LEU 232 ? F LEU 232 
2494 1 Y 1 t ALA 233 ? F ALA 233 
2495 1 Y 1 t GLY 234 ? F GLY 234 
2496 1 Y 1 t SER 235 ? F SER 235 
2497 1 Y 1 t GLU 236 ? F GLU 236 
2498 1 Y 1 t LYS 237 ? F LYS 237 
2499 1 Y 1 t VAL 238 ? F VAL 238 
2500 1 Y 1 t SER 239 ? F SER 239 
2501 1 Y 1 t LYS 240 ? F LYS 240 
2502 1 Y 1 t THR 241 ? F THR 241 
2503 1 Y 1 t GLY 242 ? F GLY 242 
2504 1 Y 1 t ALA 243 ? F ALA 243 
2505 1 Y 1 t GLU 244 ? F GLU 244 
2506 1 Y 1 t GLY 245 ? F GLY 245 
2507 1 Y 1 t ALA 246 ? F ALA 246 
2508 1 Y 1 t VAL 247 ? F VAL 247 
2509 1 Y 1 t LEU 248 ? F LEU 248 
2510 1 Y 1 t ASP 249 ? F ASP 249 
2511 1 Y 1 t GLU 250 ? F GLU 250 
2512 1 Y 1 t ALA 251 ? F ALA 251 
2513 1 Y 1 t LYS 252 ? F LYS 252 
2514 1 Y 1 t ASN 253 ? F ASN 253 
2515 1 Y 1 t ILE 254 ? F ILE 254 
2516 1 Y 1 t ASN 255 ? F ASN 255 
2517 1 Y 1 t LYS 256 ? F LYS 256 
2518 1 Y 1 t SER 257 ? F SER 257 
2519 1 Y 1 t LEU 258 ? F LEU 258 
2520 1 Y 1 t SER 259 ? F SER 259 
2521 1 Y 1 t ALA 260 ? F ALA 260 
2522 1 Y 1 t LEU 261 ? F LEU 261 
2523 1 Y 1 t GLY 262 ? F GLY 262 
2524 1 Y 1 t ASN 263 ? F ASN 263 
2525 1 Y 1 t VAL 264 ? F VAL 264 
2526 1 Y 1 t ILE 265 ? F ILE 265 
2527 1 Y 1 t SER 266 ? F SER 266 
2528 1 Y 1 t ALA 267 ? F ALA 267 
2529 1 Y 1 t LEU 268 ? F LEU 268 
2530 1 Y 1 t ALA 269 ? F ALA 269 
2531 1 Y 1 t GLU 270 ? F GLU 270 
2532 1 Y 1 t GLY 271 ? F GLY 271 
2533 1 Y 1 t SER 272 ? F SER 272 
2534 1 Y 1 t THR 273 ? F THR 273 
2535 1 Y 1 t TYR 274 ? F TYR 274 
2536 1 Y 1 t VAL 275 ? F VAL 275 
2537 1 Y 1 t PRO 276 ? F PRO 276 
2538 1 Y 1 t TYR 277 ? F TYR 277 
2539 1 Y 1 t ARG 278 ? F ARG 278 
2540 1 Y 1 t ASP 279 ? F ASP 279 
2541 1 Y 1 t SER 280 ? F SER 280 
2542 1 Y 1 t LYS 281 ? F LYS 281 
2543 1 Y 1 t MET 282 ? F MET 282 
2544 1 Y 1 t THR 283 ? F THR 283 
2545 1 Y 1 t ARG 284 ? F ARG 284 
2546 1 Y 1 t ILE 285 ? F ILE 285 
2547 1 Y 1 t LEU 286 ? F LEU 286 
2548 1 Y 1 t GLN 287 ? F GLN 287 
2549 1 Y 1 t ASP 288 ? F ASP 288 
2550 1 Y 1 t SER 289 ? F SER 289 
2551 1 Y 1 t LEU 290 ? F LEU 290 
2552 1 Y 1 t GLY 291 ? F GLY 291 
2553 1 Y 1 t GLY 292 ? F GLY 292 
2554 1 Y 1 t ASN 293 ? F ASN 293 
2555 1 Y 1 t CYS 294 ? F CYS 294 
2556 1 Y 1 t ARG 295 ? F ARG 295 
2557 1 Y 1 t THR 296 ? F THR 296 
2558 1 Y 1 t THR 297 ? F THR 297 
2559 1 Y 1 t ILE 298 ? F ILE 298 
2560 1 Y 1 t VAL 299 ? F VAL 299 
2561 1 Y 1 t ILE 300 ? F ILE 300 
2562 1 Y 1 t CYS 301 ? F CYS 301 
2563 1 Y 1 t CYS 302 ? F CYS 302 
2564 1 Y 1 t SER 303 ? F SER 303 
2565 1 Y 1 t PRO 304 ? F PRO 304 
2566 1 Y 1 t SER 305 ? F SER 305 
2567 1 Y 1 t SER 306 ? F SER 306 
2568 1 Y 1 t TYR 307 ? F TYR 307 
2569 1 Y 1 t ASN 308 ? F ASN 308 
2570 1 Y 1 t GLU 309 ? F GLU 309 
2571 1 Y 1 t SER 310 ? F SER 310 
2572 1 Y 1 t GLU 311 ? F GLU 311 
2573 1 Y 1 t THR 312 ? F THR 312 
2574 1 Y 1 t LYS 313 ? F LYS 313 
2575 1 Y 1 t SER 314 ? F SER 314 
2576 1 Y 1 t THR 315 ? F THR 315 
2577 1 Y 1 t LEU 316 ? F LEU 316 
2578 1 Y 1 t LEU 317 ? F LEU 317 
2579 1 Y 1 t PHE 318 ? F PHE 318 
2580 1 Y 1 t GLY 319 ? F GLY 319 
2581 1 Y 1 t GLN 320 ? F GLN 320 
2582 1 Y 1 t ARG 321 ? F ARG 321 
2583 1 Y 1 t ALA 322 ? F ALA 322 
2584 1 Y 1 t LYS 323 ? F LYS 323 
2585 1 Y 1 t THR 324 ? F THR 324 
2586 1 Y 1 t ILE 325 ? F ILE 325 
2587 1 Y 1 t LYS 326 ? F LYS 326 
2588 1 Y 1 t ASN 327 ? F ASN 327 
2589 1 Y 1 t THR 328 ? F THR 328 
2590 1 Y 1 t VAL 329 ? F VAL 329 
2591 1 Y 1 t CYS 330 ? F CYS 330 
2592 1 Y 1 t VAL 331 ? F VAL 331 
2593 1 Y 1 t ASN 332 ? F ASN 332 
2594 1 Y 1 t VAL 333 ? F VAL 333 
2595 1 Y 1 t GLU 334 ? F GLU 334 
2596 1 Y 1 t LEU 335 ? F LEU 335 
2597 1 Y 1 t THR 336 ? F THR 336 
2598 1 Y 1 t ALA 337 ? F ALA 337 
2599 1 Y 1 t GLU 338 ? F GLU 338 
2600 1 Y 1 t GLN 339 ? F GLN 339 
2601 1 Y 1 t TRP 340 ? F TRP 340 
2602 1 Y 1 t LYS 341 ? F LYS 341 
2603 1 Y 1 t LYS 342 ? F LYS 342 
2604 1 Y 1 t LYS 343 ? F LYS 343 
2605 1 Y 1 t TYR 344 ? F TYR 344 
2606 1 Y 1 t GLU 345 ? F GLU 345 
2607 1 Y 1 t LYS 346 ? F LYS 346 
2608 1 Y 1 t GLU 347 ? F GLU 347 
2609 1 Y 1 t LYS 348 ? F LYS 348 
2610 1 Y 1 t GLU 349 ? F GLU 349 
2611 1 Y 1 t LYS 350 ? F LYS 350 
2612 1 Y 1 t ASN 351 ? F ASN 351 
2613 1 Y 1 t LYS 352 ? F LYS 352 
2614 1 Y 1 t ILE 353 ? F ILE 353 
2615 1 Y 1 t LEU 354 ? F LEU 354 
2616 1 Y 1 t ARG 355 ? F ARG 355 
2617 1 Y 1 t ASN 356 ? F ASN 356 
2618 1 Y 1 t THR 357 ? F THR 357 
2619 1 Y 1 t ILE 358 ? F ILE 358 
2620 1 Y 1 t GLN 359 ? F GLN 359 
2621 1 Y 1 t TRP 360 ? F TRP 360 
2622 1 Y 1 t LEU 361 ? F LEU 361 
2623 1 Y 1 t GLU 362 ? F GLU 362 
2624 1 Y 1 t ASN 363 ? F ASN 363 
2625 1 Y 1 t GLU 364 ? F GLU 364 
2626 1 Y 1 t LEU 365 ? F LEU 365 
2627 1 Y 1 t ASN 366 ? F ASN 366 
2628 1 Y 1 t ARG 367 ? F ARG 367 
2629 1 Y 1 t TRP 368 ? F TRP 368 
2630 1 Y 1 t ARG 369 ? F ARG 369 
2631 1 Y 1 t ASN 370 ? F ASN 370 
2632 1 Y 1 t GLY 371 ? F GLY 371 
2633 1 Y 1 t GLU 372 ? F GLU 372 
2634 1 Y 1 t THR 373 ? F THR 373 
2635 1 Y 1 t VAL 374 ? F VAL 374 
2636 1 Y 1 t PRO 375 ? F PRO 375 
2637 1 Y 1 t ILE 376 ? F ILE 376 
2638 1 Y 1 t ASP 377 ? F ASP 377 
2639 1 Y 1 t GLU 378 ? F GLU 378 
2640 1 Y 1 t GLN 379 ? F GLN 379 
2641 1 Y 1 t PHE 380 ? F PHE 380 
2642 1 Y 1 t ASP 381 ? F ASP 381 
2643 1 Y 1 t LYS 382 ? F LYS 382 
2644 1 Y 1 t GLU 383 ? F GLU 383 
2645 1 Y 1 t LYS 384 ? F LYS 384 
2646 1 Y 1 t ALA 385 ? F ALA 385 
2647 1 Y 1 t ASN 386 ? F ASN 386 
2648 1 Y 1 t LEU 387 ? F LEU 387 
2649 1 Y 1 t GLU 388 ? F GLU 388 
2650 1 Y 1 t ALA 389 ? F ALA 389 
2651 1 Y 1 t PHE 390 ? F PHE 390 
2652 1 Y 1 t THR 391 ? F THR 391 
2653 1 Y 1 t VAL 392 ? F VAL 392 
2654 1 Y 1 t ASP 393 ? F ASP 393 
2655 1 Y 1 t LYS 394 ? F LYS 394 
2656 1 Y 1 t ASP 395 ? F ASP 395 
2657 1 Y 1 t ILE 396 ? F ILE 396 
2658 1 Y 1 t THR 397 ? F THR 397 
2659 1 Y 1 t LEU 398 ? F LEU 398 
2660 1 Y 1 t THR 399 ? F THR 399 
2661 1 Y 1 t ASN 400 ? F ASN 400 
2662 1 Y 1 t ASP 401 ? F ASP 401 
2663 1 Y 1 t LYS 402 ? F LYS 402 
2664 1 Y 1 t PRO 403 ? F PRO 403 
2665 1 Y 1 t ALA 404 ? F ALA 404 
2666 1 Y 1 t THR 405 ? F THR 405 
2667 1 Y 1 t ALA 406 ? F ALA 406 
2668 1 Y 1 t ILE 407 ? F ILE 407 
2669 1 Y 1 t GLY 408 ? F GLY 408 
2670 1 Y 1 t VAL 409 ? F VAL 409 
2671 1 Y 1 t ILE 410 ? F ILE 410 
2672 1 Y 1 t GLY 411 ? F GLY 411 
2673 1 Y 1 t ASN 412 ? F ASN 412 
2674 1 Y 1 t PHE 413 ? F PHE 413 
2675 1 Y 1 t THR 414 ? F THR 414 
2676 1 Y 1 t ASP 415 ? F ASP 415 
2677 1 Y 1 t ALA 416 ? F ALA 416 
2678 1 Y 1 t GLU 417 ? F GLU 417 
2679 1 Y 1 t ARG 418 ? F ARG 418 
2680 1 Y 1 t ARG 419 ? F ARG 419 
2681 1 Y 1 t LYS 420 ? F LYS 420 
2682 1 Y 1 t CYS 421 ? F CYS 421 
2683 1 Y 1 t GLU 422 ? F GLU 422 
2684 1 Y 1 t GLU 423 ? F GLU 423 
2685 1 Y 1 t GLU 424 ? F GLU 424 
2686 1 Y 1 t ILE 425 ? F ILE 425 
2687 1 Y 1 t ALA 426 ? F ALA 426 
2688 1 Y 1 t LYS 427 ? F LYS 427 
2689 1 Y 1 t LEU 428 ? F LEU 428 
2690 1 Y 1 t TYR 429 ? F TYR 429 
2691 1 Y 1 t LYS 430 ? F LYS 430 
2692 1 Y 1 t GLN 431 ? F GLN 431 
2693 1 Y 1 t LEU 432 ? F LEU 432 
2694 1 Y 1 t ASP 433 ? F ASP 433 
2695 1 Y 1 t ASP 434 ? F ASP 434 
2696 1 Y 1 t LYS 435 ? F LYS 435 
2697 1 Y 1 t ASP 436 ? F ASP 436 
2698 1 Y 1 t GLU 437 ? F GLU 437 
2699 1 Y 1 t GLU 438 ? F GLU 438 
2700 1 Y 1 t ILE 439 ? F ILE 439 
2701 1 Y 1 t ASN 440 ? F ASN 440 
2702 1 Y 1 t GLN 441 ? F GLN 441 
2703 1 Y 1 t GLN 442 ? F GLN 442 
2704 1 Y 1 t SER 443 ? F SER 443 
2705 1 Y 1 t GLN 444 ? F GLN 444 
2706 1 Y 1 t LEU 445 ? F LEU 445 
2707 1 Y 1 t VAL 446 ? F VAL 446 
2708 1 Y 1 t GLU 447 ? F GLU 447 
2709 1 Y 1 t LYS 448 ? F LYS 448 
2710 1 Y 1 t LEU 449 ? F LEU 449 
2711 1 Y 1 t LYS 450 ? F LYS 450 
2712 1 Y 1 t THR 451 ? F THR 451 
2713 1 Y 1 t GLN 452 ? F GLN 452 
2714 1 Y 1 t MET 453 ? F MET 453 
2715 1 Y 1 t LEU 454 ? F LEU 454 
2716 1 Y 1 t ASP 455 ? F ASP 455 
2717 1 Y 1 t GLN 456 ? F GLN 456 
2718 1 Y 1 t GLU 457 ? F GLU 457 
2719 1 Y 1 t GLU 458 ? F GLU 458 
2720 1 Y 1 t LEU 459 ? F LEU 459 
2721 1 Y 1 t LEU 460 ? F LEU 460 
2722 1 Y 1 t ALA 461 ? F ALA 461 
2723 1 Y 1 t SER 462 ? F SER 462 
2724 1 Y 1 t THR 463 ? F THR 463 
2725 1 Y 1 t ARG 464 ? F ARG 464 
2726 1 Y 1 t ARG 465 ? F ARG 465 
2727 1 Y 1 t ASP 466 ? F ASP 466 
2728 1 Y 1 t GLN 467 ? F GLN 467 
2729 1 Y 1 t ASP 468 ? F ASP 468 
2730 1 Y 1 t ASN 469 ? F ASN 469 
2731 1 Y 1 t MET 470 ? F MET 470 
2732 1 Y 1 t GLN 471 ? F GLN 471 
2733 1 Y 1 t ALA 472 ? F ALA 472 
2734 1 Y 1 t GLU 473 ? F GLU 473 
2735 1 Y 1 t LEU 474 ? F LEU 474 
2736 1 Y 1 t ASN 475 ? F ASN 475 
2737 1 Y 1 t ARG 476 ? F ARG 476 
2738 1 Y 1 t LEU 477 ? F LEU 477 
2739 1 Y 1 t GLN 478 ? F GLN 478 
2740 1 Y 1 t ALA 479 ? F ALA 479 
2741 1 Y 1 t GLU 480 ? F GLU 480 
2742 1 Y 1 t ASN 481 ? F ASN 481 
2743 1 Y 1 t ASP 482 ? F ASP 482 
2744 1 Y 1 t ALA 483 ? F ALA 483 
2745 1 Y 1 t SER 484 ? F SER 484 
2746 1 Y 1 t LYS 485 ? F LYS 485 
2747 1 Y 1 t GLU 486 ? F GLU 486 
2748 1 Y 1 t GLU 487 ? F GLU 487 
2749 1 Y 1 t VAL 488 ? F VAL 488 
2750 1 Y 1 t LYS 489 ? F LYS 489 
2751 1 Y 1 t GLU 490 ? F GLU 490 
2752 1 Y 1 t VAL 491 ? F VAL 491 
2753 1 Y 1 t LEU 492 ? F LEU 492 
2754 1 Y 1 t GLN 493 ? F GLN 493 
2755 1 Y 1 t ALA 494 ? F ALA 494 
2756 1 Y 1 t LEU 495 ? F LEU 495 
2757 1 Y 1 t GLU 496 ? F GLU 496 
2758 1 Y 1 t GLU 497 ? F GLU 497 
2759 1 Y 1 t LEU 498 ? F LEU 498 
2760 1 Y 1 t ALA 499 ? F ALA 499 
2761 1 Y 1 t VAL 500 ? F VAL 500 
2762 1 Y 1 t ASN 501 ? F ASN 501 
2763 1 Y 1 t TYR 502 ? F TYR 502 
2764 1 Y 1 t ASP 503 ? F ASP 503 
2765 1 Y 1 t GLN 504 ? F GLN 504 
2766 1 Y 1 t LYS 505 ? F LYS 505 
2767 1 Y 1 t SER 506 ? F SER 506 
2768 1 Y 1 t GLN 507 ? F GLN 507 
2769 1 Y 1 t GLU 508 ? F GLU 508 
2770 1 Y 1 t VAL 509 ? F VAL 509 
2771 1 Y 1 t GLU 510 ? F GLU 510 
2772 1 Y 1 t ASP 511 ? F ASP 511 
2773 1 Y 1 t LYS 512 ? F LYS 512 
2774 1 Y 1 t THR 513 ? F THR 513 
2775 1 Y 1 t LYS 514 ? F LYS 514 
2776 1 Y 1 t GLU 515 ? F GLU 515 
2777 1 Y 1 t TYR 516 ? F TYR 516 
2778 1 Y 1 t GLU 517 ? F GLU 517 
2779 1 Y 1 t LEU 518 ? F LEU 518 
2780 1 Y 1 t LEU 519 ? F LEU 519 
2781 1 Y 1 t SER 520 ? F SER 520 
2782 1 Y 1 t ASP 521 ? F ASP 521 
2783 1 Y 1 t GLU 522 ? F GLU 522 
2784 1 Y 1 t LEU 523 ? F LEU 523 
2785 1 Y 1 t ASN 524 ? F ASN 524 
2786 1 Y 1 t GLN 525 ? F GLN 525 
2787 1 Y 1 t LYS 526 ? F LYS 526 
2788 1 Y 1 t SER 527 ? F SER 527 
2789 1 Y 1 t ALA 528 ? F ALA 528 
2790 1 Y 1 t THR 529 ? F THR 529 
2791 1 Y 1 t LEU 530 ? F LEU 530 
2792 1 Y 1 t ALA 531 ? F ALA 531 
2793 1 Y 1 t SER 532 ? F SER 532 
2794 1 Y 1 t ILE 533 ? F ILE 533 
2795 1 Y 1 t ASP 534 ? F ASP 534 
2796 1 Y 1 t ALA 535 ? F ALA 535 
2797 1 Y 1 t GLU 536 ? F GLU 536 
2798 1 Y 1 t LEU 537 ? F LEU 537 
2799 1 Y 1 t GLN 538 ? F GLN 538 
2800 1 Y 1 t LYS 539 ? F LYS 539 
2801 1 Y 1 t LEU 540 ? F LEU 540 
2802 1 Y 1 t LYS 541 ? F LYS 541 
2803 1 Y 1 t GLU 542 ? F GLU 542 
2804 1 Y 1 t MET 543 ? F MET 543 
2805 1 Y 1 t THR 544 ? F THR 544 
2806 1 Y 1 t ASN 545 ? F ASN 545 
2807 1 Y 1 t HIS 546 ? F HIS 546 
2808 1 Y 1 t GLN 547 ? F GLN 547 
2809 1 Y 1 t LYS 548 ? F LYS 548 
2810 1 Y 1 t LYS 549 ? F LYS 549 
2811 1 Y 1 t ARG 550 ? F ARG 550 
2812 1 Y 1 t ALA 551 ? F ALA 551 
2813 1 Y 1 t ALA 552 ? F ALA 552 
2814 1 Y 1 t GLU 553 ? F GLU 553 
2815 1 Y 1 t MET 554 ? F MET 554 
2816 1 Y 1 t MET 555 ? F MET 555 
2817 1 Y 1 t ALA 556 ? F ALA 556 
2818 1 Y 1 t SER 557 ? F SER 557 
2819 1 Y 1 t LEU 558 ? F LEU 558 
2820 1 Y 1 t LEU 559 ? F LEU 559 
2821 1 Y 1 t LYS 560 ? F LYS 560 
2822 1 Y 1 t ASP 561 ? F ASP 561 
2823 1 Y 1 t LEU 562 ? F LEU 562 
2824 1 Y 1 t ALA 563 ? F ALA 563 
2825 1 Y 1 t GLU 564 ? F GLU 564 
2826 1 Y 1 t ILE 565 ? F ILE 565 
2827 1 Y 1 t GLY 566 ? F GLY 566 
2828 1 Y 1 t ILE 567 ? F ILE 567 
2829 1 Y 1 t ALA 568 ? F ALA 568 
2830 1 Y 1 t VAL 569 ? F VAL 569 
2831 1 Y 1 t GLY 570 ? F GLY 570 
2832 1 Y 1 t ASN 571 ? F ASN 571 
2833 1 Y 1 t ASN 572 ? F ASN 572 
2834 1 Y 1 t ASP 573 ? F ASP 573 
2835 1 Y 1 t VAL 574 ? F VAL 574 
2836 1 Y 1 t LYS 575 ? F LYS 575 
2837 1 Y 1 t GLN 576 ? F GLN 576 
2838 1 Y 1 t PRO 577 ? F PRO 577 
2839 1 Y 1 t GLU 578 ? F GLU 578 
2840 1 Y 1 t GLY 579 ? F GLY 579 
2841 1 Y 1 t THR 580 ? F THR 580 
2842 1 Y 1 t GLY 581 ? F GLY 581 
2843 1 Y 1 t MET 582 ? F MET 582 
2844 1 Y 1 t ILE 583 ? F ILE 583 
2845 1 Y 1 t ASP 584 ? F ASP 584 
2846 1 Y 1 t GLU 585 ? F GLU 585 
2847 1 Y 1 t GLU 586 ? F GLU 586 
2848 1 Y 1 t PHE 587 ? F PHE 587 
2849 1 Y 1 t THR 588 ? F THR 588 
2850 1 Y 1 t VAL 589 ? F VAL 589 
2851 1 Y 1 t ALA 590 ? F ALA 590 
2852 1 Y 1 t ARG 591 ? F ARG 591 
2853 1 Y 1 t LEU 592 ? F LEU 592 
2854 1 Y 1 t TYR 593 ? F TYR 593 
2855 1 Y 1 t ILE 594 ? F ILE 594 
2856 1 Y 1 t SER 595 ? F SER 595 
2857 1 Y 1 t LYS 596 ? F LYS 596 
2858 1 Y 1 t MET 597 ? F MET 597 
2859 1 Y 1 t LYS 598 ? F LYS 598 
2860 1 Y 1 t SER 599 ? F SER 599 
2861 1 Y 1 t GLU 600 ? F GLU 600 
2862 1 Y 1 t VAL 601 ? F VAL 601 
2863 1 Y 1 t LYS 602 ? F LYS 602 
2864 1 Y 1 t THR 603 ? F THR 603 
2865 1 Y 1 t MET 604 ? F MET 604 
2866 1 Y 1 t VAL 605 ? F VAL 605 
2867 1 Y 1 t LYS 606 ? F LYS 606 
2868 1 Y 1 t ARG 607 ? F ARG 607 
2869 1 Y 1 t CYS 608 ? F CYS 608 
2870 1 Y 1 t LYS 609 ? F LYS 609 
2871 1 Y 1 t GLN 610 ? F GLN 610 
2872 1 Y 1 t LEU 611 ? F LEU 611 
2873 1 Y 1 t GLU 612 ? F GLU 612 
2874 1 Y 1 t SER 613 ? F SER 613 
2875 1 Y 1 t THR 614 ? F THR 614 
2876 1 Y 1 t GLN 615 ? F GLN 615 
2877 1 Y 1 t THR 616 ? F THR 616 
2878 1 Y 1 t GLU 617 ? F GLU 617 
2879 1 Y 1 t SER 618 ? F SER 618 
2880 1 Y 1 t ASN 619 ? F ASN 619 
2881 1 Y 1 t LYS 620 ? F LYS 620 
2882 1 Y 1 t LYS 621 ? F LYS 621 
2883 1 Y 1 t MET 622 ? F MET 622 
2884 1 Y 1 t GLU 623 ? F GLU 623 
2885 1 Y 1 t GLU 624 ? F GLU 624 
2886 1 Y 1 t ASN 625 ? F ASN 625 
2887 1 Y 1 t GLU 626 ? F GLU 626 
2888 1 Y 1 t LYS 627 ? F LYS 627 
2889 1 Y 1 t GLU 628 ? F GLU 628 
2890 1 Y 1 t LEU 629 ? F LEU 629 
2891 1 Y 1 t ALA 630 ? F ALA 630 
2892 1 Y 1 t ALA 631 ? F ALA 631 
2893 1 Y 1 t CYS 632 ? F CYS 632 
2894 1 Y 1 t GLN 633 ? F GLN 633 
2895 1 Y 1 t LEU 634 ? F LEU 634 
2896 1 Y 1 t ARG 635 ? F ARG 635 
2897 1 Y 1 t ILE 636 ? F ILE 636 
2898 1 Y 1 t SER 637 ? F SER 637 
2899 1 Y 1 t GLN 638 ? F GLN 638 
2900 1 Y 1 t HIS 639 ? F HIS 639 
2901 1 Y 1 t GLU 640 ? F GLU 640 
2902 1 Y 1 t ALA 641 ? F ALA 641 
2903 1 Y 1 t LYS 642 ? F LYS 642 
2904 1 Y 1 t ILE 643 ? F ILE 643 
2905 1 Y 1 t LYS 644 ? F LYS 644 
2906 1 Y 1 t SER 645 ? F SER 645 
2907 1 Y 1 t LEU 646 ? F LEU 646 
2908 1 Y 1 t THR 647 ? F THR 647 
2909 1 Y 1 t GLU 648 ? F GLU 648 
2910 1 Y 1 t TYR 649 ? F TYR 649 
2911 1 Y 1 t LEU 650 ? F LEU 650 
2912 1 Y 1 t GLN 651 ? F GLN 651 
2913 1 Y 1 t ASN 652 ? F ASN 652 
2914 1 Y 1 t VAL 653 ? F VAL 653 
2915 1 Y 1 t GLU 654 ? F GLU 654 
2916 1 Y 1 t GLN 655 ? F GLN 655 
2917 1 Y 1 t LYS 656 ? F LYS 656 
2918 1 Y 1 t LYS 657 ? F LYS 657 
2919 1 Y 1 t ARG 658 ? F ARG 658 
2920 1 Y 1 t GLN 659 ? F GLN 659 
2921 1 Y 1 t LEU 660 ? F LEU 660 
2922 1 Y 1 t GLU 661 ? F GLU 661 
2923 1 Y 1 t GLU 662 ? F GLU 662 
2924 1 Y 1 t SER 663 ? F SER 663 
2925 1 Y 1 t VAL 664 ? F VAL 664 
2926 1 Y 1 t ASP 665 ? F ASP 665 
2927 1 Y 1 t ALA 666 ? F ALA 666 
2928 1 Y 1 t LEU 667 ? F LEU 667 
2929 1 Y 1 t SER 668 ? F SER 668 
2930 1 Y 1 t GLU 669 ? F GLU 669 
2931 1 Y 1 t GLU 670 ? F GLU 670 
2932 1 Y 1 t LEU 671 ? F LEU 671 
2933 1 Y 1 t VAL 672 ? F VAL 672 
2934 1 Y 1 t GLN 673 ? F GLN 673 
2935 1 Y 1 t LEU 674 ? F LEU 674 
2936 1 Y 1 t ARG 675 ? F ARG 675 
2937 1 Y 1 t ALA 676 ? F ALA 676 
2938 1 Y 1 t GLN 677 ? F GLN 677 
2939 1 Y 1 t GLU 678 ? F GLU 678 
2940 1 Y 1 t LYS 679 ? F LYS 679 
2941 1 Y 1 t VAL 680 ? F VAL 680 
2942 1 Y 1 t HIS 681 ? F HIS 681 
2943 1 Y 1 t GLU 682 ? F GLU 682 
2944 1 Y 1 t MET 683 ? F MET 683 
2945 1 Y 1 t GLU 684 ? F GLU 684 
2946 1 Y 1 t LYS 685 ? F LYS 685 
2947 1 Y 1 t GLU 686 ? F GLU 686 
2948 1 Y 1 t HIS 687 ? F HIS 687 
2949 1 Y 1 t LEU 688 ? F LEU 688 
2950 1 Y 1 t ASN 689 ? F ASN 689 
2951 1 Y 1 t LYS 690 ? F LYS 690 
2952 1 Y 1 t VAL 691 ? F VAL 691 
2953 1 Y 1 t GLN 692 ? F GLN 692 
2954 1 Y 1 t THR 693 ? F THR 693 
2955 1 Y 1 t ALA 694 ? F ALA 694 
2956 1 Y 1 t ASN 695 ? F ASN 695 
2957 1 Y 1 t GLU 696 ? F GLU 696 
2958 1 Y 1 t VAL 697 ? F VAL 697 
2959 1 Y 1 t LYS 698 ? F LYS 698 
2960 1 Y 1 t GLN 699 ? F GLN 699 
2961 1 Y 1 t ALA 700 ? F ALA 700 
2962 1 Y 1 t VAL 701 ? F VAL 701 
2963 1 Y 1 t GLU 702 ? F GLU 702 
2964 1 Y 1 t GLN 703 ? F GLN 703 
2965 1 Y 1 t GLN 704 ? F GLN 704 
2966 1 Y 1 t ILE 705 ? F ILE 705 
2967 1 Y 1 t GLN 706 ? F GLN 706 
2968 1 Y 1 t SER 707 ? F SER 707 
2969 1 Y 1 t HIS 708 ? F HIS 708 
2970 1 Y 1 t ARG 709 ? F ARG 709 
2971 1 Y 1 t GLU 710 ? F GLU 710 
2972 1 Y 1 t THR 711 ? F THR 711 
2973 1 Y 1 t HIS 712 ? F HIS 712 
2974 1 Y 1 t GLN 713 ? F GLN 713 
2975 1 Y 1 t LYS 714 ? F LYS 714 
2976 1 Y 1 t GLN 715 ? F GLN 715 
2977 1 Y 1 t ILE 716 ? F ILE 716 
2978 1 Y 1 t SER 717 ? F SER 717 
2979 1 Y 1 t SER 718 ? F SER 718 
2980 1 Y 1 t LEU 719 ? F LEU 719 
2981 1 Y 1 t ARG 720 ? F ARG 720 
2982 1 Y 1 t ASP 721 ? F ASP 721 
2983 1 Y 1 t GLU 722 ? F GLU 722 
2984 1 Y 1 t VAL 723 ? F VAL 723 
2985 1 Y 1 t GLU 724 ? F GLU 724 
2986 1 Y 1 t ALA 725 ? F ALA 725 
2987 1 Y 1 t LYS 726 ? F LYS 726 
2988 1 Y 1 t ALA 727 ? F ALA 727 
2989 1 Y 1 t LYS 728 ? F LYS 728 
2990 1 Y 1 t LEU 729 ? F LEU 729 
2991 1 Y 1 t ILE 730 ? F ILE 730 
2992 1 Y 1 t THR 731 ? F THR 731 
2993 1 Y 1 t ASP 732 ? F ASP 732 
2994 1 Y 1 t LEU 733 ? F LEU 733 
2995 1 Y 1 t GLN 734 ? F GLN 734 
2996 1 Y 1 t ASP 735 ? F ASP 735 
2997 1 Y 1 t GLN 736 ? F GLN 736 
2998 1 Y 1 t ASN 737 ? F ASN 737 
2999 1 Y 1 t GLN 738 ? F GLN 738 
3000 1 Y 1 t LYS 739 ? F LYS 739 
3001 1 Y 1 t MET 740 ? F MET 740 
3002 1 Y 1 t MET 741 ? F MET 741 
3003 1 Y 1 t LEU 742 ? F LEU 742 
3004 1 Y 1 t GLU 743 ? F GLU 743 
3005 1 Y 1 t GLN 744 ? F GLN 744 
3006 1 Y 1 t GLU 745 ? F GLU 745 
3007 1 Y 1 t ARG 746 ? F ARG 746 
3008 1 Y 1 t LEU 747 ? F LEU 747 
3009 1 Y 1 t ARG 748 ? F ARG 748 
3010 1 Y 1 t VAL 749 ? F VAL 749 
3011 1 Y 1 t GLU 750 ? F GLU 750 
3012 1 Y 1 t HIS 751 ? F HIS 751 
3013 1 Y 1 t GLU 752 ? F GLU 752 
3014 1 Y 1 t LYS 753 ? F LYS 753 
3015 1 Y 1 t LEU 754 ? F LEU 754 
3016 1 Y 1 t LYS 755 ? F LYS 755 
3017 1 Y 1 t ALA 756 ? F ALA 756 
3018 1 Y 1 t THR 757 ? F THR 757 
3019 1 Y 1 t ASP 758 ? F ASP 758 
3020 1 Y 1 t GLN 759 ? F GLN 759 
3021 1 Y 1 t GLU 760 ? F GLU 760 
3022 1 Y 1 t LYS 761 ? F LYS 761 
3023 1 Y 1 t SER 762 ? F SER 762 
3024 1 Y 1 t ARG 763 ? F ARG 763 
3025 1 Y 1 t LYS 764 ? F LYS 764 
3026 1 Y 1 t LEU 765 ? F LEU 765 
3027 1 Y 1 t HIS 766 ? F HIS 766 
3028 1 Y 1 t GLU 767 ? F GLU 767 
3029 1 Y 1 t LEU 768 ? F LEU 768 
3030 1 Y 1 t THR 769 ? F THR 769 
3031 1 Y 1 t VAL 770 ? F VAL 770 
3032 1 Y 1 t MET 771 ? F MET 771 
3033 1 Y 1 t GLN 772 ? F GLN 772 
3034 1 Y 1 t ASP 773 ? F ASP 773 
3035 1 Y 1 t ARG 774 ? F ARG 774 
3036 1 Y 1 t ARG 775 ? F ARG 775 
3037 1 Y 1 t GLU 776 ? F GLU 776 
3038 1 Y 1 t GLN 777 ? F GLN 777 
3039 1 Y 1 t ALA 778 ? F ALA 778 
3040 1 Y 1 t ARG 779 ? F ARG 779 
3041 1 Y 1 t GLN 780 ? F GLN 780 
3042 1 Y 1 t ASP 781 ? F ASP 781 
3043 1 Y 1 t LEU 782 ? F LEU 782 
3044 1 Y 1 t LYS 783 ? F LYS 783 
3045 1 Y 1 t GLY 784 ? F GLY 784 
3046 1 Y 1 t LEU 785 ? F LEU 785 
3047 1 Y 1 t GLU 786 ? F GLU 786 
3048 1 Y 1 t GLU 787 ? F GLU 787 
3049 1 Y 1 t THR 788 ? F THR 788 
3050 1 Y 1 t VAL 789 ? F VAL 789 
3051 1 Y 1 t ALA 790 ? F ALA 790 
3052 1 Y 1 t LYS 791 ? F LYS 791 
3053 1 Y 1 t GLU 792 ? F GLU 792 
3054 1 Y 1 t LEU 793 ? F LEU 793 
3055 1 Y 1 t GLN 794 ? F GLN 794 
3056 1 Y 1 t THR 795 ? F THR 795 
3057 1 Y 1 t LEU 796 ? F LEU 796 
3058 1 Y 1 t HIS 797 ? F HIS 797 
3059 1 Y 1 t ASN 798 ? F ASN 798 
3060 1 Y 1 t LEU 799 ? F LEU 799 
3061 1 Y 1 t ARG 800 ? F ARG 800 
3062 1 Y 1 t LYS 801 ? F LYS 801 
3063 1 Y 1 t LEU 802 ? F LEU 802 
3064 1 Y 1 t PHE 803 ? F PHE 803 
3065 1 Y 1 t VAL 804 ? F VAL 804 
3066 1 Y 1 t GLN 805 ? F GLN 805 
3067 1 Y 1 t ASP 806 ? F ASP 806 
3068 1 Y 1 t LEU 807 ? F LEU 807 
3069 1 Y 1 t ALA 808 ? F ALA 808 
3070 1 Y 1 t THR 809 ? F THR 809 
3071 1 Y 1 t ARG 810 ? F ARG 810 
3072 1 Y 1 t VAL 811 ? F VAL 811 
3073 1 Y 1 t LYS 812 ? F LYS 812 
3074 1 Y 1 t LYS 813 ? F LYS 813 
3075 1 Y 1 t SER 814 ? F SER 814 
3076 1 Y 1 t ALA 815 ? F ALA 815 
3077 1 Y 1 t GLU 816 ? F GLU 816 
3078 1 Y 1 t ILE 817 ? F ILE 817 
3079 1 Y 1 t ASP 818 ? F ASP 818 
3080 1 Y 1 t SER 819 ? F SER 819 
3081 1 Y 1 t ASP 820 ? F ASP 820 
3082 1 Y 1 t ASP 821 ? F ASP 821 
3083 1 Y 1 t THR 822 ? F THR 822 
3084 1 Y 1 t GLY 823 ? F GLY 823 
3085 1 Y 1 t GLY 824 ? F GLY 824 
3086 1 Y 1 t SER 825 ? F SER 825 
3087 1 Y 1 t ALA 826 ? F ALA 826 
3088 1 Y 1 t ALA 827 ? F ALA 827 
3089 1 Y 1 t GLN 828 ? F GLN 828 
3090 1 Y 1 t LYS 829 ? F LYS 829 
3091 1 Y 1 t GLN 830 ? F GLN 830 
3092 1 Y 1 t LYS 831 ? F LYS 831 
3093 1 Y 1 t ILE 832 ? F ILE 832 
3094 1 Y 1 t SER 833 ? F SER 833 
3095 1 Y 1 t PHE 834 ? F PHE 834 
3096 1 Y 1 t LEU 835 ? F LEU 835 
3097 1 Y 1 t GLU 836 ? F GLU 836 
3098 1 Y 1 t ASN 837 ? F ASN 837 
3099 1 Y 1 t ASN 838 ? F ASN 838 
3100 1 Y 1 t LEU 839 ? F LEU 839 
3101 1 Y 1 t GLU 840 ? F GLU 840 
3102 1 Y 1 t GLN 841 ? F GLN 841 
3103 1 Y 1 t LEU 842 ? F LEU 842 
3104 1 Y 1 t THR 843 ? F THR 843 
3105 1 Y 1 t LYS 844 ? F LYS 844 
3106 1 Y 1 t VAL 845 ? F VAL 845 
3107 1 Y 1 t HIS 846 ? F HIS 846 
3108 1 Y 1 t LYS 847 ? F LYS 847 
3109 1 Y 1 t GLN 848 ? F GLN 848 
3110 1 Y 1 t LEU 849 ? F LEU 849 
3111 1 Y 1 t VAL 850 ? F VAL 850 
3112 1 Y 1 t ARG 851 ? F ARG 851 
3113 1 Y 1 t ASP 852 ? F ASP 852 
3114 1 Y 1 t ASN 853 ? F ASN 853 
3115 1 Y 1 t ALA 854 ? F ALA 854 
3116 1 Y 1 t ASP 855 ? F ASP 855 
3117 1 Y 1 t LEU 856 ? F LEU 856 
3118 1 Y 1 t ARG 857 ? F ARG 857 
3119 1 Y 1 t CYS 858 ? F CYS 858 
3120 1 Y 1 t GLU 859 ? F GLU 859 
3121 1 Y 1 t LEU 860 ? F LEU 860 
3122 1 Y 1 t PRO 861 ? F PRO 861 
3123 1 Y 1 t LYS 862 ? F LYS 862 
3124 1 Y 1 t LEU 863 ? F LEU 863 
3125 1 Y 1 t GLU 864 ? F GLU 864 
3126 1 Y 1 t LYS 865 ? F LYS 865 
3127 1 Y 1 t ARG 866 ? F ARG 866 
3128 1 Y 1 t LEU 867 ? F LEU 867 
3129 1 Y 1 t ARG 868 ? F ARG 868 
3130 1 Y 1 t ALA 869 ? F ALA 869 
3131 1 Y 1 t THR 870 ? F THR 870 
3132 1 Y 1 t ALA 871 ? F ALA 871 
3133 1 Y 1 t GLU 872 ? F GLU 872 
3134 1 Y 1 t ARG 873 ? F ARG 873 
3135 1 Y 1 t VAL 874 ? F VAL 874 
3136 1 Y 1 t LYS 875 ? F LYS 875 
3137 1 Y 1 t ALA 876 ? F ALA 876 
3138 1 Y 1 t LEU 877 ? F LEU 877 
3139 1 Y 1 t GLU 878 ? F GLU 878 
3140 1 Y 1 t SER 879 ? F SER 879 
3141 1 Y 1 t ALA 880 ? F ALA 880 
3142 1 Y 1 t LEU 881 ? F LEU 881 
3143 1 Y 1 t LYS 882 ? F LYS 882 
3144 1 Y 1 t GLU 883 ? F GLU 883 
3145 1 Y 1 t ALA 884 ? F ALA 884 
3146 1 Y 1 t LYS 885 ? F LYS 885 
3147 1 Y 1 t GLU 886 ? F GLU 886 
3148 1 Y 1 t ASN 887 ? F ASN 887 
3149 1 Y 1 t ALA 888 ? F ALA 888 
3150 1 Y 1 t SER 889 ? F SER 889 
3151 1 Y 1 t ARG 890 ? F ARG 890 
3152 1 Y 1 t ASP 891 ? F ASP 891 
3153 1 Y 1 t ARG 892 ? F ARG 892 
3154 1 Y 1 t LYS 893 ? F LYS 893 
3155 1 Y 1 t ARG 894 ? F ARG 894 
3156 1 Y 1 t TYR 895 ? F TYR 895 
3157 1 Y 1 t GLN 896 ? F GLN 896 
3158 1 Y 1 t GLN 897 ? F GLN 897 
3159 1 Y 1 t GLU 898 ? F GLU 898 
3160 1 Y 1 t VAL 899 ? F VAL 899 
3161 1 Y 1 t ASP 900 ? F ASP 900 
3162 1 Y 1 t ARG 901 ? F ARG 901 
3163 1 Y 1 t ILE 902 ? F ILE 902 
3164 1 Y 1 t LYS 903 ? F LYS 903 
3165 1 Y 1 t GLU 904 ? F GLU 904 
3166 1 Y 1 t ALA 905 ? F ALA 905 
3167 1 Y 1 t VAL 906 ? F VAL 906 
3168 1 Y 1 t ARG 907 ? F ARG 907 
3169 1 Y 1 t SER 908 ? F SER 908 
3170 1 Y 1 t LYS 909 ? F LYS 909 
3171 1 Y 1 t ASN 910 ? F ASN 910 
3172 1 Y 1 t MET 911 ? F MET 911 
3173 1 Y 1 t ALA 912 ? F ALA 912 
3174 1 Y 1 t ARG 913 ? F ARG 913 
3175 1 Y 1 t ARG 914 ? F ARG 914 
3176 1 Y 1 t GLY 915 ? F GLY 915 
3177 1 Y 1 t HIS 916 ? F HIS 916 
3178 1 Y 1 t SER 917 ? F SER 917 
3179 1 Y 1 t GLY 927 ? F GLY 927 
3180 1 Y 1 t GLN 928 ? F GLN 928 
3181 1 Y 1 t HIS 929 ? F HIS 929 
3182 1 Y 1 t PRO 930 ? F PRO 930 
3183 1 Y 1 t ALA 931 ? F ALA 931 
3184 1 Y 1 t ALA 932 ? F ALA 932 
3185 1 Y 1 t SER 933 ? F SER 933 
3186 1 Y 1 t PRO 934 ? F PRO 934 
3187 1 Y 1 t THR 935 ? F THR 935 
3188 1 Y 1 t HIS 936 ? F HIS 936 
3189 1 Y 1 t PRO 937 ? F PRO 937 
3190 1 Y 1 t SER 938 ? F SER 938 
3191 1 Y 1 t ALA 939 ? F ALA 939 
3192 1 Y 1 t ILE 940 ? F ILE 940 
3193 1 Y 1 t ARG 941 ? F ARG 941 
3194 1 Y 1 t GLY 942 ? F GLY 942 
3195 1 Y 1 t GLY 943 ? F GLY 943 
3196 1 Y 1 t GLY 944 ? F GLY 944 
3197 1 Y 1 t ALA 945 ? F ALA 945 
3198 1 Y 1 t PHE 946 ? F PHE 946 
3199 1 Y 1 t VAL 947 ? F VAL 947 
3200 1 Y 1 t GLN 948 ? F GLN 948 
3201 1 Y 1 t ASN 949 ? F ASN 949 
3202 1 Y 1 t SER 950 ? F SER 950 
3203 1 Y 1 t GLN 951 ? F GLN 951 
3204 1 Y 1 t PRO 952 ? F PRO 952 
3205 1 Y 1 t VAL 953 ? F VAL 953 
3206 1 Y 1 t ALA 954 ? F ALA 954 
3207 1 Y 1 t VAL 955 ? F VAL 955 
3208 1 Y 1 t ARG 956 ? F ARG 956 
3209 1 Y 1 t GLY 957 ? F GLY 957 
3210 1 Y 1 t GLY 958 ? F GLY 958 
3211 1 Y 1 t GLY 959 ? F GLY 959 
3212 1 Y 1 t GLY 960 ? F GLY 960 
3213 1 Y 1 t LYS 961 ? F LYS 961 
3214 1 Y 1 t GLN 962 ? F GLN 962 
3215 1 Y 1 t VAL 963 ? F VAL 963 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GDP PB     P  N N 136 
GDP O1B    O  N N 137 
GDP O2B    O  N N 138 
GDP O3B    O  N N 139 
GDP O3A    O  N N 140 
GDP PA     P  N N 141 
GDP O1A    O  N N 142 
GDP O2A    O  N N 143 
GDP "O5'"  O  N N 144 
GDP "C5'"  C  N N 145 
GDP "C4'"  C  N R 146 
GDP "O4'"  O  N N 147 
GDP "C3'"  C  N S 148 
GDP "O3'"  O  N N 149 
GDP "C2'"  C  N R 150 
GDP "O2'"  O  N N 151 
GDP "C1'"  C  N R 152 
GDP N9     N  Y N 153 
GDP C8     C  Y N 154 
GDP N7     N  Y N 155 
GDP C5     C  Y N 156 
GDP C6     C  N N 157 
GDP O6     O  N N 158 
GDP N1     N  N N 159 
GDP C2     C  N N 160 
GDP N2     N  N N 161 
GDP N3     N  N N 162 
GDP C4     C  Y N 163 
GDP HOB2   H  N N 164 
GDP HOB3   H  N N 165 
GDP HOA2   H  N N 166 
GDP "H5'"  H  N N 167 
GDP "H5''" H  N N 168 
GDP "H4'"  H  N N 169 
GDP "H3'"  H  N N 170 
GDP "HO3'" H  N N 171 
GDP "H2'"  H  N N 172 
GDP "HO2'" H  N N 173 
GDP "H1'"  H  N N 174 
GDP H8     H  N N 175 
GDP HN1    H  N N 176 
GDP HN21   H  N N 177 
GDP HN22   H  N N 178 
GLN N      N  N N 179 
GLN CA     C  N S 180 
GLN C      C  N N 181 
GLN O      O  N N 182 
GLN CB     C  N N 183 
GLN CG     C  N N 184 
GLN CD     C  N N 185 
GLN OE1    O  N N 186 
GLN NE2    N  N N 187 
GLN OXT    O  N N 188 
GLN H      H  N N 189 
GLN H2     H  N N 190 
GLN HA     H  N N 191 
GLN HB2    H  N N 192 
GLN HB3    H  N N 193 
GLN HG2    H  N N 194 
GLN HG3    H  N N 195 
GLN HE21   H  N N 196 
GLN HE22   H  N N 197 
GLN HXT    H  N N 198 
GLU N      N  N N 199 
GLU CA     C  N S 200 
GLU C      C  N N 201 
GLU O      O  N N 202 
GLU CB     C  N N 203 
GLU CG     C  N N 204 
GLU CD     C  N N 205 
GLU OE1    O  N N 206 
GLU OE2    O  N N 207 
GLU OXT    O  N N 208 
GLU H      H  N N 209 
GLU H2     H  N N 210 
GLU HA     H  N N 211 
GLU HB2    H  N N 212 
GLU HB3    H  N N 213 
GLU HG2    H  N N 214 
GLU HG3    H  N N 215 
GLU HE2    H  N N 216 
GLU HXT    H  N N 217 
GLY N      N  N N 218 
GLY CA     C  N N 219 
GLY C      C  N N 220 
GLY O      O  N N 221 
GLY OXT    O  N N 222 
GLY H      H  N N 223 
GLY H2     H  N N 224 
GLY HA2    H  N N 225 
GLY HA3    H  N N 226 
GLY HXT    H  N N 227 
GTP PG     P  N N 228 
GTP O1G    O  N N 229 
GTP O2G    O  N N 230 
GTP O3G    O  N N 231 
GTP O3B    O  N N 232 
GTP PB     P  N N 233 
GTP O1B    O  N N 234 
GTP O2B    O  N N 235 
GTP O3A    O  N N 236 
GTP PA     P  N N 237 
GTP O1A    O  N N 238 
GTP O2A    O  N N 239 
GTP "O5'"  O  N N 240 
GTP "C5'"  C  N N 241 
GTP "C4'"  C  N R 242 
GTP "O4'"  O  N N 243 
GTP "C3'"  C  N S 244 
GTP "O3'"  O  N N 245 
GTP "C2'"  C  N R 246 
GTP "O2'"  O  N N 247 
GTP "C1'"  C  N R 248 
GTP N9     N  Y N 249 
GTP C8     C  Y N 250 
GTP N7     N  Y N 251 
GTP C5     C  Y N 252 
GTP C6     C  N N 253 
GTP O6     O  N N 254 
GTP N1     N  N N 255 
GTP C2     C  N N 256 
GTP N2     N  N N 257 
GTP N3     N  N N 258 
GTP C4     C  Y N 259 
GTP HOG2   H  N N 260 
GTP HOG3   H  N N 261 
GTP HOB2   H  N N 262 
GTP HOA2   H  N N 263 
GTP "H5'"  H  N N 264 
GTP "H5''" H  N N 265 
GTP "H4'"  H  N N 266 
GTP "H3'"  H  N N 267 
GTP "HO3'" H  N N 268 
GTP "H2'"  H  N N 269 
GTP "HO2'" H  N N 270 
GTP "H1'"  H  N N 271 
GTP H8     H  N N 272 
GTP HN1    H  N N 273 
GTP HN21   H  N N 274 
GTP HN22   H  N N 275 
HIS N      N  N N 276 
HIS CA     C  N S 277 
HIS C      C  N N 278 
HIS O      O  N N 279 
HIS CB     C  N N 280 
HIS CG     C  Y N 281 
HIS ND1    N  Y N 282 
HIS CD2    C  Y N 283 
HIS CE1    C  Y N 284 
HIS NE2    N  Y N 285 
HIS OXT    O  N N 286 
HIS H      H  N N 287 
HIS H2     H  N N 288 
HIS HA     H  N N 289 
HIS HB2    H  N N 290 
HIS HB3    H  N N 291 
HIS HD1    H  N N 292 
HIS HD2    H  N N 293 
HIS HE1    H  N N 294 
HIS HE2    H  N N 295 
HIS HXT    H  N N 296 
ILE N      N  N N 297 
ILE CA     C  N S 298 
ILE C      C  N N 299 
ILE O      O  N N 300 
ILE CB     C  N S 301 
ILE CG1    C  N N 302 
ILE CG2    C  N N 303 
ILE CD1    C  N N 304 
ILE OXT    O  N N 305 
ILE H      H  N N 306 
ILE H2     H  N N 307 
ILE HA     H  N N 308 
ILE HB     H  N N 309 
ILE HG12   H  N N 310 
ILE HG13   H  N N 311 
ILE HG21   H  N N 312 
ILE HG22   H  N N 313 
ILE HG23   H  N N 314 
ILE HD11   H  N N 315 
ILE HD12   H  N N 316 
ILE HD13   H  N N 317 
ILE HXT    H  N N 318 
LEU N      N  N N 319 
LEU CA     C  N S 320 
LEU C      C  N N 321 
LEU O      O  N N 322 
LEU CB     C  N N 323 
LEU CG     C  N N 324 
LEU CD1    C  N N 325 
LEU CD2    C  N N 326 
LEU OXT    O  N N 327 
LEU H      H  N N 328 
LEU H2     H  N N 329 
LEU HA     H  N N 330 
LEU HB2    H  N N 331 
LEU HB3    H  N N 332 
LEU HG     H  N N 333 
LEU HD11   H  N N 334 
LEU HD12   H  N N 335 
LEU HD13   H  N N 336 
LEU HD21   H  N N 337 
LEU HD22   H  N N 338 
LEU HD23   H  N N 339 
LEU HXT    H  N N 340 
LYS N      N  N N 341 
LYS CA     C  N S 342 
LYS C      C  N N 343 
LYS O      O  N N 344 
LYS CB     C  N N 345 
LYS CG     C  N N 346 
LYS CD     C  N N 347 
LYS CE     C  N N 348 
LYS NZ     N  N N 349 
LYS OXT    O  N N 350 
LYS H      H  N N 351 
LYS H2     H  N N 352 
LYS HA     H  N N 353 
LYS HB2    H  N N 354 
LYS HB3    H  N N 355 
LYS HG2    H  N N 356 
LYS HG3    H  N N 357 
LYS HD2    H  N N 358 
LYS HD3    H  N N 359 
LYS HE2    H  N N 360 
LYS HE3    H  N N 361 
LYS HZ1    H  N N 362 
LYS HZ2    H  N N 363 
LYS HZ3    H  N N 364 
LYS HXT    H  N N 365 
MET N      N  N N 366 
MET CA     C  N S 367 
MET C      C  N N 368 
MET O      O  N N 369 
MET CB     C  N N 370 
MET CG     C  N N 371 
MET SD     S  N N 372 
MET CE     C  N N 373 
MET OXT    O  N N 374 
MET H      H  N N 375 
MET H2     H  N N 376 
MET HA     H  N N 377 
MET HB2    H  N N 378 
MET HB3    H  N N 379 
MET HG2    H  N N 380 
MET HG3    H  N N 381 
MET HE1    H  N N 382 
MET HE2    H  N N 383 
MET HE3    H  N N 384 
MET HXT    H  N N 385 
MG  MG     MG N N 386 
PHE N      N  N N 387 
PHE CA     C  N S 388 
PHE C      C  N N 389 
PHE O      O  N N 390 
PHE CB     C  N N 391 
PHE CG     C  Y N 392 
PHE CD1    C  Y N 393 
PHE CD2    C  Y N 394 
PHE CE1    C  Y N 395 
PHE CE2    C  Y N 396 
PHE CZ     C  Y N 397 
PHE OXT    O  N N 398 
PHE H      H  N N 399 
PHE H2     H  N N 400 
PHE HA     H  N N 401 
PHE HB2    H  N N 402 
PHE HB3    H  N N 403 
PHE HD1    H  N N 404 
PHE HD2    H  N N 405 
PHE HE1    H  N N 406 
PHE HE2    H  N N 407 
PHE HZ     H  N N 408 
PHE HXT    H  N N 409 
PRO N      N  N N 410 
PRO CA     C  N S 411 
PRO C      C  N N 412 
PRO O      O  N N 413 
PRO CB     C  N N 414 
PRO CG     C  N N 415 
PRO CD     C  N N 416 
PRO OXT    O  N N 417 
PRO H      H  N N 418 
PRO HA     H  N N 419 
PRO HB2    H  N N 420 
PRO HB3    H  N N 421 
PRO HG2    H  N N 422 
PRO HG3    H  N N 423 
PRO HD2    H  N N 424 
PRO HD3    H  N N 425 
PRO HXT    H  N N 426 
SER N      N  N N 427 
SER CA     C  N S 428 
SER C      C  N N 429 
SER O      O  N N 430 
SER CB     C  N N 431 
SER OG     O  N N 432 
SER OXT    O  N N 433 
SER H      H  N N 434 
SER H2     H  N N 435 
SER HA     H  N N 436 
SER HB2    H  N N 437 
SER HB3    H  N N 438 
SER HG     H  N N 439 
SER HXT    H  N N 440 
TA1 O01    O  N N 441 
TA1 C01    C  N S 442 
TA1 C02    C  N S 443 
TA1 O02    O  N N 444 
TA1 C03    C  N N 445 
TA1 O03    O  N N 446 
TA1 C04    C  Y N 447 
TA1 C05    C  Y N 448 
TA1 C06    C  Y N 449 
TA1 C07    C  Y N 450 
TA1 C08    C  Y N 451 
TA1 C09    C  Y N 452 
TA1 C10    C  N R 453 
TA1 C11    C  N S 454 
TA1 O04    O  N N 455 
TA1 C12    C  N N 456 
TA1 O05    O  N N 457 
TA1 C13    C  N N 458 
TA1 C14    C  N N 459 
TA1 O06    O  N N 460 
TA1 C15    C  N R 461 
TA1 C16    C  N N 462 
TA1 C17    C  N S 463 
TA1 O07    O  N N 464 
TA1 C18    C  N S 465 
TA1 C19    C  N N 466 
TA1 C20    C  N N 467 
TA1 O08    O  N N 468 
TA1 C21    C  N R 469 
TA1 O09    O  N N 470 
TA1 C22    C  N N 471 
TA1 O10    O  N N 472 
TA1 C23    C  N N 473 
TA1 C24    C  N N 474 
TA1 C25    C  N N 475 
TA1 C26    C  N S 476 
TA1 O11    O  N N 477 
TA1 C27    C  N N 478 
TA1 O12    O  N N 479 
TA1 C28    C  N R 480 
TA1 O13    O  N N 481 
TA1 C29    C  N S 482 
TA1 N01    N  N N 483 
TA1 C30    C  N N 484 
TA1 O14    O  N N 485 
TA1 C31    C  Y N 486 
TA1 C32    C  Y N 487 
TA1 C33    C  Y N 488 
TA1 C34    C  Y N 489 
TA1 C35    C  Y N 490 
TA1 C36    C  Y N 491 
TA1 C37    C  Y N 492 
TA1 C38    C  Y N 493 
TA1 C39    C  Y N 494 
TA1 C40    C  Y N 495 
TA1 C41    C  Y N 496 
TA1 C42    C  Y N 497 
TA1 C43    C  N N 498 
TA1 C44    C  N N 499 
TA1 C45    C  N N 500 
TA1 C46    C  N N 501 
TA1 C47    C  N N 502 
TA1 H011   H  N N 503 
TA1 H021   H  N N 504 
TA1 H051   H  N N 505 
TA1 H061   H  N N 506 
TA1 HC71   H  N N 507 
TA1 H081   H  N N 508 
TA1 H091   H  N N 509 
TA1 H101   H  N N 510 
TA1 H131   H  N N 511 
TA1 H132   H  N N 512 
TA1 H133   H  N N 513 
TA1 H141   H  N N 514 
TA1 H142   H  N N 515 
TA1 H151   H  N N 516 
TA1 H161   H  N N 517 
TA1 H162   H  N N 518 
TA1 H171   H  N N 519 
TA1 H071   H  N N 520 
TA1 H191   H  N N 521 
TA1 H192   H  N N 522 
TA1 H193   H  N N 523 
TA1 H211   H  N N 524 
TA1 H231   H  N N 525 
TA1 H232   H  N N 526 
TA1 H233   H  N N 527 
TA1 H261   H  N N 528 
TA1 H281   H  N N 529 
TA1 HO11   H  N N 530 
TA1 H291   H  N N 531 
TA1 HN01   H  N N 532 
TA1 H321   H  N N 533 
TA1 H331   H  N N 534 
TA1 H341   H  N N 535 
TA1 H351   H  N N 536 
TA1 H361   H  N N 537 
TA1 H381   H  N N 538 
TA1 H391   H  N N 539 
TA1 H401   H  N N 540 
TA1 H411   H  N N 541 
TA1 H421   H  N N 542 
TA1 H431   H  N N 543 
TA1 H432   H  N N 544 
TA1 H441   H  N N 545 
TA1 H442   H  N N 546 
TA1 H443   H  N N 547 
TA1 H461   H  N N 548 
TA1 H462   H  N N 549 
TA1 H463   H  N N 550 
TA1 H471   H  N N 551 
TA1 H472   H  N N 552 
TA1 H473   H  N N 553 
THR N      N  N N 554 
THR CA     C  N S 555 
THR C      C  N N 556 
THR O      O  N N 557 
THR CB     C  N R 558 
THR OG1    O  N N 559 
THR CG2    C  N N 560 
THR OXT    O  N N 561 
THR H      H  N N 562 
THR H2     H  N N 563 
THR HA     H  N N 564 
THR HB     H  N N 565 
THR HG1    H  N N 566 
THR HG21   H  N N 567 
THR HG22   H  N N 568 
THR HG23   H  N N 569 
THR HXT    H  N N 570 
TRP N      N  N N 571 
TRP CA     C  N S 572 
TRP C      C  N N 573 
TRP O      O  N N 574 
TRP CB     C  N N 575 
TRP CG     C  Y N 576 
TRP CD1    C  Y N 577 
TRP CD2    C  Y N 578 
TRP NE1    N  Y N 579 
TRP CE2    C  Y N 580 
TRP CE3    C  Y N 581 
TRP CZ2    C  Y N 582 
TRP CZ3    C  Y N 583 
TRP CH2    C  Y N 584 
TRP OXT    O  N N 585 
TRP H      H  N N 586 
TRP H2     H  N N 587 
TRP HA     H  N N 588 
TRP HB2    H  N N 589 
TRP HB3    H  N N 590 
TRP HD1    H  N N 591 
TRP HE1    H  N N 592 
TRP HE3    H  N N 593 
TRP HZ2    H  N N 594 
TRP HZ3    H  N N 595 
TRP HH2    H  N N 596 
TRP HXT    H  N N 597 
TYR N      N  N N 598 
TYR CA     C  N S 599 
TYR C      C  N N 600 
TYR O      O  N N 601 
TYR CB     C  N N 602 
TYR CG     C  Y N 603 
TYR CD1    C  Y N 604 
TYR CD2    C  Y N 605 
TYR CE1    C  Y N 606 
TYR CE2    C  Y N 607 
TYR CZ     C  Y N 608 
TYR OH     O  N N 609 
TYR OXT    O  N N 610 
TYR H      H  N N 611 
TYR H2     H  N N 612 
TYR HA     H  N N 613 
TYR HB2    H  N N 614 
TYR HB3    H  N N 615 
TYR HD1    H  N N 616 
TYR HD2    H  N N 617 
TYR HE1    H  N N 618 
TYR HE2    H  N N 619 
TYR HH     H  N N 620 
TYR HXT    H  N N 621 
VAL N      N  N N 622 
VAL CA     C  N S 623 
VAL C      C  N N 624 
VAL O      O  N N 625 
VAL CB     C  N N 626 
VAL CG1    C  N N 627 
VAL CG2    C  N N 628 
VAL OXT    O  N N 629 
VAL H      H  N N 630 
VAL H2     H  N N 631 
VAL HA     H  N N 632 
VAL HB     H  N N 633 
VAL HG11   H  N N 634 
VAL HG12   H  N N 635 
VAL HG13   H  N N 636 
VAL HG21   H  N N 637 
VAL HG22   H  N N 638 
VAL HG23   H  N N 639 
VAL HXT    H  N N 640 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GDP PB    O1B    doub N N 133 
GDP PB    O2B    sing N N 134 
GDP PB    O3B    sing N N 135 
GDP PB    O3A    sing N N 136 
GDP O2B   HOB2   sing N N 137 
GDP O3B   HOB3   sing N N 138 
GDP O3A   PA     sing N N 139 
GDP PA    O1A    doub N N 140 
GDP PA    O2A    sing N N 141 
GDP PA    "O5'"  sing N N 142 
GDP O2A   HOA2   sing N N 143 
GDP "O5'" "C5'"  sing N N 144 
GDP "C5'" "C4'"  sing N N 145 
GDP "C5'" "H5'"  sing N N 146 
GDP "C5'" "H5''" sing N N 147 
GDP "C4'" "O4'"  sing N N 148 
GDP "C4'" "C3'"  sing N N 149 
GDP "C4'" "H4'"  sing N N 150 
GDP "O4'" "C1'"  sing N N 151 
GDP "C3'" "O3'"  sing N N 152 
GDP "C3'" "C2'"  sing N N 153 
GDP "C3'" "H3'"  sing N N 154 
GDP "O3'" "HO3'" sing N N 155 
GDP "C2'" "O2'"  sing N N 156 
GDP "C2'" "C1'"  sing N N 157 
GDP "C2'" "H2'"  sing N N 158 
GDP "O2'" "HO2'" sing N N 159 
GDP "C1'" N9     sing N N 160 
GDP "C1'" "H1'"  sing N N 161 
GDP N9    C8     sing Y N 162 
GDP N9    C4     sing Y N 163 
GDP C8    N7     doub Y N 164 
GDP C8    H8     sing N N 165 
GDP N7    C5     sing Y N 166 
GDP C5    C6     sing N N 167 
GDP C5    C4     doub Y N 168 
GDP C6    O6     doub N N 169 
GDP C6    N1     sing N N 170 
GDP N1    C2     sing N N 171 
GDP N1    HN1    sing N N 172 
GDP C2    N2     sing N N 173 
GDP C2    N3     doub N N 174 
GDP N2    HN21   sing N N 175 
GDP N2    HN22   sing N N 176 
GDP N3    C4     sing N N 177 
GLN N     CA     sing N N 178 
GLN N     H      sing N N 179 
GLN N     H2     sing N N 180 
GLN CA    C      sing N N 181 
GLN CA    CB     sing N N 182 
GLN CA    HA     sing N N 183 
GLN C     O      doub N N 184 
GLN C     OXT    sing N N 185 
GLN CB    CG     sing N N 186 
GLN CB    HB2    sing N N 187 
GLN CB    HB3    sing N N 188 
GLN CG    CD     sing N N 189 
GLN CG    HG2    sing N N 190 
GLN CG    HG3    sing N N 191 
GLN CD    OE1    doub N N 192 
GLN CD    NE2    sing N N 193 
GLN NE2   HE21   sing N N 194 
GLN NE2   HE22   sing N N 195 
GLN OXT   HXT    sing N N 196 
GLU N     CA     sing N N 197 
GLU N     H      sing N N 198 
GLU N     H2     sing N N 199 
GLU CA    C      sing N N 200 
GLU CA    CB     sing N N 201 
GLU CA    HA     sing N N 202 
GLU C     O      doub N N 203 
GLU C     OXT    sing N N 204 
GLU CB    CG     sing N N 205 
GLU CB    HB2    sing N N 206 
GLU CB    HB3    sing N N 207 
GLU CG    CD     sing N N 208 
GLU CG    HG2    sing N N 209 
GLU CG    HG3    sing N N 210 
GLU CD    OE1    doub N N 211 
GLU CD    OE2    sing N N 212 
GLU OE2   HE2    sing N N 213 
GLU OXT   HXT    sing N N 214 
GLY N     CA     sing N N 215 
GLY N     H      sing N N 216 
GLY N     H2     sing N N 217 
GLY CA    C      sing N N 218 
GLY CA    HA2    sing N N 219 
GLY CA    HA3    sing N N 220 
GLY C     O      doub N N 221 
GLY C     OXT    sing N N 222 
GLY OXT   HXT    sing N N 223 
GTP PG    O1G    doub N N 224 
GTP PG    O2G    sing N N 225 
GTP PG    O3G    sing N N 226 
GTP PG    O3B    sing N N 227 
GTP O2G   HOG2   sing N N 228 
GTP O3G   HOG3   sing N N 229 
GTP O3B   PB     sing N N 230 
GTP PB    O1B    doub N N 231 
GTP PB    O2B    sing N N 232 
GTP PB    O3A    sing N N 233 
GTP O2B   HOB2   sing N N 234 
GTP O3A   PA     sing N N 235 
GTP PA    O1A    doub N N 236 
GTP PA    O2A    sing N N 237 
GTP PA    "O5'"  sing N N 238 
GTP O2A   HOA2   sing N N 239 
GTP "O5'" "C5'"  sing N N 240 
GTP "C5'" "C4'"  sing N N 241 
GTP "C5'" "H5'"  sing N N 242 
GTP "C5'" "H5''" sing N N 243 
GTP "C4'" "O4'"  sing N N 244 
GTP "C4'" "C3'"  sing N N 245 
GTP "C4'" "H4'"  sing N N 246 
GTP "O4'" "C1'"  sing N N 247 
GTP "C3'" "O3'"  sing N N 248 
GTP "C3'" "C2'"  sing N N 249 
GTP "C3'" "H3'"  sing N N 250 
GTP "O3'" "HO3'" sing N N 251 
GTP "C2'" "O2'"  sing N N 252 
GTP "C2'" "C1'"  sing N N 253 
GTP "C2'" "H2'"  sing N N 254 
GTP "O2'" "HO2'" sing N N 255 
GTP "C1'" N9     sing N N 256 
GTP "C1'" "H1'"  sing N N 257 
GTP N9    C8     sing Y N 258 
GTP N9    C4     sing Y N 259 
GTP C8    N7     doub Y N 260 
GTP C8    H8     sing N N 261 
GTP N7    C5     sing Y N 262 
GTP C5    C6     sing N N 263 
GTP C5    C4     doub Y N 264 
GTP C6    O6     doub N N 265 
GTP C6    N1     sing N N 266 
GTP N1    C2     sing N N 267 
GTP N1    HN1    sing N N 268 
GTP C2    N2     sing N N 269 
GTP C2    N3     doub N N 270 
GTP N2    HN21   sing N N 271 
GTP N2    HN22   sing N N 272 
GTP N3    C4     sing N N 273 
HIS N     CA     sing N N 274 
HIS N     H      sing N N 275 
HIS N     H2     sing N N 276 
HIS CA    C      sing N N 277 
HIS CA    CB     sing N N 278 
HIS CA    HA     sing N N 279 
HIS C     O      doub N N 280 
HIS C     OXT    sing N N 281 
HIS CB    CG     sing N N 282 
HIS CB    HB2    sing N N 283 
HIS CB    HB3    sing N N 284 
HIS CG    ND1    sing Y N 285 
HIS CG    CD2    doub Y N 286 
HIS ND1   CE1    doub Y N 287 
HIS ND1   HD1    sing N N 288 
HIS CD2   NE2    sing Y N 289 
HIS CD2   HD2    sing N N 290 
HIS CE1   NE2    sing Y N 291 
HIS CE1   HE1    sing N N 292 
HIS NE2   HE2    sing N N 293 
HIS OXT   HXT    sing N N 294 
ILE N     CA     sing N N 295 
ILE N     H      sing N N 296 
ILE N     H2     sing N N 297 
ILE CA    C      sing N N 298 
ILE CA    CB     sing N N 299 
ILE CA    HA     sing N N 300 
ILE C     O      doub N N 301 
ILE C     OXT    sing N N 302 
ILE CB    CG1    sing N N 303 
ILE CB    CG2    sing N N 304 
ILE CB    HB     sing N N 305 
ILE CG1   CD1    sing N N 306 
ILE CG1   HG12   sing N N 307 
ILE CG1   HG13   sing N N 308 
ILE CG2   HG21   sing N N 309 
ILE CG2   HG22   sing N N 310 
ILE CG2   HG23   sing N N 311 
ILE CD1   HD11   sing N N 312 
ILE CD1   HD12   sing N N 313 
ILE CD1   HD13   sing N N 314 
ILE OXT   HXT    sing N N 315 
LEU N     CA     sing N N 316 
LEU N     H      sing N N 317 
LEU N     H2     sing N N 318 
LEU CA    C      sing N N 319 
LEU CA    CB     sing N N 320 
LEU CA    HA     sing N N 321 
LEU C     O      doub N N 322 
LEU C     OXT    sing N N 323 
LEU CB    CG     sing N N 324 
LEU CB    HB2    sing N N 325 
LEU CB    HB3    sing N N 326 
LEU CG    CD1    sing N N 327 
LEU CG    CD2    sing N N 328 
LEU CG    HG     sing N N 329 
LEU CD1   HD11   sing N N 330 
LEU CD1   HD12   sing N N 331 
LEU CD1   HD13   sing N N 332 
LEU CD2   HD21   sing N N 333 
LEU CD2   HD22   sing N N 334 
LEU CD2   HD23   sing N N 335 
LEU OXT   HXT    sing N N 336 
LYS N     CA     sing N N 337 
LYS N     H      sing N N 338 
LYS N     H2     sing N N 339 
LYS CA    C      sing N N 340 
LYS CA    CB     sing N N 341 
LYS CA    HA     sing N N 342 
LYS C     O      doub N N 343 
LYS C     OXT    sing N N 344 
LYS CB    CG     sing N N 345 
LYS CB    HB2    sing N N 346 
LYS CB    HB3    sing N N 347 
LYS CG    CD     sing N N 348 
LYS CG    HG2    sing N N 349 
LYS CG    HG3    sing N N 350 
LYS CD    CE     sing N N 351 
LYS CD    HD2    sing N N 352 
LYS CD    HD3    sing N N 353 
LYS CE    NZ     sing N N 354 
LYS CE    HE2    sing N N 355 
LYS CE    HE3    sing N N 356 
LYS NZ    HZ1    sing N N 357 
LYS NZ    HZ2    sing N N 358 
LYS NZ    HZ3    sing N N 359 
LYS OXT   HXT    sing N N 360 
MET N     CA     sing N N 361 
MET N     H      sing N N 362 
MET N     H2     sing N N 363 
MET CA    C      sing N N 364 
MET CA    CB     sing N N 365 
MET CA    HA     sing N N 366 
MET C     O      doub N N 367 
MET C     OXT    sing N N 368 
MET CB    CG     sing N N 369 
MET CB    HB2    sing N N 370 
MET CB    HB3    sing N N 371 
MET CG    SD     sing N N 372 
MET CG    HG2    sing N N 373 
MET CG    HG3    sing N N 374 
MET SD    CE     sing N N 375 
MET CE    HE1    sing N N 376 
MET CE    HE2    sing N N 377 
MET CE    HE3    sing N N 378 
MET OXT   HXT    sing N N 379 
PHE N     CA     sing N N 380 
PHE N     H      sing N N 381 
PHE N     H2     sing N N 382 
PHE CA    C      sing N N 383 
PHE CA    CB     sing N N 384 
PHE CA    HA     sing N N 385 
PHE C     O      doub N N 386 
PHE C     OXT    sing N N 387 
PHE CB    CG     sing N N 388 
PHE CB    HB2    sing N N 389 
PHE CB    HB3    sing N N 390 
PHE CG    CD1    doub Y N 391 
PHE CG    CD2    sing Y N 392 
PHE CD1   CE1    sing Y N 393 
PHE CD1   HD1    sing N N 394 
PHE CD2   CE2    doub Y N 395 
PHE CD2   HD2    sing N N 396 
PHE CE1   CZ     doub Y N 397 
PHE CE1   HE1    sing N N 398 
PHE CE2   CZ     sing Y N 399 
PHE CE2   HE2    sing N N 400 
PHE CZ    HZ     sing N N 401 
PHE OXT   HXT    sing N N 402 
PRO N     CA     sing N N 403 
PRO N     CD     sing N N 404 
PRO N     H      sing N N 405 
PRO CA    C      sing N N 406 
PRO CA    CB     sing N N 407 
PRO CA    HA     sing N N 408 
PRO C     O      doub N N 409 
PRO C     OXT    sing N N 410 
PRO CB    CG     sing N N 411 
PRO CB    HB2    sing N N 412 
PRO CB    HB3    sing N N 413 
PRO CG    CD     sing N N 414 
PRO CG    HG2    sing N N 415 
PRO CG    HG3    sing N N 416 
PRO CD    HD2    sing N N 417 
PRO CD    HD3    sing N N 418 
PRO OXT   HXT    sing N N 419 
SER N     CA     sing N N 420 
SER N     H      sing N N 421 
SER N     H2     sing N N 422 
SER CA    C      sing N N 423 
SER CA    CB     sing N N 424 
SER CA    HA     sing N N 425 
SER C     O      doub N N 426 
SER C     OXT    sing N N 427 
SER CB    OG     sing N N 428 
SER CB    HB2    sing N N 429 
SER CB    HB3    sing N N 430 
SER OG    HG     sing N N 431 
SER OXT   HXT    sing N N 432 
TA1 O01   C01    sing N N 433 
TA1 O01   H011   sing N N 434 
TA1 C01   C02    sing N N 435 
TA1 C01   C43    sing N N 436 
TA1 C01   C45    sing N N 437 
TA1 C02   O02    sing N N 438 
TA1 C02   C10    sing N N 439 
TA1 C02   H021   sing N N 440 
TA1 O02   C03    sing N N 441 
TA1 C03   O03    doub N N 442 
TA1 C03   C04    sing N N 443 
TA1 C04   C05    doub Y N 444 
TA1 C04   C09    sing Y N 445 
TA1 C05   C06    sing Y N 446 
TA1 C05   H051   sing N N 447 
TA1 C06   C07    doub Y N 448 
TA1 C06   H061   sing N N 449 
TA1 C07   C08    sing Y N 450 
TA1 C07   HC71   sing N N 451 
TA1 C08   C09    doub Y N 452 
TA1 C08   H081   sing N N 453 
TA1 C09   H091   sing N N 454 
TA1 C10   C11    sing N N 455 
TA1 C10   C18    sing N N 456 
TA1 C10   H101   sing N N 457 
TA1 C11   O04    sing N N 458 
TA1 C11   C14    sing N N 459 
TA1 C11   C15    sing N N 460 
TA1 O04   C12    sing N N 461 
TA1 C12   O05    doub N N 462 
TA1 C12   C13    sing N N 463 
TA1 C13   H131   sing N N 464 
TA1 C13   H132   sing N N 465 
TA1 C13   H133   sing N N 466 
TA1 C14   O06    sing N N 467 
TA1 C14   H141   sing N N 468 
TA1 C14   H142   sing N N 469 
TA1 O06   C15    sing N N 470 
TA1 C15   C16    sing N N 471 
TA1 C15   H151   sing N N 472 
TA1 C16   C17    sing N N 473 
TA1 C16   H161   sing N N 474 
TA1 C16   H162   sing N N 475 
TA1 C17   O07    sing N N 476 
TA1 C17   C18    sing N N 477 
TA1 C17   H171   sing N N 478 
TA1 O07   H071   sing N N 479 
TA1 C18   C19    sing N N 480 
TA1 C18   C20    sing N N 481 
TA1 C19   H191   sing N N 482 
TA1 C19   H192   sing N N 483 
TA1 C19   H193   sing N N 484 
TA1 C20   O08    doub N N 485 
TA1 C20   C21    sing N N 486 
TA1 C21   O09    sing N N 487 
TA1 C21   C24    sing N N 488 
TA1 C21   H211   sing N N 489 
TA1 O09   C22    sing N N 490 
TA1 C22   O10    doub N N 491 
TA1 C22   C23    sing N N 492 
TA1 C23   H231   sing N N 493 
TA1 C23   H232   sing N N 494 
TA1 C23   H233   sing N N 495 
TA1 C24   C25    doub N N 496 
TA1 C24   C45    sing N N 497 
TA1 C25   C26    sing N N 498 
TA1 C25   C44    sing N N 499 
TA1 C26   O11    sing N N 500 
TA1 C26   C43    sing N N 501 
TA1 C26   H261   sing N N 502 
TA1 O11   C27    sing N N 503 
TA1 C27   O12    doub N N 504 
TA1 C27   C28    sing N N 505 
TA1 C28   O13    sing N N 506 
TA1 C28   C29    sing N N 507 
TA1 C28   H281   sing N N 508 
TA1 O13   HO11   sing N N 509 
TA1 C29   N01    sing N N 510 
TA1 C29   C37    sing N N 511 
TA1 C29   H291   sing N N 512 
TA1 N01   C30    sing N N 513 
TA1 N01   HN01   sing N N 514 
TA1 C30   O14    doub N N 515 
TA1 C30   C31    sing N N 516 
TA1 C31   C32    doub Y N 517 
TA1 C31   C36    sing Y N 518 
TA1 C32   C33    sing Y N 519 
TA1 C32   H321   sing N N 520 
TA1 C33   C34    doub Y N 521 
TA1 C33   H331   sing N N 522 
TA1 C34   C35    sing Y N 523 
TA1 C34   H341   sing N N 524 
TA1 C35   C36    doub Y N 525 
TA1 C35   H351   sing N N 526 
TA1 C36   H361   sing N N 527 
TA1 C37   C38    doub Y N 528 
TA1 C37   C42    sing Y N 529 
TA1 C38   C39    sing Y N 530 
TA1 C38   H381   sing N N 531 
TA1 C39   C40    doub Y N 532 
TA1 C39   H391   sing N N 533 
TA1 C40   C41    sing Y N 534 
TA1 C40   H401   sing N N 535 
TA1 C41   C42    doub Y N 536 
TA1 C41   H411   sing N N 537 
TA1 C42   H421   sing N N 538 
TA1 C43   H431   sing N N 539 
TA1 C43   H432   sing N N 540 
TA1 C44   H441   sing N N 541 
TA1 C44   H442   sing N N 542 
TA1 C44   H443   sing N N 543 
TA1 C45   C46    sing N N 544 
TA1 C45   C47    sing N N 545 
TA1 C46   H461   sing N N 546 
TA1 C46   H462   sing N N 547 
TA1 C46   H463   sing N N 548 
TA1 C47   H471   sing N N 549 
TA1 C47   H472   sing N N 550 
TA1 C47   H473   sing N N 551 
THR N     CA     sing N N 552 
THR N     H      sing N N 553 
THR N     H2     sing N N 554 
THR CA    C      sing N N 555 
THR CA    CB     sing N N 556 
THR CA    HA     sing N N 557 
THR C     O      doub N N 558 
THR C     OXT    sing N N 559 
THR CB    OG1    sing N N 560 
THR CB    CG2    sing N N 561 
THR CB    HB     sing N N 562 
THR OG1   HG1    sing N N 563 
THR CG2   HG21   sing N N 564 
THR CG2   HG22   sing N N 565 
THR CG2   HG23   sing N N 566 
THR OXT   HXT    sing N N 567 
TRP N     CA     sing N N 568 
TRP N     H      sing N N 569 
TRP N     H2     sing N N 570 
TRP CA    C      sing N N 571 
TRP CA    CB     sing N N 572 
TRP CA    HA     sing N N 573 
TRP C     O      doub N N 574 
TRP C     OXT    sing N N 575 
TRP CB    CG     sing N N 576 
TRP CB    HB2    sing N N 577 
TRP CB    HB3    sing N N 578 
TRP CG    CD1    doub Y N 579 
TRP CG    CD2    sing Y N 580 
TRP CD1   NE1    sing Y N 581 
TRP CD1   HD1    sing N N 582 
TRP CD2   CE2    doub Y N 583 
TRP CD2   CE3    sing Y N 584 
TRP NE1   CE2    sing Y N 585 
TRP NE1   HE1    sing N N 586 
TRP CE2   CZ2    sing Y N 587 
TRP CE3   CZ3    doub Y N 588 
TRP CE3   HE3    sing N N 589 
TRP CZ2   CH2    doub Y N 590 
TRP CZ2   HZ2    sing N N 591 
TRP CZ3   CH2    sing Y N 592 
TRP CZ3   HZ3    sing N N 593 
TRP CH2   HH2    sing N N 594 
TRP OXT   HXT    sing N N 595 
TYR N     CA     sing N N 596 
TYR N     H      sing N N 597 
TYR N     H2     sing N N 598 
TYR CA    C      sing N N 599 
TYR CA    CB     sing N N 600 
TYR CA    HA     sing N N 601 
TYR C     O      doub N N 602 
TYR C     OXT    sing N N 603 
TYR CB    CG     sing N N 604 
TYR CB    HB2    sing N N 605 
TYR CB    HB3    sing N N 606 
TYR CG    CD1    doub Y N 607 
TYR CG    CD2    sing Y N 608 
TYR CD1   CE1    sing Y N 609 
TYR CD1   HD1    sing N N 610 
TYR CD2   CE2    doub Y N 611 
TYR CD2   HD2    sing N N 612 
TYR CE1   CZ     doub Y N 613 
TYR CE1   HE1    sing N N 614 
TYR CE2   CZ     sing Y N 615 
TYR CE2   HE2    sing N N 616 
TYR CZ    OH     sing N N 617 
TYR OH    HH     sing N N 618 
TYR OXT   HXT    sing N N 619 
VAL N     CA     sing N N 620 
VAL N     H      sing N N 621 
VAL N     H2     sing N N 622 
VAL CA    C      sing N N 623 
VAL CA    CB     sing N N 624 
VAL CA    HA     sing N N 625 
VAL C     O      doub N N 626 
VAL C     OXT    sing N N 627 
VAL CB    CG1    sing N N 628 
VAL CB    CG2    sing N N 629 
VAL CB    HB     sing N N 630 
VAL CG1   HG11   sing N N 631 
VAL CG1   HG12   sing N N 632 
VAL CG1   HG13   sing N N 633 
VAL CG2   HG21   sing N N 634 
VAL CG2   HG22   sing N N 635 
VAL CG2   HG23   sing N N 636 
VAL OXT   HXT    sing N N 637 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-12-15 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           8RHH 
_em_admin.last_update        2024-11-20 
_em_admin.map_release_date   2024-11-20 
_em_admin.title              'Microtubule-associated kinesin-1 tail complex bound to AMPPNP, two-headed state' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                KILODALTONS/NANOMETER 
_em_entity_assembly_molwt.value                246 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
_em_entity_assembly_naturalsource.details 
? ? 2 2 9606 'Homo sapiens' ? ? ? ? ? 
? ? 3 3 9823 'Sus scrofa'   ? ? ? ? ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   2 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         52 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? RELION  3.0 
'IMAGE ACQUISITION'             ? 2  ? ? 1 EPU     ?   
MASKING                         ? 3  ? ? ? ?       ?   
'CTF CORRECTION'                ? 4  1 ? ? CTFFIND ?   
'LAYERLINE INDEXING'            ? 5  ? ? ? ?       ?   
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?       ?   
'MODEL FITTING'                 ? 7  ? 1 ? ?       ?   
OTHER                           ? 8  ? ? ? ?       ?   
'MODEL REFINEMENT'              ? 9  ? 1 ? ?       ?   
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?       ?   
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? RELION  ?   
CLASSIFICATION                  ? 12 1 ? ? RELION  ?   
RECONSTRUCTION                  ? 13 1 ? ? RELION  ?   
'VOLUME SELECTION'              ? 14 1 1 1 ?       ?   
'SERIES ALIGNMENT'              ? 15 1 1 1 ?       ?   
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?       ?   
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?       ?   
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?       ?   
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?       ?   
# 
_em_specimen.concentration           1.16 
_em_specimen.details                 
;Kinesin 1mg/ml 
Microtubules at 0.16mg/ml
;
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Wellcome Trust'                                                 'United Kingdom' 206175/Z/17/Z 1 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/V006568/1  2 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/S000828/1  3 
# 
_atom_sites.entry_id                    8RHH 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . MET A 1 1   ? 126.160 186.027 104.385 1.00 70.27  ? 1    MET B N     1 
ATOM   2     C  CA    . MET A 1 1   ? 126.840 185.017 103.586 1.00 66.20  ? 1    MET B CA    1 
ATOM   3     C  C     . MET A 1 1   ? 128.226 184.741 104.153 1.00 67.00  ? 1    MET B C     1 
ATOM   4     O  O     . MET A 1 1   ? 128.999 185.667 104.395 1.00 71.47  ? 1    MET B O     1 
ATOM   5     C  CB    . MET A 1 1   ? 126.937 185.464 102.129 1.00 70.04  ? 1    MET B CB    1 
ATOM   6     C  CG    . MET A 1 1   ? 126.868 184.331 101.125 1.00 74.41  ? 1    MET B CG    1 
ATOM   7     S  SD    . MET A 1 1   ? 126.742 184.931 99.432  1.00 89.09  ? 1    MET B SD    1 
ATOM   8     C  CE    . MET A 1 1   ? 125.320 186.009 99.565  1.00 70.71  ? 1    MET B CE    1 
ATOM   9     N  N     . ARG A 1 2   ? 128.526 183.459 104.364 1.00 60.59  ? 2    ARG B N     1 
ATOM   10    C  CA    . ARG A 1 2   ? 129.771 183.016 104.991 1.00 61.45  ? 2    ARG B CA    1 
ATOM   11    C  C     . ARG A 1 2   ? 129.935 183.650 106.374 1.00 61.11  ? 2    ARG B C     1 
ATOM   12    O  O     . ARG A 1 2   ? 130.864 184.415 106.638 1.00 66.53  ? 2    ARG B O     1 
ATOM   13    C  CB    . ARG A 1 2   ? 130.975 183.305 104.091 1.00 60.53  ? 2    ARG B CB    1 
ATOM   14    C  CG    . ARG A 1 2   ? 130.981 182.500 102.808 1.00 60.67  ? 2    ARG B CG    1 
ATOM   15    C  CD    . ARG A 1 2   ? 132.093 182.943 101.883 1.00 58.31  ? 2    ARG B CD    1 
ATOM   16    N  NE    . ARG A 1 2   ? 132.060 184.380 101.654 1.00 57.86  ? 2    ARG B NE    1 
ATOM   17    C  CZ    . ARG A 1 2   ? 132.953 185.043 100.934 1.00 59.91  ? 2    ARG B CZ    1 
ATOM   18    N  NH1   . ARG A 1 2   ? 133.973 184.427 100.360 1.00 63.44  ? 2    ARG B NH1   1 
ATOM   19    N  NH2   . ARG A 1 2   ? 132.820 186.357 100.789 1.00 60.88  ? 2    ARG B NH2   1 
ATOM   20    N  N     . GLU A 1 3   ? 128.997 183.318 107.255 1.00 54.64  ? 3    GLU B N     1 
ATOM   21    C  CA    . GLU A 1 3   ? 128.989 183.851 108.606 1.00 53.21  ? 3    GLU B CA    1 
ATOM   22    C  C     . GLU A 1 3   ? 129.853 183.000 109.529 1.00 60.95  ? 3    GLU B C     1 
ATOM   23    O  O     . GLU A 1 3   ? 130.108 181.820 109.276 1.00 65.29  ? 3    GLU B O     1 
ATOM   24    C  CB    . GLU A 1 3   ? 127.564 183.920 109.148 1.00 56.20  ? 3    GLU B CB    1 
ATOM   25    C  CG    . GLU A 1 3   ? 126.609 184.716 108.286 1.00 60.54  ? 3    GLU B CG    1 
ATOM   26    C  CD    . GLU A 1 3   ? 125.828 183.845 107.327 1.00 70.53  ? 3    GLU B CD    1 
ATOM   27    O  OE1   . GLU A 1 3   ? 125.853 182.610 107.494 1.00 76.18  ? 3    GLU B OE1   1 
ATOM   28    O  OE2   . GLU A 1 3   ? 125.187 184.394 106.407 1.00 70.40  ? 3    GLU B OE2   1 
ATOM   29    N  N     . ILE A 1 4   ? 130.303 183.618 110.618 1.00 55.26  ? 4    ILE B N     1 
ATOM   30    C  CA    . ILE A 1 4   ? 131.146 182.962 111.610 1.00 52.81  ? 4    ILE B CA    1 
ATOM   31    C  C     . ILE A 1 4   ? 130.507 183.140 112.978 1.00 53.26  ? 4    ILE B C     1 
ATOM   32    O  O     . ILE A 1 4   ? 130.206 184.269 113.382 1.00 58.19  ? 4    ILE B O     1 
ATOM   33    C  CB    . ILE A 1 4   ? 132.577 183.520 111.606 1.00 46.78  ? 4    ILE B CB    1 
ATOM   34    C  CG1   . ILE A 1 4   ? 133.285 183.155 110.305 1.00 49.69  ? 4    ILE B CG1   1 
ATOM   35    C  CG2   . ILE A 1 4   ? 133.356 182.995 112.797 1.00 53.55  ? 4    ILE B CG2   1 
ATOM   36    C  CD1   . ILE A 1 4   ? 134.702 183.655 110.231 1.00 53.60  ? 4    ILE B CD1   1 
ATOM   37    N  N     . VAL A 1 5   ? 130.303 182.034 113.687 1.00 48.74  ? 5    VAL B N     1 
ATOM   38    C  CA    . VAL A 1 5   ? 129.805 182.082 115.056 1.00 30.89  ? 5    VAL B CA    1 
ATOM   39    C  C     . VAL A 1 5   ? 130.993 182.156 116.004 1.00 46.69  ? 5    VAL B C     1 
ATOM   40    O  O     . VAL A 1 5   ? 131.895 181.313 115.956 1.00 65.40  ? 5    VAL B O     1 
ATOM   41    C  CB    . VAL A 1 5   ? 128.925 180.861 115.361 1.00 40.60  ? 5    VAL B CB    1 
ATOM   42    C  CG1   . VAL A 1 5   ? 128.544 180.841 116.821 1.00 46.12  ? 5    VAL B CG1   1 
ATOM   43    C  CG2   . VAL A 1 5   ? 127.689 180.869 114.488 1.00 47.79  ? 5    VAL B CG2   1 
ATOM   44    N  N     . HIS A 1 6   ? 130.997 183.166 116.868 1.00 46.70  ? 6    HIS B N     1 
ATOM   45    C  CA    . HIS A 1 6   ? 132.097 183.422 117.788 1.00 43.65  ? 6    HIS B CA    1 
ATOM   46    C  C     . HIS A 1 6   ? 131.682 183.036 119.199 1.00 47.62  ? 6    HIS B C     1 
ATOM   47    O  O     . HIS A 1 6   ? 130.602 183.419 119.659 1.00 57.40  ? 6    HIS B O     1 
ATOM   48    C  CB    . HIS A 1 6   ? 132.509 184.892 117.740 1.00 39.58  ? 6    HIS B CB    1 
ATOM   49    C  CG    . HIS A 1 6   ? 133.740 185.203 118.530 1.00 46.86  ? 6    HIS B CG    1 
ATOM   50    N  ND1   . HIS A 1 6   ? 133.733 186.060 119.609 1.00 49.68  ? 6    HIS B ND1   1 
ATOM   51    C  CD2   . HIS A 1 6   ? 135.018 184.781 118.392 1.00 51.08  ? 6    HIS B CD2   1 
ATOM   52    C  CE1   . HIS A 1 6   ? 134.954 186.149 120.104 1.00 57.29  ? 6    HIS B CE1   1 
ATOM   53    N  NE2   . HIS A 1 6   ? 135.753 185.382 119.385 1.00 60.54  ? 6    HIS B NE2   1 
ATOM   54    N  N     . ILE A 1 7   ? 132.535 182.276 119.878 1.00 44.28  ? 7    ILE B N     1 
ATOM   55    C  CA    . ILE A 1 7   ? 132.277 181.812 121.234 1.00 43.52  ? 7    ILE B CA    1 
ATOM   56    C  C     . ILE A 1 7   ? 133.446 182.226 122.113 1.00 47.96  ? 7    ILE B C     1 
ATOM   57    O  O     . ILE A 1 7   ? 134.607 182.052 121.730 1.00 59.81  ? 7    ILE B O     1 
ATOM   58    C  CB    . ILE A 1 7   ? 132.078 180.288 121.288 1.00 42.18  ? 7    ILE B CB    1 
ATOM   59    C  CG1   . ILE A 1 7   ? 130.935 179.871 120.368 1.00 44.51  ? 7    ILE B CG1   1 
ATOM   60    C  CG2   . ILE A 1 7   ? 131.790 179.846 122.708 1.00 48.44  ? 7    ILE B CG2   1 
ATOM   61    C  CD1   . ILE A 1 7   ? 130.801 178.390 120.213 1.00 45.14  ? 7    ILE B CD1   1 
ATOM   62    N  N     . GLN A 1 8   ? 133.142 182.785 123.279 1.00 41.01  ? 8    GLN B N     1 
ATOM   63    C  CA    . GLN A 1 8   ? 134.147 183.171 124.260 1.00 39.19  ? 8    GLN B CA    1 
ATOM   64    C  C     . GLN A 1 8   ? 133.930 182.338 125.512 1.00 45.43  ? 8    GLN B C     1 
ATOM   65    O  O     . GLN A 1 8   ? 132.863 182.412 126.131 1.00 57.05  ? 8    GLN B O     1 
ATOM   66    C  CB    . GLN A 1 8   ? 134.048 184.662 124.578 1.00 43.39  ? 8    GLN B CB    1 
ATOM   67    C  CG    . GLN A 1 8   ? 133.911 185.536 123.352 1.00 43.32  ? 8    GLN B CG    1 
ATOM   68    C  CD    . GLN A 1 8   ? 133.518 186.953 123.694 1.00 52.15  ? 8    GLN B CD    1 
ATOM   69    O  OE1   . GLN A 1 8   ? 133.657 187.388 124.834 1.00 50.09  ? 8    GLN B OE1   1 
ATOM   70    N  NE2   . GLN A 1 8   ? 133.020 187.683 122.706 1.00 54.94  ? 8    GLN B NE2   1 
ATOM   71    N  N     . ALA A 1 9   ? 134.933 181.551 125.885 1.00 40.09  ? 9    ALA B N     1 
ATOM   72    C  CA    . ALA A 1 9   ? 134.824 180.638 127.015 1.00 40.57  ? 9    ALA B CA    1 
ATOM   73    C  C     . ALA A 1 9   ? 135.918 180.955 128.019 1.00 42.57  ? 9    ALA B C     1 
ATOM   74    O  O     . ALA A 1 9   ? 137.105 180.861 127.696 1.00 49.18  ? 9    ALA B O     1 
ATOM   75    C  CB    . ALA A 1 9   ? 134.921 179.181 126.560 1.00 46.28  ? 9    ALA B CB    1 
ATOM   76    N  N     . GLY A 1 10  ? 135.519 181.322 129.230 1.00 50.87  ? 10   GLY B N     1 
ATOM   77    C  CA    . GLY A 1 10  ? 136.458 181.602 130.291 1.00 49.17  ? 10   GLY B CA    1 
ATOM   78    C  C     . GLY A 1 10  ? 136.908 183.049 130.326 1.00 55.80  ? 10   GLY B C     1 
ATOM   79    O  O     . GLY A 1 10  ? 136.555 183.874 129.481 1.00 67.80  ? 10   GLY B O     1 
ATOM   80    N  N     . GLN A 1 11  ? 137.720 183.350 131.340 1.00 57.84  ? 11   GLN B N     1 
ATOM   81    C  CA    . GLN A 1 11  ? 138.214 184.710 131.522 1.00 55.00  ? 11   GLN B CA    1 
ATOM   82    C  C     . GLN A 1 11  ? 139.106 185.141 130.366 1.00 56.70  ? 11   GLN B C     1 
ATOM   83    O  O     . GLN A 1 11  ? 138.928 186.234 129.812 1.00 66.16  ? 11   GLN B O     1 
ATOM   84    C  CB    . GLN A 1 11  ? 138.969 184.810 132.845 1.00 55.92  ? 11   GLN B CB    1 
ATOM   85    C  CG    . GLN A 1 11  ? 139.470 186.196 133.174 1.00 56.61  ? 11   GLN B CG    1 
ATOM   86    C  CD    . GLN A 1 11  ? 140.218 186.237 134.484 1.00 61.74  ? 11   GLN B CD    1 
ATOM   87    O  OE1   . GLN A 1 11  ? 140.602 185.200 135.022 1.00 63.30  ? 11   GLN B OE1   1 
ATOM   88    N  NE2   . GLN A 1 11  ? 140.432 187.438 135.007 1.00 60.38  ? 11   GLN B NE2   1 
ATOM   89    N  N     . CYS A 1 12  ? 140.067 184.296 129.988 1.00 54.56  ? 12   CYS B N     1 
ATOM   90    C  CA    . CYS A 1 12  ? 140.967 184.636 128.893 1.00 57.20  ? 12   CYS B CA    1 
ATOM   91    C  C     . CYS A 1 12  ? 140.201 184.820 127.594 1.00 60.22  ? 12   CYS B C     1 
ATOM   92    O  O     . CYS A 1 12  ? 140.380 185.821 126.889 1.00 67.36  ? 12   CYS B O     1 
ATOM   93    C  CB    . CYS A 1 12  ? 142.030 183.554 128.732 1.00 56.78  ? 12   CYS B CB    1 
ATOM   94    S  SG    . CYS A 1 12  ? 143.423 184.037 127.702 1.00 78.79  ? 12   CYS B SG    1 
ATOM   95    N  N     . GLY A 1 13  ? 139.335 183.862 127.267 1.00 53.11  ? 13   GLY B N     1 
ATOM   96    C  CA    . GLY A 1 13  ? 138.561 183.964 126.047 1.00 53.58  ? 13   GLY B CA    1 
ATOM   97    C  C     . GLY A 1 13  ? 137.675 185.187 126.012 1.00 53.11  ? 13   GLY B C     1 
ATOM   98    O  O     . GLY A 1 13  ? 137.598 185.867 124.988 1.00 59.56  ? 13   GLY B O     1 
ATOM   99    N  N     . ASN A 1 14  ? 137.014 185.498 127.124 1.00 41.59  ? 14   ASN B N     1 
ATOM   100   C  CA    . ASN A 1 14  ? 136.131 186.653 127.161 1.00 43.46  ? 14   ASN B CA    1 
ATOM   101   C  C     . ASN A 1 14  ? 136.890 187.964 127.032 1.00 47.77  ? 14   ASN B C     1 
ATOM   102   O  O     . ASN A 1 14  ? 136.480 188.837 126.257 1.00 58.40  ? 14   ASN B O     1 
ATOM   103   C  CB    . ASN A 1 14  ? 135.320 186.647 128.452 1.00 48.80  ? 14   ASN B CB    1 
ATOM   104   C  CG    . ASN A 1 14  ? 134.122 185.741 128.374 1.00 49.13  ? 14   ASN B CG    1 
ATOM   105   O  OD1   . ASN A 1 14  ? 133.149 186.039 127.684 1.00 56.24  ? 14   ASN B OD1   1 
ATOM   106   N  ND2   . ASN A 1 14  ? 134.183 184.622 129.078 1.00 45.91  ? 14   ASN B ND2   1 
ATOM   107   N  N     . GLN A 1 15  ? 137.988 188.128 127.767 1.00 38.88  ? 15   GLN B N     1 
ATOM   108   C  CA    . GLN A 1 15  ? 138.729 189.376 127.702 1.00 45.74  ? 15   GLN B CA    1 
ATOM   109   C  C     . GLN A 1 15  ? 139.553 189.515 126.430 1.00 55.87  ? 15   GLN B C     1 
ATOM   110   O  O     . GLN A 1 15  ? 139.995 190.626 126.119 1.00 62.55  ? 15   GLN B O     1 
ATOM   111   C  CB    . GLN A 1 15  ? 139.631 189.526 128.927 1.00 46.36  ? 15   GLN B CB    1 
ATOM   112   C  CG    . GLN A 1 15  ? 138.902 190.092 130.132 1.00 50.85  ? 15   GLN B CG    1 
ATOM   113   C  CD    . GLN A 1 15  ? 139.778 190.182 131.358 1.00 57.50  ? 15   GLN B CD    1 
ATOM   114   O  OE1   . GLN A 1 15  ? 140.790 190.880 131.360 1.00 58.94  ? 15   GLN B OE1   1 
ATOM   115   N  NE2   . GLN A 1 15  ? 139.396 189.472 132.412 1.00 57.71  ? 15   GLN B NE2   1 
ATOM   116   N  N     . ILE A 1 16  ? 139.771 188.430 125.688 1.00 51.98  ? 16   ILE B N     1 
ATOM   117   C  CA    . ILE A 1 16  ? 140.335 188.566 124.351 1.00 43.45  ? 16   ILE B CA    1 
ATOM   118   C  C     . ILE A 1 16  ? 139.249 188.861 123.320 1.00 51.75  ? 16   ILE B C     1 
ATOM   119   O  O     . ILE A 1 16  ? 139.454 189.688 122.425 1.00 56.04  ? 16   ILE B O     1 
ATOM   120   C  CB    . ILE A 1 16  ? 141.133 187.311 123.968 1.00 32.27  ? 16   ILE B CB    1 
ATOM   121   C  CG1   . ILE A 1 16  ? 142.372 187.182 124.846 1.00 43.40  ? 16   ILE B CG1   1 
ATOM   122   C  CG2   . ILE A 1 16  ? 141.553 187.367 122.519 1.00 43.71  ? 16   ILE B CG2   1 
ATOM   123   C  CD1   . ILE A 1 16  ? 143.199 185.961 124.540 1.00 46.73  ? 16   ILE B CD1   1 
ATOM   124   N  N     . GLY A 1 17  ? 138.089 188.222 123.436 1.00 57.46  ? 17   GLY B N     1 
ATOM   125   C  CA    . GLY A 1 17  ? 136.986 188.461 122.531 1.00 54.52  ? 17   GLY B CA    1 
ATOM   126   C  C     . GLY A 1 17  ? 136.426 189.862 122.626 1.00 53.39  ? 17   GLY B C     1 
ATOM   127   O  O     . GLY A 1 17  ? 135.955 190.406 121.627 1.00 61.69  ? 17   GLY B O     1 
ATOM   128   N  N     . ALA A 1 18  ? 136.449 190.454 123.820 1.00 44.32  ? 18   ALA B N     1 
ATOM   129   C  CA    . ALA A 1 18  ? 135.997 191.835 123.949 1.00 44.06  ? 18   ALA B CA    1 
ATOM   130   C  C     . ALA A 1 18  ? 136.884 192.776 123.144 1.00 52.88  ? 18   ALA B C     1 
ATOM   131   O  O     . ALA A 1 18  ? 136.386 193.650 122.419 1.00 61.73  ? 18   ALA B O     1 
ATOM   132   C  CB    . ALA A 1 18  ? 135.970 192.245 125.420 1.00 46.27  ? 18   ALA B CB    1 
ATOM   133   N  N     . LYS A 1 19  ? 138.203 192.598 123.245 1.00 48.40  ? 19   LYS B N     1 
ATOM   134   C  CA    . LYS A 1 19  ? 139.117 193.380 122.421 1.00 51.13  ? 19   LYS B CA    1 
ATOM   135   C  C     . LYS A 1 19  ? 138.909 193.082 120.945 1.00 55.40  ? 19   LYS B C     1 
ATOM   136   O  O     . LYS A 1 19  ? 138.971 193.988 120.106 1.00 62.54  ? 19   LYS B O     1 
ATOM   137   C  CB    . LYS A 1 19  ? 140.561 193.100 122.828 1.00 48.63  ? 19   LYS B CB    1 
ATOM   138   C  CG    . LYS A 1 19  ? 141.471 194.305 122.726 1.00 56.86  ? 19   LYS B CG    1 
ATOM   139   C  CD    . LYS A 1 19  ? 140.970 195.447 123.585 1.00 56.66  ? 19   LYS B CD    1 
ATOM   140   C  CE    . LYS A 1 19  ? 141.873 196.660 123.462 1.00 59.71  ? 19   LYS B CE    1 
ATOM   141   N  NZ    . LYS A 1 19  ? 141.890 197.197 122.075 1.00 59.77  ? 19   LYS B NZ    1 
ATOM   142   N  N     . PHE A 1 20  ? 138.658 191.816 120.611 1.00 49.13  ? 20   PHE B N     1 
ATOM   143   C  CA    . PHE A 1 20  ? 138.414 191.447 119.222 1.00 46.38  ? 20   PHE B CA    1 
ATOM   144   C  C     . PHE A 1 20  ? 137.196 192.167 118.666 1.00 47.99  ? 20   PHE B C     1 
ATOM   145   O  O     . PHE A 1 20  ? 137.222 192.662 117.536 1.00 59.84  ? 20   PHE B O     1 
ATOM   146   C  CB    . PHE A 1 20  ? 138.246 189.932 119.114 1.00 48.84  ? 20   PHE B CB    1 
ATOM   147   C  CG    . PHE A 1 20  ? 137.615 189.476 117.834 1.00 49.24  ? 20   PHE B CG    1 
ATOM   148   C  CD1   . PHE A 1 20  ? 138.353 189.411 116.671 1.00 52.20  ? 20   PHE B CD1   1 
ATOM   149   C  CD2   . PHE A 1 20  ? 136.291 189.080 117.801 1.00 50.59  ? 20   PHE B CD2   1 
ATOM   150   C  CE1   . PHE A 1 20  ? 137.779 188.981 115.497 1.00 50.30  ? 20   PHE B CE1   1 
ATOM   151   C  CE2   . PHE A 1 20  ? 135.713 188.649 116.629 1.00 52.09  ? 20   PHE B CE2   1 
ATOM   152   C  CZ    . PHE A 1 20  ? 136.458 188.599 115.476 1.00 50.81  ? 20   PHE B CZ    1 
ATOM   153   N  N     . TRP A 1 21  ? 136.120 192.242 119.447 1.00 48.91  ? 21   TRP B N     1 
ATOM   154   C  CA    . TRP A 1 21  ? 134.906 192.888 118.965 1.00 47.93  ? 21   TRP B CA    1 
ATOM   155   C  C     . TRP A 1 21  ? 135.063 194.398 118.902 1.00 51.11  ? 21   TRP B C     1 
ATOM   156   O  O     . TRP A 1 21  ? 134.535 195.029 117.981 1.00 59.27  ? 21   TRP B O     1 
ATOM   157   C  CB    . TRP A 1 21  ? 133.714 192.498 119.834 1.00 43.38  ? 21   TRP B CB    1 
ATOM   158   C  CG    . TRP A 1 21  ? 133.209 191.133 119.511 1.00 43.43  ? 21   TRP B CG    1 
ATOM   159   C  CD1   . TRP A 1 21  ? 133.291 190.026 120.295 1.00 49.75  ? 21   TRP B CD1   1 
ATOM   160   C  CD2   . TRP A 1 21  ? 132.558 190.721 118.304 1.00 42.80  ? 21   TRP B CD2   1 
ATOM   161   N  NE1   . TRP A 1 21  ? 132.728 188.951 119.658 1.00 52.11  ? 21   TRP B NE1   1 
ATOM   162   C  CE2   . TRP A 1 21  ? 132.269 189.354 118.433 1.00 44.20  ? 21   TRP B CE2   1 
ATOM   163   C  CE3   . TRP A 1 21  ? 132.189 191.379 117.131 1.00 47.06  ? 21   TRP B CE3   1 
ATOM   164   C  CZ2   . TRP A 1 21  ? 131.632 188.631 117.434 1.00 48.92  ? 21   TRP B CZ2   1 
ATOM   165   C  CZ3   . TRP A 1 21  ? 131.559 190.662 116.143 1.00 49.05  ? 21   TRP B CZ3   1 
ATOM   166   C  CH2   . TRP A 1 21  ? 131.285 189.302 116.299 1.00 53.80  ? 21   TRP B CH2   1 
ATOM   167   N  N     . GLU A 1 22  ? 135.798 194.993 119.842 1.00 51.91  ? 22   GLU B N     1 
ATOM   168   C  CA    . GLU A 1 22  ? 136.109 196.414 119.720 1.00 53.42  ? 22   GLU B CA    1 
ATOM   169   C  C     . GLU A 1 22  ? 136.896 196.692 118.444 1.00 60.43  ? 22   GLU B C     1 
ATOM   170   O  O     . GLU A 1 22  ? 136.588 197.634 117.702 1.00 68.38  ? 22   GLU B O     1 
ATOM   171   C  CB    . GLU A 1 22  ? 136.888 196.885 120.947 1.00 58.53  ? 22   GLU B CB    1 
ATOM   172   C  CG    . GLU A 1 22  ? 137.151 198.376 120.981 1.00 65.91  ? 22   GLU B CG    1 
ATOM   173   C  CD    . GLU A 1 22  ? 137.790 198.822 122.279 1.00 71.90  ? 22   GLU B CD    1 
ATOM   174   O  OE1   . GLU A 1 22  ? 137.996 197.967 123.165 1.00 68.98  ? 22   GLU B OE1   1 
ATOM   175   O  OE2   . GLU A 1 22  ? 138.086 200.028 122.413 1.00 72.12  ? 22   GLU B OE2   1 
ATOM   176   N  N     . VAL A 1 23  ? 137.892 195.853 118.159 1.00 55.80  ? 23   VAL B N     1 
ATOM   177   C  CA    . VAL A 1 23  ? 138.706 196.001 116.956 1.00 53.52  ? 23   VAL B CA    1 
ATOM   178   C  C     . VAL A 1 23  ? 137.853 195.856 115.700 1.00 60.28  ? 23   VAL B C     1 
ATOM   179   O  O     . VAL A 1 23  ? 137.943 196.666 114.769 1.00 65.89  ? 23   VAL B O     1 
ATOM   180   C  CB    . VAL A 1 23  ? 139.852 194.976 116.983 1.00 55.81  ? 23   VAL B CB    1 
ATOM   181   C  CG1   . VAL A 1 23  ? 140.459 194.841 115.640 1.00 55.69  ? 23   VAL B CG1   1 
ATOM   182   C  CG2   . VAL A 1 23  ? 140.912 195.401 117.984 1.00 59.94  ? 23   VAL B CG2   1 
ATOM   183   N  N     . ILE A 1 24  ? 137.012 194.821 115.656 1.00 56.77  ? 24   ILE B N     1 
ATOM   184   C  CA    . ILE A 1 24  ? 136.183 194.575 114.479 1.00 49.16  ? 24   ILE B CA    1 
ATOM   185   C  C     . ILE A 1 24  ? 135.204 195.719 114.264 1.00 54.55  ? 24   ILE B C     1 
ATOM   186   O  O     . ILE A 1 24  ? 135.018 196.193 113.136 1.00 59.43  ? 24   ILE B O     1 
ATOM   187   C  CB    . ILE A 1 24  ? 135.453 193.226 114.609 1.00 46.75  ? 24   ILE B CB    1 
ATOM   188   C  CG1   . ILE A 1 24  ? 136.445 192.072 114.503 1.00 53.01  ? 24   ILE B CG1   1 
ATOM   189   C  CG2   . ILE A 1 24  ? 134.398 193.089 113.535 1.00 54.95  ? 24   ILE B CG2   1 
ATOM   190   C  CD1   . ILE A 1 24  ? 137.160 192.007 113.179 1.00 60.19  ? 24   ILE B CD1   1 
ATOM   191   N  N     . SER A 1 25  ? 134.564 196.185 115.338 1.00 56.25  ? 25   SER B N     1 
ATOM   192   C  CA    . SER A 1 25  ? 133.610 197.278 115.215 1.00 59.39  ? 25   SER B CA    1 
ATOM   193   C  C     . SER A 1 25  ? 134.292 198.554 114.747 1.00 56.41  ? 25   SER B C     1 
ATOM   194   O  O     . SER A 1 25  ? 133.726 199.309 113.948 1.00 65.38  ? 25   SER B O     1 
ATOM   195   C  CB    . SER A 1 25  ? 132.897 197.501 116.546 1.00 64.51  ? 25   SER B CB    1 
ATOM   196   O  OG    . SER A 1 25  ? 132.213 196.331 116.957 1.00 64.93  ? 25   SER B OG    1 
ATOM   197   N  N     . ASP A 1 26  ? 135.505 198.821 115.236 1.00 54.10  ? 26   ASP B N     1 
ATOM   198   C  CA    . ASP A 1 26  ? 136.246 199.971 114.731 1.00 58.34  ? 26   ASP B CA    1 
ATOM   199   C  C     . ASP A 1 26  ? 136.562 199.806 113.252 1.00 64.26  ? 26   ASP B C     1 
ATOM   200   O  O     . ASP A 1 26  ? 136.507 200.773 112.484 1.00 66.55  ? 26   ASP B O     1 
ATOM   201   C  CB    . ASP A 1 26  ? 137.531 200.171 115.531 1.00 67.02  ? 26   ASP B CB    1 
ATOM   202   C  CG    . ASP A 1 26  ? 138.164 201.526 115.282 1.00 72.51  ? 26   ASP B CG    1 
ATOM   203   O  OD1   . ASP A 1 26  ? 137.500 202.389 114.670 1.00 72.26  ? 26   ASP B OD1   1 
ATOM   204   O  OD2   . ASP A 1 26  ? 139.326 201.728 115.691 1.00 74.46  ? 26   ASP B OD2   1 
ATOM   205   N  N     . GLU A 1 27  ? 136.897 198.584 112.835 1.00 69.88  ? 27   GLU B N     1 
ATOM   206   C  CA    . GLU A 1 27  ? 137.226 198.338 111.435 1.00 64.61  ? 27   GLU B CA    1 
ATOM   207   C  C     . GLU A 1 27  ? 136.010 198.518 110.535 1.00 65.88  ? 27   GLU B C     1 
ATOM   208   O  O     . GLU A 1 27  ? 136.135 199.012 109.408 1.00 68.25  ? 27   GLU B O     1 
ATOM   209   C  CB    . GLU A 1 27  ? 137.810 196.936 111.281 1.00 64.02  ? 27   GLU B CB    1 
ATOM   210   C  CG    . GLU A 1 27  ? 138.246 196.591 109.878 1.00 65.59  ? 27   GLU B CG    1 
ATOM   211   C  CD    . GLU A 1 27  ? 139.143 195.375 109.841 1.00 71.84  ? 27   GLU B CD    1 
ATOM   212   O  OE1   . GLU A 1 27  ? 139.881 195.154 110.823 1.00 73.43  ? 27   GLU B OE1   1 
ATOM   213   O  OE2   . GLU A 1 27  ? 139.110 194.639 108.833 1.00 69.92  ? 27   GLU B OE2   1 
ATOM   214   N  N     . HIS A 1 28  ? 134.831 198.127 111.009 1.00 65.31  ? 28   HIS B N     1 
ATOM   215   C  CA    . HIS A 1 28  ? 133.606 198.212 110.224 1.00 64.97  ? 28   HIS B CA    1 
ATOM   216   C  C     . HIS A 1 28  ? 132.775 199.450 110.532 1.00 60.73  ? 28   HIS B C     1 
ATOM   217   O  O     . HIS A 1 28  ? 131.652 199.561 110.032 1.00 60.96  ? 28   HIS B O     1 
ATOM   218   C  CB    . HIS A 1 28  ? 132.756 196.959 110.438 1.00 59.14  ? 28   HIS B CB    1 
ATOM   219   C  CG    . HIS A 1 28  ? 133.208 195.782 109.635 1.00 58.65  ? 28   HIS B CG    1 
ATOM   220   N  ND1   . HIS A 1 28  ? 132.384 194.718 109.346 1.00 60.90  ? 28   HIS B ND1   1 
ATOM   221   C  CD2   . HIS A 1 28  ? 134.400 195.502 109.058 1.00 64.44  ? 28   HIS B CD2   1 
ATOM   222   C  CE1   . HIS A 1 28  ? 133.047 193.832 108.625 1.00 63.99  ? 28   HIS B CE1   1 
ATOM   223   N  NE2   . HIS A 1 28  ? 134.273 194.284 108.436 1.00 67.61  ? 28   HIS B NE2   1 
ATOM   224   N  N     . GLY A 1 29  ? 133.288 200.374 111.336 1.00 61.49  ? 29   GLY B N     1 
ATOM   225   C  CA    . GLY A 1 29  ? 132.576 201.608 111.615 1.00 61.11  ? 29   GLY B CA    1 
ATOM   226   C  C     . GLY A 1 29  ? 131.292 201.463 112.404 1.00 67.99  ? 29   GLY B C     1 
ATOM   227   O  O     . GLY A 1 29  ? 130.283 202.089 112.055 1.00 74.14  ? 29   GLY B O     1 
ATOM   228   N  N     . ILE A 1 30  ? 131.300 200.655 113.460 1.00 62.56  ? 30   ILE B N     1 
ATOM   229   C  CA    . ILE A 1 30  ? 130.158 200.505 114.353 1.00 53.62  ? 30   ILE B CA    1 
ATOM   230   C  C     . ILE A 1 30  ? 130.527 201.122 115.693 1.00 54.40  ? 30   ILE B C     1 
ATOM   231   O  O     . ILE A 1 30  ? 131.452 200.653 116.367 1.00 62.47  ? 30   ILE B O     1 
ATOM   232   C  CB    . ILE A 1 30  ? 129.757 199.033 114.523 1.00 59.29  ? 30   ILE B CB    1 
ATOM   233   C  CG1   . ILE A 1 30  ? 129.193 198.474 113.221 1.00 61.05  ? 30   ILE B CG1   1 
ATOM   234   C  CG2   . ILE A 1 30  ? 128.737 198.887 115.634 1.00 61.75  ? 30   ILE B CG2   1 
ATOM   235   C  CD1   . ILE A 1 30  ? 128.715 197.054 113.340 1.00 62.35  ? 30   ILE B CD1   1 
ATOM   236   N  N     . ASP A 1 31  ? 129.811 202.170 116.079 1.00 66.33  ? 31   ASP B N     1 
ATOM   237   C  CA    . ASP A 1 31  ? 130.013 202.773 117.383 1.00 68.92  ? 31   ASP B CA    1 
ATOM   238   C  C     . ASP A 1 31  ? 129.431 201.868 118.466 1.00 67.62  ? 31   ASP B C     1 
ATOM   239   O  O     . ASP A 1 31  ? 128.611 200.995 118.176 1.00 67.76  ? 31   ASP B O     1 
ATOM   240   C  CB    . ASP A 1 31  ? 129.389 204.169 117.416 1.00 66.77  ? 31   ASP B CB    1 
ATOM   241   C  CG    . ASP A 1 31  ? 127.881 204.140 117.470 1.00 71.16  ? 31   ASP B CG    1 
ATOM   242   O  OD1   . ASP A 1 31  ? 127.274 203.191 116.933 1.00 76.26  ? 31   ASP B OD1   1 
ATOM   243   O  OD2   . ASP A 1 31  ? 127.301 205.081 118.047 1.00 71.54  ? 31   ASP B OD2   1 
ATOM   244   N  N     . PRO A 1 32  ? 129.854 202.041 119.724 1.00 68.77  ? 32   PRO B N     1 
ATOM   245   C  CA    . PRO A 1 32  ? 129.470 201.067 120.761 1.00 68.75  ? 32   PRO B CA    1 
ATOM   246   C  C     . PRO A 1 32  ? 127.972 200.891 120.941 1.00 72.48  ? 32   PRO B C     1 
ATOM   247   O  O     . PRO A 1 32  ? 127.539 199.813 121.365 1.00 70.42  ? 32   PRO B O     1 
ATOM   248   C  CB    . PRO A 1 32  ? 130.124 201.632 122.030 1.00 67.90  ? 32   PRO B CB    1 
ATOM   249   C  CG    . PRO A 1 32  ? 130.479 203.047 121.700 1.00 67.38  ? 32   PRO B CG    1 
ATOM   250   C  CD    . PRO A 1 32  ? 130.805 203.032 120.250 1.00 70.32  ? 32   PRO B CD    1 
ATOM   251   N  N     . THR A 1 33  ? 127.161 201.905 120.634 1.00 74.26  ? 33   THR B N     1 
ATOM   252   C  CA    . THR A 1 33  ? 125.720 201.762 120.802 1.00 72.79  ? 33   THR B CA    1 
ATOM   253   C  C     . THR A 1 33  ? 125.090 200.835 119.771 1.00 71.09  ? 33   THR B C     1 
ATOM   254   O  O     . THR A 1 33  ? 123.915 200.486 119.917 1.00 71.82  ? 33   THR B O     1 
ATOM   255   C  CB    . THR A 1 33  ? 125.037 203.131 120.747 1.00 70.27  ? 33   THR B CB    1 
ATOM   256   O  OG1   . THR A 1 33  ? 123.766 203.056 121.404 1.00 68.35  ? 33   THR B OG1   1 
ATOM   257   C  CG2   . THR A 1 33  ? 124.821 203.565 119.311 1.00 67.84  ? 33   THR B CG2   1 
ATOM   258   N  N     . GLY A 1 34  ? 125.834 200.426 118.745 1.00 66.81  ? 34   GLY B N     1 
ATOM   259   C  CA    . GLY A 1 34  ? 125.312 199.565 117.707 1.00 68.62  ? 34   GLY B CA    1 
ATOM   260   C  C     . GLY A 1 34  ? 124.929 200.262 116.420 1.00 72.24  ? 34   GLY B C     1 
ATOM   261   O  O     . GLY A 1 34  ? 124.539 199.583 115.464 1.00 73.76  ? 34   GLY B O     1 
ATOM   262   N  N     . SER A 1 35  ? 125.026 201.586 116.363 1.00 66.45  ? 35   SER B N     1 
ATOM   263   C  CA    . SER A 1 35  ? 124.733 202.323 115.145 1.00 62.25  ? 35   SER B CA    1 
ATOM   264   C  C     . SER A 1 35  ? 125.916 202.227 114.184 1.00 64.96  ? 35   SER B C     1 
ATOM   265   O  O     . SER A 1 35  ? 126.976 201.685 114.511 1.00 68.99  ? 35   SER B O     1 
ATOM   266   C  CB    . SER A 1 35  ? 124.395 203.774 115.478 1.00 65.21  ? 35   SER B CB    1 
ATOM   267   O  OG    . SER A 1 35  ? 124.172 204.534 114.305 1.00 71.21  ? 35   SER B OG    1 
ATOM   268   N  N     . TYR A 1 36  ? 125.739 202.754 112.977 1.00 64.23  ? 36   TYR B N     1 
ATOM   269   C  CA    . TYR A 1 36  ? 126.773 202.740 111.952 1.00 60.75  ? 36   TYR B CA    1 
ATOM   270   C  C     . TYR A 1 36  ? 127.241 204.162 111.682 1.00 60.32  ? 36   TYR B C     1 
ATOM   271   O  O     . TYR A 1 36  ? 126.427 205.040 111.378 1.00 58.13  ? 36   TYR B O     1 
ATOM   272   C  CB    . TYR A 1 36  ? 126.263 202.098 110.662 1.00 63.10  ? 36   TYR B CB    1 
ATOM   273   C  CG    . TYR A 1 36  ? 127.183 202.297 109.483 1.00 67.42  ? 36   TYR B CG    1 
ATOM   274   C  CD1   . TYR A 1 36  ? 128.332 201.537 109.343 1.00 65.03  ? 36   TYR B CD1   1 
ATOM   275   C  CD2   . TYR A 1 36  ? 126.902 203.242 108.507 1.00 69.62  ? 36   TYR B CD2   1 
ATOM   276   C  CE1   . TYR A 1 36  ? 129.175 201.714 108.272 1.00 61.41  ? 36   TYR B CE1   1 
ATOM   277   C  CE2   . TYR A 1 36  ? 127.742 203.425 107.430 1.00 65.52  ? 36   TYR B CE2   1 
ATOM   278   C  CZ    . TYR A 1 36  ? 128.877 202.655 107.318 1.00 60.69  ? 36   TYR B CZ    1 
ATOM   279   O  OH    . TYR A 1 36  ? 129.721 202.830 106.248 1.00 69.69  ? 36   TYR B OH    1 
ATOM   280   N  N     . HIS A 1 37  ? 128.548 204.387 111.798 1.00 70.85  ? 37   HIS B N     1 
ATOM   281   C  CA    . HIS A 1 37  ? 129.146 205.696 111.556 1.00 73.27  ? 37   HIS B CA    1 
ATOM   282   C  C     . HIS A 1 37  ? 130.457 205.555 110.797 1.00 74.68  ? 37   HIS B C     1 
ATOM   283   O  O     . HIS A 1 37  ? 131.467 206.174 111.146 1.00 74.71  ? 37   HIS B O     1 
ATOM   284   C  CB    . HIS A 1 37  ? 129.352 206.459 112.862 1.00 74.84  ? 37   HIS B CB    1 
ATOM   285   C  CG    . HIS A 1 37  ? 128.093 207.049 113.418 1.00 80.28  ? 37   HIS B CG    1 
ATOM   286   N  ND1   . HIS A 1 37  ? 127.107 206.285 114.003 1.00 82.35  ? 37   HIS B ND1   1 
ATOM   287   C  CD2   . HIS A 1 37  ? 127.658 208.330 113.472 1.00 78.69  ? 37   HIS B CD2   1 
ATOM   288   C  CE1   . HIS A 1 37  ? 126.119 207.069 114.395 1.00 79.29  ? 37   HIS B CE1   1 
ATOM   289   N  NE2   . HIS A 1 37  ? 126.429 208.315 114.086 1.00 81.73  ? 37   HIS B NE2   1 
ATOM   290   N  N     . GLY A 1 38  ? 130.461 204.737 109.750 1.00 74.41  ? 38   GLY B N     1 
ATOM   291   C  CA    . GLY A 1 38  ? 131.648 204.525 108.952 1.00 74.96  ? 38   GLY B CA    1 
ATOM   292   C  C     . GLY A 1 38  ? 131.812 205.570 107.865 1.00 73.37  ? 38   GLY B C     1 
ATOM   293   O  O     . GLY A 1 38  ? 131.129 206.594 107.824 1.00 77.04  ? 38   GLY B O     1 
ATOM   294   N  N     . ASP A 1 39  ? 132.752 205.292 106.963 1.00 79.04  ? 39   ASP B N     1 
ATOM   295   C  CA    . ASP A 1 39  ? 133.043 206.185 105.850 1.00 82.32  ? 39   ASP B CA    1 
ATOM   296   C  C     . ASP A 1 39  ? 132.994 205.518 104.484 1.00 82.87  ? 39   ASP B C     1 
ATOM   297   O  O     . ASP A 1 39  ? 132.827 206.228 103.485 1.00 85.43  ? 39   ASP B O     1 
ATOM   298   C  CB    . ASP A 1 39  ? 134.425 206.832 106.031 1.00 87.12  ? 39   ASP B CB    1 
ATOM   299   C  CG    . ASP A 1 39  ? 134.475 208.259 105.518 1.00 91.11  ? 39   ASP B CG    1 
ATOM   300   O  OD1   . ASP A 1 39  ? 133.621 208.628 104.685 1.00 91.91  ? 39   ASP B OD1   1 
ATOM   301   O  OD2   . ASP A 1 39  ? 135.372 209.014 105.949 1.00 89.32  ? 39   ASP B OD2   1 
ATOM   302   N  N     . SER A 1 40  ? 133.122 204.196 104.398 1.00 82.44  ? 40   SER B N     1 
ATOM   303   C  CA    . SER A 1 40  ? 133.152 203.493 103.124 1.00 82.85  ? 40   SER B CA    1 
ATOM   304   C  C     . SER A 1 40  ? 132.068 202.426 103.099 1.00 81.66  ? 40   SER B C     1 
ATOM   305   O  O     . SER A 1 40  ? 131.693 201.874 104.136 1.00 84.49  ? 40   SER B O     1 
ATOM   306   C  CB    . SER A 1 40  ? 134.521 202.851 102.870 1.00 82.84  ? 40   SER B CB    1 
ATOM   307   O  OG    . SER A 1 40  ? 134.545 202.177 101.624 1.00 87.95  ? 40   SER B OG    1 
ATOM   308   N  N     . ASP A 1 41  ? 131.566 202.142 101.896 1.00 79.93  ? 41   ASP B N     1 
ATOM   309   C  CA    . ASP A 1 41  ? 130.496 201.165 101.735 1.00 83.95  ? 41   ASP B CA    1 
ATOM   310   C  C     . ASP A 1 41  ? 130.980 199.729 101.875 1.00 85.64  ? 41   ASP B C     1 
ATOM   311   O  O     . ASP A 1 41  ? 130.163 198.834 102.128 1.00 88.15  ? 41   ASP B O     1 
ATOM   312   C  CB    . ASP A 1 41  ? 129.820 201.347 100.375 1.00 85.25  ? 41   ASP B CB    1 
ATOM   313   C  CG    . ASP A 1 41  ? 129.435 202.789 100.105 1.00 89.48  ? 41   ASP B CG    1 
ATOM   314   O  OD1   . ASP A 1 41  ? 129.202 203.536 101.078 1.00 93.09  ? 41   ASP B OD1   1 
ATOM   315   O  OD2   . ASP A 1 41  ? 129.366 203.175 98.919  1.00 88.26  ? 41   ASP B OD2   1 
ATOM   316   N  N     . LEU A 1 42  ? 132.283 199.487 101.719 1.00 76.80  ? 42   LEU B N     1 
ATOM   317   C  CA    . LEU A 1 42  ? 132.812 198.140 101.889 1.00 73.68  ? 42   LEU B CA    1 
ATOM   318   C  C     . LEU A 1 42  ? 132.664 197.646 103.320 1.00 76.24  ? 42   LEU B C     1 
ATOM   319   O  O     . LEU A 1 42  ? 132.731 196.436 103.559 1.00 75.31  ? 42   LEU B O     1 
ATOM   320   C  CB    . LEU A 1 42  ? 134.278 198.093 101.463 1.00 69.50  ? 42   LEU B CB    1 
ATOM   321   C  CG    . LEU A 1 42  ? 134.536 198.375 99.984  1.00 73.32  ? 42   LEU B CG    1 
ATOM   322   C  CD1   . LEU A 1 42  ? 136.022 198.338 99.685  1.00 73.47  ? 42   LEU B CD1   1 
ATOM   323   C  CD2   . LEU A 1 42  ? 133.790 197.376 99.120  1.00 72.55  ? 42   LEU B CD2   1 
ATOM   324   N  N     . GLN A 1 43  ? 132.468 198.555 104.275 1.00 70.11  ? 43   GLN B N     1 
ATOM   325   C  CA    . GLN A 1 43  ? 132.212 198.145 105.649 1.00 65.51  ? 43   GLN B CA    1 
ATOM   326   C  C     . GLN A 1 43  ? 130.845 197.488 105.779 1.00 67.72  ? 43   GLN B C     1 
ATOM   327   O  O     . GLN A 1 43  ? 130.702 196.456 106.444 1.00 74.05  ? 43   GLN B O     1 
ATOM   328   C  CB    . GLN A 1 43  ? 132.329 199.351 106.574 1.00 67.06  ? 43   GLN B CB    1 
ATOM   329   C  CG    . GLN A 1 43  ? 133.631 200.103 106.414 1.00 67.80  ? 43   GLN B CG    1 
ATOM   330   C  CD    . GLN A 1 43  ? 133.694 201.340 107.273 1.00 68.88  ? 43   GLN B CD    1 
ATOM   331   O  OE1   . GLN A 1 43  ? 132.694 201.756 107.851 1.00 74.98  ? 43   GLN B OE1   1 
ATOM   332   N  NE2   . GLN A 1 43  ? 134.874 201.936 107.368 1.00 65.76  ? 43   GLN B NE2   1 
ATOM   333   N  N     . LEU A 1 44  ? 129.826 198.072 105.151 1.00 60.64  ? 44   LEU B N     1 
ATOM   334   C  CA    . LEU A 1 44  ? 128.488 197.500 105.182 1.00 62.27  ? 44   LEU B CA    1 
ATOM   335   C  C     . LEU A 1 44  ? 128.282 196.409 104.144 1.00 60.27  ? 44   LEU B C     1 
ATOM   336   O  O     . LEU A 1 44  ? 127.278 195.693 104.219 1.00 64.22  ? 44   LEU B O     1 
ATOM   337   C  CB    . LEU A 1 44  ? 127.437 198.592 104.974 1.00 62.45  ? 44   LEU B CB    1 
ATOM   338   C  CG    . LEU A 1 44  ? 127.282 199.644 106.068 1.00 69.21  ? 44   LEU B CG    1 
ATOM   339   C  CD1   . LEU A 1 44  ? 126.238 200.668 105.664 1.00 65.07  ? 44   LEU B CD1   1 
ATOM   340   C  CD2   . LEU A 1 44  ? 126.900 198.985 107.377 1.00 64.68  ? 44   LEU B CD2   1 
ATOM   341   N  N     . GLU A 1 45  ? 129.192 196.269 103.181 1.00 62.96  ? 47   GLU B N     1 
ATOM   342   C  CA    . GLU A 1 45  ? 129.012 195.259 102.145 1.00 62.79  ? 47   GLU B CA    1 
ATOM   343   C  C     . GLU A 1 45  ? 128.985 193.855 102.734 1.00 60.91  ? 47   GLU B C     1 
ATOM   344   O  O     . GLU A 1 45  ? 128.175 193.018 102.322 1.00 65.39  ? 47   GLU B O     1 
ATOM   345   C  CB    . GLU A 1 45  ? 130.118 195.381 101.097 1.00 68.33  ? 47   GLU B CB    1 
ATOM   346   C  CG    . GLU A 1 45  ? 129.888 194.551 99.848  1.00 69.06  ? 47   GLU B CG    1 
ATOM   347   C  CD    . GLU A 1 45  ? 128.761 195.089 98.987  1.00 71.41  ? 47   GLU B CD    1 
ATOM   348   O  OE1   . GLU A 1 45  ? 128.438 196.290 99.105  1.00 74.96  ? 47   GLU B OE1   1 
ATOM   349   O  OE2   . GLU A 1 45  ? 128.196 194.309 98.191  1.00 68.08  ? 47   GLU B OE2   1 
ATOM   350   N  N     . ARG A 1 46  ? 129.859 193.577 103.696 1.00 50.57  ? 48   ARG B N     1 
ATOM   351   C  CA    . ARG A 1 46  ? 129.974 192.254 104.295 1.00 54.32  ? 48   ARG B CA    1 
ATOM   352   C  C     . ARG A 1 46  ? 129.885 192.320 105.815 1.00 59.97  ? 48   ARG B C     1 
ATOM   353   O  O     . ARG A 1 46  ? 130.593 191.609 106.529 1.00 62.26  ? 48   ARG B O     1 
ATOM   354   C  CB    . ARG A 1 46  ? 131.272 191.577 103.866 1.00 58.77  ? 48   ARG B CB    1 
ATOM   355   C  CG    . ARG A 1 46  ? 131.076 190.336 103.018 1.00 59.23  ? 48   ARG B CG    1 
ATOM   356   C  CD    . ARG A 1 46  ? 130.678 190.695 101.600 1.00 55.40  ? 48   ARG B CD    1 
ATOM   357   N  NE    . ARG A 1 46  ? 130.274 189.520 100.839 1.00 53.95  ? 48   ARG B NE    1 
ATOM   358   C  CZ    . ARG A 1 46  ? 129.996 189.526 99.544  1.00 57.92  ? 48   ARG B CZ    1 
ATOM   359   N  NH1   . ARG A 1 46  ? 130.080 190.632 98.825  1.00 56.82  ? 48   ARG B NH1   1 
ATOM   360   N  NH2   . ARG A 1 46  ? 129.625 188.393 98.954  1.00 59.45  ? 48   ARG B NH2   1 
ATOM   361   N  N     . ILE A 1 47  ? 129.003 193.180 106.332 1.00 60.79  ? 49   ILE B N     1 
ATOM   362   C  CA    . ILE A 1 47  ? 128.774 193.254 107.769 1.00 50.51  ? 49   ILE B CA    1 
ATOM   363   C  C     . ILE A 1 47  ? 128.043 192.033 108.300 1.00 51.00  ? 49   ILE B C     1 
ATOM   364   O  O     . ILE A 1 47  ? 128.023 191.810 109.515 1.00 56.15  ? 49   ILE B O     1 
ATOM   365   C  CB    . ILE A 1 47  ? 127.990 194.536 108.115 1.00 49.60  ? 49   ILE B CB    1 
ATOM   366   C  CG1   . ILE A 1 47  ? 128.299 194.990 109.538 1.00 56.03  ? 49   ILE B CG1   1 
ATOM   367   C  CG2   . ILE A 1 47  ? 126.497 194.318 107.943 1.00 51.86  ? 49   ILE B CG2   1 
ATOM   368   C  CD1   . ILE A 1 47  ? 127.696 196.325 109.883 1.00 60.46  ? 49   ILE B CD1   1 
ATOM   369   N  N     . ASN A 1 48  ? 127.447 191.233 107.416 1.00 54.04  ? 50   ASN B N     1 
ATOM   370   C  CA    . ASN A 1 48  ? 126.725 190.040 107.834 1.00 51.06  ? 50   ASN B CA    1 
ATOM   371   C  C     . ASN A 1 48  ? 127.663 188.946 108.323 1.00 56.19  ? 50   ASN B C     1 
ATOM   372   O  O     . ASN A 1 48  ? 127.210 188.004 108.982 1.00 62.79  ? 50   ASN B O     1 
ATOM   373   C  CB    . ASN A 1 48  ? 125.861 189.542 106.672 1.00 57.33  ? 50   ASN B CB    1 
ATOM   374   C  CG    . ASN A 1 48  ? 125.231 188.194 106.939 1.00 67.00  ? 50   ASN B CG    1 
ATOM   375   O  OD1   . ASN A 1 48  ? 125.724 187.166 106.478 1.00 71.58  ? 50   ASN B OD1   1 
ATOM   376   N  ND2   . ASN A 1 48  ? 124.135 188.190 107.689 1.00 64.58  ? 50   ASN B ND2   1 
ATOM   377   N  N     . VAL A 1 49  ? 128.961 189.061 108.034 1.00 54.22  ? 51   VAL B N     1 
ATOM   378   C  CA    . VAL A 1 49  ? 129.909 188.022 108.424 1.00 48.41  ? 51   VAL B CA    1 
ATOM   379   C  C     . VAL A 1 49  ? 129.984 187.903 109.939 1.00 56.82  ? 51   VAL B C     1 
ATOM   380   O  O     . VAL A 1 49  ? 129.960 186.798 110.492 1.00 60.06  ? 51   VAL B O     1 
ATOM   381   C  CB    . VAL A 1 49  ? 131.291 188.308 107.812 1.00 41.93  ? 51   VAL B CB    1 
ATOM   382   C  CG1   . VAL A 1 49  ? 132.287 187.252 108.239 1.00 49.11  ? 51   VAL B CG1   1 
ATOM   383   C  CG2   . VAL A 1 49  ? 131.193 188.367 106.305 1.00 48.31  ? 51   VAL B CG2   1 
ATOM   384   N  N     . TYR A 1 50  ? 130.069 189.035 110.634 1.00 53.63  ? 52   TYR B N     1 
ATOM   385   C  CA    . TYR A 1 50  ? 130.260 189.049 112.074 1.00 47.95  ? 52   TYR B CA    1 
ATOM   386   C  C     . TYR A 1 50  ? 129.097 189.662 112.835 1.00 51.28  ? 52   TYR B C     1 
ATOM   387   O  O     . TYR A 1 50  ? 129.149 189.719 114.068 1.00 60.49  ? 52   TYR B O     1 
ATOM   388   C  CB    . TYR A 1 50  ? 131.545 189.809 112.428 1.00 47.43  ? 52   TYR B CB    1 
ATOM   389   C  CG    . TYR A 1 50  ? 132.776 188.945 112.487 1.00 46.15  ? 52   TYR B CG    1 
ATOM   390   C  CD1   . TYR A 1 50  ? 132.754 187.720 113.129 1.00 51.22  ? 52   TYR B CD1   1 
ATOM   391   C  CD2   . TYR A 1 50  ? 133.958 189.347 111.887 1.00 47.75  ? 52   TYR B CD2   1 
ATOM   392   C  CE1   . TYR A 1 50  ? 133.875 186.926 113.184 1.00 57.66  ? 52   TYR B CE1   1 
ATOM   393   C  CE2   . TYR A 1 50  ? 135.083 188.559 111.934 1.00 50.65  ? 52   TYR B CE2   1 
ATOM   394   C  CZ    . TYR A 1 50  ? 135.036 187.350 112.585 1.00 56.49  ? 52   TYR B CZ    1 
ATOM   395   O  OH    . TYR A 1 50  ? 136.155 186.556 112.639 1.00 59.88  ? 52   TYR B OH    1 
ATOM   396   N  N     . TYR A 1 51  ? 128.052 190.120 112.151 1.00 50.75  ? 53   TYR B N     1 
ATOM   397   C  CA    . TYR A 1 51  ? 126.984 190.854 112.807 1.00 46.73  ? 53   TYR B CA    1 
ATOM   398   C  C     . TYR A 1 51  ? 125.632 190.437 112.252 1.00 53.11  ? 53   TYR B C     1 
ATOM   399   O  O     . TYR A 1 51  ? 125.522 189.974 111.114 1.00 52.20  ? 53   TYR B O     1 
ATOM   400   C  CB    . TYR A 1 51  ? 127.158 192.363 112.627 1.00 44.37  ? 53   TYR B CB    1 
ATOM   401   C  CG    . TYR A 1 51  ? 128.373 192.936 113.309 1.00 44.77  ? 53   TYR B CG    1 
ATOM   402   C  CD1   . TYR A 1 51  ? 129.602 192.954 112.675 1.00 49.60  ? 53   TYR B CD1   1 
ATOM   403   C  CD2   . TYR A 1 51  ? 128.286 193.478 114.579 1.00 52.23  ? 53   TYR B CD2   1 
ATOM   404   C  CE1   . TYR A 1 51  ? 130.711 193.484 113.292 1.00 53.60  ? 53   TYR B CE1   1 
ATOM   405   C  CE2   . TYR A 1 51  ? 129.389 194.008 115.202 1.00 52.47  ? 53   TYR B CE2   1 
ATOM   406   C  CZ    . TYR A 1 51  ? 130.598 194.008 114.555 1.00 54.53  ? 53   TYR B CZ    1 
ATOM   407   O  OH    . TYR A 1 51  ? 131.702 194.539 115.178 1.00 61.10  ? 53   TYR B OH    1 
ATOM   408   N  N     . ASN A 1 52  ? 124.607 190.609 113.074 1.00 59.79  ? 54   ASN B N     1 
ATOM   409   C  CA    . ASN A 1 52  ? 123.212 190.510 112.676 1.00 52.88  ? 54   ASN B CA    1 
ATOM   410   C  C     . ASN A 1 52  ? 122.620 191.912 112.601 1.00 56.07  ? 54   ASN B C     1 
ATOM   411   O  O     . ASN A 1 52  ? 123.206 192.886 113.078 1.00 67.41  ? 54   ASN B O     1 
ATOM   412   C  CB    . ASN A 1 52  ? 122.426 189.634 113.654 1.00 50.11  ? 54   ASN B CB    1 
ATOM   413   C  CG    . ASN A 1 52  ? 122.621 188.160 113.402 1.00 58.19  ? 54   ASN B CG    1 
ATOM   414   O  OD1   . ASN A 1 52  ? 122.988 187.752 112.301 1.00 64.65  ? 54   ASN B OD1   1 
ATOM   415   N  ND2   . ASN A 1 52  ? 122.378 187.348 114.420 1.00 60.69  ? 54   ASN B ND2   1 
ATOM   416   N  N     . GLU A 1 53  ? 121.446 192.014 111.993 1.00 50.63  ? 55   GLU B N     1 
ATOM   417   C  CA    . GLU A 1 53  ? 120.752 193.285 111.888 1.00 52.24  ? 55   GLU B CA    1 
ATOM   418   C  C     . GLU A 1 53  ? 119.600 193.340 112.880 1.00 54.68  ? 55   GLU B C     1 
ATOM   419   O  O     . GLU A 1 53  ? 119.138 192.320 113.396 1.00 64.28  ? 55   GLU B O     1 
ATOM   420   C  CB    . GLU A 1 53  ? 120.233 193.519 110.468 1.00 57.84  ? 55   GLU B CB    1 
ATOM   421   C  CG    . GLU A 1 53  ? 121.287 194.038 109.508 1.00 63.69  ? 55   GLU B CG    1 
ATOM   422   C  CD    . GLU A 1 53  ? 120.687 194.773 108.328 1.00 68.46  ? 55   GLU B CD    1 
ATOM   423   O  OE1   . GLU A 1 53  ? 119.461 195.010 108.336 1.00 67.93  ? 55   GLU B OE1   1 
ATOM   424   O  OE2   . GLU A 1 53  ? 121.441 195.116 107.393 1.00 65.42  ? 55   GLU B OE2   1 
ATOM   425   N  N     . ALA A 1 54  ? 119.142 194.558 113.144 1.00 50.29  ? 56   ALA B N     1 
ATOM   426   C  CA    . ALA A 1 54  ? 118.043 194.784 114.065 1.00 57.03  ? 56   ALA B CA    1 
ATOM   427   C  C     . ALA A 1 54  ? 117.295 196.031 113.625 1.00 61.39  ? 56   ALA B C     1 
ATOM   428   O  O     . ALA A 1 54  ? 117.785 196.821 112.815 1.00 62.51  ? 56   ALA B O     1 
ATOM   429   C  CB    . ALA A 1 54  ? 118.538 194.919 115.508 1.00 59.34  ? 56   ALA B CB    1 
ATOM   430   N  N     . ALA A 1 55  ? 116.088 196.192 114.158 1.00 63.26  ? 57   ALA B N     1 
ATOM   431   C  CA    . ALA A 1 55  ? 115.277 197.352 113.825 1.00 60.18  ? 57   ALA B CA    1 
ATOM   432   C  C     . ALA A 1 55  ? 115.972 198.631 114.271 1.00 65.57  ? 57   ALA B C     1 
ATOM   433   O  O     . ALA A 1 55  ? 116.464 198.731 115.397 1.00 67.56  ? 57   ALA B O     1 
ATOM   434   C  CB    . ALA A 1 55  ? 113.904 197.242 114.482 1.00 58.38  ? 57   ALA B CB    1 
ATOM   435   N  N     . GLY A 1 56  ? 116.006 199.616 113.377 1.00 74.74  ? 58   GLY B N     1 
ATOM   436   C  CA    . GLY A 1 56  ? 116.659 200.874 113.677 1.00 75.48  ? 58   GLY B CA    1 
ATOM   437   C  C     . GLY A 1 56  ? 118.100 200.972 113.238 1.00 76.78  ? 58   GLY B C     1 
ATOM   438   O  O     . GLY A 1 56  ? 118.852 201.770 113.806 1.00 76.75  ? 58   GLY B O     1 
ATOM   439   N  N     . ASN A 1 57  ? 118.508 200.185 112.239 1.00 73.62  ? 59   ASN B N     1 
ATOM   440   C  CA    . ASN A 1 57  ? 119.878 200.195 111.725 1.00 75.98  ? 59   ASN B CA    1 
ATOM   441   C  C     . ASN A 1 57  ? 120.892 199.922 112.834 1.00 76.88  ? 59   ASN B C     1 
ATOM   442   O  O     . ASN A 1 57  ? 121.957 200.537 112.894 1.00 77.28  ? 59   ASN B O     1 
ATOM   443   C  CB    . ASN A 1 57  ? 120.194 201.511 111.011 1.00 79.84  ? 59   ASN B CB    1 
ATOM   444   C  CG    . ASN A 1 57  ? 119.238 201.798 109.871 1.00 81.71  ? 59   ASN B CG    1 
ATOM   445   O  OD1   . ASN A 1 57  ? 118.764 200.883 109.197 1.00 81.56  ? 59   ASN B OD1   1 
ATOM   446   N  ND2   . ASN A 1 57  ? 118.952 203.076 109.647 1.00 78.93  ? 59   ASN B ND2   1 
ATOM   447   N  N     . LYS A 1 58  ? 120.555 198.990 113.718 1.00 67.93  ? 60   LYS B N     1 
ATOM   448   C  CA    . LYS A 1 58  ? 121.421 198.593 114.818 1.00 65.28  ? 60   LYS B CA    1 
ATOM   449   C  C     . LYS A 1 58  ? 121.955 197.195 114.547 1.00 66.71  ? 60   LYS B C     1 
ATOM   450   O  O     . LYS A 1 58  ? 121.191 196.296 114.180 1.00 77.51  ? 60   LYS B O     1 
ATOM   451   C  CB    . LYS A 1 58  ? 120.664 198.629 116.146 1.00 65.69  ? 60   LYS B CB    1 
ATOM   452   C  CG    . LYS A 1 58  ? 121.476 198.175 117.344 1.00 72.19  ? 60   LYS B CG    1 
ATOM   453   C  CD    . LYS A 1 58  ? 120.639 198.195 118.611 1.00 74.77  ? 60   LYS B CD    1 
ATOM   454   C  CE    . LYS A 1 58  ? 121.439 197.717 119.810 1.00 74.53  ? 60   LYS B CE    1 
ATOM   455   N  NZ    . LYS A 1 58  ? 120.623 197.715 121.056 1.00 72.66  ? 60   LYS B NZ    1 
ATOM   456   N  N     . TYR A 1 59  ? 123.258 197.013 114.722 1.00 52.21  ? 61   TYR B N     1 
ATOM   457   C  CA    . TYR A 1 59  ? 123.923 195.760 114.389 1.00 54.11  ? 61   TYR B CA    1 
ATOM   458   C  C     . TYR A 1 59  ? 124.402 195.090 115.668 1.00 56.89  ? 61   TYR B C     1 
ATOM   459   O  O     . TYR A 1 59  ? 125.152 195.690 116.444 1.00 64.87  ? 61   TYR B O     1 
ATOM   460   C  CB    . TYR A 1 59  ? 125.086 196.002 113.429 1.00 54.46  ? 61   TYR B CB    1 
ATOM   461   C  CG    . TYR A 1 59  ? 124.657 196.596 112.110 1.00 53.57  ? 61   TYR B CG    1 
ATOM   462   C  CD1   . TYR A 1 59  ? 124.555 197.968 111.947 1.00 59.31  ? 61   TYR B CD1   1 
ATOM   463   C  CD2   . TYR A 1 59  ? 124.346 195.787 111.031 1.00 54.21  ? 61   TYR B CD2   1 
ATOM   464   C  CE1   . TYR A 1 59  ? 124.160 198.516 110.747 1.00 60.28  ? 61   TYR B CE1   1 
ATOM   465   C  CE2   . TYR A 1 59  ? 123.950 196.327 109.827 1.00 55.64  ? 61   TYR B CE2   1 
ATOM   466   C  CZ    . TYR A 1 59  ? 123.858 197.691 109.691 1.00 57.83  ? 61   TYR B CZ    1 
ATOM   467   O  OH    . TYR A 1 59  ? 123.464 198.235 108.492 1.00 61.91  ? 61   TYR B OH    1 
ATOM   468   N  N     . VAL A 1 60  ? 123.969 193.856 115.882 1.00 41.92  ? 62   VAL B N     1 
ATOM   469   C  CA    . VAL A 1 60  ? 124.311 193.079 117.068 1.00 39.80  ? 62   VAL B CA    1 
ATOM   470   C  C     . VAL A 1 60  ? 125.261 191.961 116.650 1.00 42.03  ? 62   VAL B C     1 
ATOM   471   O  O     . VAL A 1 60  ? 124.974 191.235 115.689 1.00 55.95  ? 62   VAL B O     1 
ATOM   472   C  CB    . VAL A 1 60  ? 123.060 192.523 117.769 1.00 47.80  ? 62   VAL B CB    1 
ATOM   473   C  CG1   . VAL A 1 60  ? 122.228 193.660 118.326 1.00 53.46  ? 62   VAL B CG1   1 
ATOM   474   C  CG2   . VAL A 1 60  ? 122.216 191.701 116.809 1.00 52.10  ? 62   VAL B CG2   1 
ATOM   475   N  N     . PRO A 1 61  ? 126.411 191.818 117.299 1.00 38.73  ? 63   PRO B N     1 
ATOM   476   C  CA    . PRO A 1 61  ? 127.319 190.720 116.963 1.00 41.54  ? 63   PRO B CA    1 
ATOM   477   C  C     . PRO A 1 61  ? 126.711 189.369 117.297 1.00 43.54  ? 63   PRO B C     1 
ATOM   478   O  O     . PRO A 1 61  ? 125.956 189.224 118.260 1.00 51.73  ? 63   PRO B O     1 
ATOM   479   C  CB    . PRO A 1 61  ? 128.549 191.000 117.831 1.00 40.10  ? 63   PRO B CB    1 
ATOM   480   C  CG    . PRO A 1 61  ? 128.431 192.422 118.231 1.00 43.15  ? 63   PRO B CG    1 
ATOM   481   C  CD    . PRO A 1 61  ? 126.978 192.708 118.320 1.00 44.84  ? 63   PRO B CD    1 
ATOM   482   N  N     . ARG A 1 62  ? 127.055 188.368 116.491 1.00 40.96  ? 64   ARG B N     1 
ATOM   483   C  CA    . ARG A 1 62  ? 126.684 186.990 116.801 1.00 46.46  ? 64   ARG B CA    1 
ATOM   484   C  C     . ARG A 1 62  ? 127.794 186.324 117.614 1.00 50.28  ? 64   ARG B C     1 
ATOM   485   O  O     . ARG A 1 62  ? 128.486 185.407 117.177 1.00 55.90  ? 64   ARG B O     1 
ATOM   486   C  CB    . ARG A 1 62  ? 126.363 186.216 115.527 1.00 49.65  ? 64   ARG B CB    1 
ATOM   487   C  CG    . ARG A 1 62  ? 127.408 186.275 114.441 1.00 49.76  ? 64   ARG B CG    1 
ATOM   488   C  CD    . ARG A 1 62  ? 127.122 185.223 113.386 1.00 47.62  ? 64   ARG B CD    1 
ATOM   489   N  NE    . ARG A 1 62  ? 125.822 185.423 112.763 1.00 42.42  ? 64   ARG B NE    1 
ATOM   490   C  CZ    . ARG A 1 62  ? 125.629 186.137 111.664 1.00 49.68  ? 64   ARG B CZ    1 
ATOM   491   N  NH1   . ARG A 1 62  ? 126.635 186.725 111.039 1.00 48.49  ? 64   ARG B NH1   1 
ATOM   492   N  NH2   . ARG A 1 62  ? 124.399 186.261 111.177 1.00 54.71  ? 64   ARG B NH2   1 
ATOM   493   N  N     . ALA A 1 63  ? 127.950 186.826 118.832 1.00 51.72  ? 65   ALA B N     1 
ATOM   494   C  CA    . ALA A 1 63  ? 128.925 186.316 119.780 1.00 47.39  ? 65   ALA B CA    1 
ATOM   495   C  C     . ALA A 1 63  ? 128.196 185.682 120.953 1.00 44.47  ? 65   ALA B C     1 
ATOM   496   O  O     . ALA A 1 63  ? 127.163 186.191 121.396 1.00 54.32  ? 65   ALA B O     1 
ATOM   497   C  CB    . ALA A 1 63  ? 129.847 187.431 120.271 1.00 47.15  ? 65   ALA B CB    1 
ATOM   498   N  N     . ILE A 1 64  ? 128.735 184.576 121.447 1.00 44.49  ? 66   ILE B N     1 
ATOM   499   C  CA    . ILE A 1 64  ? 128.153 183.840 122.558 1.00 48.45  ? 66   ILE B CA    1 
ATOM   500   C  C     . ILE A 1 64  ? 129.194 183.798 123.664 1.00 53.38  ? 66   ILE B C     1 
ATOM   501   O  O     . ILE A 1 64  ? 130.262 183.195 123.499 1.00 60.88  ? 66   ILE B O     1 
ATOM   502   C  CB    . ILE A 1 64  ? 127.720 182.433 122.138 1.00 45.52  ? 66   ILE B CB    1 
ATOM   503   C  CG1   . ILE A 1 64  ? 126.649 182.541 121.057 1.00 48.45  ? 66   ILE B CG1   1 
ATOM   504   C  CG2   . ILE A 1 64  ? 127.198 181.660 123.329 1.00 46.91  ? 66   ILE B CG2   1 
ATOM   505   C  CD1   . ILE A 1 64  ? 126.633 181.399 120.091 1.00 53.20  ? 66   ILE B CD1   1 
ATOM   506   N  N     . LEU A 1 65  ? 128.890 184.436 124.787 1.00 44.47  ? 67   LEU B N     1 
ATOM   507   C  CA    . LEU A 1 65  ? 129.807 184.543 125.913 1.00 41.78  ? 67   LEU B CA    1 
ATOM   508   C  C     . LEU A 1 65  ? 129.401 183.527 126.969 1.00 48.50  ? 67   LEU B C     1 
ATOM   509   O  O     . LEU A 1 65  ? 128.265 183.554 127.453 1.00 59.35  ? 67   LEU B O     1 
ATOM   510   C  CB    . LEU A 1 65  ? 129.798 185.957 126.492 1.00 46.61  ? 67   LEU B CB    1 
ATOM   511   C  CG    . LEU A 1 65  ? 129.859 187.135 125.521 1.00 51.89  ? 67   LEU B CG    1 
ATOM   512   C  CD1   . LEU A 1 65  ? 128.469 187.589 125.128 1.00 54.11  ? 67   LEU B CD1   1 
ATOM   513   C  CD2   . LEU A 1 65  ? 130.637 188.284 126.136 1.00 54.07  ? 67   LEU B CD2   1 
ATOM   514   N  N     . VAL A 1 66  ? 130.325 182.638 127.326 1.00 46.85  ? 68   VAL B N     1 
ATOM   515   C  CA    . VAL A 1 66  ? 130.056 181.581 128.289 1.00 43.66  ? 68   VAL B CA    1 
ATOM   516   C  C     . VAL A 1 66  ? 131.142 181.585 129.356 1.00 49.58  ? 68   VAL B C     1 
ATOM   517   O  O     . VAL A 1 66  ? 132.315 181.852 129.079 1.00 57.45  ? 68   VAL B O     1 
ATOM   518   C  CB    . VAL A 1 66  ? 129.953 180.193 127.614 1.00 45.15  ? 68   VAL B CB    1 
ATOM   519   C  CG1   . VAL A 1 66  ? 129.003 180.254 126.436 1.00 53.02  ? 68   VAL B CG1   1 
ATOM   520   C  CG2   . VAL A 1 66  ? 131.310 179.696 127.165 1.00 49.82  ? 68   VAL B CG2   1 
ATOM   521   N  N     . ASP A 1 67  ? 130.730 181.329 130.595 1.00 63.23  ? 69   ASP B N     1 
ATOM   522   C  CA    . ASP A 1 67  ? 131.645 181.160 131.717 1.00 60.63  ? 69   ASP B CA    1 
ATOM   523   C  C     . ASP A 1 67  ? 130.877 180.531 132.868 1.00 61.10  ? 69   ASP B C     1 
ATOM   524   O  O     . ASP A 1 67  ? 129.645 180.558 132.901 1.00 68.56  ? 69   ASP B O     1 
ATOM   525   C  CB    . ASP A 1 67  ? 132.270 182.484 132.160 1.00 59.24  ? 69   ASP B CB    1 
ATOM   526   C  CG    . ASP A 1 67  ? 133.401 182.287 133.150 1.00 67.60  ? 69   ASP B CG    1 
ATOM   527   O  OD1   . ASP A 1 67  ? 134.022 181.203 133.130 1.00 69.74  ? 69   ASP B OD1   1 
ATOM   528   O  OD2   . ASP A 1 67  ? 133.661 183.201 133.957 1.00 68.68  ? 69   ASP B OD2   1 
ATOM   529   N  N     . LEU A 1 68  ? 131.621 179.962 133.808 1.00 55.54  ? 70   LEU B N     1 
ATOM   530   C  CA    . LEU A 1 68  ? 131.043 179.410 135.022 1.00 53.82  ? 70   LEU B CA    1 
ATOM   531   C  C     . LEU A 1 68  ? 131.037 180.405 136.175 1.00 61.94  ? 70   LEU B C     1 
ATOM   532   O  O     . LEU A 1 68  ? 130.559 180.069 137.262 1.00 67.47  ? 70   LEU B O     1 
ATOM   533   C  CB    . LEU A 1 68  ? 131.794 178.142 135.424 1.00 59.75  ? 70   LEU B CB    1 
ATOM   534   C  CG    . LEU A 1 68  ? 131.755 177.040 134.367 1.00 61.36  ? 70   LEU B CG    1 
ATOM   535   C  CD1   . LEU A 1 68  ? 132.474 175.798 134.855 1.00 64.59  ? 70   LEU B CD1   1 
ATOM   536   C  CD2   . LEU A 1 68  ? 130.322 176.720 133.999 1.00 60.78  ? 70   LEU B CD2   1 
ATOM   537   N  N     . GLU A 1 69  ? 131.552 181.615 135.964 1.00 74.39  ? 71   GLU B N     1 
ATOM   538   C  CA    . GLU A 1 69  ? 131.488 182.697 136.930 1.00 69.91  ? 71   GLU B CA    1 
ATOM   539   C  C     . GLU A 1 69  ? 130.950 183.946 136.246 1.00 72.51  ? 71   GLU B C     1 
ATOM   540   O  O     . GLU A 1 69  ? 131.255 184.193 135.073 1.00 80.99  ? 71   GLU B O     1 
ATOM   541   C  CB    . GLU A 1 69  ? 132.867 182.999 137.531 1.00 70.71  ? 71   GLU B CB    1 
ATOM   542   C  CG    . GLU A 1 69  ? 133.585 181.794 138.100 1.00 73.77  ? 71   GLU B CG    1 
ATOM   543   C  CD    . GLU A 1 69  ? 134.934 182.150 138.692 1.00 78.11  ? 71   GLU B CD    1 
ATOM   544   O  OE1   . GLU A 1 69  ? 135.185 183.352 138.921 1.00 75.72  ? 71   GLU B OE1   1 
ATOM   545   O  OE2   . GLU A 1 69  ? 135.744 181.228 138.927 1.00 76.72  ? 71   GLU B OE2   1 
ATOM   546   N  N     . PRO A 1 70  ? 130.152 184.750 136.945 1.00 61.44  ? 72   PRO B N     1 
ATOM   547   C  CA    . PRO A 1 70  ? 129.598 185.969 136.345 1.00 68.06  ? 72   PRO B CA    1 
ATOM   548   C  C     . PRO A 1 70  ? 130.481 187.205 136.440 1.00 72.53  ? 72   PRO B C     1 
ATOM   549   O  O     . PRO A 1 70  ? 130.094 188.249 135.902 1.00 75.22  ? 72   PRO B O     1 
ATOM   550   C  CB    . PRO A 1 70  ? 128.310 186.169 137.151 1.00 64.88  ? 72   PRO B CB    1 
ATOM   551   C  CG    . PRO A 1 70  ? 128.621 185.607 138.480 1.00 63.13  ? 72   PRO B CG    1 
ATOM   552   C  CD    . PRO A 1 70  ? 129.555 184.456 138.257 1.00 61.55  ? 72   PRO B CD    1 
ATOM   553   N  N     . GLY A 1 71  ? 131.639 187.126 137.096 1.00 68.66  ? 73   GLY B N     1 
ATOM   554   C  CA    . GLY A 1 71  ? 132.458 188.316 137.269 1.00 67.41  ? 73   GLY B CA    1 
ATOM   555   C  C     . GLY A 1 71  ? 132.987 188.869 135.958 1.00 71.23  ? 73   GLY B C     1 
ATOM   556   O  O     . GLY A 1 71  ? 132.888 190.071 135.689 1.00 73.30  ? 73   GLY B O     1 
ATOM   557   N  N     . THR A 1 72  ? 133.540 187.997 135.112 1.00 66.37  ? 74   THR B N     1 
ATOM   558   C  CA    . THR A 1 72  ? 134.075 188.472 133.842 1.00 69.22  ? 74   THR B CA    1 
ATOM   559   C  C     . THR A 1 72  ? 132.960 188.885 132.890 1.00 72.40  ? 74   THR B C     1 
ATOM   560   O  O     . THR A 1 72  ? 133.149 189.796 132.076 1.00 76.10  ? 74   THR B O     1 
ATOM   561   C  CB    . THR A 1 72  ? 134.965 187.407 133.204 1.00 69.43  ? 74   THR B CB    1 
ATOM   562   O  OG1   . THR A 1 72  ? 135.445 187.880 131.940 1.00 70.91  ? 74   THR B OG1   1 
ATOM   563   C  CG2   . THR A 1 72  ? 134.196 186.121 132.993 1.00 70.32  ? 74   THR B CG2   1 
ATOM   564   N  N     . MET A 1 73  ? 131.794 188.243 132.983 1.00 66.26  ? 75   MET B N     1 
ATOM   565   C  CA    . MET A 1 73  ? 130.651 188.676 132.188 1.00 66.02  ? 75   MET B CA    1 
ATOM   566   C  C     . MET A 1 73  ? 130.207 190.074 132.588 1.00 68.23  ? 75   MET B C     1 
ATOM   567   O  O     . MET A 1 73  ? 129.897 190.906 131.728 1.00 74.91  ? 75   MET B O     1 
ATOM   568   C  CB    . MET A 1 73  ? 129.501 187.684 132.341 1.00 68.29  ? 75   MET B CB    1 
ATOM   569   C  CG    . MET A 1 73  ? 129.804 186.332 131.752 1.00 64.97  ? 75   MET B CG    1 
ATOM   570   S  SD    . MET A 1 73  ? 130.244 186.483 130.021 1.00 76.20  ? 75   MET B SD    1 
ATOM   571   C  CE    . MET A 1 73  ? 130.930 184.864 129.737 1.00 72.77  ? 75   MET B CE    1 
ATOM   572   N  N     . ASP A 1 74  ? 130.171 190.350 133.892 1.00 59.24  ? 76   ASP B N     1 
ATOM   573   C  CA    . ASP A 1 74  ? 129.848 191.694 134.352 1.00 62.07  ? 76   ASP B CA    1 
ATOM   574   C  C     . ASP A 1 74  ? 130.900 192.696 133.897 1.00 63.63  ? 76   ASP B C     1 
ATOM   575   O  O     . ASP A 1 74  ? 130.571 193.830 133.529 1.00 72.17  ? 76   ASP B O     1 
ATOM   576   C  CB    . ASP A 1 74  ? 129.709 191.706 135.874 1.00 67.31  ? 76   ASP B CB    1 
ATOM   577   C  CG    . ASP A 1 74  ? 128.785 192.802 136.368 1.00 72.28  ? 76   ASP B CG    1 
ATOM   578   O  OD1   . ASP A 1 74  ? 128.676 193.845 135.690 1.00 72.13  ? 76   ASP B OD1   1 
ATOM   579   O  OD2   . ASP A 1 74  ? 128.167 192.620 137.438 1.00 68.53  ? 76   ASP B OD2   1 
ATOM   580   N  N     . SER A 1 75  ? 132.174 192.295 133.916 1.00 54.74  ? 77   SER B N     1 
ATOM   581   C  CA    . SER A 1 75  ? 133.231 193.183 133.440 1.00 58.34  ? 77   SER B CA    1 
ATOM   582   C  C     . SER A 1 75  ? 133.060 193.511 131.961 1.00 65.30  ? 77   SER B C     1 
ATOM   583   O  O     . SER A 1 75  ? 133.241 194.663 131.548 1.00 67.53  ? 77   SER B O     1 
ATOM   584   C  CB    . SER A 1 75  ? 134.600 192.553 133.692 1.00 61.98  ? 77   SER B CB    1 
ATOM   585   O  OG    . SER A 1 75  ? 134.821 191.455 132.826 1.00 64.15  ? 77   SER B OG    1 
ATOM   586   N  N     . VAL A 1 76  ? 132.720 192.510 131.146 1.00 60.00  ? 78   VAL B N     1 
ATOM   587   C  CA    . VAL A 1 76  ? 132.489 192.748 129.722 1.00 51.22  ? 78   VAL B CA    1 
ATOM   588   C  C     . VAL A 1 76  ? 131.275 193.645 129.521 1.00 55.14  ? 78   VAL B C     1 
ATOM   589   O  O     . VAL A 1 76  ? 131.296 194.568 128.698 1.00 63.94  ? 78   VAL B O     1 
ATOM   590   C  CB    . VAL A 1 76  ? 132.335 191.412 128.971 1.00 56.88  ? 78   VAL B CB    1 
ATOM   591   C  CG1   . VAL A 1 76  ? 131.787 191.643 127.576 1.00 61.13  ? 78   VAL B CG1   1 
ATOM   592   C  CG2   . VAL A 1 76  ? 133.663 190.688 128.903 1.00 55.39  ? 78   VAL B CG2   1 
ATOM   593   N  N     . ARG A 1 77  ? 130.199 193.388 130.266 1.00 59.29  ? 79   ARG B N     1 
ATOM   594   C  CA    . ARG A 1 77  ? 128.986 194.187 130.130 1.00 56.87  ? 79   ARG B CA    1 
ATOM   595   C  C     . ARG A 1 77  ? 129.237 195.641 130.500 1.00 58.81  ? 79   ARG B C     1 
ATOM   596   O  O     . ARG A 1 77  ? 128.715 196.555 129.852 1.00 61.10  ? 79   ARG B O     1 
ATOM   597   C  CB    . ARG A 1 77  ? 127.877 193.602 131.005 1.00 55.28  ? 79   ARG B CB    1 
ATOM   598   C  CG    . ARG A 1 77  ? 126.575 193.342 130.275 1.00 62.46  ? 79   ARG B CG    1 
ATOM   599   C  CD    . ARG A 1 77  ? 125.435 193.109 131.249 1.00 63.64  ? 79   ARG B CD    1 
ATOM   600   N  NE    . ARG A 1 77  ? 125.690 191.977 132.130 1.00 65.84  ? 79   ARG B NE    1 
ATOM   601   C  CZ    . ARG A 1 77  ? 125.170 190.770 131.966 1.00 67.40  ? 79   ARG B CZ    1 
ATOM   602   N  NH1   . ARG A 1 77  ? 124.358 190.499 130.958 1.00 65.65  ? 79   ARG B NH1   1 
ATOM   603   N  NH2   . ARG A 1 77  ? 125.473 189.810 132.834 1.00 66.18  ? 79   ARG B NH2   1 
ATOM   604   N  N     . SER A 1 78  ? 130.037 195.874 131.538 1.00 63.29  ? 80   SER B N     1 
ATOM   605   C  CA    . SER A 1 78  ? 130.287 197.225 132.020 1.00 61.77  ? 80   SER B CA    1 
ATOM   606   C  C     . SER A 1 78  ? 131.331 197.965 131.198 1.00 61.87  ? 80   SER B C     1 
ATOM   607   O  O     . SER A 1 78  ? 131.577 199.147 131.456 1.00 65.28  ? 80   SER B O     1 
ATOM   608   C  CB    . SER A 1 78  ? 130.724 197.183 133.484 1.00 62.49  ? 80   SER B CB    1 
ATOM   609   O  OG    . SER A 1 78  ? 129.732 196.577 134.293 1.00 62.20  ? 80   SER B OG    1 
ATOM   610   N  N     . GLY A 1 79  ? 131.949 197.306 130.222 1.00 63.58  ? 81   GLY B N     1 
ATOM   611   C  CA    . GLY A 1 79  ? 133.000 197.911 129.442 1.00 63.53  ? 81   GLY B CA    1 
ATOM   612   C  C     . GLY A 1 79  ? 132.482 198.933 128.453 1.00 65.15  ? 81   GLY B C     1 
ATOM   613   O  O     . GLY A 1 79  ? 131.289 199.250 128.416 1.00 65.26  ? 81   GLY B O     1 
ATOM   614   N  N     . PRO A 1 80  ? 133.379 199.474 127.625 1.00 67.58  ? 82   PRO B N     1 
ATOM   615   C  CA    . PRO A 1 80  ? 132.953 200.488 126.650 1.00 67.61  ? 82   PRO B CA    1 
ATOM   616   C  C     . PRO A 1 80  ? 132.212 199.908 125.462 1.00 71.03  ? 82   PRO B C     1 
ATOM   617   O  O     . PRO A 1 80  ? 131.370 200.603 124.881 1.00 71.75  ? 82   PRO B O     1 
ATOM   618   C  CB    . PRO A 1 80  ? 134.271 201.144 126.219 1.00 68.39  ? 82   PRO B CB    1 
ATOM   619   C  CG    . PRO A 1 80  ? 135.358 200.176 126.602 1.00 70.01  ? 82   PRO B CG    1 
ATOM   620   C  CD    . PRO A 1 80  ? 134.781 199.070 127.438 1.00 69.24  ? 82   PRO B CD    1 
ATOM   621   N  N     . PHE A 1 81  ? 132.491 198.664 125.086 1.00 72.70  ? 83   PHE B N     1 
ATOM   622   C  CA    . PHE A 1 81  ? 131.809 197.983 123.995 1.00 67.47  ? 83   PHE B CA    1 
ATOM   623   C  C     . PHE A 1 81  ? 131.018 196.796 124.523 1.00 65.02  ? 83   PHE B C     1 
ATOM   624   O  O     . PHE A 1 81  ? 131.020 195.712 123.938 1.00 69.87  ? 83   PHE B O     1 
ATOM   625   C  CB    . PHE A 1 81  ? 132.798 197.532 122.924 1.00 64.91  ? 83   PHE B CB    1 
ATOM   626   C  CG    . PHE A 1 81  ? 132.961 198.512 121.804 1.00 66.43  ? 83   PHE B CG    1 
ATOM   627   C  CD1   . PHE A 1 81  ? 133.825 199.584 121.925 1.00 67.78  ? 83   PHE B CD1   1 
ATOM   628   C  CD2   . PHE A 1 81  ? 132.237 198.371 120.635 1.00 67.50  ? 83   PHE B CD2   1 
ATOM   629   C  CE1   . PHE A 1 81  ? 133.974 200.489 120.896 1.00 69.87  ? 83   PHE B CE1   1 
ATOM   630   C  CE2   . PHE A 1 81  ? 132.380 199.273 119.607 1.00 70.40  ? 83   PHE B CE2   1 
ATOM   631   C  CZ    . PHE A 1 81  ? 133.250 200.334 119.737 1.00 70.12  ? 83   PHE B CZ    1 
ATOM   632   N  N     . GLY A 1 82  ? 130.333 196.991 125.644 1.00 55.17  ? 84   GLY B N     1 
ATOM   633   C  CA    . GLY A 1 82  ? 129.612 195.907 126.275 1.00 55.01  ? 84   GLY B CA    1 
ATOM   634   C  C     . GLY A 1 82  ? 128.145 195.859 125.915 1.00 62.97  ? 84   GLY B C     1 
ATOM   635   O  O     . GLY A 1 82  ? 127.550 194.779 125.866 1.00 64.05  ? 84   GLY B O     1 
ATOM   636   N  N     . GLN A 1 83  ? 127.545 197.018 125.659 1.00 59.18  ? 85   GLN B N     1 
ATOM   637   C  CA    . GLN A 1 83  ? 126.130 197.065 125.323 1.00 57.42  ? 85   GLN B CA    1 
ATOM   638   C  C     . GLN A 1 83  ? 125.857 196.682 123.875 1.00 61.80  ? 85   GLN B C     1 
ATOM   639   O  O     . GLN A 1 83  ? 124.689 196.590 123.485 1.00 63.16  ? 85   GLN B O     1 
ATOM   640   C  CB    . GLN A 1 83  ? 125.563 198.454 125.618 1.00 53.90  ? 85   GLN B CB    1 
ATOM   641   C  CG    . GLN A 1 83  ? 126.078 199.553 124.715 1.00 63.49  ? 85   GLN B CG    1 
ATOM   642   C  CD    . GLN A 1 83  ? 125.351 200.863 124.937 1.00 67.01  ? 85   GLN B CD    1 
ATOM   643   O  OE1   . GLN A 1 83  ? 124.499 200.968 125.819 1.00 60.40  ? 85   GLN B OE1   1 
ATOM   644   N  NE2   . GLN A 1 83  ? 125.684 201.870 124.140 1.00 65.96  ? 85   GLN B NE2   1 
ATOM   645   N  N     . ILE A 1 84  ? 126.899 196.458 123.074 1.00 58.34  ? 86   ILE B N     1 
ATOM   646   C  CA    . ILE A 1 84  ? 126.701 195.998 121.706 1.00 57.42  ? 86   ILE B CA    1 
ATOM   647   C  C     . ILE A 1 84  ? 126.198 194.559 121.678 1.00 54.70  ? 86   ILE B C     1 
ATOM   648   O  O     . ILE A 1 84  ? 125.455 194.178 120.767 1.00 61.98  ? 86   ILE B O     1 
ATOM   649   C  CB    . ILE A 1 84  ? 128.001 196.165 120.897 1.00 56.16  ? 86   ILE B CB    1 
ATOM   650   C  CG1   . ILE A 1 84  ? 127.727 196.023 119.403 1.00 59.94  ? 86   ILE B CG1   1 
ATOM   651   C  CG2   . ILE A 1 84  ? 129.061 195.171 121.345 1.00 54.38  ? 86   ILE B CG2   1 
ATOM   652   C  CD1   . ILE A 1 84  ? 128.961 196.161 118.544 1.00 61.64  ? 86   ILE B CD1   1 
ATOM   653   N  N     . PHE A 1 85  ? 126.572 193.746 122.662 1.00 43.14  ? 87   PHE B N     1 
ATOM   654   C  CA    . PHE A 1 85  ? 126.216 192.335 122.651 1.00 48.53  ? 87   PHE B CA    1 
ATOM   655   C  C     . PHE A 1 85  ? 124.739 192.135 122.960 1.00 47.92  ? 87   PHE B C     1 
ATOM   656   O  O     . PHE A 1 85  ? 124.071 193.006 123.522 1.00 54.12  ? 87   PHE B O     1 
ATOM   657   C  CB    . PHE A 1 85  ? 127.057 191.559 123.662 1.00 48.32  ? 87   PHE B CB    1 
ATOM   658   C  CG    . PHE A 1 85  ? 128.521 191.550 123.355 1.00 43.94  ? 87   PHE B CG    1 
ATOM   659   C  CD1   . PHE A 1 85  ? 129.366 192.484 123.918 1.00 49.05  ? 87   PHE B CD1   1 
ATOM   660   C  CD2   . PHE A 1 85  ? 129.053 190.608 122.498 1.00 44.89  ? 87   PHE B CD2   1 
ATOM   661   C  CE1   . PHE A 1 85  ? 130.710 192.474 123.636 1.00 49.22  ? 87   PHE B CE1   1 
ATOM   662   C  CE2   . PHE A 1 85  ? 130.394 190.597 122.215 1.00 46.81  ? 87   PHE B CE2   1 
ATOM   663   C  CZ    . PHE A 1 85  ? 131.224 191.532 122.784 1.00 47.29  ? 87   PHE B CZ    1 
ATOM   664   N  N     . ARG A 1 86  ? 124.234 190.970 122.584 1.00 42.25  ? 88   ARG B N     1 
ATOM   665   C  CA    . ARG A 1 86  ? 122.854 190.625 122.886 1.00 46.85  ? 88   ARG B CA    1 
ATOM   666   C  C     . ARG A 1 86  ? 122.741 190.174 124.337 1.00 56.95  ? 88   ARG B C     1 
ATOM   667   O  O     . ARG A 1 86  ? 123.477 189.276 124.760 1.00 59.31  ? 88   ARG B O     1 
ATOM   668   C  CB    . ARG A 1 86  ? 122.364 189.525 121.955 1.00 50.89  ? 88   ARG B CB    1 
ATOM   669   C  CG    . ARG A 1 86  ? 120.922 189.119 122.183 1.00 54.28  ? 88   ARG B CG    1 
ATOM   670   C  CD    . ARG A 1 86  ? 120.439 188.211 121.073 1.00 50.78  ? 88   ARG B CD    1 
ATOM   671   N  NE    . ARG A 1 86  ? 120.512 188.874 119.779 1.00 49.45  ? 88   ARG B NE    1 
ATOM   672   C  CZ    . ARG A 1 86  ? 120.215 188.299 118.624 1.00 53.80  ? 88   ARG B CZ    1 
ATOM   673   N  NH1   . ARG A 1 86  ? 119.818 187.039 118.561 1.00 56.59  ? 88   ARG B NH1   1 
ATOM   674   N  NH2   . ARG A 1 86  ? 120.323 189.005 117.502 1.00 52.33  ? 88   ARG B NH2   1 
ATOM   675   N  N     . PRO A 1 87  ? 121.845 190.768 125.129 1.00 46.89  ? 89   PRO B N     1 
ATOM   676   C  CA    . PRO A 1 87  ? 121.720 190.355 126.534 1.00 37.66  ? 89   PRO B CA    1 
ATOM   677   C  C     . PRO A 1 87  ? 121.304 188.909 126.711 1.00 41.83  ? 89   PRO B C     1 
ATOM   678   O  O     . PRO A 1 87  ? 121.558 188.337 127.777 1.00 50.81  ? 89   PRO B O     1 
ATOM   679   C  CB    . PRO A 1 87  ? 120.662 191.317 127.089 1.00 40.09  ? 89   PRO B CB    1 
ATOM   680   C  CG    . PRO A 1 87  ? 119.937 191.824 125.899 1.00 42.44  ? 89   PRO B CG    1 
ATOM   681   C  CD    . PRO A 1 87  ? 120.942 191.882 124.801 1.00 46.21  ? 89   PRO B CD    1 
ATOM   682   N  N     . ASP A 1 88  ? 120.682 188.292 125.707 1.00 49.34  ? 90   ASP B N     1 
ATOM   683   C  CA    . ASP A 1 88  ? 120.298 186.892 125.820 1.00 51.15  ? 90   ASP B CA    1 
ATOM   684   C  C     . ASP A 1 88  ? 121.457 185.943 125.560 1.00 56.41  ? 90   ASP B C     1 
ATOM   685   O  O     . ASP A 1 88  ? 121.346 184.753 125.872 1.00 60.01  ? 90   ASP B O     1 
ATOM   686   C  CB    . ASP A 1 88  ? 119.156 186.580 124.853 1.00 56.01  ? 90   ASP B CB    1 
ATOM   687   C  CG    . ASP A 1 88  ? 117.932 187.437 125.102 1.00 68.75  ? 90   ASP B CG    1 
ATOM   688   O  OD1   . ASP A 1 88  ? 117.758 187.911 126.245 1.00 73.14  ? 90   ASP B OD1   1 
ATOM   689   O  OD2   . ASP A 1 88  ? 117.144 187.639 124.154 1.00 66.42  ? 90   ASP B OD2   1 
ATOM   690   N  N     . ASN A 1 89  ? 122.561 186.436 124.994 1.00 58.54  ? 91   ASN B N     1 
ATOM   691   C  CA    . ASN A 1 89  ? 123.685 185.569 124.662 1.00 54.01  ? 91   ASN B CA    1 
ATOM   692   C  C     . ASN A 1 89  ? 124.602 185.316 125.849 1.00 62.05  ? 91   ASN B C     1 
ATOM   693   O  O     . ASN A 1 89  ? 125.454 184.425 125.774 1.00 68.72  ? 91   ASN B O     1 
ATOM   694   C  CB    . ASN A 1 89  ? 124.488 186.168 123.510 1.00 48.06  ? 91   ASN B CB    1 
ATOM   695   C  CG    . ASN A 1 89  ? 123.838 185.930 122.166 1.00 60.20  ? 91   ASN B CG    1 
ATOM   696   O  OD1   . ASN A 1 89  ? 122.713 185.443 122.087 1.00 63.14  ? 91   ASN B OD1   1 
ATOM   697   N  ND2   . ASN A 1 89  ? 124.544 186.275 121.098 1.00 61.26  ? 91   ASN B ND2   1 
ATOM   698   N  N     . PHE A 1 90  ? 124.457 186.073 126.933 1.00 54.20  ? 92   PHE B N     1 
ATOM   699   C  CA    . PHE A 1 90  ? 125.261 185.848 128.129 1.00 44.03  ? 92   PHE B CA    1 
ATOM   700   C  C     . PHE A 1 90  ? 124.743 184.618 128.860 1.00 48.86  ? 92   PHE B C     1 
ATOM   701   O  O     . PHE A 1 90  ? 123.703 184.672 129.522 1.00 60.06  ? 92   PHE B O     1 
ATOM   702   C  CB    . PHE A 1 90  ? 125.220 187.071 129.037 1.00 46.86  ? 92   PHE B CB    1 
ATOM   703   C  CG    . PHE A 1 90  ? 125.742 188.320 128.400 1.00 48.70  ? 92   PHE B CG    1 
ATOM   704   C  CD1   . PHE A 1 90  ? 127.095 188.586 128.381 1.00 49.92  ? 92   PHE B CD1   1 
ATOM   705   C  CD2   . PHE A 1 90  ? 124.880 189.236 127.833 1.00 54.94  ? 92   PHE B CD2   1 
ATOM   706   C  CE1   . PHE A 1 90  ? 127.578 189.735 127.803 1.00 53.52  ? 92   PHE B CE1   1 
ATOM   707   C  CE2   . PHE A 1 90  ? 125.360 190.389 127.254 1.00 53.51  ? 92   PHE B CE2   1 
ATOM   708   C  CZ    . PHE A 1 90  ? 126.711 190.638 127.239 1.00 52.60  ? 92   PHE B CZ    1 
ATOM   709   N  N     . VAL A 1 91  ? 125.463 183.509 128.744 1.00 40.36  ? 93   VAL B N     1 
ATOM   710   C  CA    . VAL A 1 91  ? 125.113 182.261 129.409 1.00 43.18  ? 93   VAL B CA    1 
ATOM   711   C  C     . VAL A 1 91  ? 126.179 181.984 130.455 1.00 54.42  ? 93   VAL B C     1 
ATOM   712   O  O     . VAL A 1 91  ? 127.356 181.808 130.120 1.00 56.66  ? 93   VAL B O     1 
ATOM   713   C  CB    . VAL A 1 91  ? 124.998 181.099 128.413 1.00 45.45  ? 93   VAL B CB    1 
ATOM   714   C  CG1   . VAL A 1 91  ? 124.546 179.843 129.125 1.00 48.90  ? 93   VAL B CG1   1 
ATOM   715   C  CG2   . VAL A 1 91  ? 124.037 181.457 127.300 1.00 51.15  ? 93   VAL B CG2   1 
ATOM   716   N  N     . PHE A 1 92  ? 125.773 181.948 131.722 1.00 58.08  ? 94   PHE B N     1 
ATOM   717   C  CA    . PHE A 1 92  ? 126.727 181.778 132.804 1.00 50.40  ? 94   PHE B CA    1 
ATOM   718   C  C     . PHE A 1 92  ? 126.075 181.047 133.966 1.00 53.68  ? 94   PHE B C     1 
ATOM   719   O  O     . PHE A 1 92  ? 124.862 181.129 134.172 1.00 58.27  ? 94   PHE B O     1 
ATOM   720   C  CB    . PHE A 1 92  ? 127.284 183.125 133.277 1.00 50.97  ? 94   PHE B CB    1 
ATOM   721   C  CG    . PHE A 1 92  ? 126.230 184.144 133.592 1.00 53.24  ? 94   PHE B CG    1 
ATOM   722   C  CD1   . PHE A 1 92  ? 125.594 184.147 134.818 1.00 52.22  ? 94   PHE B CD1   1 
ATOM   723   C  CD2   . PHE A 1 92  ? 125.891 185.114 132.669 1.00 60.85  ? 94   PHE B CD2   1 
ATOM   724   C  CE1   . PHE A 1 92  ? 124.629 185.085 135.110 1.00 56.97  ? 94   PHE B CE1   1 
ATOM   725   C  CE2   . PHE A 1 92  ? 124.929 186.058 132.958 1.00 59.73  ? 94   PHE B CE2   1 
ATOM   726   C  CZ    . PHE A 1 92  ? 124.298 186.042 134.181 1.00 61.21  ? 94   PHE B CZ    1 
ATOM   727   N  N     . GLY A 1 93  ? 126.898 180.331 134.721 1.00 62.99  ? 95   GLY B N     1 
ATOM   728   C  CA    . GLY A 1 93  ? 126.489 179.727 135.970 1.00 62.35  ? 95   GLY B CA    1 
ATOM   729   C  C     . GLY A 1 93  ? 126.896 180.582 137.149 1.00 65.88  ? 95   GLY B C     1 
ATOM   730   O  O     . GLY A 1 93  ? 127.232 181.760 137.012 1.00 75.65  ? 95   GLY B O     1 
ATOM   731   N  N     . GLN A 1 94  ? 126.867 179.972 138.333 1.00 55.00  ? 96   GLN B N     1 
ATOM   732   C  CA    . GLN A 1 94  ? 127.293 180.657 139.543 1.00 58.47  ? 96   GLN B CA    1 
ATOM   733   C  C     . GLN A 1 94  ? 128.387 179.937 140.317 1.00 57.92  ? 96   GLN B C     1 
ATOM   734   O  O     . GLN A 1 94  ? 128.893 180.502 141.292 1.00 62.09  ? 96   GLN B O     1 
ATOM   735   C  CB    . GLN A 1 94  ? 126.099 180.899 140.478 1.00 60.70  ? 96   GLN B CB    1 
ATOM   736   C  CG    . GLN A 1 94  ? 125.437 182.255 140.297 1.00 58.20  ? 96   GLN B CG    1 
ATOM   737   C  CD    . GLN A 1 94  ? 124.535 182.309 139.086 1.00 61.14  ? 96   GLN B CD    1 
ATOM   738   O  OE1   . GLN A 1 94  ? 124.122 181.276 138.558 1.00 66.85  ? 96   GLN B OE1   1 
ATOM   739   N  NE2   . GLN A 1 94  ? 124.219 183.517 138.638 1.00 59.37  ? 96   GLN B NE2   1 
ATOM   740   N  N     . SER A 1 95  ? 128.766 178.725 139.928 1.00 57.98  ? 97   SER B N     1 
ATOM   741   C  CA    . SER A 1 95  ? 129.867 178.007 140.557 1.00 62.79  ? 97   SER B CA    1 
ATOM   742   C  C     . SER A 1 95  ? 130.975 177.806 139.531 1.00 64.20  ? 97   SER B C     1 
ATOM   743   O  O     . SER A 1 95  ? 130.783 177.099 138.535 1.00 69.47  ? 97   SER B O     1 
ATOM   744   C  CB    . SER A 1 95  ? 129.394 176.666 141.115 1.00 65.27  ? 97   SER B CB    1 
ATOM   745   O  OG    . SER A 1 95  ? 128.842 175.858 140.091 1.00 68.58  ? 97   SER B OG    1 
ATOM   746   N  N     . GLY A 1 96  ? 132.126 178.422 139.773 1.00 55.73  ? 98   GLY B N     1 
ATOM   747   C  CA    . GLY A 1 96  ? 133.223 178.350 138.833 1.00 58.53  ? 98   GLY B CA    1 
ATOM   748   C  C     . GLY A 1 96  ? 133.908 176.999 138.830 1.00 64.39  ? 98   GLY B C     1 
ATOM   749   O  O     . GLY A 1 96  ? 133.733 176.166 139.720 1.00 66.85  ? 98   GLY B O     1 
ATOM   750   N  N     . ALA A 1 97  ? 134.713 176.781 137.789 1.00 56.00  ? 99   ALA B N     1 
ATOM   751   C  CA    . ALA A 1 97  ? 135.420 175.514 137.660 1.00 55.06  ? 99   ALA B CA    1 
ATOM   752   C  C     . ALA A 1 97  ? 136.589 175.410 138.628 1.00 57.36  ? 99   ALA B C     1 
ATOM   753   O  O     . ALA A 1 97  ? 137.028 174.298 138.941 1.00 61.29  ? 99   ALA B O     1 
ATOM   754   C  CB    . ALA A 1 97  ? 135.912 175.321 136.227 1.00 54.70  ? 99   ALA B CB    1 
ATOM   755   N  N     . GLY A 1 98  ? 137.098 176.538 139.113 1.00 52.86  ? 100  GLY B N     1 
ATOM   756   C  CA    . GLY A 1 98  ? 138.216 176.509 140.038 1.00 52.22  ? 100  GLY B CA    1 
ATOM   757   C  C     . GLY A 1 98  ? 139.474 175.908 139.459 1.00 52.30  ? 100  GLY B C     1 
ATOM   758   O  O     . GLY A 1 98  ? 140.185 175.180 140.160 1.00 53.07  ? 100  GLY B O     1 
ATOM   759   N  N     . ASN A 1 99  ? 139.767 176.194 138.190 1.00 49.68  ? 101  ASN B N     1 
ATOM   760   C  CA    . ASN A 1 99  ? 140.937 175.657 137.496 1.00 46.93  ? 101  ASN B CA    1 
ATOM   761   C  C     . ASN A 1 99  ? 140.955 174.132 137.541 1.00 55.37  ? 101  ASN B C     1 
ATOM   762   O  O     . ASN A 1 99  ? 142.009 173.499 137.622 1.00 60.98  ? 101  ASN B O     1 
ATOM   763   C  CB    . ASN A 1 99  ? 142.230 176.243 138.061 1.00 47.55  ? 101  ASN B CB    1 
ATOM   764   C  CG    . ASN A 1 99  ? 142.279 177.746 137.948 1.00 53.93  ? 101  ASN B CG    1 
ATOM   765   O  OD1   . ASN A 1 99  ? 141.275 178.389 137.647 1.00 56.97  ? 101  ASN B OD1   1 
ATOM   766   N  ND2   . ASN A 1 99  ? 143.449 178.320 138.193 1.00 56.15  ? 101  ASN B ND2   1 
ATOM   767   N  N     . ASN A 1 100 ? 139.765 173.542 137.490 1.00 56.14  ? 102  ASN B N     1 
ATOM   768   C  CA    . ASN A 1 100 ? 139.594 172.096 137.432 1.00 48.98  ? 102  ASN B CA    1 
ATOM   769   C  C     . ASN A 1 100 ? 138.989 171.762 136.077 1.00 49.06  ? 102  ASN B C     1 
ATOM   770   O  O     . ASN A 1 100 ? 137.850 172.145 135.791 1.00 60.67  ? 102  ASN B O     1 
ATOM   771   C  CB    . ASN A 1 100 ? 138.706 171.601 138.572 1.00 52.54  ? 102  ASN B CB    1 
ATOM   772   C  CG    . ASN A 1 100 ? 138.806 170.109 138.785 1.00 55.24  ? 102  ASN B CG    1 
ATOM   773   O  OD1   . ASN A 1 100 ? 139.043 169.348 137.849 1.00 62.86  ? 102  ASN B OD1   1 
ATOM   774   N  ND2   . ASN A 1 100 ? 138.624 169.680 140.026 1.00 51.87  ? 102  ASN B ND2   1 
ATOM   775   N  N     . TRP A 1 101 ? 139.754 171.060 135.242 1.00 48.33  ? 103  TRP B N     1 
ATOM   776   C  CA    . TRP A 1 101 ? 139.242 170.648 133.941 1.00 53.40  ? 103  TRP B CA    1 
ATOM   777   C  C     . TRP A 1 101 ? 138.055 169.710 134.091 1.00 54.78  ? 103  TRP B C     1 
ATOM   778   O  O     . TRP A 1 101 ? 137.071 169.815 133.348 1.00 60.13  ? 103  TRP B O     1 
ATOM   779   C  CB    . TRP A 1 101 ? 140.349 169.980 133.133 1.00 55.10  ? 103  TRP B CB    1 
ATOM   780   C  CG    . TRP A 1 101 ? 139.979 169.712 131.719 1.00 58.95  ? 103  TRP B CG    1 
ATOM   781   C  CD1   . TRP A 1 101 ? 140.172 170.535 130.655 1.00 62.44  ? 103  TRP B CD1   1 
ATOM   782   C  CD2   . TRP A 1 101 ? 139.359 168.531 131.207 1.00 56.27  ? 103  TRP B CD2   1 
ATOM   783   N  NE1   . TRP A 1 101 ? 139.707 169.943 129.510 1.00 60.56  ? 103  TRP B NE1   1 
ATOM   784   C  CE2   . TRP A 1 101 ? 139.202 168.709 129.824 1.00 57.47  ? 103  TRP B CE2   1 
ATOM   785   C  CE3   . TRP A 1 101 ? 138.917 167.340 131.786 1.00 58.42  ? 103  TRP B CE3   1 
ATOM   786   C  CZ2   . TRP A 1 101 ? 138.624 167.745 129.011 1.00 56.42  ? 103  TRP B CZ2   1 
ATOM   787   C  CZ3   . TRP A 1 101 ? 138.344 166.385 130.977 1.00 56.05  ? 103  TRP B CZ3   1 
ATOM   788   C  CH2   . TRP A 1 101 ? 138.202 166.592 129.605 1.00 54.26  ? 103  TRP B CH2   1 
ATOM   789   N  N     . ALA A 1 102 ? 138.134 168.781 135.043 1.00 51.90  ? 104  ALA B N     1 
ATOM   790   C  CA    . ALA A 1 102 ? 137.025 167.865 135.269 1.00 49.50  ? 104  ALA B CA    1 
ATOM   791   C  C     . ALA A 1 102 ? 135.769 168.623 135.665 1.00 48.26  ? 104  ALA B C     1 
ATOM   792   O  O     . ALA A 1 102 ? 134.673 168.307 135.195 1.00 56.17  ? 104  ALA B O     1 
ATOM   793   C  CB    . ALA A 1 102 ? 137.400 166.842 136.339 1.00 57.74  ? 104  ALA B CB    1 
ATOM   794   N  N     . LYS A 1 103 ? 135.912 169.641 136.513 1.00 54.90  ? 105  LYS B N     1 
ATOM   795   C  CA    . LYS A 1 103 ? 134.749 170.398 136.959 1.00 52.61  ? 105  LYS B CA    1 
ATOM   796   C  C     . LYS A 1 103 ? 134.073 171.112 135.796 1.00 54.72  ? 105  LYS B C     1 
ATOM   797   O  O     . LYS A 1 103 ? 132.840 171.169 135.725 1.00 60.79  ? 105  LYS B O     1 
ATOM   798   C  CB    . LYS A 1 103 ? 135.165 171.394 138.041 1.00 53.83  ? 105  LYS B CB    1 
ATOM   799   C  CG    . LYS A 1 103 ? 134.042 172.268 138.554 1.00 60.17  ? 105  LYS B CG    1 
ATOM   800   C  CD    . LYS A 1 103 ? 133.862 172.098 140.052 1.00 62.03  ? 105  LYS B CD    1 
ATOM   801   C  CE    . LYS A 1 103 ? 135.120 172.475 140.807 1.00 58.38  ? 105  LYS B CE    1 
ATOM   802   N  NZ    . LYS A 1 103 ? 134.934 172.361 142.278 1.00 56.64  ? 105  LYS B NZ    1 
ATOM   803   N  N     . GLY A 1 104 ? 134.859 171.657 134.871 1.00 53.20  ? 106  GLY B N     1 
ATOM   804   C  CA    . GLY A 1 104 ? 134.296 172.358 133.734 1.00 56.28  ? 106  GLY B CA    1 
ATOM   805   C  C     . GLY A 1 104 ? 133.882 171.490 132.569 1.00 60.57  ? 106  GLY B C     1 
ATOM   806   O  O     . GLY A 1 104 ? 133.177 171.975 131.680 1.00 70.89  ? 106  GLY B O     1 
ATOM   807   N  N     . HIS A 1 105 ? 134.294 170.224 132.544 1.00 56.16  ? 107  HIS B N     1 
ATOM   808   C  CA    . HIS A 1 105 ? 133.970 169.339 131.437 1.00 55.81  ? 107  HIS B CA    1 
ATOM   809   C  C     . HIS A 1 105 ? 132.984 168.236 131.791 1.00 59.45  ? 107  HIS B C     1 
ATOM   810   O  O     . HIS A 1 105 ? 132.381 167.661 130.877 1.00 63.96  ? 107  HIS B O     1 
ATOM   811   C  CB    . HIS A 1 105 ? 135.250 168.695 130.881 1.00 56.50  ? 107  HIS B CB    1 
ATOM   812   C  CG    . HIS A 1 105 ? 135.082 168.078 129.528 1.00 59.04  ? 107  HIS B CG    1 
ATOM   813   N  ND1   . HIS A 1 105 ? 134.537 166.827 129.341 1.00 60.34  ? 107  HIS B ND1   1 
ATOM   814   C  CD2   . HIS A 1 105 ? 135.402 168.536 128.295 1.00 62.78  ? 107  HIS B CD2   1 
ATOM   815   C  CE1   . HIS A 1 105 ? 134.521 166.544 128.051 1.00 59.87  ? 107  HIS B CE1   1 
ATOM   816   N  NE2   . HIS A 1 105 ? 135.041 167.565 127.395 1.00 60.22  ? 107  HIS B NE2   1 
ATOM   817   N  N     . TYR A 1 106 ? 132.790 167.928 133.069 1.00 61.97  ? 108  TYR B N     1 
ATOM   818   C  CA    . TYR A 1 106 ? 131.973 166.801 133.490 1.00 58.07  ? 108  TYR B CA    1 
ATOM   819   C  C     . TYR A 1 106 ? 130.827 167.192 134.407 1.00 63.53  ? 108  TYR B C     1 
ATOM   820   O  O     . TYR A 1 106 ? 129.730 166.643 134.278 1.00 67.76  ? 108  TYR B O     1 
ATOM   821   C  CB    . TYR A 1 106 ? 132.849 165.764 134.207 1.00 55.65  ? 108  TYR B CB    1 
ATOM   822   C  CG    . TYR A 1 106 ? 133.583 164.805 133.297 1.00 58.17  ? 108  TYR B CG    1 
ATOM   823   C  CD1   . TYR A 1 106 ? 133.706 165.054 131.941 1.00 60.20  ? 108  TYR B CD1   1 
ATOM   824   C  CD2   . TYR A 1 106 ? 134.165 163.653 133.801 1.00 64.81  ? 108  TYR B CD2   1 
ATOM   825   C  CE1   . TYR A 1 106 ? 134.378 164.182 131.112 1.00 62.23  ? 108  TYR B CE1   1 
ATOM   826   C  CE2   . TYR A 1 106 ? 134.838 162.775 132.978 1.00 64.55  ? 108  TYR B CE2   1 
ATOM   827   C  CZ    . TYR A 1 106 ? 134.943 163.048 131.634 1.00 61.07  ? 108  TYR B CZ    1 
ATOM   828   O  OH    . TYR A 1 106 ? 135.614 162.178 130.807 1.00 58.14  ? 108  TYR B OH    1 
ATOM   829   N  N     . THR A 1 107 ? 131.044 168.129 135.332 1.00 61.77  ? 109  THR B N     1 
ATOM   830   C  CA    . THR A 1 107 ? 130.065 168.412 136.377 1.00 62.40  ? 109  THR B CA    1 
ATOM   831   C  C     . THR A 1 107 ? 129.401 169.772 136.213 1.00 65.47  ? 109  THR B C     1 
ATOM   832   O  O     . THR A 1 107 ? 128.172 169.838 136.111 1.00 68.59  ? 109  THR B O     1 
ATOM   833   C  CB    . THR A 1 107 ? 130.731 168.307 137.754 1.00 64.86  ? 109  THR B CB    1 
ATOM   834   O  OG1   . THR A 1 107 ? 131.373 167.033 137.879 1.00 67.90  ? 109  THR B OG1   1 
ATOM   835   C  CG2   . THR A 1 107 ? 129.691 168.443 138.854 1.00 64.90  ? 109  THR B CG2   1 
ATOM   836   N  N     . GLU A 1 108 ? 130.166 170.864 136.181 1.00 68.86  ? 110  GLU B N     1 
ATOM   837   C  CA    . GLU A 1 108 ? 129.549 172.183 136.087 1.00 67.54  ? 110  GLU B CA    1 
ATOM   838   C  C     . GLU A 1 108 ? 129.323 172.603 134.641 1.00 70.73  ? 110  GLU B C     1 
ATOM   839   O  O     . GLU A 1 108 ? 128.353 173.307 134.343 1.00 77.42  ? 110  GLU B O     1 
ATOM   840   C  CB    . GLU A 1 108 ? 130.403 173.225 136.809 1.00 68.41  ? 110  GLU B CB    1 
ATOM   841   C  CG    . GLU A 1 108 ? 129.990 173.485 138.248 1.00 72.45  ? 110  GLU B CG    1 
ATOM   842   C  CD    . GLU A 1 108 ? 130.066 172.249 139.121 1.00 80.49  ? 110  GLU B CD    1 
ATOM   843   O  OE1   . GLU A 1 108 ? 130.934 171.390 138.864 1.00 82.16  ? 110  GLU B OE1   1 
ATOM   844   O  OE2   . GLU A 1 108 ? 129.256 172.135 140.065 1.00 78.84  ? 110  GLU B OE2   1 
ATOM   845   N  N     . GLY A 1 109 ? 130.207 172.191 133.733 1.00 64.59  ? 111  GLY B N     1 
ATOM   846   C  CA    . GLY A 1 109 ? 130.030 172.543 132.336 1.00 62.26  ? 111  GLY B CA    1 
ATOM   847   C  C     . GLY A 1 109 ? 128.883 171.808 131.675 1.00 66.01  ? 111  GLY B C     1 
ATOM   848   O  O     . GLY A 1 109 ? 128.289 172.314 130.718 1.00 66.57  ? 111  GLY B O     1 
ATOM   849   N  N     . ALA A 1 110 ? 128.566 170.607 132.160 1.00 63.43  ? 112  ALA B N     1 
ATOM   850   C  CA    . ALA A 1 110 ? 127.469 169.842 131.580 1.00 62.14  ? 112  ALA B CA    1 
ATOM   851   C  C     . ALA A 1 110 ? 126.130 170.530 131.809 1.00 66.44  ? 112  ALA B C     1 
ATOM   852   O  O     . ALA A 1 110 ? 125.264 170.523 130.927 1.00 68.79  ? 112  ALA B O     1 
ATOM   853   C  CB    . ALA A 1 110 ? 127.455 168.429 132.157 1.00 60.87  ? 112  ALA B CB    1 
ATOM   854   N  N     . GLU A 1 111 ? 125.941 171.126 132.986 1.00 63.11  ? 113  GLU B N     1 
ATOM   855   C  CA    . GLU A 1 111 ? 124.689 171.797 133.305 1.00 63.03  ? 113  GLU B CA    1 
ATOM   856   C  C     . GLU A 1 111 ? 124.462 173.058 132.483 1.00 63.20  ? 113  GLU B C     1 
ATOM   857   O  O     . GLU A 1 111 ? 123.318 173.513 132.385 1.00 69.10  ? 113  GLU B O     1 
ATOM   858   C  CB    . GLU A 1 111 ? 124.654 172.140 134.793 1.00 65.06  ? 113  GLU B CB    1 
ATOM   859   C  CG    . GLU A 1 111 ? 124.362 170.955 135.695 1.00 69.97  ? 113  GLU B CG    1 
ATOM   860   C  CD    . GLU A 1 111 ? 124.002 171.373 137.107 1.00 76.14  ? 113  GLU B CD    1 
ATOM   861   O  OE1   . GLU A 1 111 ? 124.231 172.550 137.455 1.00 73.78  ? 113  GLU B OE1   1 
ATOM   862   O  OE2   . GLU A 1 111 ? 123.492 170.525 137.868 1.00 76.15  ? 113  GLU B OE2   1 
ATOM   863   N  N     . LEU A 1 112 ? 125.513 173.631 131.893 1.00 56.25  ? 114  LEU B N     1 
ATOM   864   C  CA    . LEU A 1 112 ? 125.400 174.860 131.123 1.00 60.96  ? 114  LEU B CA    1 
ATOM   865   C  C     . LEU A 1 112 ? 125.538 174.653 129.623 1.00 69.50  ? 114  LEU B C     1 
ATOM   866   O  O     . LEU A 1 112 ? 125.097 175.517 128.849 1.00 75.72  ? 114  LEU B O     1 
ATOM   867   C  CB    . LEU A 1 112 ? 126.462 175.866 131.586 1.00 61.61  ? 114  LEU B CB    1 
ATOM   868   C  CG    . LEU A 1 112 ? 126.067 177.337 131.657 1.00 65.22  ? 114  LEU B CG    1 
ATOM   869   C  CD1   . LEU A 1 112 ? 124.958 177.539 132.673 1.00 64.50  ? 114  LEU B CD1   1 
ATOM   870   C  CD2   . LEU A 1 112 ? 127.276 178.178 132.011 1.00 63.55  ? 114  LEU B CD2   1 
ATOM   871   N  N     . VAL A 1 113 ? 126.126 173.532 129.199 1.00 63.79  ? 115  VAL B N     1 
ATOM   872   C  CA    . VAL A 1 113 ? 126.370 173.311 127.780 1.00 58.21  ? 115  VAL B CA    1 
ATOM   873   C  C     . VAL A 1 113 ? 125.064 173.212 127.009 1.00 62.31  ? 115  VAL B C     1 
ATOM   874   O  O     . VAL A 1 113 ? 125.018 173.541 125.820 1.00 69.82  ? 115  VAL B O     1 
ATOM   875   C  CB    . VAL A 1 113 ? 127.252 172.063 127.582 1.00 59.64  ? 115  VAL B CB    1 
ATOM   876   C  CG1   . VAL A 1 113 ? 126.454 170.790 127.809 1.00 62.53  ? 115  VAL B CG1   1 
ATOM   877   C  CG2   . VAL A 1 113 ? 127.882 172.074 126.202 1.00 63.43  ? 115  VAL B CG2   1 
ATOM   878   N  N     . ASP A 1 114 ? 123.981 172.789 127.661 1.00 60.09  ? 116  ASP B N     1 
ATOM   879   C  CA    . ASP A 1 114 ? 122.698 172.706 126.969 1.00 60.14  ? 116  ASP B CA    1 
ATOM   880   C  C     . ASP A 1 114 ? 122.210 174.088 126.545 1.00 56.43  ? 116  ASP B C     1 
ATOM   881   O  O     . ASP A 1 114 ? 121.841 174.298 125.383 1.00 67.16  ? 116  ASP B O     1 
ATOM   882   C  CB    . ASP A 1 114 ? 121.667 172.015 127.860 1.00 64.99  ? 116  ASP B CB    1 
ATOM   883   C  CG    . ASP A 1 114 ? 121.765 170.504 127.796 1.00 69.48  ? 116  ASP B CG    1 
ATOM   884   O  OD1   . ASP A 1 114 ? 122.536 169.992 126.958 1.00 66.86  ? 116  ASP B OD1   1 
ATOM   885   O  OD2   . ASP A 1 114 ? 121.072 169.827 128.584 1.00 67.50  ? 116  ASP B OD2   1 
ATOM   886   N  N     . SER A 1 115 ? 122.213 175.049 127.471 1.00 40.06  ? 117  SER B N     1 
ATOM   887   C  CA    . SER A 1 115 ? 121.793 176.402 127.121 1.00 44.70  ? 117  SER B CA    1 
ATOM   888   C  C     . SER A 1 115 ? 122.770 177.046 126.147 1.00 51.05  ? 117  SER B C     1 
ATOM   889   O  O     . SER A 1 115 ? 122.361 177.789 125.239 1.00 63.38  ? 117  SER B O     1 
ATOM   890   C  CB    . SER A 1 115 ? 121.650 177.247 128.383 1.00 49.20  ? 117  SER B CB    1 
ATOM   891   O  OG    . SER A 1 115 ? 122.789 177.115 129.213 1.00 60.65  ? 117  SER B OG    1 
ATOM   892   N  N     . VAL A 1 116 ? 124.066 176.769 126.313 1.00 42.67  ? 118  VAL B N     1 
ATOM   893   C  CA    . VAL A 1 116 ? 125.046 177.318 125.382 1.00 42.84  ? 118  VAL B CA    1 
ATOM   894   C  C     . VAL A 1 116 ? 124.771 176.819 123.971 1.00 49.53  ? 118  VAL B C     1 
ATOM   895   O  O     . VAL A 1 116 ? 124.782 177.592 123.004 1.00 60.62  ? 118  VAL B O     1 
ATOM   896   C  CB    . VAL A 1 116 ? 126.473 176.968 125.836 1.00 44.23  ? 118  VAL B CB    1 
ATOM   897   C  CG1   . VAL A 1 116 ? 127.470 177.412 124.793 1.00 50.49  ? 118  VAL B CG1   1 
ATOM   898   C  CG2   . VAL A 1 116 ? 126.771 177.611 127.173 1.00 51.33  ? 118  VAL B CG2   1 
ATOM   899   N  N     . LEU A 1 117 ? 124.502 175.520 123.833 1.00 47.86  ? 119  LEU B N     1 
ATOM   900   C  CA    . LEU A 1 117 ? 124.208 174.953 122.526 1.00 46.24  ? 119  LEU B CA    1 
ATOM   901   C  C     . LEU A 1 117 ? 122.888 175.470 121.982 1.00 48.31  ? 119  LEU B C     1 
ATOM   902   O  O     . LEU A 1 117 ? 122.724 175.590 120.768 1.00 58.40  ? 119  LEU B O     1 
ATOM   903   C  CB    . LEU A 1 117 ? 124.185 173.432 122.606 1.00 48.31  ? 119  LEU B CB    1 
ATOM   904   C  CG    . LEU A 1 117 ? 125.525 172.726 122.451 1.00 51.89  ? 119  LEU B CG    1 
ATOM   905   C  CD1   . LEU A 1 117 ? 125.326 171.263 122.753 1.00 49.98  ? 119  LEU B CD1   1 
ATOM   906   C  CD2   . LEU A 1 117 ? 126.078 172.924 121.054 1.00 53.75  ? 119  LEU B CD2   1 
ATOM   907   N  N     . ASP A 1 118 ? 121.929 175.771 122.858 1.00 44.60  ? 120  ASP B N     1 
ATOM   908   C  CA    . ASP A 1 118 ? 120.690 176.378 122.384 1.00 45.55  ? 120  ASP B CA    1 
ATOM   909   C  C     . ASP A 1 118 ? 120.949 177.734 121.745 1.00 50.29  ? 120  ASP B C     1 
ATOM   910   O  O     . ASP A 1 118 ? 120.426 178.024 120.659 1.00 56.43  ? 120  ASP B O     1 
ATOM   911   C  CB    . ASP A 1 118 ? 119.696 176.515 123.535 1.00 50.49  ? 120  ASP B CB    1 
ATOM   912   C  CG    . ASP A 1 118 ? 118.366 177.084 123.088 1.00 58.94  ? 120  ASP B CG    1 
ATOM   913   O  OD1   . ASP A 1 118 ? 117.710 176.458 122.229 1.00 60.47  ? 120  ASP B OD1   1 
ATOM   914   O  OD2   . ASP A 1 118 ? 117.976 178.156 123.595 1.00 57.40  ? 120  ASP B OD2   1 
ATOM   915   N  N     . VAL A 1 119 ? 121.767 178.568 122.388 1.00 45.39  ? 121  VAL B N     1 
ATOM   916   C  CA    . VAL A 1 119 ? 122.088 179.869 121.802 1.00 48.01  ? 121  VAL B CA    1 
ATOM   917   C  C     . VAL A 1 119 ? 122.876 179.696 120.505 1.00 47.33  ? 121  VAL B C     1 
ATOM   918   O  O     . VAL A 1 119 ? 122.629 180.397 119.513 1.00 52.93  ? 121  VAL B O     1 
ATOM   919   C  CB    . VAL A 1 119 ? 122.841 180.746 122.817 1.00 51.15  ? 121  VAL B CB    1 
ATOM   920   C  CG1   . VAL A 1 119 ? 123.161 182.097 122.208 1.00 53.76  ? 121  VAL B CG1   1 
ATOM   921   C  CG2   . VAL A 1 119 ? 122.018 180.912 124.077 1.00 50.33  ? 121  VAL B CG2   1 
ATOM   922   N  N     . VAL A 1 120 ? 123.829 178.758 120.488 1.00 45.40  ? 122  VAL B N     1 
ATOM   923   C  CA    . VAL A 1 120 ? 124.600 178.493 119.273 1.00 39.21  ? 122  VAL B CA    1 
ATOM   924   C  C     . VAL A 1 120 ? 123.679 178.064 118.141 1.00 43.29  ? 122  VAL B C     1 
ATOM   925   O  O     . VAL A 1 120 ? 123.818 178.518 117.000 1.00 56.85  ? 122  VAL B O     1 
ATOM   926   C  CB    . VAL A 1 120 ? 125.681 177.429 119.539 1.00 42.48  ? 122  VAL B CB    1 
ATOM   927   C  CG1   . VAL A 1 120 ? 126.355 177.027 118.243 1.00 45.41  ? 122  VAL B CG1   1 
ATOM   928   C  CG2   . VAL A 1 120 ? 126.708 177.930 120.530 1.00 49.02  ? 122  VAL B CG2   1 
ATOM   929   N  N     . ARG A 1 121 ? 122.735 177.171 118.436 1.00 47.72  ? 123  ARG B N     1 
ATOM   930   C  CA    . ARG A 1 121 ? 121.813 176.668 117.428 1.00 50.55  ? 123  ARG B CA    1 
ATOM   931   C  C     . ARG A 1 121 ? 120.930 177.778 116.884 1.00 50.87  ? 123  ARG B C     1 
ATOM   932   O  O     . ARG A 1 121 ? 120.700 177.855 115.673 1.00 56.24  ? 123  ARG B O     1 
ATOM   933   C  CB    . ARG A 1 121 ? 120.966 175.549 118.028 1.00 52.15  ? 123  ARG B CB    1 
ATOM   934   C  CG    . ARG A 1 121 ? 120.556 174.475 117.049 1.00 54.33  ? 123  ARG B CG    1 
ATOM   935   C  CD    . ARG A 1 121 ? 119.675 173.448 117.727 1.00 55.07  ? 123  ARG B CD    1 
ATOM   936   N  NE    . ARG A 1 121 ? 120.173 173.110 119.055 1.00 54.85  ? 123  ARG B NE    1 
ATOM   937   C  CZ    . ARG A 1 121 ? 121.094 172.189 119.296 1.00 55.13  ? 123  ARG B CZ    1 
ATOM   938   N  NH1   . ARG A 1 121 ? 121.656 171.502 118.316 1.00 53.37  ? 123  ARG B NH1   1 
ATOM   939   N  NH2   . ARG A 1 121 ? 121.463 171.953 120.551 1.00 55.36  ? 123  ARG B NH2   1 
ATOM   940   N  N     . LYS A 1 122 ? 120.424 178.648 117.761 1.00 51.81  ? 124  LYS B N     1 
ATOM   941   C  CA    . LYS A 1 122 ? 119.622 179.771 117.288 1.00 49.78  ? 124  LYS B CA    1 
ATOM   942   C  C     . LYS A 1 122 ? 120.429 180.677 116.369 1.00 55.26  ? 124  LYS B C     1 
ATOM   943   O  O     . LYS A 1 122 ? 119.964 181.051 115.282 1.00 63.35  ? 124  LYS B O     1 
ATOM   944   C  CB    . LYS A 1 122 ? 119.079 180.567 118.472 1.00 52.84  ? 124  LYS B CB    1 
ATOM   945   C  CG    . LYS A 1 122 ? 117.883 181.437 118.134 1.00 54.33  ? 124  LYS B CG    1 
ATOM   946   C  CD    . LYS A 1 122 ? 117.287 182.058 119.385 1.00 61.98  ? 124  LYS B CD    1 
ATOM   947   C  CE    . LYS A 1 122 ? 115.777 182.193 119.269 1.00 59.41  ? 124  LYS B CE    1 
ATOM   948   N  NZ    . LYS A 1 122 ? 115.375 182.902 118.023 1.00 58.99  ? 124  LYS B NZ    1 
ATOM   949   N  N     . GLU A 1 123 ? 121.651 181.027 116.778 1.00 53.49  ? 125  GLU B N     1 
ATOM   950   C  CA    . GLU A 1 123 ? 122.463 181.923 115.960 1.00 48.97  ? 125  GLU B CA    1 
ATOM   951   C  C     . GLU A 1 123 ? 122.812 181.286 114.621 1.00 55.93  ? 125  GLU B C     1 
ATOM   952   O  O     . GLU A 1 123 ? 122.792 181.956 113.583 1.00 60.37  ? 125  GLU B O     1 
ATOM   953   C  CB    . GLU A 1 123 ? 123.728 182.323 116.716 1.00 54.60  ? 125  GLU B CB    1 
ATOM   954   C  CG    . GLU A 1 123 ? 123.467 183.152 117.962 1.00 63.42  ? 125  GLU B CG    1 
ATOM   955   C  CD    . GLU A 1 123 ? 123.317 184.633 117.668 1.00 66.43  ? 125  GLU B CD    1 
ATOM   956   O  OE1   . GLU A 1 123 ? 123.040 184.992 116.505 1.00 64.38  ? 125  GLU B OE1   1 
ATOM   957   O  OE2   . GLU A 1 123 ? 123.474 185.441 118.606 1.00 63.37  ? 125  GLU B OE2   1 
ATOM   958   N  N     . SER A 1 124 ? 123.136 179.991 114.625 1.00 56.65  ? 126  SER B N     1 
ATOM   959   C  CA    . SER A 1 124 ? 123.455 179.296 113.383 1.00 57.46  ? 126  SER B CA    1 
ATOM   960   C  C     . SER A 1 124 ? 122.243 179.207 112.464 1.00 58.25  ? 126  SER B C     1 
ATOM   961   O  O     . SER A 1 124 ? 122.371 179.362 111.244 1.00 62.25  ? 126  SER B O     1 
ATOM   962   C  CB    . SER A 1 124 ? 123.998 177.903 113.689 1.00 58.18  ? 126  SER B CB    1 
ATOM   963   O  OG    . SER A 1 124 ? 125.197 177.980 114.437 1.00 63.79  ? 126  SER B OG    1 
ATOM   964   N  N     . GLU A 1 125 ? 121.059 178.950 113.026 1.00 60.07  ? 127  GLU B N     1 
ATOM   965   C  CA    . GLU A 1 125 ? 119.854 178.873 112.210 1.00 59.14  ? 127  GLU B CA    1 
ATOM   966   C  C     . GLU A 1 125 ? 119.499 180.227 111.613 1.00 58.69  ? 127  GLU B C     1 
ATOM   967   O  O     . GLU A 1 125 ? 118.981 180.294 110.493 1.00 61.69  ? 127  GLU B O     1 
ATOM   968   C  CB    . GLU A 1 125 ? 118.691 178.332 113.042 1.00 63.28  ? 127  GLU B CB    1 
ATOM   969   C  CG    . GLU A 1 125 ? 117.397 178.144 112.267 1.00 66.90  ? 127  GLU B CG    1 
ATOM   970   C  CD    . GLU A 1 125 ? 117.474 177.008 111.265 1.00 71.69  ? 127  GLU B CD    1 
ATOM   971   O  OE1   . GLU A 1 125 ? 118.320 176.107 111.446 1.00 66.27  ? 127  GLU B OE1   1 
ATOM   972   O  OE2   . GLU A 1 125 ? 116.688 177.016 110.294 1.00 72.06  ? 127  GLU B OE2   1 
ATOM   973   N  N     . SER A 1 126 ? 119.770 181.314 112.336 1.00 62.75  ? 128  SER B N     1 
ATOM   974   C  CA    . SER A 1 126 ? 119.522 182.638 111.780 1.00 67.65  ? 128  SER B CA    1 
ATOM   975   C  C     . SER A 1 126 ? 120.492 183.001 110.661 1.00 68.30  ? 128  SER B C     1 
ATOM   976   O  O     . SER A 1 126 ? 120.285 184.021 109.995 1.00 63.69  ? 128  SER B O     1 
ATOM   977   C  CB    . SER A 1 126 ? 119.593 183.694 112.883 1.00 69.85  ? 128  SER B CB    1 
ATOM   978   O  OG    . SER A 1 126 ? 119.289 184.981 112.375 1.00 72.95  ? 128  SER B OG    1 
ATOM   979   N  N     . CYS A 1 127 ? 121.535 182.206 110.442 1.00 74.77  ? 129  CYS B N     1 
ATOM   980   C  CA    . CYS A 1 127 ? 122.537 182.492 109.426 1.00 69.52  ? 129  CYS B CA    1 
ATOM   981   C  C     . CYS A 1 127 ? 122.102 181.969 108.062 1.00 68.35  ? 129  CYS B C     1 
ATOM   982   O  O     . CYS A 1 127 ? 121.397 180.963 107.952 1.00 67.69  ? 129  CYS B O     1 
ATOM   983   C  CB    . CYS A 1 127 ? 123.882 181.875 109.809 1.00 69.92  ? 129  CYS B CB    1 
ATOM   984   S  SG    . CYS A 1 127 ? 124.734 182.715 111.162 1.00 86.36  ? 129  CYS B SG    1 
ATOM   985   N  N     . ASP A 1 128 ? 122.540 182.670 107.015 1.00 75.10  ? 130  ASP B N     1 
ATOM   986   C  CA    . ASP A 1 128 ? 122.195 182.289 105.650 1.00 74.11  ? 130  ASP B CA    1 
ATOM   987   C  C     . ASP A 1 128 ? 123.031 181.104 105.179 1.00 73.79  ? 130  ASP B C     1 
ATOM   988   O  O     . ASP A 1 128 ? 122.491 180.058 104.805 1.00 74.67  ? 130  ASP B O     1 
ATOM   989   C  CB    . ASP A 1 128 ? 122.379 183.485 104.713 1.00 72.72  ? 130  ASP B CB    1 
ATOM   990   C  CG    . ASP A 1 128 ? 121.792 183.246 103.338 1.00 79.83  ? 130  ASP B CG    1 
ATOM   991   O  OD1   . ASP A 1 128 ? 121.044 182.260 103.170 1.00 82.17  ? 130  ASP B OD1   1 
ATOM   992   O  OD2   . ASP A 1 128 ? 122.077 184.047 102.423 1.00 78.49  ? 130  ASP B OD2   1 
ATOM   993   N  N     . CYS A 1 129 ? 124.354 181.254 105.187 1.00 65.33  ? 131  CYS B N     1 
ATOM   994   C  CA    . CYS A 1 129 ? 125.283 180.197 104.789 1.00 63.16  ? 131  CYS B CA    1 
ATOM   995   C  C     . CYS A 1 129 ? 126.419 180.179 105.805 1.00 65.13  ? 131  CYS B C     1 
ATOM   996   O  O     . CYS A 1 129 ? 127.346 180.987 105.724 1.00 73.23  ? 131  CYS B O     1 
ATOM   997   C  CB    . CYS A 1 129 ? 125.795 180.420 103.376 1.00 68.23  ? 131  CYS B CB    1 
ATOM   998   S  SG    . CYS A 1 129 ? 126.996 179.194 102.829 1.00 83.95  ? 131  CYS B SG    1 
ATOM   999   N  N     . LEU A 1 130 ? 126.342 179.256 106.758 1.00 64.05  ? 132  LEU B N     1 
ATOM   1000  C  CA    . LEU A 1 130 ? 127.335 179.181 107.822 1.00 64.93  ? 132  LEU B CA    1 
ATOM   1001  C  C     . LEU A 1 130 ? 128.681 178.750 107.255 1.00 65.12  ? 132  LEU B C     1 
ATOM   1002  O  O     . LEU A 1 130 ? 128.758 177.801 106.468 1.00 68.26  ? 132  LEU B O     1 
ATOM   1003  C  CB    . LEU A 1 130 ? 126.871 178.211 108.904 1.00 65.04  ? 132  LEU B CB    1 
ATOM   1004  C  CG    . LEU A 1 130 ? 127.515 178.368 110.280 1.00 65.03  ? 132  LEU B CG    1 
ATOM   1005  C  CD1   . LEU A 1 130 ? 127.217 179.741 110.848 1.00 65.42  ? 132  LEU B CD1   1 
ATOM   1006  C  CD2   . LEU A 1 130 ? 127.025 177.282 111.216 1.00 66.42  ? 132  LEU B CD2   1 
ATOM   1007  N  N     . GLN A 1 131 ? 129.741 179.447 107.658 1.00 57.39  ? 133  GLN B N     1 
ATOM   1008  C  CA    . GLN A 1 131 ? 131.098 179.146 107.225 1.00 57.02  ? 133  GLN B CA    1 
ATOM   1009  C  C     . GLN A 1 131 ? 131.886 178.376 108.275 1.00 59.75  ? 133  GLN B C     1 
ATOM   1010  O  O     . GLN A 1 131 ? 132.532 177.376 107.953 1.00 66.98  ? 133  GLN B O     1 
ATOM   1011  C  CB    . GLN A 1 131 ? 131.834 180.442 106.871 1.00 57.88  ? 133  GLN B CB    1 
ATOM   1012  C  CG    . GLN A 1 131 ? 133.334 180.285 106.715 1.00 59.38  ? 133  GLN B CG    1 
ATOM   1013  C  CD    . GLN A 1 131 ? 133.709 179.295 105.638 1.00 66.45  ? 133  GLN B CD    1 
ATOM   1014  O  OE1   . GLN A 1 131 ? 134.340 178.275 105.909 1.00 70.21  ? 133  GLN B OE1   1 
ATOM   1015  N  NE2   . GLN A 1 131 ? 133.322 179.591 104.403 1.00 67.42  ? 133  GLN B NE2   1 
ATOM   1016  N  N     . GLY A 1 132 ? 131.842 178.814 109.526 1.00 55.25  ? 134  GLY B N     1 
ATOM   1017  C  CA    . GLY A 1 132 ? 132.605 178.127 110.549 1.00 57.90  ? 134  GLY B CA    1 
ATOM   1018  C  C     . GLY A 1 132 ? 132.336 178.695 111.923 1.00 55.56  ? 134  GLY B C     1 
ATOM   1019  O  O     . GLY A 1 132 ? 131.504 179.587 112.104 1.00 56.90  ? 134  GLY B O     1 
ATOM   1020  N  N     . PHE A 1 133 ? 133.064 178.154 112.896 1.00 51.98  ? 135  PHE B N     1 
ATOM   1021  C  CA    . PHE A 1 133 ? 132.943 178.541 114.292 1.00 43.29  ? 135  PHE B CA    1 
ATOM   1022  C  C     . PHE A 1 133 ? 134.276 179.072 114.796 1.00 46.42  ? 135  PHE B C     1 
ATOM   1023  O  O     . PHE A 1 133 ? 135.343 178.606 114.389 1.00 65.69  ? 135  PHE B O     1 
ATOM   1024  C  CB    . PHE A 1 133 ? 132.498 177.364 115.162 1.00 44.45  ? 135  PHE B CB    1 
ATOM   1025  C  CG    . PHE A 1 133 ? 131.161 176.806 114.787 1.00 47.63  ? 135  PHE B CG    1 
ATOM   1026  C  CD1   . PHE A 1 133 ? 131.055 175.820 113.826 1.00 53.78  ? 135  PHE B CD1   1 
ATOM   1027  C  CD2   . PHE A 1 133 ? 130.010 177.268 115.391 1.00 48.20  ? 135  PHE B CD2   1 
ATOM   1028  C  CE1   . PHE A 1 133 ? 129.829 175.307 113.477 1.00 56.62  ? 135  PHE B CE1   1 
ATOM   1029  C  CE2   . PHE A 1 133 ? 128.781 176.757 115.044 1.00 47.52  ? 135  PHE B CE2   1 
ATOM   1030  C  CZ    . PHE A 1 133 ? 128.690 175.777 114.088 1.00 54.66  ? 135  PHE B CZ    1 
ATOM   1031  N  N     . GLN A 1 134 ? 134.201 180.052 115.689 1.00 44.11  ? 136  GLN B N     1 
ATOM   1032  C  CA    . GLN A 1 134 ? 135.375 180.728 116.224 1.00 43.44  ? 136  GLN B CA    1 
ATOM   1033  C  C     . GLN A 1 134 ? 135.307 180.680 117.741 1.00 51.18  ? 136  GLN B C     1 
ATOM   1034  O  O     . GLN A 1 134 ? 134.310 181.107 118.330 1.00 58.81  ? 136  GLN B O     1 
ATOM   1035  C  CB    . GLN A 1 134 ? 135.435 182.173 115.731 1.00 48.73  ? 136  GLN B CB    1 
ATOM   1036  C  CG    . GLN A 1 134 ? 136.817 182.772 115.706 1.00 51.60  ? 136  GLN B CG    1 
ATOM   1037  C  CD    . GLN A 1 134 ? 136.835 184.127 115.039 1.00 61.28  ? 136  GLN B CD    1 
ATOM   1038  O  OE1   . GLN A 1 134 ? 135.786 184.710 114.770 1.00 60.78  ? 136  GLN B OE1   1 
ATOM   1039  N  NE2   . GLN A 1 134 ? 138.029 184.637 114.762 1.00 61.97  ? 136  GLN B NE2   1 
ATOM   1040  N  N     . LEU A 1 135 ? 136.360 180.168 118.374 1.00 50.81  ? 137  LEU B N     1 
ATOM   1041  C  CA    . LEU A 1 135 ? 136.394 180.043 119.823 1.00 49.10  ? 137  LEU B CA    1 
ATOM   1042  C  C     . LEU A 1 135 ? 137.673 180.653 120.374 1.00 51.87  ? 137  LEU B C     1 
ATOM   1043  O  O     . LEU A 1 135 ? 138.757 180.450 119.821 1.00 67.70  ? 137  LEU B O     1 
ATOM   1044  C  CB    . LEU A 1 135 ? 136.287 178.581 120.255 1.00 46.58  ? 137  LEU B CB    1 
ATOM   1045  C  CG    . LEU A 1 135 ? 136.409 178.317 121.755 1.00 53.41  ? 137  LEU B CG    1 
ATOM   1046  C  CD1   . LEU A 1 135 ? 135.351 179.077 122.524 1.00 54.25  ? 137  LEU B CD1   1 
ATOM   1047  C  CD2   . LEU A 1 135 ? 136.299 176.843 122.051 1.00 55.63  ? 137  LEU B CD2   1 
ATOM   1048  N  N     . THR A 1 136 ? 137.537 181.403 121.465 1.00 37.75  ? 138  THR B N     1 
ATOM   1049  C  CA    . THR A 1 136 ? 138.668 181.934 122.214 1.00 44.06  ? 138  THR B CA    1 
ATOM   1050  C  C     . THR A 1 136 ? 138.636 181.340 123.614 1.00 48.21  ? 138  THR B C     1 
ATOM   1051  O  O     . THR A 1 136 ? 137.629 181.465 124.318 1.00 51.53  ? 138  THR B O     1 
ATOM   1052  C  CB    . THR A 1 136 ? 138.624 183.460 122.279 1.00 48.84  ? 138  THR B CB    1 
ATOM   1053  O  OG1   . THR A 1 136 ? 138.320 183.988 120.984 1.00 42.28  ? 138  THR B OG1   1 
ATOM   1054  C  CG2   . THR A 1 136 ? 139.968 184.006 122.730 1.00 56.90  ? 138  THR B CG2   1 
ATOM   1055  N  N     . HIS A 1 137 ? 139.729 180.694 124.016 1.00 50.54  ? 139  HIS B N     1 
ATOM   1056  C  CA    . HIS A 1 137 ? 139.834 180.091 125.337 1.00 49.74  ? 139  HIS B CA    1 
ATOM   1057  C  C     . HIS A 1 137 ? 141.301 179.957 125.720 1.00 54.82  ? 139  HIS B C     1 
ATOM   1058  O  O     . HIS A 1 137 ? 142.205 180.261 124.937 1.00 60.53  ? 139  HIS B O     1 
ATOM   1059  C  CB    . HIS A 1 137 ? 139.151 178.721 125.386 1.00 51.28  ? 139  HIS B CB    1 
ATOM   1060  C  CG    . HIS A 1 137 ? 139.706 177.734 124.411 1.00 51.34  ? 139  HIS B CG    1 
ATOM   1061  N  ND1   . HIS A 1 137 ? 139.401 177.759 123.069 1.00 55.08  ? 139  HIS B ND1   1 
ATOM   1062  C  CD2   . HIS A 1 137 ? 140.543 176.686 124.587 1.00 55.59  ? 139  HIS B CD2   1 
ATOM   1063  C  CE1   . HIS A 1 137 ? 140.030 176.771 122.458 1.00 56.54  ? 139  HIS B CE1   1 
ATOM   1064  N  NE2   . HIS A 1 137 ? 140.731 176.105 123.357 1.00 58.46  ? 139  HIS B NE2   1 
ATOM   1065  N  N     . SER A 1 138 ? 141.534 179.494 126.947 1.00 57.38  ? 140  SER B N     1 
ATOM   1066  C  CA    . SER A 1 138 ? 142.877 179.241 127.458 1.00 56.25  ? 140  SER B CA    1 
ATOM   1067  C  C     . SER A 1 138 ? 142.955 177.780 127.873 1.00 59.07  ? 140  SER B C     1 
ATOM   1068  O  O     . SER A 1 138 ? 142.043 177.273 128.533 1.00 66.90  ? 140  SER B O     1 
ATOM   1069  C  CB    . SER A 1 138 ? 143.207 180.157 128.634 1.00 57.92  ? 140  SER B CB    1 
ATOM   1070  O  OG    . SER A 1 138 ? 144.547 179.975 129.053 1.00 58.95  ? 140  SER B OG    1 
ATOM   1071  N  N     . LEU A 1 139 ? 144.039 177.105 127.492 1.00 49.21  ? 141  LEU B N     1 
ATOM   1072  C  CA    . LEU A 1 139 ? 144.193 175.696 127.830 1.00 54.39  ? 141  LEU B CA    1 
ATOM   1073  C  C     . LEU A 1 139 ? 144.629 175.483 129.274 1.00 62.55  ? 141  LEU B C     1 
ATOM   1074  O  O     . LEU A 1 139 ? 144.516 174.363 129.782 1.00 68.79  ? 141  LEU B O     1 
ATOM   1075  C  CB    . LEU A 1 139 ? 145.199 175.040 126.886 1.00 58.51  ? 141  LEU B CB    1 
ATOM   1076  C  CG    . LEU A 1 139 ? 144.953 175.220 125.390 1.00 61.07  ? 141  LEU B CG    1 
ATOM   1077  C  CD1   . LEU A 1 139 ? 145.910 174.363 124.582 1.00 58.35  ? 141  LEU B CD1   1 
ATOM   1078  C  CD2   . LEU A 1 139 ? 143.517 174.877 125.050 1.00 60.95  ? 141  LEU B CD2   1 
ATOM   1079  N  N     . GLY A 1 140 ? 145.122 176.520 129.943 1.00 59.71  ? 142  GLY B N     1 
ATOM   1080  C  CA    . GLY A 1 140 ? 145.648 176.389 131.285 1.00 58.20  ? 142  GLY B CA    1 
ATOM   1081  C  C     . GLY A 1 140 ? 144.661 176.534 132.417 1.00 60.37  ? 142  GLY B C     1 
ATOM   1082  O  O     . GLY A 1 140 ? 145.062 176.449 133.580 1.00 66.25  ? 142  GLY B O     1 
ATOM   1083  N  N     . GLY A 1 141 ? 143.377 176.742 132.127 1.00 52.91  ? 143  GLY B N     1 
ATOM   1084  C  CA    . GLY A 1 141 ? 142.379 176.966 133.144 1.00 55.01  ? 143  GLY B CA    1 
ATOM   1085  C  C     . GLY A 1 141 ? 141.284 175.912 133.149 1.00 55.04  ? 143  GLY B C     1 
ATOM   1086  O  O     . GLY A 1 141 ? 141.311 174.927 132.418 1.00 58.20  ? 143  GLY B O     1 
ATOM   1087  N  N     . GLY A 1 142 ? 140.301 176.150 134.013 1.00 59.54  ? 144  GLY B N     1 
ATOM   1088  C  CA    . GLY A 1 142 ? 139.201 175.222 134.170 1.00 58.59  ? 144  GLY B CA    1 
ATOM   1089  C  C     . GLY A 1 142 ? 138.036 175.445 133.229 1.00 58.30  ? 144  GLY B C     1 
ATOM   1090  O  O     . GLY A 1 142 ? 137.690 174.550 132.452 1.00 60.51  ? 144  GLY B O     1 
ATOM   1091  N  N     . THR A 1 143 ? 137.419 176.627 133.284 1.00 58.51  ? 145  THR B N     1 
ATOM   1092  C  CA    . THR A 1 143 ? 136.241 176.872 132.457 1.00 52.14  ? 145  THR B CA    1 
ATOM   1093  C  C     . THR A 1 143 ? 136.612 176.909 130.984 1.00 53.51  ? 145  THR B C     1 
ATOM   1094  O  O     . THR A 1 143 ? 135.964 176.263 130.155 1.00 64.26  ? 145  THR B O     1 
ATOM   1095  C  CB    . THR A 1 143 ? 135.553 178.175 132.861 1.00 59.34  ? 145  THR B CB    1 
ATOM   1096  O  OG1   . THR A 1 143 ? 136.298 179.285 132.356 1.00 67.74  ? 145  THR B OG1   1 
ATOM   1097  C  CG2   . THR A 1 143 ? 135.457 178.290 134.372 1.00 62.08  ? 145  THR B CG2   1 
ATOM   1098  N  N     . GLY A 1 144 ? 137.668 177.641 130.645 1.00 54.88  ? 146  GLY B N     1 
ATOM   1099  C  CA    . GLY A 1 144 ? 138.118 177.732 129.274 1.00 54.88  ? 146  GLY B CA    1 
ATOM   1100  C  C     . GLY A 1 144 ? 138.391 176.381 128.657 1.00 59.70  ? 146  GLY B C     1 
ATOM   1101  O  O     . GLY A 1 144 ? 137.641 175.944 127.783 1.00 62.86  ? 146  GLY B O     1 
ATOM   1102  N  N     . SER A 1 145 ? 139.424 175.687 129.135 1.00 59.57  ? 147  SER B N     1 
ATOM   1103  C  CA    . SER A 1 145 ? 139.816 174.420 128.526 1.00 55.43  ? 147  SER B CA    1 
ATOM   1104  C  C     . SER A 1 145 ? 138.653 173.437 128.491 1.00 55.02  ? 147  SER B C     1 
ATOM   1105  O  O     . SER A 1 145 ? 138.208 173.025 127.414 1.00 63.05  ? 147  SER B O     1 
ATOM   1106  C  CB    . SER A 1 145 ? 141.001 173.822 129.280 1.00 57.90  ? 147  SER B CB    1 
ATOM   1107  O  OG    . SER A 1 145 ? 140.666 173.575 130.633 1.00 64.24  ? 147  SER B OG    1 
ATOM   1108  N  N     . GLY A 1 146 ? 138.129 173.074 129.657 1.00 46.99  ? 148  GLY B N     1 
ATOM   1109  C  CA    . GLY A 1 146 ? 137.084 172.073 129.738 1.00 51.79  ? 148  GLY B CA    1 
ATOM   1110  C  C     . GLY A 1 146 ? 135.793 172.420 129.025 1.00 56.09  ? 148  GLY B C     1 
ATOM   1111  O  O     . GLY A 1 146 ? 135.299 171.628 128.213 1.00 60.18  ? 148  GLY B O     1 
ATOM   1112  N  N     . MET A 1 147 ? 135.227 173.593 129.320 1.00 61.15  ? 149  MET B N     1 
ATOM   1113  C  CA    . MET A 1 147 ? 133.955 173.958 128.712 1.00 55.97  ? 149  MET B CA    1 
ATOM   1114  C  C     . MET A 1 147 ? 134.096 174.181 127.212 1.00 65.98  ? 149  MET B C     1 
ATOM   1115  O  O     . MET A 1 147 ? 133.230 173.756 126.440 1.00 75.09  ? 149  MET B O     1 
ATOM   1116  C  CB    . MET A 1 147 ? 133.373 175.196 129.387 1.00 59.44  ? 149  MET B CB    1 
ATOM   1117  C  CG    . MET A 1 147 ? 131.892 175.383 129.111 1.00 66.40  ? 149  MET B CG    1 
ATOM   1118  S  SD    . MET A 1 147 ? 131.000 176.161 130.462 1.00 93.81  ? 149  MET B SD    1 
ATOM   1119  C  CE    . MET A 1 147 ? 131.940 177.671 130.655 1.00 72.45  ? 149  MET B CE    1 
ATOM   1120  N  N     . GLY A 1 148 ? 135.169 174.846 126.772 1.00 57.66  ? 150  GLY B N     1 
ATOM   1121  C  CA    . GLY A 1 148 ? 135.376 175.015 125.348 1.00 56.29  ? 150  GLY B CA    1 
ATOM   1122  C  C     . GLY A 1 148 ? 135.569 173.696 124.632 1.00 57.76  ? 150  GLY B C     1 
ATOM   1123  O  O     . GLY A 1 148 ? 135.077 173.512 123.522 1.00 66.30  ? 150  GLY B O     1 
ATOM   1124  N  N     . THR A 1 149 ? 136.278 172.757 125.259 1.00 50.02  ? 151  THR B N     1 
ATOM   1125  C  CA    . THR A 1 149 ? 136.455 171.441 124.658 1.00 49.66  ? 151  THR B CA    1 
ATOM   1126  C  C     . THR A 1 149 ? 135.133 170.693 124.540 1.00 57.59  ? 151  THR B C     1 
ATOM   1127  O  O     . THR A 1 149 ? 134.837 170.100 123.494 1.00 64.27  ? 151  THR B O     1 
ATOM   1128  C  CB    . THR A 1 149 ? 137.461 170.643 125.483 1.00 58.13  ? 151  THR B CB    1 
ATOM   1129  O  OG1   . THR A 1 149 ? 138.789 171.079 125.168 1.00 61.11  ? 151  THR B OG1   1 
ATOM   1130  C  CG2   . THR A 1 149 ? 137.324 169.165 125.216 1.00 59.88  ? 151  THR B CG2   1 
ATOM   1131  N  N     . LEU A 1 150 ? 134.322 170.707 125.600 1.00 59.18  ? 152  LEU B N     1 
ATOM   1132  C  CA    . LEU A 1 150 ? 133.021 170.046 125.538 1.00 54.54  ? 152  LEU B CA    1 
ATOM   1133  C  C     . LEU A 1 150 ? 132.134 170.678 124.473 1.00 58.11  ? 152  LEU B C     1 
ATOM   1134  O  O     . LEU A 1 150 ? 131.471 169.973 123.698 1.00 62.06  ? 152  LEU B O     1 
ATOM   1135  C  CB    . LEU A 1 150 ? 132.343 170.105 126.904 1.00 51.39  ? 152  LEU B CB    1 
ATOM   1136  C  CG    . LEU A 1 150 ? 130.963 169.466 127.021 1.00 52.43  ? 152  LEU B CG    1 
ATOM   1137  C  CD1   . LEU A 1 150 ? 131.043 167.980 126.744 1.00 60.00  ? 152  LEU B CD1   1 
ATOM   1138  C  CD2   . LEU A 1 150 ? 130.384 169.728 128.393 1.00 56.58  ? 152  LEU B CD2   1 
ATOM   1139  N  N     . LEU A 1 151 ? 132.122 172.010 124.411 1.00 58.04  ? 153  LEU B N     1 
ATOM   1140  C  CA    . LEU A 1 151 ? 131.322 172.708 123.415 1.00 55.23  ? 153  LEU B CA    1 
ATOM   1141  C  C     . LEU A 1 151 ? 131.822 172.422 122.006 1.00 62.02  ? 153  LEU B C     1 
ATOM   1142  O  O     . LEU A 1 151 ? 131.021 172.274 121.077 1.00 65.43  ? 153  LEU B O     1 
ATOM   1143  C  CB    . LEU A 1 151 ? 131.339 174.204 123.709 1.00 47.70  ? 153  LEU B CB    1 
ATOM   1144  C  CG    . LEU A 1 151 ? 130.470 175.118 122.859 1.00 56.25  ? 153  LEU B CG    1 
ATOM   1145  C  CD1   . LEU A 1 151 ? 129.025 174.663 122.893 1.00 63.18  ? 153  LEU B CD1   1 
ATOM   1146  C  CD2   . LEU A 1 151 ? 130.601 176.528 123.379 1.00 58.33  ? 153  LEU B CD2   1 
ATOM   1147  N  N     . ILE A 1 152 ? 133.142 172.341 121.827 1.00 59.63  ? 154  ILE B N     1 
ATOM   1148  C  CA    . ILE A 1 152 ? 133.710 172.007 120.527 1.00 53.88  ? 154  ILE B CA    1 
ATOM   1149  C  C     . ILE A 1 152 ? 133.273 170.616 120.104 1.00 57.04  ? 154  ILE B C     1 
ATOM   1150  O  O     . ILE A 1 152 ? 132.897 170.396 118.949 1.00 65.67  ? 154  ILE B O     1 
ATOM   1151  C  CB    . ILE A 1 152 ? 135.244 172.123 120.570 1.00 56.14  ? 154  ILE B CB    1 
ATOM   1152  C  CG1   . ILE A 1 152 ? 135.690 173.568 120.401 1.00 56.39  ? 154  ILE B CG1   1 
ATOM   1153  C  CG2   . ILE A 1 152 ? 135.876 171.279 119.495 1.00 55.88  ? 154  ILE B CG2   1 
ATOM   1154  C  CD1   . ILE A 1 152 ? 137.168 173.740 120.612 1.00 58.23  ? 154  ILE B CD1   1 
ATOM   1155  N  N     . SER A 1 153 ? 133.323 169.655 121.025 1.00 51.78  ? 155  SER B N     1 
ATOM   1156  C  CA    . SER A 1 153 ? 132.902 168.299 120.691 1.00 49.11  ? 155  SER B CA    1 
ATOM   1157  C  C     . SER A 1 153 ? 131.433 168.269 120.288 1.00 49.25  ? 155  SER B C     1 
ATOM   1158  O  O     . SER A 1 153 ? 131.060 167.641 119.288 1.00 57.27  ? 155  SER B O     1 
ATOM   1159  C  CB    . SER A 1 153 ? 133.160 167.368 121.874 1.00 55.39  ? 155  SER B CB    1 
ATOM   1160  O  OG    . SER A 1 153 ? 134.539 167.323 122.195 1.00 61.73  ? 155  SER B OG    1 
ATOM   1161  N  N     . LYS A 1 154 ? 130.586 168.960 121.052 1.00 46.82  ? 156  LYS B N     1 
ATOM   1162  C  CA    . LYS A 1 154 ? 129.158 168.961 120.751 1.00 48.04  ? 156  LYS B CA    1 
ATOM   1163  C  C     . LYS A 1 154 ? 128.867 169.630 119.410 1.00 51.35  ? 156  LYS B C     1 
ATOM   1164  O  O     . LYS A 1 154 ? 128.070 169.122 118.613 1.00 55.96  ? 156  LYS B O     1 
ATOM   1165  C  CB    . LYS A 1 154 ? 128.394 169.651 121.876 1.00 50.77  ? 156  LYS B CB    1 
ATOM   1166  C  CG    . LYS A 1 154 ? 127.704 168.697 122.831 1.00 51.06  ? 156  LYS B CG    1 
ATOM   1167  C  CD    . LYS A 1 154 ? 128.698 167.863 123.608 1.00 52.31  ? 156  LYS B CD    1 
ATOM   1168  C  CE    . LYS A 1 154 ? 127.979 166.914 124.545 1.00 53.70  ? 156  LYS B CE    1 
ATOM   1169  N  NZ    . LYS A 1 154 ? 127.050 167.642 125.449 1.00 53.44  ? 156  LYS B NZ    1 
ATOM   1170  N  N     . ILE A 1 155 ? 129.511 170.766 119.138 1.00 53.16  ? 157  ILE B N     1 
ATOM   1171  C  CA    . ILE A 1 155 ? 129.293 171.462 117.875 1.00 54.94  ? 157  ILE B CA    1 
ATOM   1172  C  C     . ILE A 1 155 ? 129.841 170.654 116.706 1.00 58.57  ? 157  ILE B C     1 
ATOM   1173  O  O     . ILE A 1 155 ? 129.230 170.615 115.630 1.00 63.41  ? 157  ILE B O     1 
ATOM   1174  C  CB    . ILE A 1 155 ? 129.915 172.868 117.938 1.00 53.79  ? 157  ILE B CB    1 
ATOM   1175  C  CG1   . ILE A 1 155 ? 129.157 173.734 118.941 1.00 55.17  ? 157  ILE B CG1   1 
ATOM   1176  C  CG2   . ILE A 1 155 ? 129.908 173.521 116.573 1.00 56.78  ? 157  ILE B CG2   1 
ATOM   1177  C  CD1   . ILE A 1 155 ? 129.681 175.139 119.041 1.00 55.93  ? 157  ILE B CD1   1 
ATOM   1178  N  N     . ARG A 1 156 ? 130.982 169.989 116.890 1.00 60.96  ? 158  ARG B N     1 
ATOM   1179  C  CA    . ARG A 1 156 ? 131.545 169.159 115.832 1.00 57.65  ? 158  ARG B CA    1 
ATOM   1180  C  C     . ARG A 1 156 ? 130.631 167.987 115.509 1.00 60.83  ? 158  ARG B C     1 
ATOM   1181  O  O     . ARG A 1 156 ? 130.472 167.623 114.339 1.00 67.77  ? 158  ARG B O     1 
ATOM   1182  C  CB    . ARG A 1 156 ? 132.929 168.661 116.241 1.00 58.74  ? 158  ARG B CB    1 
ATOM   1183  C  CG    . ARG A 1 156 ? 133.734 168.047 115.114 1.00 59.71  ? 158  ARG B CG    1 
ATOM   1184  C  CD    . ARG A 1 156 ? 134.192 169.115 114.146 1.00 61.99  ? 158  ARG B CD    1 
ATOM   1185  N  NE    . ARG A 1 156 ? 135.161 168.609 113.184 1.00 67.93  ? 158  ARG B NE    1 
ATOM   1186  C  CZ    . ARG A 1 156 ? 135.745 169.354 112.257 1.00 67.76  ? 158  ARG B CZ    1 
ATOM   1187  N  NH1   . ARG A 1 156 ? 135.472 170.642 112.134 1.00 66.50  ? 158  ARG B NH1   1 
ATOM   1188  N  NH2   . ARG A 1 156 ? 136.624 168.793 111.432 1.00 62.96  ? 158  ARG B NH2   1 
ATOM   1189  N  N     . GLU A 1 157 ? 130.024 167.378 116.528 1.00 57.65  ? 159  GLU B N     1 
ATOM   1190  C  CA    . GLU A 1 157 ? 129.058 166.322 116.258 1.00 56.14  ? 159  GLU B CA    1 
ATOM   1191  C  C     . GLU A 1 157 ? 127.761 166.875 115.683 1.00 55.12  ? 159  GLU B C     1 
ATOM   1192  O  O     . GLU A 1 157 ? 127.036 166.141 115.005 1.00 56.49  ? 159  GLU B O     1 
ATOM   1193  C  CB    . GLU A 1 157 ? 128.801 165.508 117.534 1.00 59.49  ? 159  GLU B CB    1 
ATOM   1194  C  CG    . GLU A 1 157 ? 127.672 165.997 118.443 1.00 68.12  ? 159  GLU B CG    1 
ATOM   1195  C  CD    . GLU A 1 157 ? 126.296 165.506 118.022 1.00 71.07  ? 159  GLU B CD    1 
ATOM   1196  O  OE1   . GLU A 1 157 ? 126.215 164.645 117.121 1.00 70.90  ? 159  GLU B OE1   1 
ATOM   1197  O  OE2   . GLU A 1 157 ? 125.294 165.985 118.595 1.00 67.20  ? 159  GLU B OE2   1 
ATOM   1198  N  N     . GLU A 1 158 ? 127.461 168.153 115.919 1.00 55.00  ? 160  GLU B N     1 
ATOM   1199  C  CA    . GLU A 1 158 ? 126.252 168.767 115.380 1.00 57.20  ? 160  GLU B CA    1 
ATOM   1200  C  C     . GLU A 1 158 ? 126.448 169.314 113.970 1.00 60.10  ? 160  GLU B C     1 
ATOM   1201  O  O     . GLU A 1 158 ? 125.550 169.188 113.131 1.00 62.94  ? 160  GLU B O     1 
ATOM   1202  C  CB    . GLU A 1 158 ? 125.776 169.889 116.305 1.00 60.82  ? 160  GLU B CB    1 
ATOM   1203  C  CG    . GLU A 1 158 ? 124.292 170.191 116.208 1.00 65.01  ? 160  GLU B CG    1 
ATOM   1204  C  CD    . GLU A 1 158 ? 123.439 169.183 116.949 1.00 70.72  ? 160  GLU B CD    1 
ATOM   1205  O  OE1   . GLU A 1 158 ? 123.987 168.441 117.790 1.00 70.37  ? 160  GLU B OE1   1 
ATOM   1206  O  OE2   . GLU A 1 158 ? 122.218 169.133 116.690 1.00 70.12  ? 160  GLU B OE2   1 
ATOM   1207  N  N     . TYR A 1 159 ? 127.601 169.920 113.691 1.00 61.77  ? 161  TYR B N     1 
ATOM   1208  C  CA    . TYR A 1 159 ? 127.907 170.504 112.385 1.00 58.06  ? 161  TYR B CA    1 
ATOM   1209  C  C     . TYR A 1 159 ? 129.229 169.923 111.903 1.00 60.08  ? 161  TYR B C     1 
ATOM   1210  O  O     . TYR A 1 159 ? 130.266 170.598 111.932 1.00 67.29  ? 161  TYR B O     1 
ATOM   1211  C  CB    . TYR A 1 159 ? 127.980 172.030 112.453 1.00 57.49  ? 161  TYR B CB    1 
ATOM   1212  C  CG    . TYR A 1 159 ? 126.725 172.708 112.949 1.00 56.80  ? 161  TYR B CG    1 
ATOM   1213  C  CD1   . TYR A 1 159 ? 126.454 172.803 114.303 1.00 59.67  ? 161  TYR B CD1   1 
ATOM   1214  C  CD2   . TYR A 1 159 ? 125.823 173.271 112.063 1.00 59.64  ? 161  TYR B CD2   1 
ATOM   1215  C  CE1   . TYR A 1 159 ? 125.314 173.424 114.760 1.00 60.45  ? 161  TYR B CE1   1 
ATOM   1216  C  CE2   . TYR A 1 159 ? 124.680 173.896 112.510 1.00 61.78  ? 161  TYR B CE2   1 
ATOM   1217  C  CZ    . TYR A 1 159 ? 124.432 173.971 113.860 1.00 62.83  ? 161  TYR B CZ    1 
ATOM   1218  O  OH    . TYR A 1 159 ? 123.293 174.593 114.313 1.00 59.96  ? 161  TYR B OH    1 
ATOM   1219  N  N     . PRO A 1 160 ? 129.229 168.667 111.449 1.00 56.30  ? 162  PRO B N     1 
ATOM   1220  C  CA    . PRO A 1 160 ? 130.496 168.012 111.089 1.00 55.31  ? 162  PRO B CA    1 
ATOM   1221  C  C     . PRO A 1 160 ? 131.162 168.574 109.846 1.00 60.08  ? 162  PRO B C     1 
ATOM   1222  O  O     . PRO A 1 160 ? 132.350 168.301 109.633 1.00 61.77  ? 162  PRO B O     1 
ATOM   1223  C  CB    . PRO A 1 160 ? 130.083 166.552 110.878 1.00 57.39  ? 162  PRO B CB    1 
ATOM   1224  C  CG    . PRO A 1 160 ? 128.659 166.631 110.466 1.00 60.44  ? 162  PRO B CG    1 
ATOM   1225  C  CD    . PRO A 1 160 ? 128.067 167.796 111.206 1.00 58.66  ? 162  PRO B CD    1 
ATOM   1226  N  N     . ASP A 1 161 ? 130.453 169.344 109.023 1.00 66.20  ? 163  ASP B N     1 
ATOM   1227  C  CA    . ASP A 1 161 ? 130.983 169.832 107.756 1.00 62.07  ? 163  ASP B CA    1 
ATOM   1228  C  C     . ASP A 1 161 ? 131.273 171.329 107.788 1.00 66.51  ? 163  ASP B C     1 
ATOM   1229  O  O     . ASP A 1 161 ? 131.197 172.002 106.759 1.00 70.22  ? 163  ASP B O     1 
ATOM   1230  C  CB    . ASP A 1 161 ? 130.019 169.507 106.616 1.00 65.61  ? 163  ASP B CB    1 
ATOM   1231  C  CG    . ASP A 1 161 ? 128.649 170.126 106.816 1.00 71.12  ? 163  ASP B CG    1 
ATOM   1232  O  OD1   . ASP A 1 161 ? 128.226 170.275 107.981 1.00 71.41  ? 163  ASP B OD1   1 
ATOM   1233  O  OD2   . ASP A 1 161 ? 127.996 170.464 105.806 1.00 68.97  ? 163  ASP B OD2   1 
ATOM   1234  N  N     . ARG A 1 162 ? 131.610 171.862 108.959 1.00 64.65  ? 164  ARG B N     1 
ATOM   1235  C  CA    . ARG A 1 162 ? 131.890 173.280 109.112 1.00 59.96  ? 164  ARG B CA    1 
ATOM   1236  C  C     . ARG A 1 162 ? 133.244 173.475 109.776 1.00 62.42  ? 164  ARG B C     1 
ATOM   1237  O  O     . ARG A 1 162 ? 133.671 172.669 110.607 1.00 67.24  ? 164  ARG B O     1 
ATOM   1238  C  CB    . ARG A 1 162 ? 130.804 173.983 109.931 1.00 60.47  ? 164  ARG B CB    1 
ATOM   1239  C  CG    . ARG A 1 162 ? 129.799 174.739 109.088 1.00 63.98  ? 164  ARG B CG    1 
ATOM   1240  C  CD    . ARG A 1 162 ? 128.935 173.792 108.285 1.00 64.94  ? 164  ARG B CD    1 
ATOM   1241  N  NE    . ARG A 1 162 ? 128.140 174.491 107.284 1.00 69.81  ? 164  ARG B NE    1 
ATOM   1242  C  CZ    . ARG A 1 162 ? 128.551 174.743 106.049 1.00 70.53  ? 164  ARG B CZ    1 
ATOM   1243  N  NH1   . ARG A 1 162 ? 129.746 174.364 105.628 1.00 65.11  ? 164  ARG B NH1   1 
ATOM   1244  N  NH2   . ARG A 1 162 ? 127.744 175.394 105.216 1.00 68.41  ? 164  ARG B NH2   1 
ATOM   1245  N  N     . ILE A 1 163 ? 133.914 174.562 109.396 1.00 56.29  ? 165  ILE B N     1 
ATOM   1246  C  CA    . ILE A 1 163 ? 135.221 174.884 109.952 1.00 57.56  ? 165  ILE B CA    1 
ATOM   1247  C  C     . ILE A 1 163 ? 135.085 175.219 111.431 1.00 62.42  ? 165  ILE B C     1 
ATOM   1248  O  O     . ILE A 1 163 ? 134.138 175.894 111.851 1.00 63.86  ? 165  ILE B O     1 
ATOM   1249  C  CB    . ILE A 1 163 ? 135.855 176.043 109.165 1.00 55.39  ? 165  ILE B CB    1 
ATOM   1250  C  CG1   . ILE A 1 163 ? 136.458 175.527 107.861 1.00 57.75  ? 165  ILE B CG1   1 
ATOM   1251  C  CG2   . ILE A 1 163 ? 136.914 176.756 109.990 1.00 62.72  ? 165  ILE B CG2   1 
ATOM   1252  C  CD1   . ILE A 1 163 ? 137.620 174.588 108.064 1.00 64.14  ? 165  ILE B CD1   1 
ATOM   1253  N  N     . MET A 1 164 ? 136.020 174.722 112.238 1.00 63.80  ? 166  MET B N     1 
ATOM   1254  C  CA    . MET A 1 164 ? 136.071 175.023 113.667 1.00 56.93  ? 166  MET B CA    1 
ATOM   1255  C  C     . MET A 1 164 ? 137.477 175.524 113.972 1.00 61.03  ? 166  MET B C     1 
ATOM   1256  O  O     . MET A 1 164 ? 138.372 174.737 114.286 1.00 72.77  ? 166  MET B O     1 
ATOM   1257  C  CB    . MET A 1 164 ? 135.706 173.805 114.502 1.00 58.93  ? 166  MET B CB    1 
ATOM   1258  C  CG    . MET A 1 164 ? 135.735 174.052 115.996 1.00 65.43  ? 166  MET B CG    1 
ATOM   1259  S  SD    . MET A 1 164 ? 134.100 174.361 116.675 1.00 89.49  ? 166  MET B SD    1 
ATOM   1260  C  CE    . MET A 1 164 ? 133.468 172.690 116.760 1.00 69.63  ? 166  MET B CE    1 
ATOM   1261  N  N     . ASN A 1 165 ? 137.669 176.835 113.874 1.00 49.44  ? 167  ASN B N     1 
ATOM   1262  C  CA    . ASN A 1 165 ? 138.954 177.458 114.154 1.00 48.64  ? 167  ASN B CA    1 
ATOM   1263  C  C     . ASN A 1 165 ? 138.919 178.059 115.553 1.00 55.73  ? 167  ASN B C     1 
ATOM   1264  O  O     . ASN A 1 165 ? 138.075 178.911 115.848 1.00 64.95  ? 167  ASN B O     1 
ATOM   1265  C  CB    . ASN A 1 165 ? 139.289 178.521 113.107 1.00 50.24  ? 167  ASN B CB    1 
ATOM   1266  C  CG    . ASN A 1 165 ? 138.171 179.519 112.907 1.00 62.27  ? 167  ASN B CG    1 
ATOM   1267  O  OD1   . ASN A 1 165 ? 137.208 179.255 112.189 1.00 62.86  ? 167  ASN B OD1   1 
ATOM   1268  N  ND2   . ASN A 1 165 ? 138.294 180.678 113.542 1.00 64.25  ? 167  ASN B ND2   1 
ATOM   1269  N  N     . THR A 1 166 ? 139.834 177.612 116.410 1.00 50.94  ? 168  THR B N     1 
ATOM   1270  C  CA    . THR A 1 166 ? 139.880 178.016 117.808 1.00 44.37  ? 168  THR B CA    1 
ATOM   1271  C  C     . THR A 1 166 ? 141.178 178.760 118.074 1.00 47.90  ? 168  THR B C     1 
ATOM   1272  O  O     . THR A 1 166 ? 142.245 178.331 117.627 1.00 63.78  ? 168  THR B O     1 
ATOM   1273  C  CB    . THR A 1 166 ? 139.771 176.806 118.736 1.00 51.31  ? 168  THR B CB    1 
ATOM   1274  O  OG1   . THR A 1 166 ? 141.051 176.179 118.854 1.00 60.08  ? 168  THR B OG1   1 
ATOM   1275  C  CG2   . THR A 1 166 ? 138.785 175.805 118.174 1.00 53.81  ? 168  THR B CG2   1 
ATOM   1276  N  N     . PHE A 1 167 ? 141.085 179.869 118.803 1.00 47.32  ? 169  PHE B N     1 
ATOM   1277  C  CA    . PHE A 1 167 ? 142.242 180.702 119.132 1.00 47.74  ? 169  PHE B CA    1 
ATOM   1278  C  C     . PHE A 1 167 ? 142.576 180.489 120.605 1.00 54.16  ? 169  PHE B C     1 
ATOM   1279  O  O     . PHE A 1 167 ? 142.091 181.204 121.481 1.00 59.08  ? 169  PHE B O     1 
ATOM   1280  C  CB    . PHE A 1 167 ? 141.962 182.167 118.826 1.00 48.28  ? 169  PHE B CB    1 
ATOM   1281  C  CG    . PHE A 1 167 ? 141.873 182.471 117.362 1.00 58.23  ? 169  PHE B CG    1 
ATOM   1282  C  CD1   . PHE A 1 167 ? 140.678 182.325 116.683 1.00 56.79  ? 169  PHE B CD1   1 
ATOM   1283  C  CD2   . PHE A 1 167 ? 142.987 182.896 116.663 1.00 59.14  ? 169  PHE B CD2   1 
ATOM   1284  C  CE1   . PHE A 1 167 ? 140.595 182.604 115.338 1.00 56.02  ? 169  PHE B CE1   1 
ATOM   1285  C  CE2   . PHE A 1 167 ? 142.910 183.172 115.318 1.00 55.98  ? 169  PHE B CE2   1 
ATOM   1286  C  CZ    . PHE A 1 167 ? 141.713 183.027 114.654 1.00 56.85  ? 169  PHE B CZ    1 
ATOM   1287  N  N     . SER A 1 168 ? 143.421 179.502 120.873 1.00 53.16  ? 170  SER B N     1 
ATOM   1288  C  CA    . SER A 1 168 ? 143.713 179.072 122.230 1.00 59.12  ? 170  SER B CA    1 
ATOM   1289  C  C     . SER A 1 168 ? 145.015 179.681 122.729 1.00 56.96  ? 170  SER B C     1 
ATOM   1290  O  O     . SER A 1 168 ? 145.946 179.927 121.959 1.00 60.78  ? 170  SER B O     1 
ATOM   1291  C  CB    . SER A 1 168 ? 143.789 177.547 122.308 1.00 60.35  ? 170  SER B CB    1 
ATOM   1292  O  OG    . SER A 1 168 ? 144.764 177.042 121.415 1.00 56.95  ? 170  SER B OG    1 
ATOM   1293  N  N     . VAL A 1 169 ? 145.068 179.922 124.035 1.00 53.38  ? 171  VAL B N     1 
ATOM   1294  C  CA    . VAL A 1 169 ? 146.243 180.469 124.699 1.00 49.74  ? 171  VAL B CA    1 
ATOM   1295  C  C     . VAL A 1 169 ? 146.911 179.329 125.455 1.00 51.15  ? 171  VAL B C     1 
ATOM   1296  O  O     . VAL A 1 169 ? 146.375 178.835 126.454 1.00 59.77  ? 171  VAL B O     1 
ATOM   1297  C  CB    . VAL A 1 169 ? 145.885 181.630 125.632 1.00 46.43  ? 171  VAL B CB    1 
ATOM   1298  C  CG1   . VAL A 1 169 ? 147.108 182.081 126.405 1.00 49.09  ? 171  VAL B CG1   1 
ATOM   1299  C  CG2   . VAL A 1 169 ? 145.304 182.781 124.833 1.00 45.56  ? 171  VAL B CG2   1 
ATOM   1300  N  N     . VAL A 1 170 ? 148.081 178.912 124.982 1.00 48.97  ? 172  VAL B N     1 
ATOM   1301  C  CA    . VAL A 1 170 ? 148.764 177.733 125.507 1.00 50.11  ? 172  VAL B CA    1 
ATOM   1302  C  C     . VAL A 1 170 ? 149.616 178.118 126.712 1.00 60.14  ? 172  VAL B C     1 
ATOM   1303  O  O     . VAL A 1 170 ? 149.996 179.289 126.851 1.00 62.73  ? 172  VAL B O     1 
ATOM   1304  C  CB    . VAL A 1 170 ? 149.614 177.061 124.418 1.00 58.11  ? 172  VAL B CB    1 
ATOM   1305  C  CG1   . VAL A 1 170 ? 148.720 176.481 123.337 1.00 56.31  ? 172  VAL B CG1   1 
ATOM   1306  C  CG2   . VAL A 1 170 ? 150.602 178.052 123.826 1.00 60.26  ? 172  VAL B CG2   1 
ATOM   1307  N  N     . PRO A 1 171 ? 149.922 177.179 127.608 1.00 63.86  ? 173  PRO B N     1 
ATOM   1308  C  CA    . PRO A 1 171 ? 150.759 177.506 128.768 1.00 61.46  ? 173  PRO B CA    1 
ATOM   1309  C  C     . PRO A 1 171 ? 152.151 177.975 128.371 1.00 64.98  ? 173  PRO B C     1 
ATOM   1310  O  O     . PRO A 1 171 ? 152.765 177.464 127.432 1.00 67.81  ? 173  PRO B O     1 
ATOM   1311  C  CB    . PRO A 1 171 ? 150.817 176.185 129.541 1.00 61.88  ? 173  PRO B CB    1 
ATOM   1312  C  CG    . PRO A 1 171 ? 149.597 175.448 129.116 1.00 61.42  ? 173  PRO B CG    1 
ATOM   1313  C  CD    . PRO A 1 171 ? 149.390 175.808 127.685 1.00 62.01  ? 173  PRO B CD    1 
ATOM   1314  N  N     . SER A 1 172 ? 152.647 178.959 129.114 1.00 70.23  ? 174  SER B N     1 
ATOM   1315  C  CA    . SER A 1 172 ? 153.981 179.491 128.877 1.00 71.69  ? 174  SER B CA    1 
ATOM   1316  C  C     . SER A 1 172 ? 155.036 178.551 129.457 1.00 74.04  ? 174  SER B C     1 
ATOM   1317  O  O     . SER A 1 172 ? 154.783 177.876 130.460 1.00 71.65  ? 174  SER B O     1 
ATOM   1318  C  CB    . SER A 1 172 ? 154.110 180.881 129.502 1.00 71.62  ? 174  SER B CB    1 
ATOM   1319  O  OG    . SER A 1 172 ? 155.448 181.343 129.477 1.00 74.26  ? 174  SER B OG    1 
ATOM   1320  N  N     . PRO A 1 173 ? 156.225 178.477 128.849 1.00 66.28  ? 175  PRO B N     1 
ATOM   1321  C  CA    . PRO A 1 173 ? 157.263 177.574 129.365 1.00 63.25  ? 175  PRO B CA    1 
ATOM   1322  C  C     . PRO A 1 173 ? 157.861 177.992 130.701 1.00 64.94  ? 175  PRO B C     1 
ATOM   1323  O  O     . PRO A 1 173 ? 157.947 177.177 131.624 1.00 65.59  ? 175  PRO B O     1 
ATOM   1324  C  CB    . PRO A 1 173 ? 158.323 177.596 128.257 1.00 60.89  ? 175  PRO B CB    1 
ATOM   1325  C  CG    . PRO A 1 173 ? 158.116 178.886 127.562 1.00 59.19  ? 175  PRO B CG    1 
ATOM   1326  C  CD    . PRO A 1 173 ? 156.643 179.140 127.603 1.00 60.53  ? 175  PRO B CD    1 
ATOM   1327  N  N     . LYS A 1 174 ? 158.281 179.253 130.820 1.00 68.53  ? 176  LYS B N     1 
ATOM   1328  C  CA    . LYS A 1 174 ? 159.092 179.649 131.967 1.00 64.48  ? 176  LYS B CA    1 
ATOM   1329  C  C     . LYS A 1 174 ? 158.245 180.009 133.183 1.00 67.18  ? 176  LYS B C     1 
ATOM   1330  O  O     . LYS A 1 174 ? 158.632 179.705 134.317 1.00 72.38  ? 176  LYS B O     1 
ATOM   1331  C  CB    . LYS A 1 174 ? 160.007 180.814 131.586 1.00 66.54  ? 176  LYS B CB    1 
ATOM   1332  C  CG    . LYS A 1 174 ? 159.290 182.079 131.149 1.00 76.08  ? 176  LYS B CG    1 
ATOM   1333  C  CD    . LYS A 1 174 ? 160.285 183.187 130.839 1.00 75.94  ? 176  LYS B CD    1 
ATOM   1334  C  CE    . LYS A 1 174 ? 159.581 184.501 130.541 1.00 73.54  ? 176  LYS B CE    1 
ATOM   1335  N  NZ    . LYS A 1 174 ? 158.800 184.990 131.710 1.00 75.49  ? 176  LYS B NZ    1 
ATOM   1336  N  N     . VAL A 1 175 ? 157.097 180.648 132.981 1.00 70.26  ? 177  VAL B N     1 
ATOM   1337  C  CA    . VAL A 1 175 ? 156.242 181.096 134.073 1.00 75.04  ? 177  VAL B CA    1 
ATOM   1338  C  C     . VAL A 1 175 ? 154.880 180.435 133.923 1.00 75.51  ? 177  VAL B C     1 
ATOM   1339  O  O     . VAL A 1 175 ? 154.258 180.520 132.858 1.00 72.97  ? 177  VAL B O     1 
ATOM   1340  C  CB    . VAL A 1 175 ? 156.106 182.629 134.097 1.00 74.40  ? 177  VAL B CB    1 
ATOM   1341  C  CG1   . VAL A 1 175 ? 155.108 183.058 135.162 1.00 71.14  ? 177  VAL B CG1   1 
ATOM   1342  C  CG2   . VAL A 1 175 ? 157.461 183.277 134.337 1.00 71.03  ? 177  VAL B CG2   1 
ATOM   1343  N  N     . SER A 1 176 ? 154.421 179.784 134.987 1.00 67.25  ? 178  SER B N     1 
ATOM   1344  C  CA    . SER A 1 176 ? 153.134 179.102 135.008 1.00 63.70  ? 178  SER B CA    1 
ATOM   1345  C  C     . SER A 1 176 ? 152.184 179.875 135.908 1.00 60.07  ? 178  SER B C     1 
ATOM   1346  O  O     . SER A 1 176 ? 152.498 180.127 137.076 1.00 60.67  ? 178  SER B O     1 
ATOM   1347  C  CB    . SER A 1 176 ? 153.287 177.664 135.498 1.00 64.04  ? 178  SER B CB    1 
ATOM   1348  O  OG    . SER A 1 176 ? 153.826 177.630 136.808 1.00 64.07  ? 178  SER B OG    1 
ATOM   1349  N  N     . ASP A 1 177 ? 151.025 180.250 135.365 1.00 64.82  ? 179  ASP B N     1 
ATOM   1350  C  CA    . ASP A 1 177 ? 150.049 180.990 136.159 1.00 67.06  ? 179  ASP B CA    1 
ATOM   1351  C  C     . ASP A 1 177 ? 149.307 180.072 137.123 1.00 68.45  ? 179  ASP B C     1 
ATOM   1352  O  O     . ASP A 1 177 ? 148.957 180.485 138.234 1.00 71.05  ? 179  ASP B O     1 
ATOM   1353  C  CB    . ASP A 1 177 ? 149.069 181.717 135.241 1.00 63.05  ? 179  ASP B CB    1 
ATOM   1354  C  CG    . ASP A 1 177 ? 148.493 182.967 135.877 1.00 69.15  ? 179  ASP B CG    1 
ATOM   1355  O  OD1   . ASP A 1 177 ? 148.514 183.069 137.122 1.00 69.66  ? 179  ASP B OD1   1 
ATOM   1356  O  OD2   . ASP A 1 177 ? 148.023 183.852 135.133 1.00 70.19  ? 179  ASP B OD2   1 
ATOM   1357  N  N     . THR A 1 178 ? 149.059 178.827 136.721 1.00 54.61  ? 180  THR B N     1 
ATOM   1358  C  CA    . THR A 1 178 ? 148.369 177.862 137.564 1.00 50.76  ? 180  THR B CA    1 
ATOM   1359  C  C     . THR A 1 178 ? 149.225 176.614 137.720 1.00 50.76  ? 180  THR B C     1 
ATOM   1360  O  O     . THR A 1 178 ? 149.997 176.256 136.827 1.00 52.47  ? 180  THR B O     1 
ATOM   1361  C  CB    . THR A 1 178 ? 146.997 177.483 136.990 1.00 55.18  ? 180  THR B CB    1 
ATOM   1362  O  OG1   . THR A 1 178 ? 147.165 176.547 135.922 1.00 60.80  ? 180  THR B OG1   1 
ATOM   1363  C  CG2   . THR A 1 178 ? 146.282 178.712 136.458 1.00 54.92  ? 180  THR B CG2   1 
ATOM   1364  N  N     . VAL A 1 179 ? 149.084 175.953 138.873 1.00 46.03  ? 181  VAL B N     1 
ATOM   1365  C  CA    . VAL A 1 179 ? 149.884 174.764 139.165 1.00 47.10  ? 181  VAL B CA    1 
ATOM   1366  C  C     . VAL A 1 179 ? 149.347 173.504 138.510 1.00 48.79  ? 181  VAL B C     1 
ATOM   1367  O  O     . VAL A 1 179 ? 150.034 172.476 138.517 1.00 50.25  ? 181  VAL B O     1 
ATOM   1368  C  CB    . VAL A 1 179 ? 149.990 174.511 140.680 1.00 45.05  ? 181  VAL B CB    1 
ATOM   1369  C  CG1   . VAL A 1 179 ? 150.717 175.652 141.357 1.00 46.21  ? 181  VAL B CG1   1 
ATOM   1370  C  CG2   . VAL A 1 179 ? 148.613 174.324 141.283 1.00 48.82  ? 181  VAL B CG2   1 
ATOM   1371  N  N     . VAL A 1 180 ? 148.145 173.547 137.946 1.00 55.64  ? 182  VAL B N     1 
ATOM   1372  C  CA    . VAL A 1 180 ? 147.559 172.396 137.277 1.00 54.66  ? 182  VAL B CA    1 
ATOM   1373  C  C     . VAL A 1 180 ? 147.514 172.593 135.761 1.00 54.96  ? 182  VAL B C     1 
ATOM   1374  O  O     . VAL A 1 180 ? 146.688 171.984 135.083 1.00 53.60  ? 182  VAL B O     1 
ATOM   1375  C  CB    . VAL A 1 180 ? 146.166 172.074 137.835 1.00 53.61  ? 182  VAL B CB    1 
ATOM   1376  C  CG1   . VAL A 1 180 ? 146.283 171.410 139.190 1.00 50.95  ? 182  VAL B CG1   1 
ATOM   1377  C  CG2   . VAL A 1 180 ? 145.332 173.339 137.928 1.00 52.71  ? 182  VAL B CG2   1 
ATOM   1378  N  N     . GLU A 1 181 ? 148.386 173.443 135.222 1.00 58.46  ? 183  GLU B N     1 
ATOM   1379  C  CA    . GLU A 1 181 ? 148.431 173.657 133.777 1.00 52.50  ? 183  GLU B CA    1 
ATOM   1380  C  C     . GLU A 1 181 ? 148.703 172.388 132.982 1.00 59.32  ? 183  GLU B C     1 
ATOM   1381  O  O     . GLU A 1 181 ? 148.043 172.189 131.950 1.00 67.32  ? 183  GLU B O     1 
ATOM   1382  C  CB    . GLU A 1 181 ? 149.467 174.735 133.442 1.00 57.65  ? 183  GLU B CB    1 
ATOM   1383  C  CG    . GLU A 1 181 ? 148.920 176.145 133.402 1.00 61.82  ? 183  GLU B CG    1 
ATOM   1384  C  CD    . GLU A 1 181 ? 149.999 177.178 133.151 1.00 69.97  ? 183  GLU B CD    1 
ATOM   1385  O  OE1   . GLU A 1 181 ? 151.188 176.799 133.116 1.00 70.92  ? 183  GLU B OE1   1 
ATOM   1386  O  OE2   . GLU A 1 181 ? 149.658 178.368 132.990 1.00 70.56  ? 183  GLU B OE2   1 
ATOM   1387  N  N     . PRO A 1 182 ? 149.659 171.524 133.351 1.00 52.49  ? 184  PRO B N     1 
ATOM   1388  C  CA    . PRO A 1 182 ? 149.902 170.335 132.513 1.00 50.42  ? 184  PRO B CA    1 
ATOM   1389  C  C     . PRO A 1 182 ? 148.686 169.439 132.359 1.00 52.69  ? 184  PRO B C     1 
ATOM   1390  O  O     . PRO A 1 182 ? 148.377 169.006 131.240 1.00 61.96  ? 184  PRO B O     1 
ATOM   1391  C  CB    . PRO A 1 182 ? 151.048 169.630 133.247 1.00 54.63  ? 184  PRO B CB    1 
ATOM   1392  C  CG    . PRO A 1 182 ? 151.728 170.705 133.994 1.00 55.88  ? 184  PRO B CG    1 
ATOM   1393  C  CD    . PRO A 1 182 ? 150.647 171.621 134.440 1.00 57.68  ? 184  PRO B CD    1 
ATOM   1394  N  N     . TYR A 1 183 ? 147.973 169.162 133.452 1.00 49.39  ? 185  TYR B N     1 
ATOM   1395  C  CA    . TYR A 1 183 ? 146.795 168.305 133.374 1.00 48.85  ? 185  TYR B CA    1 
ATOM   1396  C  C     . TYR A 1 183 ? 145.747 168.905 132.447 1.00 57.99  ? 185  TYR B C     1 
ATOM   1397  O  O     . TYR A 1 183 ? 145.263 168.242 131.518 1.00 66.29  ? 185  TYR B O     1 
ATOM   1398  C  CB    . TYR A 1 183 ? 146.201 168.099 134.768 1.00 55.06  ? 185  TYR B CB    1 
ATOM   1399  C  CG    . TYR A 1 183 ? 147.026 167.257 135.712 1.00 57.58  ? 185  TYR B CG    1 
ATOM   1400  C  CD1   . TYR A 1 183 ? 147.938 167.838 136.574 1.00 54.49  ? 185  TYR B CD1   1 
ATOM   1401  C  CD2   . TYR A 1 183 ? 146.876 165.884 135.755 1.00 57.49  ? 185  TYR B CD2   1 
ATOM   1402  C  CE1   . TYR A 1 183 ? 148.679 167.072 137.444 1.00 53.20  ? 185  TYR B CE1   1 
ATOM   1403  C  CE2   . TYR A 1 183 ? 147.614 165.112 136.620 1.00 54.17  ? 185  TYR B CE2   1 
ATOM   1404  C  CZ    . TYR A 1 183 ? 148.513 165.710 137.463 1.00 51.99  ? 185  TYR B CZ    1 
ATOM   1405  O  OH    . TYR A 1 183 ? 149.255 164.942 138.327 1.00 57.11  ? 185  TYR B OH    1 
ATOM   1406  N  N     . ASN A 1 184 ? 145.389 170.169 132.688 1.00 52.35  ? 186  ASN B N     1 
ATOM   1407  C  CA    . ASN A 1 184 ? 144.353 170.820 131.898 1.00 49.48  ? 186  ASN B CA    1 
ATOM   1408  C  C     . ASN A 1 184 ? 144.750 170.900 130.433 1.00 58.29  ? 186  ASN B C     1 
ATOM   1409  O  O     . ASN A 1 184 ? 143.938 170.620 129.545 1.00 63.68  ? 186  ASN B O     1 
ATOM   1410  C  CB    . ASN A 1 184 ? 144.078 172.217 132.451 1.00 45.07  ? 186  ASN B CB    1 
ATOM   1411  C  CG    . ASN A 1 184 ? 143.584 172.192 133.879 1.00 55.75  ? 186  ASN B CG    1 
ATOM   1412  O  OD1   . ASN A 1 184 ? 143.071 171.181 134.351 1.00 60.87  ? 186  ASN B OD1   1 
ATOM   1413  N  ND2   . ASN A 1 184 ? 143.738 173.309 134.577 1.00 61.65  ? 186  ASN B ND2   1 
ATOM   1414  N  N     . ALA A 1 185 ? 146.003 171.262 130.162 1.00 51.59  ? 187  ALA B N     1 
ATOM   1415  C  CA    . ALA A 1 185 ? 146.453 171.417 128.786 1.00 46.78  ? 187  ALA B CA    1 
ATOM   1416  C  C     . ALA A 1 185 ? 146.455 170.087 128.047 1.00 49.34  ? 187  ALA B C     1 
ATOM   1417  O  O     . ALA A 1 185 ? 146.009 170.015 126.897 1.00 61.56  ? 187  ALA B O     1 
ATOM   1418  C  CB    . ALA A 1 185 ? 147.841 172.050 128.759 1.00 49.93  ? 187  ALA B CB    1 
ATOM   1419  N  N     . THR A 1 186 ? 146.958 169.025 128.679 1.00 45.28  ? 188  THR B N     1 
ATOM   1420  C  CA    . THR A 1 186 ? 146.972 167.723 128.023 1.00 46.43  ? 188  THR B CA    1 
ATOM   1421  C  C     . THR A 1 186 ? 145.555 167.233 127.755 1.00 48.65  ? 188  THR B C     1 
ATOM   1422  O  O     . THR A 1 186 ? 145.244 166.764 126.651 1.00 62.44  ? 188  THR B O     1 
ATOM   1423  C  CB    . THR A 1 186 ? 147.739 166.716 128.877 1.00 51.81  ? 188  THR B CB    1 
ATOM   1424  O  OG1   . THR A 1 186 ? 149.055 167.216 129.135 1.00 58.77  ? 188  THR B OG1   1 
ATOM   1425  C  CG2   . THR A 1 186 ? 147.853 165.391 128.155 1.00 50.99  ? 188  THR B CG2   1 
ATOM   1426  N  N     . LEU A 1 187 ? 144.672 167.356 128.750 1.00 41.63  ? 189  LEU B N     1 
ATOM   1427  C  CA    . LEU A 1 187 ? 143.299 166.904 128.563 1.00 46.08  ? 189  LEU B CA    1 
ATOM   1428  C  C     . LEU A 1 187 ? 142.568 167.737 127.518 1.00 56.21  ? 189  LEU B C     1 
ATOM   1429  O  O     . LEU A 1 187 ? 141.664 167.227 126.846 1.00 60.63  ? 189  LEU B O     1 
ATOM   1430  C  CB    . LEU A 1 187 ? 142.555 166.936 129.895 1.00 46.20  ? 189  LEU B CB    1 
ATOM   1431  C  CG    . LEU A 1 187 ? 143.058 165.959 130.958 1.00 48.88  ? 189  LEU B CG    1 
ATOM   1432  C  CD1   . LEU A 1 187 ? 142.590 166.389 132.330 1.00 56.12  ? 189  LEU B CD1   1 
ATOM   1433  C  CD2   . LEU A 1 187 ? 142.596 164.549 130.654 1.00 48.26  ? 189  LEU B CD2   1 
ATOM   1434  N  N     . SER A 1 188 ? 142.935 169.011 127.364 1.00 60.58  ? 190  SER B N     1 
ATOM   1435  C  CA    . SER A 1 188 ? 142.296 169.845 126.354 1.00 56.01  ? 190  SER B CA    1 
ATOM   1436  C  C     . SER A 1 188 ? 142.814 169.535 124.955 1.00 56.63  ? 190  SER B C     1 
ATOM   1437  O  O     . SER A 1 188 ? 142.037 169.511 123.993 1.00 66.86  ? 190  SER B O     1 
ATOM   1438  C  CB    . SER A 1 188 ? 142.507 171.320 126.689 1.00 55.20  ? 190  SER B CB    1 
ATOM   1439  O  OG    . SER A 1 188 ? 141.761 172.148 125.818 1.00 61.86  ? 190  SER B OG    1 
ATOM   1440  N  N     . VAL A 1 189 ? 144.119 169.293 124.821 1.00 45.08  ? 191  VAL B N     1 
ATOM   1441  C  CA    . VAL A 1 189 ? 144.677 168.974 123.511 1.00 46.67  ? 191  VAL B CA    1 
ATOM   1442  C  C     . VAL A 1 189 ? 144.186 167.612 123.043 1.00 47.05  ? 191  VAL B C     1 
ATOM   1443  O  O     . VAL A 1 189 ? 143.978 167.392 121.842 1.00 61.32  ? 191  VAL B O     1 
ATOM   1444  C  CB    . VAL A 1 189 ? 146.213 169.046 123.547 1.00 47.55  ? 191  VAL B CB    1 
ATOM   1445  C  CG1   . VAL A 1 189 ? 146.785 168.570 122.237 1.00 48.36  ? 191  VAL B CG1   1 
ATOM   1446  C  CG2   . VAL A 1 189 ? 146.665 170.464 123.824 1.00 49.47  ? 191  VAL B CG2   1 
ATOM   1447  N  N     . HIS A 1 190 ? 143.955 166.690 123.982 1.00 41.32  ? 192  HIS B N     1 
ATOM   1448  C  CA    . HIS A 1 190 ? 143.480 165.360 123.615 1.00 43.25  ? 192  HIS B CA    1 
ATOM   1449  C  C     . HIS A 1 190 ? 142.182 165.420 122.822 1.00 53.62  ? 192  HIS B C     1 
ATOM   1450  O  O     . HIS A 1 190 ? 141.888 164.503 122.047 1.00 59.09  ? 192  HIS B O     1 
ATOM   1451  C  CB    . HIS A 1 190 ? 143.296 164.510 124.871 1.00 48.62  ? 192  HIS B CB    1 
ATOM   1452  C  CG    . HIS A 1 190 ? 142.678 163.173 124.615 1.00 57.23  ? 192  HIS B CG    1 
ATOM   1453  N  ND1   . HIS A 1 190 ? 143.321 162.177 123.914 1.00 60.01  ? 192  HIS B ND1   1 
ATOM   1454  C  CD2   . HIS A 1 190 ? 141.478 162.663 124.977 1.00 57.99  ? 192  HIS B CD2   1 
ATOM   1455  C  CE1   . HIS A 1 190 ? 142.541 161.113 123.849 1.00 56.99  ? 192  HIS B CE1   1 
ATOM   1456  N  NE2   . HIS A 1 190 ? 141.417 161.382 124.488 1.00 57.15  ? 192  HIS B NE2   1 
ATOM   1457  N  N     . GLN A 1 191 ? 141.400 166.483 122.987 1.00 55.09  ? 193  GLN B N     1 
ATOM   1458  C  CA    . GLN A 1 191 ? 140.181 166.661 122.213 1.00 56.29  ? 193  GLN B CA    1 
ATOM   1459  C  C     . GLN A 1 191 ? 140.285 167.741 121.149 1.00 54.28  ? 193  GLN B C     1 
ATOM   1460  O  O     . GLN A 1 191 ? 139.544 167.691 120.162 1.00 64.37  ? 193  GLN B O     1 
ATOM   1461  C  CB    . GLN A 1 191 ? 139.008 166.978 123.143 1.00 55.55  ? 193  GLN B CB    1 
ATOM   1462  C  CG    . GLN A 1 191 ? 138.938 166.071 124.357 1.00 58.15  ? 193  GLN B CG    1 
ATOM   1463  C  CD    . GLN A 1 191 ? 137.522 165.699 124.725 1.00 63.89  ? 193  GLN B CD    1 
ATOM   1464  O  OE1   . GLN A 1 191 ? 136.599 165.859 123.929 1.00 65.73  ? 193  GLN B OE1   1 
ATOM   1465  N  NE2   . GLN A 1 191 ? 137.340 165.194 125.939 1.00 61.60  ? 193  GLN B NE2   1 
ATOM   1466  N  N     . LEU A 1 192 ? 141.187 168.710 121.319 1.00 47.99  ? 194  LEU B N     1 
ATOM   1467  C  CA    . LEU A 1 192 ? 141.438 169.676 120.254 1.00 46.05  ? 194  LEU B CA    1 
ATOM   1468  C  C     . LEU A 1 192 ? 141.988 168.994 119.011 1.00 54.88  ? 194  LEU B C     1 
ATOM   1469  O  O     . LEU A 1 192 ? 141.637 169.365 117.886 1.00 66.79  ? 194  LEU B O     1 
ATOM   1470  C  CB    . LEU A 1 192 ? 142.407 170.755 120.731 1.00 49.95  ? 194  LEU B CB    1 
ATOM   1471  C  CG    . LEU A 1 192 ? 141.870 171.863 121.630 1.00 56.24  ? 194  LEU B CG    1 
ATOM   1472  C  CD1   . LEU A 1 192 ? 142.925 172.933 121.811 1.00 56.24  ? 194  LEU B CD1   1 
ATOM   1473  C  CD2   . LEU A 1 192 ? 140.600 172.450 121.057 1.00 59.39  ? 194  LEU B CD2   1 
ATOM   1474  N  N     . VAL A 1 193 ? 142.862 168.001 119.192 1.00 47.20  ? 195  VAL B N     1 
ATOM   1475  C  CA    . VAL A 1 193 ? 143.441 167.305 118.047 1.00 46.59  ? 195  VAL B CA    1 
ATOM   1476  C  C     . VAL A 1 193 ? 142.349 166.643 117.217 1.00 56.10  ? 195  VAL B C     1 
ATOM   1477  O  O     . VAL A 1 193 ? 142.413 166.620 115.982 1.00 63.99  ? 195  VAL B O     1 
ATOM   1478  C  CB    . VAL A 1 193 ? 144.493 166.284 118.516 1.00 47.43  ? 195  VAL B CB    1 
ATOM   1479  C  CG1   . VAL A 1 193 ? 144.957 165.428 117.360 1.00 53.39  ? 195  VAL B CG1   1 
ATOM   1480  C  CG2   . VAL A 1 193 ? 145.670 166.993 119.144 1.00 58.16  ? 195  VAL B CG2   1 
ATOM   1481  N  N     . GLU A 1 194 ? 141.323 166.111 117.877 1.00 60.77  ? 196  GLU B N     1 
ATOM   1482  C  CA    . GLU A 1 194 ? 140.300 165.358 117.162 1.00 60.07  ? 196  GLU B CA    1 
ATOM   1483  C  C     . GLU A 1 194 ? 139.169 166.236 116.636 1.00 58.71  ? 196  GLU B C     1 
ATOM   1484  O  O     . GLU A 1 194 ? 138.631 165.952 115.560 1.00 66.63  ? 196  GLU B O     1 
ATOM   1485  C  CB    . GLU A 1 194 ? 139.729 164.267 118.067 1.00 59.82  ? 196  GLU B CB    1 
ATOM   1486  C  CG    . GLU A 1 194 ? 140.778 163.388 118.722 1.00 62.96  ? 196  GLU B CG    1 
ATOM   1487  C  CD    . GLU A 1 194 ? 141.352 162.357 117.770 1.00 69.28  ? 196  GLU B CD    1 
ATOM   1488  O  OE1   . GLU A 1 194 ? 140.764 162.151 116.688 1.00 64.46  ? 196  GLU B OE1   1 
ATOM   1489  O  OE2   . GLU A 1 194 ? 142.392 161.752 118.105 1.00 70.72  ? 196  GLU B OE2   1 
ATOM   1490  N  N     . ASN A 1 195 ? 138.789 167.294 117.354 1.00 53.62  ? 197  ASN B N     1 
ATOM   1491  C  CA    . ASN A 1 195 ? 137.546 167.999 117.060 1.00 58.56  ? 197  ASN B CA    1 
ATOM   1492  C  C     . ASN A 1 195 ? 137.756 169.412 116.521 1.00 61.56  ? 197  ASN B C     1 
ATOM   1493  O  O     . ASN A 1 195 ? 136.868 170.256 116.666 1.00 68.93  ? 197  ASN B O     1 
ATOM   1494  C  CB    . ASN A 1 195 ? 136.664 168.050 118.308 1.00 62.21  ? 197  ASN B CB    1 
ATOM   1495  C  CG    . ASN A 1 195 ? 136.402 166.683 118.897 1.00 65.97  ? 197  ASN B CG    1 
ATOM   1496  O  OD1   . ASN A 1 195 ? 137.329 165.944 119.217 1.00 67.76  ? 197  ASN B OD1   1 
ATOM   1497  N  ND2   . ASN A 1 195 ? 135.129 166.338 119.046 1.00 65.70  ? 197  ASN B ND2   1 
ATOM   1498  N  N     . THR A 1 196 ? 138.894 169.695 115.895 1.00 57.86  ? 198  THR B N     1 
ATOM   1499  C  CA    . THR A 1 196 ? 139.157 171.016 115.342 1.00 60.96  ? 198  THR B CA    1 
ATOM   1500  C  C     . THR A 1 196 ? 139.744 170.899 113.943 1.00 63.29  ? 198  THR B C     1 
ATOM   1501  O  O     . THR A 1 196 ? 140.325 169.873 113.578 1.00 69.68  ? 198  THR B O     1 
ATOM   1502  C  CB    . THR A 1 196 ? 140.116 171.826 116.222 1.00 63.25  ? 198  THR B CB    1 
ATOM   1503  O  OG1   . THR A 1 196 ? 141.297 171.058 116.482 1.00 71.69  ? 198  THR B OG1   1 
ATOM   1504  C  CG2   . THR A 1 196 ? 139.455 172.197 117.535 1.00 62.15  ? 198  THR B CG2   1 
ATOM   1505  N  N     . ASP A 1 197 ? 139.585 171.966 113.161 1.00 57.83  ? 199  ASP B N     1 
ATOM   1506  C  CA    . ASP A 1 197 ? 140.124 172.036 111.809 1.00 58.90  ? 199  ASP B CA    1 
ATOM   1507  C  C     . ASP A 1 197 ? 141.406 172.849 111.723 1.00 58.32  ? 199  ASP B C     1 
ATOM   1508  O  O     . ASP A 1 197 ? 142.295 172.510 110.938 1.00 67.15  ? 199  ASP B O     1 
ATOM   1509  C  CB    . ASP A 1 197 ? 139.084 172.624 110.852 1.00 61.62  ? 199  ASP B CB    1 
ATOM   1510  C  CG    . ASP A 1 197 ? 137.998 171.631 110.495 1.00 67.74  ? 199  ASP B CG    1 
ATOM   1511  O  OD1   . ASP A 1 197 ? 138.302 170.423 110.416 1.00 65.27  ? 199  ASP B OD1   1 
ATOM   1512  O  OD2   . ASP A 1 197 ? 136.842 172.057 110.293 1.00 68.92  ? 199  ASP B OD2   1 
ATOM   1513  N  N     . GLU A 1 198 ? 141.524 173.912 112.513 1.00 51.18  ? 200  GLU B N     1 
ATOM   1514  C  CA    . GLU A 1 198 ? 142.757 174.691 112.565 1.00 56.48  ? 200  GLU B CA    1 
ATOM   1515  C  C     . GLU A 1 198 ? 142.775 175.474 113.866 1.00 56.36  ? 200  GLU B C     1 
ATOM   1516  O  O     . GLU A 1 198 ? 141.914 176.330 114.085 1.00 62.09  ? 200  GLU B O     1 
ATOM   1517  C  CB    . GLU A 1 198 ? 142.875 175.624 111.356 1.00 62.31  ? 200  GLU B CB    1 
ATOM   1518  C  CG    . GLU A 1 198 ? 141.610 176.389 111.007 1.00 66.75  ? 200  GLU B CG    1 
ATOM   1519  C  CD    . GLU A 1 198 ? 141.823 177.370 109.874 1.00 67.28  ? 200  GLU B CD    1 
ATOM   1520  O  OE1   . GLU A 1 198 ? 142.707 177.120 109.029 1.00 64.74  ? 200  GLU B OE1   1 
ATOM   1521  O  OE2   . GLU A 1 198 ? 141.109 178.393 109.828 1.00 68.92  ? 200  GLU B OE2   1 
ATOM   1522  N  N     . THR A 1 199 ? 143.743 175.181 114.727 1.00 52.20  ? 201  THR B N     1 
ATOM   1523  C  CA    . THR A 1 199 ? 143.867 175.829 116.023 1.00 40.00  ? 201  THR B CA    1 
ATOM   1524  C  C     . THR A 1 199 ? 145.119 176.689 116.038 1.00 44.28  ? 201  THR B C     1 
ATOM   1525  O  O     . THR A 1 199 ? 146.176 176.265 115.560 1.00 59.47  ? 201  THR B O     1 
ATOM   1526  C  CB    . THR A 1 199 ? 143.900 174.800 117.156 1.00 49.41  ? 201  THR B CB    1 
ATOM   1527  O  OG1   . THR A 1 199 ? 144.226 175.449 118.389 1.00 50.42  ? 201  THR B OG1   1 
ATOM   1528  C  CG2   . THR A 1 199 ? 144.905 173.710 116.864 1.00 56.04  ? 201  THR B CG2   1 
ATOM   1529  N  N     . TYR A 1 200 ? 144.991 177.900 116.566 1.00 47.96  ? 202  TYR B N     1 
ATOM   1530  C  CA    . TYR A 1 200 ? 146.074 178.870 116.584 1.00 51.01  ? 202  TYR B CA    1 
ATOM   1531  C  C     . TYR A 1 200 ? 146.632 178.949 117.997 1.00 57.50  ? 202  TYR B C     1 
ATOM   1532  O  O     . TYR A 1 200 ? 145.895 179.245 118.944 1.00 61.62  ? 202  TYR B O     1 
ATOM   1533  C  CB    . TYR A 1 200 ? 145.589 180.239 116.112 1.00 48.54  ? 202  TYR B CB    1 
ATOM   1534  C  CG    . TYR A 1 200 ? 145.106 180.260 114.680 1.00 50.97  ? 202  TYR B CG    1 
ATOM   1535  C  CD1   . TYR A 1 200 ? 143.898 179.682 114.325 1.00 52.22  ? 202  TYR B CD1   1 
ATOM   1536  C  CD2   . TYR A 1 200 ? 145.857 180.861 113.686 1.00 56.06  ? 202  TYR B CD2   1 
ATOM   1537  C  CE1   . TYR A 1 200 ? 143.454 179.698 113.023 1.00 52.10  ? 202  TYR B CE1   1 
ATOM   1538  C  CE2   . TYR A 1 200 ? 145.419 180.883 112.380 1.00 58.56  ? 202  TYR B CE2   1 
ATOM   1539  C  CZ    . TYR A 1 200 ? 144.217 180.299 112.055 1.00 57.28  ? 202  TYR B CZ    1 
ATOM   1540  O  OH    . TYR A 1 200 ? 143.776 180.319 110.753 1.00 54.89  ? 202  TYR B OH    1 
ATOM   1541  N  N     . CYS A 1 201 ? 147.926 178.693 118.133 1.00 56.35  ? 203  CYS B N     1 
ATOM   1542  C  CA    . CYS A 1 201 ? 148.557 178.566 119.437 1.00 51.59  ? 203  CYS B CA    1 
ATOM   1543  C  C     . CYS A 1 201 ? 149.248 179.872 119.802 1.00 58.11  ? 203  CYS B C     1 
ATOM   1544  O  O     . CYS A 1 201 ? 150.162 180.317 119.099 1.00 66.24  ? 203  CYS B O     1 
ATOM   1545  C  CB    . CYS A 1 201 ? 149.552 177.409 119.431 1.00 61.16  ? 203  CYS B CB    1 
ATOM   1546  S  SG    . CYS A 1 201 ? 148.791 175.798 119.161 1.00 75.58  ? 203  CYS B SG    1 
ATOM   1547  N  N     . ILE A 1 202 ? 148.814 180.479 120.901 1.00 54.15  ? 204  ILE B N     1 
ATOM   1548  C  CA    . ILE A 1 202 ? 149.377 181.723 121.409 1.00 53.83  ? 204  ILE B CA    1 
ATOM   1549  C  C     . ILE A 1 202 ? 149.782 181.494 122.857 1.00 59.49  ? 204  ILE B C     1 
ATOM   1550  O  O     . ILE A 1 202 ? 149.039 180.869 123.620 1.00 70.84  ? 204  ILE B O     1 
ATOM   1551  C  CB    . ILE A 1 202 ? 148.372 182.885 121.295 1.00 52.03  ? 204  ILE B CB    1 
ATOM   1552  C  CG1   . ILE A 1 202 ? 147.997 183.125 119.835 1.00 56.12  ? 204  ILE B CG1   1 
ATOM   1553  C  CG2   . ILE A 1 202 ? 148.936 184.150 121.913 1.00 56.08  ? 204  ILE B CG2   1 
ATOM   1554  C  CD1   . ILE A 1 202 ? 146.648 182.573 119.450 1.00 59.24  ? 204  ILE B CD1   1 
ATOM   1555  N  N     . ASP A 1 203 ? 150.962 181.973 123.231 1.00 58.35  ? 205  ASP B N     1 
ATOM   1556  C  CA    . ASP A 1 203 ? 151.401 181.944 124.617 1.00 57.20  ? 205  ASP B CA    1 
ATOM   1557  C  C     . ASP A 1 203 ? 151.785 183.347 125.053 1.00 58.17  ? 205  ASP B C     1 
ATOM   1558  O  O     . ASP A 1 203 ? 152.282 184.143 124.251 1.00 62.61  ? 205  ASP B O     1 
ATOM   1559  C  CB    . ASP A 1 203 ? 152.571 180.987 124.818 1.00 64.78  ? 205  ASP B CB    1 
ATOM   1560  C  CG    . ASP A 1 203 ? 153.532 181.001 123.663 1.00 74.47  ? 205  ASP B CG    1 
ATOM   1561  O  OD1   . ASP A 1 203 ? 153.772 182.090 123.108 1.00 75.64  ? 205  ASP B OD1   1 
ATOM   1562  O  OD2   . ASP A 1 203 ? 154.036 179.919 123.298 1.00 75.14  ? 205  ASP B OD2   1 
ATOM   1563  N  N     . ASN A 1 204 ? 151.543 183.648 126.329 1.00 60.60  ? 206  ASN B N     1 
ATOM   1564  C  CA    . ASN A 1 204 ? 151.775 185.001 126.818 1.00 60.00  ? 206  ASN B CA    1 
ATOM   1565  C  C     . ASN A 1 204 ? 153.254 185.358 126.812 1.00 62.40  ? 206  ASN B C     1 
ATOM   1566  O  O     . ASN A 1 204 ? 153.599 186.542 126.759 1.00 72.78  ? 206  ASN B O     1 
ATOM   1567  C  CB    . ASN A 1 204 ? 151.196 185.162 128.222 1.00 59.36  ? 206  ASN B CB    1 
ATOM   1568  C  CG    . ASN A 1 204 ? 149.682 185.164 128.233 1.00 63.31  ? 206  ASN B CG    1 
ATOM   1569  O  OD1   . ASN A 1 204 ? 149.058 184.325 128.878 1.00 64.39  ? 206  ASN B OD1   1 
ATOM   1570  N  ND2   . ASN A 1 204 ? 149.083 186.109 127.524 1.00 61.78  ? 206  ASN B ND2   1 
ATOM   1571  N  N     . GLU A 1 205 ? 154.139 184.361 126.873 1.00 65.76  ? 207  GLU B N     1 
ATOM   1572  C  CA    . GLU A 1 205 ? 155.569 184.652 126.895 1.00 65.10  ? 207  GLU B CA    1 
ATOM   1573  C  C     . GLU A 1 205 ? 156.019 185.318 125.602 1.00 72.60  ? 207  GLU B C     1 
ATOM   1574  O  O     . GLU A 1 205 ? 156.753 186.314 125.629 1.00 79.09  ? 207  GLU B O     1 
ATOM   1575  C  CB    . GLU A 1 205 ? 156.361 183.371 127.144 1.00 69.50  ? 207  GLU B CB    1 
ATOM   1576  C  CG    . GLU A 1 205 ? 157.823 183.599 127.484 1.00 75.69  ? 207  GLU B CG    1 
ATOM   1577  C  CD    . GLU A 1 205 ? 158.712 183.642 126.256 1.00 83.52  ? 207  GLU B CD    1 
ATOM   1578  O  OE1   . GLU A 1 205 ? 158.283 183.149 125.192 1.00 81.13  ? 207  GLU B OE1   1 
ATOM   1579  O  OE2   . GLU A 1 205 ? 159.839 184.171 126.355 1.00 82.90  ? 207  GLU B OE2   1 
ATOM   1580  N  N     . ALA A 1 206 ? 155.581 184.789 124.459 1.00 64.57  ? 208  ALA B N     1 
ATOM   1581  C  CA    . ALA A 1 206 ? 155.941 185.401 123.186 1.00 63.16  ? 208  ALA B CA    1 
ATOM   1582  C  C     . ALA A 1 206 ? 155.312 186.779 123.042 1.00 61.90  ? 208  ALA B C     1 
ATOM   1583  O  O     . ALA A 1 206 ? 155.918 187.682 122.458 1.00 71.95  ? 208  ALA B O     1 
ATOM   1584  C  CB    . ALA A 1 206 ? 155.528 184.497 122.028 1.00 62.95  ? 208  ALA B CB    1 
ATOM   1585  N  N     . LEU A 1 207 ? 154.095 186.959 123.557 1.00 47.41  ? 209  LEU B N     1 
ATOM   1586  C  CA    . LEU A 1 207 ? 153.465 188.273 123.512 1.00 52.51  ? 209  LEU B CA    1 
ATOM   1587  C  C     . LEU A 1 207 ? 154.251 189.290 124.331 1.00 57.93  ? 209  LEU B C     1 
ATOM   1588  O  O     . LEU A 1 207 ? 154.469 190.423 123.884 1.00 67.01  ? 209  LEU B O     1 
ATOM   1589  C  CB    . LEU A 1 207 ? 152.025 188.177 124.009 1.00 54.86  ? 209  LEU B CB    1 
ATOM   1590  C  CG    . LEU A 1 207 ? 151.126 187.175 123.285 1.00 57.69  ? 209  LEU B CG    1 
ATOM   1591  C  CD1   . LEU A 1 207 ? 149.760 187.110 123.939 1.00 60.88  ? 209  LEU B CD1   1 
ATOM   1592  C  CD2   . LEU A 1 207 ? 150.995 187.545 121.826 1.00 57.52  ? 209  LEU B CD2   1 
ATOM   1593  N  N     . TYR A 1 208 ? 154.692 188.901 125.530 1.00 55.61  ? 210  TYR B N     1 
ATOM   1594  C  CA    . TYR A 1 208 ? 155.515 189.792 126.341 1.00 52.94  ? 210  TYR B CA    1 
ATOM   1595  C  C     . TYR A 1 208 ? 156.828 190.103 125.642 1.00 58.90  ? 210  TYR B C     1 
ATOM   1596  O  O     . TYR A 1 208 ? 157.304 191.244 125.673 1.00 67.22  ? 210  TYR B O     1 
ATOM   1597  C  CB    . TYR A 1 208 ? 155.788 189.169 127.710 1.00 51.37  ? 210  TYR B CB    1 
ATOM   1598  C  CG    . TYR A 1 208 ? 154.609 189.157 128.650 1.00 54.79  ? 210  TYR B CG    1 
ATOM   1599  C  CD1   . TYR A 1 208 ? 153.863 190.298 128.877 1.00 61.15  ? 210  TYR B CD1   1 
ATOM   1600  C  CD2   . TYR A 1 208 ? 154.254 188.001 129.324 1.00 55.58  ? 210  TYR B CD2   1 
ATOM   1601  C  CE1   . TYR A 1 208 ? 152.788 190.284 129.740 1.00 60.72  ? 210  TYR B CE1   1 
ATOM   1602  C  CE2   . TYR A 1 208 ? 153.183 187.977 130.183 1.00 53.92  ? 210  TYR B CE2   1 
ATOM   1603  C  CZ    . TYR A 1 208 ? 152.454 189.120 130.389 1.00 57.69  ? 210  TYR B CZ    1 
ATOM   1604  O  OH    . TYR A 1 208 ? 151.384 189.095 131.251 1.00 61.99  ? 210  TYR B OH    1 
ATOM   1605  N  N     . ASP A 1 209 ? 157.434 189.094 125.015 1.00 62.23  ? 211  ASP B N     1 
ATOM   1606  C  CA    . ASP A 1 209 ? 158.681 189.318 124.295 1.00 61.27  ? 211  ASP B CA    1 
ATOM   1607  C  C     . ASP A 1 209 ? 158.482 190.293 123.142 1.00 64.54  ? 211  ASP B C     1 
ATOM   1608  O  O     . ASP A 1 209 ? 159.303 191.190 122.934 1.00 71.39  ? 211  ASP B O     1 
ATOM   1609  C  CB    . ASP A 1 209 ? 159.237 187.991 123.787 1.00 64.39  ? 211  ASP B CB    1 
ATOM   1610  C  CG    . ASP A 1 209 ? 160.641 188.123 123.240 1.00 71.17  ? 211  ASP B CG    1 
ATOM   1611  O  OD1   . ASP A 1 209 ? 161.284 189.160 123.503 1.00 70.48  ? 211  ASP B OD1   1 
ATOM   1612  O  OD2   . ASP A 1 209 ? 161.101 187.192 122.547 1.00 73.67  ? 211  ASP B OD2   1 
ATOM   1613  N  N     . ILE A 1 210 ? 157.393 190.136 122.388 1.00 59.90  ? 212  ILE B N     1 
ATOM   1614  C  CA    . ILE A 1 210 ? 157.096 191.058 121.296 1.00 57.40  ? 212  ILE B CA    1 
ATOM   1615  C  C     . ILE A 1 210 ? 156.925 192.469 121.836 1.00 61.34  ? 212  ILE B C     1 
ATOM   1616  O  O     . ILE A 1 210 ? 157.502 193.429 121.313 1.00 67.83  ? 212  ILE B O     1 
ATOM   1617  C  CB    . ILE A 1 210 ? 155.841 190.600 120.531 1.00 55.62  ? 212  ILE B CB    1 
ATOM   1618  C  CG1   . ILE A 1 210 ? 156.127 189.339 119.721 1.00 57.90  ? 212  ILE B CG1   1 
ATOM   1619  C  CG2   . ILE A 1 210 ? 155.336 191.701 119.625 1.00 59.36  ? 212  ILE B CG2   1 
ATOM   1620  C  CD1   . ILE A 1 210 ? 154.916 188.816 118.986 1.00 57.43  ? 212  ILE B CD1   1 
ATOM   1621  N  N     . CYS A 1 211 ? 156.148 192.607 122.913 1.00 62.80  ? 213  CYS B N     1 
ATOM   1622  C  CA    . CYS A 1 211 ? 155.868 193.928 123.462 1.00 63.45  ? 213  CYS B CA    1 
ATOM   1623  C  C     . CYS A 1 211 ? 157.138 194.608 123.952 1.00 64.88  ? 213  CYS B C     1 
ATOM   1624  O  O     . CYS A 1 211 ? 157.322 195.814 123.749 1.00 74.92  ? 213  CYS B O     1 
ATOM   1625  C  CB    . CYS A 1 211 ? 154.848 193.820 124.594 1.00 66.65  ? 213  CYS B CB    1 
ATOM   1626  S  SG    . CYS A 1 211 ? 153.192 193.342 124.068 1.00 73.98  ? 213  CYS B SG    1 
ATOM   1627  N  N     . PHE A 1 212 ? 158.028 193.856 124.600 1.00 61.66  ? 214  PHE B N     1 
ATOM   1628  C  CA    . PHE A 1 212 ? 159.211 194.483 125.179 1.00 64.43  ? 214  PHE B CA    1 
ATOM   1629  C  C     . PHE A 1 212 ? 160.303 194.708 124.140 1.00 66.50  ? 214  PHE B C     1 
ATOM   1630  O  O     . PHE A 1 212 ? 161.080 195.662 124.252 1.00 71.20  ? 214  PHE B O     1 
ATOM   1631  C  CB    . PHE A 1 212 ? 159.744 193.646 126.338 1.00 64.89  ? 214  PHE B CB    1 
ATOM   1632  C  CG    . PHE A 1 212 ? 160.985 194.212 126.960 1.00 69.99  ? 214  PHE B CG    1 
ATOM   1633  C  CD1   . PHE A 1 212 ? 160.918 195.337 127.763 1.00 65.96  ? 214  PHE B CD1   1 
ATOM   1634  C  CD2   . PHE A 1 212 ? 162.219 193.630 126.732 1.00 70.56  ? 214  PHE B CD2   1 
ATOM   1635  C  CE1   . PHE A 1 212 ? 162.056 195.867 128.332 1.00 66.51  ? 214  PHE B CE1   1 
ATOM   1636  C  CE2   . PHE A 1 212 ? 163.362 194.156 127.300 1.00 69.59  ? 214  PHE B CE2   1 
ATOM   1637  C  CZ    . PHE A 1 212 ? 163.279 195.276 128.101 1.00 68.81  ? 214  PHE B CZ    1 
ATOM   1638  N  N     . ARG A 1 213 ? 160.387 193.850 123.123 1.00 58.45  ? 215  ARG B N     1 
ATOM   1639  C  CA    . ARG A 1 213 ? 161.464 193.945 122.145 1.00 57.59  ? 215  ARG B CA    1 
ATOM   1640  C  C     . ARG A 1 213 ? 161.084 194.819 120.953 1.00 61.43  ? 215  ARG B C     1 
ATOM   1641  O  O     . ARG A 1 213 ? 161.764 195.806 120.659 1.00 68.06  ? 215  ARG B O     1 
ATOM   1642  C  CB    . ARG A 1 213 ? 161.866 192.544 121.670 1.00 61.15  ? 215  ARG B CB    1 
ATOM   1643  C  CG    . ARG A 1 213 ? 162.970 191.905 122.491 1.00 63.89  ? 215  ARG B CG    1 
ATOM   1644  C  CD    . ARG A 1 213 ? 163.787 190.936 121.652 1.00 65.16  ? 215  ARG B CD    1 
ATOM   1645  N  NE    . ARG A 1 213 ? 163.406 189.546 121.865 1.00 69.01  ? 215  ARG B NE    1 
ATOM   1646  C  CZ    . ARG A 1 213 ? 164.097 188.688 122.603 1.00 69.74  ? 215  ARG B CZ    1 
ATOM   1647  N  NH1   . ARG A 1 213 ? 165.209 189.049 123.223 1.00 67.92  ? 215  ARG B NH1   1 
ATOM   1648  N  NH2   . ARG A 1 213 ? 163.663 187.437 122.722 1.00 68.17  ? 215  ARG B NH2   1 
ATOM   1649  N  N     . THR A 1 214 ? 160.007 194.464 120.254 1.00 61.12  ? 216  THR B N     1 
ATOM   1650  C  CA    . THR A 1 214 ? 159.627 195.202 119.056 1.00 62.04  ? 216  THR B CA    1 
ATOM   1651  C  C     . THR A 1 214 ? 158.851 196.465 119.410 1.00 62.18  ? 216  THR B C     1 
ATOM   1652  O  O     . THR A 1 214 ? 159.196 197.565 118.966 1.00 65.57  ? 216  THR B O     1 
ATOM   1653  C  CB    . THR A 1 214 ? 158.801 194.309 118.127 1.00 63.68  ? 216  THR B CB    1 
ATOM   1654  O  OG1   . THR A 1 214 ? 157.754 193.682 118.875 1.00 69.81  ? 216  THR B OG1   1 
ATOM   1655  C  CG2   . THR A 1 214 ? 159.673 193.236 117.506 1.00 58.58  ? 216  THR B CG2   1 
ATOM   1656  N  N     . LEU A 1 215 ? 157.799 196.323 120.213 1.00 55.89  ? 217  LEU B N     1 
ATOM   1657  C  CA    . LEU A 1 215 ? 156.954 197.450 120.581 1.00 55.29  ? 217  LEU B CA    1 
ATOM   1658  C  C     . LEU A 1 215 ? 157.594 198.370 121.611 1.00 62.28  ? 217  LEU B C     1 
ATOM   1659  O  O     . LEU A 1 215 ? 157.154 199.517 121.742 1.00 67.79  ? 217  LEU B O     1 
ATOM   1660  C  CB    . LEU A 1 215 ? 155.614 196.946 121.113 1.00 52.68  ? 217  LEU B CB    1 
ATOM   1661  C  CG    . LEU A 1 215 ? 154.711 196.248 120.099 1.00 57.56  ? 217  LEU B CG    1 
ATOM   1662  C  CD1   . LEU A 1 215 ? 153.458 195.722 120.767 1.00 59.78  ? 217  LEU B CD1   1 
ATOM   1663  C  CD2   . LEU A 1 215 ? 154.356 197.197 118.968 1.00 62.19  ? 217  LEU B CD2   1 
ATOM   1664  N  N     . LYS A 1 216 ? 158.605 197.897 122.338 1.00 61.80  ? 218  LYS B N     1 
ATOM   1665  C  CA    . LYS A 1 216 ? 159.304 198.692 123.348 1.00 57.05  ? 218  LYS B CA    1 
ATOM   1666  C  C     . LYS A 1 216 ? 158.330 199.272 124.371 1.00 58.85  ? 218  LYS B C     1 
ATOM   1667  O  O     . LYS A 1 216 ? 158.425 200.433 124.774 1.00 62.03  ? 218  LYS B O     1 
ATOM   1668  C  CB    . LYS A 1 216 ? 160.135 199.795 122.695 1.00 55.98  ? 218  LYS B CB    1 
ATOM   1669  C  CG    . LYS A 1 216 ? 161.124 199.290 121.664 1.00 59.13  ? 218  LYS B CG    1 
ATOM   1670  C  CD    . LYS A 1 216 ? 162.518 199.202 122.243 1.00 59.65  ? 218  LYS B CD    1 
ATOM   1671  C  CE    . LYS A 1 216 ? 163.545 198.961 121.156 1.00 60.42  ? 218  LYS B CE    1 
ATOM   1672  N  NZ    . LYS A 1 216 ? 163.878 197.516 121.026 1.00 60.42  ? 218  LYS B NZ    1 
ATOM   1673  N  N     . LEU A 1 217 ? 157.380 198.445 124.793 1.00 59.54  ? 219  LEU B N     1 
ATOM   1674  C  CA    . LEU A 1 217 ? 156.422 198.830 125.819 1.00 63.60  ? 219  LEU B CA    1 
ATOM   1675  C  C     . LEU A 1 217 ? 157.035 198.614 127.195 1.00 67.88  ? 219  LEU B C     1 
ATOM   1676  O  O     . LEU A 1 217 ? 157.495 197.513 127.511 1.00 69.35  ? 219  LEU B O     1 
ATOM   1677  C  CB    . LEU A 1 217 ? 155.130 198.025 125.685 1.00 62.02  ? 219  LEU B CB    1 
ATOM   1678  C  CG    . LEU A 1 217 ? 154.277 198.285 124.446 1.00 62.39  ? 219  LEU B CG    1 
ATOM   1679  C  CD1   . LEU A 1 217 ? 153.094 197.338 124.414 1.00 62.34  ? 219  LEU B CD1   1 
ATOM   1680  C  CD2   . LEU A 1 217 ? 153.806 199.727 124.425 1.00 61.00  ? 219  LEU B CD2   1 
ATOM   1681  N  N     . THR A 1 218 ? 157.045 199.672 128.008 1.00 61.75  ? 220  THR B N     1 
ATOM   1682  C  CA    . THR A 1 218 ? 157.615 199.564 129.346 1.00 57.14  ? 220  THR B CA    1 
ATOM   1683  C  C     . THR A 1 218 ? 156.756 198.690 130.249 1.00 58.18  ? 220  THR B C     1 
ATOM   1684  O  O     . THR A 1 218 ? 157.279 197.840 130.978 1.00 57.68  ? 220  THR B O     1 
ATOM   1685  C  CB    . THR A 1 218 ? 157.786 200.953 129.958 1.00 63.84  ? 220  THR B CB    1 
ATOM   1686  O  OG1   . THR A 1 218 ? 156.524 201.632 129.961 1.00 66.05  ? 220  THR B OG1   1 
ATOM   1687  C  CG2   . THR A 1 218 ? 158.793 201.767 129.157 1.00 63.99  ? 220  THR B CG2   1 
ATOM   1688  N  N     . THR A 1 219 ? 155.437 198.877 130.211 1.00 59.99  ? 221  THR B N     1 
ATOM   1689  C  CA    . THR A 1 219 ? 154.505 198.175 131.093 1.00 60.29  ? 221  THR B CA    1 
ATOM   1690  C  C     . THR A 1 219 ? 153.425 197.505 130.255 1.00 59.55  ? 221  THR B C     1 
ATOM   1691  O  O     . THR A 1 219 ? 152.307 198.023 130.134 1.00 64.61  ? 221  THR B O     1 
ATOM   1692  C  CB    . THR A 1 219 ? 153.875 199.128 132.109 1.00 63.25  ? 221  THR B CB    1 
ATOM   1693  O  OG1   . THR A 1 219 ? 153.067 200.092 131.423 1.00 63.92  ? 221  THR B OG1   1 
ATOM   1694  C  CG2   . THR A 1 219 ? 154.948 199.850 132.911 1.00 59.38  ? 221  THR B CG2   1 
ATOM   1695  N  N     . PRO A 1 220 ? 153.723 196.355 129.657 1.00 53.59  ? 222  PRO B N     1 
ATOM   1696  C  CA    . PRO A 1 220 ? 152.685 195.627 128.923 1.00 51.20  ? 222  PRO B CA    1 
ATOM   1697  C  C     . PRO A 1 220 ? 151.642 195.053 129.868 1.00 57.58  ? 222  PRO B C     1 
ATOM   1698  O  O     . PRO A 1 220 ? 151.966 194.456 130.895 1.00 60.45  ? 222  PRO B O     1 
ATOM   1699  C  CB    . PRO A 1 220 ? 153.467 194.522 128.206 1.00 54.83  ? 222  PRO B CB    1 
ATOM   1700  C  CG    . PRO A 1 220 ? 154.716 194.374 128.985 1.00 58.53  ? 222  PRO B CG    1 
ATOM   1701  C  CD    . PRO A 1 220 ? 155.047 195.735 129.498 1.00 60.54  ? 222  PRO B CD    1 
ATOM   1702  N  N     . THR A 1 221 ? 150.376 195.234 129.503 1.00 64.96  ? 223  THR B N     1 
ATOM   1703  C  CA    . THR A 1 221 ? 149.253 194.714 130.265 1.00 62.53  ? 223  THR B CA    1 
ATOM   1704  C  C     . THR A 1 221 ? 148.502 193.704 129.412 1.00 65.40  ? 223  THR B C     1 
ATOM   1705  O  O     . THR A 1 221 ? 148.845 193.465 128.251 1.00 72.79  ? 223  THR B O     1 
ATOM   1706  C  CB    . THR A 1 221 ? 148.302 195.832 130.710 1.00 58.99  ? 223  THR B CB    1 
ATOM   1707  O  OG1   . THR A 1 221 ? 147.788 196.509 129.558 1.00 60.31  ? 223  THR B OG1   1 
ATOM   1708  C  CG2   . THR A 1 221 ? 149.033 196.831 131.588 1.00 60.44  ? 223  THR B CG2   1 
ATOM   1709  N  N     . TYR A 1 222 ? 147.468 193.102 130.004 1.00 54.98  ? 224  TYR B N     1 
ATOM   1710  C  CA    . TYR A 1 222 ? 146.673 192.125 129.269 1.00 52.54  ? 224  TYR B CA    1 
ATOM   1711  C  C     . TYR A 1 222 ? 145.960 192.761 128.087 1.00 62.23  ? 224  TYR B C     1 
ATOM   1712  O  O     . TYR A 1 222 ? 145.679 192.080 127.093 1.00 69.02  ? 224  TYR B O     1 
ATOM   1713  C  CB    . TYR A 1 222 ? 145.666 191.457 130.199 1.00 50.76  ? 224  TYR B CB    1 
ATOM   1714  C  CG    . TYR A 1 222 ? 146.242 190.316 130.997 1.00 58.89  ? 224  TYR B CG    1 
ATOM   1715  C  CD1   . TYR A 1 222 ? 147.545 189.894 130.795 1.00 60.25  ? 224  TYR B CD1   1 
ATOM   1716  C  CD2   . TYR A 1 222 ? 145.484 189.661 131.954 1.00 62.39  ? 224  TYR B CD2   1 
ATOM   1717  C  CE1   . TYR A 1 222 ? 148.079 188.853 131.520 1.00 57.50  ? 224  TYR B CE1   1 
ATOM   1718  C  CE2   . TYR A 1 222 ? 146.010 188.617 132.686 1.00 63.79  ? 224  TYR B CE2   1 
ATOM   1719  C  CZ    . TYR A 1 222 ? 147.308 188.218 132.463 1.00 62.63  ? 224  TYR B CZ    1 
ATOM   1720  O  OH    . TYR A 1 222 ? 147.841 187.178 133.189 1.00 63.99  ? 224  TYR B OH    1 
ATOM   1721  N  N     . GLY A 1 223 ? 145.661 194.058 128.170 1.00 63.48  ? 225  GLY B N     1 
ATOM   1722  C  CA    . GLY A 1 223 ? 145.028 194.732 127.050 1.00 61.77  ? 225  GLY B CA    1 
ATOM   1723  C  C     . GLY A 1 223 ? 145.875 194.690 125.794 1.00 64.83  ? 225  GLY B C     1 
ATOM   1724  O  O     . GLY A 1 223 ? 145.375 194.418 124.702 1.00 73.54  ? 225  GLY B O     1 
ATOM   1725  N  N     . ASP A 1 224 ? 147.178 194.938 125.937 1.00 60.38  ? 226  ASP B N     1 
ATOM   1726  C  CA    . ASP A 1 224 ? 148.067 194.933 124.780 1.00 65.07  ? 226  ASP B CA    1 
ATOM   1727  C  C     . ASP A 1 224 ? 148.209 193.537 124.184 1.00 65.18  ? 226  ASP B C     1 
ATOM   1728  O  O     . ASP A 1 224 ? 148.248 193.379 122.956 1.00 72.48  ? 226  ASP B O     1 
ATOM   1729  C  CB    . ASP A 1 224 ? 149.429 195.495 125.178 1.00 73.28  ? 226  ASP B CB    1 
ATOM   1730  C  CG    . ASP A 1 224 ? 149.341 196.921 125.679 1.00 78.48  ? 226  ASP B CG    1 
ATOM   1731  O  OD1   . ASP A 1 224 ? 148.235 197.499 125.631 1.00 75.04  ? 226  ASP B OD1   1 
ATOM   1732  O  OD2   . ASP A 1 224 ? 150.371 197.463 126.129 1.00 77.31  ? 226  ASP B OD2   1 
ATOM   1733  N  N     . LEU A 1 225 ? 148.296 192.511 125.032 1.00 55.12  ? 227  LEU B N     1 
ATOM   1734  C  CA    . LEU A 1 225 ? 148.395 191.146 124.525 1.00 60.24  ? 227  LEU B CA    1 
ATOM   1735  C  C     . LEU A 1 225 ? 147.123 190.738 123.793 1.00 65.58  ? 227  LEU B C     1 
ATOM   1736  O  O     . LEU A 1 225 ? 147.179 190.182 122.686 1.00 68.50  ? 227  LEU B O     1 
ATOM   1737  C  CB    . LEU A 1 225 ? 148.682 190.182 125.674 1.00 58.07  ? 227  LEU B CB    1 
ATOM   1738  C  CG    . LEU A 1 225 ? 149.719 190.605 126.711 1.00 61.02  ? 227  LEU B CG    1 
ATOM   1739  C  CD1   . LEU A 1 225 ? 149.973 189.465 127.679 1.00 61.61  ? 227  LEU B CD1   1 
ATOM   1740  C  CD2   . LEU A 1 225 ? 151.014 191.045 126.050 1.00 63.91  ? 227  LEU B CD2   1 
ATOM   1741  N  N     . ASN A 1 226 ? 145.968 191.004 124.398 1.00 58.47  ? 228  ASN B N     1 
ATOM   1742  C  CA    . ASN A 1 226 ? 144.689 190.767 123.749 1.00 56.22  ? 228  ASN B CA    1 
ATOM   1743  C  C     . ASN A 1 226 ? 144.548 191.545 122.451 1.00 61.58  ? 228  ASN B C     1 
ATOM   1744  O  O     . ASN A 1 226 ? 143.949 191.035 121.503 1.00 68.25  ? 228  ASN B O     1 
ATOM   1745  C  CB    . ASN A 1 226 ? 143.549 191.133 124.699 1.00 53.20  ? 228  ASN B CB    1 
ATOM   1746  C  CG    . ASN A 1 226 ? 143.555 190.302 125.959 1.00 54.88  ? 228  ASN B CG    1 
ATOM   1747  O  OD1   . ASN A 1 226 ? 144.392 189.419 126.127 1.00 54.20  ? 228  ASN B OD1   1 
ATOM   1748  N  ND2   . ASN A 1 226 ? 142.623 190.583 126.858 1.00 60.47  ? 228  ASN B ND2   1 
ATOM   1749  N  N     . HIS A 1 227 ? 145.105 192.749 122.383 1.00 62.20  ? 229  HIS B N     1 
ATOM   1750  C  CA    . HIS A 1 227 ? 145.112 193.568 121.184 1.00 59.72  ? 229  HIS B CA    1 
ATOM   1751  C  C     . HIS A 1 227 ? 145.961 192.969 120.068 1.00 61.38  ? 229  HIS B C     1 
ATOM   1752  O  O     . HIS A 1 227 ? 145.503 192.913 118.919 1.00 64.62  ? 229  HIS B O     1 
ATOM   1753  C  CB    . HIS A 1 227 ? 145.612 194.968 121.560 1.00 61.30  ? 229  HIS B CB    1 
ATOM   1754  C  CG    . HIS A 1 227 ? 145.448 195.997 120.491 1.00 63.76  ? 229  HIS B CG    1 
ATOM   1755  N  ND1   . HIS A 1 227 ? 145.633 197.340 120.735 1.00 66.77  ? 229  HIS B ND1   1 
ATOM   1756  C  CD2   . HIS A 1 227 ? 145.122 195.893 119.183 1.00 67.87  ? 229  HIS B CD2   1 
ATOM   1757  C  CE1   . HIS A 1 227 ? 145.430 198.019 119.622 1.00 70.99  ? 229  HIS B CE1   1 
ATOM   1758  N  NE2   . HIS A 1 227 ? 145.119 197.165 118.665 1.00 73.56  ? 229  HIS B NE2   1 
ATOM   1759  N  N     . LEU A 1 228 ? 147.166 192.494 120.381 1.00 57.06  ? 230  LEU B N     1 
ATOM   1760  C  CA    . LEU A 1 228 ? 147.965 191.765 119.403 1.00 55.60  ? 230  LEU B CA    1 
ATOM   1761  C  C     . LEU A 1 228 ? 147.285 190.498 118.912 1.00 60.87  ? 230  LEU B C     1 
ATOM   1762  O  O     . LEU A 1 228 ? 147.369 190.192 117.717 1.00 65.13  ? 230  LEU B O     1 
ATOM   1763  C  CB    . LEU A 1 228 ? 149.337 191.398 119.974 1.00 49.42  ? 230  LEU B CB    1 
ATOM   1764  C  CG    . LEU A 1 228 ? 150.314 192.529 120.274 1.00 56.26  ? 230  LEU B CG    1 
ATOM   1765  C  CD1   . LEU A 1 228 ? 151.452 192.016 121.130 1.00 62.02  ? 230  LEU B CD1   1 
ATOM   1766  C  CD2   . LEU A 1 228 ? 150.836 193.135 118.985 1.00 59.20  ? 230  LEU B CD2   1 
ATOM   1767  N  N     . VAL A 1 229 ? 146.626 189.753 119.794 1.00 59.60  ? 231  VAL B N     1 
ATOM   1768  C  CA    . VAL A 1 229 ? 145.875 188.576 119.363 1.00 50.05  ? 231  VAL B CA    1 
ATOM   1769  C  C     . VAL A 1 229 ? 144.697 188.962 118.475 1.00 53.26  ? 231  VAL B C     1 
ATOM   1770  O  O     . VAL A 1 229 ? 144.425 188.300 117.468 1.00 63.98  ? 231  VAL B O     1 
ATOM   1771  C  CB    . VAL A 1 229 ? 145.415 187.765 120.589 1.00 50.55  ? 231  VAL B CB    1 
ATOM   1772  C  CG1   . VAL A 1 229 ? 144.571 186.584 120.159 1.00 51.69  ? 231  VAL B CG1   1 
ATOM   1773  C  CG2   . VAL A 1 229 ? 146.613 187.295 121.386 1.00 53.49  ? 231  VAL B CG2   1 
ATOM   1774  N  N     . SER A 1 230 ? 143.986 190.032 118.834 1.00 53.90  ? 232  SER B N     1 
ATOM   1775  C  CA    . SER A 1 230 ? 142.843 190.473 118.044 1.00 58.75  ? 232  SER B CA    1 
ATOM   1776  C  C     . SER A 1 230 ? 143.271 190.925 116.657 1.00 61.07  ? 232  SER B C     1 
ATOM   1777  O  O     . SER A 1 230 ? 142.518 190.771 115.690 1.00 66.14  ? 232  SER B O     1 
ATOM   1778  C  CB    . SER A 1 230 ? 142.110 191.597 118.773 1.00 58.29  ? 232  SER B CB    1 
ATOM   1779  O  OG    . SER A 1 230 ? 141.742 191.197 120.080 1.00 61.30  ? 232  SER B OG    1 
ATOM   1780  N  N     . ALA A 1 231 ? 144.473 191.494 116.542 1.00 57.58  ? 233  ALA B N     1 
ATOM   1781  C  CA    . ALA A 1 231 ? 144.978 191.876 115.228 1.00 57.49  ? 233  ALA B CA    1 
ATOM   1782  C  C     . ALA A 1 231 ? 145.024 190.680 114.283 1.00 60.26  ? 233  ALA B C     1 
ATOM   1783  O  O     . ALA A 1 231 ? 144.475 190.734 113.175 1.00 61.28  ? 233  ALA B O     1 
ATOM   1784  C  CB    . ALA A 1 231 ? 146.362 192.509 115.361 1.00 57.03  ? 233  ALA B CB    1 
ATOM   1785  N  N     . THR A 1 232 ? 145.643 189.579 114.712 1.00 60.35  ? 234  THR B N     1 
ATOM   1786  C  CA    . THR A 1 232 ? 145.729 188.415 113.836 1.00 59.20  ? 234  THR B CA    1 
ATOM   1787  C  C     . THR A 1 232 ? 144.381 187.720 113.691 1.00 60.08  ? 234  THR B C     1 
ATOM   1788  O  O     . THR A 1 232 ? 144.107 187.122 112.644 1.00 67.09  ? 234  THR B O     1 
ATOM   1789  C  CB    . THR A 1 232 ? 146.794 187.436 114.338 1.00 62.44  ? 234  THR B CB    1 
ATOM   1790  O  OG1   . THR A 1 232 ? 147.104 186.497 113.302 1.00 69.18  ? 234  THR B OG1   1 
ATOM   1791  C  CG2   . THR A 1 232 ? 146.316 186.677 115.558 1.00 61.68  ? 234  THR B CG2   1 
ATOM   1792  N  N     . MET A 1 233 ? 143.518 187.800 114.709 1.00 55.65  ? 235  MET B N     1 
ATOM   1793  C  CA    . MET A 1 233 ? 142.183 187.227 114.572 1.00 59.39  ? 235  MET B CA    1 
ATOM   1794  C  C     . MET A 1 233 ? 141.386 187.942 113.489 1.00 62.99  ? 235  MET B C     1 
ATOM   1795  O  O     . MET A 1 233 ? 140.700 187.298 112.687 1.00 63.29  ? 235  MET B O     1 
ATOM   1796  C  CB    . MET A 1 233 ? 141.444 187.281 115.907 1.00 59.51  ? 235  MET B CB    1 
ATOM   1797  C  CG    . MET A 1 233 ? 141.923 186.255 116.912 1.00 62.78  ? 235  MET B CG    1 
ATOM   1798  S  SD    . MET A 1 233 ? 141.124 186.432 118.511 1.00 72.85  ? 235  MET B SD    1 
ATOM   1799  C  CE    . MET A 1 233 ? 139.437 186.032 118.079 1.00 62.05  ? 235  MET B CE    1 
ATOM   1800  N  N     . SER A 1 234 ? 141.461 189.272 113.452 1.00 62.15  ? 236  SER B N     1 
ATOM   1801  C  CA    . SER A 1 234 ? 140.803 190.024 112.390 1.00 60.37  ? 236  SER B CA    1 
ATOM   1802  C  C     . SER A 1 234 ? 141.467 189.773 111.043 1.00 64.63  ? 236  SER B C     1 
ATOM   1803  O  O     . SER A 1 234 ? 140.783 189.677 110.017 1.00 68.42  ? 236  SER B O     1 
ATOM   1804  C  CB    . SER A 1 234 ? 140.811 191.515 112.723 1.00 61.02  ? 236  SER B CB    1 
ATOM   1805  O  OG    . SER A 1 234 ? 140.261 192.277 111.664 1.00 65.79  ? 236  SER B OG    1 
ATOM   1806  N  N     . GLY A 1 235 ? 142.797 189.665 111.021 1.00 60.99  ? 237  GLY B N     1 
ATOM   1807  C  CA    . GLY A 1 235 ? 143.494 189.511 109.757 1.00 58.41  ? 237  GLY B CA    1 
ATOM   1808  C  C     . GLY A 1 235 ? 143.330 188.143 109.127 1.00 63.51  ? 237  GLY B C     1 
ATOM   1809  O  O     . GLY A 1 235 ? 143.504 187.994 107.914 1.00 67.89  ? 237  GLY B O     1 
ATOM   1810  N  N     . VAL A 1 236 ? 143.007 187.127 109.929 1.00 57.25  ? 238  VAL B N     1 
ATOM   1811  C  CA    . VAL A 1 236 ? 142.837 185.783 109.383 1.00 53.80  ? 238  VAL B CA    1 
ATOM   1812  C  C     . VAL A 1 236 ? 141.648 185.735 108.432 1.00 57.40  ? 238  VAL B C     1 
ATOM   1813  O  O     . VAL A 1 236 ? 141.708 185.105 107.370 1.00 62.12  ? 238  VAL B O     1 
ATOM   1814  C  CB    . VAL A 1 236 ? 142.699 184.757 110.524 1.00 55.59  ? 238  VAL B CB    1 
ATOM   1815  C  CG1   . VAL A 1 236 ? 141.928 183.537 110.064 1.00 58.29  ? 238  VAL B CG1   1 
ATOM   1816  C  CG2   . VAL A 1 236 ? 144.071 184.349 111.031 1.00 56.07  ? 238  VAL B CG2   1 
ATOM   1817  N  N     . THR A 1 237 ? 140.557 186.413 108.785 1.00 57.98  ? 239  THR B N     1 
ATOM   1818  C  CA    . THR A 1 237 ? 139.314 186.352 108.029 1.00 60.10  ? 239  THR B CA    1 
ATOM   1819  C  C     . THR A 1 237 ? 139.022 187.641 107.267 1.00 57.58  ? 239  THR B C     1 
ATOM   1820  O  O     . THR A 1 237 ? 137.854 187.996 107.084 1.00 61.61  ? 239  THR B O     1 
ATOM   1821  C  CB    . THR A 1 237 ? 138.149 186.017 108.961 1.00 63.58  ? 239  THR B CB    1 
ATOM   1822  O  OG1   . THR A 1 237 ? 136.922 186.042 108.224 1.00 63.39  ? 239  THR B OG1   1 
ATOM   1823  C  CG2   . THR A 1 237 ? 138.076 187.017 110.103 1.00 60.37  ? 239  THR B CG2   1 
ATOM   1824  N  N     . THR A 1 238 ? 140.056 188.348 106.812 1.00 53.42  ? 240  THR B N     1 
ATOM   1825  C  CA    . THR A 1 238 ? 139.827 189.616 106.128 1.00 55.52  ? 240  THR B CA    1 
ATOM   1826  C  C     . THR A 1 238 ? 139.271 189.413 104.726 1.00 55.35  ? 240  THR B C     1 
ATOM   1827  O  O     . THR A 1 238 ? 138.546 190.275 104.217 1.00 62.35  ? 240  THR B O     1 
ATOM   1828  C  CB    . THR A 1 238 ? 141.118 190.429 106.066 1.00 59.45  ? 240  THR B CB    1 
ATOM   1829  O  OG1   . THR A 1 238 ? 140.891 191.624 105.310 1.00 61.50  ? 240  THR B OG1   1 
ATOM   1830  C  CG2   . THR A 1 238 ? 142.221 189.630 105.404 1.00 60.50  ? 240  THR B CG2   1 
ATOM   1831  N  N     . CYS A 1 239 ? 139.594 188.290 104.084 1.00 54.76  ? 241  CYS B N     1 
ATOM   1832  C  CA    . CYS A 1 239 ? 139.101 188.054 102.732 1.00 56.13  ? 241  CYS B CA    1 
ATOM   1833  C  C     . CYS A 1 239 ? 137.616 187.723 102.727 1.00 63.08  ? 241  CYS B C     1 
ATOM   1834  O  O     . CYS A 1 239 ? 136.948 187.893 101.702 1.00 63.47  ? 241  CYS B O     1 
ATOM   1835  C  CB    . CYS A 1 239 ? 139.901 186.935 102.070 1.00 59.97  ? 241  CYS B CB    1 
ATOM   1836  S  SG    . CYS A 1 239 ? 141.621 187.359 101.743 1.00 77.69  ? 241  CYS B SG    1 
ATOM   1837  N  N     . LEU A 1 240 ? 137.085 187.249 103.855 1.00 58.03  ? 242  LEU B N     1 
ATOM   1838  C  CA    . LEU A 1 240 ? 135.653 187.013 103.968 1.00 54.73  ? 242  LEU B CA    1 
ATOM   1839  C  C     . LEU A 1 240 ? 134.852 188.306 103.997 1.00 60.11  ? 242  LEU B C     1 
ATOM   1840  O  O     . LEU A 1 240 ? 133.655 188.285 103.695 1.00 62.46  ? 242  LEU B O     1 
ATOM   1841  C  CB    . LEU A 1 240 ? 135.353 186.203 105.227 1.00 52.86  ? 242  LEU B CB    1 
ATOM   1842  C  CG    . LEU A 1 240 ? 135.468 184.689 105.119 1.00 54.43  ? 242  LEU B CG    1 
ATOM   1843  C  CD1   . LEU A 1 240 ? 135.115 184.037 106.437 1.00 56.31  ? 242  LEU B CD1   1 
ATOM   1844  C  CD2   . LEU A 1 240 ? 134.559 184.195 104.028 1.00 56.59  ? 242  LEU B CD2   1 
ATOM   1845  N  N     . ARG A 1 241 ? 135.480 189.424 104.355 1.00 58.51  ? 243  ARG B N     1 
ATOM   1846  C  CA    . ARG A 1 241 ? 134.769 190.666 104.609 1.00 50.80  ? 243  ARG B CA    1 
ATOM   1847  C  C     . ARG A 1 241 ? 135.058 191.766 103.605 1.00 53.25  ? 243  ARG B C     1 
ATOM   1848  O  O     . ARG A 1 241 ? 134.201 192.623 103.390 1.00 62.40  ? 243  ARG B O     1 
ATOM   1849  C  CB    . ARG A 1 241 ? 135.105 191.187 106.010 1.00 51.76  ? 243  ARG B CB    1 
ATOM   1850  C  CG    . ARG A 1 241 ? 134.714 190.246 107.131 1.00 58.54  ? 243  ARG B CG    1 
ATOM   1851  C  CD    . ARG A 1 241 ? 135.227 190.748 108.463 1.00 60.62  ? 243  ARG B CD    1 
ATOM   1852  N  NE    . ARG A 1 241 ? 136.671 190.608 108.588 1.00 50.86  ? 243  ARG B NE    1 
ATOM   1853  C  CZ    . ARG A 1 241 ? 137.447 191.454 109.249 1.00 52.95  ? 243  ARG B CZ    1 
ATOM   1854  N  NH1   . ARG A 1 241 ? 136.954 192.536 109.827 1.00 52.44  ? 243  ARG B NH1   1 
ATOM   1855  N  NH2   . ARG A 1 241 ? 138.752 191.214 109.324 1.00 63.06  ? 243  ARG B NH2   1 
ATOM   1856  N  N     . PHE A 1 242 ? 136.235 191.777 102.992 1.00 46.54  ? 244  PHE B N     1 
ATOM   1857  C  CA    . PHE A 1 242 ? 136.568 192.859 102.087 1.00 54.60  ? 244  PHE B CA    1 
ATOM   1858  C  C     . PHE A 1 242 ? 137.053 192.310 100.752 1.00 61.28  ? 244  PHE B C     1 
ATOM   1859  O  O     . PHE A 1 242 ? 137.578 191.195 100.688 1.00 63.91  ? 244  PHE B O     1 
ATOM   1860  C  CB    . PHE A 1 242 ? 137.653 193.767 102.681 1.00 56.23  ? 244  PHE B CB    1 
ATOM   1861  C  CG    . PHE A 1 242 ? 137.225 194.507 103.911 1.00 55.15  ? 244  PHE B CG    1 
ATOM   1862  C  CD1   . PHE A 1 242 ? 136.473 195.661 103.814 1.00 56.53  ? 244  PHE B CD1   1 
ATOM   1863  C  CD2   . PHE A 1 242 ? 137.598 194.063 105.163 1.00 56.51  ? 244  PHE B CD2   1 
ATOM   1864  C  CE1   . PHE A 1 242 ? 136.087 196.347 104.943 1.00 56.53  ? 244  PHE B CE1   1 
ATOM   1865  C  CE2   . PHE A 1 242 ? 137.215 194.746 106.295 1.00 60.21  ? 244  PHE B CE2   1 
ATOM   1866  C  CZ    . PHE A 1 242 ? 136.457 195.890 106.184 1.00 58.60  ? 244  PHE B CZ    1 
ATOM   1867  N  N     . PRO A 1 243 ? 136.888 193.066 99.670  1.00 56.06  ? 245  PRO B N     1 
ATOM   1868  C  CA    . PRO A 1 243 ? 137.407 192.623 98.375  1.00 49.47  ? 245  PRO B CA    1 
ATOM   1869  C  C     . PRO A 1 243 ? 138.926 192.630 98.341  1.00 53.92  ? 245  PRO B C     1 
ATOM   1870  O  O     . PRO A 1 243 ? 139.595 193.371 99.063  1.00 59.74  ? 245  PRO B O     1 
ATOM   1871  C  CB    . PRO A 1 243 ? 136.826 193.644 97.392  1.00 52.93  ? 245  PRO B CB    1 
ATOM   1872  C  CG    . PRO A 1 243 ? 136.559 194.844 98.216  1.00 55.89  ? 245  PRO B CG    1 
ATOM   1873  C  CD    . PRO A 1 243 ? 136.143 194.330 99.556  1.00 57.38  ? 245  PRO B CD    1 
ATOM   1874  N  N     . GLY A 1 244 ? 139.469 191.780 97.474  1.00 56.74  ? 246  GLY B N     1 
ATOM   1875  C  CA    . GLY A 1 244 ? 140.907 191.691 97.306  1.00 60.09  ? 246  GLY B CA    1 
ATOM   1876  C  C     . GLY A 1 244 ? 141.250 191.031 95.991  1.00 59.18  ? 246  GLY B C     1 
ATOM   1877  O  O     . GLY A 1 244 ? 140.413 190.393 95.350  1.00 65.62  ? 246  GLY B O     1 
ATOM   1878  N  N     . GLN A 1 245 ? 142.512 191.201 95.592  1.00 50.43  ? 247  GLN B N     1 
ATOM   1879  C  CA    . GLN A 1 245 ? 142.971 190.633 94.330  1.00 45.31  ? 247  GLN B CA    1 
ATOM   1880  C  C     . GLN A 1 245 ? 142.982 189.113 94.377  1.00 51.43  ? 247  GLN B C     1 
ATOM   1881  O  O     . GLN A 1 245 ? 142.651 188.453 93.385  1.00 59.04  ? 247  GLN B O     1 
ATOM   1882  C  CB    . GLN A 1 245 ? 144.359 191.165 93.988  1.00 50.60  ? 247  GLN B CB    1 
ATOM   1883  C  CG    . GLN A 1 245 ? 144.376 192.620 93.571  1.00 59.69  ? 247  GLN B CG    1 
ATOM   1884  C  CD    . GLN A 1 245 ? 145.773 193.123 93.281  1.00 65.77  ? 247  GLN B CD    1 
ATOM   1885  O  OE1   . GLN A 1 245 ? 146.759 192.555 93.747  1.00 69.44  ? 247  GLN B OE1   1 
ATOM   1886  N  NE2   . GLN A 1 245 ? 145.865 194.198 92.506  1.00 60.88  ? 247  GLN B NE2   1 
ATOM   1887  N  N     . LEU A 1 246 ? 143.360 188.541 95.514  1.00 53.05  ? 248  LEU B N     1 
ATOM   1888  C  CA    . LEU A 1 246 ? 143.465 187.097 95.659  1.00 54.32  ? 248  LEU B CA    1 
ATOM   1889  C  C     . LEU A 1 246 ? 142.880 186.700 97.004  1.00 53.54  ? 248  LEU B C     1 
ATOM   1890  O  O     . LEU A 1 246 ? 143.504 186.924 98.045  1.00 60.01  ? 248  LEU B O     1 
ATOM   1891  C  CB    . LEU A 1 246 ? 144.924 186.652 95.541  1.00 50.95  ? 248  LEU B CB    1 
ATOM   1892  C  CG    . LEU A 1 246 ? 145.216 185.178 95.304  1.00 50.54  ? 248  LEU B CG    1 
ATOM   1893  C  CD1   . LEU A 1 246 ? 144.386 184.650 94.152  1.00 51.99  ? 248  LEU B CD1   1 
ATOM   1894  C  CD2   . LEU A 1 246 ? 146.684 185.031 95.005  1.00 51.56  ? 248  LEU B CD2   1 
ATOM   1895  N  N     . ASN A 1 247 ? 141.688 186.112 96.978  1.00 48.88  ? 249  ASN B N     1 
ATOM   1896  C  CA    . ASN A 1 247 ? 140.895 185.870 98.173  1.00 49.91  ? 249  ASN B CA    1 
ATOM   1897  C  C     . ASN A 1 247 ? 141.117 184.456 98.689  1.00 51.60  ? 249  ASN B C     1 
ATOM   1898  O  O     . ASN A 1 247 ? 141.234 183.509 97.906  1.00 57.10  ? 249  ASN B O     1 
ATOM   1899  C  CB    . ASN A 1 247 ? 139.406 186.084 97.894  1.00 58.09  ? 249  ASN B CB    1 
ATOM   1900  C  CG    . ASN A 1 247 ? 139.117 187.430 97.267  1.00 61.27  ? 249  ASN B CG    1 
ATOM   1901  O  OD1   . ASN A 1 247 ? 138.484 187.514 96.216  1.00 58.85  ? 249  ASN B OD1   1 
ATOM   1902  N  ND2   . ASN A 1 247 ? 139.579 188.493 97.911  1.00 62.89  ? 249  ASN B ND2   1 
ATOM   1903  N  N     . ALA A 1 248 ? 141.175 184.323 100.011 1.00 52.41  ? 250  ALA B N     1 
ATOM   1904  C  CA    . ALA A 1 248 ? 141.340 183.036 100.671 1.00 55.72  ? 250  ALA B CA    1 
ATOM   1905  C  C     . ALA A 1 248 ? 140.395 182.955 101.858 1.00 58.81  ? 250  ALA B C     1 
ATOM   1906  O  O     . ALA A 1 248 ? 140.474 183.776 102.776 1.00 54.29  ? 250  ALA B O     1 
ATOM   1907  C  CB    . ALA A 1 248 ? 142.784 182.832 101.128 1.00 53.26  ? 250  ALA B CB    1 
ATOM   1908  N  N     . ASP A 1 249 ? 139.510 181.963 101.839 1.00 66.90  ? 251  ASP B N     1 
ATOM   1909  C  CA    . ASP A 1 249 ? 138.578 181.727 102.927 1.00 65.20  ? 251  ASP B CA    1 
ATOM   1910  C  C     . ASP A 1 249 ? 139.263 180.926 104.032 1.00 67.28  ? 251  ASP B C     1 
ATOM   1911  O  O     . ASP A 1 249 ? 140.444 180.583 103.947 1.00 72.37  ? 251  ASP B O     1 
ATOM   1912  C  CB    . ASP A 1 249 ? 137.336 181.004 102.409 1.00 64.63  ? 251  ASP B CB    1 
ATOM   1913  C  CG    . ASP A 1 249 ? 136.124 181.206 103.298 1.00 71.68  ? 251  ASP B CG    1 
ATOM   1914  O  OD1   . ASP A 1 249 ? 136.304 181.461 104.508 1.00 74.86  ? 251  ASP B OD1   1 
ATOM   1915  O  OD2   . ASP A 1 249 ? 134.989 181.108 102.787 1.00 69.84  ? 251  ASP B OD2   1 
ATOM   1916  N  N     . LEU A 1 250 ? 138.511 180.627 105.093 1.00 51.88  ? 252  LEU B N     1 
ATOM   1917  C  CA    . LEU A 1 250 ? 139.041 179.778 106.154 1.00 53.38  ? 252  LEU B CA    1 
ATOM   1918  C  C     . LEU A 1 250 ? 139.324 178.374 105.641 1.00 58.63  ? 252  LEU B C     1 
ATOM   1919  O  O     . LEU A 1 250 ? 140.353 177.775 105.976 1.00 66.35  ? 252  LEU B O     1 
ATOM   1920  C  CB    . LEU A 1 250 ? 138.066 179.730 107.328 1.00 56.62  ? 252  LEU B CB    1 
ATOM   1921  C  CG    . LEU A 1 250 ? 137.824 181.033 108.084 1.00 56.56  ? 252  LEU B CG    1 
ATOM   1922  C  CD1   . LEU A 1 250 ? 136.905 180.797 109.266 1.00 60.01  ? 252  LEU B CD1   1 
ATOM   1923  C  CD2   . LEU A 1 250 ? 139.137 181.636 108.536 1.00 52.39  ? 252  LEU B CD2   1 
ATOM   1924  N  N     . ARG A 1 251 ? 138.423 177.834 104.820 1.00 52.38  ? 253  ARG B N     1 
ATOM   1925  C  CA    . ARG A 1 251 ? 138.619 176.488 104.295 1.00 54.37  ? 253  ARG B CA    1 
ATOM   1926  C  C     . ARG A 1 251 ? 139.777 176.442 103.310 1.00 53.38  ? 253  ARG B C     1 
ATOM   1927  O  O     . ARG A 1 251 ? 140.494 175.439 103.238 1.00 58.69  ? 253  ARG B O     1 
ATOM   1928  C  CB    . ARG A 1 251 ? 137.335 175.986 103.641 1.00 51.15  ? 253  ARG B CB    1 
ATOM   1929  C  CG    . ARG A 1 251 ? 137.405 174.548 103.184 1.00 51.39  ? 253  ARG B CG    1 
ATOM   1930  C  CD    . ARG A 1 251 ? 136.039 174.030 102.812 1.00 51.49  ? 253  ARG B CD    1 
ATOM   1931  N  NE    . ARG A 1 251 ? 135.176 173.902 103.978 1.00 57.16  ? 253  ARG B NE    1 
ATOM   1932  C  CZ    . ARG A 1 251 ? 134.211 174.753 104.293 1.00 62.07  ? 253  ARG B CZ    1 
ATOM   1933  N  NH1   . ARG A 1 251 ? 133.958 175.816 103.548 1.00 60.07  ? 253  ARG B NH1   1 
ATOM   1934  N  NH2   . ARG A 1 251 ? 133.480 174.532 105.382 1.00 61.69  ? 253  ARG B NH2   1 
ATOM   1935  N  N     . LYS A 1 252 ? 139.975 177.510 102.539 1.00 50.40  ? 254  LYS B N     1 
ATOM   1936  C  CA    . LYS A 1 252 ? 141.131 177.574 101.652 1.00 51.83  ? 254  LYS B CA    1 
ATOM   1937  C  C     . LYS A 1 252 ? 142.427 177.549 102.451 1.00 50.77  ? 254  LYS B C     1 
ATOM   1938  O  O     . LYS A 1 252 ? 143.377 176.835 102.099 1.00 58.07  ? 254  LYS B O     1 
ATOM   1939  C  CB    . LYS A 1 252 ? 141.040 178.831 100.790 1.00 51.94  ? 254  LYS B CB    1 
ATOM   1940  C  CG    . LYS A 1 252 ? 142.002 178.886 99.627  1.00 55.79  ? 254  LYS B CG    1 
ATOM   1941  C  CD    . LYS A 1 252 ? 141.518 179.897 98.603  1.00 52.56  ? 254  LYS B CD    1 
ATOM   1942  C  CE    . LYS A 1 252 ? 142.549 180.144 97.522  1.00 54.91  ? 254  LYS B CE    1 
ATOM   1943  N  NZ    . LYS A 1 252 ? 142.024 181.041 96.458  1.00 54.95  ? 254  LYS B NZ    1 
ATOM   1944  N  N     . LEU A 1 253 ? 142.470 178.307 103.548 1.00 46.92  ? 255  LEU B N     1 
ATOM   1945  C  CA    . LEU A 1 253 ? 143.629 178.289 104.430 1.00 46.05  ? 255  LEU B CA    1 
ATOM   1946  C  C     . LEU A 1 253 ? 143.850 176.903 105.017 1.00 52.10  ? 255  LEU B C     1 
ATOM   1947  O  O     . LEU A 1 253 ? 144.989 176.431 105.097 1.00 60.40  ? 255  LEU B O     1 
ATOM   1948  C  CB    . LEU A 1 253 ? 143.444 179.318 105.544 1.00 47.86  ? 255  LEU B CB    1 
ATOM   1949  C  CG    . LEU A 1 253 ? 144.227 180.626 105.454 1.00 51.59  ? 255  LEU B CG    1 
ATOM   1950  C  CD1   . LEU A 1 253 ? 144.039 181.267 104.104 1.00 50.50  ? 255  LEU B CD1   1 
ATOM   1951  C  CD2   . LEU A 1 253 ? 143.784 181.570 106.550 1.00 54.71  ? 255  LEU B CD2   1 
ATOM   1952  N  N     . ALA A 1 254 ? 142.774 176.236 105.435 1.00 55.09  ? 256  ALA B N     1 
ATOM   1953  C  CA    . ALA A 1 254 ? 142.912 174.899 106.002 1.00 50.31  ? 256  ALA B CA    1 
ATOM   1954  C  C     . ALA A 1 254 ? 143.425 173.907 104.967 1.00 53.02  ? 256  ALA B C     1 
ATOM   1955  O  O     . ALA A 1 254 ? 144.289 173.076 105.268 1.00 57.31  ? 256  ALA B O     1 
ATOM   1956  C  CB    . ALA A 1 254 ? 141.576 174.429 106.575 1.00 51.97  ? 256  ALA B CB    1 
ATOM   1957  N  N     . VAL A 1 255 ? 142.899 173.974 103.743 1.00 52.34  ? 257  VAL B N     1 
ATOM   1958  C  CA    . VAL A 1 255 ? 143.324 173.053 102.694 1.00 42.92  ? 257  VAL B CA    1 
ATOM   1959  C  C     . VAL A 1 255 ? 144.793 173.261 102.367 1.00 42.27  ? 257  VAL B C     1 
ATOM   1960  O  O     . VAL A 1 255 ? 145.552 172.298 102.210 1.00 50.78  ? 257  VAL B O     1 
ATOM   1961  C  CB    . VAL A 1 255 ? 142.440 173.216 101.445 1.00 40.21  ? 257  VAL B CB    1 
ATOM   1962  C  CG1   . VAL A 1 255 ? 143.056 172.494 100.268 1.00 40.98  ? 257  VAL B CG1   1 
ATOM   1963  C  CG2   . VAL A 1 255 ? 141.048 172.681 101.716 1.00 52.98  ? 257  VAL B CG2   1 
ATOM   1964  N  N     . ASN A 1 256 ? 145.222 174.517 102.264 1.00 45.26  ? 258  ASN B N     1 
ATOM   1965  C  CA    . ASN A 1 256 ? 146.617 174.767 101.926 1.00 43.05  ? 258  ASN B CA    1 
ATOM   1966  C  C     . ASN A 1 256 ? 147.549 174.400 103.074 1.00 50.24  ? 258  ASN B C     1 
ATOM   1967  O  O     . ASN A 1 256 ? 148.623 173.835 102.846 1.00 55.96  ? 258  ASN B O     1 
ATOM   1968  C  CB    . ASN A 1 256 ? 146.800 176.226 101.524 1.00 43.82  ? 258  ASN B CB    1 
ATOM   1969  C  CG    . ASN A 1 256 ? 146.205 176.527 100.172 1.00 49.54  ? 258  ASN B CG    1 
ATOM   1970  O  OD1   . ASN A 1 256 ? 146.913 176.586 99.169  1.00 49.08  ? 258  ASN B OD1   1 
ATOM   1971  N  ND2   . ASN A 1 256 ? 144.892 176.706 100.132 1.00 56.35  ? 258  ASN B ND2   1 
ATOM   1972  N  N     . MET A 1 257 ? 147.152 174.689 104.312 1.00 54.37  ? 259  MET B N     1 
ATOM   1973  C  CA    . MET A 1 257 ? 148.065 174.655 105.446 1.00 50.72  ? 259  MET B CA    1 
ATOM   1974  C  C     . MET A 1 257 ? 148.031 173.359 106.244 1.00 52.80  ? 259  MET B C     1 
ATOM   1975  O  O     . MET A 1 257 ? 148.879 173.174 107.120 1.00 59.99  ? 259  MET B O     1 
ATOM   1976  C  CB    . MET A 1 257 ? 147.774 175.828 106.382 1.00 46.45  ? 259  MET B CB    1 
ATOM   1977  C  CG    . MET A 1 257 ? 148.370 177.135 105.926 1.00 50.31  ? 259  MET B CG    1 
ATOM   1978  S  SD    . MET A 1 257 ? 148.619 178.256 107.305 1.00 81.85  ? 259  MET B SD    1 
ATOM   1979  C  CE    . MET A 1 257 ? 149.735 177.296 108.323 1.00 53.40  ? 259  MET B CE    1 
ATOM   1980  N  N     . VAL A 1 258 ? 147.092 172.461 105.975 1.00 46.09  ? 260  VAL B N     1 
ATOM   1981  C  CA    . VAL A 1 258 ? 147.003 171.224 106.746 1.00 42.90  ? 260  VAL B CA    1 
ATOM   1982  C  C     . VAL A 1 258 ? 147.316 170.047 105.831 1.00 49.11  ? 260  VAL B C     1 
ATOM   1983  O  O     . VAL A 1 258 ? 146.423 169.556 105.125 1.00 55.18  ? 260  VAL B O     1 
ATOM   1984  C  CB    . VAL A 1 258 ? 145.621 171.072 107.400 1.00 44.40  ? 260  VAL B CB    1 
ATOM   1985  C  CG1   . VAL A 1 258 ? 145.555 169.800 108.217 1.00 42.02  ? 260  VAL B CG1   1 
ATOM   1986  C  CG2   . VAL A 1 258 ? 145.314 172.274 108.275 1.00 50.57  ? 260  VAL B CG2   1 
ATOM   1987  N  N     . PRO A 1 259 ? 148.562 169.568 105.801 1.00 45.33  ? 261  PRO B N     1 
ATOM   1988  C  CA    . PRO A 1 259 ? 148.870 168.423 104.929 1.00 43.54  ? 261  PRO B CA    1 
ATOM   1989  C  C     . PRO A 1 259 ? 148.298 167.119 105.440 1.00 46.16  ? 261  PRO B C     1 
ATOM   1990  O  O     . PRO A 1 259 ? 147.786 166.318 104.649 1.00 51.92  ? 261  PRO B O     1 
ATOM   1991  C  CB    . PRO A 1 259 ? 150.404 168.407 104.910 1.00 45.54  ? 261  PRO B CB    1 
ATOM   1992  C  CG    . PRO A 1 259 ? 150.795 169.046 106.180 1.00 47.91  ? 261  PRO B CG    1 
ATOM   1993  C  CD    . PRO A 1 259 ? 149.763 170.094 106.466 1.00 49.92  ? 261  PRO B CD    1 
ATOM   1994  N  N     . PHE A 1 260 ? 148.367 166.883 106.743 1.00 47.78  ? 262  PHE B N     1 
ATOM   1995  C  CA    . PHE A 1 260 ? 147.818 165.690 107.360 1.00 46.35  ? 262  PHE B CA    1 
ATOM   1996  C  C     . PHE A 1 260 ? 146.865 166.092 108.473 1.00 53.70  ? 262  PHE B C     1 
ATOM   1997  O  O     . PHE A 1 260 ? 147.071 167.118 109.129 1.00 60.25  ? 262  PHE B O     1 
ATOM   1998  C  CB    . PHE A 1 260 ? 148.936 164.795 107.907 1.00 48.78  ? 262  PHE B CB    1 
ATOM   1999  C  CG    . PHE A 1 260 ? 149.908 164.352 106.858 1.00 52.61  ? 262  PHE B CG    1 
ATOM   2000  C  CD1   . PHE A 1 260 ? 151.061 165.071 106.615 1.00 55.24  ? 262  PHE B CD1   1 
ATOM   2001  C  CD2   . PHE A 1 260 ? 149.651 163.230 106.093 1.00 54.56  ? 262  PHE B CD2   1 
ATOM   2002  C  CE1   . PHE A 1 260 ? 151.947 164.670 105.643 1.00 52.56  ? 262  PHE B CE1   1 
ATOM   2003  C  CE2   . PHE A 1 260 ? 150.536 162.825 105.118 1.00 55.39  ? 262  PHE B CE2   1 
ATOM   2004  C  CZ    . PHE A 1 260 ? 151.684 163.546 104.894 1.00 54.54  ? 262  PHE B CZ    1 
ATOM   2005  N  N     . PRO A 1 261 ? 145.813 165.302 108.705 1.00 49.33  ? 263  PRO B N     1 
ATOM   2006  C  CA    . PRO A 1 261 ? 144.685 165.806 109.507 1.00 47.64  ? 263  PRO B CA    1 
ATOM   2007  C  C     . PRO A 1 261 ? 145.051 166.259 110.909 1.00 55.68  ? 263  PRO B C     1 
ATOM   2008  O  O     . PRO A 1 261 ? 144.505 167.260 111.388 1.00 60.60  ? 263  PRO B O     1 
ATOM   2009  C  CB    . PRO A 1 261 ? 143.726 164.608 109.534 1.00 48.77  ? 263  PRO B CB    1 
ATOM   2010  C  CG    . PRO A 1 261 ? 144.077 163.817 108.330 1.00 46.44  ? 263  PRO B CG    1 
ATOM   2011  C  CD    . PRO A 1 261 ? 145.556 163.951 108.185 1.00 53.24  ? 263  PRO B CD    1 
ATOM   2012  N  N     . ARG A 1 262 ? 145.961 165.563 111.584 1.00 57.09  ? 264  ARG B N     1 
ATOM   2013  C  CA    . ARG A 1 262 ? 146.244 165.858 112.981 1.00 55.20  ? 264  ARG B CA    1 
ATOM   2014  C  C     . ARG A 1 262 ? 147.238 166.995 113.171 1.00 59.18  ? 264  ARG B C     1 
ATOM   2015  O  O     . ARG A 1 262 ? 147.416 167.453 114.304 1.00 64.28  ? 264  ARG B O     1 
ATOM   2016  C  CB    . ARG A 1 262 ? 146.766 164.607 113.691 1.00 55.41  ? 264  ARG B CB    1 
ATOM   2017  C  CG    . ARG A 1 262 ? 145.717 163.545 113.921 1.00 52.99  ? 264  ARG B CG    1 
ATOM   2018  C  CD    . ARG A 1 262 ? 146.350 162.254 114.390 1.00 52.66  ? 264  ARG B CD    1 
ATOM   2019  N  NE    . ARG A 1 262 ? 147.159 162.450 115.585 1.00 50.64  ? 264  ARG B NE    1 
ATOM   2020  C  CZ    . ARG A 1 262 ? 146.685 162.406 116.821 1.00 54.12  ? 264  ARG B CZ    1 
ATOM   2021  N  NH1   . ARG A 1 262 ? 145.407 162.170 117.061 1.00 53.38  ? 264  ARG B NH1   1 
ATOM   2022  N  NH2   . ARG A 1 262 ? 147.514 162.599 117.840 1.00 57.60  ? 264  ARG B NH2   1 
ATOM   2023  N  N     . LEU A 1 263 ? 147.886 167.460 112.106 1.00 48.29  ? 265  LEU B N     1 
ATOM   2024  C  CA    . LEU A 1 263 ? 148.864 168.542 112.201 1.00 49.37  ? 265  LEU B CA    1 
ATOM   2025  C  C     . LEU A 1 263 ? 148.194 169.847 111.783 1.00 46.73  ? 265  LEU B C     1 
ATOM   2026  O  O     . LEU A 1 263 ? 148.401 170.365 110.688 1.00 50.06  ? 265  LEU B O     1 
ATOM   2027  C  CB    . LEU A 1 263 ? 150.085 168.235 111.346 1.00 48.17  ? 265  LEU B CB    1 
ATOM   2028  C  CG    . LEU A 1 263 ? 150.699 166.850 111.519 1.00 44.91  ? 265  LEU B CG    1 
ATOM   2029  C  CD1   . LEU A 1 263 ? 151.941 166.730 110.661 1.00 45.75  ? 265  LEU B CD1   1 
ATOM   2030  C  CD2   . LEU A 1 263 ? 151.024 166.602 112.976 1.00 49.94  ? 265  LEU B CD2   1 
ATOM   2031  N  N     . HIS A 1 264 ? 147.377 170.388 112.686 1.00 43.93  ? 266  HIS B N     1 
ATOM   2032  C  CA    . HIS A 1 264 ? 146.655 171.626 112.426 1.00 46.99  ? 266  HIS B CA    1 
ATOM   2033  C  C     . HIS A 1 264 ? 146.891 172.653 113.526 1.00 51.89  ? 266  HIS B C     1 
ATOM   2034  O  O     . HIS A 1 264 ? 146.012 173.462 113.826 1.00 54.66  ? 266  HIS B O     1 
ATOM   2035  C  CB    . HIS A 1 264 ? 145.161 171.363 112.252 1.00 45.86  ? 266  HIS B CB    1 
ATOM   2036  C  CG    . HIS A 1 264 ? 144.529 170.658 113.410 1.00 45.25  ? 266  HIS B CG    1 
ATOM   2037  N  ND1   . HIS A 1 264 ? 144.039 169.374 113.319 1.00 47.14  ? 266  HIS B ND1   1 
ATOM   2038  C  CD2   . HIS A 1 264 ? 144.290 171.062 114.678 1.00 47.45  ? 266  HIS B CD2   1 
ATOM   2039  C  CE1   . HIS A 1 264 ? 143.533 169.015 114.484 1.00 43.48  ? 266  HIS B CE1   1 
ATOM   2040  N  NE2   . HIS A 1 264 ? 143.674 170.021 115.326 1.00 42.51  ? 266  HIS B NE2   1 
ATOM   2041  N  N     . PHE A 1 265 ? 148.076 172.641 114.126 1.00 55.45  ? 267  PHE B N     1 
ATOM   2042  C  CA    . PHE A 1 265 ? 148.439 173.589 115.169 1.00 48.29  ? 267  PHE B CA    1 
ATOM   2043  C  C     . PHE A 1 265 ? 149.375 174.627 114.567 1.00 49.98  ? 267  PHE B C     1 
ATOM   2044  O  O     . PHE A 1 265 ? 150.436 174.278 114.040 1.00 59.19  ? 267  PHE B O     1 
ATOM   2045  C  CB    . PHE A 1 265 ? 149.098 172.874 116.346 1.00 49.44  ? 267  PHE B CB    1 
ATOM   2046  C  CG    . PHE A 1 265 ? 148.157 172.007 117.125 1.00 48.68  ? 267  PHE B CG    1 
ATOM   2047  C  CD1   . PHE A 1 265 ? 147.756 170.781 116.631 1.00 51.01  ? 267  PHE B CD1   1 
ATOM   2048  C  CD2   . PHE A 1 265 ? 147.669 172.418 118.349 1.00 55.00  ? 267  PHE B CD2   1 
ATOM   2049  C  CE1   . PHE A 1 265 ? 146.888 169.986 117.338 1.00 49.32  ? 267  PHE B CE1   1 
ATOM   2050  C  CE2   . PHE A 1 265 ? 146.797 171.624 119.061 1.00 55.78  ? 267  PHE B CE2   1 
ATOM   2051  C  CZ    . PHE A 1 265 ? 146.408 170.407 118.554 1.00 49.73  ? 267  PHE B CZ    1 
ATOM   2052  N  N     . PHE A 1 266 ? 148.981 175.894 114.640 1.00 41.79  ? 268  PHE B N     1 
ATOM   2053  C  CA    . PHE A 1 266 ? 149.631 176.952 113.886 1.00 38.16  ? 268  PHE B CA    1 
ATOM   2054  C  C     . PHE A 1 266 ? 150.210 178.008 114.816 1.00 45.74  ? 268  PHE B C     1 
ATOM   2055  O  O     . PHE A 1 266 ? 149.720 178.220 115.928 1.00 59.50  ? 268  PHE B O     1 
ATOM   2056  C  CB    . PHE A 1 266 ? 148.653 177.614 112.914 1.00 48.22  ? 268  PHE B CB    1 
ATOM   2057  C  CG    . PHE A 1 266 ? 148.075 176.673 111.901 1.00 50.25  ? 268  PHE B CG    1 
ATOM   2058  C  CD1   . PHE A 1 266 ? 148.820 175.622 111.407 1.00 56.07  ? 268  PHE B CD1   1 
ATOM   2059  C  CD2   . PHE A 1 266 ? 146.787 176.846 111.437 1.00 46.22  ? 268  PHE B CD2   1 
ATOM   2060  C  CE1   . PHE A 1 266 ? 148.287 174.761 110.476 1.00 56.65  ? 268  PHE B CE1   1 
ATOM   2061  C  CE2   . PHE A 1 266 ? 146.253 175.990 110.505 1.00 47.19  ? 268  PHE B CE2   1 
ATOM   2062  C  CZ    . PHE A 1 266 ? 147.002 174.947 110.026 1.00 53.15  ? 268  PHE B CZ    1 
ATOM   2063  N  N     . MET A 1 267 ? 151.262 178.669 114.342 1.00 53.02  ? 269  MET B N     1 
ATOM   2064  C  CA    . MET A 1 267 ? 151.870 179.793 115.043 1.00 53.72  ? 269  MET B CA    1 
ATOM   2065  C  C     . MET A 1 267 ? 151.495 181.083 114.334 1.00 57.40  ? 269  MET B C     1 
ATOM   2066  O  O     . MET A 1 267 ? 151.954 181.315 113.204 1.00 65.84  ? 269  MET B O     1 
ATOM   2067  C  CB    . MET A 1 267 ? 153.390 179.642 115.099 1.00 55.22  ? 269  MET B CB    1 
ATOM   2068  C  CG    . MET A 1 267 ? 153.865 178.340 115.706 1.00 58.87  ? 269  MET B CG    1 
ATOM   2069  S  SD    . MET A 1 267 ? 155.636 178.356 116.013 1.00 74.17  ? 269  MET B SD    1 
ATOM   2070  C  CE    . MET A 1 267 ? 156.235 178.978 114.447 1.00 58.69  ? 269  MET B CE    1 
ATOM   2071  N  N     . PRO A 1 268 ? 150.681 181.942 114.930 1.00 43.85  ? 270  PRO B N     1 
ATOM   2072  C  CA    . PRO A 1 268 ? 150.280 183.175 114.256 1.00 40.06  ? 270  PRO B CA    1 
ATOM   2073  C  C     . PRO A 1 268 ? 151.313 184.277 114.452 1.00 51.78  ? 270  PRO B C     1 
ATOM   2074  O  O     . PRO A 1 268 ? 152.210 184.194 115.289 1.00 61.51  ? 270  PRO B O     1 
ATOM   2075  C  CB    . PRO A 1 268 ? 148.953 183.528 114.929 1.00 47.91  ? 270  PRO B CB    1 
ATOM   2076  C  CG    . PRO A 1 268 ? 148.976 182.818 116.258 1.00 58.19  ? 270  PRO B CG    1 
ATOM   2077  C  CD    . PRO A 1 268 ? 150.138 181.863 116.293 1.00 55.79  ? 270  PRO B CD    1 
ATOM   2078  N  N     . GLY A 1 269 ? 151.163 185.326 113.649 1.00 54.83  ? 271  GLY B N     1 
ATOM   2079  C  CA    . GLY A 1 269 ? 152.048 186.473 113.707 1.00 48.69  ? 271  GLY B CA    1 
ATOM   2080  C  C     . GLY A 1 269 ? 151.402 187.655 113.023 1.00 51.69  ? 271  GLY B C     1 
ATOM   2081  O  O     . GLY A 1 269 ? 150.363 187.533 112.370 1.00 58.45  ? 271  GLY B O     1 
ATOM   2082  N  N     . PHE A 1 270 ? 152.033 188.814 113.182 1.00 48.16  ? 272  PHE B N     1 
ATOM   2083  C  CA    . PHE A 1 270 ? 151.477 190.048 112.654 1.00 50.58  ? 272  PHE B CA    1 
ATOM   2084  C  C     . PHE A 1 270 ? 152.604 190.985 112.256 1.00 56.39  ? 272  PHE B C     1 
ATOM   2085  O  O     . PHE A 1 270 ? 153.711 190.926 112.796 1.00 64.53  ? 272  PHE B O     1 
ATOM   2086  C  CB    . PHE A 1 270 ? 150.556 190.727 113.675 1.00 57.40  ? 272  PHE B CB    1 
ATOM   2087  C  CG    . PHE A 1 270 ? 149.783 191.886 113.118 1.00 61.83  ? 272  PHE B CG    1 
ATOM   2088  C  CD1   . PHE A 1 270 ? 148.669 191.677 112.329 1.00 62.03  ? 272  PHE B CD1   1 
ATOM   2089  C  CD2   . PHE A 1 270 ? 150.172 193.184 113.385 1.00 57.81  ? 272  PHE B CD2   1 
ATOM   2090  C  CE1   . PHE A 1 270 ? 147.959 192.743 111.817 1.00 57.58  ? 272  PHE B CE1   1 
ATOM   2091  C  CE2   . PHE A 1 270 ? 149.465 194.251 112.875 1.00 57.43  ? 272  PHE B CE2   1 
ATOM   2092  C  CZ    . PHE A 1 270 ? 148.359 194.030 112.093 1.00 54.65  ? 272  PHE B CZ    1 
ATOM   2093  N  N     . ALA A 1 271 ? 152.300 191.856 111.298 1.00 57.33  ? 273  ALA B N     1 
ATOM   2094  C  CA    . ALA A 1 271 ? 153.216 192.890 110.840 1.00 57.46  ? 273  ALA B CA    1 
ATOM   2095  C  C     . ALA A 1 271 ? 152.396 193.962 110.144 1.00 54.65  ? 273  ALA B C     1 
ATOM   2096  O  O     . ALA A 1 271 ? 151.387 193.641 109.508 1.00 61.06  ? 273  ALA B O     1 
ATOM   2097  C  CB    . ALA A 1 271 ? 154.273 192.313 109.890 1.00 57.89  ? 273  ALA B CB    1 
ATOM   2098  N  N     . PRO A 1 272 ? 152.792 195.235 110.240 1.00 50.72  ? 274  PRO B N     1 
ATOM   2099  C  CA    . PRO A 1 272 ? 153.963 195.780 110.931 1.00 57.81  ? 274  PRO B CA    1 
ATOM   2100  C  C     . PRO A 1 272 ? 153.772 195.887 112.436 1.00 68.15  ? 274  PRO B C     1 
ATOM   2101  O  O     . PRO A 1 272 ? 152.653 195.992 112.929 1.00 72.82  ? 274  PRO B O     1 
ATOM   2102  C  CB    . PRO A 1 272 ? 154.113 197.160 110.289 1.00 57.54  ? 274  PRO B CB    1 
ATOM   2103  C  CG    . PRO A 1 272 ? 152.704 197.572 110.021 1.00 60.57  ? 274  PRO B CG    1 
ATOM   2104  C  CD    . PRO A 1 272 ? 151.992 196.304 109.616 1.00 55.78  ? 274  PRO B CD    1 
ATOM   2105  N  N     . LEU A 1 273 ? 154.870 195.861 113.189 1.00 63.86  ? 275  LEU B N     1 
ATOM   2106  C  CA    . LEU A 1 273 ? 154.838 196.040 114.639 1.00 57.14  ? 275  LEU B CA    1 
ATOM   2107  C  C     . LEU A 1 273 ? 156.027 196.921 115.003 1.00 59.74  ? 275  LEU B C     1 
ATOM   2108  O  O     . LEU A 1 273 ? 157.140 196.423 115.197 1.00 63.67  ? 275  LEU B O     1 
ATOM   2109  C  CB    . LEU A 1 273 ? 154.885 194.705 115.370 1.00 54.07  ? 275  LEU B CB    1 
ATOM   2110  C  CG    . LEU A 1 273 ? 153.596 193.887 115.378 1.00 47.55  ? 275  LEU B CG    1 
ATOM   2111  C  CD1   . LEU A 1 273 ? 153.794 192.582 116.119 1.00 51.72  ? 275  LEU B CD1   1 
ATOM   2112  C  CD2   . LEU A 1 273 ? 152.467 194.687 115.994 1.00 53.42  ? 275  LEU B CD2   1 
ATOM   2113  N  N     . THR A 1 274 ? 155.788 198.224 115.090 1.00 64.05  ? 276  THR B N     1 
ATOM   2114  C  CA    . THR A 1 274 ? 156.820 199.191 115.421 1.00 60.83  ? 276  THR B CA    1 
ATOM   2115  C  C     . THR A 1 274 ? 156.421 199.940 116.682 1.00 64.03  ? 276  THR B C     1 
ATOM   2116  O  O     . THR A 1 274 ? 155.284 199.855 117.153 1.00 71.39  ? 276  THR B O     1 
ATOM   2117  C  CB    . THR A 1 274 ? 157.056 200.177 114.272 1.00 64.58  ? 276  THR B CB    1 
ATOM   2118  O  OG1   . THR A 1 274 ? 155.801 200.712 113.840 1.00 67.77  ? 276  THR B OG1   1 
ATOM   2119  C  CG2   . THR A 1 274 ? 157.730 199.478 113.104 1.00 67.82  ? 276  THR B CG2   1 
ATOM   2120  N  N     . SER A 1 275 ? 157.376 200.680 117.228 1.00 62.82  ? 277  SER B N     1 
ATOM   2121  C  CA    . SER A 1 275 ? 157.163 201.491 118.414 1.00 65.49  ? 277  SER B CA    1 
ATOM   2122  C  C     . SER A 1 275 ? 157.014 202.954 118.023 1.00 67.32  ? 277  SER B C     1 
ATOM   2123  O  O     . SER A 1 275 ? 157.636 203.422 117.066 1.00 75.08  ? 277  SER B O     1 
ATOM   2124  C  CB    . SER A 1 275 ? 158.322 201.337 119.400 1.00 67.69  ? 277  SER B CB    1 
ATOM   2125  O  OG    . SER A 1 275 ? 159.546 201.735 118.808 1.00 71.56  ? 277  SER B OG    1 
ATOM   2126  N  N     . ARG A 1 276 ? 156.170 203.669 118.763 1.00 67.21  ? 278  ARG B N     1 
ATOM   2127  C  CA    . ARG A 1 276 ? 156.050 205.103 118.558 1.00 69.16  ? 278  ARG B CA    1 
ATOM   2128  C  C     . ARG A 1 276 ? 157.414 205.756 118.728 1.00 72.90  ? 278  ARG B C     1 
ATOM   2129  O  O     . ARG A 1 276 ? 158.166 205.430 119.650 1.00 77.34  ? 278  ARG B O     1 
ATOM   2130  C  CB    . ARG A 1 276 ? 155.052 205.707 119.544 1.00 76.34  ? 278  ARG B CB    1 
ATOM   2131  C  CG    . ARG A 1 276 ? 153.640 205.163 119.428 1.00 78.60  ? 278  ARG B CG    1 
ATOM   2132  C  CD    . ARG A 1 276 ? 152.692 205.933 120.333 1.00 80.35  ? 278  ARG B CD    1 
ATOM   2133  N  NE    . ARG A 1 276 ? 153.134 205.919 121.723 1.00 80.81  ? 278  ARG B NE    1 
ATOM   2134  C  CZ    . ARG A 1 276 ? 152.531 206.571 122.708 1.00 80.77  ? 278  ARG B CZ    1 
ATOM   2135  N  NH1   . ARG A 1 276 ? 151.451 207.304 122.492 1.00 80.87  ? 278  ARG B NH1   1 
ATOM   2136  N  NH2   . ARG A 1 276 ? 153.026 206.487 123.940 1.00 77.34  ? 278  ARG B NH2   1 
ATOM   2137  N  N     . GLY A 1 277 ? 157.734 206.678 117.829 1.00 73.70  ? 279  GLY B N     1 
ATOM   2138  C  CA    . GLY A 1 277 ? 159.072 207.216 117.755 1.00 73.75  ? 279  GLY B CA    1 
ATOM   2139  C  C     . GLY A 1 277 ? 160.007 206.444 116.853 1.00 72.01  ? 279  GLY B C     1 
ATOM   2140  O  O     . GLY A 1 277 ? 161.161 206.857 116.684 1.00 74.36  ? 279  GLY B O     1 
ATOM   2141  N  N     . SER A 1 278 ? 159.548 205.337 116.271 1.00 74.26  ? 280  SER B N     1 
ATOM   2142  C  CA    . SER A 1 278 ? 160.315 204.599 115.282 1.00 75.25  ? 280  SER B CA    1 
ATOM   2143  C  C     . SER A 1 278 ? 159.577 204.406 113.967 1.00 77.03  ? 280  SER B C     1 
ATOM   2144  O  O     . SER A 1 278 ? 160.167 203.865 113.025 1.00 82.89  ? 280  SER B O     1 
ATOM   2145  C  CB    . SER A 1 278 ? 160.722 203.223 115.832 1.00 77.69  ? 280  SER B CB    1 
ATOM   2146  O  OG    . SER A 1 278 ? 161.451 202.487 114.866 1.00 79.49  ? 280  SER B OG    1 
ATOM   2147  N  N     . GLN A 1 279 ? 158.311 204.818 113.874 1.00 72.30  ? 281  GLN B N     1 
ATOM   2148  C  CA    . GLN A 1 279 ? 157.581 204.698 112.618 1.00 71.47  ? 281  GLN B CA    1 
ATOM   2149  C  C     . GLN A 1 279 ? 158.112 205.653 111.560 1.00 76.03  ? 281  GLN B C     1 
ATOM   2150  O  O     . GLN A 1 279 ? 158.125 205.312 110.372 1.00 80.99  ? 281  GLN B O     1 
ATOM   2151  C  CB    . GLN A 1 279 ? 156.092 204.947 112.847 1.00 74.98  ? 281  GLN B CB    1 
ATOM   2152  C  CG    . GLN A 1 279 ? 155.258 203.686 112.896 1.00 80.67  ? 281  GLN B CG    1 
ATOM   2153  C  CD    . GLN A 1 279 ? 155.327 202.892 111.607 1.00 85.27  ? 281  GLN B CD    1 
ATOM   2154  O  OE1   . GLN A 1 279 ? 155.545 201.680 111.621 1.00 85.74  ? 281  GLN B OE1   1 
ATOM   2155  N  NE2   . GLN A 1 279 ? 155.142 203.573 110.482 1.00 80.77  ? 281  GLN B NE2   1 
ATOM   2156  N  N     . GLN A 1 280 ? 158.546 206.847 111.963 1.00 72.79  ? 282  GLN B N     1 
ATOM   2157  C  CA    . GLN A 1 280 ? 159.107 207.803 111.017 1.00 73.65  ? 282  GLN B CA    1 
ATOM   2158  C  C     . GLN A 1 280 ? 160.404 207.316 110.389 1.00 72.71  ? 282  GLN B C     1 
ATOM   2159  O  O     . GLN A 1 280 ? 160.823 207.872 109.370 1.00 73.14  ? 282  GLN B O     1 
ATOM   2160  C  CB    . GLN A 1 280 ? 159.343 209.147 111.707 1.00 72.92  ? 282  GLN B CB    1 
ATOM   2161  C  CG    . GLN A 1 280 ? 158.180 209.627 112.556 1.00 77.40  ? 282  GLN B CG    1 
ATOM   2162  C  CD    . GLN A 1 280 ? 158.291 209.189 114.002 1.00 82.11  ? 282  GLN B CD    1 
ATOM   2163  O  OE1   . GLN A 1 280 ? 159.362 208.794 114.463 1.00 81.13  ? 282  GLN B OE1   1 
ATOM   2164  N  NE2   . GLN A 1 280 ? 157.181 209.257 114.729 1.00 80.89  ? 282  GLN B NE2   1 
ATOM   2165  N  N     . TYR A 1 281 ? 161.042 206.297 110.964 1.00 60.84  ? 283  TYR B N     1 
ATOM   2166  C  CA    . TYR A 1 281 ? 162.299 205.764 110.463 1.00 56.15  ? 283  TYR B CA    1 
ATOM   2167  C  C     . TYR A 1 281 ? 162.144 204.494 109.642 1.00 63.65  ? 283  TYR B C     1 
ATOM   2168  O  O     . TYR A 1 281 ? 163.066 204.134 108.910 1.00 69.34  ? 283  TYR B O     1 
ATOM   2169  C  CB    . TYR A 1 281 ? 163.254 205.481 111.627 1.00 54.81  ? 283  TYR B CB    1 
ATOM   2170  C  CG    . TYR A 1 281 ? 163.560 206.688 112.479 1.00 58.73  ? 283  TYR B CG    1 
ATOM   2171  C  CD1   . TYR A 1 281 ? 164.279 207.755 111.969 1.00 60.30  ? 283  TYR B CD1   1 
ATOM   2172  C  CD2   . TYR A 1 281 ? 163.135 206.755 113.795 1.00 65.01  ? 283  TYR B CD2   1 
ATOM   2173  C  CE1   . TYR A 1 281 ? 164.563 208.857 112.745 1.00 61.87  ? 283  TYR B CE1   1 
ATOM   2174  C  CE2   . TYR A 1 281 ? 163.413 207.853 114.578 1.00 64.98  ? 283  TYR B CE2   1 
ATOM   2175  C  CZ    . TYR A 1 281 ? 164.127 208.901 114.049 1.00 63.68  ? 283  TYR B CZ    1 
ATOM   2176  O  OH    . TYR A 1 281 ? 164.405 209.998 114.830 1.00 66.00  ? 283  TYR B OH    1 
ATOM   2177  N  N     . ARG A 1 282 ? 161.008 203.810 109.746 1.00 68.13  ? 284  ARG B N     1 
ATOM   2178  C  CA    . ARG A 1 282 ? 160.782 202.582 109.000 1.00 64.25  ? 284  ARG B CA    1 
ATOM   2179  C  C     . ARG A 1 282 ? 160.360 202.901 107.567 1.00 67.42  ? 284  ARG B C     1 
ATOM   2180  O  O     . ARG A 1 282 ? 160.013 204.034 107.224 1.00 74.13  ? 284  ARG B O     1 
ATOM   2181  C  CB    . ARG A 1 282 ? 159.725 201.731 109.699 1.00 64.94  ? 284  ARG B CB    1 
ATOM   2182  C  CG    . ARG A 1 282 ? 159.851 200.241 109.453 1.00 68.95  ? 284  ARG B CG    1 
ATOM   2183  C  CD    . ARG A 1 282 ? 161.235 199.733 109.827 1.00 74.56  ? 284  ARG B CD    1 
ATOM   2184  N  NE    . ARG A 1 282 ? 161.313 199.301 111.218 1.00 77.44  ? 284  ARG B NE    1 
ATOM   2185  C  CZ    . ARG A 1 282 ? 160.704 198.231 111.711 1.00 77.61  ? 284  ARG B CZ    1 
ATOM   2186  N  NH1   . ARG A 1 282 ? 159.963 197.443 110.949 1.00 72.60  ? 284  ARG B NH1   1 
ATOM   2187  N  NH2   . ARG A 1 282 ? 160.846 197.942 113.001 1.00 73.94  ? 284  ARG B NH2   1 
ATOM   2188  N  N     . ALA A 1 283 ? 160.395 201.878 106.718 1.00 72.78  ? 285  ALA B N     1 
ATOM   2189  C  CA    . ALA A 1 283 ? 159.926 201.972 105.341 1.00 71.13  ? 285  ALA B CA    1 
ATOM   2190  C  C     . ALA A 1 283 ? 158.900 200.874 105.117 1.00 72.00  ? 285  ALA B C     1 
ATOM   2191  O  O     . ALA A 1 283 ? 159.258 199.694 105.051 1.00 73.84  ? 285  ALA B O     1 
ATOM   2192  C  CB    . ALA A 1 283 ? 161.083 201.842 104.348 1.00 67.73  ? 285  ALA B CB    1 
ATOM   2193  N  N     . LEU A 1 284 ? 157.633 201.259 105.005 1.00 65.64  ? 286  LEU B N     1 
ATOM   2194  C  CA    . LEU A 1 284 ? 156.541 200.301 104.851 1.00 64.64  ? 286  LEU B CA    1 
ATOM   2195  C  C     . LEU A 1 284 ? 156.532 199.797 103.415 1.00 66.49  ? 286  LEU B C     1 
ATOM   2196  O  O     . LEU A 1 284 ? 156.074 200.486 102.501 1.00 70.55  ? 286  LEU B O     1 
ATOM   2197  C  CB    . LEU A 1 284 ? 155.208 200.934 105.227 1.00 67.83  ? 286  LEU B CB    1 
ATOM   2198  C  CG    . LEU A 1 284 ? 154.683 200.523 106.601 1.00 73.62  ? 286  LEU B CG    1 
ATOM   2199  C  CD1   . LEU A 1 284 ? 153.331 201.162 106.879 1.00 71.49  ? 286  LEU B CD1   1 
ATOM   2200  C  CD2   . LEU A 1 284 ? 154.600 199.010 106.692 1.00 67.02  ? 286  LEU B CD2   1 
ATOM   2201  N  N     . THR A 1 285 ? 157.034 198.583 103.220 1.00 65.86  ? 287  THR B N     1 
ATOM   2202  C  CA    . THR A 1 285 ? 157.045 197.944 101.915 1.00 65.22  ? 287  THR B CA    1 
ATOM   2203  C  C     . THR A 1 285 ? 156.980 196.439 102.126 1.00 66.38  ? 287  THR B C     1 
ATOM   2204  O  O     . THR A 1 285 ? 157.222 195.936 103.225 1.00 74.75  ? 287  THR B O     1 
ATOM   2205  C  CB    . THR A 1 285 ? 158.283 198.340 101.105 1.00 68.70  ? 287  THR B CB    1 
ATOM   2206  O  OG1   . THR A 1 285 ? 158.224 197.731 99.810  1.00 71.24  ? 287  THR B OG1   1 
ATOM   2207  C  CG2   . THR A 1 285 ? 159.550 197.896 101.815 1.00 68.58  ? 287  THR B CG2   1 
ATOM   2208  N  N     . VAL A 1 286 ? 156.631 195.723 101.055 1.00 53.16  ? 288  VAL B N     1 
ATOM   2209  C  CA    . VAL A 1 286 ? 156.459 194.271 101.161 1.00 55.53  ? 288  VAL B CA    1 
ATOM   2210  C  C     . VAL A 1 286 ? 157.719 193.568 101.647 1.00 64.68  ? 288  VAL B C     1 
ATOM   2211  O  O     . VAL A 1 286 ? 157.604 192.662 102.486 1.00 73.88  ? 288  VAL B O     1 
ATOM   2212  C  CB    . VAL A 1 286 ? 155.923 193.705 99.840  1.00 57.92  ? 288  VAL B CB    1 
ATOM   2213  C  CG1   . VAL A 1 286 ? 155.839 192.192 99.904  1.00 60.97  ? 288  VAL B CG1   1 
ATOM   2214  C  CG2   . VAL A 1 286 ? 154.563 194.296 99.532  1.00 56.82  ? 288  VAL B CG2   1 
ATOM   2215  N  N     . PRO A 1 287 ? 158.930 193.888 101.169 1.00 54.68  ? 289  PRO B N     1 
ATOM   2216  C  CA    . PRO A 1 287 ? 160.116 193.211 101.724 1.00 58.52  ? 289  PRO B CA    1 
ATOM   2217  C  C     . PRO A 1 287 ? 160.284 193.389 103.224 1.00 64.38  ? 289  PRO B C     1 
ATOM   2218  O  O     . PRO A 1 287 ? 160.600 192.420 103.928 1.00 68.34  ? 289  PRO B O     1 
ATOM   2219  C  CB    . PRO A 1 287 ? 161.271 193.849 100.943 1.00 56.00  ? 289  PRO B CB    1 
ATOM   2220  C  CG    . PRO A 1 287 ? 160.664 194.263 99.669  1.00 54.01  ? 289  PRO B CG    1 
ATOM   2221  C  CD    . PRO A 1 287 ? 159.287 194.722 100.008 1.00 53.48  ? 289  PRO B CD    1 
ATOM   2222  N  N     . GLU A 1 288 ? 160.073 194.603 103.738 1.00 62.80  ? 290  GLU B N     1 
ATOM   2223  C  CA    . GLU A 1 288 ? 160.180 194.828 105.175 1.00 59.97  ? 290  GLU B CA    1 
ATOM   2224  C  C     . GLU A 1 288 ? 159.109 194.055 105.929 1.00 58.71  ? 290  GLU B C     1 
ATOM   2225  O  O     . GLU A 1 288 ? 159.378 193.458 106.981 1.00 68.73  ? 290  GLU B O     1 
ATOM   2226  C  CB    . GLU A 1 288 ? 160.083 196.323 105.476 1.00 58.59  ? 290  GLU B CB    1 
ATOM   2227  C  CG    . GLU A 1 288 ? 159.671 196.656 106.900 1.00 68.70  ? 290  GLU B CG    1 
ATOM   2228  C  CD    . GLU A 1 288 ? 160.664 196.150 107.929 1.00 74.35  ? 290  GLU B CD    1 
ATOM   2229  O  OE1   . GLU A 1 288 ? 161.884 196.255 107.683 1.00 72.51  ? 290  GLU B OE1   1 
ATOM   2230  O  OE2   . GLU A 1 288 ? 160.225 195.649 108.985 1.00 70.08  ? 290  GLU B OE2   1 
ATOM   2231  N  N     . LEU A 1 289 ? 157.889 194.045 105.395 1.00 45.09  ? 291  LEU B N     1 
ATOM   2232  C  CA    . LEU A 1 289 ? 156.802 193.310 106.024 1.00 46.66  ? 291  LEU B CA    1 
ATOM   2233  C  C     . LEU A 1 289 ? 157.118 191.823 106.088 1.00 51.30  ? 291  LEU B C     1 
ATOM   2234  O  O     . LEU A 1 289 ? 156.867 191.171 107.105 1.00 60.13  ? 291  LEU B O     1 
ATOM   2235  C  CB    . LEU A 1 289 ? 155.510 193.551 105.248 1.00 54.20  ? 291  LEU B CB    1 
ATOM   2236  C  CG    . LEU A 1 289 ? 154.196 193.581 106.018 1.00 60.26  ? 291  LEU B CG    1 
ATOM   2237  C  CD1   . LEU A 1 289 ? 154.287 194.577 107.155 1.00 62.35  ? 291  LEU B CD1   1 
ATOM   2238  C  CD2   . LEU A 1 289 ? 153.059 193.933 105.084 1.00 61.77  ? 291  LEU B CD2   1 
ATOM   2239  N  N     . THR A 1 290 ? 157.690 191.274 105.015 1.00 55.62  ? 292  THR B N     1 
ATOM   2240  C  CA    . THR A 1 290 ? 158.016 189.851 104.990 1.00 57.15  ? 292  THR B CA    1 
ATOM   2241  C  C     . THR A 1 290 ? 159.164 189.525 105.937 1.00 58.14  ? 292  THR B C     1 
ATOM   2242  O  O     . THR A 1 290 ? 159.143 188.487 106.613 1.00 65.48  ? 292  THR B O     1 
ATOM   2243  C  CB    . THR A 1 290 ? 158.355 189.418 103.566 1.00 57.02  ? 292  THR B CB    1 
ATOM   2244  O  OG1   . THR A 1 290 ? 157.425 190.009 102.653 1.00 61.47  ? 292  THR B OG1   1 
ATOM   2245  C  CG2   . THR A 1 290 ? 158.276 187.909 103.444 1.00 59.20  ? 292  THR B CG2   1 
ATOM   2246  N  N     . GLN A 1 291 ? 160.177 190.393 105.996 1.00 58.61  ? 293  GLN B N     1 
ATOM   2247  C  CA    . GLN A 1 291 ? 161.268 190.189 106.943 1.00 56.60  ? 293  GLN B CA    1 
ATOM   2248  C  C     . GLN A 1 291 ? 160.748 190.181 108.372 1.00 60.54  ? 293  GLN B C     1 
ATOM   2249  O  O     . GLN A 1 291 ? 161.160 189.354 109.192 1.00 63.27  ? 293  GLN B O     1 
ATOM   2250  C  CB    . GLN A 1 291 ? 162.334 191.269 106.763 1.00 56.33  ? 293  GLN B CB    1 
ATOM   2251  C  CG    . GLN A 1 291 ? 163.622 190.778 106.122 1.00 66.96  ? 293  GLN B CG    1 
ATOM   2252  C  CD    . GLN A 1 291 ? 164.546 190.071 107.101 1.00 74.52  ? 293  GLN B CD    1 
ATOM   2253  O  OE1   . GLN A 1 291 ? 164.097 189.420 108.044 1.00 76.27  ? 293  GLN B OE1   1 
ATOM   2254  N  NE2   . GLN A 1 291 ? 165.849 190.200 106.878 1.00 68.31  ? 293  GLN B NE2   1 
ATOM   2255  N  N     . GLN A 1 292 ? 159.836 191.103 108.689 1.00 62.04  ? 294  GLN B N     1 
ATOM   2256  C  CA    . GLN A 1 292 ? 159.217 191.098 110.010 1.00 58.74  ? 294  GLN B CA    1 
ATOM   2257  C  C     . GLN A 1 292 ? 158.402 189.830 110.236 1.00 64.31  ? 294  GLN B C     1 
ATOM   2258  O  O     . GLN A 1 292 ? 158.450 189.241 111.321 1.00 73.95  ? 294  GLN B O     1 
ATOM   2259  C  CB    . GLN A 1 292 ? 158.336 192.333 110.179 1.00 57.00  ? 294  GLN B CB    1 
ATOM   2260  C  CG    . GLN A 1 292 ? 158.007 192.663 111.615 1.00 56.08  ? 294  GLN B CG    1 
ATOM   2261  C  CD    . GLN A 1 292 ? 157.782 194.141 111.830 1.00 64.16  ? 294  GLN B CD    1 
ATOM   2262  O  OE1   . GLN A 1 292 ? 157.188 194.550 112.826 1.00 64.97  ? 294  GLN B OE1   1 
ATOM   2263  N  NE2   . GLN A 1 292 ? 158.250 194.953 110.892 1.00 64.12  ? 294  GLN B NE2   1 
ATOM   2264  N  N     . MET A 1 293 ? 157.648 189.397 109.223 1.00 63.65  ? 295  MET B N     1 
ATOM   2265  C  CA    . MET A 1 293 ? 156.770 188.244 109.383 1.00 58.01  ? 295  MET B CA    1 
ATOM   2266  C  C     . MET A 1 293 ? 157.556 186.979 109.683 1.00 60.91  ? 295  MET B C     1 
ATOM   2267  O  O     . MET A 1 293 ? 157.236 186.251 110.628 1.00 65.09  ? 295  MET B O     1 
ATOM   2268  C  CB    . MET A 1 293 ? 155.933 188.039 108.124 1.00 56.72  ? 295  MET B CB    1 
ATOM   2269  C  CG    . MET A 1 293 ? 154.755 188.967 107.973 1.00 62.04  ? 295  MET B CG    1 
ATOM   2270  S  SD    . MET A 1 293 ? 154.072 188.832 106.315 1.00 82.46  ? 295  MET B SD    1 
ATOM   2271  C  CE    . MET A 1 293 ? 153.789 187.070 106.226 1.00 69.05  ? 295  MET B CE    1 
ATOM   2272  N  N     . PHE A 1 294 ? 158.587 186.700 108.893 1.00 55.78  ? 296  PHE B N     1 
ATOM   2273  C  CA    . PHE A 1 294 ? 159.300 185.437 109.019 1.00 59.46  ? 296  PHE B CA    1 
ATOM   2274  C  C     . PHE A 1 294 ? 160.351 185.454 110.117 1.00 65.67  ? 296  PHE B C     1 
ATOM   2275  O  O     . PHE A 1 294 ? 161.030 184.443 110.321 1.00 68.31  ? 296  PHE B O     1 
ATOM   2276  C  CB    . PHE A 1 294 ? 159.938 185.058 107.683 1.00 55.17  ? 296  PHE B CB    1 
ATOM   2277  C  CG    . PHE A 1 294 ? 158.969 184.461 106.709 1.00 55.86  ? 296  PHE B CG    1 
ATOM   2278  C  CD1   . PHE A 1 294 ? 158.150 185.271 105.943 1.00 59.04  ? 296  PHE B CD1   1 
ATOM   2279  C  CD2   . PHE A 1 294 ? 158.861 183.091 106.575 1.00 57.53  ? 296  PHE B CD2   1 
ATOM   2280  C  CE1   . PHE A 1 294 ? 157.251 184.725 105.052 1.00 54.01  ? 296  PHE B CE1   1 
ATOM   2281  C  CE2   . PHE A 1 294 ? 157.965 182.540 105.686 1.00 62.80  ? 296  PHE B CE2   1 
ATOM   2282  C  CZ    . PHE A 1 294 ? 157.158 183.358 104.923 1.00 57.35  ? 296  PHE B CZ    1 
ATOM   2283  N  N     . ASP A 1 295 ? 160.504 186.570 110.822 1.00 67.44  ? 297  ASP B N     1 
ATOM   2284  C  CA    . ASP A 1 295 ? 161.395 186.609 111.970 1.00 60.61  ? 297  ASP B CA    1 
ATOM   2285  C  C     . ASP A 1 295 ? 160.856 185.724 113.085 1.00 61.56  ? 297  ASP B C     1 
ATOM   2286  O  O     . ASP A 1 295 ? 159.650 185.664 113.336 1.00 64.45  ? 297  ASP B O     1 
ATOM   2287  C  CB    . ASP A 1 295 ? 161.554 188.044 112.470 1.00 61.80  ? 297  ASP B CB    1 
ATOM   2288  C  CG    . ASP A 1 295 ? 162.640 188.181 113.514 1.00 71.32  ? 297  ASP B CG    1 
ATOM   2289  O  OD1   . ASP A 1 295 ? 163.428 187.228 113.686 1.00 74.36  ? 297  ASP B OD1   1 
ATOM   2290  O  OD2   . ASP A 1 295 ? 162.707 189.245 114.165 1.00 74.00  ? 297  ASP B OD2   1 
ATOM   2291  N  N     . ALA A 1 296 ? 161.769 185.023 113.758 1.00 64.60  ? 298  ALA B N     1 
ATOM   2292  C  CA    . ALA A 1 296 ? 161.367 184.179 114.876 1.00 64.90  ? 298  ALA B CA    1 
ATOM   2293  C  C     . ALA A 1 296 ? 160.885 185.008 116.056 1.00 64.32  ? 298  ALA B C     1 
ATOM   2294  O  O     . ALA A 1 296 ? 160.079 184.529 116.861 1.00 64.70  ? 298  ALA B O     1 
ATOM   2295  C  CB    . ALA A 1 296 ? 162.525 183.278 115.296 1.00 64.74  ? 298  ALA B CB    1 
ATOM   2296  N  N     . LYS A 1 297 ? 161.365 186.246 116.179 1.00 62.59  ? 299  LYS B N     1 
ATOM   2297  C  CA    . LYS A 1 297 ? 160.939 187.111 117.270 1.00 54.85  ? 299  LYS B CA    1 
ATOM   2298  C  C     . LYS A 1 297 ? 159.478 187.520 117.154 1.00 64.69  ? 299  LYS B C     1 
ATOM   2299  O  O     . LYS A 1 297 ? 158.838 187.775 118.179 1.00 71.62  ? 299  LYS B O     1 
ATOM   2300  C  CB    . LYS A 1 297 ? 161.815 188.360 117.324 1.00 58.42  ? 299  LYS B CB    1 
ATOM   2301  C  CG    . LYS A 1 297 ? 163.303 188.075 117.372 1.00 66.39  ? 299  LYS B CG    1 
ATOM   2302  C  CD    . LYS A 1 297 ? 164.108 189.362 117.300 1.00 67.89  ? 299  LYS B CD    1 
ATOM   2303  C  CE    . LYS A 1 297 ? 165.601 189.080 117.266 1.00 70.03  ? 299  LYS B CE    1 
ATOM   2304  N  NZ    . LYS A 1 297 ? 166.397 190.330 117.124 1.00 66.91  ? 299  LYS B NZ    1 
ATOM   2305  N  N     . ASN A 1 298 ? 158.939 187.590 115.941 1.00 65.99  ? 300  ASN B N     1 
ATOM   2306  C  CA    . ASN A 1 298 ? 157.583 188.072 115.723 1.00 61.69  ? 300  ASN B CA    1 
ATOM   2307  C  C     . ASN A 1 298 ? 156.527 186.995 115.918 1.00 63.93  ? 300  ASN B C     1 
ATOM   2308  O  O     . ASN A 1 298 ? 155.333 187.307 115.881 1.00 68.85  ? 300  ASN B O     1 
ATOM   2309  C  CB    . ASN A 1 298 ? 157.458 188.663 114.318 1.00 57.66  ? 300  ASN B CB    1 
ATOM   2310  C  CG    . ASN A 1 298 ? 156.309 189.633 114.198 1.00 63.58  ? 300  ASN B CG    1 
ATOM   2311  O  OD1   . ASN A 1 298 ? 155.778 190.108 115.199 1.00 69.16  ? 300  ASN B OD1   1 
ATOM   2312  N  ND2   . ASN A 1 298 ? 155.917 189.935 112.968 1.00 63.36  ? 300  ASN B ND2   1 
ATOM   2313  N  N     . MET A 1 299 ? 156.928 185.745 116.120 1.00 57.07  ? 301  MET B N     1 
ATOM   2314  C  CA    . MET A 1 299 ? 155.962 184.687 116.373 1.00 58.76  ? 301  MET B CA    1 
ATOM   2315  C  C     . MET A 1 299 ? 155.299 184.888 117.729 1.00 63.81  ? 301  MET B C     1 
ATOM   2316  O  O     . MET A 1 299 ? 155.895 185.426 118.665 1.00 63.98  ? 301  MET B O     1 
ATOM   2317  C  CB    . MET A 1 299 ? 156.640 183.321 116.324 1.00 62.89  ? 301  MET B CB    1 
ATOM   2318  C  CG    . MET A 1 299 ? 157.374 183.042 115.029 1.00 69.28  ? 301  MET B CG    1 
ATOM   2319  S  SD    . MET A 1 299 ? 156.301 183.109 113.589 1.00 80.34  ? 301  MET B SD    1 
ATOM   2320  C  CE    . MET A 1 299 ? 157.512 183.352 112.295 1.00 64.58  ? 301  MET B CE    1 
ATOM   2321  N  N     . MET A 1 300 ? 154.046 184.450 117.828 1.00 59.33  ? 302  MET B N     1 
ATOM   2322  C  CA    . MET A 1 300 ? 153.277 184.553 119.060 1.00 57.00  ? 302  MET B CA    1 
ATOM   2323  C  C     . MET A 1 300 ? 153.173 183.215 119.782 1.00 59.34  ? 302  MET B C     1 
ATOM   2324  O  O     . MET A 1 300 ? 152.278 183.020 120.608 1.00 67.40  ? 302  MET B O     1 
ATOM   2325  C  CB    . MET A 1 300 ? 151.892 185.128 118.768 1.00 58.72  ? 302  MET B CB    1 
ATOM   2326  C  CG    . MET A 1 300 ? 151.927 186.603 118.401 1.00 60.67  ? 302  MET B CG    1 
ATOM   2327  S  SD    . MET A 1 300 ? 150.306 187.354 118.173 1.00 69.32  ? 302  MET B SD    1 
ATOM   2328  C  CE    . MET A 1 300 ? 149.826 186.662 116.598 1.00 61.74  ? 302  MET B CE    1 
ATOM   2329  N  N     . ALA A 1 301 ? 154.079 182.290 119.479 1.00 59.95  ? 303  ALA B N     1 
ATOM   2330  C  CA    . ALA A 1 301 ? 154.209 181.035 120.200 1.00 60.51  ? 303  ALA B CA    1 
ATOM   2331  C  C     . ALA A 1 301 ? 155.658 180.859 120.628 1.00 62.85  ? 303  ALA B C     1 
ATOM   2332  O  O     . ALA A 1 301 ? 156.584 181.225 119.900 1.00 62.33  ? 303  ALA B O     1 
ATOM   2333  C  CB    . ALA A 1 301 ? 153.762 179.843 119.349 1.00 59.01  ? 303  ALA B CB    1 
ATOM   2334  N  N     . ALA A 1 302 ? 155.849 180.294 121.819 1.00 69.97  ? 304  ALA B N     1 
ATOM   2335  C  CA    . ALA A 1 302 ? 157.190 180.115 122.361 1.00 71.94  ? 304  ALA B CA    1 
ATOM   2336  C  C     . ALA A 1 302 ? 157.839 178.859 121.799 1.00 75.43  ? 304  ALA B C     1 
ATOM   2337  O  O     . ALA A 1 302 ? 158.333 178.013 122.552 1.00 74.77  ? 304  ALA B O     1 
ATOM   2338  C  CB    . ALA A 1 302 ? 157.153 180.054 123.889 1.00 72.28  ? 304  ALA B CB    1 
ATOM   2339  N  N     . CYS A 1 303 ? 157.841 178.735 120.475 1.00 76.70  ? 305  CYS B N     1 
ATOM   2340  C  CA    . CYS A 1 303 ? 158.490 177.624 119.786 1.00 72.89  ? 305  CYS B CA    1 
ATOM   2341  C  C     . CYS A 1 303 ? 159.309 178.224 118.656 1.00 73.33  ? 305  CYS B C     1 
ATOM   2342  O  O     . CYS A 1 303 ? 158.744 178.708 117.671 1.00 80.09  ? 305  CYS B O     1 
ATOM   2343  C  CB    . CYS A 1 303 ? 157.470 176.621 119.253 1.00 71.86  ? 305  CYS B CB    1 
ATOM   2344  S  SG    . CYS A 1 303 ? 156.441 175.861 120.526 1.00 87.81  ? 305  CYS B SG    1 
ATOM   2345  N  N     . ASP A 1 304 ? 160.623 178.201 118.798 1.00 65.53  ? 306  ASP B N     1 
ATOM   2346  C  CA    . ASP A 1 304 ? 161.491 178.822 117.809 1.00 65.59  ? 306  ASP B CA    1 
ATOM   2347  C  C     . ASP A 1 304 ? 161.407 178.054 116.499 1.00 69.31  ? 306  ASP B C     1 
ATOM   2348  O  O     . ASP A 1 304 ? 161.737 176.861 116.472 1.00 72.29  ? 306  ASP B O     1 
ATOM   2349  C  CB    . ASP A 1 304 ? 162.924 178.851 118.322 1.00 64.82  ? 306  ASP B CB    1 
ATOM   2350  C  CG    . ASP A 1 304 ? 163.815 179.769 117.517 1.00 72.34  ? 306  ASP B CG    1 
ATOM   2351  O  OD1   . ASP A 1 304 ? 163.301 180.465 116.620 1.00 74.38  ? 306  ASP B OD1   1 
ATOM   2352  O  OD2   . ASP A 1 304 ? 165.034 179.794 117.782 1.00 70.07  ? 306  ASP B OD2   1 
ATOM   2353  N  N     . PRO A 1 305 ? 160.978 178.678 115.401 1.00 62.79  ? 307  PRO B N     1 
ATOM   2354  C  CA    . PRO A 1 305 ? 160.900 177.944 114.131 1.00 61.77  ? 307  PRO B CA    1 
ATOM   2355  C  C     . PRO A 1 305 ? 162.247 177.490 113.604 1.00 65.26  ? 307  PRO B C     1 
ATOM   2356  O  O     . PRO A 1 305 ? 162.288 176.602 112.744 1.00 68.33  ? 307  PRO B O     1 
ATOM   2357  C  CB    . PRO A 1 305 ? 160.232 178.949 113.184 1.00 62.88  ? 307  PRO B CB    1 
ATOM   2358  C  CG    . PRO A 1 305 ? 160.439 180.277 113.817 1.00 63.05  ? 307  PRO B CG    1 
ATOM   2359  C  CD    . PRO A 1 305 ? 160.423 180.035 115.288 1.00 63.20  ? 307  PRO B CD    1 
ATOM   2360  N  N     . ARG A 1 306 ? 163.351 178.068 114.082 1.00 66.62  ? 308  ARG B N     1 
ATOM   2361  C  CA    . ARG A 1 306 ? 164.664 177.605 113.652 1.00 66.61  ? 308  ARG B CA    1 
ATOM   2362  C  C     . ARG A 1 306 ? 164.928 176.174 114.099 1.00 68.36  ? 308  ARG B C     1 
ATOM   2363  O  O     . ARG A 1 306 ? 165.535 175.396 113.357 1.00 71.90  ? 308  ARG B O     1 
ATOM   2364  C  CB    . ARG A 1 306 ? 165.754 178.537 114.176 1.00 68.79  ? 308  ARG B CB    1 
ATOM   2365  C  CG    . ARG A 1 306 ? 165.522 180.005 113.876 1.00 66.89  ? 308  ARG B CG    1 
ATOM   2366  C  CD    . ARG A 1 306 ? 166.713 180.842 114.317 1.00 74.22  ? 308  ARG B CD    1 
ATOM   2367  N  NE    . ARG A 1 306 ? 166.367 181.797 115.363 1.00 81.18  ? 308  ARG B NE    1 
ATOM   2368  C  CZ    . ARG A 1 306 ? 166.019 183.058 115.145 1.00 78.62  ? 308  ARG B CZ    1 
ATOM   2369  N  NH1   . ARG A 1 306 ? 165.957 183.556 113.921 1.00 73.48  ? 308  ARG B NH1   1 
ATOM   2370  N  NH2   . ARG A 1 306 ? 165.729 183.840 116.181 1.00 74.21  ? 308  ARG B NH2   1 
ATOM   2371  N  N     . HIS A 1 307 ? 164.483 175.806 115.301 1.00 61.82  ? 309  HIS B N     1 
ATOM   2372  C  CA    . HIS A 1 307 ? 164.615 174.433 115.771 1.00 60.75  ? 309  HIS B CA    1 
ATOM   2373  C  C     . HIS A 1 307 ? 163.533 173.560 115.151 1.00 63.48  ? 309  HIS B C     1 
ATOM   2374  O  O     . HIS A 1 307 ? 162.777 172.894 115.864 1.00 67.40  ? 309  HIS B O     1 
ATOM   2375  C  CB    . HIS A 1 307 ? 164.531 174.367 117.297 1.00 61.77  ? 309  HIS B CB    1 
ATOM   2376  C  CG    . HIS A 1 307 ? 165.495 175.271 117.999 1.00 68.87  ? 309  HIS B CG    1 
ATOM   2377  N  ND1   . HIS A 1 307 ? 165.229 176.602 118.236 1.00 70.08  ? 309  HIS B ND1   1 
ATOM   2378  C  CD2   . HIS A 1 307 ? 166.724 175.036 118.514 1.00 69.37  ? 309  HIS B CD2   1 
ATOM   2379  C  CE1   . HIS A 1 307 ? 166.251 177.148 118.870 1.00 67.59  ? 309  HIS B CE1   1 
ATOM   2380  N  NE2   . HIS A 1 307 ? 167.173 176.219 119.050 1.00 69.76  ? 309  HIS B NE2   1 
ATOM   2381  N  N     . GLY A 1 308 ? 163.454 173.561 113.827 1.00 56.79  ? 310  GLY B N     1 
ATOM   2382  C  CA    . GLY A 1 308 ? 162.423 172.820 113.135 1.00 50.44  ? 310  GLY B CA    1 
ATOM   2383  C  C     . GLY A 1 308 ? 162.328 173.280 111.695 1.00 56.20  ? 310  GLY B C     1 
ATOM   2384  O  O     . GLY A 1 308 ? 163.095 174.133 111.244 1.00 67.85  ? 310  GLY B O     1 
ATOM   2385  N  N     . ARG A 1 309 ? 161.368 172.699 110.984 1.00 40.48  ? 311  ARG B N     1 
ATOM   2386  C  CA    . ARG A 1 309 ? 161.138 173.019 109.585 1.00 37.48  ? 311  ARG B CA    1 
ATOM   2387  C  C     . ARG A 1 309 ? 159.671 173.348 109.374 1.00 43.65  ? 311  ARG B C     1 
ATOM   2388  O  O     . ARG A 1 309 ? 158.790 172.700 109.943 1.00 51.67  ? 311  ARG B O     1 
ATOM   2389  C  CB    . ARG A 1 309 ? 161.543 171.864 108.670 1.00 48.25  ? 311  ARG B CB    1 
ATOM   2390  C  CG    . ARG A 1 309 ? 162.939 171.337 108.916 1.00 52.63  ? 311  ARG B CG    1 
ATOM   2391  C  CD    . ARG A 1 309 ? 163.139 169.993 108.247 1.00 51.11  ? 311  ARG B CD    1 
ATOM   2392  N  NE    . ARG A 1 309 ? 163.507 170.125 106.845 1.00 45.69  ? 311  ARG B NE    1 
ATOM   2393  C  CZ    . ARG A 1 309 ? 164.755 170.140 106.401 1.00 49.83  ? 311  ARG B CZ    1 
ATOM   2394  N  NH1   . ARG A 1 309 ? 165.783 170.033 107.226 1.00 52.83  ? 311  ARG B NH1   1 
ATOM   2395  N  NH2   . ARG A 1 309 ? 164.978 170.266 105.097 1.00 50.58  ? 311  ARG B NH2   1 
ATOM   2396  N  N     . TYR A 1 310 ? 159.419 174.363 108.554 1.00 50.74  ? 312  TYR B N     1 
ATOM   2397  C  CA    . TYR A 1 310 ? 158.053 174.741 108.225 1.00 51.92  ? 312  TYR B CA    1 
ATOM   2398  C  C     . TYR A 1 310 ? 157.430 173.710 107.297 1.00 50.03  ? 312  TYR B C     1 
ATOM   2399  O  O     . TYR A 1 310 ? 158.094 173.187 106.397 1.00 59.68  ? 312  TYR B O     1 
ATOM   2400  C  CB    . TYR A 1 310 ? 158.028 176.113 107.559 1.00 49.38  ? 312  TYR B CB    1 
ATOM   2401  C  CG    . TYR A 1 310 ? 158.118 177.276 108.509 1.00 45.70  ? 312  TYR B CG    1 
ATOM   2402  C  CD1   . TYR A 1 310 ? 157.085 177.563 109.383 1.00 44.91  ? 312  TYR B CD1   1 
ATOM   2403  C  CD2   . TYR A 1 310 ? 159.235 178.092 108.525 1.00 46.61  ? 312  TYR B CD2   1 
ATOM   2404  C  CE1   . TYR A 1 310 ? 157.165 178.628 110.249 1.00 53.04  ? 312  TYR B CE1   1 
ATOM   2405  C  CE2   . TYR A 1 310 ? 159.322 179.156 109.384 1.00 42.49  ? 312  TYR B CE2   1 
ATOM   2406  C  CZ    . TYR A 1 310 ? 158.286 179.421 110.244 1.00 53.24  ? 312  TYR B CZ    1 
ATOM   2407  O  OH    . TYR A 1 310 ? 158.372 180.488 111.105 1.00 66.34  ? 312  TYR B OH    1 
ATOM   2408  N  N     . LEU A 1 311 ? 156.152 173.416 107.517 1.00 39.79  ? 313  LEU B N     1 
ATOM   2409  C  CA    . LEU A 1 311 ? 155.413 172.579 106.582 1.00 35.99  ? 313  LEU B CA    1 
ATOM   2410  C  C     . LEU A 1 311 ? 154.666 173.440 105.571 1.00 45.06  ? 313  LEU B C     1 
ATOM   2411  O  O     . LEU A 1 311 ? 154.831 173.281 104.358 1.00 54.36  ? 313  LEU B O     1 
ATOM   2412  C  CB    . LEU A 1 311 ? 154.446 171.671 107.341 1.00 40.71  ? 313  LEU B CB    1 
ATOM   2413  C  CG    . LEU A 1 311 ? 154.845 170.210 107.514 1.00 41.92  ? 313  LEU B CG    1 
ATOM   2414  C  CD1   . LEU A 1 311 ? 156.162 170.113 108.245 1.00 43.14  ? 313  LEU B CD1   1 
ATOM   2415  C  CD2   . LEU A 1 311 ? 153.770 169.465 108.270 1.00 45.00  ? 313  LEU B CD2   1 
ATOM   2416  N  N     . THR A 1 312 ? 153.841 174.363 106.059 1.00 46.36  ? 314  THR B N     1 
ATOM   2417  C  CA    . THR A 1 312 ? 153.092 175.266 105.200 1.00 48.32  ? 314  THR B CA    1 
ATOM   2418  C  C     . THR A 1 312 ? 152.969 176.618 105.888 1.00 48.88  ? 314  THR B C     1 
ATOM   2419  O  O     . THR A 1 312 ? 152.842 176.698 107.111 1.00 55.69  ? 314  THR B O     1 
ATOM   2420  C  CB    . THR A 1 312 ? 151.702 174.718 104.873 1.00 54.14  ? 314  THR B CB    1 
ATOM   2421  O  OG1   . THR A 1 312 ? 151.792 173.321 104.575 1.00 50.44  ? 314  THR B OG1   1 
ATOM   2422  C  CG2   . THR A 1 312 ? 151.129 175.444 103.672 1.00 56.62  ? 314  THR B CG2   1 
ATOM   2423  N  N     . VAL A 1 313 ? 153.002 177.678 105.086 1.00 39.01  ? 315  VAL B N     1 
ATOM   2424  C  CA    . VAL A 1 313 ? 152.956 179.049 105.574 1.00 31.51  ? 315  VAL B CA    1 
ATOM   2425  C  C     . VAL A 1 313 ? 151.902 179.810 104.783 1.00 43.73  ? 315  VAL B C     1 
ATOM   2426  O  O     . VAL A 1 313 ? 151.790 179.644 103.564 1.00 59.42  ? 315  VAL B O     1 
ATOM   2427  C  CB    . VAL A 1 313 ? 154.335 179.731 105.455 1.00 36.10  ? 315  VAL B CB    1 
ATOM   2428  C  CG1   . VAL A 1 313 ? 154.195 181.236 105.350 1.00 44.24  ? 315  VAL B CG1   1 
ATOM   2429  C  CG2   . VAL A 1 313 ? 155.206 179.359 106.634 1.00 45.58  ? 315  VAL B CG2   1 
ATOM   2430  N  N     . ALA A 1 314 ? 151.118 180.630 105.476 1.00 43.71  ? 316  ALA B N     1 
ATOM   2431  C  CA    . ALA A 1 314 ? 150.135 181.495 104.843 1.00 36.40  ? 316  ALA B CA    1 
ATOM   2432  C  C     . ALA A 1 314 ? 150.470 182.947 105.142 1.00 37.81  ? 316  ALA B C     1 
ATOM   2433  O  O     . ALA A 1 314 ? 150.816 183.294 106.275 1.00 48.54  ? 316  ALA B O     1 
ATOM   2434  C  CB    . ALA A 1 314 ? 148.720 181.174 105.317 1.00 39.28  ? 316  ALA B CB    1 
ATOM   2435  N  N     . ALA A 1 315 ? 150.367 183.793 104.122 1.00 32.79  ? 317  ALA B N     1 
ATOM   2436  C  CA    . ALA A 1 315 ? 150.665 185.218 104.239 1.00 34.33  ? 317  ALA B CA    1 
ATOM   2437  C  C     . ALA A 1 315 ? 149.482 186.002 103.684 1.00 48.16  ? 317  ALA B C     1 
ATOM   2438  O  O     . ALA A 1 315 ? 149.365 186.179 102.468 1.00 52.07  ? 317  ALA B O     1 
ATOM   2439  C  CB    . ALA A 1 315 ? 151.953 185.566 103.507 1.00 37.65  ? 317  ALA B CB    1 
ATOM   2440  N  N     . VAL A 1 316 ? 148.610 186.473 104.572 1.00 47.16  ? 318  VAL B N     1 
ATOM   2441  C  CA    . VAL A 1 316 ? 147.388 187.171 104.169 1.00 36.17  ? 318  VAL B CA    1 
ATOM   2442  C  C     . VAL A 1 316 ? 147.699 188.664 104.210 1.00 39.36  ? 318  VAL B C     1 
ATOM   2443  O  O     . VAL A 1 316 ? 147.514 189.335 105.223 1.00 48.94  ? 318  VAL B O     1 
ATOM   2444  C  CB    . VAL A 1 316 ? 146.201 186.799 105.051 1.00 39.63  ? 318  VAL B CB    1 
ATOM   2445  C  CG1   . VAL A 1 316 ? 144.926 187.388 104.487 1.00 42.86  ? 318  VAL B CG1   1 
ATOM   2446  C  CG2   . VAL A 1 316 ? 146.082 185.294 105.159 1.00 43.34  ? 318  VAL B CG2   1 
ATOM   2447  N  N     . PHE A 1 317 ? 148.174 189.188 103.084 1.00 46.31  ? 319  PHE B N     1 
ATOM   2448  C  CA    . PHE A 1 317 ? 148.508 190.597 102.982 1.00 45.72  ? 319  PHE B CA    1 
ATOM   2449  C  C     . PHE A 1 317 ? 147.246 191.449 102.885 1.00 47.92  ? 319  PHE B C     1 
ATOM   2450  O  O     . PHE A 1 317 ? 146.186 190.994 102.449 1.00 58.03  ? 319  PHE B O     1 
ATOM   2451  C  CB    . PHE A 1 317 ? 149.397 190.855 101.770 1.00 46.07  ? 319  PHE B CB    1 
ATOM   2452  C  CG    . PHE A 1 317 ? 150.810 190.400 101.946 1.00 43.83  ? 319  PHE B CG    1 
ATOM   2453  C  CD1   . PHE A 1 317 ? 151.174 189.105 101.645 1.00 46.34  ? 319  PHE B CD1   1 
ATOM   2454  C  CD2   . PHE A 1 317 ? 151.775 191.266 102.417 1.00 47.46  ? 319  PHE B CD2   1 
ATOM   2455  C  CE1   . PHE A 1 317 ? 152.469 188.686 101.802 1.00 48.55  ? 319  PHE B CE1   1 
ATOM   2456  C  CE2   . PHE A 1 317 ? 153.075 190.848 102.578 1.00 47.84  ? 319  PHE B CE2   1 
ATOM   2457  C  CZ    . PHE A 1 317 ? 153.421 189.557 102.269 1.00 48.81  ? 319  PHE B CZ    1 
ATOM   2458  N  N     . ARG A 1 318 ? 147.376 192.707 103.300 1.00 48.41  ? 320  ARG B N     1 
ATOM   2459  C  CA    . ARG A 1 318 ? 146.273 193.654 103.270 1.00 42.21  ? 320  ARG B CA    1 
ATOM   2460  C  C     . ARG A 1 318 ? 146.777 194.996 102.766 1.00 47.38  ? 320  ARG B C     1 
ATOM   2461  O  O     . ARG A 1 318 ? 147.847 195.456 103.173 1.00 59.66  ? 320  ARG B O     1 
ATOM   2462  C  CB    . ARG A 1 318 ? 145.642 193.809 104.653 1.00 48.04  ? 320  ARG B CB    1 
ATOM   2463  C  CG    . ARG A 1 318 ? 144.964 192.550 105.149 1.00 54.86  ? 320  ARG B CG    1 
ATOM   2464  C  CD    . ARG A 1 318 ? 144.246 192.774 106.462 1.00 58.54  ? 320  ARG B CD    1 
ATOM   2465  N  NE    . ARG A 1 318 ? 143.157 193.733 106.336 1.00 60.09  ? 320  ARG B NE    1 
ATOM   2466  C  CZ    . ARG A 1 318 ? 142.450 194.197 107.356 1.00 57.11  ? 320  ARG B CZ    1 
ATOM   2467  N  NH1   . ARG A 1 318 ? 142.692 193.808 108.596 1.00 54.14  ? 320  ARG B NH1   1 
ATOM   2468  N  NH2   . ARG A 1 318 ? 141.476 195.071 107.126 1.00 51.87  ? 320  ARG B NH2   1 
ATOM   2469  N  N     . GLY A 1 319 ? 146.008 195.616 101.885 1.00 60.14  ? 321  GLY B N     1 
ATOM   2470  C  CA    . GLY A 1 319 ? 146.355 196.894 101.300 1.00 60.02  ? 321  GLY B CA    1 
ATOM   2471  C  C     . GLY A 1 319 ? 146.608 196.782 99.807  1.00 65.38  ? 321  GLY B C     1 
ATOM   2472  O  O     . GLY A 1 319 ? 146.339 195.760 99.170  1.00 65.87  ? 321  GLY B O     1 
ATOM   2473  N  N     . ARG A 1 320 ? 147.138 197.867 99.249  1.00 82.62  ? 322  ARG B N     1 
ATOM   2474  C  CA    . ARG A 1 320 ? 147.473 197.942 97.832  1.00 78.44  ? 322  ARG B CA    1 
ATOM   2475  C  C     . ARG A 1 320 ? 148.937 197.569 97.648  1.00 79.70  ? 322  ARG B C     1 
ATOM   2476  O  O     . ARG A 1 320 ? 149.825 198.263 98.153  1.00 82.78  ? 322  ARG B O     1 
ATOM   2477  C  CB    . ARG A 1 320 ? 147.210 199.341 97.276  1.00 76.60  ? 322  ARG B CB    1 
ATOM   2478  C  CG    . ARG A 1 320 ? 145.744 199.690 97.130  1.00 80.08  ? 322  ARG B CG    1 
ATOM   2479  C  CD    . ARG A 1 320 ? 145.564 201.074 96.530  1.00 84.34  ? 322  ARG B CD    1 
ATOM   2480  N  NE    . ARG A 1 320 ? 144.158 201.396 96.318  1.00 86.38  ? 322  ARG B NE    1 
ATOM   2481  C  CZ    . ARG A 1 320 ? 143.716 202.562 95.865  1.00 85.05  ? 322  ARG B CZ    1 
ATOM   2482  N  NH1   . ARG A 1 320 ? 144.547 203.546 95.564  1.00 83.93  ? 322  ARG B NH1   1 
ATOM   2483  N  NH2   . ARG A 1 320 ? 142.408 202.744 95.711  1.00 80.90  ? 322  ARG B NH2   1 
ATOM   2484  N  N     . MET A 1 321 ? 149.185 196.483 96.924  1.00 68.75  ? 323  MET B N     1 
ATOM   2485  C  CA    . MET A 1 321 ? 150.549 196.036 96.697  1.00 66.12  ? 323  MET B CA    1 
ATOM   2486  C  C     . MET A 1 321 ? 150.595 195.193 95.434  1.00 71.20  ? 323  MET B C     1 
ATOM   2487  O  O     . MET A 1 321 ? 149.581 194.654 94.985  1.00 74.20  ? 323  MET B O     1 
ATOM   2488  C  CB    . MET A 1 321 ? 151.081 195.243 97.890  1.00 66.74  ? 323  MET B CB    1 
ATOM   2489  C  CG    . MET A 1 321 ? 150.175 194.117 98.325  1.00 69.17  ? 323  MET B CG    1 
ATOM   2490  S  SD    . MET A 1 321 ? 150.637 193.487 99.939  1.00 86.78  ? 323  MET B SD    1 
ATOM   2491  C  CE    . MET A 1 321 ? 150.443 194.958 100.935 1.00 72.87  ? 323  MET B CE    1 
ATOM   2492  N  N     . SER A 1 322 ? 151.793 195.087 94.872  1.00 68.88  ? 324  SER B N     1 
ATOM   2493  C  CA    . SER A 1 322 ? 152.020 194.316 93.661  1.00 62.11  ? 324  SER B CA    1 
ATOM   2494  C  C     . SER A 1 322 ? 152.034 192.831 93.987  1.00 62.46  ? 324  SER B C     1 
ATOM   2495  O  O     . SER A 1 322 ? 152.632 192.414 94.984  1.00 73.11  ? 324  SER B O     1 
ATOM   2496  C  CB    . SER A 1 322 ? 153.339 194.723 93.010  1.00 66.68  ? 324  SER B CB    1 
ATOM   2497  O  OG    . SER A 1 322 ? 153.542 194.028 91.794  1.00 72.73  ? 324  SER B OG    1 
ATOM   2498  N  N     . MET A 1 323 ? 151.376 192.035 93.146  1.00 57.22  ? 325  MET B N     1 
ATOM   2499  C  CA    . MET A 1 323 ? 151.446 190.588 93.310  1.00 63.28  ? 325  MET B CA    1 
ATOM   2500  C  C     . MET A 1 323 ? 152.835 190.070 92.966  1.00 64.50  ? 325  MET B C     1 
ATOM   2501  O  O     . MET A 1 323 ? 153.314 189.100 93.567  1.00 65.49  ? 325  MET B O     1 
ATOM   2502  C  CB    . MET A 1 323 ? 150.384 189.911 92.448  1.00 62.69  ? 325  MET B CB    1 
ATOM   2503  C  CG    . MET A 1 323 ? 148.966 190.274 92.831  1.00 61.26  ? 325  MET B CG    1 
ATOM   2504  S  SD    . MET A 1 323 ? 148.555 189.726 94.494  1.00 77.74  ? 325  MET B SD    1 
ATOM   2505  C  CE    . MET A 1 323 ? 148.943 187.986 94.375  1.00 65.54  ? 325  MET B CE    1 
ATOM   2506  N  N     . LYS A 1 324 ? 153.496 190.707 91.998  1.00 59.29  ? 326  LYS B N     1 
ATOM   2507  C  CA    . LYS A 1 324 ? 154.868 190.345 91.663  1.00 58.04  ? 326  LYS B CA    1 
ATOM   2508  C  C     . LYS A 1 324 ? 155.789 190.517 92.859  1.00 62.75  ? 326  LYS B C     1 
ATOM   2509  O  O     . LYS A 1 324 ? 156.612 189.642 93.149  1.00 68.33  ? 326  LYS B O     1 
ATOM   2510  C  CB    . LYS A 1 324 ? 155.353 191.192 90.488  1.00 61.84  ? 326  LYS B CB    1 
ATOM   2511  C  CG    . LYS A 1 324 ? 156.853 191.442 90.447  1.00 61.20  ? 326  LYS B CG    1 
ATOM   2512  C  CD    . LYS A 1 324 ? 157.629 190.221 90.008  1.00 62.64  ? 326  LYS B CD    1 
ATOM   2513  C  CE    . LYS A 1 324 ? 159.091 190.563 89.796  1.00 64.45  ? 326  LYS B CE    1 
ATOM   2514  N  NZ    . LYS A 1 324 ? 159.663 191.291 90.959  1.00 64.67  ? 326  LYS B NZ    1 
ATOM   2515  N  N     . GLU A 1 325 ? 155.661 191.639 93.568  1.00 66.39  ? 327  GLU B N     1 
ATOM   2516  C  CA    . GLU A 1 325 ? 156.506 191.881 94.730  1.00 60.13  ? 327  GLU B CA    1 
ATOM   2517  C  C     . GLU A 1 325 ? 156.278 190.818 95.796  1.00 64.62  ? 327  GLU B C     1 
ATOM   2518  O  O     . GLU A 1 325 ? 157.234 190.254 96.341  1.00 74.48  ? 327  GLU B O     1 
ATOM   2519  C  CB    . GLU A 1 325 ? 156.229 193.279 95.282  1.00 60.01  ? 327  GLU B CB    1 
ATOM   2520  C  CG    . GLU A 1 325 ? 157.158 193.718 96.392  1.00 68.76  ? 327  GLU B CG    1 
ATOM   2521  C  CD    . GLU A 1 325 ? 157.223 195.227 96.520  1.00 75.31  ? 327  GLU B CD    1 
ATOM   2522  O  OE1   . GLU A 1 325 ? 157.548 195.892 95.516  1.00 70.28  ? 327  GLU B OE1   1 
ATOM   2523  O  OE2   . GLU A 1 325 ? 156.948 195.750 97.620  1.00 81.52  ? 327  GLU B OE2   1 
ATOM   2524  N  N     . VAL A 1 326 ? 155.012 190.505 96.075  1.00 53.42  ? 328  VAL B N     1 
ATOM   2525  C  CA    . VAL A 1 326 ? 154.692 189.530 97.113  1.00 53.76  ? 328  VAL B CA    1 
ATOM   2526  C  C     . VAL A 1 326 ? 155.238 188.157 96.744  1.00 61.71  ? 328  VAL B C     1 
ATOM   2527  O  O     . VAL A 1 326 ? 155.855 187.470 97.570  1.00 72.23  ? 328  VAL B O     1 
ATOM   2528  C  CB    . VAL A 1 326 ? 153.174 189.487 97.351  1.00 57.49  ? 328  VAL B CB    1 
ATOM   2529  C  CG1   . VAL A 1 326 ? 152.822 188.342 98.271  1.00 60.69  ? 328  VAL B CG1   1 
ATOM   2530  C  CG2   . VAL A 1 326 ? 152.693 190.805 97.927  1.00 64.49  ? 328  VAL B CG2   1 
ATOM   2531  N  N     . ASP A 1 327 ? 155.032 187.740 95.494  1.00 66.48  ? 329  ASP B N     1 
ATOM   2532  C  CA    . ASP A 1 327 ? 155.448 186.399 95.100  1.00 67.19  ? 329  ASP B CA    1 
ATOM   2533  C  C     . ASP A 1 327 ? 156.967 186.282 95.037  1.00 64.55  ? 329  ASP B C     1 
ATOM   2534  O  O     . ASP A 1 327 ? 157.530 185.259 95.442  1.00 65.38  ? 329  ASP B O     1 
ATOM   2535  C  CB    . ASP A 1 327 ? 154.815 186.025 93.764  1.00 68.24  ? 329  ASP B CB    1 
ATOM   2536  C  CG    . ASP A 1 327 ? 154.160 184.661 93.799  1.00 72.87  ? 329  ASP B CG    1 
ATOM   2537  O  OD1   . ASP A 1 327 ? 154.774 183.722 94.346  1.00 72.23  ? 329  ASP B OD1   1 
ATOM   2538  O  OD2   . ASP A 1 327 ? 153.031 184.528 93.282  1.00 71.88  ? 329  ASP B OD2   1 
ATOM   2539  N  N     . GLU A 1 328 ? 157.649 187.320 94.549  1.00 61.68  ? 330  GLU B N     1 
ATOM   2540  C  CA    . GLU A 1 328 ? 159.106 187.309 94.551  1.00 54.20  ? 330  GLU B CA    1 
ATOM   2541  C  C     . GLU A 1 328 ? 159.654 187.264 95.970  1.00 64.90  ? 330  GLU B C     1 
ATOM   2542  O  O     . GLU A 1 328 ? 160.627 186.550 96.246  1.00 76.06  ? 330  GLU B O     1 
ATOM   2543  C  CB    . GLU A 1 328 ? 159.640 188.532 93.809  1.00 58.84  ? 330  GLU B CB    1 
ATOM   2544  C  CG    . GLU A 1 328 ? 161.141 188.520 93.600  1.00 67.52  ? 330  GLU B CG    1 
ATOM   2545  C  CD    . GLU A 1 328 ? 161.656 189.819 93.015  1.00 74.52  ? 330  GLU B CD    1 
ATOM   2546  O  OE1   . GLU A 1 328 ? 161.096 190.885 93.348  1.00 74.68  ? 330  GLU B OE1   1 
ATOM   2547  O  OE2   . GLU A 1 328 ? 162.621 189.776 92.224  1.00 74.12  ? 330  GLU B OE2   1 
ATOM   2548  N  N     . GLN A 1 329 ? 159.045 188.022 96.888  1.00 54.95  ? 331  GLN B N     1 
ATOM   2549  C  CA    . GLN A 1 329 ? 159.504 187.998 98.271  1.00 50.21  ? 331  GLN B CA    1 
ATOM   2550  C  C     . GLN A 1 329 ? 159.303 186.626 98.895  1.00 52.92  ? 331  GLN B C     1 
ATOM   2551  O  O     . GLN A 1 329 ? 160.184 186.123 99.604  1.00 56.87  ? 331  GLN B O     1 
ATOM   2552  C  CB    . GLN A 1 329 ? 158.792 189.076 99.080  1.00 49.43  ? 331  GLN B CB    1 
ATOM   2553  C  CG    . GLN A 1 329 ? 159.237 190.473 98.723  1.00 53.06  ? 331  GLN B CG    1 
ATOM   2554  C  CD    . GLN A 1 329 ? 160.731 190.657 98.869  1.00 60.72  ? 331  GLN B CD    1 
ATOM   2555  O  OE1   . GLN A 1 329 ? 161.386 191.222 97.995  1.00 63.92  ? 331  GLN B OE1   1 
ATOM   2556  N  NE2   . GLN A 1 329 ? 161.278 190.187 99.983  1.00 61.77  ? 331  GLN B NE2   1 
ATOM   2557  N  N     . MET A 1 330 ? 158.159 185.994 98.633  1.00 55.13  ? 332  MET B N     1 
ATOM   2558  C  CA    . MET A 1 330 ? 157.935 184.654 99.164  1.00 56.20  ? 332  MET B CA    1 
ATOM   2559  C  C     . MET A 1 330 ? 158.931 183.655 98.588  1.00 59.11  ? 332  MET B C     1 
ATOM   2560  O  O     . MET A 1 330 ? 159.467 182.806 99.316  1.00 66.31  ? 332  MET B O     1 
ATOM   2561  C  CB    . MET A 1 330 ? 156.501 184.221 98.886  1.00 52.93  ? 332  MET B CB    1 
ATOM   2562  C  CG    . MET A 1 330 ? 155.504 185.011 99.695  1.00 57.93  ? 332  MET B CG    1 
ATOM   2563  S  SD    . MET A 1 330 ? 155.975 185.000 101.431 1.00 80.74  ? 332  MET B SD    1 
ATOM   2564  C  CE    . MET A 1 330 ? 155.097 186.432 102.030 1.00 66.15  ? 332  MET B CE    1 
ATOM   2565  N  N     . LEU A 1 331 ? 159.209 183.751 97.286  1.00 58.21  ? 333  LEU B N     1 
ATOM   2566  C  CA    . LEU A 1 331 ? 160.165 182.840 96.669  1.00 53.95  ? 333  LEU B CA    1 
ATOM   2567  C  C     . LEU A 1 331 ? 161.556 183.010 97.261  1.00 58.27  ? 333  LEU B C     1 
ATOM   2568  O  O     . LEU A 1 331 ? 162.238 182.019 97.553  1.00 65.71  ? 333  LEU B O     1 
ATOM   2569  C  CB    . LEU A 1 331 ? 160.201 183.060 95.158  1.00 55.71  ? 333  LEU B CB    1 
ATOM   2570  C  CG    . LEU A 1 331 ? 160.992 182.027 94.358  1.00 59.03  ? 333  LEU B CG    1 
ATOM   2571  C  CD1   . LEU A 1 331 ? 160.339 180.660 94.458  1.00 57.14  ? 333  LEU B CD1   1 
ATOM   2572  C  CD2   . LEU A 1 331 ? 161.126 182.465 92.911  1.00 59.20  ? 333  LEU B CD2   1 
ATOM   2573  N  N     . ASN A 1 332 ? 162.002 184.254 97.448  1.00 55.26  ? 334  ASN B N     1 
ATOM   2574  C  CA    . ASN A 1 332 ? 163.347 184.441 97.980  1.00 54.21  ? 334  ASN B CA    1 
ATOM   2575  C  C     . ASN A 1 332 ? 163.423 184.056 99.450  1.00 54.20  ? 334  ASN B C     1 
ATOM   2576  O  O     . ASN A 1 332 ? 164.469 183.585 99.908  1.00 61.77  ? 334  ASN B O     1 
ATOM   2577  C  CB    . ASN A 1 332 ? 163.835 185.876 97.744  1.00 57.65  ? 334  ASN B CB    1 
ATOM   2578  C  CG    . ASN A 1 332 ? 163.055 186.918 98.525  1.00 63.64  ? 334  ASN B CG    1 
ATOM   2579  O  OD1   . ASN A 1 332 ? 162.844 186.797 99.731  1.00 67.13  ? 334  ASN B OD1   1 
ATOM   2580  N  ND2   . ASN A 1 332 ? 162.654 187.977 97.834  1.00 64.23  ? 334  ASN B ND2   1 
ATOM   2581  N  N     . VAL A 1 333 ? 162.333 184.227 100.202 1.00 52.41  ? 335  VAL B N     1 
ATOM   2582  C  CA    . VAL A 1 333 ? 162.314 183.750 101.581 1.00 56.43  ? 335  VAL B CA    1 
ATOM   2583  C  C     . VAL A 1 333 ? 162.450 182.235 101.619 1.00 60.55  ? 335  VAL B C     1 
ATOM   2584  O  O     . VAL A 1 333 ? 163.196 181.684 102.438 1.00 64.31  ? 335  VAL B O     1 
ATOM   2585  C  CB    . VAL A 1 333 ? 161.038 184.226 102.299 1.00 54.93  ? 335  VAL B CB    1 
ATOM   2586  C  CG1   . VAL A 1 333 ? 160.733 183.340 103.486 1.00 57.86  ? 335  VAL B CG1   1 
ATOM   2587  C  CG2   . VAL A 1 333 ? 161.200 185.663 102.750 1.00 58.83  ? 335  VAL B CG2   1 
ATOM   2588  N  N     . GLN A 1 334 ? 161.739 181.535 100.731 1.00 58.32  ? 336  GLN B N     1 
ATOM   2589  C  CA    . GLN A 1 334 ? 161.861 180.081 100.687 1.00 53.99  ? 336  GLN B CA    1 
ATOM   2590  C  C     . GLN A 1 334 ? 163.265 179.648 100.280 1.00 54.29  ? 336  GLN B C     1 
ATOM   2591  O  O     . GLN A 1 334 ? 163.809 178.684 100.830 1.00 59.37  ? 336  GLN B O     1 
ATOM   2592  C  CB    . GLN A 1 334 ? 160.829 179.491 99.730  1.00 54.54  ? 336  GLN B CB    1 
ATOM   2593  C  CG    . GLN A 1 334 ? 159.407 179.580 100.222 1.00 56.03  ? 336  GLN B CG    1 
ATOM   2594  C  CD    . GLN A 1 334 ? 158.518 178.556 99.562  1.00 63.42  ? 336  GLN B CD    1 
ATOM   2595  O  OE1   . GLN A 1 334 ? 157.401 178.860 99.149  1.00 61.29  ? 336  GLN B OE1   1 
ATOM   2596  N  NE2   . GLN A 1 334 ? 159.009 177.327 99.460  1.00 63.45  ? 336  GLN B NE2   1 
ATOM   2597  N  N     . ASN A 1 335 ? 163.864 180.340 99.308  1.00 54.63  ? 337  ASN B N     1 
ATOM   2598  C  CA    . ASN A 1 335 ? 165.175 179.929 98.812  1.00 54.39  ? 337  ASN B CA    1 
ATOM   2599  C  C     . ASN A 1 335 ? 166.274 180.194 99.833  1.00 55.69  ? 337  ASN B C     1 
ATOM   2600  O  O     . ASN A 1 335 ? 167.138 179.340 100.059 1.00 58.51  ? 337  ASN B O     1 
ATOM   2601  C  CB    . ASN A 1 335 ? 165.485 180.642 97.498  1.00 58.76  ? 337  ASN B CB    1 
ATOM   2602  C  CG    . ASN A 1 335 ? 164.668 180.109 96.343  1.00 64.81  ? 337  ASN B CG    1 
ATOM   2603  O  OD1   . ASN A 1 335 ? 164.290 178.939 96.324  1.00 65.43  ? 337  ASN B OD1   1 
ATOM   2604  N  ND2   . ASN A 1 335 ? 164.389 180.967 95.369  1.00 61.39  ? 337  ASN B ND2   1 
ATOM   2605  N  N     . LYS A 1 336 ? 166.268 181.374 100.455 1.00 57.31  ? 338  LYS B N     1 
ATOM   2606  C  CA    . LYS A 1 336 ? 167.289 181.706 101.440 1.00 56.80  ? 338  LYS B CA    1 
ATOM   2607  C  C     . LYS A 1 336 ? 167.178 180.876 102.711 1.00 62.64  ? 338  LYS B C     1 
ATOM   2608  O  O     . LYS A 1 336 ? 168.168 180.748 103.438 1.00 67.21  ? 338  LYS B O     1 
ATOM   2609  C  CB    . LYS A 1 336 ? 167.220 183.191 101.798 1.00 60.99  ? 338  LYS B CB    1 
ATOM   2610  C  CG    . LYS A 1 336 ? 167.531 184.124 100.641 1.00 64.58  ? 338  LYS B CG    1 
ATOM   2611  C  CD    . LYS A 1 336 ? 167.708 185.555 101.120 1.00 67.72  ? 338  LYS B CD    1 
ATOM   2612  C  CE    . LYS A 1 336 ? 169.062 185.750 101.784 1.00 66.35  ? 338  LYS B CE    1 
ATOM   2613  N  NZ    . LYS A 1 336 ? 169.329 187.182 102.093 1.00 60.47  ? 338  LYS B NZ    1 
ATOM   2614  N  N     . ASN A 1 337 ? 166.006 180.315 102.995 1.00 61.74  ? 339  ASN B N     1 
ATOM   2615  C  CA    . ASN A 1 337 ? 165.782 179.510 104.188 1.00 61.10  ? 339  ASN B CA    1 
ATOM   2616  C  C     . ASN A 1 337 ? 165.355 178.093 103.828 1.00 62.89  ? 339  ASN B C     1 
ATOM   2617  O  O     . ASN A 1 337 ? 164.433 177.543 104.433 1.00 73.96  ? 339  ASN B O     1 
ATOM   2618  C  CB    . ASN A 1 337 ? 164.741 180.167 105.092 1.00 66.30  ? 339  ASN B CB    1 
ATOM   2619  C  CG    . ASN A 1 337 ? 165.245 181.441 105.733 1.00 68.88  ? 339  ASN B CG    1 
ATOM   2620  O  OD1   . ASN A 1 337 ? 166.240 182.016 105.298 1.00 65.01  ? 339  ASN B OD1   1 
ATOM   2621  N  ND2   . ASN A 1 337 ? 164.554 181.893 106.772 1.00 68.50  ? 339  ASN B ND2   1 
ATOM   2622  N  N     . SER A 1 338 ? 166.019 177.491 102.838 1.00 54.82  ? 340  SER B N     1 
ATOM   2623  C  CA    . SER A 1 338 ? 165.615 176.171 102.363 1.00 56.86  ? 340  SER B CA    1 
ATOM   2624  C  C     . SER A 1 338 ? 165.729 175.124 103.459 1.00 56.41  ? 340  SER B C     1 
ATOM   2625  O  O     . SER A 1 338 ? 164.944 174.170 103.504 1.00 53.67  ? 340  SER B O     1 
ATOM   2626  C  CB    . SER A 1 338 ? 166.458 175.770 101.153 1.00 57.54  ? 340  SER B CB    1 
ATOM   2627  O  OG    . SER A 1 338 ? 167.825 175.654 101.504 1.00 57.01  ? 340  SER B OG    1 
ATOM   2628  N  N     . SER A 1 339 ? 166.709 175.280 104.350 1.00 61.12  ? 341  SER B N     1 
ATOM   2629  C  CA    . SER A 1 339 ? 166.878 174.323 105.436 1.00 57.64  ? 341  SER B CA    1 
ATOM   2630  C  C     . SER A 1 339 ? 165.700 174.364 106.400 1.00 55.89  ? 341  SER B C     1 
ATOM   2631  O  O     . SER A 1 339 ? 165.360 173.350 107.019 1.00 56.66  ? 341  SER B O     1 
ATOM   2632  C  CB    . SER A 1 339 ? 168.188 174.599 106.171 1.00 59.14  ? 341  SER B CB    1 
ATOM   2633  O  OG    . SER A 1 339 ? 168.166 175.874 106.787 1.00 60.19  ? 341  SER B OG    1 
ATOM   2634  N  N     . TYR A 1 340 ? 165.066 175.524 106.540 1.00 58.14  ? 342  TYR B N     1 
ATOM   2635  C  CA    . TYR A 1 340 ? 163.943 175.685 107.455 1.00 54.98  ? 342  TYR B CA    1 
ATOM   2636  C  C     . TYR A 1 340 ? 162.608 175.310 106.831 1.00 59.45  ? 342  TYR B C     1 
ATOM   2637  O  O     . TYR A 1 340 ? 161.575 175.461 107.489 1.00 64.82  ? 342  TYR B O     1 
ATOM   2638  C  CB    . TYR A 1 340 ? 163.880 177.126 107.965 1.00 56.15  ? 342  TYR B CB    1 
ATOM   2639  C  CG    . TYR A 1 340 ? 165.111 177.574 108.718 1.00 65.29  ? 342  TYR B CG    1 
ATOM   2640  C  CD1   . TYR A 1 340 ? 165.912 176.659 109.384 1.00 63.91  ? 342  TYR B CD1   1 
ATOM   2641  C  CD2   . TYR A 1 340 ? 165.474 178.912 108.759 1.00 66.26  ? 342  TYR B CD2   1 
ATOM   2642  C  CE1   . TYR A 1 340 ? 167.038 177.063 110.071 1.00 63.78  ? 342  TYR B CE1   1 
ATOM   2643  C  CE2   . TYR A 1 340 ? 166.597 179.326 109.442 1.00 64.99  ? 342  TYR B CE2   1 
ATOM   2644  C  CZ    . TYR A 1 340 ? 167.376 178.398 110.097 1.00 66.48  ? 342  TYR B CZ    1 
ATOM   2645  O  OH    . TYR A 1 340 ? 168.499 178.806 110.781 1.00 66.72  ? 342  TYR B OH    1 
ATOM   2646  N  N     . PHE A 1 341 ? 162.600 174.835 105.591 1.00 56.23  ? 343  PHE B N     1 
ATOM   2647  C  CA    . PHE A 1 341 ? 161.386 174.442 104.894 1.00 51.18  ? 343  PHE B CA    1 
ATOM   2648  C  C     . PHE A 1 341 ? 161.455 172.969 104.512 1.00 53.66  ? 343  PHE B C     1 
ATOM   2649  O  O     . PHE A 1 341 ? 162.534 172.386 104.378 1.00 61.23  ? 343  PHE B O     1 
ATOM   2650  C  CB    . PHE A 1 341 ? 161.177 175.291 103.638 1.00 47.70  ? 343  PHE B CB    1 
ATOM   2651  C  CG    . PHE A 1 341 ? 160.589 176.642 103.907 1.00 51.29  ? 343  PHE B CG    1 
ATOM   2652  C  CD1   . PHE A 1 341 ? 159.231 176.798 104.073 1.00 55.45  ? 343  PHE B CD1   1 
ATOM   2653  C  CD2   . PHE A 1 341 ? 161.396 177.759 103.970 1.00 53.36  ? 343  PHE B CD2   1 
ATOM   2654  C  CE1   . PHE A 1 341 ? 158.691 178.038 104.312 1.00 58.67  ? 343  PHE B CE1   1 
ATOM   2655  C  CE2   . PHE A 1 341 ? 160.861 179.000 104.209 1.00 52.56  ? 343  PHE B CE2   1 
ATOM   2656  C  CZ    . PHE A 1 341 ? 159.507 179.140 104.380 1.00 55.95  ? 343  PHE B CZ    1 
ATOM   2657  N  N     . VAL A 1 342 ? 160.291 172.378 104.338 1.00 48.20  ? 344  VAL B N     1 
ATOM   2658  C  CA    . VAL A 1 342 ? 160.171 170.975 103.964 1.00 45.70  ? 344  VAL B CA    1 
ATOM   2659  C  C     . VAL A 1 342 ? 160.402 170.826 102.469 1.00 53.48  ? 344  VAL B C     1 
ATOM   2660  O  O     . VAL A 1 342 ? 159.877 171.592 101.655 1.00 57.15  ? 344  VAL B O     1 
ATOM   2661  C  CB    . VAL A 1 342 ? 158.798 170.421 104.387 1.00 42.07  ? 344  VAL B CB    1 
ATOM   2662  C  CG1   . VAL A 1 342 ? 158.424 169.235 103.540 1.00 50.00  ? 344  VAL B CG1   1 
ATOM   2663  C  CG2   . VAL A 1 342 ? 158.836 170.026 105.838 1.00 45.01  ? 344  VAL B CG2   1 
ATOM   2664  N  N     . GLU A 1 343 ? 161.201 169.823 102.100 1.00 63.72  ? 345  GLU B N     1 
ATOM   2665  C  CA    . GLU A 1 343 ? 161.579 169.615 100.709 1.00 62.47  ? 345  GLU B CA    1 
ATOM   2666  C  C     . GLU A 1 343 ? 160.574 168.794 99.912  1.00 60.67  ? 345  GLU B C     1 
ATOM   2667  O  O     . GLU A 1 343 ? 160.512 168.953 98.689  1.00 64.49  ? 345  GLU B O     1 
ATOM   2668  C  CB    . GLU A 1 343 ? 162.953 168.942 100.623 1.00 57.95  ? 345  GLU B CB    1 
ATOM   2669  C  CG    . GLU A 1 343 ? 163.032 167.585 101.289 1.00 66.94  ? 345  GLU B CG    1 
ATOM   2670  C  CD    . GLU A 1 343 ? 164.430 167.004 101.241 1.00 72.16  ? 345  GLU B CD    1 
ATOM   2671  O  OE1   . GLU A 1 343 ? 165.361 167.734 100.842 1.00 71.23  ? 345  GLU B OE1   1 
ATOM   2672  O  OE2   . GLU A 1 343 ? 164.598 165.820 101.601 1.00 73.92  ? 345  GLU B OE2   1 
ATOM   2673  N  N     . TRP A 1 344 ? 159.791 167.929 100.552 1.00 45.29  ? 346  TRP B N     1 
ATOM   2674  C  CA    . TRP A 1 344 ? 158.786 167.175 99.814  1.00 43.69  ? 346  TRP B CA    1 
ATOM   2675  C  C     . TRP A 1 344 ? 157.511 167.971 99.579  1.00 53.00  ? 346  TRP B C     1 
ATOM   2676  O  O     . TRP A 1 344 ? 156.513 167.398 99.131  1.00 57.83  ? 346  TRP B O     1 
ATOM   2677  C  CB    . TRP A 1 344 ? 158.459 165.857 100.525 1.00 43.47  ? 346  TRP B CB    1 
ATOM   2678  C  CG    . TRP A 1 344 ? 158.204 165.966 101.988 1.00 44.65  ? 346  TRP B CG    1 
ATOM   2679  C  CD1   . TRP A 1 344 ? 159.123 165.878 102.986 1.00 51.04  ? 346  TRP B CD1   1 
ATOM   2680  C  CD2   . TRP A 1 344 ? 156.935 166.144 102.625 1.00 47.66  ? 346  TRP B CD2   1 
ATOM   2681  N  NE1   . TRP A 1 344 ? 158.511 166.010 104.207 1.00 54.55  ? 346  TRP B NE1   1 
ATOM   2682  C  CE2   . TRP A 1 344 ? 157.165 166.173 104.011 1.00 53.72  ? 346  TRP B CE2   1 
ATOM   2683  C  CE3   . TRP A 1 344 ? 155.629 166.290 102.156 1.00 48.36  ? 346  TRP B CE3   1 
ATOM   2684  C  CZ2   . TRP A 1 344 ? 156.139 166.347 104.933 1.00 57.11  ? 346  TRP B CZ2   1 
ATOM   2685  C  CZ3   . TRP A 1 344 ? 154.612 166.462 103.073 1.00 50.43  ? 346  TRP B CZ3   1 
ATOM   2686  C  CH2   . TRP A 1 344 ? 154.872 166.489 104.445 1.00 56.56  ? 346  TRP B CH2   1 
ATOM   2687  N  N     . ILE A 1 345 ? 157.522 169.267 99.868  1.00 52.69  ? 347  ILE B N     1 
ATOM   2688  C  CA    . ILE A 1 345 ? 156.419 170.161 99.533  1.00 44.95  ? 347  ILE B CA    1 
ATOM   2689  C  C     . ILE A 1 345 ? 157.001 171.360 98.795  1.00 54.62  ? 347  ILE B C     1 
ATOM   2690  O  O     . ILE A 1 345 ? 157.687 172.190 99.409  1.00 57.25  ? 347  ILE B O     1 
ATOM   2691  C  CB    . ILE A 1 345 ? 155.644 170.608 100.782 1.00 42.12  ? 347  ILE B CB    1 
ATOM   2692  C  CG1   . ILE A 1 345 ? 154.725 169.498 101.277 1.00 50.06  ? 347  ILE B CG1   1 
ATOM   2693  C  CG2   . ILE A 1 345 ? 154.810 171.835 100.483 1.00 47.71  ? 347  ILE B CG2   1 
ATOM   2694  C  CD1   . ILE A 1 345 ? 153.802 169.935 102.389 1.00 50.27  ? 347  ILE B CD1   1 
ATOM   2695  N  N     . PRO A 1 346 ? 156.795 171.478 97.487  1.00 51.09  ? 348  PRO B N     1 
ATOM   2696  C  CA    . PRO A 1 346 ? 157.173 172.714 96.800  1.00 46.08  ? 348  PRO B CA    1 
ATOM   2697  C  C     . PRO A 1 346 ? 156.203 173.833 97.137  1.00 50.85  ? 348  PRO B C     1 
ATOM   2698  O  O     . PRO A 1 346 ? 155.008 173.608 97.342  1.00 53.76  ? 348  PRO B O     1 
ATOM   2699  C  CB    . PRO A 1 346 ? 157.096 172.338 95.316  1.00 43.20  ? 348  PRO B CB    1 
ATOM   2700  C  CG    . PRO A 1 346 ? 157.012 170.842 95.286  1.00 47.07  ? 348  PRO B CG    1 
ATOM   2701  C  CD    . PRO A 1 346 ? 156.319 170.457 96.545  1.00 47.33  ? 348  PRO B CD    1 
ATOM   2702  N  N     . ASN A 1 347 ? 156.733 175.052 97.189  1.00 51.68  ? 349  ASN B N     1 
ATOM   2703  C  CA    . ASN A 1 347 ? 155.943 176.252 97.459  1.00 52.47  ? 349  ASN B CA    1 
ATOM   2704  C  C     . ASN A 1 347 ? 155.175 176.124 98.775  1.00 54.22  ? 349  ASN B C     1 
ATOM   2705  O  O     . ASN A 1 347 ? 153.949 176.014 98.808  1.00 61.54  ? 349  ASN B O     1 
ATOM   2706  C  CB    . ASN A 1 347 ? 154.998 176.558 96.297  1.00 52.88  ? 349  ASN B CB    1 
ATOM   2707  C  CG    . ASN A 1 347 ? 154.327 177.905 96.437  1.00 57.62  ? 349  ASN B CG    1 
ATOM   2708  O  OD1   . ASN A 1 347 ? 154.937 178.943 96.183  1.00 58.94  ? 349  ASN B OD1   1 
ATOM   2709  N  ND2   . ASN A 1 347 ? 153.064 177.898 96.845  1.00 57.95  ? 349  ASN B ND2   1 
ATOM   2710  N  N     . ASN A 1 348 ? 155.930 176.124 99.874  1.00 47.97  ? 350  ASN B N     1 
ATOM   2711  C  CA    . ASN A 1 348 ? 155.325 176.001 101.194 1.00 49.95  ? 350  ASN B CA    1 
ATOM   2712  C  C     . ASN A 1 348 ? 154.474 177.206 101.572 1.00 55.82  ? 350  ASN B C     1 
ATOM   2713  O  O     . ASN A 1 348 ? 153.661 177.104 102.497 1.00 62.68  ? 350  ASN B O     1 
ATOM   2714  C  CB    . ASN A 1 348 ? 156.409 175.797 102.248 1.00 51.72  ? 350  ASN B CB    1 
ATOM   2715  C  CG    . ASN A 1 348 ? 157.545 174.943 101.750 1.00 55.19  ? 350  ASN B CG    1 
ATOM   2716  O  OD1   . ASN A 1 348 ? 158.388 175.401 100.980 1.00 58.47  ? 350  ASN B OD1   1 
ATOM   2717  N  ND2   . ASN A 1 348 ? 157.580 173.692 102.188 1.00 57.97  ? 350  ASN B ND2   1 
ATOM   2718  N  N     . VAL A 1 349 ? 154.634 178.332 100.898 1.00 48.65  ? 351  VAL B N     1 
ATOM   2719  C  CA    . VAL A 1 349 ? 153.933 179.553 101.275 1.00 40.59  ? 351  VAL B CA    1 
ATOM   2720  C  C     . VAL A 1 349 ? 152.649 179.688 100.471 1.00 40.45  ? 351  VAL B C     1 
ATOM   2721  O  O     . VAL A 1 349 ? 152.586 179.351 99.285  1.00 51.48  ? 351  VAL B O     1 
ATOM   2722  C  CB    . VAL A 1 349 ? 154.841 180.787 101.104 1.00 49.06  ? 351  VAL B CB    1 
ATOM   2723  C  CG1   . VAL A 1 349 ? 156.154 180.576 101.834 1.00 52.95  ? 351  VAL B CG1   1 
ATOM   2724  C  CG2   . VAL A 1 349 ? 155.093 181.069 99.636  1.00 52.82  ? 351  VAL B CG2   1 
ATOM   2725  N  N     . LYS A 1 350 ? 151.601 180.161 101.136 1.00 45.88  ? 352  LYS B N     1 
ATOM   2726  C  CA    . LYS A 1 350 ? 150.363 180.541 100.478 1.00 48.85  ? 352  LYS B CA    1 
ATOM   2727  C  C     . LYS A 1 350 ? 150.151 182.039 100.642 1.00 54.65  ? 352  LYS B C     1 
ATOM   2728  O  O     . LYS A 1 350 ? 150.492 182.621 101.675 1.00 66.24  ? 352  LYS B O     1 
ATOM   2729  C  CB    . LYS A 1 350 ? 149.155 179.790 101.032 1.00 45.05  ? 352  LYS B CB    1 
ATOM   2730  C  CG    . LYS A 1 350 ? 147.984 179.810 100.076 1.00 43.63  ? 352  LYS B CG    1 
ATOM   2731  C  CD    . LYS A 1 350 ? 146.657 179.831 100.787 1.00 51.33  ? 352  LYS B CD    1 
ATOM   2732  C  CE    . LYS A 1 350 ? 145.526 179.879 99.776  1.00 47.72  ? 352  LYS B CE    1 
ATOM   2733  N  NZ    . LYS A 1 350 ? 145.718 180.966 98.780  1.00 43.90  ? 352  LYS B NZ    1 
ATOM   2734  N  N     . THR A 1 351 ? 149.584 182.658 99.613  1.00 49.66  ? 353  THR B N     1 
ATOM   2735  C  CA    . THR A 1 351 ? 149.477 184.104 99.539  1.00 50.70  ? 353  THR B CA    1 
ATOM   2736  C  C     . THR A 1 351 ? 148.033 184.513 99.303  1.00 55.82  ? 353  THR B C     1 
ATOM   2737  O  O     . THR A 1 351 ? 147.360 183.974 98.419  1.00 64.29  ? 353  THR B O     1 
ATOM   2738  C  CB    . THR A 1 351 ? 150.363 184.658 98.419  1.00 55.86  ? 353  THR B CB    1 
ATOM   2739  O  OG1   . THR A 1 351 ? 151.741 184.518 98.783  1.00 56.94  ? 353  THR B OG1   1 
ATOM   2740  C  CG2   . THR A 1 351 ? 150.056 186.119 98.163  1.00 60.13  ? 353  THR B CG2   1 
ATOM   2741  N  N     . ALA A 1 352 ? 147.562 185.468 100.100 1.00 48.92  ? 354  ALA B N     1 
ATOM   2742  C  CA    . ALA A 1 352 ? 146.262 186.088 99.902  1.00 51.87  ? 354  ALA B CA    1 
ATOM   2743  C  C     . ALA A 1 352 ? 146.413 187.581 100.131 1.00 48.99  ? 354  ALA B C     1 
ATOM   2744  O  O     . ALA A 1 352 ? 147.019 187.997 101.121 1.00 59.53  ? 354  ALA B O     1 
ATOM   2745  C  CB    . ALA A 1 352 ? 145.213 185.504 100.851 1.00 55.18  ? 354  ALA B CB    1 
ATOM   2746  N  N     . VAL A 1 353 ? 145.876 188.383 99.219  1.00 39.82  ? 355  VAL B N     1 
ATOM   2747  C  CA    . VAL A 1 353 ? 145.984 189.834 99.293  1.00 39.12  ? 355  VAL B CA    1 
ATOM   2748  C  C     . VAL A 1 353 ? 144.580 190.415 99.330  1.00 47.14  ? 355  VAL B C     1 
ATOM   2749  O  O     . VAL A 1 353 ? 143.762 190.135 98.445  1.00 56.76  ? 355  VAL B O     1 
ATOM   2750  C  CB    . VAL A 1 353 ? 146.784 190.407 98.115  1.00 47.63  ? 355  VAL B CB    1 
ATOM   2751  C  CG1   . VAL A 1 353 ? 146.593 191.908 98.025  1.00 50.36  ? 355  VAL B CG1   1 
ATOM   2752  C  CG2   . VAL A 1 353 ? 148.249 190.064 98.265  1.00 52.02  ? 355  VAL B CG2   1 
ATOM   2753  N  N     . CYS A 1 354 ? 144.304 191.220 100.350 1.00 53.95  ? 356  CYS B N     1 
ATOM   2754  C  CA    . CYS A 1 354 ? 143.038 191.923 100.490 1.00 53.18  ? 356  CYS B CA    1 
ATOM   2755  C  C     . CYS A 1 354 ? 143.275 193.405 100.251 1.00 56.63  ? 356  CYS B C     1 
ATOM   2756  O  O     . CYS A 1 354 ? 144.200 193.988 100.823 1.00 63.03  ? 356  CYS B O     1 
ATOM   2757  C  CB    . CYS A 1 354 ? 142.434 191.692 101.874 1.00 54.02  ? 356  CYS B CB    1 
ATOM   2758  S  SG    . CYS A 1 354 ? 140.796 192.391 102.088 1.00 74.03  ? 356  CYS B SG    1 
ATOM   2759  N  N     . ASP A 1 355 ? 142.448 194.009 99.405  1.00 63.00  ? 357  ASP B N     1 
ATOM   2760  C  CA    . ASP A 1 355 ? 142.654 195.396 98.994  1.00 67.42  ? 357  ASP B CA    1 
ATOM   2761  C  C     . ASP A 1 355 ? 141.926 196.375 99.912  1.00 69.67  ? 357  ASP B C     1 
ATOM   2762  O  O     . ASP A 1 355 ? 141.254 197.298 99.458  1.00 75.36  ? 357  ASP B O     1 
ATOM   2763  C  CB    . ASP A 1 355 ? 142.208 195.569 97.547  1.00 70.21  ? 357  ASP B CB    1 
ATOM   2764  C  CG    . ASP A 1 355 ? 142.916 196.712 96.849  1.00 76.39  ? 357  ASP B CG    1 
ATOM   2765  O  OD1   . ASP A 1 355 ? 143.357 197.653 97.541  1.00 77.92  ? 357  ASP B OD1   1 
ATOM   2766  O  OD2   . ASP A 1 355 ? 143.034 196.669 95.606  1.00 75.62  ? 357  ASP B OD2   1 
ATOM   2767  N  N     . ILE A 1 356 ? 142.093 196.187 101.217 1.00 62.11  ? 358  ILE B N     1 
ATOM   2768  C  CA    . ILE A 1 356 ? 141.586 197.095 102.244 1.00 57.05  ? 358  ILE B CA    1 
ATOM   2769  C  C     . ILE A 1 356 ? 142.490 196.936 103.460 1.00 62.20  ? 358  ILE B C     1 
ATOM   2770  O  O     . ILE A 1 356 ? 142.519 195.860 104.075 1.00 64.99  ? 358  ILE B O     1 
ATOM   2771  C  CB    . ILE A 1 356 ? 140.115 196.810 102.592 1.00 59.16  ? 358  ILE B CB    1 
ATOM   2772  C  CG1   . ILE A 1 356 ? 139.174 197.533 101.630 1.00 64.04  ? 358  ILE B CG1   1 
ATOM   2773  C  CG2   . ILE A 1 356 ? 139.795 197.255 104.013 1.00 61.98  ? 358  ILE B CG2   1 
ATOM   2774  C  CD1   . ILE A 1 356 ? 139.349 199.032 101.622 1.00 64.66  ? 358  ILE B CD1   1 
ATOM   2775  N  N     . PRO A 1 357 ? 143.263 197.951 103.824 1.00 64.96  ? 359  PRO B N     1 
ATOM   2776  C  CA    . PRO A 1 357 ? 144.148 197.829 104.973 1.00 61.86  ? 359  PRO B CA    1 
ATOM   2777  C  C     . PRO A 1 357 ? 143.451 198.281 106.241 1.00 64.84  ? 359  PRO B C     1 
ATOM   2778  O  O     . PRO A 1 357 ? 142.417 198.965 106.179 1.00 70.60  ? 359  PRO B O     1 
ATOM   2779  C  CB    . PRO A 1 357 ? 145.307 198.763 104.610 1.00 60.04  ? 359  PRO B CB    1 
ATOM   2780  C  CG    . PRO A 1 357 ? 144.644 199.845 103.831 1.00 60.75  ? 359  PRO B CG    1 
ATOM   2781  C  CD    . PRO A 1 357 ? 143.483 199.212 103.095 1.00 64.61  ? 359  PRO B CD    1 
ATOM   2782  N  N     . PRO A 1 358 ? 143.971 197.916 107.409 1.00 64.65  ? 360  PRO B N     1 
ATOM   2783  C  CA    . PRO A 1 358 ? 143.418 198.450 108.653 1.00 65.46  ? 360  PRO B CA    1 
ATOM   2784  C  C     . PRO A 1 358 ? 143.630 199.952 108.740 1.00 67.69  ? 360  PRO B C     1 
ATOM   2785  O  O     . PRO A 1 358 ? 144.555 200.514 108.150 1.00 74.84  ? 360  PRO B O     1 
ATOM   2786  C  CB    . PRO A 1 358 ? 144.198 197.708 109.743 1.00 68.07  ? 360  PRO B CB    1 
ATOM   2787  C  CG    . PRO A 1 358 ? 145.433 197.236 109.073 1.00 64.79  ? 360  PRO B CG    1 
ATOM   2788  C  CD    . PRO A 1 358 ? 145.046 196.945 107.660 1.00 65.10  ? 360  PRO B CD    1 
ATOM   2789  N  N     . ARG A 1 359 ? 142.734 200.601 109.478 1.00 67.61  ? 369  ARG B N     1 
ATOM   2790  C  CA    . ARG A 1 359 ? 142.725 202.056 109.558 1.00 70.04  ? 369  ARG B CA    1 
ATOM   2791  C  C     . ARG A 1 359 ? 144.064 202.582 110.055 1.00 73.11  ? 369  ARG B C     1 
ATOM   2792  O  O     . ARG A 1 359 ? 144.624 202.073 111.026 1.00 77.32  ? 369  ARG B O     1 
ATOM   2793  C  CB    . ARG A 1 359 ? 141.600 202.515 110.485 1.00 73.22  ? 369  ARG B CB    1 
ATOM   2794  C  CG    . ARG A 1 359 ? 140.218 202.043 110.063 1.00 75.65  ? 369  ARG B CG    1 
ATOM   2795  C  CD    . ARG A 1 359 ? 139.138 202.607 110.973 1.00 75.39  ? 369  ARG B CD    1 
ATOM   2796  N  NE    . ARG A 1 359 ? 139.114 204.064 110.960 1.00 76.91  ? 369  ARG B NE    1 
ATOM   2797  C  CZ    . ARG A 1 359 ? 138.420 204.793 110.098 1.00 79.05  ? 369  ARG B CZ    1 
ATOM   2798  N  NH1   . ARG A 1 359 ? 137.677 204.231 109.159 1.00 77.36  ? 369  ARG B NH1   1 
ATOM   2799  N  NH2   . ARG A 1 359 ? 138.471 206.119 110.181 1.00 76.77  ? 369  ARG B NH2   1 
ATOM   2800  N  N     . GLY A 1 360 ? 144.590 203.596 109.375 1.00 69.40  ? 370  GLY B N     1 
ATOM   2801  C  CA    . GLY A 1 360 ? 145.839 204.207 109.768 1.00 66.81  ? 370  GLY B CA    1 
ATOM   2802  C  C     . GLY A 1 360 ? 147.081 203.458 109.342 1.00 64.79  ? 370  GLY B C     1 
ATOM   2803  O  O     . GLY A 1 360 ? 148.192 203.947 109.583 1.00 71.23  ? 370  GLY B O     1 
ATOM   2804  N  N     . LEU A 1 361 ? 146.934 202.295 108.719 1.00 60.26  ? 371  LEU B N     1 
ATOM   2805  C  CA    . LEU A 1 361 ? 148.048 201.538 108.171 1.00 63.29  ? 371  LEU B CA    1 
ATOM   2806  C  C     . LEU A 1 361 ? 147.868 201.408 106.667 1.00 70.59  ? 371  LEU B C     1 
ATOM   2807  O  O     . LEU A 1 361 ? 146.785 201.056 106.193 1.00 70.98  ? 371  LEU B O     1 
ATOM   2808  C  CB    . LEU A 1 361 ? 148.145 200.147 108.797 1.00 62.19  ? 371  LEU B CB    1 
ATOM   2809  C  CG    . LEU A 1 361 ? 148.453 200.055 110.287 1.00 66.67  ? 371  LEU B CG    1 
ATOM   2810  C  CD1   . LEU A 1 361 ? 148.397 198.610 110.737 1.00 67.49  ? 371  LEU B CD1   1 
ATOM   2811  C  CD2   . LEU A 1 361 ? 149.815 200.652 110.575 1.00 67.96  ? 371  LEU B CD2   1 
ATOM   2812  N  N     . LYS A 1 362 ? 148.929 201.701 105.919 1.00 68.74  ? 372  LYS B N     1 
ATOM   2813  C  CA    . LYS A 1 362 ? 148.877 201.502 104.478 1.00 60.68  ? 372  LYS B CA    1 
ATOM   2814  C  C     . LYS A 1 362 ? 148.980 200.029 104.112 1.00 65.16  ? 372  LYS B C     1 
ATOM   2815  O  O     . LYS A 1 362 ? 148.421 199.607 103.095 1.00 68.87  ? 372  LYS B O     1 
ATOM   2816  C  CB    . LYS A 1 362 ? 149.989 202.295 103.795 1.00 64.15  ? 372  LYS B CB    1 
ATOM   2817  C  CG    . LYS A 1 362 ? 149.935 203.789 104.059 1.00 69.70  ? 372  LYS B CG    1 
ATOM   2818  C  CD    . LYS A 1 362 ? 151.029 204.523 103.300 1.00 71.62  ? 372  LYS B CD    1 
ATOM   2819  C  CE    . LYS A 1 362 ? 150.826 204.423 101.797 1.00 69.75  ? 372  LYS B CE    1 
ATOM   2820  N  NZ    . LYS A 1 362 ? 151.842 205.214 101.049 1.00 65.85  ? 372  LYS B NZ    1 
ATOM   2821  N  N     . MET A 1 363 ? 149.677 199.239 104.924 1.00 67.45  ? 373  MET B N     1 
ATOM   2822  C  CA    . MET A 1 363 ? 149.856 197.820 104.672 1.00 64.44  ? 373  MET B CA    1 
ATOM   2823  C  C     . MET A 1 363 ? 149.798 197.063 105.989 1.00 63.62  ? 373  MET B C     1 
ATOM   2824  O  O     . MET A 1 363 ? 150.062 197.619 107.057 1.00 71.82  ? 373  MET B O     1 
ATOM   2825  C  CB    . MET A 1 363 ? 151.187 197.537 103.965 1.00 65.20  ? 373  MET B CB    1 
ATOM   2826  C  CG    . MET A 1 363 ? 151.275 198.095 102.557 1.00 70.24  ? 373  MET B CG    1 
ATOM   2827  S  SD    . MET A 1 363 ? 152.948 198.066 101.900 1.00 90.83  ? 373  MET B SD    1 
ATOM   2828  C  CE    . MET A 1 363 ? 153.474 196.434 102.409 1.00 74.27  ? 373  MET B CE    1 
ATOM   2829  N  N     . SER A 1 364 ? 149.451 195.784 105.899 1.00 52.26  ? 374  SER B N     1 
ATOM   2830  C  CA    . SER A 1 364 ? 149.404 194.903 107.055 1.00 49.28  ? 374  SER B CA    1 
ATOM   2831  C  C     . SER A 1 364 ? 149.456 193.470 106.557 1.00 46.95  ? 374  SER B C     1 
ATOM   2832  O  O     . SER A 1 364 ? 149.183 193.192 105.388 1.00 59.63  ? 374  SER B O     1 
ATOM   2833  C  CB    . SER A 1 364 ? 148.146 195.141 107.892 1.00 61.02  ? 374  SER B CB    1 
ATOM   2834  O  OG    . SER A 1 364 ? 148.082 194.240 108.982 1.00 65.16  ? 374  SER B OG    1 
ATOM   2835  N  N     . ALA A 1 365 ? 149.806 192.560 107.460 1.00 50.38  ? 375  ALA B N     1 
ATOM   2836  C  CA    . ALA A 1 365 ? 149.925 191.160 107.086 1.00 52.13  ? 375  ALA B CA    1 
ATOM   2837  C  C     . ALA A 1 365 ? 149.745 190.289 108.318 1.00 52.75  ? 375  ALA B C     1 
ATOM   2838  O  O     . ALA A 1 365 ? 150.058 190.693 109.441 1.00 61.59  ? 375  ALA B O     1 
ATOM   2839  C  CB    . ALA A 1 365 ? 151.270 190.875 106.416 1.00 52.38  ? 375  ALA B CB    1 
ATOM   2840  N  N     . THR A 1 366 ? 149.235 189.086 108.087 1.00 38.81  ? 376  THR B N     1 
ATOM   2841  C  CA    . THR A 1 366 ? 149.089 188.074 109.119 1.00 43.86  ? 376  THR B CA    1 
ATOM   2842  C  C     . THR A 1 366 ? 149.818 186.818 108.677 1.00 48.97  ? 376  THR B C     1 
ATOM   2843  O  O     . THR A 1 366 ? 149.601 186.319 107.570 1.00 55.84  ? 376  THR B O     1 
ATOM   2844  C  CB    . THR A 1 366 ? 147.624 187.750 109.394 1.00 54.66  ? 376  THR B CB    1 
ATOM   2845  O  OG1   . THR A 1 366 ? 146.904 187.700 108.156 1.00 61.74  ? 376  THR B OG1   1 
ATOM   2846  C  CG2   . THR A 1 366 ? 147.010 188.810 110.289 1.00 57.26  ? 376  THR B CG2   1 
ATOM   2847  N  N     . PHE A 1 367 ? 150.678 186.311 109.549 1.00 52.09  ? 377  PHE B N     1 
ATOM   2848  C  CA    . PHE A 1 367 ? 151.505 185.150 109.265 1.00 51.51  ? 377  PHE B CA    1 
ATOM   2849  C  C     . PHE A 1 367 ? 150.952 183.948 110.014 1.00 57.35  ? 377  PHE B C     1 
ATOM   2850  O  O     . PHE A 1 367 ? 150.811 183.987 111.239 1.00 66.12  ? 377  PHE B O     1 
ATOM   2851  C  CB    . PHE A 1 367 ? 152.956 185.418 109.667 1.00 46.81  ? 377  PHE B CB    1 
ATOM   2852  C  CG    . PHE A 1 367 ? 153.884 184.271 109.415 1.00 50.93  ? 377  PHE B CG    1 
ATOM   2853  C  CD1   . PHE A 1 367 ? 154.096 183.312 110.385 1.00 53.78  ? 377  PHE B CD1   1 
ATOM   2854  C  CD2   . PHE A 1 367 ? 154.565 184.165 108.218 1.00 57.10  ? 377  PHE B CD2   1 
ATOM   2855  C  CE1   . PHE A 1 367 ? 154.951 182.261 110.162 1.00 56.36  ? 377  PHE B CE1   1 
ATOM   2856  C  CE2   . PHE A 1 367 ? 155.426 183.116 107.991 1.00 59.51  ? 377  PHE B CE2   1 
ATOM   2857  C  CZ    . PHE A 1 367 ? 155.619 182.162 108.965 1.00 55.26  ? 377  PHE B CZ    1 
ATOM   2858  N  N     . ILE A 1 368 ? 150.633 182.889 109.278 1.00 48.29  ? 378  ILE B N     1 
ATOM   2859  C  CA    . ILE A 1 368 ? 150.200 181.624 109.856 1.00 39.36  ? 378  ILE B CA    1 
ATOM   2860  C  C     . ILE A 1 368 ? 151.224 180.572 109.467 1.00 44.06  ? 378  ILE B C     1 
ATOM   2861  O  O     . ILE A 1 368 ? 151.467 180.346 108.275 1.00 57.13  ? 378  ILE B O     1 
ATOM   2862  C  CB    . ILE A 1 368 ? 148.795 181.229 109.383 1.00 42.44  ? 378  ILE B CB    1 
ATOM   2863  C  CG1   . ILE A 1 368 ? 147.864 182.437 109.430 1.00 52.14  ? 378  ILE B CG1   1 
ATOM   2864  C  CG2   . ILE A 1 368 ? 148.239 180.131 110.260 1.00 51.16  ? 378  ILE B CG2   1 
ATOM   2865  C  CD1   . ILE A 1 368 ? 146.469 182.145 108.944 1.00 53.55  ? 378  ILE B CD1   1 
ATOM   2866  N  N     . GLY A 1 369 ? 151.825 179.930 110.465 1.00 39.98  ? 379  GLY B N     1 
ATOM   2867  C  CA    . GLY A 1 369 ? 152.883 178.977 110.206 1.00 46.95  ? 379  GLY B CA    1 
ATOM   2868  C  C     . GLY A 1 369 ? 152.678 177.615 110.832 1.00 52.89  ? 379  GLY B C     1 
ATOM   2869  O  O     . GLY A 1 369 ? 152.488 177.502 112.045 1.00 56.30  ? 379  GLY B O     1 
ATOM   2870  N  N     . ASN A 1 370 ? 152.716 176.571 110.009 1.00 53.26  ? 380  ASN B N     1 
ATOM   2871  C  CA    . ASN A 1 370 ? 152.605 175.188 110.466 1.00 47.19  ? 380  ASN B CA    1 
ATOM   2872  C  C     . ASN A 1 370 ? 154.016 174.609 110.508 1.00 49.87  ? 380  ASN B C     1 
ATOM   2873  O  O     . ASN A 1 370 ? 154.516 174.070 109.522 1.00 59.92  ? 380  ASN B O     1 
ATOM   2874  C  CB    . ASN A 1 370 ? 151.690 174.387 109.549 1.00 43.34  ? 380  ASN B CB    1 
ATOM   2875  C  CG    . ASN A 1 370 ? 151.291 173.057 110.140 1.00 50.69  ? 380  ASN B CG    1 
ATOM   2876  O  OD1   . ASN A 1 370 ? 151.861 172.608 111.132 1.00 57.75  ? 380  ASN B OD1   1 
ATOM   2877  N  ND2   . ASN A 1 370 ? 150.308 172.412 109.529 1.00 49.29  ? 380  ASN B ND2   1 
ATOM   2878  N  N     . SER A 1 371 ? 154.659 174.725 111.664 1.00 45.75  ? 381  SER B N     1 
ATOM   2879  C  CA    . SER A 1 371 ? 156.038 174.306 111.844 1.00 42.37  ? 381  SER B CA    1 
ATOM   2880  C  C     . SER A 1 371 ? 156.113 173.067 112.723 1.00 46.12  ? 381  SER B C     1 
ATOM   2881  O  O     . SER A 1 371 ? 155.275 172.858 113.604 1.00 55.28  ? 381  SER B O     1 
ATOM   2882  C  CB    . SER A 1 371 ? 156.875 175.422 112.471 1.00 47.76  ? 381  SER B CB    1 
ATOM   2883  O  OG    . SER A 1 371 ? 158.191 174.975 112.739 1.00 52.09  ? 381  SER B OG    1 
ATOM   2884  N  N     . THR A 1 372 ? 157.131 172.243 112.473 1.00 48.53  ? 382  THR B N     1 
ATOM   2885  C  CA    . THR A 1 372 ? 157.402 171.102 113.337 1.00 46.66  ? 382  THR B CA    1 
ATOM   2886  C  C     . THR A 1 372 ? 157.940 171.520 114.696 1.00 54.56  ? 382  THR B C     1 
ATOM   2887  O  O     . THR A 1 372 ? 158.023 170.678 115.596 1.00 64.17  ? 382  THR B O     1 
ATOM   2888  C  CB    . THR A 1 372 ? 158.397 170.149 112.674 1.00 45.54  ? 382  THR B CB    1 
ATOM   2889  O  OG1   . THR A 1 372 ? 159.623 170.841 112.411 1.00 56.62  ? 382  THR B OG1   1 
ATOM   2890  C  CG2   . THR A 1 372 ? 157.837 169.616 111.375 1.00 48.16  ? 382  THR B CG2   1 
ATOM   2891  N  N     . ALA A 1 373 ? 158.309 172.789 114.862 1.00 53.94  ? 383  ALA B N     1 
ATOM   2892  C  CA    . ALA A 1 373 ? 158.818 173.280 116.133 1.00 51.78  ? 383  ALA B CA    1 
ATOM   2893  C  C     . ALA A 1 373 ? 157.752 173.332 117.215 1.00 53.81  ? 383  ALA B C     1 
ATOM   2894  O  O     . ALA A 1 373 ? 158.101 173.426 118.396 1.00 62.29  ? 383  ALA B O     1 
ATOM   2895  C  CB    . ALA A 1 373 ? 159.430 174.666 115.947 1.00 54.23  ? 383  ALA B CB    1 
ATOM   2896  N  N     . ILE A 1 374 ? 156.470 173.277 116.849 1.00 48.74  ? 384  ILE B N     1 
ATOM   2897  C  CA    . ILE A 1 374 ? 155.401 173.268 117.840 1.00 49.08  ? 384  ILE B CA    1 
ATOM   2898  C  C     . ILE A 1 374 ? 155.430 172.023 118.710 1.00 56.57  ? 384  ILE B C     1 
ATOM   2899  O  O     . ILE A 1 374 ? 154.752 171.982 119.743 1.00 59.04  ? 384  ILE B O     1 
ATOM   2900  C  CB    . ILE A 1 374 ? 154.028 173.404 117.150 1.00 47.85  ? 384  ILE B CB    1 
ATOM   2901  C  CG1   . ILE A 1 374 ? 153.050 174.162 118.047 1.00 59.07  ? 384  ILE B CG1   1 
ATOM   2902  C  CG2   . ILE A 1 374 ? 153.471 172.042 116.786 1.00 55.10  ? 384  ILE B CG2   1 
ATOM   2903  C  CD1   . ILE A 1 374 ? 153.427 175.604 118.276 1.00 61.47  ? 384  ILE B CD1   1 
ATOM   2904  N  N     . GLN A 1 375 ? 156.204 171.009 118.321 1.00 55.04  ? 385  GLN B N     1 
ATOM   2905  C  CA    . GLN A 1 375 ? 156.354 169.816 119.141 1.00 55.54  ? 385  GLN B CA    1 
ATOM   2906  C  C     . GLN A 1 375 ? 157.066 170.101 120.455 1.00 56.93  ? 385  GLN B C     1 
ATOM   2907  O  O     . GLN A 1 375 ? 156.870 169.359 121.422 1.00 66.47  ? 385  GLN B O     1 
ATOM   2908  C  CB    . GLN A 1 375 ? 157.112 168.742 118.363 1.00 51.99  ? 385  GLN B CB    1 
ATOM   2909  C  CG    . GLN A 1 375 ? 158.606 168.970 118.303 1.00 49.50  ? 385  GLN B CG    1 
ATOM   2910  C  CD    . GLN A 1 375 ? 159.337 167.865 117.587 1.00 57.04  ? 385  GLN B CD    1 
ATOM   2911  O  OE1   . GLN A 1 375 ? 158.732 167.059 116.884 1.00 66.11  ? 385  GLN B OE1   1 
ATOM   2912  N  NE2   . GLN A 1 375 ? 160.651 167.819 117.759 1.00 61.04  ? 385  GLN B NE2   1 
ATOM   2913  N  N     . GLU A 1 376 ? 157.888 171.151 120.512 1.00 51.63  ? 386  GLU B N     1 
ATOM   2914  C  CA    . GLU A 1 376 ? 158.590 171.480 121.747 1.00 49.42  ? 386  GLU B CA    1 
ATOM   2915  C  C     . GLU A 1 376 ? 157.614 171.850 122.855 1.00 55.16  ? 386  GLU B C     1 
ATOM   2916  O  O     . GLU A 1 376 ? 157.782 171.433 124.008 1.00 66.38  ? 386  GLU B O     1 
ATOM   2917  C  CB    . GLU A 1 376 ? 159.576 172.620 121.499 1.00 54.84  ? 386  GLU B CB    1 
ATOM   2918  C  CG    . GLU A 1 376 ? 160.773 172.232 120.650 1.00 60.52  ? 386  GLU B CG    1 
ATOM   2919  C  CD    . GLU A 1 376 ? 161.816 171.459 121.432 1.00 71.66  ? 386  GLU B CD    1 
ATOM   2920  O  OE1   . GLU A 1 376 ? 161.947 171.698 122.650 1.00 70.97  ? 386  GLU B OE1   1 
ATOM   2921  O  OE2   . GLU A 1 376 ? 162.507 170.612 120.827 1.00 70.77  ? 386  GLU B OE2   1 
ATOM   2922  N  N     . LEU A 1 377 ? 156.587 172.632 122.523 1.00 53.19  ? 387  LEU B N     1 
ATOM   2923  C  CA    . LEU A 1 377 ? 155.557 172.974 123.498 1.00 58.56  ? 387  LEU B CA    1 
ATOM   2924  C  C     . LEU A 1 377 ? 154.856 171.724 124.010 1.00 64.48  ? 387  LEU B C     1 
ATOM   2925  O  O     . LEU A 1 377 ? 154.694 171.532 125.223 1.00 69.34  ? 387  LEU B O     1 
ATOM   2926  C  CB    . LEU A 1 377 ? 154.555 173.936 122.860 1.00 58.60  ? 387  LEU B CB    1 
ATOM   2927  C  CG    . LEU A 1 377 ? 153.306 174.340 123.636 1.00 60.19  ? 387  LEU B CG    1 
ATOM   2928  C  CD1   . LEU A 1 377 ? 153.646 175.351 124.719 1.00 64.66  ? 387  LEU B CD1   1 
ATOM   2929  C  CD2   . LEU A 1 377 ? 152.273 174.901 122.677 1.00 57.91  ? 387  LEU B CD2   1 
ATOM   2930  N  N     . PHE A 1 378 ? 154.447 170.850 123.092 1.00 60.99  ? 388  PHE B N     1 
ATOM   2931  C  CA    . PHE A 1 378 ? 153.788 169.613 123.485 1.00 55.69  ? 388  PHE B CA    1 
ATOM   2932  C  C     . PHE A 1 378 ? 154.734 168.715 124.267 1.00 58.07  ? 388  PHE B C     1 
ATOM   2933  O  O     . PHE A 1 378 ? 154.317 168.045 125.219 1.00 65.03  ? 388  PHE B O     1 
ATOM   2934  C  CB    . PHE A 1 378 ? 153.259 168.896 122.249 1.00 50.58  ? 388  PHE B CB    1 
ATOM   2935  C  CG    . PHE A 1 378 ? 152.239 169.683 121.488 1.00 57.64  ? 388  PHE B CG    1 
ATOM   2936  C  CD1   . PHE A 1 378 ? 151.415 170.582 122.138 1.00 61.58  ? 388  PHE B CD1   1 
ATOM   2937  C  CD2   . PHE A 1 378 ? 152.103 169.526 120.123 1.00 61.63  ? 388  PHE B CD2   1 
ATOM   2938  C  CE1   . PHE A 1 378 ? 150.477 171.307 121.441 1.00 58.93  ? 388  PHE B CE1   1 
ATOM   2939  C  CE2   . PHE A 1 378 ? 151.167 170.248 119.423 1.00 62.96  ? 388  PHE B CE2   1 
ATOM   2940  C  CZ    . PHE A 1 378 ? 150.353 171.140 120.083 1.00 57.76  ? 388  PHE B CZ    1 
ATOM   2941  N  N     . LYS A 1 379 ? 156.011 168.691 123.885 1.00 53.79  ? 389  LYS B N     1 
ATOM   2942  C  CA    . LYS A 1 379 ? 156.977 167.865 124.598 1.00 52.11  ? 389  LYS B CA    1 
ATOM   2943  C  C     . LYS A 1 379 ? 157.149 168.332 126.038 1.00 54.30  ? 389  LYS B C     1 
ATOM   2944  O  O     . LYS A 1 379 ? 157.183 167.508 126.960 1.00 62.80  ? 389  LYS B O     1 
ATOM   2945  C  CB    . LYS A 1 379 ? 158.315 167.871 123.862 1.00 55.37  ? 389  LYS B CB    1 
ATOM   2946  C  CG    . LYS A 1 379 ? 159.298 166.828 124.351 1.00 58.95  ? 389  LYS B CG    1 
ATOM   2947  C  CD    . LYS A 1 379 ? 160.624 166.941 123.623 1.00 56.85  ? 389  LYS B CD    1 
ATOM   2948  C  CE    . LYS A 1 379 ? 160.442 166.799 122.125 1.00 62.28  ? 389  LYS B CE    1 
ATOM   2949  N  NZ    . LYS A 1 379 ? 159.873 165.474 121.760 1.00 63.46  ? 389  LYS B NZ    1 
ATOM   2950  N  N     . ARG A 1 380 ? 157.244 169.646 126.260 1.00 49.36  ? 390  ARG B N     1 
ATOM   2951  C  CA    . ARG A 1 380 ? 157.406 170.129 127.628 1.00 52.03  ? 390  ARG B CA    1 
ATOM   2952  C  C     . ARG A 1 380 ? 156.128 169.933 128.436 1.00 57.12  ? 390  ARG B C     1 
ATOM   2953  O  O     . ARG A 1 380 ? 156.186 169.632 129.637 1.00 63.93  ? 390  ARG B O     1 
ATOM   2954  C  CB    . ARG A 1 380 ? 157.844 171.595 127.636 1.00 51.09  ? 390  ARG B CB    1 
ATOM   2955  C  CG    . ARG A 1 380 ? 156.765 172.600 127.293 1.00 58.11  ? 390  ARG B CG    1 
ATOM   2956  C  CD    . ARG A 1 380 ? 157.213 174.014 127.605 1.00 61.75  ? 390  ARG B CD    1 
ATOM   2957  N  NE    . ARG A 1 380 ? 158.350 174.415 126.786 1.00 63.81  ? 390  ARG B NE    1 
ATOM   2958  C  CZ    . ARG A 1 380 ? 158.260 175.155 125.690 1.00 65.88  ? 390  ARG B CZ    1 
ATOM   2959  N  NH1   . ARG A 1 380 ? 157.094 175.597 125.249 1.00 66.03  ? 390  ARG B NH1   1 
ATOM   2960  N  NH2   . ARG A 1 380 ? 159.367 175.459 125.019 1.00 60.29  ? 390  ARG B NH2   1 
ATOM   2961  N  N     . ILE A 1 381 ? 154.965 170.071 127.794 1.00 54.21  ? 391  ILE B N     1 
ATOM   2962  C  CA    . ILE A 1 381 ? 153.712 169.803 128.494 1.00 55.19  ? 391  ILE B CA    1 
ATOM   2963  C  C     . ILE A 1 381 ? 153.651 168.345 128.927 1.00 56.37  ? 391  ILE B C     1 
ATOM   2964  O  O     . ILE A 1 381 ? 153.271 168.034 130.062 1.00 63.28  ? 391  ILE B O     1 
ATOM   2965  C  CB    . ILE A 1 381 ? 152.512 170.187 127.611 1.00 55.14  ? 391  ILE B CB    1 
ATOM   2966  C  CG1   . ILE A 1 381 ? 152.283 171.696 127.652 1.00 59.01  ? 391  ILE B CG1   1 
ATOM   2967  C  CG2   . ILE A 1 381 ? 151.258 169.460 128.056 1.00 54.80  ? 391  ILE B CG2   1 
ATOM   2968  C  CD1   . ILE A 1 381 ? 151.117 172.154 126.814 1.00 61.21  ? 391  ILE B CD1   1 
ATOM   2969  N  N     . SER A 1 382 ? 154.042 167.429 128.039 1.00 55.30  ? 392  SER B N     1 
ATOM   2970  C  CA    . SER A 1 382 ? 154.042 166.012 128.383 1.00 58.85  ? 392  SER B CA    1 
ATOM   2971  C  C     . SER A 1 382 ? 155.057 165.704 129.478 1.00 58.73  ? 392  SER B C     1 
ATOM   2972  O  O     . SER A 1 382 ? 154.804 164.856 130.342 1.00 64.33  ? 392  SER B O     1 
ATOM   2973  C  CB    . SER A 1 382 ? 154.320 165.171 127.139 1.00 63.84  ? 392  SER B CB    1 
ATOM   2974  O  OG    . SER A 1 382 ? 154.348 163.791 127.453 1.00 68.56  ? 392  SER B OG    1 
ATOM   2975  N  N     . GLU A 1 383 ? 156.212 166.372 129.457 1.00 52.60  ? 393  GLU B N     1 
ATOM   2976  C  CA    . GLU A 1 383 ? 157.210 166.156 130.501 1.00 47.74  ? 393  GLU B CA    1 
ATOM   2977  C  C     . GLU A 1 383 ? 156.677 166.577 131.866 1.00 54.82  ? 393  GLU B C     1 
ATOM   2978  O  O     . GLU A 1 383 ? 156.802 165.838 132.854 1.00 60.84  ? 393  GLU B O     1 
ATOM   2979  C  CB    . GLU A 1 383 ? 158.491 166.917 130.160 1.00 54.14  ? 393  GLU B CB    1 
ATOM   2980  C  CG    . GLU A 1 383 ? 159.718 166.452 130.923 1.00 59.63  ? 393  GLU B CG    1 
ATOM   2981  C  CD    . GLU A 1 383 ? 159.869 167.139 132.267 1.00 70.24  ? 393  GLU B CD    1 
ATOM   2982  O  OE1   . GLU A 1 383 ? 159.277 168.224 132.452 1.00 71.35  ? 393  GLU B OE1   1 
ATOM   2983  O  OE2   . GLU A 1 383 ? 160.578 166.594 133.139 1.00 69.15  ? 393  GLU B OE2   1 
ATOM   2984  N  N     . GLN A 1 384 ? 156.066 167.762 131.940 1.00 52.65  ? 394  GLN B N     1 
ATOM   2985  C  CA    . GLN A 1 384 ? 155.478 168.204 133.201 1.00 53.12  ? 394  GLN B CA    1 
ATOM   2986  C  C     . GLN A 1 384 ? 154.341 167.285 133.630 1.00 56.92  ? 394  GLN B C     1 
ATOM   2987  O  O     . GLN A 1 384 ? 154.179 166.997 134.824 1.00 62.72  ? 394  GLN B O     1 
ATOM   2988  C  CB    . GLN A 1 384 ? 154.992 169.645 133.079 1.00 50.61  ? 394  GLN B CB    1 
ATOM   2989  C  CG    . GLN A 1 384 ? 156.110 170.662 132.995 1.00 48.50  ? 394  GLN B CG    1 
ATOM   2990  C  CD    . GLN A 1 384 ? 155.607 172.056 132.693 1.00 56.24  ? 394  GLN B CD    1 
ATOM   2991  O  OE1   . GLN A 1 384 ? 154.431 172.252 132.394 1.00 59.31  ? 394  GLN B OE1   1 
ATOM   2992  N  NE2   . GLN A 1 384 ? 156.497 173.035 132.772 1.00 55.98  ? 394  GLN B NE2   1 
ATOM   2993  N  N     . PHE A 1 385 ? 153.545 166.811 132.670 1.00 53.86  ? 395  PHE B N     1 
ATOM   2994  C  CA    . PHE A 1 385 ? 152.459 165.892 132.988 1.00 46.49  ? 395  PHE B CA    1 
ATOM   2995  C  C     . PHE A 1 385 ? 152.989 164.602 133.592 1.00 50.99  ? 395  PHE B C     1 
ATOM   2996  O  O     . PHE A 1 385 ? 152.442 164.104 134.580 1.00 58.48  ? 395  PHE B O     1 
ATOM   2997  C  CB    . PHE A 1 385 ? 151.648 165.596 131.729 1.00 49.42  ? 395  PHE B CB    1 
ATOM   2998  C  CG    . PHE A 1 385 ? 150.441 164.739 131.967 1.00 46.93  ? 395  PHE B CG    1 
ATOM   2999  C  CD1   . PHE A 1 385 ? 149.215 165.313 132.229 1.00 56.70  ? 395  PHE B CD1   1 
ATOM   3000  C  CD2   . PHE A 1 385 ? 150.530 163.364 131.913 1.00 51.08  ? 395  PHE B CD2   1 
ATOM   3001  C  CE1   . PHE A 1 385 ? 148.104 164.532 132.440 1.00 58.71  ? 395  PHE B CE1   1 
ATOM   3002  C  CE2   . PHE A 1 385 ? 149.425 162.580 132.126 1.00 54.63  ? 395  PHE B CE2   1 
ATOM   3003  C  CZ    . PHE A 1 385 ? 148.210 163.163 132.388 1.00 56.46  ? 395  PHE B CZ    1 
ATOM   3004  N  N     . THR A 1 386 ? 154.049 164.041 133.009 1.00 52.88  ? 396  THR B N     1 
ATOM   3005  C  CA    . THR A 1 386 ? 154.629 162.819 133.556 1.00 51.03  ? 396  THR B CA    1 
ATOM   3006  C  C     . THR A 1 386 ? 155.196 163.059 134.947 1.00 54.80  ? 396  THR B C     1 
ATOM   3007  O  O     . THR A 1 386 ? 155.012 162.233 135.852 1.00 63.73  ? 396  THR B O     1 
ATOM   3008  C  CB    . THR A 1 386 ? 155.711 162.278 132.625 1.00 56.35  ? 396  THR B CB    1 
ATOM   3009  O  OG1   . THR A 1 386 ? 156.618 163.332 132.279 1.00 61.78  ? 396  THR B OG1   1 
ATOM   3010  C  CG2   . THR A 1 386 ? 155.088 161.711 131.363 1.00 56.26  ? 396  THR B CG2   1 
ATOM   3011  N  N     . ALA A 1 387 ? 155.874 164.193 135.142 1.00 50.35  ? 397  ALA B N     1 
ATOM   3012  C  CA    . ALA A 1 387 ? 156.426 164.502 136.458 1.00 45.55  ? 397  ALA B CA    1 
ATOM   3013  C  C     . ALA A 1 387 ? 155.328 164.601 137.509 1.00 48.74  ? 397  ALA B C     1 
ATOM   3014  O  O     . ALA A 1 387 ? 155.491 164.115 138.634 1.00 51.22  ? 397  ALA B O     1 
ATOM   3015  C  CB    . ALA A 1 387 ? 157.232 165.798 136.399 1.00 45.98  ? 397  ALA B CB    1 
ATOM   3016  N  N     . MET A 1 388 ? 154.203 165.225 137.165 1.00 53.10  ? 398  MET B N     1 
ATOM   3017  C  CA    . MET A 1 388 ? 153.107 165.371 138.116 1.00 48.04  ? 398  MET B CA    1 
ATOM   3018  C  C     . MET A 1 388 ? 152.260 164.115 138.265 1.00 51.69  ? 398  MET B C     1 
ATOM   3019  O  O     . MET A 1 388 ? 151.572 163.973 139.280 1.00 60.41  ? 398  MET B O     1 
ATOM   3020  C  CB    . MET A 1 388 ? 152.205 166.535 137.705 1.00 49.81  ? 398  MET B CB    1 
ATOM   3021  C  CG    . MET A 1 388 ? 152.898 167.875 137.663 1.00 55.52  ? 398  MET B CG    1 
ATOM   3022  S  SD    . MET A 1 388 ? 151.729 169.235 137.538 1.00 70.79  ? 398  MET B SD    1 
ATOM   3023  C  CE    . MET A 1 388 ? 150.984 169.176 139.159 1.00 58.85  ? 398  MET B CE    1 
ATOM   3024  N  N     . PHE A 1 389 ? 152.287 163.207 137.291 1.00 47.91  ? 399  PHE B N     1 
ATOM   3025  C  CA    . PHE A 1 389 ? 151.377 162.072 137.277 1.00 48.62  ? 399  PHE B CA    1 
ATOM   3026  C  C     . PHE A 1 389 ? 152.018 160.772 137.730 1.00 53.65  ? 399  PHE B C     1 
ATOM   3027  O  O     . PHE A 1 389 ? 151.292 159.844 138.103 1.00 57.33  ? 399  PHE B O     1 
ATOM   3028  C  CB    . PHE A 1 389 ? 150.796 161.894 135.869 1.00 46.95  ? 399  PHE B CB    1 
ATOM   3029  C  CG    . PHE A 1 389 ? 149.687 160.892 135.786 1.00 44.89  ? 399  PHE B CG    1 
ATOM   3030  C  CD1   . PHE A 1 389 ? 148.469 161.142 136.382 1.00 52.51  ? 399  PHE B CD1   1 
ATOM   3031  C  CD2   . PHE A 1 389 ? 149.851 159.719 135.082 1.00 44.87  ? 399  PHE B CD2   1 
ATOM   3032  C  CE1   . PHE A 1 389 ? 147.446 160.227 136.298 1.00 57.68  ? 399  PHE B CE1   1 
ATOM   3033  C  CE2   . PHE A 1 389 ? 148.831 158.803 134.993 1.00 48.13  ? 399  PHE B CE2   1 
ATOM   3034  C  CZ    . PHE A 1 389 ? 147.628 159.057 135.601 1.00 54.72  ? 399  PHE B CZ    1 
ATOM   3035  N  N     . ARG A 1 390 ? 153.348 160.675 137.710 1.00 51.19  ? 400  ARG B N     1 
ATOM   3036  C  CA    . ARG A 1 390 ? 153.995 159.527 138.335 1.00 49.28  ? 400  ARG B CA    1 
ATOM   3037  C  C     . ARG A 1 390 ? 153.695 159.482 139.827 1.00 58.35  ? 400  ARG B C     1 
ATOM   3038  O  O     . ARG A 1 390 ? 153.541 158.401 140.407 1.00 61.97  ? 400  ARG B O     1 
ATOM   3039  C  CB    . ARG A 1 390 ? 155.503 159.574 138.101 1.00 50.15  ? 400  ARG B CB    1 
ATOM   3040  C  CG    . ARG A 1 390 ? 155.936 159.207 136.701 1.00 56.31  ? 400  ARG B CG    1 
ATOM   3041  C  CD    . ARG A 1 390 ? 157.319 158.588 136.726 1.00 57.62  ? 400  ARG B CD    1 
ATOM   3042  N  NE    . ARG A 1 390 ? 158.161 159.200 137.746 1.00 55.23  ? 400  ARG B NE    1 
ATOM   3043  C  CZ    . ARG A 1 390 ? 158.917 160.272 137.551 1.00 57.82  ? 400  ARG B CZ    1 
ATOM   3044  N  NH1   . ARG A 1 390 ? 158.966 160.878 136.376 1.00 57.81  ? 400  ARG B NH1   1 
ATOM   3045  N  NH2   . ARG A 1 390 ? 159.643 160.745 138.559 1.00 56.03  ? 400  ARG B NH2   1 
ATOM   3046  N  N     . ARG A 1 391 ? 153.607 160.647 140.464 1.00 50.31  ? 401  ARG B N     1 
ATOM   3047  C  CA    . ARG A 1 391 ? 153.399 160.750 141.900 1.00 42.40  ? 401  ARG B CA    1 
ATOM   3048  C  C     . ARG A 1 391 ? 151.971 161.126 142.274 1.00 49.94  ? 401  ARG B C     1 
ATOM   3049  O  O     . ARG A 1 391 ? 151.716 161.439 143.441 1.00 57.10  ? 401  ARG B O     1 
ATOM   3050  C  CB    . ARG A 1 391 ? 154.376 161.761 142.494 1.00 37.27  ? 401  ARG B CB    1 
ATOM   3051  C  CG    . ARG A 1 391 ? 155.825 161.367 142.333 1.00 45.59  ? 401  ARG B CG    1 
ATOM   3052  C  CD    . ARG A 1 391 ? 156.231 160.355 143.377 1.00 52.74  ? 401  ARG B CD    1 
ATOM   3053  N  NE    . ARG A 1 391 ? 156.362 160.959 144.696 1.00 51.51  ? 401  ARG B NE    1 
ATOM   3054  C  CZ    . ARG A 1 391 ? 157.495 161.440 145.185 1.00 47.57  ? 401  ARG B CZ    1 
ATOM   3055  N  NH1   . ARG A 1 391 ? 158.617 161.405 144.487 1.00 47.96  ? 401  ARG B NH1   1 
ATOM   3056  N  NH2   . ARG A 1 391 ? 157.503 161.968 146.405 1.00 48.67  ? 401  ARG B NH2   1 
ATOM   3057  N  N     . LYS A 1 392 ? 151.041 161.105 141.318 1.00 46.95  ? 402  LYS B N     1 
ATOM   3058  C  CA    . LYS A 1 392 ? 149.623 161.367 141.575 1.00 47.23  ? 402  LYS B CA    1 
ATOM   3059  C  C     . LYS A 1 392 ? 149.394 162.739 142.200 1.00 50.74  ? 402  LYS B C     1 
ATOM   3060  O  O     . LYS A 1 392 ? 148.533 162.899 143.068 1.00 57.11  ? 402  LYS B O     1 
ATOM   3061  C  CB    . LYS A 1 392 ? 149.012 160.280 142.464 1.00 53.73  ? 402  LYS B CB    1 
ATOM   3062  C  CG    . LYS A 1 392 ? 148.243 159.204 141.724 1.00 57.71  ? 402  LYS B CG    1 
ATOM   3063  C  CD    . LYS A 1 392 ? 149.167 158.301 140.934 1.00 59.28  ? 402  LYS B CD    1 
ATOM   3064  C  CE    . LYS A 1 392 ? 148.541 156.936 140.730 1.00 56.11  ? 402  LYS B CE    1 
ATOM   3065  N  NZ    . LYS A 1 392 ? 147.147 157.047 140.230 1.00 59.20  ? 402  LYS B NZ    1 
ATOM   3066  N  N     . ALA A 1 393 ? 150.155 163.740 141.772 1.00 46.19  ? 403  ALA B N     1 
ATOM   3067  C  CA    . ALA A 1 393 ? 150.042 165.065 142.363 1.00 47.72  ? 403  ALA B CA    1 
ATOM   3068  C  C     . ALA A 1 393 ? 148.807 165.786 141.839 1.00 53.85  ? 403  ALA B C     1 
ATOM   3069  O  O     . ALA A 1 393 ? 148.547 165.796 140.632 1.00 61.48  ? 403  ALA B O     1 
ATOM   3070  C  CB    . ALA A 1 393 ? 151.296 165.883 142.068 1.00 52.60  ? 403  ALA B CB    1 
ATOM   3071  N  N     . PHE A 1 394 ? 148.050 166.394 142.755 1.00 45.89  ? 404  PHE B N     1 
ATOM   3072  C  CA    . PHE A 1 394 ? 146.880 167.206 142.416 1.00 37.89  ? 404  PHE B CA    1 
ATOM   3073  C  C     . PHE A 1 394 ? 145.880 166.422 141.573 1.00 47.08  ? 404  PHE B C     1 
ATOM   3074  O  O     . PHE A 1 394 ? 145.243 166.960 140.666 1.00 56.85  ? 404  PHE B O     1 
ATOM   3075  C  CB    . PHE A 1 394 ? 147.288 168.491 141.697 1.00 44.94  ? 404  PHE B CB    1 
ATOM   3076  C  CG    . PHE A 1 394 ? 148.209 169.368 142.486 1.00 43.73  ? 404  PHE B CG    1 
ATOM   3077  C  CD1   . PHE A 1 394 ? 149.577 169.226 142.380 1.00 46.59  ? 404  PHE B CD1   1 
ATOM   3078  C  CD2   . PHE A 1 394 ? 147.707 170.345 143.320 1.00 46.25  ? 404  PHE B CD2   1 
ATOM   3079  C  CE1   . PHE A 1 394 ? 150.427 170.032 143.095 1.00 49.45  ? 404  PHE B CE1   1 
ATOM   3080  C  CE2   . PHE A 1 394 ? 148.555 171.157 144.042 1.00 49.48  ? 404  PHE B CE2   1 
ATOM   3081  C  CZ    . PHE A 1 394 ? 149.917 171.000 143.929 1.00 50.75  ? 404  PHE B CZ    1 
ATOM   3082  N  N     . LEU A 1 395 ? 145.737 165.134 141.873 1.00 50.40  ? 405  LEU B N     1 
ATOM   3083  C  CA    . LEU A 1 395 ? 144.918 164.251 141.055 1.00 50.93  ? 405  LEU B CA    1 
ATOM   3084  C  C     . LEU A 1 395 ? 143.578 163.904 141.676 1.00 49.15  ? 405  LEU B C     1 
ATOM   3085  O  O     . LEU A 1 395 ? 142.639 163.591 140.942 1.00 56.43  ? 405  LEU B O     1 
ATOM   3086  C  CB    . LEU A 1 395 ? 145.673 162.952 140.754 1.00 48.27  ? 405  LEU B CB    1 
ATOM   3087  C  CG    . LEU A 1 395 ? 145.122 162.113 139.603 1.00 49.50  ? 405  LEU B CG    1 
ATOM   3088  C  CD1   . LEU A 1 395 ? 145.251 162.863 138.293 1.00 53.67  ? 405  LEU B CD1   1 
ATOM   3089  C  CD2   . LEU A 1 395 ? 145.836 160.781 139.524 1.00 53.28  ? 405  LEU B CD2   1 
ATOM   3090  N  N     . HIS A 1 396 ? 143.460 163.952 143.001 1.00 47.61  ? 406  HIS B N     1 
ATOM   3091  C  CA    . HIS A 1 396 ? 142.182 163.643 143.629 1.00 48.35  ? 406  HIS B CA    1 
ATOM   3092  C  C     . HIS A 1 396 ? 141.134 164.705 143.324 1.00 53.58  ? 406  HIS B C     1 
ATOM   3093  O  O     . HIS A 1 396 ? 139.933 164.422 143.385 1.00 61.22  ? 406  HIS B O     1 
ATOM   3094  C  CB    . HIS A 1 396 ? 142.367 163.486 145.135 1.00 47.53  ? 406  HIS B CB    1 
ATOM   3095  C  CG    . HIS A 1 396 ? 142.798 164.742 145.822 1.00 52.98  ? 406  HIS B CG    1 
ATOM   3096  N  ND1   . HIS A 1 396 ? 144.122 165.091 145.971 1.00 58.29  ? 406  HIS B ND1   1 
ATOM   3097  C  CD2   . HIS A 1 396 ? 142.080 165.731 146.403 1.00 50.96  ? 406  HIS B CD2   1 
ATOM   3098  C  CE1   . HIS A 1 396 ? 144.200 166.243 146.612 1.00 56.46  ? 406  HIS B CE1   1 
ATOM   3099  N  NE2   . HIS A 1 396 ? 142.975 166.652 146.886 1.00 54.93  ? 406  HIS B NE2   1 
ATOM   3100  N  N     . TRP A 1 397 ? 141.562 165.928 143.001 1.00 50.00  ? 407  TRP B N     1 
ATOM   3101  C  CA    . TRP A 1 397 ? 140.612 166.960 142.602 1.00 44.37  ? 407  TRP B CA    1 
ATOM   3102  C  C     . TRP A 1 397 ? 139.964 166.623 141.266 1.00 48.67  ? 407  TRP B C     1 
ATOM   3103  O  O     . TRP A 1 397 ? 138.769 166.866 141.069 1.00 52.17  ? 407  TRP B O     1 
ATOM   3104  C  CB    . TRP A 1 397 ? 141.304 168.320 142.533 1.00 44.65  ? 407  TRP B CB    1 
ATOM   3105  C  CG    . TRP A 1 397 ? 141.642 168.895 143.869 1.00 41.78  ? 407  TRP B CG    1 
ATOM   3106  C  CD1   . TRP A 1 397 ? 142.864 168.918 144.464 1.00 44.55  ? 407  TRP B CD1   1 
ATOM   3107  C  CD2   . TRP A 1 397 ? 140.739 169.525 144.781 1.00 48.31  ? 407  TRP B CD2   1 
ATOM   3108  N  NE1   . TRP A 1 397 ? 142.782 169.527 145.689 1.00 47.98  ? 407  TRP B NE1   1 
ATOM   3109  C  CE2   . TRP A 1 397 ? 141.486 169.910 145.907 1.00 49.72  ? 407  TRP B CE2   1 
ATOM   3110  C  CE3   . TRP A 1 397 ? 139.370 169.805 144.752 1.00 57.48  ? 407  TRP B CE3   1 
ATOM   3111  C  CZ2   . TRP A 1 397 ? 140.913 170.557 146.996 1.00 49.52  ? 407  TRP B CZ2   1 
ATOM   3112  C  CZ3   . TRP A 1 397 ? 138.802 170.448 145.834 1.00 53.90  ? 407  TRP B CZ3   1 
ATOM   3113  C  CH2   . TRP A 1 397 ? 139.573 170.817 146.941 1.00 50.34  ? 407  TRP B CH2   1 
ATOM   3114  N  N     . TYR A 1 398 ? 140.739 166.071 140.332 1.00 53.51  ? 408  TYR B N     1 
ATOM   3115  C  CA    . TYR A 1 398 ? 140.181 165.690 139.039 1.00 45.28  ? 408  TYR B CA    1 
ATOM   3116  C  C     . TYR A 1 398 ? 139.372 164.405 139.144 1.00 48.17  ? 408  TYR B C     1 
ATOM   3117  O  O     . TYR A 1 398 ? 138.349 164.251 138.468 1.00 59.42  ? 408  TYR B O     1 
ATOM   3118  C  CB    . TYR A 1 398 ? 141.299 165.539 138.011 1.00 46.27  ? 408  TYR B CB    1 
ATOM   3119  C  CG    . TYR A 1 398 ? 141.919 166.848 137.591 1.00 47.48  ? 408  TYR B CG    1 
ATOM   3120  C  CD1   . TYR A 1 398 ? 142.948 167.414 138.324 1.00 48.31  ? 408  TYR B CD1   1 
ATOM   3121  C  CD2   . TYR A 1 398 ? 141.476 167.519 136.467 1.00 53.08  ? 408  TYR B CD2   1 
ATOM   3122  C  CE1   . TYR A 1 398 ? 143.514 168.607 137.948 1.00 49.33  ? 408  TYR B CE1   1 
ATOM   3123  C  CE2   . TYR A 1 398 ? 142.037 168.710 136.084 1.00 54.28  ? 408  TYR B CE2   1 
ATOM   3124  C  CZ    . TYR A 1 398 ? 143.055 169.251 136.828 1.00 51.42  ? 408  TYR B CZ    1 
ATOM   3125  O  OH    . TYR A 1 398 ? 143.621 170.445 136.449 1.00 55.24  ? 408  TYR B OH    1 
ATOM   3126  N  N     . THR A 1 399 ? 139.815 163.470 139.985 1.00 52.21  ? 409  THR B N     1 
ATOM   3127  C  CA    . THR A 1 399 ? 139.097 162.210 140.145 1.00 51.13  ? 409  THR B CA    1 
ATOM   3128  C  C     . THR A 1 399 ? 137.782 162.398 140.889 1.00 50.96  ? 409  THR B C     1 
ATOM   3129  O  O     . THR A 1 399 ? 136.817 161.670 140.633 1.00 59.15  ? 409  THR B O     1 
ATOM   3130  C  CB    . THR A 1 399 ? 139.975 161.195 140.875 1.00 50.55  ? 409  THR B CB    1 
ATOM   3131  O  OG1   . THR A 1 399 ? 141.294 161.216 140.320 1.00 59.06  ? 409  THR B OG1   1 
ATOM   3132  C  CG2   . THR A 1 399 ? 139.404 159.795 140.735 1.00 53.20  ? 409  THR B CG2   1 
ATOM   3133  N  N     . GLY A 1 400 ? 137.718 163.367 141.804 1.00 49.41  ? 410  GLY B N     1 
ATOM   3134  C  CA    . GLY A 1 400 ? 136.507 163.580 142.573 1.00 50.27  ? 410  GLY B CA    1 
ATOM   3135  C  C     . GLY A 1 400 ? 135.342 164.106 141.764 1.00 55.72  ? 410  GLY B C     1 
ATOM   3136  O  O     . GLY A 1 400 ? 134.206 164.081 142.247 1.00 60.21  ? 410  GLY B O     1 
ATOM   3137  N  N     . GLU A 1 401 ? 135.595 164.585 140.549 1.00 60.94  ? 411  GLU B N     1 
ATOM   3138  C  CA    . GLU A 1 401 ? 134.542 165.052 139.661 1.00 61.99  ? 411  GLU B CA    1 
ATOM   3139  C  C     . GLU A 1 401 ? 134.136 164.019 138.619 1.00 63.54  ? 411  GLU B C     1 
ATOM   3140  O  O     . GLU A 1 401 ? 133.289 164.315 137.773 1.00 67.25  ? 411  GLU B O     1 
ATOM   3141  C  CB    . GLU A 1 401 ? 134.972 166.348 138.970 1.00 61.73  ? 411  GLU B CB    1 
ATOM   3142  C  CG    . GLU A 1 401 ? 134.397 167.606 139.600 1.00 67.37  ? 411  GLU B CG    1 
ATOM   3143  C  CD    . GLU A 1 401 ? 135.126 168.029 140.862 1.00 70.91  ? 411  GLU B CD    1 
ATOM   3144  O  OE1   . GLU A 1 401 ? 135.988 167.266 141.346 1.00 71.52  ? 411  GLU B OE1   1 
ATOM   3145  O  OE2   . GLU A 1 401 ? 134.833 169.130 141.374 1.00 71.78  ? 411  GLU B OE2   1 
ATOM   3146  N  N     . GLY A 1 402 ? 134.713 162.821 138.655 1.00 53.62  ? 412  GLY B N     1 
ATOM   3147  C  CA    . GLY A 1 402 ? 134.282 161.737 137.799 1.00 54.02  ? 412  GLY B CA    1 
ATOM   3148  C  C     . GLY A 1 402 ? 135.262 161.266 136.745 1.00 58.70  ? 412  GLY B C     1 
ATOM   3149  O  O     . GLY A 1 402 ? 134.882 160.443 135.904 1.00 63.49  ? 412  GLY B O     1 
ATOM   3150  N  N     . MET A 1 403 ? 136.500 161.751 136.749 1.00 58.97  ? 413  MET B N     1 
ATOM   3151  C  CA    . MET A 1 403 ? 137.475 161.313 135.766 1.00 60.63  ? 413  MET B CA    1 
ATOM   3152  C  C     . MET A 1 403 ? 138.209 160.066 136.255 1.00 65.67  ? 413  MET B C     1 
ATOM   3153  O  O     . MET A 1 403 ? 138.117 159.669 137.418 1.00 67.13  ? 413  MET B O     1 
ATOM   3154  C  CB    . MET A 1 403 ? 138.453 162.440 135.443 1.00 61.58  ? 413  MET B CB    1 
ATOM   3155  C  CG    . MET A 1 403 ? 138.011 163.305 134.283 1.00 63.04  ? 413  MET B CG    1 
ATOM   3156  S  SD    . MET A 1 403 ? 139.390 163.972 133.349 1.00 75.59  ? 413  MET B SD    1 
ATOM   3157  C  CE    . MET A 1 403 ? 140.148 164.983 134.604 1.00 65.52  ? 413  MET B CE    1 
ATOM   3158  N  N     . ASP A 1 404 ? 138.950 159.438 135.346 1.00 76.73  ? 414  ASP B N     1 
ATOM   3159  C  CA    . ASP A 1 404 ? 139.706 158.232 135.642 1.00 74.33  ? 414  ASP B CA    1 
ATOM   3160  C  C     . ASP A 1 404 ? 141.146 158.421 135.192 1.00 73.69  ? 414  ASP B C     1 
ATOM   3161  O  O     . ASP A 1 404 ? 141.437 159.243 134.320 1.00 79.65  ? 414  ASP B O     1 
ATOM   3162  C  CB    . ASP A 1 404 ? 139.103 157.002 134.952 1.00 76.96  ? 414  ASP B CB    1 
ATOM   3163  C  CG    . ASP A 1 404 ? 137.824 156.533 135.610 1.00 78.90  ? 414  ASP B CG    1 
ATOM   3164  O  OD1   . ASP A 1 404 ? 136.809 157.255 135.519 1.00 77.71  ? 414  ASP B OD1   1 
ATOM   3165  O  OD2   . ASP A 1 404 ? 137.831 155.441 136.216 1.00 78.70  ? 414  ASP B OD2   1 
ATOM   3166  N  N     . GLU A 1 405 ? 142.048 157.651 135.804 1.00 63.09  ? 415  GLU B N     1 
ATOM   3167  C  CA    . GLU A 1 405 ? 143.453 157.710 135.417 1.00 68.51  ? 415  GLU B CA    1 
ATOM   3168  C  C     . GLU A 1 405 ? 143.657 157.250 133.980 1.00 76.54  ? 415  GLU B C     1 
ATOM   3169  O  O     . GLU A 1 405 ? 144.609 157.683 133.314 1.00 78.82  ? 415  GLU B O     1 
ATOM   3170  C  CB    . GLU A 1 405 ? 144.289 156.858 136.370 1.00 69.93  ? 415  GLU B CB    1 
ATOM   3171  C  CG    . GLU A 1 405 ? 143.992 157.110 137.835 1.00 71.80  ? 415  GLU B CG    1 
ATOM   3172  C  CD    . GLU A 1 405 ? 144.607 156.063 138.740 1.00 76.22  ? 415  GLU B CD    1 
ATOM   3173  O  OE1   . GLU A 1 405 ? 145.096 155.038 138.220 1.00 76.88  ? 415  GLU B OE1   1 
ATOM   3174  O  OE2   . GLU A 1 405 ? 144.601 156.263 139.973 1.00 74.14  ? 415  GLU B OE2   1 
ATOM   3175  N  N     . MET A 1 406 ? 142.777 156.376 133.486 1.00 71.34  ? 416  MET B N     1 
ATOM   3176  C  CA    . MET A 1 406 ? 142.895 155.912 132.110 1.00 66.37  ? 416  MET B CA    1 
ATOM   3177  C  C     . MET A 1 406 ? 142.716 157.059 131.126 1.00 65.92  ? 416  MET B C     1 
ATOM   3178  O  O     . MET A 1 406 ? 143.344 157.074 130.062 1.00 70.71  ? 416  MET B O     1 
ATOM   3179  C  CB    . MET A 1 406 ? 141.882 154.803 131.835 1.00 67.20  ? 416  MET B CB    1 
ATOM   3180  C  CG    . MET A 1 406 ? 142.327 153.439 132.324 1.00 72.41  ? 416  MET B CG    1 
ATOM   3181  S  SD    . MET A 1 406 ? 144.003 153.034 131.796 1.00 80.93  ? 416  MET B SD    1 
ATOM   3182  C  CE    . MET A 1 406 ? 143.833 153.098 130.016 1.00 68.25  ? 416  MET B CE    1 
ATOM   3183  N  N     . GLU A 1 407 ? 141.868 158.031 131.463 1.00 67.23  ? 417  GLU B N     1 
ATOM   3184  C  CA    . GLU A 1 407 ? 141.725 159.201 130.605 1.00 67.47  ? 417  GLU B CA    1 
ATOM   3185  C  C     . GLU A 1 407 ? 143.022 159.997 130.546 1.00 67.56  ? 417  GLU B C     1 
ATOM   3186  O  O     . GLU A 1 407 ? 143.415 160.483 129.478 1.00 77.33  ? 417  GLU B O     1 
ATOM   3187  C  CB    . GLU A 1 407 ? 140.572 160.076 131.091 1.00 67.70  ? 417  GLU B CB    1 
ATOM   3188  C  CG    . GLU A 1 407 ? 140.208 161.199 130.135 1.00 70.58  ? 417  GLU B CG    1 
ATOM   3189  C  CD    . GLU A 1 407 ? 138.934 161.911 130.535 1.00 76.29  ? 417  GLU B CD    1 
ATOM   3190  O  OE1   . GLU A 1 407 ? 138.320 161.510 131.546 1.00 76.00  ? 417  GLU B OE1   1 
ATOM   3191  O  OE2   . GLU A 1 407 ? 138.545 162.872 129.839 1.00 79.03  ? 417  GLU B OE2   1 
ATOM   3192  N  N     . PHE A 1 408 ? 143.706 160.133 131.683 1.00 53.01  ? 418  PHE B N     1 
ATOM   3193  C  CA    . PHE A 1 408 ? 144.994 160.817 131.695 1.00 53.28  ? 418  PHE B CA    1 
ATOM   3194  C  C     . PHE A 1 408 ? 146.016 160.074 130.846 1.00 57.22  ? 418  PHE B C     1 
ATOM   3195  O  O     . PHE A 1 408 ? 146.770 160.693 130.083 1.00 65.67  ? 418  PHE B O     1 
ATOM   3196  C  CB    . PHE A 1 408 ? 145.494 160.960 133.129 1.00 60.21  ? 418  PHE B CB    1 
ATOM   3197  C  CG    . PHE A 1 408 ? 144.720 161.949 133.942 1.00 58.91  ? 418  PHE B CG    1 
ATOM   3198  C  CD1   . PHE A 1 408 ? 145.024 163.292 133.896 1.00 55.54  ? 418  PHE B CD1   1 
ATOM   3199  C  CD2   . PHE A 1 408 ? 143.681 161.532 134.749 1.00 57.26  ? 418  PHE B CD2   1 
ATOM   3200  C  CE1   . PHE A 1 408 ? 144.309 164.196 134.637 1.00 56.72  ? 418  PHE B CE1   1 
ATOM   3201  C  CE2   . PHE A 1 408 ? 142.966 162.436 135.495 1.00 56.93  ? 418  PHE B CE2   1 
ATOM   3202  C  CZ    . PHE A 1 408 ? 143.284 163.768 135.440 1.00 57.77  ? 418  PHE B CZ    1 
ATOM   3203  N  N     . THR A 1 409 ? 146.052 158.745 130.960 1.00 59.80  ? 419  THR B N     1 
ATOM   3204  C  CA    . THR A 1 409 ? 146.991 157.971 130.154 1.00 56.45  ? 419  THR B CA    1 
ATOM   3205  C  C     . THR A 1 409 ? 146.680 158.098 128.667 1.00 58.61  ? 419  THR B C     1 
ATOM   3206  O  O     . THR A 1 409 ? 147.597 158.207 127.845 1.00 65.22  ? 419  THR B O     1 
ATOM   3207  C  CB    . THR A 1 409 ? 146.976 156.504 130.577 1.00 58.89  ? 419  THR B CB    1 
ATOM   3208  O  OG1   . THR A 1 409 ? 145.639 155.997 130.501 1.00 71.81  ? 419  THR B OG1   1 
ATOM   3209  C  CG2   . THR A 1 409 ? 147.486 156.358 131.999 1.00 60.51  ? 419  THR B CG2   1 
ATOM   3210  N  N     . GLU A 1 410 ? 145.397 158.081 128.302 1.00 58.84  ? 420  GLU B N     1 
ATOM   3211  C  CA    . GLU A 1 410 ? 145.023 158.229 126.900 1.00 59.47  ? 420  GLU B CA    1 
ATOM   3212  C  C     . GLU A 1 410 ? 145.403 159.603 126.367 1.00 63.42  ? 420  GLU B C     1 
ATOM   3213  O  O     . GLU A 1 410 ? 145.884 159.726 125.234 1.00 68.28  ? 420  GLU B O     1 
ATOM   3214  C  CB    . GLU A 1 410 ? 143.526 157.987 126.725 1.00 59.90  ? 420  GLU B CB    1 
ATOM   3215  C  CG    . GLU A 1 410 ? 143.119 156.538 126.863 1.00 64.47  ? 420  GLU B CG    1 
ATOM   3216  C  CD    . GLU A 1 410 ? 141.620 156.360 126.880 1.00 70.71  ? 420  GLU B CD    1 
ATOM   3217  O  OE1   . GLU A 1 410 ? 140.906 157.309 126.495 1.00 70.58  ? 420  GLU B OE1   1 
ATOM   3218  O  OE2   . GLU A 1 410 ? 141.154 155.275 127.283 1.00 72.12  ? 420  GLU B OE2   1 
ATOM   3219  N  N     . ALA A 1 411 ? 145.186 160.650 127.164 1.00 53.89  ? 421  ALA B N     1 
ATOM   3220  C  CA    . ALA A 1 411 ? 145.589 161.988 126.746 1.00 50.51  ? 421  ALA B CA    1 
ATOM   3221  C  C     . ALA A 1 411 ? 147.097 162.073 126.552 1.00 53.60  ? 421  ALA B C     1 
ATOM   3222  O  O     . ALA A 1 411 ? 147.574 162.667 125.576 1.00 60.45  ? 421  ALA B O     1 
ATOM   3223  C  CB    . ALA A 1 411 ? 145.118 163.018 127.770 1.00 50.71  ? 421  ALA B CB    1 
ATOM   3224  N  N     . GLU A 1 412 ? 147.865 161.478 127.468 1.00 55.86  ? 422  GLU B N     1 
ATOM   3225  C  CA    . GLU A 1 412 ? 149.317 161.495 127.331 1.00 54.70  ? 422  GLU B CA    1 
ATOM   3226  C  C     . GLU A 1 412 ? 149.763 160.729 126.092 1.00 59.01  ? 422  GLU B C     1 
ATOM   3227  O  O     . GLU A 1 412 ? 150.675 161.164 125.379 1.00 65.74  ? 422  GLU B O     1 
ATOM   3228  C  CB    . GLU A 1 412 ? 149.968 160.921 128.588 1.00 55.67  ? 422  GLU B CB    1 
ATOM   3229  C  CG    . GLU A 1 412 ? 151.459 161.178 128.694 1.00 60.63  ? 422  GLU B CG    1 
ATOM   3230  C  CD    . GLU A 1 412 ? 152.287 160.026 128.165 1.00 68.76  ? 422  GLU B CD    1 
ATOM   3231  O  OE1   . GLU A 1 412 ? 151.718 158.937 127.938 1.00 70.74  ? 422  GLU B OE1   1 
ATOM   3232  O  OE2   . GLU A 1 412 ? 153.508 160.207 127.975 1.00 67.67  ? 422  GLU B OE2   1 
ATOM   3233  N  N     . SER A 1 413 ? 149.128 159.588 125.817 1.00 51.56  ? 423  SER B N     1 
ATOM   3234  C  CA    . SER A 1 413 ? 149.470 158.818 124.625 1.00 50.31  ? 423  SER B CA    1 
ATOM   3235  C  C     . SER A 1 413 ? 149.143 159.590 123.355 1.00 55.77  ? 423  SER B C     1 
ATOM   3236  O  O     . SER A 1 413 ? 149.911 159.559 122.387 1.00 58.87  ? 423  SER B O     1 
ATOM   3237  C  CB    . SER A 1 413 ? 148.740 157.477 124.638 1.00 55.24  ? 423  SER B CB    1 
ATOM   3238  O  OG    . SER A 1 413 ? 147.338 157.663 124.613 1.00 61.40  ? 423  SER B OG    1 
ATOM   3239  N  N     . ASN A 1 414 ? 148.002 160.282 123.335 1.00 54.67  ? 424  ASN B N     1 
ATOM   3240  C  CA    . ASN A 1 414 ? 147.648 161.096 122.177 1.00 44.65  ? 424  ASN B CA    1 
ATOM   3241  C  C     . ASN A 1 414 ? 148.653 162.219 121.965 1.00 49.47  ? 424  ASN B C     1 
ATOM   3242  O  O     . ASN A 1 414 ? 149.067 162.494 120.830 1.00 54.11  ? 424  ASN B O     1 
ATOM   3243  C  CB    . ASN A 1 414 ? 146.244 161.663 122.353 1.00 47.32  ? 424  ASN B CB    1 
ATOM   3244  C  CG    . ASN A 1 414 ? 145.429 161.597 121.087 1.00 53.95  ? 424  ASN B CG    1 
ATOM   3245  O  OD1   . ASN A 1 414 ? 145.588 160.684 120.281 1.00 59.93  ? 424  ASN B OD1   1 
ATOM   3246  N  ND2   . ASN A 1 414 ? 144.549 162.570 120.900 1.00 54.42  ? 424  ASN B ND2   1 
ATOM   3247  N  N     . MET A 1 415 ? 149.058 162.879 123.050 1.00 49.79  ? 425  MET B N     1 
ATOM   3248  C  CA    . MET A 1 415 ? 150.061 163.933 122.948 1.00 46.71  ? 425  MET B CA    1 
ATOM   3249  C  C     . MET A 1 415 ? 151.379 163.386 122.416 1.00 54.08  ? 425  MET B C     1 
ATOM   3250  O  O     . MET A 1 415 ? 152.023 164.006 121.558 1.00 63.06  ? 425  MET B O     1 
ATOM   3251  C  CB    . MET A 1 415 ? 150.255 164.587 124.316 1.00 53.18  ? 425  MET B CB    1 
ATOM   3252  C  CG    . MET A 1 415 ? 150.960 165.925 124.293 1.00 57.57  ? 425  MET B CG    1 
ATOM   3253  S  SD    . MET A 1 415 ? 149.847 167.277 123.893 1.00 67.44  ? 425  MET B SD    1 
ATOM   3254  C  CE    . MET A 1 415 ? 150.014 167.312 122.111 1.00 60.47  ? 425  MET B CE    1 
ATOM   3255  N  N     . ASN A 1 416 ? 151.791 162.218 122.908 1.00 47.76  ? 426  ASN B N     1 
ATOM   3256  C  CA    . ASN A 1 416 ? 153.032 161.610 122.443 1.00 46.10  ? 426  ASN B CA    1 
ATOM   3257  C  C     . ASN A 1 416 ? 152.944 161.234 120.971 1.00 51.13  ? 426  ASN B C     1 
ATOM   3258  O  O     . ASN A 1 416 ? 153.920 161.381 120.228 1.00 60.08  ? 426  ASN B O     1 
ATOM   3259  C  CB    . ASN A 1 416 ? 153.360 160.383 123.289 1.00 51.32  ? 426  ASN B CB    1 
ATOM   3260  C  CG    . ASN A 1 416 ? 153.990 160.745 124.611 1.00 55.93  ? 426  ASN B CG    1 
ATOM   3261  O  OD1   . ASN A 1 416 ? 154.478 161.858 124.794 1.00 60.92  ? 426  ASN B OD1   1 
ATOM   3262  N  ND2   . ASN A 1 416 ? 153.986 159.803 125.545 1.00 56.50  ? 426  ASN B ND2   1 
ATOM   3263  N  N     . ASP A 1 417 ? 151.789 160.732 120.533 1.00 54.60  ? 427  ASP B N     1 
ATOM   3264  C  CA    . ASP A 1 417 ? 151.620 160.388 119.126 1.00 53.33  ? 427  ASP B CA    1 
ATOM   3265  C  C     . ASP A 1 417 ? 151.685 161.626 118.242 1.00 54.12  ? 427  ASP B C     1 
ATOM   3266  O  O     . ASP A 1 417 ? 152.267 161.587 117.152 1.00 61.57  ? 427  ASP B O     1 
ATOM   3267  C  CB    . ASP A 1 417 ? 150.304 159.643 118.918 1.00 60.93  ? 427  ASP B CB    1 
ATOM   3268  C  CG    . ASP A 1 417 ? 150.372 158.207 119.386 1.00 66.46  ? 427  ASP B CG    1 
ATOM   3269  O  OD1   . ASP A 1 417 ? 151.387 157.832 120.008 1.00 67.80  ? 427  ASP B OD1   1 
ATOM   3270  O  OD2   . ASP A 1 417 ? 149.414 157.449 119.130 1.00 64.05  ? 427  ASP B OD2   1 
ATOM   3271  N  N     . LEU A 1 418 ? 151.094 162.734 118.691 1.00 51.40  ? 428  LEU B N     1 
ATOM   3272  C  CA    . LEU A 1 418 ? 151.199 163.978 117.932 1.00 53.46  ? 428  LEU B CA    1 
ATOM   3273  C  C     . LEU A 1 418 ? 152.647 164.453 117.851 1.00 51.93  ? 428  LEU B C     1 
ATOM   3274  O  O     . LEU A 1 418 ? 153.111 164.894 116.788 1.00 53.54  ? 428  LEU B O     1 
ATOM   3275  C  CB    . LEU A 1 418 ? 150.308 165.046 118.559 1.00 53.28  ? 428  LEU B CB    1 
ATOM   3276  C  CG    . LEU A 1 418 ? 150.214 166.383 117.834 1.00 51.87  ? 428  LEU B CG    1 
ATOM   3277  C  CD1   . LEU A 1 418 ? 149.709 166.176 116.423 1.00 53.93  ? 428  LEU B CD1   1 
ATOM   3278  C  CD2   . LEU A 1 418 ? 149.293 167.306 118.586 1.00 47.02  ? 428  LEU B CD2   1 
ATOM   3279  N  N     . VAL A 1 419 ? 153.382 164.350 118.961 1.00 44.64  ? 429  VAL B N     1 
ATOM   3280  C  CA    . VAL A 1 419 ? 154.797 164.712 118.958 1.00 41.39  ? 429  VAL B CA    1 
ATOM   3281  C  C     . VAL A 1 419 ? 155.573 163.835 117.984 1.00 47.00  ? 429  VAL B C     1 
ATOM   3282  O  O     . VAL A 1 419 ? 156.434 164.319 117.238 1.00 51.58  ? 429  VAL B O     1 
ATOM   3283  C  CB    . VAL A 1 419 ? 155.372 164.622 120.382 1.00 51.27  ? 429  VAL B CB    1 
ATOM   3284  C  CG1   . VAL A 1 419 ? 156.884 164.689 120.349 1.00 51.05  ? 429  VAL B CG1   1 
ATOM   3285  C  CG2   . VAL A 1 419 ? 154.812 165.737 121.243 1.00 55.75  ? 429  VAL B CG2   1 
ATOM   3286  N  N     . SER A 1 420 ? 155.287 162.533 117.979 1.00 52.09  ? 430  SER B N     1 
ATOM   3287  C  CA    . SER A 1 420 ? 155.980 161.621 117.076 1.00 48.53  ? 430  SER B CA    1 
ATOM   3288  C  C     . SER A 1 420 ? 155.673 161.945 115.622 1.00 53.49  ? 430  SER B C     1 
ATOM   3289  O  O     . SER A 1 420 ? 156.563 161.888 114.765 1.00 59.63  ? 430  SER B O     1 
ATOM   3290  C  CB    . SER A 1 420 ? 155.598 160.176 117.392 1.00 53.28  ? 430  SER B CB    1 
ATOM   3291  O  OG    . SER A 1 420 ? 156.118 159.774 118.646 1.00 60.99  ? 430  SER B OG    1 
ATOM   3292  N  N     . GLU A 1 421 ? 154.417 162.278 115.322 1.00 59.26  ? 431  GLU B N     1 
ATOM   3293  C  CA    . GLU A 1 421 ? 154.057 162.639 113.955 1.00 56.81  ? 431  GLU B CA    1 
ATOM   3294  C  C     . GLU A 1 421 ? 154.799 163.889 113.511 1.00 55.92  ? 431  GLU B C     1 
ATOM   3295  O  O     . GLU A 1 421 ? 155.282 163.969 112.376 1.00 57.64  ? 431  GLU B O     1 
ATOM   3296  C  CB    . GLU A 1 421 ? 152.549 162.844 113.839 1.00 57.17  ? 431  GLU B CB    1 
ATOM   3297  C  CG    . GLU A 1 421 ? 152.084 163.162 112.431 1.00 64.29  ? 431  GLU B CG    1 
ATOM   3298  C  CD    . GLU A 1 421 ? 150.575 163.215 112.311 1.00 68.35  ? 431  GLU B CD    1 
ATOM   3299  O  OE1   . GLU A 1 421 ? 149.889 163.028 113.338 1.00 67.60  ? 431  GLU B OE1   1 
ATOM   3300  O  OE2   . GLU A 1 421 ? 150.074 163.442 111.190 1.00 65.12  ? 431  GLU B OE2   1 
ATOM   3301  N  N     . TYR A 1 422 ? 154.896 164.883 114.393 1.00 53.49  ? 432  TYR B N     1 
ATOM   3302  C  CA    . TYR A 1 422 ? 155.634 166.092 114.039 1.00 50.92  ? 432  TYR B CA    1 
ATOM   3303  C  C     . TYR A 1 422 ? 157.118 165.804 113.849 1.00 48.51  ? 432  TYR B C     1 
ATOM   3304  O  O     . TYR A 1 422 ? 157.755 166.360 112.948 1.00 58.43  ? 432  TYR B O     1 
ATOM   3305  C  CB    . TYR A 1 422 ? 155.420 167.172 115.094 1.00 54.20  ? 432  TYR B CB    1 
ATOM   3306  C  CG    . TYR A 1 422 ? 154.361 168.169 114.705 1.00 50.69  ? 432  TYR B CG    1 
ATOM   3307  C  CD1   . TYR A 1 422 ? 154.521 168.971 113.589 1.00 51.38  ? 432  TYR B CD1   1 
ATOM   3308  C  CD2   . TYR A 1 422 ? 153.199 168.303 115.443 1.00 50.41  ? 432  TYR B CD2   1 
ATOM   3309  C  CE1   . TYR A 1 422 ? 153.557 169.882 113.223 1.00 54.45  ? 432  TYR B CE1   1 
ATOM   3310  C  CE2   . TYR A 1 422 ? 152.231 169.211 115.085 1.00 51.51  ? 432  TYR B CE2   1 
ATOM   3311  C  CZ    . TYR A 1 422 ? 152.415 169.999 113.975 1.00 53.37  ? 432  TYR B CZ    1 
ATOM   3312  O  OH    . TYR A 1 422 ? 151.450 170.908 113.613 1.00 51.30  ? 432  TYR B OH    1 
ATOM   3313  N  N     . GLN A 1 423 ? 157.691 164.945 114.694 1.00 50.44  ? 433  GLN B N     1 
ATOM   3314  C  CA    . GLN A 1 423 ? 159.107 164.617 114.562 1.00 50.64  ? 433  GLN B CA    1 
ATOM   3315  C  C     . GLN A 1 423 ? 159.378 163.830 113.287 1.00 50.31  ? 433  GLN B C     1 
ATOM   3316  O  O     . GLN A 1 423 ? 160.466 163.929 112.710 1.00 53.54  ? 433  GLN B O     1 
ATOM   3317  C  CB    . GLN A 1 423 ? 159.582 163.830 115.782 1.00 54.44  ? 433  GLN B CB    1 
ATOM   3318  C  CG    . GLN A 1 423 ? 160.769 164.448 116.495 1.00 56.11  ? 433  GLN B CG    1 
ATOM   3319  C  CD    . GLN A 1 423 ? 162.075 164.230 115.758 1.00 65.25  ? 433  GLN B CD    1 
ATOM   3320  O  OE1   . GLN A 1 423 ? 162.164 163.392 114.862 1.00 66.79  ? 433  GLN B OE1   1 
ATOM   3321  N  NE2   . GLN A 1 423 ? 163.099 164.986 116.135 1.00 63.49  ? 433  GLN B NE2   1 
ATOM   3322  N  N     . GLN A 1 424 ? 158.404 163.038 112.838 1.00 57.01  ? 434  GLN B N     1 
ATOM   3323  C  CA    . GLN A 1 424 ? 158.614 162.196 111.666 1.00 54.93  ? 434  GLN B CA    1 
ATOM   3324  C  C     . GLN A 1 424 ? 158.867 163.031 110.419 1.00 60.49  ? 434  GLN B C     1 
ATOM   3325  O  O     . GLN A 1 424 ? 159.734 162.695 109.603 1.00 63.89  ? 434  GLN B O     1 
ATOM   3326  C  CB    . GLN A 1 424 ? 157.412 161.279 111.460 1.00 55.72  ? 434  GLN B CB    1 
ATOM   3327  C  CG    . GLN A 1 424 ? 157.501 160.414 110.221 1.00 59.24  ? 434  GLN B CG    1 
ATOM   3328  C  CD    . GLN A 1 424 ? 156.152 160.180 109.579 1.00 64.55  ? 434  GLN B CD    1 
ATOM   3329  O  OE1   . GLN A 1 424 ? 155.192 160.902 109.845 1.00 62.85  ? 434  GLN B OE1   1 
ATOM   3330  N  NE2   . GLN A 1 424 ? 156.070 159.164 108.728 1.00 61.87  ? 434  GLN B NE2   1 
ATOM   3331  N  N     . TYR A 1 425 ? 158.126 164.126 110.256 1.00 56.19  ? 435  TYR B N     1 
ATOM   3332  C  CA    . TYR A 1 425 ? 158.212 164.959 109.064 1.00 49.68  ? 435  TYR B CA    1 
ATOM   3333  C  C     . TYR A 1 425 ? 159.296 166.019 109.172 1.00 52.77  ? 435  TYR B C     1 
ATOM   3334  O  O     . TYR A 1 425 ? 159.230 167.045 108.482 1.00 64.03  ? 435  TYR B O     1 
ATOM   3335  C  CB    . TYR A 1 425 ? 156.856 165.607 108.787 1.00 49.87  ? 435  TYR B CB    1 
ATOM   3336  C  CG    . TYR A 1 425 ? 155.804 164.616 108.361 1.00 48.99  ? 435  TYR B CG    1 
ATOM   3337  C  CD1   . TYR A 1 425 ? 156.039 163.725 107.328 1.00 52.27  ? 435  TYR B CD1   1 
ATOM   3338  C  CD2   . TYR A 1 425 ? 154.585 164.553 109.016 1.00 56.03  ? 435  TYR B CD2   1 
ATOM   3339  C  CE1   . TYR A 1 425 ? 155.081 162.812 106.947 1.00 58.10  ? 435  TYR B CE1   1 
ATOM   3340  C  CE2   . TYR A 1 425 ? 153.623 163.642 108.643 1.00 58.43  ? 435  TYR B CE2   1 
ATOM   3341  C  CZ    . TYR A 1 425 ? 153.876 162.773 107.609 1.00 61.65  ? 435  TYR B CZ    1 
ATOM   3342  O  OH    . TYR A 1 425 ? 152.917 161.863 107.233 1.00 61.33  ? 435  TYR B OH    1 
ATOM   3343  N  N     . GLN A 1 426 ? 160.290 165.803 110.023 1.00 52.41  ? 436  GLN B N     1 
ATOM   3344  C  CA    . GLN A 1 426 ? 161.375 166.755 110.192 1.00 53.16  ? 436  GLN B CA    1 
ATOM   3345  C  C     . GLN A 1 426 ? 162.682 166.200 109.632 1.00 61.68  ? 436  GLN B C     1 
ATOM   3346  O  O     . GLN A 1 426 ? 163.007 165.028 109.811 1.00 62.97  ? 436  GLN B O     1 
ATOM   3347  C  CB    . GLN A 1 426 ? 161.540 167.108 111.668 1.00 56.95  ? 436  GLN B CB    1 
ATOM   3348  C  CG    . GLN A 1 426 ? 162.564 168.185 111.938 1.00 55.68  ? 436  GLN B CG    1 
ATOM   3349  C  CD    . GLN A 1 426 ? 162.652 168.538 113.405 1.00 60.55  ? 436  GLN B CD    1 
ATOM   3350  O  OE1   . GLN A 1 426 ? 163.116 169.617 113.769 1.00 59.94  ? 436  GLN B OE1   1 
ATOM   3351  N  NE2   . GLN A 1 426 ? 162.206 167.627 114.260 1.00 57.49  ? 436  GLN B NE2   1 
ATOM   3352  N  N     . ASP B 2 3   ? 160.574 134.215 122.481 1.00 128.64 ? 3    ASP K N     1 
ATOM   3353  C  CA    . ASP B 2 3   ? 159.182 134.497 122.811 1.00 130.48 ? 3    ASP K CA    1 
ATOM   3354  C  C     . ASP B 2 3   ? 158.479 135.207 121.660 1.00 131.35 ? 3    ASP K C     1 
ATOM   3355  O  O     . ASP B 2 3   ? 157.334 135.639 121.792 1.00 129.45 ? 3    ASP K O     1 
ATOM   3356  C  CB    . ASP B 2 3   ? 159.092 135.344 124.082 1.00 130.72 ? 3    ASP K CB    1 
ATOM   3357  C  CG    . ASP B 2 3   ? 159.624 136.752 123.884 1.00 131.07 ? 3    ASP K CG    1 
ATOM   3358  O  OD1   . ASP B 2 3   ? 160.594 136.921 123.115 1.00 130.43 ? 3    ASP K OD1   1 
ATOM   3359  O  OD2   . ASP B 2 3   ? 159.072 137.689 124.497 1.00 129.46 ? 3    ASP K OD2   1 
ATOM   3360  N  N     . LEU B 2 4   ? 159.171 135.323 120.529 1.00 119.56 ? 4    LEU K N     1 
ATOM   3361  C  CA    . LEU B 2 4   ? 158.658 136.032 119.366 1.00 118.32 ? 4    LEU K CA    1 
ATOM   3362  C  C     . LEU B 2 4   ? 158.670 135.107 118.160 1.00 118.43 ? 4    LEU K C     1 
ATOM   3363  O  O     . LEU B 2 4   ? 159.682 134.455 117.882 1.00 117.46 ? 4    LEU K O     1 
ATOM   3364  C  CB    . LEU B 2 4   ? 159.485 137.290 119.076 1.00 116.31 ? 4    LEU K CB    1 
ATOM   3365  C  CG    . LEU B 2 4   ? 159.132 138.053 117.798 1.00 115.31 ? 4    LEU K CG    1 
ATOM   3366  C  CD1   . LEU B 2 4   ? 157.651 138.385 117.770 1.00 114.91 ? 4    LEU K CD1   1 
ATOM   3367  C  CD2   . LEU B 2 4   ? 159.971 139.315 117.673 1.00 114.74 ? 4    LEU K CD2   1 
ATOM   3368  N  N     . ALA B 2 5   ? 157.545 135.054 117.448 1.00 102.86 ? 5    ALA K N     1 
ATOM   3369  C  CA    . ALA B 2 5   ? 157.409 134.293 116.207 1.00 101.33 ? 5    ALA K CA    1 
ATOM   3370  C  C     . ALA B 2 5   ? 156.718 135.210 115.203 1.00 104.57 ? 5    ALA K C     1 
ATOM   3371  O  O     . ALA B 2 5   ? 155.487 135.276 115.154 1.00 106.20 ? 5    ALA K O     1 
ATOM   3372  C  CB    . ALA B 2 5   ? 156.632 132.999 116.430 1.00 100.66 ? 5    ALA K CB    1 
ATOM   3373  N  N     . GLU B 2 6   ? 157.515 135.919 114.409 1.00 88.40  ? 6    GLU K N     1 
ATOM   3374  C  CA    . GLU B 2 6   ? 156.968 136.883 113.466 1.00 82.24  ? 6    GLU K CA    1 
ATOM   3375  C  C     . GLU B 2 6   ? 156.211 136.181 112.346 1.00 82.70  ? 6    GLU K C     1 
ATOM   3376  O  O     . GLU B 2 6   ? 156.620 135.122 111.862 1.00 85.91  ? 6    GLU K O     1 
ATOM   3377  C  CB    . GLU B 2 6   ? 158.085 137.746 112.883 1.00 80.00  ? 6    GLU K CB    1 
ATOM   3378  C  CG    . GLU B 2 6   ? 159.185 136.963 112.192 1.00 84.49  ? 6    GLU K CG    1 
ATOM   3379  C  CD    . GLU B 2 6   ? 160.275 137.859 111.638 1.00 91.01  ? 6    GLU K CD    1 
ATOM   3380  O  OE1   . GLU B 2 6   ? 160.208 139.086 111.864 1.00 92.96  ? 6    GLU K OE1   1 
ATOM   3381  O  OE2   . GLU B 2 6   ? 161.198 137.338 110.977 1.00 89.22  ? 6    GLU K OE2   1 
ATOM   3382  N  N     . CYS B 2 7   ? 155.092 136.776 111.941 1.00 66.59  ? 7    CYS K N     1 
ATOM   3383  C  CA    . CYS B 2 7   ? 154.290 136.267 110.841 1.00 68.52  ? 7    CYS K CA    1 
ATOM   3384  C  C     . CYS B 2 7   ? 153.887 137.417 109.931 1.00 74.05  ? 7    CYS K C     1 
ATOM   3385  O  O     . CYS B 2 7   ? 153.710 138.553 110.378 1.00 80.98  ? 7    CYS K O     1 
ATOM   3386  C  CB    . CYS B 2 7   ? 153.038 135.540 111.342 1.00 68.11  ? 7    CYS K CB    1 
ATOM   3387  S  SG    . CYS B 2 7   ? 151.757 136.627 111.992 1.00 76.93  ? 7    CYS K SG    1 
ATOM   3388  N  N     . ASN B 2 8   ? 153.747 137.110 108.645 1.00 54.22  ? 8    ASN K N     1 
ATOM   3389  C  CA    . ASN B 2 8   ? 153.339 138.090 107.655 1.00 51.69  ? 8    ASN K CA    1 
ATOM   3390  C  C     . ASN B 2 8   ? 151.816 138.131 107.548 1.00 56.10  ? 8    ASN K C     1 
ATOM   3391  O  O     . ASN B 2 8   ? 151.095 137.465 108.293 1.00 57.81  ? 8    ASN K O     1 
ATOM   3392  C  CB    . ASN B 2 8   ? 153.978 137.769 106.308 1.00 52.60  ? 8    ASN K CB    1 
ATOM   3393  C  CG    . ASN B 2 8   ? 155.483 137.771 106.369 1.00 55.99  ? 8    ASN K CG    1 
ATOM   3394  O  OD1   . ASN B 2 8   ? 156.095 136.840 106.888 1.00 57.19  ? 8    ASN K OD1   1 
ATOM   3395  N  ND2   . ASN B 2 8   ? 156.095 138.821 105.836 1.00 58.70  ? 8    ASN K ND2   1 
ATOM   3396  N  N     . ILE B 2 9   ? 151.320 138.927 106.611 1.00 52.35  ? 9    ILE K N     1 
ATOM   3397  C  CA    . ILE B 2 9   ? 149.894 138.995 106.321 1.00 50.04  ? 9    ILE K CA    1 
ATOM   3398  C  C     . ILE B 2 9   ? 149.593 138.041 105.178 1.00 56.19  ? 9    ILE K C     1 
ATOM   3399  O  O     . ILE B 2 9   ? 150.234 138.099 104.123 1.00 60.10  ? 9    ILE K O     1 
ATOM   3400  C  CB    . ILE B 2 9   ? 149.469 140.426 105.960 1.00 49.23  ? 9    ILE K CB    1 
ATOM   3401  C  CG1   . ILE B 2 9   ? 150.364 141.437 106.662 1.00 59.73  ? 9    ILE K CG1   1 
ATOM   3402  C  CG2   . ILE B 2 9   ? 148.009 140.658 106.300 1.00 52.41  ? 9    ILE K CG2   1 
ATOM   3403  C  CD1   . ILE B 2 9   ? 150.191 141.512 108.141 1.00 56.38  ? 9    ILE K CD1   1 
ATOM   3404  N  N     . LYS B 2 10  ? 148.619 137.160 105.384 1.00 58.64  ? 10   LYS K N     1 
ATOM   3405  C  CA    . LYS B 2 10  ? 148.248 136.180 104.368 1.00 59.53  ? 10   LYS K CA    1 
ATOM   3406  C  C     . LYS B 2 10  ? 147.206 136.811 103.450 1.00 64.52  ? 10   LYS K C     1 
ATOM   3407  O  O     . LYS B 2 10  ? 146.005 136.549 103.536 1.00 72.27  ? 10   LYS K O     1 
ATOM   3408  C  CB    . LYS B 2 10  ? 147.738 134.903 105.020 1.00 63.03  ? 10   LYS K CB    1 
ATOM   3409  C  CG    . LYS B 2 10  ? 148.553 134.465 106.221 1.00 59.07  ? 10   LYS K CG    1 
ATOM   3410  C  CD    . LYS B 2 10  ? 149.923 133.974 105.801 1.00 65.16  ? 10   LYS K CD    1 
ATOM   3411  C  CE    . LYS B 2 10  ? 149.840 132.592 105.189 1.00 63.99  ? 10   LYS K CE    1 
ATOM   3412  N  NZ    . LYS B 2 10  ? 149.301 131.599 106.156 1.00 64.37  ? 10   LYS K NZ    1 
ATOM   3413  N  N     . VAL B 2 11  ? 147.687 137.660 102.550 1.00 51.66  ? 11   VAL K N     1 
ATOM   3414  C  CA    . VAL B 2 11  ? 146.829 138.328 101.579 1.00 51.26  ? 11   VAL K CA    1 
ATOM   3415  C  C     . VAL B 2 11  ? 146.545 137.355 100.445 1.00 54.28  ? 11   VAL K C     1 
ATOM   3416  O  O     . VAL B 2 11  ? 147.472 136.804 99.842  1.00 64.72  ? 11   VAL K O     1 
ATOM   3417  C  CB    . VAL B 2 11  ? 147.478 139.614 101.051 1.00 56.62  ? 11   VAL K CB    1 
ATOM   3418  C  CG1   . VAL B 2 11  ? 146.556 140.297 100.061 1.00 58.57  ? 11   VAL K CG1   1 
ATOM   3419  C  CG2   . VAL B 2 11  ? 147.815 140.546 102.201 1.00 60.46  ? 11   VAL K CG2   1 
ATOM   3420  N  N     . MET B 2 12  ? 145.266 137.139 100.156 1.00 53.05  ? 12   MET K N     1 
ATOM   3421  C  CA    . MET B 2 12  ? 144.848 136.248 99.086  1.00 52.85  ? 12   MET K CA    1 
ATOM   3422  C  C     . MET B 2 12  ? 143.775 136.922 98.245  1.00 51.86  ? 12   MET K C     1 
ATOM   3423  O  O     . MET B 2 12  ? 142.945 137.672 98.766  1.00 56.36  ? 12   MET K O     1 
ATOM   3424  C  CB    . MET B 2 12  ? 144.343 134.919 99.644  1.00 54.10  ? 12   MET K CB    1 
ATOM   3425  C  CG    . MET B 2 12  ? 143.862 134.992 101.069 1.00 57.01  ? 12   MET K CG    1 
ATOM   3426  S  SD    . MET B 2 12  ? 143.719 133.354 101.800 1.00 81.44  ? 12   MET K SD    1 
ATOM   3427  C  CE    . MET B 2 12  ? 145.439 132.866 101.865 1.00 59.14  ? 12   MET K CE    1 
ATOM   3428  N  N     . CYS B 2 13  ? 143.796 136.646 96.945  1.00 51.97  ? 13   CYS K N     1 
ATOM   3429  C  CA    . CYS B 2 13  ? 142.969 137.350 95.977  1.00 50.50  ? 13   CYS K CA    1 
ATOM   3430  C  C     . CYS B 2 13  ? 141.841 136.458 95.479  1.00 53.55  ? 13   CYS K C     1 
ATOM   3431  O  O     . CYS B 2 13  ? 142.033 135.261 95.250  1.00 64.20  ? 13   CYS K O     1 
ATOM   3432  C  CB    . CYS B 2 13  ? 143.811 137.826 94.795  1.00 54.70  ? 13   CYS K CB    1 
ATOM   3433  S  SG    . CYS B 2 13  ? 142.955 138.953 93.680  1.00 69.48  ? 13   CYS K SG    1 
ATOM   3434  N  N     . ARG B 2 14  ? 140.663 137.053 95.315  1.00 44.40  ? 14   ARG K N     1 
ATOM   3435  C  CA    . ARG B 2 14  ? 139.480 136.354 94.836  1.00 45.68  ? 14   ARG K CA    1 
ATOM   3436  C  C     . ARG B 2 14  ? 138.872 137.137 93.686  1.00 53.41  ? 14   ARG K C     1 
ATOM   3437  O  O     . ARG B 2 14  ? 138.624 138.340 93.814  1.00 63.80  ? 14   ARG K O     1 
ATOM   3438  C  CB    . ARG B 2 14  ? 138.456 136.179 95.953  1.00 42.79  ? 14   ARG K CB    1 
ATOM   3439  C  CG    . ARG B 2 14  ? 137.255 135.360 95.560  1.00 44.22  ? 14   ARG K CG    1 
ATOM   3440  C  CD    . ARG B 2 14  ? 136.371 135.120 96.755  1.00 49.51  ? 14   ARG K CD    1 
ATOM   3441  N  NE    . ARG B 2 14  ? 135.501 133.970 96.567  1.00 45.27  ? 14   ARG K NE    1 
ATOM   3442  C  CZ    . ARG B 2 14  ? 134.189 134.047 96.411  1.00 47.34  ? 14   ARG K CZ    1 
ATOM   3443  N  NH1   . ARG B 2 14  ? 133.561 135.210 96.425  1.00 52.15  ? 14   ARG K NH1   1 
ATOM   3444  N  NH2   . ARG B 2 14  ? 133.489 132.930 96.248  1.00 48.94  ? 14   ARG K NH2   1 
ATOM   3445  N  N     . PHE B 2 15  ? 138.627 136.458 92.572  1.00 50.41  ? 15   PHE K N     1 
ATOM   3446  C  CA    . PHE B 2 15  ? 138.093 137.081 91.370  1.00 46.30  ? 15   PHE K CA    1 
ATOM   3447  C  C     . PHE B 2 15  ? 136.656 136.624 91.173  1.00 52.56  ? 15   PHE K C     1 
ATOM   3448  O  O     . PHE B 2 15  ? 136.396 135.427 91.034  1.00 54.87  ? 15   PHE K O     1 
ATOM   3449  C  CB    . PHE B 2 15  ? 138.944 136.734 90.152  1.00 44.99  ? 15   PHE K CB    1 
ATOM   3450  C  CG    . PHE B 2 15  ? 140.058 137.700 89.902  1.00 47.94  ? 15   PHE K CG    1 
ATOM   3451  C  CD1   . PHE B 2 15  ? 141.288 137.531 90.505  1.00 46.75  ? 15   PHE K CD1   1 
ATOM   3452  C  CD2   . PHE B 2 15  ? 139.874 138.781 89.062  1.00 59.93  ? 15   PHE K CD2   1 
ATOM   3453  C  CE1   . PHE B 2 15  ? 142.311 138.421 90.274  1.00 52.68  ? 15   PHE K CE1   1 
ATOM   3454  C  CE2   . PHE B 2 15  ? 140.895 139.674 88.828  1.00 58.97  ? 15   PHE K CE2   1 
ATOM   3455  C  CZ    . PHE B 2 15  ? 142.114 139.494 89.437  1.00 53.45  ? 15   PHE K CZ    1 
ATOM   3456  N  N     . ARG B 2 16  ? 135.738 137.567 91.171  1.00 55.59  ? 16   ARG K N     1 
ATOM   3457  C  CA    . ARG B 2 16  ? 134.337 137.254 90.959  1.00 53.50  ? 16   ARG K CA    1 
ATOM   3458  C  C     . ARG B 2 16  ? 134.042 137.138 89.472  1.00 61.34  ? 16   ARG K C     1 
ATOM   3459  O  O     . ARG B 2 16  ? 134.756 137.702 88.639  1.00 67.80  ? 16   ARG K O     1 
ATOM   3460  C  CB    . ARG B 2 16  ? 133.458 138.333 91.586  1.00 52.49  ? 16   ARG K CB    1 
ATOM   3461  C  CG    . ARG B 2 16  ? 133.421 139.625 90.805  1.00 52.90  ? 16   ARG K CG    1 
ATOM   3462  C  CD    . ARG B 2 16  ? 132.119 140.357 91.023  1.00 53.22  ? 16   ARG K CD    1 
ATOM   3463  N  NE    . ARG B 2 16  ? 131.746 141.135 89.851  1.00 53.71  ? 16   ARG K NE    1 
ATOM   3464  C  CZ    . ARG B 2 16  ? 132.183 142.359 89.597  1.00 57.15  ? 16   ARG K CZ    1 
ATOM   3465  N  NH1   . ARG B 2 16  ? 133.008 142.982 90.421  1.00 62.89  ? 16   ARG K NH1   1 
ATOM   3466  N  NH2   . ARG B 2 16  ? 131.785 142.973 88.487  1.00 55.58  ? 16   ARG K NH2   1 
ATOM   3467  N  N     . PRO B 2 17  ? 133.003 136.397 89.100  1.00 56.04  ? 17   PRO K N     1 
ATOM   3468  C  CA    . PRO B 2 17  ? 132.611 136.342 87.690  1.00 55.08  ? 17   PRO K CA    1 
ATOM   3469  C  C     . PRO B 2 17  ? 132.041 137.669 87.222  1.00 58.98  ? 17   PRO K C     1 
ATOM   3470  O  O     . PRO B 2 17  ? 131.567 138.490 88.010  1.00 64.47  ? 17   PRO K O     1 
ATOM   3471  C  CB    . PRO B 2 17  ? 131.544 135.242 87.655  1.00 53.79  ? 17   PRO K CB    1 
ATOM   3472  C  CG    . PRO B 2 17  ? 131.692 134.504 88.938  1.00 53.43  ? 17   PRO K CG    1 
ATOM   3473  C  CD    . PRO B 2 17  ? 132.192 135.493 89.929  1.00 54.69  ? 17   PRO K CD    1 
ATOM   3474  N  N     . LEU B 2 18  ? 132.101 137.875 85.909  1.00 53.12  ? 18   LEU K N     1 
ATOM   3475  C  CA    . LEU B 2 18  ? 131.458 139.038 85.318  1.00 55.31  ? 18   LEU K CA    1 
ATOM   3476  C  C     . LEU B 2 18  ? 129.953 138.973 85.540  1.00 63.67  ? 18   LEU K C     1 
ATOM   3477  O  O     . LEU B 2 18  ? 129.336 137.912 85.414  1.00 66.06  ? 18   LEU K O     1 
ATOM   3478  C  CB    . LEU B 2 18  ? 131.768 139.117 83.825  1.00 53.67  ? 18   LEU K CB    1 
ATOM   3479  C  CG    . LEU B 2 18  ? 133.216 139.401 83.432  1.00 57.25  ? 18   LEU K CG    1 
ATOM   3480  C  CD1   . LEU B 2 18  ? 133.323 139.633 81.939  1.00 59.08  ? 18   LEU K CD1   1 
ATOM   3481  C  CD2   . LEU B 2 18  ? 133.757 140.588 84.201  1.00 63.23  ? 18   LEU K CD2   1 
ATOM   3482  N  N     . ASN B 2 19  ? 129.360 140.116 85.872  1.00 64.64  ? 19   ASN K N     1 
ATOM   3483  C  CA    . ASN B 2 19  ? 127.945 140.170 86.197  1.00 62.82  ? 19   ASN K CA    1 
ATOM   3484  C  C     . ASN B 2 19  ? 127.128 140.601 84.981  1.00 64.16  ? 19   ASN K C     1 
ATOM   3485  O  O     . ASN B 2 19  ? 127.662 140.890 83.909  1.00 67.95  ? 19   ASN K O     1 
ATOM   3486  C  CB    . ASN B 2 19  ? 127.707 141.101 87.382  1.00 62.45  ? 19   ASN K CB    1 
ATOM   3487  C  CG    . ASN B 2 19  ? 128.452 142.404 87.251  1.00 68.28  ? 19   ASN K CG    1 
ATOM   3488  O  OD1   . ASN B 2 19  ? 129.509 142.462 86.629  1.00 70.03  ? 19   ASN K OD1   1 
ATOM   3489  N  ND2   . ASN B 2 19  ? 127.906 143.462 87.835  1.00 67.92  ? 19   ASN K ND2   1 
ATOM   3490  N  N     . GLU B 2 20  ? 125.805 140.638 85.157  1.00 69.22  ? 20   GLU K N     1 
ATOM   3491  C  CA    . GLU B 2 20  ? 124.907 140.926 84.043  1.00 68.70  ? 20   GLU K CA    1 
ATOM   3492  C  C     . GLU B 2 20  ? 125.140 142.324 83.490  1.00 71.14  ? 20   GLU K C     1 
ATOM   3493  O  O     . GLU B 2 20  ? 125.182 142.523 82.272  1.00 75.50  ? 20   GLU K O     1 
ATOM   3494  C  CB    . GLU B 2 20  ? 123.452 140.765 84.484  1.00 68.62  ? 20   GLU K CB    1 
ATOM   3495  C  CG    . GLU B 2 20  ? 123.075 139.357 84.909  1.00 72.97  ? 20   GLU K CG    1 
ATOM   3496  C  CD    . GLU B 2 20  ? 121.603 139.226 85.257  1.00 77.99  ? 20   GLU K CD    1 
ATOM   3497  O  OE1   . GLU B 2 20  ? 120.893 140.254 85.256  1.00 76.47  ? 20   GLU K OE1   1 
ATOM   3498  O  OE2   . GLU B 2 20  ? 121.155 138.092 85.532  1.00 80.55  ? 20   GLU K OE2   1 
ATOM   3499  N  N     . SER B 2 21  ? 125.298 143.309 84.376  1.00 66.08  ? 21   SER K N     1 
ATOM   3500  C  CA    . SER B 2 21  ? 125.467 144.687 83.934  1.00 64.55  ? 21   SER K CA    1 
ATOM   3501  C  C     . SER B 2 21  ? 126.789 144.898 83.211  1.00 64.72  ? 21   SER K C     1 
ATOM   3502  O  O     . SER B 2 21  ? 126.958 145.918 82.535  1.00 67.51  ? 21   SER K O     1 
ATOM   3503  C  CB    . SER B 2 21  ? 125.359 145.629 85.134  1.00 64.51  ? 21   SER K CB    1 
ATOM   3504  O  OG    . SER B 2 21  ? 125.492 146.984 84.747  1.00 68.73  ? 21   SER K OG    1 
ATOM   3505  N  N     . GLU B 2 22  ? 127.718 143.951 83.326  1.00 67.28  ? 22   GLU K N     1 
ATOM   3506  C  CA    . GLU B 2 22  ? 129.054 144.065 82.758  1.00 64.77  ? 22   GLU K CA    1 
ATOM   3507  C  C     . GLU B 2 22  ? 129.287 143.110 81.595  1.00 67.69  ? 22   GLU K C     1 
ATOM   3508  O  O     . GLU B 2 22  ? 130.156 143.364 80.758  1.00 69.73  ? 22   GLU K O     1 
ATOM   3509  C  CB    . GLU B 2 22  ? 130.097 143.810 83.850  1.00 68.01  ? 22   GLU K CB    1 
ATOM   3510  C  CG    . GLU B 2 22  ? 131.391 144.574 83.686  1.00 67.89  ? 22   GLU K CG    1 
ATOM   3511  C  CD    . GLU B 2 22  ? 132.111 144.766 85.008  1.00 72.65  ? 22   GLU K CD    1 
ATOM   3512  O  OE1   . GLU B 2 22  ? 131.700 144.143 86.008  1.00 70.62  ? 22   GLU K OE1   1 
ATOM   3513  O  OE2   . GLU B 2 22  ? 133.051 145.585 85.062  1.00 73.02  ? 22   GLU K OE2   1 
ATOM   3514  N  N     . VAL B 2 23  ? 128.542 142.004 81.531  1.00 69.45  ? 23   VAL K N     1 
ATOM   3515  C  CA    . VAL B 2 23  ? 128.683 141.096 80.398  1.00 67.29  ? 23   VAL K CA    1 
ATOM   3516  C  C     . VAL B 2 23  ? 127.860 141.582 79.215  1.00 68.59  ? 23   VAL K C     1 
ATOM   3517  O  O     . VAL B 2 23  ? 128.185 141.284 78.059  1.00 71.62  ? 23   VAL K O     1 
ATOM   3518  C  CB    . VAL B 2 23  ? 128.302 139.658 80.801  1.00 68.45  ? 23   VAL K CB    1 
ATOM   3519  C  CG1   . VAL B 2 23  ? 126.804 139.534 81.039  1.00 68.69  ? 23   VAL K CG1   1 
ATOM   3520  C  CG2   . VAL B 2 23  ? 128.765 138.666 79.744  1.00 67.80  ? 23   VAL K CG2   1 
ATOM   3521  N  N     . ASN B 2 24  ? 126.799 142.344 79.468  1.00 64.40  ? 24   ASN K N     1 
ATOM   3522  C  CA    . ASN B 2 24  ? 125.961 142.841 78.388  1.00 65.72  ? 24   ASN K CA    1 
ATOM   3523  C  C     . ASN B 2 24  ? 126.477 144.140 77.788  1.00 68.06  ? 24   ASN K C     1 
ATOM   3524  O  O     . ASN B 2 24  ? 125.861 144.656 76.850  1.00 73.95  ? 24   ASN K O     1 
ATOM   3525  C  CB    . ASN B 2 24  ? 124.522 143.030 78.876  1.00 64.00  ? 24   ASN K CB    1 
ATOM   3526  C  CG    . ASN B 2 24  ? 124.397 144.096 79.946  1.00 69.49  ? 24   ASN K CG    1 
ATOM   3527  O  OD1   . ASN B 2 24  ? 125.389 144.668 80.397  1.00 73.14  ? 24   ASN K OD1   1 
ATOM   3528  N  ND2   . ASN B 2 24  ? 123.166 144.367 80.362  1.00 67.32  ? 24   ASN K ND2   1 
ATOM   3529  N  N     . ARG B 2 25  ? 127.580 144.683 78.303  1.00 62.56  ? 25   ARG K N     1 
ATOM   3530  C  CA    . ARG B 2 25  ? 128.170 145.916 77.784  1.00 62.30  ? 25   ARG K CA    1 
ATOM   3531  C  C     . ARG B 2 25  ? 129.660 145.678 77.540  1.00 66.50  ? 25   ARG K C     1 
ATOM   3532  O  O     . ARG B 2 25  ? 130.494 145.974 78.399  1.00 74.10  ? 25   ARG K O     1 
ATOM   3533  C  CB    . ARG B 2 25  ? 127.919 147.067 78.751  1.00 65.27  ? 25   ARG K CB    1 
ATOM   3534  C  CG    . ARG B 2 25  ? 128.580 148.378 78.375  1.00 70.03  ? 25   ARG K CG    1 
ATOM   3535  C  CD    . ARG B 2 25  ? 128.961 149.146 79.628  1.00 69.98  ? 25   ARG K CD    1 
ATOM   3536  N  NE    . ARG B 2 25  ? 129.822 148.366 80.509  1.00 67.65  ? 25   ARG K NE    1 
ATOM   3537  C  CZ    . ARG B 2 25  ? 129.966 148.593 81.808  1.00 67.60  ? 25   ARG K CZ    1 
ATOM   3538  N  NH1   . ARG B 2 25  ? 129.309 149.567 82.416  1.00 68.78  ? 25   ARG K NH1   1 
ATOM   3539  N  NH2   . ARG B 2 25  ? 130.788 147.823 82.514  1.00 66.83  ? 25   ARG K NH2   1 
ATOM   3540  N  N     . GLY B 2 26  ? 129.974 145.121 76.371  1.00 68.33  ? 26   GLY K N     1 
ATOM   3541  C  CA    . GLY B 2 26  ? 131.305 145.114 75.787  1.00 68.93  ? 26   GLY K CA    1 
ATOM   3542  C  C     . GLY B 2 26  ? 132.499 145.063 76.719  1.00 69.02  ? 26   GLY K C     1 
ATOM   3543  O  O     . GLY B 2 26  ? 133.405 145.893 76.598  1.00 73.14  ? 26   GLY K O     1 
ATOM   3544  N  N     . ASP B 2 27  ? 132.524 144.115 77.650  1.00 65.62  ? 27   ASP K N     1 
ATOM   3545  C  CA    . ASP B 2 27  ? 133.615 144.003 78.606  1.00 68.22  ? 27   ASP K CA    1 
ATOM   3546  C  C     . ASP B 2 27  ? 134.310 142.659 78.452  1.00 69.97  ? 27   ASP K C     1 
ATOM   3547  O  O     . ASP B 2 27  ? 133.683 141.653 78.106  1.00 78.04  ? 27   ASP K O     1 
ATOM   3548  C  CB    . ASP B 2 27  ? 133.113 144.179 80.038  1.00 70.87  ? 27   ASP K CB    1 
ATOM   3549  C  CG    . ASP B 2 27  ? 132.906 145.635 80.403  1.00 78.77  ? 27   ASP K CG    1 
ATOM   3550  O  OD1   . ASP B 2 27  ? 133.830 146.442 80.168  1.00 74.88  ? 27   ASP K OD1   1 
ATOM   3551  O  OD2   . ASP B 2 27  ? 131.817 145.978 80.908  1.00 82.27  ? 27   ASP K OD2   1 
ATOM   3552  N  N     . LYS B 2 28  ? 135.614 142.649 78.713  1.00 57.86  ? 28   LYS K N     1 
ATOM   3553  C  CA    . LYS B 2 28  ? 136.450 141.482 78.474  1.00 61.78  ? 28   LYS K CA    1 
ATOM   3554  C  C     . LYS B 2 28  ? 137.168 141.061 79.748  1.00 64.77  ? 28   LYS K C     1 
ATOM   3555  O  O     . LYS B 2 28  ? 137.634 141.903 80.521  1.00 66.50  ? 28   LYS K O     1 
ATOM   3556  C  CB    . LYS B 2 28  ? 137.469 141.760 77.369  1.00 59.44  ? 28   LYS K CB    1 
ATOM   3557  C  CG    . LYS B 2 28  ? 138.031 143.164 77.394  1.00 61.06  ? 28   LYS K CG    1 
ATOM   3558  C  CD    . LYS B 2 28  ? 138.970 143.399 76.228  1.00 66.26  ? 28   LYS K CD    1 
ATOM   3559  C  CE    . LYS B 2 28  ? 138.299 143.057 74.909  1.00 67.14  ? 28   LYS K CE    1 
ATOM   3560  N  NZ    . LYS B 2 28  ? 137.046 143.833 74.701  1.00 67.60  ? 28   LYS K NZ    1 
ATOM   3561  N  N     . TYR B 2 29  ? 137.245 139.750 79.955  1.00 55.92  ? 29   TYR K N     1 
ATOM   3562  C  CA    . TYR B 2 29  ? 137.957 139.149 81.080  1.00 51.72  ? 29   TYR K CA    1 
ATOM   3563  C  C     . TYR B 2 29  ? 139.450 139.378 80.884  1.00 56.93  ? 29   TYR K C     1 
ATOM   3564  O  O     . TYR B 2 29  ? 140.086 138.729 80.052  1.00 62.92  ? 29   TYR K O     1 
ATOM   3565  C  CB    . TYR B 2 29  ? 137.627 137.663 81.156  1.00 53.62  ? 29   TYR K CB    1 
ATOM   3566  C  CG    . TYR B 2 29  ? 137.843 137.013 82.500  1.00 53.90  ? 29   TYR K CG    1 
ATOM   3567  C  CD1   . TYR B 2 29  ? 139.119 136.786 82.986  1.00 57.48  ? 29   TYR K CD1   1 
ATOM   3568  C  CD2   . TYR B 2 29  ? 136.771 136.586 83.262  1.00 51.60  ? 29   TYR K CD2   1 
ATOM   3569  C  CE1   . TYR B 2 29  ? 139.318 136.180 84.206  1.00 57.77  ? 29   TYR K CE1   1 
ATOM   3570  C  CE2   . TYR B 2 29  ? 136.960 135.979 84.480  1.00 54.08  ? 29   TYR K CE2   1 
ATOM   3571  C  CZ    . TYR B 2 29  ? 138.235 135.776 84.948  1.00 58.35  ? 29   TYR K CZ    1 
ATOM   3572  O  OH    . TYR B 2 29  ? 138.427 135.169 86.166  1.00 64.73  ? 29   TYR K OH    1 
ATOM   3573  N  N     . ILE B 2 30  ? 140.021 140.306 81.652  1.00 54.32  ? 30   ILE K N     1 
ATOM   3574  C  CA    . ILE B 2 30  ? 141.414 140.687 81.454  1.00 49.70  ? 30   ILE K CA    1 
ATOM   3575  C  C     . ILE B 2 30  ? 142.386 139.914 82.336  1.00 49.58  ? 30   ILE K C     1 
ATOM   3576  O  O     . ILE B 2 30  ? 143.591 139.908 82.052  1.00 50.99  ? 30   ILE K O     1 
ATOM   3577  C  CB    . ILE B 2 30  ? 141.608 142.194 81.695  1.00 54.48  ? 30   ILE K CB    1 
ATOM   3578  C  CG1   . ILE B 2 30  ? 141.276 142.547 83.144  1.00 54.50  ? 30   ILE K CG1   1 
ATOM   3579  C  CG2   . ILE B 2 30  ? 140.749 143.002 80.735  1.00 56.77  ? 30   ILE K CG2   1 
ATOM   3580  C  CD1   . ILE B 2 30  ? 141.521 143.993 83.487  1.00 57.28  ? 30   ILE K CD1   1 
ATOM   3581  N  N     . ALA B 2 31  ? 141.905 139.268 83.392  1.00 55.87  ? 31   ALA K N     1 
ATOM   3582  C  CA    . ALA B 2 31  ? 142.784 138.571 84.321  1.00 56.00  ? 31   ALA K CA    1 
ATOM   3583  C  C     . ALA B 2 31  ? 143.242 137.253 83.710  1.00 56.03  ? 31   ALA K C     1 
ATOM   3584  O  O     . ALA B 2 31  ? 142.418 136.446 83.270  1.00 60.45  ? 31   ALA K O     1 
ATOM   3585  C  CB    . ALA B 2 31  ? 142.071 138.333 85.649  1.00 56.14  ? 31   ALA K CB    1 
ATOM   3586  N  N     . LYS B 2 32  ? 144.554 137.037 83.686  1.00 51.49  ? 32   LYS K N     1 
ATOM   3587  C  CA    . LYS B 2 32  ? 145.149 135.792 83.219  1.00 48.10  ? 32   LYS K CA    1 
ATOM   3588  C  C     . LYS B 2 32  ? 145.881 135.149 84.385  1.00 52.98  ? 32   LYS K C     1 
ATOM   3589  O  O     . LYS B 2 32  ? 146.772 135.765 84.977  1.00 63.10  ? 32   LYS K O     1 
ATOM   3590  C  CB    . LYS B 2 32  ? 146.102 136.045 82.051  1.00 52.63  ? 32   LYS K CB    1 
ATOM   3591  C  CG    . LYS B 2 32  ? 146.221 134.885 81.082  1.00 58.58  ? 32   LYS K CG    1 
ATOM   3592  C  CD    . LYS B 2 32  ? 146.997 135.288 79.840  1.00 56.38  ? 32   LYS K CD    1 
ATOM   3593  C  CE    . LYS B 2 32  ? 146.411 136.537 79.204  1.00 56.70  ? 32   LYS K CE    1 
ATOM   3594  N  NZ    . LYS B 2 32  ? 144.974 136.362 78.858  1.00 55.50  ? 32   LYS K NZ    1 
ATOM   3595  N  N     . PHE B 2 33  ? 145.512 133.915 84.708  1.00 52.95  ? 33   PHE K N     1 
ATOM   3596  C  CA    . PHE B 2 33  ? 146.016 133.228 85.888  1.00 50.00  ? 33   PHE K CA    1 
ATOM   3597  C  C     . PHE B 2 33  ? 147.066 132.202 85.495  1.00 51.73  ? 33   PHE K C     1 
ATOM   3598  O  O     . PHE B 2 33  ? 146.815 131.343 84.643  1.00 56.64  ? 33   PHE K O     1 
ATOM   3599  C  CB    . PHE B 2 33  ? 144.879 132.539 86.640  1.00 50.64  ? 33   PHE K CB    1 
ATOM   3600  C  CG    . PHE B 2 33  ? 143.755 133.454 87.009  1.00 53.77  ? 33   PHE K CG    1 
ATOM   3601  C  CD1   . PHE B 2 33  ? 143.987 134.588 87.759  1.00 56.85  ? 33   PHE K CD1   1 
ATOM   3602  C  CD2   . PHE B 2 33  ? 142.464 133.180 86.602  1.00 54.68  ? 33   PHE K CD2   1 
ATOM   3603  C  CE1   . PHE B 2 33  ? 142.955 135.430 88.100  1.00 56.34  ? 33   PHE K CE1   1 
ATOM   3604  C  CE2   . PHE B 2 33  ? 141.426 134.020 86.940  1.00 57.35  ? 33   PHE K CE2   1 
ATOM   3605  C  CZ    . PHE B 2 33  ? 141.673 135.147 87.690  1.00 57.11  ? 33   PHE K CZ    1 
ATOM   3606  N  N     . GLN B 2 34  ? 148.234 132.289 86.120  1.00 58.69  ? 34   GLN K N     1 
ATOM   3607  C  CA    . GLN B 2 34  ? 149.279 131.292 85.973  1.00 63.02  ? 34   GLN K CA    1 
ATOM   3608  C  C     . GLN B 2 34  ? 149.637 130.746 87.346  1.00 65.30  ? 34   GLN K C     1 
ATOM   3609  O  O     . GLN B 2 34  ? 149.545 131.451 88.354  1.00 69.13  ? 34   GLN K O     1 
ATOM   3610  C  CB    . GLN B 2 34  ? 150.523 131.868 85.286  1.00 59.12  ? 34   GLN K CB    1 
ATOM   3611  C  CG    . GLN B 2 34  ? 151.233 132.950 86.070  1.00 58.24  ? 34   GLN K CG    1 
ATOM   3612  C  CD    . GLN B 2 34  ? 152.634 133.209 85.557  1.00 65.13  ? 34   GLN K CD    1 
ATOM   3613  O  OE1   . GLN B 2 34  ? 153.278 132.318 85.005  1.00 67.51  ? 34   GLN K OE1   1 
ATOM   3614  N  NE2   . GLN B 2 34  ? 153.114 134.433 85.735  1.00 66.56  ? 34   GLN K NE2   1 
ATOM   3615  N  N     . GLY B 2 35  ? 150.026 129.477 87.381  1.00 66.14  ? 35   GLY K N     1 
ATOM   3616  C  CA    . GLY B 2 35  ? 150.306 128.863 88.658  1.00 63.18  ? 35   GLY K CA    1 
ATOM   3617  C  C     . GLY B 2 35  ? 149.058 128.791 89.515  1.00 61.27  ? 35   GLY K C     1 
ATOM   3618  O  O     . GLY B 2 35  ? 147.926 128.756 89.024  1.00 61.50  ? 35   GLY K O     1 
ATOM   3619  N  N     . GLU B 2 36  ? 149.270 128.779 90.828  1.00 68.32  ? 36   GLU K N     1 
ATOM   3620  C  CA    . GLU B 2 36  ? 148.178 128.739 91.785  1.00 70.38  ? 36   GLU K CA    1 
ATOM   3621  C  C     . GLU B 2 36  ? 148.168 129.922 92.740  1.00 71.18  ? 36   GLU K C     1 
ATOM   3622  O  O     . GLU B 2 36  ? 147.257 130.016 93.569  1.00 68.87  ? 36   GLU K O     1 
ATOM   3623  C  CB    . GLU B 2 36  ? 148.231 127.435 92.597  1.00 72.34  ? 36   GLU K CB    1 
ATOM   3624  C  CG    . GLU B 2 36  ? 146.881 126.956 93.108  1.00 75.38  ? 36   GLU K CG    1 
ATOM   3625  C  CD    . GLU B 2 36  ? 146.981 125.666 93.898  1.00 75.86  ? 36   GLU K CD    1 
ATOM   3626  O  OE1   . GLU B 2 36  ? 148.115 125.203 94.142  1.00 75.97  ? 36   GLU K OE1   1 
ATOM   3627  O  OE2   . GLU B 2 36  ? 145.925 125.115 94.275  1.00 73.27  ? 36   GLU K OE2   1 
ATOM   3628  N  N     . ASP B 2 37  ? 149.140 130.830 92.644  1.00 69.30  ? 37   ASP K N     1 
ATOM   3629  C  CA    . ASP B 2 37  ? 149.255 131.929 93.586  1.00 69.10  ? 37   ASP K CA    1 
ATOM   3630  C  C     . ASP B 2 37  ? 149.556 133.275 92.943  1.00 69.27  ? 37   ASP K C     1 
ATOM   3631  O  O     . ASP B 2 37  ? 149.724 134.258 93.671  1.00 73.57  ? 37   ASP K O     1 
ATOM   3632  C  CB    . ASP B 2 37  ? 150.342 131.622 94.627  1.00 66.93  ? 37   ASP K CB    1 
ATOM   3633  C  CG    . ASP B 2 37  ? 151.654 131.209 93.991  1.00 69.70  ? 37   ASP K CG    1 
ATOM   3634  O  OD1   . ASP B 2 37  ? 151.692 131.051 92.754  1.00 69.87  ? 37   ASP K OD1   1 
ATOM   3635  O  OD2   . ASP B 2 37  ? 152.649 131.043 94.728  1.00 72.23  ? 37   ASP K OD2   1 
ATOM   3636  N  N     . THR B 2 38  ? 149.630 133.358 91.617  1.00 52.35  ? 38   THR K N     1 
ATOM   3637  C  CA    . THR B 2 38  ? 149.951 134.610 90.950  1.00 57.66  ? 38   THR K CA    1 
ATOM   3638  C  C     . THR B 2 38  ? 148.966 134.883 89.823  1.00 56.40  ? 38   THR K C     1 
ATOM   3639  O  O     . THR B 2 38  ? 148.464 133.963 89.173  1.00 59.31  ? 38   THR K O     1 
ATOM   3640  C  CB    . THR B 2 38  ? 151.388 134.614 90.404  1.00 58.89  ? 38   THR K CB    1 
ATOM   3641  O  OG1   . THR B 2 38  ? 151.588 135.769 89.581  1.00 60.51  ? 38   THR K OG1   1 
ATOM   3642  C  CG2   . THR B 2 38  ? 151.668 133.365 89.601  1.00 56.85  ? 38   THR K CG2   1 
ATOM   3643  N  N     . VAL B 2 39  ? 148.694 136.168 89.606  1.00 47.82  ? 39   VAL K N     1 
ATOM   3644  C  CA    . VAL B 2 39  ? 147.762 136.636 88.589  1.00 39.74  ? 39   VAL K CA    1 
ATOM   3645  C  C     . VAL B 2 39  ? 148.480 137.643 87.703  1.00 48.68  ? 39   VAL K C     1 
ATOM   3646  O  O     . VAL B 2 39  ? 149.242 138.482 88.194  1.00 56.28  ? 39   VAL K O     1 
ATOM   3647  C  CB    . VAL B 2 39  ? 146.497 137.258 89.220  1.00 42.33  ? 39   VAL K CB    1 
ATOM   3648  C  CG1   . VAL B 2 39  ? 146.868 138.351 90.199  1.00 50.45  ? 39   VAL K CG1   1 
ATOM   3649  C  CG2   . VAL B 2 39  ? 145.574 137.801 88.148  1.00 47.33  ? 39   VAL K CG2   1 
ATOM   3650  N  N     . VAL B 2 40  ? 148.257 137.546 86.396  1.00 48.94  ? 40   VAL K N     1 
ATOM   3651  C  CA    . VAL B 2 40  ? 148.880 138.432 85.420  1.00 46.77  ? 40   VAL K CA    1 
ATOM   3652  C  C     . VAL B 2 40  ? 147.809 139.352 84.851  1.00 52.86  ? 40   VAL K C     1 
ATOM   3653  O  O     . VAL B 2 40  ? 146.826 138.884 84.264  1.00 61.78  ? 40   VAL K O     1 
ATOM   3654  C  CB    . VAL B 2 40  ? 149.574 137.643 84.301  1.00 52.63  ? 40   VAL K CB    1 
ATOM   3655  C  CG1   . VAL B 2 40  ? 150.116 138.591 83.246  1.00 57.46  ? 40   VAL K CG1   1 
ATOM   3656  C  CG2   . VAL B 2 40  ? 150.687 136.784 84.874  1.00 54.43  ? 40   VAL K CG2   1 
ATOM   3657  N  N     . ILE B 2 41  ? 147.997 140.657 85.025  1.00 49.98  ? 41   ILE K N     1 
ATOM   3658  C  CA    . ILE B 2 41  ? 147.107 141.671 84.474  1.00 50.54  ? 41   ILE K CA    1 
ATOM   3659  C  C     . ILE B 2 41  ? 147.956 142.715 83.766  1.00 56.48  ? 41   ILE K C     1 
ATOM   3660  O  O     . ILE B 2 41  ? 148.897 143.257 84.356  1.00 61.07  ? 41   ILE K O     1 
ATOM   3661  C  CB    . ILE B 2 41  ? 146.238 142.330 85.561  1.00 50.88  ? 41   ILE K CB    1 
ATOM   3662  C  CG1   . ILE B 2 41  ? 145.235 141.326 86.123  1.00 56.45  ? 41   ILE K CG1   1 
ATOM   3663  C  CG2   . ILE B 2 41  ? 145.512 143.536 85.002  1.00 53.22  ? 41   ILE K CG2   1 
ATOM   3664  C  CD1   . ILE B 2 41  ? 144.319 141.907 87.165  1.00 57.22  ? 41   ILE K CD1   1 
ATOM   3665  N  N     . ALA B 2 42  ? 147.620 142.995 82.505  1.00 58.11  ? 42   ALA K N     1 
ATOM   3666  C  CA    . ALA B 2 42  ? 148.371 143.937 81.674  1.00 56.55  ? 42   ALA K CA    1 
ATOM   3667  C  C     . ALA B 2 42  ? 149.844 143.548 81.592  1.00 57.68  ? 42   ALA K C     1 
ATOM   3668  O  O     . ALA B 2 42  ? 150.736 144.399 81.610  1.00 60.69  ? 42   ALA K O     1 
ATOM   3669  C  CB    . ALA B 2 42  ? 148.210 145.371 82.180  1.00 56.52  ? 42   ALA K CB    1 
ATOM   3670  N  N     . SER B 2 43  ? 150.094 142.241 81.498  1.00 57.06  ? 43   SER K N     1 
ATOM   3671  C  CA    . SER B 2 43  ? 151.448 141.688 81.425  1.00 59.52  ? 43   SER K CA    1 
ATOM   3672  C  C     . SER B 2 43  ? 152.304 142.151 82.601  1.00 64.17  ? 43   SER K C     1 
ATOM   3673  O  O     . SER B 2 43  ? 153.487 142.464 82.453  1.00 67.71  ? 43   SER K O     1 
ATOM   3674  C  CB    . SER B 2 43  ? 152.115 142.037 80.093  1.00 61.05  ? 43   SER K CB    1 
ATOM   3675  O  OG    . SER B 2 43  ? 152.424 143.417 80.019  1.00 66.15  ? 43   SER K OG    1 
ATOM   3676  N  N     . LYS B 2 44  ? 151.700 142.193 83.783  1.00 64.78  ? 44   LYS K N     1 
ATOM   3677  C  CA    . LYS B 2 44  ? 152.392 142.588 85.010  1.00 62.56  ? 44   LYS K CA    1 
ATOM   3678  C  C     . LYS B 2 44  ? 152.107 141.556 86.091  1.00 61.01  ? 44   LYS K C     1 
ATOM   3679  O  O     . LYS B 2 44  ? 150.966 141.492 86.593  1.00 69.07  ? 44   LYS K O     1 
ATOM   3680  C  CB    . LYS B 2 44  ? 151.957 143.980 85.460  1.00 64.65  ? 44   LYS K CB    1 
ATOM   3681  C  CG    . LYS B 2 44  ? 153.068 144.807 86.079  1.00 66.36  ? 44   LYS K CG    1 
ATOM   3682  C  CD    . LYS B 2 44  ? 154.145 145.136 85.059  1.00 68.33  ? 44   LYS K CD    1 
ATOM   3683  C  CE    . LYS B 2 44  ? 155.174 146.096 85.632  1.00 70.02  ? 44   LYS K CE    1 
ATOM   3684  N  NZ    . LYS B 2 44  ? 155.863 145.523 86.821  1.00 72.14  ? 44   LYS K NZ    1 
ATOM   3685  N  N     . PRO B 2 45  ? 153.083 140.738 86.471  1.00 48.49  ? 45   PRO K N     1 
ATOM   3686  C  CA    . PRO B 2 45  ? 152.829 139.707 87.481  1.00 49.86  ? 45   PRO K CA    1 
ATOM   3687  C  C     . PRO B 2 45  ? 152.566 140.301 88.854  1.00 58.77  ? 45   PRO K C     1 
ATOM   3688  O  O     . PRO B 2 45  ? 153.062 141.373 89.205  1.00 63.33  ? 45   PRO K O     1 
ATOM   3689  C  CB    . PRO B 2 45  ? 154.120 138.880 87.479  1.00 50.03  ? 45   PRO K CB    1 
ATOM   3690  C  CG    . PRO B 2 45  ? 154.805 139.226 86.198  1.00 55.32  ? 45   PRO K CG    1 
ATOM   3691  C  CD    . PRO B 2 45  ? 154.442 140.646 85.922  1.00 54.60  ? 45   PRO K CD    1 
ATOM   3692  N  N     . TYR B 2 46  ? 151.766 139.578 89.634  1.00 55.09  ? 46   TYR K N     1 
ATOM   3693  C  CA    . TYR B 2 46  ? 151.494 139.919 91.024  1.00 52.44  ? 46   TYR K CA    1 
ATOM   3694  C  C     . TYR B 2 46  ? 151.411 138.623 91.811  1.00 58.41  ? 46   TYR K C     1 
ATOM   3695  O  O     . TYR B 2 46  ? 150.586 137.762 91.496  1.00 65.70  ? 46   TYR K O     1 
ATOM   3696  C  CB    . TYR B 2 46  ? 150.193 140.709 91.167  1.00 48.22  ? 46   TYR K CB    1 
ATOM   3697  C  CG    . TYR B 2 46  ? 150.200 142.079 90.535  1.00 48.35  ? 46   TYR K CG    1 
ATOM   3698  C  CD1   . TYR B 2 46  ? 150.981 143.099 91.050  1.00 55.89  ? 46   TYR K CD1   1 
ATOM   3699  C  CD2   . TYR B 2 46  ? 149.402 142.358 89.439  1.00 51.28  ? 46   TYR K CD2   1 
ATOM   3700  C  CE1   . TYR B 2 46  ? 150.979 144.355 90.477  1.00 60.86  ? 46   TYR K CE1   1 
ATOM   3701  C  CE2   . TYR B 2 46  ? 149.392 143.607 88.861  1.00 55.88  ? 46   TYR K CE2   1 
ATOM   3702  C  CZ    . TYR B 2 46  ? 150.180 144.602 89.382  1.00 59.96  ? 46   TYR K CZ    1 
ATOM   3703  O  OH    . TYR B 2 46  ? 150.171 145.849 88.805  1.00 64.29  ? 46   TYR K OH    1 
ATOM   3704  N  N     . ALA B 2 47  ? 152.248 138.486 92.833  1.00 56.43  ? 47   ALA K N     1 
ATOM   3705  C  CA    . ALA B 2 47  ? 152.353 137.248 93.592  1.00 50.65  ? 47   ALA K CA    1 
ATOM   3706  C  C     . ALA B 2 47  ? 151.664 137.397 94.940  1.00 58.79  ? 47   ALA K C     1 
ATOM   3707  O  O     . ALA B 2 47  ? 151.942 138.342 95.684  1.00 67.27  ? 47   ALA K O     1 
ATOM   3708  C  CB    . ALA B 2 47  ? 153.818 136.857 93.791  1.00 56.56  ? 47   ALA K CB    1 
ATOM   3709  N  N     . PHE B 2 48  ? 150.775 136.458 95.252  1.00 58.26  ? 48   PHE K N     1 
ATOM   3710  C  CA    . PHE B 2 48  ? 150.068 136.419 96.523  1.00 57.33  ? 48   PHE K CA    1 
ATOM   3711  C  C     . PHE B 2 48  ? 150.200 135.023 97.117  1.00 60.37  ? 48   PHE K C     1 
ATOM   3712  O  O     . PHE B 2 48  ? 150.882 134.153 96.569  1.00 63.18  ? 48   PHE K O     1 
ATOM   3713  C  CB    . PHE B 2 48  ? 148.594 136.794 96.351  1.00 57.66  ? 48   PHE K CB    1 
ATOM   3714  C  CG    . PHE B 2 48  ? 148.371 138.238 96.043  1.00 54.16  ? 48   PHE K CG    1 
ATOM   3715  C  CD1   . PHE B 2 48  ? 149.107 139.215 96.679  1.00 60.15  ? 48   PHE K CD1   1 
ATOM   3716  C  CD2   . PHE B 2 48  ? 147.428 138.617 95.112  1.00 55.78  ? 48   PHE K CD2   1 
ATOM   3717  C  CE1   . PHE B 2 48  ? 148.904 140.545 96.393  1.00 64.55  ? 48   PHE K CE1   1 
ATOM   3718  C  CE2   . PHE B 2 48  ? 147.221 139.940 94.825  1.00 61.30  ? 48   PHE K CE2   1 
ATOM   3719  C  CZ    . PHE B 2 48  ? 147.961 140.908 95.465  1.00 61.13  ? 48   PHE K CZ    1 
ATOM   3720  N  N     . ASP B 2 49  ? 149.546 134.810 98.258  1.00 65.08  ? 49   ASP K N     1 
ATOM   3721  C  CA    . ASP B 2 49  ? 149.556 133.486 98.867  1.00 66.12  ? 49   ASP K CA    1 
ATOM   3722  C  C     . ASP B 2 49  ? 148.661 132.524 98.098  1.00 71.27  ? 49   ASP K C     1 
ATOM   3723  O  O     . ASP B 2 49  ? 149.049 131.383 97.823  1.00 79.12  ? 49   ASP K O     1 
ATOM   3724  C  CB    . ASP B 2 49  ? 149.132 133.577 100.330 1.00 65.54  ? 49   ASP K CB    1 
ATOM   3725  C  CG    . ASP B 2 49  ? 150.140 134.318 101.178 1.00 72.49  ? 49   ASP K CG    1 
ATOM   3726  O  OD1   . ASP B 2 49  ? 151.087 134.896 100.605 1.00 72.65  ? 49   ASP K OD1   1 
ATOM   3727  O  OD2   . ASP B 2 49  ? 149.995 134.316 102.416 1.00 74.42  ? 49   ASP K OD2   1 
ATOM   3728  N  N     . ARG B 2 50  ? 147.462 132.972 97.732  1.00 66.16  ? 50   ARG K N     1 
ATOM   3729  C  CA    . ARG B 2 50  ? 146.541 132.166 96.943  1.00 64.57  ? 50   ARG K CA    1 
ATOM   3730  C  C     . ARG B 2 50  ? 145.659 133.093 96.125  1.00 62.43  ? 50   ARG K C     1 
ATOM   3731  O  O     . ARG B 2 50  ? 145.046 134.011 96.674  1.00 70.82  ? 50   ARG K O     1 
ATOM   3732  C  CB    . ARG B 2 50  ? 145.681 131.265 97.832  1.00 62.93  ? 50   ARG K CB    1 
ATOM   3733  C  CG    . ARG B 2 50  ? 146.281 129.899 98.104  1.00 66.49  ? 50   ARG K CG    1 
ATOM   3734  C  CD    . ARG B 2 50  ? 145.292 128.791 97.794  1.00 68.29  ? 50   ARG K CD    1 
ATOM   3735  N  NE    . ARG B 2 50  ? 144.915 128.772 96.386  1.00 72.16  ? 50   ARG K NE    1 
ATOM   3736  C  CZ    . ARG B 2 50  ? 144.039 127.930 95.856  1.00 74.97  ? 50   ARG K CZ    1 
ATOM   3737  N  NH1   . ARG B 2 50  ? 143.422 127.021 96.593  1.00 70.58  ? 50   ARG K NH1   1 
ATOM   3738  N  NH2   . ARG B 2 50  ? 143.774 128.002 94.555  1.00 72.65  ? 50   ARG K NH2   1 
ATOM   3739  N  N     . VAL B 2 51  ? 145.596 132.852 94.821  1.00 50.19  ? 51   VAL K N     1 
ATOM   3740  C  CA    . VAL B 2 51  ? 144.734 133.604 93.921  1.00 50.01  ? 51   VAL K CA    1 
ATOM   3741  C  C     . VAL B 2 51  ? 143.600 132.682 93.504  1.00 53.80  ? 51   VAL K C     1 
ATOM   3742  O  O     . VAL B 2 51  ? 143.812 131.714 92.764  1.00 59.94  ? 51   VAL K O     1 
ATOM   3743  C  CB    . VAL B 2 51  ? 145.498 134.135 92.703  1.00 53.74  ? 51   VAL K CB    1 
ATOM   3744  C  CG1   . VAL B 2 51  ? 144.540 134.780 91.720  1.00 55.64  ? 51   VAL K CG1   1 
ATOM   3745  C  CG2   . VAL B 2 51  ? 146.558 135.126 93.140  1.00 59.35  ? 51   VAL K CG2   1 
ATOM   3746  N  N     . PHE B 2 52  ? 142.396 132.977 93.980  1.00 52.57  ? 52   PHE K N     1 
ATOM   3747  C  CA    . PHE B 2 52  ? 141.219 132.186 93.657  1.00 47.50  ? 52   PHE K CA    1 
ATOM   3748  C  C     . PHE B 2 52  ? 140.619 132.690 92.354  1.00 57.21  ? 52   PHE K C     1 
ATOM   3749  O  O     . PHE B 2 52  ? 140.442 133.898 92.171  1.00 64.88  ? 52   PHE K O     1 
ATOM   3750  C  CB    . PHE B 2 52  ? 140.191 132.268 94.783  1.00 51.86  ? 52   PHE K CB    1 
ATOM   3751  C  CG    . PHE B 2 52  ? 140.704 131.790 96.107  1.00 56.88  ? 52   PHE K CG    1 
ATOM   3752  C  CD1   . PHE B 2 52  ? 141.437 130.622 96.201  1.00 59.23  ? 52   PHE K CD1   1 
ATOM   3753  C  CD2   . PHE B 2 52  ? 140.456 132.512 97.258  1.00 55.68  ? 52   PHE K CD2   1 
ATOM   3754  C  CE1   . PHE B 2 52  ? 141.909 130.183 97.419  1.00 60.88  ? 52   PHE K CE1   1 
ATOM   3755  C  CE2   . PHE B 2 52  ? 140.926 132.079 98.476  1.00 58.55  ? 52   PHE K CE2   1 
ATOM   3756  C  CZ    . PHE B 2 52  ? 141.653 130.913 98.558  1.00 62.13  ? 52   PHE K CZ    1 
ATOM   3757  N  N     . GLN B 2 53  ? 140.308 131.765 91.453  1.00 58.24  ? 53   GLN K N     1 
ATOM   3758  C  CA    . GLN B 2 53  ? 139.797 132.126 90.140  1.00 55.02  ? 53   GLN K CA    1 
ATOM   3759  C  C     . GLN B 2 53  ? 138.289 132.364 90.217  1.00 54.20  ? 53   GLN K C     1 
ATOM   3760  O  O     . GLN B 2 53  ? 137.685 132.352 91.293  1.00 58.55  ? 53   GLN K O     1 
ATOM   3761  C  CB    . GLN B 2 53  ? 140.172 131.056 89.122  1.00 53.65  ? 53   GLN K CB    1 
ATOM   3762  C  CG    . GLN B 2 53  ? 141.661 130.781 89.063  1.00 50.22  ? 53   GLN K CG    1 
ATOM   3763  C  CD    . GLN B 2 53  ? 142.028 129.831 87.948  1.00 57.34  ? 53   GLN K CD    1 
ATOM   3764  O  OE1   . GLN B 2 53  ? 141.286 129.678 86.979  1.00 60.79  ? 53   GLN K OE1   1 
ATOM   3765  N  NE2   . GLN B 2 53  ? 143.181 129.185 88.077  1.00 58.01  ? 53   GLN K NE2   1 
ATOM   3766  N  N     . SER B 2 54  ? 137.666 132.586 89.060  1.00 47.95  ? 54   SER K N     1 
ATOM   3767  C  CA    . SER B 2 54  ? 136.277 133.032 89.029  1.00 54.25  ? 54   SER K CA    1 
ATOM   3768  C  C     . SER B 2 54  ? 135.310 131.962 89.521  1.00 54.07  ? 54   SER K C     1 
ATOM   3769  O  O     . SER B 2 54  ? 134.222 132.292 90.003  1.00 54.57  ? 54   SER K O     1 
ATOM   3770  C  CB    . SER B 2 54  ? 135.905 133.469 87.613  1.00 59.26  ? 54   SER K CB    1 
ATOM   3771  O  OG    . SER B 2 54  ? 134.515 133.714 87.504  1.00 62.48  ? 54   SER K OG    1 
ATOM   3772  N  N     . SER B 2 55  ? 135.677 130.691 89.412  1.00 58.07  ? 55   SER K N     1 
ATOM   3773  C  CA    . SER B 2 55  ? 134.764 129.595 89.703  1.00 60.73  ? 55   SER K CA    1 
ATOM   3774  C  C     . SER B 2 55  ? 134.866 129.084 91.133  1.00 66.81  ? 55   SER K C     1 
ATOM   3775  O  O     . SER B 2 55  ? 134.194 128.104 91.470  1.00 69.43  ? 55   SER K O     1 
ATOM   3776  C  CB    . SER B 2 55  ? 135.012 128.438 88.732  1.00 60.68  ? 55   SER K CB    1 
ATOM   3777  O  OG    . SER B 2 55  ? 136.333 127.941 88.863  1.00 57.93  ? 55   SER K OG    1 
ATOM   3778  N  N     . THR B 2 56  ? 135.684 129.710 91.973  1.00 58.35  ? 56   THR K N     1 
ATOM   3779  C  CA    . THR B 2 56  ? 135.911 129.199 93.318  1.00 48.55  ? 56   THR K CA    1 
ATOM   3780  C  C     . THR B 2 56  ? 134.640 129.292 94.151  1.00 48.55  ? 56   THR K C     1 
ATOM   3781  O  O     . THR B 2 56  ? 133.952 130.317 94.143  1.00 54.40  ? 56   THR K O     1 
ATOM   3782  C  CB    . THR B 2 56  ? 137.040 129.973 93.991  1.00 51.85  ? 56   THR K CB    1 
ATOM   3783  O  OG1   . THR B 2 56  ? 138.190 129.974 93.138  1.00 61.15  ? 56   THR K OG1   1 
ATOM   3784  C  CG2   . THR B 2 56  ? 137.407 129.335 95.319  1.00 53.78  ? 56   THR K CG2   1 
ATOM   3785  N  N     . SER B 2 57  ? 134.330 128.219 94.868  1.00 57.42  ? 57   SER K N     1 
ATOM   3786  C  CA    . SER B 2 57  ? 133.178 128.185 95.752  1.00 61.12  ? 57   SER K CA    1 
ATOM   3787  C  C     . SER B 2 57  ? 133.540 128.758 97.118  1.00 63.78  ? 57   SER K C     1 
ATOM   3788  O  O     . SER B 2 57  ? 134.705 129.017 97.428  1.00 72.39  ? 57   SER K O     1 
ATOM   3789  C  CB    . SER B 2 57  ? 132.652 126.758 95.892  1.00 60.95  ? 57   SER K CB    1 
ATOM   3790  O  OG    . SER B 2 57  ? 132.227 126.247 94.641  1.00 65.78  ? 57   SER K OG    1 
ATOM   3791  N  N     . GLN B 2 58  ? 132.513 128.959 97.944  1.00 54.92  ? 58   GLN K N     1 
ATOM   3792  C  CA    . GLN B 2 58  ? 132.734 129.516 99.272  1.00 56.38  ? 58   GLN K CA    1 
ATOM   3793  C  C     . GLN B 2 58  ? 133.497 128.545 100.163 1.00 61.56  ? 58   GLN K C     1 
ATOM   3794  O  O     . GLN B 2 58  ? 134.315 128.963 100.994 1.00 64.37  ? 58   GLN K O     1 
ATOM   3795  C  CB    . GLN B 2 58  ? 131.399 129.893 99.902  1.00 54.88  ? 58   GLN K CB    1 
ATOM   3796  C  CG    . GLN B 2 58  ? 130.647 130.966 99.146  1.00 51.97  ? 58   GLN K CG    1 
ATOM   3797  C  CD    . GLN B 2 58  ? 131.043 132.361 99.571  1.00 61.09  ? 58   GLN K CD    1 
ATOM   3798  O  OE1   . GLN B 2 58  ? 132.124 132.573 100.118 1.00 65.37  ? 58   GLN K OE1   1 
ATOM   3799  N  NE2   . GLN B 2 58  ? 130.165 133.323 99.326  1.00 64.08  ? 58   GLN K NE2   1 
ATOM   3800  N  N     . GLU B 2 59  ? 133.242 127.246 100.006 1.00 63.30  ? 59   GLU K N     1 
ATOM   3801  C  CA    . GLU B 2 59  ? 133.942 126.256 100.816 1.00 61.56  ? 59   GLU K CA    1 
ATOM   3802  C  C     . GLU B 2 59  ? 135.443 126.307 100.572 1.00 61.71  ? 59   GLU K C     1 
ATOM   3803  O  O     . GLU B 2 59  ? 136.234 126.212 101.516 1.00 72.41  ? 59   GLU K O     1 
ATOM   3804  C  CB    . GLU B 2 59  ? 133.401 124.858 100.524 1.00 61.48  ? 59   GLU K CB    1 
ATOM   3805  C  CG    . GLU B 2 59  ? 131.955 124.652 100.925 1.00 68.26  ? 59   GLU K CG    1 
ATOM   3806  C  CD    . GLU B 2 59  ? 131.491 123.226 100.706 1.00 72.06  ? 59   GLU K CD    1 
ATOM   3807  O  OE1   . GLU B 2 59  ? 132.275 122.423 100.158 1.00 72.71  ? 59   GLU K OE1   1 
ATOM   3808  O  OE2   . GLU B 2 59  ? 130.343 122.908 101.080 1.00 71.18  ? 59   GLU K OE2   1 
ATOM   3809  N  N     . GLN B 2 60  ? 135.856 126.462 99.313  1.00 56.49  ? 60   GLN K N     1 
ATOM   3810  C  CA    . GLN B 2 60  ? 137.279 126.445 98.991  1.00 57.95  ? 60   GLN K CA    1 
ATOM   3811  C  C     . GLN B 2 60  ? 137.998 127.649 99.588  1.00 59.95  ? 60   GLN K C     1 
ATOM   3812  O  O     . GLN B 2 60  ? 139.074 127.510 100.185 1.00 69.14  ? 60   GLN K O     1 
ATOM   3813  C  CB    . GLN B 2 60  ? 137.467 126.400 97.476  1.00 59.59  ? 60   GLN K CB    1 
ATOM   3814  C  CG    . GLN B 2 60  ? 138.864 126.026 97.024  1.00 61.51  ? 60   GLN K CG    1 
ATOM   3815  C  CD    . GLN B 2 60  ? 139.100 124.530 97.036  1.00 65.17  ? 60   GLN K CD    1 
ATOM   3816  O  OE1   . GLN B 2 60  ? 139.078 123.894 98.089  1.00 69.20  ? 60   GLN K OE1   1 
ATOM   3817  N  NE2   . GLN B 2 60  ? 139.324 123.959 95.859  1.00 61.45  ? 60   GLN K NE2   1 
ATOM   3818  N  N     . VAL B 2 61  ? 137.418 128.842 99.439  1.00 51.01  ? 61   VAL K N     1 
ATOM   3819  C  CA    . VAL B 2 61  ? 138.055 130.036 99.983  1.00 53.77  ? 61   VAL K CA    1 
ATOM   3820  C  C     . VAL B 2 61  ? 138.072 129.983 101.504 1.00 60.06  ? 61   VAL K C     1 
ATOM   3821  O  O     . VAL B 2 61  ? 139.056 130.382 102.138 1.00 67.01  ? 61   VAL K O     1 
ATOM   3822  C  CB    . VAL B 2 61  ? 137.372 131.313 99.457  1.00 57.08  ? 61   VAL K CB    1 
ATOM   3823  C  CG1   . VAL B 2 61  ? 135.874 131.225 99.592  1.00 59.34  ? 61   VAL K CG1   1 
ATOM   3824  C  CG2   . VAL B 2 61  ? 137.893 132.542 100.185 1.00 61.09  ? 61   VAL K CG2   1 
ATOM   3825  N  N     . TYR B 2 62  ? 137.000 129.475 102.119 1.00 58.69  ? 62   TYR K N     1 
ATOM   3826  C  CA    . TYR B 2 62  ? 137.005 129.332 103.571 1.00 60.07  ? 62   TYR K CA    1 
ATOM   3827  C  C     . TYR B 2 62  ? 138.082 128.355 104.027 1.00 59.59  ? 62   TYR K C     1 
ATOM   3828  O  O     . TYR B 2 62  ? 138.789 128.608 105.009 1.00 60.91  ? 62   TYR K O     1 
ATOM   3829  C  CB    . TYR B 2 62  ? 135.639 128.880 104.072 1.00 57.42  ? 62   TYR K CB    1 
ATOM   3830  C  CG    . TYR B 2 62  ? 135.676 128.496 105.527 1.00 54.27  ? 62   TYR K CG    1 
ATOM   3831  C  CD1   . TYR B 2 62  ? 135.838 129.457 106.510 1.00 57.22  ? 62   TYR K CD1   1 
ATOM   3832  C  CD2   . TYR B 2 62  ? 135.573 127.174 105.917 1.00 56.08  ? 62   TYR K CD2   1 
ATOM   3833  C  CE1   . TYR B 2 62  ? 135.885 129.113 107.839 1.00 58.25  ? 62   TYR K CE1   1 
ATOM   3834  C  CE2   . TYR B 2 62  ? 135.618 126.821 107.244 1.00 58.43  ? 62   TYR K CE2   1 
ATOM   3835  C  CZ    . TYR B 2 62  ? 135.774 127.794 108.201 1.00 59.91  ? 62   TYR K CZ    1 
ATOM   3836  O  OH    . TYR B 2 62  ? 135.819 127.447 109.529 1.00 66.39  ? 62   TYR K OH    1 
ATOM   3837  N  N     . ASN B 2 63  ? 138.218 127.227 103.328 1.00 58.45  ? 63   ASN K N     1 
ATOM   3838  C  CA    . ASN B 2 63  ? 139.206 126.229 103.717 1.00 52.61  ? 63   ASN K CA    1 
ATOM   3839  C  C     . ASN B 2 63  ? 140.622 126.764 103.574 1.00 59.10  ? 63   ASN K C     1 
ATOM   3840  O  O     . ASN B 2 63  ? 141.474 126.526 104.438 1.00 68.37  ? 63   ASN K O     1 
ATOM   3841  C  CB    . ASN B 2 63  ? 139.030 124.960 102.885 1.00 52.43  ? 63   ASN K CB    1 
ATOM   3842  C  CG    . ASN B 2 63  ? 137.789 124.188 103.260 1.00 61.18  ? 63   ASN K CG    1 
ATOM   3843  O  OD1   . ASN B 2 63  ? 137.313 124.270 104.390 1.00 61.45  ? 63   ASN K OD1   1 
ATOM   3844  N  ND2   . ASN B 2 63  ? 137.258 123.424 102.315 1.00 63.67  ? 63   ASN K ND2   1 
ATOM   3845  N  N     . ASP B 2 64  ? 140.897 127.491 102.495 1.00 56.73  ? 64   ASP K N     1 
ATOM   3846  C  CA    . ASP B 2 64  ? 142.249 127.970 102.252 1.00 58.26  ? 64   ASP K CA    1 
ATOM   3847  C  C     . ASP B 2 64  ? 142.552 129.302 102.924 1.00 59.98  ? 64   ASP K C     1 
ATOM   3848  O  O     . ASP B 2 64  ? 143.704 129.744 102.886 1.00 59.25  ? 64   ASP K O     1 
ATOM   3849  C  CB    . ASP B 2 64  ? 142.506 128.088 100.748 1.00 59.56  ? 64   ASP K CB    1 
ATOM   3850  C  CG    . ASP B 2 64  ? 142.868 126.760 100.117 1.00 66.39  ? 64   ASP K CG    1 
ATOM   3851  O  OD1   . ASP B 2 64  ? 143.044 125.776 100.864 1.00 62.99  ? 64   ASP K OD1   1 
ATOM   3852  O  OD2   . ASP B 2 64  ? 142.973 126.699 98.876  1.00 65.68  ? 64   ASP K OD2   1 
ATOM   3853  N  N     . CYS B 2 65  ? 141.562 129.953 103.532 1.00 64.45  ? 65   CYS K N     1 
ATOM   3854  C  CA    . CYS B 2 65  ? 141.788 131.229 104.202 1.00 62.60  ? 65   CYS K CA    1 
ATOM   3855  C  C     . CYS B 2 65  ? 141.524 131.165 105.700 1.00 65.56  ? 65   CYS K C     1 
ATOM   3856  O  O     . CYS B 2 65  ? 142.421 131.471 106.491 1.00 63.79  ? 65   CYS K O     1 
ATOM   3857  C  CB    . CYS B 2 65  ? 140.913 132.313 103.562 1.00 64.89  ? 65   CYS K CB    1 
ATOM   3858  S  SG    . CYS B 2 65  ? 140.884 133.861 104.486 1.00 78.52  ? 65   CYS K SG    1 
ATOM   3859  N  N     . ALA B 2 66  ? 140.322 130.771 106.117 1.00 65.46  ? 66   ALA K N     1 
ATOM   3860  C  CA    . ALA B 2 66  ? 139.879 130.950 107.491 1.00 64.72  ? 66   ALA K CA    1 
ATOM   3861  C  C     . ALA B 2 66  ? 139.847 129.665 108.305 1.00 64.89  ? 66   ALA K C     1 
ATOM   3862  O  O     . ALA B 2 66  ? 139.392 129.693 109.453 1.00 68.59  ? 66   ALA K O     1 
ATOM   3863  C  CB    . ALA B 2 66  ? 138.491 131.598 107.513 1.00 68.34  ? 66   ALA K CB    1 
ATOM   3864  N  N     . LYS B 2 67  ? 140.306 128.541 107.753 1.00 63.75  ? 67   LYS K N     1 
ATOM   3865  C  CA    . LYS B 2 67  ? 140.326 127.309 108.534 1.00 64.46  ? 67   LYS K CA    1 
ATOM   3866  C  C     . LYS B 2 67  ? 141.356 127.381 109.653 1.00 62.28  ? 67   LYS K C     1 
ATOM   3867  O  O     . LYS B 2 67  ? 141.093 126.938 110.777 1.00 66.40  ? 67   LYS K O     1 
ATOM   3868  C  CB    . LYS B 2 67  ? 140.603 126.112 107.628 1.00 67.12  ? 67   LYS K CB    1 
ATOM   3869  C  CG    . LYS B 2 67  ? 140.735 124.797 108.372 1.00 64.13  ? 67   LYS K CG    1 
ATOM   3870  C  CD    . LYS B 2 67  ? 140.729 123.617 107.420 1.00 68.12  ? 67   LYS K CD    1 
ATOM   3871  C  CE    . LYS B 2 67  ? 139.360 123.433 106.793 1.00 68.29  ? 67   LYS K CE    1 
ATOM   3872  N  NZ    . LYS B 2 67  ? 138.305 123.252 107.828 1.00 64.02  ? 67   LYS K NZ    1 
ATOM   3873  N  N     . LYS B 2 68  ? 142.532 127.940 109.367 1.00 59.56  ? 68   LYS K N     1 
ATOM   3874  C  CA    . LYS B 2 68  ? 143.579 128.041 110.375 1.00 61.93  ? 68   LYS K CA    1 
ATOM   3875  C  C     . LYS B 2 68  ? 143.247 129.058 111.457 1.00 65.64  ? 68   LYS K C     1 
ATOM   3876  O  O     . LYS B 2 68  ? 143.774 128.953 112.571 1.00 71.12  ? 68   LYS K O     1 
ATOM   3877  C  CB    . LYS B 2 68  ? 144.906 128.406 109.710 1.00 61.52  ? 68   LYS K CB    1 
ATOM   3878  C  CG    . LYS B 2 68  ? 146.137 128.022 110.513 1.00 65.83  ? 68   LYS K CG    1 
ATOM   3879  C  CD    . LYS B 2 68  ? 146.286 126.514 110.610 1.00 67.35  ? 68   LYS K CD    1 
ATOM   3880  C  CE    . LYS B 2 68  ? 147.615 126.130 111.240 1.00 68.07  ? 68   LYS K CE    1 
ATOM   3881  N  NZ    . LYS B 2 68  ? 147.771 126.703 112.606 1.00 65.59  ? 68   LYS K NZ    1 
ATOM   3882  N  N     . ILE B 2 69  ? 142.388 130.034 111.158 1.00 61.69  ? 69   ILE K N     1 
ATOM   3883  C  CA    . ILE B 2 69  ? 142.127 131.103 112.113 1.00 59.86  ? 69   ILE K CA    1 
ATOM   3884  C  C     . ILE B 2 69  ? 141.342 130.585 113.312 1.00 64.55  ? 69   ILE K C     1 
ATOM   3885  O  O     . ILE B 2 69  ? 141.540 131.058 114.436 1.00 69.62  ? 69   ILE K O     1 
ATOM   3886  C  CB    . ILE B 2 69  ? 141.424 132.284 111.415 1.00 64.06  ? 69   ILE K CB    1 
ATOM   3887  C  CG1   . ILE B 2 69  ? 141.956 133.608 111.955 1.00 63.33  ? 69   ILE K CG1   1 
ATOM   3888  C  CG2   . ILE B 2 69  ? 139.915 132.220 111.582 1.00 68.33  ? 69   ILE K CG2   1 
ATOM   3889  C  CD1   . ILE B 2 69  ? 143.424 133.818 111.690 1.00 60.75  ? 69   ILE K CD1   1 
ATOM   3890  N  N     . VAL B 2 70  ? 140.463 129.600 113.111 1.00 62.19  ? 70   VAL K N     1 
ATOM   3891  C  CA    . VAL B 2 70  ? 139.718 129.032 114.231 1.00 60.25  ? 70   VAL K CA    1 
ATOM   3892  C  C     . VAL B 2 70  ? 140.663 128.324 115.194 1.00 64.32  ? 70   VAL K C     1 
ATOM   3893  O  O     . VAL B 2 70  ? 140.590 128.508 116.417 1.00 70.76  ? 70   VAL K O     1 
ATOM   3894  C  CB    . VAL B 2 70  ? 138.622 128.085 113.716 1.00 64.51  ? 70   VAL K CB    1 
ATOM   3895  C  CG1   . VAL B 2 70  ? 138.063 127.253 114.854 1.00 65.56  ? 70   VAL K CG1   1 
ATOM   3896  C  CG2   . VAL B 2 70  ? 137.519 128.877 113.037 1.00 63.75  ? 70   VAL K CG2   1 
ATOM   3897  N  N     . LYS B 2 71  ? 141.576 127.516 114.652 1.00 60.34  ? 71   LYS K N     1 
ATOM   3898  C  CA    . LYS B 2 71  ? 142.557 126.837 115.488 1.00 61.64  ? 71   LYS K CA    1 
ATOM   3899  C  C     . LYS B 2 71  ? 143.459 127.835 116.198 1.00 64.02  ? 71   LYS K C     1 
ATOM   3900  O  O     . LYS B 2 71  ? 143.777 127.664 117.380 1.00 67.08  ? 71   LYS K O     1 
ATOM   3901  C  CB    . LYS B 2 71  ? 143.385 125.869 114.645 1.00 62.81  ? 71   LYS K CB    1 
ATOM   3902  C  CG    . LYS B 2 71  ? 144.672 125.415 115.309 1.00 68.16  ? 71   LYS K CG    1 
ATOM   3903  C  CD    . LYS B 2 71  ? 145.491 124.532 114.386 1.00 71.19  ? 71   LYS K CD    1 
ATOM   3904  C  CE    . LYS B 2 71  ? 146.900 124.339 114.919 1.00 71.43  ? 71   LYS K CE    1 
ATOM   3905  N  NZ    . LYS B 2 71  ? 146.900 123.780 116.299 1.00 68.61  ? 71   LYS K NZ    1 
ATOM   3906  N  N     . ASP B 2 72  ? 143.880 128.889 115.496 1.00 64.17  ? 72   ASP K N     1 
ATOM   3907  C  CA    . ASP B 2 72  ? 144.738 129.891 116.120 1.00 64.57  ? 72   ASP K CA    1 
ATOM   3908  C  C     . ASP B 2 72  ? 144.016 130.616 117.250 1.00 62.00  ? 72   ASP K C     1 
ATOM   3909  O  O     . ASP B 2 72  ? 144.608 130.881 118.303 1.00 68.32  ? 72   ASP K O     1 
ATOM   3910  C  CB    . ASP B 2 72  ? 145.231 130.886 115.071 1.00 71.45  ? 72   ASP K CB    1 
ATOM   3911  C  CG    . ASP B 2 72  ? 146.200 130.261 114.089 1.00 77.09  ? 72   ASP K CG    1 
ATOM   3912  O  OD1   . ASP B 2 72  ? 146.928 129.326 114.483 1.00 77.69  ? 72   ASP K OD1   1 
ATOM   3913  O  OD2   . ASP B 2 72  ? 146.235 130.705 112.922 1.00 76.70  ? 72   ASP K OD2   1 
ATOM   3914  N  N     . VAL B 2 73  ? 142.741 130.953 117.050 1.00 52.41  ? 73   VAL K N     1 
ATOM   3915  C  CA    . VAL B 2 73  ? 141.982 131.645 118.086 1.00 50.88  ? 73   VAL K CA    1 
ATOM   3916  C  C     . VAL B 2 73  ? 141.798 130.750 119.303 1.00 57.29  ? 73   VAL K C     1 
ATOM   3917  O  O     . VAL B 2 73  ? 141.989 131.183 120.446 1.00 61.22  ? 73   VAL K O     1 
ATOM   3918  C  CB    . VAL B 2 73  ? 140.630 132.126 117.531 1.00 59.95  ? 73   VAL K CB    1 
ATOM   3919  C  CG1   . VAL B 2 73  ? 139.672 132.435 118.662 1.00 57.48  ? 73   VAL K CG1   1 
ATOM   3920  C  CG2   . VAL B 2 73  ? 140.827 133.351 116.655 1.00 65.58  ? 73   VAL K CG2   1 
ATOM   3921  N  N     . LEU B 2 74  ? 141.434 129.486 119.081 1.00 65.10  ? 74   LEU K N     1 
ATOM   3922  C  CA    . LEU B 2 74  ? 141.217 128.590 120.211 1.00 62.87  ? 74   LEU K CA    1 
ATOM   3923  C  C     . LEU B 2 74  ? 142.516 128.191 120.897 1.00 63.20  ? 74   LEU K C     1 
ATOM   3924  O  O     . LEU B 2 74  ? 142.487 127.797 122.066 1.00 63.02  ? 74   LEU K O     1 
ATOM   3925  C  CB    . LEU B 2 74  ? 140.460 127.345 119.757 1.00 59.49  ? 74   LEU K CB    1 
ATOM   3926  C  CG    . LEU B 2 74  ? 139.054 127.617 119.232 1.00 57.66  ? 74   LEU K CG    1 
ATOM   3927  C  CD1   . LEU B 2 74  ? 138.323 126.320 119.018 1.00 62.97  ? 74   LEU K CD1   1 
ATOM   3928  C  CD2   . LEU B 2 74  ? 138.298 128.495 120.201 1.00 62.19  ? 74   LEU K CD2   1 
ATOM   3929  N  N     . GLU B 2 75  ? 143.650 128.272 120.201 1.00 66.47  ? 75   GLU K N     1 
ATOM   3930  C  CA    . GLU B 2 75  ? 144.929 127.976 120.834 1.00 62.48  ? 75   GLU K CA    1 
ATOM   3931  C  C     . GLU B 2 75  ? 145.389 129.110 121.741 1.00 63.20  ? 75   GLU K C     1 
ATOM   3932  O  O     . GLU B 2 75  ? 146.158 128.874 122.678 1.00 66.72  ? 75   GLU K O     1 
ATOM   3933  C  CB    . GLU B 2 75  ? 145.985 127.686 119.768 1.00 63.53  ? 75   GLU K CB    1 
ATOM   3934  C  CG    . GLU B 2 75  ? 147.280 127.113 120.312 1.00 69.03  ? 75   GLU K CG    1 
ATOM   3935  C  CD    . GLU B 2 75  ? 148.218 126.652 119.215 1.00 74.87  ? 75   GLU K CD    1 
ATOM   3936  O  OE1   . GLU B 2 75  ? 147.768 126.530 118.057 1.00 71.31  ? 75   GLU K OE1   1 
ATOM   3937  O  OE2   . GLU B 2 75  ? 149.408 126.412 119.511 1.00 75.48  ? 75   GLU K OE2   1 
ATOM   3938  N  N     . GLY B 2 76  ? 144.937 130.334 121.485 1.00 61.53  ? 76   GLY K N     1 
ATOM   3939  C  CA    . GLY B 2 76  ? 145.267 131.451 122.346 1.00 57.87  ? 76   GLY K CA    1 
ATOM   3940  C  C     . GLY B 2 76  ? 145.645 132.714 121.601 1.00 62.41  ? 76   GLY K C     1 
ATOM   3941  O  O     . GLY B 2 76  ? 145.632 133.805 122.175 1.00 64.42  ? 76   GLY K O     1 
ATOM   3942  N  N     . TYR B 2 77  ? 145.985 132.583 120.323 1.00 64.96  ? 77   TYR K N     1 
ATOM   3943  C  CA    . TYR B 2 77  ? 146.374 133.733 119.526 1.00 58.11  ? 77   TYR K CA    1 
ATOM   3944  C  C     . TYR B 2 77  ? 145.150 134.553 119.130 1.00 59.15  ? 77   TYR K C     1 
ATOM   3945  O  O     . TYR B 2 77  ? 144.002 134.129 119.280 1.00 66.18  ? 77   TYR K O     1 
ATOM   3946  C  CB    . TYR B 2 77  ? 147.127 133.295 118.273 1.00 57.80  ? 77   TYR K CB    1 
ATOM   3947  C  CG    . TYR B 2 77  ? 148.372 132.490 118.538 1.00 51.80  ? 77   TYR K CG    1 
ATOM   3948  C  CD1   . TYR B 2 77  ? 149.544 133.105 118.937 1.00 56.18  ? 77   TYR K CD1   1 
ATOM   3949  C  CD2   . TYR B 2 77  ? 148.378 131.117 118.377 1.00 54.64  ? 77   TYR K CD2   1 
ATOM   3950  C  CE1   . TYR B 2 77  ? 150.686 132.377 119.171 1.00 59.03  ? 77   TYR K CE1   1 
ATOM   3951  C  CE2   . TYR B 2 77  ? 149.514 130.380 118.612 1.00 60.77  ? 77   TYR K CE2   1 
ATOM   3952  C  CZ    . TYR B 2 77  ? 150.666 131.014 119.010 1.00 62.98  ? 77   TYR K CZ    1 
ATOM   3953  O  OH    . TYR B 2 77  ? 151.804 130.279 119.245 1.00 66.54  ? 77   TYR K OH    1 
ATOM   3954  N  N     . ASN B 2 78  ? 145.413 135.748 118.616 1.00 51.56  ? 78   ASN K N     1 
ATOM   3955  C  CA    . ASN B 2 78  ? 144.385 136.620 118.075 1.00 44.99  ? 78   ASN K CA    1 
ATOM   3956  C  C     . ASN B 2 78  ? 144.351 136.472 116.563 1.00 55.96  ? 78   ASN K C     1 
ATOM   3957  O  O     . ASN B 2 78  ? 145.398 136.349 115.919 1.00 73.53  ? 78   ASN K O     1 
ATOM   3958  C  CB    . ASN B 2 78  ? 144.646 138.081 118.442 1.00 50.47  ? 78   ASN K CB    1 
ATOM   3959  C  CG    . ASN B 2 78  ? 144.314 138.393 119.882 1.00 61.98  ? 78   ASN K CG    1 
ATOM   3960  O  OD1   . ASN B 2 78  ? 143.443 137.766 120.482 1.00 71.15  ? 78   ASN K OD1   1 
ATOM   3961  N  ND2   . ASN B 2 78  ? 145.009 139.372 120.446 1.00 58.73  ? 78   ASN K ND2   1 
ATOM   3962  N  N     . GLY B 2 79  ? 143.151 136.482 115.999 1.00 50.59  ? 79   GLY K N     1 
ATOM   3963  C  CA    . GLY B 2 79  ? 143.011 136.425 114.561 1.00 56.98  ? 79   GLY K CA    1 
ATOM   3964  C  C     . GLY B 2 79  ? 142.150 137.548 114.032 1.00 58.60  ? 79   GLY K C     1 
ATOM   3965  O  O     . GLY B 2 79  ? 141.348 138.119 114.775 1.00 67.54  ? 79   GLY K O     1 
ATOM   3966  N  N     . THR B 2 80  ? 142.307 137.881 112.753 1.00 51.99  ? 80   THR K N     1 
ATOM   3967  C  CA    . THR B 2 80  ? 141.474 138.900 112.130 1.00 50.96  ? 80   THR K CA    1 
ATOM   3968  C  C     . THR B 2 80  ? 141.527 138.752 110.617 1.00 55.04  ? 80   THR K C     1 
ATOM   3969  O  O     . THR B 2 80  ? 142.603 138.567 110.043 1.00 59.92  ? 80   THR K O     1 
ATOM   3970  C  CB    . THR B 2 80  ? 141.902 140.307 112.565 1.00 53.54  ? 80   THR K CB    1 
ATOM   3971  O  OG1   . THR B 2 80  ? 141.074 141.289 111.928 1.00 57.65  ? 80   THR K OG1   1 
ATOM   3972  C  CG2   . THR B 2 80  ? 143.350 140.560 112.254 1.00 52.67  ? 80   THR K CG2   1 
ATOM   3973  N  N     . ILE B 2 81  ? 140.358 138.805 109.985 1.00 52.17  ? 81   ILE K N     1 
ATOM   3974  C  CA    . ILE B 2 81  ? 140.222 138.736 108.535 1.00 47.86  ? 81   ILE K CA    1 
ATOM   3975  C  C     . ILE B 2 81  ? 139.341 139.896 108.103 1.00 56.54  ? 81   ILE K C     1 
ATOM   3976  O  O     . ILE B 2 81  ? 138.251 140.086 108.657 1.00 63.76  ? 81   ILE K O     1 
ATOM   3977  C  CB    . ILE B 2 81  ? 139.609 137.404 108.075 1.00 46.90  ? 81   ILE K CB    1 
ATOM   3978  C  CG1   . ILE B 2 81  ? 140.346 136.223 108.701 1.00 50.94  ? 81   ILE K CG1   1 
ATOM   3979  C  CG2   . ILE B 2 81  ? 139.640 137.301 106.563 1.00 53.93  ? 81   ILE K CG2   1 
ATOM   3980  C  CD1   . ILE B 2 81  ? 139.789 134.888 108.295 1.00 52.89  ? 81   ILE K CD1   1 
ATOM   3981  N  N     . PHE B 2 82  ? 139.800 140.670 107.123 1.00 53.03  ? 82   PHE K N     1 
ATOM   3982  C  CA    . PHE B 2 82  ? 138.977 141.740 106.582 1.00 49.54  ? 82   PHE K CA    1 
ATOM   3983  C  C     . PHE B 2 82  ? 139.125 141.802 105.070 1.00 51.75  ? 82   PHE K C     1 
ATOM   3984  O  O     . PHE B 2 82  ? 140.233 141.700 104.539 1.00 62.89  ? 82   PHE K O     1 
ATOM   3985  C  CB    . PHE B 2 82  ? 139.311 143.094 107.225 1.00 51.46  ? 82   PHE K CB    1 
ATOM   3986  C  CG    . PHE B 2 82  ? 140.704 143.587 106.966 1.00 52.46  ? 82   PHE K CG    1 
ATOM   3987  C  CD1   . PHE B 2 82  ? 141.742 143.244 107.811 1.00 56.67  ? 82   PHE K CD1   1 
ATOM   3988  C  CD2   . PHE B 2 82  ? 140.964 144.439 105.910 1.00 52.60  ? 82   PHE K CD2   1 
ATOM   3989  C  CE1   . PHE B 2 82  ? 143.016 143.714 107.587 1.00 57.47  ? 82   PHE K CE1   1 
ATOM   3990  C  CE2   . PHE B 2 82  ? 142.235 144.911 105.682 1.00 53.62  ? 82   PHE K CE2   1 
ATOM   3991  C  CZ    . PHE B 2 82  ? 143.262 144.549 106.522 1.00 55.60  ? 82   PHE K CZ    1 
ATOM   3992  N  N     . ALA B 2 83  ? 137.994 141.965 104.387 1.00 48.07  ? 83   ALA K N     1 
ATOM   3993  C  CA    . ALA B 2 83  ? 137.948 141.977 102.933 1.00 47.30  ? 83   ALA K CA    1 
ATOM   3994  C  C     . ALA B 2 83  ? 138.082 143.397 102.404 1.00 52.56  ? 83   ALA K C     1 
ATOM   3995  O  O     . ALA B 2 83  ? 137.593 144.352 103.014 1.00 63.75  ? 83   ALA K O     1 
ATOM   3996  C  CB    . ALA B 2 83  ? 136.646 141.356 102.430 1.00 52.17  ? 83   ALA K CB    1 
ATOM   3997  N  N     . TYR B 2 84  ? 138.743 143.527 101.257 1.00 51.37  ? 84   TYR K N     1 
ATOM   3998  C  CA    . TYR B 2 84  ? 139.049 144.821 100.670 1.00 50.48  ? 84   TYR K CA    1 
ATOM   3999  C  C     . TYR B 2 84  ? 138.799 144.763 99.171  1.00 53.98  ? 84   TYR K C     1 
ATOM   4000  O  O     . TYR B 2 84  ? 138.877 143.697 98.556  1.00 60.43  ? 84   TYR K O     1 
ATOM   4001  C  CB    . TYR B 2 84  ? 140.500 145.221 100.955 1.00 52.23  ? 84   TYR K CB    1 
ATOM   4002  C  CG    . TYR B 2 84  ? 140.877 146.602 100.484 1.00 55.19  ? 84   TYR K CG    1 
ATOM   4003  C  CD1   . TYR B 2 84  ? 140.524 147.725 101.214 1.00 57.26  ? 84   TYR K CD1   1 
ATOM   4004  C  CD2   . TYR B 2 84  ? 141.599 146.783 99.316  1.00 55.86  ? 84   TYR K CD2   1 
ATOM   4005  C  CE1   . TYR B 2 84  ? 140.871 148.989 100.790 1.00 59.88  ? 84   TYR K CE1   1 
ATOM   4006  C  CE2   . TYR B 2 84  ? 141.951 148.043 98.884  1.00 56.10  ? 84   TYR K CE2   1 
ATOM   4007  C  CZ    . TYR B 2 84  ? 141.586 149.142 99.625  1.00 59.34  ? 84   TYR K CZ    1 
ATOM   4008  O  OH    . TYR B 2 84  ? 141.935 150.400 99.196  1.00 60.92  ? 84   TYR K OH    1 
ATOM   4009  N  N     . GLY B 2 85  ? 138.498 145.916 98.590  1.00 53.24  ? 85   GLY K N     1 
ATOM   4010  C  CA    . GLY B 2 85  ? 138.243 145.986 97.164  1.00 54.88  ? 85   GLY K CA    1 
ATOM   4011  C  C     . GLY B 2 85  ? 137.489 147.258 96.822  1.00 56.92  ? 85   GLY K C     1 
ATOM   4012  O  O     . GLY B 2 85  ? 137.482 148.216 97.591  1.00 61.99  ? 85   GLY K O     1 
ATOM   4013  N  N     . GLN B 2 86  ? 136.860 147.236 95.654  1.00 48.11  ? 86   GLN K N     1 
ATOM   4014  C  CA    . GLN B 2 86  ? 136.050 148.339 95.167  1.00 48.36  ? 86   GLN K CA    1 
ATOM   4015  C  C     . GLN B 2 86  ? 134.576 147.963 95.232  1.00 50.66  ? 86   GLN K C     1 
ATOM   4016  O  O     . GLN B 2 86  ? 134.202 146.890 95.711  1.00 57.25  ? 86   GLN K O     1 
ATOM   4017  C  CB    . GLN B 2 86  ? 136.458 148.717 93.744  1.00 51.06  ? 86   GLN K CB    1 
ATOM   4018  C  CG    . GLN B 2 86  ? 136.145 147.654 92.719  1.00 61.09  ? 86   GLN K CG    1 
ATOM   4019  C  CD    . GLN B 2 86  ? 136.048 148.212 91.318  1.00 62.34  ? 86   GLN K CD    1 
ATOM   4020  O  OE1   . GLN B 2 86  ? 136.571 147.628 90.373  1.00 63.05  ? 86   GLN K OE1   1 
ATOM   4021  N  NE2   . GLN B 2 86  ? 135.375 149.345 91.175  1.00 56.34  ? 86   GLN K NE2   1 
ATOM   4022  N  N     . THR B 2 87  ? 133.733 148.865 94.740  1.00 55.02  ? 87   THR K N     1 
ATOM   4023  C  CA    . THR B 2 87  ? 132.298 148.624 94.732  1.00 59.39  ? 87   THR K CA    1 
ATOM   4024  C  C     . THR B 2 87  ? 131.961 147.455 93.816  1.00 66.13  ? 87   THR K C     1 
ATOM   4025  O  O     . THR B 2 87  ? 132.510 147.329 92.718  1.00 61.33  ? 87   THR K O     1 
ATOM   4026  C  CB    . THR B 2 87  ? 131.553 149.876 94.276  1.00 58.41  ? 87   THR K CB    1 
ATOM   4027  O  OG1   . THR B 2 87  ? 132.172 151.033 94.848  1.00 61.72  ? 87   THR K OG1   1 
ATOM   4028  C  CG2   . THR B 2 87  ? 130.106 149.823 94.723  1.00 58.76  ? 87   THR K CG2   1 
ATOM   4029  N  N     . SER B 2 88  ? 131.046 146.602 94.275  1.00 64.42  ? 88   SER K N     1 
ATOM   4030  C  CA    . SER B 2 88  ? 130.617 145.418 93.533  1.00 52.73  ? 88   SER K CA    1 
ATOM   4031  C  C     . SER B 2 88  ? 131.815 144.555 93.150  1.00 55.20  ? 88   SER K C     1 
ATOM   4032  O  O     . SER B 2 88  ? 132.092 144.314 91.975  1.00 64.10  ? 88   SER K O     1 
ATOM   4033  C  CB    . SER B 2 88  ? 129.802 145.805 92.300  1.00 55.54  ? 88   SER K CB    1 
ATOM   4034  O  OG    . SER B 2 88  ? 130.618 146.416 91.318  1.00 52.65  ? 88   SER K OG    1 
ATOM   4035  N  N     . SER B 2 89  ? 132.537 144.090 94.168  1.00 51.97  ? 89   SER K N     1 
ATOM   4036  C  CA    . SER B 2 89  ? 133.733 143.287 93.962  1.00 55.53  ? 89   SER K CA    1 
ATOM   4037  C  C     . SER B 2 89  ? 133.691 141.934 94.650  1.00 58.25  ? 89   SER K C     1 
ATOM   4038  O  O     . SER B 2 89  ? 134.353 141.005 94.185  1.00 62.36  ? 89   SER K O     1 
ATOM   4039  C  CB    . SER B 2 89  ? 134.971 144.049 94.444  1.00 61.05  ? 89   SER K CB    1 
ATOM   4040  O  OG    . SER B 2 89  ? 136.151 143.497 93.893  1.00 66.48  ? 89   SER K OG    1 
ATOM   4041  N  N     . GLY B 2 90  ? 132.938 141.792 95.737  1.00 57.97  ? 90   GLY K N     1 
ATOM   4042  C  CA    . GLY B 2 90  ? 132.809 140.498 96.376  1.00 58.18  ? 90   GLY K CA    1 
ATOM   4043  C  C     . GLY B 2 90  ? 133.205 140.420 97.836  1.00 61.96  ? 90   GLY K C     1 
ATOM   4044  O  O     . GLY B 2 90  ? 133.622 139.357 98.304  1.00 65.34  ? 90   GLY K O     1 
ATOM   4045  N  N     . LYS B 2 91  ? 133.077 141.523 98.577  1.00 60.76  ? 91   LYS K N     1 
ATOM   4046  C  CA    . LYS B 2 91  ? 133.447 141.502 99.989  1.00 54.69  ? 91   LYS K CA    1 
ATOM   4047  C  C     . LYS B 2 91  ? 132.343 140.895 100.846 1.00 51.75  ? 91   LYS K C     1 
ATOM   4048  O  O     . LYS B 2 91  ? 132.601 140.007 101.666 1.00 59.88  ? 91   LYS K O     1 
ATOM   4049  C  CB    . LYS B 2 91  ? 133.789 142.909 100.468 1.00 52.05  ? 91   LYS K CB    1 
ATOM   4050  C  CG    . LYS B 2 91  ? 134.592 143.713 99.480  1.00 52.67  ? 91   LYS K CG    1 
ATOM   4051  C  CD    . LYS B 2 91  ? 134.730 145.143 99.940  1.00 54.05  ? 91   LYS K CD    1 
ATOM   4052  C  CE    . LYS B 2 91  ? 134.988 146.061 98.773  1.00 54.19  ? 91   LYS K CE    1 
ATOM   4053  N  NZ    . LYS B 2 91  ? 133.864 146.016 97.803  1.00 62.05  ? 91   LYS K NZ    1 
ATOM   4054  N  N     . THR B 2 92  ? 131.108 141.374 100.687 1.00 42.78  ? 92   THR K N     1 
ATOM   4055  C  CA    . THR B 2 92  ? 129.996 140.809 101.446 1.00 47.09  ? 92   THR K CA    1 
ATOM   4056  C  C     . THR B 2 92  ? 129.773 139.350 101.081 1.00 53.58  ? 92   THR K C     1 
ATOM   4057  O  O     . THR B 2 92  ? 129.469 138.523 101.950 1.00 68.22  ? 92   THR K O     1 
ATOM   4058  C  CB    . THR B 2 92  ? 128.726 141.627 101.208 1.00 50.95  ? 92   THR K CB    1 
ATOM   4059  O  OG1   . THR B 2 92  ? 128.878 142.931 101.780 1.00 54.78  ? 92   THR K OG1   1 
ATOM   4060  C  CG2   . THR B 2 92  ? 127.510 140.953 101.813 1.00 53.29  ? 92   THR K CG2   1 
ATOM   4061  N  N     . HIS B 2 93  ? 129.932 139.012 99.802  1.00 44.41  ? 93   HIS K N     1 
ATOM   4062  C  CA    . HIS B 2 93  ? 129.765 137.628 99.379  1.00 51.71  ? 93   HIS K CA    1 
ATOM   4063  C  C     . HIS B 2 93  ? 130.797 136.724 100.038 1.00 59.98  ? 93   HIS K C     1 
ATOM   4064  O  O     . HIS B 2 93  ? 130.482 135.599 100.442 1.00 67.83  ? 93   HIS K O     1 
ATOM   4065  C  CB    . HIS B 2 93  ? 129.865 137.538 97.860  1.00 50.98  ? 93   HIS K CB    1 
ATOM   4066  C  CG    . HIS B 2 93  ? 129.309 136.271 97.294  1.00 53.17  ? 93   HIS K CG    1 
ATOM   4067  N  ND1   . HIS B 2 93  ? 130.108 135.238 96.856  1.00 53.13  ? 93   HIS K ND1   1 
ATOM   4068  C  CD2   . HIS B 2 93  ? 128.033 135.873 97.089  1.00 54.80  ? 93   HIS K CD2   1 
ATOM   4069  C  CE1   . HIS B 2 93  ? 129.347 134.256 96.407  1.00 57.70  ? 93   HIS K CE1   1 
ATOM   4070  N  NE2   . HIS B 2 93  ? 128.083 134.617 96.537  1.00 62.18  ? 93   HIS K NE2   1 
ATOM   4071  N  N     . THR B 2 94  ? 132.037 137.199 100.154 1.00 55.56  ? 94   THR K N     1 
ATOM   4072  C  CA    . THR B 2 94  ? 133.084 136.390 100.764 1.00 46.43  ? 94   THR K CA    1 
ATOM   4073  C  C     . THR B 2 94  ? 132.906 136.292 102.273 1.00 50.90  ? 94   THR K C     1 
ATOM   4074  O  O     . THR B 2 94  ? 133.086 135.217 102.855 1.00 57.94  ? 94   THR K O     1 
ATOM   4075  C  CB    . THR B 2 94  ? 134.454 136.971 100.428 1.00 46.27  ? 94   THR K CB    1 
ATOM   4076  O  OG1   . THR B 2 94  ? 134.551 137.172 99.015  1.00 51.87  ? 94   THR K OG1   1 
ATOM   4077  C  CG2   . THR B 2 94  ? 135.555 136.029 100.873 1.00 54.32  ? 94   THR K CG2   1 
ATOM   4078  N  N     . MET B 2 95  ? 132.541 137.397 102.925 1.00 56.12  ? 95   MET K N     1 
ATOM   4079  C  CA    . MET B 2 95  ? 132.509 137.421 104.384 1.00 50.09  ? 95   MET K CA    1 
ATOM   4080  C  C     . MET B 2 95  ? 131.240 136.776 104.931 1.00 59.72  ? 95   MET K C     1 
ATOM   4081  O  O     . MET B 2 95  ? 131.307 135.820 105.711 1.00 75.92  ? 95   MET K O     1 
ATOM   4082  C  CB    . MET B 2 95  ? 132.646 138.857 104.890 1.00 51.08  ? 95   MET K CB    1 
ATOM   4083  C  CG    . MET B 2 95  ? 133.961 139.513 104.521 1.00 56.53  ? 95   MET K CG    1 
ATOM   4084  S  SD    . MET B 2 95  ? 135.392 138.564 105.051 1.00 69.88  ? 95   MET K SD    1 
ATOM   4085  C  CE    . MET B 2 95  ? 135.174 138.592 106.823 1.00 56.59  ? 95   MET K CE    1 
ATOM   4086  N  N     . GLU B 2 96  ? 130.072 137.281 104.537 1.00 52.58  ? 96   GLU K N     1 
ATOM   4087  C  CA    . GLU B 2 96  ? 128.810 136.761 105.046 1.00 53.31  ? 96   GLU K CA    1 
ATOM   4088  C  C     . GLU B 2 96  ? 128.018 136.000 103.989 1.00 57.65  ? 96   GLU K C     1 
ATOM   4089  O  O     . GLU B 2 96  ? 127.686 134.831 104.198 1.00 66.06  ? 96   GLU K O     1 
ATOM   4090  C  CB    . GLU B 2 96  ? 127.974 137.901 105.645 1.00 59.60  ? 96   GLU K CB    1 
ATOM   4091  C  CG    . GLU B 2 96  ? 127.820 139.116 104.757 1.00 68.52  ? 96   GLU K CG    1 
ATOM   4092  C  CD    . GLU B 2 96  ? 127.518 140.379 105.540 1.00 70.08  ? 96   GLU K CD    1 
ATOM   4093  O  OE1   . GLU B 2 96  ? 126.827 140.288 106.575 1.00 69.13  ? 96   GLU K OE1   1 
ATOM   4094  O  OE2   . GLU B 2 96  ? 127.972 141.463 105.117 1.00 64.53  ? 96   GLU K OE2   1 
ATOM   4095  N  N     . GLY B 2 97  ? 127.715 136.619 102.852 1.00 62.15  ? 97   GLY K N     1 
ATOM   4096  C  CA    . GLY B 2 97  ? 126.940 135.926 101.841 1.00 62.01  ? 97   GLY K CA    1 
ATOM   4097  C  C     . GLY B 2 97  ? 125.539 135.608 102.329 1.00 68.37  ? 97   GLY K C     1 
ATOM   4098  O  O     . GLY B 2 97  ? 124.958 136.317 103.157 1.00 74.69  ? 97   GLY K O     1 
ATOM   4099  N  N     . LYS B 2 98  ? 124.985 134.518 101.807 1.00 61.91  ? 98   LYS K N     1 
ATOM   4100  C  CA    . LYS B 2 98  ? 123.689 134.026 102.260 1.00 59.08  ? 98   LYS K CA    1 
ATOM   4101  C  C     . LYS B 2 98  ? 123.897 133.254 103.556 1.00 65.35  ? 98   LYS K C     1 
ATOM   4102  O  O     . LYS B 2 98  ? 124.575 132.223 103.570 1.00 70.44  ? 98   LYS K O     1 
ATOM   4103  C  CB    . LYS B 2 98  ? 123.044 133.152 101.190 1.00 60.06  ? 98   LYS K CB    1 
ATOM   4104  C  CG    . LYS B 2 98  ? 122.768 133.877 99.889  1.00 64.28  ? 98   LYS K CG    1 
ATOM   4105  C  CD    . LYS B 2 98  ? 122.111 132.957 98.879  1.00 69.98  ? 98   LYS K CD    1 
ATOM   4106  C  CE    . LYS B 2 98  ? 121.853 133.676 97.567  1.00 68.45  ? 98   LYS K CE    1 
ATOM   4107  N  NZ    . LYS B 2 98  ? 121.204 132.784 96.567  1.00 69.02  ? 98   LYS K NZ    1 
ATOM   4108  N  N     . LEU B 2 99  ? 123.314 133.753 104.648 1.00 62.34  ? 99   LEU K N     1 
ATOM   4109  C  CA    . LEU B 2 99  ? 123.605 133.202 105.968 1.00 65.24  ? 99   LEU K CA    1 
ATOM   4110  C  C     . LEU B 2 99  ? 123.131 131.760 106.101 1.00 70.54  ? 99   LEU K C     1 
ATOM   4111  O  O     . LEU B 2 99  ? 123.848 130.915 106.649 1.00 74.31  ? 99   LEU K O     1 
ATOM   4112  C  CB    . LEU B 2 99  ? 122.965 134.066 107.052 1.00 63.20  ? 99   LEU K CB    1 
ATOM   4113  C  CG    . LEU B 2 99  ? 123.466 135.499 107.222 1.00 61.80  ? 99   LEU K CG    1 
ATOM   4114  C  CD1   . LEU B 2 99  ? 124.963 135.577 107.000 1.00 63.59  ? 99   LEU K CD1   1 
ATOM   4115  C  CD2   . LEU B 2 99  ? 122.723 136.445 106.294 1.00 66.07  ? 99   LEU K CD2   1 
ATOM   4116  N  N     . HIS B 2 100 ? 121.934 131.458 105.607 1.00 70.27  ? 100  HIS K N     1 
ATOM   4117  C  CA    . HIS B 2 100 ? 121.279 130.188 105.880 1.00 69.36  ? 100  HIS K CA    1 
ATOM   4118  C  C     . HIS B 2 100 ? 121.390 129.192 104.732 1.00 71.98  ? 100  HIS K C     1 
ATOM   4119  O  O     . HIS B 2 100 ? 120.711 128.160 104.757 1.00 74.72  ? 100  HIS K O     1 
ATOM   4120  C  CB    . HIS B 2 100 ? 119.810 130.431 106.224 1.00 67.06  ? 100  HIS K CB    1 
ATOM   4121  C  CG    . HIS B 2 100 ? 119.606 131.474 107.277 1.00 71.45  ? 100  HIS K CG    1 
ATOM   4122  N  ND1   . HIS B 2 100 ? 120.501 131.679 108.304 1.00 75.33  ? 100  HIS K ND1   1 
ATOM   4123  C  CD2   . HIS B 2 100 ? 118.614 132.379 107.457 1.00 73.75  ? 100  HIS K CD2   1 
ATOM   4124  C  CE1   . HIS B 2 100 ? 120.068 132.661 109.075 1.00 73.60  ? 100  HIS K CE1   1 
ATOM   4125  N  NE2   . HIS B 2 100 ? 118.925 133.103 108.582 1.00 76.26  ? 100  HIS K NE2   1 
ATOM   4126  N  N     . ASP B 2 101 ? 122.218 129.468 103.737 1.00 65.27  ? 101  ASP K N     1 
ATOM   4127  C  CA    . ASP B 2 101 ? 122.380 128.517 102.642 1.00 63.66  ? 101  ASP K CA    1 
ATOM   4128  C  C     . ASP B 2 101 ? 123.606 127.646 102.885 1.00 67.41  ? 101  ASP K C     1 
ATOM   4129  O  O     . ASP B 2 101 ? 124.701 128.179 103.098 1.00 71.42  ? 101  ASP K O     1 
ATOM   4130  C  CB    . ASP B 2 101 ? 122.518 129.237 101.311 1.00 69.27  ? 101  ASP K CB    1 
ATOM   4131  C  CG    . ASP B 2 101 ? 122.585 128.282 100.137 1.00 73.69  ? 101  ASP K CG    1 
ATOM   4132  O  OD1   . ASP B 2 101 ? 121.554 127.651 99.824  1.00 71.77  ? 101  ASP K OD1   1 
ATOM   4133  O  OD2   . ASP B 2 101 ? 123.668 128.162 99.527  1.00 74.65  ? 101  ASP K OD2   1 
ATOM   4134  N  N     . PRO B 2 102 ? 123.463 126.319 102.874 1.00 63.29  ? 102  PRO K N     1 
ATOM   4135  C  CA    . PRO B 2 102 ? 124.619 125.451 103.152 1.00 58.05  ? 102  PRO K CA    1 
ATOM   4136  C  C     . PRO B 2 102 ? 125.764 125.601 102.166 1.00 63.08  ? 102  PRO K C     1 
ATOM   4137  O  O     . PRO B 2 102 ? 126.912 125.325 102.533 1.00 64.44  ? 102  PRO K O     1 
ATOM   4138  C  CB    . PRO B 2 102 ? 124.021 124.039 103.093 1.00 57.39  ? 102  PRO K CB    1 
ATOM   4139  C  CG    . PRO B 2 102 ? 122.560 124.230 103.307 1.00 64.78  ? 102  PRO K CG    1 
ATOM   4140  C  CD    . PRO B 2 102 ? 122.228 125.545 102.676 1.00 67.77  ? 102  PRO K CD    1 
ATOM   4141  N  N     . GLU B 2 103 ? 125.498 126.019 100.928 1.00 72.08  ? 103  GLU K N     1 
ATOM   4142  C  CA    . GLU B 2 103 ? 126.543 126.128 99.920  1.00 74.12  ? 103  GLU K CA    1 
ATOM   4143  C  C     . GLU B 2 103 ? 126.981 127.557 99.636  1.00 74.36  ? 103  GLU K C     1 
ATOM   4144  O  O     . GLU B 2 103 ? 128.116 127.758 99.196  1.00 76.21  ? 103  GLU K O     1 
ATOM   4145  C  CB    . GLU B 2 103 ? 126.085 125.481 98.605  1.00 79.40  ? 103  GLU K CB    1 
ATOM   4146  C  CG    . GLU B 2 103 ? 127.223 125.062 97.690  1.00 82.20  ? 103  GLU K CG    1 
ATOM   4147  C  CD    . GLU B 2 103 ? 126.750 124.233 96.513  1.00 82.78  ? 103  GLU K CD    1 
ATOM   4148  O  OE1   . GLU B 2 103 ? 125.524 124.174 96.280  1.00 83.89  ? 103  GLU K OE1   1 
ATOM   4149  O  OE2   . GLU B 2 103 ? 127.603 123.640 95.820  1.00 79.12  ? 103  GLU K OE2   1 
ATOM   4150  N  N     . GLY B 2 104 ? 126.123 128.546 99.877  1.00 67.99  ? 104  GLY K N     1 
ATOM   4151  C  CA    . GLY B 2 104 ? 126.456 129.932 99.624  1.00 68.68  ? 104  GLY K CA    1 
ATOM   4152  C  C     . GLY B 2 104 ? 126.814 130.768 100.832 1.00 69.72  ? 104  GLY K C     1 
ATOM   4153  O  O     . GLY B 2 104 ? 126.839 132.001 100.722 1.00 73.69  ? 104  GLY K O     1 
ATOM   4154  N  N     . MET B 2 105 ? 127.091 130.159 101.980 1.00 61.87  ? 105  MET K N     1 
ATOM   4155  C  CA    . MET B 2 105 ? 127.434 130.928 103.163 1.00 57.84  ? 105  MET K CA    1 
ATOM   4156  C  C     . MET B 2 105 ? 128.887 131.387 103.098 1.00 64.62  ? 105  MET K C     1 
ATOM   4157  O  O     . MET B 2 105 ? 129.713 130.824 102.377 1.00 70.28  ? 105  MET K O     1 
ATOM   4158  C  CB    . MET B 2 105 ? 127.187 130.107 104.428 1.00 59.69  ? 105  MET K CB    1 
ATOM   4159  C  CG    . MET B 2 105 ? 128.195 129.003 104.665 1.00 68.02  ? 105  MET K CG    1 
ATOM   4160  S  SD    . MET B 2 105 ? 127.494 127.622 105.586 1.00 87.42  ? 105  MET K SD    1 
ATOM   4161  C  CE    . MET B 2 105 ? 126.402 128.489 106.708 1.00 66.24  ? 105  MET K CE    1 
ATOM   4162  N  N     . GLY B 2 106 ? 129.193 132.423 103.871 1.00 59.58  ? 106  GLY K N     1 
ATOM   4163  C  CA    . GLY B 2 106 ? 130.469 133.095 103.806 1.00 53.81  ? 106  GLY K CA    1 
ATOM   4164  C  C     . GLY B 2 106 ? 131.430 132.675 104.897 1.00 55.68  ? 106  GLY K C     1 
ATOM   4165  O  O     . GLY B 2 106 ? 131.329 131.588 105.477 1.00 62.34  ? 106  GLY K O     1 
ATOM   4166  N  N     . ILE B 2 107 ? 132.386 133.561 105.179 1.00 52.70  ? 107  ILE K N     1 
ATOM   4167  C  CA    . ILE B 2 107 ? 133.444 133.258 106.136 1.00 43.20  ? 107  ILE K CA    1 
ATOM   4168  C  C     . ILE B 2 107 ? 132.899 133.209 107.559 1.00 58.08  ? 107  ILE K C     1 
ATOM   4169  O  O     . ILE B 2 107 ? 133.261 132.322 108.339 1.00 66.13  ? 107  ILE K O     1 
ATOM   4170  C  CB    . ILE B 2 107 ? 134.580 134.287 105.999 1.00 45.85  ? 107  ILE K CB    1 
ATOM   4171  C  CG1   . ILE B 2 107 ? 135.379 134.033 104.724 1.00 44.82  ? 107  ILE K CG1   1 
ATOM   4172  C  CG2   . ILE B 2 107 ? 135.494 134.250 107.202 1.00 54.90  ? 107  ILE K CG2   1 
ATOM   4173  C  CD1   . ILE B 2 107 ? 136.116 132.723 104.726 1.00 52.22  ? 107  ILE K CD1   1 
ATOM   4174  N  N     . ILE B 2 108 ? 132.038 134.162 107.927 1.00 58.38  ? 108  ILE K N     1 
ATOM   4175  C  CA    . ILE B 2 108 ? 131.599 134.266 109.322 1.00 51.86  ? 108  ILE K CA    1 
ATOM   4176  C  C     . ILE B 2 108 ? 130.807 133.046 109.786 1.00 56.26  ? 108  ILE K C     1 
ATOM   4177  O  O     . ILE B 2 108 ? 131.137 132.493 110.850 1.00 63.24  ? 108  ILE K O     1 
ATOM   4178  C  CB    . ILE B 2 108 ? 130.834 135.585 109.536 1.00 44.79  ? 108  ILE K CB    1 
ATOM   4179  C  CG1   . ILE B 2 108 ? 131.721 136.778 109.192 1.00 51.45  ? 108  ILE K CG1   1 
ATOM   4180  C  CG2   . ILE B 2 108 ? 130.345 135.686 110.967 1.00 52.55  ? 108  ILE K CG2   1 
ATOM   4181  C  CD1   . ILE B 2 108 ? 131.043 138.108 109.383 1.00 52.00  ? 108  ILE K CD1   1 
ATOM   4182  N  N     . PRO B 2 109 ? 129.756 132.596 109.085 1.00 44.37  ? 109  PRO K N     1 
ATOM   4183  C  CA    . PRO B 2 109 ? 129.040 131.401 109.563 1.00 54.31  ? 109  PRO K CA    1 
ATOM   4184  C  C     . PRO B 2 109 ? 129.905 130.156 109.620 1.00 56.76  ? 109  PRO K C     1 
ATOM   4185  O  O     . PRO B 2 109 ? 129.786 129.359 110.562 1.00 64.93  ? 109  PRO K O     1 
ATOM   4186  C  CB    . PRO B 2 109 ? 127.898 131.257 108.551 1.00 57.25  ? 109  PRO K CB    1 
ATOM   4187  C  CG    . PRO B 2 109 ? 127.714 132.611 107.999 1.00 51.92  ? 109  PRO K CG    1 
ATOM   4188  C  CD    . PRO B 2 109 ? 129.085 133.180 107.911 1.00 42.43  ? 109  PRO K CD    1 
ATOM   4189  N  N     . ARG B 2 110 ? 130.781 129.963 108.636 1.00 50.07  ? 110  ARG K N     1 
ATOM   4190  C  CA    . ARG B 2 110 ? 131.657 128.800 108.663 1.00 50.41  ? 110  ARG K CA    1 
ATOM   4191  C  C     . ARG B 2 110 ? 132.622 128.875 109.836 1.00 55.79  ? 110  ARG K C     1 
ATOM   4192  O  O     . ARG B 2 110 ? 132.885 127.864 110.498 1.00 63.17  ? 110  ARG K O     1 
ATOM   4193  C  CB    . ARG B 2 110 ? 132.406 128.678 107.340 1.00 52.33  ? 110  ARG K CB    1 
ATOM   4194  C  CG    . ARG B 2 110 ? 131.489 128.478 106.150 1.00 55.65  ? 110  ARG K CG    1 
ATOM   4195  C  CD    . ARG B 2 110 ? 132.243 127.999 104.931 1.00 55.63  ? 110  ARG K CD    1 
ATOM   4196  N  NE    . ARG B 2 110 ? 131.375 127.896 103.766 1.00 52.55  ? 110  ARG K NE    1 
ATOM   4197  C  CZ    . ARG B 2 110 ? 130.620 126.843 103.486 1.00 58.47  ? 110  ARG K CZ    1 
ATOM   4198  N  NH1   . ARG B 2 110 ? 130.602 125.779 104.271 1.00 61.11  ? 110  ARG K NH1   1 
ATOM   4199  N  NH2   . ARG B 2 110 ? 129.863 126.860 102.394 1.00 58.97  ? 110  ARG K NH2   1 
ATOM   4200  N  N     . ILE B 2 111 ? 133.140 130.070 110.123 1.00 51.82  ? 111  ILE K N     1 
ATOM   4201  C  CA    . ILE B 2 111 ? 134.043 130.237 111.256 1.00 52.87  ? 111  ILE K CA    1 
ATOM   4202  C  C     . ILE B 2 111 ? 133.330 129.918 112.560 1.00 59.86  ? 111  ILE K C     1 
ATOM   4203  O  O     . ILE B 2 111 ? 133.882 129.235 113.428 1.00 68.43  ? 111  ILE K O     1 
ATOM   4204  C  CB    . ILE B 2 111 ? 134.643 131.655 111.272 1.00 53.35  ? 111  ILE K CB    1 
ATOM   4205  C  CG1   . ILE B 2 111 ? 135.923 131.700 110.442 1.00 57.28  ? 111  ILE K CG1   1 
ATOM   4206  C  CG2   . ILE B 2 111 ? 134.933 132.109 112.692 1.00 57.35  ? 111  ILE K CG2   1 
ATOM   4207  C  CD1   . ILE B 2 111 ? 136.557 133.062 110.394 1.00 60.97  ? 111  ILE K CD1   1 
ATOM   4208  N  N     . VAL B 2 112 ? 132.095 130.397 112.725 1.00 49.01  ? 112  VAL K N     1 
ATOM   4209  C  CA    . VAL B 2 112 ? 131.416 130.159 113.997 1.00 51.99  ? 112  VAL K CA    1 
ATOM   4210  C  C     . VAL B 2 112 ? 131.059 128.681 114.151 1.00 55.35  ? 112  VAL K C     1 
ATOM   4211  O  O     . VAL B 2 112 ? 131.219 128.099 115.235 1.00 64.18  ? 112  VAL K O     1 
ATOM   4212  C  CB    . VAL B 2 112 ? 130.192 131.081 114.158 1.00 49.38  ? 112  VAL K CB    1 
ATOM   4213  C  CG1   . VAL B 2 112 ? 130.609 132.530 114.000 1.00 54.31  ? 112  VAL K CG1   1 
ATOM   4214  C  CG2   . VAL B 2 112 ? 129.091 130.736 113.189 1.00 50.80  ? 112  VAL K CG2   1 
ATOM   4215  N  N     . GLN B 2 113 ? 130.607 128.036 113.071 1.00 55.42  ? 113  GLN K N     1 
ATOM   4216  C  CA    . GLN B 2 113 ? 130.303 126.612 113.158 1.00 55.95  ? 113  GLN K CA    1 
ATOM   4217  C  C     . GLN B 2 113 ? 131.554 125.800 113.473 1.00 61.14  ? 113  GLN K C     1 
ATOM   4218  O  O     . GLN B 2 113 ? 131.522 124.898 114.321 1.00 69.80  ? 113  GLN K O     1 
ATOM   4219  C  CB    . GLN B 2 113 ? 129.656 126.131 111.862 1.00 61.09  ? 113  GLN K CB    1 
ATOM   4220  C  CG    . GLN B 2 113 ? 128.260 126.682 111.640 1.00 65.49  ? 113  GLN K CG    1 
ATOM   4221  C  CD    . GLN B 2 113 ? 127.608 126.136 110.387 1.00 71.15  ? 113  GLN K CD    1 
ATOM   4222  O  OE1   . GLN B 2 113 ? 128.185 125.308 109.683 1.00 69.82  ? 113  GLN K OE1   1 
ATOM   4223  N  NE2   . GLN B 2 113 ? 126.397 126.600 110.101 1.00 69.22  ? 113  GLN K NE2   1 
ATOM   4224  N  N     . ASP B 2 114 ? 132.674 126.116 112.815 1.00 55.74  ? 114  ASP K N     1 
ATOM   4225  C  CA    . ASP B 2 114 ? 133.904 125.382 113.079 1.00 56.36  ? 114  ASP K CA    1 
ATOM   4226  C  C     . ASP B 2 114 ? 134.434 125.651 114.477 1.00 61.25  ? 114  ASP K C     1 
ATOM   4227  O  O     . ASP B 2 114 ? 134.995 124.747 115.103 1.00 69.75  ? 114  ASP K O     1 
ATOM   4228  C  CB    . ASP B 2 114 ? 134.964 125.724 112.039 1.00 58.47  ? 114  ASP K CB    1 
ATOM   4229  C  CG    . ASP B 2 114 ? 135.008 124.723 110.907 1.00 68.56  ? 114  ASP K CG    1 
ATOM   4230  O  OD1   . ASP B 2 114 ? 134.693 123.540 111.149 1.00 68.44  ? 114  ASP K OD1   1 
ATOM   4231  O  OD2   . ASP B 2 114 ? 135.362 125.115 109.777 1.00 70.69  ? 114  ASP K OD2   1 
ATOM   4232  N  N     . ILE B 2 115 ? 134.277 126.875 114.985 1.00 56.63  ? 115  ILE K N     1 
ATOM   4233  C  CA    . ILE B 2 115 ? 134.742 127.161 116.335 1.00 55.49  ? 115  ILE K CA    1 
ATOM   4234  C  C     . ILE B 2 115 ? 133.933 126.360 117.343 1.00 54.89  ? 115  ILE K C     1 
ATOM   4235  O  O     . ILE B 2 115 ? 134.490 125.797 118.292 1.00 61.19  ? 115  ILE K O     1 
ATOM   4236  C  CB    . ILE B 2 115 ? 134.716 128.680 116.616 1.00 54.98  ? 115  ILE K CB    1 
ATOM   4237  C  CG1   . ILE B 2 115 ? 135.815 129.057 117.604 1.00 62.81  ? 115  ILE K CG1   1 
ATOM   4238  C  CG2   . ILE B 2 115 ? 133.394 129.149 117.176 1.00 51.59  ? 115  ILE K CG2   1 
ATOM   4239  C  CD1   . ILE B 2 115 ? 136.091 130.541 117.655 1.00 60.36  ? 115  ILE K CD1   1 
ATOM   4240  N  N     . PHE B 2 116 ? 132.622 126.229 117.122 1.00 52.50  ? 116  PHE K N     1 
ATOM   4241  C  CA    . PHE B 2 116 ? 131.822 125.433 118.047 1.00 53.57  ? 116  PHE K CA    1 
ATOM   4242  C  C     . PHE B 2 116 ? 132.164 123.950 117.948 1.00 61.24  ? 116  PHE K C     1 
ATOM   4243  O  O     . PHE B 2 116 ? 132.236 123.255 118.970 1.00 73.10  ? 116  PHE K O     1 
ATOM   4244  C  CB    . PHE B 2 116 ? 130.338 125.676 117.803 1.00 49.62  ? 116  PHE K CB    1 
ATOM   4245  C  CG    . PHE B 2 116 ? 129.832 126.936 118.431 1.00 54.06  ? 116  PHE K CG    1 
ATOM   4246  C  CD1   . PHE B 2 116 ? 129.960 127.138 119.789 1.00 56.92  ? 116  PHE K CD1   1 
ATOM   4247  C  CD2   . PHE B 2 116 ? 129.242 127.923 117.666 1.00 61.07  ? 116  PHE K CD2   1 
ATOM   4248  C  CE1   . PHE B 2 116 ? 129.505 128.295 120.376 1.00 61.39  ? 116  PHE K CE1   1 
ATOM   4249  C  CE2   . PHE B 2 116 ? 128.785 129.086 118.250 1.00 61.30  ? 116  PHE K CE2   1 
ATOM   4250  C  CZ    . PHE B 2 116 ? 128.916 129.270 119.606 1.00 62.12  ? 116  PHE K CZ    1 
ATOM   4251  N  N     . ASN B 2 117 ? 132.398 123.448 116.733 1.00 54.49  ? 117  ASN K N     1 
ATOM   4252  C  CA    . ASN B 2 117 ? 132.768 122.042 116.584 1.00 50.63  ? 117  ASN K CA    1 
ATOM   4253  C  C     . ASN B 2 117 ? 134.113 121.746 117.239 1.00 49.50  ? 117  ASN K C     1 
ATOM   4254  O  O     . ASN B 2 117 ? 134.268 120.729 117.932 1.00 62.65  ? 117  ASN K O     1 
ATOM   4255  C  CB    . ASN B 2 117 ? 132.789 121.660 115.106 1.00 55.10  ? 117  ASN K CB    1 
ATOM   4256  C  CG    . ASN B 2 117 ? 131.399 121.563 114.512 1.00 61.56  ? 117  ASN K CG    1 
ATOM   4257  O  OD1   . ASN B 2 117 ? 131.079 122.236 113.534 1.00 56.22  ? 117  ASN K OD1   1 
ATOM   4258  N  ND2   . ASN B 2 117 ? 130.562 120.722 115.106 1.00 61.24  ? 117  ASN K ND2   1 
ATOM   4259  N  N     . TYR B 2 118 ? 135.095 122.627 117.045 1.00 51.30  ? 118  TYR K N     1 
ATOM   4260  C  CA    . TYR B 2 118 ? 136.393 122.442 117.682 1.00 56.78  ? 118  TYR K CA    1 
ATOM   4261  C  C     . TYR B 2 118 ? 136.279 122.524 119.197 1.00 57.41  ? 118  TYR K C     1 
ATOM   4262  O  O     . TYR B 2 118 ? 136.961 121.785 119.917 1.00 60.71  ? 118  TYR K O     1 
ATOM   4263  C  CB    . TYR B 2 118 ? 137.386 123.477 117.161 1.00 61.37  ? 118  TYR K CB    1 
ATOM   4264  C  CG    . TYR B 2 118 ? 138.193 123.021 115.970 1.00 64.42  ? 118  TYR K CG    1 
ATOM   4265  C  CD1   . TYR B 2 118 ? 139.265 122.156 116.124 1.00 64.54  ? 118  TYR K CD1   1 
ATOM   4266  C  CD2   . TYR B 2 118 ? 137.888 123.464 114.691 1.00 61.96  ? 118  TYR K CD2   1 
ATOM   4267  C  CE1   . TYR B 2 118 ? 140.007 121.739 115.035 1.00 67.19  ? 118  TYR K CE1   1 
ATOM   4268  C  CE2   . TYR B 2 118 ? 138.623 123.055 113.598 1.00 60.72  ? 118  TYR K CE2   1 
ATOM   4269  C  CZ    . TYR B 2 118 ? 139.680 122.193 113.774 1.00 64.99  ? 118  TYR K CZ    1 
ATOM   4270  O  OH    . TYR B 2 118 ? 140.414 121.783 112.686 1.00 63.86  ? 118  TYR K OH    1 
ATOM   4271  N  N     . ILE B 2 119 ? 135.429 123.421 119.704 1.00 49.70  ? 119  ILE K N     1 
ATOM   4272  C  CA    . ILE B 2 119 ? 135.180 123.474 121.140 1.00 48.09  ? 119  ILE K CA    1 
ATOM   4273  C  C     . ILE B 2 119 ? 134.635 122.140 121.627 1.00 57.29  ? 119  ILE K C     1 
ATOM   4274  O  O     . ILE B 2 119 ? 135.059 121.617 122.665 1.00 65.97  ? 119  ILE K O     1 
ATOM   4275  C  CB    . ILE B 2 119 ? 134.219 124.630 121.475 1.00 51.57  ? 119  ILE K CB    1 
ATOM   4276  C  CG1   . ILE B 2 119 ? 134.914 125.978 121.309 1.00 57.27  ? 119  ILE K CG1   1 
ATOM   4277  C  CG2   . ILE B 2 119 ? 133.678 124.488 122.884 1.00 55.86  ? 119  ILE K CG2   1 
ATOM   4278  C  CD1   . ILE B 2 119 ? 136.219 126.079 122.034 1.00 62.72  ? 119  ILE K CD1   1 
ATOM   4279  N  N     . TYR B 2 120 ? 133.687 121.567 120.882 1.00 56.29  ? 120  TYR K N     1 
ATOM   4280  C  CA    . TYR B 2 120 ? 133.117 120.281 121.270 1.00 50.46  ? 120  TYR K CA    1 
ATOM   4281  C  C     . TYR B 2 120 ? 134.163 119.175 121.262 1.00 53.54  ? 120  TYR K C     1 
ATOM   4282  O  O     . TYR B 2 120 ? 134.094 118.253 122.081 1.00 56.46  ? 120  TYR K O     1 
ATOM   4283  C  CB    . TYR B 2 120 ? 131.960 119.918 120.341 1.00 52.68  ? 120  TYR K CB    1 
ATOM   4284  C  CG    . TYR B 2 120 ? 130.810 120.894 120.386 1.00 57.74  ? 120  TYR K CG    1 
ATOM   4285  C  CD1   . TYR B 2 120 ? 130.588 121.683 121.503 1.00 57.45  ? 120  TYR K CD1   1 
ATOM   4286  C  CD2   . TYR B 2 120 ? 129.948 121.027 119.309 1.00 56.21  ? 120  TYR K CD2   1 
ATOM   4287  C  CE1   . TYR B 2 120 ? 129.539 122.577 121.547 1.00 60.07  ? 120  TYR K CE1   1 
ATOM   4288  C  CE2   . TYR B 2 120 ? 128.897 121.919 119.343 1.00 57.58  ? 120  TYR K CE2   1 
ATOM   4289  C  CZ    . TYR B 2 120 ? 128.697 122.691 120.463 1.00 62.50  ? 120  TYR K CZ    1 
ATOM   4290  O  OH    . TYR B 2 120 ? 127.648 123.581 120.502 1.00 60.81  ? 120  TYR K OH    1 
ATOM   4291  N  N     . SER B 2 121 ? 135.134 119.241 120.349 1.00 57.71  ? 121  SER K N     1 
ATOM   4292  C  CA    . SER B 2 121 ? 136.166 118.215 120.246 1.00 53.01  ? 121  SER K CA    1 
ATOM   4293  C  C     . SER B 2 121 ? 137.401 118.523 121.089 1.00 53.76  ? 121  SER K C     1 
ATOM   4294  O  O     . SER B 2 121 ? 138.477 117.972 120.823 1.00 53.56  ? 121  SER K O     1 
ATOM   4295  C  CB    . SER B 2 121 ? 136.562 118.017 118.784 1.00 61.10  ? 121  SER K CB    1 
ATOM   4296  O  OG    . SER B 2 121 ? 137.571 117.031 118.661 1.00 63.34  ? 121  SER K OG    1 
ATOM   4297  N  N     . MET B 2 122 ? 137.282 119.380 122.100 1.00 71.70  ? 122  MET K N     1 
ATOM   4298  C  CA    . MET B 2 122 ? 138.418 119.775 122.918 1.00 72.96  ? 122  MET K CA    1 
ATOM   4299  C  C     . MET B 2 122 ? 138.567 118.852 124.126 1.00 72.54  ? 122  MET K C     1 
ATOM   4300  O  O     . MET B 2 122 ? 137.830 117.879 124.299 1.00 74.07  ? 122  MET K O     1 
ATOM   4301  C  CB    . MET B 2 122 ? 138.269 121.226 123.373 1.00 73.03  ? 122  MET K CB    1 
ATOM   4302  C  CG    . MET B 2 122 ? 138.836 122.255 122.413 1.00 74.59  ? 122  MET K CG    1 
ATOM   4303  S  SD    . MET B 2 122 ? 140.635 122.264 122.377 1.00 81.93  ? 122  MET K SD    1 
ATOM   4304  C  CE    . MET B 2 122 ? 140.935 123.665 121.306 1.00 71.35  ? 122  MET K CE    1 
ATOM   4305  N  N     . ASP B 2 123 ? 139.544 119.165 124.973 1.00 83.25  ? 123  ASP K N     1 
ATOM   4306  C  CA    . ASP B 2 123 ? 139.726 118.433 126.217 1.00 84.42  ? 123  ASP K CA    1 
ATOM   4307  C  C     . ASP B 2 123 ? 138.577 118.720 127.175 1.00 80.83  ? 123  ASP K C     1 
ATOM   4308  O  O     . ASP B 2 123 ? 137.947 119.780 127.128 1.00 84.83  ? 123  ASP K O     1 
ATOM   4309  C  CB    . ASP B 2 123 ? 141.058 118.803 126.867 1.00 85.10  ? 123  ASP K CB    1 
ATOM   4310  C  CG    . ASP B 2 123 ? 142.250 118.357 126.044 1.00 87.68  ? 123  ASP K CG    1 
ATOM   4311  O  OD1   . ASP B 2 123 ? 142.041 117.789 124.952 1.00 86.94  ? 123  ASP K OD1   1 
ATOM   4312  O  OD2   . ASP B 2 123 ? 143.397 118.574 126.489 1.00 84.61  ? 123  ASP K OD2   1 
ATOM   4313  N  N     . GLU B 2 124 ? 138.306 117.755 128.054 1.00 80.40  ? 124  GLU K N     1 
ATOM   4314  C  CA    . GLU B 2 124 ? 137.112 117.836 128.888 1.00 87.51  ? 124  GLU K CA    1 
ATOM   4315  C  C     . GLU B 2 124 ? 137.251 118.884 129.984 1.00 87.07  ? 124  GLU K C     1 
ATOM   4316  O  O     . GLU B 2 124 ? 136.248 119.459 130.421 1.00 86.57  ? 124  GLU K O     1 
ATOM   4317  C  CB    . GLU B 2 124 ? 136.807 116.465 129.493 1.00 89.66  ? 124  GLU K CB    1 
ATOM   4318  C  CG    . GLU B 2 124 ? 135.549 116.417 130.346 1.00 90.86  ? 124  GLU K CG    1 
ATOM   4319  C  CD    . GLU B 2 124 ? 134.281 116.590 129.531 1.00 92.94  ? 124  GLU K CD    1 
ATOM   4320  O  OE1   . GLU B 2 124 ? 134.312 116.320 128.312 1.00 94.64  ? 124  GLU K OE1   1 
ATOM   4321  O  OE2   . GLU B 2 124 ? 133.252 116.999 130.110 1.00 89.06  ? 124  GLU K OE2   1 
ATOM   4322  N  N     . ASN B 2 125 ? 138.474 119.159 130.431 1.00 79.79  ? 125  ASN K N     1 
ATOM   4323  C  CA    . ASN B 2 125 ? 138.672 120.038 131.576 1.00 79.27  ? 125  ASN K CA    1 
ATOM   4324  C  C     . ASN B 2 125 ? 138.547 121.517 131.237 1.00 78.64  ? 125  ASN K C     1 
ATOM   4325  O  O     . ASN B 2 125 ? 138.574 122.345 132.154 1.00 81.38  ? 125  ASN K O     1 
ATOM   4326  C  CB    . ASN B 2 125 ? 140.040 119.779 132.213 1.00 77.73  ? 125  ASN K CB    1 
ATOM   4327  C  CG    . ASN B 2 125 ? 140.458 118.326 132.131 1.00 82.05  ? 125  ASN K CG    1 
ATOM   4328  O  OD1   . ASN B 2 125 ? 141.573 118.014 131.716 1.00 82.20  ? 125  ASN K OD1   1 
ATOM   4329  N  ND2   . ASN B 2 125 ? 139.567 117.429 132.537 1.00 84.00  ? 125  ASN K ND2   1 
ATOM   4330  N  N     . LEU B 2 126 ? 138.414 121.874 129.965 1.00 68.66  ? 126  LEU K N     1 
ATOM   4331  C  CA    . LEU B 2 126 ? 138.353 123.276 129.584 1.00 61.34  ? 126  LEU K CA    1 
ATOM   4332  C  C     . LEU B 2 126 ? 136.936 123.820 129.726 1.00 64.79  ? 126  LEU K C     1 
ATOM   4333  O  O     . LEU B 2 126 ? 135.948 123.104 129.546 1.00 71.14  ? 126  LEU K O     1 
ATOM   4334  C  CB    . LEU B 2 126 ? 138.837 123.461 128.148 1.00 64.22  ? 126  LEU K CB    1 
ATOM   4335  C  CG    . LEU B 2 126 ? 140.322 123.207 127.892 1.00 69.27  ? 126  LEU K CG    1 
ATOM   4336  C  CD1   . LEU B 2 126 ? 140.628 123.235 126.405 1.00 70.67  ? 126  LEU K CD1   1 
ATOM   4337  C  CD2   . LEU B 2 126 ? 141.175 124.220 128.634 1.00 68.43  ? 126  LEU K CD2   1 
ATOM   4338  N  N     . GLU B 2 127 ? 136.850 125.106 130.054 1.00 69.96  ? 127  GLU K N     1 
ATOM   4339  C  CA    . GLU B 2 127 ? 135.589 125.832 130.118 1.00 68.12  ? 127  GLU K CA    1 
ATOM   4340  C  C     . GLU B 2 127 ? 135.728 127.090 129.279 1.00 72.14  ? 127  GLU K C     1 
ATOM   4341  O  O     . GLU B 2 127 ? 136.708 127.828 129.424 1.00 79.57  ? 127  GLU K O     1 
ATOM   4342  C  CB    . GLU B 2 127 ? 135.220 126.189 131.559 1.00 70.51  ? 127  GLU K CB    1 
ATOM   4343  C  CG    . GLU B 2 127 ? 135.029 124.985 132.467 1.00 79.31  ? 127  GLU K CG    1 
ATOM   4344  C  CD    . GLU B 2 127 ? 134.644 125.377 133.879 1.00 81.65  ? 127  GLU K CD    1 
ATOM   4345  O  OE1   . GLU B 2 127 ? 134.353 126.571 134.108 1.00 78.34  ? 127  GLU K OE1   1 
ATOM   4346  O  OE2   . GLU B 2 127 ? 134.631 124.493 134.761 1.00 79.78  ? 127  GLU K OE2   1 
ATOM   4347  N  N     . PHE B 2 128 ? 134.757 127.335 128.407 1.00 56.82  ? 128  PHE K N     1 
ATOM   4348  C  CA    . PHE B 2 128 ? 134.851 128.393 127.414 1.00 52.94  ? 128  PHE K CA    1 
ATOM   4349  C  C     . PHE B 2 128 ? 133.754 129.424 127.620 1.00 56.41  ? 128  PHE K C     1 
ATOM   4350  O  O     . PHE B 2 128 ? 132.585 129.075 127.805 1.00 66.27  ? 128  PHE K O     1 
ATOM   4351  C  CB    . PHE B 2 128 ? 134.758 127.824 125.998 1.00 54.30  ? 128  PHE K CB    1 
ATOM   4352  C  CG    . PHE B 2 128 ? 135.900 126.928 125.627 1.00 49.77  ? 128  PHE K CG    1 
ATOM   4353  C  CD1   . PHE B 2 128 ? 137.103 127.459 125.211 1.00 56.73  ? 128  PHE K CD1   1 
ATOM   4354  C  CD2   . PHE B 2 128 ? 135.765 125.555 125.684 1.00 51.33  ? 128  PHE K CD2   1 
ATOM   4355  C  CE1   . PHE B 2 128 ? 138.153 126.639 124.867 1.00 60.34  ? 128  PHE K CE1   1 
ATOM   4356  C  CE2   . PHE B 2 128 ? 136.810 124.731 125.341 1.00 54.77  ? 128  PHE K CE2   1 
ATOM   4357  C  CZ    . PHE B 2 128 ? 138.006 125.272 124.932 1.00 61.44  ? 128  PHE K CZ    1 
ATOM   4358  N  N     . HIS B 2 129 ? 134.140 130.697 127.587 1.00 54.88  ? 129  HIS K N     1 
ATOM   4359  C  CA    . HIS B 2 129 ? 133.202 131.811 127.545 1.00 57.93  ? 129  HIS K CA    1 
ATOM   4360  C  C     . HIS B 2 129 ? 133.372 132.516 126.209 1.00 61.89  ? 129  HIS K C     1 
ATOM   4361  O  O     . HIS B 2 129 ? 134.481 132.942 125.869 1.00 70.97  ? 129  HIS K O     1 
ATOM   4362  C  CB    . HIS B 2 129 ? 133.438 132.788 128.698 1.00 57.47  ? 129  HIS K CB    1 
ATOM   4363  C  CG    . HIS B 2 129 ? 133.318 132.170 130.054 1.00 62.17  ? 129  HIS K CG    1 
ATOM   4364  N  ND1   . HIS B 2 129 ? 134.282 131.338 130.581 1.00 69.30  ? 129  HIS K ND1   1 
ATOM   4365  C  CD2   . HIS B 2 129 ? 132.352 132.272 130.997 1.00 60.29  ? 129  HIS K CD2   1 
ATOM   4366  C  CE1   . HIS B 2 129 ? 133.912 130.949 131.788 1.00 66.54  ? 129  HIS K CE1   1 
ATOM   4367  N  NE2   . HIS B 2 129 ? 132.745 131.501 132.064 1.00 65.65  ? 129  HIS K NE2   1 
ATOM   4368  N  N     . ILE B 2 130 ? 132.283 132.639 125.456 1.00 52.81  ? 130  ILE K N     1 
ATOM   4369  C  CA    . ILE B 2 130 ? 132.302 133.250 124.134 1.00 48.07  ? 130  ILE K CA    1 
ATOM   4370  C  C     . ILE B 2 130 ? 131.342 134.428 124.136 1.00 55.35  ? 130  ILE K C     1 
ATOM   4371  O  O     . ILE B 2 130 ? 130.176 134.283 124.522 1.00 64.59  ? 130  ILE K O     1 
ATOM   4372  C  CB    . ILE B 2 130 ? 131.927 132.240 123.037 1.00 50.21  ? 130  ILE K CB    1 
ATOM   4373  C  CG1   . ILE B 2 130 ? 132.762 130.970 123.175 1.00 49.74  ? 130  ILE K CG1   1 
ATOM   4374  C  CG2   . ILE B 2 130 ? 132.129 132.848 121.666 1.00 55.32  ? 130  ILE K CG2   1 
ATOM   4375  C  CD1   . ILE B 2 130 ? 132.484 129.945 122.108 1.00 57.40  ? 130  ILE K CD1   1 
ATOM   4376  N  N     . LYS B 2 131 ? 131.828 135.591 123.709 1.00 52.83  ? 131  LYS K N     1 
ATOM   4377  C  CA    . LYS B 2 131 ? 131.019 136.799 123.649 1.00 56.86  ? 131  LYS K CA    1 
ATOM   4378  C  C     . LYS B 2 131 ? 131.138 137.422 122.267 1.00 59.85  ? 131  LYS K C     1 
ATOM   4379  O  O     . LYS B 2 131 ? 132.224 137.461 121.684 1.00 62.78  ? 131  LYS K O     1 
ATOM   4380  C  CB    . LYS B 2 131 ? 131.433 137.803 124.727 1.00 57.24  ? 131  LYS K CB    1 
ATOM   4381  C  CG    . LYS B 2 131 ? 132.919 137.841 125.007 1.00 61.47  ? 131  LYS K CG    1 
ATOM   4382  C  CD    . LYS B 2 131 ? 133.205 138.447 126.370 1.00 65.57  ? 131  LYS K CD    1 
ATOM   4383  C  CE    . LYS B 2 131 ? 132.673 139.865 126.467 1.00 65.35  ? 131  LYS K CE    1 
ATOM   4384  N  NZ    . LYS B 2 131 ? 133.263 140.749 125.426 1.00 66.13  ? 131  LYS K NZ    1 
ATOM   4385  N  N     . VAL B 2 132 ? 130.014 137.911 121.753 1.00 56.00  ? 132  VAL K N     1 
ATOM   4386  C  CA    . VAL B 2 132 ? 129.897 138.369 120.375 1.00 43.98  ? 132  VAL K CA    1 
ATOM   4387  C  C     . VAL B 2 132 ? 129.533 139.846 120.380 1.00 52.43  ? 132  VAL K C     1 
ATOM   4388  O  O     . VAL B 2 132 ? 128.574 140.252 121.046 1.00 66.41  ? 132  VAL K O     1 
ATOM   4389  C  CB    . VAL B 2 132 ? 128.844 137.555 119.605 1.00 54.39  ? 132  VAL K CB    1 
ATOM   4390  C  CG1   . VAL B 2 132 ? 128.513 138.225 118.290 1.00 58.36  ? 132  VAL K CG1   1 
ATOM   4391  C  CG2   . VAL B 2 132 ? 129.325 136.135 119.386 1.00 57.84  ? 132  VAL K CG2   1 
ATOM   4392  N  N     . SER B 2 133 ? 130.293 140.642 119.636 1.00 47.59  ? 133  SER K N     1 
ATOM   4393  C  CA    . SER B 2 133 ? 129.996 142.050 119.430 1.00 51.02  ? 133  SER K CA    1 
ATOM   4394  C  C     . SER B 2 133 ? 129.942 142.330 117.936 1.00 56.63  ? 133  SER K C     1 
ATOM   4395  O  O     . SER B 2 133 ? 130.691 141.744 117.152 1.00 66.57  ? 133  SER K O     1 
ATOM   4396  C  CB    . SER B 2 133 ? 131.039 142.952 120.098 1.00 50.41  ? 133  SER K CB    1 
ATOM   4397  O  OG    . SER B 2 133 ? 131.060 142.753 121.500 1.00 57.35  ? 133  SER K OG    1 
ATOM   4398  N  N     . TYR B 2 134 ? 129.043 143.231 117.548 1.00 55.34  ? 134  TYR K N     1 
ATOM   4399  C  CA    . TYR B 2 134 ? 128.802 143.511 116.135 1.00 51.65  ? 134  TYR K CA    1 
ATOM   4400  C  C     . TYR B 2 134 ? 128.434 144.980 115.998 1.00 54.16  ? 134  TYR K C     1 
ATOM   4401  O  O     . TYR B 2 134 ? 127.342 145.383 116.406 1.00 66.10  ? 134  TYR K O     1 
ATOM   4402  C  CB    . TYR B 2 134 ? 127.696 142.614 115.591 1.00 58.29  ? 134  TYR K CB    1 
ATOM   4403  C  CG    . TYR B 2 134 ? 127.625 142.532 114.085 1.00 59.32  ? 134  TYR K CG    1 
ATOM   4404  C  CD1   . TYR B 2 134 ? 128.678 142.018 113.347 1.00 60.88  ? 134  TYR K CD1   1 
ATOM   4405  C  CD2   . TYR B 2 134 ? 126.495 142.947 113.403 1.00 61.79  ? 134  TYR K CD2   1 
ATOM   4406  C  CE1   . TYR B 2 134 ? 128.612 141.933 111.974 1.00 59.71  ? 134  TYR K CE1   1 
ATOM   4407  C  CE2   . TYR B 2 134 ? 126.421 142.865 112.031 1.00 63.93  ? 134  TYR K CE2   1 
ATOM   4408  C  CZ    . TYR B 2 134 ? 127.481 142.359 111.321 1.00 62.26  ? 134  TYR K CZ    1 
ATOM   4409  O  OH    . TYR B 2 134 ? 127.408 142.278 109.951 1.00 62.15  ? 134  TYR K OH    1 
ATOM   4410  N  N     . PHE B 2 135 ? 129.334 145.774 115.428 1.00 46.18  ? 135  PHE K N     1 
ATOM   4411  C  CA    . PHE B 2 135 ? 129.106 147.197 115.239 1.00 55.58  ? 135  PHE K CA    1 
ATOM   4412  C  C     . PHE B 2 135 ? 129.543 147.598 113.836 1.00 54.12  ? 135  PHE K C     1 
ATOM   4413  O  O     . PHE B 2 135 ? 130.024 146.777 113.050 1.00 63.34  ? 135  PHE K O     1 
ATOM   4414  C  CB    . PHE B 2 135 ? 129.836 148.024 116.304 1.00 57.18  ? 135  PHE K CB    1 
ATOM   4415  C  CG    . PHE B 2 135 ? 131.307 147.755 116.381 1.00 53.66  ? 135  PHE K CG    1 
ATOM   4416  C  CD1   . PHE B 2 135 ? 131.797 146.732 117.169 1.00 55.28  ? 135  PHE K CD1   1 
ATOM   4417  C  CD2   . PHE B 2 135 ? 132.202 148.537 115.679 1.00 58.68  ? 135  PHE K CD2   1 
ATOM   4418  C  CE1   . PHE B 2 135 ? 133.148 146.487 117.242 1.00 58.39  ? 135  PHE K CE1   1 
ATOM   4419  C  CE2   . PHE B 2 135 ? 133.554 148.297 115.752 1.00 62.12  ? 135  PHE K CE2   1 
ATOM   4420  C  CZ    . PHE B 2 135 ? 134.027 147.272 116.536 1.00 59.00  ? 135  PHE K CZ    1 
ATOM   4421  N  N     . GLU B 2 136 ? 129.373 148.880 113.523 1.00 51.55  ? 136  GLU K N     1 
ATOM   4422  C  CA    . GLU B 2 136 ? 129.690 149.396 112.201 1.00 46.24  ? 136  GLU K CA    1 
ATOM   4423  C  C     . GLU B 2 136 ? 130.209 150.818 112.328 1.00 50.41  ? 136  GLU K C     1 
ATOM   4424  O  O     . GLU B 2 136 ? 129.991 151.493 113.335 1.00 64.85  ? 136  GLU K O     1 
ATOM   4425  C  CB    . GLU B 2 136 ? 128.470 149.366 111.279 1.00 50.00  ? 136  GLU K CB    1 
ATOM   4426  C  CG    . GLU B 2 136 ? 127.487 150.491 111.534 1.00 50.71  ? 136  GLU K CG    1 
ATOM   4427  C  CD    . GLU B 2 136 ? 126.377 150.537 110.508 1.00 62.23  ? 136  GLU K CD    1 
ATOM   4428  O  OE1   . GLU B 2 136 ? 126.212 149.547 109.766 1.00 66.85  ? 136  GLU K OE1   1 
ATOM   4429  O  OE2   . GLU B 2 136 ? 125.665 151.560 110.445 1.00 64.45  ? 136  GLU K OE2   1 
ATOM   4430  N  N     . ILE B 2 137 ? 130.905 151.266 111.287 1.00 48.16  ? 137  ILE K N     1 
ATOM   4431  C  CA    . ILE B 2 137 ? 131.378 152.640 111.176 1.00 49.45  ? 137  ILE K CA    1 
ATOM   4432  C  C     . ILE B 2 137 ? 130.600 153.305 110.049 1.00 54.92  ? 137  ILE K C     1 
ATOM   4433  O  O     . ILE B 2 137 ? 130.809 152.989 108.872 1.00 57.80  ? 137  ILE K O     1 
ATOM   4434  C  CB    . ILE B 2 137 ? 132.889 152.703 110.908 1.00 46.72  ? 137  ILE K CB    1 
ATOM   4435  C  CG1   . ILE B 2 137 ? 133.621 151.586 111.651 1.00 49.75  ? 137  ILE K CG1   1 
ATOM   4436  C  CG2   . ILE B 2 137 ? 133.441 154.058 111.311 1.00 50.56  ? 137  ILE K CG2   1 
ATOM   4437  C  CD1   . ILE B 2 137 ? 133.586 151.716 113.148 1.00 56.86  ? 137  ILE K CD1   1 
ATOM   4438  N  N     . TYR B 2 138 ? 129.708 154.226 110.405 1.00 54.06  ? 138  TYR K N     1 
ATOM   4439  C  CA    . TYR B 2 138 ? 128.878 154.923 109.428 1.00 46.15  ? 138  TYR K CA    1 
ATOM   4440  C  C     . TYR B 2 138 ? 129.043 156.418 109.633 1.00 52.93  ? 138  TYR K C     1 
ATOM   4441  O  O     . TYR B 2 138 ? 128.746 156.930 110.716 1.00 58.95  ? 138  TYR K O     1 
ATOM   4442  C  CB    . TYR B 2 138 ? 127.408 154.525 109.567 1.00 47.74  ? 138  TYR K CB    1 
ATOM   4443  C  CG    . TYR B 2 138 ? 126.499 155.147 108.536 1.00 51.40  ? 138  TYR K CG    1 
ATOM   4444  C  CD1   . TYR B 2 138 ? 126.966 155.472 107.273 1.00 59.73  ? 138  TYR K CD1   1 
ATOM   4445  C  CD2   . TYR B 2 138 ? 125.177 155.426 108.833 1.00 52.78  ? 138  TYR K CD2   1 
ATOM   4446  C  CE1   . TYR B 2 138 ? 126.135 156.044 106.334 1.00 61.97  ? 138  TYR K CE1   1 
ATOM   4447  C  CE2   . TYR B 2 138 ? 124.341 155.998 107.902 1.00 52.45  ? 138  TYR K CE2   1 
ATOM   4448  C  CZ    . TYR B 2 138 ? 124.823 156.306 106.656 1.00 54.38  ? 138  TYR K CZ    1 
ATOM   4449  O  OH    . TYR B 2 138 ? 123.989 156.879 105.725 1.00 56.97  ? 138  TYR K OH    1 
ATOM   4450  N  N     . LEU B 2 139 ? 129.499 157.113 108.591 1.00 48.41  ? 139  LEU K N     1 
ATOM   4451  C  CA    . LEU B 2 139 ? 129.772 158.547 108.647 1.00 47.26  ? 139  LEU K CA    1 
ATOM   4452  C  C     . LEU B 2 139 ? 130.667 158.891 109.835 1.00 54.24  ? 139  LEU K C     1 
ATOM   4453  O  O     . LEU B 2 139 ? 130.397 159.813 110.606 1.00 54.45  ? 139  LEU K O     1 
ATOM   4454  C  CB    . LEU B 2 139 ? 128.474 159.355 108.683 1.00 50.73  ? 139  LEU K CB    1 
ATOM   4455  C  CG    . LEU B 2 139 ? 127.495 159.129 107.531 1.00 55.08  ? 139  LEU K CG    1 
ATOM   4456  C  CD1   . LEU B 2 139 ? 126.370 160.146 107.582 1.00 54.64  ? 139  LEU K CD1   1 
ATOM   4457  C  CD2   . LEU B 2 139 ? 128.212 159.193 106.198 1.00 53.03  ? 139  LEU K CD2   1 
ATOM   4458  N  N     . ASP B 2 140 ? 131.744 158.118 109.980 1.00 61.85  ? 140  ASP K N     1 
ATOM   4459  C  CA    . ASP B 2 140 ? 132.738 158.315 111.035 1.00 62.44  ? 140  ASP K CA    1 
ATOM   4460  C  C     . ASP B 2 140 ? 132.124 158.184 112.424 1.00 63.64  ? 140  ASP K C     1 
ATOM   4461  O  O     . ASP B 2 140 ? 132.570 158.827 113.376 1.00 70.17  ? 140  ASP K O     1 
ATOM   4462  C  CB    . ASP B 2 140 ? 133.443 159.667 110.885 1.00 65.68  ? 140  ASP K CB    1 
ATOM   4463  C  CG    . ASP B 2 140 ? 134.885 159.628 111.347 1.00 70.35  ? 140  ASP K CG    1 
ATOM   4464  O  OD1   . ASP B 2 140 ? 135.191 158.866 112.286 1.00 72.80  ? 140  ASP K OD1   1 
ATOM   4465  O  OD2   . ASP B 2 140 ? 135.714 160.361 110.768 1.00 68.93  ? 140  ASP K OD2   1 
ATOM   4466  N  N     . LYS B 2 141 ? 131.092 157.353 112.553 1.00 54.95  ? 141  LYS K N     1 
ATOM   4467  C  CA    . LYS B 2 141 ? 130.434 157.111 113.828 1.00 53.43  ? 141  LYS K CA    1 
ATOM   4468  C  C     . LYS B 2 141 ? 130.311 155.612 114.041 1.00 57.08  ? 141  LYS K C     1 
ATOM   4469  O  O     . LYS B 2 141 ? 129.887 154.887 113.136 1.00 63.54  ? 141  LYS K O     1 
ATOM   4470  C  CB    . LYS B 2 141 ? 129.053 157.769 113.878 1.00 55.01  ? 141  LYS K CB    1 
ATOM   4471  C  CG    . LYS B 2 141 ? 129.066 159.262 113.616 1.00 59.01  ? 141  LYS K CG    1 
ATOM   4472  C  CD    . LYS B 2 141 ? 128.747 160.047 114.873 1.00 60.44  ? 141  LYS K CD    1 
ATOM   4473  C  CE    . LYS B 2 141 ? 128.877 161.539 114.633 1.00 60.44  ? 141  LYS K CE    1 
ATOM   4474  N  NZ    . LYS B 2 141 ? 128.044 161.986 113.484 1.00 58.45  ? 141  LYS K NZ    1 
ATOM   4475  N  N     . ILE B 2 142 ? 130.677 155.152 115.235 1.00 51.08  ? 142  ILE K N     1 
ATOM   4476  C  CA    . ILE B 2 142 ? 130.633 153.735 115.574 1.00 47.71  ? 142  ILE K CA    1 
ATOM   4477  C  C     . ILE B 2 142 ? 129.235 153.435 116.102 1.00 52.37  ? 142  ILE K C     1 
ATOM   4478  O  O     . ILE B 2 142 ? 128.887 153.803 117.224 1.00 58.78  ? 142  ILE K O     1 
ATOM   4479  C  CB    . ILE B 2 142 ? 131.714 153.364 116.588 1.00 47.26  ? 142  ILE K CB    1 
ATOM   4480  C  CG1   . ILE B 2 142 ? 133.085 153.786 116.070 1.00 52.40  ? 142  ILE K CG1   1 
ATOM   4481  C  CG2   . ILE B 2 142 ? 131.684 151.878 116.871 1.00 50.98  ? 142  ILE K CG2   1 
ATOM   4482  C  CD1   . ILE B 2 142 ? 134.219 153.287 116.912 1.00 56.26  ? 142  ILE K CD1   1 
ATOM   4483  N  N     . ARG B 2 143 ? 128.435 152.751 115.294 1.00 56.08  ? 143  ARG K N     1 
ATOM   4484  C  CA    . ARG B 2 143 ? 127.067 152.407 115.648 1.00 53.23  ? 143  ARG K CA    1 
ATOM   4485  C  C     . ARG B 2 143 ? 126.978 150.934 116.009 1.00 56.79  ? 143  ARG K C     1 
ATOM   4486  O  O     . ARG B 2 143 ? 127.603 150.088 115.364 1.00 66.35  ? 143  ARG K O     1 
ATOM   4487  C  CB    . ARG B 2 143 ? 126.111 152.707 114.496 1.00 54.63  ? 143  ARG K CB    1 
ATOM   4488  C  CG    . ARG B 2 143 ? 126.310 154.056 113.847 1.00 54.03  ? 143  ARG K CG    1 
ATOM   4489  C  CD    . ARG B 2 143 ? 124.976 154.731 113.630 1.00 57.15  ? 143  ARG K CD    1 
ATOM   4490  N  NE    . ARG B 2 143 ? 123.954 153.765 113.249 1.00 61.81  ? 143  ARG K NE    1 
ATOM   4491  C  CZ    . ARG B 2 143 ? 122.663 154.044 113.140 1.00 63.34  ? 143  ARG K CZ    1 
ATOM   4492  N  NH1   . ARG B 2 143 ? 122.197 155.258 113.375 1.00 60.15  ? 143  ARG K NH1   1 
ATOM   4493  N  NH2   . ARG B 2 143 ? 121.819 153.078 112.787 1.00 62.74  ? 143  ARG K NH2   1 
ATOM   4494  N  N     . ASP B 2 144 ? 126.194 150.632 117.036 1.00 60.61  ? 144  ASP K N     1 
ATOM   4495  C  CA    . ASP B 2 144 ? 125.964 149.257 117.454 1.00 57.88  ? 144  ASP K CA    1 
ATOM   4496  C  C     . ASP B 2 144 ? 124.807 148.684 116.647 1.00 59.80  ? 144  ASP K C     1 
ATOM   4497  O  O     . ASP B 2 144 ? 123.692 149.213 116.691 1.00 65.93  ? 144  ASP K O     1 
ATOM   4498  C  CB    . ASP B 2 144 ? 125.664 149.190 118.949 1.00 65.49  ? 144  ASP K CB    1 
ATOM   4499  C  CG    . ASP B 2 144 ? 125.675 147.775 119.481 1.00 71.96  ? 144  ASP K CG    1 
ATOM   4500  O  OD1   . ASP B 2 144 ? 126.123 146.866 118.751 1.00 72.53  ? 144  ASP K OD1   1 
ATOM   4501  O  OD2   . ASP B 2 144 ? 125.233 147.568 120.630 1.00 74.90  ? 144  ASP K OD2   1 
ATOM   4502  N  N     . LEU B 2 145 ? 125.073 147.611 115.909 1.00 50.43  ? 145  LEU K N     1 
ATOM   4503  C  CA    . LEU B 2 145 ? 124.051 146.982 115.086 1.00 56.33  ? 145  LEU K CA    1 
ATOM   4504  C  C     . LEU B 2 145 ? 123.136 146.066 115.882 1.00 62.32  ? 145  LEU K C     1 
ATOM   4505  O  O     . LEU B 2 145 ? 122.164 145.548 115.324 1.00 66.32  ? 145  LEU K O     1 
ATOM   4506  C  CB    . LEU B 2 145 ? 124.704 146.208 113.940 1.00 53.12  ? 145  LEU K CB    1 
ATOM   4507  C  CG    . LEU B 2 145 ? 125.391 147.105 112.910 1.00 55.06  ? 145  LEU K CG    1 
ATOM   4508  C  CD1   . LEU B 2 145 ? 126.076 146.285 111.840 1.00 56.95  ? 145  LEU K CD1   1 
ATOM   4509  C  CD2   . LEU B 2 145 ? 124.383 148.055 112.292 1.00 62.99  ? 145  LEU K CD2   1 
ATOM   4510  N  N     . LEU B 2 146 ? 123.423 145.854 117.165 1.00 62.27  ? 146  LEU K N     1 
ATOM   4511  C  CA    . LEU B 2 146 ? 122.560 145.086 118.047 1.00 60.62  ? 146  LEU K CA    1 
ATOM   4512  C  C     . LEU B 2 146 ? 121.724 145.964 118.969 1.00 63.45  ? 146  LEU K C     1 
ATOM   4513  O  O     . LEU B 2 146 ? 120.759 145.471 119.562 1.00 66.58  ? 146  LEU K O     1 
ATOM   4514  C  CB    . LEU B 2 146 ? 123.400 144.116 118.883 1.00 56.86  ? 146  LEU K CB    1 
ATOM   4515  C  CG    . LEU B 2 146 ? 124.313 143.188 118.084 1.00 58.70  ? 146  LEU K CG    1 
ATOM   4516  C  CD1   . LEU B 2 146 ? 125.089 142.277 119.012 1.00 61.32  ? 146  LEU K CD1   1 
ATOM   4517  C  CD2   . LEU B 2 146 ? 123.501 142.379 117.092 1.00 58.98  ? 146  LEU K CD2   1 
ATOM   4518  N  N     . ASP B 2 147 ? 122.067 147.244 119.100 1.00 71.69  ? 147  ASP K N     1 
ATOM   4519  C  CA    . ASP B 2 147 ? 121.295 148.183 119.908 1.00 71.57  ? 147  ASP K CA    1 
ATOM   4520  C  C     . ASP B 2 147 ? 121.332 149.538 119.222 1.00 73.07  ? 147  ASP K C     1 
ATOM   4521  O  O     . ASP B 2 147 ? 122.405 150.133 119.087 1.00 75.68  ? 147  ASP K O     1 
ATOM   4522  C  CB    . ASP B 2 147 ? 121.852 148.282 121.328 1.00 71.87  ? 147  ASP K CB    1 
ATOM   4523  C  CG    . ASP B 2 147 ? 120.987 149.132 122.235 1.00 77.91  ? 147  ASP K CG    1 
ATOM   4524  O  OD1   . ASP B 2 147 ? 119.843 149.449 121.847 1.00 76.29  ? 147  ASP K OD1   1 
ATOM   4525  O  OD2   . ASP B 2 147 ? 121.450 149.485 123.340 1.00 81.08  ? 147  ASP K OD2   1 
ATOM   4526  N  N     . VAL B 2 148 ? 120.165 150.027 118.796 1.00 72.20  ? 148  VAL K N     1 
ATOM   4527  C  CA    . VAL B 2 148 ? 120.101 151.285 118.055 1.00 73.52  ? 148  VAL K CA    1 
ATOM   4528  C  C     . VAL B 2 148 ? 120.260 152.512 118.937 1.00 76.93  ? 148  VAL K C     1 
ATOM   4529  O  O     . VAL B 2 148 ? 120.461 153.614 118.413 1.00 76.91  ? 148  VAL K O     1 
ATOM   4530  C  CB    . VAL B 2 148 ? 118.776 151.394 117.280 1.00 74.00  ? 148  VAL K CB    1 
ATOM   4531  C  CG1   . VAL B 2 148 ? 118.645 150.246 116.298 1.00 73.00  ? 148  VAL K CG1   1 
ATOM   4532  C  CG2   . VAL B 2 148 ? 117.599 151.417 118.243 1.00 74.84  ? 148  VAL K CG2   1 
ATOM   4533  N  N     . SER B 2 149 ? 120.172 152.358 120.260 1.00 75.67  ? 149  SER K N     1 
ATOM   4534  C  CA    . SER B 2 149 ? 120.349 153.502 121.147 1.00 73.72  ? 149  SER K CA    1 
ATOM   4535  C  C     . SER B 2 149 ? 121.790 153.998 121.146 1.00 75.36  ? 149  SER K C     1 
ATOM   4536  O  O     . SER B 2 149 ? 122.028 155.201 121.295 1.00 77.68  ? 149  SER K O     1 
ATOM   4537  C  CB    . SER B 2 149 ? 119.913 153.139 122.565 1.00 75.66  ? 149  SER K CB    1 
ATOM   4538  O  OG    . SER B 2 149 ? 120.740 152.125 123.109 1.00 79.86  ? 149  SER K OG    1 
ATOM   4539  N  N     . LYS B 2 150 ? 122.758 153.097 120.981 1.00 69.39  ? 150  LYS K N     1 
ATOM   4540  C  CA    . LYS B 2 150 ? 124.172 153.467 120.930 1.00 66.80  ? 150  LYS K CA    1 
ATOM   4541  C  C     . LYS B 2 150 ? 124.476 154.013 119.538 1.00 67.36  ? 150  LYS K C     1 
ATOM   4542  O  O     . LYS B 2 150 ? 125.023 153.333 118.667 1.00 70.43  ? 150  LYS K O     1 
ATOM   4543  C  CB    . LYS B 2 150 ? 125.054 152.273 121.266 1.00 69.75  ? 150  LYS K CB    1 
ATOM   4544  C  CG    . LYS B 2 150 ? 124.527 151.386 122.379 1.00 68.15  ? 150  LYS K CG    1 
ATOM   4545  C  CD    . LYS B 2 150 ? 124.579 152.081 123.723 1.00 69.58  ? 150  LYS K CD    1 
ATOM   4546  C  CE    . LYS B 2 150 ? 124.444 151.083 124.859 1.00 70.55  ? 150  LYS K CE    1 
ATOM   4547  N  NZ    . LYS B 2 150 ? 123.232 150.232 124.711 1.00 75.70  ? 150  LYS K NZ    1 
ATOM   4548  N  N     . THR B 2 151 ? 124.105 155.278 119.330 1.00 73.47  ? 151  THR K N     1 
ATOM   4549  C  CA    . THR B 2 151 ? 124.263 155.886 118.012 1.00 74.38  ? 151  THR K CA    1 
ATOM   4550  C  C     . THR B 2 151 ? 125.732 156.092 117.659 1.00 76.22  ? 151  THR K C     1 
ATOM   4551  O  O     . THR B 2 151 ? 126.130 155.888 116.506 1.00 79.59  ? 151  THR K O     1 
ATOM   4552  C  CB    . THR B 2 151 ? 123.488 157.205 117.940 1.00 77.30  ? 151  THR K CB    1 
ATOM   4553  O  OG1   . THR B 2 151 ? 123.653 157.792 116.643 1.00 76.53  ? 151  THR K OG1   1 
ATOM   4554  C  CG2   . THR B 2 151 ? 123.948 158.186 119.016 1.00 73.60  ? 151  THR K CG2   1 
ATOM   4555  N  N     . ASN B 2 152 ? 126.554 156.499 118.624 1.00 70.99  ? 152  ASN K N     1 
ATOM   4556  C  CA    . ASN B 2 152 ? 127.983 156.646 118.398 1.00 68.31  ? 152  ASN K CA    1 
ATOM   4557  C  C     . ASN B 2 152 ? 128.736 156.205 119.643 1.00 70.40  ? 152  ASN K C     1 
ATOM   4558  O  O     . ASN B 2 152 ? 128.284 156.417 120.771 1.00 75.32  ? 152  ASN K O     1 
ATOM   4559  C  CB    . ASN B 2 152 ? 128.364 158.085 118.025 1.00 64.75  ? 152  ASN K CB    1 
ATOM   4560  C  CG    . ASN B 2 152 ? 128.191 159.051 119.173 1.00 70.13  ? 152  ASN K CG    1 
ATOM   4561  O  OD1   . ASN B 2 152 ? 127.269 158.922 119.977 1.00 74.34  ? 152  ASN K OD1   1 
ATOM   4562  N  ND2   . ASN B 2 152 ? 129.082 160.031 119.256 1.00 68.63  ? 152  ASN K ND2   1 
ATOM   4563  N  N     . LEU B 2 153 ? 129.889 155.583 119.423 1.00 61.73  ? 153  LEU K N     1 
ATOM   4564  C  CA    . LEU B 2 153 ? 130.719 155.048 120.488 1.00 54.30  ? 153  LEU K CA    1 
ATOM   4565  C  C     . LEU B 2 153 ? 132.100 155.682 120.400 1.00 62.53  ? 153  LEU K C     1 
ATOM   4566  O  O     . LEU B 2 153 ? 132.347 156.574 119.583 1.00 71.77  ? 153  LEU K O     1 
ATOM   4567  C  CB    . LEU B 2 153 ? 130.805 153.520 120.404 1.00 56.79  ? 153  LEU K CB    1 
ATOM   4568  C  CG    . LEU B 2 153 ? 129.475 152.766 120.418 1.00 56.15  ? 153  LEU K CG    1 
ATOM   4569  C  CD1   . LEU B 2 153 ? 129.701 151.280 120.227 1.00 60.89  ? 153  LEU K CD1   1 
ATOM   4570  C  CD2   . LEU B 2 153 ? 128.730 153.028 121.708 1.00 55.69  ? 153  LEU K CD2   1 
ATOM   4571  N  N     . SER B 2 154 ? 133.011 155.216 121.248 1.00 56.50  ? 154  SER K N     1 
ATOM   4572  C  CA    . SER B 2 154 ? 134.362 155.748 121.297 1.00 59.42  ? 154  SER K CA    1 
ATOM   4573  C  C     . SER B 2 154 ? 135.364 154.607 121.369 1.00 57.35  ? 154  SER K C     1 
ATOM   4574  O  O     . SER B 2 154 ? 135.053 153.515 121.851 1.00 66.85  ? 154  SER K O     1 
ATOM   4575  C  CB    . SER B 2 154 ? 134.550 156.684 122.496 1.00 61.54  ? 154  SER K CB    1 
ATOM   4576  O  OG    . SER B 2 154 ? 133.625 157.756 122.452 1.00 63.83  ? 154  SER K OG    1 
ATOM   4577  N  N     . VAL B 2 155 ? 136.571 154.869 120.885 1.00 52.26  ? 155  VAL K N     1 
ATOM   4578  C  CA    . VAL B 2 155 ? 137.668 153.912 120.938 1.00 51.82  ? 155  VAL K CA    1 
ATOM   4579  C  C     . VAL B 2 155 ? 138.624 154.377 122.026 1.00 57.72  ? 155  VAL K C     1 
ATOM   4580  O  O     . VAL B 2 155 ? 139.257 155.430 121.902 1.00 62.70  ? 155  VAL K O     1 
ATOM   4581  C  CB    . VAL B 2 155 ? 138.384 153.787 119.588 1.00 55.14  ? 155  VAL K CB    1 
ATOM   4582  C  CG1   . VAL B 2 155 ? 139.230 152.526 119.555 1.00 56.51  ? 155  VAL K CG1   1 
ATOM   4583  C  CG2   . VAL B 2 155 ? 137.382 153.785 118.459 1.00 58.13  ? 155  VAL K CG2   1 
ATOM   4584  N  N     . HIS B 2 156 ? 138.728 153.597 123.092 1.00 64.76  ? 156  HIS K N     1 
ATOM   4585  C  CA    . HIS B 2 156 ? 139.636 153.883 124.187 1.00 61.44  ? 156  HIS K CA    1 
ATOM   4586  C  C     . HIS B 2 156 ? 140.871 152.997 124.066 1.00 64.05  ? 156  HIS K C     1 
ATOM   4587  O  O     . HIS B 2 156 ? 141.060 152.289 123.075 1.00 71.70  ? 156  HIS K O     1 
ATOM   4588  C  CB    . HIS B 2 156 ? 138.920 153.694 125.523 1.00 61.48  ? 156  HIS K CB    1 
ATOM   4589  C  CG    . HIS B 2 156 ? 137.975 154.802 125.863 1.00 66.20  ? 156  HIS K CG    1 
ATOM   4590  N  ND1   . HIS B 2 156 ? 137.061 155.303 124.963 1.00 68.28  ? 156  HIS K ND1   1 
ATOM   4591  C  CD2   . HIS B 2 156 ? 137.800 155.505 127.007 1.00 69.63  ? 156  HIS K CD2   1 
ATOM   4592  C  CE1   . HIS B 2 156 ? 136.364 156.268 125.536 1.00 67.40  ? 156  HIS K CE1   1 
ATOM   4593  N  NE2   . HIS B 2 156 ? 136.793 156.410 126.777 1.00 73.20  ? 156  HIS K NE2   1 
ATOM   4594  N  N     . GLU B 2 157 ? 141.728 153.036 125.081 1.00 67.80  ? 157  GLU K N     1 
ATOM   4595  C  CA    . GLU B 2 157 ? 142.946 152.246 125.111 1.00 66.42  ? 157  GLU K CA    1 
ATOM   4596  C  C     . GLU B 2 157 ? 143.012 151.479 126.423 1.00 68.39  ? 157  GLU K C     1 
ATOM   4597  O  O     . GLU B 2 157 ? 142.321 151.798 127.393 1.00 73.13  ? 157  GLU K O     1 
ATOM   4598  C  CB    . GLU B 2 157 ? 144.188 153.127 124.940 1.00 66.82  ? 157  GLU K CB    1 
ATOM   4599  C  CG    . GLU B 2 157 ? 144.737 153.153 123.528 1.00 69.82  ? 157  GLU K CG    1 
ATOM   4600  C  CD    . GLU B 2 157 ? 145.936 154.067 123.389 1.00 75.58  ? 157  GLU K CD    1 
ATOM   4601  O  OE1   . GLU B 2 157 ? 146.054 155.020 124.187 1.00 76.45  ? 157  GLU K OE1   1 
ATOM   4602  O  OE2   . GLU B 2 157 ? 146.761 153.833 122.481 1.00 77.83  ? 157  GLU K OE2   1 
ATOM   4603  N  N     . ASP B 2 158 ? 143.853 150.453 126.444 1.00 77.23  ? 158  ASP K N     1 
ATOM   4604  C  CA    . ASP B 2 158 ? 144.039 149.596 127.602 1.00 79.05  ? 158  ASP K CA    1 
ATOM   4605  C  C     . ASP B 2 158 ? 145.358 149.931 128.290 1.00 83.70  ? 158  ASP K C     1 
ATOM   4606  O  O     . ASP B 2 158 ? 146.063 150.873 127.918 1.00 84.96  ? 158  ASP K O     1 
ATOM   4607  C  CB    . ASP B 2 158 ? 143.992 148.123 127.192 1.00 81.76  ? 158  ASP K CB    1 
ATOM   4608  C  CG    . ASP B 2 158 ? 142.580 147.631 126.952 1.00 88.36  ? 158  ASP K CG    1 
ATOM   4609  O  OD1   . ASP B 2 158 ? 141.629 148.333 127.355 1.00 86.68  ? 158  ASP K OD1   1 
ATOM   4610  O  OD2   . ASP B 2 158 ? 142.420 146.542 126.363 1.00 89.24  ? 158  ASP K OD2   1 
ATOM   4611  N  N     . LYS B 2 159 ? 145.681 149.146 129.319 1.00 88.88  ? 159  LYS K N     1 
ATOM   4612  C  CA    . LYS B 2 159 ? 146.930 149.350 130.045 1.00 85.06  ? 159  LYS K CA    1 
ATOM   4613  C  C     . LYS B 2 159 ? 148.136 149.115 129.146 1.00 84.80  ? 159  LYS K C     1 
ATOM   4614  O  O     . LYS B 2 159 ? 149.107 149.880 129.184 1.00 84.77  ? 159  LYS K O     1 
ATOM   4615  C  CB    . LYS B 2 159 ? 146.981 148.428 131.262 1.00 86.61  ? 159  LYS K CB    1 
ATOM   4616  C  CG    . LYS B 2 159 ? 145.844 148.637 132.247 1.00 85.79  ? 159  LYS K CG    1 
ATOM   4617  C  CD    . LYS B 2 159 ? 145.669 147.430 133.153 1.00 87.20  ? 159  LYS K CD    1 
ATOM   4618  C  CE    . LYS B 2 159 ? 145.200 146.215 132.370 1.00 87.23  ? 159  LYS K CE    1 
ATOM   4619  N  NZ    . LYS B 2 159 ? 143.904 146.464 131.681 1.00 86.26  ? 159  LYS K NZ    1 
ATOM   4620  N  N     . ASN B 2 160 ? 148.093 148.064 128.327 1.00 87.27  ? 160  ASN K N     1 
ATOM   4621  C  CA    . ASN B 2 160 ? 149.178 147.739 127.413 1.00 86.09  ? 160  ASN K CA    1 
ATOM   4622  C  C     . ASN B 2 160 ? 149.025 148.422 126.061 1.00 88.04  ? 160  ASN K C     1 
ATOM   4623  O  O     . ASN B 2 160 ? 149.613 147.963 125.075 1.00 89.36  ? 160  ASN K O     1 
ATOM   4624  C  CB    . ASN B 2 160 ? 149.281 146.223 127.235 1.00 84.48  ? 160  ASN K CB    1 
ATOM   4625  C  CG    . ASN B 2 160 ? 147.968 145.595 126.819 1.00 89.73  ? 160  ASN K CG    1 
ATOM   4626  O  OD1   . ASN B 2 160 ? 147.113 145.307 127.656 1.00 91.18  ? 160  ASN K OD1   1 
ATOM   4627  N  ND2   . ASN B 2 160 ? 147.801 145.376 125.520 1.00 89.25  ? 160  ASN K ND2   1 
ATOM   4628  N  N     . ARG B 2 161 ? 148.241 149.500 125.998 1.00 83.33  ? 161  ARG K N     1 
ATOM   4629  C  CA    . ARG B 2 161 ? 148.130 150.347 124.811 1.00 80.64  ? 161  ARG K CA    1 
ATOM   4630  C  C     . ARG B 2 161 ? 147.580 149.574 123.613 1.00 83.45  ? 161  ARG K C     1 
ATOM   4631  O  O     . ARG B 2 161 ? 148.196 149.511 122.547 1.00 85.24  ? 161  ARG K O     1 
ATOM   4632  C  CB    . ARG B 2 161 ? 149.475 150.995 124.478 1.00 82.92  ? 161  ARG K CB    1 
ATOM   4633  C  CG    . ARG B 2 161 ? 149.366 152.373 123.853 1.00 83.12  ? 161  ARG K CG    1 
ATOM   4634  C  CD    . ARG B 2 161 ? 150.732 152.897 123.445 1.00 85.14  ? 161  ARG K CD    1 
ATOM   4635  N  NE    . ARG B 2 161 ? 151.688 152.826 124.543 1.00 90.11  ? 161  ARG K NE    1 
ATOM   4636  C  CZ    . ARG B 2 161 ? 151.953 153.827 125.371 1.00 90.18  ? 161  ARG K CZ    1 
ATOM   4637  N  NH1   . ARG B 2 161 ? 151.352 155.000 125.254 1.00 87.89  ? 161  ARG K NH1   1 
ATOM   4638  N  NH2   . ARG B 2 161 ? 152.845 153.647 126.342 1.00 88.86  ? 161  ARG K NH2   1 
ATOM   4639  N  N     . VAL B 2 162 ? 146.400 148.980 123.794 1.00 70.68  ? 162  VAL K N     1 
ATOM   4640  C  CA    . VAL B 2 162 ? 145.664 148.349 122.710 1.00 65.71  ? 162  VAL K CA    1 
ATOM   4641  C  C     . VAL B 2 162 ? 144.280 148.984 122.655 1.00 66.54  ? 162  VAL K C     1 
ATOM   4642  O  O     . VAL B 2 162 ? 143.651 149.188 123.699 1.00 77.27  ? 162  VAL K O     1 
ATOM   4643  C  CB    . VAL B 2 162 ? 145.569 146.818 122.858 1.00 69.60  ? 162  VAL K CB    1 
ATOM   4644  C  CG1   . VAL B 2 162 ? 144.398 146.382 123.729 1.00 69.16  ? 162  VAL K CG1   1 
ATOM   4645  C  CG2   . VAL B 2 162 ? 145.487 146.162 121.489 1.00 73.82  ? 162  VAL K CG2   1 
ATOM   4646  N  N     . PRO B 2 163 ? 143.807 149.406 121.491 1.00 55.36  ? 163  PRO K N     1 
ATOM   4647  C  CA    . PRO B 2 163 ? 142.501 150.060 121.411 1.00 59.26  ? 163  PRO K CA    1 
ATOM   4648  C  C     . PRO B 2 163 ? 141.354 149.062 121.352 1.00 62.91  ? 163  PRO K C     1 
ATOM   4649  O  O     . PRO B 2 163 ? 141.494 147.927 120.897 1.00 70.29  ? 163  PRO K O     1 
ATOM   4650  C  CB    . PRO B 2 163 ? 142.591 150.869 120.114 1.00 57.25  ? 163  PRO K CB    1 
ATOM   4651  C  CG    . PRO B 2 163 ? 143.648 150.207 119.335 1.00 63.60  ? 163  PRO K CG    1 
ATOM   4652  C  CD    . PRO B 2 163 ? 144.623 149.640 120.293 1.00 62.59  ? 163  PRO K CD    1 
ATOM   4653  N  N     . TYR B 2 164 ? 140.199 149.519 121.830 1.00 60.12  ? 164  TYR K N     1 
ATOM   4654  C  CA    . TYR B 2 164 ? 138.995 148.702 121.857 1.00 59.33  ? 164  TYR K CA    1 
ATOM   4655  C  C     . TYR B 2 164 ? 137.781 149.613 121.939 1.00 62.67  ? 164  TYR K C     1 
ATOM   4656  O  O     . TYR B 2 164 ? 137.842 150.697 122.524 1.00 66.83  ? 164  TYR K O     1 
ATOM   4657  C  CB    . TYR B 2 164 ? 139.010 147.725 123.037 1.00 60.52  ? 164  TYR K CB    1 
ATOM   4658  C  CG    . TYR B 2 164 ? 138.624 148.352 124.355 1.00 62.25  ? 164  TYR K CG    1 
ATOM   4659  C  CD1   . TYR B 2 164 ? 139.468 149.245 124.995 1.00 59.87  ? 164  TYR K CD1   1 
ATOM   4660  C  CD2   . TYR B 2 164 ? 137.415 148.046 124.962 1.00 65.42  ? 164  TYR K CD2   1 
ATOM   4661  C  CE1   . TYR B 2 164 ? 139.120 149.818 126.197 1.00 63.51  ? 164  TYR K CE1   1 
ATOM   4662  C  CE2   . TYR B 2 164 ? 137.060 148.615 126.166 1.00 65.93  ? 164  TYR K CE2   1 
ATOM   4663  C  CZ    . TYR B 2 164 ? 137.916 149.500 126.779 1.00 67.84  ? 164  TYR K CZ    1 
ATOM   4664  O  OH    . TYR B 2 164 ? 137.567 150.071 127.980 1.00 70.44  ? 164  TYR K OH    1 
ATOM   4665  N  N     . VAL B 2 165 ? 136.680 149.162 121.346 1.00 61.60  ? 165  VAL K N     1 
ATOM   4666  C  CA    . VAL B 2 165 ? 135.431 149.915 121.383 1.00 61.03  ? 165  VAL K CA    1 
ATOM   4667  C  C     . VAL B 2 165 ? 134.792 149.749 122.754 1.00 66.75  ? 165  VAL K C     1 
ATOM   4668  O  O     . VAL B 2 165 ? 134.696 148.633 123.279 1.00 70.38  ? 165  VAL K O     1 
ATOM   4669  C  CB    . VAL B 2 165 ? 134.480 149.454 120.268 1.00 60.14  ? 165  VAL K CB    1 
ATOM   4670  C  CG1   . VAL B 2 165 ? 134.827 150.141 118.961 1.00 60.51  ? 165  VAL K CG1   1 
ATOM   4671  C  CG2   . VAL B 2 165 ? 134.543 147.941 120.115 1.00 67.15  ? 165  VAL K CG2   1 
ATOM   4672  N  N     . LYS B 2 166 ? 134.355 150.859 123.338 1.00 68.74  ? 166  LYS K N     1 
ATOM   4673  C  CA    . LYS B 2 166 ? 133.758 150.872 124.664 1.00 65.38  ? 166  LYS K CA    1 
ATOM   4674  C  C     . LYS B 2 166 ? 132.254 151.072 124.552 1.00 68.96  ? 166  LYS K C     1 
ATOM   4675  O  O     . LYS B 2 166 ? 131.784 151.900 123.766 1.00 73.88  ? 166  LYS K O     1 
ATOM   4676  C  CB    . LYS B 2 166 ? 134.368 151.977 125.530 1.00 65.16  ? 166  LYS K CB    1 
ATOM   4677  C  CG    . LYS B 2 166 ? 133.634 152.218 126.836 1.00 69.19  ? 166  LYS K CG    1 
ATOM   4678  C  CD    . LYS B 2 166 ? 134.344 153.246 127.693 1.00 66.80  ? 166  LYS K CD    1 
ATOM   4679  C  CE    . LYS B 2 166 ? 135.654 152.703 128.231 1.00 66.77  ? 166  LYS K CE    1 
ATOM   4680  N  NZ    . LYS B 2 166 ? 136.297 153.650 129.183 1.00 67.07  ? 166  LYS K NZ    1 
ATOM   4681  N  N     . GLY B 2 167 ? 131.504 150.310 125.343 1.00 64.38  ? 167  GLY K N     1 
ATOM   4682  C  CA    . GLY B 2 167 ? 130.063 150.416 125.365 1.00 62.34  ? 167  GLY K CA    1 
ATOM   4683  C  C     . GLY B 2 167 ? 129.334 149.508 124.402 1.00 67.52  ? 167  GLY K C     1 
ATOM   4684  O  O     . GLY B 2 167 ? 128.098 149.483 124.420 1.00 72.88  ? 167  GLY K O     1 
ATOM   4685  N  N     . CYS B 2 168 ? 130.051 148.768 123.562 1.00 73.92  ? 168  CYS K N     1 
ATOM   4686  C  CA    . CYS B 2 168 ? 129.402 147.867 122.621 1.00 76.01  ? 168  CYS K CA    1 
ATOM   4687  C  C     . CYS B 2 168 ? 128.723 146.723 123.361 1.00 74.31  ? 168  CYS K C     1 
ATOM   4688  O  O     . CYS B 2 168 ? 129.227 146.227 124.372 1.00 74.25  ? 168  CYS K O     1 
ATOM   4689  C  CB    . CYS B 2 168 ? 130.419 147.317 121.621 1.00 76.01  ? 168  CYS K CB    1 
ATOM   4690  S  SG    . CYS B 2 168 ? 131.794 146.413 122.367 1.00 84.13  ? 168  CYS K SG    1 
ATOM   4691  N  N     . THR B 2 169 ? 127.566 146.309 122.853 1.00 65.76  ? 169  THR K N     1 
ATOM   4692  C  CA    . THR B 2 169 ? 126.835 145.208 123.462 1.00 66.52  ? 169  THR K CA    1 
ATOM   4693  C  C     . THR B 2 169 ? 127.606 143.908 123.281 1.00 70.91  ? 169  THR K C     1 
ATOM   4694  O  O     . THR B 2 169 ? 127.942 143.522 122.158 1.00 76.33  ? 169  THR K O     1 
ATOM   4695  C  CB    . THR B 2 169 ? 125.444 145.089 122.845 1.00 72.27  ? 169  THR K CB    1 
ATOM   4696  O  OG1   . THR B 2 169 ? 124.761 146.342 122.961 1.00 77.18  ? 169  THR K OG1   1 
ATOM   4697  C  CG2   . THR B 2 169 ? 124.640 144.015 123.554 1.00 70.79  ? 169  THR K CG2   1 
ATOM   4698  N  N     . GLU B 2 170 ? 127.886 143.233 124.391 1.00 70.88  ? 170  GLU K N     1 
ATOM   4699  C  CA    . GLU B 2 170 ? 128.620 141.973 124.392 1.00 70.97  ? 170  GLU K CA    1 
ATOM   4700  C  C     . GLU B 2 170 ? 127.652 140.867 124.787 1.00 73.44  ? 170  GLU K C     1 
ATOM   4701  O  O     . GLU B 2 170 ? 127.313 140.723 125.966 1.00 76.65  ? 170  GLU K O     1 
ATOM   4702  C  CB    . GLU B 2 170 ? 129.808 142.035 125.348 1.00 69.97  ? 170  GLU K CB    1 
ATOM   4703  C  CG    . GLU B 2 170 ? 130.739 143.207 125.096 1.00 74.64  ? 170  GLU K CG    1 
ATOM   4704  C  CD    . GLU B 2 170 ? 131.694 143.451 126.248 1.00 80.19  ? 170  GLU K CD    1 
ATOM   4705  O  OE1   . GLU B 2 170 ? 131.515 142.825 127.313 1.00 80.45  ? 170  GLU K OE1   1 
ATOM   4706  O  OE2   . GLU B 2 170 ? 132.623 144.270 126.087 1.00 78.82  ? 170  GLU K OE2   1 
ATOM   4707  N  N     . ARG B 2 171 ? 127.208 140.090 123.805 1.00 62.83  ? 171  ARG K N     1 
ATOM   4708  C  CA    . ARG B 2 171 ? 126.241 139.026 124.028 1.00 59.50  ? 171  ARG K CA    1 
ATOM   4709  C  C     . ARG B 2 171 ? 126.970 137.696 124.151 1.00 65.01  ? 171  ARG K C     1 
ATOM   4710  O  O     . ARG B 2 171 ? 127.676 137.282 123.225 1.00 69.71  ? 171  ARG K O     1 
ATOM   4711  C  CB    . ARG B 2 171 ? 125.219 138.969 122.894 1.00 59.11  ? 171  ARG K CB    1 
ATOM   4712  C  CG    . ARG B 2 171 ? 124.187 140.073 122.935 1.00 63.04  ? 171  ARG K CG    1 
ATOM   4713  C  CD    . ARG B 2 171 ? 122.798 139.526 122.679 1.00 63.15  ? 171  ARG K CD    1 
ATOM   4714  N  NE    . ARG B 2 171 ? 122.379 139.707 121.296 1.00 66.76  ? 171  ARG K NE    1 
ATOM   4715  C  CZ    . ARG B 2 171 ? 121.569 140.671 120.882 1.00 69.15  ? 171  ARG K CZ    1 
ATOM   4716  N  NH1   . ARG B 2 171 ? 121.076 141.566 121.721 1.00 67.23  ? 171  ARG K NH1   1 
ATOM   4717  N  NH2   . ARG B 2 171 ? 121.246 140.739 119.594 1.00 66.79  ? 171  ARG K NH2   1 
ATOM   4718  N  N     . PHE B 2 172 ? 126.803 137.035 125.292 1.00 63.26  ? 172  PHE K N     1 
ATOM   4719  C  CA    . PHE B 2 172 ? 127.327 135.690 125.458 1.00 58.64  ? 172  PHE K CA    1 
ATOM   4720  C  C     . PHE B 2 172 ? 126.520 134.710 124.618 1.00 62.65  ? 172  PHE K C     1 
ATOM   4721  O  O     . PHE B 2 172 ? 125.305 134.850 124.457 1.00 66.57  ? 172  PHE K O     1 
ATOM   4722  C  CB    . PHE B 2 172 ? 127.290 135.276 126.926 1.00 56.28  ? 172  PHE K CB    1 
ATOM   4723  C  CG    . PHE B 2 172 ? 128.249 136.031 127.792 1.00 58.54  ? 172  PHE K CG    1 
ATOM   4724  C  CD1   . PHE B 2 172 ? 127.900 137.255 128.328 1.00 63.26  ? 172  PHE K CD1   1 
ATOM   4725  C  CD2   . PHE B 2 172 ? 129.497 135.513 128.076 1.00 59.76  ? 172  PHE K CD2   1 
ATOM   4726  C  CE1   . PHE B 2 172 ? 128.779 137.949 129.126 1.00 64.84  ? 172  PHE K CE1   1 
ATOM   4727  C  CE2   . PHE B 2 172 ? 130.380 136.203 128.876 1.00 63.62  ? 172  PHE K CE2   1 
ATOM   4728  C  CZ    . PHE B 2 172 ? 130.021 137.423 129.401 1.00 65.23  ? 172  PHE K CZ    1 
ATOM   4729  N  N     . VAL B 2 173 ? 127.207 133.707 124.077 1.00 53.94  ? 173  VAL K N     1 
ATOM   4730  C  CA    . VAL B 2 173 ? 126.572 132.727 123.209 1.00 55.80  ? 173  VAL K CA    1 
ATOM   4731  C  C     . VAL B 2 173 ? 126.912 131.327 123.697 1.00 60.33  ? 173  VAL K C     1 
ATOM   4732  O  O     . VAL B 2 173 ? 127.922 131.100 124.365 1.00 59.86  ? 173  VAL K O     1 
ATOM   4733  C  CB    . VAL B 2 173 ? 126.987 132.900 121.734 1.00 61.63  ? 173  VAL K CB    1 
ATOM   4734  C  CG1   . VAL B 2 173 ? 126.572 134.267 121.223 1.00 59.23  ? 173  VAL K CG1   1 
ATOM   4735  C  CG2   . VAL B 2 173 ? 128.482 132.701 121.579 1.00 63.86  ? 173  VAL K CG2   1 
ATOM   4736  N  N     . CYS B 2 174 ? 126.039 130.387 123.357 1.00 65.43  ? 174  CYS K N     1 
ATOM   4737  C  CA    . CYS B 2 174 ? 126.197 128.982 123.709 1.00 59.33  ? 174  CYS K CA    1 
ATOM   4738  C  C     . CYS B 2 174 ? 126.111 128.054 122.511 1.00 63.21  ? 174  CYS K C     1 
ATOM   4739  O  O     . CYS B 2 174 ? 126.818 127.046 122.466 1.00 70.70  ? 174  CYS K O     1 
ATOM   4740  C  CB    . CYS B 2 174 ? 125.135 128.573 124.736 1.00 63.29  ? 174  CYS K CB    1 
ATOM   4741  S  SG    . CYS B 2 174 ? 125.228 129.458 126.302 1.00 77.69  ? 174  CYS K SG    1 
ATOM   4742  N  N     . SER B 2 175 ? 125.268 128.369 121.540 1.00 67.26  ? 175  SER K N     1 
ATOM   4743  C  CA    . SER B 2 175 ? 125.046 127.553 120.359 1.00 72.66  ? 175  SER K CA    1 
ATOM   4744  C  C     . SER B 2 175 ? 125.217 128.408 119.116 1.00 70.25  ? 175  SER K C     1 
ATOM   4745  O  O     . SER B 2 175 ? 125.062 129.632 119.170 1.00 74.93  ? 175  SER K O     1 
ATOM   4746  C  CB    . SER B 2 175 ? 123.642 126.929 120.377 1.00 74.34  ? 175  SER K CB    1 
ATOM   4747  O  OG    . SER B 2 175 ? 123.465 126.104 121.515 1.00 75.39  ? 175  SER K OG    1 
ATOM   4748  N  N     . PRO B 2 176 ? 125.552 127.795 117.978 1.00 62.74  ? 176  PRO K N     1 
ATOM   4749  C  CA    . PRO B 2 176 ? 125.673 128.578 116.738 1.00 63.34  ? 176  PRO K CA    1 
ATOM   4750  C  C     . PRO B 2 176 ? 124.384 129.256 116.316 1.00 65.13  ? 176  PRO K C     1 
ATOM   4751  O  O     . PRO B 2 176 ? 124.438 130.231 115.557 1.00 72.84  ? 176  PRO K O     1 
ATOM   4752  C  CB    . PRO B 2 176 ? 126.124 127.537 115.705 1.00 65.78  ? 176  PRO K CB    1 
ATOM   4753  C  CG    . PRO B 2 176 ? 125.781 126.214 116.306 1.00 67.87  ? 176  PRO K CG    1 
ATOM   4754  C  CD    . PRO B 2 176 ? 125.940 126.391 117.778 1.00 66.61  ? 176  PRO K CD    1 
ATOM   4755  N  N     . ASP B 2 177 ? 123.229 128.777 116.780 1.00 71.49  ? 177  ASP K N     1 
ATOM   4756  C  CA    . ASP B 2 177 ? 121.971 129.435 116.448 1.00 75.41  ? 177  ASP K CA    1 
ATOM   4757  C  C     . ASP B 2 177 ? 121.922 130.848 117.015 1.00 78.77  ? 177  ASP K C     1 
ATOM   4758  O  O     . ASP B 2 177 ? 121.425 131.771 116.359 1.00 82.98  ? 177  ASP K O     1 
ATOM   4759  C  CB    . ASP B 2 177 ? 120.795 128.608 116.964 1.00 79.12  ? 177  ASP K CB    1 
ATOM   4760  C  CG    . ASP B 2 177 ? 119.466 129.067 116.397 1.00 82.36  ? 177  ASP K CG    1 
ATOM   4761  O  OD1   . ASP B 2 177 ? 119.471 129.841 115.417 1.00 79.81  ? 177  ASP K OD1   1 
ATOM   4762  O  OD2   . ASP B 2 177 ? 118.416 128.653 116.932 1.00 83.44  ? 177  ASP K OD2   1 
ATOM   4763  N  N     . GLU B 2 178 ? 122.424 131.035 118.237 1.00 73.58  ? 178  GLU K N     1 
ATOM   4764  C  CA    . GLU B 2 178 ? 122.445 132.368 118.830 1.00 69.34  ? 178  GLU K CA    1 
ATOM   4765  C  C     . GLU B 2 178 ? 123.351 133.307 118.044 1.00 69.87  ? 178  GLU K C     1 
ATOM   4766  O  O     . GLU B 2 178 ? 123.005 134.473 117.818 1.00 76.05  ? 178  GLU K O     1 
ATOM   4767  C  CB    . GLU B 2 178 ? 122.889 132.286 120.289 1.00 71.02  ? 178  GLU K CB    1 
ATOM   4768  C  CG    . GLU B 2 178 ? 122.078 131.318 121.129 1.00 77.94  ? 178  GLU K CG    1 
ATOM   4769  C  CD    . GLU B 2 178 ? 122.506 131.309 122.583 1.00 80.14  ? 178  GLU K CD    1 
ATOM   4770  O  OE1   . GLU B 2 178 ? 123.196 132.260 123.007 1.00 77.04  ? 178  GLU K OE1   1 
ATOM   4771  O  OE2   . GLU B 2 178 ? 122.153 130.351 123.302 1.00 79.01  ? 178  GLU K OE2   1 
ATOM   4772  N  N     . VAL B 2 179 ? 124.513 132.816 117.610 1.00 62.23  ? 179  VAL K N     1 
ATOM   4773  C  CA    . VAL B 2 179 ? 125.412 133.640 116.807 1.00 63.87  ? 179  VAL K CA    1 
ATOM   4774  C  C     . VAL B 2 179 ? 124.764 133.986 115.473 1.00 68.80  ? 179  VAL K C     1 
ATOM   4775  O  O     . VAL B 2 179 ? 124.904 135.108 114.971 1.00 77.55  ? 179  VAL K O     1 
ATOM   4776  C  CB    . VAL B 2 179 ? 126.764 132.930 116.613 1.00 65.13  ? 179  VAL K CB    1 
ATOM   4777  C  CG1   . VAL B 2 179 ? 127.725 133.826 115.859 1.00 67.99  ? 179  VAL K CG1   1 
ATOM   4778  C  CG2   . VAL B 2 179 ? 127.352 132.531 117.952 1.00 64.37  ? 179  VAL K CG2   1 
ATOM   4779  N  N     . MET B 2 180 ? 124.053 133.030 114.873 1.00 67.16  ? 180  MET K N     1 
ATOM   4780  C  CA    . MET B 2 180 ? 123.381 133.299 113.606 1.00 65.65  ? 180  MET K CA    1 
ATOM   4781  C  C     . MET B 2 180 ? 122.272 134.330 113.772 1.00 68.91  ? 180  MET K C     1 
ATOM   4782  O  O     . MET B 2 180 ? 122.082 135.193 112.907 1.00 75.50  ? 180  MET K O     1 
ATOM   4783  C  CB    . MET B 2 180 ? 122.833 132.002 113.018 1.00 68.97  ? 180  MET K CB    1 
ATOM   4784  C  CG    . MET B 2 180 ? 123.905 131.072 112.484 1.00 70.96  ? 180  MET K CG    1 
ATOM   4785  S  SD    . MET B 2 180 ? 124.686 131.709 110.993 1.00 82.47  ? 180  MET K SD    1 
ATOM   4786  C  CE    . MET B 2 180 ? 126.211 132.362 111.659 1.00 69.64  ? 180  MET K CE    1 
ATOM   4787  N  N     . ASP B 2 181 ? 121.525 134.256 114.874 1.00 65.36  ? 181  ASP K N     1 
ATOM   4788  C  CA    . ASP B 2 181 ? 120.502 135.263 115.139 1.00 67.72  ? 181  ASP K CA    1 
ATOM   4789  C  C     . ASP B 2 181 ? 121.127 136.633 115.370 1.00 69.54  ? 181  ASP K C     1 
ATOM   4790  O  O     . ASP B 2 181 ? 120.577 137.655 114.941 1.00 77.61  ? 181  ASP K O     1 
ATOM   4791  C  CB    . ASP B 2 181 ? 119.653 134.849 116.339 1.00 72.54  ? 181  ASP K CB    1 
ATOM   4792  C  CG    . ASP B 2 181 ? 118.868 133.581 116.085 1.00 74.85  ? 181  ASP K CG    1 
ATOM   4793  O  OD1   . ASP B 2 181 ? 119.012 133.001 114.989 1.00 75.13  ? 181  ASP K OD1   1 
ATOM   4794  O  OD2   . ASP B 2 181 ? 118.105 133.163 116.981 1.00 74.45  ? 181  ASP K OD2   1 
ATOM   4795  N  N     . THR B 2 182 ? 122.274 136.673 116.051 1.00 59.16  ? 182  THR K N     1 
ATOM   4796  C  CA    . THR B 2 182 ? 122.995 137.930 116.211 1.00 56.94  ? 182  THR K CA    1 
ATOM   4797  C  C     . THR B 2 182 ? 123.410 138.496 114.859 1.00 62.42  ? 182  THR K C     1 
ATOM   4798  O  O     . THR B 2 182 ? 123.261 139.697 114.605 1.00 71.47  ? 182  THR K O     1 
ATOM   4799  C  CB    . THR B 2 182 ? 124.219 137.720 117.101 1.00 59.57  ? 182  THR K CB    1 
ATOM   4800  O  OG1   . THR B 2 182 ? 123.800 137.281 118.398 1.00 61.88  ? 182  THR K OG1   1 
ATOM   4801  C  CG2   . THR B 2 182 ? 125.004 139.009 117.243 1.00 64.64  ? 182  THR K CG2   1 
ATOM   4802  N  N     . ILE B 2 183 ? 123.915 137.636 113.974 1.00 56.53  ? 183  ILE K N     1 
ATOM   4803  C  CA    . ILE B 2 183 ? 124.305 138.068 112.635 1.00 53.25  ? 183  ILE K CA    1 
ATOM   4804  C  C     . ILE B 2 183 ? 123.102 138.616 111.878 1.00 59.25  ? 183  ILE K C     1 
ATOM   4805  O  O     . ILE B 2 183 ? 123.194 139.645 111.200 1.00 68.71  ? 183  ILE K O     1 
ATOM   4806  C  CB    . ILE B 2 183 ? 124.971 136.906 111.875 1.00 58.01  ? 183  ILE K CB    1 
ATOM   4807  C  CG1   . ILE B 2 183 ? 126.380 136.655 112.406 1.00 57.38  ? 183  ILE K CG1   1 
ATOM   4808  C  CG2   . ILE B 2 183 ? 125.011 137.191 110.383 1.00 62.31  ? 183  ILE K CG2   1 
ATOM   4809  C  CD1   . ILE B 2 183 ? 127.367 137.723 112.011 1.00 60.69  ? 183  ILE K CD1   1 
ATOM   4810  N  N     . ASP B 2 184 ? 121.959 137.936 111.977 1.00 57.46  ? 184  ASP K N     1 
ATOM   4811  C  CA    . ASP B 2 184 ? 120.761 138.383 111.273 1.00 60.86  ? 184  ASP K CA    1 
ATOM   4812  C  C     . ASP B 2 184 ? 120.291 139.740 111.785 1.00 66.16  ? 184  ASP K C     1 
ATOM   4813  O  O     . ASP B 2 184 ? 119.998 140.650 110.996 1.00 72.54  ? 184  ASP K O     1 
ATOM   4814  C  CB    . ASP B 2 184 ? 119.655 137.340 111.422 1.00 63.48  ? 184  ASP K CB    1 
ATOM   4815  C  CG    . ASP B 2 184 ? 118.525 137.543 110.434 1.00 74.51  ? 184  ASP K CG    1 
ATOM   4816  O  OD1   . ASP B 2 184 ? 118.659 138.409 109.545 1.00 75.26  ? 184  ASP K OD1   1 
ATOM   4817  O  OD2   . ASP B 2 184 ? 117.501 136.837 110.547 1.00 75.92  ? 184  ASP K OD2   1 
ATOM   4818  N  N     . GLU B 2 185 ? 120.222 139.895 113.108 1.00 63.57  ? 185  GLU K N     1 
ATOM   4819  C  CA    . GLU B 2 185 ? 119.782 141.162 113.682 1.00 59.91  ? 185  GLU K CA    1 
ATOM   4820  C  C     . GLU B 2 185 ? 120.741 142.288 113.327 1.00 62.28  ? 185  GLU K C     1 
ATOM   4821  O  O     . GLU B 2 185 ? 120.315 143.425 113.092 1.00 67.32  ? 185  GLU K O     1 
ATOM   4822  C  CB    . GLU B 2 185 ? 119.640 141.033 115.197 1.00 61.13  ? 185  GLU K CB    1 
ATOM   4823  C  CG    . GLU B 2 185 ? 119.011 142.244 115.860 1.00 67.04  ? 185  GLU K CG    1 
ATOM   4824  C  CD    . GLU B 2 185 ? 118.786 142.045 117.345 1.00 72.77  ? 185  GLU K CD    1 
ATOM   4825  O  OE1   . GLU B 2 185 ? 119.265 141.027 117.888 1.00 75.55  ? 185  GLU K OE1   1 
ATOM   4826  O  OE2   . GLU B 2 185 ? 118.130 142.905 117.969 1.00 70.66  ? 185  GLU K OE2   1 
ATOM   4827  N  N     . GLY B 2 186 ? 122.041 141.997 113.287 1.00 59.53  ? 186  GLY K N     1 
ATOM   4828  C  CA    . GLY B 2 186 ? 122.996 143.009 112.871 1.00 62.47  ? 186  GLY K CA    1 
ATOM   4829  C  C     . GLY B 2 186 ? 122.855 143.384 111.409 1.00 63.39  ? 186  GLY K C     1 
ATOM   4830  O  O     . GLY B 2 186 ? 122.949 144.559 111.047 1.00 66.12  ? 186  GLY K O     1 
ATOM   4831  N  N     . LYS B 2 187 ? 122.629 142.390 110.547 1.00 58.41  ? 187  LYS K N     1 
ATOM   4832  C  CA    . LYS B 2 187 ? 122.500 142.661 109.120 1.00 54.20  ? 187  LYS K CA    1 
ATOM   4833  C  C     . LYS B 2 187 ? 121.247 143.466 108.822 1.00 58.05  ? 187  LYS K C     1 
ATOM   4834  O  O     . LYS B 2 187 ? 121.225 144.266 107.879 1.00 65.82  ? 187  LYS K O     1 
ATOM   4835  C  CB    . LYS B 2 187 ? 122.487 141.352 108.334 1.00 54.92  ? 187  LYS K CB    1 
ATOM   4836  C  CG    . LYS B 2 187 ? 123.776 141.061 107.599 1.00 63.98  ? 187  LYS K CG    1 
ATOM   4837  C  CD    . LYS B 2 187 ? 123.614 139.877 106.665 1.00 68.80  ? 187  LYS K CD    1 
ATOM   4838  C  CE    . LYS B 2 187 ? 122.436 140.072 105.725 1.00 65.50  ? 187  LYS K CE    1 
ATOM   4839  N  NZ    . LYS B 2 187 ? 122.603 141.282 104.875 1.00 66.75  ? 187  LYS K NZ    1 
ATOM   4840  N  N     . SER B 2 188 ? 120.187 143.258 109.603 1.00 57.33  ? 188  SER K N     1 
ATOM   4841  C  CA    . SER B 2 188 ? 118.962 144.021 109.388 1.00 62.12  ? 188  SER K CA    1 
ATOM   4842  C  C     . SER B 2 188 ? 119.202 145.515 109.564 1.00 63.32  ? 188  SER K C     1 
ATOM   4843  O  O     . SER B 2 188 ? 118.603 146.335 108.859 1.00 67.26  ? 188  SER K O     1 
ATOM   4844  C  CB    . SER B 2 188 ? 117.871 143.538 110.343 1.00 64.83  ? 188  SER K CB    1 
ATOM   4845  O  OG    . SER B 2 188 ? 116.685 144.296 110.186 1.00 65.67  ? 188  SER K OG    1 
ATOM   4846  N  N     . ASN B 2 189 ? 120.075 145.888 110.497 1.00 55.95  ? 189  ASN K N     1 
ATOM   4847  C  CA    . ASN B 2 189 ? 120.297 147.286 110.835 1.00 57.82  ? 189  ASN K CA    1 
ATOM   4848  C  C     . ASN B 2 189 ? 121.486 147.909 110.116 1.00 61.24  ? 189  ASN K C     1 
ATOM   4849  O  O     . ASN B 2 189 ? 121.712 149.114 110.267 1.00 62.82  ? 189  ASN K O     1 
ATOM   4850  C  CB    . ASN B 2 189 ? 120.488 147.431 112.346 1.00 56.97  ? 189  ASN K CB    1 
ATOM   4851  C  CG    . ASN B 2 189 ? 119.204 147.229 113.114 1.00 59.71  ? 189  ASN K CG    1 
ATOM   4852  O  OD1   . ASN B 2 189 ? 118.205 146.770 112.563 1.00 62.38  ? 189  ASN K OD1   1 
ATOM   4853  N  ND2   . ASN B 2 189 ? 119.223 147.561 114.397 1.00 60.47  ? 189  ASN K ND2   1 
ATOM   4854  N  N     . ARG B 2 190 ? 122.252 147.135 109.353 1.00 60.18  ? 190  ARG K N     1 
ATOM   4855  C  CA    . ARG B 2 190 ? 123.367 147.704 108.610 1.00 51.72  ? 190  ARG K CA    1 
ATOM   4856  C  C     . ARG B 2 190 ? 122.856 148.562 107.458 1.00 57.38  ? 190  ARG K C     1 
ATOM   4857  O  O     . ARG B 2 190 ? 121.829 148.268 106.841 1.00 61.55  ? 190  ARG K O     1 
ATOM   4858  C  CB    . ARG B 2 190 ? 124.280 146.601 108.080 1.00 50.73  ? 190  ARG K CB    1 
ATOM   4859  C  CG    . ARG B 2 190 ? 125.590 147.113 107.518 1.00 55.69  ? 190  ARG K CG    1 
ATOM   4860  C  CD    . ARG B 2 190 ? 126.442 145.987 106.974 1.00 60.66  ? 190  ARG K CD    1 
ATOM   4861  N  NE    . ARG B 2 190 ? 127.646 146.490 106.326 1.00 58.75  ? 190  ARG K NE    1 
ATOM   4862  C  CZ    . ARG B 2 190 ? 128.508 145.737 105.659 1.00 59.53  ? 190  ARG K CZ    1 
ATOM   4863  N  NH1   . ARG B 2 190 ? 128.330 144.433 105.529 1.00 61.53  ? 190  ARG K NH1   1 
ATOM   4864  N  NH2   . ARG B 2 190 ? 129.575 146.306 105.106 1.00 56.86  ? 190  ARG K NH2   1 
ATOM   4865  N  N     . HIS B 2 191 ? 123.587 149.634 107.171 1.00 52.69  ? 191  HIS K N     1 
ATOM   4866  C  CA    . HIS B 2 191 ? 123.157 150.627 106.196 1.00 57.00  ? 191  HIS K CA    1 
ATOM   4867  C  C     . HIS B 2 191 ? 123.534 150.190 104.789 1.00 56.24  ? 191  HIS K C     1 
ATOM   4868  O  O     . HIS B 2 191 ? 124.702 149.899 104.512 1.00 60.41  ? 191  HIS K O     1 
ATOM   4869  C  CB    . HIS B 2 191 ? 123.775 151.988 106.508 1.00 53.88  ? 191  HIS K CB    1 
ATOM   4870  C  CG    . HIS B 2 191 ? 123.063 152.738 107.587 1.00 52.08  ? 191  HIS K CG    1 
ATOM   4871  N  ND1   . HIS B 2 191 ? 123.462 152.703 108.905 1.00 53.41  ? 191  HIS K ND1   1 
ATOM   4872  C  CD2   . HIS B 2 191 ? 121.973 153.540 107.545 1.00 53.07  ? 191  HIS K CD2   1 
ATOM   4873  C  CE1   . HIS B 2 191 ? 122.649 153.452 109.628 1.00 54.89  ? 191  HIS K CE1   1 
ATOM   4874  N  NE2   . HIS B 2 191 ? 121.738 153.972 108.826 1.00 56.22  ? 191  HIS K NE2   1 
ATOM   4875  N  N     . VAL B 2 192 ? 122.540 150.151 103.903 1.00 45.80  ? 192  VAL K N     1 
ATOM   4876  C  CA    . VAL B 2 192 ? 122.735 149.774 102.513 1.00 42.16  ? 192  VAL K CA    1 
ATOM   4877  C  C     . VAL B 2 192 ? 122.072 150.818 101.628 1.00 44.46  ? 192  VAL K C     1 
ATOM   4878  O  O     . VAL B 2 192 ? 121.144 151.518 102.039 1.00 53.33  ? 192  VAL K O     1 
ATOM   4879  C  CB    . VAL B 2 192 ? 122.175 148.371 102.204 1.00 42.86  ? 192  VAL K CB    1 
ATOM   4880  C  CG1   . VAL B 2 192 ? 122.984 147.310 102.924 1.00 42.24  ? 192  VAL K CG1   1 
ATOM   4881  C  CG2   . VAL B 2 192 ? 120.715 148.290 102.601 1.00 46.13  ? 192  VAL K CG2   1 
ATOM   4882  N  N     . ALA B 2 193 ? 122.563 150.917 100.396 1.00 43.32  ? 193  ALA K N     1 
ATOM   4883  C  CA    . ALA B 2 193 ? 122.050 151.893 99.450  1.00 38.98  ? 193  ALA K CA    1 
ATOM   4884  C  C     . ALA B 2 193 ? 122.116 151.313 98.047  1.00 47.34  ? 193  ALA K C     1 
ATOM   4885  O  O     . ALA B 2 193 ? 122.875 150.381 97.774  1.00 54.61  ? 193  ALA K O     1 
ATOM   4886  C  CB    . ALA B 2 193 ? 122.826 153.211 99.523  1.00 47.92  ? 193  ALA K CB    1 
ATOM   4887  N  N     . VAL B 2 194 ? 121.307 151.879 97.158  1.00 54.87  ? 194  VAL K N     1 
ATOM   4888  C  CA    . VAL B 2 194 ? 121.219 151.437 95.772  1.00 47.61  ? 194  VAL K CA    1 
ATOM   4889  C  C     . VAL B 2 194 ? 122.152 152.295 94.933  1.00 46.91  ? 194  VAL K C     1 
ATOM   4890  O  O     . VAL B 2 194 ? 122.006 153.521 94.886  1.00 55.36  ? 194  VAL K O     1 
ATOM   4891  C  CB    . VAL B 2 194 ? 119.779 151.518 95.247  1.00 45.67  ? 194  VAL K CB    1 
ATOM   4892  C  CG1   . VAL B 2 194 ? 119.748 151.243 93.756  1.00 49.32  ? 194  VAL K CG1   1 
ATOM   4893  C  CG2   . VAL B 2 194 ? 118.891 150.537 95.989  1.00 50.64  ? 194  VAL K CG2   1 
ATOM   4894  N  N     . THR B 2 195 ? 123.108 151.653 94.269  1.00 48.83  ? 195  THR K N     1 
ATOM   4895  C  CA    . THR B 2 195 ? 124.048 152.337 93.399  1.00 51.00  ? 195  THR K CA    1 
ATOM   4896  C  C     . THR B 2 195 ? 124.057 151.652 92.042  1.00 57.81  ? 195  THR K C     1 
ATOM   4897  O  O     . THR B 2 195 ? 123.584 150.523 91.890  1.00 68.54  ? 195  THR K O     1 
ATOM   4898  C  CB    . THR B 2 195 ? 125.466 152.359 93.986  1.00 59.18  ? 195  THR K CB    1 
ATOM   4899  O  OG1   . THR B 2 195 ? 125.887 151.021 94.273  1.00 64.27  ? 195  THR K OG1   1 
ATOM   4900  C  CG2   . THR B 2 195 ? 125.503 153.180 95.261  1.00 60.52  ? 195  THR K CG2   1 
ATOM   4901  N  N     . ASN B 2 196 ? 124.592 152.360 91.049  1.00 55.17  ? 196  ASN K N     1 
ATOM   4902  C  CA    . ASN B 2 196 ? 124.614 151.826 89.692  1.00 52.77  ? 196  ASN K CA    1 
ATOM   4903  C  C     . ASN B 2 196 ? 125.466 150.567 89.603  1.00 62.40  ? 196  ASN K C     1 
ATOM   4904  O  O     . ASN B 2 196 ? 125.103 149.612 88.908  1.00 70.12  ? 196  ASN K O     1 
ATOM   4905  C  CB    . ASN B 2 196 ? 125.116 152.889 88.721  1.00 52.85  ? 196  ASN K CB    1 
ATOM   4906  C  CG    . ASN B 2 196 ? 124.162 154.056 88.597  1.00 57.97  ? 196  ASN K CG    1 
ATOM   4907  O  OD1   . ASN B 2 196 ? 123.156 153.975 87.896  1.00 61.85  ? 196  ASN K OD1   1 
ATOM   4908  N  ND2   . ASN B 2 196 ? 124.471 155.149 89.282  1.00 63.52  ? 196  ASN K ND2   1 
ATOM   4909  N  N     . MET B 2 197 ? 126.606 150.546 90.295  1.00 61.57  ? 197  MET K N     1 
ATOM   4910  C  CA    . MET B 2 197 ? 127.469 149.372 90.242  1.00 62.18  ? 197  MET K CA    1 
ATOM   4911  C  C     . MET B 2 197 ? 126.874 148.204 91.020  1.00 62.82  ? 197  MET K C     1 
ATOM   4912  O  O     . MET B 2 197 ? 126.876 147.066 90.536  1.00 68.29  ? 197  MET K O     1 
ATOM   4913  C  CB    . MET B 2 197 ? 128.860 149.717 90.767  1.00 63.25  ? 197  MET K CB    1 
ATOM   4914  C  CG    . MET B 2 197 ? 129.601 150.719 89.907  1.00 67.13  ? 197  MET K CG    1 
ATOM   4915  S  SD    . MET B 2 197 ? 131.386 150.505 89.959  1.00 81.21  ? 197  MET K SD    1 
ATOM   4916  C  CE    . MET B 2 197 ? 131.552 148.910 89.169  1.00 66.66  ? 197  MET K CE    1 
ATOM   4917  N  N     . ASN B 2 198 ? 126.362 148.461 92.220  1.00 58.74  ? 198  ASN K N     1 
ATOM   4918  C  CA    . ASN B 2 198 ? 125.829 147.415 93.083  1.00 55.39  ? 198  ASN K CA    1 
ATOM   4919  C  C     . ASN B 2 198 ? 124.470 147.842 93.612  1.00 60.45  ? 198  ASN K C     1 
ATOM   4920  O  O     . ASN B 2 198 ? 124.326 148.949 94.140  1.00 70.27  ? 198  ASN K O     1 
ATOM   4921  C  CB    . ASN B 2 198 ? 126.785 147.124 94.241  1.00 57.35  ? 198  ASN K CB    1 
ATOM   4922  C  CG    . ASN B 2 198 ? 126.333 145.959 95.089  1.00 65.49  ? 198  ASN K CG    1 
ATOM   4923  O  OD1   . ASN B 2 198 ? 125.394 145.247 94.738  1.00 69.63  ? 198  ASN K OD1   1 
ATOM   4924  N  ND2   . ASN B 2 198 ? 127.006 145.752 96.213  1.00 67.23  ? 198  ASN K ND2   1 
ATOM   4925  N  N     . GLU B 2 199 ? 123.479 146.961 93.475  1.00 61.82  ? 199  GLU K N     1 
ATOM   4926  C  CA    . GLU B 2 199 ? 122.127 147.284 93.912  1.00 64.58  ? 199  GLU K CA    1 
ATOM   4927  C  C     . GLU B 2 199 ? 121.972 147.209 95.425  1.00 67.65  ? 199  GLU K C     1 
ATOM   4928  O  O     . GLU B 2 199 ? 121.146 147.930 95.994  1.00 72.85  ? 199  GLU K O     1 
ATOM   4929  C  CB    . GLU B 2 199 ? 121.120 146.355 93.232  1.00 63.82  ? 199  GLU K CB    1 
ATOM   4930  C  CG    . GLU B 2 199 ? 121.463 144.876 93.326  1.00 69.49  ? 199  GLU K CG    1 
ATOM   4931  C  CD    . GLU B 2 199 ? 122.323 144.398 92.172  1.00 77.02  ? 199  GLU K CD    1 
ATOM   4932  O  OE1   . GLU B 2 199 ? 122.640 145.217 91.284  1.00 79.28  ? 199  GLU K OE1   1 
ATOM   4933  O  OE2   . GLU B 2 199 ? 122.681 143.201 92.152  1.00 73.20  ? 199  GLU K OE2   1 
ATOM   4934  N  N     . HIS B 2 200 ? 122.743 146.353 96.090  1.00 62.91  ? 200  HIS K N     1 
ATOM   4935  C  CA    . HIS B 2 200 ? 122.704 146.196 97.538  1.00 55.93  ? 200  HIS K CA    1 
ATOM   4936  C  C     . HIS B 2 200 ? 124.023 146.622 98.164  1.00 57.17  ? 200  HIS K C     1 
ATOM   4937  O  O     . HIS B 2 200 ? 124.572 145.937 99.027  1.00 63.42  ? 200  HIS K O     1 
ATOM   4938  C  CB    . HIS B 2 200 ? 122.376 144.758 97.929  1.00 59.21  ? 200  HIS K CB    1 
ATOM   4939  C  CG    . HIS B 2 200 ? 121.106 144.242 97.332  1.00 64.82  ? 200  HIS K CG    1 
ATOM   4940  N  ND1   . HIS B 2 200 ? 121.087 143.306 96.322  1.00 69.17  ? 200  HIS K ND1   1 
ATOM   4941  C  CD2   . HIS B 2 200 ? 119.812 144.529 97.604  1.00 65.59  ? 200  HIS K CD2   1 
ATOM   4942  C  CE1   . HIS B 2 200 ? 119.835 143.039 95.997  1.00 69.56  ? 200  HIS K CE1   1 
ATOM   4943  N  NE2   . HIS B 2 200 ? 119.042 143.768 96.760  1.00 71.66  ? 200  HIS K NE2   1 
ATOM   4944  N  N     . SER B 2 201 ? 124.552 147.759 97.721  1.00 53.73  ? 201  SER K N     1 
ATOM   4945  C  CA    . SER B 2 201 ? 125.852 148.214 98.192  1.00 56.61  ? 201  SER K CA    1 
ATOM   4946  C  C     . SER B 2 201 ? 125.821 148.497 99.686  1.00 57.71  ? 201  SER K C     1 
ATOM   4947  O  O     . SER B 2 201 ? 124.843 149.030 100.216 1.00 64.85  ? 201  SER K O     1 
ATOM   4948  C  CB    . SER B 2 201 ? 126.280 149.467 97.431  1.00 61.52  ? 201  SER K CB    1 
ATOM   4949  O  OG    . SER B 2 201 ? 127.532 149.937 97.895  1.00 64.60  ? 201  SER K OG    1 
ATOM   4950  N  N     . SER B 2 202 ? 126.905 148.138 100.364 1.00 53.35  ? 202  SER K N     1 
ATOM   4951  C  CA    . SER B 2 202 ? 127.043 148.372 101.792 1.00 49.27  ? 202  SER K CA    1 
ATOM   4952  C  C     . SER B 2 202 ? 127.794 149.675 102.021 1.00 46.09  ? 202  SER K C     1 
ATOM   4953  O  O     . SER B 2 202 ? 128.847 149.907 101.420 1.00 50.94  ? 202  SER K O     1 
ATOM   4954  C  CB    . SER B 2 202 ? 127.772 147.209 102.460 1.00 50.91  ? 202  SER K CB    1 
ATOM   4955  O  OG    . SER B 2 202 ? 129.003 146.942 101.818 1.00 53.22  ? 202  SER K OG    1 
ATOM   4956  N  N     . ARG B 2 203 ? 127.244 150.527 102.885 1.00 45.74  ? 203  ARG K N     1 
ATOM   4957  C  CA    . ARG B 2 203 ? 127.794 151.852 103.137 1.00 45.52  ? 203  ARG K CA    1 
ATOM   4958  C  C     . ARG B 2 203 ? 128.407 151.970 104.526 1.00 48.96  ? 203  ARG K C     1 
ATOM   4959  O  O     . ARG B 2 203 ? 128.536 153.079 105.051 1.00 49.30  ? 203  ARG K O     1 
ATOM   4960  C  CB    . ARG B 2 203 ? 126.716 152.917 102.941 1.00 40.96  ? 203  ARG K CB    1 
ATOM   4961  C  CG    . ARG B 2 203 ? 125.753 152.629 101.807 1.00 48.60  ? 203  ARG K CG    1 
ATOM   4962  C  CD    . ARG B 2 203 ? 126.475 152.536 100.478 1.00 44.00  ? 203  ARG K CD    1 
ATOM   4963  N  NE    . ARG B 2 203 ? 126.945 153.835 100.018 1.00 42.08  ? 203  ARG K NE    1 
ATOM   4964  C  CZ    . ARG B 2 203 ? 127.602 154.030 98.884  1.00 48.14  ? 203  ARG K CZ    1 
ATOM   4965  N  NH1   . ARG B 2 203 ? 127.895 153.027 98.076  1.00 52.97  ? 203  ARG K NH1   1 
ATOM   4966  N  NH2   . ARG B 2 203 ? 127.972 155.263 98.553  1.00 53.09  ? 203  ARG K NH2   1 
ATOM   4967  N  N     . SER B 2 204 ? 128.791 150.851 105.130 1.00 50.92  ? 204  SER K N     1 
ATOM   4968  C  CA    . SER B 2 204 ? 129.369 150.853 106.461 1.00 44.53  ? 204  SER K CA    1 
ATOM   4969  C  C     . SER B 2 204 ? 130.492 149.831 106.525 1.00 51.29  ? 204  SER K C     1 
ATOM   4970  O  O     . SER B 2 204 ? 130.558 148.897 105.723 1.00 58.60  ? 204  SER K O     1 
ATOM   4971  C  CB    . SER B 2 204 ? 128.316 150.548 107.530 1.00 53.87  ? 204  SER K CB    1 
ATOM   4972  O  OG    . SER B 2 204 ? 127.263 151.494 107.492 1.00 60.63  ? 204  SER K OG    1 
ATOM   4973  N  N     . HIS B 2 205 ? 131.381 150.024 107.496 1.00 48.68  ? 205  HIS K N     1 
ATOM   4974  C  CA    . HIS B 2 205 ? 132.476 149.093 107.753 1.00 53.19  ? 205  HIS K CA    1 
ATOM   4975  C  C     . HIS B 2 205 ? 132.064 148.193 108.915 1.00 54.44  ? 205  HIS K C     1 
ATOM   4976  O  O     . HIS B 2 205 ? 132.383 148.444 110.077 1.00 65.85  ? 205  HIS K O     1 
ATOM   4977  C  CB    . HIS B 2 205 ? 133.765 149.843 108.062 1.00 54.07  ? 205  HIS K CB    1 
ATOM   4978  C  CG    . HIS B 2 205 ? 134.271 150.687 106.936 1.00 48.04  ? 205  HIS K CG    1 
ATOM   4979  N  ND1   . HIS B 2 205 ? 133.590 150.835 105.748 1.00 59.04  ? 205  HIS K ND1   1 
ATOM   4980  C  CD2   . HIS B 2 205 ? 135.396 151.429 106.820 1.00 48.13  ? 205  HIS K CD2   1 
ATOM   4981  C  CE1   . HIS B 2 205 ? 134.275 151.633 104.949 1.00 61.00  ? 205  HIS K CE1   1 
ATOM   4982  N  NE2   . HIS B 2 205 ? 135.375 152.007 105.575 1.00 51.31  ? 205  HIS K NE2   1 
ATOM   4983  N  N     . SER B 2 206 ? 131.340 147.128 108.589 1.00 47.75  ? 206  SER K N     1 
ATOM   4984  C  CA    . SER B 2 206 ? 130.856 146.220 109.619 1.00 50.75  ? 206  SER K CA    1 
ATOM   4985  C  C     . SER B 2 206 ? 132.010 145.453 110.250 1.00 49.86  ? 206  SER K C     1 
ATOM   4986  O  O     . SER B 2 206 ? 132.912 144.974 109.558 1.00 55.44  ? 206  SER K O     1 
ATOM   4987  C  CB    . SER B 2 206 ? 129.836 145.245 109.035 1.00 54.92  ? 206  SER K CB    1 
ATOM   4988  O  OG    . SER B 2 206 ? 130.406 144.471 107.996 1.00 64.05  ? 206  SER K OG    1 
ATOM   4989  N  N     . ILE B 2 207 ? 131.974 145.337 111.574 1.00 49.38  ? 207  ILE K N     1 
ATOM   4990  C  CA    . ILE B 2 207 ? 132.983 144.618 112.342 1.00 49.34  ? 207  ILE K CA    1 
ATOM   4991  C  C     . ILE B 2 207 ? 132.283 143.569 113.191 1.00 55.91  ? 207  ILE K C     1 
ATOM   4992  O  O     . ILE B 2 207 ? 131.344 143.886 113.929 1.00 62.44  ? 207  ILE K O     1 
ATOM   4993  C  CB    . ILE B 2 207 ? 133.809 145.565 113.228 1.00 49.30  ? 207  ILE K CB    1 
ATOM   4994  C  CG1   . ILE B 2 207 ? 134.650 146.506 112.370 1.00 50.13  ? 207  ILE K CG1   1 
ATOM   4995  C  CG2   . ILE B 2 207 ? 134.695 144.769 114.160 1.00 56.81  ? 207  ILE K CG2   1 
ATOM   4996  C  CD1   . ILE B 2 207 ? 135.693 147.267 113.153 1.00 55.48  ? 207  ILE K CD1   1 
ATOM   4997  N  N     . PHE B 2 208 ? 132.741 142.327 113.088 1.00 55.10  ? 208  PHE K N     1 
ATOM   4998  C  CA    . PHE B 2 208 ? 132.230 141.218 113.881 1.00 48.41  ? 208  PHE K CA    1 
ATOM   4999  C  C     . PHE B 2 208 ? 133.331 140.765 114.830 1.00 54.38  ? 208  PHE K C     1 
ATOM   5000  O  O     . PHE B 2 208 ? 134.429 140.415 114.386 1.00 63.24  ? 208  PHE K O     1 
ATOM   5001  C  CB    . PHE B 2 208 ? 131.777 140.071 112.979 1.00 52.33  ? 208  PHE K CB    1 
ATOM   5002  C  CG    . PHE B 2 208 ? 131.136 138.934 113.715 1.00 53.85  ? 208  PHE K CG    1 
ATOM   5003  C  CD1   . PHE B 2 208 ? 129.870 139.065 114.252 1.00 53.17  ? 208  PHE K CD1   1 
ATOM   5004  C  CD2   . PHE B 2 208 ? 131.793 137.729 113.856 1.00 58.71  ? 208  PHE K CD2   1 
ATOM   5005  C  CE1   . PHE B 2 208 ? 129.278 138.024 114.919 1.00 52.34  ? 208  PHE K CE1   1 
ATOM   5006  C  CE2   . PHE B 2 208 ? 131.203 136.682 114.524 1.00 60.33  ? 208  PHE K CE2   1 
ATOM   5007  C  CZ    . PHE B 2 208 ? 129.943 136.832 115.058 1.00 57.21  ? 208  PHE K CZ    1 
ATOM   5008  N  N     . LEU B 2 209 ? 133.037 140.772 116.126 1.00 53.76  ? 209  LEU K N     1 
ATOM   5009  C  CA    . LEU B 2 209 ? 134.011 140.461 117.162 1.00 46.85  ? 209  LEU K CA    1 
ATOM   5010  C  C     . LEU B 2 209 ? 133.524 139.274 117.978 1.00 53.99  ? 209  LEU K C     1 
ATOM   5011  O  O     . LEU B 2 209 ? 132.383 139.270 118.448 1.00 65.60  ? 209  LEU K O     1 
ATOM   5012  C  CB    . LEU B 2 209 ? 134.229 141.671 118.073 1.00 45.65  ? 209  LEU K CB    1 
ATOM   5013  C  CG    . LEU B 2 209 ? 135.574 141.873 118.768 1.00 49.87  ? 209  LEU K CG    1 
ATOM   5014  C  CD1   . LEU B 2 209 ? 135.609 143.249 119.410 1.00 55.89  ? 209  LEU K CD1   1 
ATOM   5015  C  CD2   . LEU B 2 209 ? 135.832 140.801 119.805 1.00 50.82  ? 209  LEU K CD2   1 
ATOM   5016  N  N     . ILE B 2 210 ? 134.384 138.271 118.145 1.00 51.40  ? 210  ILE K N     1 
ATOM   5017  C  CA    . ILE B 2 210 ? 134.134 137.179 119.078 1.00 54.20  ? 210  ILE K CA    1 
ATOM   5018  C  C     . ILE B 2 210 ? 135.362 136.997 119.960 1.00 51.91  ? 210  ILE K C     1 
ATOM   5019  O  O     . ILE B 2 210 ? 136.486 136.883 119.458 1.00 58.62  ? 210  ILE K O     1 
ATOM   5020  C  CB    . ILE B 2 210 ? 133.765 135.863 118.363 1.00 46.05  ? 210  ILE K CB    1 
ATOM   5021  C  CG1   . ILE B 2 210 ? 134.817 135.453 117.341 1.00 52.26  ? 210  ILE K CG1   1 
ATOM   5022  C  CG2   . ILE B 2 210 ? 132.427 135.990 117.677 1.00 52.91  ? 210  ILE K CG2   1 
ATOM   5023  C  CD1   . ILE B 2 210 ? 134.543 134.104 116.725 1.00 58.24  ? 210  ILE K CD1   1 
ATOM   5024  N  N     . ASN B 2 211 ? 135.146 136.995 121.272 1.00 51.65  ? 211  ASN K N     1 
ATOM   5025  C  CA    . ASN B 2 211 ? 136.186 136.722 122.253 1.00 50.02  ? 211  ASN K CA    1 
ATOM   5026  C  C     . ASN B 2 211 ? 135.996 135.310 122.780 1.00 55.66  ? 211  ASN K C     1 
ATOM   5027  O  O     . ASN B 2 211 ? 134.895 134.948 123.205 1.00 65.25  ? 211  ASN K O     1 
ATOM   5028  C  CB    . ASN B 2 211 ? 136.132 137.713 123.417 1.00 51.62  ? 211  ASN K CB    1 
ATOM   5029  C  CG    . ASN B 2 211 ? 136.368 139.136 122.984 1.00 58.01  ? 211  ASN K CG    1 
ATOM   5030  O  OD1   . ASN B 2 211 ? 137.342 139.433 122.296 1.00 61.35  ? 211  ASN K OD1   1 
ATOM   5031  N  ND2   . ASN B 2 211 ? 135.475 140.032 123.387 1.00 58.95  ? 211  ASN K ND2   1 
ATOM   5032  N  N     . VAL B 2 212 ? 137.059 134.519 122.755 1.00 49.84  ? 212  VAL K N     1 
ATOM   5033  C  CA    . VAL B 2 212 ? 137.035 133.169 123.297 1.00 50.79  ? 212  VAL K CA    1 
ATOM   5034  C  C     . VAL B 2 212 ? 137.951 133.148 124.511 1.00 55.41  ? 212  VAL K C     1 
ATOM   5035  O  O     . VAL B 2 212 ? 139.179 133.208 124.378 1.00 60.18  ? 212  VAL K O     1 
ATOM   5036  C  CB    . VAL B 2 212 ? 137.458 132.126 122.258 1.00 48.51  ? 212  VAL K CB    1 
ATOM   5037  C  CG1   . VAL B 2 212 ? 137.545 130.757 122.901 1.00 52.08  ? 212  VAL K CG1   1 
ATOM   5038  C  CG2   . VAL B 2 212 ? 136.472 132.112 121.108 1.00 50.80  ? 212  VAL K CG2   1 
ATOM   5039  N  N     . LYS B 2 213 ? 137.355 133.065 125.695 1.00 55.51  ? 213  LYS K N     1 
ATOM   5040  C  CA    . LYS B 2 213 ? 138.097 132.939 126.940 1.00 53.55  ? 213  LYS K CA    1 
ATOM   5041  C  C     . LYS B 2 213 ? 138.095 131.474 127.350 1.00 55.98  ? 213  LYS K C     1 
ATOM   5042  O  O     . LYS B 2 213 ? 137.031 130.861 127.476 1.00 62.35  ? 213  LYS K O     1 
ATOM   5043  C  CB    . LYS B 2 213 ? 137.489 133.812 128.035 1.00 58.43  ? 213  LYS K CB    1 
ATOM   5044  C  CG    . LYS B 2 213 ? 137.162 135.224 127.589 1.00 59.84  ? 213  LYS K CG    1 
ATOM   5045  C  CD    . LYS B 2 213 ? 137.164 136.184 128.763 1.00 64.39  ? 213  LYS K CD    1 
ATOM   5046  C  CE    . LYS B 2 213 ? 138.578 136.468 129.236 1.00 64.78  ? 213  LYS K CE    1 
ATOM   5047  N  NZ    . LYS B 2 213 ? 139.405 137.081 128.161 1.00 63.82  ? 213  LYS K NZ    1 
ATOM   5048  N  N     . GLN B 2 214 ? 139.283 130.920 127.556 1.00 59.07  ? 214  GLN K N     1 
ATOM   5049  C  CA    . GLN B 2 214 ? 139.466 129.498 127.793 1.00 56.10  ? 214  GLN K CA    1 
ATOM   5050  C  C     . GLN B 2 214 ? 140.162 129.294 129.128 1.00 64.34  ? 214  GLN K C     1 
ATOM   5051  O  O     . GLN B 2 214 ? 141.239 129.852 129.363 1.00 75.51  ? 214  GLN K O     1 
ATOM   5052  C  CB    . GLN B 2 214 ? 140.278 128.873 126.661 1.00 54.23  ? 214  GLN K CB    1 
ATOM   5053  C  CG    . GLN B 2 214 ? 140.919 127.553 126.995 1.00 60.66  ? 214  GLN K CG    1 
ATOM   5054  C  CD    . GLN B 2 214 ? 141.820 127.070 125.884 1.00 66.68  ? 214  GLN K CD    1 
ATOM   5055  O  OE1   . GLN B 2 214 ? 141.791 127.602 124.778 1.00 64.51  ? 214  GLN K OE1   1 
ATOM   5056  N  NE2   . GLN B 2 214 ? 142.630 126.059 126.172 1.00 68.85  ? 214  GLN K NE2   1 
ATOM   5057  N  N     . GLU B 2 215 ? 139.550 128.493 129.996 1.00 73.49  ? 215  GLU K N     1 
ATOM   5058  C  CA    . GLU B 2 215 ? 140.079 128.227 131.324 1.00 72.93  ? 215  GLU K CA    1 
ATOM   5059  C  C     . GLU B 2 215 ? 140.183 126.726 131.535 1.00 74.89  ? 215  GLU K C     1 
ATOM   5060  O  O     . GLU B 2 215 ? 139.225 125.992 131.274 1.00 82.51  ? 215  GLU K O     1 
ATOM   5061  C  CB    . GLU B 2 215 ? 139.194 128.852 132.404 1.00 75.13  ? 215  GLU K CB    1 
ATOM   5062  C  CG    . GLU B 2 215 ? 139.711 128.655 133.817 1.00 79.15  ? 215  GLU K CG    1 
ATOM   5063  C  CD    . GLU B 2 215 ? 138.914 129.435 134.843 1.00 81.49  ? 215  GLU K CD    1 
ATOM   5064  O  OE1   . GLU B 2 215 ? 138.122 130.312 134.440 1.00 84.63  ? 215  GLU K OE1   1 
ATOM   5065  O  OE2   . GLU B 2 215 ? 139.081 129.170 136.052 1.00 79.68  ? 215  GLU K OE2   1 
ATOM   5066  N  N     . ASN B 2 216 ? 141.340 126.275 132.006 1.00 70.34  ? 216  ASN K N     1 
ATOM   5067  C  CA    . ASN B 2 216 ? 141.559 124.878 132.351 1.00 68.66  ? 216  ASN K CA    1 
ATOM   5068  C  C     . ASN B 2 216 ? 141.412 124.718 133.856 1.00 73.28  ? 216  ASN K C     1 
ATOM   5069  O  O     . ASN B 2 216 ? 141.977 125.500 134.624 1.00 80.17  ? 216  ASN K O     1 
ATOM   5070  C  CB    . ASN B 2 216 ? 142.941 124.409 131.899 1.00 68.41  ? 216  ASN K CB    1 
ATOM   5071  C  CG    . ASN B 2 216 ? 143.061 122.901 131.859 1.00 73.84  ? 216  ASN K CG    1 
ATOM   5072  O  OD1   . ASN B 2 216 ? 142.346 122.190 132.562 1.00 79.04  ? 216  ASN K OD1   1 
ATOM   5073  N  ND2   . ASN B 2 216 ? 143.972 122.403 131.033 1.00 73.99  ? 216  ASN K ND2   1 
ATOM   5074  N  N     . THR B 2 217 ? 140.640 123.716 134.276 1.00 73.97  ? 217  THR K N     1 
ATOM   5075  C  CA    . THR B 2 217 ? 140.395 123.540 135.703 1.00 75.11  ? 217  THR K CA    1 
ATOM   5076  C  C     . THR B 2 217 ? 141.599 122.921 136.404 1.00 77.96  ? 217  THR K C     1 
ATOM   5077  O  O     . THR B 2 217 ? 141.929 123.302 137.532 1.00 80.06  ? 217  THR K O     1 
ATOM   5078  C  CB    . THR B 2 217 ? 139.143 122.691 135.917 1.00 79.13  ? 217  THR K CB    1 
ATOM   5079  O  OG1   . THR B 2 217 ? 138.019 123.342 135.312 1.00 76.95  ? 217  THR K OG1   1 
ATOM   5080  C  CG2   . THR B 2 217 ? 138.867 122.504 137.402 1.00 78.50  ? 217  THR K CG2   1 
ATOM   5081  N  N     . GLN B 2 218 ? 142.278 121.980 135.747 1.00 84.29  ? 218  GLN K N     1 
ATOM   5082  C  CA    . GLN B 2 218 ? 143.363 121.260 136.406 1.00 84.66  ? 218  GLN K CA    1 
ATOM   5083  C  C     . GLN B 2 218 ? 144.620 122.117 136.510 1.00 84.72  ? 218  GLN K C     1 
ATOM   5084  O  O     . GLN B 2 218 ? 145.108 122.385 137.615 1.00 89.44  ? 218  GLN K O     1 
ATOM   5085  C  CB    . GLN B 2 218 ? 143.657 119.961 135.659 1.00 83.98  ? 218  GLN K CB    1 
ATOM   5086  C  CG    . GLN B 2 218 ? 142.536 118.942 135.747 1.00 88.30  ? 218  GLN K CG    1 
ATOM   5087  C  CD    . GLN B 2 218 ? 142.262 118.506 137.171 1.00 87.99  ? 218  GLN K CD    1 
ATOM   5088  O  OE1   . GLN B 2 218 ? 141.132 118.590 137.650 1.00 85.80  ? 218  GLN K OE1   1 
ATOM   5089  N  NE2   . GLN B 2 218 ? 143.298 118.036 137.857 1.00 86.43  ? 218  GLN K NE2   1 
ATOM   5090  N  N     . THR B 2 219 ? 145.161 122.557 135.374 1.00 82.82  ? 219  THR K N     1 
ATOM   5091  C  CA    . THR B 2 219 ? 146.391 123.339 135.369 1.00 84.11  ? 219  THR K CA    1 
ATOM   5092  C  C     . THR B 2 219 ? 146.156 124.823 135.604 1.00 83.47  ? 219  THR K C     1 
ATOM   5093  O  O     . THR B 2 219 ? 147.129 125.575 135.717 1.00 81.61  ? 219  THR K O     1 
ATOM   5094  C  CB    . THR B 2 219 ? 147.142 123.155 134.045 1.00 83.93  ? 219  THR K CB    1 
ATOM   5095  O  OG1   . THR B 2 219 ? 148.426 123.783 134.133 1.00 82.29  ? 219  THR K OG1   1 
ATOM   5096  C  CG2   . THR B 2 219 ? 146.368 123.785 132.906 1.00 84.97  ? 219  THR K CG2   1 
ATOM   5097  N  N     . GLU B 2 220 ? 144.897 125.259 135.639 1.00 91.59  ? 220  GLU K N     1 
ATOM   5098  C  CA    . GLU B 2 220 ? 144.501 126.626 135.967 1.00 92.13  ? 220  GLU K CA    1 
ATOM   5099  C  C     . GLU B 2 220 ? 144.937 127.630 134.906 1.00 95.26  ? 220  GLU K C     1 
ATOM   5100  O  O     . GLU B 2 220 ? 144.532 128.795 134.956 1.00 97.63  ? 220  GLU K O     1 
ATOM   5101  C  CB    . GLU B 2 220 ? 145.046 127.032 137.338 1.00 91.30  ? 220  GLU K CB    1 
ATOM   5102  C  CG    . GLU B 2 220 ? 144.208 128.079 138.054 1.00 95.82  ? 220  GLU K CG    1 
ATOM   5103  C  CD    . GLU B 2 220 ? 142.734 127.728 138.097 1.00 97.45  ? 220  GLU K CD    1 
ATOM   5104  O  OE1   . GLU B 2 220 ? 142.403 126.564 138.408 1.00 97.32  ? 220  GLU K OE1   1 
ATOM   5105  O  OE2   . GLU B 2 220 ? 141.904 128.618 137.816 1.00 94.76  ? 220  GLU K OE2   1 
ATOM   5106  N  N     . GLN B 2 221 ? 145.710 127.184 133.918 1.00 90.41  ? 221  GLN K N     1 
ATOM   5107  C  CA    . GLN B 2 221 ? 146.222 128.089 132.898 1.00 87.56  ? 221  GLN K CA    1 
ATOM   5108  C  C     . GLN B 2 221 ? 145.075 128.639 132.060 1.00 88.34  ? 221  GLN K C     1 
ATOM   5109  O  O     . GLN B 2 221 ? 144.177 127.896 131.655 1.00 91.24  ? 221  GLN K O     1 
ATOM   5110  C  CB    . GLN B 2 221 ? 147.233 127.368 132.012 1.00 86.28  ? 221  GLN K CB    1 
ATOM   5111  C  CG    . GLN B 2 221 ? 147.953 128.268 131.027 1.00 90.73  ? 221  GLN K CG    1 
ATOM   5112  C  CD    . GLN B 2 221 ? 149.072 127.553 130.300 1.00 94.24  ? 221  GLN K CD    1 
ATOM   5113  O  OE1   . GLN B 2 221 ? 149.326 126.373 130.537 1.00 93.32  ? 221  GLN K OE1   1 
ATOM   5114  N  NE2   . GLN B 2 221 ? 149.751 128.267 129.410 1.00 92.30  ? 221  GLN K NE2   1 
ATOM   5115  N  N     . LYS B 2 222 ? 145.107 129.941 131.800 1.00 75.19  ? 222  LYS K N     1 
ATOM   5116  C  CA    . LYS B 2 222 ? 144.019 130.635 131.130 1.00 71.89  ? 222  LYS K CA    1 
ATOM   5117  C  C     . LYS B 2 222 ? 144.521 131.288 129.851 1.00 78.25  ? 222  LYS K C     1 
ATOM   5118  O  O     . LYS B 2 222 ? 145.614 131.861 129.822 1.00 83.63  ? 222  LYS K O     1 
ATOM   5119  C  CB    . LYS B 2 222 ? 143.401 131.690 132.047 1.00 68.28  ? 222  LYS K CB    1 
ATOM   5120  C  CG    . LYS B 2 222 ? 142.093 132.254 131.547 1.00 72.74  ? 222  LYS K CG    1 
ATOM   5121  C  CD    . LYS B 2 222 ? 141.655 133.434 132.391 1.00 78.30  ? 222  LYS K CD    1 
ATOM   5122  C  CE    . LYS B 2 222 ? 141.660 133.085 133.867 1.00 76.74  ? 222  LYS K CE    1 
ATOM   5123  N  NZ    . LYS B 2 222 ? 140.770 131.932 134.167 1.00 75.59  ? 222  LYS K NZ    1 
ATOM   5124  N  N     . LEU B 2 223 ? 143.714 131.195 128.796 1.00 67.08  ? 223  LEU K N     1 
ATOM   5125  C  CA    . LEU B 2 223 ? 144.035 131.773 127.502 1.00 54.02  ? 223  LEU K CA    1 
ATOM   5126  C  C     . LEU B 2 223 ? 142.844 132.566 126.991 1.00 55.97  ? 223  LEU K C     1 
ATOM   5127  O  O     . LEU B 2 223 ? 141.690 132.236 127.274 1.00 66.29  ? 223  LEU K O     1 
ATOM   5128  C  CB    . LEU B 2 223 ? 144.407 130.697 126.485 1.00 53.60  ? 223  LEU K CB    1 
ATOM   5129  C  CG    . LEU B 2 223 ? 145.588 129.800 126.838 1.00 62.43  ? 223  LEU K CG    1 
ATOM   5130  C  CD1   . LEU B 2 223 ? 145.660 128.619 125.891 1.00 63.72  ? 223  LEU K CD1   1 
ATOM   5131  C  CD2   . LEU B 2 223 ? 146.877 130.591 126.802 1.00 67.18  ? 223  LEU K CD2   1 
ATOM   5132  N  N     . SER B 2 224 ? 143.133 133.619 126.235 1.00 54.22  ? 224  SER K N     1 
ATOM   5133  C  CA    . SER B 2 224 ? 142.105 134.444 125.624 1.00 58.92  ? 224  SER K CA    1 
ATOM   5134  C  C     . SER B 2 224 ? 142.458 134.696 124.167 1.00 59.51  ? 224  SER K C     1 
ATOM   5135  O  O     . SER B 2 224 ? 143.628 134.849 123.812 1.00 69.98  ? 224  SER K O     1 
ATOM   5136  C  CB    . SER B 2 224 ? 141.940 135.778 126.358 1.00 61.00  ? 224  SER K CB    1 
ATOM   5137  O  OG    . SER B 2 224 ? 140.964 136.589 125.728 1.00 65.08  ? 224  SER K OG    1 
ATOM   5138  N  N     . GLY B 2 225 ? 141.431 134.743 123.326 1.00 50.66  ? 225  GLY K N     1 
ATOM   5139  C  CA    . GLY B 2 225 ? 141.630 134.968 121.910 1.00 48.60  ? 225  GLY K CA    1 
ATOM   5140  C  C     . GLY B 2 225 ? 140.573 135.868 121.310 1.00 49.85  ? 225  GLY K C     1 
ATOM   5141  O  O     . GLY B 2 225 ? 139.376 135.677 121.543 1.00 59.76  ? 225  GLY K O     1 
ATOM   5142  N  N     . LYS B 2 226 ? 141.004 136.854 120.533 1.00 47.04  ? 226  LYS K N     1 
ATOM   5143  C  CA    . LYS B 2 226 ? 140.119 137.840 119.935 1.00 44.93  ? 226  LYS K CA    1 
ATOM   5144  C  C     . LYS B 2 226 ? 140.109 137.639 118.430 1.00 53.71  ? 226  LYS K C     1 
ATOM   5145  O  O     . LYS B 2 226 ? 141.170 137.600 117.800 1.00 67.93  ? 226  LYS K O     1 
ATOM   5146  C  CB    . LYS B 2 226 ? 140.576 139.256 120.287 1.00 47.88  ? 226  LYS K CB    1 
ATOM   5147  C  CG    . LYS B 2 226 ? 139.499 140.311 120.214 1.00 52.63  ? 226  LYS K CG    1 
ATOM   5148  C  CD    . LYS B 2 226 ? 139.875 141.506 121.073 1.00 59.47  ? 226  LYS K CD    1 
ATOM   5149  C  CE    . LYS B 2 226 ? 138.732 142.497 121.186 1.00 59.29  ? 226  LYS K CE    1 
ATOM   5150  N  NZ    . LYS B 2 226 ? 139.046 143.599 122.135 1.00 56.81  ? 226  LYS K NZ    1 
ATOM   5151  N  N     . LEU B 2 227 ? 138.917 137.510 117.856 1.00 44.64  ? 227  LEU K N     1 
ATOM   5152  C  CA    . LEU B 2 227 ? 138.761 137.273 116.428 1.00 40.83  ? 227  LEU K CA    1 
ATOM   5153  C  C     . LEU B 2 227 ? 137.938 138.402 115.830 1.00 47.81  ? 227  LEU K C     1 
ATOM   5154  O  O     . LEU B 2 227 ? 136.796 138.628 116.241 1.00 59.60  ? 227  LEU K O     1 
ATOM   5155  C  CB    . LEU B 2 227 ? 138.106 135.916 116.167 1.00 38.04  ? 227  LEU K CB    1 
ATOM   5156  C  CG    . LEU B 2 227 ? 138.026 135.425 114.724 1.00 44.24  ? 227  LEU K CG    1 
ATOM   5157  C  CD1   . LEU B 2 227 ? 139.373 135.527 114.049 1.00 50.91  ? 227  LEU K CD1   1 
ATOM   5158  C  CD2   . LEU B 2 227 ? 137.529 133.997 114.683 1.00 48.31  ? 227  LEU K CD2   1 
ATOM   5159  N  N     . TYR B 2 228 ? 138.521 139.105 114.866 1.00 49.21  ? 228  TYR K N     1 
ATOM   5160  C  CA    . TYR B 2 228 ? 137.866 140.199 114.165 1.00 45.34  ? 228  TYR K CA    1 
ATOM   5161  C  C     . TYR B 2 228 ? 137.505 139.742 112.761 1.00 49.97  ? 228  TYR K C     1 
ATOM   5162  O  O     . TYR B 2 228 ? 138.330 139.137 112.070 1.00 55.24  ? 228  TYR K O     1 
ATOM   5163  C  CB    . TYR B 2 228 ? 138.776 141.425 114.092 1.00 49.59  ? 228  TYR K CB    1 
ATOM   5164  C  CG    . TYR B 2 228 ? 138.649 142.389 115.243 1.00 53.01  ? 228  TYR K CG    1 
ATOM   5165  C  CD1   . TYR B 2 228 ? 137.504 143.147 115.415 1.00 58.71  ? 228  TYR K CD1   1 
ATOM   5166  C  CD2   . TYR B 2 228 ? 139.687 142.560 116.145 1.00 50.12  ? 228  TYR K CD2   1 
ATOM   5167  C  CE1   . TYR B 2 228 ? 137.390 144.038 116.459 1.00 57.63  ? 228  TYR K CE1   1 
ATOM   5168  C  CE2   . TYR B 2 228 ? 139.582 143.445 117.192 1.00 51.84  ? 228  TYR K CE2   1 
ATOM   5169  C  CZ    . TYR B 2 228 ? 138.430 144.182 117.345 1.00 56.41  ? 228  TYR K CZ    1 
ATOM   5170  O  OH    . TYR B 2 228 ? 138.316 145.070 118.388 1.00 53.51  ? 228  TYR K OH    1 
ATOM   5171  N  N     . LEU B 2 229 ? 136.279 140.033 112.341 1.00 50.20  ? 229  LEU K N     1 
ATOM   5172  C  CA    . LEU B 2 229 ? 135.807 139.712 110.997 1.00 53.37  ? 229  LEU K CA    1 
ATOM   5173  C  C     . LEU B 2 229 ? 135.174 140.978 110.427 1.00 59.08  ? 229  LEU K C     1 
ATOM   5174  O  O     . LEU B 2 229 ? 134.021 141.294 110.732 1.00 66.85  ? 229  LEU K O     1 
ATOM   5175  C  CB    . LEU B 2 229 ? 134.824 138.548 111.023 1.00 57.86  ? 229  LEU K CB    1 
ATOM   5176  C  CG    . LEU B 2 229 ? 135.347 137.263 111.668 1.00 57.49  ? 229  LEU K CG    1 
ATOM   5177  C  CD1   . LEU B 2 229 ? 134.254 136.216 111.749 1.00 57.35  ? 229  LEU K CD1   1 
ATOM   5178  C  CD2   . LEU B 2 229 ? 136.541 136.728 110.904 1.00 59.71  ? 229  LEU K CD2   1 
ATOM   5179  N  N     . VAL B 2 230 ? 135.927 141.697 109.598 1.00 51.52  ? 230  VAL K N     1 
ATOM   5180  C  CA    . VAL B 2 230 ? 135.543 143.019 109.119 1.00 49.26  ? 230  VAL K CA    1 
ATOM   5181  C  C     . VAL B 2 230 ? 135.180 142.935 107.644 1.00 53.78  ? 230  VAL K C     1 
ATOM   5182  O  O     . VAL B 2 230 ? 135.881 142.293 106.855 1.00 61.68  ? 230  VAL K O     1 
ATOM   5183  C  CB    . VAL B 2 230 ? 136.668 144.046 109.346 1.00 53.51  ? 230  VAL K CB    1 
ATOM   5184  C  CG1   . VAL B 2 230 ? 136.137 145.460 109.194 1.00 55.88  ? 230  VAL K CG1   1 
ATOM   5185  C  CG2   . VAL B 2 230 ? 137.300 143.851 110.711 1.00 55.54  ? 230  VAL K CG2   1 
ATOM   5186  N  N     . ASP B 2 231 ? 134.078 143.582 107.276 1.00 56.56  ? 231  ASP K N     1 
ATOM   5187  C  CA    . ASP B 2 231 ? 133.599 143.647 105.897 1.00 52.67  ? 231  ASP K CA    1 
ATOM   5188  C  C     . ASP B 2 231 ? 133.614 145.113 105.475 1.00 54.92  ? 231  ASP K C     1 
ATOM   5189  O  O     . ASP B 2 231 ? 132.626 145.831 105.641 1.00 59.31  ? 231  ASP K O     1 
ATOM   5190  C  CB    . ASP B 2 231 ? 132.208 143.038 105.771 1.00 54.73  ? 231  ASP K CB    1 
ATOM   5191  C  CG    . ASP B 2 231 ? 131.692 143.051 104.350 1.00 66.83  ? 231  ASP K CG    1 
ATOM   5192  O  OD1   . ASP B 2 231 ? 132.508 143.203 103.418 1.00 72.44  ? 231  ASP K OD1   1 
ATOM   5193  O  OD2   . ASP B 2 231 ? 130.466 142.912 104.163 1.00 69.38  ? 231  ASP K OD2   1 
ATOM   5194  N  N     . LEU B 2 232 ? 134.741 145.550 104.926 1.00 50.70  ? 232  LEU K N     1 
ATOM   5195  C  CA    . LEU B 2 232 ? 134.925 146.947 104.571 1.00 52.41  ? 232  LEU K CA    1 
ATOM   5196  C  C     . LEU B 2 232 ? 134.066 147.326 103.370 1.00 61.60  ? 232  LEU K C     1 
ATOM   5197  O  O     . LEU B 2 232 ? 133.621 146.478 102.592 1.00 68.32  ? 232  LEU K O     1 
ATOM   5198  C  CB    . LEU B 2 232 ? 136.393 147.233 104.257 1.00 53.49  ? 232  LEU K CB    1 
ATOM   5199  C  CG    . LEU B 2 232 ? 137.376 147.327 105.421 1.00 57.92  ? 232  LEU K CG    1 
ATOM   5200  C  CD1   . LEU B 2 232 ? 137.733 145.957 105.942 1.00 58.60  ? 232  LEU K CD1   1 
ATOM   5201  C  CD2   . LEU B 2 232 ? 138.621 148.053 104.980 1.00 54.03  ? 232  LEU K CD2   1 
ATOM   5202  N  N     . ALA B 2 233 ? 133.824 148.624 103.235 1.00 58.21  ? 233  ALA K N     1 
ATOM   5203  C  CA    . ALA B 2 233 ? 133.206 149.168 102.039 1.00 52.14  ? 233  ALA K CA    1 
ATOM   5204  C  C     . ALA B 2 233 ? 134.274 149.434 100.985 1.00 56.16  ? 233  ALA K C     1 
ATOM   5205  O  O     . ALA B 2 233 ? 135.468 149.510 101.281 1.00 60.39  ? 233  ALA K O     1 
ATOM   5206  C  CB    . ALA B 2 233 ? 132.436 150.448 102.354 1.00 47.84  ? 233  ALA K CB    1 
ATOM   5207  N  N     . GLY B 2 234 ? 133.831 149.564 99.740  1.00 53.04  ? 234  GLY K N     1 
ATOM   5208  C  CA    . GLY B 2 234 ? 134.733 149.685 98.620  1.00 52.61  ? 234  GLY K CA    1 
ATOM   5209  C  C     . GLY B 2 234 ? 134.919 151.110 98.143  1.00 54.21  ? 234  GLY K C     1 
ATOM   5210  O  O     . GLY B 2 234 ? 134.080 151.978 98.365  1.00 58.48  ? 234  GLY K O     1 
ATOM   5211  N  N     . SER B 2 235 ? 136.049 151.339 97.481  1.00 50.75  ? 235  SER K N     1 
ATOM   5212  C  CA    . SER B 2 235 ? 136.312 152.632 96.872  1.00 55.56  ? 235  SER K CA    1 
ATOM   5213  C  C     . SER B 2 235 ? 135.353 152.867 95.715  1.00 55.53  ? 235  SER K C     1 
ATOM   5214  O  O     . SER B 2 235 ? 135.087 151.968 94.913  1.00 55.55  ? 235  SER K O     1 
ATOM   5215  C  CB    . SER B 2 235 ? 137.758 152.704 96.387  1.00 55.12  ? 235  SER K CB    1 
ATOM   5216  O  OG    . SER B 2 235 ? 138.053 151.630 95.512  1.00 58.14  ? 235  SER K OG    1 
ATOM   5217  N  N     . GLU B 2 236 ? 134.830 154.086 95.630  1.00 55.99  ? 236  GLU K N     1 
ATOM   5218  C  CA    . GLU B 2 236 ? 133.796 154.423 94.668  1.00 56.08  ? 236  GLU K CA    1 
ATOM   5219  C  C     . GLU B 2 236 ? 134.224 155.619 93.835  1.00 60.39  ? 236  GLU K C     1 
ATOM   5220  O  O     . GLU B 2 236 ? 135.036 156.441 94.266  1.00 65.90  ? 236  GLU K O     1 
ATOM   5221  C  CB    . GLU B 2 236 ? 132.470 154.737 95.364  1.00 59.90  ? 236  GLU K CB    1 
ATOM   5222  C  CG    . GLU B 2 236 ? 132.125 153.777 96.481  1.00 64.31  ? 236  GLU K CG    1 
ATOM   5223  C  CD    . GLU B 2 236 ? 130.730 153.987 97.022  1.00 69.24  ? 236  GLU K CD    1 
ATOM   5224  O  OE1   . GLU B 2 236 ? 130.045 154.923 96.558  1.00 68.60  ? 236  GLU K OE1   1 
ATOM   5225  O  OE2   . GLU B 2 236 ? 130.317 153.213 97.910  1.00 68.79  ? 236  GLU K OE2   1 
ATOM   5226  N  N     . LYS B 2 237 ? 133.663 155.703 92.635  1.00 56.70  ? 237  LYS K N     1 
ATOM   5227  C  CA    . LYS B 2 237 ? 133.845 156.843 91.752  1.00 54.88  ? 237  LYS K CA    1 
ATOM   5228  C  C     . LYS B 2 237 ? 132.476 157.391 91.376  1.00 58.83  ? 237  LYS K C     1 
ATOM   5229  O  O     . LYS B 2 237 ? 131.560 156.626 91.057  1.00 68.17  ? 237  LYS K O     1 
ATOM   5230  C  CB    . LYS B 2 237 ? 134.629 156.453 90.499  1.00 61.93  ? 237  LYS K CB    1 
ATOM   5231  C  CG    . LYS B 2 237 ? 135.436 157.586 89.894  1.00 64.09  ? 237  LYS K CG    1 
ATOM   5232  C  CD    . LYS B 2 237 ? 136.196 157.126 88.664  1.00 65.78  ? 237  LYS K CD    1 
ATOM   5233  C  CE    . LYS B 2 237 ? 137.017 155.884 88.958  1.00 64.22  ? 237  LYS K CE    1 
ATOM   5234  N  NZ    . LYS B 2 237 ? 138.002 156.115 90.048  1.00 62.19  ? 237  LYS K NZ    1 
ATOM   5235  N  N     . VAL B 2 238 ? 132.339 158.717 91.424  1.00 57.51  ? 238  VAL K N     1 
ATOM   5236  C  CA    . VAL B 2 238 ? 131.043 159.341 91.175  1.00 61.57  ? 238  VAL K CA    1 
ATOM   5237  C  C     . VAL B 2 238 ? 130.587 159.098 89.743  1.00 67.15  ? 238  VAL K C     1 
ATOM   5238  O  O     . VAL B 2 238 ? 129.384 158.989 89.477  1.00 70.95  ? 238  VAL K O     1 
ATOM   5239  C  CB    . VAL B 2 238 ? 131.107 160.843 91.507  1.00 62.27  ? 238  VAL K CB    1 
ATOM   5240  C  CG1   . VAL B 2 238 ? 129.743 161.488 91.344  1.00 64.33  ? 238  VAL K CG1   1 
ATOM   5241  C  CG2   . VAL B 2 238 ? 131.624 161.043 92.918  1.00 60.20  ? 238  VAL K CG2   1 
ATOM   5242  N  N     . SER B 2 239 ? 131.527 159.003 88.802  1.00 63.03  ? 239  SER K N     1 
ATOM   5243  C  CA    . SER B 2 239 ? 131.159 158.717 87.420  1.00 65.97  ? 239  SER K CA    1 
ATOM   5244  C  C     . SER B 2 239 ? 130.506 157.348 87.292  1.00 66.26  ? 239  SER K C     1 
ATOM   5245  O  O     . SER B 2 239 ? 129.516 157.188 86.568  1.00 68.80  ? 239  SER K O     1 
ATOM   5246  C  CB    . SER B 2 239 ? 132.389 158.809 86.519  1.00 67.66  ? 239  SER K CB    1 
ATOM   5247  O  OG    . SER B 2 239 ? 133.367 157.855 86.893  1.00 71.67  ? 239  SER K OG    1 
ATOM   5248  N  N     . LYS B 2 240 ? 131.044 156.346 87.985  1.00 55.83  ? 240  LYS K N     1 
ATOM   5249  C  CA    . LYS B 2 240 ? 130.491 154.999 87.900  1.00 56.01  ? 240  LYS K CA    1 
ATOM   5250  C  C     . LYS B 2 240 ? 129.277 154.833 88.806  1.00 60.91  ? 240  LYS K C     1 
ATOM   5251  O  O     . LYS B 2 240 ? 128.242 154.311 88.379  1.00 66.68  ? 240  LYS K O     1 
ATOM   5252  C  CB    . LYS B 2 240 ? 131.565 153.970 88.253  1.00 55.45  ? 240  LYS K CB    1 
ATOM   5253  C  CG    . LYS B 2 240 ? 132.763 153.988 87.325  1.00 61.73  ? 240  LYS K CG    1 
ATOM   5254  C  CD    . LYS B 2 240 ? 133.770 152.921 87.700  1.00 62.48  ? 240  LYS K CD    1 
ATOM   5255  C  CE    . LYS B 2 240 ? 134.924 152.896 86.717  1.00 61.27  ? 240  LYS K CE    1 
ATOM   5256  N  NZ    . LYS B 2 240 ? 135.936 151.871 87.082  1.00 58.99  ? 240  LYS K NZ    1 
ATOM   5257  N  N     . THR B 2 241 ? 129.385 155.270 90.061  1.00 63.41  ? 241  THR K N     1 
ATOM   5258  C  CA    . THR B 2 241 ? 128.307 155.055 91.019  1.00 64.26  ? 241  THR K CA    1 
ATOM   5259  C  C     . THR B 2 241 ? 127.138 156.008 90.808  1.00 63.90  ? 241  THR K C     1 
ATOM   5260  O  O     . THR B 2 241 ? 125.989 155.631 91.059  1.00 69.93  ? 241  THR K O     1 
ATOM   5261  C  CB    . THR B 2 241 ? 128.836 155.194 92.446  1.00 68.54  ? 241  THR K CB    1 
ATOM   5262  O  OG1   . THR B 2 241 ? 129.418 156.491 92.617  1.00 74.13  ? 241  THR K OG1   1 
ATOM   5263  C  CG2   . THR B 2 241 ? 129.885 154.131 92.728  1.00 66.93  ? 241  THR K CG2   1 
ATOM   5264  N  N     . GLY B 2 242 ? 127.399 157.227 90.350  1.00 57.76  ? 242  GLY K N     1 
ATOM   5265  C  CA    . GLY B 2 242 ? 126.332 158.195 90.159  1.00 60.37  ? 242  GLY K CA    1 
ATOM   5266  C  C     . GLY B 2 242 ? 125.650 158.618 91.442  1.00 64.19  ? 242  GLY K C     1 
ATOM   5267  O  O     . GLY B 2 242 ? 124.417 158.717 91.480  1.00 67.19  ? 242  GLY K O     1 
ATOM   5268  N  N     . ALA B 2 243 ? 126.422 158.872 92.493  1.00 66.80  ? 243  ALA K N     1 
ATOM   5269  C  CA    . ALA B 2 243 ? 125.856 159.180 93.797  1.00 68.26  ? 243  ALA K CA    1 
ATOM   5270  C  C     . ALA B 2 243 ? 125.418 160.636 93.875  1.00 71.63  ? 243  ALA K C     1 
ATOM   5271  O  O     . ALA B 2 243 ? 126.111 161.537 93.393  1.00 78.21  ? 243  ALA K O     1 
ATOM   5272  C  CB    . ALA B 2 243 ? 126.871 158.882 94.900  1.00 68.09  ? 243  ALA K CB    1 
ATOM   5273  N  N     . GLU B 2 244 ? 124.260 160.859 94.493  1.00 65.69  ? 244  GLU K N     1 
ATOM   5274  C  CA    . GLU B 2 244 ? 123.715 162.196 94.699  1.00 64.33  ? 244  GLU K CA    1 
ATOM   5275  C  C     . GLU B 2 244 ? 122.977 162.215 96.028  1.00 67.42  ? 244  GLU K C     1 
ATOM   5276  O  O     . GLU B 2 244 ? 122.046 161.430 96.229  1.00 74.00  ? 244  GLU K O     1 
ATOM   5277  C  CB    . GLU B 2 244 ? 122.766 162.592 93.563  1.00 67.30  ? 244  GLU K CB    1 
ATOM   5278  C  CG    . GLU B 2 244 ? 123.437 162.837 92.225  1.00 73.25  ? 244  GLU K CG    1 
ATOM   5279  C  CD    . GLU B 2 244 ? 122.438 162.992 91.099  1.00 78.68  ? 244  GLU K CD    1 
ATOM   5280  O  OE1   . GLU B 2 244 ? 121.244 162.699 91.320  1.00 77.93  ? 244  GLU K OE1   1 
ATOM   5281  O  OE2   . GLU B 2 244 ? 122.844 163.408 89.993  1.00 80.44  ? 244  GLU K OE2   1 
ATOM   5282  N  N     . GLY B 2 245 ? 123.382 163.103 96.923  1.00 60.32  ? 245  GLY K N     1 
ATOM   5283  C  CA    . GLY B 2 245 ? 122.681 163.294 98.181  1.00 59.85  ? 245  GLY K CA    1 
ATOM   5284  C  C     . GLY B 2 245 ? 123.359 162.553 99.326  1.00 61.79  ? 245  GLY K C     1 
ATOM   5285  O  O     . GLY B 2 245 ? 124.555 162.719 99.558  1.00 66.09  ? 245  GLY K O     1 
ATOM   5286  N  N     . ALA B 2 246 ? 122.581 161.741 100.046 1.00 60.07  ? 246  ALA K N     1 
ATOM   5287  C  CA    . ALA B 2 246 ? 123.128 161.004 101.181 1.00 59.49  ? 246  ALA K CA    1 
ATOM   5288  C  C     . ALA B 2 246 ? 124.186 160.004 100.735 1.00 61.55  ? 246  ALA K C     1 
ATOM   5289  O  O     . ALA B 2 246 ? 125.201 159.811 101.419 1.00 66.07  ? 246  ALA K O     1 
ATOM   5290  C  CB    . ALA B 2 246 ? 122.005 160.296 101.937 1.00 57.91  ? 246  ALA K CB    1 
ATOM   5291  N  N     . VAL B 2 247 ? 123.962 159.352 99.592  1.00 56.34  ? 247  VAL K N     1 
ATOM   5292  C  CA    . VAL B 2 247 ? 124.934 158.396 99.076  1.00 51.64  ? 247  VAL K CA    1 
ATOM   5293  C  C     . VAL B 2 247 ? 126.263 159.078 98.796  1.00 55.91  ? 247  VAL K C     1 
ATOM   5294  O  O     . VAL B 2 247 ? 127.326 158.468 98.958  1.00 61.75  ? 247  VAL K O     1 
ATOM   5295  C  CB    . VAL B 2 247 ? 124.381 157.694 97.824  1.00 51.78  ? 247  VAL K CB    1 
ATOM   5296  C  CG1   . VAL B 2 247 ? 123.395 156.619 98.221  1.00 50.76  ? 247  VAL K CG1   1 
ATOM   5297  C  CG2   . VAL B 2 247 ? 123.717 158.699 96.908  1.00 61.12  ? 247  VAL K CG2   1 
ATOM   5298  N  N     . LEU B 2 248 ? 126.236 160.349 98.391  1.00 54.45  ? 248  LEU K N     1 
ATOM   5299  C  CA    . LEU B 2 248 ? 127.485 161.067 98.159  1.00 53.10  ? 248  LEU K CA    1 
ATOM   5300  C  C     . LEU B 2 248 ? 128.255 161.279 99.457  1.00 58.33  ? 248  LEU K C     1 
ATOM   5301  O  O     . LEU B 2 248 ? 129.482 161.134 99.485  1.00 68.09  ? 248  LEU K O     1 
ATOM   5302  C  CB    . LEU B 2 248 ? 127.204 162.400 97.470  1.00 58.84  ? 248  LEU K CB    1 
ATOM   5303  C  CG    . LEU B 2 248 ? 128.426 163.094 96.870  1.00 60.47  ? 248  LEU K CG    1 
ATOM   5304  C  CD1   . LEU B 2 248 ? 129.187 162.140 95.975  1.00 56.60  ? 248  LEU K CD1   1 
ATOM   5305  C  CD2   . LEU B 2 248 ? 128.010 164.334 96.100  1.00 55.14  ? 248  LEU K CD2   1 
ATOM   5306  N  N     . ASP B 2 249 ? 127.557 161.620 100.545 1.00 59.09  ? 249  ASP K N     1 
ATOM   5307  C  CA    . ASP B 2 249 ? 128.227 161.765 101.835 1.00 59.21  ? 249  ASP K CA    1 
ATOM   5308  C  C     . ASP B 2 249 ? 128.796 160.435 102.309 1.00 61.08  ? 249  ASP K C     1 
ATOM   5309  O  O     . ASP B 2 249 ? 129.922 160.373 102.830 1.00 68.12  ? 249  ASP K O     1 
ATOM   5310  C  CB    . ASP B 2 249 ? 127.257 162.330 102.871 1.00 57.36  ? 249  ASP K CB    1 
ATOM   5311  C  CG    . ASP B 2 249 ? 126.585 163.604 102.405 1.00 64.10  ? 249  ASP K CG    1 
ATOM   5312  O  OD1   . ASP B 2 249 ? 126.876 164.054 101.278 1.00 66.96  ? 249  ASP K OD1   1 
ATOM   5313  O  OD2   . ASP B 2 249 ? 125.764 164.156 103.167 1.00 64.01  ? 249  ASP K OD2   1 
ATOM   5314  N  N     . GLU B 2 250 ? 128.025 159.358 102.139 1.00 49.58  ? 250  GLU K N     1 
ATOM   5315  C  CA    . GLU B 2 250 ? 128.529 158.034 102.482 1.00 47.85  ? 250  GLU K CA    1 
ATOM   5316  C  C     . GLU B 2 250 ? 129.781 157.707 101.683 1.00 49.97  ? 250  GLU K C     1 
ATOM   5317  O  O     . GLU B 2 250 ? 130.750 157.168 102.228 1.00 57.72  ? 250  GLU K O     1 
ATOM   5318  C  CB    . GLU B 2 250 ? 127.449 156.981 102.238 1.00 52.19  ? 250  GLU K CB    1 
ATOM   5319  C  CG    . GLU B 2 250 ? 126.179 157.186 103.042 1.00 54.34  ? 250  GLU K CG    1 
ATOM   5320  C  CD    . GLU B 2 250 ? 125.062 156.258 102.610 1.00 61.18  ? 250  GLU K CD    1 
ATOM   5321  O  OE1   . GLU B 2 250 ? 125.078 155.813 101.444 1.00 67.01  ? 250  GLU K OE1   1 
ATOM   5322  O  OE2   . GLU B 2 250 ? 124.167 155.975 103.432 1.00 61.02  ? 250  GLU K OE2   1 
ATOM   5323  N  N     . ALA B 2 251 ? 129.778 158.030 100.388 1.00 54.27  ? 251  ALA K N     1 
ATOM   5324  C  CA    . ALA B 2 251 ? 130.941 157.769 99.549  1.00 55.88  ? 251  ALA K CA    1 
ATOM   5325  C  C     . ALA B 2 251 ? 132.141 158.584 100.002 1.00 52.47  ? 251  ALA K C     1 
ATOM   5326  O  O     . ALA B 2 251 ? 133.270 158.083 100.013 1.00 62.20  ? 251  ALA K O     1 
ATOM   5327  C  CB    . ALA B 2 251 ? 130.610 158.067 98.088  1.00 51.73  ? 251  ALA K CB    1 
ATOM   5328  N  N     . LYS B 2 252 ? 131.918 159.845 100.371 1.00 43.69  ? 252  LYS K N     1 
ATOM   5329  C  CA    . LYS B 2 252 ? 133.010 160.682 100.855 1.00 44.47  ? 252  LYS K CA    1 
ATOM   5330  C  C     . LYS B 2 252 ? 133.657 160.068 102.088 1.00 49.45  ? 252  LYS K C     1 
ATOM   5331  O  O     . LYS B 2 252 ? 134.887 159.924 102.159 1.00 54.49  ? 252  LYS K O     1 
ATOM   5332  C  CB    . LYS B 2 252 ? 132.493 162.089 101.156 1.00 47.13  ? 252  LYS K CB    1 
ATOM   5333  C  CG    . LYS B 2 252 ? 132.137 162.889 99.919  1.00 52.47  ? 252  LYS K CG    1 
ATOM   5334  C  CD    . LYS B 2 252 ? 131.005 163.867 100.181 1.00 50.72  ? 252  LYS K CD    1 
ATOM   5335  C  CE    . LYS B 2 252 ? 131.411 164.944 101.163 1.00 53.92  ? 252  LYS K CE    1 
ATOM   5336  N  NZ    . LYS B 2 252 ? 130.322 165.940 101.352 1.00 48.21  ? 252  LYS K NZ    1 
ATOM   5337  N  N     . ASN B 2 253 ? 132.837 159.670 103.062 1.00 50.40  ? 253  ASN K N     1 
ATOM   5338  C  CA    . ASN B 2 253 ? 133.391 159.090 104.283 1.00 45.63  ? 253  ASN K CA    1 
ATOM   5339  C  C     . ASN B 2 253 ? 134.075 157.754 104.009 1.00 49.06  ? 253  ASN K C     1 
ATOM   5340  O  O     . ASN B 2 253 ? 135.138 157.467 104.577 1.00 55.44  ? 253  ASN K O     1 
ATOM   5341  C  CB    . ASN B 2 253 ? 132.298 158.940 105.335 1.00 48.53  ? 253  ASN K CB    1 
ATOM   5342  C  CG    . ASN B 2 253 ? 132.089 160.207 106.134 1.00 54.72  ? 253  ASN K CG    1 
ATOM   5343  O  OD1   . ASN B 2 253 ? 131.034 160.834 106.061 1.00 55.01  ? 253  ASN K OD1   1 
ATOM   5344  N  ND2   . ASN B 2 253 ? 133.102 160.598 106.895 1.00 52.12  ? 253  ASN K ND2   1 
ATOM   5345  N  N     . ILE B 2 254 ? 133.488 156.928 103.140 1.00 44.88  ? 254  ILE K N     1 
ATOM   5346  C  CA    . ILE B 2 254 ? 134.079 155.631 102.820 1.00 39.89  ? 254  ILE K CA    1 
ATOM   5347  C  C     . ILE B 2 254 ? 135.441 155.816 102.169 1.00 45.90  ? 254  ILE K C     1 
ATOM   5348  O  O     . ILE B 2 254 ? 136.417 155.143 102.522 1.00 54.69  ? 254  ILE K O     1 
ATOM   5349  C  CB    . ILE B 2 254 ? 133.132 154.822 101.915 1.00 44.87  ? 254  ILE K CB    1 
ATOM   5350  C  CG1   . ILE B 2 254 ? 131.958 154.272 102.721 1.00 44.91  ? 254  ILE K CG1   1 
ATOM   5351  C  CG2   . ILE B 2 254 ? 133.877 153.691 101.236 1.00 50.44  ? 254  ILE K CG2   1 
ATOM   5352  C  CD1   . ILE B 2 254 ? 130.838 153.736 101.863 1.00 51.59  ? 254  ILE K CD1   1 
ATOM   5353  N  N     . ASN B 2 255 ? 135.524 156.732 101.203 1.00 45.89  ? 255  ASN K N     1 
ATOM   5354  C  CA    . ASN B 2 255 ? 136.787 156.981 100.525 1.00 40.28  ? 255  ASN K CA    1 
ATOM   5355  C  C     . ASN B 2 255 ? 137.834 157.504 101.495 1.00 44.42  ? 255  ASN K C     1 
ATOM   5356  O  O     . ASN B 2 255 ? 138.999 157.095 101.440 1.00 49.11  ? 255  ASN K O     1 
ATOM   5357  C  CB    . ASN B 2 255 ? 136.575 157.965 99.376  1.00 41.12  ? 255  ASN K CB    1 
ATOM   5358  C  CG    . ASN B 2 255 ? 135.681 157.407 98.293  1.00 49.23  ? 255  ASN K CG    1 
ATOM   5359  O  OD1   . ASN B 2 255 ? 135.095 156.338 98.448  1.00 50.13  ? 255  ASN K OD1   1 
ATOM   5360  N  ND2   . ASN B 2 255 ? 135.563 158.134 97.191  1.00 52.83  ? 255  ASN K ND2   1 
ATOM   5361  N  N     . LYS B 2 256 ? 137.440 158.412 102.393 1.00 47.77  ? 256  LYS K N     1 
ATOM   5362  C  CA    . LYS B 2 256 ? 138.389 158.941 103.367 1.00 41.21  ? 256  LYS K CA    1 
ATOM   5363  C  C     . LYS B 2 256 ? 138.928 157.837 104.273 1.00 39.74  ? 256  LYS K C     1 
ATOM   5364  O  O     . LYS B 2 256 ? 140.142 157.752 104.514 1.00 45.64  ? 256  LYS K O     1 
ATOM   5365  C  CB    . LYS B 2 256 ? 137.717 160.044 104.183 1.00 41.92  ? 256  LYS K CB    1 
ATOM   5366  C  CG    . LYS B 2 256 ? 138.665 160.975 104.908 1.00 46.82  ? 256  LYS K CG    1 
ATOM   5367  C  CD    . LYS B 2 256 ? 137.919 162.182 105.443 1.00 42.79  ? 256  LYS K CD    1 
ATOM   5368  C  CE    . LYS B 2 256 ? 138.811 163.045 106.312 1.00 45.62  ? 256  LYS K CE    1 
ATOM   5369  N  NZ    . LYS B 2 256 ? 139.979 163.571 105.559 1.00 43.91  ? 256  LYS K NZ    1 
ATOM   5370  N  N     . SER B 2 257 ? 138.043 156.966 104.766 1.00 36.43  ? 257  SER K N     1 
ATOM   5371  C  CA    . SER B 2 257 ? 138.484 155.876 105.633 1.00 35.97  ? 257  SER K CA    1 
ATOM   5372  C  C     . SER B 2 257 ? 139.403 154.910 104.894 1.00 42.04  ? 257  SER K C     1 
ATOM   5373  O  O     . SER B 2 257 ? 140.416 154.456 105.445 1.00 45.15  ? 257  SER K O     1 
ATOM   5374  C  CB    . SER B 2 257 ? 137.273 155.135 106.196 1.00 38.76  ? 257  SER K CB    1 
ATOM   5375  O  OG    . SER B 2 257 ? 136.424 156.017 106.908 1.00 48.89  ? 257  SER K OG    1 
ATOM   5376  N  N     . LEU B 2 258 ? 139.065 154.577 103.647 1.00 45.64  ? 258  LEU K N     1 
ATOM   5377  C  CA    . LEU B 2 258 ? 139.900 153.656 102.886 1.00 37.94  ? 258  LEU K CA    1 
ATOM   5378  C  C     . LEU B 2 258 ? 141.259 154.269 102.579 1.00 41.14  ? 258  LEU K C     1 
ATOM   5379  O  O     . LEU B 2 258 ? 142.275 153.565 102.569 1.00 48.96  ? 258  LEU K O     1 
ATOM   5380  C  CB    . LEU B 2 258 ? 139.191 153.241 101.602 1.00 38.38  ? 258  LEU K CB    1 
ATOM   5381  C  CG    . LEU B 2 258 ? 137.959 152.365 101.800 1.00 40.17  ? 258  LEU K CG    1 
ATOM   5382  C  CD1   . LEU B 2 258 ? 137.369 151.992 100.459 1.00 45.65  ? 258  LEU K CD1   1 
ATOM   5383  C  CD2   . LEU B 2 258 ? 138.310 151.128 102.597 1.00 44.65  ? 258  LEU K CD2   1 
ATOM   5384  N  N     . SER B 2 259 ? 141.301 155.578 102.327 1.00 41.42  ? 259  SER K N     1 
ATOM   5385  C  CA    . SER B 2 259 ? 142.581 156.247 102.133 1.00 40.23  ? 259  SER K CA    1 
ATOM   5386  C  C     . SER B 2 259 ? 143.420 156.201 103.402 1.00 44.54  ? 259  SER K C     1 
ATOM   5387  O  O     . SER B 2 259 ? 144.640 156.014 103.340 1.00 48.69  ? 259  SER K O     1 
ATOM   5388  C  CB    . SER B 2 259 ? 142.357 157.690 101.687 1.00 45.47  ? 259  SER K CB    1 
ATOM   5389  O  OG    . SER B 2 259 ? 143.590 158.345 101.454 1.00 51.40  ? 259  SER K OG    1 
ATOM   5390  N  N     . ALA B 2 260 ? 142.785 156.374 104.565 1.00 47.15  ? 260  ALA K N     1 
ATOM   5391  C  CA    . ALA B 2 260 ? 143.522 156.259 105.821 1.00 41.59  ? 260  ALA K CA    1 
ATOM   5392  C  C     . ALA B 2 260 ? 144.096 154.857 106.000 1.00 46.46  ? 260  ALA K C     1 
ATOM   5393  O  O     . ALA B 2 260 ? 145.252 154.693 106.419 1.00 52.36  ? 260  ALA K O     1 
ATOM   5394  C  CB    . ALA B 2 260 ? 142.617 156.623 106.996 1.00 43.22  ? 260  ALA K CB    1 
ATOM   5395  N  N     . LEU B 2 261 ? 143.302 153.833 105.682 1.00 49.06  ? 261  LEU K N     1 
ATOM   5396  C  CA    . LEU B 2 261 ? 143.794 152.460 105.781 1.00 44.21  ? 261  LEU K CA    1 
ATOM   5397  C  C     . LEU B 2 261 ? 144.951 152.213 104.820 1.00 43.65  ? 261  LEU K C     1 
ATOM   5398  O  O     . LEU B 2 261 ? 145.934 151.546 105.171 1.00 48.28  ? 261  LEU K O     1 
ATOM   5399  C  CB    . LEU B 2 261 ? 142.659 151.476 105.515 1.00 43.92  ? 261  LEU K CB    1 
ATOM   5400  C  CG    . LEU B 2 261 ? 143.020 150.000 105.649 1.00 48.26  ? 261  LEU K CG    1 
ATOM   5401  C  CD1   . LEU B 2 261 ? 143.111 149.598 107.106 1.00 50.16  ? 261  LEU K CD1   1 
ATOM   5402  C  CD2   . LEU B 2 261 ? 142.013 149.143 104.916 1.00 48.46  ? 261  LEU K CD2   1 
ATOM   5403  N  N     . GLY B 2 262 ? 144.849 152.731 103.597 1.00 44.63  ? 262  GLY K N     1 
ATOM   5404  C  CA    . GLY B 2 262 ? 145.947 152.599 102.656 1.00 41.43  ? 262  GLY K CA    1 
ATOM   5405  C  C     . GLY B 2 262 ? 147.203 153.297 103.135 1.00 43.31  ? 262  GLY K C     1 
ATOM   5406  O  O     . GLY B 2 262 ? 148.313 152.791 102.955 1.00 47.54  ? 262  GLY K O     1 
ATOM   5407  N  N     . ASN B 2 263 ? 147.044 154.466 103.758 1.00 45.05  ? 263  ASN K N     1 
ATOM   5408  C  CA    . ASN B 2 263 ? 148.191 155.172 104.315 1.00 39.98  ? 263  ASN K CA    1 
ATOM   5409  C  C     . ASN B 2 263 ? 148.859 154.357 105.411 1.00 43.26  ? 263  ASN K C     1 
ATOM   5410  O  O     . ASN B 2 263 ? 150.090 154.281 105.473 1.00 54.65  ? 263  ASN K O     1 
ATOM   5411  C  CB    . ASN B 2 263 ? 147.761 156.535 104.852 1.00 38.95  ? 263  ASN K CB    1 
ATOM   5412  C  CG    . ASN B 2 263 ? 147.396 157.504 103.752 1.00 50.11  ? 263  ASN K CG    1 
ATOM   5413  O  OD1   . ASN B 2 263 ? 147.216 157.112 102.601 1.00 57.73  ? 263  ASN K OD1   1 
ATOM   5414  N  ND2   . ASN B 2 263 ? 147.288 158.778 104.100 1.00 48.35  ? 263  ASN K ND2   1 
ATOM   5415  N  N     . VAL B 2 264 ? 148.066 153.735 106.286 1.00 41.44  ? 264  VAL K N     1 
ATOM   5416  C  CA    . VAL B 2 264 ? 148.672 152.959 107.366 1.00 42.88  ? 264  VAL K CA    1 
ATOM   5417  C  C     . VAL B 2 264 ? 149.359 151.712 106.815 1.00 42.98  ? 264  VAL K C     1 
ATOM   5418  O  O     . VAL B 2 264 ? 150.431 151.321 107.293 1.00 46.44  ? 264  VAL K O     1 
ATOM   5419  C  CB    . VAL B 2 264 ? 147.638 152.627 108.459 1.00 44.37  ? 264  VAL K CB    1 
ATOM   5420  C  CG1   . VAL B 2 264 ? 146.817 151.401 108.115 1.00 43.52  ? 264  VAL K CG1   1 
ATOM   5421  C  CG2   . VAL B 2 264 ? 148.338 152.431 109.787 1.00 44.19  ? 264  VAL K CG2   1 
ATOM   5422  N  N     . ILE B 2 265 ? 148.780 151.082 105.789 1.00 44.86  ? 265  ILE K N     1 
ATOM   5423  C  CA    . ILE B 2 265 ? 149.425 149.913 105.196 1.00 34.45  ? 265  ILE K CA    1 
ATOM   5424  C  C     . ILE B 2 265 ? 150.733 150.310 104.521 1.00 39.13  ? 265  ILE K C     1 
ATOM   5425  O  O     . ILE B 2 265 ? 151.748 149.611 104.641 1.00 45.42  ? 265  ILE K O     1 
ATOM   5426  C  CB    . ILE B 2 265 ? 148.468 149.205 104.222 1.00 37.62  ? 265  ILE K CB    1 
ATOM   5427  C  CG1   . ILE B 2 265 ? 147.446 148.372 104.994 1.00 41.22  ? 265  ILE K CG1   1 
ATOM   5428  C  CG2   . ILE B 2 265 ? 149.238 148.318 103.267 1.00 42.34  ? 265  ILE K CG2   1 
ATOM   5429  C  CD1   . ILE B 2 265 ? 148.052 147.227 105.760 1.00 49.30  ? 265  ILE K CD1   1 
ATOM   5430  N  N     . SER B 2 266 ? 150.737 151.442 103.815 1.00 46.67  ? 266  SER K N     1 
ATOM   5431  C  CA    . SER B 2 266 ? 151.967 151.931 103.202 1.00 46.19  ? 266  SER K CA    1 
ATOM   5432  C  C     . SER B 2 266 ? 153.015 152.259 104.257 1.00 44.10  ? 266  SER K C     1 
ATOM   5433  O  O     . SER B 2 266 ? 154.210 152.014 104.052 1.00 44.51  ? 266  SER K O     1 
ATOM   5434  C  CB    . SER B 2 266 ? 151.670 153.156 102.340 1.00 48.91  ? 266  SER K CB    1 
ATOM   5435  O  OG    . SER B 2 266 ? 152.854 153.664 101.752 1.00 56.41  ? 266  SER K OG    1 
ATOM   5436  N  N     . ALA B 2 267 ? 152.589 152.825 105.388 1.00 45.88  ? 267  ALA K N     1 
ATOM   5437  C  CA    . ALA B 2 267 ? 153.526 153.128 106.464 1.00 45.15  ? 267  ALA K CA    1 
ATOM   5438  C  C     . ALA B 2 267 ? 154.136 151.860 107.043 1.00 48.01  ? 267  ALA K C     1 
ATOM   5439  O  O     . ALA B 2 267 ? 155.336 151.822 107.336 1.00 51.80  ? 267  ALA K O     1 
ATOM   5440  C  CB    . ALA B 2 267 ? 152.826 153.932 107.558 1.00 46.05  ? 267  ALA K CB    1 
ATOM   5441  N  N     . LEU B 2 268 ? 153.327 150.814 107.226 1.00 44.86  ? 268  LEU K N     1 
ATOM   5442  C  CA    . LEU B 2 268 ? 153.881 149.542 107.684 1.00 37.33  ? 268  LEU K CA    1 
ATOM   5443  C  C     . LEU B 2 268 ? 154.868 148.974 106.671 1.00 44.22  ? 268  LEU K C     1 
ATOM   5444  O  O     . LEU B 2 268 ? 155.934 148.474 107.045 1.00 40.87  ? 268  LEU K O     1 
ATOM   5445  C  CB    . LEU B 2 268 ? 152.774 148.522 107.948 1.00 38.11  ? 268  LEU K CB    1 
ATOM   5446  C  CG    . LEU B 2 268 ? 152.075 148.367 109.301 1.00 42.19  ? 268  LEU K CG    1 
ATOM   5447  C  CD1   . LEU B 2 268 ? 153.068 148.003 110.396 1.00 40.69  ? 268  LEU K CD1   1 
ATOM   5448  C  CD2   . LEU B 2 268 ? 151.253 149.563 109.667 1.00 49.16  ? 268  LEU K CD2   1 
ATOM   5449  N  N     . ALA B 2 269 ? 154.522 149.032 105.382 1.00 45.31  ? 269  ALA K N     1 
ATOM   5450  C  CA    . ALA B 2 269 ? 155.359 148.412 104.359 1.00 36.19  ? 269  ALA K CA    1 
ATOM   5451  C  C     . ALA B 2 269 ? 156.687 149.138 104.199 1.00 39.14  ? 269  ALA K C     1 
ATOM   5452  O  O     . ALA B 2 269 ? 157.738 148.499 104.077 1.00 41.00  ? 269  ALA K O     1 
ATOM   5453  C  CB    . ALA B 2 269 ? 154.611 148.367 103.029 1.00 43.23  ? 269  ALA K CB    1 
ATOM   5454  N  N     . GLU B 2 270 ? 156.663 150.470 104.193 1.00 49.12  ? 270  GLU K N     1 
ATOM   5455  C  CA    . GLU B 2 270 ? 157.882 151.244 103.998 1.00 48.03  ? 270  GLU K CA    1 
ATOM   5456  C  C     . GLU B 2 270 ? 158.797 151.229 105.212 1.00 54.57  ? 270  GLU K C     1 
ATOM   5457  O  O     . GLU B 2 270 ? 159.929 151.712 105.115 1.00 60.50  ? 270  GLU K O     1 
ATOM   5458  C  CB    . GLU B 2 270 ? 157.531 152.688 103.639 1.00 56.91  ? 270  GLU K CB    1 
ATOM   5459  C  CG    . GLU B 2 270 ? 156.851 152.842 102.291 1.00 60.55  ? 270  GLU K CG    1 
ATOM   5460  C  CD    . GLU B 2 270 ? 156.554 154.288 101.952 1.00 63.84  ? 270  GLU K CD    1 
ATOM   5461  O  OE1   . GLU B 2 270 ? 156.873 155.171 102.776 1.00 62.47  ? 270  GLU K OE1   1 
ATOM   5462  O  OE2   . GLU B 2 270 ? 156.001 154.544 100.862 1.00 61.78  ? 270  GLU K OE2   1 
ATOM   5463  N  N     . GLY B 2 271 ? 158.345 150.695 106.342 1.00 57.03  ? 271  GLY K N     1 
ATOM   5464  C  CA    . GLY B 2 271 ? 159.151 150.720 107.545 1.00 49.82  ? 271  GLY K CA    1 
ATOM   5465  C  C     . GLY B 2 271 ? 159.203 152.065 108.226 1.00 52.21  ? 271  GLY K C     1 
ATOM   5466  O  O     . GLY B 2 271 ? 160.211 152.392 108.860 1.00 53.01  ? 271  GLY K O     1 
ATOM   5467  N  N     . SER B 2 272 ? 158.143 152.860 108.115 1.00 53.50  ? 272  SER K N     1 
ATOM   5468  C  CA    . SER B 2 272 ? 158.120 154.186 108.708 1.00 51.40  ? 272  SER K CA    1 
ATOM   5469  C  C     . SER B 2 272 ? 158.083 154.082 110.231 1.00 54.57  ? 272  SER K C     1 
ATOM   5470  O  O     . SER B 2 272 ? 158.030 152.995 110.812 1.00 58.39  ? 272  SER K O     1 
ATOM   5471  C  CB    . SER B 2 272 ? 156.927 154.979 108.184 1.00 52.76  ? 272  SER K CB    1 
ATOM   5472  O  OG    . SER B 2 272 ? 156.891 156.279 108.747 1.00 59.28  ? 272  SER K OG    1 
ATOM   5473  N  N     . THR B 2 273 ? 158.107 155.239 110.889 1.00 51.66  ? 273  THR K N     1 
ATOM   5474  C  CA    . THR B 2 273 ? 158.133 155.303 112.344 1.00 45.28  ? 273  THR K CA    1 
ATOM   5475  C  C     . THR B 2 273 ? 156.805 155.752 112.941 1.00 53.11  ? 273  THR K C     1 
ATOM   5476  O  O     . THR B 2 273 ? 156.343 155.165 113.924 1.00 60.53  ? 273  THR K O     1 
ATOM   5477  C  CB    . THR B 2 273 ? 159.256 156.237 112.805 1.00 48.14  ? 273  THR K CB    1 
ATOM   5478  O  OG1   . THR B 2 273 ? 160.513 155.743 112.329 1.00 53.95  ? 273  THR K OG1   1 
ATOM   5479  C  CG2   . THR B 2 273 ? 159.296 156.314 114.321 1.00 48.76  ? 273  THR K CG2   1 
ATOM   5480  N  N     . TYR B 2 274 ? 156.174 156.781 112.370 1.00 51.25  ? 274  TYR K N     1 
ATOM   5481  C  CA    . TYR B 2 274 ? 154.946 157.297 112.967 1.00 50.34  ? 274  TYR K CA    1 
ATOM   5482  C  C     . TYR B 2 274 ? 153.789 156.318 112.818 1.00 57.35  ? 274  TYR K C     1 
ATOM   5483  O  O     . TYR B 2 274 ? 152.973 156.183 113.737 1.00 62.22  ? 274  TYR K O     1 
ATOM   5484  C  CB    . TYR B 2 274 ? 154.568 158.645 112.364 1.00 49.00  ? 274  TYR K CB    1 
ATOM   5485  C  CG    . TYR B 2 274 ? 153.218 159.115 112.846 1.00 51.81  ? 274  TYR K CG    1 
ATOM   5486  C  CD1   . TYR B 2 274 ? 152.936 159.194 114.201 1.00 49.15  ? 274  TYR K CD1   1 
ATOM   5487  C  CD2   . TYR B 2 274 ? 152.217 159.456 111.951 1.00 57.01  ? 274  TYR K CD2   1 
ATOM   5488  C  CE1   . TYR B 2 274 ? 151.702 159.604 114.651 1.00 51.93  ? 274  TYR K CE1   1 
ATOM   5489  C  CE2   . TYR B 2 274 ? 150.980 159.873 112.393 1.00 57.68  ? 274  TYR K CE2   1 
ATOM   5490  C  CZ    . TYR B 2 274 ? 150.729 159.946 113.744 1.00 57.12  ? 274  TYR K CZ    1 
ATOM   5491  O  OH    . TYR B 2 274 ? 149.497 160.362 114.191 1.00 58.86  ? 274  TYR K OH    1 
ATOM   5492  N  N     . VAL B 2 275 ? 153.698 155.642 111.673 1.00 44.52  ? 275  VAL K N     1 
ATOM   5493  C  CA    . VAL B 2 275 ? 152.668 154.643 111.364 1.00 41.38  ? 275  VAL K CA    1 
ATOM   5494  C  C     . VAL B 2 275 ? 151.282 155.136 111.780 1.00 41.29  ? 275  VAL K C     1 
ATOM   5495  O  O     . VAL B 2 275 ? 150.769 154.763 112.846 1.00 49.39  ? 275  VAL K O     1 
ATOM   5496  C  CB    . VAL B 2 275 ? 153.022 153.255 111.940 1.00 45.67  ? 275  VAL K CB    1 
ATOM   5497  C  CG1   . VAL B 2 275 ? 153.261 153.233 113.458 1.00 51.38  ? 275  VAL K CG1   1 
ATOM   5498  C  CG2   . VAL B 2 275 ? 151.971 152.262 111.551 1.00 47.37  ? 275  VAL K CG2   1 
ATOM   5499  N  N     . PRO B 2 276 ? 150.647 155.992 110.975 1.00 46.32  ? 276  PRO K N     1 
ATOM   5500  C  CA    . PRO B 2 276 ? 149.492 156.769 111.451 1.00 48.90  ? 276  PRO K CA    1 
ATOM   5501  C  C     . PRO B 2 276 ? 148.245 155.946 111.719 1.00 53.18  ? 276  PRO K C     1 
ATOM   5502  O  O     . PRO B 2 276 ? 147.346 155.880 110.875 1.00 56.71  ? 276  PRO K O     1 
ATOM   5503  C  CB    . PRO B 2 276 ? 149.236 157.753 110.300 1.00 51.44  ? 276  PRO K CB    1 
ATOM   5504  C  CG    . PRO B 2 276 ? 150.420 157.640 109.387 1.00 54.58  ? 276  PRO K CG    1 
ATOM   5505  C  CD    . PRO B 2 276 ? 150.935 156.259 109.560 1.00 53.18  ? 276  PRO K CD    1 
ATOM   5506  N  N     . TYR B 2 277 ? 148.176 155.317 112.892 1.00 52.08  ? 277  TYR K N     1 
ATOM   5507  C  CA    . TYR B 2 277 ? 146.981 154.571 113.264 1.00 44.11  ? 277  TYR K CA    1 
ATOM   5508  C  C     . TYR B 2 277 ? 145.816 155.473 113.646 1.00 47.20  ? 277  TYR K C     1 
ATOM   5509  O  O     . TYR B 2 277 ? 144.665 155.030 113.588 1.00 57.64  ? 277  TYR K O     1 
ATOM   5510  C  CB    . TYR B 2 277 ? 147.274 153.636 114.435 1.00 43.59  ? 277  TYR K CB    1 
ATOM   5511  C  CG    . TYR B 2 277 ? 148.301 152.565 114.168 1.00 45.89  ? 277  TYR K CG    1 
ATOM   5512  C  CD1   . TYR B 2 277 ? 148.095 151.609 113.189 1.00 46.96  ? 277  TYR K CD1   1 
ATOM   5513  C  CD2   . TYR B 2 277 ? 149.459 152.488 114.923 1.00 49.06  ? 277  TYR K CD2   1 
ATOM   5514  C  CE1   . TYR B 2 277 ? 149.025 150.621 112.952 1.00 45.48  ? 277  TYR K CE1   1 
ATOM   5515  C  CE2   . TYR B 2 277 ? 150.393 151.503 114.695 1.00 47.52  ? 277  TYR K CE2   1 
ATOM   5516  C  CZ    . TYR B 2 277 ? 150.169 150.570 113.713 1.00 45.25  ? 277  TYR K CZ    1 
ATOM   5517  O  OH    . TYR B 2 277 ? 151.103 149.589 113.480 1.00 54.30  ? 277  TYR K OH    1 
ATOM   5518  N  N     . ARG B 2 278 ? 146.079 156.718 114.030 1.00 48.46  ? 278  ARG K N     1 
ATOM   5519  C  CA    . ARG B 2 278 ? 145.077 157.556 114.673 1.00 54.42  ? 278  ARG K CA    1 
ATOM   5520  C  C     . ARG B 2 278 ? 144.301 158.434 113.702 1.00 56.31  ? 278  ARG K C     1 
ATOM   5521  O  O     . ARG B 2 278 ? 143.525 159.285 114.146 1.00 56.30  ? 278  ARG K O     1 
ATOM   5522  C  CB    . ARG B 2 278 ? 145.734 158.434 115.738 1.00 52.96  ? 278  ARG K CB    1 
ATOM   5523  C  CG    . ARG B 2 278 ? 146.224 157.668 116.949 1.00 56.36  ? 278  ARG K CG    1 
ATOM   5524  C  CD    . ARG B 2 278 ? 146.658 158.611 118.049 1.00 56.52  ? 278  ARG K CD    1 
ATOM   5525  N  NE    . ARG B 2 278 ? 145.890 158.413 119.270 1.00 59.67  ? 278  ARG K NE    1 
ATOM   5526  C  CZ    . ARG B 2 278 ? 146.254 157.612 120.261 1.00 57.88  ? 278  ARG K CZ    1 
ATOM   5527  N  NH1   . ARG B 2 278 ? 147.378 156.918 120.211 1.00 54.22  ? 278  ARG K NH1   1 
ATOM   5528  N  NH2   . ARG B 2 278 ? 145.471 157.506 121.330 1.00 56.35  ? 278  ARG K NH2   1 
ATOM   5529  N  N     . ASP B 2 279 ? 144.487 158.257 112.397 1.00 59.23  ? 279  ASP K N     1 
ATOM   5530  C  CA    . ASP B 2 279 ? 143.825 159.125 111.433 1.00 58.01  ? 279  ASP K CA    1 
ATOM   5531  C  C     . ASP B 2 279 ? 142.376 158.737 111.166 1.00 63.14  ? 279  ASP K C     1 
ATOM   5532  O  O     . ASP B 2 279 ? 141.658 159.513 110.527 1.00 68.55  ? 279  ASP K O     1 
ATOM   5533  C  CB    . ASP B 2 279 ? 144.603 159.135 110.116 1.00 62.55  ? 279  ASP K CB    1 
ATOM   5534  C  CG    . ASP B 2 279 ? 144.924 157.740 109.616 1.00 70.77  ? 279  ASP K CG    1 
ATOM   5535  O  OD1   . ASP B 2 279 ? 144.600 156.763 110.323 1.00 70.14  ? 279  ASP K OD1   1 
ATOM   5536  O  OD2   . ASP B 2 279 ? 145.501 157.621 108.515 1.00 72.67  ? 279  ASP K OD2   1 
ATOM   5537  N  N     . SER B 2 280 ? 141.927 157.573 111.629 1.00 58.15  ? 280  SER K N     1 
ATOM   5538  C  CA    . SER B 2 280 ? 140.549 157.157 111.406 1.00 53.58  ? 280  SER K CA    1 
ATOM   5539  C  C     . SER B 2 280 ? 140.153 156.137 112.463 1.00 55.27  ? 280  SER K C     1 
ATOM   5540  O  O     . SER B 2 280 ? 141.004 155.519 113.106 1.00 59.73  ? 280  SER K O     1 
ATOM   5541  C  CB    . SER B 2 280 ? 140.358 156.577 110.003 1.00 52.97  ? 280  SER K CB    1 
ATOM   5542  O  OG    . SER B 2 280 ? 141.181 155.441 109.807 1.00 61.31  ? 280  SER K OG    1 
ATOM   5543  N  N     . LYS B 2 281 ? 138.838 155.974 112.632 1.00 53.93  ? 281  LYS K N     1 
ATOM   5544  C  CA    . LYS B 2 281 ? 138.325 155.001 113.592 1.00 55.78  ? 281  LYS K CA    1 
ATOM   5545  C  C     . LYS B 2 281 ? 138.685 153.580 113.184 1.00 59.74  ? 281  LYS K C     1 
ATOM   5546  O  O     . LYS B 2 281 ? 139.077 152.763 114.027 1.00 65.67  ? 281  LYS K O     1 
ATOM   5547  C  CB    . LYS B 2 281 ? 136.810 155.138 113.716 1.00 55.45  ? 281  LYS K CB    1 
ATOM   5548  C  CG    . LYS B 2 281 ? 136.324 156.515 114.111 1.00 57.04  ? 281  LYS K CG    1 
ATOM   5549  C  CD    . LYS B 2 281 ? 136.470 156.756 115.596 1.00 59.41  ? 281  LYS K CD    1 
ATOM   5550  C  CE    . LYS B 2 281 ? 135.421 157.739 116.083 1.00 55.85  ? 281  LYS K CE    1 
ATOM   5551  N  NZ    . LYS B 2 281 ? 135.383 158.960 115.237 1.00 54.62  ? 281  LYS K NZ    1 
ATOM   5552  N  N     . MET B 2 282 ? 138.544 153.264 111.895 1.00 60.55  ? 282  MET K N     1 
ATOM   5553  C  CA    . MET B 2 282 ? 138.811 151.909 111.427 1.00 59.29  ? 282  MET K CA    1 
ATOM   5554  C  C     . MET B 2 282 ? 140.272 151.535 111.623 1.00 61.11  ? 282  MET K C     1 
ATOM   5555  O  O     . MET B 2 282 ? 140.584 150.411 112.033 1.00 68.85  ? 282  MET K O     1 
ATOM   5556  C  CB    . MET B 2 282 ? 138.411 151.778 109.958 1.00 63.90  ? 282  MET K CB    1 
ATOM   5557  C  CG    . MET B 2 282 ? 138.710 150.425 109.346 1.00 68.41  ? 282  MET K CG    1 
ATOM   5558  S  SD    . MET B 2 282 ? 138.079 149.058 110.333 1.00 95.39  ? 282  MET K SD    1 
ATOM   5559  C  CE    . MET B 2 282 ? 136.346 149.481 110.428 1.00 71.72  ? 282  MET K CE    1 
ATOM   5560  N  N     . THR B 2 283 ? 141.183 152.465 111.337 1.00 49.78  ? 283  THR K N     1 
ATOM   5561  C  CA    . THR B 2 283 ? 142.598 152.196 111.557 1.00 48.43  ? 283  THR K CA    1 
ATOM   5562  C  C     . THR B 2 283 ? 142.903 152.055 113.041 1.00 50.45  ? 283  THR K C     1 
ATOM   5563  O  O     . THR B 2 283 ? 143.778 151.272 113.429 1.00 57.90  ? 283  THR K O     1 
ATOM   5564  C  CB    . THR B 2 283 ? 143.443 153.304 110.939 1.00 57.07  ? 283  THR K CB    1 
ATOM   5565  O  OG1   . THR B 2 283 ? 142.937 153.621 109.638 1.00 60.97  ? 283  THR K OG1   1 
ATOM   5566  C  CG2   . THR B 2 283 ? 144.878 152.856 110.816 1.00 56.13  ? 283  THR K CG2   1 
ATOM   5567  N  N     . ARG B 2 284 ? 142.194 152.806 113.883 1.00 48.94  ? 284  ARG K N     1 
ATOM   5568  C  CA    . ARG B 2 284 ? 142.368 152.674 115.324 1.00 48.59  ? 284  ARG K CA    1 
ATOM   5569  C  C     . ARG B 2 284 ? 141.964 151.286 115.799 1.00 57.25  ? 284  ARG K C     1 
ATOM   5570  O  O     . ARG B 2 284 ? 142.714 150.624 116.523 1.00 65.28  ? 284  ARG K O     1 
ATOM   5571  C  CB    . ARG B 2 284 ? 141.555 153.745 116.048 1.00 50.48  ? 284  ARG K CB    1 
ATOM   5572  C  CG    . ARG B 2 284 ? 142.229 155.094 116.114 1.00 53.27  ? 284  ARG K CG    1 
ATOM   5573  C  CD    . ARG B 2 284 ? 143.345 155.084 117.130 1.00 54.28  ? 284  ARG K CD    1 
ATOM   5574  N  NE    . ARG B 2 284 ? 142.832 155.003 118.490 1.00 54.52  ? 284  ARG K NE    1 
ATOM   5575  C  CZ    . ARG B 2 284 ? 143.589 154.869 119.569 1.00 57.34  ? 284  ARG K CZ    1 
ATOM   5576  N  NH1   . ARG B 2 284 ? 144.906 154.783 119.482 1.00 56.80  ? 284  ARG K NH1   1 
ATOM   5577  N  NH2   . ARG B 2 284 ? 143.011 154.819 120.765 1.00 57.03  ? 284  ARG K NH2   1 
ATOM   5578  N  N     . ILE B 2 285 ? 140.789 150.817 115.379 1.00 54.99  ? 285  ILE K N     1 
ATOM   5579  C  CA    . ILE B 2 285 ? 140.292 149.530 115.859 1.00 49.56  ? 285  ILE K CA    1 
ATOM   5580  C  C     . ILE B 2 285 ? 141.200 148.394 115.401 1.00 53.36  ? 285  ILE K C     1 
ATOM   5581  O  O     . ILE B 2 285 ? 141.477 147.459 116.162 1.00 57.14  ? 285  ILE K O     1 
ATOM   5582  C  CB    . ILE B 2 285 ? 138.839 149.318 115.400 1.00 48.84  ? 285  ILE K CB    1 
ATOM   5583  C  CG1   . ILE B 2 285 ? 137.943 150.425 115.950 1.00 57.31  ? 285  ILE K CG1   1 
ATOM   5584  C  CG2   . ILE B 2 285 ? 138.328 147.965 115.853 1.00 53.72  ? 285  ILE K CG2   1 
ATOM   5585  C  CD1   . ILE B 2 285 ? 136.512 150.332 115.490 1.00 56.63  ? 285  ILE K CD1   1 
ATOM   5586  N  N     . LEU B 2 286 ? 141.689 148.458 114.164 1.00 60.11  ? 286  LEU K N     1 
ATOM   5587  C  CA    . LEU B 2 286 ? 142.512 147.405 113.586 1.00 58.79  ? 286  LEU K CA    1 
ATOM   5588  C  C     . LEU B 2 286 ? 144.005 147.638 113.778 1.00 58.80  ? 286  LEU K C     1 
ATOM   5589  O  O     . LEU B 2 286 ? 144.804 147.120 112.993 1.00 68.78  ? 286  LEU K O     1 
ATOM   5590  C  CB    . LEU B 2 286 ? 142.208 147.259 112.095 1.00 60.97  ? 286  LEU K CB    1 
ATOM   5591  C  CG    . LEU B 2 286 ? 140.778 146.902 111.697 1.00 62.25  ? 286  LEU K CG    1 
ATOM   5592  C  CD1   . LEU B 2 286 ? 140.709 146.605 110.210 1.00 63.27  ? 286  LEU K CD1   1 
ATOM   5593  C  CD2   . LEU B 2 286 ? 140.275 145.721 112.509 1.00 63.97  ? 286  LEU K CD2   1 
ATOM   5594  N  N     . GLN B 2 287 ? 144.400 148.406 114.793 1.00 40.32  ? 287  GLN K N     1 
ATOM   5595  C  CA    . GLN B 2 287 ? 145.815 148.716 114.977 1.00 44.63  ? 287  GLN K CA    1 
ATOM   5596  C  C     . GLN B 2 287 ? 146.611 147.470 115.344 1.00 57.61  ? 287  GLN K C     1 
ATOM   5597  O  O     . GLN B 2 287 ? 147.634 147.159 114.717 1.00 60.28  ? 287  GLN K O     1 
ATOM   5598  C  CB    . GLN B 2 287 ? 145.968 149.795 116.047 1.00 49.93  ? 287  GLN K CB    1 
ATOM   5599  C  CG    . GLN B 2 287 ? 147.370 149.945 116.593 1.00 57.33  ? 287  GLN K CG    1 
ATOM   5600  C  CD    . GLN B 2 287 ? 147.459 151.005 117.667 1.00 54.25  ? 287  GLN K CD    1 
ATOM   5601  O  OE1   . GLN B 2 287 ? 146.574 151.849 117.796 1.00 51.53  ? 287  GLN K OE1   1 
ATOM   5602  N  NE2   . GLN B 2 287 ? 148.532 150.970 118.445 1.00 54.50  ? 287  GLN K NE2   1 
ATOM   5603  N  N     . ASP B 2 288 ? 146.147 146.736 116.358 1.00 63.85  ? 288  ASP K N     1 
ATOM   5604  C  CA    . ASP B 2 288 ? 146.795 145.486 116.731 1.00 60.85  ? 288  ASP K CA    1 
ATOM   5605  C  C     . ASP B 2 288 ? 146.660 144.444 115.631 1.00 61.47  ? 288  ASP K C     1 
ATOM   5606  O  O     . ASP B 2 288 ? 147.476 143.521 115.546 1.00 60.95  ? 288  ASP K O     1 
ATOM   5607  C  CB    . ASP B 2 288 ? 146.204 144.962 118.039 1.00 57.58  ? 288  ASP K CB    1 
ATOM   5608  C  CG    . ASP B 2 288 ? 147.118 143.982 118.742 1.00 66.66  ? 288  ASP K CG    1 
ATOM   5609  O  OD1   . ASP B 2 288 ? 148.168 144.415 119.260 1.00 66.25  ? 288  ASP K OD1   1 
ATOM   5610  O  OD2   . ASP B 2 288 ? 146.788 142.778 118.778 1.00 71.79  ? 288  ASP K OD2   1 
ATOM   5611  N  N     . SER B 2 289 ? 145.636 144.575 114.789 1.00 60.08  ? 289  SER K N     1 
ATOM   5612  C  CA    . SER B 2 289 ? 145.467 143.658 113.669 1.00 52.07  ? 289  SER K CA    1 
ATOM   5613  C  C     . SER B 2 289 ? 146.566 143.847 112.632 1.00 46.95  ? 289  SER K C     1 
ATOM   5614  O  O     . SER B 2 289 ? 147.135 142.871 112.131 1.00 52.21  ? 289  SER K O     1 
ATOM   5615  C  CB    . SER B 2 289 ? 144.092 143.862 113.037 1.00 53.26  ? 289  SER K CB    1 
ATOM   5616  O  OG    . SER B 2 289 ? 143.060 143.601 113.971 1.00 59.06  ? 289  SER K OG    1 
ATOM   5617  N  N     . LEU B 2 290 ? 146.882 145.098 112.302 1.00 50.54  ? 290  LEU K N     1 
ATOM   5618  C  CA    . LEU B 2 290 ? 147.796 145.359 111.198 1.00 55.36  ? 290  LEU K CA    1 
ATOM   5619  C  C     . LEU B 2 290 ? 149.251 145.365 111.646 1.00 60.59  ? 290  LEU K C     1 
ATOM   5620  O  O     . LEU B 2 290 ? 150.131 144.937 110.892 1.00 66.49  ? 290  LEU K O     1 
ATOM   5621  C  CB    . LEU B 2 290 ? 147.440 146.682 110.528 1.00 56.02  ? 290  LEU K CB    1 
ATOM   5622  C  CG    . LEU B 2 290 ? 146.141 146.660 109.727 1.00 59.85  ? 290  LEU K CG    1 
ATOM   5623  C  CD1   . LEU B 2 290 ? 145.829 148.035 109.175 1.00 61.91  ? 290  LEU K CD1   1 
ATOM   5624  C  CD2   . LEU B 2 290 ? 146.231 145.639 108.610 1.00 61.21  ? 290  LEU K CD2   1 
ATOM   5625  N  N     . GLY B 2 291 ? 149.534 145.839 112.855 1.00 62.90  ? 291  GLY K N     1 
ATOM   5626  C  CA    . GLY B 2 291 ? 150.921 145.901 113.272 1.00 60.98  ? 291  GLY K CA    1 
ATOM   5627  C  C     . GLY B 2 291 ? 151.186 145.413 114.679 1.00 63.70  ? 291  GLY K C     1 
ATOM   5628  O  O     . GLY B 2 291 ? 152.097 145.910 115.347 1.00 65.81  ? 291  GLY K O     1 
ATOM   5629  N  N     . GLY B 2 292 ? 150.409 144.441 115.144 1.00 65.19  ? 292  GLY K N     1 
ATOM   5630  C  CA    . GLY B 2 292 ? 150.537 144.007 116.518 1.00 64.73  ? 292  GLY K CA    1 
ATOM   5631  C  C     . GLY B 2 292 ? 150.421 142.516 116.746 1.00 65.24  ? 292  GLY K C     1 
ATOM   5632  O  O     . GLY B 2 292 ? 151.043 141.715 116.044 1.00 69.62  ? 292  GLY K O     1 
ATOM   5633  N  N     . ASN B 2 293 ? 149.622 142.139 117.739 1.00 62.46  ? 293  ASN K N     1 
ATOM   5634  C  CA    . ASN B 2 293 ? 149.519 140.752 118.180 1.00 61.78  ? 293  ASN K CA    1 
ATOM   5635  C  C     . ASN B 2 293 ? 148.300 140.089 117.540 1.00 65.32  ? 293  ASN K C     1 
ATOM   5636  O  O     . ASN B 2 293 ? 147.335 139.708 118.201 1.00 71.31  ? 293  ASN K O     1 
ATOM   5637  C  CB    . ASN B 2 293 ? 149.458 140.695 119.704 1.00 60.39  ? 293  ASN K CB    1 
ATOM   5638  C  CG    . ASN B 2 293 ? 149.454 139.282 120.238 1.00 67.74  ? 293  ASN K CG    1 
ATOM   5639  O  OD1   . ASN B 2 293 ? 149.823 138.340 119.540 1.00 73.50  ? 293  ASN K OD1   1 
ATOM   5640  N  ND2   . ASN B 2 293 ? 149.033 139.125 121.486 1.00 66.40  ? 293  ASN K ND2   1 
ATOM   5641  N  N     . CYS B 2 294 ? 148.363 139.953 116.217 1.00 57.69  ? 294  CYS K N     1 
ATOM   5642  C  CA    . CYS B 2 294 ? 147.292 139.312 115.471 1.00 55.81  ? 294  CYS K CA    1 
ATOM   5643  C  C     . CYS B 2 294 ? 147.879 138.577 114.277 1.00 59.61  ? 294  CYS K C     1 
ATOM   5644  O  O     . CYS B 2 294 ? 148.850 139.030 113.666 1.00 68.87  ? 294  CYS K O     1 
ATOM   5645  C  CB    . CYS B 2 294 ? 146.243 140.321 114.995 1.00 65.28  ? 294  CYS K CB    1 
ATOM   5646  S  SG    . CYS B 2 294 ? 145.209 141.021 116.301 1.00 87.11  ? 294  CYS K SG    1 
ATOM   5647  N  N     . ARG B 2 295 ? 147.280 137.435 113.954 1.00 58.71  ? 295  ARG K N     1 
ATOM   5648  C  CA    . ARG B 2 295 ? 147.590 136.695 112.732 1.00 57.96  ? 295  ARG K CA    1 
ATOM   5649  C  C     . ARG B 2 295 ? 146.511 137.064 111.722 1.00 62.94  ? 295  ARG K C     1 
ATOM   5650  O  O     . ARG B 2 295 ? 145.421 136.494 111.713 1.00 71.27  ? 295  ARG K O     1 
ATOM   5651  C  CB    . ARG B 2 295 ? 147.639 135.195 112.990 1.00 60.60  ? 295  ARG K CB    1 
ATOM   5652  C  CG    . ARG B 2 295 ? 148.377 134.807 114.252 1.00 60.42  ? 295  ARG K CG    1 
ATOM   5653  C  CD    . ARG B 2 295 ? 148.371 133.304 114.450 1.00 62.85  ? 295  ARG K CD    1 
ATOM   5654  N  NE    . ARG B 2 295 ? 149.331 132.638 113.580 1.00 64.43  ? 295  ARG K NE    1 
ATOM   5655  C  CZ    . ARG B 2 295 ? 150.555 132.286 113.949 1.00 64.63  ? 295  ARG K CZ    1 
ATOM   5656  N  NH1   . ARG B 2 295 ? 151.002 132.520 115.171 1.00 67.98  ? 295  ARG K NH1   1 
ATOM   5657  N  NH2   . ARG B 2 295 ? 151.349 131.682 113.070 1.00 64.10  ? 295  ARG K NH2   1 
ATOM   5658  N  N     . THR B 2 296 ? 146.822 138.026 110.864 1.00 46.14  ? 296  THR K N     1 
ATOM   5659  C  CA    . THR B 2 296 ? 145.826 138.643 110.003 1.00 52.10  ? 296  THR K CA    1 
ATOM   5660  C  C     . THR B 2 296 ? 145.955 138.169 108.564 1.00 55.68  ? 296  THR K C     1 
ATOM   5661  O  O     . THR B 2 296 ? 147.062 138.002 108.044 1.00 67.74  ? 296  THR K O     1 
ATOM   5662  C  CB    . THR B 2 296 ? 145.934 140.167 110.064 1.00 61.38  ? 296  THR K CB    1 
ATOM   5663  O  OG1   . THR B 2 296 ? 145.032 140.757 109.118 1.00 63.83  ? 296  THR K OG1   1 
ATOM   5664  C  CG2   . THR B 2 296 ? 147.338 140.620 109.798 1.00 60.66  ? 296  THR K CG2   1 
ATOM   5665  N  N     . THR B 2 297 ? 144.808 137.934 107.933 1.00 51.59  ? 297  THR K N     1 
ATOM   5666  C  CA    . THR B 2 297 ? 144.719 137.614 106.516 1.00 52.37  ? 297  THR K CA    1 
ATOM   5667  C  C     . THR B 2 297 ? 143.777 138.609 105.858 1.00 53.95  ? 297  THR K C     1 
ATOM   5668  O  O     . THR B 2 297 ? 142.681 138.860 106.367 1.00 62.36  ? 297  THR K O     1 
ATOM   5669  C  CB    . THR B 2 297 ? 144.210 136.187 106.288 1.00 57.01  ? 297  THR K CB    1 
ATOM   5670  O  OG1   . THR B 2 297 ? 142.785 136.158 106.425 1.00 65.32  ? 297  THR K OG1   1 
ATOM   5671  C  CG2   . THR B 2 297 ? 144.826 135.226 107.293 1.00 55.38  ? 297  THR K CG2   1 
ATOM   5672  N  N     . ILE B 2 298 ? 144.199 139.170 104.730 1.00 44.47  ? 298  ILE K N     1 
ATOM   5673  C  CA    . ILE B 2 298 ? 143.388 140.104 103.960 1.00 40.54  ? 298  ILE K CA    1 
ATOM   5674  C  C     . ILE B 2 298 ? 142.879 139.370 102.730 1.00 52.12  ? 298  ILE K C     1 
ATOM   5675  O  O     . ILE B 2 298 ? 143.670 138.813 101.959 1.00 64.10  ? 298  ILE K O     1 
ATOM   5676  C  CB    . ILE B 2 298 ? 144.182 141.354 103.558 1.00 42.94  ? 298  ILE K CB    1 
ATOM   5677  C  CG1   . ILE B 2 298 ? 144.890 141.956 104.767 1.00 50.38  ? 298  ILE K CG1   1 
ATOM   5678  C  CG2   . ILE B 2 298 ? 143.267 142.381 102.920 1.00 48.48  ? 298  ILE K CG2   1 
ATOM   5679  C  CD1   . ILE B 2 298 ? 145.729 143.160 104.431 1.00 54.74  ? 298  ILE K CD1   1 
ATOM   5680  N  N     . VAL B 2 299 ? 141.565 139.364 102.544 1.00 50.55  ? 299  VAL K N     1 
ATOM   5681  C  CA    . VAL B 2 299 ? 140.942 138.736 101.382 1.00 44.90  ? 299  VAL K CA    1 
ATOM   5682  C  C     . VAL B 2 299 ? 140.561 139.873 100.441 1.00 45.87  ? 299  VAL K C     1 
ATOM   5683  O  O     . VAL B 2 299 ? 139.479 140.452 100.536 1.00 54.43  ? 299  VAL K O     1 
ATOM   5684  C  CB    . VAL B 2 299 ? 139.739 137.880 101.768 1.00 47.96  ? 299  VAL K CB    1 
ATOM   5685  C  CG1   . VAL B 2 299 ? 139.162 137.201 100.543 1.00 46.28  ? 299  VAL K CG1   1 
ATOM   5686  C  CG2   . VAL B 2 299 ? 140.136 136.857 102.805 1.00 47.49  ? 299  VAL K CG2   1 
ATOM   5687  N  N     . ILE B 2 300 ? 141.458 140.198 99.518  1.00 41.27  ? 300  ILE K N     1 
ATOM   5688  C  CA    . ILE B 2 300 ? 141.185 141.246 98.542  1.00 42.60  ? 300  ILE K CA    1 
ATOM   5689  C  C     . ILE B 2 300 ? 140.349 140.661 97.414  1.00 51.53  ? 300  ILE K C     1 
ATOM   5690  O  O     . ILE B 2 300 ? 140.667 139.596 96.872  1.00 60.09  ? 300  ILE K O     1 
ATOM   5691  C  CB    . ILE B 2 300 ? 142.488 141.867 98.016  1.00 47.10  ? 300  ILE K CB    1 
ATOM   5692  C  CG1   . ILE B 2 300 ? 143.431 140.795 97.482  1.00 48.86  ? 300  ILE K CG1   1 
ATOM   5693  C  CG2   . ILE B 2 300 ? 143.176 142.662 99.109  1.00 55.35  ? 300  ILE K CG2   1 
ATOM   5694  C  CD1   . ILE B 2 300 ? 144.707 141.358 96.918  1.00 52.62  ? 300  ILE K CD1   1 
ATOM   5695  N  N     . CYS B 2 301 ? 139.265 141.345 97.070  1.00 49.49  ? 301  CYS K N     1 
ATOM   5696  C  CA    . CYS B 2 301 ? 138.361 140.909 96.019  1.00 52.35  ? 301  CYS K CA    1 
ATOM   5697  C  C     . CYS B 2 301 ? 138.446 141.873 94.846  1.00 55.21  ? 301  CYS K C     1 
ATOM   5698  O  O     . CYS B 2 301 ? 138.462 143.093 95.032  1.00 56.53  ? 301  CYS K O     1 
ATOM   5699  C  CB    . CYS B 2 301 ? 136.926 140.824 96.535  1.00 52.71  ? 301  CYS K CB    1 
ATOM   5700  S  SG    . CYS B 2 301 ? 136.722 139.704 97.931  1.00 65.59  ? 301  CYS K SG    1 
ATOM   5701  N  N     . CYS B 2 302 ? 138.498 141.322 93.635  1.00 52.47  ? 302  CYS K N     1 
ATOM   5702  C  CA    . CYS B 2 302 ? 138.746 142.115 92.442  1.00 51.92  ? 302  CYS K CA    1 
ATOM   5703  C  C     . CYS B 2 302 ? 137.778 141.719 91.338  1.00 54.00  ? 302  CYS K C     1 
ATOM   5704  O  O     . CYS B 2 302 ? 137.259 140.601 91.315  1.00 59.02  ? 302  CYS K O     1 
ATOM   5705  C  CB    . CYS B 2 302 ? 140.188 141.940 91.958  1.00 55.43  ? 302  CYS K CB    1 
ATOM   5706  S  SG    . CYS B 2 302 ? 141.421 142.159 93.253  1.00 72.79  ? 302  CYS K SG    1 
ATOM   5707  N  N     . SER B 2 303 ? 137.541 142.657 90.420  1.00 58.82  ? 303  SER K N     1 
ATOM   5708  C  CA    . SER B 2 303 ? 136.709 142.430 89.246  1.00 60.64  ? 303  SER K CA    1 
ATOM   5709  C  C     . SER B 2 303 ? 137.588 142.166 88.037  1.00 63.79  ? 303  SER K C     1 
ATOM   5710  O  O     . SER B 2 303 ? 138.591 142.867 87.844  1.00 68.19  ? 303  SER K O     1 
ATOM   5711  C  CB    . SER B 2 303 ? 135.817 143.637 88.980  1.00 61.54  ? 303  SER K CB    1 
ATOM   5712  O  OG    . SER B 2 303 ? 134.931 143.386 87.903  1.00 68.28  ? 303  SER K OG    1 
ATOM   5713  N  N     . PRO B 2 304 ? 137.257 141.184 87.202  1.00 55.12  ? 304  PRO K N     1 
ATOM   5714  C  CA    . PRO B 2 304 ? 138.120 140.826 86.069  1.00 51.72  ? 304  PRO K CA    1 
ATOM   5715  C  C     . PRO B 2 304 ? 137.836 141.571 84.773  1.00 59.33  ? 304  PRO K C     1 
ATOM   5716  O  O     . PRO B 2 304 ? 138.329 141.143 83.726  1.00 64.30  ? 304  PRO K O     1 
ATOM   5717  C  CB    . PRO B 2 304 ? 137.817 139.334 85.897  1.00 51.93  ? 304  PRO K CB    1 
ATOM   5718  C  CG    . PRO B 2 304 ? 136.409 139.166 86.393  1.00 56.16  ? 304  PRO K CG    1 
ATOM   5719  C  CD    . PRO B 2 304 ? 136.046 140.353 87.245  1.00 55.47  ? 304  PRO K CD    1 
ATOM   5720  N  N     . SER B 2 305 ? 137.074 142.657 84.806  1.00 59.76  ? 305  SER K N     1 
ATOM   5721  C  CA    . SER B 2 305 ? 136.667 143.345 83.593  1.00 59.41  ? 305  SER K CA    1 
ATOM   5722  C  C     . SER B 2 305 ? 137.615 144.489 83.265  1.00 64.49  ? 305  SER K C     1 
ATOM   5723  O  O     . SER B 2 305 ? 138.311 145.015 84.137  1.00 70.32  ? 305  SER K O     1 
ATOM   5724  C  CB    . SER B 2 305 ? 135.246 143.880 83.734  1.00 60.68  ? 305  SER K CB    1 
ATOM   5725  O  OG    . SER B 2 305 ? 134.897 144.684 82.625  1.00 68.67  ? 305  SER K OG    1 
ATOM   5726  N  N     . SER B 2 306 ? 137.637 144.869 81.986  1.00 60.83  ? 306  SER K N     1 
ATOM   5727  C  CA    . SER B 2 306 ? 138.438 146.008 81.557  1.00 56.26  ? 306  SER K CA    1 
ATOM   5728  C  C     . SER B 2 306 ? 137.848 147.329 82.024  1.00 54.77  ? 306  SER K C     1 
ATOM   5729  O  O     . SER B 2 306 ? 138.572 148.327 82.104  1.00 62.70  ? 306  SER K O     1 
ATOM   5730  C  CB    . SER B 2 306 ? 138.583 146.009 80.037  1.00 60.67  ? 306  SER K CB    1 
ATOM   5731  O  OG    . SER B 2 306 ? 137.324 146.164 79.406  1.00 66.14  ? 306  SER K OG    1 
ATOM   5732  N  N     . TYR B 2 307 ? 136.553 147.357 82.332  1.00 49.96  ? 307  TYR K N     1 
ATOM   5733  C  CA    . TYR B 2 307 ? 135.922 148.549 82.876  1.00 53.49  ? 307  TYR K CA    1 
ATOM   5734  C  C     . TYR B 2 307 ? 136.419 148.888 84.273  1.00 64.31  ? 307  TYR K C     1 
ATOM   5735  O  O     . TYR B 2 307 ? 136.191 150.009 84.739  1.00 66.25  ? 307  TYR K O     1 
ATOM   5736  C  CB    . TYR B 2 307 ? 134.405 148.359 82.892  1.00 58.57  ? 307  TYR K CB    1 
ATOM   5737  C  CG    . TYR B 2 307 ? 133.611 149.616 83.146  1.00 60.42  ? 307  TYR K CG    1 
ATOM   5738  C  CD1   . TYR B 2 307 ? 133.591 150.646 82.219  1.00 61.79  ? 307  TYR K CD1   1 
ATOM   5739  C  CD2   . TYR B 2 307 ? 132.860 149.762 84.301  1.00 62.70  ? 307  TYR K CD2   1 
ATOM   5740  C  CE1   . TYR B 2 307 ? 132.860 151.792 82.444  1.00 63.75  ? 307  TYR K CE1   1 
ATOM   5741  C  CE2   . TYR B 2 307 ? 132.126 150.902 84.534  1.00 66.11  ? 307  TYR K CE2   1 
ATOM   5742  C  CZ    . TYR B 2 307 ? 132.127 151.913 83.603  1.00 66.22  ? 307  TYR K CZ    1 
ATOM   5743  O  OH    . TYR B 2 307 ? 131.395 153.054 83.833  1.00 63.45  ? 307  TYR K OH    1 
ATOM   5744  N  N     . ASN B 2 308 ? 137.089 147.956 84.944  1.00 69.11  ? 308  ASN K N     1 
ATOM   5745  C  CA    . ASN B 2 308 ? 137.577 148.127 86.306  1.00 60.88  ? 308  ASN K CA    1 
ATOM   5746  C  C     . ASN B 2 308 ? 139.048 147.760 86.400  1.00 59.87  ? 308  ASN K C     1 
ATOM   5747  O  O     . ASN B 2 308 ? 139.496 147.165 87.382  1.00 67.89  ? 308  ASN K O     1 
ATOM   5748  C  CB    . ASN B 2 308 ? 136.759 147.290 87.284  1.00 58.35  ? 308  ASN K CB    1 
ATOM   5749  C  CG    . ASN B 2 308 ? 135.275 147.551 87.175  1.00 62.80  ? 308  ASN K CG    1 
ATOM   5750  O  OD1   . ASN B 2 308 ? 134.753 148.485 87.780  1.00 67.02  ? 308  ASN K OD1   1 
ATOM   5751  N  ND2   . ASN B 2 308 ? 134.585 146.722 86.404  1.00 61.95  ? 308  ASN K ND2   1 
ATOM   5752  N  N     . GLU B 2 309 ? 139.826 148.100 85.373  1.00 61.78  ? 309  GLU K N     1 
ATOM   5753  C  CA    . GLU B 2 309 ? 141.231 147.709 85.364  1.00 59.52  ? 309  GLU K CA    1 
ATOM   5754  C  C     . GLU B 2 309 ? 142.047 148.551 86.335  1.00 67.56  ? 309  GLU K C     1 
ATOM   5755  O  O     . GLU B 2 309 ? 142.900 148.020 87.056  1.00 76.81  ? 309  GLU K O     1 
ATOM   5756  C  CB    . GLU B 2 309 ? 141.797 147.818 83.951  1.00 60.10  ? 309  GLU K CB    1 
ATOM   5757  C  CG    . GLU B 2 309 ? 143.210 147.288 83.808  1.00 69.75  ? 309  GLU K CG    1 
ATOM   5758  C  CD    . GLU B 2 309 ? 143.821 147.621 82.462  1.00 76.24  ? 309  GLU K CD    1 
ATOM   5759  O  OE1   . GLU B 2 309 ? 143.246 148.460 81.737  1.00 74.37  ? 309  GLU K OE1   1 
ATOM   5760  O  OE2   . GLU B 2 309 ? 144.877 147.043 82.128  1.00 75.31  ? 309  GLU K OE2   1 
ATOM   5761  N  N     . SER B 2 310 ? 141.803 149.863 86.369  1.00 62.17  ? 310  SER K N     1 
ATOM   5762  C  CA    . SER B 2 310 ? 142.551 150.730 87.274  1.00 62.86  ? 310  SER K CA    1 
ATOM   5763  C  C     . SER B 2 310 ? 142.287 150.373 88.731  1.00 65.15  ? 310  SER K C     1 
ATOM   5764  O  O     . SER B 2 310 ? 143.220 150.297 89.541  1.00 66.10  ? 310  SER K O     1 
ATOM   5765  C  CB    . SER B 2 310 ? 142.197 152.190 87.004  1.00 62.23  ? 310  SER K CB    1 
ATOM   5766  O  OG    . SER B 2 310 ? 142.917 153.056 87.865  1.00 70.85  ? 310  SER K OG    1 
ATOM   5767  N  N     . GLU B 2 311 ? 141.021 150.144 89.083  1.00 60.22  ? 311  GLU K N     1 
ATOM   5768  C  CA    . GLU B 2 311 ? 140.693 149.766 90.453  1.00 58.39  ? 311  GLU K CA    1 
ATOM   5769  C  C     . GLU B 2 311 ? 141.282 148.408 90.806  1.00 57.53  ? 311  GLU K C     1 
ATOM   5770  O  O     . GLU B 2 311 ? 141.758 148.203 91.929  1.00 67.58  ? 311  GLU K O     1 
ATOM   5771  C  CB    . GLU B 2 311 ? 139.179 149.764 90.649  1.00 64.70  ? 311  GLU K CB    1 
ATOM   5772  C  CG    . GLU B 2 311 ? 138.543 151.140 90.578  1.00 66.33  ? 311  GLU K CG    1 
ATOM   5773  C  CD    . GLU B 2 311 ? 138.301 151.598 89.154  1.00 72.53  ? 311  GLU K CD    1 
ATOM   5774  O  OE1   . GLU B 2 311 ? 138.476 150.781 88.226  1.00 71.05  ? 311  GLU K OE1   1 
ATOM   5775  O  OE2   . GLU B 2 311 ? 137.935 152.776 88.962  1.00 72.15  ? 311  GLU K OE2   1 
ATOM   5776  N  N     . THR B 2 312 ? 141.251 147.463 89.864  1.00 54.01  ? 312  THR K N     1 
ATOM   5777  C  CA    . THR B 2 312 ? 141.844 146.155 90.119  1.00 52.36  ? 312  THR K CA    1 
ATOM   5778  C  C     . THR B 2 312 ? 143.342 146.271 90.357  1.00 54.05  ? 312  THR K C     1 
ATOM   5779  O  O     . THR B 2 312 ? 143.885 145.625 91.258  1.00 64.01  ? 312  THR K O     1 
ATOM   5780  C  CB    . THR B 2 312 ? 141.558 145.205 88.958  1.00 54.08  ? 312  THR K CB    1 
ATOM   5781  O  OG1   . THR B 2 312 ? 140.150 145.168 88.707  1.00 61.00  ? 312  THR K OG1   1 
ATOM   5782  C  CG2   . THR B 2 312 ? 142.035 143.805 89.292  1.00 58.55  ? 312  THR K CG2   1 
ATOM   5783  N  N     . LYS B 2 313 ? 144.027 147.100 89.568  1.00 50.68  ? 313  LYS K N     1 
ATOM   5784  C  CA    . LYS B 2 313 ? 145.459 147.288 89.769  1.00 53.37  ? 313  LYS K CA    1 
ATOM   5785  C  C     . LYS B 2 313 ? 145.749 147.960 91.106  1.00 59.51  ? 313  LYS K C     1 
ATOM   5786  O  O     . LYS B 2 313 ? 146.718 147.604 91.786  1.00 64.11  ? 313  LYS K O     1 
ATOM   5787  C  CB    . LYS B 2 313 ? 146.049 148.095 88.613  1.00 56.24  ? 313  LYS K CB    1 
ATOM   5788  C  CG    . LYS B 2 313 ? 145.984 147.379 87.273  1.00 58.17  ? 313  LYS K CG    1 
ATOM   5789  C  CD    . LYS B 2 313 ? 146.219 148.332 86.116  1.00 58.80  ? 313  LYS K CD    1 
ATOM   5790  C  CE    . LYS B 2 313 ? 147.699 148.491 85.826  1.00 63.81  ? 313  LYS K CE    1 
ATOM   5791  N  NZ    . LYS B 2 313 ? 148.298 147.223 85.330  1.00 64.48  ? 313  LYS K NZ    1 
ATOM   5792  N  N     . SER B 2 314 ? 144.924 148.933 91.501  1.00 59.70  ? 314  SER K N     1 
ATOM   5793  C  CA    . SER B 2 314 ? 145.109 149.567 92.804  1.00 52.65  ? 314  SER K CA    1 
ATOM   5794  C  C     . SER B 2 314 ? 144.927 148.565 93.939  1.00 53.66  ? 314  SER K C     1 
ATOM   5795  O  O     . SER B 2 314 ? 145.721 148.537 94.889  1.00 57.83  ? 314  SER K O     1 
ATOM   5796  C  CB    . SER B 2 314 ? 144.136 150.734 92.963  1.00 52.70  ? 314  SER K CB    1 
ATOM   5797  O  OG    . SER B 2 314 ? 144.341 151.709 91.957  1.00 58.87  ? 314  SER K OG    1 
ATOM   5798  N  N     . THR B 2 315 ? 143.888 147.731 93.855  1.00 53.85  ? 315  THR K N     1 
ATOM   5799  C  CA    . THR B 2 315 ? 143.671 146.705 94.870  1.00 50.50  ? 315  THR K CA    1 
ATOM   5800  C  C     . THR B 2 315 ? 144.826 145.712 94.900  1.00 54.69  ? 315  THR K C     1 
ATOM   5801  O  O     . THR B 2 315 ? 145.254 145.275 95.975  1.00 64.70  ? 315  THR K O     1 
ATOM   5802  C  CB    . THR B 2 315 ? 142.352 145.980 94.607  1.00 49.30  ? 315  THR K CB    1 
ATOM   5803  O  OG1   . THR B 2 315 ? 141.305 146.937 94.415  1.00 51.34  ? 315  THR K OG1   1 
ATOM   5804  C  CG2   . THR B 2 315 ? 141.997 145.082 95.776  1.00 54.95  ? 315  THR K CG2   1 
ATOM   5805  N  N     . LEU B 2 316 ? 145.335 145.340 93.726  1.00 48.29  ? 316  LEU K N     1 
ATOM   5806  C  CA    . LEU B 2 316 ? 146.460 144.418 93.655  1.00 45.46  ? 316  LEU K CA    1 
ATOM   5807  C  C     . LEU B 2 316 ? 147.699 145.012 94.309  1.00 52.63  ? 316  LEU K C     1 
ATOM   5808  O  O     . LEU B 2 316 ? 148.421 144.319 95.034  1.00 60.52  ? 316  LEU K O     1 
ATOM   5809  C  CB    . LEU B 2 316 ? 146.747 144.063 92.197  1.00 54.47  ? 316  LEU K CB    1 
ATOM   5810  C  CG    . LEU B 2 316 ? 146.077 142.837 91.577  1.00 57.72  ? 316  LEU K CG    1 
ATOM   5811  C  CD1   . LEU B 2 316 ? 146.873 141.592 91.872  1.00 63.26  ? 316  LEU K CD1   1 
ATOM   5812  C  CD2   . LEU B 2 316 ? 144.660 142.671 92.065  1.00 55.51  ? 316  LEU K CD2   1 
ATOM   5813  N  N     . LEU B 2 317 ? 147.968 146.294 94.057  1.00 55.95  ? 317  LEU K N     1 
ATOM   5814  C  CA    . LEU B 2 317 ? 149.114 146.946 94.682  1.00 53.72  ? 317  LEU K CA    1 
ATOM   5815  C  C     . LEU B 2 317 ? 148.940 147.031 96.192  1.00 56.24  ? 317  LEU K C     1 
ATOM   5816  O  O     . LEU B 2 317 ? 149.904 146.852 96.946  1.00 59.76  ? 317  LEU K O     1 
ATOM   5817  C  CB    . LEU B 2 317 ? 149.320 148.335 94.083  1.00 56.07  ? 317  LEU K CB    1 
ATOM   5818  C  CG    . LEU B 2 317 ? 149.750 148.372 92.618  1.00 60.58  ? 317  LEU K CG    1 
ATOM   5819  C  CD1   . LEU B 2 317 ? 149.875 149.805 92.131  1.00 55.85  ? 317  LEU K CD1   1 
ATOM   5820  C  CD2   . LEU B 2 317 ? 151.055 147.620 92.425  1.00 59.52  ? 317  LEU K CD2   1 
ATOM   5821  N  N     . PHE B 2 318 ? 147.717 147.306 96.652  1.00 57.31  ? 318  PHE K N     1 
ATOM   5822  C  CA    . PHE B 2 318 ? 147.453 147.321 98.088  1.00 50.74  ? 318  PHE K CA    1 
ATOM   5823  C  C     . PHE B 2 318 ? 147.722 145.956 98.707  1.00 49.61  ? 318  PHE K C     1 
ATOM   5824  O  O     . PHE B 2 318 ? 148.337 145.854 99.774  1.00 55.15  ? 318  PHE K O     1 
ATOM   5825  C  CB    . PHE B 2 318 ? 146.012 147.753 98.354  1.00 49.45  ? 318  PHE K CB    1 
ATOM   5826  C  CG    . PHE B 2 318 ? 145.618 147.689 99.800  1.00 49.64  ? 318  PHE K CG    1 
ATOM   5827  C  CD1   . PHE B 2 318 ? 145.916 148.728 100.657 1.00 55.63  ? 318  PHE K CD1   1 
ATOM   5828  C  CD2   . PHE B 2 318 ? 144.942 146.591 100.299 1.00 53.44  ? 318  PHE K CD2   1 
ATOM   5829  C  CE1   . PHE B 2 318 ? 145.553 148.672 101.984 1.00 57.77  ? 318  PHE K CE1   1 
ATOM   5830  C  CE2   . PHE B 2 318 ? 144.579 146.530 101.626 1.00 56.37  ? 318  PHE K CE2   1 
ATOM   5831  C  CZ    . PHE B 2 318 ? 144.884 147.570 102.468 1.00 54.63  ? 318  PHE K CZ    1 
ATOM   5832  N  N     . GLY B 2 319 ? 147.259 144.894 98.050  1.00 55.41  ? 319  GLY K N     1 
ATOM   5833  C  CA    . GLY B 2 319 ? 147.499 143.557 98.567  1.00 54.57  ? 319  GLY K CA    1 
ATOM   5834  C  C     . GLY B 2 319 ? 148.968 143.182 98.557  1.00 54.66  ? 319  GLY K C     1 
ATOM   5835  O  O     . GLY B 2 319 ? 149.452 142.502 99.465  1.00 63.27  ? 319  GLY K O     1 
ATOM   5836  N  N     . GLN B 2 320 ? 149.694 143.610 97.525  1.00 51.47  ? 320  GLN K N     1 
ATOM   5837  C  CA    . GLN B 2 320 ? 151.115 143.300 97.438  1.00 48.43  ? 320  GLN K CA    1 
ATOM   5838  C  C     . GLN B 2 320 ? 151.908 144.039 98.507  1.00 53.40  ? 320  GLN K C     1 
ATOM   5839  O  O     . GLN B 2 320 ? 152.848 143.485 99.088  1.00 53.16  ? 320  GLN K O     1 
ATOM   5840  C  CB    . GLN B 2 320 ? 151.634 143.647 96.045  1.00 50.74  ? 320  GLN K CB    1 
ATOM   5841  C  CG    . GLN B 2 320 ? 152.846 142.851 95.617  1.00 53.00  ? 320  GLN K CG    1 
ATOM   5842  C  CD    . GLN B 2 320 ? 153.222 143.110 94.177  1.00 59.39  ? 320  GLN K CD    1 
ATOM   5843  O  OE1   . GLN B 2 320 ? 152.742 144.060 93.561  1.00 56.99  ? 320  GLN K OE1   1 
ATOM   5844  N  NE2   . GLN B 2 320 ? 154.086 142.265 93.629  1.00 62.21  ? 320  GLN K NE2   1 
ATOM   5845  N  N     . ARG B 2 321 ? 151.550 145.297 98.774  1.00 58.83  ? 321  ARG K N     1 
ATOM   5846  C  CA    . ARG B 2 321 ? 152.256 146.065 99.795  1.00 52.77  ? 321  ARG K CA    1 
ATOM   5847  C  C     . ARG B 2 321 ? 151.981 145.520 101.191 1.00 54.59  ? 321  ARG K C     1 
ATOM   5848  O  O     . ARG B 2 321 ? 152.876 145.502 102.042 1.00 60.78  ? 321  ARG K O     1 
ATOM   5849  C  CB    . ARG B 2 321 ? 151.865 147.539 99.708  1.00 52.77  ? 321  ARG K CB    1 
ATOM   5850  C  CG    . ARG B 2 321 ? 153.026 148.462 99.395  1.00 56.85  ? 321  ARG K CG    1 
ATOM   5851  C  CD    . ARG B 2 321 ? 152.645 149.921 99.561  1.00 60.58  ? 321  ARG K CD    1 
ATOM   5852  N  NE    . ARG B 2 321 ? 151.694 150.363 98.548  1.00 60.70  ? 321  ARG K NE    1 
ATOM   5853  C  CZ    . ARG B 2 321 ? 150.402 150.556 98.770  1.00 62.92  ? 321  ARG K CZ    1 
ATOM   5854  N  NH1   . ARG B 2 321 ? 149.867 150.350 99.962  1.00 61.09  ? 321  ARG K NH1   1 
ATOM   5855  N  NH2   . ARG B 2 321 ? 149.627 150.966 97.771  1.00 59.61  ? 321  ARG K NH2   1 
ATOM   5856  N  N     . ALA B 2 322 ? 150.748 145.078 101.445 1.00 51.01  ? 322  ALA K N     1 
ATOM   5857  C  CA    . ALA B 2 322 ? 150.407 144.555 102.763 1.00 47.90  ? 322  ALA K CA    1 
ATOM   5858  C  C     . ALA B 2 322 ? 151.139 143.257 103.063 1.00 51.40  ? 322  ALA K C     1 
ATOM   5859  O  O     . ALA B 2 322 ? 151.484 142.998 104.220 1.00 61.47  ? 322  ALA K O     1 
ATOM   5860  C  CB    . ALA B 2 322 ? 148.899 144.346 102.874 1.00 47.82  ? 322  ALA K CB    1 
ATOM   5861  N  N     . LYS B 2 323 ? 151.390 142.435 102.044 1.00 48.98  ? 323  LYS K N     1 
ATOM   5862  C  CA    . LYS B 2 323 ? 152.009 141.134 102.263 1.00 47.32  ? 323  LYS K CA    1 
ATOM   5863  C  C     . LYS B 2 323 ? 153.404 141.248 102.861 1.00 46.53  ? 323  LYS K C     1 
ATOM   5864  O  O     . LYS B 2 323 ? 153.879 140.293 103.483 1.00 47.79  ? 323  LYS K O     1 
ATOM   5865  C  CB    . LYS B 2 323 ? 152.063 140.365 100.944 1.00 53.65  ? 323  LYS K CB    1 
ATOM   5866  C  CG    . LYS B 2 323 ? 152.108 138.863 101.092 1.00 51.11  ? 323  LYS K CG    1 
ATOM   5867  C  CD    . LYS B 2 323 ? 152.079 138.191 99.736  1.00 54.66  ? 323  LYS K CD    1 
ATOM   5868  C  CE    . LYS B 2 323 ? 153.398 138.368 99.010  1.00 57.35  ? 323  LYS K CE    1 
ATOM   5869  N  NZ    . LYS B 2 323 ? 154.502 137.634 99.687  1.00 55.44  ? 323  LYS K NZ    1 
ATOM   5870  N  N     . THR B 2 324 ? 154.067 142.391 102.691 1.00 48.38  ? 324  THR K N     1 
ATOM   5871  C  CA    . THR B 2 324 ? 155.431 142.549 103.179 1.00 47.97  ? 324  THR K CA    1 
ATOM   5872  C  C     . THR B 2 324 ? 155.489 142.905 104.659 1.00 50.56  ? 324  THR K C     1 
ATOM   5873  O  O     . THR B 2 324 ? 156.510 142.654 105.307 1.00 51.87  ? 324  THR K O     1 
ATOM   5874  C  CB    . THR B 2 324 ? 156.159 143.617 102.365 1.00 48.13  ? 324  THR K CB    1 
ATOM   5875  O  OG1   . THR B 2 324 ? 155.511 144.881 102.547 1.00 55.27  ? 324  THR K OG1   1 
ATOM   5876  C  CG2   . THR B 2 324 ? 156.150 143.258 100.890 1.00 44.31  ? 324  THR K CG2   1 
ATOM   5877  N  N     . ILE B 2 325 ? 154.425 143.487 105.213 1.00 50.83  ? 325  ILE K N     1 
ATOM   5878  C  CA    . ILE B 2 325 ? 154.483 143.961 106.589 1.00 45.70  ? 325  ILE K CA    1 
ATOM   5879  C  C     . ILE B 2 325 ? 154.384 142.779 107.546 1.00 48.04  ? 325  ILE K C     1 
ATOM   5880  O  O     . ILE B 2 325 ? 153.735 141.764 107.260 1.00 48.24  ? 325  ILE K O     1 
ATOM   5881  C  CB    . ILE B 2 325 ? 153.386 145.007 106.854 1.00 40.57  ? 325  ILE K CB    1 
ATOM   5882  C  CG1   . ILE B 2 325 ? 152.032 144.353 107.059 1.00 42.64  ? 325  ILE K CG1   1 
ATOM   5883  C  CG2   . ILE B 2 325 ? 153.262 145.926 105.671 1.00 45.13  ? 325  ILE K CG2   1 
ATOM   5884  C  CD1   . ILE B 2 325 ? 151.007 145.259 107.679 1.00 49.02  ? 325  ILE K CD1   1 
ATOM   5885  N  N     . LYS B 2 326 ? 155.051 142.903 108.689 1.00 58.75  ? 326  LYS K N     1 
ATOM   5886  C  CA    . LYS B 2 326 ? 155.226 141.802 109.623 1.00 55.66  ? 326  LYS K CA    1 
ATOM   5887  C  C     . LYS B 2 326 ? 154.451 142.055 110.906 1.00 61.86  ? 326  LYS K C     1 
ATOM   5888  O  O     . LYS B 2 326 ? 154.198 143.202 111.287 1.00 69.43  ? 326  LYS K O     1 
ATOM   5889  C  CB    . LYS B 2 326 ? 156.703 141.590 109.961 1.00 51.99  ? 326  LYS K CB    1 
ATOM   5890  C  CG    . LYS B 2 326 ? 157.514 140.988 108.836 1.00 56.06  ? 326  LYS K CG    1 
ATOM   5891  C  CD    . LYS B 2 326 ? 158.923 140.674 109.284 1.00 58.99  ? 326  LYS K CD    1 
ATOM   5892  C  CE    . LYS B 2 326 ? 159.663 139.894 108.218 1.00 58.35  ? 326  LYS K CE    1 
ATOM   5893  N  NZ    . LYS B 2 326 ? 161.032 139.515 108.655 1.00 58.98  ? 326  LYS K NZ    1 
ATOM   5894  N  N     . ASN B 2 327 ? 154.081 140.966 111.570 1.00 59.56  ? 327  ASN K N     1 
ATOM   5895  C  CA    . ASN B 2 327 ? 153.383 141.010 112.842 1.00 55.74  ? 327  ASN K CA    1 
ATOM   5896  C  C     . ASN B 2 327 ? 154.189 140.283 113.909 1.00 63.18  ? 327  ASN K C     1 
ATOM   5897  O  O     . ASN B 2 327 ? 154.927 139.337 113.627 1.00 68.28  ? 327  ASN K O     1 
ATOM   5898  C  CB    . ASN B 2 327 ? 151.992 140.385 112.730 1.00 54.67  ? 327  ASN K CB    1 
ATOM   5899  C  CG    . ASN B 2 327 ? 150.975 141.332 112.147 1.00 60.94  ? 327  ASN K CG    1 
ATOM   5900  O  OD1   . ASN B 2 327 ? 150.207 140.964 111.262 1.00 65.69  ? 327  ASN K OD1   1 
ATOM   5901  N  ND2   . ASN B 2 327 ? 150.957 142.560 112.644 1.00 64.30  ? 327  ASN K ND2   1 
ATOM   5902  N  N     . THR B 2 328 ? 154.036 140.743 115.146 1.00 69.47  ? 328  THR K N     1 
ATOM   5903  C  CA    . THR B 2 328 ? 154.664 140.128 116.312 1.00 69.62  ? 328  THR K CA    1 
ATOM   5904  C  C     . THR B 2 328 ? 153.548 139.507 117.145 1.00 69.42  ? 328  THR K C     1 
ATOM   5905  O  O     . THR B 2 328 ? 152.833 140.216 117.859 1.00 73.09  ? 328  THR K O     1 
ATOM   5906  C  CB    . THR B 2 328 ? 155.458 141.155 117.112 1.00 70.46  ? 328  THR K CB    1 
ATOM   5907  O  OG1   . THR B 2 328 ? 154.598 142.239 117.485 1.00 70.00  ? 328  THR K OG1   1 
ATOM   5908  C  CG2   . THR B 2 328 ? 156.613 141.694 116.282 1.00 69.68  ? 328  THR K CG2   1 
ATOM   5909  N  N     . VAL B 2 329 ? 153.398 138.189 117.057 1.00 62.21  ? 329  VAL K N     1 
ATOM   5910  C  CA    . VAL B 2 329 ? 152.264 137.480 117.640 1.00 61.46  ? 329  VAL K CA    1 
ATOM   5911  C  C     . VAL B 2 329 ? 152.756 136.599 118.779 1.00 69.66  ? 329  VAL K C     1 
ATOM   5912  O  O     . VAL B 2 329 ? 153.727 135.850 118.621 1.00 73.66  ? 329  VAL K O     1 
ATOM   5913  C  CB    . VAL B 2 329 ? 151.523 136.645 116.584 1.00 60.48  ? 329  VAL K CB    1 
ATOM   5914  C  CG1   . VAL B 2 329 ? 150.245 136.080 117.165 1.00 63.50  ? 329  VAL K CG1   1 
ATOM   5915  C  CG2   . VAL B 2 329 ? 151.219 137.497 115.372 1.00 67.47  ? 329  VAL K CG2   1 
ATOM   5916  N  N     . CYS B 2 330 ? 152.080 136.690 119.925 1.00 70.84  ? 330  CYS K N     1 
ATOM   5917  C  CA    . CYS B 2 330 ? 152.406 135.897 121.100 1.00 65.31  ? 330  CYS K CA    1 
ATOM   5918  C  C     . CYS B 2 330 ? 151.119 135.375 121.722 1.00 61.54  ? 330  CYS K C     1 
ATOM   5919  O  O     . CYS B 2 330 ? 150.039 135.935 121.525 1.00 64.73  ? 330  CYS K O     1 
ATOM   5920  C  CB    . CYS B 2 330 ? 153.202 136.711 122.128 1.00 67.95  ? 330  CYS K CB    1 
ATOM   5921  S  SG    . CYS B 2 330 ? 152.360 138.197 122.716 1.00 76.72  ? 330  CYS K SG    1 
ATOM   5922  N  N     . VAL B 2 331 ? 151.247 134.288 122.482 1.00 58.63  ? 331  VAL K N     1 
ATOM   5923  C  CA    . VAL B 2 331 ? 150.086 133.664 123.104 1.00 61.97  ? 331  VAL K CA    1 
ATOM   5924  C  C     . VAL B 2 331 ? 149.612 134.519 124.270 1.00 63.24  ? 331  VAL K C     1 
ATOM   5925  O  O     . VAL B 2 331 ? 150.416 134.987 125.086 1.00 65.99  ? 331  VAL K O     1 
ATOM   5926  C  CB    . VAL B 2 331 ? 150.419 132.238 123.565 1.00 62.81  ? 331  VAL K CB    1 
ATOM   5927  C  CG1   . VAL B 2 331 ? 149.149 131.487 123.919 1.00 58.27  ? 331  VAL K CG1   1 
ATOM   5928  C  CG2   . VAL B 2 331 ? 151.202 131.499 122.495 1.00 64.61  ? 331  VAL K CG2   1 
ATOM   5929  N  N     . ASN B 2 332 ? 148.301 134.726 124.354 1.00 61.00  ? 332  ASN K N     1 
ATOM   5930  C  CA    . ASN B 2 332 ? 147.709 135.534 125.418 1.00 60.28  ? 332  ASN K CA    1 
ATOM   5931  C  C     . ASN B 2 332 ? 147.456 134.633 126.619 1.00 67.71  ? 332  ASN K C     1 
ATOM   5932  O  O     . ASN B 2 332 ? 146.396 134.023 126.758 1.00 71.64  ? 332  ASN K O     1 
ATOM   5933  C  CB    . ASN B 2 332 ? 146.428 136.201 124.937 1.00 61.34  ? 332  ASN K CB    1 
ATOM   5934  C  CG    . ASN B 2 332 ? 146.651 137.083 123.730 1.00 63.99  ? 332  ASN K CG    1 
ATOM   5935  O  OD1   . ASN B 2 332 ? 147.663 136.965 123.043 1.00 67.25  ? 332  ASN K OD1   1 
ATOM   5936  N  ND2   . ASN B 2 332 ? 145.705 137.973 123.465 1.00 62.89  ? 332  ASN K ND2   1 
ATOM   5937  N  N     . VAL B 2 333 ? 148.448 134.549 127.499 1.00 75.50  ? 333  VAL K N     1 
ATOM   5938  C  CA    . VAL B 2 333 ? 148.384 133.709 128.689 1.00 71.86  ? 333  VAL K CA    1 
ATOM   5939  C  C     . VAL B 2 333 ? 148.127 134.629 129.876 1.00 70.42  ? 333  VAL K C     1 
ATOM   5940  O  O     . VAL B 2 333 ? 149.055 135.224 130.430 1.00 72.20  ? 333  VAL K O     1 
ATOM   5941  C  CB    . VAL B 2 333 ? 149.663 132.891 128.877 1.00 70.91  ? 333  VAL K CB    1 
ATOM   5942  C  CG1   . VAL B 2 333 ? 149.488 131.887 130.006 1.00 70.89  ? 333  VAL K CG1   1 
ATOM   5943  C  CG2   . VAL B 2 333 ? 150.042 132.190 127.583 1.00 71.86  ? 333  VAL K CG2   1 
ATOM   5944  N  N     . GLU B 2 334 ? 146.864 134.748 130.269 1.00 88.64  ? 334  GLU K N     1 
ATOM   5945  C  CA    . GLU B 2 334 ? 146.509 135.527 131.446 1.00 91.26  ? 334  GLU K CA    1 
ATOM   5946  C  C     . GLU B 2 334 ? 146.882 134.753 132.702 1.00 96.02  ? 334  GLU K C     1 
ATOM   5947  O  O     . GLU B 2 334 ? 146.566 133.566 132.827 1.00 96.77  ? 334  GLU K O     1 
ATOM   5948  C  CB    . GLU B 2 334 ? 145.017 135.852 131.442 1.00 91.79  ? 334  GLU K CB    1 
ATOM   5949  C  CG    . GLU B 2 334 ? 144.571 136.720 132.600 1.00 93.96  ? 334  GLU K CG    1 
ATOM   5950  C  CD    . GLU B 2 334 ? 143.115 137.121 132.494 1.00 97.45  ? 334  GLU K CD    1 
ATOM   5951  O  OE1   . GLU B 2 334 ? 142.485 136.804 131.463 1.00 95.74  ? 334  GLU K OE1   1 
ATOM   5952  O  OE2   . GLU B 2 334 ? 142.600 137.752 133.440 1.00 97.24  ? 334  GLU K OE2   1 
ATOM   5953  N  N     . LEU B 2 335 ? 147.560 135.426 133.629 1.00 110.30 ? 335  LEU K N     1 
ATOM   5954  C  CA    . LEU B 2 335 ? 148.006 134.774 134.851 1.00 110.53 ? 335  LEU K CA    1 
ATOM   5955  C  C     . LEU B 2 335 ? 146.815 134.342 135.696 1.00 111.41 ? 335  LEU K C     1 
ATOM   5956  O  O     . LEU B 2 335 ? 145.765 134.989 135.715 1.00 110.17 ? 335  LEU K O     1 
ATOM   5957  C  CB    . LEU B 2 335 ? 148.914 135.703 135.655 1.00 109.77 ? 335  LEU K CB    1 
ATOM   5958  C  CG    . LEU B 2 335 ? 150.319 135.897 135.086 1.00 107.96 ? 335  LEU K CG    1 
ATOM   5959  C  CD1   . LEU B 2 335 ? 151.144 136.802 135.986 1.00 109.77 ? 335  LEU K CD1   1 
ATOM   5960  C  CD2   . LEU B 2 335 ? 151.005 134.555 134.895 1.00 106.33 ? 335  LEU K CD2   1 
ATOM   5961  N  N     . THR B 2 336 ? 146.990 133.229 136.399 1.00 120.95 ? 336  THR K N     1 
ATOM   5962  C  CA    . THR B 2 336 ? 145.900 132.614 137.135 1.00 121.72 ? 336  THR K CA    1 
ATOM   5963  C  C     . THR B 2 336 ? 145.888 133.118 138.577 1.00 124.00 ? 336  THR K C     1 
ATOM   5964  O  O     . THR B 2 336 ? 146.885 133.629 139.094 1.00 123.03 ? 336  THR K O     1 
ATOM   5965  C  CB    . THR B 2 336 ? 146.036 131.096 137.089 1.00 121.09 ? 336  THR K CB    1 
ATOM   5966  O  OG1   . THR B 2 336 ? 146.853 130.661 138.179 1.00 122.04 ? 336  THR K OG1   1 
ATOM   5967  C  CG2   . THR B 2 336 ? 146.731 130.693 135.801 1.00 117.79 ? 336  THR K CG2   1 
ATOM   5968  N  N     . ALA B 2 337 ? 144.742 132.973 139.240 1.00 129.88 ? 337  ALA K N     1 
ATOM   5969  C  CA    . ALA B 2 337 ? 144.613 133.328 140.648 1.00 127.79 ? 337  ALA K CA    1 
ATOM   5970  C  C     . ALA B 2 337 ? 145.397 132.399 141.565 1.00 128.81 ? 337  ALA K C     1 
ATOM   5971  O  O     . ALA B 2 337 ? 146.087 132.871 142.476 1.00 131.71 ? 337  ALA K O     1 
ATOM   5972  C  CB    . ALA B 2 337 ? 143.139 133.324 141.063 1.00 125.35 ? 337  ALA K CB    1 
ATOM   5973  N  N     . GLU B 2 338 ? 145.306 131.087 141.340 1.00 132.26 ? 338  GLU K N     1 
ATOM   5974  C  CA    . GLU B 2 338 ? 146.060 130.142 142.156 1.00 134.43 ? 338  GLU K CA    1 
ATOM   5975  C  C     . GLU B 2 338 ? 147.561 130.341 141.984 1.00 135.21 ? 338  GLU K C     1 
ATOM   5976  O  O     . GLU B 2 338 ? 148.314 130.316 142.964 1.00 135.27 ? 338  GLU K O     1 
ATOM   5977  C  CB    . GLU B 2 338 ? 145.662 128.709 141.804 1.00 133.86 ? 338  GLU K CB    1 
ATOM   5978  C  CG    . GLU B 2 338 ? 146.357 127.651 142.644 1.00 135.97 ? 338  GLU K CG    1 
ATOM   5979  C  CD    . GLU B 2 338 ? 145.834 127.600 144.067 1.00 136.50 ? 338  GLU K CD    1 
ATOM   5980  O  OE1   . GLU B 2 338 ? 144.687 128.039 144.297 1.00 135.63 ? 338  GLU K OE1   1 
ATOM   5981  O  OE2   . GLU B 2 338 ? 146.570 127.122 144.955 1.00 135.79 ? 338  GLU K OE2   1 
ATOM   5982  N  N     . GLN B 2 339 ? 148.017 130.545 140.745 1.00 131.40 ? 339  GLN K N     1 
ATOM   5983  C  CA    . GLN B 2 339 ? 149.435 130.813 140.535 1.00 130.85 ? 339  GLN K CA    1 
ATOM   5984  C  C     . GLN B 2 339 ? 149.833 132.167 141.101 1.00 131.07 ? 339  GLN K C     1 
ATOM   5985  O  O     . GLN B 2 339 ? 150.962 132.328 141.574 1.00 133.76 ? 339  GLN K O     1 
ATOM   5986  C  CB    . GLN B 2 339 ? 149.786 130.731 139.050 1.00 131.93 ? 339  GLN K CB    1 
ATOM   5987  C  CG    . GLN B 2 339 ? 151.268 130.532 138.777 1.00 132.47 ? 339  GLN K CG    1 
ATOM   5988  C  CD    . GLN B 2 339 ? 151.532 129.899 137.425 1.00 132.81 ? 339  GLN K CD    1 
ATOM   5989  O  OE1   . GLN B 2 339 ? 150.622 129.743 136.611 1.00 132.96 ? 339  GLN K OE1   1 
ATOM   5990  N  NE2   . GLN B 2 339 ? 152.784 129.530 137.179 1.00 132.46 ? 339  GLN K NE2   1 
ATOM   5991  N  N     . TRP B 2 340 ? 148.926 133.146 141.071 1.00 127.64 ? 340  TRP K N     1 
ATOM   5992  C  CA    . TRP B 2 340 ? 149.204 134.429 141.710 1.00 130.96 ? 340  TRP K CA    1 
ATOM   5993  C  C     . TRP B 2 340 ? 149.457 134.245 143.202 1.00 132.96 ? 340  TRP K C     1 
ATOM   5994  O  O     . TRP B 2 340 ? 150.437 134.767 143.751 1.00 132.68 ? 340  TRP K O     1 
ATOM   5995  C  CB    . TRP B 2 340 ? 148.037 135.392 141.486 1.00 128.56 ? 340  TRP K CB    1 
ATOM   5996  C  CG    . TRP B 2 340 ? 148.246 136.402 140.394 1.00 129.51 ? 340  TRP K CG    1 
ATOM   5997  C  CD1   . TRP B 2 340 ? 147.406 136.658 139.350 1.00 129.10 ? 340  TRP K CD1   1 
ATOM   5998  C  CD2   . TRP B 2 340 ? 149.361 137.292 140.236 1.00 131.46 ? 340  TRP K CD2   1 
ATOM   5999  N  NE1   . TRP B 2 340 ? 147.925 137.649 138.554 1.00 129.72 ? 340  TRP K NE1   1 
ATOM   6000  C  CE2   . TRP B 2 340 ? 149.124 138.055 139.075 1.00 129.92 ? 340  TRP K CE2   1 
ATOM   6001  C  CE3   . TRP B 2 340 ? 150.535 137.517 140.963 1.00 129.75 ? 340  TRP K CE3   1 
ATOM   6002  C  CZ2   . TRP B 2 340 ? 150.016 139.024 138.624 1.00 127.96 ? 340  TRP K CZ2   1 
ATOM   6003  C  CZ3   . TRP B 2 340 ? 151.419 138.481 140.512 1.00 129.44 ? 340  TRP K CZ3   1 
ATOM   6004  C  CH2   . TRP B 2 340 ? 151.154 139.222 139.354 1.00 129.47 ? 340  TRP K CH2   1 
ATOM   6005  N  N     . LYS B 2 341 ? 148.586 133.486 143.873 1.00 132.56 ? 341  LYS K N     1 
ATOM   6006  C  CA    . LYS B 2 341 ? 148.759 133.271 145.305 1.00 130.90 ? 341  LYS K CA    1 
ATOM   6007  C  C     . LYS B 2 341 ? 149.987 132.418 145.599 1.00 130.74 ? 341  LYS K C     1 
ATOM   6008  O  O     . LYS B 2 341 ? 150.653 132.628 146.618 1.00 131.51 ? 341  LYS K O     1 
ATOM   6009  C  CB    . LYS B 2 341 ? 147.496 132.646 145.906 1.00 130.87 ? 341  LYS K CB    1 
ATOM   6010  C  CG    . LYS B 2 341 ? 147.455 131.126 145.918 1.00 132.28 ? 341  LYS K CG    1 
ATOM   6011  C  CD    . LYS B 2 341 ? 146.165 130.615 146.538 1.00 131.61 ? 341  LYS K CD    1 
ATOM   6012  C  CE    . LYS B 2 341 ? 144.956 131.009 145.706 1.00 131.96 ? 341  LYS K CE    1 
ATOM   6013  N  NZ    . LYS B 2 341 ? 143.695 130.436 146.252 1.00 131.38 ? 341  LYS K NZ    1 
ATOM   6014  N  N     . LYS B 2 342 ? 150.314 131.468 144.720 1.00 132.53 ? 342  LYS K N     1 
ATOM   6015  C  CA    . LYS B 2 342 ? 151.521 130.674 144.918 1.00 135.61 ? 342  LYS K CA    1 
ATOM   6016  C  C     . LYS B 2 342 ? 152.773 131.533 144.781 1.00 135.62 ? 342  LYS K C     1 
ATOM   6017  O  O     . LYS B 2 342 ? 153.727 131.377 145.553 1.00 136.48 ? 342  LYS K O     1 
ATOM   6018  C  CB    . LYS B 2 342 ? 151.554 129.507 143.932 1.00 136.05 ? 342  LYS K CB    1 
ATOM   6019  C  CG    . LYS B 2 342 ? 152.644 128.485 144.219 1.00 135.67 ? 342  LYS K CG    1 
ATOM   6020  C  CD    . LYS B 2 342 ? 152.490 127.885 145.610 1.00 135.68 ? 342  LYS K CD    1 
ATOM   6021  C  CE    . LYS B 2 342 ? 151.186 127.114 145.744 1.00 134.71 ? 342  LYS K CE    1 
ATOM   6022  N  NZ    . LYS B 2 342 ? 150.997 126.576 147.120 1.00 132.41 ? 342  LYS K NZ    1 
ATOM   6023  N  N     . LYS B 2 343 ? 152.788 132.443 143.804 1.00 137.10 ? 343  LYS K N     1 
ATOM   6024  C  CA    . LYS B 2 343 ? 153.918 133.354 143.658 1.00 137.11 ? 343  LYS K CA    1 
ATOM   6025  C  C     . LYS B 2 343 ? 154.022 134.291 144.852 1.00 139.06 ? 343  LYS K C     1 
ATOM   6026  O  O     . LYS B 2 343 ? 155.128 134.625 145.294 1.00 139.35 ? 343  LYS K O     1 
ATOM   6027  C  CB    . LYS B 2 343 ? 153.792 134.149 142.358 1.00 136.79 ? 343  LYS K CB    1 
ATOM   6028  C  CG    . LYS B 2 343 ? 153.990 133.317 141.101 1.00 138.77 ? 343  LYS K CG    1 
ATOM   6029  C  CD    . LYS B 2 343 ? 155.364 132.667 141.077 1.00 138.00 ? 343  LYS K CD    1 
ATOM   6030  C  CE    . LYS B 2 343 ? 155.555 131.826 139.826 1.00 137.91 ? 343  LYS K CE    1 
ATOM   6031  N  NZ    . LYS B 2 343 ? 156.898 131.184 139.788 1.00 137.16 ? 343  LYS K NZ    1 
ATOM   6032  N  N     . TYR B 2 344 ? 152.880 134.737 145.382 1.00 141.25 ? 344  TYR K N     1 
ATOM   6033  C  CA    . TYR B 2 344 ? 152.902 135.551 146.594 1.00 140.52 ? 344  TYR K CA    1 
ATOM   6034  C  C     . TYR B 2 344 ? 153.500 134.776 147.763 1.00 140.29 ? 344  TYR K C     1 
ATOM   6035  O  O     . TYR B 2 344 ? 154.349 135.293 148.498 1.00 138.39 ? 344  TYR K O     1 
ATOM   6036  C  CB    . TYR B 2 344 ? 151.491 136.026 146.940 1.00 139.72 ? 344  TYR K CB    1 
ATOM   6037  C  CG    . TYR B 2 344 ? 151.293 136.286 148.417 1.00 139.95 ? 344  TYR K CG    1 
ATOM   6038  C  CD1   . TYR B 2 344 ? 151.725 137.470 148.996 1.00 138.81 ? 344  TYR K CD1   1 
ATOM   6039  C  CD2   . TYR B 2 344 ? 150.675 135.345 149.233 1.00 140.51 ? 344  TYR K CD2   1 
ATOM   6040  C  CE1   . TYR B 2 344 ? 151.549 137.713 150.345 1.00 140.42 ? 344  TYR K CE1   1 
ATOM   6041  C  CE2   . TYR B 2 344 ? 150.497 135.578 150.584 1.00 141.80 ? 344  TYR K CE2   1 
ATOM   6042  C  CZ    . TYR B 2 344 ? 150.934 136.765 151.134 1.00 142.14 ? 344  TYR K CZ    1 
ATOM   6043  O  OH    . TYR B 2 344 ? 150.758 137.003 152.478 1.00 139.95 ? 344  TYR K OH    1 
ATOM   6044  N  N     . GLU B 2 345 ? 153.059 133.530 147.951 1.00 143.15 ? 345  GLU K N     1 
ATOM   6045  C  CA    . GLU B 2 345 ? 153.532 132.731 149.077 1.00 142.85 ? 345  GLU K CA    1 
ATOM   6046  C  C     . GLU B 2 345 ? 155.019 132.419 148.955 1.00 143.88 ? 345  GLU K C     1 
ATOM   6047  O  O     . GLU B 2 345 ? 155.754 132.476 149.948 1.00 142.83 ? 345  GLU K O     1 
ATOM   6048  C  CB    . GLU B 2 345 ? 152.718 131.441 149.180 1.00 140.99 ? 345  GLU K CB    1 
ATOM   6049  C  CG    . GLU B 2 345 ? 153.023 130.614 150.419 1.00 141.31 ? 345  GLU K CG    1 
ATOM   6050  C  CD    . GLU B 2 345 ? 152.117 129.406 150.551 1.00 142.09 ? 345  GLU K CD    1 
ATOM   6051  O  OE1   . GLU B 2 345 ? 151.305 129.167 149.632 1.00 141.53 ? 345  GLU K OE1   1 
ATOM   6052  O  OE2   . GLU B 2 345 ? 152.217 128.695 151.573 1.00 142.18 ? 345  GLU K OE2   1 
ATOM   6053  N  N     . LYS B 2 346 ? 155.480 132.089 147.753 1.00 139.87 ? 346  LYS K N     1 
ATOM   6054  C  CA    . LYS B 2 346 ? 156.884 131.758 147.539 1.00 138.09 ? 346  LYS K CA    1 
ATOM   6055  C  C     . LYS B 2 346 ? 157.676 132.984 147.099 1.00 136.25 ? 346  LYS K C     1 
ATOM   6056  O  O     . LYS B 2 346 ? 158.541 133.471 147.828 1.00 135.05 ? 346  LYS K O     1 
ATOM   6057  C  CB    . LYS B 2 346 ? 157.018 130.642 146.500 1.00 135.66 ? 346  LYS K CB    1 
ATOM   6058  C  CG    . LYS B 2 346 ? 158.446 130.175 146.272 1.00 135.45 ? 346  LYS K CG    1 
ATOM   6059  C  CD    . LYS B 2 346 ? 158.500 129.047 145.253 1.00 134.96 ? 346  LYS K CD    1 
ATOM   6060  C  CE    . LYS B 2 346 ? 159.924 128.558 145.045 1.00 135.97 ? 346  LYS K CE    1 
ATOM   6061  N  NZ    . LYS B 2 346 ? 159.990 127.451 144.051 1.00 135.07 ? 346  LYS K NZ    1 
ATOM   6062  N  N     . LEU C 2 4   ? 133.238 131.848 165.717 1.00 91.95  ? 4    LEU L N     1 
ATOM   6063  C  CA    . LEU C 2 4   ? 132.506 131.602 164.480 1.00 91.83  ? 4    LEU L CA    1 
ATOM   6064  C  C     . LEU C 2 4   ? 131.020 131.412 164.775 1.00 92.32  ? 4    LEU L C     1 
ATOM   6065  O  O     . LEU C 2 4   ? 130.398 132.250 165.428 1.00 91.08  ? 4    LEU L O     1 
ATOM   6066  C  CB    . LEU C 2 4   ? 133.073 130.378 163.756 1.00 91.92  ? 4    LEU L CB    1 
ATOM   6067  C  CG    . LEU C 2 4   ? 132.981 130.365 162.228 1.00 91.73  ? 4    LEU L CG    1 
ATOM   6068  C  CD1   . LEU C 2 4   ? 133.754 131.532 161.634 1.00 89.77  ? 4    LEU L CD1   1 
ATOM   6069  C  CD2   . LEU C 2 4   ? 133.488 129.043 161.673 1.00 91.51  ? 4    LEU L CD2   1 
ATOM   6070  N  N     . ALA C 2 5   ? 130.454 130.309 164.291 1.00 81.94  ? 5    ALA L N     1 
ATOM   6071  C  CA    . ALA C 2 5   ? 129.055 129.996 164.543 1.00 79.10  ? 5    ALA L CA    1 
ATOM   6072  C  C     . ALA C 2 5   ? 128.871 128.488 164.493 1.00 76.31  ? 5    ALA L C     1 
ATOM   6073  O  O     . ALA C 2 5   ? 129.473 127.811 163.654 1.00 73.15  ? 5    ALA L O     1 
ATOM   6074  C  CB    . ALA C 2 5   ? 128.131 130.681 163.528 1.00 77.08  ? 5    ALA L CB    1 
ATOM   6075  N  N     . GLU C 2 6   ? 128.043 127.972 165.396 1.00 77.39  ? 6    GLU L N     1 
ATOM   6076  C  CA    . GLU C 2 6   ? 127.725 126.554 165.461 1.00 76.75  ? 6    GLU L CA    1 
ATOM   6077  C  C     . GLU C 2 6   ? 126.241 126.364 165.187 1.00 74.03  ? 6    GLU L C     1 
ATOM   6078  O  O     . GLU C 2 6   ? 125.398 126.960 165.865 1.00 76.59  ? 6    GLU L O     1 
ATOM   6079  C  CB    . GLU C 2 6   ? 128.108 125.965 166.822 1.00 75.72  ? 6    GLU L CB    1 
ATOM   6080  C  CG    . GLU C 2 6   ? 127.926 126.919 167.993 1.00 75.92  ? 6    GLU L CG    1 
ATOM   6081  C  CD    . GLU C 2 6   ? 126.596 126.741 168.695 1.00 75.23  ? 6    GLU L CD    1 
ATOM   6082  O  OE1   . GLU C 2 6   ? 125.902 125.742 168.416 1.00 76.53  ? 6    GLU L OE1   1 
ATOM   6083  O  OE2   . GLU C 2 6   ? 126.244 127.602 169.529 1.00 76.10  ? 6    GLU L OE2   1 
ATOM   6084  N  N     . CYS C 2 7   ? 125.929 125.540 164.192 1.00 46.95  ? 7    CYS L N     1 
ATOM   6085  C  CA    . CYS C 2 7   ? 124.558 125.284 163.784 1.00 43.81  ? 7    CYS L CA    1 
ATOM   6086  C  C     . CYS C 2 7   ? 124.299 123.787 163.793 1.00 44.59  ? 7    CYS L C     1 
ATOM   6087  O  O     . CYS C 2 7   ? 125.126 122.994 163.335 1.00 48.87  ? 7    CYS L O     1 
ATOM   6088  C  CB    . CYS C 2 7   ? 124.272 125.857 162.393 1.00 45.86  ? 7    CYS L CB    1 
ATOM   6089  S  SG    . CYS C 2 7   ? 124.560 127.635 162.256 1.00 54.48  ? 7    CYS L SG    1 
ATOM   6090  N  N     . ASN C 2 8   ? 123.141 123.408 164.319 1.00 35.54  ? 8    ASN L N     1 
ATOM   6091  C  CA    . ASN C 2 8   ? 122.794 122.003 164.443 1.00 29.36  ? 8    ASN L CA    1 
ATOM   6092  C  C     . ASN C 2 8   ? 122.378 121.424 163.097 1.00 26.12  ? 8    ASN L C     1 
ATOM   6093  O  O     . ASN C 2 8   ? 121.743 122.092 162.278 1.00 31.87  ? 8    ASN L O     1 
ATOM   6094  C  CB    . ASN C 2 8   ? 121.660 121.816 165.450 1.00 31.43  ? 8    ASN L CB    1 
ATOM   6095  C  CG    . ASN C 2 8   ? 121.914 122.540 166.753 1.00 35.70  ? 8    ASN L CG    1 
ATOM   6096  O  OD1   . ASN C 2 8   ? 122.531 123.604 166.773 1.00 38.80  ? 8    ASN L OD1   1 
ATOM   6097  N  ND2   . ASN C 2 8   ? 121.438 121.967 167.851 1.00 37.97  ? 8    ASN L ND2   1 
ATOM   6098  N  N     . ILE C 2 9   ? 122.742 120.165 162.878 1.00 18.18  ? 9    ILE L N     1 
ATOM   6099  C  CA    . ILE C 2 9   ? 122.221 119.407 161.747 1.00 25.09  ? 9    ILE L CA    1 
ATOM   6100  C  C     . ILE C 2 9   ? 120.771 119.065 162.068 1.00 30.08  ? 9    ILE L C     1 
ATOM   6101  O  O     . ILE C 2 9   ? 120.495 118.250 162.951 1.00 28.68  ? 9    ILE L O     1 
ATOM   6102  C  CB    . ILE C 2 9   ? 123.047 118.145 161.478 1.00 31.72  ? 9    ILE L CB    1 
ATOM   6103  C  CG1   . ILE C 2 9   ? 124.393 118.519 160.860 1.00 35.55  ? 9    ILE L CG1   1 
ATOM   6104  C  CG2   . ILE C 2 9   ? 122.288 117.189 160.571 1.00 35.27  ? 9    ILE L CG2   1 
ATOM   6105  C  CD1   . ILE C 2 9   ? 125.159 117.341 160.317 1.00 32.87  ? 9    ILE L CD1   1 
ATOM   6106  N  N     . LYS C 2 10  ? 119.843 119.706 161.367 1.00 33.74  ? 10   LYS L N     1 
ATOM   6107  C  CA    . LYS C 2 10  ? 118.432 119.527 161.664 1.00 28.47  ? 10   LYS L CA    1 
ATOM   6108  C  C     . LYS C 2 10  ? 117.990 118.110 161.332 1.00 24.39  ? 10   LYS L C     1 
ATOM   6109  O  O     . LYS C 2 10  ? 118.525 117.470 160.423 1.00 36.49  ? 10   LYS L O     1 
ATOM   6110  C  CB    . LYS C 2 10  ? 117.596 120.537 160.882 1.00 33.76  ? 10   LYS L CB    1 
ATOM   6111  C  CG    . LYS C 2 10  ? 118.075 121.967 161.031 1.00 30.69  ? 10   LYS L CG    1 
ATOM   6112  C  CD    . LYS C 2 10  ? 117.189 122.926 160.260 1.00 33.22  ? 10   LYS L CD    1 
ATOM   6113  C  CE    . LYS C 2 10  ? 115.785 122.958 160.835 1.00 37.01  ? 10   LYS L CE    1 
ATOM   6114  N  NZ    . LYS C 2 10  ? 115.773 123.400 162.256 1.00 38.87  ? 10   LYS L NZ    1 
ATOM   6115  N  N     . VAL C 2 11  ? 117.018 117.614 162.089 1.00 26.98  ? 11   VAL L N     1 
ATOM   6116  C  CA    . VAL C 2 11  ? 116.401 116.319 161.835 1.00 36.05  ? 11   VAL L CA    1 
ATOM   6117  C  C     . VAL C 2 11  ? 114.891 116.507 161.847 1.00 42.03  ? 11   VAL L C     1 
ATOM   6118  O  O     . VAL C 2 11  ? 114.338 117.055 162.806 1.00 50.26  ? 11   VAL L O     1 
ATOM   6119  C  CB    . VAL C 2 11  ? 116.822 115.266 162.876 1.00 43.57  ? 11   VAL L CB    1 
ATOM   6120  C  CG1   . VAL C 2 11  ? 116.117 113.950 162.603 1.00 43.57  ? 11   VAL L CG1   1 
ATOM   6121  C  CG2   . VAL C 2 11  ? 118.330 115.080 162.865 1.00 39.20  ? 11   VAL L CG2   1 
ATOM   6122  N  N     . MET C 2 12  ? 114.228 116.049 160.789 1.00 49.60  ? 12   MET L N     1 
ATOM   6123  C  CA    . MET C 2 12  ? 112.786 116.172 160.659 1.00 47.52  ? 12   MET L CA    1 
ATOM   6124  C  C     . MET C 2 12  ? 112.176 114.799 160.424 1.00 56.74  ? 12   MET L C     1 
ATOM   6125  O  O     . MET C 2 12  ? 112.787 113.930 159.797 1.00 60.29  ? 12   MET L O     1 
ATOM   6126  C  CB    . MET C 2 12  ? 112.415 117.119 159.520 1.00 49.03  ? 12   MET L CB    1 
ATOM   6127  C  CG    . MET C 2 12  ? 113.074 118.480 159.627 1.00 52.40  ? 12   MET L CG    1 
ATOM   6128  S  SD    . MET C 2 12  ? 112.494 119.631 158.370 1.00 68.57  ? 12   MET L SD    1 
ATOM   6129  C  CE    . MET C 2 12  ? 113.440 121.089 158.791 1.00 57.86  ? 12   MET L CE    1 
ATOM   6130  N  N     . CYS C 2 13  ? 110.966 114.610 160.939 1.00 78.38  ? 13   CYS L N     1 
ATOM   6131  C  CA    . CYS C 2 13  ? 110.267 113.334 160.863 1.00 81.16  ? 13   CYS L CA    1 
ATOM   6132  C  C     . CYS C 2 13  ? 109.021 113.488 160.003 1.00 83.86  ? 13   CYS L C     1 
ATOM   6133  O  O     . CYS C 2 13  ? 108.216 114.398 160.228 1.00 80.93  ? 13   CYS L O     1 
ATOM   6134  C  CB    . CYS C 2 13  ? 109.890 112.832 162.258 1.00 81.83  ? 13   CYS L CB    1 
ATOM   6135  S  SG    . CYS C 2 13  ? 109.073 111.219 162.277 1.00 88.49  ? 13   CYS L SG    1 
ATOM   6136  N  N     . ARG C 2 14  ? 108.863 112.595 159.029 1.00 90.89  ? 14   ARG L N     1 
ATOM   6137  C  CA    . ARG C 2 14  ? 107.740 112.623 158.104 1.00 90.61  ? 14   ARG L CA    1 
ATOM   6138  C  C     . ARG C 2 14  ? 106.991 111.298 158.155 1.00 90.25  ? 14   ARG L C     1 
ATOM   6139  O  O     . ARG C 2 14  ? 107.605 110.230 158.253 1.00 91.83  ? 14   ARG L O     1 
ATOM   6140  C  CB    . ARG C 2 14  ? 108.210 112.906 156.673 1.00 87.09  ? 14   ARG L CB    1 
ATOM   6141  C  CG    . ARG C 2 14  ? 107.085 112.963 155.656 1.00 89.28  ? 14   ARG L CG    1 
ATOM   6142  C  CD    . ARG C 2 14  ? 107.547 113.565 154.343 1.00 89.84  ? 14   ARG L CD    1 
ATOM   6143  N  NE    . ARG C 2 14  ? 106.423 113.842 153.457 1.00 89.76  ? 14   ARG L NE    1 
ATOM   6144  C  CZ    . ARG C 2 14  ? 106.509 114.527 152.325 1.00 88.21  ? 14   ARG L CZ    1 
ATOM   6145  N  NH1   . ARG C 2 14  ? 107.660 115.030 151.908 1.00 86.20  ? 14   ARG L NH1   1 
ATOM   6146  N  NH2   . ARG C 2 14  ? 105.413 114.717 151.597 1.00 91.00  ? 14   ARG L NH2   1 
ATOM   6147  N  N     . PHE C 2 15  ? 105.664 111.373 158.094 1.00 90.61  ? 15   PHE L N     1 
ATOM   6148  C  CA    . PHE C 2 15  ? 104.802 110.200 158.095 1.00 91.07  ? 15   PHE L CA    1 
ATOM   6149  C  C     . PHE C 2 15  ? 103.905 110.229 156.867 1.00 95.06  ? 15   PHE L C     1 
ATOM   6150  O  O     . PHE C 2 15  ? 103.372 111.283 156.507 1.00 95.05  ? 15   PHE L O     1 
ATOM   6151  C  CB    . PHE C 2 15  ? 103.955 110.137 159.366 1.00 91.29  ? 15   PHE L CB    1 
ATOM   6152  C  CG    . PHE C 2 15  ? 104.521 109.244 160.428 1.00 93.81  ? 15   PHE L CG    1 
ATOM   6153  C  CD1   . PHE C 2 15  ? 105.511 109.700 161.281 1.00 95.29  ? 15   PHE L CD1   1 
ATOM   6154  C  CD2   . PHE C 2 15  ? 104.061 107.946 160.576 1.00 92.90  ? 15   PHE L CD2   1 
ATOM   6155  C  CE1   . PHE C 2 15  ? 106.032 108.880 162.262 1.00 95.91  ? 15   PHE L CE1   1 
ATOM   6156  C  CE2   . PHE C 2 15  ? 104.578 107.120 161.555 1.00 94.21  ? 15   PHE L CE2   1 
ATOM   6157  C  CZ    . PHE C 2 15  ? 105.564 107.589 162.400 1.00 95.74  ? 15   PHE L CZ    1 
ATOM   6158  N  N     . ARG C 2 16  ? 103.739 109.055 156.221 1.00 116.06 ? 16   ARG L N     1 
ATOM   6159  C  CA    . ARG C 2 16  ? 102.923 108.832 155.039 1.00 114.26 ? 16   ARG L CA    1 
ATOM   6160  C  C     . ARG C 2 16  ? 101.632 108.107 155.404 1.00 113.70 ? 16   ARG L C     1 
ATOM   6161  O  O     . ARG C 2 16  ? 101.578 107.387 156.406 1.00 115.40 ? 16   ARG L O     1 
ATOM   6162  C  CB    . ARG C 2 16  ? 103.691 108.011 153.998 1.00 114.21 ? 16   ARG L CB    1 
ATOM   6163  C  CG    . ARG C 2 16  ? 104.120 106.637 154.483 1.00 114.72 ? 16   ARG L CG    1 
ATOM   6164  C  CD    . ARG C 2 16  ? 104.629 105.782 153.336 1.00 113.86 ? 16   ARG L CD    1 
ATOM   6165  N  NE    . ARG C 2 16  ? 105.092 104.477 153.791 1.00 114.47 ? 16   ARG L NE    1 
ATOM   6166  C  CZ    . ARG C 2 16  ? 104.301 103.436 154.012 1.00 116.48 ? 16   ARG L CZ    1 
ATOM   6167  N  NH1   . ARG C 2 16  ? 102.993 103.510 153.830 1.00 117.11 ? 16   ARG L NH1   1 
ATOM   6168  N  NH2   . ARG C 2 16  ? 104.836 102.291 154.427 1.00 115.66 ? 16   ARG L NH2   1 
ATOM   6169  N  N     . PRO C 2 17  ? 100.573 108.283 154.614 1.00 121.34 ? 17   PRO L N     1 
ATOM   6170  C  CA    . PRO C 2 17  ? 99.317  107.580 154.901 1.00 123.09 ? 17   PRO L CA    1 
ATOM   6171  C  C     . PRO C 2 17  ? 99.468  106.073 154.755 1.00 124.88 ? 17   PRO L C     1 
ATOM   6172  O  O     . PRO C 2 17  ? 100.337 105.577 154.033 1.00 123.94 ? 17   PRO L O     1 
ATOM   6173  C  CB    . PRO C 2 17  ? 98.345  108.147 153.859 1.00 123.12 ? 17   PRO L CB    1 
ATOM   6174  C  CG    . PRO C 2 17  ? 98.949  109.443 153.433 1.00 123.66 ? 17   PRO L CG    1 
ATOM   6175  C  CD    . PRO C 2 17  ? 100.428 109.240 153.504 1.00 122.43 ? 17   PRO L CD    1 
ATOM   6176  N  N     . LEU C 2 18  ? 98.610  105.344 155.468 1.00 147.91 ? 18   LEU L N     1 
ATOM   6177  C  CA    . LEU C 2 18  ? 98.629  103.887 155.428 1.00 148.06 ? 18   LEU L CA    1 
ATOM   6178  C  C     . LEU C 2 18  ? 98.342  103.385 154.017 1.00 146.88 ? 18   LEU L C     1 
ATOM   6179  O  O     . LEU C 2 18  ? 97.451  103.895 153.331 1.00 147.47 ? 18   LEU L O     1 
ATOM   6180  C  CB    . LEU C 2 18  ? 97.603  103.326 156.413 1.00 149.37 ? 18   LEU L CB    1 
ATOM   6181  C  CG    . LEU C 2 18  ? 97.915  101.987 157.086 1.00 150.51 ? 18   LEU L CG    1 
ATOM   6182  C  CD1   . LEU C 2 18  ? 99.000  102.153 158.135 1.00 149.80 ? 18   LEU L CD1   1 
ATOM   6183  C  CD2   . LEU C 2 18  ? 96.663  101.397 157.711 1.00 148.31 ? 18   LEU L CD2   1 
ATOM   6184  N  N     . ASN C 2 19  ? 99.100  102.380 153.587 1.00 147.26 ? 19   ASN L N     1 
ATOM   6185  C  CA    . ASN C 2 19  ? 98.965  101.851 152.239 1.00 149.92 ? 19   ASN L CA    1 
ATOM   6186  C  C     . ASN C 2 19  ? 97.736  100.953 152.122 1.00 151.58 ? 19   ASN L C     1 
ATOM   6187  O  O     . ASN C 2 19  ? 97.204  100.444 153.112 1.00 151.30 ? 19   ASN L O     1 
ATOM   6188  C  CB    . ASN C 2 19  ? 100.220 101.075 151.836 1.00 150.15 ? 19   ASN L CB    1 
ATOM   6189  C  CG    . ASN C 2 19  ? 101.383 101.986 151.494 1.00 149.71 ? 19   ASN L CG    1 
ATOM   6190  O  OD1   . ASN C 2 19  ? 102.486 101.826 152.017 1.00 150.52 ? 19   ASN L OD1   1 
ATOM   6191  N  ND2   . ASN C 2 19  ? 101.141 102.948 150.612 1.00 148.85 ? 19   ASN L ND2   1 
ATOM   6192  N  N     . GLU C 2 20  ? 97.286  100.765 150.877 1.00 163.30 ? 20   GLU L N     1 
ATOM   6193  C  CA    . GLU C 2 20  ? 96.131  99.909  150.621 1.00 162.94 ? 20   GLU L CA    1 
ATOM   6194  C  C     . GLU C 2 20  ? 96.421  98.453  150.963 1.00 162.67 ? 20   GLU L C     1 
ATOM   6195  O  O     . GLU C 2 20  ? 95.527  97.733  151.422 1.00 162.15 ? 20   GLU L O     1 
ATOM   6196  C  CB    . GLU C 2 20  ? 95.692  100.035 149.161 1.00 163.10 ? 20   GLU L CB    1 
ATOM   6197  C  CG    . GLU C 2 20  ? 95.120  101.396 148.793 1.00 163.75 ? 20   GLU L CG    1 
ATOM   6198  C  CD    . GLU C 2 20  ? 96.194  102.420 148.480 1.00 163.85 ? 20   GLU L CD    1 
ATOM   6199  O  OE1   . GLU C 2 20  ? 97.344  102.014 148.210 1.00 163.28 ? 20   GLU L OE1   1 
ATOM   6200  O  OE2   . GLU C 2 20  ? 95.888  103.630 148.503 1.00 163.43 ? 20   GLU L OE2   1 
ATOM   6201  N  N     . SER C 2 21  ? 97.654  97.996  150.737 1.00 159.50 ? 21   SER L N     1 
ATOM   6202  C  CA    . SER C 2 21  ? 98.018  96.644  151.145 1.00 159.18 ? 21   SER L CA    1 
ATOM   6203  C  C     . SER C 2 21  ? 97.917  96.487  152.657 1.00 158.61 ? 21   SER L C     1 
ATOM   6204  O  O     . SER C 2 21  ? 97.466  95.448  153.154 1.00 158.44 ? 21   SER L O     1 
ATOM   6205  C  CB    . SER C 2 21  ? 99.428  96.310  150.660 1.00 158.75 ? 21   SER L CB    1 
ATOM   6206  O  OG    . SER C 2 21  ? 100.376 97.225  151.182 1.00 158.32 ? 21   SER L OG    1 
ATOM   6207  N  N     . GLU C 2 22  ? 98.329  97.514  153.403 1.00 154.86 ? 22   GLU L N     1 
ATOM   6208  C  CA    . GLU C 2 22  ? 98.251  97.460  154.858 1.00 155.49 ? 22   GLU L CA    1 
ATOM   6209  C  C     . GLU C 2 22  ? 96.809  97.427  155.353 1.00 155.89 ? 22   GLU L C     1 
ATOM   6210  O  O     . GLU C 2 22  ? 96.502  96.698  156.303 1.00 155.43 ? 22   GLU L O     1 
ATOM   6211  C  CB    . GLU C 2 22  ? 99.004  98.645  155.462 1.00 155.90 ? 22   GLU L CB    1 
ATOM   6212  C  CG    . GLU C 2 22  ? 100.506 98.595  155.216 1.00 155.49 ? 22   GLU L CG    1 
ATOM   6213  C  CD    . GLU C 2 22  ? 101.202 99.897  155.556 1.00 154.55 ? 22   GLU L CD    1 
ATOM   6214  O  OE1   . GLU C 2 22  ? 100.532 100.950 155.549 1.00 153.64 ? 22   GLU L OE1   1 
ATOM   6215  O  OE2   . GLU C 2 22  ? 102.420 99.867  155.832 1.00 154.38 ? 22   GLU L OE2   1 
ATOM   6216  N  N     . VAL C 2 23  ? 95.913  98.202  154.735 1.00 160.83 ? 23   VAL L N     1 
ATOM   6217  C  CA    . VAL C 2 23  ? 94.511  98.154  155.142 1.00 160.17 ? 23   VAL L CA    1 
ATOM   6218  C  C     . VAL C 2 23  ? 93.837  96.867  154.685 1.00 160.60 ? 23   VAL L C     1 
ATOM   6219  O  O     . VAL C 2 23  ? 92.861  96.433  155.310 1.00 160.32 ? 23   VAL L O     1 
ATOM   6220  C  CB    . VAL C 2 23  ? 93.723  99.374  154.628 1.00 160.27 ? 23   VAL L CB    1 
ATOM   6221  C  CG1   . VAL C 2 23  ? 94.447  100.664 154.975 1.00 160.10 ? 23   VAL L CG1   1 
ATOM   6222  C  CG2   . VAL C 2 23  ? 93.461  99.279  153.134 1.00 159.80 ? 23   VAL L CG2   1 
ATOM   6223  N  N     . ASN C 2 24  ? 94.325  96.243  153.609 1.00 156.82 ? 24   ASN L N     1 
ATOM   6224  C  CA    . ASN C 2 24  ? 93.807  94.936  153.222 1.00 156.37 ? 24   ASN L CA    1 
ATOM   6225  C  C     . ASN C 2 24  ? 94.237  93.866  154.218 1.00 155.11 ? 24   ASN L C     1 
ATOM   6226  O  O     . ASN C 2 24  ? 93.431  93.014  154.611 1.00 152.03 ? 24   ASN L O     1 
ATOM   6227  C  CB    . ASN C 2 24  ? 94.278  94.584  151.810 1.00 156.05 ? 24   ASN L CB    1 
ATOM   6228  C  CG    . ASN C 2 24  ? 93.320  93.653  151.088 1.00 155.42 ? 24   ASN L CG    1 
ATOM   6229  O  OD1   . ASN C 2 24  ? 92.758  92.736  151.686 1.00 156.04 ? 24   ASN L OD1   1 
ATOM   6230  N  ND2   . ASN C 2 24  ? 93.131  93.887  149.794 1.00 153.23 ? 24   ASN L ND2   1 
ATOM   6231  N  N     . ARG C 2 25  ? 95.500  93.908  154.649 1.00 157.73 ? 25   ARG L N     1 
ATOM   6232  C  CA    . ARG C 2 25  ? 96.034  92.953  155.612 1.00 158.17 ? 25   ARG L CA    1 
ATOM   6233  C  C     . ARG C 2 25  ? 95.573  93.219  157.039 1.00 157.17 ? 25   ARG L C     1 
ATOM   6234  O  O     . ARG C 2 25  ? 95.851  92.403  157.924 1.00 156.62 ? 25   ARG L O     1 
ATOM   6235  C  CB    . ARG C 2 25  ? 97.565  92.956  155.560 1.00 157.81 ? 25   ARG L CB    1 
ATOM   6236  C  CG    . ARG C 2 25  ? 98.140  92.411  154.262 1.00 156.58 ? 25   ARG L CG    1 
ATOM   6237  C  CD    . ARG C 2 25  ? 99.637  92.646  154.171 1.00 156.10 ? 25   ARG L CD    1 
ATOM   6238  N  NE    . ARG C 2 25  ? 100.365 91.960  155.232 1.00 157.20 ? 25   ARG L NE    1 
ATOM   6239  C  CZ    . ARG C 2 25  ? 101.678 92.024  155.402 1.00 156.98 ? 25   ARG L CZ    1 
ATOM   6240  N  NH1   . ARG C 2 25  ? 102.445 92.741  154.596 1.00 156.47 ? 25   ARG L NH1   1 
ATOM   6241  N  NH2   . ARG C 2 25  ? 102.236 91.353  156.405 1.00 157.29 ? 25   ARG L NH2   1 
ATOM   6242  N  N     . GLY C 2 26  ? 94.887  94.331  157.287 1.00 159.98 ? 26   GLY L N     1 
ATOM   6243  C  CA    . GLY C 2 26  ? 94.381  94.626  158.611 1.00 160.37 ? 26   GLY L CA    1 
ATOM   6244  C  C     . GLY C 2 26  ? 95.317  95.391  159.514 1.00 160.79 ? 26   GLY L C     1 
ATOM   6245  O  O     . GLY C 2 26  ? 95.123  95.375  160.735 1.00 160.73 ? 26   GLY L O     1 
ATOM   6246  N  N     . ASP C 2 27  ? 96.330  96.056  158.963 1.00 162.38 ? 27   ASP L N     1 
ATOM   6247  C  CA    . ASP C 2 27  ? 97.237  96.847  159.781 1.00 162.06 ? 27   ASP L CA    1 
ATOM   6248  C  C     . ASP C 2 27  ? 96.506  98.040  160.388 1.00 160.52 ? 27   ASP L C     1 
ATOM   6249  O  O     . ASP C 2 27  ? 95.645  98.652  159.751 1.00 160.13 ? 27   ASP L O     1 
ATOM   6250  C  CB    . ASP C 2 27  ? 98.427  97.323  158.949 1.00 162.22 ? 27   ASP L CB    1 
ATOM   6251  C  CG    . ASP C 2 27  ? 99.228  96.174  158.368 1.00 162.55 ? 27   ASP L CG    1 
ATOM   6252  O  OD1   . ASP C 2 27  ? 98.853  95.006  158.605 1.00 162.77 ? 27   ASP L OD1   1 
ATOM   6253  O  OD2   . ASP C 2 27  ? 100.234 96.438  157.677 1.00 162.56 ? 27   ASP L OD2   1 
ATOM   6254  N  N     . LYS C 2 28  ? 96.854  98.365  161.628 1.00 147.98 ? 28   LYS L N     1 
ATOM   6255  C  CA    . LYS C 2 28  ? 96.212  99.437  162.366 1.00 148.04 ? 28   LYS L CA    1 
ATOM   6256  C  C     . LYS C 2 28  ? 97.097  100.684 162.358 1.00 147.97 ? 28   LYS L C     1 
ATOM   6257  O  O     . LYS C 2 28  ? 98.110  100.755 161.654 1.00 146.34 ? 28   LYS L O     1 
ATOM   6258  C  CB    . LYS C 2 28  ? 95.892  98.974  163.790 1.00 148.49 ? 28   LYS L CB    1 
ATOM   6259  C  CG    . LYS C 2 28  ? 97.107  98.840  164.695 1.00 147.95 ? 28   LYS L CG    1 
ATOM   6260  C  CD    . LYS C 2 28  ? 96.740  98.217  166.032 1.00 147.85 ? 28   LYS L CD    1 
ATOM   6261  C  CE    . LYS C 2 28  ? 96.294  96.773  165.867 1.00 147.83 ? 28   LYS L CE    1 
ATOM   6262  N  NZ    . LYS C 2 28  ? 97.363  95.926  165.268 1.00 147.75 ? 28   LYS L NZ    1 
ATOM   6263  N  N     . TYR C 2 29  ? 96.706  101.684 163.143 1.00 138.67 ? 29   TYR L N     1 
ATOM   6264  C  CA    . TYR C 2 29  ? 97.414  102.958 163.254 1.00 138.29 ? 29   TYR L CA    1 
ATOM   6265  C  C     . TYR C 2 29  ? 98.024  103.023 164.654 1.00 136.38 ? 29   TYR L C     1 
ATOM   6266  O  O     . TYR C 2 29  ? 97.387  103.482 165.604 1.00 135.80 ? 29   TYR L O     1 
ATOM   6267  C  CB    . TYR C 2 29  ? 96.458  104.123 162.994 1.00 137.08 ? 29   TYR L CB    1 
ATOM   6268  C  CG    . TYR C 2 29  ? 97.104  105.353 162.397 1.00 136.65 ? 29   TYR L CG    1 
ATOM   6269  C  CD1   . TYR C 2 29  ? 97.778  106.264 163.195 1.00 136.21 ? 29   TYR L CD1   1 
ATOM   6270  C  CD2   . TYR C 2 29  ? 97.026  105.609 161.034 1.00 136.28 ? 29   TYR L CD2   1 
ATOM   6271  C  CE1   . TYR C 2 29  ? 98.365  107.392 162.654 1.00 135.21 ? 29   TYR L CE1   1 
ATOM   6272  C  CE2   . TYR C 2 29  ? 97.610  106.735 160.484 1.00 136.11 ? 29   TYR L CE2   1 
ATOM   6273  C  CZ    . TYR C 2 29  ? 98.279  107.623 161.299 1.00 135.30 ? 29   TYR L CZ    1 
ATOM   6274  O  OH    . TYR C 2 29  ? 98.862  108.745 160.758 1.00 134.49 ? 29   TYR L OH    1 
ATOM   6275  N  N     . ILE C 2 30  ? 99.268  102.554 164.779 1.00 121.58 ? 30   ILE L N     1 
ATOM   6276  C  CA    . ILE C 2 30  ? 99.906  102.495 166.092 1.00 121.77 ? 30   ILE L CA    1 
ATOM   6277  C  C     . ILE C 2 30  ? 100.414 103.870 166.509 1.00 121.38 ? 30   ILE L C     1 
ATOM   6278  O  O     . ILE C 2 30  ? 100.099 104.360 167.600 1.00 122.64 ? 30   ILE L O     1 
ATOM   6279  C  CB    . ILE C 2 30  ? 101.039 101.453 166.097 1.00 122.85 ? 30   ILE L CB    1 
ATOM   6280  C  CG1   . ILE C 2 30  ? 100.467 100.035 166.032 1.00 123.62 ? 30   ILE L CG1   1 
ATOM   6281  C  CG2   . ILE C 2 30  ? 101.915 101.623 167.332 1.00 122.99 ? 30   ILE L CG2   1 
ATOM   6282  C  CD1   . ILE C 2 30  ? 101.484 98.954  166.335 1.00 123.18 ? 30   ILE L CD1   1 
ATOM   6283  N  N     . ALA C 2 31  ? 101.209 104.509 165.654 1.00 110.50 ? 31   ALA L N     1 
ATOM   6284  C  CA    . ALA C 2 31  ? 101.813 105.785 166.007 1.00 110.27 ? 31   ALA L CA    1 
ATOM   6285  C  C     . ALA C 2 31  ? 100.747 106.861 166.164 1.00 111.20 ? 31   ALA L C     1 
ATOM   6286  O  O     . ALA C 2 31  ? 99.784  106.921 165.397 1.00 111.16 ? 31   ALA L O     1 
ATOM   6287  C  CB    . ALA C 2 31  ? 102.828 106.205 164.945 1.00 109.88 ? 31   ALA L CB    1 
ATOM   6288  N  N     . LYS C 2 32  ? 100.924 107.713 167.169 1.00 107.37 ? 32   LYS L N     1 
ATOM   6289  C  CA    . LYS C 2 32  ? 99.985  108.787 167.456 1.00 108.18 ? 32   LYS L CA    1 
ATOM   6290  C  C     . LYS C 2 32  ? 100.734 110.108 167.525 1.00 109.05 ? 32   LYS L C     1 
ATOM   6291  O  O     . LYS C 2 32  ? 101.883 110.158 167.974 1.00 108.12 ? 32   LYS L O     1 
ATOM   6292  C  CB    . LYS C 2 32  ? 99.230  108.536 168.769 1.00 108.95 ? 32   LYS L CB    1 
ATOM   6293  C  CG    . LYS C 2 32  ? 100.112 108.089 169.923 1.00 108.00 ? 32   LYS L CG    1 
ATOM   6294  C  CD    . LYS C 2 32  ? 99.282  107.600 171.100 1.00 108.03 ? 32   LYS L CD    1 
ATOM   6295  C  CE    . LYS C 2 32  ? 100.165 107.033 172.200 1.00 108.31 ? 32   LYS L CE    1 
ATOM   6296  N  NZ    . LYS C 2 32  ? 99.364  106.492 173.333 1.00 107.70 ? 32   LYS L NZ    1 
ATOM   6297  N  N     . PHE C 2 33  ? 100.078 111.174 167.076 1.00 102.19 ? 33   PHE L N     1 
ATOM   6298  C  CA    . PHE C 2 33  ? 100.685 112.497 167.034 1.00 102.61 ? 33   PHE L CA    1 
ATOM   6299  C  C     . PHE C 2 33  ? 100.342 113.270 168.300 1.00 100.55 ? 33   PHE L C     1 
ATOM   6300  O  O     . PHE C 2 33  ? 99.169  113.382 168.670 1.00 102.06 ? 33   PHE L O     1 
ATOM   6301  C  CB    . PHE C 2 33  ? 100.215 113.266 165.799 1.00 100.87 ? 33   PHE L CB    1 
ATOM   6302  C  CG    . PHE C 2 33  ? 100.644 112.646 164.499 1.00 103.10 ? 33   PHE L CG    1 
ATOM   6303  C  CD1   . PHE C 2 33  ? 99.889  111.645 163.910 1.00 103.79 ? 33   PHE L CD1   1 
ATOM   6304  C  CD2   . PHE C 2 33  ? 101.804 113.064 163.869 1.00 102.35 ? 33   PHE L CD2   1 
ATOM   6305  C  CE1   . PHE C 2 33  ? 100.283 111.073 162.716 1.00 103.47 ? 33   PHE L CE1   1 
ATOM   6306  C  CE2   . PHE C 2 33  ? 102.203 112.496 162.675 1.00 99.72  ? 33   PHE L CE2   1 
ATOM   6307  C  CZ    . PHE C 2 33  ? 101.442 111.499 162.097 1.00 101.22 ? 33   PHE L CZ    1 
ATOM   6308  N  N     . GLN C 2 34  ? 101.370 113.800 168.961 1.00 84.87  ? 34   GLN L N     1 
ATOM   6309  C  CA    . GLN C 2 34  ? 101.208 114.605 170.166 1.00 85.21  ? 34   GLN L CA    1 
ATOM   6310  C  C     . GLN C 2 34  ? 102.005 115.887 169.980 1.00 88.26  ? 34   GLN L C     1 
ATOM   6311  O  O     . GLN C 2 34  ? 103.240 115.860 169.992 1.00 87.08  ? 34   GLN L O     1 
ATOM   6312  C  CB    . GLN C 2 34  ? 101.670 113.844 171.409 1.00 89.16  ? 34   GLN L CB    1 
ATOM   6313  C  CG    . GLN C 2 34  ? 101.395 114.567 172.719 1.00 91.03  ? 34   GLN L CG    1 
ATOM   6314  C  CD    . GLN C 2 34  ? 99.921  114.583 173.081 1.00 91.24  ? 34   GLN L CD    1 
ATOM   6315  O  OE1   . GLN C 2 34  ? 99.134  113.791 172.563 1.00 91.49  ? 34   GLN L OE1   1 
ATOM   6316  N  NE2   . GLN C 2 34  ? 99.542  115.489 173.975 1.00 89.96  ? 34   GLN L NE2   1 
ATOM   6317  N  N     . GLY C 2 35  ? 101.303 117.004 169.810 1.00 102.59 ? 35   GLY L N     1 
ATOM   6318  C  CA    . GLY C 2 35  ? 101.983 118.243 169.503 1.00 102.10 ? 35   GLY L CA    1 
ATOM   6319  C  C     . GLY C 2 35  ? 102.496 118.234 168.070 1.00 102.14 ? 35   GLY L C     1 
ATOM   6320  O  O     . GLY C 2 35  ? 102.075 117.439 167.225 1.00 104.56 ? 35   GLY L O     1 
ATOM   6321  N  N     . GLU C 2 36  ? 103.429 119.146 167.803 1.00 82.46  ? 36   GLU L N     1 
ATOM   6322  C  CA    . GLU C 2 36  ? 104.061 119.234 166.496 1.00 80.48  ? 36   GLU L CA    1 
ATOM   6323  C  C     . GLU C 2 36  ? 105.559 118.976 166.523 1.00 84.03  ? 36   GLU L C     1 
ATOM   6324  O  O     . GLU C 2 36  ? 106.158 118.816 165.454 1.00 85.60  ? 36   GLU L O     1 
ATOM   6325  C  CB    . GLU C 2 36  ? 103.806 120.611 165.866 1.00 80.59  ? 36   GLU L CB    1 
ATOM   6326  C  CG    . GLU C 2 36  ? 104.576 121.744 166.522 1.00 82.87  ? 36   GLU L CG    1 
ATOM   6327  C  CD    . GLU C 2 36  ? 104.398 123.063 165.796 1.00 84.63  ? 36   GLU L CD    1 
ATOM   6328  O  OE1   . GLU C 2 36  ? 103.496 123.153 164.938 1.00 84.04  ? 36   GLU L OE1   1 
ATOM   6329  O  OE2   . GLU C 2 36  ? 105.161 124.008 166.083 1.00 84.24  ? 36   GLU L OE2   1 
ATOM   6330  N  N     . ASP C 2 37  ? 106.179 118.929 167.700 1.00 82.69  ? 37   ASP L N     1 
ATOM   6331  C  CA    . ASP C 2 37  ? 107.617 118.745 167.823 1.00 82.45  ? 37   ASP L CA    1 
ATOM   6332  C  C     . ASP C 2 37  ? 107.994 117.359 168.335 1.00 83.25  ? 37   ASP L C     1 
ATOM   6333  O  O     . ASP C 2 37  ? 109.114 117.175 168.822 1.00 78.09  ? 37   ASP L O     1 
ATOM   6334  C  CB    . ASP C 2 37  ? 108.205 119.826 168.733 1.00 81.30  ? 37   ASP L CB    1 
ATOM   6335  C  CG    . ASP C 2 37  ? 108.041 121.221 168.157 1.00 78.10  ? 37   ASP L CG    1 
ATOM   6336  O  OD1   . ASP C 2 37  ? 108.381 121.418 166.973 1.00 75.68  ? 37   ASP L OD1   1 
ATOM   6337  O  OD2   . ASP C 2 37  ? 107.565 122.117 168.885 1.00 77.02  ? 37   ASP L OD2   1 
ATOM   6338  N  N     . THR C 2 38  ? 107.084 116.391 168.247 1.00 91.89  ? 38   THR L N     1 
ATOM   6339  C  CA    . THR C 2 38  ? 107.383 115.010 168.603 1.00 88.18  ? 38   THR L CA    1 
ATOM   6340  C  C     . THR C 2 38  ? 106.255 114.121 168.104 1.00 90.35  ? 38   THR L C     1 
ATOM   6341  O  O     . THR C 2 38  ? 105.178 114.599 167.737 1.00 87.12  ? 38   THR L O     1 
ATOM   6342  C  CB    . THR C 2 38  ? 107.570 114.833 170.115 1.00 88.32  ? 38   THR L CB    1 
ATOM   6343  O  OG1   . THR C 2 38  ? 107.888 113.466 170.401 1.00 88.61  ? 38   THR L OG1   1 
ATOM   6344  C  CG2   . THR C 2 38  ? 106.304 115.222 170.861 1.00 89.65  ? 38   THR L CG2   1 
ATOM   6345  N  N     . VAL C 2 39  ? 106.523 112.818 168.087 1.00 97.95  ? 39   VAL L N     1 
ATOM   6346  C  CA    . VAL C 2 39  ? 105.520 111.807 167.774 1.00 98.26  ? 39   VAL L CA    1 
ATOM   6347  C  C     . VAL C 2 39  ? 105.682 110.659 168.760 1.00 98.44  ? 39   VAL L C     1 
ATOM   6348  O  O     . VAL C 2 39  ? 106.801 110.208 169.027 1.00 99.67  ? 39   VAL L O     1 
ATOM   6349  C  CB    . VAL C 2 39  ? 105.635 111.315 166.315 1.00 97.34  ? 39   VAL L CB    1 
ATOM   6350  C  CG1   . VAL C 2 39  ? 107.070 110.924 165.987 1.00 97.64  ? 39   VAL L CG1   1 
ATOM   6351  C  CG2   . VAL C 2 39  ? 104.688 110.151 166.068 1.00 96.14  ? 39   VAL L CG2   1 
ATOM   6352  N  N     . VAL C 2 40  ? 104.565 110.194 169.312 1.00 102.03 ? 40   VAL L N     1 
ATOM   6353  C  CA    . VAL C 2 40  ? 104.562 109.157 170.337 1.00 106.18 ? 40   VAL L CA    1 
ATOM   6354  C  C     . VAL C 2 40  ? 104.187 107.832 169.688 1.00 107.04 ? 40   VAL L C     1 
ATOM   6355  O  O     . VAL C 2 40  ? 103.158 107.734 169.009 1.00 104.32 ? 40   VAL L O     1 
ATOM   6356  C  CB    . VAL C 2 40  ? 103.600 109.502 171.486 1.00 103.44 ? 40   VAL L CB    1 
ATOM   6357  C  CG1   . VAL C 2 40  ? 103.646 108.422 172.556 1.00 104.38 ? 40   VAL L CG1   1 
ATOM   6358  C  CG2   . VAL C 2 40  ? 103.952 110.860 172.079 1.00 100.30 ? 40   VAL L CG2   1 
ATOM   6359  N  N     . ILE C 2 41  ? 105.027 106.818 169.892 1.00 107.00 ? 41   ILE L N     1 
ATOM   6360  C  CA    . ILE C 2 41  ? 104.766 105.471 169.403 1.00 105.25 ? 41   ILE L CA    1 
ATOM   6361  C  C     . ILE C 2 41  ? 105.311 104.476 170.417 1.00 106.14 ? 41   ILE L C     1 
ATOM   6362  O  O     . ILE C 2 41  ? 106.328 104.721 171.073 1.00 106.87 ? 41   ILE L O     1 
ATOM   6363  C  CB    . ILE C 2 41  ? 105.373 105.233 167.999 1.00 105.86 ? 41   ILE L CB    1 
ATOM   6364  C  CG1   . ILE C 2 41  ? 104.846 103.927 167.395 1.00 105.35 ? 41   ILE L CG1   1 
ATOM   6365  C  CG2   . ILE C 2 41  ? 106.893 105.239 168.051 1.00 105.58 ? 41   ILE L CG2   1 
ATOM   6366  C  CD1   . ILE C 2 41  ? 105.267 103.697 165.960 1.00 102.56 ? 41   ILE L CD1   1 
ATOM   6367  N  N     . ALA C 2 42  ? 104.600 103.355 170.563 1.00 107.82 ? 42   ALA L N     1 
ATOM   6368  C  CA    . ALA C 2 42  ? 104.978 102.282 171.485 1.00 106.38 ? 42   ALA L CA    1 
ATOM   6369  C  C     . ALA C 2 42  ? 105.090 102.793 172.919 1.00 104.17 ? 42   ALA L C     1 
ATOM   6370  O  O     . ALA C 2 42  ? 105.857 102.264 173.726 1.00 102.53 ? 42   ALA L O     1 
ATOM   6371  C  CB    . ALA C 2 42  ? 106.278 101.603 171.046 1.00 103.95 ? 42   ALA L CB    1 
ATOM   6372  N  N     . SER C 2 43  ? 104.306 103.824 173.240 1.00 102.93 ? 43   SER L N     1 
ATOM   6373  C  CA    . SER C 2 43  ? 104.330 104.461 174.557 1.00 104.52 ? 43   SER L CA    1 
ATOM   6374  C  C     . SER C 2 43  ? 105.740 104.921 174.922 1.00 104.41 ? 43   SER L C     1 
ATOM   6375  O  O     . SER C 2 43  ? 106.188 104.787 176.062 1.00 106.01 ? 43   SER L O     1 
ATOM   6376  C  CB    . SER C 2 43  ? 103.761 103.530 175.632 1.00 106.03 ? 43   SER L CB    1 
ATOM   6377  O  OG    . SER C 2 43  ? 104.579 102.387 175.810 1.00 104.29 ? 43   SER L OG    1 
ATOM   6378  N  N     . LYS C 2 44  ? 106.447 105.470 173.936 1.00 101.92 ? 44   LYS L N     1 
ATOM   6379  C  CA    . LYS C 2 44  ? 107.819 105.943 174.125 1.00 102.00 ? 44   LYS L CA    1 
ATOM   6380  C  C     . LYS C 2 44  ? 107.989 107.218 173.316 1.00 101.22 ? 44   LYS L C     1 
ATOM   6381  O  O     . LYS C 2 44  ? 108.074 107.176 172.079 1.00 102.51 ? 44   LYS L O     1 
ATOM   6382  C  CB    . LYS C 2 44  ? 108.845 104.891 173.712 1.00 102.75 ? 44   LYS L CB    1 
ATOM   6383  C  CG    . LYS C 2 44  ? 110.285 105.377 173.748 1.00 101.31 ? 44   LYS L CG    1 
ATOM   6384  C  CD    . LYS C 2 44  ? 110.666 105.888 175.131 1.00 104.74 ? 44   LYS L CD    1 
ATOM   6385  C  CE    . LYS C 2 44  ? 110.586 104.785 176.175 1.00 105.29 ? 44   LYS L CE    1 
ATOM   6386  N  NZ    . LYS C 2 44  ? 110.873 105.295 177.544 1.00 104.19 ? 44   LYS L NZ    1 
ATOM   6387  N  N     . PRO C 2 45  ? 108.023 108.376 173.972 1.00 105.91 ? 45   PRO L N     1 
ATOM   6388  C  CA    . PRO C 2 45  ? 108.142 109.637 173.232 1.00 109.14 ? 45   PRO L CA    1 
ATOM   6389  C  C     . PRO C 2 45  ? 109.464 109.728 172.484 1.00 109.55 ? 45   PRO L C     1 
ATOM   6390  O  O     . PRO C 2 45  ? 110.515 109.324 172.985 1.00 107.40 ? 45   PRO L O     1 
ATOM   6391  C  CB    . PRO C 2 45  ? 108.042 110.704 174.330 1.00 108.26 ? 45   PRO L CB    1 
ATOM   6392  C  CG    . PRO C 2 45  ? 107.405 110.008 175.494 1.00 109.48 ? 45   PRO L CG    1 
ATOM   6393  C  CD    . PRO C 2 45  ? 107.882 108.593 175.420 1.00 106.62 ? 45   PRO L CD    1 
ATOM   6394  N  N     . TYR C 2 46  ? 109.399 110.275 171.272 1.00 110.85 ? 46   TYR L N     1 
ATOM   6395  C  CA    . TYR C 2 46  ? 110.573 110.532 170.448 1.00 108.02 ? 46   TYR L CA    1 
ATOM   6396  C  C     . TYR C 2 46  ? 110.592 112.011 170.096 1.00 106.74 ? 46   TYR L C     1 
ATOM   6397  O  O     . TYR C 2 46  ? 109.689 112.499 169.407 1.00 101.05 ? 46   TYR L O     1 
ATOM   6398  C  CB    . TYR C 2 46  ? 110.562 109.674 169.180 1.00 106.13 ? 46   TYR L CB    1 
ATOM   6399  C  CG    . TYR C 2 46  ? 110.788 108.202 169.433 1.00 108.01 ? 46   TYR L CG    1 
ATOM   6400  C  CD1   . TYR C 2 46  ? 112.069 107.695 169.603 1.00 108.07 ? 46   TYR L CD1   1 
ATOM   6401  C  CD2   . TYR C 2 46  ? 109.720 107.317 169.493 1.00 107.08 ? 46   TYR L CD2   1 
ATOM   6402  C  CE1   . TYR C 2 46  ? 112.280 106.349 169.834 1.00 108.02 ? 46   TYR L CE1   1 
ATOM   6403  C  CE2   . TYR C 2 46  ? 109.922 105.969 169.724 1.00 109.08 ? 46   TYR L CE2   1 
ATOM   6404  C  CZ    . TYR C 2 46  ? 111.204 105.491 169.893 1.00 109.28 ? 46   TYR L CZ    1 
ATOM   6405  O  OH    . TYR C 2 46  ? 111.409 104.150 170.121 1.00 108.09 ? 46   TYR L OH    1 
ATOM   6406  N  N     . ALA C 2 47  ? 111.616 112.718 170.563 1.00 100.32 ? 47   ALA L N     1 
ATOM   6407  C  CA    . ALA C 2 47  ? 111.716 114.158 170.372 1.00 99.38  ? 47   ALA L CA    1 
ATOM   6408  C  C     . ALA C 2 47  ? 112.431 114.451 169.059 1.00 99.46  ? 47   ALA L C     1 
ATOM   6409  O  O     . ALA C 2 47  ? 113.559 113.994 168.844 1.00 98.37  ? 47   ALA L O     1 
ATOM   6410  C  CB    . ALA C 2 47  ? 112.452 114.808 171.543 1.00 97.32  ? 47   ALA L CB    1 
ATOM   6411  N  N     . PHE C 2 48  ? 111.774 115.211 168.187 1.00 83.27  ? 48   PHE L N     1 
ATOM   6412  C  CA    . PHE C 2 48  ? 112.349 115.639 166.922 1.00 77.67  ? 48   PHE L CA    1 
ATOM   6413  C  C     . PHE C 2 48  ? 112.160 117.141 166.777 1.00 76.44  ? 48   PHE L C     1 
ATOM   6414  O  O     . PHE C 2 48  ? 111.429 117.774 167.542 1.00 81.16  ? 48   PHE L O     1 
ATOM   6415  C  CB    . PHE C 2 48  ? 111.715 114.902 165.736 1.00 72.84  ? 48   PHE L CB    1 
ATOM   6416  C  CG    . PHE C 2 48  ? 112.089 113.452 165.658 1.00 76.93  ? 48   PHE L CG    1 
ATOM   6417  C  CD1   . PHE C 2 48  ? 113.241 113.055 165.004 1.00 73.15  ? 48   PHE L CD1   1 
ATOM   6418  C  CD2   . PHE C 2 48  ? 111.288 112.486 166.239 1.00 80.53  ? 48   PHE L CD2   1 
ATOM   6419  C  CE1   . PHE C 2 48  ? 113.588 111.725 164.934 1.00 72.58  ? 48   PHE L CE1   1 
ATOM   6420  C  CE2   . PHE C 2 48  ? 111.631 111.153 166.169 1.00 76.83  ? 48   PHE L CE2   1 
ATOM   6421  C  CZ    . PHE C 2 48  ? 112.783 110.773 165.514 1.00 72.91  ? 48   PHE L CZ    1 
ATOM   6422  N  N     . ASP C 2 49  ? 112.845 117.721 165.791 1.00 56.68  ? 49   ASP L N     1 
ATOM   6423  C  CA    . ASP C 2 49  ? 112.683 119.149 165.546 1.00 56.57  ? 49   ASP L CA    1 
ATOM   6424  C  C     . ASP C 2 49  ? 111.281 119.463 165.039 1.00 60.47  ? 49   ASP L C     1 
ATOM   6425  O  O     . ASP C 2 49  ? 110.690 120.481 165.419 1.00 63.32  ? 49   ASP L O     1 
ATOM   6426  C  CB    . ASP C 2 49  ? 113.737 119.640 164.557 1.00 49.75  ? 49   ASP L CB    1 
ATOM   6427  C  CG    . ASP C 2 49  ? 113.926 121.139 164.610 1.00 46.56  ? 49   ASP L CG    1 
ATOM   6428  O  OD1   . ASP C 2 49  ? 113.265 121.793 165.443 1.00 52.96  ? 49   ASP L OD1   1 
ATOM   6429  O  OD2   . ASP C 2 49  ? 114.737 121.666 163.822 1.00 48.66  ? 49   ASP L OD2   1 
ATOM   6430  N  N     . ARG C 2 50  ? 110.731 118.599 164.189 1.00 67.06  ? 50   ARG L N     1 
ATOM   6431  C  CA    . ARG C 2 50  ? 109.399 118.799 163.640 1.00 60.66  ? 50   ARG L CA    1 
ATOM   6432  C  C     . ARG C 2 50  ? 108.905 117.477 163.077 1.00 66.42  ? 50   ARG L C     1 
ATOM   6433  O  O     . ARG C 2 50  ? 109.664 116.751 162.432 1.00 72.99  ? 50   ARG L O     1 
ATOM   6434  C  CB    . ARG C 2 50  ? 109.406 119.877 162.554 1.00 56.44  ? 50   ARG L CB    1 
ATOM   6435  C  CG    . ARG C 2 50  ? 108.071 120.112 161.892 1.00 62.02  ? 50   ARG L CG    1 
ATOM   6436  C  CD    . ARG C 2 50  ? 107.990 121.520 161.332 1.00 67.88  ? 50   ARG L CD    1 
ATOM   6437  N  NE    . ARG C 2 50  ? 109.211 121.911 160.637 1.00 70.43  ? 50   ARG L NE    1 
ATOM   6438  C  CZ    . ARG C 2 50  ? 110.110 122.760 161.119 1.00 70.40  ? 50   ARG L CZ    1 
ATOM   6439  N  NH1   . ARG C 2 50  ? 109.962 123.321 162.308 1.00 71.61  ? 50   ARG L NH1   1 
ATOM   6440  N  NH2   . ARG C 2 50  ? 111.185 123.048 160.393 1.00 67.78  ? 50   ARG L NH2   1 
ATOM   6441  N  N     . VAL C 2 51  ? 107.634 117.174 163.322 1.00 86.45  ? 51   VAL L N     1 
ATOM   6442  C  CA    . VAL C 2 51  ? 107.014 115.934 162.870 1.00 89.89  ? 51   VAL L CA    1 
ATOM   6443  C  C     . VAL C 2 51  ? 105.866 116.285 161.935 1.00 89.84  ? 51   VAL L C     1 
ATOM   6444  O  O     . VAL C 2 51  ? 105.000 117.096 162.285 1.00 89.46  ? 51   VAL L O     1 
ATOM   6445  C  CB    . VAL C 2 51  ? 106.519 115.080 164.051 1.00 92.88  ? 51   VAL L CB    1 
ATOM   6446  C  CG1   . VAL C 2 51  ? 105.783 113.849 163.545 1.00 91.08  ? 51   VAL L CG1   1 
ATOM   6447  C  CG2   . VAL C 2 51  ? 107.688 114.679 164.935 1.00 92.94  ? 51   VAL L CG2   1 
ATOM   6448  N  N     . PHE C 2 52  ? 105.863 115.678 160.753 1.00 90.03  ? 52   PHE L N     1 
ATOM   6449  C  CA    . PHE C 2 52  ? 104.828 115.905 159.756 1.00 92.26  ? 52   PHE L CA    1 
ATOM   6450  C  C     . PHE C 2 52  ? 103.718 114.874 159.908 1.00 94.50  ? 52   PHE L C     1 
ATOM   6451  O  O     . PHE C 2 52  ? 103.980 113.698 160.178 1.00 96.33  ? 52   PHE L O     1 
ATOM   6452  C  CB    . PHE C 2 52  ? 105.406 115.841 158.342 1.00 91.61  ? 52   PHE L CB    1 
ATOM   6453  C  CG    . PHE C 2 52  ? 106.571 116.762 158.117 1.00 91.74  ? 52   PHE L CG    1 
ATOM   6454  C  CD1   . PHE C 2 52  ? 106.414 118.135 158.209 1.00 94.18  ? 52   PHE L CD1   1 
ATOM   6455  C  CD2   . PHE C 2 52  ? 107.819 116.256 157.801 1.00 89.25  ? 52   PHE L CD2   1 
ATOM   6456  C  CE1   . PHE C 2 52  ? 107.485 118.983 157.998 1.00 93.09  ? 52   PHE L CE1   1 
ATOM   6457  C  CE2   . PHE C 2 52  ? 108.890 117.097 157.589 1.00 87.46  ? 52   PHE L CE2   1 
ATOM   6458  C  CZ    . PHE C 2 52  ? 108.724 118.461 157.687 1.00 89.00  ? 52   PHE L CZ    1 
ATOM   6459  N  N     . GLN C 2 53  ? 102.478 115.324 159.734 1.00 100.94 ? 53   GLN L N     1 
ATOM   6460  C  CA    . GLN C 2 53  ? 101.340 114.422 159.768 1.00 101.40 ? 53   GLN L CA    1 
ATOM   6461  C  C     . GLN C 2 53  ? 101.302 113.566 158.503 1.00 103.61 ? 53   GLN L C     1 
ATOM   6462  O  O     . GLN C 2 53  ? 102.045 113.786 157.541 1.00 102.78 ? 53   GLN L O     1 
ATOM   6463  C  CB    . GLN C 2 53  ? 100.036 115.204 159.921 1.00 99.03  ? 53   GLN L CB    1 
ATOM   6464  C  CG    . GLN C 2 53  ? 99.640  115.491 161.359 1.00 100.41 ? 53   GLN L CG    1 
ATOM   6465  C  CD    . GLN C 2 53  ? 100.600 116.435 162.055 1.00 101.51 ? 53   GLN L CD    1 
ATOM   6466  O  OE1   . GLN C 2 53  ? 101.253 117.259 161.415 1.00 102.56 ? 53   GLN L OE1   1 
ATOM   6467  N  NE2   . GLN C 2 53  ? 100.690 116.318 163.375 1.00 100.65 ? 53   GLN L NE2   1 
ATOM   6468  N  N     . SER C 2 54  ? 100.416 112.568 158.518 1.00 107.96 ? 54   SER L N     1 
ATOM   6469  C  CA    . SER C 2 54  ? 100.295 111.665 157.379 1.00 106.72 ? 54   SER L CA    1 
ATOM   6470  C  C     . SER C 2 54  ? 99.799  112.398 156.137 1.00 108.65 ? 54   SER L C     1 
ATOM   6471  O  O     . SER C 2 54  ? 100.248 112.115 155.020 1.00 108.70 ? 54   SER L O     1 
ATOM   6472  C  CB    . SER C 2 54  ? 99.361  110.507 157.730 1.00 105.29 ? 54   SER L CB    1 
ATOM   6473  O  OG    . SER C 2 54  ? 99.729  109.914 158.962 1.00 104.48 ? 54   SER L OG    1 
ATOM   6474  N  N     . SER C 2 55  ? 98.879  113.344 156.311 1.00 103.08 ? 55   SER L N     1 
ATOM   6475  C  CA    . SER C 2 55  ? 98.225  114.019 155.198 1.00 99.58  ? 55   SER L CA    1 
ATOM   6476  C  C     . SER C 2 55  ? 98.848  115.369 154.857 1.00 98.99  ? 55   SER L C     1 
ATOM   6477  O  O     . SER C 2 55  ? 98.265  116.120 154.069 1.00 98.97  ? 55   SER L O     1 
ATOM   6478  C  CB    . SER C 2 55  ? 96.735  114.205 155.501 1.00 99.88  ? 55   SER L CB    1 
ATOM   6479  O  OG    . SER C 2 55  ? 96.103  112.960 155.742 1.00 101.44 ? 55   SER L OG    1 
ATOM   6480  N  N     . THR C 2 56  ? 100.006 115.697 155.428 1.00 98.90  ? 56   THR L N     1 
ATOM   6481  C  CA    . THR C 2 56  ? 100.618 116.995 155.171 1.00 99.55  ? 56   THR L CA    1 
ATOM   6482  C  C     . THR C 2 56  ? 101.061 117.113 153.717 1.00 96.69  ? 56   THR L C     1 
ATOM   6483  O  O     . THR C 2 56  ? 101.365 116.121 153.050 1.00 96.48  ? 56   THR L O     1 
ATOM   6484  C  CB    . THR C 2 56  ? 101.813 117.223 156.099 1.00 98.70  ? 56   THR L CB    1 
ATOM   6485  O  OG1   . THR C 2 56  ? 102.696 116.095 156.040 1.00 99.55  ? 56   THR L OG1   1 
ATOM   6486  C  CG2   . THR C 2 56  ? 101.348 117.437 157.527 1.00 93.85  ? 56   THR L CG2   1 
ATOM   6487  N  N     . SER C 2 57  ? 101.089 118.349 153.227 1.00 84.56  ? 57   SER L N     1 
ATOM   6488  C  CA    . SER C 2 57  ? 101.464 118.635 151.852 1.00 86.64  ? 57   SER L CA    1 
ATOM   6489  C  C     . SER C 2 57  ? 102.976 118.803 151.727 1.00 84.30  ? 57   SER L C     1 
ATOM   6490  O  O     . SER C 2 57  ? 103.671 119.159 152.682 1.00 80.26  ? 57   SER L O     1 
ATOM   6491  C  CB    . SER C 2 57  ? 100.751 119.891 151.348 1.00 85.65  ? 57   SER L CB    1 
ATOM   6492  O  OG    . SER C 2 57  ? 101.046 121.010 152.166 1.00 84.96  ? 57   SER L OG    1 
ATOM   6493  N  N     . GLN C 2 58  ? 103.479 118.538 150.520 1.00 68.26  ? 58   GLN L N     1 
ATOM   6494  C  CA    . GLN C 2 58  ? 104.914 118.603 150.269 1.00 67.32  ? 58   GLN L CA    1 
ATOM   6495  C  C     . GLN C 2 58  ? 105.427 120.035 150.206 1.00 68.44  ? 58   GLN L C     1 
ATOM   6496  O  O     . GLN C 2 58  ? 106.592 120.285 150.537 1.00 74.31  ? 58   GLN L O     1 
ATOM   6497  C  CB    . GLN C 2 58  ? 105.247 117.853 148.982 1.00 64.48  ? 58   GLN L CB    1 
ATOM   6498  C  CG    . GLN C 2 58  ? 104.255 118.077 147.868 1.00 65.47  ? 58   GLN L CG    1 
ATOM   6499  C  CD    . GLN C 2 58  ? 104.233 116.927 146.890 1.00 66.11  ? 58   GLN L CD    1 
ATOM   6500  O  OE1   . GLN C 2 58  ? 105.276 116.488 146.409 1.00 68.66  ? 58   GLN L OE1   1 
ATOM   6501  N  NE2   . GLN C 2 58  ? 103.040 116.428 146.590 1.00 68.08  ? 58   GLN L NE2   1 
ATOM   6502  N  N     . GLU C 2 59  ? 104.586 120.982 149.786 1.00 63.17  ? 59   GLU L N     1 
ATOM   6503  C  CA    . GLU C 2 59  ? 104.972 122.385 149.882 1.00 67.53  ? 59   GLU L CA    1 
ATOM   6504  C  C     . GLU C 2 59  ? 105.249 122.775 151.329 1.00 63.71  ? 59   GLU L C     1 
ATOM   6505  O  O     . GLU C 2 59  ? 106.141 123.585 151.602 1.00 58.02  ? 59   GLU L O     1 
ATOM   6506  C  CB    . GLU C 2 59  ? 103.884 123.280 149.289 1.00 67.40  ? 59   GLU L CB    1 
ATOM   6507  C  CG    . GLU C 2 59  ? 104.195 124.766 149.392 1.00 68.29  ? 59   GLU L CG    1 
ATOM   6508  C  CD    . GLU C 2 59  ? 103.063 125.641 148.898 1.00 64.87  ? 59   GLU L CD    1 
ATOM   6509  O  OE1   . GLU C 2 59  ? 102.124 125.106 148.272 1.00 67.15  ? 59   GLU L OE1   1 
ATOM   6510  O  OE2   . GLU C 2 59  ? 103.111 126.865 149.143 1.00 61.77  ? 59   GLU L OE2   1 
ATOM   6511  N  N     . GLN C 2 60  ? 104.495 122.203 152.270 1.00 74.00  ? 60   GLN L N     1 
ATOM   6512  C  CA    . GLN C 2 60  ? 104.714 122.503 153.681 1.00 78.59  ? 60   GLN L CA    1 
ATOM   6513  C  C     . GLN C 2 60  ? 106.113 122.088 154.119 1.00 78.68  ? 60   GLN L C     1 
ATOM   6514  O  O     . GLN C 2 60  ? 106.838 122.870 154.745 1.00 80.39  ? 60   GLN L O     1 
ATOM   6515  C  CB    . GLN C 2 60  ? 103.653 121.810 154.536 1.00 79.82  ? 60   GLN L CB    1 
ATOM   6516  C  CG    . GLN C 2 60  ? 103.885 121.928 156.036 1.00 79.86  ? 60   GLN L CG    1 
ATOM   6517  C  CD    . GLN C 2 60  ? 103.447 123.268 156.597 1.00 79.45  ? 60   GLN L CD    1 
ATOM   6518  O  OE1   . GLN C 2 60  ? 102.923 124.116 155.876 1.00 79.40  ? 60   GLN L OE1   1 
ATOM   6519  N  NE2   . GLN C 2 60  ? 103.663 123.464 157.893 1.00 77.55  ? 60   GLN L NE2   1 
ATOM   6520  N  N     . VAL C 2 61  ? 106.515 120.857 153.790 1.00 80.10  ? 61   VAL L N     1 
ATOM   6521  C  CA    . VAL C 2 61  ? 107.840 120.398 154.193 1.00 82.75  ? 61   VAL L CA    1 
ATOM   6522  C  C     . VAL C 2 61  ? 108.923 121.160 153.439 1.00 80.76  ? 61   VAL L C     1 
ATOM   6523  O  O     . VAL C 2 61  ? 110.000 121.422 153.988 1.00 82.34  ? 61   VAL L O     1 
ATOM   6524  C  CB    . VAL C 2 61  ? 107.972 118.871 154.018 1.00 82.88  ? 61   VAL L CB    1 
ATOM   6525  C  CG1   . VAL C 2 61  ? 106.728 118.166 154.543 1.00 83.09  ? 61   VAL L CG1   1 
ATOM   6526  C  CG2   . VAL C 2 61  ? 108.240 118.489 152.569 1.00 77.57  ? 61   VAL L CG2   1 
ATOM   6527  N  N     . TYR C 2 62  ? 108.660 121.545 152.186 1.00 70.95  ? 62   TYR L N     1 
ATOM   6528  C  CA    . TYR C 2 62  ? 109.634 122.344 151.451 1.00 71.87  ? 62   TYR L CA    1 
ATOM   6529  C  C     . TYR C 2 62  ? 109.852 123.697 152.121 1.00 74.31  ? 62   TYR L C     1 
ATOM   6530  O  O     . TYR C 2 62  ? 110.992 124.147 152.283 1.00 76.07  ? 62   TYR L O     1 
ATOM   6531  C  CB    . TYR C 2 62  ? 109.188 122.532 150.001 1.00 73.25  ? 62   TYR L CB    1 
ATOM   6532  C  CG    . TYR C 2 62  ? 109.941 123.646 149.318 1.00 71.68  ? 62   TYR L CG    1 
ATOM   6533  C  CD1   . TYR C 2 62  ? 111.242 123.459 148.882 1.00 71.43  ? 62   TYR L CD1   1 
ATOM   6534  C  CD2   . TYR C 2 62  ? 109.359 124.890 149.128 1.00 71.69  ? 62   TYR L CD2   1 
ATOM   6535  C  CE1   . TYR C 2 62  ? 111.940 124.476 148.273 1.00 68.17  ? 62   TYR L CE1   1 
ATOM   6536  C  CE2   . TYR C 2 62  ? 110.049 125.912 148.519 1.00 69.99  ? 62   TYR L CE2   1 
ATOM   6537  C  CZ    . TYR C 2 62  ? 111.338 125.700 148.094 1.00 67.53  ? 62   TYR L CZ    1 
ATOM   6538  O  OH    . TYR C 2 62  ? 112.029 126.715 147.487 1.00 70.54  ? 62   TYR L OH    1 
ATOM   6539  N  N     . ASN C 2 63  ? 108.762 124.362 152.516 1.00 69.19  ? 63   ASN L N     1 
ATOM   6540  C  CA    . ASN C 2 63  ? 108.883 125.655 153.180 1.00 65.57  ? 63   ASN L CA    1 
ATOM   6541  C  C     . ASN C 2 63  ? 109.514 125.523 154.557 1.00 67.20  ? 63   ASN L C     1 
ATOM   6542  O  O     . ASN C 2 63  ? 110.239 126.423 154.994 1.00 65.32  ? 63   ASN L O     1 
ATOM   6543  C  CB    . ASN C 2 63  ? 107.515 126.323 153.299 1.00 65.47  ? 63   ASN L CB    1 
ATOM   6544  C  CG    . ASN C 2 63  ? 106.932 126.702 151.956 1.00 71.67  ? 63   ASN L CG    1 
ATOM   6545  O  OD1   . ASN C 2 63  ? 107.267 126.111 150.933 1.00 70.32  ? 63   ASN L OD1   1 
ATOM   6546  N  ND2   . ASN C 2 63  ? 106.053 127.697 151.952 1.00 74.34  ? 63   ASN L ND2   1 
ATOM   6547  N  N     . ASP C 2 64  ? 109.247 124.421 155.256 1.00 78.14  ? 64   ASP L N     1 
ATOM   6548  C  CA    . ASP C 2 64  ? 109.812 124.225 156.583 1.00 79.58  ? 64   ASP L CA    1 
ATOM   6549  C  C     . ASP C 2 64  ? 111.275 123.801 156.554 1.00 78.23  ? 64   ASP L C     1 
ATOM   6550  O  O     . ASP C 2 64  ? 111.975 123.988 157.555 1.00 81.09  ? 64   ASP L O     1 
ATOM   6551  C  CB    . ASP C 2 64  ? 108.994 123.186 157.354 1.00 82.27  ? 64   ASP L CB    1 
ATOM   6552  C  CG    . ASP C 2 64  ? 107.573 123.646 157.629 1.00 83.67  ? 64   ASP L CG    1 
ATOM   6553  O  OD1   . ASP C 2 64  ? 107.285 124.844 157.426 1.00 84.34  ? 64   ASP L OD1   1 
ATOM   6554  O  OD2   . ASP C 2 64  ? 106.743 122.810 158.044 1.00 79.53  ? 64   ASP L OD2   1 
ATOM   6555  N  N     . CYS C 2 65  ? 111.758 123.237 155.446 1.00 78.52  ? 65   CYS L N     1 
ATOM   6556  C  CA    . CYS C 2 65  ? 113.099 122.662 155.429 1.00 81.07  ? 65   CYS L CA    1 
ATOM   6557  C  C     . CYS C 2 65  ? 114.033 123.303 154.415 1.00 82.08  ? 65   CYS L C     1 
ATOM   6558  O  O     . CYS C 2 65  ? 115.168 123.650 154.764 1.00 82.78  ? 65   CYS L O     1 
ATOM   6559  C  CB    . CYS C 2 65  ? 113.012 121.148 155.167 1.00 80.81  ? 65   CYS L CB    1 
ATOM   6560  S  SG    . CYS C 2 65  ? 113.014 120.678 153.422 1.00 90.05  ? 65   CYS L SG    1 
ATOM   6561  N  N     . ALA C 2 66  ? 113.598 123.474 153.166 1.00 64.10  ? 66   ALA L N     1 
ATOM   6562  C  CA    . ALA C 2 66  ? 114.543 123.688 152.076 1.00 60.02  ? 66   ALA L CA    1 
ATOM   6563  C  C     . ALA C 2 66  ? 114.822 125.151 151.760 1.00 59.12  ? 66   ALA L C     1 
ATOM   6564  O  O     . ALA C 2 66  ? 115.922 125.463 151.291 1.00 62.57  ? 66   ALA L O     1 
ATOM   6565  C  CB    . ALA C 2 66  ? 114.048 122.989 150.809 1.00 59.40  ? 66   ALA L CB    1 
ATOM   6566  N  N     . LYS C 2 67  ? 113.870 126.057 151.997 1.00 61.02  ? 67   LYS L N     1 
ATOM   6567  C  CA    . LYS C 2 67  ? 114.047 127.444 151.567 1.00 64.80  ? 67   LYS L CA    1 
ATOM   6568  C  C     . LYS C 2 67  ? 115.281 128.076 152.205 1.00 65.77  ? 67   LYS L C     1 
ATOM   6569  O  O     . LYS C 2 67  ? 116.017 128.832 151.550 1.00 67.74  ? 67   LYS L O     1 
ATOM   6570  C  CB    . LYS C 2 67  ? 112.795 128.256 151.897 1.00 67.41  ? 67   LYS L CB    1 
ATOM   6571  C  CG    . LYS C 2 67  ? 112.810 129.675 151.356 1.00 63.59  ? 67   LYS L CG    1 
ATOM   6572  C  CD    . LYS C 2 67  ? 111.490 130.379 151.621 1.00 63.29  ? 67   LYS L CD    1 
ATOM   6573  C  CE    . LYS C 2 67  ? 110.325 129.619 151.007 1.00 65.04  ? 67   LYS L CE    1 
ATOM   6574  N  NZ    . LYS C 2 67  ? 110.487 129.444 149.537 1.00 65.27  ? 67   LYS L NZ    1 
ATOM   6575  N  N     . LYS C 2 68  ? 115.523 127.774 153.482 1.00 56.93  ? 68   LYS L N     1 
ATOM   6576  C  CA    . LYS C 2 68  ? 116.735 128.246 154.138 1.00 55.20  ? 68   LYS L CA    1 
ATOM   6577  C  C     . LYS C 2 68  ? 117.974 127.732 153.419 1.00 62.92  ? 68   LYS L C     1 
ATOM   6578  O  O     . LYS C 2 68  ? 118.948 128.473 153.235 1.00 64.95  ? 68   LYS L O     1 
ATOM   6579  C  CB    . LYS C 2 68  ? 116.736 127.814 155.604 1.00 57.73  ? 68   LYS L CB    1 
ATOM   6580  C  CG    . LYS C 2 68  ? 118.034 128.087 156.346 1.00 61.74  ? 68   LYS L CG    1 
ATOM   6581  C  CD    . LYS C 2 68  ? 118.799 126.799 156.611 1.00 60.85  ? 68   LYS L CD    1 
ATOM   6582  C  CE    . LYS C 2 68  ? 117.957 125.807 157.396 1.00 62.80  ? 68   LYS L CE    1 
ATOM   6583  N  NZ    . LYS C 2 68  ? 118.687 124.533 157.642 1.00 60.53  ? 68   LYS L NZ    1 
ATOM   6584  N  N     . ILE C 2 69  ? 117.950 126.466 152.994 1.00 62.72  ? 69   ILE L N     1 
ATOM   6585  C  CA    . ILE C 2 69  ? 119.058 125.922 152.217 1.00 52.57  ? 69   ILE L CA    1 
ATOM   6586  C  C     . ILE C 2 69  ? 119.224 126.696 150.918 1.00 51.71  ? 69   ILE L C     1 
ATOM   6587  O  O     . ILE C 2 69  ? 120.348 126.968 150.484 1.00 56.99  ? 69   ILE L O     1 
ATOM   6588  C  CB    . ILE C 2 69  ? 118.848 124.418 151.960 1.00 55.09  ? 69   ILE L CB    1 
ATOM   6589  C  CG1   . ILE C 2 69  ? 118.620 123.678 153.279 1.00 56.52  ? 69   ILE L CG1   1 
ATOM   6590  C  CG2   . ILE C 2 69  ? 120.038 123.832 151.217 1.00 53.92  ? 69   ILE L CG2   1 
ATOM   6591  C  CD1   . ILE C 2 69  ? 119.773 123.791 154.251 1.00 56.04  ? 69   ILE L CD1   1 
ATOM   6592  N  N     . VAL C 2 70  ? 118.111 127.081 150.285 1.00 46.65  ? 70   VAL L N     1 
ATOM   6593  C  CA    . VAL C 2 70  ? 118.193 127.818 149.025 1.00 37.82  ? 70   VAL L CA    1 
ATOM   6594  C  C     . VAL C 2 70  ? 118.906 129.146 149.232 1.00 43.51  ? 70   VAL L C     1 
ATOM   6595  O  O     . VAL C 2 70  ? 119.868 129.470 148.524 1.00 51.94  ? 70   VAL L O     1 
ATOM   6596  C  CB    . VAL C 2 70  ? 116.793 128.032 148.425 1.00 42.31  ? 70   VAL L CB    1 
ATOM   6597  C  CG1   . VAL C 2 70  ? 116.907 128.531 146.996 1.00 44.41  ? 70   VAL L CG1   1 
ATOM   6598  C  CG2   . VAL C 2 70  ? 115.987 126.758 148.480 1.00 50.12  ? 70   VAL L CG2   1 
ATOM   6599  N  N     . LYS C 2 71  ? 118.464 129.930 150.218 1.00 49.91  ? 71   LYS L N     1 
ATOM   6600  C  CA    . LYS C 2 71  ? 119.085 131.240 150.402 1.00 53.66  ? 71   LYS L CA    1 
ATOM   6601  C  C     . LYS C 2 71  ? 120.533 131.110 150.861 1.00 47.93  ? 71   LYS L C     1 
ATOM   6602  O  O     . LYS C 2 71  ? 121.403 131.876 150.422 1.00 52.69  ? 71   LYS L O     1 
ATOM   6603  C  CB    . LYS C 2 71  ? 118.278 132.094 151.382 1.00 56.21  ? 71   LYS L CB    1 
ATOM   6604  C  CG    . LYS C 2 71  ? 117.790 131.389 152.632 1.00 54.67  ? 71   LYS L CG    1 
ATOM   6605  C  CD    . LYS C 2 71  ? 117.204 132.401 153.610 1.00 57.17  ? 71   LYS L CD    1 
ATOM   6606  C  CE    . LYS C 2 71  ? 116.282 131.746 154.624 1.00 58.05  ? 71   LYS L CE    1 
ATOM   6607  N  NZ    . LYS C 2 71  ? 115.036 131.233 153.992 1.00 61.52  ? 71   LYS L NZ    1 
ATOM   6608  N  N     . ASP C 2 72  ? 120.819 130.138 151.730 1.00 44.54  ? 72   ASP L N     1 
ATOM   6609  C  CA    . ASP C 2 72  ? 122.174 129.992 152.247 1.00 50.59  ? 72   ASP L CA    1 
ATOM   6610  C  C     . ASP C 2 72  ? 123.141 129.521 151.166 1.00 51.21  ? 72   ASP L C     1 
ATOM   6611  O  O     . ASP C 2 72  ? 124.290 129.976 151.118 1.00 49.53  ? 72   ASP L O     1 
ATOM   6612  C  CB    . ASP C 2 72  ? 122.168 129.040 153.442 1.00 54.96  ? 72   ASP L CB    1 
ATOM   6613  C  CG    . ASP C 2 72  ? 121.402 129.605 154.624 1.00 55.85  ? 72   ASP L CG    1 
ATOM   6614  O  OD1   . ASP C 2 72  ? 121.057 130.805 154.589 1.00 57.19  ? 72   ASP L OD1   1 
ATOM   6615  O  OD2   . ASP C 2 72  ? 121.130 128.853 155.581 1.00 48.97  ? 72   ASP L OD2   1 
ATOM   6616  N  N     . VAL C 2 73  ? 122.704 128.612 150.289 1.00 49.47  ? 73   VAL L N     1 
ATOM   6617  C  CA    . VAL C 2 73  ? 123.551 128.218 149.170 1.00 42.81  ? 73   VAL L CA    1 
ATOM   6618  C  C     . VAL C 2 73  ? 123.682 129.359 148.179 1.00 42.54  ? 73   VAL L C     1 
ATOM   6619  O  O     . VAL C 2 73  ? 124.702 129.479 147.491 1.00 46.12  ? 73   VAL L O     1 
ATOM   6620  C  CB    . VAL C 2 73  ? 123.018 126.939 148.496 1.00 43.17  ? 73   VAL L CB    1 
ATOM   6621  C  CG1   . VAL C 2 73  ? 121.893 127.266 147.535 1.00 44.37  ? 73   VAL L CG1   1 
ATOM   6622  C  CG2   . VAL C 2 73  ? 124.144 126.218 147.771 1.00 40.31  ? 73   VAL L CG2   1 
ATOM   6623  N  N     . LEU C 2 74  ? 122.663 130.215 148.082 1.00 42.10  ? 74   LEU L N     1 
ATOM   6624  C  CA    . LEU C 2 74  ? 122.773 131.371 147.207 1.00 37.79  ? 74   LEU L CA    1 
ATOM   6625  C  C     . LEU C 2 74  ? 123.840 132.333 147.704 1.00 44.39  ? 74   LEU L C     1 
ATOM   6626  O  O     . LEU C 2 74  ? 124.580 132.915 146.903 1.00 42.82  ? 74   LEU L O     1 
ATOM   6627  C  CB    . LEU C 2 74  ? 121.425 132.074 147.094 1.00 40.75  ? 74   LEU L CB    1 
ATOM   6628  C  CG    . LEU C 2 74  ? 121.246 132.891 145.820 1.00 49.09  ? 74   LEU L CG    1 
ATOM   6629  C  CD1   . LEU C 2 74  ? 121.508 132.031 144.599 1.00 47.13  ? 74   LEU L CD1   1 
ATOM   6630  C  CD2   . LEU C 2 74  ? 119.853 133.457 145.780 1.00 49.11  ? 74   LEU L CD2   1 
ATOM   6631  N  N     . GLU C 2 75  ? 123.937 132.521 149.022 1.00 54.79  ? 75   GLU L N     1 
ATOM   6632  C  CA    . GLU C 2 75  ? 124.920 133.484 149.520 1.00 51.08  ? 75   GLU L CA    1 
ATOM   6633  C  C     . GLU C 2 75  ? 126.318 132.875 149.605 1.00 46.45  ? 75   GLU L C     1 
ATOM   6634  O  O     . GLU C 2 75  ? 127.200 133.214 148.812 1.00 53.91  ? 75   GLU L O     1 
ATOM   6635  C  CB    . GLU C 2 75  ? 124.478 134.021 150.885 1.00 46.81  ? 75   GLU L CB    1 
ATOM   6636  C  CG    . GLU C 2 75  ? 123.105 134.671 150.886 1.00 44.65  ? 75   GLU L CG    1 
ATOM   6637  C  CD    . GLU C 2 75  ? 122.327 134.385 152.155 1.00 49.11  ? 75   GLU L CD    1 
ATOM   6638  O  OE1   . GLU C 2 75  ? 122.785 133.544 152.957 1.00 50.48  ? 75   GLU L OE1   1 
ATOM   6639  O  OE2   . GLU C 2 75  ? 121.259 135.001 152.351 1.00 49.91  ? 75   GLU L OE2   1 
ATOM   6640  N  N     . GLY C 2 76  ? 126.542 131.970 150.557 1.00 30.76  ? 76   GLY L N     1 
ATOM   6641  C  CA    . GLY C 2 76  ? 127.836 131.319 150.633 1.00 32.60  ? 76   GLY L CA    1 
ATOM   6642  C  C     . GLY C 2 76  ? 127.898 129.943 151.265 1.00 33.17  ? 76   GLY L C     1 
ATOM   6643  O  O     . GLY C 2 76  ? 128.993 129.397 151.432 1.00 32.19  ? 76   GLY L O     1 
ATOM   6644  N  N     . TYR C 2 77  ? 126.759 129.361 151.621 1.00 38.77  ? 77   TYR L N     1 
ATOM   6645  C  CA    . TYR C 2 77  ? 126.728 128.247 152.559 1.00 40.40  ? 77   TYR L CA    1 
ATOM   6646  C  C     . TYR C 2 77  ? 126.370 126.947 151.855 1.00 38.67  ? 77   TYR L C     1 
ATOM   6647  O  O     . TYR C 2 77  ? 125.308 126.842 151.236 1.00 42.94  ? 77   TYR L O     1 
ATOM   6648  C  CB    . TYR C 2 77  ? 125.733 128.515 153.690 1.00 40.43  ? 77   TYR L CB    1 
ATOM   6649  C  CG    . TYR C 2 77  ? 126.040 129.757 154.495 1.00 43.51  ? 77   TYR L CG    1 
ATOM   6650  C  CD1   . TYR C 2 77  ? 127.223 129.867 155.210 1.00 41.88  ? 77   TYR L CD1   1 
ATOM   6651  C  CD2   . TYR C 2 77  ? 125.143 130.815 154.544 1.00 44.03  ? 77   TYR L CD2   1 
ATOM   6652  C  CE1   . TYR C 2 77  ? 127.507 130.996 155.949 1.00 41.66  ? 77   TYR L CE1   1 
ATOM   6653  C  CE2   . TYR C 2 77  ? 125.418 131.949 155.280 1.00 42.83  ? 77   TYR L CE2   1 
ATOM   6654  C  CZ    . TYR C 2 77  ? 126.602 132.034 155.980 1.00 45.04  ? 77   TYR L CZ    1 
ATOM   6655  O  OH    . TYR C 2 77  ? 126.881 133.163 156.716 1.00 51.16  ? 77   TYR L OH    1 
ATOM   6656  N  N     . ASN C 2 78  ? 127.245 125.955 151.978 1.00 6.72   ? 78   ASN L N     1 
ATOM   6657  C  CA    . ASN C 2 78  ? 126.944 124.628 151.472 1.00 4.76   ? 78   ASN L CA    1 
ATOM   6658  C  C     . ASN C 2 78  ? 125.754 124.032 152.213 1.00 13.17  ? 78   ASN L C     1 
ATOM   6659  O  O     . ASN C 2 78  ? 125.560 124.260 153.409 1.00 27.43  ? 78   ASN L O     1 
ATOM   6660  C  CB    . ASN C 2 78  ? 128.163 123.721 151.612 1.00 9.20   ? 78   ASN L CB    1 
ATOM   6661  C  CG    . ASN C 2 78  ? 129.429 124.377 151.114 1.00 21.34  ? 78   ASN L CG    1 
ATOM   6662  O  OD1   . ASN C 2 78  ? 129.807 124.221 149.954 1.00 37.09  ? 78   ASN L OD1   1 
ATOM   6663  N  ND2   . ASN C 2 78  ? 130.093 125.121 151.989 1.00 17.63  ? 78   ASN L ND2   1 
ATOM   6664  N  N     . GLY C 2 79  ? 124.946 123.265 151.485 1.00 10.68  ? 79   GLY L N     1 
ATOM   6665  C  CA    . GLY C 2 79  ? 123.761 122.666 152.058 1.00 18.30  ? 79   GLY L CA    1 
ATOM   6666  C  C     . GLY C 2 79  ? 123.645 121.210 151.660 1.00 17.04  ? 79   GLY L C     1 
ATOM   6667  O  O     . GLY C 2 79  ? 124.284 120.747 150.713 1.00 34.35  ? 79   GLY L O     1 
ATOM   6668  N  N     . THR C 2 80  ? 122.818 120.487 152.412 1.00 10.88  ? 80   THR L N     1 
ATOM   6669  C  CA    . THR C 2 80  ? 122.595 119.072 152.144 1.00 17.28  ? 80   THR L CA    1 
ATOM   6670  C  C     . THR C 2 80  ? 121.285 118.651 152.786 1.00 16.38  ? 80   THR L C     1 
ATOM   6671  O  O     . THR C 2 80  ? 121.051 118.938 153.963 1.00 33.19  ? 80   THR L O     1 
ATOM   6672  C  CB    . THR C 2 80  ? 123.746 118.212 152.681 1.00 28.63  ? 80   THR L CB    1 
ATOM   6673  O  OG1   . THR C 2 80  ? 124.966 118.565 152.017 1.00 29.68  ? 80   THR L OG1   1 
ATOM   6674  C  CG2   . THR C 2 80  ? 123.463 116.737 152.453 1.00 27.43  ? 80   THR L CG2   1 
ATOM   6675  N  N     . ILE C 2 81  ? 120.438 117.977 152.016 1.00 17.94  ? 81   ILE L N     1 
ATOM   6676  C  CA    . ILE C 2 81  ? 119.202 117.402 152.529 1.00 21.00  ? 81   ILE L CA    1 
ATOM   6677  C  C     . ILE C 2 81  ? 119.074 115.987 151.986 1.00 26.43  ? 81   ILE L C     1 
ATOM   6678  O  O     . ILE C 2 81  ? 119.268 115.752 150.789 1.00 44.70  ? 81   ILE L O     1 
ATOM   6679  C  CB    . ILE C 2 81  ? 117.980 118.261 152.151 1.00 37.26  ? 81   ILE L CB    1 
ATOM   6680  C  CG1   . ILE C 2 81  ? 118.021 118.628 150.671 1.00 40.08  ? 81   ILE L CG1   1 
ATOM   6681  C  CG2   . ILE C 2 81  ? 117.946 119.530 152.977 1.00 40.20  ? 81   ILE L CG2   1 
ATOM   6682  C  CD1   . ILE C 2 81  ? 116.670 118.939 150.101 1.00 37.54  ? 81   ILE L CD1   1 
ATOM   6683  N  N     . PHE C 2 82  ? 118.763 115.038 152.867 1.00 51.55  ? 82   PHE L N     1 
ATOM   6684  C  CA    . PHE C 2 82  ? 118.608 113.654 152.442 1.00 60.66  ? 82   PHE L CA    1 
ATOM   6685  C  C     . PHE C 2 82  ? 117.625 112.939 153.353 1.00 65.28  ? 82   PHE L C     1 
ATOM   6686  O  O     . PHE C 2 82  ? 117.290 113.414 154.441 1.00 71.52  ? 82   PHE L O     1 
ATOM   6687  C  CB    . PHE C 2 82  ? 119.947 112.903 152.409 1.00 63.16  ? 82   PHE L CB    1 
ATOM   6688  C  CG    . PHE C 2 82  ? 120.708 112.930 153.705 1.00 65.35  ? 82   PHE L CG    1 
ATOM   6689  C  CD1   . PHE C 2 82  ? 120.497 111.958 154.670 1.00 66.28  ? 82   PHE L CD1   1 
ATOM   6690  C  CD2   . PHE C 2 82  ? 121.659 113.907 153.943 1.00 63.87  ? 82   PHE L CD2   1 
ATOM   6691  C  CE1   . PHE C 2 82  ? 121.206 111.974 155.855 1.00 64.93  ? 82   PHE L CE1   1 
ATOM   6692  C  CE2   . PHE C 2 82  ? 122.371 113.928 155.126 1.00 65.03  ? 82   PHE L CE2   1 
ATOM   6693  C  CZ    . PHE C 2 82  ? 122.144 112.960 156.083 1.00 65.26  ? 82   PHE L CZ    1 
ATOM   6694  N  N     . ALA C 2 83  ? 117.170 111.778 152.888 1.00 71.92  ? 83   ALA L N     1 
ATOM   6695  C  CA    . ALA C 2 83  ? 116.145 111.001 153.565 1.00 74.76  ? 83   ALA L CA    1 
ATOM   6696  C  C     . ALA C 2 83  ? 116.685 109.634 153.955 1.00 78.03  ? 83   ALA L C     1 
ATOM   6697  O  O     . ALA C 2 83  ? 117.387 108.984 153.174 1.00 79.56  ? 83   ALA L O     1 
ATOM   6698  C  CB    . ALA C 2 83  ? 114.907 110.840 152.680 1.00 77.37  ? 83   ALA L CB    1 
ATOM   6699  N  N     . TYR C 2 84  ? 116.351 109.207 155.171 1.00 93.55  ? 84   TYR L N     1 
ATOM   6700  C  CA    . TYR C 2 84  ? 116.718 107.897 155.691 1.00 94.20  ? 84   TYR L CA    1 
ATOM   6701  C  C     . TYR C 2 84  ? 115.452 107.205 156.170 1.00 94.66  ? 84   TYR L C     1 
ATOM   6702  O  O     . TYR C 2 84  ? 114.665 107.799 156.914 1.00 93.05  ? 84   TYR L O     1 
ATOM   6703  C  CB    . TYR C 2 84  ? 117.733 108.024 156.836 1.00 91.19  ? 84   TYR L CB    1 
ATOM   6704  C  CG    . TYR C 2 84  ? 118.128 106.715 157.485 1.00 91.16  ? 84   TYR L CG    1 
ATOM   6705  C  CD1   . TYR C 2 84  ? 117.396 106.191 158.543 1.00 92.12  ? 84   TYR L CD1   1 
ATOM   6706  C  CD2   . TYR C 2 84  ? 119.240 106.011 157.049 1.00 92.53  ? 84   TYR L CD2   1 
ATOM   6707  C  CE1   . TYR C 2 84  ? 117.754 104.998 159.139 1.00 92.66  ? 84   TYR L CE1   1 
ATOM   6708  C  CE2   . TYR C 2 84  ? 119.608 104.818 157.640 1.00 93.88  ? 84   TYR L CE2   1 
ATOM   6709  C  CZ    . TYR C 2 84  ? 118.862 104.316 158.684 1.00 92.70  ? 84   TYR L CZ    1 
ATOM   6710  O  OH    . TYR C 2 84  ? 119.224 103.128 159.277 1.00 91.89  ? 84   TYR L OH    1 
ATOM   6711  N  N     . GLY C 2 85  ? 115.255 105.961 155.753 1.00 106.08 ? 85   GLY L N     1 
ATOM   6712  C  CA    . GLY C 2 85  ? 114.071 105.242 156.177 1.00 105.57 ? 85   GLY L CA    1 
ATOM   6713  C  C     . GLY C 2 85  ? 113.999 103.866 155.555 1.00 107.31 ? 85   GLY L C     1 
ATOM   6714  O  O     . GLY C 2 85  ? 114.909 103.427 154.848 1.00 108.30 ? 85   GLY L O     1 
ATOM   6715  N  N     . GLN C 2 86  ? 112.889 103.191 155.839 1.00 111.78 ? 86   GLN L N     1 
ATOM   6716  C  CA    . GLN C 2 86  ? 112.626 101.848 155.351 1.00 112.53 ? 86   GLN L CA    1 
ATOM   6717  C  C     . GLN C 2 86  ? 112.206 101.886 153.882 1.00 110.95 ? 86   GLN L C     1 
ATOM   6718  O  O     . GLN C 2 86  ? 111.882 102.937 153.323 1.00 104.47 ? 86   GLN L O     1 
ATOM   6719  C  CB    . GLN C 2 86  ? 111.544 101.183 156.204 1.00 111.75 ? 86   GLN L CB    1 
ATOM   6720  C  CG    . GLN C 2 86  ? 111.561 99.664  156.211 1.00 112.43 ? 86   GLN L CG    1 
ATOM   6721  C  CD    . GLN C 2 86  ? 110.407 99.076  157.000 1.00 111.41 ? 86   GLN L CD    1 
ATOM   6722  O  OE1   . GLN C 2 86  ? 109.613 99.805  157.597 1.00 108.88 ? 86   GLN L OE1   1 
ATOM   6723  N  NE2   . GLN C 2 86  ? 110.304 97.752  157.003 1.00 111.21 ? 86   GLN L NE2   1 
ATOM   6724  N  N     . THR C 2 87  ? 112.229 100.714 153.251 1.00 117.39 ? 87   THR L N     1 
ATOM   6725  C  CA    . THR C 2 87  ? 111.746 100.593 151.883 1.00 116.52 ? 87   THR L CA    1 
ATOM   6726  C  C     . THR C 2 87  ? 110.260 100.925 151.822 1.00 115.92 ? 87   THR L C     1 
ATOM   6727  O  O     . THR C 2 87  ? 109.482 100.535 152.697 1.00 117.08 ? 87   THR L O     1 
ATOM   6728  C  CB    . THR C 2 87  ? 112.000 99.178  151.355 1.00 115.97 ? 87   THR L CB    1 
ATOM   6729  O  OG1   . THR C 2 87  ? 113.409 98.924  151.331 1.00 116.25 ? 87   THR L OG1   1 
ATOM   6730  C  CG2   . THR C 2 87  ? 111.439 99.011  149.949 1.00 116.34 ? 87   THR L CG2   1 
ATOM   6731  N  N     . SER C 2 88  ? 109.876 101.669 150.784 1.00 112.05 ? 88   SER L N     1 
ATOM   6732  C  CA    . SER C 2 88  ? 108.504 102.119 150.559 0.00 113.16 ? 88   SER L CA    1 
ATOM   6733  C  C     . SER C 2 88  ? 108.003 103.035 151.671 1.00 115.47 ? 88   SER L C     1 
ATOM   6734  O  O     . SER C 2 88  ? 106.791 103.160 151.876 1.00 115.68 ? 88   SER L O     1 
ATOM   6735  C  CB    . SER C 2 88  ? 107.548 100.933 150.378 1.00 113.56 ? 88   SER L CB    1 
ATOM   6736  O  OG    . SER C 2 88  ? 107.946 100.120 149.288 1.00 113.76 ? 88   SER L OG    1 
ATOM   6737  N  N     . SER C 2 89  ? 108.915 103.683 152.399 1.00 111.55 ? 89   SER L N     1 
ATOM   6738  C  CA    . SER C 2 89  ? 108.511 104.636 153.425 1.00 109.26 ? 89   SER L CA    1 
ATOM   6739  C  C     . SER C 2 89  ? 108.270 106.033 152.871 1.00 106.70 ? 89   SER L C     1 
ATOM   6740  O  O     . SER C 2 89  ? 107.665 106.860 153.562 1.00 106.11 ? 89   SER L O     1 
ATOM   6741  C  CB    . SER C 2 89  ? 109.560 104.703 154.536 1.00 109.29 ? 89   SER L CB    1 
ATOM   6742  O  OG    . SER C 2 89  ? 109.625 103.478 155.244 1.00 108.42 ? 89   SER L OG    1 
ATOM   6743  N  N     . GLY C 2 90  ? 108.714 106.314 151.649 1.00 97.36  ? 90   GLY L N     1 
ATOM   6744  C  CA    . GLY C 2 90  ? 108.452 107.607 151.053 1.00 95.21  ? 90   GLY L CA    1 
ATOM   6745  C  C     . GLY C 2 90  ? 109.643 108.526 150.875 1.00 95.68  ? 90   GLY L C     1 
ATOM   6746  O  O     . GLY C 2 90  ? 109.523 109.735 151.096 1.00 96.42  ? 90   GLY L O     1 
ATOM   6747  N  N     . LYS C 2 91  ? 110.799 107.987 150.483 1.00 90.56  ? 91   LYS L N     1 
ATOM   6748  C  CA    . LYS C 2 91  ? 111.957 108.847 150.275 1.00 87.89  ? 91   LYS L CA    1 
ATOM   6749  C  C     . LYS C 2 91  ? 112.241 109.140 148.803 1.00 85.50  ? 91   LYS L C     1 
ATOM   6750  O  O     . LYS C 2 91  ? 113.312 109.675 148.496 1.00 86.54  ? 91   LYS L O     1 
ATOM   6751  C  CB    . LYS C 2 91  ? 113.197 108.250 150.954 1.00 90.64  ? 91   LYS L CB    1 
ATOM   6752  C  CG    . LYS C 2 91  ? 113.751 106.984 150.339 1.00 92.11  ? 91   LYS L CG    1 
ATOM   6753  C  CD    . LYS C 2 91  ? 114.913 106.439 151.152 1.00 89.05  ? 91   LYS L CD    1 
ATOM   6754  C  CE    . LYS C 2 91  ? 115.516 105.211 150.492 1.00 88.24  ? 91   LYS L CE    1 
ATOM   6755  N  NZ    . LYS C 2 91  ? 115.874 105.467 149.069 1.00 89.02  ? 91   LYS L NZ    1 
ATOM   6756  N  N     . THR C 2 92  ? 111.324 108.814 147.890 1.00 70.18  ? 92   THR L N     1 
ATOM   6757  C  CA    . THR C 2 92  ? 111.380 109.378 146.543 1.00 69.74  ? 92   THR L CA    1 
ATOM   6758  C  C     . THR C 2 92  ? 110.435 110.565 146.406 1.00 67.87  ? 92   THR L C     1 
ATOM   6759  O  O     . THR C 2 92  ? 110.830 111.623 145.909 1.00 70.24  ? 92   THR L O     1 
ATOM   6760  C  CB    . THR C 2 92  ? 111.033 108.332 145.477 1.00 71.49  ? 92   THR L CB    1 
ATOM   6761  O  OG1   . THR C 2 92  ? 109.655 107.957 145.597 1.00 70.35  ? 92   THR L OG1   1 
ATOM   6762  C  CG2   . THR C 2 92  ? 111.924 107.106 145.596 1.00 72.42  ? 92   THR L CG2   1 
ATOM   6763  N  N     . HIS C 2 93  ? 109.182 110.395 146.836 1.00 67.89  ? 93   HIS L N     1 
ATOM   6764  C  CA    . HIS C 2 93  ? 108.233 111.501 146.812 1.00 70.64  ? 93   HIS L CA    1 
ATOM   6765  C  C     . HIS C 2 93  ? 108.696 112.655 147.689 1.00 71.58  ? 93   HIS L C     1 
ATOM   6766  O  O     . HIS C 2 93  ? 108.431 113.820 147.369 1.00 72.85  ? 93   HIS L O     1 
ATOM   6767  C  CB    . HIS C 2 93  ? 106.851 111.019 147.252 1.00 72.57  ? 93   HIS L CB    1 
ATOM   6768  C  CG    . HIS C 2 93  ? 105.912 112.126 147.619 1.00 69.46  ? 93   HIS L CG    1 
ATOM   6769  N  ND1   . HIS C 2 93  ? 105.317 112.216 148.858 1.00 64.26  ? 93   HIS L ND1   1 
ATOM   6770  C  CD2   . HIS C 2 93  ? 105.467 113.190 146.910 1.00 69.24  ? 93   HIS L CD2   1 
ATOM   6771  C  CE1   . HIS C 2 93  ? 104.543 113.286 148.896 1.00 67.28  ? 93   HIS L CE1   1 
ATOM   6772  N  NE2   . HIS C 2 93  ? 104.618 113.895 147.727 1.00 69.33  ? 93   HIS L NE2   1 
ATOM   6773  N  N     . THR C 2 94  ? 109.382 112.355 148.793 1.00 72.49  ? 94   THR L N     1 
ATOM   6774  C  CA    . THR C 2 94  ? 109.920 113.415 149.637 1.00 70.55  ? 94   THR L CA    1 
ATOM   6775  C  C     . THR C 2 94  ? 110.963 114.235 148.891 1.00 71.77  ? 94   THR L C     1 
ATOM   6776  O  O     . THR C 2 94  ? 110.993 115.465 149.007 1.00 74.38  ? 94   THR L O     1 
ATOM   6777  C  CB    . THR C 2 94  ? 110.519 112.820 150.911 1.00 69.30  ? 94   THR L CB    1 
ATOM   6778  O  OG1   . THR C 2 94  ? 109.547 111.985 151.554 1.00 71.74  ? 94   THR L OG1   1 
ATOM   6779  C  CG2   . THR C 2 94  ? 110.941 113.924 151.869 1.00 70.12  ? 94   THR L CG2   1 
ATOM   6780  N  N     . MET C 2 95  ? 111.819 113.576 148.112 1.00 61.63  ? 95   MET L N     1 
ATOM   6781  C  CA    . MET C 2 95  ? 112.898 114.267 147.413 1.00 55.51  ? 95   MET L CA    1 
ATOM   6782  C  C     . MET C 2 95  ? 112.500 114.651 145.990 1.00 61.93  ? 95   MET L C     1 
ATOM   6783  O  O     . MET C 2 95  ? 112.518 115.831 145.630 1.00 65.72  ? 95   MET L O     1 
ATOM   6784  C  CB    . MET C 2 95  ? 114.157 113.396 147.403 1.00 57.57  ? 95   MET L CB    1 
ATOM   6785  C  CG    . MET C 2 95  ? 115.426 114.161 147.080 1.00 63.82  ? 95   MET L CG    1 
ATOM   6786  S  SD    . MET C 2 95  ? 115.667 115.570 148.179 1.00 67.65  ? 95   MET L SD    1 
ATOM   6787  C  CE    . MET C 2 95  ? 115.699 114.756 149.775 1.00 60.84  ? 95   MET L CE    1 
ATOM   6788  N  N     . GLU C 2 96  ? 112.139 113.666 145.171 1.00 66.83  ? 96   GLU L N     1 
ATOM   6789  C  CA    . GLU C 2 96  ? 111.768 113.947 143.789 1.00 66.86  ? 96   GLU L CA    1 
ATOM   6790  C  C     . GLU C 2 96  ? 110.280 114.247 143.647 1.00 65.87  ? 96   GLU L C     1 
ATOM   6791  O  O     . GLU C 2 96  ? 109.903 115.297 143.118 1.00 64.89  ? 96   GLU L O     1 
ATOM   6792  C  CB    . GLU C 2 96  ? 112.159 112.771 142.889 1.00 63.21  ? 96   GLU L CB    1 
ATOM   6793  C  CG    . GLU C 2 96  ? 113.658 112.552 142.771 1.00 64.32  ? 96   GLU L CG    1 
ATOM   6794  C  CD    . GLU C 2 96  ? 114.002 111.273 142.035 1.00 64.57  ? 96   GLU L CD    1 
ATOM   6795  O  OE1   . GLU C 2 96  ? 113.138 110.374 141.969 1.00 63.58  ? 96   GLU L OE1   1 
ATOM   6796  O  OE2   . GLU C 2 96  ? 115.135 111.167 141.522 1.00 65.84  ? 96   GLU L OE2   1 
ATOM   6797  N  N     . GLY C 2 97  ? 109.427 113.342 144.116 1.00 56.88  ? 97   GLY L N     1 
ATOM   6798  C  CA    . GLY C 2 97  ? 107.997 113.523 143.983 1.00 50.95  ? 97   GLY L CA    1 
ATOM   6799  C  C     . GLY C 2 97  ? 107.532 113.432 142.548 1.00 51.80  ? 97   GLY L C     1 
ATOM   6800  O  O     . GLY C 2 97  ? 107.566 112.360 141.937 1.00 48.36  ? 97   GLY L O     1 
ATOM   6801  N  N     . LYS C 2 98  ? 107.091 114.558 142.000 1.00 59.32  ? 98   LYS L N     1 
ATOM   6802  C  CA    . LYS C 2 98  ? 106.637 114.639 140.619 1.00 62.11  ? 98   LYS L CA    1 
ATOM   6803  C  C     . LYS C 2 98  ? 107.593 115.536 139.850 1.00 62.72  ? 98   LYS L C     1 
ATOM   6804  O  O     . LYS C 2 98  ? 107.753 116.713 140.189 1.00 58.12  ? 98   LYS L O     1 
ATOM   6805  C  CB    . LYS C 2 98  ? 105.209 115.175 140.547 1.00 53.16  ? 98   LYS L CB    1 
ATOM   6806  C  CG    . LYS C 2 98  ? 104.162 114.229 141.111 1.00 55.16  ? 98   LYS L CG    1 
ATOM   6807  C  CD    . LYS C 2 98  ? 104.135 112.916 140.341 1.00 58.29  ? 98   LYS L CD    1 
ATOM   6808  C  CE    . LYS C 2 98  ? 103.070 111.976 140.882 1.00 57.24  ? 98   LYS L CE    1 
ATOM   6809  N  NZ    . LYS C 2 98  ? 103.007 110.704 140.111 1.00 58.31  ? 98   LYS L NZ    1 
ATOM   6810  N  N     . LEU C 2 99  ? 108.235 114.977 138.822 1.00 59.73  ? 99   LEU L N     1 
ATOM   6811  C  CA    . LEU C 2 99  ? 109.180 115.758 138.032 1.00 55.12  ? 99   LEU L CA    1 
ATOM   6812  C  C     . LEU C 2 99  ? 108.463 116.812 137.197 1.00 57.94  ? 99   LEU L C     1 
ATOM   6813  O  O     . LEU C 2 99  ? 108.888 117.972 137.147 1.00 57.41  ? 99   LEU L O     1 
ATOM   6814  C  CB    . LEU C 2 99  ? 110.010 114.838 137.139 1.00 50.11  ? 99   LEU L CB    1 
ATOM   6815  C  CG    . LEU C 2 99  ? 111.187 114.131 137.808 1.00 54.78  ? 99   LEU L CG    1 
ATOM   6816  C  CD1   . LEU C 2 99  ? 112.129 113.567 136.758 1.00 57.31  ? 99   LEU L CD1   1 
ATOM   6817  C  CD2   . LEU C 2 99  ? 111.921 115.079 138.742 1.00 54.82  ? 99   LEU L CD2   1 
ATOM   6818  N  N     . HIS C 2 100 ? 107.373 116.431 136.537 1.00 56.07  ? 100  HIS L N     1 
ATOM   6819  C  CA    . HIS C 2 100 ? 106.655 117.333 135.644 1.00 49.53  ? 100  HIS L CA    1 
ATOM   6820  C  C     . HIS C 2 100 ? 105.168 117.352 135.963 1.00 50.37  ? 100  HIS L C     1 
ATOM   6821  O  O     . HIS C 2 100 ? 104.321 117.405 135.068 1.00 53.12  ? 100  HIS L O     1 
ATOM   6822  C  CB    . HIS C 2 100 ? 106.895 116.960 134.185 1.00 49.09  ? 100  HIS L CB    1 
ATOM   6823  C  CG    . HIS C 2 100 ? 108.228 117.400 133.664 1.00 53.19  ? 100  HIS L CG    1 
ATOM   6824  N  ND1   . HIS C 2 100 ? 109.381 116.672 133.860 1.00 57.34  ? 100  HIS L ND1   1 
ATOM   6825  C  CD2   . HIS C 2 100 ? 108.591 118.497 132.960 1.00 54.17  ? 100  HIS L CD2   1 
ATOM   6826  C  CE1   . HIS C 2 100 ? 110.397 117.300 133.296 1.00 55.05  ? 100  HIS L CE1   1 
ATOM   6827  N  NE2   . HIS C 2 100 ? 109.944 118.411 132.742 1.00 53.98  ? 100  HIS L NE2   1 
ATOM   6828  N  N     . ASP C 2 101 ? 104.829 117.306 137.248 1.00 55.64  ? 101  ASP L N     1 
ATOM   6829  C  CA    . ASP C 2 101 ? 103.474 117.580 137.711 1.00 56.07  ? 101  ASP L CA    1 
ATOM   6830  C  C     . ASP C 2 101 ? 103.544 118.742 138.691 1.00 60.41  ? 101  ASP L C     1 
ATOM   6831  O  O     . ASP C 2 101 ? 104.195 118.617 139.743 1.00 60.00  ? 101  ASP L O     1 
ATOM   6832  C  CB    . ASP C 2 101 ? 102.842 116.349 138.366 1.00 53.00  ? 101  ASP L CB    1 
ATOM   6833  C  CG    . ASP C 2 101 ? 101.390 116.569 138.752 1.00 53.67  ? 101  ASP L CG    1 
ATOM   6834  O  OD1   . ASP C 2 101 ? 101.122 117.399 139.643 1.00 53.20  ? 101  ASP L OD1   1 
ATOM   6835  O  OD2   . ASP C 2 101 ? 100.512 115.906 138.162 1.00 57.55  ? 101  ASP L OD2   1 
ATOM   6836  N  N     . PRO C 2 102 ? 102.913 119.881 138.394 1.00 67.03  ? 102  PRO L N     1 
ATOM   6837  C  CA    . PRO C 2 102 ? 103.072 121.059 139.266 0.00 62.60  ? 102  PRO L CA    1 
ATOM   6838  C  C     . PRO C 2 102 ? 102.629 120.829 140.699 1.00 63.70  ? 102  PRO L C     1 
ATOM   6839  O  O     . PRO C 2 102 ? 103.178 121.459 141.612 1.00 67.79  ? 102  PRO L O     1 
ATOM   6840  C  CB    . PRO C 2 102 ? 102.208 122.124 138.575 1.00 60.80  ? 102  PRO L CB    1 
ATOM   6841  C  CG    . PRO C 2 102 ? 102.091 121.664 137.156 1.00 60.11  ? 102  PRO L CG    1 
ATOM   6842  C  CD    . PRO C 2 102 ? 102.073 120.168 137.220 1.00 65.03  ? 102  PRO L CD    1 
ATOM   6843  N  N     . GLU C 2 103 ? 101.646 119.956 140.926 1.00 61.87  ? 103  GLU L N     1 
ATOM   6844  C  CA    . GLU C 2 103 ? 101.143 119.747 142.280 1.00 61.74  ? 103  GLU L CA    1 
ATOM   6845  C  C     . GLU C 2 103 ? 102.208 119.138 143.182 1.00 60.39  ? 103  GLU L C     1 
ATOM   6846  O  O     . GLU C 2 103 ? 102.420 119.603 144.308 1.00 61.82  ? 103  GLU L O     1 
ATOM   6847  C  CB    . GLU C 2 103 ? 99.896  118.865 142.248 1.00 64.18  ? 103  GLU L CB    1 
ATOM   6848  C  CG    . GLU C 2 103 ? 99.041  118.955 143.501 1.00 65.76  ? 103  GLU L CG    1 
ATOM   6849  C  CD    . GLU C 2 103 ? 98.338  120.293 143.637 1.00 66.64  ? 103  GLU L CD    1 
ATOM   6850  O  OE1   . GLU C 2 103 ? 98.138  120.971 142.607 1.00 67.41  ? 103  GLU L OE1   1 
ATOM   6851  O  OE2   . GLU C 2 103 ? 97.985  120.666 144.776 1.00 64.37  ? 103  GLU L OE2   1 
ATOM   6852  N  N     . GLY C 2 104 ? 102.886 118.093 142.713 1.00 60.55  ? 104  GLY L N     1 
ATOM   6853  C  CA    . GLY C 2 104 ? 103.879 117.451 143.550 1.00 60.34  ? 104  GLY L CA    1 
ATOM   6854  C  C     . GLY C 2 104 ? 105.133 118.276 143.758 1.00 60.75  ? 104  GLY L C     1 
ATOM   6855  O  O     . GLY C 2 104 ? 105.315 118.852 144.834 1.00 65.17  ? 104  GLY L O     1 
ATOM   6856  N  N     . MET C 2 105 ? 105.961 118.381 142.718 1.00 47.97  ? 105  MET L N     1 
ATOM   6857  C  CA    . MET C 2 105 ? 107.213 119.143 142.731 1.00 48.69  ? 105  MET L CA    1 
ATOM   6858  C  C     . MET C 2 105 ? 107.884 119.080 144.102 1.00 52.30  ? 105  MET L C     1 
ATOM   6859  O  O     . MET C 2 105 ? 108.111 120.092 144.765 1.00 48.40  ? 105  MET L O     1 
ATOM   6860  C  CB    . MET C 2 105 ? 106.979 120.587 142.300 1.00 52.51  ? 105  MET L CB    1 
ATOM   6861  C  CG    . MET C 2 105 ? 106.478 120.732 140.872 1.00 56.31  ? 105  MET L CG    1 
ATOM   6862  S  SD    . MET C 2 105 ? 107.452 119.780 139.692 1.00 58.63  ? 105  MET L SD    1 
ATOM   6863  C  CE    . MET C 2 105 ? 106.739 120.324 138.142 1.00 51.29  ? 105  MET L CE    1 
ATOM   6864  N  N     . GLY C 2 106 ? 108.184 117.852 144.522 1.00 60.34  ? 106  GLY L N     1 
ATOM   6865  C  CA    . GLY C 2 106 ? 108.549 117.572 145.898 1.00 60.76  ? 106  GLY L CA    1 
ATOM   6866  C  C     . GLY C 2 106 ? 109.644 118.430 146.497 1.00 60.35  ? 106  GLY L C     1 
ATOM   6867  O  O     . GLY C 2 106 ? 109.374 119.240 147.388 1.00 61.46  ? 106  GLY L O     1 
ATOM   6868  N  N     . ILE C 2 107 ? 110.879 118.274 146.028 1.00 56.97  ? 107  ILE L N     1 
ATOM   6869  C  CA    . ILE C 2 107 ? 111.972 119.091 146.543 1.00 59.06  ? 107  ILE L CA    1 
ATOM   6870  C  C     . ILE C 2 107 ? 112.817 119.662 145.411 1.00 62.27  ? 107  ILE L C     1 
ATOM   6871  O  O     . ILE C 2 107 ? 113.083 120.865 145.382 1.00 63.87  ? 107  ILE L O     1 
ATOM   6872  C  CB    . ILE C 2 107 ? 112.843 118.303 147.538 1.00 58.91  ? 107  ILE L CB    1 
ATOM   6873  C  CG1   . ILE C 2 107 ? 112.225 118.356 148.937 1.00 58.64  ? 107  ILE L CG1   1 
ATOM   6874  C  CG2   . ILE C 2 107 ? 114.258 118.848 147.559 1.00 57.36  ? 107  ILE L CG2   1 
ATOM   6875  C  CD1   . ILE C 2 107 ? 113.110 117.786 150.025 1.00 62.04  ? 107  ILE L CD1   1 
ATOM   6876  N  N     . ILE C 2 108 ? 113.254 118.815 144.483 1.00 51.75  ? 108  ILE L N     1 
ATOM   6877  C  CA    . ILE C 2 108 ? 114.268 119.212 143.505 1.00 46.50  ? 108  ILE L CA    1 
ATOM   6878  C  C     . ILE C 2 108 ? 113.724 120.205 142.477 1.00 47.72  ? 108  ILE L C     1 
ATOM   6879  O  O     . ILE C 2 108 ? 114.348 121.259 142.266 1.00 54.78  ? 108  ILE L O     1 
ATOM   6880  C  CB    . ILE C 2 108 ? 114.882 117.981 142.818 1.00 47.99  ? 108  ILE L CB    1 
ATOM   6881  C  CG1   . ILE C 2 108 ? 115.175 116.889 143.847 1.00 50.38  ? 108  ILE L CG1   1 
ATOM   6882  C  CG2   . ILE C 2 108 ? 116.161 118.364 142.099 1.00 53.81  ? 108  ILE L CG2   1 
ATOM   6883  C  CD1   . ILE C 2 108 ? 115.794 115.643 143.253 1.00 49.42  ? 108  ILE L CD1   1 
ATOM   6884  N  N     . PRO C 2 109 ? 112.611 119.928 141.784 1.00 43.86  ? 109  PRO L N     1 
ATOM   6885  C  CA    . PRO C 2 109 ? 112.104 120.942 140.842 1.00 48.45  ? 109  PRO L CA    1 
ATOM   6886  C  C     . PRO C 2 109 ? 111.730 122.244 141.523 1.00 45.69  ? 109  PRO L C     1 
ATOM   6887  O  O     . PRO C 2 109 ? 112.010 123.332 140.998 1.00 49.09  ? 109  PRO L O     1 
ATOM   6888  C  CB    . PRO C 2 109 ? 110.882 120.258 140.212 1.00 53.42  ? 109  PRO L CB    1 
ATOM   6889  C  CG    . PRO C 2 109 ? 111.069 118.804 140.471 1.00 54.03  ? 109  PRO L CG    1 
ATOM   6890  C  CD    . PRO C 2 109 ? 111.748 118.734 141.796 1.00 48.92  ? 109  PRO L CD    1 
ATOM   6891  N  N     . ARG C 2 110 ? 111.119 122.158 142.703 1.00 44.05  ? 110  ARG L N     1 
ATOM   6892  C  CA    . ARG C 2 110 ? 110.752 123.361 143.436 1.00 47.45  ? 110  ARG L CA    1 
ATOM   6893  C  C     . ARG C 2 110 ? 111.986 124.158 143.836 1.00 52.16  ? 110  ARG L C     1 
ATOM   6894  O  O     . ARG C 2 110 ? 111.993 125.388 143.736 1.00 53.16  ? 110  ARG L O     1 
ATOM   6895  C  CB    . ARG C 2 110 ? 109.925 122.987 144.664 1.00 52.77  ? 110  ARG L CB    1 
ATOM   6896  C  CG    . ARG C 2 110 ? 109.003 124.081 145.153 1.00 52.83  ? 110  ARG L CG    1 
ATOM   6897  C  CD    . ARG C 2 110 ? 108.017 123.536 146.165 1.00 50.25  ? 110  ARG L CD    1 
ATOM   6898  N  NE    . ARG C 2 110 ? 107.097 122.572 145.574 1.00 53.46  ? 110  ARG L NE    1 
ATOM   6899  C  CZ    . ARG C 2 110 ? 105.887 122.873 145.122 1.00 54.23  ? 110  ARG L CZ    1 
ATOM   6900  N  NH1   . ARG C 2 110 ? 105.423 124.111 145.162 1.00 53.50  ? 110  ARG L NH1   1 
ATOM   6901  N  NH2   . ARG C 2 110 ? 105.123 121.908 144.622 1.00 52.47  ? 110  ARG L NH2   1 
ATOM   6902  N  N     . ILE C 2 111 ? 113.047 123.476 144.273 1.00 56.84  ? 111  ILE L N     1 
ATOM   6903  C  CA    . ILE C 2 111 ? 114.240 124.180 144.729 1.00 54.03  ? 111  ILE L CA    1 
ATOM   6904  C  C     . ILE C 2 111 ? 114.967 124.823 143.556 1.00 54.45  ? 111  ILE L C     1 
ATOM   6905  O  O     . ILE C 2 111 ? 115.495 125.933 143.678 1.00 57.44  ? 111  ILE L O     1 
ATOM   6906  C  CB    . ILE C 2 111 ? 115.160 123.245 145.542 1.00 50.36  ? 111  ILE L CB    1 
ATOM   6907  C  CG1   . ILE C 2 111 ? 116.207 124.060 146.295 1.00 53.26  ? 111  ILE L CG1   1 
ATOM   6908  C  CG2   . ILE C 2 111 ? 115.882 122.251 144.666 1.00 53.22  ? 111  ILE L CG2   1 
ATOM   6909  C  CD1   . ILE C 2 111 ? 117.143 123.224 147.135 1.00 54.36  ? 111  ILE L CD1   1 
ATOM   6910  N  N     . VAL C 2 112 ? 115.001 124.157 142.397 1.00 49.09  ? 112  VAL L N     1 
ATOM   6911  C  CA    . VAL C 2 112 ? 115.675 124.773 141.257 1.00 42.87  ? 112  VAL L CA    1 
ATOM   6912  C  C     . VAL C 2 112 ? 114.870 125.964 140.742 1.00 45.62  ? 112  VAL L C     1 
ATOM   6913  O  O     . VAL C 2 112 ? 115.438 127.011 140.400 1.00 50.18  ? 112  VAL L O     1 
ATOM   6914  C  CB    . VAL C 2 112 ? 115.967 123.734 140.156 1.00 47.11  ? 112  VAL L CB    1 
ATOM   6915  C  CG1   . VAL C 2 112 ? 116.809 122.600 140.720 1.00 45.40  ? 112  VAL L CG1   1 
ATOM   6916  C  CG2   . VAL C 2 112 ? 114.697 123.195 139.532 1.00 49.61  ? 112  VAL L CG2   1 
ATOM   6917  N  N     . GLN C 2 113 ? 113.538 125.849 140.721 1.00 56.49  ? 113  GLN L N     1 
ATOM   6918  C  CA    . GLN C 2 113 ? 112.720 126.995 140.337 1.00 60.62  ? 113  GLN L CA    1 
ATOM   6919  C  C     . GLN C 2 113 ? 112.898 128.148 141.318 1.00 61.35  ? 113  GLN L C     1 
ATOM   6920  O  O     . GLN C 2 113 ? 112.985 129.313 140.910 1.00 64.44  ? 113  GLN L O     1 
ATOM   6921  C  CB    . GLN C 2 113 ? 111.250 126.588 140.241 1.00 62.67  ? 113  GLN L CB    1 
ATOM   6922  C  CG    . GLN C 2 113 ? 110.925 125.719 139.036 1.00 63.73  ? 113  GLN L CG    1 
ATOM   6923  C  CD    . GLN C 2 113 ? 109.450 125.376 138.946 1.00 67.35  ? 113  GLN L CD    1 
ATOM   6924  O  OE1   . GLN C 2 113 ? 108.607 126.047 139.541 1.00 65.74  ? 113  GLN L OE1   1 
ATOM   6925  N  NE2   . GLN C 2 113 ? 109.132 124.326 138.197 1.00 65.38  ? 113  GLN L NE2   1 
ATOM   6926  N  N     . ASP C 2 114 ? 112.965 127.844 142.615 1.00 53.99  ? 114  ASP L N     1 
ATOM   6927  C  CA    . ASP C 2 114 ? 113.123 128.892 143.616 1.00 54.07  ? 114  ASP L CA    1 
ATOM   6928  C  C     . ASP C 2 114 ? 114.484 129.565 143.513 1.00 57.12  ? 114  ASP L C     1 
ATOM   6929  O  O     . ASP C 2 114 ? 114.588 130.787 143.667 1.00 61.59  ? 114  ASP L O     1 
ATOM   6930  C  CB    . ASP C 2 114 ? 112.919 128.315 145.014 1.00 58.82  ? 114  ASP L CB    1 
ATOM   6931  C  CG    . ASP C 2 114 ? 112.655 129.387 146.053 1.00 62.00  ? 114  ASP L CG    1 
ATOM   6932  O  OD1   . ASP C 2 114 ? 112.442 130.554 145.664 1.00 65.54  ? 114  ASP L OD1   1 
ATOM   6933  O  OD2   . ASP C 2 114 ? 112.663 129.062 147.259 1.00 62.23  ? 114  ASP L OD2   1 
ATOM   6934  N  N     . ILE C 2 115 ? 115.545 128.789 143.276 1.00 62.22  ? 115  ILE L N     1 
ATOM   6935  C  CA    . ILE C 2 115 ? 116.865 129.397 143.154 1.00 63.00  ? 115  ILE L CA    1 
ATOM   6936  C  C     . ILE C 2 115 ? 116.934 130.256 141.899 1.00 57.34  ? 115  ILE L C     1 
ATOM   6937  O  O     . ILE C 2 115 ? 117.561 131.321 141.898 1.00 59.17  ? 115  ILE L O     1 
ATOM   6938  C  CB    . ILE C 2 115 ? 117.978 128.331 143.197 1.00 63.71  ? 115  ILE L CB    1 
ATOM   6939  C  CG1   . ILE C 2 115 ? 119.323 128.990 143.506 1.00 65.15  ? 115  ILE L CG1   1 
ATOM   6940  C  CG2   . ILE C 2 115 ? 118.078 127.558 141.897 1.00 55.46  ? 115  ILE L CG2   1 
ATOM   6941  C  CD1   . ILE C 2 115 ? 120.482 128.025 143.547 1.00 62.73  ? 115  ILE L CD1   1 
ATOM   6942  N  N     . PHE C 2 116 ? 116.260 129.839 140.823 1.00 51.09  ? 116  PHE L N     1 
ATOM   6943  C  CA    . PHE C 2 116 ? 116.230 130.681 139.632 1.00 52.53  ? 116  PHE L CA    1 
ATOM   6944  C  C     . PHE C 2 116 ? 115.432 131.957 139.873 1.00 53.55  ? 116  PHE L C     1 
ATOM   6945  O  O     . PHE C 2 116 ? 115.812 133.029 139.390 1.00 55.41  ? 116  PHE L O     1 
ATOM   6946  C  CB    . PHE C 2 116 ? 115.674 129.899 138.445 1.00 54.65  ? 116  PHE L CB    1 
ATOM   6947  C  CG    . PHE C 2 116 ? 116.739 129.315 137.566 1.00 53.48  ? 116  PHE L CG    1 
ATOM   6948  C  CD1   . PHE C 2 116 ? 117.789 130.099 137.124 1.00 51.75  ? 116  PHE L CD1   1 
ATOM   6949  C  CD2   . PHE C 2 116 ? 116.703 127.984 137.199 1.00 50.76  ? 116  PHE L CD2   1 
ATOM   6950  C  CE1   . PHE C 2 116 ? 118.775 129.570 136.321 1.00 53.56  ? 116  PHE L CE1   1 
ATOM   6951  C  CE2   . PHE C 2 116 ? 117.689 127.449 136.398 1.00 52.58  ? 116  PHE L CE2   1 
ATOM   6952  C  CZ    . PHE C 2 116 ? 118.725 128.244 135.956 1.00 55.75  ? 116  PHE L CZ    1 
ATOM   6953  N  N     . ASN C 2 117 ? 114.328 131.868 140.619 1.00 61.62  ? 117  ASN L N     1 
ATOM   6954  C  CA    . ASN C 2 117 ? 113.569 133.070 140.958 1.00 61.02  ? 117  ASN L CA    1 
ATOM   6955  C  C     . ASN C 2 117 ? 114.400 134.028 141.803 1.00 60.57  ? 117  ASN L C     1 
ATOM   6956  O  O     . ASN C 2 117 ? 114.418 135.240 141.552 1.00 65.48  ? 117  ASN L O     1 
ATOM   6957  C  CB    . ASN C 2 117 ? 112.284 132.690 141.693 1.00 59.17  ? 117  ASN L CB    1 
ATOM   6958  C  CG    . ASN C 2 117 ? 111.227 132.128 140.766 1.00 63.67  ? 117  ASN L CG    1 
ATOM   6959  O  OD1   . ASN C 2 117 ? 110.384 132.861 140.252 1.00 68.01  ? 117  ASN L OD1   1 
ATOM   6960  N  ND2   . ASN C 2 117 ? 111.265 130.820 140.549 1.00 63.59  ? 117  ASN L ND2   1 
ATOM   6961  N  N     . TYR C 2 118 ? 115.100 133.498 142.807 1.00 54.81  ? 118  TYR L N     1 
ATOM   6962  C  CA    . TYR C 2 118 ? 115.942 134.337 143.651 1.00 55.25  ? 118  TYR L CA    1 
ATOM   6963  C  C     . TYR C 2 118 ? 117.073 134.963 142.847 1.00 56.88  ? 118  TYR L C     1 
ATOM   6964  O  O     . TYR C 2 118 ? 117.448 136.117 143.084 1.00 58.16  ? 118  TYR L O     1 
ATOM   6965  C  CB    . TYR C 2 118 ? 116.496 133.516 144.813 1.00 57.20  ? 118  TYR L CB    1 
ATOM   6966  C  CG    . TYR C 2 118 ? 115.481 133.185 145.881 1.00 56.13  ? 118  TYR L CG    1 
ATOM   6967  C  CD1   . TYR C 2 118 ? 114.377 133.999 146.094 1.00 58.21  ? 118  TYR L CD1   1 
ATOM   6968  C  CD2   . TYR C 2 118 ? 115.628 132.059 146.677 1.00 52.96  ? 118  TYR L CD2   1 
ATOM   6969  C  CE1   . TYR C 2 118 ? 113.447 133.699 147.072 1.00 58.14  ? 118  TYR L CE1   1 
ATOM   6970  C  CE2   . TYR C 2 118 ? 114.704 131.750 147.656 1.00 58.79  ? 118  TYR L CE2   1 
ATOM   6971  C  CZ    . TYR C 2 118 ? 113.615 132.573 147.849 1.00 59.68  ? 118  TYR L CZ    1 
ATOM   6972  O  OH    . TYR C 2 118 ? 112.692 132.269 148.823 1.00 56.62  ? 118  TYR L OH    1 
ATOM   6973  N  N     . ILE C 2 119 ? 117.636 134.213 141.896 1.00 58.06  ? 119  ILE L N     1 
ATOM   6974  C  CA    . ILE C 2 119 ? 118.659 134.766 141.013 1.00 57.08  ? 119  ILE L CA    1 
ATOM   6975  C  C     . ILE C 2 119 ? 118.076 135.898 140.176 1.00 63.73  ? 119  ILE L C     1 
ATOM   6976  O  O     . ILE C 2 119 ? 118.697 136.955 140.008 1.00 68.65  ? 119  ILE L O     1 
ATOM   6977  C  CB    . ILE C 2 119 ? 119.258 133.657 140.131 1.00 55.98  ? 119  ILE L CB    1 
ATOM   6978  C  CG1   . ILE C 2 119 ? 120.288 132.847 140.922 1.00 58.74  ? 119  ILE L CG1   1 
ATOM   6979  C  CG2   . ILE C 2 119 ? 119.882 134.242 138.877 1.00 58.27  ? 119  ILE L CG2   1 
ATOM   6980  C  CD1   . ILE C 2 119 ? 120.908 131.713 140.134 1.00 59.20  ? 119  ILE L CD1   1 
ATOM   6981  N  N     . TYR C 2 120 ? 116.869 135.692 139.642 1.00 65.66  ? 120  TYR L N     1 
ATOM   6982  C  CA    . TYR C 2 120 ? 116.192 136.743 138.889 1.00 62.25  ? 120  TYR L CA    1 
ATOM   6983  C  C     . TYR C 2 120 ? 115.966 137.982 139.742 1.00 61.20  ? 120  TYR L C     1 
ATOM   6984  O  O     . TYR C 2 120 ? 115.997 139.106 139.227 1.00 61.99  ? 120  TYR L O     1 
ATOM   6985  C  CB    . TYR C 2 120 ? 114.861 136.223 138.345 1.00 61.71  ? 120  TYR L CB    1 
ATOM   6986  C  CG    . TYR C 2 120 ? 113.984 137.293 137.737 1.00 68.09  ? 120  TYR L CG    1 
ATOM   6987  C  CD1   . TYR C 2 120 ? 114.269 137.824 136.486 1.00 68.12  ? 120  TYR L CD1   1 
ATOM   6988  C  CD2   . TYR C 2 120 ? 112.867 137.769 138.411 1.00 67.62  ? 120  TYR L CD2   1 
ATOM   6989  C  CE1   . TYR C 2 120 ? 113.470 138.802 135.924 1.00 68.12  ? 120  TYR L CE1   1 
ATOM   6990  C  CE2   . TYR C 2 120 ? 112.061 138.747 137.858 1.00 65.40  ? 120  TYR L CE2   1 
ATOM   6991  C  CZ    . TYR C 2 120 ? 112.367 139.259 136.615 1.00 66.66  ? 120  TYR L CZ    1 
ATOM   6992  O  OH    . TYR C 2 120 ? 111.568 140.232 136.060 1.00 65.79  ? 120  TYR L OH    1 
ATOM   6993  N  N     . SER C 2 121 ? 115.750 137.802 141.039 1.00 59.18  ? 121  SER L N     1 
ATOM   6994  C  CA    . SER C 2 121 ? 115.593 138.925 141.953 1.00 60.45  ? 121  SER L CA    1 
ATOM   6995  C  C     . SER C 2 121 ? 116.969 139.492 142.302 1.00 59.54  ? 121  SER L C     1 
ATOM   6996  O  O     . SER C 2 121 ? 117.966 139.228 141.625 1.00 57.44  ? 121  SER L O     1 
ATOM   6997  C  CB    . SER C 2 121 ? 114.817 138.494 143.194 1.00 59.67  ? 121  SER L CB    1 
ATOM   6998  O  OG    . SER C 2 121 ? 115.583 137.610 143.993 1.00 61.31  ? 121  SER L OG    1 
ATOM   6999  N  N     . MET C 2 122 ? 117.014 140.323 143.346 1.00 68.19  ? 122  MET L N     1 
ATOM   7000  C  CA    . MET C 2 122 ? 118.231 140.867 143.948 1.00 68.44  ? 122  MET L CA    1 
ATOM   7001  C  C     . MET C 2 122 ? 119.117 141.620 142.960 1.00 67.05  ? 122  MET L C     1 
ATOM   7002  O  O     . MET C 2 122 ? 118.717 141.871 141.818 1.00 65.50  ? 122  MET L O     1 
ATOM   7003  C  CB    . MET C 2 122 ? 119.025 139.759 144.659 1.00 69.40  ? 122  MET L CB    1 
ATOM   7004  C  CG    . MET C 2 122 ? 119.968 138.922 143.804 1.00 69.52  ? 122  MET L CG    1 
ATOM   7005  S  SD    . MET C 2 122 ? 120.755 137.632 144.781 1.00 70.17  ? 122  MET L SD    1 
ATOM   7006  C  CE    . MET C 2 122 ? 119.323 136.949 145.605 1.00 67.38  ? 122  MET L CE    1 
ATOM   7007  N  N     . ASP C 2 123 ? 120.316 141.996 143.407 1.00 81.39  ? 123  ASP L N     1 
ATOM   7008  C  CA    . ASP C 2 123 ? 121.140 142.957 142.684 1.00 84.44  ? 123  ASP L CA    1 
ATOM   7009  C  C     . ASP C 2 123 ? 121.488 142.459 141.288 1.00 86.18  ? 123  ASP L C     1 
ATOM   7010  O  O     . ASP C 2 123 ? 121.860 141.299 141.095 1.00 88.11  ? 123  ASP L O     1 
ATOM   7011  C  CB    . ASP C 2 123 ? 122.419 143.245 143.470 1.00 84.94  ? 123  ASP L CB    1 
ATOM   7012  C  CG    . ASP C 2 123 ? 122.143 143.869 144.823 1.00 89.13  ? 123  ASP L CG    1 
ATOM   7013  O  OD1   . ASP C 2 123 ? 121.120 144.573 144.957 1.00 87.44  ? 123  ASP L OD1   1 
ATOM   7014  O  OD2   . ASP C 2 123 ? 122.950 143.657 145.752 1.00 90.66  ? 123  ASP L OD2   1 
ATOM   7015  N  N     . GLU C 2 124 ? 121.367 143.359 140.309 1.00 85.92  ? 124  GLU L N     1 
ATOM   7016  C  CA    . GLU C 2 124 ? 121.682 143.009 138.929 1.00 85.21  ? 124  GLU L CA    1 
ATOM   7017  C  C     . GLU C 2 124 ? 123.184 142.891 138.706 1.00 86.42  ? 124  GLU L C     1 
ATOM   7018  O  O     . GLU C 2 124 ? 123.622 142.119 137.845 1.00 86.42  ? 124  GLU L O     1 
ATOM   7019  C  CB    . GLU C 2 124 ? 121.077 144.043 137.978 1.00 85.51  ? 124  GLU L CB    1 
ATOM   7020  C  CG    . GLU C 2 124 ? 121.126 143.654 136.508 1.00 86.87  ? 124  GLU L CG    1 
ATOM   7021  C  CD    . GLU C 2 124 ? 122.369 144.169 135.809 1.00 87.55  ? 124  GLU L CD    1 
ATOM   7022  O  OE1   . GLU C 2 124 ? 123.039 145.064 136.368 1.00 87.59  ? 124  GLU L OE1   1 
ATOM   7023  O  OE2   . GLU C 2 124 ? 122.677 143.679 134.703 1.00 85.66  ? 124  GLU L OE2   1 
ATOM   7024  N  N     . ASN C 2 125 ? 123.987 143.634 139.469 1.00 88.52  ? 125  ASN L N     1 
ATOM   7025  C  CA    . ASN C 2 125 ? 125.442 143.624 139.312 1.00 88.98  ? 125  ASN L CA    1 
ATOM   7026  C  C     . ASN C 2 125 ? 126.020 142.380 139.990 1.00 86.42  ? 125  ASN L C     1 
ATOM   7027  O  O     . ASN C 2 125 ? 126.716 142.440 141.005 1.00 83.85  ? 125  ASN L O     1 
ATOM   7028  C  CB    . ASN C 2 125 ? 126.046 144.902 139.875 1.00 88.95  ? 125  ASN L CB    1 
ATOM   7029  C  CG    . ASN C 2 125 ? 125.513 146.146 139.195 1.00 89.34  ? 125  ASN L CG    1 
ATOM   7030  O  OD1   . ASN C 2 125 ? 124.905 147.005 139.833 1.00 88.88  ? 125  ASN L OD1   1 
ATOM   7031  N  ND2   . ASN C 2 125 ? 125.740 146.251 137.890 1.00 87.68  ? 125  ASN L ND2   1 
ATOM   7032  N  N     . LEU C 2 126 ? 125.718 141.228 139.392 1.00 78.08  ? 126  LEU L N     1 
ATOM   7033  C  CA    . LEU C 2 126 ? 126.187 139.944 139.897 1.00 74.06  ? 126  LEU L CA    1 
ATOM   7034  C  C     . LEU C 2 126 ? 126.233 138.958 138.742 1.00 74.23  ? 126  LEU L C     1 
ATOM   7035  O  O     . LEU C 2 126 ? 125.277 138.869 137.966 1.00 73.70  ? 126  LEU L O     1 
ATOM   7036  C  CB    . LEU C 2 126 ? 125.272 139.418 141.009 1.00 70.77  ? 126  LEU L CB    1 
ATOM   7037  C  CG    . LEU C 2 126 ? 125.609 139.796 142.451 1.00 74.09  ? 126  LEU L CG    1 
ATOM   7038  C  CD1   . LEU C 2 126 ? 124.511 139.333 143.394 1.00 76.58  ? 126  LEU L CD1   1 
ATOM   7039  C  CD2   . LEU C 2 126 ? 126.947 139.209 142.856 1.00 71.93  ? 126  LEU L CD2   1 
ATOM   7040  N  N     . GLU C 2 127 ? 127.334 138.222 138.631 1.00 60.83  ? 127  GLU L N     1 
ATOM   7041  C  CA    . GLU C 2 127 ? 127.498 137.198 137.609 1.00 56.93  ? 127  GLU L CA    1 
ATOM   7042  C  C     . GLU C 2 127 ? 127.405 135.824 138.256 1.00 54.54  ? 127  GLU L C     1 
ATOM   7043  O  O     . GLU C 2 127 ? 128.162 135.517 139.183 1.00 59.66  ? 127  GLU L O     1 
ATOM   7044  C  CB    . GLU C 2 127 ? 128.833 137.354 136.880 1.00 55.68  ? 127  GLU L CB    1 
ATOM   7045  C  CG    . GLU C 2 127 ? 128.890 138.546 135.945 1.00 57.81  ? 127  GLU L CG    1 
ATOM   7046  C  CD    . GLU C 2 127 ? 130.146 138.560 135.098 1.00 64.38  ? 127  GLU L CD    1 
ATOM   7047  O  OE1   . GLU C 2 127 ? 130.969 137.631 135.240 1.00 63.57  ? 127  GLU L OE1   1 
ATOM   7048  O  OE2   . GLU C 2 127 ? 130.312 139.498 134.291 1.00 64.24  ? 127  GLU L OE2   1 
ATOM   7049  N  N     . PHE C 2 128 ? 126.482 135.003 137.766 1.00 33.72  ? 128  PHE L N     1 
ATOM   7050  C  CA    . PHE C 2 128 ? 126.239 133.672 138.302 1.00 29.51  ? 128  PHE L CA    1 
ATOM   7051  C  C     . PHE C 2 128 ? 126.657 132.625 137.281 1.00 36.93  ? 128  PHE L C     1 
ATOM   7052  O  O     . PHE C 2 128 ? 126.212 132.664 136.129 1.00 43.36  ? 128  PHE L O     1 
ATOM   7053  C  CB    . PHE C 2 128 ? 124.763 133.481 138.658 1.00 30.38  ? 128  PHE L CB    1 
ATOM   7054  C  CG    . PHE C 2 128 ? 124.306 134.296 139.830 1.00 35.56  ? 128  PHE L CG    1 
ATOM   7055  C  CD1   . PHE C 2 128 ? 124.991 134.261 141.028 1.00 39.73  ? 128  PHE L CD1   1 
ATOM   7056  C  CD2   . PHE C 2 128 ? 123.183 135.099 139.731 1.00 40.10  ? 128  PHE L CD2   1 
ATOM   7057  C  CE1   . PHE C 2 128 ? 124.565 135.011 142.105 1.00 40.23  ? 128  PHE L CE1   1 
ATOM   7058  C  CE2   . PHE C 2 128 ? 122.752 135.851 140.805 1.00 37.37  ? 128  PHE L CE2   1 
ATOM   7059  C  CZ    . PHE C 2 128 ? 123.446 135.808 141.993 1.00 39.93  ? 128  PHE L CZ    1 
ATOM   7060  N  N     . HIS C 2 129 ? 127.507 131.696 137.704 1.00 23.54  ? 129  HIS L N     1 
ATOM   7061  C  CA    . HIS C 2 129 ? 127.826 130.499 136.936 1.00 14.69  ? 129  HIS L CA    1 
ATOM   7062  C  C     . HIS C 2 129 ? 127.376 129.303 137.761 1.00 24.80  ? 129  HIS L C     1 
ATOM   7063  O  O     . HIS C 2 129 ? 128.042 128.930 138.732 1.00 40.79  ? 129  HIS L O     1 
ATOM   7064  C  CB    . HIS C 2 129 ? 129.318 130.409 136.624 1.00 25.00  ? 129  HIS L CB    1 
ATOM   7065  C  CG    . HIS C 2 129 ? 129.800 131.437 135.651 1.00 30.97  ? 129  HIS L CG    1 
ATOM   7066  N  ND1   . HIS C 2 129 ? 130.063 132.740 136.012 1.00 31.69  ? 129  HIS L ND1   1 
ATOM   7067  C  CD2   . HIS C 2 129 ? 130.078 131.350 134.329 1.00 32.02  ? 129  HIS L CD2   1 
ATOM   7068  C  CE1   . HIS C 2 129 ? 130.478 133.413 134.955 1.00 32.41  ? 129  HIS L CE1   1 
ATOM   7069  N  NE2   . HIS C 2 129 ? 130.495 132.593 133.920 1.00 29.58  ? 129  HIS L NE2   1 
ATOM   7070  N  N     . ILE C 2 130 ? 126.253 128.702 137.383 1.00 16.23  ? 130  ILE L N     1 
ATOM   7071  C  CA    . ILE C 2 130 ? 125.689 127.571 138.108 1.00 18.95  ? 130  ILE L CA    1 
ATOM   7072  C  C     . ILE C 2 130 ? 125.925 126.305 137.294 1.00 21.94  ? 130  ILE L C     1 
ATOM   7073  O  O     . ILE C 2 130 ? 125.667 126.272 136.084 1.00 34.05  ? 130  ILE L O     1 
ATOM   7074  C  CB    . ILE C 2 130 ? 124.199 127.792 138.432 1.00 17.24  ? 130  ILE L CB    1 
ATOM   7075  C  CG1   . ILE C 2 130 ? 123.325 127.737 137.184 1.00 30.98  ? 130  ILE L CG1   1 
ATOM   7076  C  CG2   . ILE C 2 130 ? 124.005 129.126 139.125 1.00 14.51  ? 130  ILE L CG2   1 
ATOM   7077  C  CD1   . ILE C 2 130 ? 121.848 127.711 137.494 1.00 32.66  ? 130  ILE L CD1   1 
ATOM   7078  N  N     . LYS C 2 131 ? 126.467 125.283 137.950 1.00 23.68  ? 131  LYS L N     1 
ATOM   7079  C  CA    . LYS C 2 131 ? 126.792 124.010 137.327 1.00 21.43  ? 131  LYS L CA    1 
ATOM   7080  C  C     . LYS C 2 131 ? 126.092 122.886 138.072 1.00 23.42  ? 131  LYS L C     1 
ATOM   7081  O  O     . LYS C 2 131 ? 126.101 122.851 139.305 1.00 36.33  ? 131  LYS L O     1 
ATOM   7082  C  CB    . LYS C 2 131 ? 128.299 123.758 137.333 1.00 13.77  ? 131  LYS L CB    1 
ATOM   7083  C  CG    . LYS C 2 131 ? 129.132 124.943 136.894 1.00 23.89  ? 131  LYS L CG    1 
ATOM   7084  C  CD    . LYS C 2 131 ? 130.615 124.648 137.031 1.00 25.44  ? 131  LYS L CD    1 
ATOM   7085  C  CE    . LYS C 2 131 ? 131.031 123.488 136.146 1.00 33.00  ? 131  LYS L CE    1 
ATOM   7086  N  NZ    . LYS C 2 131 ? 132.476 123.166 136.299 1.00 36.52  ? 131  LYS L NZ    1 
ATOM   7087  N  N     . VAL C 2 132 ? 125.496 121.964 137.325 1.00 6.63   ? 132  VAL L N     1 
ATOM   7088  C  CA    . VAL C 2 132 ? 124.843 120.805 137.911 1.00 6.42   ? 132  VAL L CA    1 
ATOM   7089  C  C     . VAL C 2 132 ? 125.635 119.559 137.541 1.00 19.83  ? 132  VAL L C     1 
ATOM   7090  O  O     . VAL C 2 132 ? 126.344 119.516 136.533 1.00 39.96  ? 132  VAL L O     1 
ATOM   7091  C  CB    . VAL C 2 132 ? 123.375 120.670 137.468 1.00 12.67  ? 132  VAL L CB    1 
ATOM   7092  C  CG1   . VAL C 2 132 ? 122.613 121.938 137.789 1.00 21.11  ? 132  VAL L CG1   1 
ATOM   7093  C  CG2   . VAL C 2 132 ? 123.293 120.357 135.985 1.00 31.75  ? 132  VAL L CG2   1 
ATOM   7094  N  N     . SER C 2 133 ? 125.517 118.541 138.387 1.00 18.28  ? 133  SER L N     1 
ATOM   7095  C  CA    . SER C 2 133 ? 126.216 117.279 138.166 1.00 15.98  ? 133  SER L CA    1 
ATOM   7096  C  C     . SER C 2 133 ? 125.478 116.190 138.922 1.00 28.96  ? 133  SER L C     1 
ATOM   7097  O  O     . SER C 2 133 ? 125.476 116.187 140.157 1.00 42.64  ? 133  SER L O     1 
ATOM   7098  C  CB    . SER C 2 133 ? 127.669 117.373 138.624 1.00 21.31  ? 133  SER L CB    1 
ATOM   7099  O  OG    . SER C 2 133 ? 127.760 117.931 139.922 1.00 35.02  ? 133  SER L OG    1 
ATOM   7100  N  N     . TYR C 2 134 ? 124.856 115.273 138.190 1.00 37.12  ? 134  TYR L N     1 
ATOM   7101  C  CA    . TYR C 2 134 ? 124.049 114.209 138.767 1.00 39.73  ? 134  TYR L CA    1 
ATOM   7102  C  C     . TYR C 2 134 ? 124.775 112.881 138.606 1.00 44.45  ? 134  TYR L C     1 
ATOM   7103  O  O     . TYR C 2 134 ? 125.142 112.501 137.488 1.00 53.41  ? 134  TYR L O     1 
ATOM   7104  C  CB    . TYR C 2 134 ? 122.675 114.154 138.096 1.00 38.89  ? 134  TYR L CB    1 
ATOM   7105  C  CG    . TYR C 2 134 ? 121.608 113.430 138.883 1.00 39.02  ? 134  TYR L CG    1 
ATOM   7106  C  CD1   . TYR C 2 134 ? 121.876 112.898 140.136 1.00 50.45  ? 134  TYR L CD1   1 
ATOM   7107  C  CD2   . TYR C 2 134 ? 120.329 113.280 138.370 1.00 41.75  ? 134  TYR L CD2   1 
ATOM   7108  C  CE1   . TYR C 2 134 ? 120.899 112.234 140.853 1.00 52.32  ? 134  TYR L CE1   1 
ATOM   7109  C  CE2   . TYR C 2 134 ? 119.348 112.622 139.078 1.00 44.48  ? 134  TYR L CE2   1 
ATOM   7110  C  CZ    . TYR C 2 134 ? 119.637 112.100 140.319 1.00 50.17  ? 134  TYR L CZ    1 
ATOM   7111  O  OH    . TYR C 2 134 ? 118.658 111.442 141.028 1.00 51.55  ? 134  TYR L OH    1 
ATOM   7112  N  N     . PHE C 2 135 ? 124.982 112.180 139.718 1.00 52.61  ? 135  PHE L N     1 
ATOM   7113  C  CA    . PHE C 2 135 ? 125.624 110.876 139.686 1.00 51.20  ? 135  PHE L CA    1 
ATOM   7114  C  C     . PHE C 2 135 ? 125.113 110.035 140.845 1.00 56.15  ? 135  PHE L C     1 
ATOM   7115  O  O     . PHE C 2 135 ? 124.611 110.556 141.844 1.00 56.96  ? 135  PHE L O     1 
ATOM   7116  C  CB    . PHE C 2 135 ? 127.151 110.995 139.734 1.00 49.80  ? 135  PHE L CB    1 
ATOM   7117  C  CG    . PHE C 2 135 ? 127.680 111.577 141.015 1.00 49.48  ? 135  PHE L CG    1 
ATOM   7118  C  CD1   . PHE C 2 135 ? 127.711 112.946 141.208 1.00 52.48  ? 135  PHE L CD1   1 
ATOM   7119  C  CD2   . PHE C 2 135 ? 128.164 110.754 142.016 1.00 53.00  ? 135  PHE L CD2   1 
ATOM   7120  C  CE1   . PHE C 2 135 ? 128.205 113.484 142.380 1.00 56.66  ? 135  PHE L CE1   1 
ATOM   7121  C  CE2   . PHE C 2 135 ? 128.659 111.286 143.189 1.00 52.82  ? 135  PHE L CE2   1 
ATOM   7122  C  CZ    . PHE C 2 135 ? 128.681 112.653 143.370 1.00 52.49  ? 135  PHE L CZ    1 
ATOM   7123  N  N     . GLU C 2 136 ? 125.250 108.719 140.701 1.00 75.96  ? 136  GLU L N     1 
ATOM   7124  C  CA    . GLU C 2 136 ? 124.781 107.773 141.701 1.00 77.42  ? 136  GLU L CA    1 
ATOM   7125  C  C     . GLU C 2 136 ? 125.852 106.718 141.932 1.00 76.96  ? 136  GLU L C     1 
ATOM   7126  O  O     . GLU C 2 136 ? 126.760 106.532 141.119 1.00 80.42  ? 136  GLU L O     1 
ATOM   7127  C  CB    . GLU C 2 136 ? 123.461 107.114 141.280 1.00 75.53  ? 136  GLU L CB    1 
ATOM   7128  C  CG    . GLU C 2 136 ? 123.538 106.357 139.966 1.00 77.58  ? 136  GLU L CG    1 
ATOM   7129  C  CD    . GLU C 2 136 ? 122.290 105.542 139.690 1.00 80.05  ? 136  GLU L CD    1 
ATOM   7130  O  OE1   . GLU C 2 136 ? 121.564 105.218 140.653 1.00 77.56  ? 136  GLU L OE1   1 
ATOM   7131  O  OE2   . GLU C 2 136 ? 122.034 105.224 138.509 1.00 78.51  ? 136  GLU L OE2   1 
ATOM   7132  N  N     . ILE C 2 137 ? 125.745 106.022 143.063 1.00 72.90  ? 137  ILE L N     1 
ATOM   7133  C  CA    . ILE C 2 137 ? 126.668 104.950 143.402 1.00 73.62  ? 137  ILE L CA    1 
ATOM   7134  C  C     . ILE C 2 137 ? 125.867 103.694 143.712 1.00 77.14  ? 137  ILE L C     1 
ATOM   7135  O  O     . ILE C 2 137 ? 124.693 103.750 144.085 1.00 79.14  ? 137  ILE L O     1 
ATOM   7136  C  CB    . ILE C 2 137 ? 127.581 105.309 144.592 1.00 73.49  ? 137  ILE L CB    1 
ATOM   7137  C  CG1   . ILE C 2 137 ? 126.778 105.371 145.887 1.00 73.60  ? 137  ILE L CG1   1 
ATOM   7138  C  CG2   . ILE C 2 137 ? 128.274 106.635 144.352 1.00 74.14  ? 137  ILE L CG2   1 
ATOM   7139  C  CD1   . ILE C 2 137 ? 127.611 105.090 147.110 1.00 73.91  ? 137  ILE L CD1   1 
ATOM   7140  N  N     . TYR C 2 138 ? 126.521 102.547 143.543 1.00 95.08  ? 138  TYR L N     1 
ATOM   7141  C  CA    . TYR C 2 138 ? 125.896 101.260 143.822 1.00 96.43  ? 138  TYR L CA    1 
ATOM   7142  C  C     . TYR C 2 138 ? 126.984 100.255 144.162 1.00 95.94  ? 138  TYR L C     1 
ATOM   7143  O  O     . TYR C 2 138 ? 127.992 100.175 143.454 1.00 93.49  ? 138  TYR L O     1 
ATOM   7144  C  CB    . TYR C 2 138 ? 125.069 100.769 142.627 1.00 97.64  ? 138  TYR L CB    1 
ATOM   7145  C  CG    . TYR C 2 138 ? 124.326 99.477  142.887 1.00 99.03  ? 138  TYR L CG    1 
ATOM   7146  C  CD1   . TYR C 2 138 ? 123.059 99.485  143.455 1.00 96.56  ? 138  TYR L CD1   1 
ATOM   7147  C  CD2   . TYR C 2 138 ? 124.890 98.249  142.563 1.00 97.89  ? 138  TYR L CD2   1 
ATOM   7148  C  CE1   . TYR C 2 138 ? 122.375 98.308  143.695 1.00 96.26  ? 138  TYR L CE1   1 
ATOM   7149  C  CE2   . TYR C 2 138 ? 124.214 97.066  142.799 1.00 96.77  ? 138  TYR L CE2   1 
ATOM   7150  C  CZ    . TYR C 2 138 ? 122.957 97.101  143.365 1.00 96.75  ? 138  TYR L CZ    1 
ATOM   7151  O  OH    . TYR C 2 138 ? 122.279 95.927  143.602 1.00 96.46  ? 138  TYR L OH    1 
ATOM   7152  N  N     . LEU C 2 139 ? 126.773 99.497  145.239 1.00 100.35 ? 139  LEU L N     1 
ATOM   7153  C  CA    . LEU C 2 139 ? 127.712 98.463  145.677 1.00 102.80 ? 139  LEU L CA    1 
ATOM   7154  C  C     . LEU C 2 139 ? 129.119 99.034  145.847 1.00 103.11 ? 139  LEU L C     1 
ATOM   7155  O  O     . LEU C 2 139 ? 130.117 98.410  145.480 1.00 104.05 ? 139  LEU L O     1 
ATOM   7156  C  CB    . LEU C 2 139 ? 127.711 97.277  144.708 1.00 101.94 ? 139  LEU L CB    1 
ATOM   7157  C  CG    . LEU C 2 139 ? 128.108 95.913  145.278 1.00 103.74 ? 139  LEU L CG    1 
ATOM   7158  C  CD1   . LEU C 2 139 ? 127.186 95.515  146.420 1.00 102.68 ? 139  LEU L CD1   1 
ATOM   7159  C  CD2   . LEU C 2 139 ? 128.100 94.854  144.187 1.00 101.92 ? 139  LEU L CD2   1 
ATOM   7160  N  N     . ASP C 2 140 ? 129.190 100.241 146.413 1.00 99.59  ? 140  ASP L N     1 
ATOM   7161  C  CA    . ASP C 2 140 ? 130.446 100.972 146.592 1.00 98.54  ? 140  ASP L CA    1 
ATOM   7162  C  C     . ASP C 2 140 ? 131.168 101.195 145.266 1.00 98.91  ? 140  ASP L C     1 
ATOM   7163  O  O     . ASP C 2 140 ? 132.400 101.166 145.205 1.00 99.35  ? 140  ASP L O     1 
ATOM   7164  C  CB    . ASP C 2 140 ? 131.367 100.264 147.590 1.00 100.16 ? 140  ASP L CB    1 
ATOM   7165  C  CG    . ASP C 2 140 ? 130.787 100.220 148.989 1.00 101.80 ? 140  ASP L CG    1 
ATOM   7166  O  OD1   . ASP C 2 140 ? 129.683 100.768 149.192 1.00 100.83 ? 140  ASP L OD1   1 
ATOM   7167  O  OD2   . ASP C 2 140 ? 131.434 99.638  149.885 1.00 102.90 ? 140  ASP L OD2   1 
ATOM   7168  N  N     . LYS C 2 141 ? 130.410 101.418 144.194 1.00 91.43  ? 141  LYS L N     1 
ATOM   7169  C  CA    . LYS C 2 141 ? 130.967 101.736 142.883 1.00 92.16  ? 141  LYS L CA    1 
ATOM   7170  C  C     . LYS C 2 141 ? 130.315 103.018 142.385 1.00 94.61  ? 141  LYS L C     1 
ATOM   7171  O  O     . LYS C 2 141 ? 129.093 103.067 142.215 1.00 91.80  ? 141  LYS L O     1 
ATOM   7172  C  CB    . LYS C 2 141 ? 130.739 100.593 141.889 1.00 91.48  ? 141  LYS L CB    1 
ATOM   7173  C  CG    . LYS C 2 141 ? 130.915 99.202  142.481 1.00 90.88  ? 141  LYS L CG    1 
ATOM   7174  C  CD    . LYS C 2 141 ? 132.368 98.904  142.813 1.00 91.53  ? 141  LYS L CD    1 
ATOM   7175  C  CE    . LYS C 2 141 ? 133.169 98.598  141.560 1.00 93.29  ? 141  LYS L CE    1 
ATOM   7176  N  NZ    . LYS C 2 141 ? 134.588 98.271  141.875 1.00 93.07  ? 141  LYS L NZ    1 
ATOM   7177  N  N     . ILE C 2 142 ? 131.126 104.045 142.146 1.00 83.71  ? 142  ILE L N     1 
ATOM   7178  C  CA    . ILE C 2 142 ? 130.632 105.356 141.735 1.00 76.13  ? 142  ILE L CA    1 
ATOM   7179  C  C     . ILE C 2 142 ? 130.463 105.365 140.222 1.00 77.80  ? 142  ILE L C     1 
ATOM   7180  O  O     . ILE C 2 142 ? 131.409 105.074 139.482 1.00 84.50  ? 142  ILE L O     1 
ATOM   7181  C  CB    . ILE C 2 142 ? 131.582 106.474 142.184 1.00 75.94  ? 142  ILE L CB    1 
ATOM   7182  C  CG1   . ILE C 2 142 ? 131.795 106.418 143.697 1.00 82.16  ? 142  ILE L CG1   1 
ATOM   7183  C  CG2   . ILE C 2 142 ? 131.038 107.825 141.764 1.00 73.82  ? 142  ILE L CG2   1 
ATOM   7184  C  CD1   . ILE C 2 142 ? 132.739 107.474 144.217 1.00 81.39  ? 142  ILE L CD1   1 
ATOM   7185  N  N     . ARG C 2 143 ? 129.264 105.711 139.760 1.00 71.52  ? 143  ARG L N     1 
ATOM   7186  C  CA    . ARG C 2 143 ? 128.942 105.709 138.341 1.00 69.65  ? 143  ARG L CA    1 
ATOM   7187  C  C     . ARG C 2 143 ? 128.283 107.027 137.970 1.00 71.74  ? 143  ARG L C     1 
ATOM   7188  O  O     . ARG C 2 143 ? 127.356 107.474 138.652 1.00 74.98  ? 143  ARG L O     1 
ATOM   7189  C  CB    . ARG C 2 143 ? 128.017 104.541 137.987 1.00 69.97  ? 143  ARG L CB    1 
ATOM   7190  C  CG    . ARG C 2 143 ? 128.584 103.169 138.309 1.00 72.32  ? 143  ARG L CG    1 
ATOM   7191  C  CD    . ARG C 2 143 ? 127.481 102.120 138.358 1.00 74.42  ? 143  ARG L CD    1 
ATOM   7192  N  NE    . ARG C 2 143 ? 127.994 100.791 138.666 1.00 75.95  ? 143  ARG L NE    1 
ATOM   7193  C  CZ    . ARG C 2 143 ? 128.098 99.804  137.786 1.00 76.93  ? 143  ARG L CZ    1 
ATOM   7194  N  NH1   . ARG C 2 143 ? 127.718 99.958  136.528 1.00 76.63  ? 143  ARG L NH1   1 
ATOM   7195  N  NH2   . ARG C 2 143 ? 128.592 98.633  138.179 1.00 75.32  ? 143  ARG L NH2   1 
ATOM   7196  N  N     . ASP C 2 144 ? 128.758 107.646 136.894 1.00 68.08  ? 144  ASP L N     1 
ATOM   7197  C  CA    . ASP C 2 144 ? 128.120 108.856 136.397 1.00 64.70  ? 144  ASP L CA    1 
ATOM   7198  C  C     . ASP C 2 144 ? 126.734 108.533 135.856 1.00 62.14  ? 144  ASP L C     1 
ATOM   7199  O  O     . ASP C 2 144 ? 126.524 107.505 135.208 1.00 66.43  ? 144  ASP L O     1 
ATOM   7200  C  CB    . ASP C 2 144 ? 128.976 109.504 135.310 1.00 68.20  ? 144  ASP L CB    1 
ATOM   7201  C  CG    . ASP C 2 144 ? 128.595 110.950 135.047 1.00 69.33  ? 144  ASP L CG    1 
ATOM   7202  O  OD1   . ASP C 2 144 ? 127.387 111.267 135.055 1.00 68.45  ? 144  ASP L OD1   1 
ATOM   7203  O  OD2   . ASP C 2 144 ? 129.509 111.774 134.832 1.00 69.66  ? 144  ASP L OD2   1 
ATOM   7204  N  N     . LEU C 2 145 ? 125.783 109.424 136.124 1.00 59.16  ? 145  LEU L N     1 
ATOM   7205  C  CA    . LEU C 2 145 ? 124.399 109.224 135.717 1.00 60.99  ? 145  LEU L CA    1 
ATOM   7206  C  C     . LEU C 2 145 ? 124.053 109.913 134.407 1.00 61.68  ? 145  LEU L C     1 
ATOM   7207  O  O     . LEU C 2 145 ? 123.106 109.497 133.732 1.00 61.18  ? 145  LEU L O     1 
ATOM   7208  C  CB    . LEU C 2 145 ? 123.453 109.722 136.814 1.00 62.90  ? 145  LEU L CB    1 
ATOM   7209  C  CG    . LEU C 2 145 ? 121.989 109.306 136.700 1.00 65.02  ? 145  LEU L CG    1 
ATOM   7210  C  CD1   . LEU C 2 145 ? 121.887 107.806 136.494 1.00 63.76  ? 145  LEU L CD1   1 
ATOM   7211  C  CD2   . LEU C 2 145 ? 121.225 109.736 137.940 1.00 64.53  ? 145  LEU L CD2   1 
ATOM   7212  N  N     . LEU C 2 146 ? 124.799 110.950 134.030 1.00 70.14  ? 146  LEU L N     1 
ATOM   7213  C  CA    . LEU C 2 146 ? 124.550 111.653 132.780 1.00 72.62  ? 146  LEU L CA    1 
ATOM   7214  C  C     . LEU C 2 146 ? 125.235 111.002 131.586 1.00 72.28  ? 146  LEU L C     1 
ATOM   7215  O  O     . LEU C 2 146 ? 125.018 111.443 130.452 1.00 72.28  ? 146  LEU L O     1 
ATOM   7216  C  CB    . LEU C 2 146 ? 125.002 113.109 132.907 1.00 69.02  ? 146  LEU L CB    1 
ATOM   7217  C  CG    . LEU C 2 146 ? 124.473 113.852 134.134 1.00 67.42  ? 146  LEU L CG    1 
ATOM   7218  C  CD1   . LEU C 2 146 ? 124.999 115.276 134.169 1.00 67.73  ? 146  LEU L CD1   1 
ATOM   7219  C  CD2   . LEU C 2 146 ? 122.955 113.839 134.153 1.00 65.56  ? 146  LEU L CD2   1 
ATOM   7220  N  N     . ASP C 2 147 ? 126.049 109.972 131.810 1.00 76.93  ? 147  ASP L N     1 
ATOM   7221  C  CA    . ASP C 2 147 ? 126.736 109.274 130.725 1.00 74.14  ? 147  ASP L CA    1 
ATOM   7222  C  C     . ASP C 2 147 ? 127.049 107.865 131.206 1.00 74.93  ? 147  ASP L C     1 
ATOM   7223  O  O     . ASP C 2 147 ? 127.833 107.690 132.143 1.00 73.01  ? 147  ASP L O     1 
ATOM   7224  C  CB    . ASP C 2 147 ? 128.006 110.012 130.312 1.00 74.78  ? 147  ASP L CB    1 
ATOM   7225  C  CG    . ASP C 2 147 ? 128.609 109.466 129.033 1.00 77.16  ? 147  ASP L CG    1 
ATOM   7226  O  OD1   . ASP C 2 147 ? 127.962 108.619 128.381 1.00 79.39  ? 147  ASP L OD1   1 
ATOM   7227  O  OD2   . ASP C 2 147 ? 129.731 109.885 128.679 1.00 77.55  ? 147  ASP L OD2   1 
ATOM   7228  N  N     . VAL C 2 148 ? 126.439 106.865 130.566 1.00 75.93  ? 148  VAL L N     1 
ATOM   7229  C  CA    . VAL C 2 148 ? 126.615 105.479 130.985 1.00 76.04  ? 148  VAL L CA    1 
ATOM   7230  C  C     . VAL C 2 148 ? 128.010 104.944 130.706 1.00 79.45  ? 148  VAL L C     1 
ATOM   7231  O  O     . VAL C 2 148 ? 128.352 103.858 131.189 1.00 79.83  ? 148  VAL L O     1 
ATOM   7232  C  CB    . VAL C 2 148 ? 125.573 104.573 130.301 1.00 77.03  ? 148  VAL L CB    1 
ATOM   7233  C  CG1   . VAL C 2 148 ? 124.166 104.991 130.696 1.00 75.47  ? 148  VAL L CG1   1 
ATOM   7234  C  CG2   . VAL C 2 148 ? 125.743 104.615 128.790 1.00 76.65  ? 148  VAL L CG2   1 
ATOM   7235  N  N     . SER C 2 149 ? 128.822 105.669 129.932 1.00 81.51  ? 149  SER L N     1 
ATOM   7236  C  CA    . SER C 2 149 ? 130.183 105.216 129.659 1.00 78.39  ? 149  SER L CA    1 
ATOM   7237  C  C     . SER C 2 149 ? 131.012 105.156 130.936 1.00 79.72  ? 149  SER L C     1 
ATOM   7238  O  O     . SER C 2 149 ? 131.783 104.211 131.141 1.00 81.39  ? 149  SER L O     1 
ATOM   7239  C  CB    . SER C 2 149 ? 130.847 106.134 128.633 1.00 72.56  ? 149  SER L CB    1 
ATOM   7240  O  OG    . SER C 2 149 ? 130.129 106.138 127.412 1.00 72.41  ? 149  SER L OG    1 
ATOM   7241  N  N     . LYS C 2 150 ? 130.867 106.153 131.803 1.00 75.50  ? 150  LYS L N     1 
ATOM   7242  C  CA    . LYS C 2 150 ? 131.641 106.191 133.035 1.00 74.43  ? 150  LYS L CA    1 
ATOM   7243  C  C     . LYS C 2 150 ? 131.095 105.177 134.033 1.00 74.28  ? 150  LYS L C     1 
ATOM   7244  O  O     . LYS C 2 150 ? 129.881 105.071 134.228 1.00 76.17  ? 150  LYS L O     1 
ATOM   7245  C  CB    . LYS C 2 150 ? 131.614 107.596 133.630 1.00 77.12  ? 150  LYS L CB    1 
ATOM   7246  C  CG    . LYS C 2 150 ? 131.518 108.697 132.587 1.00 77.28  ? 150  LYS L CG    1 
ATOM   7247  C  CD    . LYS C 2 150 ? 131.894 110.046 133.171 1.00 75.59  ? 150  LYS L CD    1 
ATOM   7248  C  CE    . LYS C 2 150 ? 133.384 110.120 133.454 1.00 75.23  ? 150  LYS L CE    1 
ATOM   7249  N  NZ    . LYS C 2 150 ? 134.191 109.959 132.213 1.00 73.25  ? 150  LYS L NZ    1 
ATOM   7250  N  N     . THR C 2 151 ? 131.998 104.428 134.661 1.00 80.59  ? 151  THR L N     1 
ATOM   7251  C  CA    . THR C 2 151 ? 131.618 103.397 135.615 1.00 83.04  ? 151  THR L CA    1 
ATOM   7252  C  C     . THR C 2 151 ? 132.792 103.151 136.551 1.00 82.56  ? 151  THR L C     1 
ATOM   7253  O  O     . THR C 2 151 ? 133.944 103.124 136.109 1.00 82.95  ? 151  THR L O     1 
ATOM   7254  C  CB    . THR C 2 151 ? 131.218 102.095 134.905 1.00 84.58  ? 151  THR L CB    1 
ATOM   7255  O  OG1   . THR C 2 151 ? 130.105 102.341 134.036 1.00 81.50  ? 151  THR L OG1   1 
ATOM   7256  C  CG2   . THR C 2 151 ? 130.835 101.021 135.913 1.00 81.48  ? 151  THR L CG2   1 
ATOM   7257  N  N     . ASN C 2 152 ? 132.489 102.976 137.838 1.00 80.54  ? 152  ASN L N     1 
ATOM   7258  C  CA    . ASN C 2 152 ? 133.491 102.692 138.865 1.00 81.17  ? 152  ASN L CA    1 
ATOM   7259  C  C     . ASN C 2 152 ? 134.554 103.793 138.914 1.00 84.72  ? 152  ASN L C     1 
ATOM   7260  O  O     . ASN C 2 152 ? 135.746 103.563 138.702 1.00 86.32  ? 152  ASN L O     1 
ATOM   7261  C  CB    . ASN C 2 152 ? 134.127 101.315 138.645 1.00 84.20  ? 152  ASN L CB    1 
ATOM   7262  C  CG    . ASN C 2 152 ? 135.002 100.883 139.806 1.00 86.34  ? 152  ASN L CG    1 
ATOM   7263  O  OD1   . ASN C 2 152 ? 134.875 101.397 140.918 1.00 86.31  ? 152  ASN L OD1   1 
ATOM   7264  N  ND2   . ASN C 2 152 ? 135.896 99.935  139.553 1.00 83.95  ? 152  ASN L ND2   1 
ATOM   7265  N  N     . LEU C 2 153 ? 134.093 105.009 139.195 1.00 80.11  ? 153  LEU L N     1 
ATOM   7266  C  CA    . LEU C 2 153 ? 134.993 106.139 139.344 1.00 75.16  ? 153  LEU L CA    1 
ATOM   7267  C  C     . LEU C 2 153 ? 135.619 106.131 140.737 1.00 76.33  ? 153  LEU L C     1 
ATOM   7268  O  O     . LEU C 2 153 ? 135.479 105.179 141.510 1.00 77.47  ? 153  LEU L O     1 
ATOM   7269  C  CB    . LEU C 2 153 ? 134.255 107.448 139.079 1.00 73.48  ? 153  LEU L CB    1 
ATOM   7270  C  CG    . LEU C 2 153 ? 134.086 107.832 137.609 1.00 72.29  ? 153  LEU L CG    1 
ATOM   7271  C  CD1   . LEU C 2 153 ? 133.384 109.176 137.484 1.00 71.79  ? 153  LEU L CD1   1 
ATOM   7272  C  CD2   . LEU C 2 153 ? 135.436 107.859 136.914 1.00 72.41  ? 153  LEU L CD2   1 
ATOM   7273  N  N     . SER C 2 154 ? 136.321 107.213 141.065 1.00 66.45  ? 154  SER L N     1 
ATOM   7274  C  CA    . SER C 2 154 ? 137.010 107.331 142.339 1.00 63.23  ? 154  SER L CA    1 
ATOM   7275  C  C     . SER C 2 154 ? 136.915 108.767 142.827 1.00 57.12  ? 154  SER L C     1 
ATOM   7276  O  O     . SER C 2 154 ? 136.458 109.663 142.114 1.00 56.64  ? 154  SER L O     1 
ATOM   7277  C  CB    . SER C 2 154 ? 138.476 106.893 142.229 1.00 67.46  ? 154  SER L CB    1 
ATOM   7278  O  OG    . SER C 2 154 ? 138.576 105.547 141.797 1.00 67.36  ? 154  SER L OG    1 
ATOM   7279  N  N     . VAL C 2 155 ? 137.360 108.979 144.061 1.00 67.48  ? 155  VAL L N     1 
ATOM   7280  C  CA    . VAL C 2 155 ? 137.315 110.280 144.715 1.00 71.83  ? 155  VAL L CA    1 
ATOM   7281  C  C     . VAL C 2 155 ? 138.740 110.739 144.980 1.00 74.13  ? 155  VAL L C     1 
ATOM   7282  O  O     . VAL C 2 155 ? 139.533 110.007 145.585 1.00 75.04  ? 155  VAL L O     1 
ATOM   7283  C  CB    . VAL C 2 155 ? 136.508 110.221 146.022 1.00 73.35  ? 155  VAL L CB    1 
ATOM   7284  C  CG1   . VAL C 2 155 ? 136.565 111.555 146.728 1.00 71.21  ? 155  VAL L CG1   1 
ATOM   7285  C  CG2   . VAL C 2 155 ? 135.071 109.821 145.740 1.00 73.79  ? 155  VAL L CG2   1 
ATOM   7286  N  N     . HIS C 2 156 ? 139.063 111.945 144.530 1.00 80.56  ? 156  HIS L N     1 
ATOM   7287  C  CA    . HIS C 2 156 ? 140.363 112.558 144.748 1.00 78.01  ? 156  HIS L CA    1 
ATOM   7288  C  C     . HIS C 2 156 ? 140.265 113.575 145.880 1.00 77.27  ? 156  HIS L C     1 
ATOM   7289  O  O     . HIS C 2 156 ? 139.238 113.698 146.554 1.00 79.70  ? 156  HIS L O     1 
ATOM   7290  C  CB    . HIS C 2 156 ? 140.876 113.208 143.461 1.00 80.98  ? 156  HIS L CB    1 
ATOM   7291  C  CG    . HIS C 2 156 ? 141.243 112.226 142.392 1.00 83.72  ? 156  HIS L CG    1 
ATOM   7292  N  ND1   . HIS C 2 156 ? 140.349 111.309 141.883 1.00 85.14  ? 156  HIS L ND1   1 
ATOM   7293  C  CD2   . HIS C 2 156 ? 142.409 112.017 141.735 1.00 83.46  ? 156  HIS L CD2   1 
ATOM   7294  C  CE1   . HIS C 2 156 ? 140.947 110.578 140.960 1.00 84.70  ? 156  HIS L CE1   1 
ATOM   7295  N  NE2   . HIS C 2 156 ? 142.198 110.988 140.850 1.00 84.08  ? 156  HIS L NE2   1 
ATOM   7296  N  N     . GLU C 2 157 ? 141.352 114.311 146.086 1.00 81.32  ? 157  GLU L N     1 
ATOM   7297  C  CA    . GLU C 2 157 ? 141.441 115.310 147.140 1.00 84.47  ? 157  GLU L CA    1 
ATOM   7298  C  C     . GLU C 2 157 ? 141.678 116.678 146.517 1.00 86.72  ? 157  GLU L C     1 
ATOM   7299  O  O     . GLU C 2 157 ? 142.593 116.844 145.704 1.00 85.95  ? 157  GLU L O     1 
ATOM   7300  C  CB    . GLU C 2 157 ? 142.562 114.961 148.125 1.00 85.58  ? 157  GLU L CB    1 
ATOM   7301  C  CG    . GLU C 2 157 ? 143.132 116.140 148.896 1.00 85.17  ? 157  GLU L CG    1 
ATOM   7302  C  CD    . GLU C 2 157 ? 142.176 116.688 149.939 1.00 84.48  ? 157  GLU L CD    1 
ATOM   7303  O  OE1   . GLU C 2 157 ? 141.174 116.011 150.253 1.00 84.62  ? 157  GLU L OE1   1 
ATOM   7304  O  OE2   . GLU C 2 157 ? 142.437 117.794 150.454 1.00 84.14  ? 157  GLU L OE2   1 
ATOM   7305  N  N     . ASP C 2 158 ? 140.853 117.649 146.897 1.00 101.35 ? 158  ASP L N     1 
ATOM   7306  C  CA    . ASP C 2 158 ? 140.962 119.007 146.382 1.00 102.54 ? 158  ASP L CA    1 
ATOM   7307  C  C     . ASP C 2 158 ? 142.023 119.764 147.181 1.00 103.07 ? 158  ASP L C     1 
ATOM   7308  O  O     . ASP C 2 158 ? 142.806 119.176 147.932 1.00 103.38 ? 158  ASP L O     1 
ATOM   7309  C  CB    . ASP C 2 158 ? 139.600 119.696 146.425 1.00 101.24 ? 158  ASP L CB    1 
ATOM   7310  C  CG    . ASP C 2 158 ? 139.471 120.802 145.396 1.00 102.98 ? 158  ASP L CG    1 
ATOM   7311  O  OD1   . ASP C 2 158 ? 139.396 120.488 144.189 1.00 101.73 ? 158  ASP L OD1   1 
ATOM   7312  O  OD2   . ASP C 2 158 ? 139.444 121.986 145.794 1.00 103.63 ? 158  ASP L OD2   1 
ATOM   7313  N  N     . LYS C 2 159 ? 142.073 121.087 147.014 1.00 107.85 ? 159  LYS L N     1 
ATOM   7314  C  CA    . LYS C 2 159 ? 143.008 121.898 147.788 1.00 108.54 ? 159  LYS L CA    1 
ATOM   7315  C  C     . LYS C 2 159 ? 142.710 121.795 149.279 1.00 107.06 ? 159  LYS L C     1 
ATOM   7316  O  O     . LYS C 2 159 ? 143.607 121.542 150.092 1.00 106.12 ? 159  LYS L O     1 
ATOM   7317  C  CB    . LYS C 2 159 ? 142.952 123.354 147.320 1.00 106.62 ? 159  LYS L CB    1 
ATOM   7318  C  CG    . LYS C 2 159 ? 143.966 123.710 146.241 1.00 107.48 ? 159  LYS L CG    1 
ATOM   7319  C  CD    . LYS C 2 159 ? 143.676 122.991 144.933 1.00 108.25 ? 159  LYS L CD    1 
ATOM   7320  C  CE    . LYS C 2 159 ? 142.311 123.375 144.384 1.00 109.53 ? 159  LYS L CE    1 
ATOM   7321  N  NZ    . LYS C 2 159 ? 142.006 122.670 143.108 1.00 107.05 ? 159  LYS L NZ    1 
ATOM   7322  N  N     . ASN C 2 160 ? 141.451 121.984 149.656 1.00 105.78 ? 160  ASN L N     1 
ATOM   7323  C  CA    . ASN C 2 160 ? 141.039 121.790 151.036 1.00 106.26 ? 160  ASN L CA    1 
ATOM   7324  C  C     . ASN C 2 160 ? 140.659 120.334 151.265 1.00 107.16 ? 160  ASN L C     1 
ATOM   7325  O  O     . ASN C 2 160 ? 140.351 119.596 150.325 1.00 106.86 ? 160  ASN L O     1 
ATOM   7326  C  CB    . ASN C 2 160 ? 139.862 122.703 151.383 1.00 106.80 ? 160  ASN L CB    1 
ATOM   7327  C  CG    . ASN C 2 160 ? 140.208 124.173 151.253 1.00 108.66 ? 160  ASN L CG    1 
ATOM   7328  O  OD1   . ASN C 2 160 ? 141.361 124.569 151.426 1.00 108.58 ? 160  ASN L OD1   1 
ATOM   7329  N  ND2   . ASN C 2 160 ? 139.209 124.992 150.948 1.00 108.16 ? 160  ASN L ND2   1 
ATOM   7330  N  N     . ARG C 2 161 ? 140.671 119.924 152.533 1.00 107.36 ? 161  ARG L N     1 
ATOM   7331  C  CA    . ARG C 2 161 ? 140.374 118.535 152.860 1.00 106.54 ? 161  ARG L CA    1 
ATOM   7332  C  C     . ARG C 2 161 ? 138.884 118.269 152.698 1.00 106.35 ? 161  ARG L C     1 
ATOM   7333  O  O     . ARG C 2 161 ? 138.136 118.225 153.680 1.00 107.76 ? 161  ARG L O     1 
ATOM   7334  C  CB    . ARG C 2 161 ? 140.838 118.198 154.279 1.00 106.05 ? 161  ARG L CB    1 
ATOM   7335  C  CG    . ARG C 2 161 ? 140.724 119.344 155.271 1.00 105.04 ? 161  ARG L CG    1 
ATOM   7336  C  CD    . ARG C 2 161 ? 140.801 118.832 156.700 1.00 106.03 ? 161  ARG L CD    1 
ATOM   7337  N  NE    . ARG C 2 161 ? 139.547 118.229 157.137 1.00 105.86 ? 161  ARG L NE    1 
ATOM   7338  C  CZ    . ARG C 2 161 ? 139.460 117.223 157.996 1.00 105.26 ? 161  ARG L CZ    1 
ATOM   7339  N  NH1   . ARG C 2 161 ? 140.539 116.678 158.534 1.00 103.69 ? 161  ARG L NH1   1 
ATOM   7340  N  NH2   . ARG C 2 161 ? 138.261 116.751 158.324 1.00 105.37 ? 161  ARG L NH2   1 
ATOM   7341  N  N     . VAL C 2 162 ? 138.452 118.089 151.454 1.00 92.06  ? 162  VAL L N     1 
ATOM   7342  C  CA    . VAL C 2 162 ? 137.053 117.837 151.124 1.00 89.13  ? 162  VAL L CA    1 
ATOM   7343  C  C     . VAL C 2 162 ? 137.002 116.886 149.931 1.00 90.79  ? 162  VAL L C     1 
ATOM   7344  O  O     . VAL C 2 162 ? 137.212 117.305 148.783 1.00 91.87  ? 162  VAL L O     1 
ATOM   7345  C  CB    . VAL C 2 162 ? 136.297 119.152 150.863 1.00 89.32  ? 162  VAL L CB    1 
ATOM   7346  C  CG1   . VAL C 2 162 ? 137.097 120.075 149.949 1.00 89.72  ? 162  VAL L CG1   1 
ATOM   7347  C  CG2   . VAL C 2 162 ? 134.922 118.872 150.273 1.00 90.07  ? 162  VAL L CG2   1 
ATOM   7348  N  N     . PRO C 2 163 ? 136.778 115.595 150.161 1.00 83.69  ? 163  PRO L N     1 
ATOM   7349  C  CA    . PRO C 2 163 ? 136.680 114.654 149.042 1.00 82.72  ? 163  PRO L CA    1 
ATOM   7350  C  C     . PRO C 2 163 ? 135.541 115.017 148.100 1.00 83.16  ? 163  PRO L C     1 
ATOM   7351  O  O     . PRO C 2 163 ? 134.471 115.458 148.526 1.00 83.56  ? 163  PRO L O     1 
ATOM   7352  C  CB    . PRO C 2 163 ? 136.435 113.311 149.736 1.00 85.37  ? 163  PRO L CB    1 
ATOM   7353  C  CG    . PRO C 2 163 ? 137.067 113.469 151.074 1.00 85.99  ? 163  PRO L CG    1 
ATOM   7354  C  CD    . PRO C 2 163 ? 136.850 114.905 151.459 1.00 84.45  ? 163  PRO L CD    1 
ATOM   7355  N  N     . TYR C 2 164 ? 135.785 114.826 146.806 1.00 77.44  ? 164  TYR L N     1 
ATOM   7356  C  CA    . TYR C 2 164 ? 134.815 115.155 145.773 1.00 73.42  ? 164  TYR L CA    1 
ATOM   7357  C  C     . TYR C 2 164 ? 135.039 114.241 144.579 1.00 69.09  ? 164  TYR L C     1 
ATOM   7358  O  O     . TYR C 2 164 ? 136.150 113.754 144.353 1.00 74.05  ? 164  TYR L O     1 
ATOM   7359  C  CB    . TYR C 2 164 ? 134.930 116.619 145.340 1.00 74.86  ? 164  TYR L CB    1 
ATOM   7360  C  CG    . TYR C 2 164 ? 136.082 116.876 144.398 1.00 74.72  ? 164  TYR L CG    1 
ATOM   7361  C  CD1   . TYR C 2 164 ? 137.394 116.843 144.849 1.00 78.42  ? 164  TYR L CD1   1 
ATOM   7362  C  CD2   . TYR C 2 164 ? 135.858 117.150 143.056 1.00 75.02  ? 164  TYR L CD2   1 
ATOM   7363  C  CE1   . TYR C 2 164 ? 138.452 117.075 143.990 1.00 78.86  ? 164  TYR L CE1   1 
ATOM   7364  C  CE2   . TYR C 2 164 ? 136.908 117.384 142.189 1.00 77.52  ? 164  TYR L CE2   1 
ATOM   7365  C  CZ    . TYR C 2 164 ? 138.202 117.345 142.661 1.00 76.90  ? 164  TYR L CZ    1 
ATOM   7366  O  OH    . TYR C 2 164 ? 139.250 117.578 141.802 1.00 75.29  ? 164  TYR L OH    1 
ATOM   7367  N  N     . VAL C 2 165 ? 133.974 114.019 143.809 1.00 56.85  ? 165  VAL L N     1 
ATOM   7368  C  CA    . VAL C 2 165 ? 134.062 113.127 142.662 1.00 58.58  ? 165  VAL L CA    1 
ATOM   7369  C  C     . VAL C 2 165 ? 134.840 113.806 141.544 1.00 63.80  ? 165  VAL L C     1 
ATOM   7370  O  O     . VAL C 2 165 ? 134.630 114.988 141.237 1.00 66.02  ? 165  VAL L O     1 
ATOM   7371  C  CB    . VAL C 2 165 ? 132.659 112.695 142.202 1.00 58.55  ? 165  VAL L CB    1 
ATOM   7372  C  CG1   . VAL C 2 165 ? 131.807 113.903 141.833 1.00 60.29  ? 165  VAL L CG1   1 
ATOM   7373  C  CG2   . VAL C 2 165 ? 132.758 111.725 141.041 1.00 56.45  ? 165  VAL L CG2   1 
ATOM   7374  N  N     . LYS C 2 166 ? 135.764 113.063 140.940 1.00 76.18  ? 166  LYS L N     1 
ATOM   7375  C  CA    . LYS C 2 166 ? 136.647 113.580 139.903 1.00 73.65  ? 166  LYS L CA    1 
ATOM   7376  C  C     . LYS C 2 166 ? 136.336 112.895 138.580 1.00 70.23  ? 166  LYS L C     1 
ATOM   7377  O  O     . LYS C 2 166 ? 136.338 111.663 138.499 1.00 73.08  ? 166  LYS L O     1 
ATOM   7378  C  CB    . LYS C 2 166 ? 138.114 113.364 140.279 1.00 71.59  ? 166  LYS L CB    1 
ATOM   7379  C  CG    . LYS C 2 166 ? 139.094 113.749 139.191 1.00 72.93  ? 166  LYS L CG    1 
ATOM   7380  C  CD    . LYS C 2 166 ? 139.015 115.232 138.877 1.00 74.49  ? 166  LYS L CD    1 
ATOM   7381  C  CE    . LYS C 2 166 ? 139.928 115.593 137.719 1.00 75.95  ? 166  LYS L CE    1 
ATOM   7382  N  NZ    . LYS C 2 166 ? 141.346 115.236 138.002 1.00 75.53  ? 166  LYS L NZ    1 
ATOM   7383  N  N     . GLY C 2 167 ? 136.079 113.696 137.549 1.00 61.63  ? 167  GLY L N     1 
ATOM   7384  C  CA    . GLY C 2 167 ? 135.803 113.192 136.222 1.00 65.63  ? 167  GLY L CA    1 
ATOM   7385  C  C     . GLY C 2 167 ? 134.349 113.232 135.803 1.00 69.57  ? 167  GLY L C     1 
ATOM   7386  O  O     . GLY C 2 167 ? 134.065 113.066 134.610 1.00 70.45  ? 167  GLY L O     1 
ATOM   7387  N  N     . CYS C 2 168 ? 133.423 113.445 136.734 1.00 67.03  ? 168  CYS L N     1 
ATOM   7388  C  CA    . CYS C 2 168 ? 132.012 113.503 136.377 1.00 63.45  ? 168  CYS L CA    1 
ATOM   7389  C  C     . CYS C 2 168 ? 131.723 114.743 135.543 1.00 59.98  ? 168  CYS L C     1 
ATOM   7390  O  O     . CYS C 2 168 ? 132.314 115.806 135.754 1.00 61.69  ? 168  CYS L O     1 
ATOM   7391  C  CB    . CYS C 2 168 ? 131.140 113.498 137.631 1.00 63.16  ? 168  CYS L CB    1 
ATOM   7392  S  SG    . CYS C 2 168 ? 130.630 111.851 138.174 1.00 73.20  ? 168  CYS L SG    1 
ATOM   7393  N  N     . THR C 2 169 ? 130.811 114.601 134.586 1.00 51.03  ? 169  THR L N     1 
ATOM   7394  C  CA    . THR C 2 169 ? 130.455 115.723 133.730 1.00 52.79  ? 169  THR L CA    1 
ATOM   7395  C  C     . THR C 2 169 ? 129.640 116.751 134.507 1.00 49.68  ? 169  THR L C     1 
ATOM   7396  O  O     . THR C 2 169 ? 128.733 116.408 135.271 1.00 48.47  ? 169  THR L O     1 
ATOM   7397  C  CB    . THR C 2 169 ? 129.683 115.237 132.499 1.00 53.17  ? 169  THR L CB    1 
ATOM   7398  O  OG1   . THR C 2 169 ? 129.362 116.353 131.659 1.00 52.75  ? 169  THR L OG1   1 
ATOM   7399  C  CG2   . THR C 2 169 ? 128.406 114.505 132.896 1.00 53.32  ? 169  THR L CG2   1 
ATOM   7400  N  N     . GLU C 2 170 ? 129.988 118.020 134.326 1.00 38.74  ? 170  GLU L N     1 
ATOM   7401  C  CA    . GLU C 2 170 ? 129.340 119.132 135.015 1.00 35.85  ? 170  GLU L CA    1 
ATOM   7402  C  C     . GLU C 2 170 ? 128.749 120.051 133.952 1.00 34.26  ? 170  GLU L C     1 
ATOM   7403  O  O     . GLU C 2 170 ? 129.471 120.829 133.322 1.00 35.99  ? 170  GLU L O     1 
ATOM   7404  C  CB    . GLU C 2 170 ? 130.330 119.867 135.912 1.00 37.73  ? 170  GLU L CB    1 
ATOM   7405  C  CG    . GLU C 2 170 ? 131.119 118.950 136.831 1.00 42.36  ? 170  GLU L CG    1 
ATOM   7406  C  CD    . GLU C 2 170 ? 132.047 119.707 137.761 1.00 47.39  ? 170  GLU L CD    1 
ATOM   7407  O  OE1   . GLU C 2 170 ? 131.826 120.918 137.968 1.00 45.58  ? 170  GLU L OE1   1 
ATOM   7408  O  OE2   . GLU C 2 170 ? 132.998 119.090 138.285 1.00 47.68  ? 170  GLU L OE2   1 
ATOM   7409  N  N     . ARG C 2 171 ? 127.437 119.961 133.758 1.00 30.58  ? 171  ARG L N     1 
ATOM   7410  C  CA    . ARG C 2 171 ? 126.758 120.687 132.694 1.00 33.53  ? 171  ARG L CA    1 
ATOM   7411  C  C     . ARG C 2 171 ? 126.287 122.040 133.209 1.00 27.29  ? 171  ARG L C     1 
ATOM   7412  O  O     . ARG C 2 171 ? 125.541 122.110 134.191 1.00 37.27  ? 171  ARG L O     1 
ATOM   7413  C  CB    . ARG C 2 171 ? 125.571 119.883 132.165 1.00 40.91  ? 171  ARG L CB    1 
ATOM   7414  C  CG    . ARG C 2 171 ? 125.949 118.697 131.297 1.00 46.87  ? 171  ARG L CG    1 
ATOM   7415  C  CD    . ARG C 2 171 ? 124.709 117.931 130.872 1.00 50.49  ? 171  ARG L CD    1 
ATOM   7416  N  NE    . ARG C 2 171 ? 123.619 118.828 130.509 1.00 50.68  ? 171  ARG L NE    1 
ATOM   7417  C  CZ    . ARG C 2 171 ? 122.408 118.429 130.144 1.00 47.46  ? 171  ARG L CZ    1 
ATOM   7418  N  NH1   . ARG C 2 171 ? 122.094 117.145 130.081 1.00 47.05  ? 171  ARG L NH1   1 
ATOM   7419  N  NH2   . ARG C 2 171 ? 121.490 119.340 129.835 1.00 42.53  ? 171  ARG L NH2   1 
ATOM   7420  N  N     . PHE C 2 172 ? 126.719 123.106 132.547 1.00 16.58  ? 172  PHE L N     1 
ATOM   7421  C  CA    . PHE C 2 172 ? 126.208 124.430 132.860 1.00 19.10  ? 172  PHE L CA    1 
ATOM   7422  C  C     . PHE C 2 172 ? 124.739 124.524 132.476 1.00 25.41  ? 172  PHE L C     1 
ATOM   7423  O  O     . PHE C 2 172 ? 124.308 123.966 131.464 1.00 38.55  ? 172  PHE L O     1 
ATOM   7424  C  CB    . PHE C 2 172 ? 127.014 125.500 132.128 1.00 27.59  ? 172  PHE L CB    1 
ATOM   7425  C  CG    . PHE C 2 172 ? 128.426 125.629 132.612 1.00 24.85  ? 172  PHE L CG    1 
ATOM   7426  C  CD1   . PHE C 2 172 ? 129.418 124.795 132.128 1.00 33.26  ? 172  PHE L CD1   1 
ATOM   7427  C  CD2   . PHE C 2 172 ? 128.762 126.585 133.550 1.00 17.59  ? 172  PHE L CD2   1 
ATOM   7428  C  CE1   . PHE C 2 172 ? 130.719 124.912 132.575 1.00 30.95  ? 172  PHE L CE1   1 
ATOM   7429  C  CE2   . PHE C 2 172 ? 130.061 126.706 133.999 1.00 23.26  ? 172  PHE L CE2   1 
ATOM   7430  C  CZ    . PHE C 2 172 ? 131.040 125.868 133.510 1.00 25.54  ? 172  PHE L CZ    1 
ATOM   7431  N  N     . VAL C 2 173 ? 123.967 125.229 133.295 1.00 25.14  ? 173  VAL L N     1 
ATOM   7432  C  CA    . VAL C 2 173 ? 122.548 125.431 133.047 1.00 33.76  ? 173  VAL L CA    1 
ATOM   7433  C  C     . VAL C 2 173 ? 122.242 126.917 133.145 1.00 34.63  ? 173  VAL L C     1 
ATOM   7434  O  O     . VAL C 2 173 ? 122.849 127.647 133.935 1.00 33.32  ? 173  VAL L O     1 
ATOM   7435  C  CB    . VAL C 2 173 ? 121.673 124.616 134.021 1.00 35.34  ? 173  VAL L CB    1 
ATOM   7436  C  CG1   . VAL C 2 173 ? 121.678 123.150 133.626 1.00 31.89  ? 173  VAL L CG1   1 
ATOM   7437  C  CG2   . VAL C 2 173 ? 122.177 124.774 135.438 1.00 35.49  ? 173  VAL L CG2   1 
ATOM   7438  N  N     . CYS C 2 174 ? 121.294 127.367 132.323 1.00 48.83  ? 174  CYS L N     1 
ATOM   7439  C  CA    . CYS C 2 174 ? 120.995 128.789 132.214 1.00 48.73  ? 174  CYS L CA    1 
ATOM   7440  C  C     . CYS C 2 174 ? 119.527 129.083 132.491 1.00 51.13  ? 174  CYS L C     1 
ATOM   7441  O  O     . CYS C 2 174 ? 119.182 130.180 132.941 1.00 51.34  ? 174  CYS L O     1 
ATOM   7442  C  CB    . CYS C 2 174 ? 121.377 129.302 130.825 1.00 52.09  ? 174  CYS L CB    1 
ATOM   7443  S  SG    . CYS C 2 174 ? 123.120 129.089 130.402 1.00 65.21  ? 174  CYS L SG    1 
ATOM   7444  N  N     . SER C 2 175 ? 118.658 128.114 132.230 1.00 54.62  ? 175  SER L N     1 
ATOM   7445  C  CA    . SER C 2 175 ? 117.224 128.294 132.367 1.00 54.11  ? 175  SER L CA    1 
ATOM   7446  C  C     . SER C 2 175 ? 116.643 127.171 133.209 1.00 49.16  ? 175  SER L C     1 
ATOM   7447  O  O     . SER C 2 175 ? 117.194 126.066 133.240 1.00 52.80  ? 175  SER L O     1 
ATOM   7448  C  CB    . SER C 2 175 ? 116.544 128.316 130.988 1.00 58.34  ? 175  SER L CB    1 
ATOM   7449  O  OG    . SER C 2 175 ? 115.135 128.408 131.098 1.00 60.33  ? 175  SER L OG    1 
ATOM   7450  N  N     . PRO C 2 176 ? 115.538 127.427 133.914 1.00 51.52  ? 176  PRO L N     1 
ATOM   7451  C  CA    . PRO C 2 176 ? 114.893 126.341 134.670 1.00 53.15  ? 176  PRO L CA    1 
ATOM   7452  C  C     . PRO C 2 176 ? 114.488 125.165 133.803 1.00 53.87  ? 176  PRO L C     1 
ATOM   7453  O  O     . PRO C 2 176 ? 114.485 124.027 134.286 1.00 59.69  ? 176  PRO L O     1 
ATOM   7454  C  CB    . PRO C 2 176 ? 113.674 127.027 135.307 1.00 55.42  ? 176  PRO L CB    1 
ATOM   7455  C  CG    . PRO C 2 176 ? 113.525 128.337 134.584 1.00 61.02  ? 176  PRO L CG    1 
ATOM   7456  C  CD    . PRO C 2 176 ? 114.907 128.727 134.182 1.00 59.51  ? 176  PRO L CD    1 
ATOM   7457  N  N     . ASP C 2 177 ? 114.150 125.403 132.534 1.00 60.62  ? 177  ASP L N     1 
ATOM   7458  C  CA    . ASP C 2 177 ? 113.832 124.298 131.635 1.00 69.02  ? 177  ASP L CA    1 
ATOM   7459  C  C     . ASP C 2 177 ? 115.036 123.384 131.435 1.00 70.82  ? 177  ASP L C     1 
ATOM   7460  O  O     . ASP C 2 177 ? 114.887 122.158 131.354 1.00 71.22  ? 177  ASP L O     1 
ATOM   7461  C  CB    . ASP C 2 177 ? 113.337 124.839 130.295 1.00 66.41  ? 177  ASP L CB    1 
ATOM   7462  C  CG    . ASP C 2 177 ? 112.115 125.722 130.441 1.00 68.26  ? 177  ASP L CG    1 
ATOM   7463  O  OD1   . ASP C 2 177 ? 111.698 125.973 131.591 1.00 67.40  ? 177  ASP L OD1   1 
ATOM   7464  O  OD2   . ASP C 2 177 ? 111.571 126.164 129.407 1.00 67.65  ? 177  ASP L OD2   1 
ATOM   7465  N  N     . GLU C 2 178 ? 116.237 123.962 131.343 1.00 63.75  ? 178  GLU L N     1 
ATOM   7466  C  CA    . GLU C 2 178 ? 117.439 123.147 131.197 1.00 58.91  ? 178  GLU L CA    1 
ATOM   7467  C  C     . GLU C 2 178 ? 117.652 122.253 132.411 1.00 55.09  ? 178  GLU L C     1 
ATOM   7468  O  O     . GLU C 2 178 ? 117.955 121.060 132.271 1.00 58.33  ? 178  GLU L O     1 
ATOM   7469  C  CB    . GLU C 2 178 ? 118.656 124.041 130.967 1.00 57.56  ? 178  GLU L CB    1 
ATOM   7470  C  CG    . GLU C 2 178 ? 118.648 124.760 129.633 1.00 58.90  ? 178  GLU L CG    1 
ATOM   7471  C  CD    . GLU C 2 178 ? 119.923 125.536 129.383 1.00 61.09  ? 178  GLU L CD    1 
ATOM   7472  O  OE1   . GLU C 2 178 ? 120.814 125.514 130.256 1.00 57.46  ? 178  GLU L OE1   1 
ATOM   7473  O  OE2   . GLU C 2 178 ? 120.036 126.168 128.312 1.00 62.87  ? 178  GLU L OE2   1 
ATOM   7474  N  N     . VAL C 2 179 ? 117.490 122.809 133.613 1.00 41.82  ? 179  VAL L N     1 
ATOM   7475  C  CA    . VAL C 2 179 ? 117.638 122.005 134.821 1.00 44.86  ? 179  VAL L CA    1 
ATOM   7476  C  C     . VAL C 2 179 ? 116.569 120.924 134.870 1.00 46.35  ? 179  VAL L C     1 
ATOM   7477  O  O     . VAL C 2 179 ? 116.838 119.780 135.258 1.00 53.83  ? 179  VAL L O     1 
ATOM   7478  C  CB    . VAL C 2 179 ? 117.598 122.901 136.072 1.00 49.88  ? 179  VAL L CB    1 
ATOM   7479  C  CG1   . VAL C 2 179 ? 117.897 122.083 137.314 1.00 50.10  ? 179  VAL L CG1   1 
ATOM   7480  C  CG2   . VAL C 2 179 ? 118.588 124.040 135.938 1.00 48.33  ? 179  VAL L CG2   1 
ATOM   7481  N  N     . MET C 2 180 ? 115.341 121.263 134.475 1.00 45.42  ? 180  MET L N     1 
ATOM   7482  C  CA    . MET C 2 180 ? 114.271 120.273 134.495 1.00 48.57  ? 180  MET L CA    1 
ATOM   7483  C  C     . MET C 2 180 ? 114.564 119.121 133.545 1.00 52.30  ? 180  MET L C     1 
ATOM   7484  O  O     . MET C 2 180 ? 114.385 117.951 133.905 1.00 58.43  ? 180  MET L O     1 
ATOM   7485  C  CB    . MET C 2 180 ? 112.935 120.930 134.150 1.00 47.64  ? 180  MET L CB    1 
ATOM   7486  C  CG    . MET C 2 180 ? 112.411 121.862 135.227 1.00 51.54  ? 180  MET L CG    1 
ATOM   7487  S  SD    . MET C 2 180 ? 112.598 121.176 136.882 1.00 49.60  ? 180  MET L SD    1 
ATOM   7488  C  CE    . MET C 2 180 ? 111.572 119.714 136.754 1.00 48.24  ? 180  MET L CE    1 
ATOM   7489  N  N     . ASP C 2 181 ? 115.035 119.424 132.333 1.00 50.93  ? 181  ASP L N     1 
ATOM   7490  C  CA    . ASP C 2 181 ? 115.304 118.343 131.392 1.00 53.85  ? 181  ASP L CA    1 
ATOM   7491  C  C     . ASP C 2 181 ? 116.515 117.520 131.811 1.00 54.99  ? 181  ASP L C     1 
ATOM   7492  O  O     . ASP C 2 181 ? 116.524 116.302 131.609 1.00 55.02  ? 181  ASP L O     1 
ATOM   7493  C  CB    . ASP C 2 181 ? 115.462 118.876 129.963 1.00 58.49  ? 181  ASP L CB    1 
ATOM   7494  C  CG    . ASP C 2 181 ? 116.666 119.785 129.786 1.00 60.61  ? 181  ASP L CG    1 
ATOM   7495  O  OD1   . ASP C 2 181 ? 117.805 119.367 130.082 1.00 55.96  ? 181  ASP L OD1   1 
ATOM   7496  O  OD2   . ASP C 2 181 ? 116.467 120.918 129.304 1.00 63.20  ? 181  ASP L OD2   1 
ATOM   7497  N  N     . THR C 2 182 ? 117.537 118.145 132.408 1.00 50.69  ? 182  THR L N     1 
ATOM   7498  C  CA    . THR C 2 182 ? 118.677 117.349 132.855 1.00 51.13  ? 182  THR L CA    1 
ATOM   7499  C  C     . THR C 2 182 ? 118.296 116.457 134.035 1.00 47.93  ? 182  THR L C     1 
ATOM   7500  O  O     . THR C 2 182 ? 118.755 115.312 134.123 1.00 50.36  ? 182  THR L O     1 
ATOM   7501  C  CB    . THR C 2 182 ? 119.876 118.247 133.188 1.00 49.35  ? 182  THR L CB    1 
ATOM   7502  O  OG1   . THR C 2 182 ? 121.069 117.452 133.224 1.00 47.15  ? 182  THR L OG1   1 
ATOM   7503  C  CG2   . THR C 2 182 ? 119.715 118.949 134.525 1.00 49.98  ? 182  THR L CG2   1 
ATOM   7504  N  N     . ILE C 2 183 ? 117.425 116.939 134.925 1.00 46.97  ? 183  ILE L N     1 
ATOM   7505  C  CA    . ILE C 2 183 ? 116.940 116.097 136.014 1.00 44.73  ? 183  ILE L CA    1 
ATOM   7506  C  C     . ILE C 2 183 ? 116.109 114.943 135.465 1.00 51.10  ? 183  ILE L C     1 
ATOM   7507  O  O     . ILE C 2 183 ? 116.224 113.799 135.928 1.00 59.04  ? 183  ILE L O     1 
ATOM   7508  C  CB    . ILE C 2 183 ? 116.144 116.943 137.026 1.00 41.82  ? 183  ILE L CB    1 
ATOM   7509  C  CG1   . ILE C 2 183 ? 117.079 117.882 137.786 1.00 44.98  ? 183  ILE L CG1   1 
ATOM   7510  C  CG2   . ILE C 2 183 ? 115.392 116.054 137.998 1.00 44.89  ? 183  ILE L CG2   1 
ATOM   7511  C  CD1   . ILE C 2 183 ? 116.356 118.962 138.553 1.00 50.05  ? 183  ILE L CD1   1 
ATOM   7512  N  N     . ASP C 2 184 ? 115.258 115.223 134.474 1.00 49.20  ? 184  ASP L N     1 
ATOM   7513  C  CA    . ASP C 2 184 ? 114.451 114.167 133.874 1.00 50.49  ? 184  ASP L CA    1 
ATOM   7514  C  C     . ASP C 2 184 ? 115.328 113.116 133.204 1.00 53.20  ? 184  ASP L C     1 
ATOM   7515  O  O     . ASP C 2 184 ? 115.082 111.912 133.343 1.00 55.76  ? 184  ASP L O     1 
ATOM   7516  C  CB    . ASP C 2 184 ? 113.465 114.766 132.873 1.00 52.17  ? 184  ASP L CB    1 
ATOM   7517  C  CG    . ASP C 2 184 ? 112.364 113.798 132.491 1.00 54.50  ? 184  ASP L CG    1 
ATOM   7518  O  OD1   . ASP C 2 184 ? 112.243 112.744 133.149 1.00 53.71  ? 184  ASP L OD1   1 
ATOM   7519  O  OD2   . ASP C 2 184 ? 111.618 114.091 131.533 1.00 54.46  ? 184  ASP L OD2   1 
ATOM   7520  N  N     . GLU C 2 185 ? 116.361 113.552 132.479 1.00 54.46  ? 185  GLU L N     1 
ATOM   7521  C  CA    . GLU C 2 185 ? 117.279 112.606 131.851 1.00 62.13  ? 185  GLU L CA    1 
ATOM   7522  C  C     . GLU C 2 185 ? 118.014 111.775 132.894 1.00 58.26  ? 185  GLU L C     1 
ATOM   7523  O  O     . GLU C 2 185 ? 118.174 110.558 132.732 1.00 57.11  ? 185  GLU L O     1 
ATOM   7524  C  CB    . GLU C 2 185 ? 118.274 113.352 130.963 1.00 61.83  ? 185  GLU L CB    1 
ATOM   7525  C  CG    . GLU C 2 185 ? 117.659 113.969 129.719 1.00 61.41  ? 185  GLU L CG    1 
ATOM   7526  C  CD    . GLU C 2 185 ? 118.633 114.855 128.968 1.00 62.11  ? 185  GLU L CD    1 
ATOM   7527  O  OE1   . GLU C 2 185 ? 119.824 114.885 129.345 1.00 65.78  ? 185  GLU L OE1   1 
ATOM   7528  O  OE2   . GLU C 2 185 ? 118.209 115.523 128.001 1.00 62.44  ? 185  GLU L OE2   1 
ATOM   7529  N  N     . GLY C 2 186 ? 118.470 112.414 133.973 1.00 54.65  ? 186  GLY L N     1 
ATOM   7530  C  CA    . GLY C 2 186 ? 119.150 111.675 135.021 1.00 54.20  ? 186  GLY L CA    1 
ATOM   7531  C  C     . GLY C 2 186 ? 118.266 110.621 135.657 1.00 55.48  ? 186  GLY L C     1 
ATOM   7532  O  O     . GLY C 2 186 ? 118.700 109.489 135.885 1.00 60.17  ? 186  GLY L O     1 
ATOM   7533  N  N     . LYS C 2 187 ? 117.012 110.973 135.948 1.00 56.30  ? 187  LYS L N     1 
ATOM   7534  C  CA    . LYS C 2 187 ? 116.108 109.987 136.530 1.00 57.68  ? 187  LYS L CA    1 
ATOM   7535  C  C     . LYS C 2 187 ? 115.760 108.890 135.531 1.00 60.05  ? 187  LYS L C     1 
ATOM   7536  O  O     . LYS C 2 187 ? 115.567 107.734 135.926 1.00 60.74  ? 187  LYS L O     1 
ATOM   7537  C  CB    . LYS C 2 187 ? 114.838 110.658 137.050 1.00 57.55  ? 187  LYS L CB    1 
ATOM   7538  C  CG    . LYS C 2 187 ? 113.937 109.714 137.830 1.00 54.28  ? 187  LYS L CG    1 
ATOM   7539  C  CD    . LYS C 2 187 ? 112.767 110.444 138.460 1.00 55.88  ? 187  LYS L CD    1 
ATOM   7540  C  CE    . LYS C 2 187 ? 111.814 109.471 139.135 1.00 59.03  ? 187  LYS L CE    1 
ATOM   7541  N  NZ    . LYS C 2 187 ? 110.663 110.171 139.770 1.00 64.78  ? 187  LYS L NZ    1 
ATOM   7542  N  N     . SER C 2 188 ? 115.677 109.226 134.240 1.00 67.65  ? 188  SER L N     1 
ATOM   7543  C  CA    . SER C 2 188 ? 115.441 108.203 133.227 1.00 69.21  ? 188  SER L CA    1 
ATOM   7544  C  C     . SER C 2 188 ? 116.600 107.219 133.148 1.00 66.81  ? 188  SER L C     1 
ATOM   7545  O  O     . SER C 2 188 ? 116.380 106.021 132.939 1.00 66.42  ? 188  SER L O     1 
ATOM   7546  C  CB    . SER C 2 188 ? 115.200 108.852 131.865 1.00 66.67  ? 188  SER L CB    1 
ATOM   7547  O  OG    . SER C 2 188 ? 116.376 109.475 131.381 1.00 65.34  ? 188  SER L OG    1 
ATOM   7548  N  N     . ASN C 2 189 ? 117.831 107.697 133.314 1.00 72.36  ? 189  ASN L N     1 
ATOM   7549  C  CA    . ASN C 2 189 ? 118.997 106.823 133.303 1.00 72.13  ? 189  ASN L CA    1 
ATOM   7550  C  C     . ASN C 2 189 ? 119.091 105.931 134.537 1.00 72.15  ? 189  ASN L C     1 
ATOM   7551  O  O     . ASN C 2 189 ? 120.066 105.182 134.661 1.00 73.66  ? 189  ASN L O     1 
ATOM   7552  C  CB    . ASN C 2 189 ? 120.278 107.650 133.169 1.00 71.83  ? 189  ASN L CB    1 
ATOM   7553  C  CG    . ASN C 2 189 ? 120.738 107.789 131.731 1.00 71.37  ? 189  ASN L CG    1 
ATOM   7554  O  OD1   . ASN C 2 189 ? 120.742 108.885 131.171 1.00 73.74  ? 189  ASN L OD1   1 
ATOM   7555  N  ND2   . ASN C 2 189 ? 121.137 106.677 131.129 1.00 70.12  ? 189  ASN L ND2   1 
ATOM   7556  N  N     . ARG C 2 190 ? 118.118 105.988 135.444 1.00 82.87  ? 190  ARG L N     1 
ATOM   7557  C  CA    . ARG C 2 190 ? 118.091 105.142 136.630 1.00 87.62  ? 190  ARG L CA    1 
ATOM   7558  C  C     . ARG C 2 190 ? 117.045 104.050 136.454 1.00 89.13  ? 190  ARG L C     1 
ATOM   7559  O  O     . ARG C 2 190 ? 115.904 104.332 136.075 1.00 88.53  ? 190  ARG L O     1 
ATOM   7560  C  CB    . ARG C 2 190 ? 117.788 105.958 137.890 1.00 84.51  ? 190  ARG L CB    1 
ATOM   7561  C  CG    . ARG C 2 190 ? 118.917 106.871 138.327 1.00 84.36  ? 190  ARG L CG    1 
ATOM   7562  C  CD    . ARG C 2 190 ? 118.464 107.856 139.396 1.00 85.74  ? 190  ARG L CD    1 
ATOM   7563  N  NE    . ARG C 2 190 ? 118.244 107.219 140.689 1.00 87.96  ? 190  ARG L NE    1 
ATOM   7564  C  CZ    . ARG C 2 190 ? 117.050 106.955 141.203 1.00 87.17  ? 190  ARG L CZ    1 
ATOM   7565  N  NH1   . ARG C 2 190 ? 115.937 107.253 140.554 1.00 85.62  ? 190  ARG L NH1   1 
ATOM   7566  N  NH2   . ARG C 2 190 ? 116.972 106.383 142.401 1.00 84.87  ? 190  ARG L NH2   1 
ATOM   7567  N  N     . HIS C 2 191 ? 117.437 102.810 136.731 1.00 109.18 ? 191  HIS L N     1 
ATOM   7568  C  CA    . HIS C 2 191 ? 116.527 101.676 136.631 1.00 109.54 ? 191  HIS L CA    1 
ATOM   7569  C  C     . HIS C 2 191 ? 115.811 101.431 137.956 1.00 108.46 ? 191  HIS L C     1 
ATOM   7570  O  O     . HIS C 2 191 ? 116.341 100.764 138.844 1.00 109.36 ? 191  HIS L O     1 
ATOM   7571  C  CB    . HIS C 2 191 ? 117.282 100.417 136.201 1.00 110.76 ? 191  HIS L CB    1 
ATOM   7572  C  CG    . HIS C 2 191 ? 116.414 99.202  136.087 1.00 110.23 ? 191  HIS L CG    1 
ATOM   7573  N  ND1   . HIS C 2 191 ? 115.363 99.118  135.199 1.00 110.39 ? 191  HIS L ND1   1 
ATOM   7574  C  CD2   . HIS C 2 191 ? 116.441 98.021  136.749 1.00 108.34 ? 191  HIS L CD2   1 
ATOM   7575  C  CE1   . HIS C 2 191 ? 114.780 97.939  135.319 1.00 110.23 ? 191  HIS L CE1   1 
ATOM   7576  N  NE2   . HIS C 2 191 ? 115.415 97.254  136.253 1.00 108.83 ? 191  HIS L NE2   1 
ATOM   7577  N  N     . SER C 2 202 ? 115.035 100.062 144.608 1.00 147.39 ? 202  SER L N     1 
ATOM   7578  C  CA    . SER C 2 202 ? 116.091 101.045 144.396 1.00 147.26 ? 202  SER L CA    1 
ATOM   7579  C  C     . SER C 2 202 ? 117.121 100.994 145.521 1.00 148.12 ? 202  SER L C     1 
ATOM   7580  O  O     . SER C 2 202 ? 116.936 101.606 146.573 1.00 147.09 ? 202  SER L O     1 
ATOM   7581  C  CB    . SER C 2 202 ? 115.498 102.452 144.282 1.00 145.25 ? 202  SER L CB    1 
ATOM   7582  O  OG    . SER C 2 202 ? 114.709 102.766 145.416 1.00 144.57 ? 202  SER L OG    1 
ATOM   7583  N  N     . ARG C 2 203 ? 118.206 100.257 145.291 1.00 144.95 ? 203  ARG L N     1 
ATOM   7584  C  CA    . ARG C 2 203 ? 119.274 100.099 146.269 1.00 143.00 ? 203  ARG L CA    1 
ATOM   7585  C  C     . ARG C 2 203 ? 120.416 101.086 146.059 1.00 142.61 ? 203  ARG L C     1 
ATOM   7586  O  O     . ARG C 2 203 ? 121.424 101.009 146.768 1.00 141.53 ? 203  ARG L O     1 
ATOM   7587  C  CB    . ARG C 2 203 ? 119.816 98.669  146.232 1.00 142.11 ? 203  ARG L CB    1 
ATOM   7588  C  CG    . ARG C 2 203 ? 118.752 97.583  146.254 1.00 142.00 ? 203  ARG L CG    1 
ATOM   7589  C  CD    . ARG C 2 203 ? 117.922 97.634  147.526 1.00 141.83 ? 203  ARG L CD    1 
ATOM   7590  N  NE    . ARG C 2 203 ? 117.032 96.484  147.637 1.00 143.32 ? 203  ARG L NE    1 
ATOM   7591  C  CZ    . ARG C 2 203 ? 115.813 96.426  147.120 1.00 143.10 ? 203  ARG L CZ    1 
ATOM   7592  N  NH1   . ARG C 2 203 ? 115.300 97.440  146.443 1.00 142.16 ? 203  ARG L NH1   1 
ATOM   7593  N  NH2   . ARG C 2 203 ? 115.090 95.322  147.284 1.00 142.66 ? 203  ARG L NH2   1 
ATOM   7594  N  N     . SER C 2 204 ? 120.284 102.006 145.109 1.00 134.58 ? 204  SER L N     1 
ATOM   7595  C  CA    . SER C 2 204 ? 121.355 102.924 144.754 1.00 133.09 ? 204  SER L CA    1 
ATOM   7596  C  C     . SER C 2 204 ? 121.185 104.262 145.463 1.00 132.20 ? 204  SER L C     1 
ATOM   7597  O  O     . SER C 2 204 ? 120.069 104.688 145.772 1.00 131.69 ? 204  SER L O     1 
ATOM   7598  C  CB    . SER C 2 204 ? 121.403 103.143 143.241 1.00 130.06 ? 204  SER L CB    1 
ATOM   7599  O  OG    . SER C 2 204 ? 122.393 104.096 142.898 1.00 128.76 ? 204  SER L OG    1 
ATOM   7600  N  N     . HIS C 2 205 ? 122.312 104.923 145.716 1.00 125.40 ? 205  HIS L N     1 
ATOM   7601  C  CA    . HIS C 2 205 ? 122.338 106.237 146.344 1.00 124.74 ? 205  HIS L CA    1 
ATOM   7602  C  C     . HIS C 2 205 ? 122.526 107.292 145.262 1.00 123.42 ? 205  HIS L C     1 
ATOM   7603  O  O     . HIS C 2 205 ? 123.541 107.287 144.558 1.00 124.65 ? 205  HIS L O     1 
ATOM   7604  C  CB    . HIS C 2 205 ? 123.461 106.333 147.377 1.00 124.32 ? 205  HIS L CB    1 
ATOM   7605  C  CG    . HIS C 2 205 ? 123.341 105.352 148.500 1.00 124.66 ? 205  HIS L CG    1 
ATOM   7606  N  ND1   . HIS C 2 205 ? 123.042 105.732 149.790 1.00 123.79 ? 205  HIS L ND1   1 
ATOM   7607  C  CD2   . HIS C 2 205 ? 123.491 104.006 148.530 1.00 124.85 ? 205  HIS L CD2   1 
ATOM   7608  C  CE1   . HIS C 2 205 ? 123.007 104.663 150.565 1.00 123.96 ? 205  HIS L CE1   1 
ATOM   7609  N  NE2   . HIS C 2 205 ? 123.276 103.603 149.825 1.00 124.98 ? 205  HIS L NE2   1 
ATOM   7610  N  N     . SER C 2 206 ? 121.560 108.197 145.139 1.00 103.22 ? 206  SER L N     1 
ATOM   7611  C  CA    . SER C 2 206 ? 121.617 109.255 144.140 1.00 100.95 ? 206  SER L CA    1 
ATOM   7612  C  C     . SER C 2 206 ? 122.202 110.514 144.763 1.00 99.93  ? 206  SER L C     1 
ATOM   7613  O  O     . SER C 2 206 ? 121.756 110.952 145.826 1.00 101.83 ? 206  SER L O     1 
ATOM   7614  C  CB    . SER C 2 206 ? 120.226 109.542 143.576 1.00 101.68 ? 206  SER L CB    1 
ATOM   7615  O  OG    . SER C 2 206 ? 119.342 109.970 144.597 1.00 105.57 ? 206  SER L OG    1 
ATOM   7616  N  N     . ILE C 2 207 ? 123.201 111.089 144.101 1.00 88.10  ? 207  ILE L N     1 
ATOM   7617  C  CA    . ILE C 2 207 ? 123.878 112.291 144.573 1.00 88.03  ? 207  ILE L CA    1 
ATOM   7618  C  C     . ILE C 2 207 ? 123.663 113.384 143.537 1.00 92.16  ? 207  ILE L C     1 
ATOM   7619  O  O     . ILE C 2 207 ? 124.100 113.250 142.387 1.00 96.16  ? 207  ILE L O     1 
ATOM   7620  C  CB    . ILE C 2 207 ? 125.377 112.047 144.805 1.00 91.22  ? 207  ILE L CB    1 
ATOM   7621  C  CG1   . ILE C 2 207 ? 125.599 110.729 145.554 1.00 94.74  ? 207  ILE L CG1   1 
ATOM   7622  C  CG2   . ILE C 2 207 ? 126.003 113.214 145.553 1.00 90.47  ? 207  ILE L CG2   1 
ATOM   7623  C  CD1   . ILE C 2 207 ? 125.017 110.706 146.950 1.00 92.08  ? 207  ILE L CD1   1 
ATOM   7624  N  N     . PHE C 2 208 ? 123.000 114.463 143.941 1.00 80.91  ? 208  PHE L N     1 
ATOM   7625  C  CA    . PHE C 2 208 ? 122.736 115.596 143.064 1.00 75.16  ? 208  PHE L CA    1 
ATOM   7626  C  C     . PHE C 2 208 ? 123.408 116.829 143.641 1.00 75.06  ? 208  PHE L C     1 
ATOM   7627  O  O     . PHE C 2 208 ? 123.191 117.172 144.807 1.00 84.06  ? 208  PHE L O     1 
ATOM   7628  C  CB    . PHE C 2 208 ? 121.235 115.835 142.898 1.00 70.05  ? 208  PHE L CB    1 
ATOM   7629  C  CG    . PHE C 2 208 ? 120.902 116.942 141.942 1.00 73.25  ? 208  PHE L CG    1 
ATOM   7630  C  CD1   . PHE C 2 208 ? 121.173 116.812 140.592 1.00 78.74  ? 208  PHE L CD1   1 
ATOM   7631  C  CD2   . PHE C 2 208 ? 120.309 118.109 142.393 1.00 74.64  ? 208  PHE L CD2   1 
ATOM   7632  C  CE1   . PHE C 2 208 ? 120.864 117.829 139.707 1.00 78.04  ? 208  PHE L CE1   1 
ATOM   7633  C  CE2   . PHE C 2 208 ? 119.997 119.128 141.513 1.00 77.23  ? 208  PHE L CE2   1 
ATOM   7634  C  CZ    . PHE C 2 208 ? 120.276 118.988 140.169 1.00 77.76  ? 208  PHE L CZ    1 
ATOM   7635  N  N     . LEU C 2 209 ? 124.219 117.491 142.825 1.00 59.08  ? 209  LEU L N     1 
ATOM   7636  C  CA    . LEU C 2 209 ? 125.038 118.605 143.270 1.00 56.89  ? 209  LEU L CA    1 
ATOM   7637  C  C     . LEU C 2 209 ? 124.893 119.751 142.286 1.00 62.18  ? 209  LEU L C     1 
ATOM   7638  O  O     . LEU C 2 209 ? 125.046 119.554 141.077 1.00 70.65  ? 209  LEU L O     1 
ATOM   7639  C  CB    . LEU C 2 209 ? 126.508 118.181 143.385 1.00 58.62  ? 209  LEU L CB    1 
ATOM   7640  C  CG    . LEU C 2 209 ? 127.567 119.161 143.899 1.00 65.86  ? 209  LEU L CG    1 
ATOM   7641  C  CD1   . LEU C 2 209 ? 128.194 119.967 142.764 1.00 63.19  ? 209  LEU L CD1   1 
ATOM   7642  C  CD2   . LEU C 2 209 ? 126.996 120.077 144.969 1.00 68.51  ? 209  LEU L CD2   1 
ATOM   7643  N  N     . ILE C 2 210 ? 124.598 120.942 142.798 1.00 47.49  ? 210  ILE L N     1 
ATOM   7644  C  CA    . ILE C 2 210 ? 124.690 122.161 142.010 1.00 53.37  ? 210  ILE L CA    1 
ATOM   7645  C  C     . ILE C 2 210 ? 125.724 123.055 142.675 1.00 44.35  ? 210  ILE L C     1 
ATOM   7646  O  O     . ILE C 2 210 ? 125.800 123.129 143.906 1.00 50.06  ? 210  ILE L O     1 
ATOM   7647  C  CB    . ILE C 2 210 ? 123.335 122.886 141.845 1.00 51.68  ? 210  ILE L CB    1 
ATOM   7648  C  CG1   . ILE C 2 210 ? 123.010 123.760 143.047 1.00 48.26  ? 210  ILE L CG1   1 
ATOM   7649  C  CG2   . ILE C 2 210 ? 122.217 121.887 141.621 1.00 53.47  ? 210  ILE L CG2   1 
ATOM   7650  C  CD1   . ILE C 2 210 ? 121.889 124.734 142.796 1.00 54.43  ? 210  ILE L CD1   1 
ATOM   7651  N  N     . ASN C 2 211 ? 126.558 123.688 141.859 1.00 52.76  ? 211  ASN L N     1 
ATOM   7652  C  CA    . ASN C 2 211 ? 127.653 124.519 142.343 1.00 49.62  ? 211  ASN L CA    1 
ATOM   7653  C  C     . ASN C 2 211 ? 127.383 125.942 141.874 1.00 56.22  ? 211  ASN L C     1 
ATOM   7654  O  O     . ASN C 2 211 ? 127.892 126.374 140.838 1.00 64.43  ? 211  ASN L O     1 
ATOM   7655  C  CB    . ASN C 2 211 ? 128.989 123.997 141.836 1.00 53.46  ? 211  ASN L CB    1 
ATOM   7656  C  CG    . ASN C 2 211 ? 130.162 124.551 142.610 1.00 62.01  ? 211  ASN L CG    1 
ATOM   7657  O  OD1   . ASN C 2 211 ? 130.079 125.624 143.206 1.00 68.87  ? 211  ASN L OD1   1 
ATOM   7658  N  ND2   . ASN C 2 211 ? 131.269 123.818 142.607 1.00 62.83  ? 211  ASN L ND2   1 
ATOM   7659  N  N     . VAL C 2 212 ? 126.587 126.674 142.646 1.00 49.27  ? 212  VAL L N     1 
ATOM   7660  C  CA    . VAL C 2 212 ? 126.299 128.067 142.331 1.00 48.37  ? 212  VAL L CA    1 
ATOM   7661  C  C     . VAL C 2 212 ? 127.489 128.915 142.759 1.00 52.91  ? 212  VAL L C     1 
ATOM   7662  O  O     . VAL C 2 212 ? 127.921 128.868 143.915 1.00 64.22  ? 212  VAL L O     1 
ATOM   7663  C  CB    . VAL C 2 212 ? 124.997 128.533 142.999 1.00 48.65  ? 212  VAL L CB    1 
ATOM   7664  C  CG1   . VAL C 2 212 ? 124.998 128.211 144.485 1.00 56.52  ? 212  VAL L CG1   1 
ATOM   7665  C  CG2   . VAL C 2 212 ? 124.795 130.020 142.777 1.00 52.98  ? 212  VAL L CG2   1 
ATOM   7666  N  N     . LYS C 2 213 ? 128.041 129.671 141.818 1.00 68.08  ? 213  LYS L N     1 
ATOM   7667  C  CA    . LYS C 2 213 ? 129.260 130.444 142.031 1.00 68.74  ? 213  LYS L CA    1 
ATOM   7668  C  C     . LYS C 2 213 ? 128.925 131.916 141.826 1.00 73.10  ? 213  LYS L C     1 
ATOM   7669  O  O     . LYS C 2 213 ? 128.880 132.402 140.692 1.00 78.19  ? 213  LYS L O     1 
ATOM   7670  C  CB    . LYS C 2 213 ? 130.362 129.978 141.087 1.00 70.26  ? 213  LYS L CB    1 
ATOM   7671  C  CG    . LYS C 2 213 ? 131.762 130.150 141.635 1.00 71.18  ? 213  LYS L CG    1 
ATOM   7672  C  CD    . LYS C 2 213 ? 132.802 129.666 140.638 1.00 77.85  ? 213  LYS L CD    1 
ATOM   7673  C  CE    . LYS C 2 213 ? 132.464 128.276 140.119 1.00 77.85  ? 213  LYS L CE    1 
ATOM   7674  N  NZ    . LYS C 2 213 ? 132.377 127.276 141.219 1.00 76.41  ? 213  LYS L NZ    1 
ATOM   7675  N  N     . GLN C 2 214 ? 128.695 132.624 142.928 1.00 84.09  ? 214  GLN L N     1 
ATOM   7676  C  CA    . GLN C 2 214 ? 128.291 134.024 142.891 1.00 82.70  ? 214  GLN L CA    1 
ATOM   7677  C  C     . GLN C 2 214 ? 129.539 134.898 142.894 1.00 82.69  ? 214  GLN L C     1 
ATOM   7678  O  O     . GLN C 2 214 ? 130.301 134.901 143.866 1.00 92.44  ? 214  GLN L O     1 
ATOM   7679  C  CB    . GLN C 2 214 ? 127.386 134.350 144.076 1.00 87.42  ? 214  GLN L CB    1 
ATOM   7680  C  CG    . GLN C 2 214 ? 127.166 135.835 144.299 1.00 88.47  ? 214  GLN L CG    1 
ATOM   7681  C  CD    . GLN C 2 214 ? 127.576 136.284 145.687 1.00 89.76  ? 214  GLN L CD    1 
ATOM   7682  O  OE1   . GLN C 2 214 ? 127.624 135.485 146.622 1.00 85.64  ? 214  GLN L OE1   1 
ATOM   7683  N  NE2   . GLN C 2 214 ? 127.873 137.570 145.829 1.00 88.87  ? 214  GLN L NE2   1 
ATOM   7684  N  N     . GLU C 2 215 ? 129.746 135.638 141.810 1.00 99.74  ? 215  GLU L N     1 
ATOM   7685  C  CA    . GLU C 2 215 ? 130.866 136.559 141.682 1.00 103.95 ? 215  GLU L CA    1 
ATOM   7686  C  C     . GLU C 2 215 ? 130.331 137.971 141.503 1.00 109.65 ? 215  GLU L C     1 
ATOM   7687  O  O     . GLU C 2 215 ? 129.496 138.216 140.627 1.00 111.37 ? 215  GLU L O     1 
ATOM   7688  C  CB    . GLU C 2 215 ? 131.763 136.180 140.504 1.00 108.48 ? 215  GLU L CB    1 
ATOM   7689  C  CG    . GLU C 2 215 ? 132.938 137.119 140.298 1.00 108.98 ? 215  GLU L CG    1 
ATOM   7690  C  CD    . GLU C 2 215 ? 133.852 136.670 139.176 1.00 110.80 ? 215  GLU L CD    1 
ATOM   7691  O  OE1   . GLU C 2 215 ? 133.558 135.633 138.546 1.00 109.67 ? 215  GLU L OE1   1 
ATOM   7692  O  OE2   . GLU C 2 215 ? 134.865 137.355 138.922 1.00 111.61 ? 215  GLU L OE2   1 
ATOM   7693  N  N     . ASN C 2 216 ? 130.814 138.894 142.330 1.00 125.64 ? 216  ASN L N     1 
ATOM   7694  C  CA    . ASN C 2 216 ? 130.395 140.288 142.281 1.00 125.72 ? 216  ASN L CA    1 
ATOM   7695  C  C     . ASN C 2 216 ? 131.455 141.108 141.560 1.00 125.64 ? 216  ASN L C     1 
ATOM   7696  O  O     . ASN C 2 216 ? 132.627 141.097 141.949 1.00 124.62 ? 216  ASN L O     1 
ATOM   7697  C  CB    . ASN C 2 216 ? 130.164 140.837 143.688 1.00 125.90 ? 216  ASN L CB    1 
ATOM   7698  C  CG    . ASN C 2 216 ? 129.562 142.228 143.679 1.00 126.40 ? 216  ASN L CG    1 
ATOM   7699  O  OD1   . ASN C 2 216 ? 129.054 142.691 142.659 1.00 126.31 ? 216  ASN L OD1   1 
ATOM   7700  N  ND2   . ASN C 2 216 ? 129.614 142.902 144.822 1.00 125.78 ? 216  ASN L ND2   1 
ATOM   7701  N  N     . THR C 2 217 ? 131.037 141.815 140.509 1.00 134.72 ? 217  THR L N     1 
ATOM   7702  C  CA    . THR C 2 217 ? 131.986 142.589 139.715 1.00 136.18 ? 217  THR L CA    1 
ATOM   7703  C  C     . THR C 2 217 ? 132.522 143.787 140.489 1.00 136.15 ? 217  THR L C     1 
ATOM   7704  O  O     . THR C 2 217 ? 133.715 144.102 140.407 1.00 136.02 ? 217  THR L O     1 
ATOM   7705  C  CB    . THR C 2 217 ? 131.327 143.044 138.412 1.00 134.91 ? 217  THR L CB    1 
ATOM   7706  O  OG1   . THR C 2 217 ? 130.131 143.775 138.710 1.00 134.86 ? 217  THR L OG1   1 
ATOM   7707  C  CG2   . THR C 2 217 ? 130.977 141.843 137.548 1.00 134.00 ? 217  THR L CG2   1 
ATOM   7708  N  N     . GLN C 2 218 ? 131.657 144.471 141.241 1.00 136.85 ? 218  GLN L N     1 
ATOM   7709  C  CA    . GLN C 2 218 ? 132.068 145.701 141.912 1.00 136.32 ? 218  GLN L CA    1 
ATOM   7710  C  C     . GLN C 2 218 ? 133.054 145.421 143.040 1.00 137.45 ? 218  GLN L C     1 
ATOM   7711  O  O     . GLN C 2 218 ? 134.100 146.072 143.138 1.00 138.80 ? 218  GLN L O     1 
ATOM   7712  C  CB    . GLN C 2 218 ? 130.839 146.443 142.439 1.00 135.44 ? 218  GLN L CB    1 
ATOM   7713  C  CG    . GLN C 2 218 ? 130.143 147.313 141.401 1.00 136.68 ? 218  GLN L CG    1 
ATOM   7714  C  CD    . GLN C 2 218 ? 129.524 146.503 140.278 1.00 137.84 ? 218  GLN L CD    1 
ATOM   7715  O  OE1   . GLN C 2 218 ? 129.173 145.337 140.458 1.00 137.32 ? 218  GLN L OE1   1 
ATOM   7716  N  NE2   . GLN C 2 218 ? 129.391 147.118 139.109 1.00 136.97 ? 218  GLN L NE2   1 
ATOM   7717  N  N     . THR C 2 219 ? 132.739 144.458 143.904 1.00 139.59 ? 219  THR L N     1 
ATOM   7718  C  CA    . THR C 2 219 ? 133.587 144.153 145.048 1.00 138.47 ? 219  THR L CA    1 
ATOM   7719  C  C     . THR C 2 219 ? 134.681 143.142 144.734 1.00 139.37 ? 219  THR L C     1 
ATOM   7720  O  O     . THR C 2 219 ? 135.556 142.924 145.580 1.00 137.88 ? 219  THR L O     1 
ATOM   7721  C  CB    . THR C 2 219 ? 132.740 143.631 146.216 1.00 137.10 ? 219  THR L CB    1 
ATOM   7722  O  OG1   . THR C 2 219 ? 132.019 142.463 145.804 1.00 137.61 ? 219  THR L OG1   1 
ATOM   7723  C  CG2   . THR C 2 219 ? 131.756 144.696 146.677 1.00 137.36 ? 219  THR L CG2   1 
ATOM   7724  N  N     . GLU C 2 220 ? 134.657 142.532 143.547 1.00 142.02 ? 220  GLU L N     1 
ATOM   7725  C  CA    . GLU C 2 220 ? 135.636 141.517 143.155 1.00 140.23 ? 220  GLU L CA    1 
ATOM   7726  C  C     . GLU C 2 220 ? 135.709 140.394 144.187 1.00 140.01 ? 220  GLU L C     1 
ATOM   7727  O  O     . GLU C 2 220 ? 136.788 139.926 144.558 1.00 140.00 ? 220  GLU L O     1 
ATOM   7728  C  CB    . GLU C 2 220 ? 137.014 142.140 142.924 1.00 139.39 ? 220  GLU L CB    1 
ATOM   7729  C  CG    . GLU C 2 220 ? 137.079 143.074 141.726 1.00 139.61 ? 220  GLU L CG    1 
ATOM   7730  C  CD    . GLU C 2 220 ? 136.929 142.342 140.405 1.00 141.31 ? 220  GLU L CD    1 
ATOM   7731  O  OE1   . GLU C 2 220 ? 137.253 141.137 140.349 1.00 141.94 ? 220  GLU L OE1   1 
ATOM   7732  O  OE2   . GLU C 2 220 ? 136.485 142.972 139.423 1.00 141.38 ? 220  GLU L OE2   1 
ATOM   7733  N  N     . GLN C 2 221 ? 134.544 139.965 144.663 1.00 125.85 ? 221  GLN L N     1 
ATOM   7734  C  CA    . GLN C 2 221 ? 134.433 138.892 145.640 1.00 122.77 ? 221  GLN L CA    1 
ATOM   7735  C  C     . GLN C 2 221 ? 133.588 137.773 145.053 1.00 122.47 ? 221  GLN L C     1 
ATOM   7736  O  O     . GLN C 2 221 ? 132.469 138.015 144.588 1.00 125.04 ? 221  GLN L O     1 
ATOM   7737  C  CB    . GLN C 2 221 ? 133.813 139.399 146.945 1.00 122.44 ? 221  GLN L CB    1 
ATOM   7738  C  CG    . GLN C 2 221 ? 133.941 138.439 148.117 1.00 124.82 ? 221  GLN L CG    1 
ATOM   7739  C  CD    . GLN C 2 221 ? 135.294 138.523 148.798 1.00 125.76 ? 221  GLN L CD    1 
ATOM   7740  O  OE1   . GLN C 2 221 ? 136.330 138.271 148.182 1.00 125.59 ? 221  GLN L OE1   1 
ATOM   7741  N  NE2   . GLN C 2 221 ? 135.290 138.881 150.076 1.00 123.54 ? 221  GLN L NE2   1 
ATOM   7742  N  N     . LYS C 2 222 ? 134.119 136.555 145.074 1.00 104.32 ? 222  LYS L N     1 
ATOM   7743  C  CA    . LYS C 2 222 ? 133.417 135.387 144.566 1.00 104.45 ? 222  LYS L CA    1 
ATOM   7744  C  C     . LYS C 2 222 ? 133.040 134.467 145.719 1.00 101.55 ? 222  LYS L C     1 
ATOM   7745  O  O     . LYS C 2 222 ? 133.853 134.206 146.611 1.00 103.17 ? 222  LYS L O     1 
ATOM   7746  C  CB    . LYS C 2 222 ? 134.263 134.631 143.535 1.00 104.90 ? 222  LYS L CB    1 
ATOM   7747  C  CG    . LYS C 2 222 ? 135.618 134.163 144.037 1.00 104.20 ? 222  LYS L CG    1 
ATOM   7748  C  CD    . LYS C 2 222 ? 136.172 133.045 143.167 1.00 104.21 ? 222  LYS L CD    1 
ATOM   7749  C  CE    . LYS C 2 222 ? 136.431 133.524 141.748 1.00 105.34 ? 222  LYS L CE    1 
ATOM   7750  N  NZ    . LYS C 2 222 ? 137.517 134.541 141.695 1.00 106.72 ? 222  LYS L NZ    1 
ATOM   7751  N  N     . LEU C 2 223 ? 131.797 133.993 145.703 1.00 79.83  ? 223  LEU L N     1 
ATOM   7752  C  CA    . LEU C 2 223 ? 131.283 133.099 146.732 1.00 80.07  ? 223  LEU L CA    1 
ATOM   7753  C  C     . LEU C 2 223 ? 130.739 131.850 146.058 1.00 78.99  ? 223  LEU L C     1 
ATOM   7754  O  O     . LEU C 2 223 ? 129.871 131.943 145.184 1.00 85.06  ? 223  LEU L O     1 
ATOM   7755  C  CB    . LEU C 2 223 ? 130.195 133.782 147.567 1.00 82.92  ? 223  LEU L CB    1 
ATOM   7756  C  CG    . LEU C 2 223 ? 130.634 134.911 148.504 1.00 86.65  ? 223  LEU L CG    1 
ATOM   7757  C  CD1   . LEU C 2 223 ? 130.725 136.238 147.766 1.00 84.72  ? 223  LEU L CD1   1 
ATOM   7758  C  CD2   . LEU C 2 223 ? 129.694 135.023 149.695 1.00 83.23  ? 223  LEU L CD2   1 
ATOM   7759  N  N     . SER C 2 224 ? 131.244 130.690 146.463 1.00 62.86  ? 224  SER L N     1 
ATOM   7760  C  CA    . SER C 2 224 ? 130.867 129.415 145.870 1.00 60.83  ? 224  SER L CA    1 
ATOM   7761  C  C     . SER C 2 224 ? 130.032 128.617 146.860 1.00 60.74  ? 224  SER L C     1 
ATOM   7762  O  O     . SER C 2 224 ? 130.449 128.409 148.003 1.00 68.34  ? 224  SER L O     1 
ATOM   7763  C  CB    . SER C 2 224 ? 132.106 128.615 145.463 1.00 63.41  ? 224  SER L CB    1 
ATOM   7764  O  OG    . SER C 2 224 ? 132.937 129.369 144.599 1.00 67.39  ? 224  SER L OG    1 
ATOM   7765  N  N     . GLY C 2 225 ? 128.863 128.169 146.418 1.00 54.98  ? 225  GLY L N     1 
ATOM   7766  C  CA    . GLY C 2 225 ? 128.002 127.366 147.260 1.00 58.17  ? 225  GLY L CA    1 
ATOM   7767  C  C     . GLY C 2 225 ? 127.599 126.069 146.596 1.00 56.59  ? 225  GLY L C     1 
ATOM   7768  O  O     . GLY C 2 225 ? 127.306 126.044 145.397 1.00 65.42  ? 225  GLY L O     1 
ATOM   7769  N  N     . LYS C 2 226 ? 127.579 124.982 147.360 1.00 50.63  ? 226  LYS L N     1 
ATOM   7770  C  CA    . LYS C 2 226 ? 127.255 123.658 146.844 1.00 49.53  ? 226  LYS L CA    1 
ATOM   7771  C  C     . LYS C 2 226 ? 126.160 123.048 147.707 1.00 52.49  ? 226  LYS L C     1 
ATOM   7772  O  O     . LYS C 2 226 ? 126.390 122.749 148.884 1.00 65.80  ? 226  LYS L O     1 
ATOM   7773  C  CB    . LYS C 2 226 ? 128.493 122.764 146.833 1.00 51.67  ? 226  LYS L CB    1 
ATOM   7774  C  CG    . LYS C 2 226 ? 129.704 123.372 146.153 1.00 54.69  ? 226  LYS L CG    1 
ATOM   7775  C  CD    . LYS C 2 226 ? 130.889 122.423 146.205 1.00 55.34  ? 226  LYS L CD    1 
ATOM   7776  C  CE    . LYS C 2 226 ? 130.584 121.128 145.475 1.00 61.11  ? 226  LYS L CE    1 
ATOM   7777  N  NZ    . LYS C 2 226 ? 131.725 120.175 145.526 1.00 60.11  ? 226  LYS L NZ    1 
ATOM   7778  N  N     . LEU C 2 227 ? 124.977 122.855 147.132 1.00 51.05  ? 227  LEU L N     1 
ATOM   7779  C  CA    . LEU C 2 227 ? 123.916 122.123 147.806 1.00 55.80  ? 227  LEU L CA    1 
ATOM   7780  C  C     . LEU C 2 227 ? 123.876 120.693 147.288 1.00 55.38  ? 227  LEU L C     1 
ATOM   7781  O  O     . LEU C 2 227 ? 124.017 120.450 146.087 1.00 63.44  ? 227  LEU L O     1 
ATOM   7782  C  CB    . LEU C 2 227 ? 122.548 122.795 147.630 1.00 58.18  ? 227  LEU L CB    1 
ATOM   7783  C  CG    . LEU C 2 227 ? 121.911 123.133 146.281 1.00 58.33  ? 227  LEU L CG    1 
ATOM   7784  C  CD1   . LEU C 2 227 ? 121.345 121.915 145.573 0.00 59.52  ? 227  LEU L CD1   1 
ATOM   7785  C  CD2   . LEU C 2 227 ? 120.803 124.144 146.482 1.00 58.01  ? 227  LEU L CD2   1 
ATOM   7786  N  N     . TYR C 2 228 ? 123.708 119.749 148.205 1.00 64.01  ? 228  TYR L N     1 
ATOM   7787  C  CA    . TYR C 2 228 ? 123.652 118.332 147.880 1.00 63.33  ? 228  TYR L CA    1 
ATOM   7788  C  C     . TYR C 2 228 ? 122.249 117.818 148.164 1.00 66.87  ? 228  TYR L C     1 
ATOM   7789  O  O     . TYR C 2 228 ? 121.854 117.696 149.328 1.00 77.94  ? 228  TYR L O     1 
ATOM   7790  C  CB    . TYR C 2 228 ? 124.682 117.544 148.687 1.00 69.93  ? 228  TYR L CB    1 
ATOM   7791  C  CG    . TYR C 2 228 ? 126.109 117.727 148.230 1.00 69.07  ? 228  TYR L CG    1 
ATOM   7792  C  CD1   . TYR C 2 228 ? 126.902 118.736 148.752 1.00 71.15  ? 228  TYR L CD1   1 
ATOM   7793  C  CD2   . TYR C 2 228 ? 126.668 116.878 147.288 1.00 66.34  ? 228  TYR L CD2   1 
ATOM   7794  C  CE1   . TYR C 2 228 ? 128.209 118.901 148.339 1.00 68.99  ? 228  TYR L CE1   1 
ATOM   7795  C  CE2   . TYR C 2 228 ? 127.970 117.034 146.870 1.00 66.98  ? 228  TYR L CE2   1 
ATOM   7796  C  CZ    . TYR C 2 228 ? 128.737 118.047 147.398 1.00 70.54  ? 228  TYR L CZ    1 
ATOM   7797  O  OH    . TYR C 2 228 ? 130.038 118.208 146.984 1.00 73.34  ? 228  TYR L OH    1 
ATOM   7798  N  N     . LEU C 2 229 ? 121.504 117.514 147.109 1.00 66.37  ? 229  LEU L N     1 
ATOM   7799  C  CA    . LEU C 2 229 ? 120.179 116.913 147.225 1.00 72.41  ? 229  LEU L CA    1 
ATOM   7800  C  C     . LEU C 2 229 ? 120.355 115.424 146.953 1.00 75.96  ? 229  LEU L C     1 
ATOM   7801  O  O     . LEU C 2 229 ? 120.167 114.956 145.829 1.00 84.65  ? 229  LEU L O     1 
ATOM   7802  C  CB    . LEU C 2 229 ? 119.185 117.545 146.257 1.00 78.45  ? 229  LEU L CB    1 
ATOM   7803  C  CG    . LEU C 2 229 ? 119.246 119.058 146.061 1.00 75.02  ? 229  LEU L CG    1 
ATOM   7804  C  CD1   . LEU C 2 229 ? 118.208 119.495 145.044 1.00 75.42  ? 229  LEU L CD1   1 
ATOM   7805  C  CD2   . LEU C 2 229 ? 119.042 119.782 147.378 1.00 74.65  ? 229  LEU L CD2   1 
ATOM   7806  N  N     . VAL C 2 230 ? 120.713 114.680 147.992 1.00 80.97  ? 230  VAL L N     1 
ATOM   7807  C  CA    . VAL C 2 230 ? 121.039 113.273 147.845 1.00 84.57  ? 230  VAL L CA    1 
ATOM   7808  C  C     . VAL C 2 230 ? 119.933 112.431 148.466 1.00 87.28  ? 230  VAL L C     1 
ATOM   7809  O  O     . VAL C 2 230 ? 119.162 112.887 149.315 1.00 89.80  ? 230  VAL L O     1 
ATOM   7810  C  CB    . VAL C 2 230 ? 122.411 112.937 148.463 1.00 83.95  ? 230  VAL L CB    1 
ATOM   7811  C  CG1   . VAL C 2 230 ? 123.466 113.880 147.924 1.00 83.45  ? 230  VAL L CG1   1 
ATOM   7812  C  CG2   . VAL C 2 230 ? 122.356 113.024 149.962 1.00 88.01  ? 230  VAL L CG2   1 
ATOM   7813  N  N     . ASP C 2 231 ? 119.848 111.184 148.010 1.00 104.01 ? 231  ASP L N     1 
ATOM   7814  C  CA    . ASP C 2 231 ? 118.873 110.225 148.504 1.00 107.52 ? 231  ASP L CA    1 
ATOM   7815  C  C     . ASP C 2 231 ? 119.579 108.914 148.820 1.00 110.76 ? 231  ASP L C     1 
ATOM   7816  O  O     . ASP C 2 231 ? 120.511 108.508 148.120 1.00 108.16 ? 231  ASP L O     1 
ATOM   7817  C  CB    . ASP C 2 231 ? 117.749 109.996 147.484 1.00 105.25 ? 231  ASP L CB    1 
ATOM   7818  C  CG    . ASP C 2 231 ? 116.556 109.280 148.082 1.00 107.76 ? 231  ASP L CG    1 
ATOM   7819  O  OD1   . ASP C 2 231 ? 116.455 109.222 149.325 1.00 108.39 ? 231  ASP L OD1   1 
ATOM   7820  O  OD2   . ASP C 2 231 ? 115.719 108.773 147.306 1.00 107.77 ? 231  ASP L OD2   1 
ATOM   7821  N  N     . LEU C 2 232 ? 119.128 108.256 149.882 1.00 123.92 ? 232  LEU L N     1 
ATOM   7822  C  CA    . LEU C 2 232 ? 119.771 107.054 150.393 1.00 122.29 ? 232  LEU L CA    1 
ATOM   7823  C  C     . LEU C 2 232 ? 119.099 105.798 149.846 1.00 122.17 ? 232  LEU L C     1 
ATOM   7824  O  O     . LEU C 2 232 ? 118.260 105.846 148.944 1.00 119.17 ? 232  LEU L O     1 
ATOM   7825  C  CB    . LEU C 2 232 ? 119.750 107.045 151.926 1.00 120.53 ? 232  LEU L CB    1 
ATOM   7826  C  CG    . LEU C 2 232 ? 120.944 107.663 152.659 1.00 121.28 ? 232  LEU L CG    1 
ATOM   7827  C  CD1   . LEU C 2 232 ? 121.097 109.140 152.327 1.00 120.93 ? 232  LEU L CD1   1 
ATOM   7828  C  CD2   . LEU C 2 232 ? 120.809 107.461 154.160 1.00 120.22 ? 232  LEU L CD2   1 
ATOM   7829  N  N     . ALA C 2 233 ? 119.496 104.658 150.406 1.00 132.91 ? 233  ALA L N     1 
ATOM   7830  C  CA    . ALA C 2 233 ? 118.952 103.357 150.058 1.00 132.09 ? 233  ALA L CA    1 
ATOM   7831  C  C     . ALA C 2 233 ? 118.182 102.786 151.248 1.00 132.29 ? 233  ALA L C     1 
ATOM   7832  O  O     . ALA C 2 233 ? 118.001 103.445 152.277 1.00 131.31 ? 233  ALA L O     1 
ATOM   7833  C  CB    . ALA C 2 233 ? 120.075 102.423 149.602 1.00 131.24 ? 233  ALA L CB    1 
ATOM   7834  N  N     . GLY C 2 234 ? 117.717 101.545 151.111 1.00 131.44 ? 234  GLY L N     1 
ATOM   7835  C  CA    . GLY C 2 234 ? 116.967 100.917 152.178 1.00 131.29 ? 234  GLY L CA    1 
ATOM   7836  C  C     . GLY C 2 234 ? 117.827 100.589 153.383 1.00 131.63 ? 234  GLY L C     1 
ATOM   7837  O  O     . GLY C 2 234 ? 119.056 100.534 153.319 1.00 130.03 ? 234  GLY L O     1 
ATOM   7838  N  N     . SER C 2 235 ? 117.156 100.365 154.510 1.00 133.43 ? 235  SER L N     1 
ATOM   7839  C  CA    . SER C 2 235 ? 117.805 100.125 155.796 1.00 132.81 ? 235  SER L CA    1 
ATOM   7840  C  C     . SER C 2 235 ? 117.167 98.938  156.506 1.00 133.10 ? 235  SER L C     1 
ATOM   7841  O  O     . SER C 2 235 ? 116.836 98.991  157.692 1.00 131.89 ? 235  SER L O     1 
ATOM   7842  C  CB    . SER C 2 235 ? 117.745 101.376 156.668 1.00 131.63 ? 235  SER L CB    1 
ATOM   7843  O  OG    . SER C 2 235 ? 118.287 102.494 155.987 1.00 131.16 ? 235  SER L OG    1 
ATOM   7844  N  N     . GLU C 2 236 ? 116.984 97.840  155.776 1.00 139.31 ? 236  GLU L N     1 
ATOM   7845  C  CA    . GLU C 2 236 ? 116.366 96.629  156.312 1.00 139.07 ? 236  GLU L CA    1 
ATOM   7846  C  C     . GLU C 2 236 ? 117.476 95.674  156.738 1.00 138.57 ? 236  GLU L C     1 
ATOM   7847  O  O     . GLU C 2 236 ? 118.032 94.944  155.914 1.00 138.37 ? 236  GLU L O     1 
ATOM   7848  C  CB    . GLU C 2 236 ? 115.442 95.988  155.281 1.00 139.26 ? 236  GLU L CB    1 
ATOM   7849  C  CG    . GLU C 2 236 ? 114.215 96.819  154.949 1.00 139.18 ? 236  GLU L CG    1 
ATOM   7850  C  CD    . GLU C 2 236 ? 114.523 97.949  153.988 1.00 139.33 ? 236  GLU L CD    1 
ATOM   7851  O  OE1   . GLU C 2 236 ? 115.507 97.833  153.228 1.00 139.11 ? 236  GLU L OE1   1 
ATOM   7852  O  OE2   . GLU C 2 236 ? 113.790 98.959  154.001 1.00 138.54 ? 236  GLU L OE2   1 
ATOM   7853  N  N     . LYS C 2 237 ? 117.794 95.681  158.028 1.00 135.79 ? 237  LYS L N     1 
ATOM   7854  C  CA    . LYS C 2 237 ? 118.819 94.798  158.572 1.00 136.11 ? 237  LYS L CA    1 
ATOM   7855  C  C     . LYS C 2 237 ? 118.658 94.635  160.079 1.00 135.53 ? 237  LYS L C     1 
ATOM   7856  O  O     . LYS C 2 237 ? 117.996 95.442  160.733 1.00 135.04 ? 237  LYS L O     1 
ATOM   7857  C  CB    . LYS C 2 237 ? 120.217 95.329  158.247 1.00 136.49 ? 237  LYS L CB    1 
ATOM   7858  C  CG    . LYS C 2 237 ? 121.324 94.303  158.429 1.00 135.22 ? 237  LYS L CG    1 
ATOM   7859  C  CD    . LYS C 2 237 ? 121.117 93.106  157.514 1.00 134.99 ? 237  LYS L CD    1 
ATOM   7860  C  CE    . LYS C 2 237 ? 121.126 93.520  156.051 1.00 135.04 ? 237  LYS L CE    1 
ATOM   7861  N  NZ    . LYS C 2 237 ? 120.852 92.372  155.145 1.00 135.35 ? 237  LYS L NZ    1 
ATOM   7862  N  N     . ILE C 2 254 ? 125.012 91.741  151.008 1.00 138.00 ? 254  ILE L N     1 
ATOM   7863  C  CA    . ILE C 2 254 ? 124.722 92.413  152.268 1.00 139.00 ? 254  ILE L CA    1 
ATOM   7864  C  C     . ILE C 2 254 ? 125.048 93.897  152.154 1.00 138.88 ? 254  ILE L C     1 
ATOM   7865  O  O     . ILE C 2 254 ? 126.103 94.272  151.642 1.00 138.03 ? 254  ILE L O     1 
ATOM   7866  C  CB    . ILE C 2 254 ? 125.496 91.770  153.434 1.00 136.87 ? 254  ILE L CB    1 
ATOM   7867  C  CG1   . ILE C 2 254 ? 125.358 90.247  153.391 1.00 136.82 ? 254  ILE L CG1   1 
ATOM   7868  C  CG2   . ILE C 2 254 ? 125.001 92.312  154.767 1.00 135.58 ? 254  ILE L CG2   1 
ATOM   7869  C  CD1   . ILE C 2 254 ? 123.934 89.757  153.544 1.00 136.92 ? 254  ILE L CD1   1 
ATOM   7870  N  N     . ASN C 2 255 ? 124.133 94.738  152.631 1.00 126.59 ? 255  ASN L N     1 
ATOM   7871  C  CA    . ASN C 2 255 ? 124.344 96.179  152.590 1.00 124.93 ? 255  ASN L CA    1 
ATOM   7872  C  C     . ASN C 2 255 ? 125.468 96.573  153.540 1.00 123.14 ? 255  ASN L C     1 
ATOM   7873  O  O     . ASN C 2 255 ? 125.549 96.072  154.665 1.00 121.90 ? 255  ASN L O     1 
ATOM   7874  C  CB    . ASN C 2 255 ? 123.053 96.910  152.954 1.00 122.97 ? 255  ASN L CB    1 
ATOM   7875  C  CG    . ASN C 2 255 ? 123.140 98.401  152.713 1.00 121.27 ? 255  ASN L CG    1 
ATOM   7876  O  OD1   . ASN C 2 255 ? 124.031 98.880  152.011 1.00 119.23 ? 255  ASN L OD1   1 
ATOM   7877  N  ND2   . ASN C 2 255 ? 122.208 99.147  153.291 1.00 122.99 ? 255  ASN L ND2   1 
ATOM   7878  N  N     . LYS C 2 256 ? 126.335 97.472  153.085 1.00 120.35 ? 256  LYS L N     1 
ATOM   7879  C  CA    . LYS C 2 256 ? 127.504 97.883  153.853 1.00 121.26 ? 256  LYS L CA    1 
ATOM   7880  C  C     . LYS C 2 256 ? 127.604 99.387  154.049 1.00 119.25 ? 256  LYS L C     1 
ATOM   7881  O  O     . LYS C 2 256 ? 128.062 99.834  155.103 1.00 119.63 ? 256  LYS L O     1 
ATOM   7882  C  CB    . LYS C 2 256 ? 128.784 97.378  153.172 1.00 121.43 ? 256  LYS L CB    1 
ATOM   7883  C  CG    . LYS C 2 256 ? 128.849 95.869  153.003 1.00 120.97 ? 256  LYS L CG    1 
ATOM   7884  C  CD    . LYS C 2 256 ? 129.988 95.471  152.081 1.00 119.71 ? 256  LYS L CD    1 
ATOM   7885  C  CE    . LYS C 2 256 ? 129.816 96.086  150.702 1.00 119.63 ? 256  LYS L CE    1 
ATOM   7886  N  NZ    . LYS C 2 256 ? 130.913 95.695  149.775 1.00 119.66 ? 256  LYS L NZ    1 
ATOM   7887  N  N     . SER C 2 257 ? 127.194 100.181 153.056 1.00 107.06 ? 257  SER L N     1 
ATOM   7888  C  CA    . SER C 2 257 ? 127.325 101.630 153.166 1.00 106.46 ? 257  SER L CA    1 
ATOM   7889  C  C     . SER C 2 257 ? 126.481 102.180 154.310 1.00 106.17 ? 257  SER L C     1 
ATOM   7890  O  O     . SER C 2 257 ? 126.925 103.070 155.045 1.00 107.08 ? 257  SER L O     1 
ATOM   7891  C  CB    . SER C 2 257 ? 126.938 102.293 151.845 1.00 105.55 ? 257  SER L CB    1 
ATOM   7892  O  OG    . SER C 2 257 ? 127.789 101.865 150.796 1.00 105.40 ? 257  SER L OG    1 
ATOM   7893  N  N     . LEU C 2 258 ? 125.260 101.667 154.473 1.00 106.21 ? 258  LEU L N     1 
ATOM   7894  C  CA    . LEU C 2 258 ? 124.418 102.114 155.579 1.00 105.59 ? 258  LEU L CA    1 
ATOM   7895  C  C     . LEU C 2 258 ? 124.995 101.684 156.922 1.00 102.28 ? 258  LEU L C     1 
ATOM   7896  O  O     . LEU C 2 258 ? 124.859 102.403 157.919 1.00 100.76 ? 258  LEU L O     1 
ATOM   7897  C  CB    . LEU C 2 258 ? 122.994 101.587 155.408 1.00 106.41 ? 258  LEU L CB    1 
ATOM   7898  C  CG    . LEU C 2 258 ? 122.033 102.466 154.604 1.00 106.70 ? 258  LEU L CG    1 
ATOM   7899  C  CD1   . LEU C 2 258 ? 122.060 103.895 155.121 1.00 104.69 ? 258  LEU L CD1   1 
ATOM   7900  C  CD2   . LEU C 2 258 ? 122.358 102.427 153.121 1.00 106.53 ? 258  LEU L CD2   1 
ATOM   7901  N  N     . SER C 2 259 ? 125.632 100.511 156.971 1.00 104.68 ? 259  SER L N     1 
ATOM   7902  C  CA    . SER C 2 259 ? 126.268 100.071 158.209 1.00 108.65 ? 259  SER L CA    1 
ATOM   7903  C  C     . SER C 2 259 ? 127.370 101.035 158.630 1.00 106.53 ? 259  SER L C     1 
ATOM   7904  O  O     . SER C 2 259 ? 127.459 101.413 159.804 1.00 108.16 ? 259  SER L O     1 
ATOM   7905  C  CB    . SER C 2 259 ? 126.822 98.656  158.044 1.00 107.58 ? 259  SER L CB    1 
ATOM   7906  O  OG    . SER C 2 259 ? 127.837 98.616  157.058 1.00 108.01 ? 259  SER L OG    1 
ATOM   7907  N  N     . ALA C 2 260 ? 128.217 101.449 157.685 1.00 88.76  ? 260  ALA L N     1 
ATOM   7908  C  CA    . ALA C 2 260 ? 129.182 102.503 157.978 1.00 85.00  ? 260  ALA L CA    1 
ATOM   7909  C  C     . ALA C 2 260 ? 128.486 103.833 158.219 1.00 88.53  ? 260  ALA L C     1 
ATOM   7910  O  O     . ALA C 2 260 ? 128.963 104.643 159.021 1.00 90.37  ? 260  ALA L O     1 
ATOM   7911  C  CB    . ALA C 2 260 ? 130.194 102.630 156.841 1.00 86.02  ? 260  ALA L CB    1 
ATOM   7912  N  N     . LEU C 2 261 ? 127.365 104.077 157.535 1.00 93.20  ? 261  LEU L N     1 
ATOM   7913  C  CA    . LEU C 2 261 ? 126.568 105.265 157.822 1.00 95.19  ? 261  LEU L CA    1 
ATOM   7914  C  C     . LEU C 2 261 ? 126.026 105.222 159.244 1.00 94.86  ? 261  LEU L C     1 
ATOM   7915  O  O     . LEU C 2 261 ? 125.960 106.252 159.924 1.00 96.37  ? 261  LEU L O     1 
ATOM   7916  C  CB    . LEU C 2 261 ? 125.426 105.393 156.813 1.00 98.74  ? 261  LEU L CB    1 
ATOM   7917  C  CG    . LEU C 2 261 ? 124.966 106.810 156.460 1.00 97.07  ? 261  LEU L CG    1 
ATOM   7918  C  CD1   . LEU C 2 261 ? 124.333 106.827 155.082 1.00 93.64  ? 261  LEU L CD1   1 
ATOM   7919  C  CD2   . LEU C 2 261 ? 123.997 107.353 157.497 1.00 94.64  ? 261  LEU L CD2   1 
ATOM   7920  N  N     . GLY C 2 262 ? 125.621 104.039 159.708 1.00 89.73  ? 262  GLY L N     1 
ATOM   7921  C  CA    . GLY C 2 262 ? 125.265 103.893 161.107 1.00 92.14  ? 262  GLY L CA    1 
ATOM   7922  C  C     . GLY C 2 262 ? 126.471 103.935 162.022 1.00 89.16  ? 262  GLY L C     1 
ATOM   7923  O  O     . GLY C 2 262 ? 126.347 104.277 163.202 1.00 88.46  ? 262  GLY L O     1 
ATOM   7924  N  N     . ASN C 2 263 ? 127.648 103.585 161.501 1.00 80.12  ? 263  ASN L N     1 
ATOM   7925  C  CA    . ASN C 2 263 ? 128.866 103.644 162.300 1.00 78.96  ? 263  ASN L CA    1 
ATOM   7926  C  C     . ASN C 2 263 ? 129.384 105.070 162.439 1.00 77.42  ? 263  ASN L C     1 
ATOM   7927  O  O     . ASN C 2 263 ? 129.875 105.449 163.509 1.00 81.84  ? 263  ASN L O     1 
ATOM   7928  C  CB    . ASN C 2 263 ? 129.940 102.743 161.692 1.00 83.53  ? 263  ASN L CB    1 
ATOM   7929  C  CG    . ASN C 2 263 ? 129.656 101.269 161.908 1.00 83.87  ? 263  ASN L CG    1 
ATOM   7930  O  OD1   . ASN C 2 263 ? 129.059 100.881 162.912 1.00 79.45  ? 263  ASN L OD1   1 
ATOM   7931  N  ND2   . ASN C 2 263 ? 130.082 100.438 160.964 1.00 83.45  ? 263  ASN L ND2   1 
ATOM   7932  N  N     . VAL C 2 264 ? 129.294 105.874 161.377 1.00 62.34  ? 264  VAL L N     1 
ATOM   7933  C  CA    . VAL C 2 264 ? 129.816 107.236 161.451 1.00 63.40  ? 264  VAL L CA    1 
ATOM   7934  C  C     . VAL C 2 264 ? 128.948 108.092 162.367 1.00 70.54  ? 264  VAL L C     1 
ATOM   7935  O  O     . VAL C 2 264 ? 129.461 108.912 163.137 1.00 73.35  ? 264  VAL L O     1 
ATOM   7936  C  CB    . VAL C 2 264 ? 129.950 107.849 160.045 1.00 66.80  ? 264  VAL L CB    1 
ATOM   7937  C  CG1   . VAL C 2 264 ? 128.646 107.765 159.286 1.00 74.82  ? 264  VAL L CG1   1 
ATOM   7938  C  CG2   . VAL C 2 264 ? 130.420 109.291 160.134 1.00 67.91  ? 264  VAL L CG2   1 
ATOM   7939  N  N     . ILE C 2 265 ? 127.626 107.914 162.309 1.00 76.30  ? 265  ILE L N     1 
ATOM   7940  C  CA    . ILE C 2 265 ? 126.756 108.639 163.229 1.00 76.96  ? 265  ILE L CA    1 
ATOM   7941  C  C     . ILE C 2 265 ? 126.966 108.149 164.656 1.00 80.48  ? 265  ILE L C     1 
ATOM   7942  O  O     . ILE C 2 265 ? 126.925 108.937 165.608 1.00 81.16  ? 265  ILE L O     1 
ATOM   7943  C  CB    . ILE C 2 265 ? 125.282 108.525 162.798 1.00 77.49  ? 265  ILE L CB    1 
ATOM   7944  C  CG1   . ILE C 2 265 ? 124.806 107.074 162.863 1.00 77.76  ? 265  ILE L CG1   1 
ATOM   7945  C  CG2   . ILE C 2 265 ? 125.090 109.097 161.401 1.00 75.77  ? 265  ILE L CG2   1 
ATOM   7946  C  CD1   . ILE C 2 265 ? 123.335 106.935 163.163 1.00 80.06  ? 265  ILE L CD1   1 
ATOM   7947  N  N     . SER C 2 266 ? 127.190 106.842 164.832 1.00 75.62  ? 266  SER L N     1 
ATOM   7948  C  CA    . SER C 2 266 ? 127.528 106.329 166.155 1.00 75.87  ? 266  SER L CA    1 
ATOM   7949  C  C     . SER C 2 266 ? 128.856 106.893 166.635 1.00 71.96  ? 266  SER L C     1 
ATOM   7950  O  O     . SER C 2 266 ? 129.056 107.077 167.840 1.00 72.90  ? 266  SER L O     1 
ATOM   7951  C  CB    . SER C 2 266 ? 127.576 104.801 166.138 1.00 77.92  ? 266  SER L CB    1 
ATOM   7952  O  OG    . SER C 2 266 ? 128.732 104.334 165.467 1.00 76.48  ? 266  SER L OG    1 
ATOM   7953  N  N     . ALA C 2 267 ? 129.778 107.157 165.707 1.00 54.07  ? 267  ALA L N     1 
ATOM   7954  C  CA    . ALA C 2 267 ? 130.994 107.875 166.060 1.00 52.36  ? 267  ALA L CA    1 
ATOM   7955  C  C     . ALA C 2 267 ? 130.690 109.325 166.409 1.00 60.32  ? 267  ALA L C     1 
ATOM   7956  O  O     . ALA C 2 267 ? 131.278 109.884 167.342 1.00 64.30  ? 267  ALA L O     1 
ATOM   7957  C  CB    . ALA C 2 267 ? 132.000 107.794 164.914 1.00 52.61  ? 267  ALA L CB    1 
ATOM   7958  N  N     . LEU C 2 268 ? 129.775 109.953 165.667 1.00 56.47  ? 268  LEU L N     1 
ATOM   7959  C  CA    . LEU C 2 268 ? 129.434 111.348 165.921 1.00 57.32  ? 268  LEU L CA    1 
ATOM   7960  C  C     . LEU C 2 268 ? 128.569 111.500 167.166 1.00 57.66  ? 268  LEU L C     1 
ATOM   7961  O  O     . LEU C 2 268 ? 128.783 112.422 167.961 1.00 58.01  ? 268  LEU L O     1 
ATOM   7962  C  CB    . LEU C 2 268 ? 128.728 111.945 164.705 1.00 48.58  ? 268  LEU L CB    1 
ATOM   7963  C  CG    . LEU C 2 268 ? 129.586 112.718 163.700 1.00 52.63  ? 268  LEU L CG    1 
ATOM   7964  C  CD1   . LEU C 2 268 ? 130.788 111.908 163.244 1.00 56.94  ? 268  LEU L CD1   1 
ATOM   7965  C  CD2   . LEU C 2 268 ? 128.747 113.146 162.506 1.00 56.14  ? 268  LEU L CD2   1 
ATOM   7966  N  N     . ALA C 2 269 ? 127.586 110.614 167.349 1.00 61.06  ? 269  ALA L N     1 
ATOM   7967  C  CA    . ALA C 2 269 ? 126.724 110.698 168.524 1.00 59.43  ? 269  ALA L CA    1 
ATOM   7968  C  C     . ALA C 2 269 ? 127.507 110.445 169.806 1.00 65.16  ? 269  ALA L C     1 
ATOM   7969  O  O     . ALA C 2 269 ? 127.339 111.167 170.795 1.00 62.12  ? 269  ALA L O     1 
ATOM   7970  C  CB    . ALA C 2 269 ? 125.564 109.711 168.399 1.00 55.21  ? 269  ALA L CB    1 
ATOM   7971  N  N     . GLU C 2 270 ? 128.368 109.426 169.808 1.00 83.19  ? 270  GLU L N     1 
ATOM   7972  C  CA    . GLU C 2 270 ? 129.205 109.163 170.973 1.00 81.40  ? 270  GLU L CA    1 
ATOM   7973  C  C     . GLU C 2 270 ? 130.365 110.142 171.080 1.00 83.54  ? 270  GLU L C     1 
ATOM   7974  O  O     . GLU C 2 270 ? 130.978 110.243 172.148 1.00 84.44  ? 270  GLU L O     1 
ATOM   7975  C  CB    . GLU C 2 270 ? 129.737 107.729 170.929 1.00 79.82  ? 270  GLU L CB    1 
ATOM   7976  C  CG    . GLU C 2 270 ? 128.684 106.666 171.193 1.00 83.30  ? 270  GLU L CG    1 
ATOM   7977  C  CD    . GLU C 2 270 ? 128.362 106.516 172.667 1.00 86.96  ? 270  GLU L CD    1 
ATOM   7978  O  OE1   . GLU C 2 270 ? 129.135 107.031 173.502 1.00 88.62  ? 270  GLU L OE1   1 
ATOM   7979  O  OE2   . GLU C 2 270 ? 127.335 105.883 172.991 1.00 86.63  ? 270  GLU L OE2   1 
ATOM   7980  N  N     . GLY C 2 271 ? 130.681 110.858 170.003 1.00 81.04  ? 271  GLY L N     1 
ATOM   7981  C  CA    . GLY C 2 271 ? 131.769 111.810 170.008 1.00 79.66  ? 271  GLY L CA    1 
ATOM   7982  C  C     . GLY C 2 271 ? 133.149 111.210 169.868 1.00 74.85  ? 271  GLY L C     1 
ATOM   7983  O  O     . GLY C 2 271 ? 134.139 111.947 169.967 1.00 76.13  ? 271  GLY L O     1 
ATOM   7984  N  N     . SER C 2 272 ? 133.251 109.903 169.646 1.00 68.22  ? 272  SER L N     1 
ATOM   7985  C  CA    . SER C 2 272 ? 134.550 109.259 169.541 1.00 74.46  ? 272  SER L CA    1 
ATOM   7986  C  C     . SER C 2 272 ? 135.285 109.721 168.288 1.00 76.60  ? 272  SER L C     1 
ATOM   7987  O  O     . SER C 2 272 ? 134.688 109.933 167.229 1.00 77.65  ? 272  SER L O     1 
ATOM   7988  C  CB    . SER C 2 272 ? 134.392 107.739 169.524 1.00 76.57  ? 272  SER L CB    1 
ATOM   7989  O  OG    . SER C 2 272 ? 133.795 107.275 170.722 1.00 79.87  ? 272  SER L OG    1 
ATOM   7990  N  N     . THR C 2 273 ? 136.599 109.878 168.420 1.00 71.91  ? 273  THR L N     1 
ATOM   7991  C  CA    . THR C 2 273 ? 137.449 110.257 167.300 1.00 66.32  ? 273  THR L CA    1 
ATOM   7992  C  C     . THR C 2 273 ? 137.753 109.020 166.457 1.00 58.35  ? 273  THR L C     1 
ATOM   7993  O  O     . THR C 2 273 ? 137.138 107.963 166.621 1.00 58.60  ? 273  THR L O     1 
ATOM   7994  C  CB    . THR C 2 273 ? 138.721 110.936 167.803 1.00 69.74  ? 273  THR L CB    1 
ATOM   7995  O  OG1   . THR C 2 273 ? 139.426 110.047 168.679 1.00 71.65  ? 273  THR L OG1   1 
ATOM   7996  C  CG2   . THR C 2 273 ? 138.381 112.217 168.551 1.00 65.70  ? 273  THR L CG2   1 
ATOM   7997  N  N     . TYR C 2 274 ? 138.714 109.144 165.542 1.00 67.77  ? 274  TYR L N     1 
ATOM   7998  C  CA    . TYR C 2 274 ? 139.067 108.073 164.611 1.00 76.18  ? 274  TYR L CA    1 
ATOM   7999  C  C     . TYR C 2 274 ? 137.828 107.588 163.862 1.00 77.14  ? 274  TYR L C     1 
ATOM   8000  O  O     . TYR C 2 274 ? 137.619 106.392 163.647 1.00 74.39  ? 274  TYR L O     1 
ATOM   8001  C  CB    . TYR C 2 274 ? 139.769 106.921 165.334 1.00 75.15  ? 274  TYR L CB    1 
ATOM   8002  C  CG    . TYR C 2 274 ? 140.506 105.974 164.412 1.00 75.59  ? 274  TYR L CG    1 
ATOM   8003  C  CD1   . TYR C 2 274 ? 141.599 106.406 163.671 1.00 75.45  ? 274  TYR L CD1   1 
ATOM   8004  C  CD2   . TYR C 2 274 ? 140.114 104.647 164.288 1.00 73.92  ? 274  TYR L CD2   1 
ATOM   8005  C  CE1   . TYR C 2 274 ? 142.276 105.546 162.828 1.00 74.06  ? 274  TYR L CE1   1 
ATOM   8006  C  CE2   . TYR C 2 274 ? 140.785 103.780 163.448 1.00 76.62  ? 274  TYR L CE2   1 
ATOM   8007  C  CZ    . TYR C 2 274 ? 141.865 104.234 162.721 1.00 76.46  ? 274  TYR L CZ    1 
ATOM   8008  O  OH    . TYR C 2 274 ? 142.537 103.374 161.883 1.00 76.21  ? 274  TYR L OH    1 
ATOM   8009  N  N     . VAL C 2 275 ? 137.000 108.548 163.468 1.00 74.74  ? 275  VAL L N     1 
ATOM   8010  C  CA    . VAL C 2 275 ? 135.708 108.251 162.841 1.00 69.83  ? 275  VAL L CA    1 
ATOM   8011  C  C     . VAL C 2 275 ? 135.937 107.519 161.522 1.00 68.80  ? 275  VAL L C     1 
ATOM   8012  O  O     . VAL C 2 275 ? 136.782 107.943 160.714 1.00 67.67  ? 275  VAL L O     1 
ATOM   8013  C  CB    . VAL C 2 275 ? 134.911 109.544 162.638 1.00 65.66  ? 275  VAL L CB    1 
ATOM   8014  C  CG1   . VAL C 2 275 ? 135.731 110.571 161.873 1.00 68.41  ? 275  VAL L CG1   1 
ATOM   8015  C  CG2   . VAL C 2 275 ? 133.604 109.260 161.920 1.00 68.80  ? 275  VAL L CG2   1 
ATOM   8016  N  N     . PRO C 2 276 ? 135.241 106.411 161.270 1.00 68.80  ? 276  PRO L N     1 
ATOM   8017  C  CA    . PRO C 2 276 ? 135.449 105.642 160.026 1.00 65.95  ? 276  PRO L CA    1 
ATOM   8018  C  C     . PRO C 2 276 ? 134.745 106.271 158.830 1.00 66.36  ? 276  PRO L C     1 
ATOM   8019  O  O     . PRO C 2 276 ? 133.723 105.793 158.328 1.00 66.32  ? 276  PRO L O     1 
ATOM   8020  C  CB    . PRO C 2 276 ? 134.881 104.269 160.395 1.00 67.15  ? 276  PRO L CB    1 
ATOM   8021  C  CG    . PRO C 2 276 ? 133.807 104.570 161.377 1.00 70.38  ? 276  PRO L CG    1 
ATOM   8022  C  CD    . PRO C 2 276 ? 134.294 105.744 162.181 1.00 73.87  ? 276  PRO L CD    1 
ATOM   8023  N  N     . TYR C 2 277 ? 135.303 107.382 158.350 1.00 72.29  ? 277  TYR L N     1 
ATOM   8024  C  CA    . TYR C 2 277 ? 134.751 108.037 157.171 1.00 70.79  ? 277  TYR L CA    1 
ATOM   8025  C  C     . TYR C 2 277 ? 135.080 107.281 155.892 1.00 76.79  ? 277  TYR L C     1 
ATOM   8026  O  O     . TYR C 2 277 ? 134.332 107.374 154.912 1.00 79.49  ? 277  TYR L O     1 
ATOM   8027  C  CB    . TYR C 2 277 ? 135.273 109.470 157.067 1.00 72.66  ? 277  TYR L CB    1 
ATOM   8028  C  CG    . TYR C 2 277 ? 134.351 110.506 157.661 1.00 71.97  ? 277  TYR L CG    1 
ATOM   8029  C  CD1   . TYR C 2 277 ? 133.025 110.590 157.266 1.00 68.13  ? 277  TYR L CD1   1 
ATOM   8030  C  CD2   . TYR C 2 277 ? 134.812 111.411 158.606 1.00 73.66  ? 277  TYR L CD2   1 
ATOM   8031  C  CE1   . TYR C 2 277 ? 132.179 111.538 157.806 1.00 71.90  ? 277  TYR L CE1   1 
ATOM   8032  C  CE2   . TYR C 2 277 ? 133.976 112.363 159.150 1.00 75.18  ? 277  TYR L CE2   1 
ATOM   8033  C  CZ    . TYR C 2 277 ? 132.661 112.423 158.747 1.00 75.61  ? 277  TYR L CZ    1 
ATOM   8034  O  OH    . TYR C 2 277 ? 131.827 113.373 159.289 1.00 73.20  ? 277  TYR L OH    1 
ATOM   8035  N  N     . ARG C 2 278 ? 136.182 106.536 155.880 1.00 81.26  ? 278  ARG L N     1 
ATOM   8036  C  CA    . ARG C 2 278 ? 136.663 105.864 154.681 1.00 81.14  ? 278  ARG L CA    1 
ATOM   8037  C  C     . ARG C 2 278 ? 136.179 104.426 154.556 1.00 82.96  ? 278  ARG L C     1 
ATOM   8038  O  O     . ARG C 2 278 ? 136.578 103.739 153.610 1.00 84.52  ? 278  ARG L O     1 
ATOM   8039  C  CB    . ARG C 2 278 ? 138.194 105.890 154.649 1.00 79.10  ? 278  ARG L CB    1 
ATOM   8040  C  CG    . ARG C 2 278 ? 138.802 107.276 154.805 1.00 79.64  ? 278  ARG L CG    1 
ATOM   8041  C  CD    . ARG C 2 278 ? 138.665 108.097 153.531 1.00 85.12  ? 278  ARG L CD    1 
ATOM   8042  N  NE    . ARG C 2 278 ? 137.488 108.958 153.543 1.00 86.25  ? 278  ARG L NE    1 
ATOM   8043  C  CZ    . ARG C 2 278 ? 137.194 109.835 152.594 1.00 82.51  ? 278  ARG L CZ    1 
ATOM   8044  N  NH1   . ARG C 2 278 ? 137.967 109.989 151.531 1.00 81.00  ? 278  ARG L NH1   1 
ATOM   8045  N  NH2   . ARG C 2 278 ? 136.098 110.579 152.713 1.00 76.89  ? 278  ARG L NH2   1 
ATOM   8046  N  N     . ASP C 2 279 ? 135.343 103.948 155.482 1.00 93.57  ? 279  ASP L N     1 
ATOM   8047  C  CA    . ASP C 2 279 ? 134.879 102.565 155.411 1.00 94.76  ? 279  ASP L CA    1 
ATOM   8048  C  C     . ASP C 2 279 ? 134.052 102.316 154.155 1.00 95.36  ? 279  ASP L C     1 
ATOM   8049  O  O     . ASP C 2 279 ? 134.209 101.282 153.495 1.00 94.61  ? 279  ASP L O     1 
ATOM   8050  C  CB    . ASP C 2 279 ? 134.073 102.212 156.661 1.00 92.64  ? 279  ASP L CB    1 
ATOM   8051  C  CG    . ASP C 2 279 ? 134.954 101.929 157.862 1.00 93.77  ? 279  ASP L CG    1 
ATOM   8052  O  OD1   . ASP C 2 279 ? 136.175 102.178 157.778 1.00 95.74  ? 279  ASP L OD1   1 
ATOM   8053  O  OD2   . ASP C 2 279 ? 134.426 101.450 158.887 1.00 93.33  ? 279  ASP L OD2   1 
ATOM   8054  N  N     . SER C 2 280 ? 133.169 103.248 153.808 1.00 93.61  ? 280  SER L N     1 
ATOM   8055  C  CA    . SER C 2 280 ? 132.314 103.115 152.639 1.00 93.20  ? 280  SER L CA    1 
ATOM   8056  C  C     . SER C 2 280 ? 132.386 104.386 151.808 1.00 95.70  ? 280  SER L C     1 
ATOM   8057  O  O     . SER C 2 280 ? 132.571 105.484 152.338 1.00 96.30  ? 280  SER L O     1 
ATOM   8058  C  CB    . SER C 2 280 ? 130.859 102.829 153.034 1.00 93.78  ? 280  SER L CB    1 
ATOM   8059  O  OG    . SER C 2 280 ? 130.749 101.594 153.721 1.00 93.83  ? 280  SER L OG    1 
ATOM   8060  N  N     . LYS C 2 281 ? 132.231 104.225 150.491 1.00 91.12  ? 281  LYS L N     1 
ATOM   8061  C  CA    . LYS C 2 281 ? 132.339 105.361 149.583 1.00 89.40  ? 281  LYS L CA    1 
ATOM   8062  C  C     . LYS C 2 281 ? 131.126 106.279 149.644 1.00 89.84  ? 281  LYS L C     1 
ATOM   8063  O  O     . LYS C 2 281 ? 131.222 107.434 149.216 1.00 87.55  ? 281  LYS L O     1 
ATOM   8064  C  CB    . LYS C 2 281 ? 132.547 104.872 148.149 1.00 84.67  ? 281  LYS L CB    1 
ATOM   8065  C  CG    . LYS C 2 281 ? 133.826 104.078 147.951 1.00 86.63  ? 281  LYS L CG    1 
ATOM   8066  C  CD    . LYS C 2 281 ? 134.014 103.679 146.499 1.00 88.89  ? 281  LYS L CD    1 
ATOM   8067  C  CE    . LYS C 2 281 ? 135.294 102.881 146.311 1.00 88.50  ? 281  LYS L CE    1 
ATOM   8068  N  NZ    . LYS C 2 281 ? 135.499 102.483 144.892 1.00 89.80  ? 281  LYS L NZ    1 
ATOM   8069  N  N     . MET C 2 282 ? 129.991 105.798 150.158 1.00 90.75  ? 282  MET L N     1 
ATOM   8070  C  CA    . MET C 2 282 ? 128.822 106.661 150.285 1.00 87.89  ? 282  MET L CA    1 
ATOM   8071  C  C     . MET C 2 282 ? 129.101 107.821 151.229 1.00 86.38  ? 282  MET L C     1 
ATOM   8072  O  O     . MET C 2 282 ? 128.747 108.969 150.940 1.00 89.23  ? 282  MET L O     1 
ATOM   8073  C  CB    . MET C 2 282 ? 127.618 105.858 150.779 1.00 90.50  ? 282  MET L CB    1 
ATOM   8074  C  CG    . MET C 2 282 ? 126.305 106.210 150.095 1.00 91.27  ? 282  MET L CG    1 
ATOM   8075  S  SD    . MET C 2 282 ? 125.839 107.945 150.244 1.00 95.97  ? 282  MET L SD    1 
ATOM   8076  C  CE    . MET C 2 282 ? 125.715 108.115 152.020 1.00 90.79  ? 282  MET L CE    1 
ATOM   8077  N  N     . THR C 2 283 ? 129.738 107.539 152.365 1.00 86.16  ? 283  THR L N     1 
ATOM   8078  C  CA    . THR C 2 283 ? 130.039 108.585 153.332 1.00 90.57  ? 283  THR L CA    1 
ATOM   8079  C  C     . THR C 2 283 ? 131.207 109.454 152.881 1.00 88.17  ? 283  THR L C     1 
ATOM   8080  O  O     . THR C 2 283 ? 131.404 110.546 153.425 1.00 90.37  ? 283  THR L O     1 
ATOM   8081  C  CB    . THR C 2 283 ? 130.328 107.951 154.696 1.00 91.16  ? 283  THR L CB    1 
ATOM   8082  O  OG1   . THR C 2 283 ? 129.312 106.986 154.993 1.00 89.29  ? 283  THR L OG1   1 
ATOM   8083  C  CG2   . THR C 2 283 ? 130.315 108.999 155.797 1.00 88.20  ? 283  THR L CG2   1 
ATOM   8084  N  N     . ARG C 2 284 ? 131.969 109.008 151.881 1.00 78.31  ? 284  ARG L N     1 
ATOM   8085  C  CA    . ARG C 2 284 ? 133.140 109.754 151.437 1.00 79.70  ? 284  ARG L CA    1 
ATOM   8086  C  C     . ARG C 2 284 ? 132.788 110.997 150.631 1.00 83.07  ? 284  ARG L C     1 
ATOM   8087  O  O     . ARG C 2 284 ? 133.680 111.808 150.364 1.00 88.17  ? 284  ARG L O     1 
ATOM   8088  C  CB    . ARG C 2 284 ? 134.058 108.848 150.615 1.00 83.69  ? 284  ARG L CB    1 
ATOM   8089  C  CG    . ARG C 2 284 ? 134.673 107.708 151.409 1.00 86.35  ? 284  ARG L CG    1 
ATOM   8090  C  CD    . ARG C 2 284 ? 135.720 106.965 150.595 1.00 84.64  ? 284  ARG L CD    1 
ATOM   8091  N  NE    . ARG C 2 284 ? 136.328 105.876 151.350 1.00 84.86  ? 284  ARG L NE    1 
ATOM   8092  C  CZ    . ARG C 2 284 ? 137.353 105.150 150.925 1.00 85.98  ? 284  ARG L CZ    1 
ATOM   8093  N  NH1   . ARG C 2 284 ? 137.913 105.369 149.746 1.00 85.95  ? 284  ARG L NH1   1 
ATOM   8094  N  NH2   . ARG C 2 284 ? 137.829 104.181 151.701 1.00 84.92  ? 284  ARG L NH2   1 
ATOM   8095  N  N     . ILE C 2 285 ? 131.530 111.166 150.236 1.00 74.26  ? 285  ILE L N     1 
ATOM   8096  C  CA    . ILE C 2 285 ? 131.100 112.342 149.493 1.00 71.41  ? 285  ILE L CA    1 
ATOM   8097  C  C     . ILE C 2 285 ? 130.432 113.367 150.401 1.00 73.66  ? 285  ILE L C     1 
ATOM   8098  O  O     . ILE C 2 285 ? 130.630 114.571 150.233 1.00 77.17  ? 285  ILE L O     1 
ATOM   8099  C  CB    . ILE C 2 285 ? 130.165 111.924 148.338 1.00 72.95  ? 285  ILE L CB    1 
ATOM   8100  C  CG1   . ILE C 2 285 ? 130.914 111.032 147.349 1.00 73.83  ? 285  ILE L CG1   1 
ATOM   8101  C  CG2   . ILE C 2 285 ? 129.603 113.145 147.626 1.00 74.76  ? 285  ILE L CG2   1 
ATOM   8102  C  CD1   . ILE C 2 285 ? 132.087 111.713 146.693 1.00 74.37  ? 285  ILE L CD1   1 
ATOM   8103  N  N     . LEU C 2 286 ? 129.652 112.907 151.380 1.00 61.88  ? 286  LEU L N     1 
ATOM   8104  C  CA    . LEU C 2 286 ? 128.955 113.781 152.315 1.00 56.15  ? 286  LEU L CA    1 
ATOM   8105  C  C     . LEU C 2 286 ? 129.752 114.015 153.594 1.00 61.51  ? 286  LEU L C     1 
ATOM   8106  O  O     . LEU C 2 286 ? 129.163 114.240 154.657 1.00 63.56  ? 286  LEU L O     1 
ATOM   8107  C  CB    . LEU C 2 286 ? 127.581 113.205 152.651 1.00 54.16  ? 286  LEU L CB    1 
ATOM   8108  C  CG    . LEU C 2 286 ? 126.657 112.930 151.467 1.00 61.39  ? 286  LEU L CG    1 
ATOM   8109  C  CD1   . LEU C 2 286 ? 125.369 112.281 151.943 1.00 63.17  ? 286  LEU L CD1   1 
ATOM   8110  C  CD2   . LEU C 2 286 ? 126.368 114.215 150.711 1.00 63.51  ? 286  LEU L CD2   1 
ATOM   8111  N  N     . GLN C 2 287 ? 131.084 113.961 153.513 1.00 64.75  ? 287  GLN L N     1 
ATOM   8112  C  CA    . GLN C 2 287 ? 131.903 114.112 154.711 1.00 65.55  ? 287  GLN L CA    1 
ATOM   8113  C  C     . GLN C 2 287 ? 131.762 115.508 155.312 1.00 65.24  ? 287  GLN L C     1 
ATOM   8114  O  O     . GLN C 2 287 ? 131.741 115.659 156.539 1.00 61.37  ? 287  GLN L O     1 
ATOM   8115  C  CB    . GLN C 2 287 ? 133.365 113.789 154.396 1.00 56.38  ? 287  GLN L CB    1 
ATOM   8116  C  CG    . GLN C 2 287 ? 134.126 114.876 153.662 1.00 58.62  ? 287  GLN L CG    1 
ATOM   8117  C  CD    . GLN C 2 287 ? 133.531 115.196 152.307 1.00 62.90  ? 287  GLN L CD    1 
ATOM   8118  O  OE1   . GLN C 2 287 ? 133.147 114.299 151.558 1.00 68.23  ? 287  GLN L OE1   1 
ATOM   8119  N  NE2   . GLN C 2 287 ? 133.444 116.481 151.987 1.00 61.48  ? 287  GLN L NE2   1 
ATOM   8120  N  N     . ASP C 2 288 ? 131.665 116.540 154.471 1.00 55.66  ? 288  ASP L N     1 
ATOM   8121  C  CA    . ASP C 2 288 ? 131.391 117.881 154.970 1.00 54.10  ? 288  ASP L CA    1 
ATOM   8122  C  C     . ASP C 2 288 ? 129.927 118.071 155.336 1.00 52.93  ? 288  ASP L C     1 
ATOM   8123  O  O     . ASP C 2 288 ? 129.610 118.961 156.132 1.00 52.73  ? 288  ASP L O     1 
ATOM   8124  C  CB    . ASP C 2 288 ? 131.807 118.933 153.942 1.00 54.31  ? 288  ASP L CB    1 
ATOM   8125  C  CG    . ASP C 2 288 ? 133.236 119.397 154.134 0.00 53.68  ? 288  ASP L CG    1 
ATOM   8126  O  OD1   . ASP C 2 288 ? 133.730 119.340 155.278 1.00 54.57  ? 288  ASP L OD1   1 
ATOM   8127  O  OD2   . ASP C 2 288 ? 133.862 119.828 153.144 1.00 55.29  ? 288  ASP L OD2   1 
ATOM   8128  N  N     . SER C 2 289 ? 129.032 117.265 154.767 1.00 51.30  ? 289  SER L N     1 
ATOM   8129  C  CA    . SER C 2 289 ? 127.639 117.301 155.193 1.00 52.59  ? 289  SER L CA    1 
ATOM   8130  C  C     . SER C 2 289 ? 127.477 116.692 156.579 1.00 57.94  ? 289  SER L C     1 
ATOM   8131  O  O     . SER C 2 289 ? 126.640 117.144 157.369 1.00 63.68  ? 289  SER L O     1 
ATOM   8132  C  CB    . SER C 2 289 ? 126.761 116.571 154.178 1.00 58.74  ? 289  SER L CB    1 
ATOM   8133  O  OG    . SER C 2 289 ? 126.904 117.132 152.884 1.00 58.52  ? 289  SER L OG    1 
ATOM   8134  N  N     . LEU C 2 290 ? 128.269 115.664 156.893 1.00 46.02  ? 290  LEU L N     1 
ATOM   8135  C  CA    . LEU C 2 290 ? 128.119 114.986 158.175 1.00 42.32  ? 290  LEU L CA    1 
ATOM   8136  C  C     . LEU C 2 290 ? 128.634 115.840 159.328 1.00 42.84  ? 290  LEU L C     1 
ATOM   8137  O  O     . LEU C 2 290 ? 127.977 115.941 160.370 1.00 53.85  ? 290  LEU L O     1 
ATOM   8138  C  CB    . LEU C 2 290 ? 128.835 113.637 158.140 1.00 49.51  ? 290  LEU L CB    1 
ATOM   8139  C  CG    . LEU C 2 290 ? 127.936 112.413 157.955 1.00 55.48  ? 290  LEU L CG    1 
ATOM   8140  C  CD1   . LEU C 2 290 ? 126.990 112.259 159.136 1.00 50.66  ? 290  LEU L CD1   1 
ATOM   8141  C  CD2   . LEU C 2 290 ? 127.157 112.505 156.652 1.00 52.14  ? 290  LEU L CD2   1 
ATOM   8142  N  N     . GLY C 2 291 ? 129.809 116.447 159.178 1.00 32.79  ? 291  GLY L N     1 
ATOM   8143  C  CA    . GLY C 2 291 ? 130.344 117.263 160.251 1.00 37.52  ? 291  GLY L CA    1 
ATOM   8144  C  C     . GLY C 2 291 ? 131.126 118.490 159.828 1.00 35.53  ? 291  GLY L C     1 
ATOM   8145  O  O     . GLY C 2 291 ? 131.696 119.184 160.675 1.00 31.47  ? 291  GLY L O     1 
ATOM   8146  N  N     . GLY C 2 292 ? 131.169 118.772 158.531 1.00 42.67  ? 292  GLY L N     1 
ATOM   8147  C  CA    . GLY C 2 292 ? 132.047 119.782 157.987 1.00 42.06  ? 292  GLY L CA    1 
ATOM   8148  C  C     . GLY C 2 292 ? 131.388 121.136 157.826 1.00 45.88  ? 292  GLY L C     1 
ATOM   8149  O  O     . GLY C 2 292 ? 130.351 121.436 158.429 1.00 53.45  ? 292  GLY L O     1 
ATOM   8150  N  N     . ASN C 2 293 ? 132.011 121.970 156.992 1.00 46.02  ? 293  ASN L N     1 
ATOM   8151  C  CA    . ASN C 2 293 ? 131.556 123.337 156.735 1.00 39.06  ? 293  ASN L CA    1 
ATOM   8152  C  C     . ASN C 2 293 ? 130.342 123.296 155.805 1.00 26.58  ? 293  ASN L C     1 
ATOM   8153  O  O     . ASN C 2 293 ? 130.400 123.626 154.619 1.00 35.94  ? 293  ASN L O     1 
ATOM   8154  C  CB    . ASN C 2 293 ? 132.696 124.163 156.151 1.00 36.20  ? 293  ASN L CB    1 
ATOM   8155  C  CG    . ASN C 2 293 ? 132.287 125.586 155.823 1.00 34.68  ? 293  ASN L CG    1 
ATOM   8156  O  OD1   . ASN C 2 293 ? 131.261 126.076 156.290 1.00 39.05  ? 293  ASN L OD1   1 
ATOM   8157  N  ND2   . ASN C 2 293 ? 133.095 126.257 155.013 1.00 37.44  ? 293  ASN L ND2   1 
ATOM   8158  N  N     . CYS C 2 294 ? 129.216 122.875 156.378 1.00 19.64  ? 294  CYS L N     1 
ATOM   8159  C  CA    . CYS C 2 294 ? 127.980 122.729 155.623 1.00 29.37  ? 294  CYS L CA    1 
ATOM   8160  C  C     . CYS C 2 294 ? 126.793 122.577 156.563 1.00 28.27  ? 294  CYS L C     1 
ATOM   8161  O  O     . CYS C 2 294 ? 126.815 121.735 157.466 1.00 35.40  ? 294  CYS L O     1 
ATOM   8162  C  CB    . CYS C 2 294 ? 128.073 121.525 154.682 1.00 40.35  ? 294  CYS L CB    1 
ATOM   8163  S  SG    . CYS C 2 294 ? 126.566 121.156 153.761 1.00 42.13  ? 294  CYS L SG    1 
ATOM   8164  N  N     . ARG C 2 295 ? 125.754 123.382 156.365 1.00 32.16  ? 295  ARG L N     1 
ATOM   8165  C  CA    . ARG C 2 295 ? 124.540 123.276 157.161 1.00 25.89  ? 295  ARG L CA    1 
ATOM   8166  C  C     . ARG C 2 295 ? 123.565 122.331 156.475 1.00 28.50  ? 295  ARG L C     1 
ATOM   8167  O  O     . ARG C 2 295 ? 123.165 122.563 155.330 1.00 41.52  ? 295  ARG L O     1 
ATOM   8168  C  CB    . ARG C 2 295 ? 123.901 124.648 157.365 1.00 21.34  ? 295  ARG L CB    1 
ATOM   8169  C  CG    . ARG C 2 295 ? 124.057 125.580 156.192 1.00 28.89  ? 295  ARG L CG    1 
ATOM   8170  C  CD    . ARG C 2 295 ? 123.328 126.874 156.451 1.00 26.62  ? 295  ARG L CD    1 
ATOM   8171  N  NE    . ARG C 2 295 ? 123.438 127.293 157.842 1.00 28.47  ? 295  ARG L NE    1 
ATOM   8172  C  CZ    . ARG C 2 295 ? 124.422 128.038 158.324 1.00 40.24  ? 295  ARG L CZ    1 
ATOM   8173  N  NH1   . ARG C 2 295 ? 125.396 128.482 157.548 1.00 41.44  ? 295  ARG L NH1   1 
ATOM   8174  N  NH2   . ARG C 2 295 ? 124.426 128.350 159.617 1.00 41.74  ? 295  ARG L NH2   1 
ATOM   8175  N  N     . THR C 2 296 ? 123.187 121.266 157.177 1.00 17.54  ? 296  THR L N     1 
ATOM   8176  C  CA    . THR C 2 296 ? 122.415 120.183 156.592 1.00 19.53  ? 296  THR L CA    1 
ATOM   8177  C  C     . THR C 2 296 ? 121.171 119.914 157.423 1.00 19.49  ? 296  THR L C     1 
ATOM   8178  O  O     . THR C 2 296 ? 121.138 120.180 158.627 1.00 38.22  ? 296  THR L O     1 
ATOM   8179  C  CB    . THR C 2 296 ? 123.240 118.895 156.498 1.00 37.02  ? 296  THR L CB    1 
ATOM   8180  O  OG1   . THR C 2 296 ? 123.358 118.312 157.798 1.00 40.22  ? 296  THR L OG1   1 
ATOM   8181  C  CG2   . THR C 2 296 ? 124.629 119.194 155.983 1.00 27.28  ? 296  THR L CG2   1 
ATOM   8182  N  N     . THR C 2 297 ? 120.145 119.383 156.763 1.00 24.00  ? 297  THR L N     1 
ATOM   8183  C  CA    . THR C 2 297 ? 118.949 118.890 157.430 1.00 41.19  ? 297  THR L CA    1 
ATOM   8184  C  C     . THR C 2 297 ? 118.666 117.477 156.942 1.00 36.87  ? 297  THR L C     1 
ATOM   8185  O  O     . THR C 2 297 ? 118.960 117.139 155.792 1.00 41.96  ? 297  THR L O     1 
ATOM   8186  C  CB    . THR C 2 297 ? 117.723 119.781 157.173 1.00 46.53  ? 297  THR L CB    1 
ATOM   8187  O  OG1   . THR C 2 297 ? 117.072 119.368 155.966 1.00 46.64  ? 297  THR L OG1   1 
ATOM   8188  C  CG2   . THR C 2 297 ? 118.129 121.242 157.047 1.00 43.97  ? 297  THR L CG2   1 
ATOM   8189  N  N     . ILE C 2 298 ? 118.097 116.657 157.819 1.00 46.57  ? 298  ILE L N     1 
ATOM   8190  C  CA    . ILE C 2 298 ? 117.809 115.257 157.532 1.00 46.02  ? 298  ILE L CA    1 
ATOM   8191  C  C     . ILE C 2 298 ? 116.324 115.018 157.757 1.00 49.29  ? 298  ILE L C     1 
ATOM   8192  O  O     . ILE C 2 298 ? 115.748 115.526 158.726 1.00 58.84  ? 298  ILE L O     1 
ATOM   8193  C  CB    . ILE C 2 298 ? 118.651 114.315 158.410 1.00 51.76  ? 298  ILE L CB    1 
ATOM   8194  C  CG1   . ILE C 2 298 ? 120.123 114.731 158.386 1.00 55.25  ? 298  ILE L CG1   1 
ATOM   8195  C  CG2   . ILE C 2 298 ? 118.491 112.871 157.956 1.00 50.34  ? 298  ILE L CG2   1 
ATOM   8196  C  CD1   . ILE C 2 298 ? 121.002 113.906 159.301 1.00 52.99  ? 298  ILE L CD1   1 
ATOM   8197  N  N     . VAL C 2 299 ? 115.706 114.249 156.864 1.00 41.42  ? 299  VAL L N     1 
ATOM   8198  C  CA    . VAL C 2 299 ? 114.306 113.866 156.982 1.00 47.83  ? 299  VAL L CA    1 
ATOM   8199  C  C     . VAL C 2 299 ? 114.224 112.348 157.061 1.00 35.58  ? 299  VAL L C     1 
ATOM   8200  O  O     . VAL C 2 299 ? 114.989 111.640 156.398 1.00 46.17  ? 299  VAL L O     1 
ATOM   8201  C  CB    . VAL C 2 299 ? 113.461 114.406 155.808 1.00 50.07  ? 299  VAL L CB    1 
ATOM   8202  C  CG1   . VAL C 2 299 ? 113.400 115.923 155.857 1.00 45.01  ? 299  VAL L CG1   1 
ATOM   8203  C  CG2   . VAL C 2 299 ? 114.027 113.945 154.478 1.00 48.48  ? 299  VAL L CG2   1 
ATOM   8204  N  N     . ILE C 2 300 ? 113.318 111.848 157.897 1.00 42.44  ? 300  ILE L N     1 
ATOM   8205  C  CA    . ILE C 2 300 ? 113.089 110.417 158.036 1.00 49.49  ? 300  ILE L CA    1 
ATOM   8206  C  C     . ILE C 2 300 ? 111.617 110.127 157.777 1.00 53.61  ? 300  ILE L C     1 
ATOM   8207  O  O     . ILE C 2 300 ? 110.740 110.903 158.173 1.00 60.10  ? 300  ILE L O     1 
ATOM   8208  C  CB    . ILE C 2 300 ? 113.513 109.892 159.425 1.00 55.86  ? 300  ILE L CB    1 
ATOM   8209  C  CG1   . ILE C 2 300 ? 112.814 110.673 160.538 1.00 58.39  ? 300  ILE L CG1   1 
ATOM   8210  C  CG2   . ILE C 2 300 ? 115.024 109.965 159.583 1.00 56.64  ? 300  ILE L CG2   1 
ATOM   8211  C  CD1   . ILE C 2 300 ? 113.032 110.087 161.911 1.00 58.68  ? 300  ILE L CD1   1 
ATOM   8212  N  N     . CYS C 2 301 ? 111.350 109.014 157.103 1.00 52.87  ? 301  CYS L N     1 
ATOM   8213  C  CA    . CYS C 2 301 ? 109.998 108.590 156.772 1.00 55.89  ? 301  CYS L CA    1 
ATOM   8214  C  C     . CYS C 2 301 ? 109.666 107.312 157.530 1.00 61.02  ? 301  CYS L C     1 
ATOM   8215  O  O     . CYS C 2 301 ? 110.494 106.398 157.606 1.00 60.99  ? 301  CYS L O     1 
ATOM   8216  C  CB    . CYS C 2 301 ? 109.850 108.368 155.267 1.00 58.98  ? 301  CYS L CB    1 
ATOM   8217  S  SG    . CYS C 2 301 ? 110.253 109.811 154.257 1.00 74.94  ? 301  CYS L SG    1 
ATOM   8218  N  N     . CYS C 2 302 ? 108.458 107.252 158.087 1.00 70.81  ? 302  CYS L N     1 
ATOM   8219  C  CA    . CYS C 2 302 ? 108.005 106.101 158.853 1.00 69.11  ? 302  CYS L CA    1 
ATOM   8220  C  C     . CYS C 2 302 ? 106.551 105.798 158.520 1.00 64.97  ? 302  CYS L C     1 
ATOM   8221  O  O     . CYS C 2 302 ? 105.837 106.622 157.943 1.00 62.83  ? 302  CYS L O     1 
ATOM   8222  C  CB    . CYS C 2 302 ? 108.158 106.327 160.362 1.00 69.07  ? 302  CYS L CB    1 
ATOM   8223  S  SG    . CYS C 2 302 ? 107.586 104.945 161.374 1.00 60.91  ? 302  CYS L SG    1 
ATOM   8224  N  N     . SER C 2 303 ? 106.121 104.591 158.892 1.00 71.46  ? 303  SER L N     1 
ATOM   8225  C  CA    . SER C 2 303 ? 104.783 104.098 158.612 1.00 74.76  ? 303  SER L CA    1 
ATOM   8226  C  C     . SER C 2 303 ? 104.011 103.850 159.903 1.00 77.92  ? 303  SER L C     1 
ATOM   8227  O  O     . SER C 2 303 ? 104.573 103.320 160.868 1.00 80.29  ? 303  SER L O     1 
ATOM   8228  C  CB    . SER C 2 303 ? 104.840 102.796 157.801 1.00 70.82  ? 303  SER L CB    1 
ATOM   8229  O  OG    . SER C 2 303 ? 103.555 102.217 157.661 1.00 69.80  ? 303  SER L OG    1 
ATOM   8230  N  N     . PRO C 2 304 ? 102.732 104.224 159.953 1.00 76.26  ? 304  PRO L N     1 
ATOM   8231  C  CA    . PRO C 2 304 ? 101.906 103.937 161.132 1.00 74.49  ? 304  PRO L CA    1 
ATOM   8232  C  C     . PRO C 2 304 ? 101.406 102.503 161.220 1.00 76.84  ? 304  PRO L C     1 
ATOM   8233  O  O     . PRO C 2 304 ? 100.567 102.216 162.078 1.00 67.99  ? 304  PRO L O     1 
ATOM   8234  C  CB    . PRO C 2 304 ? 100.727 104.907 160.959 1.00 69.41  ? 304  PRO L CB    1 
ATOM   8235  C  CG    . PRO C 2 304 ? 100.612 105.083 159.491 1.00 70.62  ? 304  PRO L CG    1 
ATOM   8236  C  CD    . PRO C 2 304 ? 102.009 105.020 158.945 1.00 69.65  ? 304  PRO L CD    1 
ATOM   8237  N  N     . SER C 2 305 ? 101.897 101.605 160.370 1.00 100.48 ? 305  SER L N     1 
ATOM   8238  C  CA    . SER C 2 305 ? 101.398 100.240 160.325 1.00 100.59 ? 305  SER L CA    1 
ATOM   8239  C  C     . SER C 2 305 ? 101.790 99.471  161.586 1.00 99.54  ? 305  SER L C     1 
ATOM   8240  O  O     . SER C 2 305 ? 102.680 99.868  162.344 1.00 94.25  ? 305  SER L O     1 
ATOM   8241  C  CB    . SER C 2 305 ? 101.928 99.518  159.085 1.00 96.37  ? 305  SER L CB    1 
ATOM   8242  O  OG    . SER C 2 305 ? 101.579 98.145  159.104 1.00 98.85  ? 305  SER L OG    1 
ATOM   8243  N  N     . SER C 2 306 ? 101.098 98.352  161.805 1.00 93.08  ? 306  SER L N     1 
ATOM   8244  C  CA    . SER C 2 306 ? 101.334 97.511  162.971 1.00 87.94  ? 306  SER L CA    1 
ATOM   8245  C  C     . SER C 2 306 ? 102.144 96.259  162.662 1.00 92.64  ? 306  SER L C     1 
ATOM   8246  O  O     . SER C 2 306 ? 102.734 95.682  163.582 1.00 93.52  ? 306  SER L O     1 
ATOM   8247  C  CB    . SER C 2 306 ? 100.001 97.099  163.603 1.00 83.34  ? 306  SER L CB    1 
ATOM   8248  O  OG    . SER C 2 306 ? 99.163  96.462  162.656 1.00 84.69  ? 306  SER L OG    1 
ATOM   8249  N  N     . TYR C 2 307 ? 102.185 95.824  161.401 1.00 96.60  ? 307  TYR L N     1 
ATOM   8250  C  CA    . TYR C 2 307 ? 102.958 94.642  161.036 1.00 96.74  ? 307  TYR L CA    1 
ATOM   8251  C  C     . TYR C 2 307 ? 104.460 94.905  161.058 1.00 93.48  ? 307  TYR L C     1 
ATOM   8252  O  O     . TYR C 2 307 ? 105.244 93.953  161.140 1.00 92.28  ? 307  TYR L O     1 
ATOM   8253  C  CB    . TYR C 2 307 ? 102.516 94.146  159.653 1.00 97.28  ? 307  TYR L CB    1 
ATOM   8254  C  CG    . TYR C 2 307 ? 103.487 93.212  158.962 1.00 98.20  ? 307  TYR L CG    1 
ATOM   8255  C  CD1   . TYR C 2 307 ? 103.637 91.895  159.382 1.00 96.62  ? 307  TYR L CD1   1 
ATOM   8256  C  CD2   . TYR C 2 307 ? 104.249 93.645  157.884 1.00 95.50  ? 307  TYR L CD2   1 
ATOM   8257  C  CE1   . TYR C 2 307 ? 104.523 91.039  158.751 1.00 95.02  ? 307  TYR L CE1   1 
ATOM   8258  C  CE2   . TYR C 2 307 ? 105.136 92.797  157.246 1.00 94.88  ? 307  TYR L CE2   1 
ATOM   8259  C  CZ    . TYR C 2 307 ? 105.269 91.496  157.683 1.00 95.26  ? 307  TYR L CZ    1 
ATOM   8260  O  OH    . TYR C 2 307 ? 106.151 90.650  157.050 1.00 94.48  ? 307  TYR L OH    1 
ATOM   8261  N  N     . ASN C 2 308 ? 104.875 96.168  161.020 1.00 69.99  ? 308  ASN L N     1 
ATOM   8262  C  CA    . ASN C 2 308 ? 106.279 96.543  160.901 1.00 70.87  ? 308  ASN L CA    1 
ATOM   8263  C  C     . ASN C 2 308 ? 106.778 97.277  162.142 1.00 72.70  ? 308  ASN L C     1 
ATOM   8264  O  O     . ASN C 2 308 ? 107.489 98.278  162.044 1.00 73.48  ? 308  ASN L O     1 
ATOM   8265  C  CB    . ASN C 2 308 ? 106.494 97.397  159.657 1.00 70.56  ? 308  ASN L CB    1 
ATOM   8266  C  CG    . ASN C 2 308 ? 105.696 98.678  159.694 1.00 66.68  ? 308  ASN L CG    1 
ATOM   8267  O  OD1   . ASN C 2 308 ? 104.765 98.815  160.484 1.00 63.73  ? 308  ASN L OD1   1 
ATOM   8268  N  ND2   . ASN C 2 308 ? 106.053 99.624  158.835 1.00 72.45  ? 308  ASN L ND2   1 
ATOM   8269  N  N     . GLU C 2 309 ? 106.413 96.784  163.327 1.00 81.84  ? 309  GLU L N     1 
ATOM   8270  C  CA    . GLU C 2 309 ? 106.830 97.449  164.557 1.00 81.95  ? 309  GLU L CA    1 
ATOM   8271  C  C     . GLU C 2 309 ? 108.344 97.413  164.741 1.00 81.82  ? 309  GLU L C     1 
ATOM   8272  O  O     . GLU C 2 309 ? 108.931 98.386  165.228 1.00 75.04  ? 309  GLU L O     1 
ATOM   8273  C  CB    . GLU C 2 309 ? 106.119 96.825  165.763 1.00 81.44  ? 309  GLU L CB    1 
ATOM   8274  C  CG    . GLU C 2 309 ? 106.603 95.436  166.164 1.00 82.33  ? 309  GLU L CG    1 
ATOM   8275  C  CD    . GLU C 2 309 ? 106.076 94.343  165.253 1.00 84.66  ? 309  GLU L CD    1 
ATOM   8276  O  OE1   . GLU C 2 309 ? 105.200 94.637  164.414 1.00 81.27  ? 309  GLU L OE1   1 
ATOM   8277  O  OE2   . GLU C 2 309 ? 106.541 93.190  165.377 1.00 87.44  ? 309  GLU L OE2   1 
ATOM   8278  N  N     . SER C 2 310 ? 108.995 96.314  164.349 1.00 91.37  ? 310  SER L N     1 
ATOM   8279  C  CA    . SER C 2 310 ? 110.426 96.169  164.601 1.00 89.36  ? 310  SER L CA    1 
ATOM   8280  C  C     . SER C 2 310 ? 111.244 97.139  163.755 1.00 88.56  ? 310  SER L C     1 
ATOM   8281  O  O     . SER C 2 310 ? 112.127 97.834  164.271 1.00 86.94  ? 310  SER L O     1 
ATOM   8282  C  CB    . SER C 2 310 ? 110.859 94.726  164.335 1.00 85.58  ? 310  SER L CB    1 
ATOM   8283  O  OG    . SER C 2 310 ? 110.186 93.823  165.195 1.00 83.56  ? 310  SER L OG    1 
ATOM   8284  N  N     . GLU C 2 311 ? 110.965 97.201  162.451 1.00 82.52  ? 311  GLU L N     1 
ATOM   8285  C  CA    . GLU C 2 311 ? 111.763 98.037  161.561 1.00 77.09  ? 311  GLU L CA    1 
ATOM   8286  C  C     . GLU C 2 311 ? 111.445 99.519  161.711 1.00 73.18  ? 311  GLU L C     1 
ATOM   8287  O  O     . GLU C 2 311 ? 112.259 100.358 161.310 1.00 73.24  ? 311  GLU L O     1 
ATOM   8288  C  CB    . GLU C 2 311 ? 111.558 97.609  160.106 1.00 75.65  ? 311  GLU L CB    1 
ATOM   8289  C  CG    . GLU C 2 311 ? 111.774 96.123  159.851 1.00 76.71  ? 311  GLU L CG    1 
ATOM   8290  C  CD    . GLU C 2 311 ? 110.488 95.321  159.939 1.00 75.08  ? 311  GLU L CD    1 
ATOM   8291  O  OE1   . GLU C 2 311 ? 109.404 95.937  159.959 1.00 73.17  ? 311  GLU L OE1   1 
ATOM   8292  O  OE2   . GLU C 2 311 ? 110.561 94.076  159.990 1.00 72.87  ? 311  GLU L OE2   1 
ATOM   8293  N  N     . THR C 2 312 ? 110.285 99.859  162.277 1.00 66.18  ? 312  THR L N     1 
ATOM   8294  C  CA    . THR C 2 312 ? 109.910 101.262 162.409 1.00 70.13  ? 312  THR L CA    1 
ATOM   8295  C  C     . THR C 2 312 ? 110.699 101.950 163.516 1.00 70.63  ? 312  THR L C     1 
ATOM   8296  O  O     . THR C 2 312 ? 111.053 103.128 163.394 1.00 64.18  ? 312  THR L O     1 
ATOM   8297  C  CB    . THR C 2 312 ? 108.411 101.378 162.669 1.00 72.15  ? 312  THR L CB    1 
ATOM   8298  O  OG1   . THR C 2 312 ? 107.987 100.288 163.496 1.00 66.04  ? 312  THR L OG1   1 
ATOM   8299  C  CG2   . THR C 2 312 ? 107.641 101.350 161.357 1.00 73.19  ? 312  THR L CG2   1 
ATOM   8300  N  N     . LYS C 2 313 ? 110.976 101.234 164.609 1.00 77.42  ? 313  LYS L N     1 
ATOM   8301  C  CA    . LYS C 2 313 ? 111.710 101.833 165.719 1.00 74.66  ? 313  LYS L CA    1 
ATOM   8302  C  C     . LYS C 2 313 ? 113.148 102.157 165.338 1.00 70.40  ? 313  LYS L C     1 
ATOM   8303  O  O     . LYS C 2 313 ? 113.722 103.119 165.861 1.00 71.15  ? 313  LYS L O     1 
ATOM   8304  C  CB    . LYS C 2 313 ? 111.685 100.902 166.931 1.00 75.48  ? 313  LYS L CB    1 
ATOM   8305  C  CG    . LYS C 2 313 ? 110.292 100.596 167.458 1.00 76.07  ? 313  LYS L CG    1 
ATOM   8306  C  CD    . LYS C 2 313 ? 110.354 100.004 168.858 1.00 76.46  ? 313  LYS L CD    1 
ATOM   8307  C  CE    . LYS C 2 313 ? 111.245 98.772  168.900 1.00 74.41  ? 313  LYS L CE    1 
ATOM   8308  N  NZ    . LYS C 2 313 ? 111.376 98.227  170.279 1.00 74.19  ? 313  LYS L NZ    1 
ATOM   8309  N  N     . SER C 2 314 ? 113.746 101.369 164.441 1.00 66.22  ? 314  SER L N     1 
ATOM   8310  C  CA    . SER C 2 314 ? 115.140 101.591 164.071 1.00 66.80  ? 314  SER L CA    1 
ATOM   8311  C  C     . SER C 2 314 ? 115.334 102.952 163.414 1.00 71.01  ? 314  SER L C     1 
ATOM   8312  O  O     . SER C 2 314 ? 116.302 103.661 163.712 1.00 71.37  ? 314  SER L O     1 
ATOM   8313  C  CB    . SER C 2 314 ? 115.619 100.474 163.145 1.00 70.58  ? 314  SER L CB    1 
ATOM   8314  O  OG    . SER C 2 314 ? 114.834 100.418 161.967 1.00 73.90  ? 314  SER L OG    1 
ATOM   8315  N  N     . THR C 2 315 ? 114.426 103.334 162.513 1.00 70.34  ? 315  THR L N     1 
ATOM   8316  C  CA    . THR C 2 315 ? 114.533 104.636 161.863 1.00 64.58  ? 315  THR L CA    1 
ATOM   8317  C  C     . THR C 2 315 ? 114.225 105.772 162.830 1.00 58.05  ? 315  THR L C     1 
ATOM   8318  O  O     . THR C 2 315 ? 114.778 106.869 162.695 1.00 48.81  ? 315  THR L O     1 
ATOM   8319  C  CB    . THR C 2 315 ? 113.599 104.699 160.655 1.00 58.91  ? 315  THR L CB    1 
ATOM   8320  O  OG1   . THR C 2 315 ? 113.715 103.490 159.897 1.00 56.37  ? 315  THR L OG1   1 
ATOM   8321  C  CG2   . THR C 2 315 ? 113.957 105.873 159.764 1.00 61.31  ? 315  THR L CG2   1 
ATOM   8322  N  N     . LEU C 2 316 ? 113.345 105.530 163.804 1.00 63.66  ? 316  LEU L N     1 
ATOM   8323  C  CA    . LEU C 2 316 ? 113.017 106.559 164.783 1.00 66.43  ? 316  LEU L CA    1 
ATOM   8324  C  C     . LEU C 2 316 ? 114.231 106.911 165.636 1.00 68.72  ? 316  LEU L C     1 
ATOM   8325  O  O     . LEU C 2 316 ? 114.527 108.090 165.859 1.00 75.25  ? 316  LEU L O     1 
ATOM   8326  C  CB    . LEU C 2 316 ? 111.854 106.091 165.660 1.00 69.19  ? 316  LEU L CB    1 
ATOM   8327  C  CG    . LEU C 2 316 ? 110.438 106.514 165.258 1.00 73.62  ? 316  LEU L CG    1 
ATOM   8328  C  CD1   . LEU C 2 316 ? 110.219 107.992 165.534 1.00 71.24  ? 316  LEU L CD1   1 
ATOM   8329  C  CD2   . LEU C 2 316 ? 110.154 106.196 163.797 1.00 74.44  ? 316  LEU L CD2   1 
ATOM   8330  N  N     . LEU C 2 317 ? 114.949 105.896 166.120 1.00 71.82  ? 317  LEU L N     1 
ATOM   8331  C  CA    . LEU C 2 317 ? 116.148 106.153 166.911 1.00 75.34  ? 317  LEU L CA    1 
ATOM   8332  C  C     . LEU C 2 317 ? 117.237 106.815 166.078 1.00 76.85  ? 317  LEU L C     1 
ATOM   8333  O  O     . LEU C 2 317 ? 118.077 107.542 166.621 1.00 75.11  ? 317  LEU L O     1 
ATOM   8334  C  CB    . LEU C 2 317 ? 116.667 104.851 167.522 1.00 75.53  ? 317  LEU L CB    1 
ATOM   8335  C  CG    . LEU C 2 317 ? 115.770 104.161 168.551 1.00 75.34  ? 317  LEU L CG    1 
ATOM   8336  C  CD1   . LEU C 2 317 ? 116.359 102.822 168.964 1.00 74.78  ? 317  LEU L CD1   1 
ATOM   8337  C  CD2   . LEU C 2 317 ? 115.571 105.055 169.764 1.00 76.92  ? 317  LEU L CD2   1 
ATOM   8338  N  N     . PHE C 2 318 ? 117.240 106.575 164.765 1.00 77.90  ? 318  PHE L N     1 
ATOM   8339  C  CA    . PHE C 2 318 ? 118.245 107.179 163.897 1.00 74.43  ? 318  PHE L CA    1 
ATOM   8340  C  C     . PHE C 2 318 ? 118.148 108.699 163.919 1.00 68.89  ? 318  PHE L C     1 
ATOM   8341  O  O     . PHE C 2 318 ? 119.165 109.393 164.018 1.00 67.46  ? 318  PHE L O     1 
ATOM   8342  C  CB    . PHE C 2 318 ? 118.078 106.647 162.473 1.00 79.49  ? 318  PHE L CB    1 
ATOM   8343  C  CG    . PHE C 2 318 ? 119.280 106.853 161.597 1.00 80.49  ? 318  PHE L CG    1 
ATOM   8344  C  CD1   . PHE C 2 318 ? 119.497 108.065 160.965 1.00 80.37  ? 318  PHE L CD1   1 
ATOM   8345  C  CD2   . PHE C 2 318 ? 120.185 105.824 161.392 1.00 79.15  ? 318  PHE L CD2   1 
ATOM   8346  C  CE1   . PHE C 2 318 ? 120.599 108.252 160.154 1.00 78.58  ? 318  PHE L CE1   1 
ATOM   8347  C  CE2   . PHE C 2 318 ? 121.285 106.003 160.578 1.00 76.46  ? 318  PHE L CE2   1 
ATOM   8348  C  CZ    . PHE C 2 318 ? 121.494 107.220 159.962 1.00 76.92  ? 318  PHE L CZ    1 
ATOM   8349  N  N     . GLY C 2 319 ? 116.929 109.232 163.834 1.00 73.02  ? 319  GLY L N     1 
ATOM   8350  C  CA    . GLY C 2 319 ? 116.760 110.675 163.857 1.00 80.59  ? 319  GLY L CA    1 
ATOM   8351  C  C     . GLY C 2 319 ? 117.126 111.294 165.192 1.00 83.91  ? 319  GLY L C     1 
ATOM   8352  O  O     . GLY C 2 319 ? 117.666 112.402 165.245 1.00 82.69  ? 319  GLY L O     1 
ATOM   8353  N  N     . GLN C 2 320 ? 116.823 110.596 166.290 1.00 84.23  ? 320  GLN L N     1 
ATOM   8354  C  CA    . GLN C 2 320 ? 117.156 111.117 167.612 1.00 83.36  ? 320  GLN L CA    1 
ATOM   8355  C  C     . GLN C 2 320 ? 118.663 111.254 167.789 1.00 81.63  ? 320  GLN L C     1 
ATOM   8356  O  O     . GLN C 2 320 ? 119.144 112.259 168.326 1.00 82.63  ? 320  GLN L O     1 
ATOM   8357  C  CB    . GLN C 2 320 ? 116.567 110.211 168.695 1.00 85.26  ? 320  GLN L CB    1 
ATOM   8358  C  CG    . GLN C 2 320 ? 117.046 110.526 170.105 1.00 82.68  ? 320  GLN L CG    1 
ATOM   8359  C  CD    . GLN C 2 320 ? 116.601 111.894 170.585 1.00 82.57  ? 320  GLN L CD    1 
ATOM   8360  O  OE1   . GLN C 2 320 ? 115.595 112.432 170.121 1.00 84.65  ? 320  GLN L OE1   1 
ATOM   8361  N  NE2   . GLN C 2 320 ? 117.351 112.465 171.521 1.00 82.27  ? 320  GLN L NE2   1 
ATOM   8362  N  N     . ARG C 2 321 ? 119.425 110.255 167.341 1.00 68.52  ? 321  ARG L N     1 
ATOM   8363  C  CA    . ARG C 2 321 ? 120.876 110.320 167.475 1.00 71.18  ? 321  ARG L CA    1 
ATOM   8364  C  C     . ARG C 2 321 ? 121.484 111.345 166.528 1.00 71.58  ? 321  ARG L C     1 
ATOM   8365  O  O     . ARG C 2 321 ? 122.497 111.969 166.863 1.00 74.11  ? 321  ARG L O     1 
ATOM   8366  C  CB    . ARG C 2 321 ? 121.488 108.942 167.228 1.00 72.74  ? 321  ARG L CB    1 
ATOM   8367  C  CG    . ARG C 2 321 ? 120.946 107.852 168.136 1.00 72.25  ? 321  ARG L CG    1 
ATOM   8368  C  CD    . ARG C 2 321 ? 121.489 106.490 167.743 1.00 73.89  ? 321  ARG L CD    1 
ATOM   8369  N  NE    . ARG C 2 321 ? 122.919 106.378 168.004 1.00 73.92  ? 321  ARG L NE    1 
ATOM   8370  C  CZ    . ARG C 2 321 ? 123.638 105.288 167.777 1.00 73.25  ? 321  ARG L CZ    1 
ATOM   8371  N  NH1   . ARG C 2 321 ? 123.095 104.195 167.267 1.00 71.85  ? 321  ARG L NH1   1 
ATOM   8372  N  NH2   . ARG C 2 321 ? 124.935 105.294 168.070 1.00 72.65  ? 321  ARG L NH2   1 
ATOM   8373  N  N     . ALA C 2 322 ? 120.891 111.528 165.347 1.00 54.09  ? 322  ALA L N     1 
ATOM   8374  C  CA    . ALA C 2 322 ? 121.445 112.455 164.368 1.00 48.27  ? 322  ALA L CA    1 
ATOM   8375  C  C     . ALA C 2 322 ? 121.399 113.899 164.844 1.00 45.98  ? 322  ALA L C     1 
ATOM   8376  O  O     . ALA C 2 322 ? 122.189 114.718 164.369 1.00 53.10  ? 322  ALA L O     1 
ATOM   8377  C  CB    . ALA C 2 322 ? 120.704 112.322 163.039 1.00 57.21  ? 322  ALA L CB    1 
ATOM   8378  N  N     . LYS C 2 323 ? 120.499 114.228 165.768 1.00 58.79  ? 323  LYS L N     1 
ATOM   8379  C  CA    . LYS C 2 323 ? 120.425 115.580 166.304 1.00 68.12  ? 323  LYS L CA    1 
ATOM   8380  C  C     . LYS C 2 323 ? 121.601 115.909 167.214 1.00 65.76  ? 323  LYS L C     1 
ATOM   8381  O  O     . LYS C 2 323 ? 121.862 117.089 167.470 1.00 66.30  ? 323  LYS L O     1 
ATOM   8382  C  CB    . LYS C 2 323 ? 119.102 115.762 167.058 1.00 71.25  ? 323  LYS L CB    1 
ATOM   8383  C  CG    . LYS C 2 323 ? 118.790 117.188 167.494 1.00 67.28  ? 323  LYS L CG    1 
ATOM   8384  C  CD    . LYS C 2 323 ? 118.960 117.348 168.998 1.00 71.15  ? 323  LYS L CD    1 
ATOM   8385  C  CE    . LYS C 2 323 ? 118.573 118.745 169.456 1.00 70.20  ? 323  LYS L CE    1 
ATOM   8386  N  NZ    . LYS C 2 323 ? 118.694 118.894 170.933 1.00 67.84  ? 323  LYS L NZ    1 
ATOM   8387  N  N     . THR C 2 324 ? 122.331 114.896 167.685 1.00 59.38  ? 324  THR L N     1 
ATOM   8388  C  CA    . THR C 2 324 ? 123.404 115.113 168.647 1.00 60.93  ? 324  THR L CA    1 
ATOM   8389  C  C     . THR C 2 324 ? 124.639 115.760 168.035 1.00 57.29  ? 324  THR L C     1 
ATOM   8390  O  O     . THR C 2 324 ? 125.550 116.132 168.783 1.00 62.55  ? 324  THR L O     1 
ATOM   8391  C  CB    . THR C 2 324 ? 123.802 113.789 169.301 1.00 57.67  ? 324  THR L CB    1 
ATOM   8392  O  OG1   . THR C 2 324 ? 124.307 112.897 168.301 1.00 64.11  ? 324  THR L OG1   1 
ATOM   8393  C  CG2   . THR C 2 324 ? 122.600 113.150 169.982 1.00 58.03  ? 324  THR L CG2   1 
ATOM   8394  N  N     . ILE C 2 325 ? 124.702 115.903 166.719 1.00 34.70  ? 325  ILE L N     1 
ATOM   8395  C  CA    . ILE C 2 325 ? 125.892 116.431 166.063 1.00 36.06  ? 325  ILE L CA    1 
ATOM   8396  C  C     . ILE C 2 325 ? 125.784 117.943 165.940 1.00 37.10  ? 325  ILE L C     1 
ATOM   8397  O  O     . ILE C 2 325 ? 124.703 118.495 165.707 1.00 46.78  ? 325  ILE L O     1 
ATOM   8398  C  CB    . ILE C 2 325 ? 126.108 115.767 164.689 1.00 36.45  ? 325  ILE L CB    1 
ATOM   8399  C  CG1   . ILE C 2 325 ? 127.440 116.215 164.082 1.00 32.22  ? 325  ILE L CG1   1 
ATOM   8400  C  CG2   . ILE C 2 325 ? 124.963 116.079 163.751 1.00 38.30  ? 325  ILE L CG2   1 
ATOM   8401  C  CD1   . ILE C 2 325 ? 128.630 116.015 164.996 1.00 36.77  ? 325  ILE L CD1   1 
ATOM   8402  N  N     . LYS C 2 326 ? 126.917 118.615 166.125 1.00 30.76  ? 326  LYS L N     1 
ATOM   8403  C  CA    . LYS C 2 326 ? 127.044 120.054 165.964 1.00 28.32  ? 326  LYS L CA    1 
ATOM   8404  C  C     . LYS C 2 326 ? 128.173 120.333 164.985 1.00 36.88  ? 326  LYS L C     1 
ATOM   8405  O  O     . LYS C 2 326 ? 129.267 119.774 165.115 1.00 43.52  ? 326  LYS L O     1 
ATOM   8406  C  CB    . LYS C 2 326 ? 127.332 120.733 167.304 1.00 32.76  ? 326  LYS L CB    1 
ATOM   8407  C  CG    . LYS C 2 326 ? 127.495 122.230 167.211 1.00 38.42  ? 326  LYS L CG    1 
ATOM   8408  C  CD    . LYS C 2 326 ? 126.153 122.893 166.974 1.00 39.25  ? 326  LYS L CD    1 
ATOM   8409  C  CE    . LYS C 2 326 ? 125.191 122.578 168.107 1.00 42.83  ? 326  LYS L CE    1 
ATOM   8410  N  NZ    . LYS C 2 326 ? 125.692 123.075 169.417 1.00 36.94  ? 326  LYS L NZ    1 
ATOM   8411  N  N     . ASN C 2 327 ? 127.916 121.197 164.008 1.00 32.61  ? 327  ASN L N     1 
ATOM   8412  C  CA    . ASN C 2 327 ? 128.873 121.455 162.944 1.00 27.29  ? 327  ASN L CA    1 
ATOM   8413  C  C     . ASN C 2 327 ? 129.207 122.937 162.872 1.00 29.03  ? 327  ASN L C     1 
ATOM   8414  O  O     . ASN C 2 327 ? 128.385 123.796 163.204 1.00 30.42  ? 327  ASN L O     1 
ATOM   8415  C  CB    . ASN C 2 327 ? 128.344 120.972 161.587 1.00 20.49  ? 327  ASN L CB    1 
ATOM   8416  C  CG    . ASN C 2 327 ? 127.290 121.889 161.014 1.00 27.85  ? 327  ASN L CG    1 
ATOM   8417  O  OD1   . ASN C 2 327 ? 127.602 122.863 160.330 1.00 29.93  ? 327  ASN L OD1   1 
ATOM   8418  N  ND2   . ASN C 2 327 ? 126.027 121.580 161.284 1.00 33.04  ? 327  ASN L ND2   1 
ATOM   8419  N  N     . THR C 2 328 ? 130.431 123.222 162.434 1.00 48.27  ? 328  THR L N     1 
ATOM   8420  C  CA    . THR C 2 328 ? 130.950 124.577 162.320 1.00 46.88  ? 328  THR L CA    1 
ATOM   8421  C  C     . THR C 2 328 ? 130.945 124.994 160.857 1.00 48.00  ? 328  THR L C     1 
ATOM   8422  O  O     . THR C 2 328 ? 131.521 124.304 160.009 1.00 47.78  ? 328  THR L O     1 
ATOM   8423  C  CB    . THR C 2 328 ? 132.366 124.671 162.892 1.00 47.48  ? 328  THR L CB    1 
ATOM   8424  O  OG1   . THR C 2 328 ? 133.209 123.704 162.251 1.00 41.88  ? 328  THR L OG1   1 
ATOM   8425  C  CG2   . THR C 2 328 ? 132.353 124.408 164.391 1.00 49.03  ? 328  THR L CG2   1 
ATOM   8426  N  N     . VAL C 2 329 ? 130.304 126.123 160.566 1.00 45.34  ? 329  VAL L N     1 
ATOM   8427  C  CA    . VAL C 2 329 ? 130.107 126.596 159.202 1.00 39.65  ? 329  VAL L CA    1 
ATOM   8428  C  C     . VAL C 2 329 ? 130.785 127.949 159.045 1.00 45.35  ? 329  VAL L C     1 
ATOM   8429  O  O     . VAL C 2 329 ? 130.655 128.823 159.910 1.00 49.39  ? 329  VAL L O     1 
ATOM   8430  C  CB    . VAL C 2 329 ? 128.612 126.684 158.840 1.00 31.72  ? 329  VAL L CB    1 
ATOM   8431  C  CG1   . VAL C 2 329 ? 127.846 127.474 159.889 1.00 33.95  ? 329  VAL L CG1   1 
ATOM   8432  C  CG2   . VAL C 2 329 ? 128.437 127.308 157.471 1.00 36.04  ? 329  VAL L CG2   1 
ATOM   8433  N  N     . CYS C 2 330 ? 131.524 128.111 157.950 1.00 41.69  ? 330  CYS L N     1 
ATOM   8434  C  CA    . CYS C 2 330 ? 132.123 129.381 157.577 1.00 37.85  ? 330  CYS L CA    1 
ATOM   8435  C  C     . CYS C 2 330 ? 131.764 129.687 156.132 1.00 36.78  ? 330  CYS L C     1 
ATOM   8436  O  O     . CYS C 2 330 ? 131.586 128.779 155.316 1.00 43.45  ? 330  CYS L O     1 
ATOM   8437  C  CB    . CYS C 2 330 ? 133.646 129.364 157.748 1.00 45.52  ? 330  CYS L CB    1 
ATOM   8438  S  SG    . CYS C 2 330 ? 134.465 130.896 157.254 1.00 60.74  ? 330  CYS L SG    1 
ATOM   8439  N  N     . VAL C 2 331 ? 131.653 130.978 155.823 1.00 37.98  ? 331  VAL L N     1 
ATOM   8440  C  CA    . VAL C 2 331 ? 131.264 131.393 154.481 1.00 39.72  ? 331  VAL L CA    1 
ATOM   8441  C  C     . VAL C 2 331 ? 132.365 131.021 153.499 1.00 47.36  ? 331  VAL L C     1 
ATOM   8442  O  O     . VAL C 2 331 ? 133.543 131.338 153.710 1.00 56.57  ? 331  VAL L O     1 
ATOM   8443  C  CB    . VAL C 2 331 ? 130.976 132.901 154.444 1.00 40.87  ? 331  VAL L CB    1 
ATOM   8444  C  CG1   . VAL C 2 331 ? 130.322 133.282 153.128 1.00 39.21  ? 331  VAL L CG1   1 
ATOM   8445  C  CG2   . VAL C 2 331 ? 130.105 133.306 155.621 1.00 42.48  ? 331  VAL L CG2   1 
ATOM   8446  N  N     . ASN C 2 332 ? 131.987 130.343 152.419 1.00 32.71  ? 332  ASN L N     1 
ATOM   8447  C  CA    . ASN C 2 332 ? 132.935 129.969 151.373 1.00 21.00  ? 332  ASN L CA    1 
ATOM   8448  C  C     . ASN C 2 332 ? 133.231 131.210 150.546 1.00 24.04  ? 332  ASN L C     1 
ATOM   8449  O  O     . ASN C 2 332 ? 132.459 131.583 149.660 1.00 41.26  ? 332  ASN L O     1 
ATOM   8450  C  CB    . ASN C 2 332 ? 132.376 128.844 150.511 1.00 29.50  ? 332  ASN L CB    1 
ATOM   8451  C  CG    . ASN C 2 332 ? 132.482 127.489 151.179 1.00 36.06  ? 332  ASN L CG    1 
ATOM   8452  O  OD1   . ASN C 2 332 ? 131.669 127.139 152.034 1.00 39.64  ? 332  ASN L OD1   1 
ATOM   8453  N  ND2   . ASN C 2 332 ? 133.486 126.714 150.787 1.00 33.71  ? 332  ASN L ND2   1 
ATOM   8454  N  N     . VAL C 2 333 ? 134.352 131.859 150.841 1.00 21.15  ? 333  VAL L N     1 
ATOM   8455  C  CA    . VAL C 2 333 ? 134.745 133.098 150.185 1.00 29.78  ? 333  VAL L CA    1 
ATOM   8456  C  C     . VAL C 2 333 ? 136.126 132.905 149.578 1.00 42.49  ? 333  VAL L C     1 
ATOM   8457  O  O     . VAL C 2 333 ? 137.041 132.409 150.245 1.00 39.97  ? 333  VAL L O     1 
ATOM   8458  C  CB    . VAL C 2 333 ? 134.735 134.289 151.164 1.00 32.21  ? 333  VAL L CB    1 
ATOM   8459  C  CG1   . VAL C 2 333 ? 135.438 133.925 152.465 1.00 37.59  ? 333  VAL L CG1   1 
ATOM   8460  C  CG2   . VAL C 2 333 ? 135.378 135.508 150.528 1.00 36.52  ? 333  VAL L CG2   1 
ATOM   8461  N  N     . GLU C 2 334 ? 136.271 133.281 148.310 1.00 56.38  ? 334  GLU L N     1 
ATOM   8462  C  CA    . GLU C 2 334 ? 137.542 133.211 147.610 1.00 50.51  ? 334  GLU L CA    1 
ATOM   8463  C  C     . GLU C 2 334 ? 137.859 134.577 147.022 1.00 56.19  ? 334  GLU L C     1 
ATOM   8464  O  O     . GLU C 2 334 ? 136.958 135.356 146.700 1.00 55.17  ? 334  GLU L O     1 
ATOM   8465  C  CB    . GLU C 2 334 ? 137.523 132.151 146.502 1.00 50.78  ? 334  GLU L CB    1 
ATOM   8466  C  CG    . GLU C 2 334 ? 138.171 130.833 146.893 1.00 53.26  ? 334  GLU L CG    1 
ATOM   8467  C  CD    . GLU C 2 334 ? 139.686 130.902 146.885 0.00 55.60  ? 334  GLU L CD    1 
ATOM   8468  O  OE1   . GLU C 2 334 ? 140.237 131.847 146.282 1.00 57.45  ? 334  GLU L OE1   1 
ATOM   8469  O  OE2   . GLU C 2 334 ? 140.326 130.011 147.483 0.00 55.33  ? 334  GLU L OE2   1 
ATOM   8470  N  N     . LEU C 2 335 ? 139.149 134.864 146.894 1.00 77.52  ? 335  LEU L N     1 
ATOM   8471  C  CA    . LEU C 2 335 ? 139.613 136.140 146.374 1.00 80.01  ? 335  LEU L CA    1 
ATOM   8472  C  C     . LEU C 2 335 ? 139.827 136.036 144.870 1.00 77.65  ? 335  LEU L C     1 
ATOM   8473  O  O     . LEU C 2 335 ? 140.315 135.018 144.371 1.00 79.81  ? 335  LEU L O     1 
ATOM   8474  C  CB    . LEU C 2 335 ? 140.909 136.572 147.063 1.00 80.98  ? 335  LEU L CB    1 
ATOM   8475  C  CG    . LEU C 2 335 ? 140.950 136.443 148.588 1.00 82.75  ? 335  LEU L CG    1 
ATOM   8476  C  CD1   . LEU C 2 335 ? 142.236 137.038 149.142 1.00 78.26  ? 335  LEU L CD1   1 
ATOM   8477  C  CD2   . LEU C 2 335 ? 139.732 137.092 149.234 1.00 79.47  ? 335  LEU L CD2   1 
ATOM   8478  N  N     . THR C 2 336 ? 139.456 137.093 144.154 1.00 86.82  ? 336  THR L N     1 
ATOM   8479  C  CA    . THR C 2 336 ? 139.596 137.102 142.707 1.00 89.67  ? 336  THR L CA    1 
ATOM   8480  C  C     . THR C 2 336 ? 141.071 137.178 142.313 1.00 87.92  ? 336  THR L C     1 
ATOM   8481  O  O     . THR C 2 336 ? 141.957 137.406 143.140 1.00 89.67  ? 336  THR L O     1 
ATOM   8482  C  CB    . THR C 2 336 ? 138.821 138.270 142.099 1.00 89.73  ? 336  THR L CB    1 
ATOM   8483  O  OG1   . THR C 2 336 ? 139.038 139.451 142.882 1.00 90.14  ? 336  THR L OG1   1 
ATOM   8484  C  CG2   . THR C 2 336 ? 137.333 137.956 142.054 1.00 90.36  ? 336  THR L CG2   1 
ATOM   8485  N  N     . ALA C 2 337 ? 141.324 136.978 141.016 1.00 84.84  ? 337  ALA L N     1 
ATOM   8486  C  CA    . ALA C 2 337 ? 142.697 136.939 140.524 1.00 87.05  ? 337  ALA L CA    1 
ATOM   8487  C  C     . ALA C 2 337 ? 143.417 138.256 140.778 1.00 90.18  ? 337  ALA L C     1 
ATOM   8488  O  O     . ALA C 2 337 ? 144.621 138.270 141.060 1.00 93.25  ? 337  ALA L O     1 
ATOM   8489  C  CB    . ALA C 2 337 ? 142.711 136.598 139.034 1.00 89.12  ? 337  ALA L CB    1 
ATOM   8490  N  N     . GLU C 2 338 ? 142.698 139.375 140.675 1.00 99.65  ? 338  GLU L N     1 
ATOM   8491  C  CA    . GLU C 2 338 ? 143.301 140.668 140.981 1.00 101.89 ? 338  GLU L CA    1 
ATOM   8492  C  C     . GLU C 2 338 ? 143.679 140.764 142.454 1.00 98.49  ? 338  GLU L C     1 
ATOM   8493  O  O     . GLU C 2 338 ? 144.728 141.320 142.798 1.00 96.76  ? 338  GLU L O     1 
ATOM   8494  C  CB    . GLU C 2 338 ? 142.345 141.797 140.597 1.00 102.94 ? 338  GLU L CB    1 
ATOM   8495  C  CG    . GLU C 2 338 ? 141.909 141.783 139.138 1.00 101.70 ? 338  GLU L CG    1 
ATOM   8496  C  CD    . GLU C 2 338 ? 140.657 140.957 138.905 1.00 100.79 ? 338  GLU L CD    1 
ATOM   8497  O  OE1   . GLU C 2 338 ? 140.338 140.100 139.755 1.00 101.14 ? 338  GLU L OE1   1 
ATOM   8498  O  OE2   . GLU C 2 338 ? 139.992 141.166 137.869 1.00 97.88  ? 338  GLU L OE2   1 
ATOM   8499  N  N     . GLN C 2 339 ? 142.835 140.225 143.338 1.00 90.28  ? 339  GLN L N     1 
ATOM   8500  C  CA    . GLN C 2 339 ? 143.084 140.344 144.771 1.00 87.59  ? 339  GLN L CA    1 
ATOM   8501  C  C     . GLN C 2 339 ? 144.358 139.617 145.183 1.00 86.48  ? 339  GLN L C     1 
ATOM   8502  O  O     . GLN C 2 339 ? 145.139 140.137 145.988 1.00 89.96  ? 339  GLN L O     1 
ATOM   8503  C  CB    . GLN C 2 339 ? 141.885 139.816 145.557 1.00 87.95  ? 339  GLN L CB    1 
ATOM   8504  C  CG    . GLN C 2 339 ? 141.893 140.207 147.025 1.00 91.03  ? 339  GLN L CG    1 
ATOM   8505  C  CD    . GLN C 2 339 ? 140.529 140.076 147.670 1.00 92.23  ? 339  GLN L CD    1 
ATOM   8506  O  OE1   . GLN C 2 339 ? 139.559 139.682 147.024 1.00 91.11  ? 339  GLN L OE1   1 
ATOM   8507  N  NE2   . GLN C 2 339 ? 140.448 140.408 148.954 1.00 91.89  ? 339  GLN L NE2   1 
ATOM   8508  N  N     . TRP C 2 340 ? 144.586 138.413 144.651 1.00 81.45  ? 340  TRP L N     1 
ATOM   8509  C  CA    . TRP C 2 340 ? 145.825 137.706 144.959 1.00 84.25  ? 340  TRP L CA    1 
ATOM   8510  C  C     . TRP C 2 340 ? 147.038 138.450 144.419 1.00 87.23  ? 340  TRP L C     1 
ATOM   8511  O  O     . TRP C 2 340 ? 148.112 138.406 145.028 1.00 86.92  ? 340  TRP L O     1 
ATOM   8512  C  CB    . TRP C 2 340 ? 145.789 136.286 144.395 1.00 84.06  ? 340  TRP L CB    1 
ATOM   8513  C  CG    . TRP C 2 340 ? 144.657 135.446 144.901 1.00 84.91  ? 340  TRP L CG    1 
ATOM   8514  C  CD1   . TRP C 2 340 ? 143.545 135.072 144.206 1.00 88.09  ? 340  TRP L CD1   1 
ATOM   8515  C  CD2   . TRP C 2 340 ? 144.532 134.862 146.203 1.00 83.54  ? 340  TRP L CD2   1 
ATOM   8516  N  NE1   . TRP C 2 340 ? 142.731 134.298 144.996 1.00 88.21  ? 340  TRP L NE1   1 
ATOM   8517  C  CE2   . TRP C 2 340 ? 143.314 134.155 146.227 1.00 85.93  ? 340  TRP L CE2   1 
ATOM   8518  C  CE3   . TRP C 2 340 ? 145.326 134.875 147.353 1.00 83.76  ? 340  TRP L CE3   1 
ATOM   8519  C  CZ2   . TRP C 2 340 ? 142.873 133.465 147.354 1.00 85.98  ? 340  TRP L CZ2   1 
ATOM   8520  C  CZ3   . TRP C 2 340 ? 144.887 134.187 148.469 1.00 85.77  ? 340  TRP L CZ3   1 
ATOM   8521  C  CH2   . TRP C 2 340 ? 143.672 133.493 148.462 1.00 85.02  ? 340  TRP L CH2   1 
ATOM   8522  N  N     . LYS C 2 341 ? 146.890 139.127 143.278 1.00 100.55 ? 341  LYS L N     1 
ATOM   8523  C  CA    . LYS C 2 341 ? 147.986 139.928 142.744 1.00 100.76 ? 341  LYS L CA    1 
ATOM   8524  C  C     . LYS C 2 341 ? 148.327 141.085 143.675 1.00 101.78 ? 341  LYS L C     1 
ATOM   8525  O  O     . LYS C 2 341 ? 149.506 141.375 143.913 1.00 102.14 ? 341  LYS L O     1 
ATOM   8526  C  CB    . LYS C 2 341 ? 147.624 140.442 141.351 1.00 99.82  ? 341  LYS L CB    1 
ATOM   8527  C  CG    . LYS C 2 341 ? 148.551 141.522 140.818 1.00 98.51  ? 341  LYS L CG    1 
ATOM   8528  C  CD    . LYS C 2 341 ? 148.011 142.122 139.528 1.00 98.51  ? 341  LYS L CD    1 
ATOM   8529  C  CE    . LYS C 2 341 ? 148.861 143.292 139.063 1.00 99.07  ? 341  LYS L CE    1 
ATOM   8530  N  NZ    . LYS C 2 341 ? 148.299 143.933 137.842 1.00 99.16  ? 341  LYS L NZ    1 
ATOM   8531  N  N     . LYS C 2 342 ? 147.306 141.758 144.213 1.00 102.28 ? 342  LYS L N     1 
ATOM   8532  C  CA    . LYS C 2 342 ? 147.550 142.879 145.116 1.00 101.02 ? 342  LYS L CA    1 
ATOM   8533  C  C     . LYS C 2 342 ? 148.245 142.423 146.393 1.00 100.41 ? 342  LYS L C     1 
ATOM   8534  O  O     . LYS C 2 342 ? 149.169 143.090 146.873 1.00 99.65  ? 342  LYS L O     1 
ATOM   8535  C  CB    . LYS C 2 342 ? 146.236 143.586 145.444 1.00 100.58 ? 342  LYS L CB    1 
ATOM   8536  C  CG    . LYS C 2 342 ? 145.494 144.114 144.229 1.00 99.75  ? 342  LYS L CG    1 
ATOM   8537  C  CD    . LYS C 2 342 ? 146.354 145.079 143.431 1.00 100.71 ? 342  LYS L CD    1 
ATOM   8538  C  CE    . LYS C 2 342 ? 146.636 146.350 144.217 1.00 101.24 ? 342  LYS L CE    1 
ATOM   8539  N  NZ    . LYS C 2 342 ? 145.388 147.101 144.525 1.00 100.63 ? 342  LYS L NZ    1 
ATOM   8540  N  N     . LYS C 2 343 ? 147.815 141.292 146.958 1.00 101.32 ? 343  LYS L N     1 
ATOM   8541  C  CA    . LYS C 2 343 ? 148.438 140.797 148.181 1.00 101.10 ? 343  LYS L CA    1 
ATOM   8542  C  C     . LYS C 2 343 ? 149.889 140.396 147.946 1.00 101.54 ? 343  LYS L C     1 
ATOM   8543  O  O     . LYS C 2 343 ? 150.696 140.404 148.883 1.00 100.63 ? 343  LYS L O     1 
ATOM   8544  C  CB    . LYS C 2 343 ? 147.635 139.622 148.739 1.00 101.04 ? 343  LYS L CB    1 
ATOM   8545  C  CG    . LYS C 2 343 ? 148.064 139.182 150.129 1.00 101.74 ? 343  LYS L CG    1 
ATOM   8546  C  CD    . LYS C 2 343 ? 147.325 137.929 150.571 1.00 102.41 ? 343  LYS L CD    1 
ATOM   8547  C  CE    . LYS C 2 343 ? 147.426 136.830 149.530 1.00 101.22 ? 343  LYS L CE    1 
ATOM   8548  N  NZ    . LYS C 2 343 ? 147.248 135.483 150.140 1.00 102.89 ? 343  LYS L NZ    1 
ATOM   8549  N  N     . TYR C 2 344 ? 150.242 140.048 146.706 1.00 113.22 ? 344  TYR L N     1 
ATOM   8550  C  CA    . TYR C 2 344 ? 151.640 139.784 146.382 1.00 113.76 ? 344  TYR L CA    1 
ATOM   8551  C  C     . TYR C 2 344 ? 152.477 141.056 146.430 1.00 117.12 ? 344  TYR L C     1 
ATOM   8552  O  O     . TYR C 2 344 ? 153.667 141.000 146.762 1.00 117.33 ? 344  TYR L O     1 
ATOM   8553  C  CB    . TYR C 2 344 ? 151.746 139.132 145.003 1.00 113.36 ? 344  TYR L CB    1 
ATOM   8554  C  CG    . TYR C 2 344 ? 153.108 139.273 144.362 1.00 114.10 ? 344  TYR L CG    1 
ATOM   8555  C  CD1   . TYR C 2 344 ? 154.178 138.494 144.780 1.00 113.26 ? 344  TYR L CD1   1 
ATOM   8556  C  CD2   . TYR C 2 344 ? 153.323 140.187 143.338 1.00 114.69 ? 344  TYR L CD2   1 
ATOM   8557  C  CE1   . TYR C 2 344 ? 155.425 138.621 144.196 1.00 113.48 ? 344  TYR L CE1   1 
ATOM   8558  C  CE2   . TYR C 2 344 ? 154.565 140.322 142.749 1.00 115.37 ? 344  TYR L CE2   1 
ATOM   8559  C  CZ    . TYR C 2 344 ? 155.613 139.536 143.181 1.00 115.04 ? 344  TYR L CZ    1 
ATOM   8560  O  OH    . TYR C 2 344 ? 156.852 139.666 142.597 1.00 114.25 ? 344  TYR L OH    1 
ATOM   8561  N  N     . GLU C 2 345 ? 151.877 142.203 146.102 1.00 123.35 ? 345  GLU L N     1 
ATOM   8562  C  CA    . GLU C 2 345 ? 152.628 143.454 146.073 1.00 123.12 ? 345  GLU L CA    1 
ATOM   8563  C  C     . GLU C 2 345 ? 153.161 143.813 147.454 1.00 123.40 ? 345  GLU L C     1 
ATOM   8564  O  O     . GLU C 2 345 ? 154.299 144.279 147.586 1.00 123.31 ? 345  GLU L O     1 
ATOM   8565  C  CB    . GLU C 2 345 ? 151.748 144.577 145.525 1.00 121.60 ? 345  GLU L CB    1 
ATOM   8566  C  CG    . GLU C 2 345 ? 151.201 144.305 144.132 1.00 120.80 ? 345  GLU L CG    1 
ATOM   8567  C  CD    . GLU C 2 345 ? 150.375 145.457 143.593 1.00 122.00 ? 345  GLU L CD    1 
ATOM   8568  O  OE1   . GLU C 2 345 ? 150.184 146.448 144.328 1.00 122.69 ? 345  GLU L OE1   1 
ATOM   8569  O  OE2   . GLU C 2 345 ? 149.917 145.370 142.435 1.00 121.14 ? 345  GLU L OE2   1 
ATOM   8570  N  N     . LYS C 2 346 ? 152.358 143.606 148.493 1.00 117.99 ? 346  LYS L N     1 
ATOM   8571  C  CA    . LYS C 2 346 ? 152.791 143.884 149.856 1.00 116.50 ? 346  LYS L CA    1 
ATOM   8572  C  C     . LYS C 2 346 ? 153.808 142.846 150.321 1.00 116.28 ? 346  LYS L C     1 
ATOM   8573  O  O     . LYS C 2 346 ? 154.906 143.191 150.758 1.00 116.13 ? 346  LYS L O     1 
ATOM   8574  C  CB    . LYS C 2 346 ? 151.595 143.912 150.809 1.00 115.24 ? 346  LYS L CB    1 
ATOM   8575  C  CG    . LYS C 2 346 ? 151.206 142.547 151.352 1.00 114.94 ? 346  LYS L CG    1 
ATOM   8576  C  CD    . LYS C 2 346 ? 150.138 142.664 152.427 1.00 116.86 ? 346  LYS L CD    1 
ATOM   8577  C  CE    . LYS C 2 346 ? 149.934 141.341 153.147 1.00 117.35 ? 346  LYS L CE    1 
ATOM   8578  N  NZ    . LYS C 2 346 ? 151.173 140.892 153.840 1.00 116.64 ? 346  LYS L NZ    1 
ATOM   8579  N  N     . MET D 3 1   ? 125.469 185.844 61.536  1.00 84.54  ? 1    MET A N     1 
ATOM   8580  C  CA    . MET D 3 1   ? 126.722 186.503 61.876  1.00 87.55  ? 1    MET A CA    1 
ATOM   8581  C  C     . MET D 3 1   ? 127.599 185.607 62.743  1.00 85.09  ? 1    MET A C     1 
ATOM   8582  O  O     . MET D 3 1   ? 127.103 184.728 63.444  1.00 88.35  ? 1    MET A O     1 
ATOM   8583  C  CB    . MET D 3 1   ? 126.452 187.827 62.593  1.00 90.00  ? 1    MET A CB    1 
ATOM   8584  C  CG    . MET D 3 1   ? 125.437 188.715 61.892  1.00 91.03  ? 1    MET A CG    1 
ATOM   8585  S  SD    . MET D 3 1   ? 125.883 189.066 60.181  1.00 98.77  ? 1    MET A SD    1 
ATOM   8586  C  CE    . MET D 3 1   ? 127.424 189.950 60.406  1.00 84.58  ? 1    MET A CE    1 
ATOM   8587  N  N     . ARG D 3 2   ? 128.907 185.841 62.691  1.00 71.68  ? 2    ARG A N     1 
ATOM   8588  C  CA    . ARG D 3 2   ? 129.872 185.048 63.441  1.00 71.26  ? 2    ARG A CA    1 
ATOM   8589  C  C     . ARG D 3 2   ? 129.921 185.557 64.875  1.00 75.26  ? 2    ARG A C     1 
ATOM   8590  O  O     . ARG D 3 2   ? 130.335 186.696 65.118  1.00 82.32  ? 2    ARG A O     1 
ATOM   8591  C  CB    . ARG D 3 2   ? 131.250 185.133 62.790  1.00 77.44  ? 2    ARG A CB    1 
ATOM   8592  C  CG    . ARG D 3 2   ? 131.227 184.973 61.283  1.00 77.83  ? 2    ARG A CG    1 
ATOM   8593  C  CD    . ARG D 3 2   ? 132.170 185.956 60.614  1.00 76.71  ? 2    ARG A CD    1 
ATOM   8594  N  NE    . ARG D 3 2   ? 131.898 187.330 61.016  1.00 78.30  ? 2    ARG A NE    1 
ATOM   8595  C  CZ    . ARG D 3 2   ? 131.001 188.116 60.438  1.00 78.79  ? 2    ARG A CZ    1 
ATOM   8596  N  NH1   . ARG D 3 2   ? 130.262 187.694 59.425  1.00 78.68  ? 2    ARG A NH1   1 
ATOM   8597  N  NH2   . ARG D 3 2   ? 130.842 189.358 60.886  1.00 78.72  ? 2    ARG A NH2   1 
ATOM   8598  N  N     . GLU D 3 3   ? 129.502 184.720 65.821  1.00 69.89  ? 3    GLU A N     1 
ATOM   8599  C  CA    . GLU D 3 3   ? 129.350 185.136 67.206  1.00 70.49  ? 3    GLU A CA    1 
ATOM   8600  C  C     . GLU D 3 3   ? 129.995 184.120 68.139  1.00 70.68  ? 3    GLU A C     1 
ATOM   8601  O  O     . GLU D 3 3   ? 129.954 182.912 67.892  1.00 73.95  ? 3    GLU A O     1 
ATOM   8602  C  CB    . GLU D 3 3   ? 127.868 185.325 67.555  1.00 69.14  ? 3    GLU A CB    1 
ATOM   8603  C  CG    . GLU D 3 3   ? 127.167 186.323 66.639  1.00 76.27  ? 3    GLU A CG    1 
ATOM   8604  C  CD    . GLU D 3 3   ? 125.718 186.560 67.004  1.00 79.50  ? 3    GLU A CD    1 
ATOM   8605  O  OE1   . GLU D 3 3   ? 125.231 185.925 67.959  1.00 79.07  ? 3    GLU A OE1   1 
ATOM   8606  O  OE2   . GLU D 3 3   ? 125.061 187.379 66.329  1.00 78.28  ? 3    GLU A OE2   1 
ATOM   8607  N  N     . CYS D 3 4   ? 130.597 184.627 69.215  1.00 65.36  ? 4    CYS A N     1 
ATOM   8608  C  CA    . CYS D 3 4   ? 131.321 183.809 70.178  1.00 62.31  ? 4    CYS A CA    1 
ATOM   8609  C  C     . CYS D 3 4   ? 130.780 184.039 71.580  1.00 64.49  ? 4    CYS A C     1 
ATOM   8610  O  O     . CYS D 3 4   ? 130.278 185.119 71.902  1.00 69.18  ? 4    CYS A O     1 
ATOM   8611  C  CB    . CYS D 3 4   ? 132.823 184.110 70.163  1.00 60.23  ? 4    CYS A CB    1 
ATOM   8612  S  SG    . CYS D 3 4   ? 133.659 183.683 68.626  1.00 88.29  ? 4    CYS A SG    1 
ATOM   8613  N  N     . ILE D 3 5   ? 130.889 183.008 72.412  1.00 47.57  ? 5    ILE A N     1 
ATOM   8614  C  CA    . ILE D 3 5   ? 130.452 183.054 73.802  1.00 37.98  ? 5    ILE A CA    1 
ATOM   8615  C  C     . ILE D 3 5   ? 131.690 183.026 74.685  1.00 50.09  ? 5    ILE A C     1 
ATOM   8616  O  O     . ILE D 3 5   ? 132.575 182.183 74.499  1.00 64.41  ? 5    ILE A O     1 
ATOM   8617  C  CB    . ILE D 3 5   ? 129.516 181.885 74.138  1.00 35.40  ? 5    ILE A CB    1 
ATOM   8618  C  CG1   . ILE D 3 5   ? 128.229 181.968 73.328  1.00 43.92  ? 5    ILE A CG1   1 
ATOM   8619  C  CG2   . ILE D 3 5   ? 129.190 181.874 75.613  1.00 51.54  ? 5    ILE A CG2   1 
ATOM   8620  C  CD1   . ILE D 3 5   ? 127.265 180.858 73.634  1.00 50.80  ? 5    ILE A CD1   1 
ATOM   8621  N  N     . SER D 3 6   ? 131.760 183.944 75.642  1.00 43.67  ? 6    SER A N     1 
ATOM   8622  C  CA    . SER D 3 6   ? 132.864 184.002 76.588  1.00 42.54  ? 6    SER A CA    1 
ATOM   8623  C  C     . SER D 3 6   ? 132.387 183.528 77.953  1.00 48.52  ? 6    SER A C     1 
ATOM   8624  O  O     . SER D 3 6   ? 131.393 184.037 78.479  1.00 61.21  ? 6    SER A O     1 
ATOM   8625  C  CB    . SER D 3 6   ? 133.420 185.420 76.682  1.00 49.76  ? 6    SER A CB    1 
ATOM   8626  O  OG    . SER D 3 6   ? 133.868 185.871 75.416  1.00 53.72  ? 6    SER A OG    1 
ATOM   8627  N  N     . ILE D 3 7   ? 133.094 182.557 78.521  1.00 43.32  ? 7    ILE A N     1 
ATOM   8628  C  CA    . ILE D 3 7   ? 132.799 182.031 79.847  1.00 41.13  ? 7    ILE A CA    1 
ATOM   8629  C  C     . ILE D 3 7   ? 134.010 182.275 80.733  1.00 43.35  ? 7    ILE A C     1 
ATOM   8630  O  O     . ILE D 3 7   ? 135.123 181.857 80.396  1.00 56.81  ? 7    ILE A O     1 
ATOM   8631  C  CB    . ILE D 3 7   ? 132.451 180.533 79.804  1.00 44.70  ? 7    ILE A CB    1 
ATOM   8632  C  CG1   . ILE D 3 7   ? 131.340 180.271 78.792  1.00 48.58  ? 7    ILE A CG1   1 
ATOM   8633  C  CG2   . ILE D 3 7   ? 132.044 180.048 81.174  1.00 49.19  ? 7    ILE A CG2   1 
ATOM   8634  C  CD1   . ILE D 3 7   ? 131.093 178.810 78.542  1.00 49.78  ? 7    ILE A CD1   1 
ATOM   8635  N  N     . HIS D 3 8   ? 133.794 182.948 81.858  1.00 35.96  ? 8    HIS A N     1 
ATOM   8636  C  CA    . HIS D 3 8   ? 134.860 183.273 82.794  1.00 34.02  ? 8    HIS A CA    1 
ATOM   8637  C  C     . HIS D 3 8   ? 134.598 182.551 84.106  1.00 42.31  ? 8    HIS A C     1 
ATOM   8638  O  O     . HIS D 3 8   ? 133.600 182.824 84.780  1.00 55.77  ? 8    HIS A O     1 
ATOM   8639  C  CB    . HIS D 3 8   ? 134.952 184.781 83.002  1.00 40.62  ? 8    HIS A CB    1 
ATOM   8640  C  CG    . HIS D 3 8   ? 134.836 185.565 81.735  1.00 43.67  ? 8    HIS A CG    1 
ATOM   8641  N  ND1   . HIS D 3 8   ? 135.932 185.992 81.020  1.00 39.26  ? 8    HIS A ND1   1 
ATOM   8642  C  CD2   . HIS D 3 8   ? 133.750 185.988 81.047  1.00 51.46  ? 8    HIS A CD2   1 
ATOM   8643  C  CE1   . HIS D 3 8   ? 135.528 186.649 79.949  1.00 44.28  ? 8    HIS A CE1   1 
ATOM   8644  N  NE2   . HIS D 3 8   ? 134.208 186.664 79.943  1.00 50.76  ? 8    HIS A NE2   1 
ATOM   8645  N  N     . VAL D 3 9   ? 135.497 181.641 84.466  1.00 34.98  ? 9    VAL A N     1 
ATOM   8646  C  CA    . VAL D 3 9   ? 135.333 180.770 85.621  1.00 34.26  ? 9    VAL A CA    1 
ATOM   8647  C  C     . VAL D 3 9   ? 136.459 181.047 86.602  1.00 41.48  ? 9    VAL A C     1 
ATOM   8648  O  O     . VAL D 3 9   ? 137.636 181.012 86.229  1.00 48.68  ? 9    VAL A O     1 
ATOM   8649  C  CB    . VAL D 3 9   ? 135.325 179.285 85.216  1.00 40.87  ? 9    VAL A CB    1 
ATOM   8650  C  CG1   . VAL D 3 9   ? 135.188 178.404 86.439  1.00 47.02  ? 9    VAL A CG1   1 
ATOM   8651  C  CG2   . VAL D 3 9   ? 134.198 179.014 84.241  1.00 43.60  ? 9    VAL A CG2   1 
ATOM   8652  N  N     . GLY D 3 10  ? 136.099 181.320 87.849  1.00 48.46  ? 10   GLY A N     1 
ATOM   8653  C  CA    . GLY D 3 10  ? 137.073 181.585 88.881  1.00 43.87  ? 10   GLY A CA    1 
ATOM   8654  C  C     . GLY D 3 10  ? 137.533 183.027 88.887  1.00 47.39  ? 10   GLY A C     1 
ATOM   8655  O  O     . GLY D 3 10  ? 137.220 183.828 88.002  1.00 58.62  ? 10   GLY A O     1 
ATOM   8656  N  N     . GLN D 3 11  ? 138.308 183.358 89.920  1.00 49.43  ? 11   GLN A N     1 
ATOM   8657  C  CA    . GLN D 3 11  ? 138.753 184.735 90.096  1.00 52.97  ? 11   GLN A CA    1 
ATOM   8658  C  C     . GLN D 3 11  ? 139.631 185.189 88.940  1.00 57.11  ? 11   GLN A C     1 
ATOM   8659  O  O     . GLN D 3 11  ? 139.461 186.299 88.425  1.00 68.23  ? 11   GLN A O     1 
ATOM   8660  C  CB    . GLN D 3 11  ? 139.499 184.888 91.417  1.00 53.44  ? 11   GLN A CB    1 
ATOM   8661  C  CG    . GLN D 3 11  ? 139.707 186.328 91.814  1.00 53.17  ? 11   GLN A CG    1 
ATOM   8662  C  CD    . GLN D 3 11  ? 140.204 186.475 93.225  1.00 53.89  ? 11   GLN A CD    1 
ATOM   8663  O  OE1   . GLN D 3 11  ? 140.710 185.526 93.818  1.00 57.07  ? 11   GLN A OE1   1 
ATOM   8664  N  NE2   . GLN D 3 11  ? 140.058 187.670 93.779  1.00 53.91  ? 11   GLN A NE2   1 
ATOM   8665  N  N     . ALA D 3 12  ? 140.580 184.353 88.521  1.00 47.98  ? 12   ALA A N     1 
ATOM   8666  C  CA    . ALA D 3 12  ? 141.446 184.744 87.416  1.00 50.63  ? 12   ALA A CA    1 
ATOM   8667  C  C     . ALA D 3 12  ? 140.642 184.955 86.144  1.00 52.09  ? 12   ALA A C     1 
ATOM   8668  O  O     . ALA D 3 12  ? 140.837 185.948 85.431  1.00 61.98  ? 12   ALA A O     1 
ATOM   8669  C  CB    . ALA D 3 12  ? 142.529 183.694 87.199  1.00 54.23  ? 12   ALA A CB    1 
ATOM   8670  N  N     . GLY D 3 13  ? 139.717 184.040 85.857  1.00 46.16  ? 13   GLY A N     1 
ATOM   8671  C  CA    . GLY D 3 13  ? 138.894 184.181 84.672  1.00 45.32  ? 13   GLY A CA    1 
ATOM   8672  C  C     . GLY D 3 13  ? 138.072 185.453 84.681  1.00 51.38  ? 13   GLY A C     1 
ATOM   8673  O  O     . GLY D 3 13  ? 137.989 186.150 83.672  1.00 61.95  ? 13   GLY A O     1 
ATOM   8674  N  N     . VAL D 3 14  ? 137.471 185.787 85.825  1.00 38.66  ? 14   VAL A N     1 
ATOM   8675  C  CA    . VAL D 3 14  ? 136.618 186.970 85.858  1.00 38.03  ? 14   VAL A CA    1 
ATOM   8676  C  C     . VAL D 3 14  ? 137.439 188.257 85.823  1.00 45.42  ? 14   VAL A C     1 
ATOM   8677  O  O     . VAL D 3 14  ? 137.003 189.252 85.236  1.00 60.94  ? 14   VAL A O     1 
ATOM   8678  C  CB    . VAL D 3 14  ? 135.669 186.925 87.068  1.00 44.33  ? 14   VAL A CB    1 
ATOM   8679  C  CG1   . VAL D 3 14  ? 134.754 185.725 86.963  1.00 46.63  ? 14   VAL A CG1   1 
ATOM   8680  C  CG2   . VAL D 3 14  ? 136.441 186.872 88.346  1.00 52.90  ? 14   VAL A CG2   1 
ATOM   8681  N  N     . GLN D 3 15  ? 138.625 188.278 86.440  1.00 42.03  ? 15   GLN A N     1 
ATOM   8682  C  CA    . GLN D 3 15  ? 139.485 189.455 86.324  1.00 48.87  ? 15   GLN A CA    1 
ATOM   8683  C  C     . GLN D 3 15  ? 139.906 189.677 84.873  1.00 53.99  ? 15   GLN A C     1 
ATOM   8684  O  O     . GLN D 3 15  ? 139.805 190.795 84.334  1.00 58.45  ? 15   GLN A O     1 
ATOM   8685  C  CB    . GLN D 3 15  ? 140.715 189.296 87.220  1.00 59.32  ? 15   GLN A CB    1 
ATOM   8686  C  CG    . GLN D 3 15  ? 140.432 189.130 88.710  1.00 52.74  ? 15   GLN A CG    1 
ATOM   8687  C  CD    . GLN D 3 15  ? 140.401 190.435 89.468  1.00 59.10  ? 15   GLN A CD    1 
ATOM   8688  O  OE1   . GLN D 3 15  ? 141.133 191.370 89.148  1.00 63.90  ? 15   GLN A OE1   1 
ATOM   8689  N  NE2   . GLN D 3 15  ? 139.562 190.501 90.493  1.00 57.42  ? 15   GLN A NE2   1 
ATOM   8690  N  N     . ILE D 3 16  ? 140.371 188.608 84.217  1.00 48.69  ? 16   ILE A N     1 
ATOM   8691  C  CA    . ILE D 3 16  ? 140.742 188.706 82.811  1.00 44.86  ? 16   ILE A CA    1 
ATOM   8692  C  C     . ILE D 3 16  ? 139.540 189.120 81.978  1.00 55.19  ? 16   ILE A C     1 
ATOM   8693  O  O     . ILE D 3 16  ? 139.671 189.869 81.008  1.00 65.33  ? 16   ILE A O     1 
ATOM   8694  C  CB    . ILE D 3 16  ? 141.345 187.379 82.320  1.00 48.04  ? 16   ILE A CB    1 
ATOM   8695  C  CG1   . ILE D 3 16  ? 142.564 187.011 83.158  1.00 51.03  ? 16   ILE A CG1   1 
ATOM   8696  C  CG2   . ILE D 3 16  ? 141.722 187.473 80.853  1.00 56.25  ? 16   ILE A CG2   1 
ATOM   8697  C  CD1   . ILE D 3 16  ? 143.344 185.849 82.606  1.00 56.71  ? 16   ILE A CD1   1 
ATOM   8698  N  N     . GLY D 3 17  ? 138.350 188.641 82.342  1.00 55.01  ? 17   GLY A N     1 
ATOM   8699  C  CA    . GLY D 3 17  ? 137.155 189.020 81.612  1.00 53.50  ? 17   GLY A CA    1 
ATOM   8700  C  C     . GLY D 3 17  ? 136.808 190.485 81.768  1.00 53.28  ? 17   GLY A C     1 
ATOM   8701  O  O     . GLY D 3 17  ? 136.361 191.127 80.818  1.00 64.12  ? 17   GLY A O     1 
ATOM   8702  N  N     . ASN D 3 18  ? 136.991 191.030 82.969  1.00 43.91  ? 18   ASN A N     1 
ATOM   8703  C  CA    . ASN D 3 18  ? 136.800 192.462 83.161  1.00 47.76  ? 18   ASN A CA    1 
ATOM   8704  C  C     . ASN D 3 18  ? 137.723 193.245 82.241  1.00 51.57  ? 18   ASN A C     1 
ATOM   8705  O  O     . ASN D 3 18  ? 137.293 194.181 81.549  1.00 58.04  ? 18   ASN A O     1 
ATOM   8706  C  CB    . ASN D 3 18  ? 137.051 192.838 84.620  1.00 49.95  ? 18   ASN A CB    1 
ATOM   8707  C  CG    . ASN D 3 18  ? 135.994 192.296 85.552  1.00 61.20  ? 18   ASN A CG    1 
ATOM   8708  O  OD1   . ASN D 3 18  ? 134.843 192.108 85.161  1.00 63.33  ? 18   ASN A OD1   1 
ATOM   8709  N  ND2   . ASN D 3 18  ? 136.378 192.039 86.796  1.00 58.94  ? 18   ASN A ND2   1 
ATOM   8710  N  N     . ALA D 3 19  ? 138.997 192.847 82.193  1.00 51.52  ? 19   ALA A N     1 
ATOM   8711  C  CA    . ALA D 3 19  ? 139.938 193.526 81.302  1.00 55.32  ? 19   ALA A CA    1 
ATOM   8712  C  C     . ALA D 3 19  ? 139.528 193.380 79.838  1.00 57.69  ? 19   ALA A C     1 
ATOM   8713  O  O     . ALA D 3 19  ? 139.534 194.359 79.077  1.00 64.52  ? 19   ALA A O     1 
ATOM   8714  C  CB    . ALA D 3 19  ? 141.349 192.983 81.518  1.00 54.35  ? 19   ALA A CB    1 
ATOM   8715  N  N     . CYS D 3 20  ? 139.148 192.167 79.434  1.00 54.38  ? 20   CYS A N     1 
ATOM   8716  C  CA    . CYS D 3 20  ? 138.788 191.904 78.045  1.00 50.24  ? 20   CYS A CA    1 
ATOM   8717  C  C     . CYS D 3 20  ? 137.561 192.696 77.629  1.00 57.92  ? 20   CYS A C     1 
ATOM   8718  O  O     . CYS D 3 20  ? 137.493 193.203 76.505  1.00 64.72  ? 20   CYS A O     1 
ATOM   8719  C  CB    . CYS D 3 20  ? 138.544 190.410 77.842  1.00 54.70  ? 20   CYS A CB    1 
ATOM   8720  S  SG    . CYS D 3 20  ? 140.002 189.367 78.014  1.00 72.58  ? 20   CYS A SG    1 
ATOM   8721  N  N     . TRP D 3 21  ? 136.572 192.801 78.511  1.00 51.96  ? 21   TRP A N     1 
ATOM   8722  C  CA    . TRP D 3 21  ? 135.346 193.495 78.149  1.00 47.77  ? 21   TRP A CA    1 
ATOM   8723  C  C     . TRP D 3 21  ? 135.532 195.001 78.157  1.00 49.73  ? 21   TRP A C     1 
ATOM   8724  O  O     . TRP D 3 21  ? 134.930 195.693 77.329  1.00 60.48  ? 21   TRP A O     1 
ATOM   8725  C  CB    . TRP D 3 21  ? 134.212 193.068 79.075  1.00 47.85  ? 21   TRP A CB    1 
ATOM   8726  C  CG    . TRP D 3 21  ? 133.711 191.724 78.697  1.00 46.42  ? 21   TRP A CG    1 
ATOM   8727  C  CD1   . TRP D 3 21  ? 133.847 190.571 79.403  1.00 51.52  ? 21   TRP A CD1   1 
ATOM   8728  C  CD2   . TRP D 3 21  ? 133.042 191.376 77.486  1.00 43.35  ? 21   TRP A CD2   1 
ATOM   8729  N  NE1   . TRP D 3 21  ? 133.281 189.527 78.718  1.00 56.67  ? 21   TRP A NE1   1 
ATOM   8730  C  CE2   . TRP D 3 21  ? 132.781 189.998 77.534  1.00 50.68  ? 21   TRP A CE2   1 
ATOM   8731  C  CE3   . TRP D 3 21  ? 132.623 192.100 76.370  1.00 49.08  ? 21   TRP A CE3   1 
ATOM   8732  C  CZ2   . TRP D 3 21  ? 132.123 189.330 76.511  1.00 52.61  ? 21   TRP A CZ2   1 
ATOM   8733  C  CZ3   . TRP D 3 21  ? 131.976 191.437 75.359  1.00 48.55  ? 21   TRP A CZ3   1 
ATOM   8734  C  CH2   . TRP D 3 21  ? 131.729 190.066 75.434  1.00 48.35  ? 21   TRP A CH2   1 
ATOM   8735  N  N     . GLU D 3 22  ? 136.379 195.524 79.046  1.00 47.39  ? 22   GLU A N     1 
ATOM   8736  C  CA    . GLU D 3 22  ? 136.792 196.915 78.907  1.00 51.68  ? 22   GLU A CA    1 
ATOM   8737  C  C     . GLU D 3 22  ? 137.430 197.151 77.543  1.00 52.10  ? 22   GLU A C     1 
ATOM   8738  O  O     . GLU D 3 22  ? 137.095 198.120 76.846  1.00 60.73  ? 22   GLU A O     1 
ATOM   8739  C  CB    . GLU D 3 22  ? 137.758 197.281 80.031  1.00 55.41  ? 22   GLU A CB    1 
ATOM   8740  C  CG    . GLU D 3 22  ? 138.368 198.662 79.916  1.00 63.64  ? 22   GLU A CG    1 
ATOM   8741  C  CD    . GLU D 3 22  ? 139.259 199.000 81.094  1.00 63.59  ? 22   GLU A CD    1 
ATOM   8742  O  OE1   . GLU D 3 22  ? 139.757 198.062 81.751  1.00 56.83  ? 22   GLU A OE1   1 
ATOM   8743  O  OE2   . GLU D 3 22  ? 139.455 200.202 81.368  1.00 61.32  ? 22   GLU A OE2   1 
ATOM   8744  N  N     . LEU D 3 23  ? 138.322 196.248 77.131  1.00 49.80  ? 23   LEU A N     1 
ATOM   8745  C  CA    . LEU D 3 23  ? 138.989 196.397 75.841  1.00 49.95  ? 23   LEU A CA    1 
ATOM   8746  C  C     . LEU D 3 23  ? 137.997 196.346 74.685  1.00 63.05  ? 23   LEU A C     1 
ATOM   8747  O  O     . LEU D 3 23  ? 138.084 197.148 73.748  1.00 66.75  ? 23   LEU A O     1 
ATOM   8748  C  CB    . LEU D 3 23  ? 140.047 195.310 75.681  1.00 51.76  ? 23   LEU A CB    1 
ATOM   8749  C  CG    . LEU D 3 23  ? 141.015 195.490 74.523  1.00 57.58  ? 23   LEU A CG    1 
ATOM   8750  C  CD1   . LEU D 3 23  ? 141.792 196.765 74.717  1.00 60.06  ? 23   LEU A CD1   1 
ATOM   8751  C  CD2   . LEU D 3 23  ? 141.955 194.309 74.444  1.00 60.90  ? 23   LEU A CD2   1 
ATOM   8752  N  N     . TYR D 3 24  ? 137.050 195.407 74.729  1.00 62.67  ? 24   TYR A N     1 
ATOM   8753  C  CA    . TYR D 3 24  ? 136.083 195.273 73.643  1.00 49.96  ? 24   TYR A CA    1 
ATOM   8754  C  C     . TYR D 3 24  ? 135.168 196.485 73.566  1.00 50.21  ? 24   TYR A C     1 
ATOM   8755  O  O     . TYR D 3 24  ? 134.890 196.997 72.472  1.00 55.98  ? 24   TYR A O     1 
ATOM   8756  C  CB    . TYR D 3 24  ? 135.258 194.002 73.824  1.00 46.48  ? 24   TYR A CB    1 
ATOM   8757  C  CG    . TYR D 3 24  ? 136.062 192.731 73.756  1.00 53.12  ? 24   TYR A CG    1 
ATOM   8758  C  CD1   . TYR D 3 24  ? 137.230 192.666 73.017  1.00 58.81  ? 24   TYR A CD1   1 
ATOM   8759  C  CD2   . TYR D 3 24  ? 135.657 191.598 74.442  1.00 55.84  ? 24   TYR A CD2   1 
ATOM   8760  C  CE1   . TYR D 3 24  ? 137.969 191.506 72.958  1.00 62.01  ? 24   TYR A CE1   1 
ATOM   8761  C  CE2   . TYR D 3 24  ? 136.389 190.435 74.389  1.00 58.95  ? 24   TYR A CE2   1 
ATOM   8762  C  CZ    . TYR D 3 24  ? 137.543 190.394 73.644  1.00 64.71  ? 24   TYR A CZ    1 
ATOM   8763  O  OH    . TYR D 3 24  ? 138.276 189.232 73.589  1.00 65.79  ? 24   TYR A OH    1 
ATOM   8764  N  N     . CYS D 3 25  ? 134.678 196.953 74.716  1.00 52.00  ? 25   CYS A N     1 
ATOM   8765  C  CA    . CYS D 3 25  ? 133.825 198.132 74.727  1.00 52.46  ? 25   CYS A CA    1 
ATOM   8766  C  C     . CYS D 3 25  ? 134.567 199.342 74.184  1.00 54.80  ? 25   CYS A C     1 
ATOM   8767  O  O     . CYS D 3 25  ? 133.979 200.178 73.489  1.00 66.28  ? 25   CYS A O     1 
ATOM   8768  C  CB    . CYS D 3 25  ? 133.313 198.396 76.142  1.00 57.93  ? 25   CYS A CB    1 
ATOM   8769  S  SG    . CYS D 3 25  ? 132.148 197.163 76.759  1.00 72.60  ? 25   CYS A SG    1 
ATOM   8770  N  N     . LEU D 3 26  ? 135.861 199.457 74.489  1.00 52.19  ? 26   LEU A N     1 
ATOM   8771  C  CA    . LEU D 3 26  ? 136.644 200.538 73.901  1.00 53.44  ? 26   LEU A CA    1 
ATOM   8772  C  C     . LEU D 3 26  ? 136.780 200.366 72.393  1.00 57.29  ? 26   LEU A C     1 
ATOM   8773  O  O     . LEU D 3 26  ? 136.664 201.337 71.637  1.00 59.75  ? 26   LEU A O     1 
ATOM   8774  C  CB    . LEU D 3 26  ? 138.019 200.610 74.560  1.00 60.21  ? 26   LEU A CB    1 
ATOM   8775  C  CG    . LEU D 3 26  ? 138.071 201.378 75.879  1.00 64.01  ? 26   LEU A CG    1 
ATOM   8776  C  CD1   . LEU D 3 26  ? 139.456 201.288 76.485  1.00 61.61  ? 26   LEU A CD1   1 
ATOM   8777  C  CD2   . LEU D 3 26  ? 137.660 202.826 75.675  1.00 60.49  ? 26   LEU A CD2   1 
ATOM   8778  N  N     . GLU D 3 27  ? 137.029 199.136 71.939  1.00 67.55  ? 27   GLU A N     1 
ATOM   8779  C  CA    . GLU D 3 27  ? 137.237 198.890 70.515  1.00 67.54  ? 27   GLU A CA    1 
ATOM   8780  C  C     . GLU D 3 27  ? 136.004 199.257 69.703  1.00 67.87  ? 27   GLU A C     1 
ATOM   8781  O  O     . GLU D 3 27  ? 136.105 199.907 68.657  1.00 72.10  ? 27   GLU A O     1 
ATOM   8782  C  CB    . GLU D 3 27  ? 137.599 197.422 70.284  1.00 68.43  ? 27   GLU A CB    1 
ATOM   8783  C  CG    . GLU D 3 27  ? 139.064 197.089 70.461  1.00 72.61  ? 27   GLU A CG    1 
ATOM   8784  C  CD    . GLU D 3 27  ? 139.883 197.367 69.214  1.00 79.60  ? 27   GLU A CD    1 
ATOM   8785  O  OE1   . GLU D 3 27  ? 139.312 197.869 68.223  1.00 79.85  ? 27   GLU A OE1   1 
ATOM   8786  O  OE2   . GLU D 3 27  ? 141.098 197.082 69.225  1.00 78.33  ? 27   GLU A OE2   1 
ATOM   8787  N  N     . HIS D 3 28  ? 134.828 198.850 70.170  1.00 62.01  ? 28   HIS A N     1 
ATOM   8788  C  CA    . HIS D 3 28  ? 133.604 199.017 69.400  1.00 56.26  ? 28   HIS A CA    1 
ATOM   8789  C  C     . HIS D 3 28  ? 132.869 200.314 69.707  1.00 61.85  ? 28   HIS A C     1 
ATOM   8790  O  O     . HIS D 3 28  ? 131.767 200.519 69.190  1.00 66.25  ? 28   HIS A O     1 
ATOM   8791  C  CB    . HIS D 3 28  ? 132.677 197.828 69.640  1.00 59.59  ? 28   HIS A CB    1 
ATOM   8792  C  CG    . HIS D 3 28  ? 133.209 196.541 69.099  1.00 63.30  ? 28   HIS A CG    1 
ATOM   8793  N  ND1   . HIS D 3 28  ? 132.559 195.338 69.263  1.00 72.33  ? 28   HIS A ND1   1 
ATOM   8794  C  CD2   . HIS D 3 28  ? 134.327 196.270 68.387  1.00 64.03  ? 28   HIS A CD2   1 
ATOM   8795  C  CE1   . HIS D 3 28  ? 133.257 194.380 68.682  1.00 71.76  ? 28   HIS A CE1   1 
ATOM   8796  N  NE2   . HIS D 3 28  ? 134.335 194.919 68.142  1.00 67.85  ? 28   HIS A NE2   1 
ATOM   8797  N  N     . GLY D 3 29  ? 133.444 201.188 70.525  1.00 60.70  ? 29   GLY A N     1 
ATOM   8798  C  CA    . GLY D 3 29  ? 132.808 202.453 70.843  1.00 58.59  ? 29   GLY A CA    1 
ATOM   8799  C  C     . GLY D 3 29  ? 131.536 202.335 71.653  1.00 61.74  ? 29   GLY A C     1 
ATOM   8800  O  O     . GLY D 3 29  ? 130.570 203.061 71.388  1.00 68.38  ? 29   GLY A O     1 
ATOM   8801  N  N     . ILE D 3 30  ? 131.510 201.442 72.638  1.00 57.49  ? 30   ILE A N     1 
ATOM   8802  C  CA    . ILE D 3 30  ? 130.361 201.260 73.517  1.00 57.14  ? 30   ILE A CA    1 
ATOM   8803  C  C     . ILE D 3 30  ? 130.711 201.829 74.882  1.00 61.48  ? 30   ILE A C     1 
ATOM   8804  O  O     . ILE D 3 30  ? 131.714 201.435 75.488  1.00 63.64  ? 30   ILE A O     1 
ATOM   8805  C  CB    . ILE D 3 30  ? 129.960 199.781 73.635  1.00 55.87  ? 30   ILE A CB    1 
ATOM   8806  C  CG1   . ILE D 3 30  ? 129.695 199.185 72.259  1.00 59.63  ? 30   ILE A CG1   1 
ATOM   8807  C  CG2   . ILE D 3 30  ? 128.730 199.633 74.506  1.00 58.59  ? 30   ILE A CG2   1 
ATOM   8808  C  CD1   . ILE D 3 30  ? 129.296 197.737 72.304  1.00 60.02  ? 30   ILE A CD1   1 
ATOM   8809  N  N     . GLN D 3 31  ? 129.887 202.753 75.364  1.00 72.27  ? 31   GLN A N     1 
ATOM   8810  C  CA    . GLN D 3 31  ? 130.043 203.258 76.711  1.00 69.40  ? 31   GLN A CA    1 
ATOM   8811  C  C     . GLN D 3 31  ? 129.700 202.160 77.714  1.00 73.47  ? 31   GLN A C     1 
ATOM   8812  O  O     . GLN D 3 31  ? 128.952 201.233 77.398  1.00 79.16  ? 31   GLN A O     1 
ATOM   8813  C  CB    . GLN D 3 31  ? 129.157 204.481 76.922  1.00 64.90  ? 31   GLN A CB    1 
ATOM   8814  C  CG    . GLN D 3 31  ? 129.513 205.648 76.028  1.00 66.68  ? 31   GLN A CG    1 
ATOM   8815  C  CD    . GLN D 3 31  ? 128.656 206.864 76.299  1.00 74.25  ? 31   GLN A CD    1 
ATOM   8816  O  OE1   . GLN D 3 31  ? 127.732 206.818 77.108  1.00 73.93  ? 31   GLN A OE1   1 
ATOM   8817  N  NE2   . GLN D 3 31  ? 128.961 207.964 75.622  1.00 74.34  ? 31   GLN A NE2   1 
ATOM   8818  N  N     . PRO D 3 32  ? 130.250 202.232 78.929  1.00 70.87  ? 32   PRO A N     1 
ATOM   8819  C  CA    . PRO D 3 32  ? 130.022 201.144 79.892  1.00 70.24  ? 32   PRO A CA    1 
ATOM   8820  C  C     . PRO D 3 32  ? 128.561 200.925 80.239  1.00 73.54  ? 32   PRO A C     1 
ATOM   8821  O  O     . PRO D 3 32  ? 128.191 199.811 80.628  1.00 78.74  ? 32   PRO A O     1 
ATOM   8822  C  CB    . PRO D 3 32  ? 130.840 201.581 81.117  1.00 68.65  ? 32   PRO A CB    1 
ATOM   8823  C  CG    . PRO D 3 32  ? 131.105 203.037 80.915  1.00 71.91  ? 32   PRO A CG    1 
ATOM   8824  C  CD    . PRO D 3 32  ? 131.209 203.221 79.442  1.00 71.68  ? 32   PRO A CD    1 
ATOM   8825  N  N     . ASP D 3 33  ? 127.713 201.945 80.110  1.00 77.63  ? 33   ASP A N     1 
ATOM   8826  C  CA    . ASP D 3 33  ? 126.289 201.754 80.358  1.00 80.11  ? 33   ASP A CA    1 
ATOM   8827  C  C     . ASP D 3 33  ? 125.597 200.971 79.250  1.00 80.78  ? 33   ASP A C     1 
ATOM   8828  O  O     . ASP D 3 33  ? 124.432 200.596 79.418  1.00 80.51  ? 33   ASP A O     1 
ATOM   8829  C  CB    . ASP D 3 33  ? 125.596 203.104 80.551  1.00 82.26  ? 33   ASP A CB    1 
ATOM   8830  C  CG    . ASP D 3 33  ? 126.002 204.124 79.510  1.00 84.42  ? 33   ASP A CG    1 
ATOM   8831  O  OD1   . ASP D 3 33  ? 125.714 203.906 78.316  1.00 81.25  ? 33   ASP A OD1   1 
ATOM   8832  O  OD2   . ASP D 3 33  ? 126.610 205.147 79.887  1.00 86.19  ? 33   ASP A OD2   1 
ATOM   8833  N  N     . GLY D 3 34  ? 126.274 200.716 78.135  1.00 74.61  ? 34   GLY A N     1 
ATOM   8834  C  CA    . GLY D 3 34  ? 125.697 199.969 77.040  1.00 71.20  ? 34   GLY A CA    1 
ATOM   8835  C  C     . GLY D 3 34  ? 125.091 200.793 75.928  1.00 72.56  ? 34   GLY A C     1 
ATOM   8836  O  O     . GLY D 3 34  ? 124.428 200.223 75.055  1.00 74.10  ? 34   GLY A O     1 
ATOM   8837  N  N     . GLN D 3 35  ? 125.292 202.106 75.927  1.00 73.91  ? 35   GLN A N     1 
ATOM   8838  C  CA    . GLN D 3 35  ? 124.731 202.992 74.916  1.00 73.80  ? 35   GLN A CA    1 
ATOM   8839  C  C     . GLN D 3 35  ? 125.843 203.442 73.980  1.00 75.61  ? 35   GLN A C     1 
ATOM   8840  O  O     . GLN D 3 35  ? 126.865 203.971 74.432  1.00 79.82  ? 35   GLN A O     1 
ATOM   8841  C  CB    . GLN D 3 35  ? 124.053 204.200 75.563  1.00 77.91  ? 35   GLN A CB    1 
ATOM   8842  C  CG    . GLN D 3 35  ? 122.823 203.860 76.382  1.00 76.78  ? 35   GLN A CG    1 
ATOM   8843  C  CD    . GLN D 3 35  ? 121.618 203.549 75.520  1.00 78.40  ? 35   GLN A CD    1 
ATOM   8844  O  OE1   . GLN D 3 35  ? 121.523 204.001 74.379  1.00 79.12  ? 35   GLN A OE1   1 
ATOM   8845  N  NE2   . GLN D 3 35  ? 120.686 202.774 76.063  1.00 77.42  ? 35   GLN A NE2   1 
ATOM   8846  N  N     . MET D 3 36  ? 125.645 203.234 72.690  1.00 79.79  ? 36   MET A N     1 
ATOM   8847  C  CA    . MET D 3 36  ? 126.624 203.659 71.699  1.00 77.14  ? 36   MET A CA    1 
ATOM   8848  C  C     . MET D 3 36  ? 126.244 205.030 71.155  1.00 77.38  ? 36   MET A C     1 
ATOM   8849  O  O     . MET D 3 36  ? 125.176 205.175 70.553  1.00 79.51  ? 36   MET A O     1 
ATOM   8850  C  CB    . MET D 3 36  ? 126.704 202.646 70.563  1.00 80.39  ? 36   MET A CB    1 
ATOM   8851  C  CG    . MET D 3 36  ? 127.804 202.911 69.558  1.00 81.29  ? 36   MET A CG    1 
ATOM   8852  S  SD    . MET D 3 36  ? 127.912 201.611 68.317  1.00 92.02  ? 36   MET A SD    1 
ATOM   8853  C  CE    . MET D 3 36  ? 129.308 202.182 67.352  1.00 80.83  ? 36   MET A CE    1 
ATOM   8854  N  N     . PRO D 3 37  ? 127.083 206.057 71.342  1.00 84.29  ? 37   PRO A N     1 
ATOM   8855  C  CA    . PRO D 3 37  ? 126.766 207.410 70.886  1.00 86.01  ? 37   PRO A CA    1 
ATOM   8856  C  C     . PRO D 3 37  ? 127.177 207.653 69.437  1.00 86.78  ? 37   PRO A C     1 
ATOM   8857  O  O     . PRO D 3 37  ? 126.708 206.941 68.549  1.00 86.31  ? 37   PRO A O     1 
ATOM   8858  C  CB    . PRO D 3 37  ? 127.576 208.293 71.836  1.00 85.77  ? 37   PRO A CB    1 
ATOM   8859  C  CG    . PRO D 3 37  ? 128.705 207.418 72.328  1.00 84.99  ? 37   PRO A CG    1 
ATOM   8860  C  CD    . PRO D 3 37  ? 128.422 205.987 71.949  1.00 85.08  ? 37   PRO A CD    1 
ATOM   8861  N  N     . ASP D 3 47  ? 128.288 198.410 62.440  1.00 67.82  ? 47   ASP A N     1 
ATOM   8862  C  CA    . ASP D 3 47  ? 128.243 197.003 62.815  1.00 72.76  ? 47   ASP A CA    1 
ATOM   8863  C  C     . ASP D 3 47  ? 129.558 196.577 63.461  1.00 78.32  ? 47   ASP A C     1 
ATOM   8864  O  O     . ASP D 3 47  ? 130.155 197.339 64.224  1.00 79.53  ? 47   ASP A O     1 
ATOM   8865  C  CB    . ASP D 3 47  ? 127.942 196.133 61.594  1.00 71.31  ? 47   ASP A CB    1 
ATOM   8866  C  CG    . ASP D 3 47  ? 127.272 194.826 61.961  1.00 74.05  ? 47   ASP A CG    1 
ATOM   8867  O  OD1   . ASP D 3 47  ? 127.719 194.182 62.932  1.00 72.63  ? 47   ASP A OD1   1 
ATOM   8868  O  OD2   . ASP D 3 47  ? 126.297 194.443 61.281  1.00 73.81  ? 47   ASP A OD2   1 
ATOM   8869  N  N     . SER D 3 48  ? 129.996 195.355 63.152  1.00 72.90  ? 48   SER A N     1 
ATOM   8870  C  CA    . SER D 3 48  ? 131.259 194.806 63.647  1.00 72.62  ? 48   SER A CA    1 
ATOM   8871  C  C     . SER D 3 48  ? 131.279 194.692 65.168  1.00 73.21  ? 48   SER A C     1 
ATOM   8872  O  O     . SER D 3 48  ? 132.341 194.760 65.791  1.00 76.76  ? 48   SER A O     1 
ATOM   8873  C  CB    . SER D 3 48  ? 132.453 195.633 63.160  1.00 75.83  ? 48   SER A CB    1 
ATOM   8874  O  OG    . SER D 3 48  ? 132.534 195.626 61.745  1.00 75.78  ? 48   SER A OG    1 
ATOM   8875  N  N     . PHE D 3 49  ? 130.108 194.518 65.777  1.00 64.04  ? 49   PHE A N     1 
ATOM   8876  C  CA    . PHE D 3 49  ? 130.010 194.263 67.205  1.00 62.73  ? 49   PHE A CA    1 
ATOM   8877  C  C     . PHE D 3 49  ? 129.155 193.050 67.533  1.00 63.62  ? 49   PHE A C     1 
ATOM   8878  O  O     . PHE D 3 49  ? 129.060 192.681 68.707  1.00 72.33  ? 49   PHE A O     1 
ATOM   8879  C  CB    . PHE D 3 49  ? 129.448 195.488 67.945  1.00 64.18  ? 49   PHE A CB    1 
ATOM   8880  C  CG    . PHE D 3 49  ? 128.145 195.993 67.393  1.00 70.20  ? 49   PHE A CG    1 
ATOM   8881  C  CD1   . PHE D 3 49  ? 126.947 195.395 67.744  1.00 69.57  ? 49   PHE A CD1   1 
ATOM   8882  C  CD2   . PHE D 3 49  ? 128.116 197.085 66.546  1.00 71.33  ? 49   PHE A CD2   1 
ATOM   8883  C  CE1   . PHE D 3 49  ? 125.750 195.860 67.241  1.00 68.63  ? 49   PHE A CE1   1 
ATOM   8884  C  CE2   . PHE D 3 49  ? 126.920 197.557 66.042  1.00 70.63  ? 49   PHE A CE2   1 
ATOM   8885  C  CZ    . PHE D 3 49  ? 125.736 196.944 66.390  1.00 69.11  ? 49   PHE A CZ    1 
ATOM   8886  N  N     . ASN D 3 50  ? 128.530 192.426 66.536  1.00 53.89  ? 50   ASN A N     1 
ATOM   8887  C  CA    . ASN D 3 50  ? 127.633 191.311 66.797  1.00 54.87  ? 50   ASN A CA    1 
ATOM   8888  C  C     . ASN D 3 50  ? 128.370 190.082 67.298  1.00 55.51  ? 50   ASN A C     1 
ATOM   8889  O  O     . ASN D 3 50  ? 127.737 189.184 67.859  1.00 60.78  ? 50   ASN A O     1 
ATOM   8890  C  CB    . ASN D 3 50  ? 126.851 190.964 65.532  1.00 60.80  ? 50   ASN A CB    1 
ATOM   8891  C  CG    . ASN D 3 50  ? 125.436 190.524 65.824  1.00 63.90  ? 50   ASN A CG    1 
ATOM   8892  O  OD1   . ASN D 3 50  ? 125.117 190.119 66.941  1.00 64.90  ? 50   ASN A OD1   1 
ATOM   8893  N  ND2   . ASN D 3 50  ? 124.575 190.601 64.818  1.00 61.68  ? 50   ASN A ND2   1 
ATOM   8894  N  N     . THR D 3 51  ? 129.688 190.017 67.103  1.00 55.18  ? 51   THR A N     1 
ATOM   8895  C  CA    . THR D 3 51  ? 130.442 188.854 67.554  1.00 55.97  ? 51   THR A CA    1 
ATOM   8896  C  C     . THR D 3 51  ? 130.415 188.733 69.071  1.00 58.16  ? 51   THR A C     1 
ATOM   8897  O  O     . THR D 3 51  ? 130.239 187.636 69.611  1.00 63.11  ? 51   THR A O     1 
ATOM   8898  C  CB    . THR D 3 51  ? 131.881 188.935 67.050  1.00 62.51  ? 51   THR A CB    1 
ATOM   8899  O  OG1   . THR D 3 51  ? 131.881 189.058 65.623  1.00 71.79  ? 51   THR A OG1   1 
ATOM   8900  C  CG2   . THR D 3 51  ? 132.654 187.688 67.443  1.00 62.58  ? 51   THR A CG2   1 
ATOM   8901  N  N     . PHE D 3 52  ? 130.573 189.852 69.775  1.00 54.85  ? 52   PHE A N     1 
ATOM   8902  C  CA    . PHE D 3 52  ? 130.675 189.841 71.223  1.00 54.88  ? 52   PHE A CA    1 
ATOM   8903  C  C     . PHE D 3 52  ? 129.551 190.575 71.937  1.00 54.19  ? 52   PHE A C     1 
ATOM   8904  O  O     . PHE D 3 52  ? 129.518 190.555 73.172  1.00 61.90  ? 52   PHE A O     1 
ATOM   8905  C  CB    . PHE D 3 52  ? 132.016 190.446 71.664  1.00 55.71  ? 52   PHE A CB    1 
ATOM   8906  C  CG    . PHE D 3 52  ? 133.185 189.534 71.461  1.00 50.30  ? 52   PHE A CG    1 
ATOM   8907  C  CD1   . PHE D 3 52  ? 133.295 188.361 72.178  1.00 54.13  ? 52   PHE A CD1   1 
ATOM   8908  C  CD2   . PHE D 3 52  ? 134.173 189.851 70.550  1.00 52.88  ? 52   PHE A CD2   1 
ATOM   8909  C  CE1   . PHE D 3 52  ? 134.368 187.522 71.992  1.00 59.89  ? 52   PHE A CE1   1 
ATOM   8910  C  CE2   . PHE D 3 52  ? 135.248 189.016 70.360  1.00 60.06  ? 52   PHE A CE2   1 
ATOM   8911  C  CZ    . PHE D 3 52  ? 135.346 187.850 71.082  1.00 61.48  ? 52   PHE A CZ    1 
ATOM   8912  N  N     . PHE D 3 53  ? 128.635 191.215 71.216  1.00 46.27  ? 53   PHE A N     1 
ATOM   8913  C  CA    . PHE D 3 53  ? 127.563 191.978 71.837  1.00 46.95  ? 53   PHE A CA    1 
ATOM   8914  C  C     . PHE D 3 53  ? 126.233 191.669 71.168  1.00 52.67  ? 53   PHE A C     1 
ATOM   8915  O  O     . PHE D 3 53  ? 126.179 191.302 69.992  1.00 54.34  ? 53   PHE A O     1 
ATOM   8916  C  CB    . PHE D 3 53  ? 127.834 193.479 71.766  1.00 49.74  ? 53   PHE A CB    1 
ATOM   8917  C  CG    . PHE D 3 53  ? 129.025 193.920 72.561  1.00 52.52  ? 53   PHE A CG    1 
ATOM   8918  C  CD1   . PHE D 3 53  ? 130.299 193.814 72.040  1.00 50.37  ? 53   PHE A CD1   1 
ATOM   8919  C  CD2   . PHE D 3 53  ? 128.869 194.456 73.823  1.00 56.44  ? 53   PHE A CD2   1 
ATOM   8920  C  CE1   . PHE D 3 53  ? 131.393 194.222 72.766  1.00 52.85  ? 53   PHE A CE1   1 
ATOM   8921  C  CE2   . PHE D 3 53  ? 129.960 194.868 74.552  1.00 54.78  ? 53   PHE A CE2   1 
ATOM   8922  C  CZ    . PHE D 3 53  ? 131.222 194.751 74.023  1.00 54.61  ? 53   PHE A CZ    1 
ATOM   8923  N  N     . SER D 3 54  ? 125.157 191.825 71.934  1.00 65.73  ? 54   SER A N     1 
ATOM   8924  C  CA    . SER D 3 54  ? 123.797 191.625 71.458  1.00 61.49  ? 54   SER A CA    1 
ATOM   8925  C  C     . SER D 3 54  ? 123.036 192.941 71.533  1.00 62.53  ? 54   SER A C     1 
ATOM   8926  O  O     . SER D 3 54  ? 123.133 193.668 72.525  1.00 69.05  ? 54   SER A O     1 
ATOM   8927  C  CB    . SER D 3 54  ? 123.075 190.555 72.280  1.00 59.31  ? 54   SER A CB    1 
ATOM   8928  O  OG    . SER D 3 54  ? 121.763 190.339 71.797  1.00 58.07  ? 54   SER A OG    1 
ATOM   8929  N  N     . GLU D 3 55  ? 122.279 193.242 70.485  1.00 58.57  ? 55   GLU A N     1 
ATOM   8930  C  CA    . GLU D 3 55  ? 121.551 194.498 70.377  1.00 57.29  ? 55   GLU A CA    1 
ATOM   8931  C  C     . GLU D 3 55  ? 120.124 194.310 70.870  1.00 64.58  ? 55   GLU A C     1 
ATOM   8932  O  O     . GLU D 3 55  ? 119.442 193.365 70.462  1.00 65.70  ? 55   GLU A O     1 
ATOM   8933  C  CB    . GLU D 3 55  ? 121.543 194.995 68.932  1.00 66.23  ? 55   GLU A CB    1 
ATOM   8934  C  CG    . GLU D 3 55  ? 120.851 196.328 68.735  1.00 71.97  ? 55   GLU A CG    1 
ATOM   8935  C  CD    . GLU D 3 55  ? 121.722 197.495 69.140  1.00 75.44  ? 55   GLU A CD    1 
ATOM   8936  O  OE1   . GLU D 3 55  ? 122.956 197.390 68.987  1.00 74.02  ? 55   GLU A OE1   1 
ATOM   8937  O  OE2   . GLU D 3 55  ? 121.177 198.515 69.613  1.00 72.77  ? 55   GLU A OE2   1 
ATOM   8938  N  N     . THR D 3 56  ? 119.680 195.206 71.744  1.00 75.30  ? 56   THR A N     1 
ATOM   8939  C  CA    . THR D 3 56  ? 118.316 195.183 72.246  1.00 73.52  ? 56   THR A CA    1 
ATOM   8940  C  C     . THR D 3 56  ? 117.456 196.132 71.410  1.00 72.42  ? 56   THR A C     1 
ATOM   8941  O  O     . THR D 3 56  ? 117.891 196.650 70.378  1.00 72.94  ? 56   THR A O     1 
ATOM   8942  C  CB    . THR D 3 56  ? 118.291 195.532 73.733  1.00 69.15  ? 56   THR A CB    1 
ATOM   8943  O  OG1   . THR D 3 56  ? 117.084 195.035 74.322  1.00 70.53  ? 56   THR A OG1   1 
ATOM   8944  C  CG2   . THR D 3 56  ? 118.360 197.036 73.936  1.00 70.27  ? 56   THR A CG2   1 
ATOM   8945  N  N     . GLY D 3 57  ? 116.216 196.360 71.846  1.00 81.87  ? 57   GLY A N     1 
ATOM   8946  C  CA    . GLY D 3 57  ? 115.306 197.188 71.072  1.00 84.04  ? 57   GLY A CA    1 
ATOM   8947  C  C     . GLY D 3 57  ? 115.817 198.599 70.849  1.00 82.00  ? 57   GLY A C     1 
ATOM   8948  O  O     . GLY D 3 57  ? 115.653 199.161 69.764  1.00 79.75  ? 57   GLY A O     1 
ATOM   8949  N  N     . ALA D 3 58  ? 116.442 199.193 71.866  1.00 76.98  ? 58   ALA A N     1 
ATOM   8950  C  CA    . ALA D 3 58  ? 116.877 200.584 71.754  1.00 76.41  ? 58   ALA A CA    1 
ATOM   8951  C  C     . ALA D 3 58  ? 118.159 200.774 72.561  1.00 75.44  ? 58   ALA A C     1 
ATOM   8952  O  O     . ALA D 3 58  ? 118.103 201.029 73.767  1.00 77.43  ? 58   ALA A O     1 
ATOM   8953  C  CB    . ALA D 3 58  ? 115.783 201.534 72.220  1.00 75.85  ? 58   ALA A CB    1 
ATOM   8954  N  N     . GLY D 3 59  ? 119.301 200.656 71.888  1.00 69.58  ? 59   GLY A N     1 
ATOM   8955  C  CA    . GLY D 3 59  ? 120.557 201.098 72.458  1.00 71.25  ? 59   GLY A CA    1 
ATOM   8956  C  C     . GLY D 3 59  ? 121.361 200.074 73.230  1.00 72.15  ? 59   GLY A C     1 
ATOM   8957  O  O     . GLY D 3 59  ? 122.522 199.819 72.895  1.00 78.51  ? 59   GLY A O     1 
ATOM   8958  N  N     . LYS D 3 60  ? 120.769 199.497 74.272  1.00 70.61  ? 60   LYS A N     1 
ATOM   8959  C  CA    . LYS D 3 60  ? 121.520 198.665 75.204  1.00 72.01  ? 60   LYS A CA    1 
ATOM   8960  C  C     . LYS D 3 60  ? 122.158 197.478 74.493  1.00 70.28  ? 60   LYS A C     1 
ATOM   8961  O  O     . LYS D 3 60  ? 121.473 196.663 73.871  1.00 74.52  ? 60   LYS A O     1 
ATOM   8962  C  CB    . LYS D 3 60  ? 120.600 198.188 76.330  1.00 71.78  ? 60   LYS A CB    1 
ATOM   8963  C  CG    . LYS D 3 60  ? 121.219 197.193 77.296  1.00 69.73  ? 60   LYS A CG    1 
ATOM   8964  C  CD    . LYS D 3 60  ? 120.184 196.691 78.303  1.00 77.62  ? 60   LYS A CD    1 
ATOM   8965  C  CE    . LYS D 3 60  ? 119.047 195.933 77.619  1.00 76.89  ? 60   LYS A CE    1 
ATOM   8966  N  NZ    . LYS D 3 60  ? 118.047 195.387 78.586  1.00 55.29  ? 60   LYS A NZ    1 
ATOM   8967  N  N     . HIS D 3 61  ? 123.481 197.388 74.587  1.00 58.08  ? 61   HIS A N     1 
ATOM   8968  C  CA    . HIS D 3 61  ? 124.243 196.276 74.042  1.00 52.41  ? 61   HIS A CA    1 
ATOM   8969  C  C     . HIS D 3 61  ? 124.602 195.335 75.181  1.00 60.74  ? 61   HIS A C     1 
ATOM   8970  O  O     . HIS D 3 61  ? 125.266 195.742 76.139  1.00 69.92  ? 61   HIS A O     1 
ATOM   8971  C  CB    . HIS D 3 61  ? 125.514 196.762 73.346  1.00 56.39  ? 61   HIS A CB    1 
ATOM   8972  C  CG    . HIS D 3 61  ? 125.268 197.504 72.071  1.00 64.44  ? 61   HIS A CG    1 
ATOM   8973  N  ND1   . HIS D 3 61  ? 124.598 198.707 72.026  1.00 65.67  ? 61   HIS A ND1   1 
ATOM   8974  C  CD2   . HIS D 3 61  ? 125.622 197.224 70.795  1.00 64.95  ? 61   HIS A CD2   1 
ATOM   8975  C  CE1   . HIS D 3 61  ? 124.545 199.133 70.777  1.00 57.20  ? 61   HIS A CE1   1 
ATOM   8976  N  NE2   . HIS D 3 61  ? 125.155 198.249 70.010  1.00 57.84  ? 61   HIS A NE2   1 
ATOM   8977  N  N     . VAL D 3 62  ? 124.169 194.085 75.078  1.00 48.74  ? 62   VAL A N     1 
ATOM   8978  C  CA    . VAL D 3 62  ? 124.394 193.090 76.119  1.00 45.68  ? 62   VAL A CA    1 
ATOM   8979  C  C     . VAL D 3 62  ? 125.526 192.176 75.658  1.00 45.82  ? 62   VAL A C     1 
ATOM   8980  O  O     . VAL D 3 62  ? 125.383 191.472 74.648  1.00 53.75  ? 62   VAL A O     1 
ATOM   8981  C  CB    . VAL D 3 62  ? 123.122 192.292 76.427  1.00 53.52  ? 62   VAL A CB    1 
ATOM   8982  C  CG1   . VAL D 3 62  ? 123.400 191.259 77.504  1.00 56.21  ? 62   VAL A CG1   1 
ATOM   8983  C  CG2   . VAL D 3 62  ? 122.008 193.227 76.861  1.00 51.76  ? 62   VAL A CG2   1 
ATOM   8984  N  N     . PRO D 3 63  ? 126.662 192.160 76.350  1.00 42.15  ? 63   PRO A N     1 
ATOM   8985  C  CA    . PRO D 3 63  ? 127.753 191.266 75.962  1.00 47.49  ? 63   PRO A CA    1 
ATOM   8986  C  C     . PRO D 3 63  ? 127.364 189.803 76.093  1.00 51.48  ? 63   PRO A C     1 
ATOM   8987  O  O     . PRO D 3 63  ? 126.568 189.421 76.952  1.00 55.13  ? 63   PRO A O     1 
ATOM   8988  C  CB    . PRO D 3 63  ? 128.870 191.631 76.943  1.00 51.73  ? 63   PRO A CB    1 
ATOM   8989  C  CG    . PRO D 3 63  ? 128.539 193.002 77.402  1.00 53.68  ? 63   PRO A CG    1 
ATOM   8990  C  CD    . PRO D 3 63  ? 127.052 193.062 77.442  1.00 51.50  ? 63   PRO A CD    1 
ATOM   8991  N  N     . ARG D 3 64  ? 127.945 188.979 75.223  1.00 51.26  ? 64   ARG A N     1 
ATOM   8992  C  CA    . ARG D 3 64  ? 127.738 187.532 75.258  1.00 51.14  ? 64   ARG A CA    1 
ATOM   8993  C  C     . ARG D 3 64  ? 128.777 186.889 76.175  1.00 57.82  ? 64   ARG A C     1 
ATOM   8994  O  O     . ARG D 3 64  ? 129.703 186.199 75.747  1.00 66.90  ? 64   ARG A O     1 
ATOM   8995  C  CB    . ARG D 3 64  ? 127.794 186.951 73.853  1.00 48.07  ? 64   ARG A CB    1 
ATOM   8996  C  CG    . ARG D 3 64  ? 126.664 187.396 72.956  1.00 52.57  ? 64   ARG A CG    1 
ATOM   8997  C  CD    . ARG D 3 64  ? 126.740 186.735 71.599  1.00 53.18  ? 64   ARG A CD    1 
ATOM   8998  N  NE    . ARG D 3 64  ? 125.615 187.119 70.758  1.00 53.41  ? 64   ARG A NE    1 
ATOM   8999  C  CZ    . ARG D 3 64  ? 125.612 188.170 69.952  1.00 57.85  ? 64   ARG A CZ    1 
ATOM   9000  N  NH1   . ARG D 3 64  ? 126.670 188.954 69.836  1.00 62.33  ? 64   ARG A NH1   1 
ATOM   9001  N  NH2   . ARG D 3 64  ? 124.520 188.441 69.244  1.00 54.26  ? 64   ARG A NH2   1 
ATOM   9002  N  N     . ALA D 3 65  ? 128.597 187.124 77.470  1.00 44.87  ? 65   ALA A N     1 
ATOM   9003  C  CA    . ALA D 3 65  ? 129.488 186.595 78.486  1.00 42.35  ? 65   ALA A CA    1 
ATOM   9004  C  C     . ALA D 3 65  ? 128.683 185.961 79.606  1.00 39.79  ? 65   ALA A C     1 
ATOM   9005  O  O     . ALA D 3 65  ? 127.553 186.365 79.888  1.00 47.64  ? 65   ALA A O     1 
ATOM   9006  C  CB    . ALA D 3 65  ? 130.396 187.685 79.060  1.00 42.95  ? 65   ALA A CB    1 
ATOM   9007  N  N     . VAL D 3 66  ? 129.278 184.956 80.240  1.00 37.90  ? 66   VAL A N     1 
ATOM   9008  C  CA    . VAL D 3 66  ? 128.717 184.306 81.418  1.00 43.18  ? 66   VAL A CA    1 
ATOM   9009  C  C     . VAL D 3 66  ? 129.814 184.297 82.475  1.00 49.78  ? 66   VAL A C     1 
ATOM   9010  O  O     . VAL D 3 66  ? 130.759 183.506 82.391  1.00 56.74  ? 66   VAL A O     1 
ATOM   9011  C  CB    . VAL D 3 66  ? 128.219 182.887 81.129  1.00 47.07  ? 66   VAL A CB    1 
ATOM   9012  C  CG1   . VAL D 3 66  ? 127.557 182.303 82.354  1.00 40.21  ? 66   VAL A CG1   1 
ATOM   9013  C  CG2   . VAL D 3 66  ? 127.254 182.891 79.962  1.00 50.87  ? 66   VAL A CG2   1 
ATOM   9014  N  N     . PHE D 3 67  ? 129.694 185.172 83.468  1.00 42.81  ? 67   PHE A N     1 
ATOM   9015  C  CA    . PHE D 3 67  ? 130.637 185.228 84.577  1.00 36.88  ? 67   PHE A CA    1 
ATOM   9016  C  C     . PHE D 3 67  ? 130.180 184.263 85.662  1.00 40.57  ? 67   PHE A C     1 
ATOM   9017  O  O     . PHE D 3 67  ? 129.098 184.433 86.232  1.00 49.68  ? 67   PHE A O     1 
ATOM   9018  C  CB    . PHE D 3 67  ? 130.736 186.645 85.134  1.00 37.20  ? 67   PHE A CB    1 
ATOM   9019  C  CG    . PHE D 3 67  ? 131.579 187.569 84.311  1.00 41.42  ? 67   PHE A CG    1 
ATOM   9020  C  CD1   . PHE D 3 67  ? 131.350 187.724 82.960  1.00 40.79  ? 67   PHE A CD1   1 
ATOM   9021  C  CD2   . PHE D 3 67  ? 132.596 188.295 84.897  1.00 50.08  ? 67   PHE A CD2   1 
ATOM   9022  C  CE1   . PHE D 3 67  ? 132.125 188.578 82.209  1.00 44.52  ? 67   PHE A CE1   1 
ATOM   9023  C  CE2   . PHE D 3 67  ? 133.374 189.149 84.150  1.00 50.11  ? 67   PHE A CE2   1 
ATOM   9024  C  CZ    . PHE D 3 67  ? 133.137 189.290 82.804  1.00 46.93  ? 67   PHE A CZ    1 
ATOM   9025  N  N     . VAL D 3 68  ? 131.002 183.259 85.956  1.00 39.94  ? 68   VAL A N     1 
ATOM   9026  C  CA    . VAL D 3 68  ? 130.661 182.226 86.925  1.00 40.14  ? 68   VAL A CA    1 
ATOM   9027  C  C     . VAL D 3 68  ? 131.776 182.125 87.951  1.00 48.38  ? 68   VAL A C     1 
ATOM   9028  O  O     . VAL D 3 68  ? 132.953 182.038 87.589  1.00 54.66  ? 68   VAL A O     1 
ATOM   9029  C  CB    . VAL D 3 68  ? 130.433 180.860 86.256  1.00 47.02  ? 68   VAL A CB    1 
ATOM   9030  C  CG1   . VAL D 3 68  ? 129.959 179.852 87.278  1.00 48.17  ? 68   VAL A CG1   1 
ATOM   9031  C  CG2   . VAL D 3 68  ? 129.432 180.986 85.131  1.00 55.82  ? 68   VAL A CG2   1 
ATOM   9032  N  N     . ASP D 3 69  ? 131.404 182.133 89.227  1.00 62.80  ? 69   ASP A N     1 
ATOM   9033  C  CA    . ASP D 3 69  ? 132.358 181.944 90.307  1.00 60.79  ? 69   ASP A CA    1 
ATOM   9034  C  C     . ASP D 3 69  ? 131.610 181.442 91.528  1.00 57.23  ? 69   ASP A C     1 
ATOM   9035  O  O     . ASP D 3 69  ? 130.481 181.862 91.787  1.00 63.52  ? 69   ASP A O     1 
ATOM   9036  C  CB    . ASP D 3 69  ? 133.101 183.243 90.637  1.00 64.60  ? 69   ASP A CB    1 
ATOM   9037  C  CG    . ASP D 3 69  ? 134.183 183.045 91.679  1.00 71.66  ? 69   ASP A CG    1 
ATOM   9038  O  OD1   . ASP D 3 69  ? 134.537 181.881 91.961  1.00 70.62  ? 69   ASP A OD1   1 
ATOM   9039  O  OD2   . ASP D 3 69  ? 134.680 184.054 92.217  1.00 71.88  ? 69   ASP A OD2   1 
ATOM   9040  N  N     . LEU D 3 70  ? 132.245 180.538 92.270  1.00 58.32  ? 70   LEU A N     1 
ATOM   9041  C  CA    . LEU D 3 70  ? 131.668 180.098 93.533  1.00 60.04  ? 70   LEU A CA    1 
ATOM   9042  C  C     . LEU D 3 70  ? 131.853 181.151 94.618  1.00 65.88  ? 70   LEU A C     1 
ATOM   9043  O  O     . LEU D 3 70  ? 131.004 181.279 95.507  1.00 64.05  ? 70   LEU A O     1 
ATOM   9044  C  CB    . LEU D 3 70  ? 132.280 178.765 93.961  1.00 65.48  ? 70   LEU A CB    1 
ATOM   9045  C  CG    . LEU D 3 70  ? 131.784 177.490 93.267  1.00 64.94  ? 70   LEU A CG    1 
ATOM   9046  C  CD1   . LEU D 3 70  ? 130.290 177.316 93.488  1.00 67.89  ? 70   LEU A CD1   1 
ATOM   9047  C  CD2   . LEU D 3 70  ? 132.123 177.437 91.786  1.00 61.69  ? 70   LEU A CD2   1 
ATOM   9048  N  N     . GLU D 3 71  ? 132.946 181.902 94.565  1.00 80.57  ? 71   GLU A N     1 
ATOM   9049  C  CA    . GLU D 3 71  ? 133.101 183.067 95.429  1.00 74.41  ? 71   GLU A CA    1 
ATOM   9050  C  C     . GLU D 3 71  ? 132.203 184.192 94.930  1.00 78.03  ? 71   GLU A C     1 
ATOM   9051  O  O     . GLU D 3 71  ? 132.271 184.554 93.749  1.00 82.43  ? 71   GLU A O     1 
ATOM   9052  C  CB    . GLU D 3 71  ? 134.551 183.546 95.447  1.00 73.99  ? 71   GLU A CB    1 
ATOM   9053  C  CG    . GLU D 3 71  ? 135.544 182.569 96.028  1.00 77.30  ? 71   GLU A CG    1 
ATOM   9054  C  CD    . GLU D 3 71  ? 136.956 183.122 96.052  1.00 84.36  ? 71   GLU A CD    1 
ATOM   9055  O  OE1   . GLU D 3 71  ? 137.187 184.189 95.446  1.00 83.73  ? 71   GLU A OE1   1 
ATOM   9056  O  OE2   . GLU D 3 71  ? 137.832 182.493 96.680  1.00 83.17  ? 71   GLU A OE2   1 
ATOM   9057  N  N     . PRO D 3 72  ? 131.355 184.770 95.783  1.00 59.34  ? 72   PRO A N     1 
ATOM   9058  C  CA    . PRO D 3 72  ? 130.532 185.904 95.346  1.00 58.58  ? 72   PRO A CA    1 
ATOM   9059  C  C     . PRO D 3 72  ? 131.258 187.238 95.317  1.00 64.36  ? 72   PRO A C     1 
ATOM   9060  O  O     . PRO D 3 72  ? 130.713 188.196 94.756  1.00 71.97  ? 72   PRO A O     1 
ATOM   9061  C  CB    . PRO D 3 72  ? 129.401 185.923 96.378  1.00 52.88  ? 72   PRO A CB    1 
ATOM   9062  C  CG    . PRO D 3 72  ? 129.991 185.317 97.588  1.00 51.19  ? 72   PRO A CG    1 
ATOM   9063  C  CD    . PRO D 3 72  ? 130.985 184.297 97.125  1.00 56.93  ? 72   PRO A CD    1 
ATOM   9064  N  N     . THR D 3 73  ? 132.463 187.334 95.884  1.00 63.27  ? 73   THR A N     1 
ATOM   9065  C  CA    . THR D 3 73  ? 133.086 188.638 96.103  1.00 64.38  ? 73   THR A CA    1 
ATOM   9066  C  C     . THR D 3 73  ? 133.394 189.353 94.792  1.00 67.03  ? 73   THR A C     1 
ATOM   9067  O  O     . THR D 3 73  ? 132.999 190.508 94.593  1.00 67.52  ? 73   THR A O     1 
ATOM   9068  C  CB    . THR D 3 73  ? 134.362 188.473 96.925  1.00 64.51  ? 73   THR A CB    1 
ATOM   9069  O  OG1   . THR D 3 73  ? 135.132 187.385 96.401  1.00 62.94  ? 73   THR A OG1   1 
ATOM   9070  C  CG2   . THR D 3 73  ? 134.027 188.200 98.376  1.00 63.68  ? 73   THR A CG2   1 
ATOM   9071  N  N     . VAL D 3 74  ? 134.103 188.684 93.882  1.00 58.64  ? 74   VAL A N     1 
ATOM   9072  C  CA    . VAL D 3 74  ? 134.581 189.372 92.687  1.00 56.17  ? 74   VAL A CA    1 
ATOM   9073  C  C     . VAL D 3 74  ? 133.440 189.651 91.713  1.00 60.31  ? 74   VAL A C     1 
ATOM   9074  O  O     . VAL D 3 74  ? 133.406 190.710 91.066  1.00 65.77  ? 74   VAL A O     1 
ATOM   9075  C  CB    . VAL D 3 74  ? 135.724 188.567 92.045  1.00 55.06  ? 74   VAL A CB    1 
ATOM   9076  C  CG1   . VAL D 3 74  ? 135.268 187.167 91.700  1.00 52.99  ? 74   VAL A CG1   1 
ATOM   9077  C  CG2   . VAL D 3 74  ? 136.266 189.299 90.832  1.00 64.91  ? 74   VAL A CG2   1 
ATOM   9078  N  N     . ILE D 3 75  ? 132.483 188.731 91.592  1.00 55.23  ? 75   ILE A N     1 
ATOM   9079  C  CA    . ILE D 3 75  ? 131.313 189.032 90.778  1.00 52.83  ? 75   ILE A CA    1 
ATOM   9080  C  C     . ILE D 3 75  ? 130.513 190.164 91.405  1.00 56.15  ? 75   ILE A C     1 
ATOM   9081  O  O     . ILE D 3 75  ? 129.867 190.941 90.696  1.00 59.82  ? 75   ILE A O     1 
ATOM   9082  C  CB    . ILE D 3 75  ? 130.455 187.775 90.567  1.00 57.34  ? 75   ILE A CB    1 
ATOM   9083  C  CG1   . ILE D 3 75  ? 131.301 186.639 90.004  1.00 59.72  ? 75   ILE A CG1   1 
ATOM   9084  C  CG2   . ILE D 3 75  ? 129.319 188.066 89.611  1.00 59.13  ? 75   ILE A CG2   1 
ATOM   9085  C  CD1   . ILE D 3 75  ? 131.742 186.867 88.586  1.00 64.40  ? 75   ILE A CD1   1 
ATOM   9086  N  N     . ASP D 3 76  ? 130.547 190.293 92.732  1.00 57.43  ? 76   ASP A N     1 
ATOM   9087  C  CA    . ASP D 3 76  ? 129.921 191.447 93.367  1.00 57.16  ? 76   ASP A CA    1 
ATOM   9088  C  C     . ASP D 3 76  ? 130.653 192.735 93.015  1.00 60.91  ? 76   ASP A C     1 
ATOM   9089  O  O     . ASP D 3 76  ? 130.024 193.785 92.840  1.00 69.62  ? 76   ASP A O     1 
ATOM   9090  C  CB    . ASP D 3 76  ? 129.863 191.256 94.879  1.00 60.31  ? 76   ASP A CB    1 
ATOM   9091  C  CG    . ASP D 3 76  ? 128.731 190.347 95.306  1.00 65.27  ? 76   ASP A CG    1 
ATOM   9092  O  OD1   . ASP D 3 76  ? 127.713 190.289 94.585  1.00 66.49  ? 76   ASP A OD1   1 
ATOM   9093  O  OD2   . ASP D 3 76  ? 128.857 189.691 96.360  1.00 66.21  ? 76   ASP A OD2   1 
ATOM   9094  N  N     . GLU D 3 77  ? 131.982 192.677 92.918  1.00 60.17  ? 77   GLU A N     1 
ATOM   9095  C  CA    . GLU D 3 77  ? 132.731 193.841 92.455  1.00 63.36  ? 77   GLU A CA    1 
ATOM   9096  C  C     . GLU D 3 77  ? 132.316 194.221 91.041  1.00 63.40  ? 77   GLU A C     1 
ATOM   9097  O  O     . GLU D 3 77  ? 132.202 195.408 90.714  1.00 64.90  ? 77   GLU A O     1 
ATOM   9098  C  CB    . GLU D 3 77  ? 134.232 193.562 92.512  1.00 65.40  ? 77   GLU A CB    1 
ATOM   9099  C  CG    . GLU D 3 77  ? 134.737 193.114 93.867  1.00 68.45  ? 77   GLU A CG    1 
ATOM   9100  C  CD    . GLU D 3 77  ? 136.153 192.580 93.806  1.00 74.52  ? 77   GLU A CD    1 
ATOM   9101  O  OE1   . GLU D 3 77  ? 136.866 192.893 92.828  1.00 72.60  ? 77   GLU A OE1   1 
ATOM   9102  O  OE2   . GLU D 3 77  ? 136.553 191.841 94.729  1.00 69.51  ? 77   GLU A OE2   1 
ATOM   9103  N  N     . VAL D 3 78  ? 132.097 193.221 90.187  1.00 57.20  ? 78   VAL A N     1 
ATOM   9104  C  CA    . VAL D 3 78  ? 131.580 193.486 88.845  1.00 52.48  ? 78   VAL A CA    1 
ATOM   9105  C  C     . VAL D 3 78  ? 130.194 194.117 88.918  1.00 54.43  ? 78   VAL A C     1 
ATOM   9106  O  O     . VAL D 3 78  ? 129.889 195.070 88.193  1.00 56.86  ? 78   VAL A O     1 
ATOM   9107  C  CB    . VAL D 3 78  ? 131.568 192.193 88.010  1.00 60.27  ? 78   VAL A CB    1 
ATOM   9108  C  CG1   . VAL D 3 78  ? 130.928 192.442 86.659  1.00 59.52  ? 78   VAL A CG1   1 
ATOM   9109  C  CG2   . VAL D 3 78  ? 132.975 191.661 87.841  1.00 58.94  ? 78   VAL A CG2   1 
ATOM   9110  N  N     . ARG D 3 79  ? 129.335 193.596 89.799  1.00 56.96  ? 79   ARG A N     1 
ATOM   9111  C  CA    . ARG D 3 79  ? 127.975 194.103 89.952  1.00 54.16  ? 79   ARG A CA    1 
ATOM   9112  C  C     . ARG D 3 79  ? 127.936 195.537 90.456  1.00 53.06  ? 79   ARG A C     1 
ATOM   9113  O  O     . ARG D 3 79  ? 126.990 196.264 90.141  1.00 59.15  ? 79   ARG A O     1 
ATOM   9114  C  CB    . ARG D 3 79  ? 127.184 193.220 90.917  1.00 49.61  ? 79   ARG A CB    1 
ATOM   9115  C  CG    . ARG D 3 79  ? 126.762 191.880 90.359  1.00 50.79  ? 79   ARG A CG    1 
ATOM   9116  C  CD    . ARG D 3 79  ? 125.628 191.304 91.173  1.00 47.49  ? 79   ARG A CD    1 
ATOM   9117  N  NE    . ARG D 3 79  ? 125.350 189.916 90.832  1.00 49.86  ? 79   ARG A NE    1 
ATOM   9118  C  CZ    . ARG D 3 79  ? 125.647 188.881 91.605  1.00 55.52  ? 79   ARG A CZ    1 
ATOM   9119  N  NH1   . ARG D 3 79  ? 126.254 189.039 92.768  1.00 58.83  ? 79   ARG A NH1   1 
ATOM   9120  N  NH2   . ARG D 3 79  ? 125.326 187.656 91.200  1.00 54.99  ? 79   ARG A NH2   1 
ATOM   9121  N  N     . THR D 3 80  ? 128.922 195.954 91.244  1.00 54.95  ? 80   THR A N     1 
ATOM   9122  C  CA    . THR D 3 80  ? 128.956 197.299 91.790  1.00 55.74  ? 80   THR A CA    1 
ATOM   9123  C  C     . THR D 3 80  ? 129.960 198.205 91.090  1.00 59.53  ? 80   THR A C     1 
ATOM   9124  O  O     . THR D 3 80  ? 129.980 199.410 91.364  1.00 61.86  ? 80   THR A O     1 
ATOM   9125  C  CB    . THR D 3 80  ? 129.274 197.248 93.293  1.00 62.05  ? 80   THR A CB    1 
ATOM   9126  O  OG1   . THR D 3 80  ? 128.686 196.074 93.863  1.00 63.45  ? 80   THR A OG1   1 
ATOM   9127  C  CG2   . THR D 3 80  ? 128.709 198.469 94.007  1.00 61.92  ? 80   THR A CG2   1 
ATOM   9128  N  N     . GLY D 3 81  ? 130.773 197.671 90.185  1.00 67.05  ? 81   GLY A N     1 
ATOM   9129  C  CA    . GLY D 3 81  ? 131.806 198.442 89.532  1.00 61.99  ? 81   GLY A CA    1 
ATOM   9130  C  C     . GLY D 3 81  ? 131.264 199.334 88.433  1.00 61.30  ? 81   GLY A C     1 
ATOM   9131  O  O     . GLY D 3 81  ? 130.060 199.542 88.283  1.00 63.78  ? 81   GLY A O     1 
ATOM   9132  N  N     . THR D 3 82  ? 132.197 199.881 87.650  1.00 59.59  ? 82   THR A N     1 
ATOM   9133  C  CA    . THR D 3 82  ? 131.819 200.772 86.557  1.00 59.44  ? 82   THR A CA    1 
ATOM   9134  C  C     . THR D 3 82  ? 131.044 200.035 85.474  1.00 64.11  ? 82   THR A C     1 
ATOM   9135  O  O     . THR D 3 82  ? 130.203 200.636 84.796  1.00 65.71  ? 82   THR A O     1 
ATOM   9136  C  CB    . THR D 3 82  ? 133.061 201.430 85.960  1.00 61.37  ? 82   THR A CB    1 
ATOM   9137  O  OG1   . THR D 3 82  ? 133.970 200.418 85.510  1.00 67.84  ? 82   THR A OG1   1 
ATOM   9138  C  CG2   . THR D 3 82  ? 133.753 202.296 87.000  1.00 62.83  ? 82   THR A CG2   1 
ATOM   9139  N  N     . TYR D 3 83  ? 131.318 198.747 85.285  1.00 69.24  ? 83   TYR A N     1 
ATOM   9140  C  CA    . TYR D 3 83  ? 130.580 197.933 84.322  1.00 65.02  ? 83   TYR A CA    1 
ATOM   9141  C  C     . TYR D 3 83  ? 129.448 197.180 85.023  1.00 64.21  ? 83   TYR A C     1 
ATOM   9142  O  O     . TYR D 3 83  ? 129.342 195.956 84.982  1.00 71.64  ? 83   TYR A O     1 
ATOM   9143  C  CB    . TYR D 3 83  ? 131.526 196.980 83.602  1.00 65.73  ? 83   TYR A CB    1 
ATOM   9144  C  CG    . TYR D 3 83  ? 132.569 197.686 82.774  1.00 61.90  ? 83   TYR A CG    1 
ATOM   9145  C  CD1   . TYR D 3 83  ? 132.251 198.210 81.532  1.00 67.93  ? 83   TYR A CD1   1 
ATOM   9146  C  CD2   . TYR D 3 83  ? 133.868 197.827 83.230  1.00 60.50  ? 83   TYR A CD2   1 
ATOM   9147  C  CE1   . TYR D 3 83  ? 133.194 198.859 80.770  1.00 71.92  ? 83   TYR A CE1   1 
ATOM   9148  C  CE2   . TYR D 3 83  ? 134.820 198.474 82.474  1.00 65.68  ? 83   TYR A CE2   1 
ATOM   9149  C  CZ    . TYR D 3 83  ? 134.476 198.988 81.244  1.00 73.80  ? 83   TYR A CZ    1 
ATOM   9150  O  OH    . TYR D 3 83  ? 135.417 199.637 80.480  1.00 74.67  ? 83   TYR A OH    1 
ATOM   9151  N  N     . ARG D 3 84  ? 128.591 197.957 85.678  1.00 61.32  ? 84   ARG A N     1 
ATOM   9152  C  CA    . ARG D 3 84  ? 127.459 197.416 86.419  1.00 64.81  ? 84   ARG A CA    1 
ATOM   9153  C  C     . ARG D 3 84  ? 126.232 197.237 85.541  1.00 68.35  ? 84   ARG A C     1 
ATOM   9154  O  O     . ARG D 3 84  ? 125.608 196.171 85.558  1.00 69.89  ? 84   ARG A O     1 
ATOM   9155  C  CB    . ARG D 3 84  ? 127.121 198.332 87.597  1.00 66.33  ? 84   ARG A CB    1 
ATOM   9156  C  CG    . ARG D 3 84  ? 125.686 198.230 88.078  1.00 67.99  ? 84   ARG A CG    1 
ATOM   9157  C  CD    . ARG D 3 84  ? 125.417 199.194 89.220  1.00 69.71  ? 84   ARG A CD    1 
ATOM   9158  N  NE    . ARG D 3 84  ? 125.604 200.583 88.817  1.00 71.89  ? 84   ARG A NE    1 
ATOM   9159  C  CZ    . ARG D 3 84  ? 126.647 201.328 89.154  1.00 70.32  ? 84   ARG A CZ    1 
ATOM   9160  N  NH1   . ARG D 3 84  ? 127.625 200.848 89.904  1.00 70.69  ? 84   ARG A NH1   1 
ATOM   9161  N  NH2   . ARG D 3 84  ? 126.708 202.587 88.731  1.00 67.04  ? 84   ARG A NH2   1 
ATOM   9162  N  N     . GLN D 3 85  ? 125.874 198.264 84.770  1.00 73.24  ? 85   GLN A N     1 
ATOM   9163  C  CA    . GLN D 3 85  ? 124.720 198.222 83.883  1.00 72.14  ? 85   GLN A CA    1 
ATOM   9164  C  C     . GLN D 3 85  ? 125.103 197.822 82.465  1.00 71.17  ? 85   GLN A C     1 
ATOM   9165  O  O     . GLN D 3 85  ? 124.448 198.233 81.502  1.00 73.58  ? 85   GLN A O     1 
ATOM   9166  C  CB    . GLN D 3 85  ? 124.002 199.570 83.889  1.00 68.50  ? 85   GLN A CB    1 
ATOM   9167  C  CG    . GLN D 3 85  ? 124.926 200.757 84.027  1.00 69.40  ? 85   GLN A CG    1 
ATOM   9168  C  CD    . GLN D 3 85  ? 124.186 202.012 84.429  1.00 74.98  ? 85   GLN A CD    1 
ATOM   9169  O  OE1   . GLN D 3 85  ? 122.968 201.999 84.596  1.00 73.21  ? 85   GLN A OE1   1 
ATOM   9170  N  NE2   . GLN D 3 85  ? 124.919 203.109 84.586  1.00 77.35  ? 85   GLN A NE2   1 
ATOM   9171  N  N     . LEU D 3 86  ? 126.159 197.024 82.323  1.00 60.48  ? 86   LEU A N     1 
ATOM   9172  C  CA    . LEU D 3 86  ? 126.556 196.454 81.044  1.00 57.00  ? 86   LEU A CA    1 
ATOM   9173  C  C     . LEU D 3 86  ? 126.118 195.003 80.903  1.00 57.52  ? 86   LEU A C     1 
ATOM   9174  O  O     . LEU D 3 86  ? 125.547 194.624 79.878  1.00 59.03  ? 86   LEU A O     1 
ATOM   9175  C  CB    . LEU D 3 86  ? 128.075 196.555 80.871  1.00 61.60  ? 86   LEU A CB    1 
ATOM   9176  C  CG    . LEU D 3 86  ? 128.640 196.004 79.565  1.00 63.47  ? 86   LEU A CG    1 
ATOM   9177  C  CD1   . LEU D 3 86  ? 128.109 196.787 78.379  1.00 59.64  ? 86   LEU A CD1   1 
ATOM   9178  C  CD2   . LEU D 3 86  ? 130.154 196.023 79.593  1.00 62.95  ? 86   LEU A CD2   1 
ATOM   9179  N  N     . PHE D 3 87  ? 126.368 194.186 81.918  1.00 55.06  ? 87   PHE A N     1 
ATOM   9180  C  CA    . PHE D 3 87  ? 126.036 192.773 81.864  1.00 56.07  ? 87   PHE A CA    1 
ATOM   9181  C  C     . PHE D 3 87  ? 124.599 192.535 82.299  1.00 54.77  ? 87   PHE A C     1 
ATOM   9182  O  O     . PHE D 3 87  ? 124.061 193.237 83.159  1.00 56.25  ? 87   PHE A O     1 
ATOM   9183  C  CB    . PHE D 3 87  ? 126.978 191.954 82.750  1.00 57.20  ? 87   PHE A CB    1 
ATOM   9184  C  CG    . PHE D 3 87  ? 128.410 191.984 82.308  1.00 54.75  ? 87   PHE A CG    1 
ATOM   9185  C  CD1   . PHE D 3 87  ? 128.860 191.121 81.331  1.00 59.89  ? 87   PHE A CD1   1 
ATOM   9186  C  CD2   . PHE D 3 87  ? 129.307 192.861 82.880  1.00 47.69  ? 87   PHE A CD2   1 
ATOM   9187  C  CE1   . PHE D 3 87  ? 130.172 191.142 80.928  1.00 59.48  ? 87   PHE A CE1   1 
ATOM   9188  C  CE2   . PHE D 3 87  ? 130.620 192.884 82.479  1.00 50.06  ? 87   PHE A CE2   1 
ATOM   9189  C  CZ    . PHE D 3 87  ? 131.053 192.024 81.504  1.00 55.95  ? 87   PHE A CZ    1 
ATOM   9190  N  N     . HIS D 3 88  ? 123.981 191.541 81.686  1.00 56.87  ? 88   HIS A N     1 
ATOM   9191  C  CA    . HIS D 3 88  ? 122.682 191.067 82.134  1.00 55.98  ? 88   HIS A CA    1 
ATOM   9192  C  C     . HIS D 3 88  ? 122.863 190.431 83.504  1.00 57.66  ? 88   HIS A C     1 
ATOM   9193  O  O     . HIS D 3 88  ? 123.712 189.544 83.652  1.00 62.85  ? 88   HIS A O     1 
ATOM   9194  C  CB    . HIS D 3 88  ? 122.120 190.070 81.123  1.00 56.46  ? 88   HIS A CB    1 
ATOM   9195  C  CG    . HIS D 3 88  ? 120.771 189.525 81.477  1.00 58.78  ? 88   HIS A CG    1 
ATOM   9196  N  ND1   . HIS D 3 88  ? 119.894 190.181 82.313  1.00 63.51  ? 88   HIS A ND1   1 
ATOM   9197  C  CD2   . HIS D 3 88  ? 120.145 188.387 81.096  1.00 57.06  ? 88   HIS A CD2   1 
ATOM   9198  C  CE1   . HIS D 3 88  ? 118.790 189.467 82.438  1.00 60.39  ? 88   HIS A CE1   1 
ATOM   9199  N  NE2   . HIS D 3 88  ? 118.917 188.374 81.709  1.00 56.90  ? 88   HIS A NE2   1 
ATOM   9200  N  N     . PRO D 3 89  ? 122.123 190.859 84.529  1.00 43.13  ? 89   PRO A N     1 
ATOM   9201  C  CA    . PRO D 3 89  ? 122.361 190.323 85.877  1.00 45.77  ? 89   PRO A CA    1 
ATOM   9202  C  C     . PRO D 3 89  ? 122.204 188.818 85.979  1.00 54.48  ? 89   PRO A C     1 
ATOM   9203  O  O     . PRO D 3 89  ? 122.807 188.211 86.873  1.00 59.09  ? 89   PRO A O     1 
ATOM   9204  C  CB    . PRO D 3 89  ? 121.321 191.056 86.736  1.00 46.27  ? 89   PRO A CB    1 
ATOM   9205  C  CG    . PRO D 3 89  ? 120.377 191.699 85.761  1.00 44.49  ? 89   PRO A CG    1 
ATOM   9206  C  CD    . PRO D 3 89  ? 121.189 191.992 84.557  1.00 43.54  ? 89   PRO A CD    1 
ATOM   9207  N  N     . GLU D 3 90  ? 121.419 188.193 85.102  1.00 53.85  ? 90   GLU A N     1 
ATOM   9208  C  CA    . GLU D 3 90  ? 121.316 186.740 85.128  1.00 55.69  ? 90   GLU A CA    1 
ATOM   9209  C  C     . GLU D 3 90  ? 122.583 186.080 84.594  1.00 57.67  ? 90   GLU A C     1 
ATOM   9210  O  O     . GLU D 3 90  ? 122.850 184.915 84.907  1.00 58.41  ? 90   GLU A O     1 
ATOM   9211  C  CB    . GLU D 3 90  ? 120.094 186.287 84.331  1.00 60.86  ? 90   GLU A CB    1 
ATOM   9212  C  CG    . GLU D 3 90  ? 119.673 184.851 84.597  1.00 67.04  ? 90   GLU A CG    1 
ATOM   9213  C  CD    . GLU D 3 90  ? 119.214 184.629 86.025  1.00 69.15  ? 90   GLU A CD    1 
ATOM   9214  O  OE1   . GLU D 3 90  ? 118.655 185.571 86.627  1.00 67.06  ? 90   GLU A OE1   1 
ATOM   9215  O  OE2   . GLU D 3 90  ? 119.413 183.512 86.547  1.00 66.67  ? 90   GLU A OE2   1 
ATOM   9216  N  N     . GLN D 3 91  ? 123.371 186.798 83.792  1.00 56.05  ? 91   GLN A N     1 
ATOM   9217  C  CA    . GLN D 3 91  ? 124.643 186.255 83.327  1.00 52.68  ? 91   GLN A CA    1 
ATOM   9218  C  C     . GLN D 3 91  ? 125.628 186.102 84.477  1.00 59.11  ? 91   GLN A C     1 
ATOM   9219  O  O     . GLN D 3 91  ? 126.356 185.106 84.557  1.00 64.04  ? 91   GLN A O     1 
ATOM   9220  C  CB    . GLN D 3 91  ? 125.235 187.144 82.235  1.00 58.90  ? 91   GLN A CB    1 
ATOM   9221  C  CG    . GLN D 3 91  ? 124.369 187.283 81.004  1.00 61.24  ? 91   GLN A CG    1 
ATOM   9222  C  CD    . GLN D 3 91  ? 124.887 188.340 80.053  1.00 68.57  ? 91   GLN A CD    1 
ATOM   9223  O  OE1   . GLN D 3 91  ? 125.613 189.248 80.455  1.00 67.82  ? 91   GLN A OE1   1 
ATOM   9224  N  NE2   . GLN D 3 91  ? 124.517 188.228 78.783  1.00 64.42  ? 91   GLN A NE2   1 
ATOM   9225  N  N     . LEU D 3 92  ? 125.670 187.081 85.375  1.00 50.48  ? 92   LEU A N     1 
ATOM   9226  C  CA    . LEU D 3 92  ? 126.565 187.030 86.526  1.00 40.18  ? 92   LEU A CA    1 
ATOM   9227  C  C     . LEU D 3 92  ? 126.013 186.041 87.545  1.00 45.77  ? 92   LEU A C     1 
ATOM   9228  O  O     . LEU D 3 92  ? 124.972 186.288 88.160  1.00 50.12  ? 92   LEU A O     1 
ATOM   9229  C  CB    . LEU D 3 92  ? 126.711 188.421 87.130  1.00 42.94  ? 92   LEU A CB    1 
ATOM   9230  C  CG    . LEU D 3 92  ? 126.878 189.557 86.125  1.00 45.84  ? 92   LEU A CG    1 
ATOM   9231  C  CD1   . LEU D 3 92  ? 126.920 190.894 86.829  1.00 49.83  ? 92   LEU A CD1   1 
ATOM   9232  C  CD2   . LEU D 3 92  ? 128.136 189.351 85.313  1.00 50.59  ? 92   LEU A CD2   1 
ATOM   9233  N  N     . ILE D 3 93  ? 126.707 184.922 87.727  1.00 52.54  ? 93   ILE A N     1 
ATOM   9234  C  CA    . ILE D 3 93  ? 126.248 183.827 88.572  1.00 51.67  ? 93   ILE A CA    1 
ATOM   9235  C  C     . ILE D 3 93  ? 127.252 183.625 89.696  1.00 58.51  ? 93   ILE A C     1 
ATOM   9236  O  O     . ILE D 3 93  ? 128.459 183.524 89.448  1.00 64.56  ? 93   ILE A O     1 
ATOM   9237  C  CB    . ILE D 3 93  ? 126.062 182.534 87.762  1.00 49.26  ? 93   ILE A CB    1 
ATOM   9238  C  CG1   . ILE D 3 93  ? 125.070 182.760 86.624  1.00 58.07  ? 93   ILE A CG1   1 
ATOM   9239  C  CG2   . ILE D 3 93  ? 125.592 181.407 88.660  1.00 51.88  ? 93   ILE A CG2   1 
ATOM   9240  C  CD1   . ILE D 3 93  ? 124.858 181.549 85.754  1.00 60.41  ? 93   ILE A CD1   1 
ATOM   9241  N  N     . THR D 3 94  ? 126.755 183.565 90.928  1.00 58.23  ? 94   THR A N     1 
ATOM   9242  C  CA    . THR D 3 94  ? 127.589 183.411 92.109  1.00 50.91  ? 94   THR A CA    1 
ATOM   9243  C  C     . THR D 3 94  ? 127.086 182.256 92.960  1.00 49.63  ? 94   THR A C     1 
ATOM   9244  O  O     . THR D 3 94  ? 125.905 181.904 92.925  1.00 52.82  ? 94   THR A O     1 
ATOM   9245  C  CB    . THR D 3 94  ? 127.603 184.679 92.965  1.00 60.30  ? 94   THR A CB    1 
ATOM   9246  O  OG1   . THR D 3 94  ? 126.311 184.870 93.555  1.00 68.02  ? 94   THR A OG1   1 
ATOM   9247  C  CG2   . THR D 3 94  ? 127.936 185.881 92.125  1.00 57.00  ? 94   THR A CG2   1 
ATOM   9248  N  N     . GLY D 3 95  ? 127.994 181.674 93.724  1.00 59.17  ? 95   GLY A N     1 
ATOM   9249  C  CA    . GLY D 3 95  ? 127.674 180.639 94.686  1.00 62.44  ? 95   GLY A CA    1 
ATOM   9250  C  C     . GLY D 3 95  ? 127.605 181.186 96.095  1.00 65.16  ? 95   GLY A C     1 
ATOM   9251  O  O     . GLY D 3 95  ? 127.385 182.383 96.308  1.00 70.46  ? 95   GLY A O     1 
ATOM   9252  N  N     . LYS D 3 96  ? 127.794 180.302 97.068  1.00 58.31  ? 96   LYS A N     1 
ATOM   9253  C  CA    . LYS D 3 96  ? 127.806 180.678 98.475  1.00 57.56  ? 96   LYS A CA    1 
ATOM   9254  C  C     . LYS D 3 96  ? 129.171 180.475 99.109  1.00 60.50  ? 96   LYS A C     1 
ATOM   9255  O  O     . LYS D 3 96  ? 129.694 181.391 99.753  1.00 63.47  ? 96   LYS A O     1 
ATOM   9256  C  CB    . LYS D 3 96  ? 126.748 179.871 99.241  1.00 62.44  ? 96   LYS A CB    1 
ATOM   9257  C  CG    . LYS D 3 96  ? 125.436 179.702 98.497  1.00 62.06  ? 96   LYS A CG    1 
ATOM   9258  C  CD    . LYS D 3 96  ? 124.642 180.993 98.467  1.00 61.16  ? 96   LYS A CD    1 
ATOM   9259  C  CE    . LYS D 3 96  ? 123.993 181.266 99.809  1.00 63.19  ? 96   LYS A CE    1 
ATOM   9260  N  NZ    . LYS D 3 96  ? 123.019 182.388 99.731  1.00 63.10  ? 96   LYS A NZ    1 
ATOM   9261  N  N     . GLU D 3 97  ? 129.762 179.296 98.945  1.00 71.62  ? 97   GLU A N     1 
ATOM   9262  C  CA    . GLU D 3 97  ? 131.084 178.988 99.464  1.00 70.55  ? 97   GLU A CA    1 
ATOM   9263  C  C     . GLU D 3 97  ? 132.019 178.656 98.310  1.00 73.60  ? 97   GLU A C     1 
ATOM   9264  O  O     . GLU D 3 97  ? 131.590 178.167 97.262  1.00 74.27  ? 97   GLU A O     1 
ATOM   9265  C  CB    . GLU D 3 97  ? 131.043 177.815 100.449 1.00 73.53  ? 97   GLU A CB    1 
ATOM   9266  C  CG    . GLU D 3 97  ? 130.145 178.045 101.649 1.00 75.50  ? 97   GLU A CG    1 
ATOM   9267  C  CD    . GLU D 3 97  ? 130.218 176.915 102.656 1.00 80.14  ? 97   GLU A CD    1 
ATOM   9268  O  OE1   . GLU D 3 97  ? 131.213 176.161 102.634 1.00 79.62  ? 97   GLU A OE1   1 
ATOM   9269  O  OE2   . GLU D 3 97  ? 129.280 176.780 103.470 1.00 78.81  ? 97   GLU A OE2   1 
ATOM   9270  N  N     . ASP D 3 98  ? 133.302 178.925 98.513  1.00 75.16  ? 98   ASP A N     1 
ATOM   9271  C  CA    . ASP D 3 98  ? 134.286 178.715 97.467  1.00 68.06  ? 98   ASP A CA    1 
ATOM   9272  C  C     . ASP D 3 98  ? 134.700 177.252 97.390  1.00 69.36  ? 98   ASP A C     1 
ATOM   9273  O  O     . ASP D 3 98  ? 134.379 176.436 98.258  1.00 73.90  ? 98   ASP A O     1 
ATOM   9274  C  CB    . ASP D 3 98  ? 135.522 179.577 97.706  1.00 70.53  ? 98   ASP A CB    1 
ATOM   9275  C  CG    . ASP D 3 98  ? 136.043 179.470 99.122  1.00 80.29  ? 98   ASP A CG    1 
ATOM   9276  O  OD1   . ASP D 3 98  ? 135.335 178.900 99.979  1.00 77.06  ? 98   ASP A OD1   1 
ATOM   9277  O  OD2   . ASP D 3 98  ? 137.166 179.953 99.378  1.00 80.36  ? 98   ASP A OD2   1 
ATOM   9278  N  N     . ALA D 3 99  ? 135.425 176.926 96.322  1.00 59.31  ? 99   ALA A N     1 
ATOM   9279  C  CA    . ALA D 3 99  ? 136.039 175.615 96.188  1.00 58.29  ? 99   ALA A CA    1 
ATOM   9280  C  C     . ALA D 3 99  ? 137.239 175.438 97.105  1.00 63.53  ? 99   ALA A C     1 
ATOM   9281  O  O     . ALA D 3 99  ? 137.671 174.300 97.312  1.00 73.52  ? 99   ALA A O     1 
ATOM   9282  C  CB    . ALA D 3 99  ? 136.458 175.375 94.739  1.00 57.23  ? 99   ALA A CB    1 
ATOM   9283  N  N     . ALA D 3 100 ? 137.777 176.529 97.651  1.00 56.11  ? 100  ALA A N     1 
ATOM   9284  C  CA    . ALA D 3 100 ? 138.843 176.479 98.650  1.00 55.13  ? 100  ALA A CA    1 
ATOM   9285  C  C     . ALA D 3 100 ? 140.043 175.675 98.157  1.00 54.19  ? 100  ALA A C     1 
ATOM   9286  O  O     . ALA D 3 100 ? 140.604 174.857 98.888  1.00 64.23  ? 100  ALA A O     1 
ATOM   9287  C  CB    . ALA D 3 100 ? 138.326 175.921 99.975  1.00 55.66  ? 100  ALA A CB    1 
ATOM   9288  N  N     . ASN D 3 101 ? 140.438 175.917 96.909  1.00 41.05  ? 101  ASN A N     1 
ATOM   9289  C  CA    . ASN D 3 101 ? 141.581 175.245 96.295  1.00 44.87  ? 101  ASN A CA    1 
ATOM   9290  C  C     . ASN D 3 101 ? 141.436 173.730 96.366  1.00 56.12  ? 101  ASN A C     1 
ATOM   9291  O  O     . ASN D 3 101 ? 142.396 173.001 96.618  1.00 63.21  ? 101  ASN A O     1 
ATOM   9292  C  CB    . ASN D 3 101 ? 142.892 175.696 96.931  1.00 48.67  ? 101  ASN A CB    1 
ATOM   9293  C  CG    . ASN D 3 101 ? 143.371 177.018 96.387  1.00 55.77  ? 101  ASN A CG    1 
ATOM   9294  O  OD1   . ASN D 3 101 ? 142.714 177.629 95.547  1.00 58.22  ? 101  ASN A OD1   1 
ATOM   9295  N  ND2   . ASN D 3 101 ? 144.520 177.472 96.866  1.00 60.89  ? 101  ASN A ND2   1 
ATOM   9296  N  N     . ASN D 3 102 ? 140.218 173.253 96.139  1.00 50.57  ? 102  ASN A N     1 
ATOM   9297  C  CA    . ASN D 3 102 ? 139.923 171.826 96.113  1.00 50.98  ? 102  ASN A CA    1 
ATOM   9298  C  C     . ASN D 3 102 ? 139.252 171.507 94.786  1.00 52.41  ? 102  ASN A C     1 
ATOM   9299  O  O     . ASN D 3 102 ? 138.169 172.023 94.491  1.00 59.75  ? 102  ASN A O     1 
ATOM   9300  C  CB    . ASN D 3 102 ? 139.036 171.426 97.287  1.00 48.07  ? 102  ASN A CB    1 
ATOM   9301  C  CG    . ASN D 3 102 ? 139.271 170.005 97.729  1.00 50.20  ? 102  ASN A CG    1 
ATOM   9302  O  OD1   . ASN D 3 102 ? 139.562 169.131 96.915  1.00 56.64  ? 102  ASN A OD1   1 
ATOM   9303  N  ND2   . ASN D 3 102 ? 139.149 169.762 99.025  1.00 53.88  ? 102  ASN A ND2   1 
ATOM   9304  N  N     . TYR D 3 103 ? 139.902 170.662 93.985  1.00 46.31  ? 103  TYR A N     1 
ATOM   9305  C  CA    . TYR D 3 103 ? 139.305 170.222 92.731  1.00 43.55  ? 103  TYR A CA    1 
ATOM   9306  C  C     . TYR D 3 103 ? 137.997 169.486 92.985  1.00 52.59  ? 103  TYR A C     1 
ATOM   9307  O  O     . TYR D 3 103 ? 137.025 169.649 92.236  1.00 61.47  ? 103  TYR A O     1 
ATOM   9308  C  CB    . TYR D 3 103 ? 140.294 169.337 91.975  1.00 45.65  ? 103  TYR A CB    1 
ATOM   9309  C  CG    . TYR D 3 103 ? 139.707 168.618 90.788  1.00 50.65  ? 103  TYR A CG    1 
ATOM   9310  C  CD1   . TYR D 3 103 ? 139.690 169.207 89.538  1.00 53.40  ? 103  TYR A CD1   1 
ATOM   9311  C  CD2   . TYR D 3 103 ? 139.174 167.345 90.917  1.00 53.90  ? 103  TYR A CD2   1 
ATOM   9312  C  CE1   . TYR D 3 103 ? 139.153 168.553 88.453  1.00 56.95  ? 103  TYR A CE1   1 
ATOM   9313  C  CE2   . TYR D 3 103 ? 138.632 166.687 89.839  1.00 50.62  ? 103  TYR A CE2   1 
ATOM   9314  C  CZ    . TYR D 3 103 ? 138.626 167.295 88.610  1.00 55.75  ? 103  TYR A CZ    1 
ATOM   9315  O  OH    . TYR D 3 103 ? 138.088 166.639 87.531  1.00 59.10  ? 103  TYR A OH    1 
ATOM   9316  N  N     . ALA D 3 104 ? 137.956 168.674 94.042  1.00 49.58  ? 104  ALA A N     1 
ATOM   9317  C  CA    . ALA D 3 104 ? 136.756 167.906 94.343  1.00 48.23  ? 104  ALA A CA    1 
ATOM   9318  C  C     . ALA D 3 104 ? 135.576 168.818 94.638  1.00 53.82  ? 104  ALA A C     1 
ATOM   9319  O  O     . ALA D 3 104 ? 134.459 168.558 94.185  1.00 61.47  ? 104  ALA A O     1 
ATOM   9320  C  CB    . ALA D 3 104 ? 137.016 166.969 95.520  1.00 51.58  ? 104  ALA A CB    1 
ATOM   9321  N  N     . ARG D 3 105 ? 135.801 169.894 95.391  1.00 51.32  ? 105  ARG A N     1 
ATOM   9322  C  CA    . ARG D 3 105 ? 134.711 170.821 95.673  1.00 51.94  ? 105  ARG A CA    1 
ATOM   9323  C  C     . ARG D 3 105 ? 134.202 171.477 94.399  1.00 57.52  ? 105  ARG A C     1 
ATOM   9324  O  O     . ARG D 3 105 ? 132.989 171.632 94.215  1.00 61.76  ? 105  ARG A O     1 
ATOM   9325  C  CB    . ARG D 3 105 ? 135.165 171.877 96.678  1.00 53.47  ? 105  ARG A CB    1 
ATOM   9326  C  CG    . ARG D 3 105 ? 135.364 171.337 98.072  1.00 53.17  ? 105  ARG A CG    1 
ATOM   9327  C  CD    . ARG D 3 105 ? 135.790 172.417 99.037  1.00 51.09  ? 105  ARG A CD    1 
ATOM   9328  N  NE    . ARG D 3 105 ? 134.784 173.461 99.168  1.00 50.03  ? 105  ARG A NE    1 
ATOM   9329  C  CZ    . ARG D 3 105 ? 133.750 173.402 99.994  1.00 53.38  ? 105  ARG A CZ    1 
ATOM   9330  N  NH1   . ARG D 3 105 ? 133.550 172.355 100.776 1.00 52.86  ? 105  ARG A NH1   1 
ATOM   9331  N  NH2   . ARG D 3 105 ? 132.896 174.419 100.037 1.00 56.82  ? 105  ARG A NH2   1 
ATOM   9332  N  N     . GLY D 3 106 ? 135.109 171.864 93.505  1.00 50.55  ? 106  GLY A N     1 
ATOM   9333  C  CA    . GLY D 3 106 ? 134.686 172.522 92.283  1.00 44.03  ? 106  GLY A CA    1 
ATOM   9334  C  C     . GLY D 3 106 ? 133.988 171.586 91.317  1.00 50.90  ? 106  GLY A C     1 
ATOM   9335  O  O     . GLY D 3 106 ? 133.188 172.025 90.487  1.00 57.96  ? 106  GLY A O     1 
ATOM   9336  N  N     . HIS D 3 107 ? 134.277 170.290 91.404  1.00 52.25  ? 107  HIS A N     1 
ATOM   9337  C  CA    . HIS D 3 107 ? 133.743 169.336 90.438  1.00 52.33  ? 107  HIS A CA    1 
ATOM   9338  C  C     . HIS D 3 107 ? 132.534 168.564 90.954  1.00 55.78  ? 107  HIS A C     1 
ATOM   9339  O  O     . HIS D 3 107 ? 131.469 168.601 90.332  1.00 60.76  ? 107  HIS A O     1 
ATOM   9340  C  CB    . HIS D 3 107 ? 134.842 168.359 90.013  1.00 49.52  ? 107  HIS A CB    1 
ATOM   9341  C  CG    . HIS D 3 107 ? 134.536 167.619 88.750  1.00 53.58  ? 107  HIS A CG    1 
ATOM   9342  N  ND1   . HIS D 3 107 ? 135.395 166.688 88.208  1.00 55.68  ? 107  HIS A ND1   1 
ATOM   9343  C  CD2   . HIS D 3 107 ? 133.469 167.674 87.921  1.00 59.48  ? 107  HIS A CD2   1 
ATOM   9344  C  CE1   . HIS D 3 107 ? 134.869 166.201 87.100  1.00 55.12  ? 107  HIS A CE1   1 
ATOM   9345  N  NE2   . HIS D 3 107 ? 133.700 166.782 86.903  1.00 61.33  ? 107  HIS A NE2   1 
ATOM   9346  N  N     . TYR D 3 108 ? 132.672 167.862 92.076  1.00 57.67  ? 108  TYR A N     1 
ATOM   9347  C  CA    . TYR D 3 108 ? 131.665 166.922 92.549  1.00 59.36  ? 108  TYR A CA    1 
ATOM   9348  C  C     . TYR D 3 108 ? 130.662 167.544 93.513  1.00 58.82  ? 108  TYR A C     1 
ATOM   9349  O  O     . TYR D 3 108 ? 129.453 167.371 93.340  1.00 66.74  ? 108  TYR A O     1 
ATOM   9350  C  CB    . TYR D 3 108 ? 132.349 165.729 93.224  1.00 57.03  ? 108  TYR A CB    1 
ATOM   9351  C  CG    . TYR D 3 108 ? 133.368 165.029 92.358  1.00 59.42  ? 108  TYR A CG    1 
ATOM   9352  C  CD1   . TYR D 3 108 ? 132.987 164.037 91.470  1.00 60.35  ? 108  TYR A CD1   1 
ATOM   9353  C  CD2   . TYR D 3 108 ? 134.712 165.353 92.439  1.00 62.10  ? 108  TYR A CD2   1 
ATOM   9354  C  CE1   . TYR D 3 108 ? 133.918 163.392 90.680  1.00 62.02  ? 108  TYR A CE1   1 
ATOM   9355  C  CE2   . TYR D 3 108 ? 135.648 164.713 91.654  1.00 62.98  ? 108  TYR A CE2   1 
ATOM   9356  C  CZ    . TYR D 3 108 ? 135.246 163.734 90.778  1.00 62.82  ? 108  TYR A CZ    1 
ATOM   9357  O  OH    . TYR D 3 108 ? 136.176 163.096 89.993  1.00 64.61  ? 108  TYR A OH    1 
ATOM   9358  N  N     . THR D 3 109 ? 131.134 168.265 94.530  1.00 53.17  ? 109  THR A N     1 
ATOM   9359  C  CA    . THR D 3 109 ? 130.263 168.684 95.625  1.00 59.46  ? 109  THR A CA    1 
ATOM   9360  C  C     . THR D 3 109 ? 129.647 170.061 95.393  1.00 62.63  ? 109  THR A C     1 
ATOM   9361  O  O     . THR D 3 109 ? 128.427 170.185 95.252  1.00 64.26  ? 109  THR A O     1 
ATOM   9362  C  CB    . THR D 3 109 ? 131.044 168.674 96.943  1.00 61.95  ? 109  THR A CB    1 
ATOM   9363  O  OG1   . THR D 3 109 ? 131.553 167.359 97.187  1.00 63.27  ? 109  THR A OG1   1 
ATOM   9364  C  CG2   . THR D 3 109 ? 130.142 169.079 98.095  1.00 61.32  ? 109  THR A CG2   1 
ATOM   9365  N  N     . ILE D 3 110 ? 130.475 171.100 95.348  1.00 57.08  ? 110  ILE A N     1 
ATOM   9366  C  CA    . ILE D 3 110 ? 129.953 172.455 95.227  1.00 55.40  ? 110  ILE A CA    1 
ATOM   9367  C  C     . ILE D 3 110 ? 129.707 172.832 93.770  1.00 53.17  ? 110  ILE A C     1 
ATOM   9368  O  O     . ILE D 3 110 ? 128.877 173.701 93.488  1.00 54.02  ? 110  ILE A O     1 
ATOM   9369  C  CB    . ILE D 3 110 ? 130.905 173.452 95.908  1.00 57.09  ? 110  ILE A CB    1 
ATOM   9370  C  CG1   . ILE D 3 110 ? 131.326 172.930 97.279  1.00 60.66  ? 110  ILE A CG1   1 
ATOM   9371  C  CG2   . ILE D 3 110 ? 130.236 174.799 96.077  1.00 59.55  ? 110  ILE A CG2   1 
ATOM   9372  C  CD1   . ILE D 3 110 ? 130.177 172.769 98.249  1.00 63.02  ? 110  ILE A CD1   1 
ATOM   9373  N  N     . GLY D 3 111 ? 130.401 172.185 92.834  1.00 57.07  ? 111  GLY A N     1 
ATOM   9374  C  CA    . GLY D 3 111 ? 130.181 172.481 91.430  1.00 58.44  ? 111  GLY A CA    1 
ATOM   9375  C  C     . GLY D 3 111 ? 128.803 172.074 90.949  1.00 64.11  ? 111  GLY A C     1 
ATOM   9376  O  O     . GLY D 3 111 ? 128.174 172.788 90.164  1.00 70.61  ? 111  GLY A O     1 
ATOM   9377  N  N     . LYS D 3 112 ? 128.312 170.924 91.410  1.00 63.41  ? 112  LYS A N     1 
ATOM   9378  C  CA    . LYS D 3 112 ? 127.007 170.447 90.972  1.00 58.58  ? 112  LYS A CA    1 
ATOM   9379  C  C     . LYS D 3 112 ? 125.890 171.061 91.803  1.00 60.01  ? 112  LYS A C     1 
ATOM   9380  O  O     . LYS D 3 112 ? 125.018 170.352 92.315  1.00 64.85  ? 112  LYS A O     1 
ATOM   9381  C  CB    . LYS D 3 112 ? 126.942 168.921 91.033  1.00 58.77  ? 112  LYS A CB    1 
ATOM   9382  C  CG    . LYS D 3 112 ? 127.947 168.231 90.130  1.00 60.36  ? 112  LYS A CG    1 
ATOM   9383  C  CD    . LYS D 3 112 ? 127.850 166.722 90.237  1.00 63.03  ? 112  LYS A CD    1 
ATOM   9384  C  CE    . LYS D 3 112 ? 128.873 166.046 89.340  1.00 66.57  ? 112  LYS A CE    1 
ATOM   9385  N  NZ    . LYS D 3 112 ? 128.814 164.562 89.447  1.00 69.33  ? 112  LYS A NZ    1 
ATOM   9386  N  N     . GLU D 3 113 ? 125.915 172.382 91.937  1.00 64.16  ? 113  GLU A N     1 
ATOM   9387  C  CA    . GLU D 3 113 ? 124.797 173.147 92.468  1.00 58.79  ? 113  GLU A CA    1 
ATOM   9388  C  C     . GLU D 3 113 ? 124.458 174.360 91.626  1.00 61.71  ? 113  GLU A C     1 
ATOM   9389  O  O     . GLU D 3 113 ? 123.331 174.858 91.723  1.00 68.08  ? 113  GLU A O     1 
ATOM   9390  C  CB    . GLU D 3 113 ? 125.083 173.607 93.905  1.00 60.52  ? 113  GLU A CB    1 
ATOM   9391  C  CG    . GLU D 3 113 ? 125.199 172.477 94.913  1.00 68.36  ? 113  GLU A CG    1 
ATOM   9392  C  CD    . GLU D 3 113 ? 125.572 172.969 96.297  1.00 71.63  ? 113  GLU A CD    1 
ATOM   9393  O  OE1   . GLU D 3 113 ? 125.968 174.146 96.425  1.00 72.96  ? 113  GLU A OE1   1 
ATOM   9394  O  OE2   . GLU D 3 113 ? 125.468 172.178 97.258  1.00 68.36  ? 113  GLU A OE2   1 
ATOM   9395  N  N     . ILE D 3 114 ? 125.387 174.851 90.808  1.00 57.55  ? 114  ILE A N     1 
ATOM   9396  C  CA    . ILE D 3 114 ? 125.134 175.938 89.874  1.00 59.41  ? 114  ILE A CA    1 
ATOM   9397  C  C     . ILE D 3 114 ? 125.408 175.540 88.434  1.00 65.21  ? 114  ILE A C     1 
ATOM   9398  O  O     . ILE D 3 114 ? 125.357 176.399 87.548  1.00 75.20  ? 114  ILE A O     1 
ATOM   9399  C  CB    . ILE D 3 114 ? 125.951 177.193 90.241  1.00 61.36  ? 114  ILE A CB    1 
ATOM   9400  C  CG1   . ILE D 3 114 ? 127.444 176.914 90.092  1.00 61.38  ? 114  ILE A CG1   1 
ATOM   9401  C  CG2   . ILE D 3 114 ? 125.636 177.641 91.655  1.00 61.44  ? 114  ILE A CG2   1 
ATOM   9402  C  CD1   . ILE D 3 114 ? 128.309 178.127 90.320  1.00 64.22  ? 114  ILE A CD1   1 
ATOM   9403  N  N     . ILE D 3 115 ? 125.701 174.265 88.171  1.00 60.25  ? 115  ILE A N     1 
ATOM   9404  C  CA    . ILE D 3 115 ? 126.033 173.845 86.813  1.00 58.97  ? 115  ILE A CA    1 
ATOM   9405  C  C     . ILE D 3 115 ? 124.803 173.903 85.916  1.00 66.40  ? 115  ILE A C     1 
ATOM   9406  O  O     . ILE D 3 115 ? 124.891 174.266 84.736  1.00 74.86  ? 115  ILE A O     1 
ATOM   9407  C  CB    . ILE D 3 115 ? 126.680 172.447 86.825  1.00 57.32  ? 115  ILE A CB    1 
ATOM   9408  C  CG1   . ILE D 3 115 ? 127.226 172.105 85.442  1.00 59.22  ? 115  ILE A CG1   1 
ATOM   9409  C  CG2   . ILE D 3 115 ? 125.707 171.387 87.322  1.00 62.44  ? 115  ILE A CG2   1 
ATOM   9410  C  CD1   . ILE D 3 115 ? 128.402 172.952 85.038  1.00 62.10  ? 115  ILE A CD1   1 
ATOM   9411  N  N     . ASP D 3 116 ? 123.634 173.557 86.458  1.00 70.29  ? 116  ASP A N     1 
ATOM   9412  C  CA    . ASP D 3 116 ? 122.410 173.666 85.675  1.00 69.59  ? 116  ASP A CA    1 
ATOM   9413  C  C     . ASP D 3 116 ? 122.132 175.114 85.303  1.00 69.46  ? 116  ASP A C     1 
ATOM   9414  O  O     . ASP D 3 116 ? 121.701 175.404 84.181  1.00 74.65  ? 116  ASP A O     1 
ATOM   9415  C  CB    . ASP D 3 116 ? 121.236 173.071 86.449  1.00 71.68  ? 116  ASP A CB    1 
ATOM   9416  C  CG    . ASP D 3 116 ? 121.415 171.595 86.724  1.00 76.85  ? 116  ASP A CG    1 
ATOM   9417  O  OD1   . ASP D 3 116 ? 122.459 171.041 86.325  1.00 75.43  ? 116  ASP A OD1   1 
ATOM   9418  O  OD2   . ASP D 3 116 ? 120.514 170.989 87.341  1.00 78.08  ? 116  ASP A OD2   1 
ATOM   9419  N  N     . LEU D 3 117 ? 122.387 176.040 86.228  1.00 57.01  ? 117  LEU A N     1 
ATOM   9420  C  CA    . LEU D 3 117 ? 122.163 177.454 85.948  1.00 55.40  ? 117  LEU A CA    1 
ATOM   9421  C  C     . LEU D 3 117 ? 123.068 177.953 84.830  1.00 64.14  ? 117  LEU A C     1 
ATOM   9422  O  O     . LEU D 3 117 ? 122.612 178.656 83.918  1.00 69.27  ? 117  LEU A O     1 
ATOM   9423  C  CB    . LEU D 3 117 ? 122.380 178.271 87.218  1.00 52.33  ? 117  LEU A CB    1 
ATOM   9424  C  CG    . LEU D 3 117 ? 121.106 178.725 87.918  1.00 61.25  ? 117  LEU A CG    1 
ATOM   9425  C  CD1   . LEU D 3 117 ? 121.438 179.476 89.193  1.00 64.93  ? 117  LEU A CD1   1 
ATOM   9426  C  CD2   . LEU D 3 117 ? 120.281 179.592 86.985  1.00 61.23  ? 117  LEU A CD2   1 
ATOM   9427  N  N     . VAL D 3 118 ? 124.355 177.603 84.877  1.00 56.07  ? 118  VAL A N     1 
ATOM   9428  C  CA    . VAL D 3 118 ? 125.276 178.087 83.856  1.00 54.24  ? 118  VAL A CA    1 
ATOM   9429  C  C     . VAL D 3 118 ? 124.966 177.444 82.510  1.00 60.10  ? 118  VAL A C     1 
ATOM   9430  O  O     . VAL D 3 118 ? 125.054 178.098 81.464  1.00 69.45  ? 118  VAL A O     1 
ATOM   9431  C  CB    . VAL D 3 118 ? 126.739 177.870 84.287  1.00 53.80  ? 118  VAL A CB    1 
ATOM   9432  C  CG1   . VAL D 3 118 ? 127.045 176.410 84.499  1.00 53.49  ? 118  VAL A CG1   1 
ATOM   9433  C  CG2   . VAL D 3 118 ? 127.683 178.458 83.254  1.00 63.56  ? 118  VAL A CG2   1 
ATOM   9434  N  N     . LEU D 3 119 ? 124.579 176.165 82.507  1.00 55.17  ? 119  LEU A N     1 
ATOM   9435  C  CA    . LEU D 3 119 ? 124.196 175.531 81.250  1.00 53.62  ? 119  LEU A CA    1 
ATOM   9436  C  C     . LEU D 3 119 ? 122.939 176.167 80.673  1.00 59.48  ? 119  LEU A C     1 
ATOM   9437  O  O     . LEU D 3 119 ? 122.833 176.352 79.455  1.00 68.44  ? 119  LEU A O     1 
ATOM   9438  C  CB    . LEU D 3 119 ? 124.007 174.029 81.442  1.00 53.61  ? 119  LEU A CB    1 
ATOM   9439  C  CG    . LEU D 3 119 ? 125.228 173.146 81.173  1.00 58.58  ? 119  LEU A CG    1 
ATOM   9440  C  CD1   . LEU D 3 119 ? 125.610 173.210 79.703  1.00 60.65  ? 119  LEU A CD1   1 
ATOM   9441  C  CD2   . LEU D 3 119 ? 126.406 173.527 82.040  1.00 61.69  ? 119  LEU A CD2   1 
ATOM   9442  N  N     . ASP D 3 120 ? 121.975 176.514 81.528  1.00 57.34  ? 120  ASP A N     1 
ATOM   9443  C  CA    . ASP D 3 120 ? 120.771 177.181 81.047  1.00 56.68  ? 120  ASP A CA    1 
ATOM   9444  C  C     . ASP D 3 120 ? 121.095 178.551 80.470  1.00 60.63  ? 120  ASP A C     1 
ATOM   9445  O  O     . ASP D 3 120 ? 120.547 178.942 79.433  1.00 67.66  ? 120  ASP A O     1 
ATOM   9446  C  CB    . ASP D 3 120 ? 119.750 177.301 82.176  1.00 57.27  ? 120  ASP A CB    1 
ATOM   9447  C  CG    . ASP D 3 120 ? 118.953 176.028 82.377  1.00 66.10  ? 120  ASP A CG    1 
ATOM   9448  O  OD1   . ASP D 3 120 ? 118.643 175.355 81.372  1.00 67.27  ? 120  ASP A OD1   1 
ATOM   9449  O  OD2   . ASP D 3 120 ? 118.639 175.698 83.540  1.00 67.64  ? 120  ASP A OD2   1 
ATOM   9450  N  N     . ARG D 3 121 ? 121.984 179.297 81.127  1.00 54.95  ? 121  ARG A N     1 
ATOM   9451  C  CA    . ARG D 3 121 ? 122.378 180.600 80.601  1.00 52.73  ? 121  ARG A CA    1 
ATOM   9452  C  C     . ARG D 3 121 ? 123.097 180.466 79.264  1.00 59.99  ? 121  ARG A C     1 
ATOM   9453  O  O     . ARG D 3 121 ? 122.865 181.259 78.344  1.00 70.51  ? 121  ARG A O     1 
ATOM   9454  C  CB    . ARG D 3 121 ? 123.253 181.333 81.612  1.00 55.76  ? 121  ARG A CB    1 
ATOM   9455  C  CG    . ARG D 3 121 ? 122.499 181.799 82.836  1.00 63.56  ? 121  ARG A CG    1 
ATOM   9456  C  CD    . ARG D 3 121 ? 121.194 182.465 82.446  1.00 62.52  ? 121  ARG A CD    1 
ATOM   9457  N  NE    . ARG D 3 121 ? 121.398 183.548 81.491  1.00 63.01  ? 121  ARG A NE    1 
ATOM   9458  C  CZ    . ARG D 3 121 ? 120.426 184.298 80.994  1.00 65.85  ? 121  ARG A CZ    1 
ATOM   9459  N  NH1   . ARG D 3 121 ? 119.164 184.116 81.345  1.00 61.00  ? 121  ARG A NH1   1 
ATOM   9460  N  NH2   . ARG D 3 121 ? 120.727 185.257 80.123  1.00 67.32  ? 121  ARG A NH2   1 
ATOM   9461  N  N     . ILE D 3 122 ? 123.974 179.470 79.137  1.00 52.42  ? 122  ILE A N     1 
ATOM   9462  C  CA    . ILE D 3 122 ? 124.663 179.248 77.869  1.00 44.82  ? 122  ILE A CA    1 
ATOM   9463  C  C     . ILE D 3 122 ? 123.667 178.886 76.777  1.00 51.84  ? 122  ILE A C     1 
ATOM   9464  O  O     . ILE D 3 122 ? 123.750 179.390 75.650  1.00 62.67  ? 122  ILE A O     1 
ATOM   9465  C  CB    . ILE D 3 122 ? 125.745 178.166 78.031  1.00 48.67  ? 122  ILE A CB    1 
ATOM   9466  C  CG1   . ILE D 3 122 ? 126.886 178.684 78.901  1.00 51.40  ? 122  ILE A CG1   1 
ATOM   9467  C  CG2   . ILE D 3 122 ? 126.272 177.728 76.679  1.00 53.41  ? 122  ILE A CG2   1 
ATOM   9468  C  CD1   . ILE D 3 122 ? 127.822 177.599 79.358  1.00 54.92  ? 122  ILE A CD1   1 
ATOM   9469  N  N     . ARG D 3 123 ? 122.708 178.013 77.091  1.00 57.15  ? 123  ARG A N     1 
ATOM   9470  C  CA    . ARG D 3 123 ? 121.701 177.629 76.108  1.00 54.60  ? 123  ARG A CA    1 
ATOM   9471  C  C     . ARG D 3 123 ? 120.866 178.825 75.679  1.00 50.81  ? 123  ARG A C     1 
ATOM   9472  O  O     . ARG D 3 123 ? 120.537 178.972 74.496  1.00 61.49  ? 123  ARG A O     1 
ATOM   9473  C  CB    . ARG D 3 123 ? 120.807 176.529 76.674  1.00 53.19  ? 123  ARG A CB    1 
ATOM   9474  C  CG    . ARG D 3 123 ? 119.885 175.903 75.650  1.00 58.47  ? 123  ARG A CG    1 
ATOM   9475  C  CD    . ARG D 3 123 ? 119.092 174.758 76.249  1.00 61.12  ? 123  ARG A CD    1 
ATOM   9476  N  NE    . ARG D 3 123 ? 118.267 175.195 77.367  1.00 69.64  ? 123  ARG A NE    1 
ATOM   9477  C  CZ    . ARG D 3 123 ? 117.029 175.654 77.249  1.00 72.27  ? 123  ARG A CZ    1 
ATOM   9478  N  NH1   . ARG D 3 123 ? 116.438 175.751 76.069  1.00 64.55  ? 123  ARG A NH1   1 
ATOM   9479  N  NH2   . ARG D 3 123 ? 116.367 176.025 78.341  1.00 69.23  ? 123  ARG A NH2   1 
ATOM   9480  N  N     . LYS D 3 124 ? 120.505 179.687 76.628  1.00 44.69  ? 124  LYS A N     1 
ATOM   9481  C  CA    . LYS D 3 124 ? 119.744 180.880 76.285  1.00 48.17  ? 124  LYS A CA    1 
ATOM   9482  C  C     . LYS D 3 124 ? 120.565 181.818 75.414  1.00 49.94  ? 124  LYS A C     1 
ATOM   9483  O  O     . LYS D 3 124 ? 120.036 182.440 74.486  1.00 57.85  ? 124  LYS A O     1 
ATOM   9484  C  CB    . LYS D 3 124 ? 119.281 181.582 77.560  1.00 54.72  ? 124  LYS A CB    1 
ATOM   9485  C  CG    . LYS D 3 124 ? 118.099 182.504 77.370  1.00 56.13  ? 124  LYS A CG    1 
ATOM   9486  C  CD    . LYS D 3 124 ? 117.472 182.848 78.707  1.00 61.88  ? 124  LYS A CD    1 
ATOM   9487  C  CE    . LYS D 3 124 ? 117.063 181.588 79.454  1.00 62.09  ? 124  LYS A CE    1 
ATOM   9488  N  NZ    . LYS D 3 124 ? 116.494 181.893 80.795  1.00 59.07  ? 124  LYS A NZ    1 
ATOM   9489  N  N     . LEU D 3 125 ? 121.863 181.936 75.698  1.00 50.62  ? 125  LEU A N     1 
ATOM   9490  C  CA    . LEU D 3 125 ? 122.736 182.728 74.840  1.00 50.25  ? 125  LEU A CA    1 
ATOM   9491  C  C     . LEU D 3 125 ? 122.951 182.045 73.496  1.00 56.19  ? 125  LEU A C     1 
ATOM   9492  O  O     . LEU D 3 125 ? 123.075 182.713 72.464  1.00 58.63  ? 125  LEU A O     1 
ATOM   9493  C  CB    . LEU D 3 125 ? 124.075 182.968 75.535  1.00 45.48  ? 125  LEU A CB    1 
ATOM   9494  C  CG    . LEU D 3 125 ? 124.151 184.118 76.536  1.00 52.53  ? 125  LEU A CG    1 
ATOM   9495  C  CD1   . LEU D 3 125 ? 125.561 184.254 77.059  1.00 55.62  ? 125  LEU A CD1   1 
ATOM   9496  C  CD2   . LEU D 3 125 ? 123.686 185.416 75.901  1.00 54.86  ? 125  LEU A CD2   1 
ATOM   9497  N  N     . ALA D 3 126 ? 123.001 180.712 73.490  1.00 57.05  ? 126  ALA A N     1 
ATOM   9498  C  CA    . ALA D 3 126 ? 123.218 179.985 72.245  1.00 50.65  ? 126  ALA A CA    1 
ATOM   9499  C  C     . ALA D 3 126 ? 121.987 180.031 71.351  1.00 50.00  ? 126  ALA A C     1 
ATOM   9500  O  O     . ALA D 3 126 ? 122.088 179.849 70.133  1.00 60.08  ? 126  ALA A O     1 
ATOM   9501  C  CB    . ALA D 3 126 ? 123.609 178.539 72.544  1.00 55.93  ? 126  ALA A CB    1 
ATOM   9502  N  N     . ASP D 3 127 ? 120.809 180.254 71.935  1.00 56.15  ? 127  ASP A N     1 
ATOM   9503  C  CA    . ASP D 3 127 ? 119.598 180.352 71.130  1.00 55.67  ? 127  ASP A CA    1 
ATOM   9504  C  C     . ASP D 3 127 ? 119.429 181.727 70.500  1.00 60.56  ? 127  ASP A C     1 
ATOM   9505  O  O     . ASP D 3 127 ? 118.610 181.878 69.588  1.00 67.04  ? 127  ASP A O     1 
ATOM   9506  C  CB    . ASP D 3 127 ? 118.373 180.014 71.978  1.00 62.86  ? 127  ASP A CB    1 
ATOM   9507  C  CG    . ASP D 3 127 ? 118.269 178.535 72.285  1.00 71.29  ? 127  ASP A CG    1 
ATOM   9508  O  OD1   . ASP D 3 127 ? 119.136 177.768 71.817  1.00 71.08  ? 127  ASP A OD1   1 
ATOM   9509  O  OD2   . ASP D 3 127 ? 117.318 178.137 72.990  1.00 71.30  ? 127  ASP A OD2   1 
ATOM   9510  N  N     . GLN D 3 128 ? 120.174 182.726 70.962  1.00 59.56  ? 128  GLN A N     1 
ATOM   9511  C  CA    . GLN D 3 128 ? 120.117 184.068 70.403  1.00 56.11  ? 128  GLN A CA    1 
ATOM   9512  C  C     . GLN D 3 128 ? 121.191 184.314 69.356  1.00 59.68  ? 128  GLN A C     1 
ATOM   9513  O  O     . GLN D 3 128 ? 121.296 185.433 68.847  1.00 64.27  ? 128  GLN A O     1 
ATOM   9514  C  CB    . GLN D 3 128 ? 120.236 185.112 71.517  1.00 57.36  ? 128  GLN A CB    1 
ATOM   9515  C  CG    . GLN D 3 128 ? 118.905 185.616 72.043  1.00 64.46  ? 128  GLN A CG    1 
ATOM   9516  C  CD    . GLN D 3 128 ? 118.243 186.612 71.111  1.00 68.29  ? 128  GLN A CD    1 
ATOM   9517  O  OE1   . GLN D 3 128 ? 118.825 187.025 70.108  1.00 66.41  ? 128  GLN A OE1   1 
ATOM   9518  N  NE2   . GLN D 3 128 ? 117.016 187.002 71.438  1.00 65.18  ? 128  GLN A NE2   1 
ATOM   9519  N  N     . CYS D 3 129 ? 121.988 183.304 69.026  1.00 65.66  ? 129  CYS A N     1 
ATOM   9520  C  CA    . CYS D 3 129 ? 123.055 183.428 68.046  1.00 65.80  ? 129  CYS A CA    1 
ATOM   9521  C  C     . CYS D 3 129 ? 122.753 182.531 66.856  1.00 68.69  ? 129  CYS A C     1 
ATOM   9522  O  O     . CYS D 3 129 ? 122.409 181.358 67.028  1.00 64.27  ? 129  CYS A O     1 
ATOM   9523  C  CB    . CYS D 3 129 ? 124.412 183.070 68.661  1.00 71.08  ? 129  CYS A CB    1 
ATOM   9524  S  SG    . CYS D 3 129 ? 124.571 181.383 69.256  1.00 94.41  ? 129  CYS A SG    1 
ATOM   9525  N  N     . THR D 3 130 ? 122.864 183.091 65.653  1.00 75.17  ? 130  THR A N     1 
ATOM   9526  C  CA    . THR D 3 130 ? 122.647 182.306 64.439  1.00 71.76  ? 130  THR A CA    1 
ATOM   9527  C  C     . THR D 3 130 ? 123.907 181.536 64.058  1.00 69.45  ? 130  THR A C     1 
ATOM   9528  O  O     . THR D 3 130 ? 123.904 180.304 63.995  1.00 71.44  ? 130  THR A O     1 
ATOM   9529  C  CB    . THR D 3 130 ? 122.199 183.221 63.296  1.00 67.49  ? 130  THR A CB    1 
ATOM   9530  O  OG1   . THR D 3 130 ? 123.314 183.991 62.835  1.00 66.46  ? 130  THR A OG1   1 
ATOM   9531  C  CG2   . THR D 3 130 ? 121.102 184.162 63.768  1.00 69.33  ? 130  THR A CG2   1 
ATOM   9532  N  N     . GLY D 3 131 ? 124.995 182.254 63.802  1.00 73.30  ? 131  GLY A N     1 
ATOM   9533  C  CA    . GLY D 3 131 ? 126.243 181.626 63.424  1.00 74.46  ? 131  GLY A CA    1 
ATOM   9534  C  C     . GLY D 3 131 ? 127.229 181.481 64.563  1.00 74.10  ? 131  GLY A C     1 
ATOM   9535  O  O     . GLY D 3 131 ? 128.288 182.114 64.552  1.00 77.29  ? 131  GLY A O     1 
ATOM   9536  N  N     . LEU D 3 132 ? 126.893 180.662 65.555  1.00 62.13  ? 132  LEU A N     1 
ATOM   9537  C  CA    . LEU D 3 132 ? 127.807 180.425 66.662  1.00 61.68  ? 132  LEU A CA    1 
ATOM   9538  C  C     . LEU D 3 132 ? 129.072 179.739 66.162  1.00 66.71  ? 132  LEU A C     1 
ATOM   9539  O  O     . LEU D 3 132 ? 129.013 178.785 65.382  1.00 69.51  ? 132  LEU A O     1 
ATOM   9540  C  CB    . LEU D 3 132 ? 127.136 179.571 67.733  1.00 62.96  ? 132  LEU A CB    1 
ATOM   9541  C  CG    . LEU D 3 132 ? 127.878 179.435 69.062  1.00 64.30  ? 132  LEU A CG    1 
ATOM   9542  C  CD1   . LEU D 3 132 ? 128.090 180.798 69.690  1.00 59.45  ? 132  LEU A CD1   1 
ATOM   9543  C  CD2   . LEU D 3 132 ? 127.121 178.520 70.005  1.00 62.57  ? 132  LEU A CD2   1 
ATOM   9544  N  N     . GLN D 3 133 ? 130.221 180.226 66.620  1.00 63.75  ? 133  GLN A N     1 
ATOM   9545  C  CA    . GLN D 3 133 ? 131.512 179.736 66.156  1.00 58.77  ? 133  GLN A CA    1 
ATOM   9546  C  C     . GLN D 3 133 ? 132.275 178.940 67.198  1.00 62.63  ? 133  GLN A C     1 
ATOM   9547  O  O     . GLN D 3 133 ? 132.979 177.994 66.844  1.00 68.98  ? 133  GLN A O     1 
ATOM   9548  C  CB    . GLN D 3 133 ? 132.381 180.902 65.686  1.00 56.42  ? 133  GLN A CB    1 
ATOM   9549  C  CG    . GLN D 3 133 ? 131.892 181.553 64.412  1.00 63.63  ? 133  GLN A CG    1 
ATOM   9550  C  CD    . GLN D 3 133 ? 133.026 181.915 63.483  1.00 72.04  ? 133  GLN A CD    1 
ATOM   9551  O  OE1   . GLN D 3 133 ? 134.180 181.996 63.900  1.00 78.30  ? 133  GLN A OE1   1 
ATOM   9552  N  NE2   . GLN D 3 133 ? 132.707 182.126 62.213  1.00 67.83  ? 133  GLN A NE2   1 
ATOM   9553  N  N     . GLY D 3 134 ? 132.166 179.295 68.469  1.00 56.97  ? 134  GLY A N     1 
ATOM   9554  C  CA    . GLY D 3 134 ? 132.885 178.567 69.492  1.00 59.52  ? 134  GLY A CA    1 
ATOM   9555  C  C     . GLY D 3 134 ? 132.753 179.243 70.836  1.00 55.53  ? 134  GLY A C     1 
ATOM   9556  O  O     . GLY D 3 134 ? 132.035 180.233 71.000  1.00 60.54  ? 134  GLY A O     1 
ATOM   9557  N  N     . PHE D 3 135 ? 133.470 178.680 71.802  1.00 40.92  ? 135  PHE A N     1 
ATOM   9558  C  CA    . PHE D 3 135 ? 133.481 179.160 73.173  1.00 39.93  ? 135  PHE A CA    1 
ATOM   9559  C  C     . PHE D 3 135 ? 134.870 179.660 73.538  1.00 46.31  ? 135  PHE A C     1 
ATOM   9560  O  O     . PHE D 3 135 ? 135.876 179.033 73.194  1.00 58.30  ? 135  PHE A O     1 
ATOM   9561  C  CB    . PHE D 3 135 ? 133.061 178.056 74.142  1.00 44.44  ? 135  PHE A CB    1 
ATOM   9562  C  CG    . PHE D 3 135 ? 131.645 177.612 73.971  1.00 47.59  ? 135  PHE A CG    1 
ATOM   9563  C  CD1   . PHE D 3 135 ? 130.621 178.276 74.614  1.00 53.58  ? 135  PHE A CD1   1 
ATOM   9564  C  CD2   . PHE D 3 135 ? 131.336 176.531 73.175  1.00 46.34  ? 135  PHE A CD2   1 
ATOM   9565  C  CE1   . PHE D 3 135 ? 129.319 177.872 74.460  1.00 53.35  ? 135  PHE A CE1   1 
ATOM   9566  C  CE2   . PHE D 3 135 ? 130.036 176.126 73.019  1.00 48.53  ? 135  PHE A CE2   1 
ATOM   9567  C  CZ    . PHE D 3 135 ? 129.028 176.797 73.661  1.00 49.28  ? 135  PHE A CZ    1 
ATOM   9568  N  N     . LEU D 3 136 ? 134.920 180.786 74.234  1.00 45.95  ? 136  LEU A N     1 
ATOM   9569  C  CA    . LEU D 3 136 ? 136.163 181.343 74.753  1.00 46.83  ? 136  LEU A CA    1 
ATOM   9570  C  C     . LEU D 3 136 ? 136.095 181.229 76.273  1.00 51.02  ? 136  LEU A C     1 
ATOM   9571  O  O     . LEU D 3 136 ? 135.666 182.155 76.962  1.00 57.35  ? 136  LEU A O     1 
ATOM   9572  C  CB    . LEU D 3 136 ? 136.350 182.785 74.298  1.00 47.31  ? 136  LEU A CB    1 
ATOM   9573  C  CG    . LEU D 3 136 ? 136.459 183.026 72.794  1.00 53.07  ? 136  LEU A CG    1 
ATOM   9574  C  CD1   . LEU D 3 136 ? 136.457 184.509 72.501  1.00 55.86  ? 136  LEU A CD1   1 
ATOM   9575  C  CD2   . LEU D 3 136 ? 137.714 182.377 72.245  1.00 56.49  ? 136  LEU A CD2   1 
ATOM   9576  N  N     . VAL D 3 137 ? 136.513 180.080 76.790  1.00 50.22  ? 137  VAL A N     1 
ATOM   9577  C  CA    . VAL D 3 137 ? 136.470 179.805 78.221  1.00 44.13  ? 137  VAL A CA    1 
ATOM   9578  C  C     . VAL D 3 137 ? 137.729 180.371 78.863  1.00 52.14  ? 137  VAL A C     1 
ATOM   9579  O  O     . VAL D 3 137 ? 138.846 180.014 78.476  1.00 63.51  ? 137  VAL A O     1 
ATOM   9580  C  CB    . VAL D 3 137 ? 136.347 178.300 78.492  1.00 44.39  ? 137  VAL A CB    1 
ATOM   9581  C  CG1   . VAL D 3 137 ? 136.458 178.022 79.975  1.00 45.82  ? 137  VAL A CG1   1 
ATOM   9582  C  CG2   . VAL D 3 137 ? 135.035 177.774 77.950  1.00 53.16  ? 137  VAL A CG2   1 
ATOM   9583  N  N     . PHE D 3 138 ? 137.552 181.250 79.847  1.00 50.52  ? 138  PHE A N     1 
ATOM   9584  C  CA    . PHE D 3 138 ? 138.665 181.854 80.572  1.00 41.94  ? 138  PHE A CA    1 
ATOM   9585  C  C     . PHE D 3 138 ? 138.675 181.290 81.986  1.00 47.97  ? 138  PHE A C     1 
ATOM   9586  O  O     . PHE D 3 138 ? 137.701 181.443 82.729  1.00 58.81  ? 138  PHE A O     1 
ATOM   9587  C  CB    . PHE D 3 138 ? 138.556 183.376 80.597  1.00 43.90  ? 138  PHE A CB    1 
ATOM   9588  C  CG    . PHE D 3 138 ? 138.624 184.015 79.244  1.00 46.95  ? 138  PHE A CG    1 
ATOM   9589  C  CD1   . PHE D 3 138 ? 137.478 184.210 78.499  1.00 52.06  ? 138  PHE A CD1   1 
ATOM   9590  C  CD2   . PHE D 3 138 ? 139.833 184.423 78.720  1.00 49.72  ? 138  PHE A CD2   1 
ATOM   9591  C  CE1   . PHE D 3 138 ? 137.537 184.801 77.259  1.00 54.09  ? 138  PHE A CE1   1 
ATOM   9592  C  CE2   . PHE D 3 138 ? 139.898 185.013 77.480  1.00 53.99  ? 138  PHE A CE2   1 
ATOM   9593  C  CZ    . PHE D 3 138 ? 138.748 185.201 76.747  1.00 55.87  ? 138  PHE A CZ    1 
ATOM   9594  N  N     . HIS D 3 139 ? 139.778 180.647 82.358  1.00 46.34  ? 139  HIS A N     1 
ATOM   9595  C  CA    . HIS D 3 139 ? 139.920 180.041 83.673  1.00 39.52  ? 139  HIS A CA    1 
ATOM   9596  C  C     . HIS D 3 139 ? 141.399 179.967 84.024  1.00 45.89  ? 139  HIS A C     1 
ATOM   9597  O  O     . HIS D 3 139 ? 142.261 180.441 83.278  1.00 55.69  ? 139  HIS A O     1 
ATOM   9598  C  CB    . HIS D 3 139 ? 139.272 178.656 83.716  1.00 43.40  ? 139  HIS A CB    1 
ATOM   9599  C  CG    . HIS D 3 139 ? 140.033 177.613 82.966  1.00 51.69  ? 139  HIS A CG    1 
ATOM   9600  N  ND1   . HIS D 3 139 ? 140.724 176.601 83.594  1.00 48.57  ? 139  HIS A ND1   1 
ATOM   9601  C  CD2   . HIS D 3 139 ? 140.215 177.427 81.639  1.00 58.16  ? 139  HIS A CD2   1 
ATOM   9602  C  CE1   . HIS D 3 139 ? 141.296 175.834 82.685  1.00 51.18  ? 139  HIS A CE1   1 
ATOM   9603  N  NE2   . HIS D 3 139 ? 141.005 176.314 81.491  1.00 55.68  ? 139  HIS A NE2   1 
ATOM   9604  N  N     . SER D 3 140 ? 141.696 179.373 85.177  1.00 49.56  ? 140  SER A N     1 
ATOM   9605  C  CA    . SER D 3 140 ? 143.065 179.288 85.672  1.00 47.85  ? 140  SER A CA    1 
ATOM   9606  C  C     . SER D 3 140 ? 143.323 177.898 86.225  1.00 46.61  ? 140  SER A C     1 
ATOM   9607  O  O     . SER D 3 140 ? 142.547 177.403 87.048  1.00 57.03  ? 140  SER A O     1 
ATOM   9608  C  CB    . SER D 3 140 ? 143.325 180.334 86.754  1.00 56.46  ? 140  SER A CB    1 
ATOM   9609  O  OG    . SER D 3 140 ? 142.321 180.291 87.751  1.00 57.86  ? 140  SER A OG    1 
ATOM   9610  N  N     . PHE D 3 141 ? 144.409 177.277 85.778  1.00 55.12  ? 141  PHE A N     1 
ATOM   9611  C  CA    . PHE D 3 141 ? 144.864 176.041 86.392  1.00 59.54  ? 141  PHE A CA    1 
ATOM   9612  C  C     . PHE D 3 141 ? 145.326 176.309 87.818  1.00 66.78  ? 141  PHE A C     1 
ATOM   9613  O  O     . PHE D 3 141 ? 145.936 177.342 88.106  1.00 69.02  ? 141  PHE A O     1 
ATOM   9614  C  CB    . PHE D 3 141 ? 146.011 175.434 85.585  1.00 60.59  ? 141  PHE A CB    1 
ATOM   9615  C  CG    . PHE D 3 141 ? 145.579 174.744 84.327  1.00 61.52  ? 141  PHE A CG    1 
ATOM   9616  C  CD1   . PHE D 3 141 ? 144.247 174.481 84.080  1.00 65.11  ? 141  PHE A CD1   1 
ATOM   9617  C  CD2   . PHE D 3 141 ? 146.517 174.347 83.393  1.00 63.19  ? 141  PHE A CD2   1 
ATOM   9618  C  CE1   . PHE D 3 141 ? 143.861 173.838 82.922  1.00 66.94  ? 141  PHE A CE1   1 
ATOM   9619  C  CE2   . PHE D 3 141 ? 146.137 173.706 82.237  1.00 61.88  ? 141  PHE A CE2   1 
ATOM   9620  C  CZ    . PHE D 3 141 ? 144.808 173.452 82.000  1.00 63.44  ? 141  PHE A CZ    1 
ATOM   9621  N  N     . GLY D 3 142 ? 145.036 175.373 88.713  1.00 60.78  ? 142  GLY A N     1 
ATOM   9622  C  CA    . GLY D 3 142 ? 145.517 175.481 90.074  1.00 60.75  ? 142  GLY A CA    1 
ATOM   9623  C  C     . GLY D 3 142 ? 144.447 175.780 91.100  1.00 62.26  ? 142  GLY A C     1 
ATOM   9624  O  O     . GLY D 3 142 ? 144.447 175.201 92.189  1.00 72.64  ? 142  GLY A O     1 
ATOM   9625  N  N     . GLY D 3 143 ? 143.529 176.681 90.770  1.00 51.10  ? 143  GLY A N     1 
ATOM   9626  C  CA    . GLY D 3 143 ? 142.439 176.973 91.676  1.00 56.26  ? 143  GLY A CA    1 
ATOM   9627  C  C     . GLY D 3 143 ? 141.410 175.860 91.692  1.00 58.55  ? 143  GLY A C     1 
ATOM   9628  O  O     . GLY D 3 143 ? 141.285 175.080 90.751  1.00 59.97  ? 143  GLY A O     1 
ATOM   9629  N  N     . GLY D 3 144 ? 140.660 175.787 92.791  1.00 64.89  ? 144  GLY A N     1 
ATOM   9630  C  CA    . GLY D 3 144 ? 139.635 174.764 92.900  1.00 66.77  ? 144  GLY A CA    1 
ATOM   9631  C  C     . GLY D 3 144 ? 138.513 174.959 91.901  1.00 65.31  ? 144  GLY A C     1 
ATOM   9632  O  O     . GLY D 3 144 ? 138.056 174.007 91.265  1.00 69.54  ? 144  GLY A O     1 
ATOM   9633  N  N     . THR D 3 145 ? 138.050 176.201 91.752  1.00 50.05  ? 145  THR A N     1 
ATOM   9634  C  CA    . THR D 3 145 ? 136.976 176.488 90.809  1.00 42.52  ? 145  THR A CA    1 
ATOM   9635  C  C     . THR D 3 145 ? 137.465 176.373 89.371  1.00 52.65  ? 145  THR A C     1 
ATOM   9636  O  O     . THR D 3 145 ? 136.835 175.714 88.537  1.00 59.61  ? 145  THR A O     1 
ATOM   9637  C  CB    . THR D 3 145 ? 136.406 177.877 91.076  1.00 46.57  ? 145  THR A CB    1 
ATOM   9638  O  OG1   . THR D 3 145 ? 135.858 177.920 92.398  1.00 54.21  ? 145  THR A OG1   1 
ATOM   9639  C  CG2   . THR D 3 145 ? 135.313 178.200 90.081  1.00 52.98  ? 145  THR A CG2   1 
ATOM   9640  N  N     . GLY D 3 146 ? 138.615 176.970 89.076  1.00 58.89  ? 146  GLY A N     1 
ATOM   9641  C  CA    . GLY D 3 146 ? 139.133 177.006 87.723  1.00 56.76  ? 146  GLY A CA    1 
ATOM   9642  C  C     . GLY D 3 146 ? 139.787 175.716 87.279  1.00 59.86  ? 146  GLY A C     1 
ATOM   9643  O  O     . GLY D 3 146 ? 140.416 175.665 86.219  1.00 63.66  ? 146  GLY A O     1 
ATOM   9644  N  N     . SER D 3 147 ? 139.673 174.677 88.095  1.00 55.42  ? 147  SER A N     1 
ATOM   9645  C  CA    . SER D 3 147 ? 140.084 173.333 87.723  1.00 56.71  ? 147  SER A CA    1 
ATOM   9646  C  C     . SER D 3 147 ? 138.967 172.314 87.834  1.00 54.48  ? 147  SER A C     1 
ATOM   9647  O  O     . SER D 3 147 ? 138.912 171.388 87.023  1.00 65.32  ? 147  SER A O     1 
ATOM   9648  C  CB    . SER D 3 147 ? 141.261 172.866 88.590  1.00 60.22  ? 147  SER A CB    1 
ATOM   9649  O  OG    . SER D 3 147 ? 142.384 173.713 88.425  1.00 66.14  ? 147  SER A OG    1 
ATOM   9650  N  N     . GLY D 3 148 ? 138.078 172.459 88.809  1.00 45.61  ? 148  GLY A N     1 
ATOM   9651  C  CA    . GLY D 3 148 ? 136.964 171.552 88.963  1.00 54.24  ? 148  GLY A CA    1 
ATOM   9652  C  C     . GLY D 3 148 ? 135.742 171.983 88.184  1.00 58.17  ? 148  GLY A C     1 
ATOM   9653  O  O     . GLY D 3 148 ? 135.174 171.187 87.432  1.00 63.95  ? 148  GLY A O     1 
ATOM   9654  N  N     . PHE D 3 149 ? 135.320 173.238 88.354  1.00 52.95  ? 149  PHE A N     1 
ATOM   9655  C  CA    . PHE D 3 149 ? 134.112 173.684 87.673  1.00 54.15  ? 149  PHE A CA    1 
ATOM   9656  C  C     . PHE D 3 149 ? 134.317 173.780 86.170  1.00 61.15  ? 149  PHE A C     1 
ATOM   9657  O  O     . PHE D 3 149 ? 133.392 173.493 85.402  1.00 66.91  ? 149  PHE A O     1 
ATOM   9658  C  CB    . PHE D 3 149 ? 133.645 175.025 88.227  1.00 52.58  ? 149  PHE A CB    1 
ATOM   9659  C  CG    . PHE D 3 149 ? 132.314 175.457 87.697  1.00 52.52  ? 149  PHE A CG    1 
ATOM   9660  C  CD1   . PHE D 3 149 ? 131.145 174.982 88.253  1.00 53.22  ? 149  PHE A CD1   1 
ATOM   9661  C  CD2   . PHE D 3 149 ? 132.233 176.329 86.629  1.00 56.62  ? 149  PHE A CD2   1 
ATOM   9662  C  CE1   . PHE D 3 149 ? 129.923 175.372 87.762  1.00 56.18  ? 149  PHE A CE1   1 
ATOM   9663  C  CE2   . PHE D 3 149 ? 131.015 176.721 86.132  1.00 61.51  ? 149  PHE A CE2   1 
ATOM   9664  C  CZ    . PHE D 3 149 ? 129.857 176.244 86.700  1.00 61.10  ? 149  PHE A CZ    1 
ATOM   9665  N  N     . THR D 3 150 ? 135.510 174.179 85.728  1.00 52.00  ? 150  THR A N     1 
ATOM   9666  C  CA    . THR D 3 150 ? 135.766 174.251 84.296  1.00 45.14  ? 150  THR A CA    1 
ATOM   9667  C  C     . THR D 3 150 ? 135.742 172.866 83.663  1.00 48.93  ? 150  THR A C     1 
ATOM   9668  O  O     . THR D 3 150 ? 135.323 172.714 82.514  1.00 58.67  ? 150  THR A O     1 
ATOM   9669  C  CB    . THR D 3 150 ? 137.099 174.945 84.020  1.00 53.24  ? 150  THR A CB    1 
ATOM   9670  O  OG1   . THR D 3 150 ? 137.302 175.038 82.606  1.00 58.97  ? 150  THR A OG1   1 
ATOM   9671  C  CG2   . THR D 3 150 ? 138.245 174.164 84.625  1.00 58.71  ? 150  THR A CG2   1 
ATOM   9672  N  N     . SER D 3 151 ? 136.186 171.842 84.395  1.00 51.35  ? 151  SER A N     1 
ATOM   9673  C  CA    . SER D 3 151 ? 136.159 170.488 83.851  1.00 56.70  ? 151  SER A CA    1 
ATOM   9674  C  C     . SER D 3 151 ? 134.731 169.987 83.692  1.00 60.20  ? 151  SER A C     1 
ATOM   9675  O  O     . SER D 3 151 ? 134.373 169.415 82.654  1.00 68.11  ? 151  SER A O     1 
ATOM   9676  C  CB    . SER D 3 151 ? 136.960 169.549 84.748  1.00 59.21  ? 151  SER A CB    1 
ATOM   9677  O  OG    . SER D 3 151 ? 136.777 168.203 84.355  1.00 65.92  ? 151  SER A OG    1 
ATOM   9678  N  N     . LEU D 3 152 ? 133.900 170.200 84.711  1.00 52.32  ? 152  LEU A N     1 
ATOM   9679  C  CA    . LEU D 3 152 ? 132.493 169.833 84.622  1.00 50.23  ? 152  LEU A CA    1 
ATOM   9680  C  C     . LEU D 3 152 ? 131.805 170.588 83.493  1.00 60.56  ? 152  LEU A C     1 
ATOM   9681  O  O     . LEU D 3 152 ? 131.027 170.007 82.723  1.00 69.97  ? 152  LEU A O     1 
ATOM   9682  C  CB    . LEU D 3 152 ? 131.815 170.117 85.960  1.00 49.89  ? 152  LEU A CB    1 
ATOM   9683  C  CG    . LEU D 3 152 ? 130.415 169.584 86.241  1.00 59.07  ? 152  LEU A CG    1 
ATOM   9684  C  CD1   . LEU D 3 152 ? 130.382 168.074 86.110  1.00 60.48  ? 152  LEU A CD1   1 
ATOM   9685  C  CD2   . LEU D 3 152 ? 129.972 170.018 87.624  1.00 59.51  ? 152  LEU A CD2   1 
ATOM   9686  N  N     . LEU D 3 153 ? 132.094 171.883 83.370  1.00 58.31  ? 153  LEU A N     1 
ATOM   9687  C  CA    . LEU D 3 153 ? 131.486 172.686 82.317  1.00 55.58  ? 153  LEU A CA    1 
ATOM   9688  C  C     . LEU D 3 153 ? 131.929 172.217 80.938  1.00 54.96  ? 153  LEU A C     1 
ATOM   9689  O  O     . LEU D 3 153 ? 131.123 172.182 80.002  1.00 61.62  ? 153  LEU A O     1 
ATOM   9690  C  CB    . LEU D 3 153 ? 131.829 174.158 82.528  1.00 54.80  ? 153  LEU A CB    1 
ATOM   9691  C  CG    . LEU D 3 153 ? 131.150 175.178 81.622  1.00 56.47  ? 153  LEU A CG    1 
ATOM   9692  C  CD1   . LEU D 3 153 ? 129.649 175.105 81.778  1.00 56.46  ? 153  LEU A CD1   1 
ATOM   9693  C  CD2   . LEU D 3 153 ? 131.651 176.563 81.958  1.00 58.24  ? 153  LEU A CD2   1 
ATOM   9694  N  N     . MET D 3 154 ? 133.206 171.860 80.787  1.00 54.42  ? 154  MET A N     1 
ATOM   9695  C  CA    . MET D 3 154 ? 133.681 171.366 79.500  1.00 60.44  ? 154  MET A CA    1 
ATOM   9696  C  C     . MET D 3 154 ? 133.043 170.031 79.153  1.00 59.69  ? 154  MET A C     1 
ATOM   9697  O  O     . MET D 3 154 ? 132.688 169.793 77.994  1.00 64.57  ? 154  MET A O     1 
ATOM   9698  C  CB    . MET D 3 154 ? 135.204 171.251 79.501  1.00 62.30  ? 154  MET A CB    1 
ATOM   9699  C  CG    . MET D 3 154 ? 135.925 172.586 79.459  1.00 62.00  ? 154  MET A CG    1 
ATOM   9700  S  SD    . MET D 3 154 ? 135.564 173.538 77.976  1.00 71.70  ? 154  MET A SD    1 
ATOM   9701  C  CE    . MET D 3 154 ? 136.441 172.583 76.744  1.00 64.91  ? 154  MET A CE    1 
ATOM   9702  N  N     . GLU D 3 155 ? 132.882 169.148 80.142  1.00 60.15  ? 155  GLU A N     1 
ATOM   9703  C  CA    . GLU D 3 155 ? 132.188 167.888 79.892  1.00 62.28  ? 155  GLU A CA    1 
ATOM   9704  C  C     . GLU D 3 155 ? 130.764 168.142 79.418  1.00 61.66  ? 155  GLU A C     1 
ATOM   9705  O  O     . GLU D 3 155 ? 130.308 167.556 78.426  1.00 67.03  ? 155  GLU A O     1 
ATOM   9706  C  CB    . GLU D 3 155 ? 132.187 167.027 81.155  1.00 64.93  ? 155  GLU A CB    1 
ATOM   9707  C  CG    . GLU D 3 155 ? 133.545 166.467 81.533  1.00 70.20  ? 155  GLU A CG    1 
ATOM   9708  C  CD    . GLU D 3 155 ? 133.475 165.513 82.708  1.00 75.57  ? 155  GLU A CD    1 
ATOM   9709  O  OE1   . GLU D 3 155 ? 132.363 165.294 83.232  1.00 78.67  ? 155  GLU A OE1   1 
ATOM   9710  O  OE2   . GLU D 3 155 ? 134.532 164.981 83.107  1.00 73.32  ? 155  GLU A OE2   1 
ATOM   9711  N  N     . ARG D 3 156 ? 130.053 169.034 80.110  1.00 57.60  ? 156  ARG A N     1 
ATOM   9712  C  CA    . ARG D 3 156 ? 128.676 169.333 79.737  1.00 56.94  ? 156  ARG A CA    1 
ATOM   9713  C  C     . ARG D 3 156 ? 128.595 169.932 78.339  1.00 60.06  ? 156  ARG A C     1 
ATOM   9714  O  O     . ARG D 3 156 ? 127.727 169.554 77.544  1.00 68.37  ? 156  ARG A O     1 
ATOM   9715  C  CB    . ARG D 3 156 ? 128.054 170.281 80.759  1.00 59.59  ? 156  ARG A CB    1 
ATOM   9716  C  CG    . ARG D 3 156 ? 127.878 169.676 82.134  1.00 59.16  ? 156  ARG A CG    1 
ATOM   9717  C  CD    . ARG D 3 156 ? 127.189 168.336 82.062  1.00 57.84  ? 156  ARG A CD    1 
ATOM   9718  N  NE    . ARG D 3 156 ? 126.818 167.861 83.387  1.00 63.91  ? 156  ARG A NE    1 
ATOM   9719  C  CZ    . ARG D 3 156 ? 125.658 168.123 83.972  1.00 67.21  ? 156  ARG A CZ    1 
ATOM   9720  N  NH1   . ARG D 3 156 ? 124.741 168.870 83.381  1.00 61.90  ? 156  ARG A NH1   1 
ATOM   9721  N  NH2   . ARG D 3 156 ? 125.415 167.629 85.182  1.00 67.66  ? 156  ARG A NH2   1 
ATOM   9722  N  N     . LEU D 3 157 ? 129.487 170.870 78.022  1.00 52.57  ? 157  LEU A N     1 
ATOM   9723  C  CA    . LEU D 3 157 ? 129.456 171.512 76.713  1.00 53.33  ? 157  LEU A CA    1 
ATOM   9724  C  C     . LEU D 3 157 ? 129.794 170.529 75.601  1.00 58.73  ? 157  LEU A C     1 
ATOM   9725  O  O     . LEU D 3 157 ? 129.179 170.565 74.529  1.00 65.50  ? 157  LEU A O     1 
ATOM   9726  C  CB    . LEU D 3 157 ? 130.415 172.699 76.688  1.00 58.42  ? 157  LEU A CB    1 
ATOM   9727  C  CG    . LEU D 3 157 ? 129.960 173.958 77.417  1.00 61.27  ? 157  LEU A CG    1 
ATOM   9728  C  CD1   . LEU D 3 157 ? 130.973 175.066 77.220  1.00 60.69  ? 157  LEU A CD1   1 
ATOM   9729  C  CD2   . LEU D 3 157 ? 128.587 174.387 76.936  1.00 59.66  ? 157  LEU A CD2   1 
ATOM   9730  N  N     . SER D 3 158 ? 130.774 169.653 75.825  1.00 61.12  ? 158  SER A N     1 
ATOM   9731  C  CA    . SER D 3 158 ? 131.110 168.655 74.817  1.00 58.82  ? 158  SER A CA    1 
ATOM   9732  C  C     . SER D 3 158 ? 129.952 167.694 74.588  1.00 57.81  ? 158  SER A C     1 
ATOM   9733  O  O     . SER D 3 158 ? 129.672 167.311 73.447  1.00 61.45  ? 158  SER A O     1 
ATOM   9734  C  CB    . SER D 3 158 ? 132.367 167.892 75.230  1.00 66.21  ? 158  SER A CB    1 
ATOM   9735  O  OG    . SER D 3 158 ? 132.686 166.887 74.285  1.00 68.81  ? 158  SER A OG    1 
ATOM   9736  N  N     . VAL D 3 159 ? 129.268 167.286 75.658  1.00 58.20  ? 159  VAL A N     1 
ATOM   9737  C  CA    . VAL D 3 159 ? 128.129 166.389 75.491  1.00 56.68  ? 159  VAL A CA    1 
ATOM   9738  C  C     . VAL D 3 159 ? 126.988 167.094 74.766  1.00 58.57  ? 159  VAL A C     1 
ATOM   9739  O  O     . VAL D 3 159 ? 126.323 166.505 73.907  1.00 60.59  ? 159  VAL A O     1 
ATOM   9740  C  CB    . VAL D 3 159 ? 127.682 165.834 76.856  1.00 61.45  ? 159  VAL A CB    1 
ATOM   9741  C  CG1   . VAL D 3 159 ? 126.343 165.129 76.733  1.00 58.74  ? 159  VAL A CG1   1 
ATOM   9742  C  CG2   . VAL D 3 159 ? 128.734 164.888 77.411  1.00 61.27  ? 159  VAL A CG2   1 
ATOM   9743  N  N     . ASP D 3 160 ? 126.753 168.368 75.085  1.00 65.27  ? 160  ASP A N     1 
ATOM   9744  C  CA    . ASP D 3 160 ? 125.591 169.074 74.554  1.00 60.89  ? 160  ASP A CA    1 
ATOM   9745  C  C     . ASP D 3 160 ? 125.831 169.570 73.132  1.00 60.61  ? 160  ASP A C     1 
ATOM   9746  O  O     . ASP D 3 160 ? 125.056 169.268 72.219  1.00 65.19  ? 160  ASP A O     1 
ATOM   9747  C  CB    . ASP D 3 160 ? 125.225 170.240 75.473  1.00 63.17  ? 160  ASP A CB    1 
ATOM   9748  C  CG    . ASP D 3 160 ? 123.865 170.828 75.157  1.00 73.24  ? 160  ASP A CG    1 
ATOM   9749  O  OD1   . ASP D 3 160 ? 123.121 170.220 74.358  1.00 71.70  ? 160  ASP A OD1   1 
ATOM   9750  O  OD2   . ASP D 3 160 ? 123.538 171.900 75.706  1.00 76.88  ? 160  ASP A OD2   1 
ATOM   9751  N  N     . TYR D 3 161 ? 126.897 170.341 72.927  1.00 55.52  ? 161  TYR A N     1 
ATOM   9752  C  CA    . TYR D 3 161 ? 127.185 170.916 71.616  1.00 57.81  ? 161  TYR A CA    1 
ATOM   9753  C  C     . TYR D 3 161 ? 128.154 170.050 70.816  1.00 60.14  ? 161  TYR A C     1 
ATOM   9754  O  O     . TYR D 3 161 ? 127.827 169.598 69.714  1.00 60.66  ? 161  TYR A O     1 
ATOM   9755  C  CB    . TYR D 3 161 ? 127.717 172.340 71.791  1.00 56.32  ? 161  TYR A CB    1 
ATOM   9756  C  CG    . TYR D 3 161 ? 126.737 173.229 72.516  1.00 56.42  ? 161  TYR A CG    1 
ATOM   9757  C  CD1   . TYR D 3 161 ? 125.399 173.247 72.158  1.00 57.10  ? 161  TYR A CD1   1 
ATOM   9758  C  CD2   . TYR D 3 161 ? 127.138 174.022 73.573  1.00 56.49  ? 161  TYR A CD2   1 
ATOM   9759  C  CE1   . TYR D 3 161 ? 124.496 174.048 72.818  1.00 56.35  ? 161  TYR A CE1   1 
ATOM   9760  C  CE2   . TYR D 3 161 ? 126.243 174.821 74.240  1.00 56.08  ? 161  TYR A CE2   1 
ATOM   9761  C  CZ    . TYR D 3 161 ? 124.925 174.832 73.860  1.00 57.65  ? 161  TYR A CZ    1 
ATOM   9762  O  OH    . TYR D 3 161 ? 124.028 175.633 74.527  1.00 61.79  ? 161  TYR A OH    1 
ATOM   9763  N  N     . GLY D 3 162 ? 129.347 169.817 71.350  1.00 69.24  ? 162  GLY A N     1 
ATOM   9764  C  CA    . GLY D 3 162 ? 130.253 168.857 70.751  1.00 66.95  ? 162  GLY A CA    1 
ATOM   9765  C  C     . GLY D 3 162 ? 130.896 169.317 69.462  1.00 66.35  ? 162  GLY A C     1 
ATOM   9766  O  O     . GLY D 3 162 ? 132.110 169.530 69.408  1.00 69.41  ? 162  GLY A O     1 
ATOM   9767  N  N     . LYS D 3 163 ? 130.089 169.469 68.410  1.00 67.81  ? 163  LYS A N     1 
ATOM   9768  C  CA    . LYS D 3 163 ? 130.631 169.884 67.121  1.00 69.46  ? 163  LYS A CA    1 
ATOM   9769  C  C     . LYS D 3 163 ? 131.169 171.306 67.166  1.00 68.35  ? 163  LYS A C     1 
ATOM   9770  O  O     . LYS D 3 163 ? 132.013 171.674 66.342  1.00 69.50  ? 163  LYS A O     1 
ATOM   9771  C  CB    . LYS D 3 163 ? 129.563 169.760 66.035  1.00 71.55  ? 163  LYS A CB    1 
ATOM   9772  C  CG    . LYS D 3 163 ? 129.110 168.335 65.768  1.00 72.16  ? 163  LYS A CG    1 
ATOM   9773  C  CD    . LYS D 3 163 ? 128.123 168.281 64.615  1.00 71.58  ? 163  LYS A CD    1 
ATOM   9774  C  CE    . LYS D 3 163 ? 127.703 166.852 64.313  1.00 72.00  ? 163  LYS A CE    1 
ATOM   9775  N  NZ    . LYS D 3 163 ? 126.755 166.785 63.167  1.00 71.35  ? 163  LYS A NZ    1 
ATOM   9776  N  N     . LYS D 3 164 ? 130.701 172.113 68.110  1.00 63.69  ? 164  LYS A N     1 
ATOM   9777  C  CA    . LYS D 3 164 ? 131.144 173.494 68.198  1.00 64.08  ? 164  LYS A CA    1 
ATOM   9778  C  C     . LYS D 3 164 ? 132.531 173.573 68.825  1.00 67.04  ? 164  LYS A C     1 
ATOM   9779  O  O     . LYS D 3 164 ? 132.902 172.764 69.678  1.00 69.53  ? 164  LYS A O     1 
ATOM   9780  C  CB    . LYS D 3 164 ? 130.147 174.321 69.006  1.00 64.79  ? 164  LYS A CB    1 
ATOM   9781  C  CG    . LYS D 3 164 ? 130.078 175.776 68.594  1.00 65.40  ? 164  LYS A CG    1 
ATOM   9782  C  CD    . LYS D 3 164 ? 129.396 175.927 67.246  1.00 66.28  ? 164  LYS A CD    1 
ATOM   9783  C  CE    . LYS D 3 164 ? 127.973 175.400 67.284  1.00 66.32  ? 164  LYS A CE    1 
ATOM   9784  N  NZ    . LYS D 3 164 ? 127.293 175.551 65.970  1.00 63.81  ? 164  LYS A NZ    1 
ATOM   9785  N  N     . SER D 3 165 ? 133.300 174.565 68.387  1.00 58.99  ? 165  SER A N     1 
ATOM   9786  C  CA    . SER D 3 165 ? 134.660 174.743 68.868  1.00 53.94  ? 165  SER A CA    1 
ATOM   9787  C  C     . SER D 3 165 ? 134.675 175.180 70.327  1.00 58.10  ? 165  SER A C     1 
ATOM   9788  O  O     . SER D 3 165 ? 133.698 175.723 70.849  1.00 65.00  ? 165  SER A O     1 
ATOM   9789  C  CB    . SER D 3 165 ? 135.391 175.776 68.017  1.00 58.42  ? 165  SER A CB    1 
ATOM   9790  O  OG    . SER D 3 165 ? 136.675 176.050 68.546  1.00 66.72  ? 165  SER A OG    1 
ATOM   9791  N  N     . LYS D 3 166 ? 135.804 174.935 70.988  1.00 52.92  ? 166  LYS A N     1 
ATOM   9792  C  CA    . LYS D 3 166 ? 135.990 175.302 72.389  1.00 51.80  ? 166  LYS A CA    1 
ATOM   9793  C  C     . LYS D 3 166 ? 137.439 175.720 72.582  1.00 51.82  ? 166  LYS A C     1 
ATOM   9794  O  O     . LYS D 3 166 ? 138.348 174.898 72.435  1.00 57.68  ? 166  LYS A O     1 
ATOM   9795  C  CB    . LYS D 3 166 ? 135.628 174.146 73.318  1.00 49.69  ? 166  LYS A CB    1 
ATOM   9796  C  CG    . LYS D 3 166 ? 134.150 174.044 73.630  1.00 57.99  ? 166  LYS A CG    1 
ATOM   9797  C  CD    . LYS D 3 166 ? 133.798 172.687 74.200  1.00 58.21  ? 166  LYS A CD    1 
ATOM   9798  C  CE    . LYS D 3 166 ? 133.785 171.629 73.117  1.00 63.83  ? 166  LYS A CE    1 
ATOM   9799  N  NZ    . LYS D 3 166 ? 132.782 171.942 72.069  1.00 57.04  ? 166  LYS A NZ    1 
ATOM   9800  N  N     . LEU D 3 167 ? 137.653 176.987 72.913  1.00 51.02  ? 167  LEU A N     1 
ATOM   9801  C  CA    . LEU D 3 167 ? 138.979 177.533 73.150  1.00 52.05  ? 167  LEU A CA    1 
ATOM   9802  C  C     . LEU D 3 167 ? 139.125 177.918 74.615  1.00 59.29  ? 167  LEU A C     1 
ATOM   9803  O  O     . LEU D 3 167 ? 138.203 178.483 75.212  1.00 64.29  ? 167  LEU A O     1 
ATOM   9804  C  CB    . LEU D 3 167 ? 139.240 178.751 72.264  1.00 51.12  ? 167  LEU A CB    1 
ATOM   9805  C  CG    . LEU D 3 167 ? 138.996 178.569 70.768  1.00 53.59  ? 167  LEU A CG    1 
ATOM   9806  C  CD1   . LEU D 3 167 ? 139.341 179.840 70.018  1.00 59.23  ? 167  LEU A CD1   1 
ATOM   9807  C  CD2   . LEU D 3 167 ? 139.799 177.398 70.239  1.00 56.02  ? 167  LEU A CD2   1 
ATOM   9808  N  N     . GLU D 3 168 ? 140.284 177.612 75.189  1.00 64.21  ? 168  GLU A N     1 
ATOM   9809  C  CA    . GLU D 3 168 ? 140.567 177.888 76.588  1.00 56.03  ? 168  GLU A CA    1 
ATOM   9810  C  C     . GLU D 3 168 ? 141.778 178.800 76.708  1.00 62.02  ? 168  GLU A C     1 
ATOM   9811  O  O     . GLU D 3 168 ? 142.728 178.705 75.925  1.00 72.30  ? 168  GLU A O     1 
ATOM   9812  C  CB    . GLU D 3 168 ? 140.819 176.596 77.362  1.00 54.72  ? 168  GLU A CB    1 
ATOM   9813  C  CG    . GLU D 3 168 ? 139.580 175.766 77.607  1.00 68.02  ? 168  GLU A CG    1 
ATOM   9814  C  CD    . GLU D 3 168 ? 139.846 174.594 78.529  1.00 77.97  ? 168  GLU A CD    1 
ATOM   9815  O  OE1   . GLU D 3 168 ? 141.026 174.218 78.686  1.00 73.78  ? 168  GLU A OE1   1 
ATOM   9816  O  OE2   . GLU D 3 168 ? 138.876 174.047 79.095  1.00 77.83  ? 168  GLU A OE2   1 
ATOM   9817  N  N     . PHE D 3 169 ? 141.737 179.690 77.698  1.00 59.56  ? 169  PHE A N     1 
ATOM   9818  C  CA    . PHE D 3 169 ? 142.838 180.603 78.000  1.00 58.87  ? 169  PHE A CA    1 
ATOM   9819  C  C     . PHE D 3 169 ? 143.161 180.418 79.478  1.00 62.81  ? 169  PHE A C     1 
ATOM   9820  O  O     . PHE D 3 169 ? 142.636 181.134 80.333  1.00 70.16  ? 169  PHE A O     1 
ATOM   9821  C  CB    . PHE D 3 169 ? 142.474 182.042 77.668  1.00 58.88  ? 169  PHE A CB    1 
ATOM   9822  C  CG    . PHE D 3 169 ? 142.361 182.312 76.197  1.00 65.76  ? 169  PHE A CG    1 
ATOM   9823  C  CD1   . PHE D 3 169 ? 141.244 181.909 75.489  1.00 68.54  ? 169  PHE A CD1   1 
ATOM   9824  C  CD2   . PHE D 3 169 ? 143.372 182.971 75.522  1.00 68.28  ? 169  PHE A CD2   1 
ATOM   9825  C  CE1   . PHE D 3 169 ? 141.137 182.154 74.137  1.00 69.30  ? 169  PHE A CE1   1 
ATOM   9826  C  CE2   . PHE D 3 169 ? 143.270 183.220 74.169  1.00 66.30  ? 169  PHE A CE2   1 
ATOM   9827  C  CZ    . PHE D 3 169 ? 142.151 182.812 73.476  1.00 68.76  ? 169  PHE A CZ    1 
ATOM   9828  N  N     . SER D 3 170 ? 144.026 179.456 79.771  1.00 58.22  ? 170  SER A N     1 
ATOM   9829  C  CA    . SER D 3 170 ? 144.314 179.064 81.140  1.00 58.82  ? 170  SER A CA    1 
ATOM   9830  C  C     . SER D 3 170 ? 145.548 179.783 81.670  1.00 59.70  ? 170  SER A C     1 
ATOM   9831  O  O     . SER D 3 170 ? 146.400 180.258 80.916  1.00 67.15  ? 170  SER A O     1 
ATOM   9832  C  CB    . SER D 3 170 ? 144.511 177.552 81.231  1.00 62.55  ? 170  SER A CB    1 
ATOM   9833  O  OG    . SER D 3 170 ? 143.500 176.864 80.518  1.00 67.27  ? 170  SER A OG    1 
ATOM   9834  N  N     . ILE D 3 171 ? 145.633 179.854 82.993  1.00 52.84  ? 171  ILE A N     1 
ATOM   9835  C  CA    . ILE D 3 171 ? 146.782 180.434 83.682  1.00 54.44  ? 171  ILE A CA    1 
ATOM   9836  C  C     . ILE D 3 171 ? 147.580 179.254 84.225  1.00 61.48  ? 171  ILE A C     1 
ATOM   9837  O  O     . ILE D 3 171 ? 147.301 178.727 85.302  1.00 68.29  ? 171  ILE A O     1 
ATOM   9838  C  CB    . ILE D 3 171 ? 146.360 181.402 84.782  1.00 56.18  ? 171  ILE A CB    1 
ATOM   9839  C  CG1   . ILE D 3 171 ? 145.478 182.509 84.211  1.00 57.29  ? 171  ILE A CG1   1 
ATOM   9840  C  CG2   . ILE D 3 171 ? 147.581 181.999 85.457  1.00 59.42  ? 171  ILE A CG2   1 
ATOM   9841  C  CD1   . ILE D 3 171 ? 146.203 183.440 83.291  1.00 60.22  ? 171  ILE A CD1   1 
ATOM   9842  N  N     . TYR D 3 172 ? 148.580 178.830 83.463  1.00 59.69  ? 172  TYR A N     1 
ATOM   9843  C  CA    . TYR D 3 172 ? 149.363 177.668 83.848  1.00 58.71  ? 172  TYR A CA    1 
ATOM   9844  C  C     . TYR D 3 172 ? 150.230 177.996 85.064  1.00 65.00  ? 172  TYR A C     1 
ATOM   9845  O  O     . TYR D 3 172 ? 150.724 179.120 85.187  1.00 67.94  ? 172  TYR A O     1 
ATOM   9846  C  CB    . TYR D 3 172 ? 150.238 177.217 82.680  1.00 62.20  ? 172  TYR A CB    1 
ATOM   9847  C  CG    . TYR D 3 172 ? 150.893 175.874 82.877  1.00 66.37  ? 172  TYR A CG    1 
ATOM   9848  C  CD1   . TYR D 3 172 ? 150.132 174.728 83.046  1.00 66.92  ? 172  TYR A CD1   1 
ATOM   9849  C  CD2   . TYR D 3 172 ? 152.272 175.753 82.893  1.00 64.73  ? 172  TYR A CD2   1 
ATOM   9850  C  CE1   . TYR D 3 172 ? 150.725 173.503 83.232  1.00 68.24  ? 172  TYR A CE1   1 
ATOM   9851  C  CE2   . TYR D 3 172 ? 152.875 174.531 83.077  1.00 67.40  ? 172  TYR A CE2   1 
ATOM   9852  C  CZ    . TYR D 3 172 ? 152.098 173.407 83.244  1.00 70.08  ? 172  TYR A CZ    1 
ATOM   9853  O  OH    . TYR D 3 172 ? 152.702 172.184 83.425  1.00 73.25  ? 172  TYR A OH    1 
ATOM   9854  N  N     . PRO D 3 173 ? 150.409 177.051 85.988  1.00 63.16  ? 173  PRO A N     1 
ATOM   9855  C  CA    . PRO D 3 173 ? 151.322 177.288 87.111  1.00 59.07  ? 173  PRO A CA    1 
ATOM   9856  C  C     . PRO D 3 173 ? 152.743 177.564 86.640  1.00 60.21  ? 173  PRO A C     1 
ATOM   9857  O  O     . PRO D 3 173 ? 153.240 176.946 85.698  1.00 61.58  ? 173  PRO A O     1 
ATOM   9858  C  CB    . PRO D 3 173 ? 151.240 175.984 87.909  1.00 53.17  ? 173  PRO A CB    1 
ATOM   9859  C  CG    . PRO D 3 173 ? 149.895 175.456 87.606  1.00 56.74  ? 173  PRO A CG    1 
ATOM   9860  C  CD    . PRO D 3 173 ? 149.608 175.832 86.184  1.00 59.22  ? 173  PRO A CD    1 
ATOM   9861  N  N     . ALA D 3 174 ? 153.395 178.500 87.318  1.00 60.41  ? 174  ALA A N     1 
ATOM   9862  C  CA    . ALA D 3 174 ? 154.762 178.872 87.006  1.00 61.49  ? 174  ALA A CA    1 
ATOM   9863  C  C     . ALA D 3 174 ? 155.742 177.898 87.653  1.00 56.23  ? 174  ALA A C     1 
ATOM   9864  O  O     . ALA D 3 174 ? 155.391 177.185 88.595  1.00 60.82  ? 174  ALA A O     1 
ATOM   9865  C  CB    . ALA D 3 174 ? 155.032 180.297 87.477  1.00 60.48  ? 174  ALA A CB    1 
ATOM   9866  N  N     . PRO D 3 175 ? 156.979 177.830 87.146  1.00 42.86  ? 175  PRO A N     1 
ATOM   9867  C  CA    . PRO D 3 175 ? 157.971 176.931 87.748  1.00 47.85  ? 175  PRO A CA    1 
ATOM   9868  C  C     . PRO D 3 175 ? 158.258 177.239 89.208  1.00 54.65  ? 175  PRO A C     1 
ATOM   9869  O  O     . PRO D 3 175 ? 158.086 176.380 90.077  1.00 59.21  ? 175  PRO A O     1 
ATOM   9870  C  CB    . PRO D 3 175 ? 159.215 177.157 86.880  1.00 54.91  ? 175  PRO A CB    1 
ATOM   9871  C  CG    . PRO D 3 175 ? 158.685 177.629 85.586  1.00 53.52  ? 175  PRO A CG    1 
ATOM   9872  C  CD    . PRO D 3 175 ? 157.494 178.465 85.922  1.00 50.78  ? 175  PRO A CD    1 
ATOM   9873  N  N     . GLN D 3 176 ? 158.693 178.466 89.489  1.00 61.48  ? 176  GLN A N     1 
ATOM   9874  C  CA    . GLN D 3 176 ? 159.118 178.858 90.828  1.00 57.06  ? 176  GLN A CA    1 
ATOM   9875  C  C     . GLN D 3 176 ? 158.054 179.680 91.546  1.00 58.32  ? 176  GLN A C     1 
ATOM   9876  O  O     . GLN D 3 176 ? 157.666 179.357 92.672  1.00 63.09  ? 176  GLN A O     1 
ATOM   9877  C  CB    . GLN D 3 176 ? 160.434 179.640 90.742  1.00 60.20  ? 176  GLN A CB    1 
ATOM   9878  C  CG    . GLN D 3 176 ? 161.557 178.881 90.063  1.00 60.96  ? 176  GLN A CG    1 
ATOM   9879  C  CD    . GLN D 3 176 ? 162.747 178.676 90.973  1.00 68.79  ? 176  GLN A CD    1 
ATOM   9880  O  OE1   . GLN D 3 176 ? 163.705 179.448 90.944  1.00 70.41  ? 176  GLN A OE1   1 
ATOM   9881  N  NE2   . GLN D 3 176 ? 162.692 177.634 91.792  1.00 66.17  ? 176  GLN A NE2   1 
ATOM   9882  N  N     . VAL D 3 177 ? 157.577 180.748 90.909  1.00 60.10  ? 177  VAL A N     1 
ATOM   9883  C  CA    . VAL D 3 177 ? 156.531 181.573 91.499  1.00 60.93  ? 177  VAL A CA    1 
ATOM   9884  C  C     . VAL D 3 177 ? 155.247 180.762 91.586  1.00 64.36  ? 177  VAL A C     1 
ATOM   9885  O  O     . VAL D 3 177 ? 154.795 180.178 90.594  1.00 69.58  ? 177  VAL A O     1 
ATOM   9886  C  CB    . VAL D 3 177 ? 156.338 182.852 90.679  1.00 63.94  ? 177  VAL A CB    1 
ATOM   9887  C  CG1   . VAL D 3 177 ? 154.930 183.384 90.835  1.00 61.15  ? 177  VAL A CG1   1 
ATOM   9888  C  CG2   . VAL D 3 177 ? 157.358 183.900 91.090  1.00 62.61  ? 177  VAL A CG2   1 
ATOM   9889  N  N     . SER D 3 178 ? 154.657 180.711 92.776  1.00 64.01  ? 178  SER A N     1 
ATOM   9890  C  CA    . SER D 3 178 ? 153.385 180.030 92.957  1.00 64.46  ? 178  SER A CA    1 
ATOM   9891  C  C     . SER D 3 178 ? 152.677 180.613 94.169  1.00 63.91  ? 178  SER A C     1 
ATOM   9892  O  O     . SER D 3 178 ? 153.296 181.232 95.037  1.00 66.65  ? 178  SER A O     1 
ATOM   9893  C  CB    . SER D 3 178 ? 153.567 178.519 93.117  1.00 64.07  ? 178  SER A CB    1 
ATOM   9894  O  OG    . SER D 3 178 ? 152.318 177.880 93.308  1.00 68.96  ? 178  SER A OG    1 
ATOM   9895  N  N     . THR D 3 179 ? 151.363 180.405 94.217  1.00 65.66  ? 179  THR A N     1 
ATOM   9896  C  CA    . THR D 3 179 ? 150.533 180.901 95.305  1.00 68.13  ? 179  THR A CA    1 
ATOM   9897  C  C     . THR D 3 179 ? 150.007 179.778 96.187  1.00 70.19  ? 179  THR A C     1 
ATOM   9898  O  O     . THR D 3 179 ? 150.248 179.775 97.396  1.00 72.06  ? 179  THR A O     1 
ATOM   9899  C  CB    . THR D 3 179 ? 149.363 181.716 94.745  1.00 69.58  ? 179  THR A CB    1 
ATOM   9900  O  OG1   . THR D 3 179 ? 149.861 182.891 94.096  1.00 69.06  ? 179  THR A OG1   1 
ATOM   9901  C  CG2   . THR D 3 179 ? 148.424 182.111 95.869  1.00 67.02  ? 179  THR A CG2   1 
ATOM   9902  N  N     . ALA D 3 180 ? 149.298 178.815 95.611  1.00 59.15  ? 180  ALA A N     1 
ATOM   9903  C  CA    . ALA D 3 180 ? 148.746 177.721 96.387  1.00 56.41  ? 180  ALA A CA    1 
ATOM   9904  C  C     . ALA D 3 180 ? 149.810 176.663 96.655  1.00 59.08  ? 180  ALA A C     1 
ATOM   9905  O  O     . ALA D 3 180 ? 150.872 176.630 96.029  1.00 60.45  ? 180  ALA A O     1 
ATOM   9906  C  CB    . ALA D 3 180 ? 147.553 177.103 95.664  1.00 53.92  ? 180  ALA A CB    1 
ATOM   9907  N  N     . VAL D 3 181 ? 149.512 175.788 97.611  1.00 54.04  ? 181  VAL A N     1 
ATOM   9908  C  CA    . VAL D 3 181 ? 150.378 174.665 97.919  1.00 53.40  ? 181  VAL A CA    1 
ATOM   9909  C  C     . VAL D 3 181 ? 149.881 173.368 97.290  1.00 60.70  ? 181  VAL A C     1 
ATOM   9910  O  O     . VAL D 3 181 ? 150.679 172.445 97.090  1.00 66.59  ? 181  VAL A O     1 
ATOM   9911  C  CB    . VAL D 3 181 ? 150.533 174.506 99.445  1.00 53.90  ? 181  VAL A CB    1 
ATOM   9912  C  CG1   . VAL D 3 181 ? 151.777 173.705 99.777  1.00 57.44  ? 181  VAL A CG1   1 
ATOM   9913  C  CG2   . VAL D 3 181 ? 150.570 175.863 100.112 1.00 52.40  ? 181  VAL A CG2   1 
ATOM   9914  N  N     . VAL D 3 182 ? 148.594 173.277 96.960  1.00 58.95  ? 182  VAL A N     1 
ATOM   9915  C  CA    . VAL D 3 182 ? 148.014 172.083 96.361  1.00 55.13  ? 182  VAL A CA    1 
ATOM   9916  C  C     . VAL D 3 182 ? 147.802 172.322 94.874  1.00 57.40  ? 182  VAL A C     1 
ATOM   9917  O  O     . VAL D 3 182 ? 146.994 171.643 94.230  1.00 65.89  ? 182  VAL A O     1 
ATOM   9918  C  CB    . VAL D 3 182 ? 146.694 171.706 97.053  1.00 59.90  ? 182  VAL A CB    1 
ATOM   9919  C  CG1   . VAL D 3 182 ? 146.955 171.264 98.476  1.00 62.86  ? 182  VAL A CG1   1 
ATOM   9920  C  CG2   . VAL D 3 182 ? 145.737 172.881 97.030  1.00 56.75  ? 182  VAL A CG2   1 
ATOM   9921  N  N     . GLU D 3 183 ? 148.522 173.296 94.324  1.00 60.26  ? 183  GLU A N     1 
ATOM   9922  C  CA    . GLU D 3 183 ? 148.371 173.628 92.911  1.00 56.97  ? 183  GLU A CA    1 
ATOM   9923  C  C     . GLU D 3 183 ? 148.723 172.486 91.961  1.00 64.43  ? 183  GLU A C     1 
ATOM   9924  O  O     . GLU D 3 183 ? 147.968 172.280 90.994  1.00 71.07  ? 183  GLU A O     1 
ATOM   9925  C  CB    . GLU D 3 183 ? 149.200 174.877 92.591  1.00 59.25  ? 183  GLU A CB    1 
ATOM   9926  C  CG    . GLU D 3 183 ? 148.829 175.551 91.291  1.00 66.23  ? 183  GLU A CG    1 
ATOM   9927  C  CD    . GLU D 3 183 ? 149.424 176.937 91.166  1.00 71.99  ? 183  GLU A CD    1 
ATOM   9928  O  OE1   . GLU D 3 183 ? 150.349 177.259 91.941  1.00 70.64  ? 183  GLU A OE1   1 
ATOM   9929  O  OE2   . GLU D 3 183 ? 148.967 177.706 90.294  1.00 72.38  ? 183  GLU A OE2   1 
ATOM   9930  N  N     . PRO D 3 184 ? 149.829 171.744 92.134  1.00 54.56  ? 184  PRO A N     1 
ATOM   9931  C  CA    . PRO D 3 184 ? 150.108 170.646 91.191  1.00 54.52  ? 184  PRO A CA    1 
ATOM   9932  C  C     . PRO D 3 184 ? 148.992 169.624 91.099  1.00 55.88  ? 184  PRO A C     1 
ATOM   9933  O  O     . PRO D 3 184 ? 148.680 169.145 89.999  1.00 65.25  ? 184  PRO A O     1 
ATOM   9934  C  CB    . PRO D 3 184 ? 151.393 170.028 91.754  1.00 56.61  ? 184  PRO A CB    1 
ATOM   9935  C  CG    . PRO D 3 184 ? 152.038 171.125 92.488  1.00 59.16  ? 184  PRO A CG    1 
ATOM   9936  C  CD    . PRO D 3 184 ? 150.929 171.911 93.100  1.00 54.43  ? 184  PRO A CD    1 
ATOM   9937  N  N     . TYR D 3 185 ? 148.371 169.286 92.230  1.00 49.00  ? 185  TYR A N     1 
ATOM   9938  C  CA    . TYR D 3 185 ? 147.276 168.324 92.219  1.00 51.74  ? 185  TYR A CA    1 
ATOM   9939  C  C     . TYR D 3 185 ? 146.137 168.818 91.339  1.00 57.00  ? 185  TYR A C     1 
ATOM   9940  O  O     . TYR D 3 185 ? 145.657 168.096 90.454  1.00 66.80  ? 185  TYR A O     1 
ATOM   9941  C  CB    . TYR D 3 185 ? 146.771 168.083 93.642  1.00 51.02  ? 185  TYR A CB    1 
ATOM   9942  C  CG    . TYR D 3 185 ? 147.674 167.256 94.529  1.00 56.23  ? 185  TYR A CG    1 
ATOM   9943  C  CD1   . TYR D 3 185 ? 148.907 166.811 94.087  1.00 56.45  ? 185  TYR A CD1   1 
ATOM   9944  C  CD2   . TYR D 3 185 ? 147.280 166.912 95.809  1.00 58.25  ? 185  TYR A CD2   1 
ATOM   9945  C  CE1   . TYR D 3 185 ? 149.725 166.054 94.902  1.00 55.49  ? 185  TYR A CE1   1 
ATOM   9946  C  CE2   . TYR D 3 185 ? 148.087 166.157 96.625  1.00 51.73  ? 185  TYR A CE2   1 
ATOM   9947  C  CZ    . TYR D 3 185 ? 149.306 165.731 96.171  1.00 57.02  ? 185  TYR A CZ    1 
ATOM   9948  O  OH    . TYR D 3 185 ? 150.110 164.977 96.990  1.00 64.99  ? 185  TYR A OH    1 
ATOM   9949  N  N     . ASN D 3 186 ? 145.702 170.059 91.566  1.00 51.58  ? 186  ASN A N     1 
ATOM   9950  C  CA    . ASN D 3 186 ? 144.598 170.615 90.796  1.00 52.43  ? 186  ASN A CA    1 
ATOM   9951  C  C     . ASN D 3 186 ? 144.944 170.688 89.318  1.00 53.72  ? 186  ASN A C     1 
ATOM   9952  O  O     . ASN D 3 186 ? 144.124 170.334 88.461  1.00 63.49  ? 186  ASN A O     1 
ATOM   9953  C  CB    . ASN D 3 186 ? 144.236 172.001 91.328  1.00 50.64  ? 186  ASN A CB    1 
ATOM   9954  C  CG    . ASN D 3 186 ? 143.736 171.966 92.753  1.00 55.80  ? 186  ASN A CG    1 
ATOM   9955  O  OD1   . ASN D 3 186 ? 143.062 171.025 93.162  1.00 64.96  ? 186  ASN A OD1   1 
ATOM   9956  N  ND2   . ASN D 3 186 ? 144.059 172.999 93.519  1.00 56.28  ? 186  ASN A ND2   1 
ATOM   9957  N  N     . SER D 3 187 ? 146.158 171.136 89.001  1.00 50.75  ? 187  SER A N     1 
ATOM   9958  C  CA    . SER D 3 187 ? 146.542 171.291 87.605  1.00 49.12  ? 187  SER A CA    1 
ATOM   9959  C  C     . SER D 3 187 ? 146.553 169.954 86.878  1.00 55.97  ? 187  SER A C     1 
ATOM   9960  O  O     . SER D 3 187 ? 146.001 169.836 85.777  1.00 66.09  ? 187  SER A O     1 
ATOM   9961  C  CB    . SER D 3 187 ? 147.904 171.974 87.516  1.00 54.24  ? 187  SER A CB    1 
ATOM   9962  O  OG    . SER D 3 187 ? 148.846 171.343 88.364  1.00 65.76  ? 187  SER A OG    1 
ATOM   9963  N  N     . ILE D 3 188 ? 147.149 168.927 87.485  1.00 51.46  ? 188  ILE A N     1 
ATOM   9964  C  CA    . ILE D 3 188 ? 147.204 167.631 86.820  1.00 44.15  ? 188  ILE A CA    1 
ATOM   9965  C  C     . ILE D 3 188 ? 145.813 167.024 86.701  1.00 50.02  ? 188  ILE A C     1 
ATOM   9966  O  O     . ILE D 3 188 ? 145.467 166.443 85.666  1.00 57.74  ? 188  ILE A O     1 
ATOM   9967  C  CB    . ILE D 3 188 ? 148.192 166.700 87.542  1.00 43.68  ? 188  ILE A CB    1 
ATOM   9968  C  CG1   . ILE D 3 188 ? 149.604 166.976 87.036  1.00 48.54  ? 188  ILE A CG1   1 
ATOM   9969  C  CG2   . ILE D 3 188 ? 147.838 165.252 87.337  1.00 52.73  ? 188  ILE A CG2   1 
ATOM   9970  C  CD1   . ILE D 3 188 ? 150.667 166.205 87.739  1.00 58.17  ? 188  ILE A CD1   1 
ATOM   9971  N  N     . LEU D 3 189 ? 144.976 167.179 87.727  1.00 46.44  ? 189  LEU A N     1 
ATOM   9972  C  CA    . LEU D 3 189 ? 143.622 166.645 87.636  1.00 46.23  ? 189  LEU A CA    1 
ATOM   9973  C  C     . LEU D 3 189 ? 142.840 167.308 86.504  1.00 51.30  ? 189  LEU A C     1 
ATOM   9974  O  O     . LEU D 3 189 ? 142.182 166.626 85.705  1.00 57.29  ? 189  LEU A O     1 
ATOM   9975  C  CB    . LEU D 3 189 ? 142.908 166.812 88.976  1.00 50.42  ? 189  LEU A CB    1 
ATOM   9976  C  CG    . LEU D 3 189 ? 143.319 165.826 90.072  1.00 48.06  ? 189  LEU A CG    1 
ATOM   9977  C  CD1   . LEU D 3 189 ? 142.683 166.188 91.399  1.00 52.97  ? 189  LEU A CD1   1 
ATOM   9978  C  CD2   . LEU D 3 189 ? 142.938 164.417 89.676  1.00 49.19  ? 189  LEU A CD2   1 
ATOM   9979  N  N     . THR D 3 190 ? 142.930 168.637 86.389  1.00 55.88  ? 190  THR A N     1 
ATOM   9980  C  CA    . THR D 3 190 ? 142.112 169.325 85.393  1.00 53.91  ? 190  THR A CA    1 
ATOM   9981  C  C     . THR D 3 190 ? 142.638 169.092 83.982  1.00 51.74  ? 190  THR A C     1 
ATOM   9982  O  O     . THR D 3 190 ? 141.850 168.986 83.036  1.00 62.10  ? 190  THR A O     1 
ATOM   9983  C  CB    . THR D 3 190 ? 142.026 170.821 85.703  1.00 51.05  ? 190  THR A CB    1 
ATOM   9984  O  OG1   . THR D 3 190 ? 141.165 171.465 84.758  1.00 50.79  ? 190  THR A OG1   1 
ATOM   9985  C  CG2   . THR D 3 190 ? 143.380 171.463 85.620  1.00 50.26  ? 190  THR A CG2   1 
ATOM   9986  N  N     . THR D 3 191 ? 143.959 168.998 83.809  1.00 52.61  ? 191  THR A N     1 
ATOM   9987  C  CA    . THR D 3 191 ? 144.477 168.764 82.466  1.00 62.80  ? 191  THR A CA    1 
ATOM   9988  C  C     . THR D 3 191 ? 144.436 167.284 82.104  1.00 56.40  ? 191  THR A C     1 
ATOM   9989  O  O     . THR D 3 191 ? 144.697 166.915 80.953  1.00 53.52  ? 191  THR A O     1 
ATOM   9990  C  CB    . THR D 3 191 ? 145.887 169.338 82.322  1.00 67.34  ? 191  THR A CB    1 
ATOM   9991  O  OG1   . THR D 3 191 ? 146.248 169.369 80.933  1.00 67.35  ? 191  THR A OG1   1 
ATOM   9992  C  CG2   . THR D 3 191 ? 146.874 168.525 83.108  1.00 57.73  ? 191  THR A CG2   1 
ATOM   9993  N  N     . HIS D 3 192 ? 144.162 166.414 83.075  1.00 63.38  ? 192  HIS A N     1 
ATOM   9994  C  CA    . HIS D 3 192 ? 143.773 165.053 82.736  1.00 70.52  ? 192  HIS A CA    1 
ATOM   9995  C  C     . HIS D 3 192 ? 142.324 164.996 82.280  1.00 64.62  ? 192  HIS A C     1 
ATOM   9996  O  O     . HIS D 3 192 ? 141.997 164.311 81.304  1.00 59.92  ? 192  HIS A O     1 
ATOM   9997  C  CB    . HIS D 3 192 ? 143.987 164.132 83.933  1.00 73.09  ? 192  HIS A CB    1 
ATOM   9998  C  CG    . HIS D 3 192 ? 142.998 163.011 84.011  1.00 74.85  ? 192  HIS A CG    1 
ATOM   9999  N  ND1   . HIS D 3 192 ? 142.917 162.021 83.056  1.00 75.13  ? 192  HIS A ND1   1 
ATOM   10000 C  CD2   . HIS D 3 192 ? 142.046 162.724 84.930  1.00 71.01  ? 192  HIS A CD2   1 
ATOM   10001 C  CE1   . HIS D 3 192 ? 141.958 161.174 83.383  1.00 72.86  ? 192  HIS A CE1   1 
ATOM   10002 N  NE2   . HIS D 3 192 ? 141.415 161.576 84.517  1.00 74.68  ? 192  HIS A NE2   1 
ATOM   10003 N  N     . THR D 3 193 ? 141.439 165.712 82.973  1.00 67.09  ? 193  THR A N     1 
ATOM   10004 C  CA    . THR D 3 193 ? 140.018 165.615 82.657  1.00 69.15  ? 193  THR A CA    1 
ATOM   10005 C  C     . THR D 3 193 ? 139.671 166.346 81.364  1.00 68.12  ? 193  THR A C     1 
ATOM   10006 O  O     . THR D 3 193 ? 138.892 165.838 80.550  1.00 67.63  ? 193  THR A O     1 
ATOM   10007 C  CB    . THR D 3 193 ? 139.185 166.147 83.823  1.00 70.92  ? 193  THR A CB    1 
ATOM   10008 O  OG1   . THR D 3 193 ? 139.674 167.436 84.218  1.00 71.74  ? 193  THR A OG1   1 
ATOM   10009 C  CG2   . THR D 3 193 ? 139.257 165.188 85.004  1.00 66.05  ? 193  THR A CG2   1 
ATOM   10010 N  N     . THR D 3 194 ? 140.241 167.529 81.147  1.00 68.09  ? 194  THR A N     1 
ATOM   10011 C  CA    . THR D 3 194 ? 139.877 168.379 80.022  1.00 62.49  ? 194  THR A CA    1 
ATOM   10012 C  C     . THR D 3 194 ? 140.801 168.211 78.824  1.00 65.06  ? 194  THR A C     1 
ATOM   10013 O  O     . THR D 3 194 ? 140.744 169.020 77.895  1.00 70.33  ? 194  THR A O     1 
ATOM   10014 C  CB    . THR D 3 194 ? 139.861 169.844 80.453  1.00 64.89  ? 194  THR A CB    1 
ATOM   10015 O  OG1   . THR D 3 194 ? 141.199 170.274 80.733  1.00 70.18  ? 194  THR A OG1   1 
ATOM   10016 C  CG2   . THR D 3 194 ? 139.011 170.016 81.694  1.00 63.72  ? 194  THR A CG2   1 
ATOM   10017 N  N     . LEU D 3 195 ? 141.658 167.190 78.828  1.00 67.14  ? 195  LEU A N     1 
ATOM   10018 C  CA    . LEU D 3 195 ? 142.476 166.911 77.652  1.00 60.80  ? 195  LEU A CA    1 
ATOM   10019 C  C     . LEU D 3 195 ? 141.633 166.386 76.499  1.00 61.00  ? 195  LEU A C     1 
ATOM   10020 O  O     . LEU D 3 195 ? 141.980 166.595 75.332  1.00 62.79  ? 195  LEU A O     1 
ATOM   10021 C  CB    . LEU D 3 195 ? 143.576 165.912 78.010  1.00 63.82  ? 195  LEU A CB    1 
ATOM   10022 C  CG    . LEU D 3 195 ? 144.479 165.394 76.893  1.00 61.31  ? 195  LEU A CG    1 
ATOM   10023 C  CD1   . LEU D 3 195 ? 145.137 166.544 76.171  1.00 63.04  ? 195  LEU A CD1   1 
ATOM   10024 C  CD2   . LEU D 3 195 ? 145.525 164.449 77.458  1.00 65.73  ? 195  LEU A CD2   1 
ATOM   10025 N  N     . GLU D 3 196 ? 140.522 165.717 76.802  1.00 65.07  ? 196  GLU A N     1 
ATOM   10026 C  CA    . GLU D 3 196 ? 139.687 165.089 75.789  1.00 63.61  ? 196  GLU A CA    1 
ATOM   10027 C  C     . GLU D 3 196 ? 138.548 165.973 75.300  1.00 61.98  ? 196  GLU A C     1 
ATOM   10028 O  O     . GLU D 3 196 ? 137.789 165.542 74.426  1.00 65.43  ? 196  GLU A O     1 
ATOM   10029 C  CB    . GLU D 3 196 ? 139.099 163.782 76.330  1.00 62.22  ? 196  GLU A CB    1 
ATOM   10030 C  CG    . GLU D 3 196 ? 140.127 162.827 76.901  1.00 66.23  ? 196  GLU A CG    1 
ATOM   10031 C  CD    . GLU D 3 196 ? 140.638 161.837 75.873  1.00 73.45  ? 196  GLU A CD    1 
ATOM   10032 O  OE1   . GLU D 3 196 ? 140.111 161.830 74.741  1.00 71.66  ? 196  GLU A OE1   1 
ATOM   10033 O  OE2   . GLU D 3 196 ? 141.566 161.068 76.197  1.00 71.56  ? 196  GLU A OE2   1 
ATOM   10034 N  N     . HIS D 3 197 ? 138.402 167.184 75.828  1.00 56.55  ? 197  HIS A N     1 
ATOM   10035 C  CA    . HIS D 3 197 ? 137.264 168.037 75.500  1.00 58.67  ? 197  HIS A CA    1 
ATOM   10036 C  C     . HIS D 3 197 ? 137.646 169.341 74.823  1.00 58.99  ? 197  HIS A C     1 
ATOM   10037 O  O     . HIS D 3 197 ? 136.987 169.746 73.865  1.00 64.53  ? 197  HIS A O     1 
ATOM   10038 C  CB    . HIS D 3 197 ? 136.458 168.343 76.765  1.00 59.66  ? 197  HIS A CB    1 
ATOM   10039 C  CG    . HIS D 3 197 ? 135.852 167.131 77.398  1.00 64.16  ? 197  HIS A CG    1 
ATOM   10040 N  ND1   . HIS D 3 197 ? 135.605 165.972 76.696  1.00 66.54  ? 197  HIS A ND1   1 
ATOM   10041 C  CD2   . HIS D 3 197 ? 135.455 166.894 78.669  1.00 66.49  ? 197  HIS A CD2   1 
ATOM   10042 C  CE1   . HIS D 3 197 ? 135.075 165.074 77.507  1.00 65.22  ? 197  HIS A CE1   1 
ATOM   10043 N  NE2   . HIS D 3 197 ? 134.975 165.608 78.710  1.00 67.42  ? 197  HIS A NE2   1 
ATOM   10044 N  N     . SER D 3 198 ? 138.686 170.018 75.298  1.00 60.63  ? 198  SER A N     1 
ATOM   10045 C  CA    . SER D 3 198 ? 139.122 171.253 74.668  1.00 62.72  ? 198  SER A CA    1 
ATOM   10046 C  C     . SER D 3 198 ? 139.758 170.969 73.314  1.00 64.71  ? 198  SER A C     1 
ATOM   10047 O  O     . SER D 3 198 ? 140.327 169.900 73.081  1.00 73.78  ? 198  SER A O     1 
ATOM   10048 C  CB    . SER D 3 198 ? 140.112 171.990 75.566  1.00 68.88  ? 198  SER A CB    1 
ATOM   10049 O  OG    . SER D 3 198 ? 140.560 173.187 74.955  1.00 70.90  ? 198  SER A OG    1 
ATOM   10050 N  N     . ASP D 3 199 ? 139.657 171.943 72.412  1.00 58.99  ? 199  ASP A N     1 
ATOM   10051 C  CA    . ASP D 3 199 ? 140.213 171.809 71.074  1.00 59.62  ? 199  ASP A CA    1 
ATOM   10052 C  C     . ASP D 3 199 ? 141.478 172.618 70.857  1.00 58.43  ? 199  ASP A C     1 
ATOM   10053 O  O     . ASP D 3 199 ? 142.288 172.253 70.004  1.00 70.08  ? 199  ASP A O     1 
ATOM   10054 C  CB    . ASP D 3 199 ? 139.177 172.217 70.023  1.00 64.09  ? 199  ASP A CB    1 
ATOM   10055 C  CG    . ASP D 3 199 ? 138.001 171.266 69.968  1.00 72.72  ? 199  ASP A CG    1 
ATOM   10056 O  OD1   . ASP D 3 199 ? 137.978 170.303 70.761  1.00 72.16  ? 199  ASP A OD1   1 
ATOM   10057 O  OD2   . ASP D 3 199 ? 137.100 171.480 69.130  1.00 73.14  ? 199  ASP A OD2   1 
ATOM   10058 N  N     . CYS D 3 200 ? 141.662 173.706 71.597  1.00 55.98  ? 200  CYS A N     1 
ATOM   10059 C  CA    . CYS D 3 200 ? 142.899 174.477 71.533  1.00 58.92  ? 200  CYS A CA    1 
ATOM   10060 C  C     . CYS D 3 200 ? 142.999 175.263 72.831  1.00 61.47  ? 200  CYS A C     1 
ATOM   10061 O  O     . CYS D 3 200 ? 142.254 176.228 73.026  1.00 72.43  ? 200  CYS A O     1 
ATOM   10062 C  CB    . CYS D 3 200 ? 142.905 175.400 70.321  1.00 61.86  ? 200  CYS A CB    1 
ATOM   10063 S  SG    . CYS D 3 200 ? 144.534 176.004 69.847  1.00 81.34  ? 200  CYS A SG    1 
ATOM   10064 N  N     . ALA D 3 201 ? 143.905 174.851 73.710  1.00 50.39  ? 201  ALA A N     1 
ATOM   10065 C  CA    . ALA D 3 201 ? 144.048 175.446 75.033  1.00 51.98  ? 201  ALA A CA    1 
ATOM   10066 C  C     . ALA D 3 201 ? 145.283 176.334 75.038  1.00 47.89  ? 201  ALA A C     1 
ATOM   10067 O  O     . ALA D 3 201 ? 146.412 175.837 75.116  1.00 56.79  ? 201  ALA A O     1 
ATOM   10068 C  CB    . ALA D 3 201 ? 144.143 174.367 76.107  1.00 53.53  ? 201  ALA A CB    1 
ATOM   10069 N  N     . PHE D 3 202 ? 145.071 177.643 74.957  1.00 52.31  ? 202  PHE A N     1 
ATOM   10070 C  CA    . PHE D 3 202 ? 146.168 178.599 75.018  1.00 56.25  ? 202  PHE A CA    1 
ATOM   10071 C  C     . PHE D 3 202 ? 146.553 178.811 76.474  1.00 62.35  ? 202  PHE A C     1 
ATOM   10072 O  O     . PHE D 3 202 ? 145.697 179.117 77.310  1.00 67.96  ? 202  PHE A O     1 
ATOM   10073 C  CB    . PHE D 3 202 ? 145.766 179.916 74.362  1.00 55.59  ? 202  PHE A CB    1 
ATOM   10074 C  CG    . PHE D 3 202 ? 145.123 179.747 73.022  1.00 54.35  ? 202  PHE A CG    1 
ATOM   10075 C  CD1   . PHE D 3 202 ? 145.892 179.606 71.887  1.00 54.72  ? 202  PHE A CD1   1 
ATOM   10076 C  CD2   . PHE D 3 202 ? 143.747 179.722 72.900  1.00 57.61  ? 202  PHE A CD2   1 
ATOM   10077 C  CE1   . PHE D 3 202 ? 145.303 179.442 70.656  1.00 61.37  ? 202  PHE A CE1   1 
ATOM   10078 C  CE2   . PHE D 3 202 ? 143.153 179.561 71.669  1.00 61.30  ? 202  PHE A CE2   1 
ATOM   10079 C  CZ    . PHE D 3 202 ? 143.932 179.422 70.545  1.00 65.31  ? 202  PHE A CZ    1 
ATOM   10080 N  N     . MET D 3 203 ? 147.834 178.651 76.779  1.00 58.09  ? 203  MET A N     1 
ATOM   10081 C  CA    . MET D 3 203 ? 148.322 178.695 78.146  1.00 54.54  ? 203  MET A CA    1 
ATOM   10082 C  C     . MET D 3 203 ? 149.255 179.880 78.338  1.00 61.03  ? 203  MET A C     1 
ATOM   10083 O  O     . MET D 3 203 ? 150.030 180.224 77.442  1.00 69.04  ? 203  MET A O     1 
ATOM   10084 C  CB    . MET D 3 203 ? 149.048 177.398 78.507  1.00 55.27  ? 203  MET A CB    1 
ATOM   10085 C  CG    . MET D 3 203 ? 148.242 176.150 78.224  1.00 60.78  ? 203  MET A CG    1 
ATOM   10086 S  SD    . MET D 3 203 ? 148.503 174.866 79.456  1.00 84.94  ? 203  MET A SD    1 
ATOM   10087 C  CE    . MET D 3 203 ? 150.290 174.788 79.479  1.00 68.08  ? 203  MET A CE    1 
ATOM   10088 N  N     . VAL D 3 204 ? 149.150 180.516 79.505  1.00 54.33  ? 204  VAL A N     1 
ATOM   10089 C  CA    . VAL D 3 204 ? 150.075 181.554 79.938  1.00 56.15  ? 204  VAL A CA    1 
ATOM   10090 C  C     . VAL D 3 204 ? 150.384 181.321 81.411  1.00 59.24  ? 204  VAL A C     1 
ATOM   10091 O  O     . VAL D 3 204 ? 149.651 180.629 82.119  1.00 65.26  ? 204  VAL A O     1 
ATOM   10092 C  CB    . VAL D 3 204 ? 149.513 182.976 79.719  1.00 55.92  ? 204  VAL A CB    1 
ATOM   10093 C  CG1   . VAL D 3 204 ? 149.454 183.300 78.241  1.00 55.88  ? 204  VAL A CG1   1 
ATOM   10094 C  CG2   . VAL D 3 204 ? 148.140 183.099 80.334  1.00 59.77  ? 204  VAL A CG2   1 
ATOM   10095 N  N     . ASP D 3 205 ? 151.493 181.895 81.870  1.00 70.00  ? 205  ASP A N     1 
ATOM   10096 C  CA    . ASP D 3 205 ? 151.845 181.850 83.281  1.00 72.77  ? 205  ASP A CA    1 
ATOM   10097 C  C     . ASP D 3 205 ? 152.241 183.241 83.749  1.00 70.67  ? 205  ASP A C     1 
ATOM   10098 O  O     . ASP D 3 205 ? 152.763 184.051 82.979  1.00 75.15  ? 205  ASP A O     1 
ATOM   10099 C  CB    . ASP D 3 205 ? 152.975 180.848 83.571  1.00 72.96  ? 205  ASP A CB    1 
ATOM   10100 C  CG    . ASP D 3 205 ? 154.171 181.034 82.671  1.00 78.56  ? 205  ASP A CG    1 
ATOM   10101 O  OD1   . ASP D 3 205 ? 154.158 181.966 81.847  1.00 82.55  ? 205  ASP A OD1   1 
ATOM   10102 O  OD2   . ASP D 3 205 ? 155.130 180.243 82.787  1.00 80.03  ? 205  ASP A OD2   1 
ATOM   10103 N  N     . ASN D 3 206 ? 151.974 183.512 85.027  1.00 58.71  ? 206  ASN A N     1 
ATOM   10104 C  CA    . ASN D 3 206 ? 152.168 184.855 85.556  1.00 58.00  ? 206  ASN A CA    1 
ATOM   10105 C  C     . ASN D 3 206 ? 153.636 185.259 85.576  1.00 66.99  ? 206  ASN A C     1 
ATOM   10106 O  O     . ASN D 3 206 ? 153.944 186.449 85.471  1.00 74.34  ? 206  ASN A O     1 
ATOM   10107 C  CB    . ASN D 3 206 ? 151.576 184.952 86.960  1.00 64.01  ? 206  ASN A CB    1 
ATOM   10108 C  CG    . ASN D 3 206 ? 150.072 184.806 86.968  1.00 63.75  ? 206  ASN A CG    1 
ATOM   10109 O  OD1   . ASN D 3 206 ? 149.380 185.331 86.100  1.00 64.45  ? 206  ASN A OD1   1 
ATOM   10110 N  ND2   . ASN D 3 206 ? 149.555 184.086 87.953  1.00 65.63  ? 206  ASN A ND2   1 
ATOM   10111 N  N     . GLU D 3 207 ? 154.551 184.298 85.718  1.00 74.23  ? 207  GLU A N     1 
ATOM   10112 C  CA    . GLU D 3 207 ? 155.959 184.646 85.880  1.00 73.16  ? 207  GLU A CA    1 
ATOM   10113 C  C     . GLU D 3 207 ? 156.548 185.206 84.591  1.00 77.90  ? 207  GLU A C     1 
ATOM   10114 O  O     . GLU D 3 207 ? 157.311 186.182 84.616  1.00 80.64  ? 207  GLU A O     1 
ATOM   10115 C  CB    . GLU D 3 207 ? 156.745 183.425 86.351  1.00 71.95  ? 207  GLU A CB    1 
ATOM   10116 C  CG    . GLU D 3 207 ? 158.174 183.724 86.751  1.00 77.06  ? 207  GLU A CG    1 
ATOM   10117 C  CD    . GLU D 3 207 ? 158.868 182.523 87.356  1.00 80.77  ? 207  GLU A CD    1 
ATOM   10118 O  OE1   . GLU D 3 207 ? 158.228 181.457 87.465  1.00 81.00  ? 207  GLU A OE1   1 
ATOM   10119 O  OE2   . GLU D 3 207 ? 160.055 182.644 87.725  1.00 80.06  ? 207  GLU A OE2   1 
ATOM   10120 N  N     . ALA D 3 208 ? 156.198 184.609 83.450  1.00 71.79  ? 208  ALA A N     1 
ATOM   10121 C  CA    . ALA D 3 208 ? 156.683 185.125 82.176  1.00 67.78  ? 208  ALA A CA    1 
ATOM   10122 C  C     . ALA D 3 208 ? 156.140 186.520 81.904  1.00 68.65  ? 208  ALA A C     1 
ATOM   10123 O  O     . ALA D 3 208 ? 156.859 187.383 81.390  1.00 75.31  ? 208  ALA A O     1 
ATOM   10124 C  CB    . ALA D 3 208 ? 156.306 184.173 81.042  1.00 66.31  ? 208  ALA A CB    1 
ATOM   10125 N  N     . ILE D 3 209 ? 154.873 186.762 82.236  1.00 62.64  ? 209  ILE A N     1 
ATOM   10126 C  CA    . ILE D 3 209 ? 154.306 188.089 82.032  1.00 62.39  ? 209  ILE A CA    1 
ATOM   10127 C  C     . ILE D 3 209 ? 154.943 189.094 82.983  1.00 65.39  ? 209  ILE A C     1 
ATOM   10128 O  O     . ILE D 3 209 ? 155.142 190.260 82.628  1.00 73.58  ? 209  ILE A O     1 
ATOM   10129 C  CB    . ILE D 3 209 ? 152.776 188.051 82.176  1.00 65.25  ? 209  ILE A CB    1 
ATOM   10130 C  CG1   . ILE D 3 209 ? 152.207 186.864 81.401  1.00 64.56  ? 209  ILE A CG1   1 
ATOM   10131 C  CG2   . ILE D 3 209 ? 152.174 189.334 81.653  1.00 66.09  ? 209  ILE A CG2   1 
ATOM   10132 C  CD1   . ILE D 3 209 ? 150.704 186.775 81.434  1.00 66.23  ? 209  ILE A CD1   1 
ATOM   10133 N  N     . TYR D 3 210 ? 155.275 188.662 84.200  1.00 66.44  ? 210  TYR A N     1 
ATOM   10134 C  CA    . TYR D 3 210 ? 156.014 189.525 85.116  1.00 66.45  ? 210  TYR A CA    1 
ATOM   10135 C  C     . TYR D 3 210 ? 157.353 189.926 84.514  1.00 68.24  ? 210  TYR A C     1 
ATOM   10136 O  O     . TYR D 3 210 ? 157.745 191.098 84.558  1.00 73.54  ? 210  TYR A O     1 
ATOM   10137 C  CB    . TYR D 3 210 ? 156.233 188.815 86.453  1.00 68.60  ? 210  TYR A CB    1 
ATOM   10138 C  CG    . TYR D 3 210 ? 155.015 188.724 87.341  1.00 67.88  ? 210  TYR A CG    1 
ATOM   10139 C  CD1   . TYR D 3 210 ? 154.020 189.683 87.293  1.00 69.06  ? 210  TYR A CD1   1 
ATOM   10140 C  CD2   . TYR D 3 210 ? 154.871 187.676 88.235  1.00 68.25  ? 210  TYR A CD2   1 
ATOM   10141 C  CE1   . TYR D 3 210 ? 152.911 189.597 88.108  1.00 70.66  ? 210  TYR A CE1   1 
ATOM   10142 C  CE2   . TYR D 3 210 ? 153.770 187.581 89.051  1.00 67.51  ? 210  TYR A CE2   1 
ATOM   10143 C  CZ    . TYR D 3 210 ? 152.793 188.542 88.984  1.00 69.55  ? 210  TYR A CZ    1 
ATOM   10144 O  OH    . TYR D 3 210 ? 151.692 188.448 89.801  1.00 70.92  ? 210  TYR A OH    1 
ATOM   10145 N  N     . ASP D 3 211 ? 158.072 188.956 83.946  1.00 73.45  ? 211  ASP A N     1 
ATOM   10146 C  CA    . ASP D 3 211 ? 159.363 189.256 83.335  1.00 77.95  ? 211  ASP A CA    1 
ATOM   10147 C  C     . ASP D 3 211 ? 159.206 190.176 82.129  1.00 79.01  ? 211  ASP A C     1 
ATOM   10148 O  O     . ASP D 3 211 ? 160.024 191.082 81.918  1.00 82.69  ? 211  ASP A O     1 
ATOM   10149 C  CB    . ASP D 3 211 ? 160.067 187.962 82.938  1.00 82.21  ? 211  ASP A CB    1 
ATOM   10150 C  CG    . ASP D 3 211 ? 160.484 187.136 84.137  1.00 83.99  ? 211  ASP A CG    1 
ATOM   10151 O  OD1   . ASP D 3 211 ? 160.152 187.530 85.275  1.00 80.22  ? 211  ASP A OD1   1 
ATOM   10152 O  OD2   . ASP D 3 211 ? 161.147 186.095 83.944  1.00 86.32  ? 211  ASP A OD2   1 
ATOM   10153 N  N     . ILE D 3 212 ? 158.166 189.954 81.324  1.00 71.16  ? 212  ILE A N     1 
ATOM   10154 C  CA    . ILE D 3 212 ? 157.906 190.818 80.176  1.00 66.93  ? 212  ILE A CA    1 
ATOM   10155 C  C     . ILE D 3 212 ? 157.642 192.243 80.636  1.00 69.81  ? 212  ILE A C     1 
ATOM   10156 O  O     . ILE D 3 212 ? 158.162 193.204 80.060  1.00 76.02  ? 212  ILE A O     1 
ATOM   10157 C  CB    . ILE D 3 212 ? 156.732 190.268 79.346  1.00 67.19  ? 212  ILE A CB    1 
ATOM   10158 C  CG1   . ILE D 3 212 ? 157.150 189.003 78.599  1.00 70.53  ? 212  ILE A CG1   1 
ATOM   10159 C  CG2   . ILE D 3 212 ? 156.228 191.314 78.372  1.00 69.78  ? 212  ILE A CG2   1 
ATOM   10160 C  CD1   . ILE D 3 212 ? 156.040 188.388 77.778  1.00 70.28  ? 212  ILE A CD1   1 
ATOM   10161 N  N     . CYS D 3 213 ? 156.832 192.402 81.683  1.00 73.82  ? 213  CYS A N     1 
ATOM   10162 C  CA    . CYS D 3 213 ? 156.553 193.732 82.207  1.00 74.76  ? 213  CYS A CA    1 
ATOM   10163 C  C     . CYS D 3 213 ? 157.817 194.386 82.747  1.00 73.20  ? 213  CYS A C     1 
ATOM   10164 O  O     . CYS D 3 213 ? 158.023 195.593 82.574  1.00 81.02  ? 213  CYS A O     1 
ATOM   10165 C  CB    . CYS D 3 213 ? 155.482 193.652 83.293  1.00 76.07  ? 213  CYS A CB    1 
ATOM   10166 S  SG    . CYS D 3 213 ? 153.844 193.182 82.694  1.00 93.14  ? 213  CYS A SG    1 
ATOM   10167 N  N     . ARG D 3 214 ? 158.674 193.607 83.408  1.00 66.38  ? 214  ARG A N     1 
ATOM   10168 C  CA    . ARG D 3 214 ? 159.883 194.173 83.995  1.00 68.07  ? 214  ARG A CA    1 
ATOM   10169 C  C     . ARG D 3 214 ? 160.858 194.635 82.920  1.00 70.80  ? 214  ARG A C     1 
ATOM   10170 O  O     . ARG D 3 214 ? 161.471 195.702 83.039  1.00 72.57  ? 214  ARG A O     1 
ATOM   10171 C  CB    . ARG D 3 214 ? 160.548 193.153 84.917  1.00 72.10  ? 214  ARG A CB    1 
ATOM   10172 C  CG    . ARG D 3 214 ? 161.861 193.630 85.509  1.00 72.05  ? 214  ARG A CG    1 
ATOM   10173 C  CD    . ARG D 3 214 ? 162.556 192.526 86.279  1.00 72.30  ? 214  ARG A CD    1 
ATOM   10174 N  NE    . ARG D 3 214 ? 162.887 191.393 85.423  1.00 75.72  ? 214  ARG A NE    1 
ATOM   10175 C  CZ    . ARG D 3 214 ? 163.981 191.312 84.679  1.00 77.31  ? 214  ARG A CZ    1 
ATOM   10176 N  NH1   . ARG D 3 214 ? 164.872 192.289 84.652  1.00 73.03  ? 214  ARG A NH1   1 
ATOM   10177 N  NH2   . ARG D 3 214 ? 164.184 190.225 83.940  1.00 76.90  ? 214  ARG A NH2   1 
ATOM   10178 N  N     . ARG D 3 215 ? 161.018 193.844 81.859  1.00 70.34  ? 215  ARG A N     1 
ATOM   10179 C  CA    . ARG D 3 215 ? 162.019 194.181 80.852  1.00 67.04  ? 215  ARG A CA    1 
ATOM   10180 C  C     . ARG D 3 215 ? 161.490 195.175 79.828  1.00 67.84  ? 215  ARG A C     1 
ATOM   10181 O  O     . ARG D 3 215 ? 162.115 196.213 79.587  1.00 73.48  ? 215  ARG A O     1 
ATOM   10182 C  CB    . ARG D 3 215 ? 162.505 192.917 80.150  1.00 66.94  ? 215  ARG A CB    1 
ATOM   10183 C  CG    . ARG D 3 215 ? 163.572 192.162 80.911  1.00 69.55  ? 215  ARG A CG    1 
ATOM   10184 C  CD    . ARG D 3 215 ? 164.147 191.050 80.060  1.00 71.89  ? 215  ARG A CD    1 
ATOM   10185 N  NE    . ARG D 3 215 ? 163.095 190.267 79.425  1.00 72.87  ? 215  ARG A NE    1 
ATOM   10186 C  CZ    . ARG D 3 215 ? 162.446 189.273 80.014  1.00 75.15  ? 215  ARG A CZ    1 
ATOM   10187 N  NH1   . ARG D 3 215 ? 162.722 188.907 81.254  1.00 72.88  ? 215  ARG A NH1   1 
ATOM   10188 N  NH2   . ARG D 3 215 ? 161.496 188.629 79.341  1.00 75.30  ? 215  ARG A NH2   1 
ATOM   10189 N  N     . ASN D 3 216 ? 160.346 194.880 79.219  1.00 61.75  ? 216  ASN A N     1 
ATOM   10190 C  CA    . ASN D 3 216 ? 159.827 195.669 78.112  1.00 62.19  ? 216  ASN A CA    1 
ATOM   10191 C  C     . ASN D 3 216 ? 159.081 196.912 78.584  1.00 67.20  ? 216  ASN A C     1 
ATOM   10192 O  O     . ASN D 3 216 ? 159.371 198.021 78.129  1.00 69.74  ? 216  ASN A O     1 
ATOM   10193 C  CB    . ASN D 3 216 ? 158.913 194.795 77.254  1.00 61.06  ? 216  ASN A CB    1 
ATOM   10194 C  CG    . ASN D 3 216 ? 159.643 193.633 76.627  1.00 60.52  ? 216  ASN A CG    1 
ATOM   10195 O  OD1   . ASN D 3 216 ? 160.773 193.325 76.999  1.00 65.72  ? 216  ASN A OD1   1 
ATOM   10196 N  ND2   . ASN D 3 216 ? 159.002 192.976 75.673  1.00 61.75  ? 216  ASN A ND2   1 
ATOM   10197 N  N     . LEU D 3 217 ? 158.121 196.746 79.489  1.00 70.19  ? 217  LEU A N     1 
ATOM   10198 C  CA    . LEU D 3 217 ? 157.315 197.852 79.986  1.00 70.27  ? 217  LEU A CA    1 
ATOM   10199 C  C     . LEU D 3 217 ? 158.010 198.656 81.076  1.00 72.79  ? 217  LEU A C     1 
ATOM   10200 O  O     . LEU D 3 217 ? 157.516 199.727 81.440  1.00 75.03  ? 217  LEU A O     1 
ATOM   10201 C  CB    . LEU D 3 217 ? 155.976 197.329 80.507  1.00 71.22  ? 217  LEU A CB    1 
ATOM   10202 C  CG    . LEU D 3 217 ? 155.092 196.642 79.468  1.00 72.90  ? 217  LEU A CG    1 
ATOM   10203 C  CD1   . LEU D 3 217 ? 154.005 195.831 80.144  1.00 72.27  ? 217  LEU A CD1   1 
ATOM   10204 C  CD2   . LEU D 3 217 ? 154.490 197.670 78.526  1.00 74.08  ? 217  LEU A CD2   1 
ATOM   10205 N  N     . ASP D 3 218 ? 159.136 198.167 81.596  1.00 73.72  ? 218  ASP A N     1 
ATOM   10206 C  CA    . ASP D 3 218 ? 159.928 198.881 82.599  1.00 71.85  ? 218  ASP A CA    1 
ATOM   10207 C  C     . ASP D 3 218 ? 159.094 199.260 83.821  1.00 73.98  ? 218  ASP A C     1 
ATOM   10208 O  O     . ASP D 3 218 ? 159.181 200.378 84.331  1.00 76.59  ? 218  ASP A O     1 
ATOM   10209 C  CB    . ASP D 3 218 ? 160.596 200.118 81.997  1.00 75.98  ? 218  ASP A CB    1 
ATOM   10210 C  CG    . ASP D 3 218 ? 161.729 199.768 81.056  1.00 82.11  ? 218  ASP A CG    1 
ATOM   10211 O  OD1   . ASP D 3 218 ? 162.345 198.698 81.240  1.00 82.02  ? 218  ASP A OD1   1 
ATOM   10212 O  OD2   . ASP D 3 218 ? 162.006 200.564 80.135  1.00 82.05  ? 218  ASP A OD2   1 
ATOM   10213 N  N     . ILE D 3 219 ? 158.276 198.324 84.294  1.00 73.52  ? 219  ILE A N     1 
ATOM   10214 C  CA    . ILE D 3 219 ? 157.540 198.478 85.543  1.00 70.44  ? 219  ILE A CA    1 
ATOM   10215 C  C     . ILE D 3 219 ? 158.054 197.429 86.518  1.00 72.95  ? 219  ILE A C     1 
ATOM   10216 O  O     . ILE D 3 219 ? 158.022 196.227 86.227  1.00 74.37  ? 219  ILE A O     1 
ATOM   10217 C  CB    . ILE D 3 219 ? 156.021 198.366 85.333  1.00 68.99  ? 219  ILE A CB    1 
ATOM   10218 C  CG1   . ILE D 3 219 ? 155.664 197.136 84.500  1.00 71.21  ? 219  ILE A CG1   1 
ATOM   10219 C  CG2   . ILE D 3 219 ? 155.482 199.624 84.673  1.00 71.07  ? 219  ILE A CG2   1 
ATOM   10220 C  CD1   . ILE D 3 219 ? 154.193 196.794 84.536  1.00 72.91  ? 219  ILE A CD1   1 
ATOM   10221 N  N     . GLU D 3 220 ? 158.552 197.884 87.667  1.00 81.20  ? 220  GLU A N     1 
ATOM   10222 C  CA    . GLU D 3 220 ? 159.146 196.981 88.643  1.00 81.59  ? 220  GLU A CA    1 
ATOM   10223 C  C     . GLU D 3 220 ? 158.126 196.364 89.588  1.00 81.29  ? 220  GLU A C     1 
ATOM   10224 O  O     . GLU D 3 220 ? 158.475 195.437 90.325  1.00 77.55  ? 220  GLU A O     1 
ATOM   10225 C  CB    . GLU D 3 220 ? 160.216 197.715 89.455  1.00 79.89  ? 220  GLU A CB    1 
ATOM   10226 C  CG    . GLU D 3 220 ? 161.403 198.193 88.633  1.00 83.02  ? 220  GLU A CG    1 
ATOM   10227 C  CD    . GLU D 3 220 ? 162.332 197.064 88.229  1.00 85.22  ? 220  GLU A CD    1 
ATOM   10228 O  OE1   . GLU D 3 220 ? 162.245 195.973 88.830  1.00 85.82  ? 220  GLU A OE1   1 
ATOM   10229 O  OE2   . GLU D 3 220 ? 163.152 197.268 87.310  1.00 84.04  ? 220  GLU A OE2   1 
ATOM   10230 N  N     . ARG D 3 221 ? 156.885 196.845 89.588  1.00 80.20  ? 221  ARG A N     1 
ATOM   10231 C  CA    . ARG D 3 221 ? 155.831 196.326 90.461  1.00 76.34  ? 221  ARG A CA    1 
ATOM   10232 C  C     . ARG D 3 221 ? 154.591 196.010 89.636  1.00 72.05  ? 221  ARG A C     1 
ATOM   10233 O  O     . ARG D 3 221 ? 153.552 196.664 89.785  1.00 75.87  ? 221  ARG A O     1 
ATOM   10234 C  CB    . ARG D 3 221 ? 155.487 197.329 91.562  1.00 75.85  ? 221  ARG A CB    1 
ATOM   10235 C  CG    . ARG D 3 221 ? 156.604 198.280 91.938  1.00 78.81  ? 221  ARG A CG    1 
ATOM   10236 C  CD    . ARG D 3 221 ? 157.639 197.612 92.818  1.00 79.21  ? 221  ARG A CD    1 
ATOM   10237 N  NE    . ARG D 3 221 ? 158.670 198.554 93.234  1.00 80.45  ? 221  ARG A NE    1 
ATOM   10238 C  CZ    . ARG D 3 221 ? 158.529 199.425 94.223  1.00 78.90  ? 221  ARG A CZ    1 
ATOM   10239 N  NH1   . ARG D 3 221 ? 157.404 199.510 94.914  1.00 75.08  ? 221  ARG A NH1   1 
ATOM   10240 N  NH2   . ARG D 3 221 ? 159.541 200.234 94.525  1.00 78.30  ? 221  ARG A NH2   1 
ATOM   10241 N  N     . PRO D 3 222 ? 154.659 195.016 88.754  1.00 64.15  ? 222  PRO A N     1 
ATOM   10242 C  CA    . PRO D 3 222 ? 153.459 194.632 88.008  1.00 64.21  ? 222  PRO A CA    1 
ATOM   10243 C  C     . PRO D 3 222 ? 152.460 193.925 88.906  1.00 69.42  ? 222  PRO A C     1 
ATOM   10244 O  O     . PRO D 3 222 ? 152.824 193.207 89.840  1.00 73.63  ? 222  PRO A O     1 
ATOM   10245 C  CB    . PRO D 3 222 ? 153.997 193.695 86.924  1.00 73.58  ? 222  PRO A CB    1 
ATOM   10246 C  CG    . PRO D 3 222 ? 155.244 193.153 87.485  1.00 76.21  ? 222  PRO A CG    1 
ATOM   10247 C  CD    . PRO D 3 222 ? 155.829 194.216 88.359  1.00 73.02  ? 222  PRO A CD    1 
ATOM   10248 N  N     . THR D 3 223 ? 151.180 194.135 88.611  1.00 73.71  ? 223  THR A N     1 
ATOM   10249 C  CA    . THR D 3 223 ? 150.097 193.566 89.396  1.00 74.03  ? 223  THR A CA    1 
ATOM   10250 C  C     . THR D 3 223 ? 149.184 192.779 88.468  1.00 72.12  ? 223  THR A C     1 
ATOM   10251 O  O     . THR D 3 223 ? 149.490 192.568 87.290  1.00 77.52  ? 223  THR A O     1 
ATOM   10252 C  CB    . THR D 3 223 ? 149.317 194.652 90.145  1.00 72.60  ? 223  THR A CB    1 
ATOM   10253 O  OG1   . THR D 3 223 ? 148.127 194.087 90.704  1.00 77.71  ? 223  THR A OG1   1 
ATOM   10254 C  CG2   . THR D 3 223 ? 148.938 195.782 89.205  1.00 71.62  ? 223  THR A CG2   1 
ATOM   10255 N  N     . TYR D 3 224 ? 148.046 192.341 89.008  1.00 63.42  ? 224  TYR A N     1 
ATOM   10256 C  CA    . TYR D 3 224 ? 147.127 191.522 88.229  1.00 61.73  ? 224  TYR A CA    1 
ATOM   10257 C  C     . TYR D 3 224 ? 146.473 192.311 87.103  1.00 68.70  ? 224  TYR A C     1 
ATOM   10258 O  O     . TYR D 3 224 ? 146.189 191.748 86.040  1.00 72.90  ? 224  TYR A O     1 
ATOM   10259 C  CB    . TYR D 3 224 ? 146.063 190.917 89.141  1.00 62.53  ? 224  TYR A CB    1 
ATOM   10260 C  CG    . TYR D 3 224 ? 146.520 189.678 89.868  1.00 63.67  ? 224  TYR A CG    1 
ATOM   10261 C  CD1   . TYR D 3 224 ? 147.729 189.080 89.559  1.00 64.86  ? 224  TYR A CD1   1 
ATOM   10262 C  CD2   . TYR D 3 224 ? 145.738 189.100 90.854  1.00 71.63  ? 224  TYR A CD2   1 
ATOM   10263 C  CE1   . TYR D 3 224 ? 148.151 187.945 90.215  1.00 66.80  ? 224  TYR A CE1   1 
ATOM   10264 C  CE2   . TYR D 3 224 ? 146.152 187.965 91.516  1.00 74.02  ? 224  TYR A CE2   1 
ATOM   10265 C  CZ    . TYR D 3 224 ? 147.360 187.391 91.192  1.00 69.44  ? 224  TYR A CZ    1 
ATOM   10266 O  OH    . TYR D 3 224 ? 147.779 186.258 91.848  1.00 67.42  ? 224  TYR A OH    1 
ATOM   10267 N  N     . THR D 3 225 ? 146.227 193.606 87.312  1.00 66.00  ? 225  THR A N     1 
ATOM   10268 C  CA    . THR D 3 225 ? 145.553 194.409 86.296  1.00 63.49  ? 225  THR A CA    1 
ATOM   10269 C  C     . THR D 3 225 ? 146.356 194.449 85.001  1.00 68.56  ? 225  THR A C     1 
ATOM   10270 O  O     . THR D 3 225 ? 145.803 194.296 83.905  1.00 75.37  ? 225  THR A O     1 
ATOM   10271 C  CB    . THR D 3 225 ? 145.315 195.824 86.823  1.00 65.69  ? 225  THR A CB    1 
ATOM   10272 O  OG1   . THR D 3 225 ? 144.468 195.770 87.977  1.00 67.30  ? 225  THR A OG1   1 
ATOM   10273 C  CG2   . THR D 3 225 ? 144.654 196.685 85.761  1.00 68.00  ? 225  THR A CG2   1 
ATOM   10274 N  N     . ASN D 3 226 ? 147.671 194.647 85.110  1.00 66.25  ? 226  ASN A N     1 
ATOM   10275 C  CA    . ASN D 3 226 ? 148.513 194.713 83.920  1.00 67.36  ? 226  ASN A CA    1 
ATOM   10276 C  C     . ASN D 3 226 ? 148.537 193.381 83.179  1.00 69.54  ? 226  ASN A C     1 
ATOM   10277 O  O     . ASN D 3 226 ? 148.469 193.344 81.941  1.00 76.47  ? 226  ASN A O     1 
ATOM   10278 C  CB    . ASN D 3 226 ? 149.924 195.136 84.318  1.00 68.48  ? 226  ASN A CB    1 
ATOM   10279 C  CG    . ASN D 3 226 ? 149.934 196.380 85.183  1.00 75.39  ? 226  ASN A CG    1 
ATOM   10280 O  OD1   . ASN D 3 226 ? 150.444 196.367 86.302  1.00 77.16  ? 226  ASN A OD1   1 
ATOM   10281 N  ND2   . ASN D 3 226 ? 149.367 197.464 84.668  1.00 72.63  ? 226  ASN A ND2   1 
ATOM   10282 N  N     . LEU D 3 227 ? 148.642 192.278 83.920  1.00 62.09  ? 227  LEU A N     1 
ATOM   10283 C  CA    . LEU D 3 227 ? 148.645 190.959 83.301  1.00 63.66  ? 227  LEU A CA    1 
ATOM   10284 C  C     . LEU D 3 227 ? 147.331 190.698 82.579  1.00 68.19  ? 227  LEU A C     1 
ATOM   10285 O  O     . LEU D 3 227 ? 147.313 190.161 81.462  1.00 75.03  ? 227  LEU A O     1 
ATOM   10286 C  CB    . LEU D 3 227 ? 148.893 189.892 84.367  1.00 63.60  ? 227  LEU A CB    1 
ATOM   10287 C  CG    . LEU D 3 227 ? 150.332 189.506 84.706  1.00 63.72  ? 227  LEU A CG    1 
ATOM   10288 C  CD1   . LEU D 3 227 ? 151.151 190.715 85.116  1.00 65.44  ? 227  LEU A CD1   1 
ATOM   10289 C  CD2   . LEU D 3 227 ? 150.344 188.464 85.806  1.00 66.56  ? 227  LEU A CD2   1 
ATOM   10290 N  N     . ASN D 3 228 ? 146.219 191.082 83.205  1.00 58.40  ? 228  ASN A N     1 
ATOM   10291 C  CA    . ASN D 3 228 ? 144.918 190.925 82.573  1.00 55.45  ? 228  ASN A CA    1 
ATOM   10292 C  C     . ASN D 3 228 ? 144.810 191.772 81.312  1.00 61.56  ? 228  ASN A C     1 
ATOM   10293 O  O     . ASN D 3 228 ? 144.221 191.335 80.320  1.00 71.33  ? 228  ASN A O     1 
ATOM   10294 C  CB    . ASN D 3 228 ? 143.812 191.277 83.565  1.00 60.13  ? 228  ASN A CB    1 
ATOM   10295 C  CG    . ASN D 3 228 ? 143.868 190.431 84.818  1.00 63.30  ? 228  ASN A CG    1 
ATOM   10296 O  OD1   . ASN D 3 228 ? 144.268 189.271 84.779  1.00 64.83  ? 228  ASN A OD1   1 
ATOM   10297 N  ND2   . ASN D 3 228 ? 143.468 191.011 85.941  1.00 63.13  ? 228  ASN A ND2   1 
ATOM   10298 N  N     . ARG D 3 229 ? 145.369 192.984 81.328  1.00 55.36  ? 229  ARG A N     1 
ATOM   10299 C  CA    . ARG D 3 229 ? 145.360 193.810 80.122  1.00 57.74  ? 229  ARG A CA    1 
ATOM   10300 C  C     . ARG D 3 229 ? 146.149 193.160 78.992  1.00 58.00  ? 229  ARG A C     1 
ATOM   10301 O  O     . ARG D 3 229 ? 145.715 193.172 77.834  1.00 65.28  ? 229  ARG A O     1 
ATOM   10302 C  CB    . ARG D 3 229 ? 145.918 195.199 80.417  1.00 56.47  ? 229  ARG A CB    1 
ATOM   10303 C  CG    . ARG D 3 229 ? 145.029 196.055 81.282  1.00 57.04  ? 229  ARG A CG    1 
ATOM   10304 C  CD    . ARG D 3 229 ? 145.523 197.482 81.304  1.00 59.37  ? 229  ARG A CD    1 
ATOM   10305 N  NE    . ARG D 3 229 ? 145.082 198.190 82.497  1.00 61.73  ? 229  ARG A NE    1 
ATOM   10306 C  CZ    . ARG D 3 229 ? 143.898 198.771 82.624  1.00 62.94  ? 229  ARG A CZ    1 
ATOM   10307 N  NH1   . ARG D 3 229 ? 143.002 198.732 81.653  1.00 64.01  ? 229  ARG A NH1   1 
ATOM   10308 N  NH2   . ARG D 3 229 ? 143.605 199.404 83.756  1.00 61.51  ? 229  ARG A NH2   1 
ATOM   10309 N  N     . LEU D 3 230 ? 147.318 192.599 79.305  1.00 52.96  ? 230  LEU A N     1 
ATOM   10310 C  CA    . LEU D 3 230 ? 148.105 191.933 78.267  1.00 53.47  ? 230  LEU A CA    1 
ATOM   10311 C  C     . LEU D 3 230 ? 147.361 190.733 77.689  1.00 56.20  ? 230  LEU A C     1 
ATOM   10312 O  O     . LEU D 3 230 ? 147.327 190.536 76.464  1.00 65.23  ? 230  LEU A O     1 
ATOM   10313 C  CB    . LEU D 3 230 ? 149.458 191.504 78.829  1.00 59.44  ? 230  LEU A CB    1 
ATOM   10314 C  CG    . LEU D 3 230 ? 150.625 192.444 78.540  1.00 60.21  ? 230  LEU A CG    1 
ATOM   10315 C  CD1   . LEU D 3 230 ? 151.920 191.843 79.041  1.00 62.37  ? 230  LEU A CD1   1 
ATOM   10316 C  CD2   . LEU D 3 230 ? 150.711 192.734 77.053  1.00 61.85  ? 230  LEU A CD2   1 
ATOM   10317 N  N     . ILE D 3 231 ? 146.748 189.924 78.554  1.00 44.14  ? 231  ILE A N     1 
ATOM   10318 C  CA    . ILE D 3 231 ? 145.999 188.768 78.071  1.00 45.37  ? 231  ILE A CA    1 
ATOM   10319 C  C     . ILE D 3 231 ? 144.795 189.218 77.254  1.00 50.84  ? 231  ILE A C     1 
ATOM   10320 O  O     . ILE D 3 231 ? 144.417 188.576 76.264  1.00 57.40  ? 231  ILE A O     1 
ATOM   10321 C  CB    . ILE D 3 231 ? 145.593 187.870 79.252  1.00 50.00  ? 231  ILE A CB    1 
ATOM   10322 C  CG1   . ILE D 3 231 ? 146.844 187.346 79.956  1.00 55.05  ? 231  ILE A CG1   1 
ATOM   10323 C  CG2   . ILE D 3 231 ? 144.731 186.717 78.779  1.00 55.25  ? 231  ILE A CG2   1 
ATOM   10324 C  CD1   . ILE D 3 231 ? 146.560 186.464 81.140  1.00 55.58  ? 231  ILE A CD1   1 
ATOM   10325 N  N     . SER D 3 232 ? 144.178 190.334 77.647  1.00 51.02  ? 232  SER A N     1 
ATOM   10326 C  CA    . SER D 3 232 ? 143.063 190.874 76.883  1.00 52.77  ? 232  SER A CA    1 
ATOM   10327 C  C     . SER D 3 232 ? 143.511 191.314 75.500  1.00 49.62  ? 232  SER A C     1 
ATOM   10328 O  O     . SER D 3 232 ? 142.790 191.125 74.517  1.00 58.11  ? 232  SER A O     1 
ATOM   10329 C  CB    . SER D 3 232 ? 142.426 192.042 77.636  1.00 56.53  ? 232  SER A CB    1 
ATOM   10330 O  OG    . SER D 3 232 ? 143.301 193.154 77.685  1.00 59.75  ? 232  SER A OG    1 
ATOM   10331 N  N     . GLN D 3 233 ? 144.694 191.919 75.405  1.00 49.46  ? 233  GLN A N     1 
ATOM   10332 C  CA    . GLN D 3 233 ? 145.219 192.278 74.093  1.00 51.40  ? 233  GLN A CA    1 
ATOM   10333 C  C     . GLN D 3 233 ? 145.458 191.040 73.242  1.00 53.30  ? 233  GLN A C     1 
ATOM   10334 O  O     . GLN D 3 233 ? 145.161 191.036 72.041  1.00 57.98  ? 233  GLN A O     1 
ATOM   10335 C  CB    . GLN D 3 233 ? 146.505 193.088 74.237  1.00 50.29  ? 233  GLN A CB    1 
ATOM   10336 C  CG    . GLN D 3 233 ? 146.305 194.471 74.822  1.00 55.06  ? 233  GLN A CG    1 
ATOM   10337 C  CD    . GLN D 3 233 ? 145.634 195.419 73.855  1.00 53.24  ? 233  GLN A CD    1 
ATOM   10338 O  OE1   . GLN D 3 233 ? 145.496 195.121 72.671  1.00 56.82  ? 233  GLN A OE1   1 
ATOM   10339 N  NE2   . GLN D 3 233 ? 145.214 196.571 74.354  1.00 55.87  ? 233  GLN A NE2   1 
ATOM   10340 N  N     . ILE D 3 234 ? 145.989 189.976 73.847  1.00 55.33  ? 234  ILE A N     1 
ATOM   10341 C  CA    . ILE D 3 234 ? 146.218 188.742 73.094  1.00 51.80  ? 234  ILE A CA    1 
ATOM   10342 C  C     . ILE D 3 234 ? 144.901 188.187 72.560  1.00 50.31  ? 234  ILE A C     1 
ATOM   10343 O  O     . ILE D 3 234 ? 144.793 187.808 71.386  1.00 49.72  ? 234  ILE A O     1 
ATOM   10344 C  CB    . ILE D 3 234 ? 146.952 187.706 73.964  1.00 50.10  ? 234  ILE A CB    1 
ATOM   10345 C  CG1   . ILE D 3 234 ? 148.431 188.058 74.081  1.00 50.58  ? 234  ILE A CG1   1 
ATOM   10346 C  CG2   . ILE D 3 234 ? 146.791 186.315 73.387  1.00 48.93  ? 234  ILE A CG2   1 
ATOM   10347 C  CD1   . ILE D 3 234 ? 149.268 186.950 74.666  1.00 54.89  ? 234  ILE A CD1   1 
ATOM   10348 N  N     . VAL D 3 235 ? 143.872 188.143 73.408  1.00 54.07  ? 235  VAL A N     1 
ATOM   10349 C  CA    . VAL D 3 235 ? 142.603 187.563 72.971  1.00 53.70  ? 235  VAL A CA    1 
ATOM   10350 C  C     . VAL D 3 235 ? 141.904 188.470 71.960  1.00 54.35  ? 235  VAL A C     1 
ATOM   10351 O  O     . VAL D 3 235 ? 141.223 187.984 71.046  1.00 60.92  ? 235  VAL A O     1 
ATOM   10352 C  CB    . VAL D 3 235 ? 141.706 187.239 74.181  1.00 51.61  ? 235  VAL A CB    1 
ATOM   10353 C  CG1   . VAL D 3 235 ? 141.166 188.496 74.816  1.00 50.83  ? 235  VAL A CG1   1 
ATOM   10354 C  CG2   . VAL D 3 235 ? 140.570 186.322 73.762  1.00 52.42  ? 235  VAL A CG2   1 
ATOM   10355 N  N     . SER D 3 236 ? 142.063 189.789 72.090  1.00 52.48  ? 236  SER A N     1 
ATOM   10356 C  CA    . SER D 3 236 ? 141.532 190.700 71.084  1.00 53.11  ? 236  SER A CA    1 
ATOM   10357 C  C     . SER D 3 236 ? 142.213 190.485 69.742  1.00 54.84  ? 236  SER A C     1 
ATOM   10358 O  O     . SER D 3 236 ? 141.559 190.511 68.697  1.00 60.29  ? 236  SER A O     1 
ATOM   10359 C  CB    . SER D 3 236 ? 141.698 192.147 71.539  1.00 58.52  ? 236  SER A CB    1 
ATOM   10360 O  OG    . SER D 3 236 ? 141.213 193.044 70.557  1.00 65.93  ? 236  SER A OG    1 
ATOM   10361 N  N     . SER D 3 237 ? 143.529 190.275 69.751  1.00 51.63  ? 237  SER A N     1 
ATOM   10362 C  CA    . SER D 3 237 ? 144.228 189.957 68.512  1.00 49.27  ? 237  SER A CA    1 
ATOM   10363 C  C     . SER D 3 237 ? 143.731 188.643 67.927  1.00 53.62  ? 237  SER A C     1 
ATOM   10364 O  O     . SER D 3 237 ? 143.614 188.503 66.704  1.00 59.35  ? 237  SER A O     1 
ATOM   10365 C  CB    . SER D 3 237 ? 145.734 189.901 68.762  1.00 55.64  ? 237  SER A CB    1 
ATOM   10366 O  OG    . SER D 3 237 ? 146.050 188.913 69.726  1.00 62.60  ? 237  SER A OG    1 
ATOM   10367 N  N     . ILE D 3 238 ? 143.443 187.666 68.785  1.00 51.04  ? 238  ILE A N     1 
ATOM   10368 C  CA    . ILE D 3 238 ? 142.956 186.376 68.306  1.00 43.19  ? 238  ILE A CA    1 
ATOM   10369 C  C     . ILE D 3 238 ? 141.597 186.524 67.634  1.00 46.90  ? 238  ILE A C     1 
ATOM   10370 O  O     . ILE D 3 238 ? 141.356 185.959 66.562  1.00 55.03  ? 238  ILE A O     1 
ATOM   10371 C  CB    . ILE D 3 238 ? 142.910 185.363 69.464  1.00 47.15  ? 238  ILE A CB    1 
ATOM   10372 C  CG1   . ILE D 3 238 ? 144.302 184.792 69.728  1.00 57.94  ? 238  ILE A CG1   1 
ATOM   10373 C  CG2   . ILE D 3 238 ? 141.929 184.245 69.168  1.00 50.63  ? 238  ILE A CG2   1 
ATOM   10374 C  CD1   . ILE D 3 238 ? 144.323 183.710 70.777  1.00 61.10  ? 238  ILE A CD1   1 
ATOM   10375 N  N     . THR D 3 239 ? 140.693 187.291 68.239  1.00 49.79  ? 239  THR A N     1 
ATOM   10376 C  CA    . THR D 3 239 ? 139.320 187.385 67.759  1.00 49.41  ? 239  THR A CA    1 
ATOM   10377 C  C     . THR D 3 239 ? 139.075 188.576 66.834  1.00 49.06  ? 239  THR A C     1 
ATOM   10378 O  O     . THR D 3 239 ? 137.938 188.781 66.402  1.00 51.46  ? 239  THR A O     1 
ATOM   10379 C  CB    . THR D 3 239 ? 138.353 187.445 68.942  1.00 55.23  ? 239  THR A CB    1 
ATOM   10380 O  OG1   . THR D 3 239 ? 138.693 188.553 69.784  1.00 57.27  ? 239  THR A OG1   1 
ATOM   10381 C  CG2   . THR D 3 239 ? 138.421 186.161 69.750  1.00 52.55  ? 239  THR A CG2   1 
ATOM   10382 N  N     . ALA D 3 240 ? 140.106 189.362 66.520  1.00 53.34  ? 240  ALA A N     1 
ATOM   10383 C  CA    . ALA D 3 240 ? 139.914 190.541 65.683  1.00 49.59  ? 240  ALA A CA    1 
ATOM   10384 C  C     . ALA D 3 240 ? 139.553 190.202 64.247  1.00 56.34  ? 240  ALA A C     1 
ATOM   10385 O  O     . ALA D 3 240 ? 138.971 191.044 63.557  1.00 63.27  ? 240  ALA A O     1 
ATOM   10386 C  CB    . ALA D 3 240 ? 141.173 191.405 65.702  1.00 52.31  ? 240  ALA A CB    1 
ATOM   10387 N  N     . SER D 3 241 ? 139.888 189.002 63.776  1.00 60.22  ? 241  SER A N     1 
ATOM   10388 C  CA    . SER D 3 241 ? 139.570 188.643 62.399  1.00 53.27  ? 241  SER A CA    1 
ATOM   10389 C  C     . SER D 3 241 ? 138.066 188.550 62.188  1.00 57.03  ? 241  SER A C     1 
ATOM   10390 O  O     . SER D 3 241 ? 137.562 188.876 61.107  1.00 55.03  ? 241  SER A O     1 
ATOM   10391 C  CB    . SER D 3 241 ? 140.251 187.329 62.033  1.00 56.31  ? 241  SER A CB    1 
ATOM   10392 O  OG    . SER D 3 241 ? 139.771 186.839 60.797  1.00 66.92  ? 241  SER A OG    1 
ATOM   10393 N  N     . LEU D 3 242 ? 137.333 188.103 63.207  1.00 63.53  ? 242  LEU A N     1 
ATOM   10394 C  CA    . LEU D 3 242 ? 135.879 188.042 63.110  1.00 65.00  ? 242  LEU A CA    1 
ATOM   10395 C  C     . LEU D 3 242 ? 135.267 189.437 63.097  1.00 64.50  ? 242  LEU A C     1 
ATOM   10396 O  O     . LEU D 3 242 ? 134.378 189.731 62.290  1.00 65.87  ? 242  LEU A O     1 
ATOM   10397 C  CB    . LEU D 3 242 ? 135.315 187.230 64.274  1.00 57.91  ? 242  LEU A CB    1 
ATOM   10398 C  CG    . LEU D 3 242 ? 135.558 185.725 64.284  1.00 58.84  ? 242  LEU A CG    1 
ATOM   10399 C  CD1   . LEU D 3 242 ? 135.002 185.122 65.553  1.00 54.67  ? 242  LEU A CD1   1 
ATOM   10400 C  CD2   . LEU D 3 242 ? 134.932 185.078 63.065  1.00 61.37  ? 242  LEU A CD2   1 
ATOM   10401 N  N     . ARG D 3 243 ? 135.730 190.308 63.992  1.00 58.70  ? 243  ARG A N     1 
ATOM   10402 C  CA    . ARG D 3 243 ? 135.061 191.585 64.207  1.00 55.33  ? 243  ARG A CA    1 
ATOM   10403 C  C     . ARG D 3 243 ? 135.297 192.555 63.056  1.00 58.15  ? 243  ARG A C     1 
ATOM   10404 O  O     . ARG D 3 243 ? 134.350 193.176 62.561  1.00 66.41  ? 243  ARG A O     1 
ATOM   10405 C  CB    . ARG D 3 243 ? 135.530 192.187 65.529  1.00 58.29  ? 243  ARG A CB    1 
ATOM   10406 C  CG    . ARG D 3 243 ? 135.111 191.379 66.740  1.00 56.57  ? 243  ARG A CG    1 
ATOM   10407 C  CD    . ARG D 3 243 ? 135.722 191.926 68.011  1.00 57.35  ? 243  ARG A CD    1 
ATOM   10408 N  NE    . ARG D 3 243 ? 137.161 191.707 68.059  1.00 58.48  ? 243  ARG A NE    1 
ATOM   10409 C  CZ    . ARG D 3 243 ? 137.982 192.332 68.889  1.00 62.27  ? 243  ARG A CZ    1 
ATOM   10410 N  NH1   . ARG D 3 243 ? 137.541 193.235 69.748  1.00 60.23  ? 243  ARG A NH1   1 
ATOM   10411 N  NH2   . ARG D 3 243 ? 139.281 192.048 68.853  1.00 62.24  ? 243  ARG A NH2   1 
ATOM   10412 N  N     . PHE D 3 244 ? 136.539 192.696 62.607  1.00 50.39  ? 244  PHE A N     1 
ATOM   10413 C  CA    . PHE D 3 244 ? 136.891 193.700 61.617  1.00 51.51  ? 244  PHE A CA    1 
ATOM   10414 C  C     . PHE D 3 244 ? 137.369 193.038 60.333  1.00 61.23  ? 244  PHE A C     1 
ATOM   10415 O  O     . PHE D 3 244 ? 137.596 191.827 60.277  1.00 65.20  ? 244  PHE A O     1 
ATOM   10416 C  CB    . PHE D 3 244 ? 137.973 194.647 62.142  1.00 53.10  ? 244  PHE A CB    1 
ATOM   10417 C  CG    . PHE D 3 244 ? 137.710 195.162 63.523  1.00 57.20  ? 244  PHE A CG    1 
ATOM   10418 C  CD1   . PHE D 3 244 ? 136.774 196.155 63.741  1.00 58.55  ? 244  PHE A CD1   1 
ATOM   10419 C  CD2   . PHE D 3 244 ? 138.419 194.671 64.602  1.00 59.61  ? 244  PHE A CD2   1 
ATOM   10420 C  CE1   . PHE D 3 244 ? 136.540 196.633 65.010  1.00 60.81  ? 244  PHE A CE1   1 
ATOM   10421 C  CE2   . PHE D 3 244 ? 138.189 195.146 65.871  1.00 58.81  ? 244  PHE A CE2   1 
ATOM   10422 C  CZ    . PHE D 3 244 ? 137.249 196.127 66.076  1.00 61.48  ? 244  PHE A CZ    1 
ATOM   10423 N  N     . ASP D 3 245 ? 137.526 193.856 59.297  1.00 63.50  ? 245  ASP A N     1 
ATOM   10424 C  CA    . ASP D 3 245 ? 137.890 193.357 57.983  1.00 63.03  ? 245  ASP A CA    1 
ATOM   10425 C  C     . ASP D 3 245 ? 139.397 193.458 57.761  1.00 61.71  ? 245  ASP A C     1 
ATOM   10426 O  O     . ASP D 3 245 ? 140.117 194.156 58.478  1.00 63.39  ? 245  ASP A O     1 
ATOM   10427 C  CB    . ASP D 3 245 ? 137.144 194.125 56.896  1.00 68.51  ? 245  ASP A CB    1 
ATOM   10428 C  CG    . ASP D 3 245 ? 137.400 195.616 56.959  1.00 74.25  ? 245  ASP A CG    1 
ATOM   10429 O  OD1   . ASP D 3 245 ? 137.574 196.143 58.078  1.00 73.21  ? 245  ASP A OD1   1 
ATOM   10430 O  OD2   . ASP D 3 245 ? 137.429 196.262 55.891  1.00 69.89  ? 245  ASP A OD2   1 
ATOM   10431 N  N     . GLY D 3 246 ? 139.866 192.750 56.747  1.00 54.31  ? 246  GLY A N     1 
ATOM   10432 C  CA    . GLY D 3 246 ? 141.271 192.764 56.402  1.00 55.54  ? 246  GLY A CA    1 
ATOM   10433 C  C     . GLY D 3 246 ? 141.587 191.673 55.403  1.00 54.26  ? 246  GLY A C     1 
ATOM   10434 O  O     . GLY D 3 246 ? 140.722 190.898 54.996  1.00 57.14  ? 246  GLY A O     1 
ATOM   10435 N  N     . ALA D 3 247 ? 142.858 191.629 55.018  1.00 50.03  ? 247  ALA A N     1 
ATOM   10436 C  CA    . ALA D 3 247 ? 143.331 190.607 54.096  1.00 44.32  ? 247  ALA A CA    1 
ATOM   10437 C  C     . ALA D 3 247 ? 143.772 189.375 54.872  1.00 47.96  ? 247  ALA A C     1 
ATOM   10438 O  O     . ALA D 3 247 ? 144.508 189.483 55.856  1.00 55.90  ? 247  ALA A O     1 
ATOM   10439 C  CB    . ALA D 3 247 ? 144.485 191.142 53.252  1.00 43.58  ? 247  ALA A CB    1 
ATOM   10440 N  N     . LEU D 3 248 ? 143.334 188.202 54.417  1.00 51.10  ? 248  LEU A N     1 
ATOM   10441 C  CA    . LEU D 3 248 ? 143.587 186.933 55.100  1.00 55.66  ? 248  LEU A CA    1 
ATOM   10442 C  C     . LEU D 3 248 ? 142.971 186.926 56.501  1.00 54.76  ? 248  LEU A C     1 
ATOM   10443 O  O     . LEU D 3 248 ? 143.663 186.884 57.519  1.00 60.44  ? 248  LEU A O     1 
ATOM   10444 C  CB    . LEU D 3 248 ? 145.087 186.622 55.154  1.00 54.30  ? 248  LEU A CB    1 
ATOM   10445 C  CG    . LEU D 3 248 ? 145.834 186.683 53.825  1.00 56.64  ? 248  LEU A CG    1 
ATOM   10446 C  CD1   . LEU D 3 248 ? 147.317 186.458 54.036  1.00 52.65  ? 248  LEU A CD1   1 
ATOM   10447 C  CD2   . LEU D 3 248 ? 145.269 185.665 52.846  1.00 56.07  ? 248  LEU A CD2   1 
ATOM   10448 N  N     . ASN D 3 249 ? 141.643 186.981 56.533  1.00 50.51  ? 249  ASN A N     1 
ATOM   10449 C  CA    . ASN D 3 249 ? 140.916 186.779 57.777  1.00 53.68  ? 249  ASN A CA    1 
ATOM   10450 C  C     . ASN D 3 249 ? 140.942 185.308 58.176  1.00 58.56  ? 249  ASN A C     1 
ATOM   10451 O  O     . ASN D 3 249 ? 140.887 184.411 57.332  1.00 64.23  ? 249  ASN A O     1 
ATOM   10452 C  CB    . ASN D 3 249 ? 139.475 187.263 57.638  1.00 60.43  ? 249  ASN A CB    1 
ATOM   10453 C  CG    . ASN D 3 249 ? 139.359 188.771 57.708  1.00 66.72  ? 249  ASN A CG    1 
ATOM   10454 O  OD1   . ASN D 3 249 ? 140.110 189.429 58.426  1.00 68.00  ? 249  ASN A OD1   1 
ATOM   10455 N  ND2   . ASN D 3 249 ? 138.415 189.329 56.958  1.00 64.08  ? 249  ASN A ND2   1 
ATOM   10456 N  N     . VAL D 3 250 ? 141.017 185.066 59.484  1.00 56.10  ? 250  VAL A N     1 
ATOM   10457 C  CA    . VAL D 3 250 ? 141.196 183.729 60.041  1.00 52.40  ? 250  VAL A CA    1 
ATOM   10458 C  C     . VAL D 3 250 ? 140.103 183.473 61.070  1.00 57.17  ? 250  VAL A C     1 
ATOM   10459 O  O     . VAL D 3 250 ? 139.895 184.288 61.974  1.00 63.39  ? 250  VAL A O     1 
ATOM   10460 C  CB    . VAL D 3 250 ? 142.587 183.571 60.684  1.00 54.96  ? 250  VAL A CB    1 
ATOM   10461 C  CG1   . VAL D 3 250 ? 142.731 182.206 61.320  1.00 56.23  ? 250  VAL A CG1   1 
ATOM   10462 C  CG2   . VAL D 3 250 ? 143.679 183.802 59.657  1.00 56.32  ? 250  VAL A CG2   1 
ATOM   10463 N  N     . ASP D 3 251 ? 139.422 182.341 60.946  1.00 68.27  ? 251  ASP A N     1 
ATOM   10464 C  CA    . ASP D 3 251 ? 138.371 181.944 61.872  1.00 68.01  ? 251  ASP A CA    1 
ATOM   10465 C  C     . ASP D 3 251 ? 138.935 180.994 62.925  1.00 70.59  ? 251  ASP A C     1 
ATOM   10466 O  O     . ASP D 3 251 ? 140.103 180.597 62.879  1.00 79.65  ? 251  ASP A O     1 
ATOM   10467 C  CB    . ASP D 3 251 ? 137.207 181.301 61.118  1.00 71.89  ? 251  ASP A CB    1 
ATOM   10468 C  CG    . ASP D 3 251 ? 136.597 182.228 60.085  1.00 80.16  ? 251  ASP A CG    1 
ATOM   10469 O  OD1   . ASP D 3 251 ? 137.048 183.388 59.984  1.00 79.25  ? 251  ASP A OD1   1 
ATOM   10470 O  OD2   . ASP D 3 251 ? 135.667 181.796 59.372  1.00 80.86  ? 251  ASP A OD2   1 
ATOM   10471 N  N     . LEU D 3 252 ? 138.087 180.631 63.891  1.00 62.87  ? 252  LEU A N     1 
ATOM   10472 C  CA    . LEU D 3 252 ? 138.520 179.731 64.957  1.00 71.77  ? 252  LEU A CA    1 
ATOM   10473 C  C     . LEU D 3 252 ? 138.764 178.319 64.435  1.00 75.95  ? 252  LEU A C     1 
ATOM   10474 O  O     . LEU D 3 252 ? 139.733 177.656 64.838  1.00 79.95  ? 252  LEU A O     1 
ATOM   10475 C  CB    . LEU D 3 252 ? 137.486 179.715 66.079  1.00 69.79  ? 252  LEU A CB    1 
ATOM   10476 C  CG    . LEU D 3 252 ? 137.090 181.065 66.672  1.00 67.66  ? 252  LEU A CG    1 
ATOM   10477 C  CD1   . LEU D 3 252 ? 136.222 180.861 67.896  1.00 71.58  ? 252  LEU A CD1   1 
ATOM   10478 C  CD2   . LEU D 3 252 ? 138.315 181.886 67.017  1.00 66.94  ? 252  LEU A CD2   1 
ATOM   10479 N  N     . THR D 3 253 ? 137.889 177.833 63.552  1.00 71.65  ? 253  THR A N     1 
ATOM   10480 C  CA    . THR D 3 253 ? 138.121 176.533 62.935  1.00 72.77  ? 253  THR A CA    1 
ATOM   10481 C  C     . THR D 3 253 ? 139.436 176.516 62.171  1.00 75.58  ? 253  THR A C     1 
ATOM   10482 O  O     . THR D 3 253 ? 140.109 175.480 62.113  1.00 74.74  ? 253  THR A O     1 
ATOM   10483 C  CB    . THR D 3 253 ? 136.961 176.171 62.010  1.00 73.31  ? 253  THR A CB    1 
ATOM   10484 O  OG1   . THR D 3 253 ? 136.809 177.188 61.012  1.00 76.35  ? 253  THR A OG1   1 
ATOM   10485 C  CG2   . THR D 3 253 ? 135.673 176.053 62.805  1.00 72.61  ? 253  THR A CG2   1 
ATOM   10486 N  N     . GLU D 3 254 ? 139.825 177.653 61.594  1.00 67.15  ? 254  GLU A N     1 
ATOM   10487 C  CA    . GLU D 3 254 ? 141.132 177.756 60.956  1.00 61.42  ? 254  GLU A CA    1 
ATOM   10488 C  C     . GLU D 3 254 ? 142.252 177.610 61.979  1.00 66.12  ? 254  GLU A C     1 
ATOM   10489 O  O     . GLU D 3 254 ? 143.263 176.945 61.719  1.00 72.02  ? 254  GLU A O     1 
ATOM   10490 C  CB    . GLU D 3 254 ? 141.242 179.082 60.206  1.00 63.37  ? 254  GLU A CB    1 
ATOM   10491 C  CG    . GLU D 3 254 ? 140.072 179.359 59.280  1.00 71.21  ? 254  GLU A CG    1 
ATOM   10492 C  CD    . GLU D 3 254 ? 140.377 180.440 58.263  1.00 75.21  ? 254  GLU A CD    1 
ATOM   10493 O  OE1   . GLU D 3 254 ? 141.551 180.853 58.166  1.00 75.70  ? 254  GLU A OE1   1 
ATOM   10494 O  OE2   . GLU D 3 254 ? 139.441 180.875 57.559  1.00 73.39  ? 254  GLU A OE2   1 
ATOM   10495 N  N     . PHE D 3 255 ? 142.091 178.228 63.152  1.00 69.20  ? 255  PHE A N     1 
ATOM   10496 C  CA    . PHE D 3 255 ? 143.044 178.030 64.237  1.00 70.27  ? 255  PHE A CA    1 
ATOM   10497 C  C     . PHE D 3 255 ? 143.217 176.552 64.541  1.00 73.29  ? 255  PHE A C     1 
ATOM   10498 O  O     . PHE D 3 255 ? 144.342 176.049 64.638  1.00 78.92  ? 255  PHE A O     1 
ATOM   10499 C  CB    . PHE D 3 255 ? 142.595 178.761 65.507  1.00 65.17  ? 255  PHE A CB    1 
ATOM   10500 C  CG    . PHE D 3 255 ? 142.836 180.232 65.484  1.00 67.33  ? 255  PHE A CG    1 
ATOM   10501 C  CD1   . PHE D 3 255 ? 143.965 180.754 64.887  1.00 70.20  ? 255  PHE A CD1   1 
ATOM   10502 C  CD2   . PHE D 3 255 ? 141.937 181.096 66.077  1.00 73.61  ? 255  PHE A CD2   1 
ATOM   10503 C  CE1   . PHE D 3 255 ? 144.186 182.112 64.873  1.00 75.98  ? 255  PHE A CE1   1 
ATOM   10504 C  CE2   . PHE D 3 255 ? 142.151 182.452 66.066  1.00 76.41  ? 255  PHE A CE2   1 
ATOM   10505 C  CZ    . PHE D 3 255 ? 143.277 182.961 65.465  1.00 78.78  ? 255  PHE A CZ    1 
ATOM   10506 N  N     . GLN D 3 256 ? 142.102 175.842 64.709  1.00 70.36  ? 256  GLN A N     1 
ATOM   10507 C  CA    . GLN D 3 256 ? 142.185 174.432 65.071  1.00 68.78  ? 256  GLN A CA    1 
ATOM   10508 C  C     . GLN D 3 256 ? 142.824 173.608 63.958  1.00 71.43  ? 256  GLN A C     1 
ATOM   10509 O  O     . GLN D 3 256 ? 143.657 172.731 64.216  1.00 72.78  ? 256  GLN A O     1 
ATOM   10510 C  CB    . GLN D 3 256 ? 140.801 173.895 65.422  1.00 67.51  ? 256  GLN A CB    1 
ATOM   10511 C  CG    . GLN D 3 256 ? 140.225 174.494 66.680  1.00 68.60  ? 256  GLN A CG    1 
ATOM   10512 C  CD    . GLN D 3 256 ? 138.812 174.035 66.939  1.00 76.15  ? 256  GLN A CD    1 
ATOM   10513 O  OE1   . GLN D 3 256 ? 138.200 174.410 67.937  1.00 81.75  ? 256  GLN A OE1   1 
ATOM   10514 N  NE2   . GLN D 3 256 ? 138.285 173.209 66.045  1.00 73.94  ? 256  GLN A NE2   1 
ATOM   10515 N  N     . THR D 3 257 ? 142.449 173.877 62.706  1.00 59.27  ? 257  THR A N     1 
ATOM   10516 C  CA    . THR D 3 257 ? 142.957 173.076 61.598  1.00 56.56  ? 257  THR A CA    1 
ATOM   10517 C  C     . THR D 3 257 ? 144.395 173.408 61.237  1.00 55.24  ? 257  THR A C     1 
ATOM   10518 O  O     . THR D 3 257 ? 145.026 172.627 60.519  1.00 59.30  ? 257  THR A O     1 
ATOM   10519 C  CB    . THR D 3 257 ? 142.073 173.247 60.362  1.00 58.76  ? 257  THR A CB    1 
ATOM   10520 O  OG1   . THR D 3 257 ? 142.268 172.135 59.482  1.00 60.88  ? 257  THR A OG1   1 
ATOM   10521 C  CG2   . THR D 3 257 ? 142.418 174.529 59.626  1.00 62.18  ? 257  THR A CG2   1 
ATOM   10522 N  N     . ASN D 3 258 ? 144.926 174.538 61.702  1.00 54.59  ? 258  ASN A N     1 
ATOM   10523 C  CA    . ASN D 3 258 ? 146.294 174.914 61.389  1.00 53.50  ? 258  ASN A CA    1 
ATOM   10524 C  C     . ASN D 3 258 ? 147.246 174.820 62.569  1.00 56.51  ? 258  ASN A C     1 
ATOM   10525 O  O     . ASN D 3 258 ? 148.461 174.874 62.362  1.00 64.15  ? 258  ASN A O     1 
ATOM   10526 C  CB    . ASN D 3 258 ? 146.332 176.344 60.834  1.00 52.14  ? 258  ASN A CB    1 
ATOM   10527 C  CG    . ASN D 3 258 ? 145.705 176.448 59.466  1.00 58.31  ? 258  ASN A CG    1 
ATOM   10528 O  OD1   . ASN D 3 258 ? 144.766 177.212 59.258  1.00 65.99  ? 258  ASN A OD1   1 
ATOM   10529 N  ND2   . ASN D 3 258 ? 146.222 175.676 58.519  1.00 61.53  ? 258  ASN A ND2   1 
ATOM   10530 N  N     . LEU D 3 259 ? 146.734 174.683 63.790  1.00 54.51  ? 259  LEU A N     1 
ATOM   10531 C  CA    . LEU D 3 259 ? 147.562 174.664 64.986  1.00 56.94  ? 259  LEU A CA    1 
ATOM   10532 C  C     . LEU D 3 259 ? 147.624 173.301 65.655  1.00 58.05  ? 259  LEU A C     1 
ATOM   10533 O  O     . LEU D 3 259 ? 148.544 173.061 66.443  1.00 70.12  ? 259  LEU A O     1 
ATOM   10534 C  CB    . LEU D 3 259 ? 147.047 175.689 66.003  1.00 58.09  ? 259  LEU A CB    1 
ATOM   10535 C  CG    . LEU D 3 259 ? 147.679 177.077 65.992  1.00 55.99  ? 259  LEU A CG    1 
ATOM   10536 C  CD1   . LEU D 3 259 ? 147.160 177.899 67.153  1.00 57.99  ? 259  LEU A CD1   1 
ATOM   10537 C  CD2   . LEU D 3 259 ? 149.188 176.967 66.046  1.00 57.60  ? 259  LEU A CD2   1 
ATOM   10538 N  N     . VAL D 3 260 ? 146.680 172.413 65.371  1.00 55.07  ? 260  VAL A N     1 
ATOM   10539 C  CA    . VAL D 3 260 ? 146.625 171.121 66.046  1.00 59.62  ? 260  VAL A CA    1 
ATOM   10540 C  C     . VAL D 3 260 ? 146.999 170.031 65.048  1.00 66.50  ? 260  VAL A C     1 
ATOM   10541 O  O     . VAL D 3 260 ? 146.160 169.626 64.229  1.00 71.49  ? 260  VAL A O     1 
ATOM   10542 C  CB    . VAL D 3 260 ? 145.236 170.877 66.653  1.00 60.10  ? 260  VAL A CB    1 
ATOM   10543 C  CG1   . VAL D 3 260 ? 145.181 169.527 67.330  1.00 63.27  ? 260  VAL A CG1   1 
ATOM   10544 C  CG2   . VAL D 3 260 ? 144.894 171.979 67.636  1.00 63.32  ? 260  VAL A CG2   1 
ATOM   10545 N  N     . PRO D 3 261 ? 148.239 169.541 65.067  1.00 62.35  ? 261  PRO A N     1 
ATOM   10546 C  CA    . PRO D 3 261 ? 148.629 168.473 64.139  1.00 55.68  ? 261  PRO A CA    1 
ATOM   10547 C  C     . PRO D 3 261 ? 147.907 167.170 64.425  1.00 62.51  ? 261  PRO A C     1 
ATOM   10548 O  O     . PRO D 3 261 ? 147.288 166.575 63.539  1.00 66.06  ? 261  PRO A O     1 
ATOM   10549 C  CB    . PRO D 3 261 ? 150.137 168.331 64.380  1.00 56.71  ? 261  PRO A CB    1 
ATOM   10550 C  CG    . PRO D 3 261 ? 150.543 169.559 65.121  1.00 63.48  ? 261  PRO A CG    1 
ATOM   10551 C  CD    . PRO D 3 261 ? 149.356 169.959 65.924  1.00 64.66  ? 261  PRO A CD    1 
ATOM   10552 N  N     . TYR D 3 262 ? 147.984 166.727 65.672  1.00 67.73  ? 262  TYR A N     1 
ATOM   10553 C  CA    . TYR D 3 262 ? 147.394 165.490 66.140  1.00 67.77  ? 262  TYR A CA    1 
ATOM   10554 C  C     . TYR D 3 262 ? 146.378 165.794 67.232  1.00 69.20  ? 262  TYR A C     1 
ATOM   10555 O  O     . TYR D 3 262 ? 146.546 166.761 67.980  1.00 73.18  ? 262  TYR A O     1 
ATOM   10556 C  CB    . TYR D 3 262 ? 148.478 164.553 66.683  1.00 66.04  ? 262  TYR A CB    1 
ATOM   10557 C  CG    . TYR D 3 262 ? 149.466 164.117 65.631  1.00 65.53  ? 262  TYR A CG    1 
ATOM   10558 C  CD1   . TYR D 3 262 ? 149.068 163.922 64.318  1.00 67.51  ? 262  TYR A CD1   1 
ATOM   10559 C  CD2   . TYR D 3 262 ? 150.801 163.923 65.942  1.00 68.40  ? 262  TYR A CD2   1 
ATOM   10560 C  CE1   . TYR D 3 262 ? 149.968 163.532 63.350  1.00 68.17  ? 262  TYR A CE1   1 
ATOM   10561 C  CE2   . TYR D 3 262 ? 151.707 163.534 64.980  1.00 71.81  ? 262  TYR A CE2   1 
ATOM   10562 C  CZ    . TYR D 3 262 ? 151.285 163.342 63.686  1.00 74.18  ? 262  TYR A CZ    1 
ATOM   10563 O  OH    . TYR D 3 262 ? 152.185 162.953 62.723  1.00 80.16  ? 262  TYR A OH    1 
ATOM   10564 N  N     . PRO D 3 263 ? 145.325 164.983 67.362  1.00 69.66  ? 263  PRO A N     1 
ATOM   10565 C  CA    . PRO D 3 263 ? 144.215 165.367 68.250  1.00 68.30  ? 263  PRO A CA    1 
ATOM   10566 C  C     . PRO D 3 263 ? 144.622 165.587 69.694  1.00 65.62  ? 263  PRO A C     1 
ATOM   10567 O  O     . PRO D 3 263 ? 143.934 166.321 70.413  1.00 69.44  ? 263  PRO A O     1 
ATOM   10568 C  CB    . PRO D 3 263 ? 143.235 164.192 68.112  1.00 66.72  ? 263  PRO A CB    1 
ATOM   10569 C  CG    . PRO D 3 263 ? 144.043 163.070 67.550  1.00 68.96  ? 263  PRO A CG    1 
ATOM   10570 C  CD    . PRO D 3 263 ? 145.054 163.717 66.664  1.00 71.13  ? 263  PRO A CD    1 
ATOM   10571 N  N     . ARG D 3 264 ? 145.711 164.980 70.145  1.00 62.80  ? 264  ARG A N     1 
ATOM   10572 C  CA    . ARG D 3 264 ? 146.152 165.116 71.525  1.00 64.14  ? 264  ARG A CA    1 
ATOM   10573 C  C     . ARG D 3 264 ? 147.185 166.218 71.721  1.00 68.96  ? 264  ARG A C     1 
ATOM   10574 O  O     . ARG D 3 264 ? 147.676 166.389 72.840  1.00 73.47  ? 264  ARG A O     1 
ATOM   10575 C  CB    . ARG D 3 264 ? 146.719 163.785 72.020  1.00 69.25  ? 264  ARG A CB    1 
ATOM   10576 C  CG    . ARG D 3 264 ? 146.173 163.331 73.357  1.00 66.04  ? 264  ARG A CG    1 
ATOM   10577 C  CD    . ARG D 3 264 ? 146.498 161.871 73.600  1.00 61.54  ? 264  ARG A CD    1 
ATOM   10578 N  NE    . ARG D 3 264 ? 145.917 161.384 74.842  1.00 60.67  ? 264  ARG A NE    1 
ATOM   10579 C  CZ    . ARG D 3 264 ? 146.578 161.287 75.987  1.00 69.60  ? 264  ARG A CZ    1 
ATOM   10580 N  NH1   . ARG D 3 264 ? 147.852 161.625 76.078  1.00 70.07  ? 264  ARG A NH1   1 
ATOM   10581 N  NH2   . ARG D 3 264 ? 145.943 160.839 77.066  1.00 76.06  ? 264  ARG A NH2   1 
ATOM   10582 N  N     . ILE D 3 265 ? 147.526 166.963 70.677  1.00 66.74  ? 265  ILE A N     1 
ATOM   10583 C  CA    . ILE D 3 265 ? 148.527 168.027 70.759  1.00 67.60  ? 265  ILE A CA    1 
ATOM   10584 C  C     . ILE D 3 265 ? 147.806 169.334 70.448  1.00 69.22  ? 265  ILE A C     1 
ATOM   10585 O  O     . ILE D 3 265 ? 147.777 169.794 69.304  1.00 71.26  ? 265  ILE A O     1 
ATOM   10586 C  CB    . ILE D 3 265 ? 149.700 167.797 69.804  1.00 67.87  ? 265  ILE A CB    1 
ATOM   10587 C  CG1   . ILE D 3 265 ? 150.260 166.385 69.971  1.00 65.47  ? 265  ILE A CG1   1 
ATOM   10588 C  CG2   . ILE D 3 265 ? 150.787 168.826 70.038  1.00 70.17  ? 265  ILE A CG2   1 
ATOM   10589 C  CD1   . ILE D 3 265 ? 150.762 166.090 71.359  1.00 66.59  ? 265  ILE A CD1   1 
ATOM   10590 N  N     . HIS D 3 266 ? 147.225 169.951 71.474  1.00 65.04  ? 266  HIS A N     1 
ATOM   10591 C  CA    . HIS D 3 266 ? 146.458 171.181 71.307  1.00 60.75  ? 266  HIS A CA    1 
ATOM   10592 C  C     . HIS D 3 266 ? 146.758 172.159 72.439  1.00 66.33  ? 266  HIS A C     1 
ATOM   10593 O  O     . HIS D 3 266 ? 145.856 172.746 73.039  1.00 72.12  ? 266  HIS A O     1 
ATOM   10594 C  CB    . HIS D 3 266 ? 144.961 170.891 71.215  1.00 58.29  ? 266  HIS A CB    1 
ATOM   10595 C  CG    . HIS D 3 266 ? 144.435 170.031 72.320  1.00 55.85  ? 266  HIS A CG    1 
ATOM   10596 N  ND1   . HIS D 3 266 ? 144.639 170.319 73.650  1.00 57.45  ? 266  HIS A ND1   1 
ATOM   10597 C  CD2   . HIS D 3 266 ? 143.692 168.900 72.291  1.00 58.40  ? 266  HIS A CD2   1 
ATOM   10598 C  CE1   . HIS D 3 266 ? 144.053 169.399 74.394  1.00 59.91  ? 266  HIS A CE1   1 
ATOM   10599 N  NE2   . HIS D 3 266 ? 143.471 168.526 73.593  1.00 59.95  ? 266  HIS A NE2   1 
ATOM   10600 N  N     . PHE D 3 267 ? 148.037 172.348 72.752  1.00 59.09  ? 267  PHE A N     1 
ATOM   10601 C  CA    . PHE D 3 267 ? 148.457 173.230 73.840  1.00 53.45  ? 267  PHE A CA    1 
ATOM   10602 C  C     . PHE D 3 267 ? 149.454 174.258 73.323  1.00 50.19  ? 267  PHE A C     1 
ATOM   10603 O  O     . PHE D 3 267 ? 150.647 174.203 73.645  1.00 61.99  ? 267  PHE A O     1 
ATOM   10604 C  CB    . PHE D 3 267 ? 149.064 172.423 74.987  1.00 57.77  ? 267  PHE A CB    1 
ATOM   10605 C  CG    . PHE D 3 267 ? 148.078 171.560 75.707  1.00 60.22  ? 267  PHE A CG    1 
ATOM   10606 C  CD1   . PHE D 3 267 ? 147.308 172.072 76.734  1.00 59.16  ? 267  PHE A CD1   1 
ATOM   10607 C  CD2   . PHE D 3 267 ? 147.918 170.238 75.354  1.00 58.32  ? 267  PHE A CD2   1 
ATOM   10608 C  CE1   . PHE D 3 267 ? 146.400 171.276 77.395  1.00 58.41  ? 267  PHE A CE1   1 
ATOM   10609 C  CE2   . PHE D 3 267 ? 147.015 169.441 76.008  1.00 60.86  ? 267  PHE A CE2   1 
ATOM   10610 C  CZ    . PHE D 3 267 ? 146.253 169.958 77.030  1.00 61.44  ? 267  PHE A CZ    1 
ATOM   10611 N  N     . PRO D 3 268 ? 149.000 175.213 72.517  1.00 36.48  ? 268  PRO A N     1 
ATOM   10612 C  CA    . PRO D 3 268 ? 149.900 176.266 72.045  1.00 41.84  ? 268  PRO A CA    1 
ATOM   10613 C  C     . PRO D 3 268 ? 150.139 177.306 73.126  1.00 51.88  ? 268  PRO A C     1 
ATOM   10614 O  O     . PRO D 3 268 ? 149.428 177.389 74.129  1.00 65.10  ? 268  PRO A O     1 
ATOM   10615 C  CB    . PRO D 3 268 ? 149.157 176.871 70.850  1.00 47.99  ? 268  PRO A CB    1 
ATOM   10616 C  CG    . PRO D 3 268 ? 148.021 175.947 70.573  1.00 52.67  ? 268  PRO A CG    1 
ATOM   10617 C  CD    . PRO D 3 268 ? 147.683 175.324 71.879  1.00 48.18  ? 268  PRO A CD    1 
ATOM   10618 N  N     . LEU D 3 269 ? 151.168 178.113 72.903  1.00 47.07  ? 269  LEU A N     1 
ATOM   10619 C  CA    . LEU D 3 269 ? 151.511 179.211 73.791  1.00 48.91  ? 269  LEU A CA    1 
ATOM   10620 C  C     . LEU D 3 269 ? 151.508 180.514 73.007  1.00 54.56  ? 269  LEU A C     1 
ATOM   10621 O  O     . LEU D 3 269 ? 152.111 180.608 71.934  1.00 59.93  ? 269  LEU A O     1 
ATOM   10622 C  CB    . LEU D 3 269 ? 152.868 178.971 74.467  1.00 53.53  ? 269  LEU A CB    1 
ATOM   10623 C  CG    . LEU D 3 269 ? 154.099 178.660 73.617  1.00 56.88  ? 269  LEU A CG    1 
ATOM   10624 C  CD1   . LEU D 3 269 ? 154.898 179.914 73.331  1.00 57.04  ? 269  LEU A CD1   1 
ATOM   10625 C  CD2   . LEU D 3 269 ? 154.958 177.625 74.315  1.00 51.81  ? 269  LEU A CD2   1 
ATOM   10626 N  N     . ALA D 3 270 ? 150.807 181.508 73.537  1.00 50.11  ? 270  ALA A N     1 
ATOM   10627 C  CA    . ALA D 3 270 ? 150.630 182.771 72.844  1.00 48.23  ? 270  ALA A CA    1 
ATOM   10628 C  C     . ALA D 3 270 ? 151.807 183.700 73.107  1.00 54.06  ? 270  ALA A C     1 
ATOM   10629 O  O     . ALA D 3 270 ? 152.518 183.581 74.106  1.00 58.03  ? 270  ALA A O     1 
ATOM   10630 C  CB    . ALA D 3 270 ? 149.326 183.442 73.273  1.00 54.71  ? 270  ALA A CB    1 
ATOM   10631 N  N     . THR D 3 271 ? 152.004 184.635 72.184  1.00 58.61  ? 271  THR A N     1 
ATOM   10632 C  CA    . THR D 3 271 ? 153.064 185.627 72.289  1.00 60.61  ? 271  THR A CA    1 
ATOM   10633 C  C     . THR D 3 271 ? 152.568 186.899 71.623  1.00 58.87  ? 271  THR A C     1 
ATOM   10634 O  O     . THR D 3 271 ? 151.827 186.830 70.640  1.00 64.51  ? 271  THR A O     1 
ATOM   10635 C  CB    . THR D 3 271 ? 154.358 185.137 71.625  1.00 62.70  ? 271  THR A CB    1 
ATOM   10636 O  OG1   . THR D 3 271 ? 154.706 183.849 72.149  1.00 64.00  ? 271  THR A OG1   1 
ATOM   10637 C  CG2   . THR D 3 271 ? 155.501 186.096 71.902  1.00 60.96  ? 271  THR A CG2   1 
ATOM   10638 N  N     . TYR D 3 272 ? 152.959 188.047 72.160  1.00 43.87  ? 272  TYR A N     1 
ATOM   10639 C  CA    . TYR D 3 272 ? 152.501 189.331 71.661  1.00 42.38  ? 272  TYR A CA    1 
ATOM   10640 C  C     . TYR D 3 272 ? 153.684 190.248 71.399  1.00 45.03  ? 272  TYR A C     1 
ATOM   10641 O  O     . TYR D 3 272 ? 154.712 190.175 72.076  1.00 51.64  ? 272  TYR A O     1 
ATOM   10642 C  CB    . TYR D 3 272 ? 151.538 189.990 72.653  1.00 46.19  ? 272  TYR A CB    1 
ATOM   10643 C  CG    . TYR D 3 272 ? 150.798 191.182 72.100  1.00 51.02  ? 272  TYR A CG    1 
ATOM   10644 C  CD1   . TYR D 3 272 ? 149.794 191.025 71.158  1.00 51.83  ? 272  TYR A CD1   1 
ATOM   10645 C  CD2   . TYR D 3 272 ? 151.093 192.463 72.532  1.00 50.05  ? 272  TYR A CD2   1 
ATOM   10646 C  CE1   . TYR D 3 272 ? 149.115 192.111 70.654  1.00 46.95  ? 272  TYR A CE1   1 
ATOM   10647 C  CE2   . TYR D 3 272 ? 150.420 193.554 72.034  1.00 45.13  ? 272  TYR A CE2   1 
ATOM   10648 C  CZ    . TYR D 3 272 ? 149.432 193.372 71.096  1.00 46.68  ? 272  TYR A CZ    1 
ATOM   10649 O  OH    . TYR D 3 272 ? 148.755 194.459 70.597  1.00 55.92  ? 272  TYR A OH    1 
ATOM   10650 N  N     . ALA D 3 273 ? 153.527 191.111 70.399  1.00 49.26  ? 273  ALA A N     1 
ATOM   10651 C  CA    . ALA D 3 273 ? 154.524 192.116 70.065  1.00 46.72  ? 273  ALA A CA    1 
ATOM   10652 C  C     . ALA D 3 273 ? 153.830 193.235 69.312  1.00 50.69  ? 273  ALA A C     1 
ATOM   10653 O  O     . ALA D 3 273 ? 152.949 192.964 68.490  1.00 62.40  ? 273  ALA A O     1 
ATOM   10654 C  CB    . ALA D 3 273 ? 155.655 191.519 69.217  1.00 49.04  ? 273  ALA A CB    1 
ATOM   10655 N  N     . PRO D 3 274 ? 154.198 194.493 69.559  1.00 45.40  ? 274  PRO A N     1 
ATOM   10656 C  CA    . PRO D 3 274 ? 155.209 194.967 70.502  1.00 51.20  ? 274  PRO A CA    1 
ATOM   10657 C  C     . PRO D 3 274 ? 154.623 195.359 71.853  1.00 62.90  ? 274  PRO A C     1 
ATOM   10658 O  O     . PRO D 3 274 ? 153.600 196.035 71.926  1.00 66.57  ? 274  PRO A O     1 
ATOM   10659 C  CB    . PRO D 3 274 ? 155.805 196.186 69.778  1.00 52.08  ? 274  PRO A CB    1 
ATOM   10660 C  CG    . PRO D 3 274 ? 154.853 196.519 68.628  1.00 53.58  ? 274  PRO A CG    1 
ATOM   10661 C  CD    . PRO D 3 274 ? 153.669 195.606 68.764  1.00 50.94  ? 274  PRO A CD    1 
ATOM   10662 N  N     . VAL D 3 275 ? 155.256 194.947 72.944  1.00 56.72  ? 275  VAL A N     1 
ATOM   10663 C  CA    . VAL D 3 275 ? 154.860 195.364 74.285  1.00 54.23  ? 275  VAL A CA    1 
ATOM   10664 C  C     . VAL D 3 275 ? 155.912 196.373 74.729  1.00 59.23  ? 275  VAL A C     1 
ATOM   10665 O  O     . VAL D 3 275 ? 156.961 196.015 75.259  1.00 69.45  ? 275  VAL A O     1 
ATOM   10666 C  CB    . VAL D 3 275 ? 154.751 194.181 75.242  1.00 58.47  ? 275  VAL A CB    1 
ATOM   10667 C  CG1   . VAL D 3 275 ? 154.051 194.601 76.522  1.00 64.83  ? 275  VAL A CG1   1 
ATOM   10668 C  CG2   . VAL D 3 275 ? 154.011 193.033 74.583  1.00 55.31  ? 275  VAL A CG2   1 
ATOM   10669 N  N     . ILE D 3 276 ? 155.637 197.656 74.500  1.00 61.85  ? 276  ILE A N     1 
ATOM   10670 C  CA    . ILE D 3 276 ? 156.591 198.714 74.802  1.00 65.18  ? 276  ILE A CA    1 
ATOM   10671 C  C     . ILE D 3 276 ? 155.883 199.856 75.513  1.00 66.11  ? 276  ILE A C     1 
ATOM   10672 O  O     . ILE D 3 276 ? 154.661 200.002 75.451  1.00 67.24  ? 276  ILE A O     1 
ATOM   10673 C  CB    . ILE D 3 276 ? 157.307 199.238 73.539  1.00 64.12  ? 276  ILE A CB    1 
ATOM   10674 C  CG1   . ILE D 3 276 ? 156.305 199.896 72.595  1.00 66.43  ? 276  ILE A CG1   1 
ATOM   10675 C  CG2   . ILE D 3 276 ? 158.066 198.121 72.837  1.00 63.31  ? 276  ILE A CG2   1 
ATOM   10676 C  CD1   . ILE D 3 276 ? 156.933 200.435 71.346  1.00 69.06  ? 276  ILE A CD1   1 
ATOM   10677 N  N     . SER D 3 277 ? 156.678 200.674 76.195  1.00 69.35  ? 277  SER A N     1 
ATOM   10678 C  CA    . SER D 3 277 ? 156.176 201.838 76.901  1.00 71.85  ? 277  SER A CA    1 
ATOM   10679 C  C     . SER D 3 277 ? 156.076 203.027 75.950  1.00 70.47  ? 277  SER A C     1 
ATOM   10680 O  O     . SER D 3 277 ? 156.481 202.966 74.787  1.00 76.46  ? 277  SER A O     1 
ATOM   10681 C  CB    . SER D 3 277 ? 157.073 202.163 78.093  1.00 72.51  ? 277  SER A CB    1 
ATOM   10682 O  OG    . SER D 3 277 ? 156.633 203.334 78.757  1.00 72.71  ? 277  SER A OG    1 
ATOM   10683 N  N     . ALA D 3 278 ? 155.525 204.132 76.452  1.00 66.87  ? 278  ALA A N     1 
ATOM   10684 C  CA    . ALA D 3 278 ? 155.421 205.336 75.639  1.00 68.07  ? 278  ALA A CA    1 
ATOM   10685 C  C     . ALA D 3 278 ? 156.784 205.967 75.395  1.00 73.74  ? 278  ALA A C     1 
ATOM   10686 O  O     . ALA D 3 278 ? 157.015 206.545 74.326  1.00 73.13  ? 278  ALA A O     1 
ATOM   10687 C  CB    . ALA D 3 278 ? 154.481 206.340 76.302  1.00 68.76  ? 278  ALA A CB    1 
ATOM   10688 N  N     . GLU D 3 279 ? 157.692 205.877 76.369  1.00 76.86  ? 279  GLU A N     1 
ATOM   10689 C  CA    . GLU D 3 279 ? 159.029 206.433 76.193  1.00 71.27  ? 279  GLU A CA    1 
ATOM   10690 C  C     . GLU D 3 279 ? 159.778 205.719 75.077  1.00 71.79  ? 279  GLU A C     1 
ATOM   10691 O  O     . GLU D 3 279 ? 160.460 206.358 74.267  1.00 75.70  ? 279  GLU A O     1 
ATOM   10692 C  CB    . GLU D 3 279 ? 159.808 206.346 77.504  1.00 75.28  ? 279  GLU A CB    1 
ATOM   10693 C  CG    . GLU D 3 279 ? 161.306 206.534 77.353  1.00 80.21  ? 279  GLU A CG    1 
ATOM   10694 C  CD    . GLU D 3 279 ? 162.071 206.147 78.603  1.00 84.14  ? 279  GLU A CD    1 
ATOM   10695 O  OE1   . GLU D 3 279 ? 161.448 206.065 79.682  1.00 83.14  ? 279  GLU A OE1   1 
ATOM   10696 O  OE2   . GLU D 3 279 ? 163.296 205.923 78.506  1.00 85.69  ? 279  GLU A OE2   1 
ATOM   10697 N  N     . LYS D 3 280 ? 159.659 204.398 75.014  1.00 69.28  ? 280  LYS A N     1 
ATOM   10698 C  CA    . LYS D 3 280 ? 160.306 203.605 73.982  1.00 71.07  ? 280  LYS A CA    1 
ATOM   10699 C  C     . LYS D 3 280 ? 159.435 203.411 72.749  1.00 69.99  ? 280  LYS A C     1 
ATOM   10700 O  O     . LYS D 3 280 ? 159.869 202.750 71.802  1.00 68.15  ? 280  LYS A O     1 
ATOM   10701 C  CB    . LYS D 3 280 ? 160.713 202.243 74.547  1.00 74.24  ? 280  LYS A CB    1 
ATOM   10702 C  CG    . LYS D 3 280 ? 161.905 202.306 75.480  1.00 74.41  ? 280  LYS A CG    1 
ATOM   10703 C  CD    . LYS D 3 280 ? 162.386 200.919 75.857  1.00 76.07  ? 280  LYS A CD    1 
ATOM   10704 C  CE    . LYS D 3 280 ? 161.365 200.208 76.722  1.00 77.12  ? 280  LYS A CE    1 
ATOM   10705 N  NZ    . LYS D 3 280 ? 161.145 200.924 78.006  1.00 77.49  ? 280  LYS A NZ    1 
ATOM   10706 N  N     . ALA D 3 281 ? 158.214 203.950 72.742  1.00 73.20  ? 281  ALA A N     1 
ATOM   10707 C  CA    . ALA D 3 281 ? 157.427 203.955 71.514  1.00 69.85  ? 281  ALA A CA    1 
ATOM   10708 C  C     . ALA D 3 281 ? 158.121 204.764 70.433  1.00 74.89  ? 281  ALA A C     1 
ATOM   10709 O  O     . ALA D 3 281 ? 158.147 204.356 69.266  1.00 76.86  ? 281  ALA A O     1 
ATOM   10710 C  CB    . ALA D 3 281 ? 156.027 204.506 71.782  1.00 73.79  ? 281  ALA A CB    1 
ATOM   10711 N  N     . TYR D 3 282 ? 158.684 205.907 70.801  1.00 74.11  ? 282  TYR A N     1 
ATOM   10712 C  CA    . TYR D 3 282 ? 159.636 206.610 69.963  1.00 67.06  ? 282  TYR A CA    1 
ATOM   10713 C  C     . TYR D 3 282 ? 160.973 205.878 70.007  1.00 66.54  ? 282  TYR A C     1 
ATOM   10714 O  O     . TYR D 3 282 ? 161.151 204.904 70.740  1.00 74.80  ? 282  TYR A O     1 
ATOM   10715 C  CB    . TYR D 3 282 ? 159.791 208.054 70.430  1.00 67.26  ? 282  TYR A CB    1 
ATOM   10716 C  CG    . TYR D 3 282 ? 158.539 208.626 71.053  1.00 72.33  ? 282  TYR A CG    1 
ATOM   10717 C  CD1   . TYR D 3 282 ? 157.336 208.636 70.361  1.00 72.06  ? 282  TYR A CD1   1 
ATOM   10718 C  CD2   . TYR D 3 282 ? 158.558 209.148 72.337  1.00 75.40  ? 282  TYR A CD2   1 
ATOM   10719 C  CE1   . TYR D 3 282 ? 156.192 209.155 70.928  1.00 72.76  ? 282  TYR A CE1   1 
ATOM   10720 C  CE2   . TYR D 3 282 ? 157.419 209.669 72.913  1.00 77.44  ? 282  TYR A CE2   1 
ATOM   10721 C  CZ    . TYR D 3 282 ? 156.239 209.670 72.204  1.00 77.82  ? 282  TYR A CZ    1 
ATOM   10722 O  OH    . TYR D 3 282 ? 155.100 210.189 72.775  1.00 75.58  ? 282  TYR A OH    1 
ATOM   10723 N  N     . HIS D 3 283 ? 161.918 206.346 69.198  1.00 59.29  ? 283  HIS A N     1 
ATOM   10724 C  CA    . HIS D 3 283 ? 163.254 205.777 69.061  1.00 69.19  ? 283  HIS A CA    1 
ATOM   10725 C  C     . HIS D 3 283 ? 163.252 204.385 68.442  1.00 75.62  ? 283  HIS A C     1 
ATOM   10726 O  O     . HIS D 3 283 ? 164.332 203.815 68.245  1.00 79.21  ? 283  HIS A O     1 
ATOM   10727 C  CB    . HIS D 3 283 ? 164.012 205.702 70.396  1.00 67.39  ? 283  HIS A CB    1 
ATOM   10728 C  CG    . HIS D 3 283 ? 163.897 206.935 71.236  1.00 69.82  ? 283  HIS A CG    1 
ATOM   10729 N  ND1   . HIS D 3 283 ? 162.953 207.073 72.229  1.00 73.42  ? 283  HIS A ND1   1 
ATOM   10730 C  CD2   . HIS D 3 283 ? 164.624 208.076 71.247  1.00 70.73  ? 283  HIS A CD2   1 
ATOM   10731 C  CE1   . HIS D 3 283 ? 163.096 208.252 72.808  1.00 72.04  ? 283  HIS A CE1   1 
ATOM   10732 N  NE2   . HIS D 3 283 ? 164.103 208.881 72.230  1.00 71.88  ? 283  HIS A NE2   1 
ATOM   10733 N  N     . GLU D 3 284 ? 162.092 203.815 68.125  1.00 74.42  ? 284  GLU A N     1 
ATOM   10734 C  CA    . GLU D 3 284 ? 162.014 202.482 67.544  1.00 72.87  ? 284  GLU A CA    1 
ATOM   10735 C  C     . GLU D 3 284 ? 161.168 202.521 66.283  1.00 71.64  ? 284  GLU A C     1 
ATOM   10736 O  O     . GLU D 3 284 ? 160.117 203.168 66.254  1.00 71.53  ? 284  GLU A O     1 
ATOM   10737 C  CB    . GLU D 3 284 ? 161.432 201.472 68.538  1.00 75.63  ? 284  GLU A CB    1 
ATOM   10738 C  CG    . GLU D 3 284 ? 162.070 201.504 69.917  1.00 81.42  ? 284  GLU A CG    1 
ATOM   10739 C  CD    . GLU D 3 284 ? 163.538 201.118 69.897  1.00 83.95  ? 284  GLU A CD    1 
ATOM   10740 O  OE1   . GLU D 3 284 ? 163.937 200.328 69.016  1.00 80.60  ? 284  GLU A OE1   1 
ATOM   10741 O  OE2   . GLU D 3 284 ? 164.292 201.605 70.767  1.00 77.27  ? 284  GLU A OE2   1 
ATOM   10742 N  N     . GLN D 3 285 ? 161.630 201.825 65.243  1.00 67.47  ? 285  GLN A N     1 
ATOM   10743 C  CA    . GLN D 3 285 ? 160.881 201.774 63.993  1.00 67.71  ? 285  GLN A CA    1 
ATOM   10744 C  C     . GLN D 3 285 ? 159.627 200.921 64.121  1.00 68.12  ? 285  GLN A C     1 
ATOM   10745 O  O     . GLN D 3 285 ? 158.594 201.256 63.531  1.00 64.64  ? 285  GLN A O     1 
ATOM   10746 C  CB    . GLN D 3 285 ? 161.771 201.243 62.870  1.00 65.95  ? 285  GLN A CB    1 
ATOM   10747 C  CG    . GLN D 3 285 ? 162.507 202.322 62.103  1.00 65.67  ? 285  GLN A CG    1 
ATOM   10748 C  CD    . GLN D 3 285 ? 161.650 202.952 61.025  1.00 72.36  ? 285  GLN A CD    1 
ATOM   10749 O  OE1   . GLN D 3 285 ? 160.819 202.286 60.409  1.00 73.29  ? 285  GLN A OE1   1 
ATOM   10750 N  NE2   . GLN D 3 285 ? 161.846 204.244 60.793  1.00 71.64  ? 285  GLN A NE2   1 
ATOM   10751 N  N     . LEU D 3 286 ? 159.700 199.827 64.880  1.00 67.77  ? 286  LEU A N     1 
ATOM   10752 C  CA    . LEU D 3 286 ? 158.585 198.896 65.051  1.00 62.39  ? 286  LEU A CA    1 
ATOM   10753 C  C     . LEU D 3 286 ? 158.127 198.331 63.710  1.00 64.47  ? 286  LEU A C     1 
ATOM   10754 O  O     . LEU D 3 286 ? 156.933 198.192 63.439  1.00 64.86  ? 286  LEU A O     1 
ATOM   10755 C  CB    . LEU D 3 286 ? 157.426 199.558 65.791  1.00 62.06  ? 286  LEU A CB    1 
ATOM   10756 C  CG    . LEU D 3 286 ? 157.273 199.200 67.263  1.00 65.14  ? 286  LEU A CG    1 
ATOM   10757 C  CD1   . LEU D 3 286 ? 158.599 199.300 67.982  1.00 62.84  ? 286  LEU A CD1   1 
ATOM   10758 C  CD2   . LEU D 3 286 ? 156.258 200.129 67.884  1.00 69.64  ? 286  LEU A CD2   1 
ATOM   10759 N  N     . SER D 3 287 ? 159.098 198.000 62.865  1.00 65.15  ? 287  SER A N     1 
ATOM   10760 C  CA    . SER D 3 287 ? 158.795 197.427 61.568  1.00 65.51  ? 287  SER A CA    1 
ATOM   10761 C  C     . SER D 3 287 ? 158.263 196.005 61.729  1.00 65.68  ? 287  SER A C     1 
ATOM   10762 O  O     . SER D 3 287 ? 158.354 195.391 62.794  1.00 73.96  ? 287  SER A O     1 
ATOM   10763 C  CB    . SER D 3 287 ? 160.035 197.432 60.676  1.00 67.84  ? 287  SER A CB    1 
ATOM   10764 O  OG    . SER D 3 287 ? 161.081 196.672 61.254  1.00 70.37  ? 287  SER A OG    1 
ATOM   10765 N  N     . VAL D 3 288 ? 157.697 195.483 60.641  1.00 54.56  ? 288  VAL A N     1 
ATOM   10766 C  CA    . VAL D 3 288 ? 157.116 194.145 60.670  1.00 58.23  ? 288  VAL A CA    1 
ATOM   10767 C  C     . VAL D 3 288 ? 158.191 193.107 60.965  1.00 63.19  ? 288  VAL A C     1 
ATOM   10768 O  O     . VAL D 3 288 ? 157.981 192.171 61.748  1.00 73.55  ? 288  VAL A O     1 
ATOM   10769 C  CB    . VAL D 3 288 ? 156.391 193.850 59.347  1.00 59.77  ? 288  VAL A CB    1 
ATOM   10770 C  CG1   . VAL D 3 288 ? 155.907 192.416 59.314  1.00 60.77  ? 288  VAL A CG1   1 
ATOM   10771 C  CG2   . VAL D 3 288 ? 155.232 194.807 59.163  1.00 62.65  ? 288  VAL A CG2   1 
ATOM   10772 N  N     . ALA D 3 289 ? 159.362 193.259 60.344  1.00 56.06  ? 289  ALA A N     1 
ATOM   10773 C  CA    . ALA D 3 289 ? 160.443 192.306 60.566  1.00 60.73  ? 289  ALA A CA    1 
ATOM   10774 C  C     . ALA D 3 289 ? 160.896 192.311 62.018  1.00 62.05  ? 289  ALA A C     1 
ATOM   10775 O  O     . ALA D 3 289 ? 161.085 191.247 62.622  1.00 67.09  ? 289  ALA A O     1 
ATOM   10776 C  CB    . ALA D 3 289 ? 161.615 192.619 59.637  1.00 61.66  ? 289  ALA A CB    1 
ATOM   10777 N  N     . GLU D 3 290 ? 161.071 193.500 62.598  1.00 67.67  ? 290  GLU A N     1 
ATOM   10778 C  CA    . GLU D 3 290 ? 161.471 193.592 63.997  1.00 67.31  ? 290  GLU A CA    1 
ATOM   10779 C  C     . GLU D 3 290 ? 160.415 192.989 64.909  1.00 64.77  ? 290  GLU A C     1 
ATOM   10780 O  O     . GLU D 3 290 ? 160.742 192.290 65.873  1.00 69.17  ? 290  GLU A O     1 
ATOM   10781 C  CB    . GLU D 3 290 ? 161.730 195.049 64.375  1.00 68.18  ? 290  GLU A CB    1 
ATOM   10782 C  CG    . GLU D 3 290 ? 162.304 195.236 65.768  1.00 72.77  ? 290  GLU A CG    1 
ATOM   10783 C  CD    . GLU D 3 290 ? 162.751 196.661 66.027  1.00 78.86  ? 290  GLU A CD    1 
ATOM   10784 O  OE1   . GLU D 3 290 ? 162.582 197.511 65.128  1.00 77.95  ? 290  GLU A OE1   1 
ATOM   10785 O  OE2   . GLU D 3 290 ? 163.270 196.931 67.130  1.00 80.09  ? 290  GLU A OE2   1 
ATOM   10786 N  N     . ILE D 3 291 ? 159.141 193.248 64.616  1.00 55.01  ? 291  ILE A N     1 
ATOM   10787 C  CA    . ILE D 3 291 ? 158.063 192.714 65.439  1.00 53.58  ? 291  ILE A CA    1 
ATOM   10788 C  C     . ILE D 3 291 ? 158.069 191.192 65.404  1.00 61.14  ? 291  ILE A C     1 
ATOM   10789 O  O     . ILE D 3 291 ? 158.001 190.536 66.450  1.00 68.74  ? 291  ILE A O     1 
ATOM   10790 C  CB    . ILE D 3 291 ? 156.712 193.290 64.980  1.00 57.58  ? 291  ILE A CB    1 
ATOM   10791 C  CG1   . ILE D 3 291 ? 156.591 194.752 65.398  1.00 64.12  ? 291  ILE A CG1   1 
ATOM   10792 C  CG2   . ILE D 3 291 ? 155.573 192.504 65.563  1.00 62.66  ? 291  ILE A CG2   1 
ATOM   10793 C  CD1   . ILE D 3 291 ? 155.260 195.367 65.055  1.00 64.43  ? 291  ILE A CD1   1 
ATOM   10794 N  N     . THR D 3 292 ? 158.179 190.606 64.210  1.00 52.99  ? 292  THR A N     1 
ATOM   10795 C  CA    . THR D 3 292 ? 158.192 189.149 64.107  1.00 53.53  ? 292  THR A CA    1 
ATOM   10796 C  C     . THR D 3 292 ? 159.406 188.551 64.812  1.00 59.14  ? 292  THR A C     1 
ATOM   10797 O  O     . THR D 3 292 ? 159.282 187.571 65.563  1.00 62.93  ? 292  THR A O     1 
ATOM   10798 C  CB    . THR D 3 292 ? 158.168 188.730 62.638  1.00 55.34  ? 292  THR A CB    1 
ATOM   10799 O  OG1   . THR D 3 292 ? 157.162 189.475 61.941  1.00 55.98  ? 292  THR A OG1   1 
ATOM   10800 C  CG2   . THR D 3 292 ? 157.866 187.246 62.515  1.00 61.10  ? 292  THR A CG2   1 
ATOM   10801 N  N     . ASN D 3 293 ? 160.590 189.133 64.594  1.00 61.17  ? 293  ASN A N     1 
ATOM   10802 C  CA    . ASN D 3 293 ? 161.798 188.599 65.212  1.00 57.50  ? 293  ASN A CA    1 
ATOM   10803 C  C     . ASN D 3 293 ? 161.720 188.672 66.730  1.00 61.23  ? 293  ASN A C     1 
ATOM   10804 O  O     . ASN D 3 293 ? 162.046 187.700 67.421  1.00 64.12  ? 293  ASN A O     1 
ATOM   10805 C  CB    . ASN D 3 293 ? 163.026 189.354 64.706  1.00 54.54  ? 293  ASN A CB    1 
ATOM   10806 C  CG    . ASN D 3 293 ? 163.280 189.130 63.234  1.00 62.91  ? 293  ASN A CG    1 
ATOM   10807 O  OD1   . ASN D 3 293 ? 162.920 188.092 62.681  1.00 67.96  ? 293  ASN A OD1   1 
ATOM   10808 N  ND2   . ASN D 3 293 ? 163.903 190.105 62.586  1.00 63.33  ? 293  ASN A ND2   1 
ATOM   10809 N  N     . ALA D 3 294 ? 161.290 189.815 67.269  1.00 67.74  ? 294  ALA A N     1 
ATOM   10810 C  CA    . ALA D 3 294 ? 161.143 189.936 68.713  1.00 66.87  ? 294  ALA A CA    1 
ATOM   10811 C  C     . ALA D 3 294 ? 160.054 189.017 69.237  1.00 64.52  ? 294  ALA A C     1 
ATOM   10812 O  O     . ALA D 3 294 ? 160.099 188.598 70.399  1.00 69.54  ? 294  ALA A O     1 
ATOM   10813 C  CB    . ALA D 3 294 ? 160.844 191.386 69.093  1.00 66.28  ? 294  ALA A CB    1 
ATOM   10814 N  N     . CYS D 3 295 ? 159.071 188.690 68.400  1.00 55.80  ? 295  CYS A N     1 
ATOM   10815 C  CA    . CYS D 3 295 ? 158.011 187.797 68.839  1.00 57.05  ? 295  CYS A CA    1 
ATOM   10816 C  C     . CYS D 3 295 ? 158.491 186.357 68.900  1.00 55.95  ? 295  CYS A C     1 
ATOM   10817 O  O     . CYS D 3 295 ? 157.957 185.562 69.678  1.00 63.51  ? 295  CYS A O     1 
ATOM   10818 C  CB    . CYS D 3 295 ? 156.808 187.927 67.909  1.00 62.06  ? 295  CYS A CB    1 
ATOM   10819 S  SG    . CYS D 3 295 ? 155.263 187.379 68.632  1.00 71.89  ? 295  CYS A SG    1 
ATOM   10820 N  N     . PHE D 3 296 ? 159.494 186.003 68.099  1.00 60.70  ? 296  PHE A N     1 
ATOM   10821 C  CA    . PHE D 3 296 ? 160.074 184.667 68.193  1.00 65.03  ? 296  PHE A CA    1 
ATOM   10822 C  C     . PHE D 3 296 ? 161.179 184.561 69.238  1.00 63.62  ? 296  PHE A C     1 
ATOM   10823 O  O     . PHE D 3 296 ? 161.736 183.475 69.414  1.00 57.57  ? 296  PHE A O     1 
ATOM   10824 C  CB    . PHE D 3 296 ? 160.614 184.221 66.834  1.00 60.92  ? 296  PHE A CB    1 
ATOM   10825 C  CG    . PHE D 3 296 ? 159.703 183.287 66.103  1.00 62.75  ? 296  PHE A CG    1 
ATOM   10826 C  CD1   . PHE D 3 296 ? 158.810 183.763 65.165  1.00 63.97  ? 296  PHE A CD1   1 
ATOM   10827 C  CD2   . PHE D 3 296 ? 159.728 181.934 66.369  1.00 66.40  ? 296  PHE A CD2   1 
ATOM   10828 C  CE1   . PHE D 3 296 ? 157.969 182.906 64.500  1.00 61.78  ? 296  PHE A CE1   1 
ATOM   10829 C  CE2   . PHE D 3 296 ? 158.888 181.074 65.707  1.00 68.30  ? 296  PHE A CE2   1 
ATOM   10830 C  CZ    . PHE D 3 296 ? 158.008 181.559 64.771  1.00 64.98  ? 296  PHE A CZ    1 
ATOM   10831 N  N     . GLU D 3 297 ? 161.509 185.649 69.924  1.00 72.60  ? 297  GLU A N     1 
ATOM   10832 C  CA    . GLU D 3 297 ? 162.566 185.611 70.923  1.00 64.03  ? 297  GLU A CA    1 
ATOM   10833 C  C     . GLU D 3 297 ? 162.102 184.836 72.155  1.00 70.08  ? 297  GLU A C     1 
ATOM   10834 O  O     . GLU D 3 297 ? 160.959 184.997 72.594  1.00 75.40  ? 297  GLU A O     1 
ATOM   10835 C  CB    . GLU D 3 297 ? 162.971 187.032 71.314  1.00 68.70  ? 297  GLU A CB    1 
ATOM   10836 C  CG    . GLU D 3 297 ? 164.117 187.121 72.302  1.00 74.17  ? 297  GLU A CG    1 
ATOM   10837 C  CD    . GLU D 3 297 ? 164.417 188.547 72.719  1.00 80.34  ? 297  GLU A CD    1 
ATOM   10838 O  OE1   . GLU D 3 297 ? 163.742 189.469 72.214  1.00 80.39  ? 297  GLU A OE1   1 
ATOM   10839 O  OE2   . GLU D 3 297 ? 165.327 188.745 73.551  1.00 79.95  ? 297  GLU A OE2   1 
ATOM   10840 N  N     . PRO D 3 298 ? 162.956 183.983 72.726  1.00 64.26  ? 298  PRO A N     1 
ATOM   10841 C  CA    . PRO D 3 298 ? 162.547 183.217 73.915  1.00 62.18  ? 298  PRO A CA    1 
ATOM   10842 C  C     . PRO D 3 298 ? 162.196 184.077 75.115  1.00 59.93  ? 298  PRO A C     1 
ATOM   10843 O  O     . PRO D 3 298 ? 161.326 183.685 75.902  1.00 65.04  ? 298  PRO A O     1 
ATOM   10844 C  CB    . PRO D 3 298 ? 163.769 182.333 74.199  1.00 66.05  ? 298  PRO A CB    1 
ATOM   10845 C  CG    . PRO D 3 298 ? 164.906 183.026 73.528  1.00 70.63  ? 298  PRO A CG    1 
ATOM   10846 C  CD    . PRO D 3 298 ? 164.320 183.639 72.296  1.00 64.63  ? 298  PRO A CD    1 
ATOM   10847 N  N     . ALA D 3 299 ? 162.838 185.231 75.288  1.00 53.10  ? 299  ALA A N     1 
ATOM   10848 C  CA    . ALA D 3 299 ? 162.529 186.096 76.418  1.00 57.82  ? 299  ALA A CA    1 
ATOM   10849 C  C     . ALA D 3 299 ? 161.160 186.753 76.306  1.00 63.02  ? 299  ALA A C     1 
ATOM   10850 O  O     . ALA D 3 299 ? 160.663 187.286 77.303  1.00 65.68  ? 299  ALA A O     1 
ATOM   10851 C  CB    . ALA D 3 299 ? 163.605 187.173 76.565  1.00 61.58  ? 299  ALA A CB    1 
ATOM   10852 N  N     . ASN D 3 300 ? 160.548 186.735 75.125  1.00 63.76  ? 300  ASN A N     1 
ATOM   10853 C  CA    . ASN D 3 300 ? 159.229 187.314 74.912  1.00 57.41  ? 300  ASN A CA    1 
ATOM   10854 C  C     . ASN D 3 300 ? 158.104 186.294 75.009  1.00 60.56  ? 300  ASN A C     1 
ATOM   10855 O  O     . ASN D 3 300 ? 156.949 186.645 74.753  1.00 64.24  ? 300  ASN A O     1 
ATOM   10856 C  CB    . ASN D 3 300 ? 159.170 188.001 73.548  1.00 60.57  ? 300  ASN A CB    1 
ATOM   10857 C  CG    . ASN D 3 300 ? 159.369 189.491 73.641  1.00 65.03  ? 300  ASN A CG    1 
ATOM   10858 O  OD1   . ASN D 3 300 ? 158.407 190.254 73.670  1.00 62.31  ? 300  ASN A OD1   1 
ATOM   10859 N  ND2   . ASN D 3 300 ? 160.624 189.917 73.687  1.00 66.49  ? 300  ASN A ND2   1 
ATOM   10860 N  N     . GLN D 3 301 ? 158.404 185.049 75.361  1.00 59.86  ? 301  GLN A N     1 
ATOM   10861 C  CA    . GLN D 3 301 ? 157.360 184.044 75.477  1.00 60.08  ? 301  GLN A CA    1 
ATOM   10862 C  C     . GLN D 3 301 ? 156.545 184.269 76.742  1.00 66.79  ? 301  GLN A C     1 
ATOM   10863 O  O     . GLN D 3 301 ? 157.071 184.656 77.788  1.00 69.84  ? 301  GLN A O     1 
ATOM   10864 C  CB    . GLN D 3 301 ? 157.962 182.641 75.486  1.00 60.72  ? 301  GLN A CB    1 
ATOM   10865 C  CG    . GLN D 3 301 ? 158.832 182.319 74.280  1.00 67.34  ? 301  GLN A CG    1 
ATOM   10866 C  CD    . GLN D 3 301 ? 158.123 182.547 72.959  1.00 69.90  ? 301  GLN A CD    1 
ATOM   10867 O  OE1   . GLN D 3 301 ? 156.937 182.258 72.819  1.00 73.98  ? 301  GLN A OE1   1 
ATOM   10868 N  NE2   . GLN D 3 301 ? 158.852 183.068 71.981  1.00 62.38  ? 301  GLN A NE2   1 
ATOM   10869 N  N     . MET D 3 302 ? 155.243 184.023 76.638  1.00 71.69  ? 302  MET A N     1 
ATOM   10870 C  CA    . MET D 3 302 ? 154.327 184.182 77.756  1.00 67.24  ? 302  MET A CA    1 
ATOM   10871 C  C     . MET D 3 302 ? 154.190 182.907 78.572  1.00 64.85  ? 302  MET A C     1 
ATOM   10872 O  O     . MET D 3 302 ? 153.334 182.837 79.456  1.00 72.10  ? 302  MET A O     1 
ATOM   10873 C  CB    . MET D 3 302 ? 152.958 184.643 77.257  1.00 68.13  ? 302  MET A CB    1 
ATOM   10874 C  CG    . MET D 3 302 ? 152.923 186.100 76.828  1.00 67.05  ? 302  MET A CG    1 
ATOM   10875 S  SD    . MET D 3 302 ? 151.512 187.006 77.475  1.00 86.77  ? 302  MET A SD    1 
ATOM   10876 C  CE    . MET D 3 302 ? 151.951 188.679 77.013  1.00 70.25  ? 302  MET A CE    1 
ATOM   10877 N  N     . VAL D 3 303 ? 154.995 181.892 78.273  1.00 63.55  ? 303  VAL A N     1 
ATOM   10878 C  CA    . VAL D 3 303 ? 155.108 180.688 79.084  1.00 65.43  ? 303  VAL A CA    1 
ATOM   10879 C  C     . VAL D 3 303 ? 156.584 180.460 79.370  1.00 72.47  ? 303  VAL A C     1 
ATOM   10880 O  O     . VAL D 3 303 ? 157.426 180.600 78.476  1.00 80.06  ? 303  VAL A O     1 
ATOM   10881 C  CB    . VAL D 3 303 ? 154.490 179.457 78.391  1.00 65.78  ? 303  VAL A CB    1 
ATOM   10882 C  CG1   . VAL D 3 303 ? 154.608 178.232 79.278  1.00 65.90  ? 303  VAL A CG1   1 
ATOM   10883 C  CG2   . VAL D 3 303 ? 153.045 179.720 78.047  1.00 68.33  ? 303  VAL A CG2   1 
ATOM   10884 N  N     . LYS D 3 304 ? 156.899 180.109 80.614  1.00 67.22  ? 304  LYS A N     1 
ATOM   10885 C  CA    . LYS D 3 304 ? 158.287 179.994 81.038  1.00 61.61  ? 304  LYS A CA    1 
ATOM   10886 C  C     . LYS D 3 304 ? 158.939 178.736 80.481  1.00 68.77  ? 304  LYS A C     1 
ATOM   10887 O  O     . LYS D 3 304 ? 159.255 177.809 81.233  1.00 76.73  ? 304  LYS A O     1 
ATOM   10888 C  CB    . LYS D 3 304 ? 158.379 180.001 82.563  1.00 68.37  ? 304  LYS A CB    1 
ATOM   10889 C  CG    . LYS D 3 304 ? 158.862 181.313 83.150  1.00 71.14  ? 304  LYS A CG    1 
ATOM   10890 C  CD    . LYS D 3 304 ? 160.284 181.620 82.725  1.00 70.00  ? 304  LYS A CD    1 
ATOM   10891 C  CE    . LYS D 3 304 ? 160.792 182.886 83.391  1.00 68.10  ? 304  LYS A CE    1 
ATOM   10892 N  NZ    . LYS D 3 304 ? 159.971 184.072 83.024  1.00 75.08  ? 304  LYS A NZ    1 
ATOM   10893 N  N     . CYS D 3 305 ? 159.148 178.698 79.169  1.00 68.13  ? 305  CYS A N     1 
ATOM   10894 C  CA    . CYS D 3 305 ? 159.830 177.583 78.528  1.00 66.94  ? 305  CYS A CA    1 
ATOM   10895 C  C     . CYS D 3 305 ? 160.570 178.113 77.314  1.00 71.36  ? 305  CYS A C     1 
ATOM   10896 O  O     . CYS D 3 305 ? 159.989 178.842 76.505  1.00 75.07  ? 305  CYS A O     1 
ATOM   10897 C  CB    . CYS D 3 305 ? 158.846 176.483 78.119  1.00 65.63  ? 305  CYS A CB    1 
ATOM   10898 S  SG    . CYS D 3 305 ? 157.496 177.029 77.054  1.00 80.45  ? 305  CYS A SG    1 
ATOM   10899 N  N     . ASP D 3 306 ? 161.843 177.762 77.194  1.00 80.58  ? 306  ASP A N     1 
ATOM   10900 C  CA    . ASP D 3 306 ? 162.627 178.220 76.058  1.00 77.11  ? 306  ASP A CA    1 
ATOM   10901 C  C     . ASP D 3 306 ? 162.281 177.382 74.836  1.00 75.48  ? 306  ASP A C     1 
ATOM   10902 O  O     . ASP D 3 306 ? 162.478 176.162 74.858  1.00 79.47  ? 306  ASP A O     1 
ATOM   10903 C  CB    . ASP D 3 306 ? 164.117 178.134 76.355  1.00 76.38  ? 306  ASP A CB    1 
ATOM   10904 C  CG    . ASP D 3 306 ? 164.495 176.861 77.077  1.00 82.98  ? 306  ASP A CG    1 
ATOM   10905 O  OD1   . ASP D 3 306 ? 163.583 176.133 77.520  1.00 86.60  ? 306  ASP A OD1   1 
ATOM   10906 O  OD2   . ASP D 3 306 ? 165.707 176.590 77.202  1.00 81.42  ? 306  ASP A OD2   1 
ATOM   10907 N  N     . PRO D 3 307 ? 161.762 177.982 73.764  1.00 63.38  ? 307  PRO A N     1 
ATOM   10908 C  CA    . PRO D 3 307 ? 161.459 177.196 72.561  1.00 67.20  ? 307  PRO A CA    1 
ATOM   10909 C  C     . PRO D 3 307 ? 162.690 176.601 71.909  1.00 70.41  ? 307  PRO A C     1 
ATOM   10910 O  O     . PRO D 3 307 ? 162.558 175.691 71.082  1.00 76.49  ? 307  PRO A O     1 
ATOM   10911 C  CB    . PRO D 3 307 ? 160.770 178.211 71.642  1.00 66.89  ? 307  PRO A CB    1 
ATOM   10912 C  CG    . PRO D 3 307 ? 161.209 179.542 72.146  1.00 66.41  ? 307  PRO A CG    1 
ATOM   10913 C  CD    . PRO D 3 307 ? 161.367 179.390 73.621  1.00 64.61  ? 307  PRO A CD    1 
ATOM   10914 N  N     . ARG D 3 308 ? 163.883 177.090 72.250  1.00 64.52  ? 308  ARG A N     1 
ATOM   10915 C  CA    . ARG D 3 308 ? 165.109 176.511 71.721  1.00 59.46  ? 308  ARG A CA    1 
ATOM   10916 C  C     . ARG D 3 308 ? 165.293 175.065 72.157  1.00 65.32  ? 308  ARG A C     1 
ATOM   10917 O  O     . ARG D 3 308 ? 166.021 174.317 71.495  1.00 70.32  ? 308  ARG A O     1 
ATOM   10918 C  CB    . ARG D 3 308 ? 166.304 177.355 72.157  1.00 61.49  ? 308  ARG A CB    1 
ATOM   10919 C  CG    . ARG D 3 308 ? 166.231 178.795 71.684  1.00 65.67  ? 308  ARG A CG    1 
ATOM   10920 C  CD    . ARG D 3 308 ? 167.420 179.605 72.164  1.00 67.29  ? 308  ARG A CD    1 
ATOM   10921 N  NE    . ARG D 3 308 ? 167.469 179.688 73.618  1.00 69.99  ? 308  ARG A NE    1 
ATOM   10922 C  CZ    . ARG D 3 308 ? 168.393 180.352 74.299  1.00 69.94  ? 308  ARG A CZ    1 
ATOM   10923 N  NH1   . ARG D 3 308 ? 169.366 181.005 73.686  1.00 69.56  ? 308  ARG A NH1   1 
ATOM   10924 N  NH2   . ARG D 3 308 ? 168.339 180.361 75.628  1.00 69.71  ? 308  ARG A NH2   1 
ATOM   10925 N  N     . HIS D 3 309 ? 164.657 174.656 73.251  1.00 68.74  ? 309  HIS A N     1 
ATOM   10926 C  CA    . HIS D 3 309 ? 164.709 173.272 73.719  1.00 66.78  ? 309  HIS A CA    1 
ATOM   10927 C  C     . HIS D 3 309 ? 163.559 172.451 73.151  1.00 65.21  ? 309  HIS A C     1 
ATOM   10928 O  O     . HIS D 3 309 ? 162.833 171.772 73.872  1.00 70.70  ? 309  HIS A O     1 
ATOM   10929 C  CB    . HIS D 3 309 ? 164.702 173.240 75.241  1.00 67.73  ? 309  HIS A CB    1 
ATOM   10930 C  CG    . HIS D 3 309 ? 166.035 173.523 75.856  1.00 72.42  ? 309  HIS A CG    1 
ATOM   10931 N  ND1   . HIS D 3 309 ? 166.182 173.900 77.173  1.00 72.93  ? 309  HIS A ND1   1 
ATOM   10932 C  CD2   . HIS D 3 309 ? 167.285 173.480 75.335  1.00 71.33  ? 309  HIS A CD2   1 
ATOM   10933 C  CE1   . HIS D 3 309 ? 167.464 174.079 77.437  1.00 72.21  ? 309  HIS A CE1   1 
ATOM   10934 N  NE2   . HIS D 3 309 ? 168.154 173.831 76.339  1.00 72.12  ? 309  HIS A NE2   1 
ATOM   10935 N  N     . GLY D 3 310 ? 163.399 172.504 71.837  1.00 56.02  ? 310  GLY A N     1 
ATOM   10936 C  CA    . GLY D 3 310 ? 162.306 171.812 71.189  1.00 55.03  ? 310  GLY A CA    1 
ATOM   10937 C  C     . GLY D 3 310 ? 162.171 172.268 69.755  1.00 58.87  ? 310  GLY A C     1 
ATOM   10938 O  O     . GLY D 3 310 ? 162.977 173.052 69.245  1.00 62.18  ? 310  GLY A O     1 
ATOM   10939 N  N     . LYS D 3 311 ? 161.126 171.763 69.111  1.00 55.06  ? 311  LYS A N     1 
ATOM   10940 C  CA    . LYS D 3 311 ? 160.875 172.038 67.706  1.00 55.21  ? 311  LYS A CA    1 
ATOM   10941 C  C     . LYS D 3 311 ? 159.463 172.567 67.517  1.00 55.90  ? 311  LYS A C     1 
ATOM   10942 O  O     . LYS D 3 311 ? 158.506 172.023 68.076  1.00 64.16  ? 311  LYS A O     1 
ATOM   10943 C  CB    . LYS D 3 311 ? 161.078 170.783 66.853  1.00 58.60  ? 311  LYS A CB    1 
ATOM   10944 C  CG    . LYS D 3 311 ? 162.450 170.150 66.999  1.00 57.00  ? 311  LYS A CG    1 
ATOM   10945 C  CD    . LYS D 3 311 ? 162.609 168.967 66.064  1.00 57.99  ? 311  LYS A CD    1 
ATOM   10946 C  CE    . LYS D 3 311 ? 163.986 168.356 66.195  1.00 55.39  ? 311  LYS A CE    1 
ATOM   10947 N  NZ    . LYS D 3 311 ? 165.051 169.364 65.949  1.00 56.36  ? 311  LYS A NZ    1 
ATOM   10948 N  N     . TYR D 3 312 ? 159.340 173.628 66.725  1.00 58.55  ? 312  TYR A N     1 
ATOM   10949 C  CA    . TYR D 3 312 ? 158.032 174.179 66.401  1.00 55.49  ? 312  TYR A CA    1 
ATOM   10950 C  C     . TYR D 3 312 ? 157.295 173.248 65.448  1.00 56.52  ? 312  TYR A C     1 
ATOM   10951 O  O     . TYR D 3 312 ? 157.870 172.765 64.468  1.00 65.53  ? 312  TYR A O     1 
ATOM   10952 C  CB    . TYR D 3 312 ? 158.174 175.558 65.762  1.00 54.16  ? 312  TYR A CB    1 
ATOM   10953 C  CG    . TYR D 3 312 ? 158.534 176.683 66.703  1.00 52.59  ? 312  TYR A CG    1 
ATOM   10954 C  CD1   . TYR D 3 312 ? 159.834 176.858 67.143  1.00 55.25  ? 312  TYR A CD1   1 
ATOM   10955 C  CD2   . TYR D 3 312 ? 157.578 177.590 67.124  1.00 55.43  ? 312  TYR A CD2   1 
ATOM   10956 C  CE1   . TYR D 3 312 ? 160.166 177.890 67.990  1.00 52.17  ? 312  TYR A CE1   1 
ATOM   10957 C  CE2   . TYR D 3 312 ? 157.901 178.624 67.970  1.00 55.81  ? 312  TYR A CE2   1 
ATOM   10958 C  CZ    . TYR D 3 312 ? 159.195 178.771 68.398  1.00 54.80  ? 312  TYR A CZ    1 
ATOM   10959 O  OH    . TYR D 3 312 ? 159.511 179.808 69.242  1.00 62.98  ? 312  TYR A OH    1 
ATOM   10960 N  N     . MET D 3 313 ? 156.019 172.997 65.730  1.00 55.00  ? 313  MET A N     1 
ATOM   10961 C  CA    . MET D 3 313 ? 155.181 172.226 64.819  1.00 52.50  ? 313  MET A CA    1 
ATOM   10962 C  C     . MET D 3 313 ? 154.387 173.146 63.896  1.00 54.92  ? 313  MET A C     1 
ATOM   10963 O  O     . MET D 3 313 ? 154.519 173.076 62.671  1.00 58.84  ? 313  MET A O     1 
ATOM   10964 C  CB    . MET D 3 313 ? 154.234 171.318 65.608  1.00 46.55  ? 313  MET A CB    1 
ATOM   10965 C  CG    . MET D 3 313 ? 154.925 170.318 66.496  1.00 47.63  ? 313  MET A CG    1 
ATOM   10966 S  SD    . MET D 3 313 ? 153.786 169.072 67.112  1.00 54.55  ? 313  MET A SD    1 
ATOM   10967 C  CE    . MET D 3 313 ? 154.228 169.061 68.841  1.00 55.80  ? 313  MET A CE    1 
ATOM   10968 N  N     . ALA D 3 314 ? 153.566 174.015 64.477  1.00 60.52  ? 314  ALA A N     1 
ATOM   10969 C  CA    . ALA D 3 314 ? 152.722 174.927 63.724  1.00 58.92  ? 314  ALA A CA    1 
ATOM   10970 C  C     . ALA D 3 314 ? 152.747 176.290 64.392  1.00 57.75  ? 314  ALA A C     1 
ATOM   10971 O  O     . ALA D 3 314 ? 152.710 176.386 65.620  1.00 63.56  ? 314  ALA A O     1 
ATOM   10972 C  CB    . ALA D 3 314 ? 151.284 174.410 63.634  1.00 61.08  ? 314  ALA A CB    1 
ATOM   10973 N  N     . CYS D 3 315 ? 152.809 177.340 63.580  1.00 55.56  ? 315  CYS A N     1 
ATOM   10974 C  CA    . CYS D 3 315 ? 152.927 178.697 64.087  1.00 54.07  ? 315  CYS A CA    1 
ATOM   10975 C  C     . CYS D 3 315 ? 152.067 179.620 63.244  1.00 58.37  ? 315  CYS A C     1 
ATOM   10976 O  O     . CYS D 3 315 ? 152.343 179.809 62.057  1.00 65.25  ? 315  CYS A O     1 
ATOM   10977 C  CB    . CYS D 3 315 ? 154.384 179.165 64.064  1.00 57.01  ? 315  CYS A CB    1 
ATOM   10978 S  SG    . CYS D 3 315 ? 154.598 180.943 64.277  1.00 82.70  ? 315  CYS A SG    1 
ATOM   10979 N  N     . CYS D 3 316 ? 151.034 180.196 63.851  1.00 57.56  ? 316  CYS A N     1 
ATOM   10980 C  CA    . CYS D 3 316 ? 150.133 181.098 63.151  1.00 56.72  ? 316  CYS A CA    1 
ATOM   10981 C  C     . CYS D 3 316 ? 150.362 182.527 63.618  1.00 53.18  ? 316  CYS A C     1 
ATOM   10982 O  O     . CYS D 3 316 ? 150.396 182.801 64.821  1.00 58.73  ? 316  CYS A O     1 
ATOM   10983 C  CB    . CYS D 3 316 ? 148.666 180.698 63.348  1.00 56.23  ? 316  CYS A CB    1 
ATOM   10984 S  SG    . CYS D 3 316 ? 148.023 180.831 65.019  1.00 80.93  ? 316  CYS A SG    1 
ATOM   10985 N  N     . LEU D 3 317 ? 150.537 183.428 62.659  1.00 48.83  ? 317  LEU A N     1 
ATOM   10986 C  CA    . LEU D 3 317 ? 150.787 184.836 62.924  1.00 49.46  ? 317  LEU A CA    1 
ATOM   10987 C  C     . LEU D 3 317 ? 149.541 185.645 62.599  1.00 56.11  ? 317  LEU A C     1 
ATOM   10988 O  O     . LEU D 3 317 ? 148.968 185.510 61.514  1.00 64.64  ? 317  LEU A O     1 
ATOM   10989 C  CB    . LEU D 3 317 ? 151.969 185.349 62.101  1.00 48.88  ? 317  LEU A CB    1 
ATOM   10990 C  CG    . LEU D 3 317 ? 153.297 184.616 62.267  1.00 49.88  ? 317  LEU A CG    1 
ATOM   10991 C  CD1   . LEU D 3 317 ? 154.417 185.425 61.668  1.00 50.78  ? 317  LEU A CD1   1 
ATOM   10992 C  CD2   . LEU D 3 317 ? 153.570 184.356 63.720  1.00 57.16  ? 317  LEU A CD2   1 
ATOM   10993 N  N     . LEU D 3 318 ? 149.121 186.482 63.542  1.00 49.65  ? 318  LEU A N     1 
ATOM   10994 C  CA    . LEU D 3 318 ? 147.939 187.322 63.373  1.00 47.34  ? 318  LEU A CA    1 
ATOM   10995 C  C     . LEU D 3 318 ? 148.373 188.778 63.461  1.00 47.95  ? 318  LEU A C     1 
ATOM   10996 O  O     . LEU D 3 318 ? 148.394 189.369 64.543  1.00 58.02  ? 318  LEU A O     1 
ATOM   10997 C  CB    . LEU D 3 318 ? 146.878 186.993 64.401  1.00 49.39  ? 318  LEU A CB    1 
ATOM   10998 C  CG    . LEU D 3 318 ? 146.204 185.635 64.242  1.00 46.56  ? 318  LEU A CG    1 
ATOM   10999 C  CD1   . LEU D 3 318 ? 146.621 184.694 65.348  1.00 46.37  ? 318  LEU A CD1   1 
ATOM   11000 C  CD2   . LEU D 3 318 ? 144.700 185.810 64.213  1.00 49.06  ? 318  LEU A CD2   1 
ATOM   11001 N  N     . TYR D 3 319 ? 148.716 189.355 62.316  1.00 45.41  ? 319  TYR A N     1 
ATOM   11002 C  CA    . TYR D 3 319 ? 149.127 190.747 62.269  1.00 48.84  ? 319  TYR A CA    1 
ATOM   11003 C  C     . TYR D 3 319 ? 147.912 191.660 62.326  1.00 47.89  ? 319  TYR A C     1 
ATOM   11004 O  O     . TYR D 3 319 ? 146.802 191.282 61.944  1.00 53.46  ? 319  TYR A O     1 
ATOM   11005 C  CB    . TYR D 3 319 ? 149.926 191.031 61.000  1.00 48.57  ? 319  TYR A CB    1 
ATOM   11006 C  CG    . TYR D 3 319 ? 151.291 190.393 60.972  1.00 42.15  ? 319  TYR A CG    1 
ATOM   11007 C  CD1   . TYR D 3 319 ? 151.465 189.112 60.482  1.00 45.59  ? 319  TYR A CD1   1 
ATOM   11008 C  CD2   . TYR D 3 319 ? 152.406 191.073 61.430  1.00 43.97  ? 319  TYR A CD2   1 
ATOM   11009 C  CE1   . TYR D 3 319 ? 152.705 188.526 60.449  1.00 46.97  ? 319  TYR A CE1   1 
ATOM   11010 C  CE2   . TYR D 3 319 ? 153.650 190.493 61.399  1.00 45.99  ? 319  TYR A CE2   1 
ATOM   11011 C  CZ    . TYR D 3 319 ? 153.794 189.219 60.904  1.00 50.20  ? 319  TYR A CZ    1 
ATOM   11012 O  OH    . TYR D 3 319 ? 155.036 188.632 60.873  1.00 59.64  ? 319  TYR A OH    1 
ATOM   11013 N  N     . ARG D 3 320 ? 148.132 192.875 62.814  1.00 40.14  ? 320  ARG A N     1 
ATOM   11014 C  CA    . ARG D 3 320 ? 147.082 193.869 62.928  1.00 34.43  ? 320  ARG A CA    1 
ATOM   11015 C  C     . ARG D 3 320 ? 147.613 195.220 62.478  1.00 43.33  ? 320  ARG A C     1 
ATOM   11016 O  O     . ARG D 3 320 ? 148.819 195.473 62.498  1.00 57.43  ? 320  ARG A O     1 
ATOM   11017 C  CB    . ARG D 3 320 ? 146.558 193.972 64.363  1.00 50.79  ? 320  ARG A CB    1 
ATOM   11018 C  CG    . ARG D 3 320 ? 146.036 192.671 64.933  1.00 56.90  ? 320  ARG A CG    1 
ATOM   11019 C  CD    . ARG D 3 320 ? 145.415 192.886 66.299  1.00 58.71  ? 320  ARG A CD    1 
ATOM   11020 N  NE    . ARG D 3 320 ? 144.350 193.878 66.251  1.00 59.68  ? 320  ARG A NE    1 
ATOM   11021 C  CZ    . ARG D 3 320 ? 143.704 194.339 67.312  1.00 52.31  ? 320  ARG A CZ    1 
ATOM   11022 N  NH1   . ARG D 3 320 ? 143.989 193.915 68.531  1.00 51.45  ? 320  ARG A NH1   1 
ATOM   11023 N  NH2   . ARG D 3 320 ? 142.748 195.245 67.146  1.00 48.18  ? 320  ARG A NH2   1 
ATOM   11024 N  N     . GLY D 3 321 ? 146.696 196.088 62.063  1.00 48.76  ? 321  GLY A N     1 
ATOM   11025 C  CA    . GLY D 3 321 ? 147.073 197.436 61.688  1.00 55.09  ? 321  GLY A CA    1 
ATOM   11026 C  C     . GLY D 3 321 ? 147.662 197.514 60.289  1.00 60.11  ? 321  GLY A C     1 
ATOM   11027 O  O     . GLY D 3 321 ? 147.379 196.694 59.416  1.00 63.87  ? 321  GLY A O     1 
ATOM   11028 N  N     . ASP D 3 322 ? 148.503 198.527 60.085  1.00 62.80  ? 322  ASP A N     1 
ATOM   11029 C  CA    . ASP D 3 322 ? 149.138 198.755 58.794  1.00 61.95  ? 322  ASP A CA    1 
ATOM   11030 C  C     . ASP D 3 322 ? 150.207 197.704 58.541  1.00 59.21  ? 322  ASP A C     1 
ATOM   11031 O  O     . ASP D 3 322 ? 151.364 197.879 58.933  1.00 64.89  ? 322  ASP A O     1 
ATOM   11032 C  CB    . ASP D 3 322 ? 149.743 200.160 58.740  1.00 65.53  ? 322  ASP A CB    1 
ATOM   11033 C  CG    . ASP D 3 322 ? 150.044 200.618 57.325  1.00 72.97  ? 322  ASP A CG    1 
ATOM   11034 O  OD1   . ASP D 3 322 ? 150.543 199.806 56.519  1.00 74.60  ? 322  ASP A OD1   1 
ATOM   11035 O  OD2   . ASP D 3 322 ? 149.783 201.801 57.019  1.00 71.89  ? 322  ASP A OD2   1 
ATOM   11036 N  N     . VAL D 3 323 ? 149.829 196.609 57.891  1.00 52.54  ? 323  VAL A N     1 
ATOM   11037 C  CA    . VAL D 3 323 ? 150.743 195.520 57.577  1.00 55.69  ? 323  VAL A CA    1 
ATOM   11038 C  C     . VAL D 3 323 ? 150.532 195.124 56.124  1.00 61.23  ? 323  VAL A C     1 
ATOM   11039 O  O     . VAL D 3 323 ? 149.395 194.890 55.700  1.00 62.58  ? 323  VAL A O     1 
ATOM   11040 C  CB    . VAL D 3 323 ? 150.532 194.310 58.505  1.00 58.42  ? 323  VAL A CB    1 
ATOM   11041 C  CG1   . VAL D 3 323 ? 151.438 193.172 58.098  1.00 60.13  ? 323  VAL A CG1   1 
ATOM   11042 C  CG2   . VAL D 3 323 ? 150.780 194.694 59.952  1.00 57.42  ? 323  VAL A CG2   1 
ATOM   11043 N  N     . VAL D 3 324 ? 151.620 195.049 55.365  1.00 66.39  ? 324  VAL A N     1 
ATOM   11044 C  CA    . VAL D 3 324 ? 151.561 194.685 53.953  1.00 60.96  ? 324  VAL A CA    1 
ATOM   11045 C  C     . VAL D 3 324 ? 152.043 193.245 53.814  1.00 65.71  ? 324  VAL A C     1 
ATOM   11046 O  O     . VAL D 3 324 ? 153.020 192.857 54.472  1.00 76.61  ? 324  VAL A O     1 
ATOM   11047 C  CB    . VAL D 3 324 ? 152.394 195.649 53.094  1.00 65.21  ? 324  VAL A CB    1 
ATOM   11048 C  CG1   . VAL D 3 324 ? 151.937 195.612 51.646  1.00 66.37  ? 324  VAL A CG1   1 
ATOM   11049 C  CG2   . VAL D 3 324 ? 152.302 197.059 53.647  1.00 67.80  ? 324  VAL A CG2   1 
ATOM   11050 N  N     . PRO D 3 325 ? 151.388 192.420 52.994  1.00 60.09  ? 325  PRO A N     1 
ATOM   11051 C  CA    . PRO D 3 325 ? 151.788 191.006 52.898  1.00 65.10  ? 325  PRO A CA    1 
ATOM   11052 C  C     . PRO D 3 325 ? 153.224 190.783 52.451  1.00 66.65  ? 325  PRO A C     1 
ATOM   11053 O  O     . PRO D 3 325 ? 153.819 189.763 52.818  1.00 69.99  ? 325  PRO A O     1 
ATOM   11054 C  CB    . PRO D 3 325 ? 150.790 190.438 51.882  1.00 67.23  ? 325  PRO A CB    1 
ATOM   11055 C  CG    . PRO D 3 325 ? 149.589 191.301 52.031  1.00 67.75  ? 325  PRO A CG    1 
ATOM   11056 C  CD    . PRO D 3 325 ? 150.108 192.679 52.315  1.00 63.41  ? 325  PRO A CD    1 
ATOM   11057 N  N     . LYS D 3 326 ? 153.798 191.689 51.657  1.00 59.22  ? 326  LYS A N     1 
ATOM   11058 C  CA    . LYS D 3 326 ? 155.190 191.528 51.247  1.00 60.43  ? 326  LYS A CA    1 
ATOM   11059 C  C     . LYS D 3 326 ? 156.125 191.585 52.450  1.00 63.65  ? 326  LYS A C     1 
ATOM   11060 O  O     . LYS D 3 326 ? 157.084 190.806 52.548  1.00 65.62  ? 326  LYS A O     1 
ATOM   11061 C  CB    . LYS D 3 326 ? 155.559 192.592 50.211  1.00 61.25  ? 326  LYS A CB    1 
ATOM   11062 C  CG    . LYS D 3 326 ? 154.937 193.957 50.455  1.00 63.04  ? 326  LYS A CG    1 
ATOM   11063 C  CD    . LYS D 3 326 ? 155.503 195.006 49.502  1.00 69.99  ? 326  LYS A CD    1 
ATOM   11064 C  CE    . LYS D 3 326 ? 154.748 195.049 48.174  1.00 69.59  ? 326  LYS A CE    1 
ATOM   11065 N  NZ    . LYS D 3 326 ? 153.445 195.775 48.250  1.00 56.51  ? 326  LYS A NZ    1 
ATOM   11066 N  N     . ASP D 3 327 ? 155.856 192.501 53.382  1.00 58.34  ? 327  ASP A N     1 
ATOM   11067 C  CA    . ASP D 3 327 ? 156.652 192.575 54.600  1.00 56.03  ? 327  ASP A CA    1 
ATOM   11068 C  C     . ASP D 3 327 ? 156.545 191.285 55.399  1.00 59.92  ? 327  ASP A C     1 
ATOM   11069 O  O     . ASP D 3 327 ? 157.544 190.786 55.933  1.00 68.08  ? 327  ASP A O     1 
ATOM   11070 C  CB    . ASP D 3 327 ? 156.199 193.763 55.447  1.00 61.04  ? 327  ASP A CB    1 
ATOM   11071 C  CG    . ASP D 3 327 ? 156.121 195.048 54.653  1.00 68.29  ? 327  ASP A CG    1 
ATOM   11072 O  OD1   . ASP D 3 327 ? 156.446 195.023 53.448  1.00 69.87  ? 327  ASP A OD1   1 
ATOM   11073 O  OD2   . ASP D 3 327 ? 155.733 196.083 55.233  1.00 68.57  ? 327  ASP A OD2   1 
ATOM   11074 N  N     . VAL D 3 328 ? 155.336 190.732 55.492  1.00 52.83  ? 328  VAL A N     1 
ATOM   11075 C  CA    . VAL D 3 328 ? 155.132 189.487 56.222  1.00 52.97  ? 328  VAL A CA    1 
ATOM   11076 C  C     . VAL D 3 328 ? 155.906 188.353 55.567  1.00 63.07  ? 328  VAL A C     1 
ATOM   11077 O  O     . VAL D 3 328 ? 156.520 187.525 56.249  1.00 68.58  ? 328  VAL A O     1 
ATOM   11078 C  CB    . VAL D 3 328 ? 153.633 189.168 56.317  1.00 53.91  ? 328  VAL A CB    1 
ATOM   11079 C  CG1   . VAL D 3 328 ? 153.426 187.742 56.762  1.00 58.40  ? 328  VAL A CG1   1 
ATOM   11080 C  CG2   . VAL D 3 328 ? 152.966 190.114 57.276  1.00 57.93  ? 328  VAL A CG2   1 
ATOM   11081 N  N     . ASN D 3 329 ? 155.873 188.285 54.235  1.00 58.17  ? 329  ASN A N     1 
ATOM   11082 C  CA    . ASN D 3 329 ? 156.608 187.237 53.533  1.00 48.79  ? 329  ASN A CA    1 
ATOM   11083 C  C     . ASN D 3 329 ? 158.105 187.361 53.773  1.00 50.63  ? 329  ASN A C     1 
ATOM   11084 O  O     . ASN D 3 329 ? 158.791 186.357 53.996  1.00 53.14  ? 329  ASN A O     1 
ATOM   11085 C  CB    . ASN D 3 329 ? 156.295 187.288 52.041  1.00 53.77  ? 329  ASN A CB    1 
ATOM   11086 C  CG    . ASN D 3 329 ? 155.104 186.432 51.670  1.00 61.50  ? 329  ASN A CG    1 
ATOM   11087 O  OD1   . ASN D 3 329 ? 154.409 185.909 52.539  1.00 63.72  ? 329  ASN A OD1   1 
ATOM   11088 N  ND2   . ASN D 3 329 ? 154.862 186.285 50.374  1.00 60.94  ? 329  ASN A ND2   1 
ATOM   11089 N  N     . ALA D 3 330 ? 158.630 188.586 53.736  1.00 47.74  ? 330  ALA A N     1 
ATOM   11090 C  CA    . ALA D 3 330 ? 160.048 188.783 54.019  1.00 47.24  ? 330  ALA A CA    1 
ATOM   11091 C  C     . ALA D 3 330 ? 160.393 188.348 55.437  1.00 51.39  ? 330  ALA A C     1 
ATOM   11092 O  O     . ALA D 3 330 ? 161.417 187.690 55.663  1.00 60.26  ? 330  ALA A O     1 
ATOM   11093 C  CB    . ALA D 3 330 ? 160.430 190.245 53.797  1.00 52.43  ? 330  ALA A CB    1 
ATOM   11094 N  N     . ALA D 3 331 ? 159.546 188.703 56.406  1.00 47.30  ? 331  ALA A N     1 
ATOM   11095 C  CA    . ALA D 3 331 ? 159.799 188.312 57.789  1.00 47.40  ? 331  ALA A CA    1 
ATOM   11096 C  C     . ALA D 3 331 ? 159.771 186.797 57.953  1.00 49.43  ? 331  ALA A C     1 
ATOM   11097 O  O     . ALA D 3 331 ? 160.616 186.222 58.651  1.00 62.60  ? 331  ALA A O     1 
ATOM   11098 C  CB    . ALA D 3 331 ? 158.779 188.971 58.715  1.00 55.28  ? 331  ALA A CB    1 
ATOM   11099 N  N     . ILE D 3 332 ? 158.806 186.133 57.314  1.00 39.63  ? 332  ILE A N     1 
ATOM   11100 C  CA    . ILE D 3 332 ? 158.706 184.680 57.409  1.00 46.36  ? 332  ILE A CA    1 
ATOM   11101 C  C     . ILE D 3 332 ? 159.922 184.020 56.773  1.00 55.60  ? 332  ILE A C     1 
ATOM   11102 O  O     . ILE D 3 332 ? 160.450 183.029 57.290  1.00 57.30  ? 332  ILE A O     1 
ATOM   11103 C  CB    . ILE D 3 332 ? 157.390 184.191 56.776  1.00 49.40  ? 332  ILE A CB    1 
ATOM   11104 C  CG1   . ILE D 3 332 ? 156.306 184.044 57.840  1.00 43.75  ? 332  ILE A CG1   1 
ATOM   11105 C  CG2   . ILE D 3 332 ? 157.586 182.869 56.045  1.00 52.90  ? 332  ILE A CG2   1 
ATOM   11106 C  CD1   . ILE D 3 332 ? 155.909 185.337 58.482  1.00 48.44  ? 332  ILE A CD1   1 
ATOM   11107 N  N     . ALA D 3 333 ? 160.386 184.555 55.641  1.00 52.62  ? 333  ALA A N     1 
ATOM   11108 C  CA    . ALA D 3 333 ? 161.581 184.008 55.009  1.00 47.13  ? 333  ALA A CA    1 
ATOM   11109 C  C     . ALA D 3 333 ? 162.801 184.169 55.904  1.00 44.32  ? 333  ALA A C     1 
ATOM   11110 O  O     . ALA D 3 333 ? 163.612 183.244 56.035  1.00 54.32  ? 333  ALA A O     1 
ATOM   11111 C  CB    . ALA D 3 333 ? 161.813 184.680 53.656  1.00 51.07  ? 333  ALA A CB    1 
ATOM   11112 N  N     . THR D 3 334 ? 162.949 185.338 56.533  1.00 42.32  ? 334  THR A N     1 
ATOM   11113 C  CA    . THR D 3 334 ? 164.078 185.544 57.433  1.00 44.55  ? 334  THR A CA    1 
ATOM   11114 C  C     . THR D 3 334 ? 164.016 184.589 58.616  1.00 49.11  ? 334  THR A C     1 
ATOM   11115 O  O     . THR D 3 334 ? 165.048 184.072 59.059  1.00 59.53  ? 334  THR A O     1 
ATOM   11116 C  CB    . THR D 3 334 ? 164.122 186.990 57.922  1.00 47.30  ? 334  THR A CB    1 
ATOM   11117 O  OG1   . THR D 3 334 ? 162.853 187.350 58.478  1.00 54.64  ? 334  THR A OG1   1 
ATOM   11118 C  CG2   . THR D 3 334 ? 164.458 187.931 56.778  1.00 48.58  ? 334  THR A CG2   1 
ATOM   11119 N  N     . ILE D 3 335 ? 162.817 184.348 59.147  1.00 44.18  ? 335  ILE A N     1 
ATOM   11120 C  CA    . ILE D 3 335 ? 162.679 183.405 60.253  1.00 45.96  ? 335  ILE A CA    1 
ATOM   11121 C  C     . ILE D 3 335 ? 163.046 181.997 59.802  1.00 42.89  ? 335  ILE A C     1 
ATOM   11122 O  O     . ILE D 3 335 ? 163.781 181.282 60.492  1.00 54.29  ? 335  ILE A O     1 
ATOM   11123 C  CB    . ILE D 3 335 ? 161.257 183.465 60.835  1.00 52.22  ? 335  ILE A CB    1 
ATOM   11124 C  CG1   . ILE D 3 335 ? 161.052 184.774 61.594  1.00 53.68  ? 335  ILE A CG1   1 
ATOM   11125 C  CG2   . ILE D 3 335 ? 161.009 182.286 61.754  1.00 54.93  ? 335  ILE A CG2   1 
ATOM   11126 C  CD1   . ILE D 3 335 ? 161.968 184.936 62.779  1.00 56.60  ? 335  ILE A CD1   1 
ATOM   11127 N  N     . LYS D 3 336 ? 162.561 181.586 58.631  1.00 48.30  ? 336  LYS A N     1 
ATOM   11128 C  CA    . LYS D 3 336 ? 162.819 180.232 58.152  1.00 54.26  ? 336  LYS A CA    1 
ATOM   11129 C  C     . LYS D 3 336 ? 164.300 180.011 57.869  1.00 54.12  ? 336  LYS A C     1 
ATOM   11130 O  O     . LYS D 3 336 ? 164.816 178.904 58.062  1.00 57.16  ? 336  LYS A O     1 
ATOM   11131 C  CB    . LYS D 3 336 ? 161.991 179.957 56.899  1.00 58.92  ? 336  LYS A CB    1 
ATOM   11132 C  CG    . LYS D 3 336 ? 161.876 178.490 56.541  1.00 60.47  ? 336  LYS A CG    1 
ATOM   11133 C  CD    . LYS D 3 336 ? 160.721 177.843 57.281  1.00 62.15  ? 336  LYS A CD    1 
ATOM   11134 C  CE    . LYS D 3 336 ? 159.391 178.396 56.801  1.00 62.05  ? 336  LYS A CE    1 
ATOM   11135 N  NZ    . LYS D 3 336 ? 159.203 178.198 55.339  1.00 53.57  ? 336  LYS A NZ    1 
ATOM   11136 N  N     . THR D 3 337 ? 165.000 181.046 57.399  1.00 60.47  ? 337  THR A N     1 
ATOM   11137 C  CA    . THR D 3 337 ? 166.426 180.897 57.125  1.00 56.96  ? 337  THR A CA    1 
ATOM   11138 C  C     . THR D 3 337 ? 167.244 180.791 58.404  1.00 55.07  ? 337  THR A C     1 
ATOM   11139 O  O     . THR D 3 337 ? 168.367 180.278 58.377  1.00 59.40  ? 337  THR A O     1 
ATOM   11140 C  CB    . THR D 3 337 ? 166.931 182.067 56.281  1.00 64.86  ? 337  THR A CB    1 
ATOM   11141 O  OG1   . THR D 3 337 ? 166.537 183.303 56.890  1.00 66.84  ? 337  THR A OG1   1 
ATOM   11142 C  CG2   . THR D 3 337 ? 166.365 181.993 54.871  1.00 66.45  ? 337  THR A CG2   1 
ATOM   11143 N  N     . LYS D 3 338 ? 166.712 181.271 59.524  1.00 66.02  ? 338  LYS A N     1 
ATOM   11144 C  CA    . LYS D 3 338 ? 167.467 181.268 60.769  1.00 65.43  ? 338  LYS A CA    1 
ATOM   11145 C  C     . LYS D 3 338 ? 167.607 179.851 61.311  1.00 70.13  ? 338  LYS A C     1 
ATOM   11146 O  O     . LYS D 3 338 ? 166.686 179.036 61.215  1.00 72.23  ? 338  LYS A O     1 
ATOM   11147 C  CB    . LYS D 3 338 ? 166.782 182.168 61.795  1.00 65.62  ? 338  LYS A CB    1 
ATOM   11148 C  CG    . LYS D 3 338 ? 167.641 182.520 62.988  1.00 72.61  ? 338  LYS A CG    1 
ATOM   11149 C  CD    . LYS D 3 338 ? 166.980 183.600 63.822  1.00 74.88  ? 338  LYS A CD    1 
ATOM   11150 C  CE    . LYS D 3 338 ? 166.678 184.828 62.981  1.00 71.54  ? 338  LYS A CE    1 
ATOM   11151 N  NZ    . LYS D 3 338 ? 167.900 185.360 62.318  1.00 75.07  ? 338  LYS A NZ    1 
ATOM   11152 N  N     . ARG D 3 339 ? 168.772 179.561 61.888  1.00 74.05  ? 339  ARG A N     1 
ATOM   11153 C  CA    . ARG D 3 339 ? 169.089 178.216 62.352  1.00 71.51  ? 339  ARG A CA    1 
ATOM   11154 C  C     . ARG D 3 339 ? 168.670 177.971 63.797  1.00 70.81  ? 339  ARG A C     1 
ATOM   11155 O  O     . ARG D 3 339 ? 168.425 176.822 64.178  1.00 68.67  ? 339  ARG A O     1 
ATOM   11156 C  CB    . ARG D 3 339 ? 170.589 177.951 62.198  1.00 73.54  ? 339  ARG A CB    1 
ATOM   11157 C  CG    . ARG D 3 339 ? 171.064 177.914 60.755  1.00 75.60  ? 339  ARG A CG    1 
ATOM   11158 C  CD    . ARG D 3 339 ? 172.574 177.762 60.671  1.00 77.29  ? 339  ARG A CD    1 
ATOM   11159 N  NE    . ARG D 3 339 ? 173.030 176.492 61.224  1.00 81.49  ? 339  ARG A NE    1 
ATOM   11160 C  CZ    . ARG D 3 339 ? 174.297 176.202 61.485  1.00 79.55  ? 339  ARG A CZ    1 
ATOM   11161 N  NH1   . ARG D 3 339 ? 175.267 177.072 61.256  1.00 75.78  ? 339  ARG A NH1   1 
ATOM   11162 N  NH2   . ARG D 3 339 ? 174.599 175.008 61.987  1.00 75.36  ? 339  ARG A NH2   1 
ATOM   11163 N  N     . SER D 3 340 ? 168.594 179.024 64.613  1.00 74.18  ? 340  SER A N     1 
ATOM   11164 C  CA    . SER D 3 340 ? 168.215 178.852 66.013  1.00 72.38  ? 340  SER A CA    1 
ATOM   11165 C  C     . SER D 3 340 ? 166.794 178.317 66.137  1.00 74.32  ? 340  SER A C     1 
ATOM   11166 O  O     . SER D 3 340 ? 166.526 177.418 66.942  1.00 74.40  ? 340  SER A O     1 
ATOM   11167 C  CB    . SER D 3 340 ? 168.344 180.174 66.772  1.00 30.00  ? 340  SER A CB    1 
ATOM   11168 O  OG    . SER D 3 340 ? 167.442 181.143 66.266  1.00 30.00  ? 340  SER A OG    1 
ATOM   11169 N  N     . ILE D 3 341 ? 165.865 178.861 65.351  1.00 69.58  ? 341  ILE A N     1 
ATOM   11170 C  CA    . ILE D 3 341 ? 164.505 178.335 65.311  1.00 62.25  ? 341  ILE A CA    1 
ATOM   11171 C  C     . ILE D 3 341 ? 164.553 176.975 64.629  1.00 64.25  ? 341  ILE A C     1 
ATOM   11172 O  O     . ILE D 3 341 ? 165.240 176.799 63.617  1.00 69.45  ? 341  ILE A O     1 
ATOM   11173 C  CB    . ILE D 3 341 ? 163.530 179.294 64.600  1.00 59.07  ? 341  ILE A CB    1 
ATOM   11174 C  CG1   . ILE D 3 341 ? 163.877 179.440 63.120  1.00 64.32  ? 341  ILE A CG1   1 
ATOM   11175 C  CG2   . ILE D 3 341 ? 163.536 180.655 65.265  1.00 64.30  ? 341  ILE A CG2   1 
ATOM   11176 C  CD1   . ILE D 3 341 ? 162.895 178.748 62.194  1.00 64.92  ? 341  ILE A CD1   1 
ATOM   11177 N  N     . GLN D 3 342 ? 163.858 175.996 65.192  1.00 57.35  ? 342  GLN A N     1 
ATOM   11178 C  CA    . GLN D 3 342 ? 163.876 174.639 64.667  1.00 57.98  ? 342  GLN A CA    1 
ATOM   11179 C  C     . GLN D 3 342 ? 162.450 174.176 64.409  1.00 58.81  ? 342  GLN A C     1 
ATOM   11180 O  O     . GLN D 3 342 ? 161.669 174.002 65.349  1.00 63.17  ? 342  GLN A O     1 
ATOM   11181 C  CB    . GLN D 3 342 ? 164.586 173.690 65.629  1.00 60.66  ? 342  GLN A CB    1 
ATOM   11182 C  CG    . GLN D 3 342 ? 166.086 173.640 65.433  1.00 60.71  ? 342  GLN A CG    1 
ATOM   11183 C  CD    . GLN D 3 342 ? 166.481 172.848 64.209  1.00 65.03  ? 342  GLN A CD    1 
ATOM   11184 O  OE1   . GLN D 3 342 ? 165.720 172.012 63.724  1.00 65.93  ? 342  GLN A OE1   1 
ATOM   11185 N  NE2   . GLN D 3 342 ? 167.678 173.108 63.698  1.00 64.82  ? 342  GLN A NE2   1 
ATOM   11186 N  N     . PHE D 3 343 ? 162.118 173.983 63.141  1.00 55.07  ? 343  PHE A N     1 
ATOM   11187 C  CA    . PHE D 3 343 ? 160.832 173.442 62.740  1.00 51.60  ? 343  PHE A CA    1 
ATOM   11188 C  C     . PHE D 3 343 ? 160.959 171.945 62.509  1.00 54.88  ? 343  PHE A C     1 
ATOM   11189 O  O     . PHE D 3 343 ? 161.994 171.454 62.052  1.00 61.34  ? 343  PHE A O     1 
ATOM   11190 C  CB    . PHE D 3 343 ? 160.323 174.125 61.471  1.00 52.63  ? 343  PHE A CB    1 
ATOM   11191 C  CG    . PHE D 3 343 ? 159.432 175.298 61.731  1.00 54.66  ? 343  PHE A CG    1 
ATOM   11192 C  CD1   . PHE D 3 343 ? 158.063 175.145 61.774  1.00 58.03  ? 343  PHE A CD1   1 
ATOM   11193 C  CD2   . PHE D 3 343 ? 159.965 176.554 61.931  1.00 58.06  ? 343  PHE A CD2   1 
ATOM   11194 C  CE1   . PHE D 3 343 ? 157.241 176.220 62.013  1.00 60.70  ? 343  PHE A CE1   1 
ATOM   11195 C  CE2   . PHE D 3 343 ? 159.150 177.635 62.171  1.00 63.12  ? 343  PHE A CE2   1 
ATOM   11196 C  CZ    . PHE D 3 343 ? 157.785 177.468 62.212  1.00 64.12  ? 343  PHE A CZ    1 
ATOM   11197 N  N     . VAL D 3 344 ? 159.892 171.219 62.836  1.00 48.68  ? 344  VAL A N     1 
ATOM   11198 C  CA    . VAL D 3 344 ? 159.922 169.772 62.698  1.00 48.21  ? 344  VAL A CA    1 
ATOM   11199 C  C     . VAL D 3 344 ? 159.954 169.387 61.221  1.00 55.97  ? 344  VAL A C     1 
ATOM   11200 O  O     . VAL D 3 344 ? 159.590 170.164 60.330  1.00 58.80  ? 344  VAL A O     1 
ATOM   11201 C  CB    . VAL D 3 344 ? 158.723 169.140 63.420  1.00 46.51  ? 344  VAL A CB    1 
ATOM   11202 C  CG1   . VAL D 3 344 ? 157.508 169.141 62.518  1.00 54.03  ? 344  VAL A CG1   1 
ATOM   11203 C  CG2   . VAL D 3 344 ? 159.061 167.738 63.894  1.00 51.09  ? 344  VAL A CG2   1 
ATOM   11204 N  N     . ASP D 3 345 ? 160.416 168.162 60.962  1.00 64.11  ? 345  ASP A N     1 
ATOM   11205 C  CA    . ASP D 3 345 ? 160.599 167.709 59.586  1.00 56.40  ? 345  ASP A CA    1 
ATOM   11206 C  C     . ASP D 3 345 ? 159.270 167.542 58.862  1.00 56.97  ? 345  ASP A C     1 
ATOM   11207 O  O     . ASP D 3 345 ? 159.150 167.910 57.688  1.00 63.01  ? 345  ASP A O     1 
ATOM   11208 C  CB    . ASP D 3 345 ? 161.380 166.398 59.566  1.00 58.70  ? 345  ASP A CB    1 
ATOM   11209 C  CG    . ASP D 3 345 ? 160.801 165.362 60.506  1.00 68.62  ? 345  ASP A CG    1 
ATOM   11210 O  OD1   . ASP D 3 345 ? 159.673 164.892 60.253  1.00 68.55  ? 345  ASP A OD1   1 
ATOM   11211 O  OD2   . ASP D 3 345 ? 161.475 165.016 61.498  1.00 70.45  ? 345  ASP A OD2   1 
ATOM   11212 N  N     . TRP D 3 346 ? 158.262 166.994 59.535  1.00 47.52  ? 346  TRP A N     1 
ATOM   11213 C  CA    . TRP D 3 346 ? 157.011 166.660 58.866  1.00 50.16  ? 346  TRP A CA    1 
ATOM   11214 C  C     . TRP D 3 346 ? 156.119 167.869 58.609  1.00 60.86  ? 346  TRP A C     1 
ATOM   11215 O  O     . TRP D 3 346 ? 154.950 167.688 58.255  1.00 66.69  ? 346  TRP A O     1 
ATOM   11216 C  CB    . TRP D 3 346 ? 156.241 165.607 59.669  1.00 48.68  ? 346  TRP A CB    1 
ATOM   11217 C  CG    . TRP D 3 346 ? 156.086 165.910 61.122  1.00 47.47  ? 346  TRP A CG    1 
ATOM   11218 C  CD1   . TRP D 3 346 ? 156.851 165.433 62.140  1.00 52.68  ? 346  TRP A CD1   1 
ATOM   11219 C  CD2   . TRP D 3 346 ? 155.089 166.741 61.726  1.00 52.26  ? 346  TRP A CD2   1 
ATOM   11220 N  NE1   . TRP D 3 346 ? 156.401 165.920 63.340  1.00 47.79  ? 346  TRP A NE1   1 
ATOM   11221 C  CE2   . TRP D 3 346 ? 155.318 166.725 63.113  1.00 51.53  ? 346  TRP A CE2   1 
ATOM   11222 C  CE3   . TRP D 3 346 ? 154.027 167.500 61.227  1.00 57.66  ? 346  TRP A CE3   1 
ATOM   11223 C  CZ2   . TRP D 3 346 ? 154.530 167.440 64.007  1.00 58.12  ? 346  TRP A CZ2   1 
ATOM   11224 C  CZ3   . TRP D 3 346 ? 153.245 168.208 62.117  1.00 60.15  ? 346  TRP A CZ3   1 
ATOM   11225 C  CH2   . TRP D 3 346 ? 153.500 168.174 63.491  1.00 61.80  ? 346  TRP A CH2   1 
ATOM   11226 N  N     . CYS D 3 347 ? 156.630 169.088 58.766  1.00 62.32  ? 347  CYS A N     1 
ATOM   11227 C  CA    . CYS D 3 347 ? 155.875 170.308 58.487  1.00 55.75  ? 347  CYS A CA    1 
ATOM   11228 C  C     . CYS D 3 347 ? 156.720 171.209 57.599  1.00 55.18  ? 347  CYS A C     1 
ATOM   11229 O  O     . CYS D 3 347 ? 157.422 172.103 58.089  1.00 59.96  ? 347  CYS A O     1 
ATOM   11230 C  CB    . CYS D 3 347 ? 155.472 171.019 59.778  1.00 58.60  ? 347  CYS A CB    1 
ATOM   11231 S  SG    . CYS D 3 347 ? 154.180 172.251 59.564  1.00 76.71  ? 347  CYS A SG    1 
ATOM   11232 N  N     . PRO D 3 348 ? 156.690 170.989 56.282  1.00 54.85  ? 348  PRO A N     1 
ATOM   11233 C  CA    . PRO D 3 348 ? 157.443 171.874 55.378  1.00 57.76  ? 348  PRO A CA    1 
ATOM   11234 C  C     . PRO D 3 348 ? 157.014 173.327 55.460  1.00 60.86  ? 348  PRO A C     1 
ATOM   11235 O  O     . PRO D 3 348 ? 157.853 174.227 55.328  1.00 66.38  ? 348  PRO A O     1 
ATOM   11236 C  CB    . PRO D 3 348 ? 157.164 171.275 53.993  1.00 62.06  ? 348  PRO A CB    1 
ATOM   11237 C  CG    . PRO D 3 348 ? 156.752 169.863 54.259  1.00 64.73  ? 348  PRO A CG    1 
ATOM   11238 C  CD    . PRO D 3 348 ? 156.018 169.899 55.559  1.00 62.30  ? 348  PRO A CD    1 
ATOM   11239 N  N     . THR D 3 349 ? 155.729 173.585 55.673  1.00 60.16  ? 349  THR A N     1 
ATOM   11240 C  CA    . THR D 3 349 ? 155.193 174.939 55.793  1.00 60.95  ? 349  THR A CA    1 
ATOM   11241 C  C     . THR D 3 349 ? 154.447 175.025 57.118  1.00 62.84  ? 349  THR A C     1 
ATOM   11242 O  O     . THR D 3 349 ? 153.321 174.532 57.236  1.00 69.90  ? 349  THR A O     1 
ATOM   11243 C  CB    . THR D 3 349 ? 154.274 175.275 54.625  1.00 68.72  ? 349  THR A CB    1 
ATOM   11244 O  OG1   . THR D 3 349 ? 153.169 174.363 54.614  1.00 68.55  ? 349  THR A OG1   1 
ATOM   11245 C  CG2   . THR D 3 349 ? 155.025 175.173 53.304  1.00 67.49  ? 349  THR A CG2   1 
ATOM   11246 N  N     . GLY D 3 350 ? 155.069 175.650 58.112  1.00 64.67  ? 350  GLY A N     1 
ATOM   11247 C  CA    . GLY D 3 350 ? 154.467 175.752 59.426  1.00 68.70  ? 350  GLY A CA    1 
ATOM   11248 C  C     . GLY D 3 350 ? 154.112 177.169 59.817  1.00 69.96  ? 350  GLY A C     1 
ATOM   11249 O  O     . GLY D 3 350 ? 154.232 177.547 60.985  1.00 75.47  ? 350  GLY A O     1 
ATOM   11250 N  N     . PHE D 3 351 ? 153.673 177.964 58.847  1.00 47.31  ? 351  PHE A N     1 
ATOM   11251 C  CA    . PHE D 3 351 ? 153.378 179.369 59.067  1.00 41.68  ? 351  PHE A CA    1 
ATOM   11252 C  C     . PHE D 3 351 ? 152.017 179.705 58.481  1.00 47.73  ? 351  PHE A C     1 
ATOM   11253 O  O     . PHE D 3 351 ? 151.788 179.504 57.284  1.00 57.58  ? 351  PHE A O     1 
ATOM   11254 C  CB    . PHE D 3 351 ? 154.456 180.249 58.437  1.00 44.26  ? 351  PHE A CB    1 
ATOM   11255 C  CG    . PHE D 3 351 ? 155.692 180.378 59.270  1.00 43.26  ? 351  PHE A CG    1 
ATOM   11256 C  CD1   . PHE D 3 351 ? 155.606 180.572 60.633  1.00 47.41  ? 351  PHE A CD1   1 
ATOM   11257 C  CD2   . PHE D 3 351 ? 156.941 180.292 58.690  1.00 50.79  ? 351  PHE A CD2   1 
ATOM   11258 C  CE1   . PHE D 3 351 ? 156.744 180.690 61.399  1.00 50.48  ? 351  PHE A CE1   1 
ATOM   11259 C  CE2   . PHE D 3 351 ? 158.081 180.406 59.451  1.00 53.15  ? 351  PHE A CE2   1 
ATOM   11260 C  CZ    . PHE D 3 351 ? 157.982 180.606 60.807  1.00 53.67  ? 351  PHE A CZ    1 
ATOM   11261 N  N     . LYS D 3 352 ? 151.118 180.213 59.319  1.00 53.22  ? 352  LYS A N     1 
ATOM   11262 C  CA    . LYS D 3 352 ? 149.858 180.776 58.859  1.00 57.14  ? 352  LYS A CA    1 
ATOM   11263 C  C     . LYS D 3 352 ? 149.807 182.245 59.237  1.00 57.09  ? 352  LYS A C     1 
ATOM   11264 O  O     . LYS D 3 352 ? 150.114 182.614 60.374  1.00 64.37  ? 352  LYS A O     1 
ATOM   11265 C  CB    . LYS D 3 352 ? 148.647 180.057 59.442  1.00 57.89  ? 352  LYS A CB    1 
ATOM   11266 C  CG    . LYS D 3 352 ? 147.353 180.543 58.827  1.00 56.89  ? 352  LYS A CG    1 
ATOM   11267 C  CD    . LYS D 3 352 ? 146.138 179.992 59.525  1.00 60.76  ? 352  LYS A CD    1 
ATOM   11268 C  CE    . LYS D 3 352 ? 144.875 180.436 58.808  1.00 63.06  ? 352  LYS A CE    1 
ATOM   11269 N  NZ    . LYS D 3 352 ? 144.775 179.843 57.448  1.00 56.04  ? 352  LYS A NZ    1 
ATOM   11270 N  N     . VAL D 3 353 ? 149.423 183.079 58.282  1.00 44.60  ? 353  VAL A N     1 
ATOM   11271 C  CA    . VAL D 3 353 ? 149.474 184.521 58.454  1.00 47.08  ? 353  VAL A CA    1 
ATOM   11272 C  C     . VAL D 3 353 ? 148.065 185.088 58.391  1.00 51.48  ? 353  VAL A C     1 
ATOM   11273 O  O     . VAL D 3 353 ? 147.230 184.656 57.590  1.00 55.45  ? 353  VAL A O     1 
ATOM   11274 C  CB    . VAL D 3 353 ? 150.392 185.174 57.399  1.00 51.28  ? 353  VAL A CB    1 
ATOM   11275 C  CG1   . VAL D 3 353 ? 151.812 184.687 57.587  1.00 50.90  ? 353  VAL A CG1   1 
ATOM   11276 C  CG2   . VAL D 3 353 ? 149.914 184.846 55.998  1.00 55.28  ? 353  VAL A CG2   1 
ATOM   11277 N  N     . GLY D 3 354 ? 147.798 186.049 59.268  1.00 52.23  ? 354  GLY A N     1 
ATOM   11278 C  CA    . GLY D 3 354 ? 146.530 186.747 59.270  1.00 47.87  ? 354  GLY A CA    1 
ATOM   11279 C  C     . GLY D 3 354 ? 146.728 188.238 59.427  1.00 47.68  ? 354  GLY A C     1 
ATOM   11280 O  O     . GLY D 3 354 ? 147.358 188.684 60.389  1.00 59.29  ? 354  GLY A O     1 
ATOM   11281 N  N     . ILE D 3 355 ? 146.204 189.021 58.491  1.00 38.11  ? 355  ILE A N     1 
ATOM   11282 C  CA    . ILE D 3 355 ? 146.377 190.467 58.482  1.00 36.46  ? 355  ILE A CA    1 
ATOM   11283 C  C     . ILE D 3 355 ? 145.019 191.116 58.690  1.00 45.64  ? 355  ILE A C     1 
ATOM   11284 O  O     . ILE D 3 355 ? 144.009 190.647 58.154  1.00 55.49  ? 355  ILE A O     1 
ATOM   11285 C  CB    . ILE D 3 355 ? 147.025 190.951 57.175  1.00 47.65  ? 355  ILE A CB    1 
ATOM   11286 C  CG1   . ILE D 3 355 ? 148.106 189.974 56.720  1.00 53.98  ? 355  ILE A CG1   1 
ATOM   11287 C  CG2   . ILE D 3 355 ? 147.609 192.334 57.356  1.00 51.47  ? 355  ILE A CG2   1 
ATOM   11288 C  CD1   . ILE D 3 355 ? 149.294 189.908 57.638  1.00 52.81  ? 355  ILE A CD1   1 
ATOM   11289 N  N     . ASN D 3 356 ? 144.989 192.179 59.482  1.00 53.07  ? 356  ASN A N     1 
ATOM   11290 C  CA    . ASN D 3 356 ? 143.763 192.909 59.748  1.00 42.13  ? 356  ASN A CA    1 
ATOM   11291 C  C     . ASN D 3 356 ? 144.059 194.401 59.738  1.00 46.72  ? 356  ASN A C     1 
ATOM   11292 O  O     . ASN D 3 356 ? 145.191 194.825 59.979  1.00 60.77  ? 356  ASN A O     1 
ATOM   11293 C  CB    . ASN D 3 356 ? 143.152 192.489 61.082  1.00 39.42  ? 356  ASN A CB    1 
ATOM   11294 C  CG    . ASN D 3 356 ? 141.682 192.798 61.167  1.00 50.63  ? 356  ASN A CG    1 
ATOM   11295 O  OD1   . ASN D 3 356 ? 141.288 193.910 61.513  1.00 62.78  ? 356  ASN A OD1   1 
ATOM   11296 N  ND2   . ASN D 3 356 ? 140.854 191.815 60.843  1.00 53.63  ? 356  ASN A ND2   1 
ATOM   11297 N  N     . TYR D 3 357 ? 143.032 195.194 59.456  1.00 46.49  ? 357  TYR A N     1 
ATOM   11298 C  CA    . TYR D 3 357 ? 143.199 196.627 59.269  1.00 50.01  ? 357  TYR A CA    1 
ATOM   11299 C  C     . TYR D 3 357 ? 142.899 197.439 60.521  1.00 54.42  ? 357  TYR A C     1 
ATOM   11300 O  O     . TYR D 3 357 ? 142.956 198.671 60.469  1.00 50.69  ? 357  TYR A O     1 
ATOM   11301 C  CB    . TYR D 3 357 ? 142.315 197.112 58.119  1.00 55.63  ? 357  TYR A CB    1 
ATOM   11302 C  CG    . TYR D 3 357 ? 142.660 196.509 56.777  1.00 56.53  ? 357  TYR A CG    1 
ATOM   11303 C  CD1   . TYR D 3 357 ? 143.976 196.245 56.431  1.00 56.66  ? 357  TYR A CD1   1 
ATOM   11304 C  CD2   . TYR D 3 357 ? 141.668 196.212 55.853  1.00 54.12  ? 357  TYR A CD2   1 
ATOM   11305 C  CE1   . TYR D 3 357 ? 144.294 195.698 55.207  1.00 57.86  ? 357  TYR A CE1   1 
ATOM   11306 C  CE2   . TYR D 3 357 ? 141.977 195.665 54.626  1.00 56.17  ? 357  TYR A CE2   1 
ATOM   11307 C  CZ    . TYR D 3 357 ? 143.290 195.409 54.308  1.00 59.23  ? 357  TYR A CZ    1 
ATOM   11308 O  OH    . TYR D 3 357 ? 143.604 194.864 53.086  1.00 60.56  ? 357  TYR A OH    1 
ATOM   11309 N  N     . GLN D 3 358 ? 142.587 196.791 61.641  1.00 61.12  ? 358  GLN A N     1 
ATOM   11310 C  CA    . GLN D 3 358 ? 142.238 197.519 62.850  1.00 52.46  ? 358  GLN A CA    1 
ATOM   11311 C  C     . GLN D 3 358 ? 143.434 197.563 63.784  1.00 59.62  ? 358  GLN A C     1 
ATOM   11312 O  O     . GLN D 3 358 ? 143.826 196.517 64.322  1.00 61.56  ? 358  GLN A O     1 
ATOM   11313 C  CB    . GLN D 3 358 ? 141.045 196.872 63.545  1.00 54.53  ? 358  GLN A CB    1 
ATOM   11314 C  CG    . GLN D 3 358 ? 140.447 197.722 64.656  1.00 63.71  ? 358  GLN A CG    1 
ATOM   11315 C  CD    . GLN D 3 358 ? 139.811 199.001 64.144  1.00 65.84  ? 358  GLN A CD    1 
ATOM   11316 O  OE1   . GLN D 3 358 ? 139.429 199.097 62.978  1.00 66.90  ? 358  GLN A OE1   1 
ATOM   11317 N  NE2   . GLN D 3 358 ? 139.696 199.994 65.017  1.00 60.26  ? 358  GLN A NE2   1 
ATOM   11318 N  N     . PRO D 3 359 ? 144.039 198.729 64.012  1.00 63.59  ? 359  PRO A N     1 
ATOM   11319 C  CA    . PRO D 3 359 ? 145.201 198.785 64.891  1.00 62.07  ? 359  PRO A CA    1 
ATOM   11320 C  C     . PRO D 3 359 ? 144.803 198.508 66.327  1.00 62.63  ? 359  PRO A C     1 
ATOM   11321 O  O     . PRO D 3 359 ? 143.633 198.689 66.709  1.00 63.94  ? 359  PRO A O     1 
ATOM   11322 C  CB    . PRO D 3 359 ? 145.704 200.228 64.717  1.00 63.56  ? 359  PRO A CB    1 
ATOM   11323 C  CG    . PRO D 3 359 ? 144.490 200.991 64.342  1.00 60.42  ? 359  PRO A CG    1 
ATOM   11324 C  CD    . PRO D 3 359 ? 143.664 200.059 63.504  1.00 61.70  ? 359  PRO A CD    1 
ATOM   11325 N  N     . PRO D 3 360 ? 145.736 198.053 67.161  1.00 63.17  ? 360  PRO A N     1 
ATOM   11326 C  CA    . PRO D 3 360 ? 145.407 197.818 68.568  1.00 63.64  ? 360  PRO A CA    1 
ATOM   11327 C  C     . PRO D 3 360 ? 145.033 199.113 69.269  1.00 65.70  ? 360  PRO A C     1 
ATOM   11328 O  O     . PRO D 3 360 ? 145.605 200.173 69.012  1.00 71.28  ? 360  PRO A O     1 
ATOM   11329 C  CB    . PRO D 3 360 ? 146.696 197.220 69.140  1.00 60.75  ? 360  PRO A CB    1 
ATOM   11330 C  CG    . PRO D 3 360 ? 147.763 197.710 68.237  1.00 64.37  ? 360  PRO A CG    1 
ATOM   11331 C  CD    . PRO D 3 360 ? 147.152 197.778 66.873  1.00 61.95  ? 360  PRO A CD    1 
ATOM   11332 N  N     . THR D 3 361 ? 144.061 199.015 70.167  1.00 61.96  ? 361  THR A N     1 
ATOM   11333 C  CA    . THR D 3 361 ? 143.589 200.164 70.919  1.00 64.76  ? 361  THR A CA    1 
ATOM   11334 C  C     . THR D 3 361 ? 144.274 200.216 72.277  1.00 63.50  ? 361  THR A C     1 
ATOM   11335 O  O     . THR D 3 361 ? 144.662 199.190 72.840  1.00 63.51  ? 361  THR A O     1 
ATOM   11336 C  CB    . THR D 3 361 ? 142.071 200.123 71.098  1.00 58.94  ? 361  THR A CB    1 
ATOM   11337 O  OG1   . THR D 3 361 ? 141.635 201.312 71.768  1.00 68.38  ? 361  THR A OG1   1 
ATOM   11338 C  CG2   . THR D 3 361 ? 141.671 198.924 71.913  1.00 58.55  ? 361  THR A CG2   1 
ATOM   11339 N  N     . VAL D 3 362 ? 144.436 201.430 72.789  1.00 59.61  ? 362  VAL A N     1 
ATOM   11340 C  CA    . VAL D 3 362 ? 145.123 201.670 74.049  1.00 62.99  ? 362  VAL A CA    1 
ATOM   11341 C  C     . VAL D 3 362 ? 144.082 202.054 75.086  1.00 67.43  ? 362  VAL A C     1 
ATOM   11342 O  O     . VAL D 3 362 ? 143.393 203.071 74.939  1.00 67.99  ? 362  VAL A O     1 
ATOM   11343 C  CB    . VAL D 3 362 ? 146.193 202.762 73.912  1.00 67.18  ? 362  VAL A CB    1 
ATOM   11344 C  CG1   . VAL D 3 362 ? 146.777 203.102 75.273  1.00 67.16  ? 362  VAL A CG1   1 
ATOM   11345 C  CG2   . VAL D 3 362 ? 147.281 202.305 72.962  1.00 66.63  ? 362  VAL A CG2   1 
ATOM   11346 N  N     . VAL D 3 363 ? 143.966 201.242 76.127  1.00 66.04  ? 363  VAL A N     1 
ATOM   11347 C  CA    . VAL D 3 363 ? 143.060 201.578 77.230  1.00 64.80  ? 363  VAL A CA    1 
ATOM   11348 C  C     . VAL D 3 363 ? 143.616 202.782 77.976  1.00 64.13  ? 363  VAL A C     1 
ATOM   11349 O  O     . VAL D 3 363 ? 144.819 202.802 78.296  1.00 68.24  ? 363  VAL A O     1 
ATOM   11350 C  CB    . VAL D 3 363 ? 142.897 200.380 78.164  1.00 66.39  ? 363  VAL A CB    1 
ATOM   11351 C  CG1   . VAL D 3 363 ? 141.877 200.692 79.246  1.00 65.59  ? 363  VAL A CG1   1 
ATOM   11352 C  CG2   . VAL D 3 363 ? 142.489 199.150 77.379  1.00 64.81  ? 363  VAL A CG2   1 
ATOM   11353 N  N     . PRO D 3 364 ? 142.812 203.807 78.253  1.00 62.70  ? 364  PRO A N     1 
ATOM   11354 C  CA    . PRO D 3 364 ? 143.315 204.938 79.038  1.00 65.74  ? 364  PRO A CA    1 
ATOM   11355 C  C     . PRO D 3 364 ? 143.808 204.476 80.400  1.00 69.24  ? 364  PRO A C     1 
ATOM   11356 O  O     . PRO D 3 364 ? 143.231 203.581 81.020  1.00 70.10  ? 364  PRO A O     1 
ATOM   11357 C  CB    . PRO D 3 364 ? 142.095 205.856 79.156  1.00 65.37  ? 364  PRO A CB    1 
ATOM   11358 C  CG    . PRO D 3 364 ? 141.262 205.516 77.971  1.00 64.96  ? 364  PRO A CG    1 
ATOM   11359 C  CD    . PRO D 3 364 ? 141.448 204.044 77.755  1.00 64.82  ? 364  PRO A CD    1 
ATOM   11360 N  N     . GLY D 3 365 ? 144.889 205.095 80.859  1.00 77.47  ? 365  GLY A N     1 
ATOM   11361 C  CA    . GLY D 3 365 ? 145.545 204.628 82.065  1.00 76.85  ? 365  GLY A CA    1 
ATOM   11362 C  C     . GLY D 3 365 ? 146.165 203.257 81.902  1.00 82.36  ? 365  GLY A C     1 
ATOM   11363 O  O     . GLY D 3 365 ? 146.043 202.415 82.800  1.00 82.20  ? 365  GLY A O     1 
ATOM   11364 N  N     . GLY D 3 366 ? 146.822 203.010 80.772  1.00 88.31  ? 366  GLY A N     1 
ATOM   11365 C  CA    . GLY D 3 366 ? 147.414 201.715 80.503  1.00 84.23  ? 366  GLY A CA    1 
ATOM   11366 C  C     . GLY D 3 366 ? 148.896 201.781 80.202  1.00 83.08  ? 366  GLY A C     1 
ATOM   11367 O  O     . GLY D 3 366 ? 149.417 202.834 79.823  1.00 86.30  ? 366  GLY A O     1 
ATOM   11368 N  N     . ASP D 3 367 ? 149.589 200.655 80.374  1.00 80.26  ? 367  ASP A N     1 
ATOM   11369 C  CA    . ASP D 3 367 ? 151.033 200.622 80.169  1.00 81.43  ? 367  ASP A CA    1 
ATOM   11370 C  C     . ASP D 3 367 ? 151.407 200.582 78.692  1.00 81.82  ? 367  ASP A C     1 
ATOM   11371 O  O     . ASP D 3 367 ? 152.427 201.157 78.297  1.00 79.42  ? 367  ASP A O     1 
ATOM   11372 C  CB    . ASP D 3 367 ? 151.634 199.429 80.912  1.00 85.09  ? 367  ASP A CB    1 
ATOM   11373 C  CG    . ASP D 3 367 ? 150.806 198.171 80.758  1.00 88.03  ? 367  ASP A CG    1 
ATOM   11374 O  OD1   . ASP D 3 367 ? 149.742 198.236 80.108  1.00 87.79  ? 367  ASP A OD1   1 
ATOM   11375 O  OD2   . ASP D 3 367 ? 151.217 197.118 81.288  1.00 88.57  ? 367  ASP A OD2   1 
ATOM   11376 N  N     . LEU D 3 368 ? 150.609 199.913 77.864  1.00 77.44  ? 368  LEU A N     1 
ATOM   11377 C  CA    . LEU D 3 368 ? 150.937 199.797 76.451  1.00 71.49  ? 368  LEU A CA    1 
ATOM   11378 C  C     . LEU D 3 368 ? 150.805 201.146 75.750  1.00 73.90  ? 368  LEU A C     1 
ATOM   11379 O  O     . LEU D 3 368 ? 150.025 202.014 76.148  1.00 76.29  ? 368  LEU A O     1 
ATOM   11380 C  CB    . LEU D 3 368 ? 150.039 198.766 75.769  1.00 68.16  ? 368  LEU A CB    1 
ATOM   11381 C  CG    . LEU D 3 368 ? 150.403 197.288 75.917  1.00 72.10  ? 368  LEU A CG    1 
ATOM   11382 C  CD1   . LEU D 3 368 ? 150.007 196.756 77.277  1.00 74.78  ? 368  LEU A CD1   1 
ATOM   11383 C  CD2   . LEU D 3 368 ? 149.750 196.466 74.819  1.00 73.65  ? 368  LEU A CD2   1 
ATOM   11384 N  N     . ALA D 3 369 ? 151.589 201.314 74.690  1.00 69.57  ? 369  ALA A N     1 
ATOM   11385 C  CA    . ALA D 3 369 ? 151.623 202.544 73.916  1.00 68.53  ? 369  ALA A CA    1 
ATOM   11386 C  C     . ALA D 3 369 ? 150.880 202.365 72.600  1.00 67.98  ? 369  ALA A C     1 
ATOM   11387 O  O     . ALA D 3 369 ? 150.611 201.246 72.158  1.00 71.07  ? 369  ALA A O     1 
ATOM   11388 C  CB    . ALA D 3 369 ? 153.066 202.983 73.645  1.00 69.37  ? 369  ALA A CB    1 
ATOM   11389 N  N     . LYS D 3 370 ? 150.545 203.492 71.979  1.00 63.93  ? 370  LYS A N     1 
ATOM   11390 C  CA    . LYS D 3 370 ? 149.825 203.464 70.713  1.00 64.55  ? 370  LYS A CA    1 
ATOM   11391 C  C     . LYS D 3 370 ? 150.777 203.082 69.590  1.00 64.38  ? 370  LYS A C     1 
ATOM   11392 O  O     . LYS D 3 370 ? 151.724 203.817 69.290  1.00 64.80  ? 370  LYS A O     1 
ATOM   11393 C  CB    . LYS D 3 370 ? 149.180 204.819 70.440  1.00 63.24  ? 370  LYS A CB    1 
ATOM   11394 C  CG    . LYS D 3 370 ? 148.190 204.807 69.293  1.00 66.70  ? 370  LYS A CG    1 
ATOM   11395 C  CD    . LYS D 3 370 ? 147.450 206.128 69.192  1.00 66.01  ? 370  LYS A CD    1 
ATOM   11396 C  CE    . LYS D 3 370 ? 146.398 206.087 68.098  1.00 66.18  ? 370  LYS A CE    1 
ATOM   11397 N  NZ    . LYS D 3 370 ? 147.000 205.828 66.762  1.00 65.72  ? 370  LYS A NZ    1 
ATOM   11398 N  N     . VAL D 3 371 ? 150.527 201.934 68.971  1.00 62.29  ? 371  VAL A N     1 
ATOM   11399 C  CA    . VAL D 3 371 ? 151.383 201.395 67.924  1.00 61.43  ? 371  VAL A CA    1 
ATOM   11400 C  C     . VAL D 3 371 ? 150.537 201.155 66.684  1.00 64.77  ? 371  VAL A C     1 
ATOM   11401 O  O     . VAL D 3 371 ? 149.350 200.828 66.784  1.00 68.38  ? 371  VAL A O     1 
ATOM   11402 C  CB    . VAL D 3 371 ? 152.078 200.095 68.376  1.00 64.06  ? 371  VAL A CB    1 
ATOM   11403 C  CG1   . VAL D 3 371 ? 153.078 200.393 69.473  1.00 64.30  ? 371  VAL A CG1   1 
ATOM   11404 C  CG2   . VAL D 3 371 ? 151.056 199.085 68.857  1.00 63.82  ? 371  VAL A CG2   1 
ATOM   11405 N  N     . GLN D 3 372 ? 151.148 201.330 65.511  1.00 59.48  ? 372  GLN A N     1 
ATOM   11406 C  CA    . GLN D 3 372 ? 150.403 201.173 64.268  1.00 55.80  ? 372  GLN A CA    1 
ATOM   11407 C  C     . GLN D 3 372 ? 150.150 199.709 63.934  1.00 60.83  ? 372  GLN A C     1 
ATOM   11408 O  O     . GLN D 3 372 ? 149.132 199.389 63.313  1.00 68.05  ? 372  GLN A O     1 
ATOM   11409 C  CB    . GLN D 3 372 ? 151.140 201.858 63.119  1.00 60.53  ? 372  GLN A CB    1 
ATOM   11410 C  CG    . GLN D 3 372 ? 150.638 203.256 62.811  1.00 62.24  ? 372  GLN A CG    1 
ATOM   11411 C  CD    . GLN D 3 372 ? 150.982 204.250 63.897  1.00 64.17  ? 372  GLN A CD    1 
ATOM   11412 O  OE1   . GLN D 3 372 ? 152.150 204.450 64.223  1.00 68.88  ? 372  GLN A OE1   1 
ATOM   11413 N  NE2   . GLN D 3 372 ? 149.963 204.880 64.468  1.00 63.45  ? 372  GLN A NE2   1 
ATOM   11414 N  N     . ARG D 3 373 ? 151.049 198.812 64.329  1.00 53.54  ? 373  ARG A N     1 
ATOM   11415 C  CA    . ARG D 3 373 ? 150.893 197.403 64.001  1.00 53.31  ? 373  ARG A CA    1 
ATOM   11416 C  C     . ARG D 3 373 ? 151.272 196.548 65.200  1.00 54.70  ? 373  ARG A C     1 
ATOM   11417 O  O     . ARG D 3 373 ? 152.078 196.953 66.041  1.00 60.12  ? 373  ARG A O     1 
ATOM   11418 C  CB    . ARG D 3 373 ? 151.741 197.014 62.785  1.00 53.75  ? 373  ARG A CB    1 
ATOM   11419 C  CG    . ARG D 3 373 ? 153.199 197.390 62.903  1.00 57.52  ? 373  ARG A CG    1 
ATOM   11420 C  CD    . ARG D 3 373 ? 153.861 197.443 61.544  1.00 57.96  ? 373  ARG A CD    1 
ATOM   11421 N  NE    . ARG D 3 373 ? 153.382 198.565 60.748  1.00 60.52  ? 373  ARG A NE    1 
ATOM   11422 C  CZ    . ARG D 3 373 ? 153.901 199.783 60.784  1.00 58.86  ? 373  ARG A CZ    1 
ATOM   11423 N  NH1   . ARG D 3 373 ? 154.922 200.076 61.572  1.00 59.18  ? 373  ARG A NH1   1 
ATOM   11424 N  NH2   . ARG D 3 373 ? 153.382 200.732 60.012  1.00 58.47  ? 373  ARG A NH2   1 
ATOM   11425 N  N     . ALA D 3 374 ? 150.680 195.358 65.268  1.00 51.19  ? 374  ALA A N     1 
ATOM   11426 C  CA    . ALA D 3 374 ? 150.990 194.406 66.323  1.00 48.73  ? 374  ALA A CA    1 
ATOM   11427 C  C     . ALA D 3 374 ? 150.777 192.998 65.793  1.00 45.12  ? 374  ALA A C     1 
ATOM   11428 O  O     . ALA D 3 374 ? 150.036 192.785 64.831  1.00 55.00  ? 374  ALA A O     1 
ATOM   11429 C  CB    . ALA D 3 374 ? 150.135 194.650 67.569  1.00 48.32  ? 374  ALA A CB    1 
ATOM   11430 N  N     . VAL D 3 375 ? 151.443 192.035 66.433  1.00 40.37  ? 375  VAL A N     1 
ATOM   11431 C  CA    . VAL D 3 375 ? 151.365 190.635 66.037  1.00 46.31  ? 375  VAL A CA    1 
ATOM   11432 C  C     . VAL D 3 375 ? 150.999 189.799 67.256  1.00 49.33  ? 375  VAL A C     1 
ATOM   11433 O  O     . VAL D 3 375 ? 151.174 190.215 68.403  1.00 58.95  ? 375  VAL A O     1 
ATOM   11434 C  CB    . VAL D 3 375 ? 152.686 190.118 65.420  1.00 51.84  ? 375  VAL A CB    1 
ATOM   11435 C  CG1   . VAL D 3 375 ? 153.679 189.768 66.507  1.00 49.44  ? 375  VAL A CG1   1 
ATOM   11436 C  CG2   . VAL D 3 375 ? 152.433 188.928 64.510  1.00 51.30  ? 375  VAL A CG2   1 
ATOM   11437 N  N     . CYS D 3 376 ? 150.474 188.607 66.991  1.00 42.78  ? 376  CYS A N     1 
ATOM   11438 C  CA    . CYS D 3 376 ? 150.149 187.630 68.023  1.00 31.59  ? 376  CYS A CA    1 
ATOM   11439 C  C     . CYS D 3 376 ? 150.574 186.265 67.508  1.00 45.55  ? 376  CYS A C     1 
ATOM   11440 O  O     . CYS D 3 376 ? 149.946 185.721 66.594  1.00 55.52  ? 376  CYS A O     1 
ATOM   11441 C  CB    . CYS D 3 376 ? 148.661 187.653 68.355  1.00 42.37  ? 376  CYS A CB    1 
ATOM   11442 S  SG    . CYS D 3 376 ? 148.228 186.823 69.891  1.00 66.85  ? 376  CYS A SG    1 
ATOM   11443 N  N     . MET D 3 377 ? 151.637 185.714 68.084  1.00 60.13  ? 377  MET A N     1 
ATOM   11444 C  CA    . MET D 3 377 ? 152.230 184.467 67.613  1.00 62.85  ? 377  MET A CA    1 
ATOM   11445 C  C     . MET D 3 377 ? 151.717 183.317 68.467  1.00 65.12  ? 377  MET A C     1 
ATOM   11446 O  O     . MET D 3 377 ? 152.077 183.194 69.642  1.00 70.30  ? 377  MET A O     1 
ATOM   11447 C  CB    . MET D 3 377 ? 153.754 184.546 67.654  1.00 60.96  ? 377  MET A CB    1 
ATOM   11448 C  CG    . MET D 3 377 ? 154.478 183.420 66.954  1.00 57.97  ? 377  MET A CG    1 
ATOM   11449 S  SD    . MET D 3 377 ? 154.977 182.125 68.091  1.00 80.70  ? 377  MET A SD    1 
ATOM   11450 C  CE    . MET D 3 377 ? 156.202 182.982 69.072  1.00 68.35  ? 377  MET A CE    1 
ATOM   11451 N  N     . LEU D 3 378 ? 150.878 182.479 67.875  1.00 51.00  ? 378  LEU A N     1 
ATOM   11452 C  CA    . LEU D 3 378 ? 150.388 181.267 68.513  1.00 47.25  ? 378  LEU A CA    1 
ATOM   11453 C  C     . LEU D 3 378 ? 151.153 180.097 67.911  1.00 54.02  ? 378  LEU A C     1 
ATOM   11454 O  O     . LEU D 3 378 ? 150.960 179.761 66.738  1.00 66.35  ? 378  LEU A O     1 
ATOM   11455 C  CB    . LEU D 3 378 ? 148.884 181.113 68.307  1.00 48.02  ? 378  LEU A CB    1 
ATOM   11456 C  CG    . LEU D 3 378 ? 147.888 181.866 69.191  1.00 61.83  ? 378  LEU A CG    1 
ATOM   11457 C  CD1   . LEU D 3 378 ? 148.320 183.289 69.489  1.00 62.84  ? 378  LEU A CD1   1 
ATOM   11458 C  CD2   . LEU D 3 378 ? 146.534 181.870 68.507  1.00 60.74  ? 378  LEU A CD2   1 
ATOM   11459 N  N     . SER D 3 379 ? 152.019 179.481 68.706  1.00 43.46  ? 379  SER A N     1 
ATOM   11460 C  CA    . SER D 3 379 ? 152.894 178.422 68.229  1.00 49.55  ? 379  SER A CA    1 
ATOM   11461 C  C     . SER D 3 379 ? 152.644 177.136 68.996  1.00 59.32  ? 379  SER A C     1 
ATOM   11462 O  O     . SER D 3 379 ? 152.423 177.156 70.210  1.00 62.97  ? 379  SER A O     1 
ATOM   11463 C  CB    . SER D 3 379 ? 154.359 178.812 68.372  1.00 54.63  ? 379  SER A CB    1 
ATOM   11464 O  OG    . SER D 3 379 ? 154.641 179.223 69.697  1.00 63.21  ? 379  SER A OG    1 
ATOM   11465 N  N     . ASN D 3 380 ? 152.686 176.021 68.280  1.00 59.43  ? 380  ASN A N     1 
ATOM   11466 C  CA    . ASN D 3 380 ? 152.597 174.694 68.875  1.00 57.42  ? 380  ASN A CA    1 
ATOM   11467 C  C     . ASN D 3 380 ? 154.003 174.107 68.854  1.00 60.06  ? 380  ASN A C     1 
ATOM   11468 O  O     . ASN D 3 380 ? 154.449 173.573 67.837  1.00 66.33  ? 380  ASN A O     1 
ATOM   11469 C  CB    . ASN D 3 380 ? 151.607 173.822 68.113  1.00 55.19  ? 380  ASN A CB    1 
ATOM   11470 C  CG    . ASN D 3 380 ? 151.152 172.622 68.911  1.00 61.42  ? 380  ASN A CG    1 
ATOM   11471 O  OD1   . ASN D 3 380 ? 151.855 172.151 69.802  1.00 66.64  ? 380  ASN A OD1   1 
ATOM   11472 N  ND2   . ASN D 3 380 ? 149.967 172.119 68.594  1.00 58.42  ? 380  ASN A ND2   1 
ATOM   11473 N  N     . THR D 3 381 ? 154.704 174.213 69.977  1.00 52.35  ? 381  THR A N     1 
ATOM   11474 C  CA    . THR D 3 381 ? 156.075 173.748 70.081  1.00 48.00  ? 381  THR A CA    1 
ATOM   11475 C  C     . THR D 3 381 ? 156.186 172.674 71.154  1.00 54.34  ? 381  THR A C     1 
ATOM   11476 O  O     . THR D 3 381 ? 155.384 172.610 72.088  1.00 61.26  ? 381  THR A O     1 
ATOM   11477 C  CB    . THR D 3 381 ? 157.035 174.899 70.395  1.00 54.52  ? 381  THR A CB    1 
ATOM   11478 O  OG1   . THR D 3 381 ? 158.384 174.419 70.363  1.00 64.10  ? 381  THR A OG1   1 
ATOM   11479 C  CG2   . THR D 3 381 ? 156.745 175.480 71.766  1.00 59.31  ? 381  THR A CG2   1 
ATOM   11480 N  N     . THR D 3 382 ? 157.194 171.820 70.998  1.00 52.23  ? 382  THR A N     1 
ATOM   11481 C  CA    . THR D 3 382 ? 157.456 170.748 71.946  1.00 51.50  ? 382  THR A CA    1 
ATOM   11482 C  C     . THR D 3 382 ? 158.119 171.240 73.223  1.00 54.20  ? 382  THR A C     1 
ATOM   11483 O  O     . THR D 3 382 ? 158.289 170.449 74.156  1.00 57.89  ? 382  THR A O     1 
ATOM   11484 C  CB    . THR D 3 382 ? 158.334 169.672 71.302  1.00 50.26  ? 382  THR A CB    1 
ATOM   11485 O  OG1   . THR D 3 382 ? 159.509 170.276 70.750  1.00 59.73  ? 382  THR A OG1   1 
ATOM   11486 C  CG2   . THR D 3 382 ? 157.584 168.960 70.198  1.00 44.17  ? 382  THR A CG2   1 
ATOM   11487 N  N     . ALA D 3 383 ? 158.497 172.518 73.288  1.00 56.51  ? 383  ALA A N     1 
ATOM   11488 C  CA    . ALA D 3 383 ? 159.147 173.050 74.478  1.00 58.23  ? 383  ALA A CA    1 
ATOM   11489 C  C     . ALA D 3 383 ? 158.217 173.087 75.679  1.00 62.95  ? 383  ALA A C     1 
ATOM   11490 O  O     . ALA D 3 383 ? 158.686 173.281 76.805  1.00 69.39  ? 383  ALA A O     1 
ATOM   11491 C  CB    . ALA D 3 383 ? 159.689 174.451 74.198  1.00 62.35  ? 383  ALA A CB    1 
ATOM   11492 N  N     . ILE D 3 384 ? 156.912 172.908 75.468  1.00 57.78  ? 384  ILE A N     1 
ATOM   11493 C  CA    . ILE D 3 384 ? 155.970 172.916 76.576  1.00 57.83  ? 384  ILE A CA    1 
ATOM   11494 C  C     . ILE D 3 384 ? 156.021 171.616 77.364  1.00 60.54  ? 384  ILE A C     1 
ATOM   11495 O  O     . ILE D 3 384 ? 155.395 171.511 78.424  1.00 68.46  ? 384  ILE A O     1 
ATOM   11496 C  CB    . ILE D 3 384 ? 154.552 173.198 76.048  1.00 56.16  ? 384  ILE A CB    1 
ATOM   11497 C  CG1   . ILE D 3 384 ? 153.741 173.982 77.078  1.00 59.46  ? 384  ILE A CG1   1 
ATOM   11498 C  CG2   . ILE D 3 384 ? 153.852 171.906 75.668  1.00 56.46  ? 384  ILE A CG2   1 
ATOM   11499 C  CD1   . ILE D 3 384 ? 152.466 174.572 76.522  1.00 61.92  ? 384  ILE A CD1   1 
ATOM   11500 N  N     . ALA D 3 385 ? 156.769 170.622 76.880  1.00 57.59  ? 385  ALA A N     1 
ATOM   11501 C  CA    . ALA D 3 385 ? 156.846 169.343 77.576  1.00 56.61  ? 385  ALA A CA    1 
ATOM   11502 C  C     . ALA D 3 385 ? 157.591 169.469 78.896  1.00 59.36  ? 385  ALA A C     1 
ATOM   11503 O  O     . ALA D 3 385 ? 157.291 168.750 79.856  1.00 64.66  ? 385  ALA A O     1 
ATOM   11504 C  CB    . ALA D 3 385 ? 157.514 168.300 76.681  1.00 58.38  ? 385  ALA A CB    1 
ATOM   11505 N  N     . GLU D 3 386 ? 158.574 170.368 78.965  1.00 59.46  ? 386  GLU A N     1 
ATOM   11506 C  CA    . GLU D 3 386 ? 159.342 170.518 80.196  1.00 62.90  ? 386  GLU A CA    1 
ATOM   11507 C  C     . GLU D 3 386 ? 158.501 171.114 81.319  1.00 72.00  ? 386  GLU A C     1 
ATOM   11508 O  O     . GLU D 3 386 ? 158.725 170.795 82.494  1.00 74.49  ? 386  GLU A O     1 
ATOM   11509 C  CB    . GLU D 3 386 ? 160.588 171.365 79.943  1.00 64.87  ? 386  GLU A CB    1 
ATOM   11510 C  CG    . GLU D 3 386 ? 160.313 172.824 79.619  1.00 75.45  ? 386  GLU A CG    1 
ATOM   11511 C  CD    . GLU D 3 386 ? 161.582 173.611 79.361  1.00 77.85  ? 386  GLU A CD    1 
ATOM   11512 O  OE1   . GLU D 3 386 ? 162.596 172.996 78.968  1.00 74.91  ? 386  GLU A OE1   1 
ATOM   11513 O  OE2   . GLU D 3 386 ? 161.567 174.846 79.551  1.00 75.63  ? 386  GLU A OE2   1 
ATOM   11514 N  N     . ALA D 3 387 ? 157.538 171.978 80.987  1.00 65.45  ? 387  ALA A N     1 
ATOM   11515 C  CA    . ALA D 3 387 ? 156.619 172.481 82.003  1.00 60.47  ? 387  ALA A CA    1 
ATOM   11516 C  C     . ALA D 3 387 ? 155.778 171.353 82.584  1.00 65.47  ? 387  ALA A C     1 
ATOM   11517 O  O     . ALA D 3 387 ? 155.611 171.254 83.809  1.00 69.00  ? 387  ALA A O     1 
ATOM   11518 C  CB    . ALA D 3 387 ? 155.731 173.569 81.407  1.00 59.22  ? 387  ALA A CB    1 
ATOM   11519 N  N     . TRP D 3 388 ? 155.249 170.484 81.718  1.00 54.00  ? 388  TRP A N     1 
ATOM   11520 C  CA    . TRP D 3 388 ? 154.574 169.284 82.195  1.00 55.13  ? 388  TRP A CA    1 
ATOM   11521 C  C     . TRP D 3 388 ? 155.506 168.451 83.060  1.00 59.16  ? 388  TRP A C     1 
ATOM   11522 O  O     . TRP D 3 388 ? 155.087 167.898 84.082  1.00 67.73  ? 388  TRP A O     1 
ATOM   11523 C  CB    . TRP D 3 388 ? 154.069 168.452 81.015  1.00 59.34  ? 388  TRP A CB    1 
ATOM   11524 C  CG    . TRP D 3 388 ? 153.174 169.172 80.049  1.00 61.24  ? 388  TRP A CG    1 
ATOM   11525 C  CD1   . TRP D 3 388 ? 153.345 169.272 78.700  1.00 66.42  ? 388  TRP A CD1   1 
ATOM   11526 C  CD2   . TRP D 3 388 ? 151.944 169.842 80.346  1.00 58.38  ? 388  TRP A CD2   1 
ATOM   11527 N  NE1   . TRP D 3 388 ? 152.317 169.989 78.142  1.00 63.15  ? 388  TRP A NE1   1 
ATOM   11528 C  CE2   . TRP D 3 388 ? 151.442 170.348 79.132  1.00 62.07  ? 388  TRP A CE2   1 
ATOM   11529 C  CE3   . TRP D 3 388 ? 151.225 170.073 81.520  1.00 63.48  ? 388  TRP A CE3   1 
ATOM   11530 C  CZ2   . TRP D 3 388 ? 150.257 171.070 79.059  1.00 64.44  ? 388  TRP A CZ2   1 
ATOM   11531 C  CZ3   . TRP D 3 388 ? 150.047 170.790 81.445  1.00 65.65  ? 388  TRP A CZ3   1 
ATOM   11532 C  CH2   . TRP D 3 388 ? 149.576 171.281 80.224  1.00 64.56  ? 388  TRP A CH2   1 
ATOM   11533 N  N     . ALA D 3 389 ? 156.779 168.358 82.670  1.00 50.20  ? 389  ALA A N     1 
ATOM   11534 C  CA    . ALA D 3 389 ? 157.729 167.539 83.414  1.00 50.66  ? 389  ALA A CA    1 
ATOM   11535 C  C     . ALA D 3 389 ? 157.930 168.067 84.828  1.00 59.56  ? 389  ALA A C     1 
ATOM   11536 O  O     . ALA D 3 389 ? 157.903 167.301 85.799  1.00 65.86  ? 389  ALA A O     1 
ATOM   11537 C  CB    . ALA D 3 389 ? 159.061 167.477 82.667  1.00 53.63  ? 389  ALA A CB    1 
ATOM   11538 N  N     . ARG D 3 390 ? 158.125 169.379 84.971  1.00 58.68  ? 390  ARG A N     1 
ATOM   11539 C  CA    . ARG D 3 390 ? 158.363 169.928 86.302  1.00 57.62  ? 390  ARG A CA    1 
ATOM   11540 C  C     . ARG D 3 390 ? 157.100 169.879 87.153  1.00 61.66  ? 390  ARG A C     1 
ATOM   11541 O  O     . ARG D 3 390 ? 157.167 169.619 88.364  1.00 67.57  ? 390  ARG A O     1 
ATOM   11542 C  CB    . ARG D 3 390 ? 158.907 171.354 86.206  1.00 56.85  ? 390  ARG A CB    1 
ATOM   11543 C  CG    . ARG D 3 390 ? 158.040 172.322 85.437  1.00 59.69  ? 390  ARG A CG    1 
ATOM   11544 C  CD    . ARG D 3 390 ? 158.539 173.744 85.603  1.00 62.48  ? 390  ARG A CD    1 
ATOM   11545 N  NE    . ARG D 3 390 ? 159.959 173.864 85.299  1.00 65.43  ? 390  ARG A NE    1 
ATOM   11546 C  CZ    . ARG D 3 390 ? 160.443 174.252 84.128  1.00 67.22  ? 390  ARG A CZ    1 
ATOM   11547 N  NH1   . ARG D 3 390 ? 159.645 174.569 83.122  1.00 62.95  ? 390  ARG A NH1   1 
ATOM   11548 N  NH2   . ARG D 3 390 ? 161.760 174.326 83.962  1.00 64.09  ? 390  ARG A NH2   1 
ATOM   11549 N  N     . LEU D 3 391 ? 155.936 170.105 86.540  1.00 58.40  ? 391  LEU A N     1 
ATOM   11550 C  CA    . LEU D 3 391 ? 154.693 169.986 87.291  1.00 57.99  ? 391  LEU A CA    1 
ATOM   11551 C  C     . LEU D 3 391 ? 154.488 168.558 87.781  1.00 60.11  ? 391  LEU A C     1 
ATOM   11552 O  O     . LEU D 3 391 ? 154.068 168.337 88.925  1.00 70.28  ? 391  LEU A O     1 
ATOM   11553 C  CB    . LEU D 3 391 ? 153.521 170.442 86.428  1.00 57.41  ? 391  LEU A CB    1 
ATOM   11554 C  CG    . LEU D 3 391 ? 152.274 170.893 87.177  1.00 57.33  ? 391  LEU A CG    1 
ATOM   11555 C  CD1   . LEU D 3 391 ? 152.610 172.053 88.089  1.00 59.44  ? 391  LEU A CD1   1 
ATOM   11556 C  CD2   . LEU D 3 391 ? 151.198 171.282 86.185  1.00 61.10  ? 391  LEU A CD2   1 
ATOM   11557 N  N     . ASP D 3 392 ? 154.795 167.573 86.935  1.00 57.10  ? 392  ASP A N     1 
ATOM   11558 C  CA    . ASP D 3 392 ? 154.687 166.181 87.349  1.00 59.89  ? 392  ASP A CA    1 
ATOM   11559 C  C     . ASP D 3 392 ? 155.699 165.838 88.430  1.00 65.60  ? 392  ASP A C     1 
ATOM   11560 O  O     . ASP D 3 392 ? 155.409 165.018 89.304  1.00 69.75  ? 392  ASP A O     1 
ATOM   11561 C  CB    . ASP D 3 392 ? 154.864 165.259 86.146  1.00 64.45  ? 392  ASP A CB    1 
ATOM   11562 C  CG    . ASP D 3 392 ? 153.760 165.417 85.125  1.00 69.95  ? 392  ASP A CG    1 
ATOM   11563 O  OD1   . ASP D 3 392 ? 152.906 166.309 85.308  1.00 71.21  ? 392  ASP A OD1   1 
ATOM   11564 O  OD2   . ASP D 3 392 ? 153.746 164.650 84.140  1.00 70.78  ? 392  ASP A OD2   1 
ATOM   11565 N  N     . HIS D 3 393 ? 156.888 166.439 88.384  1.00 59.85  ? 393  HIS A N     1 
ATOM   11566 C  CA    . HIS D 3 393 ? 157.860 166.217 89.448  1.00 55.59  ? 393  HIS A CA    1 
ATOM   11567 C  C     . HIS D 3 393 ? 157.339 166.729 90.785  1.00 56.82  ? 393  HIS A C     1 
ATOM   11568 O  O     . HIS D 3 393 ? 157.454 166.045 91.811  1.00 64.00  ? 393  HIS A O     1 
ATOM   11569 C  CB    . HIS D 3 393 ? 159.184 166.889 89.094  1.00 57.64  ? 393  HIS A CB    1 
ATOM   11570 C  CG    . HIS D 3 393 ? 160.263 166.660 90.103  1.00 57.52  ? 393  HIS A CG    1 
ATOM   11571 N  ND1   . HIS D 3 393 ? 160.719 165.402 90.428  1.00 56.44  ? 393  HIS A ND1   1 
ATOM   11572 C  CD2   . HIS D 3 393 ? 160.972 167.526 90.863  1.00 59.59  ? 393  HIS A CD2   1 
ATOM   11573 C  CE1   . HIS D 3 393 ? 161.665 165.503 91.344  1.00 59.41  ? 393  HIS A CE1   1 
ATOM   11574 N  NE2   . HIS D 3 393 ? 161.837 166.781 91.625  1.00 61.93  ? 393  HIS A NE2   1 
ATOM   11575 N  N     . LYS D 3 394 ? 156.755 167.930 90.791  1.00 52.27  ? 394  LYS A N     1 
ATOM   11576 C  CA    . LYS D 3 394 ? 156.169 168.455 92.023  1.00 51.12  ? 394  LYS A CA    1 
ATOM   11577 C  C     . LYS D 3 394 ? 155.031 167.565 92.512  1.00 55.72  ? 394  LYS A C     1 
ATOM   11578 O  O     . LYS D 3 394 ? 154.922 167.279 93.715  1.00 66.65  ? 394  LYS A O     1 
ATOM   11579 C  CB    . LYS D 3 394 ? 155.682 169.886 91.803  1.00 49.31  ? 394  LYS A CB    1 
ATOM   11580 C  CG    . LYS D 3 394 ? 156.785 170.843 91.396  1.00 53.49  ? 394  LYS A CG    1 
ATOM   11581 C  CD    . LYS D 3 394 ? 156.238 172.164 90.896  1.00 53.16  ? 394  LYS A CD    1 
ATOM   11582 C  CE    . LYS D 3 394 ? 155.557 172.940 92.002  1.00 60.08  ? 394  LYS A CE    1 
ATOM   11583 N  NZ    . LYS D 3 394 ? 155.108 174.277 91.526  1.00 57.19  ? 394  LYS A NZ    1 
ATOM   11584 N  N     . PHE D 3 395 ? 154.184 167.106 91.589  1.00 49.83  ? 395  PHE A N     1 
ATOM   11585 C  CA    . PHE D 3 395 ? 153.093 166.209 91.955  1.00 52.04  ? 395  PHE A CA    1 
ATOM   11586 C  C     . PHE D 3 395 ? 153.616 164.922 92.571  1.00 56.06  ? 395  PHE A C     1 
ATOM   11587 O  O     . PHE D 3 395 ? 153.082 164.450 93.578  1.00 56.73  ? 395  PHE A O     1 
ATOM   11588 C  CB    . PHE D 3 395 ? 152.251 165.899 90.723  1.00 49.24  ? 395  PHE A CB    1 
ATOM   11589 C  CG    . PHE D 3 395 ? 151.174 164.875 90.952  1.00 48.50  ? 395  PHE A CG    1 
ATOM   11590 C  CD1   . PHE D 3 395 ? 149.903 165.266 91.313  1.00 53.64  ? 395  PHE A CD1   1 
ATOM   11591 C  CD2   . PHE D 3 395 ? 151.424 163.530 90.772  1.00 52.79  ? 395  PHE A CD2   1 
ATOM   11592 C  CE1   . PHE D 3 395 ? 148.912 164.337 91.513  1.00 54.19  ? 395  PHE A CE1   1 
ATOM   11593 C  CE2   . PHE D 3 395 ? 150.437 162.599 90.974  1.00 53.07  ? 395  PHE A CE2   1 
ATOM   11594 C  CZ    . PHE D 3 395 ? 149.179 163.003 91.344  1.00 53.18  ? 395  PHE A CZ    1 
ATOM   11595 N  N     . ASP D 3 396 ? 154.645 164.328 91.967  1.00 61.37  ? 396  ASP A N     1 
ATOM   11596 C  CA    . ASP D 3 396 ? 155.190 163.079 92.483  1.00 59.73  ? 396  ASP A CA    1 
ATOM   11597 C  C     . ASP D 3 396 ? 155.803 163.276 93.860  1.00 60.78  ? 396  ASP A C     1 
ATOM   11598 O  O     . ASP D 3 396 ? 155.629 162.433 94.748  1.00 65.52  ? 396  ASP A O     1 
ATOM   11599 C  CB    . ASP D 3 396 ? 156.223 162.516 91.510  1.00 62.00  ? 396  ASP A CB    1 
ATOM   11600 C  CG    . ASP D 3 396 ? 155.605 162.062 90.206  1.00 68.67  ? 396  ASP A CG    1 
ATOM   11601 O  OD1   . ASP D 3 396 ? 154.432 161.634 90.220  1.00 71.32  ? 396  ASP A OD1   1 
ATOM   11602 O  OD2   . ASP D 3 396 ? 156.291 162.135 89.165  1.00 68.74  ? 396  ASP A OD2   1 
ATOM   11603 N  N     . LEU D 3 397 ? 156.517 164.385 94.058  1.00 54.77  ? 397  LEU A N     1 
ATOM   11604 C  CA    . LEU D 3 397 ? 157.090 164.661 95.370  1.00 46.02  ? 397  LEU A CA    1 
ATOM   11605 C  C     . LEU D 3 397 ? 156.005 164.793 96.429  1.00 54.04  ? 397  LEU A C     1 
ATOM   11606 O  O     . LEU D 3 397 ? 156.143 164.263 97.537  1.00 55.37  ? 397  LEU A O     1 
ATOM   11607 C  CB    . LEU D 3 397 ? 157.941 165.926 95.317  1.00 46.10  ? 397  LEU A CB    1 
ATOM   11608 C  CG    . LEU D 3 397 ? 159.432 165.733 95.063  1.00 54.35  ? 397  LEU A CG    1 
ATOM   11609 C  CD1   . LEU D 3 397 ? 160.134 167.077 95.031  1.00 55.06  ? 397  LEU A CD1   1 
ATOM   11610 C  CD2   . LEU D 3 397 ? 160.044 164.829 96.118  1.00 56.24  ? 397  LEU A CD2   1 
ATOM   11611 N  N     . MET D 3 398 ? 154.918 165.501 96.114  1.00 61.41  ? 398  MET A N     1 
ATOM   11612 C  CA    . MET D 3 398 ? 153.856 165.671 97.104  1.00 56.36  ? 398  MET A CA    1 
ATOM   11613 C  C     . MET D 3 398 ? 153.088 164.374 97.336  1.00 57.27  ? 398  MET A C     1 
ATOM   11614 O  O     . MET D 3 398 ? 152.647 164.100 98.457  1.00 60.68  ? 398  MET A O     1 
ATOM   11615 C  CB    . MET D 3 398 ? 152.905 166.784 96.671  1.00 54.67  ? 398  MET A CB    1 
ATOM   11616 C  CG    . MET D 3 398 ? 153.245 168.136 97.253  1.00 53.89  ? 398  MET A CG    1 
ATOM   11617 S  SD    . MET D 3 398 ? 152.348 169.464 96.443  1.00 70.77  ? 398  MET A SD    1 
ATOM   11618 C  CE    . MET D 3 398 ? 150.665 169.011 96.842  1.00 61.84  ? 398  MET A CE    1 
ATOM   11619 N  N     . TYR D 3 399 ? 152.914 163.566 96.291  1.00 54.66  ? 399  TYR A N     1 
ATOM   11620 C  CA    . TYR D 3 399 ? 152.076 162.378 96.366  1.00 55.73  ? 399  TYR A CA    1 
ATOM   11621 C  C     . TYR D 3 399 ? 152.806 161.169 96.931  1.00 57.75  ? 399  TYR A C     1 
ATOM   11622 O  O     . TYR D 3 399 ? 152.149 160.230 97.391  1.00 58.35  ? 399  TYR A O     1 
ATOM   11623 C  CB    . TYR D 3 399 ? 151.529 162.058 94.974  1.00 57.09  ? 399  TYR A CB    1 
ATOM   11624 C  CG    . TYR D 3 399 ? 150.421 161.035 94.944  1.00 53.37  ? 399  TYR A CG    1 
ATOM   11625 C  CD1   . TYR D 3 399 ? 149.226 161.258 95.604  1.00 56.65  ? 399  TYR A CD1   1 
ATOM   11626 C  CD2   . TYR D 3 399 ? 150.557 159.862 94.221  1.00 53.13  ? 399  TYR A CD2   1 
ATOM   11627 C  CE1   . TYR D 3 399 ? 148.209 160.331 95.568  1.00 59.10  ? 399  TYR A CE1   1 
ATOM   11628 C  CE2   . TYR D 3 399 ? 149.546 158.931 94.180  1.00 51.14  ? 399  TYR A CE2   1 
ATOM   11629 C  CZ    . TYR D 3 399 ? 148.374 159.170 94.855  1.00 54.10  ? 399  TYR A CZ    1 
ATOM   11630 O  OH    . TYR D 3 399 ? 147.361 158.242 94.815  1.00 59.78  ? 399  TYR A OH    1 
ATOM   11631 N  N     . ALA D 3 400 ? 154.140 161.162 96.899  1.00 61.45  ? 400  ALA A N     1 
ATOM   11632 C  CA    . ALA D 3 400 ? 154.877 160.073 97.529  1.00 56.36  ? 400  ALA A CA    1 
ATOM   11633 C  C     . ALA D 3 400 ? 154.602 160.018 99.025  1.00 62.15  ? 400  ALA A C     1 
ATOM   11634 O  O     . ALA D 3 400 ? 154.369 158.940 99.583  1.00 65.19  ? 400  ALA A O     1 
ATOM   11635 C  CB    . ALA D 3 400 ? 156.373 160.229 97.264  1.00 55.26  ? 400  ALA A CB    1 
ATOM   11636 N  N     . LYS D 3 401 ? 154.618 161.172 99.690  1.00 57.53  ? 401  LYS A N     1 
ATOM   11637 C  CA    . LYS D 3 401 ? 154.240 161.265 101.092 1.00 46.26  ? 401  LYS A CA    1 
ATOM   11638 C  C     . LYS D 3 401 ? 152.734 161.322 101.289 1.00 50.09  ? 401  LYS A C     1 
ATOM   11639 O  O     . LYS D 3 401 ? 152.275 161.293 102.434 1.00 55.97  ? 401  LYS A O     1 
ATOM   11640 C  CB    . LYS D 3 401 ? 154.880 162.498 101.735 1.00 48.15  ? 401  LYS A CB    1 
ATOM   11641 C  CG    . LYS D 3 401 ? 156.390 162.539 101.639 1.00 50.84  ? 401  LYS A CG    1 
ATOM   11642 C  CD    . LYS D 3 401 ? 157.021 161.291 102.213 1.00 53.47  ? 401  LYS A CD    1 
ATOM   11643 C  CE    . LYS D 3 401 ? 158.525 161.312 102.028 1.00 53.65  ? 401  LYS A CE    1 
ATOM   11644 N  NZ    . LYS D 3 401 ? 158.900 161.368 100.592 1.00 58.89  ? 401  LYS A NZ    1 
ATOM   11645 N  N     . ARG D 3 402 ? 151.966 161.413 100.203 1.00 56.56  ? 402  ARG A N     1 
ATOM   11646 C  CA    . ARG D 3 402 ? 150.504 161.421 100.248 1.00 55.11  ? 402  ARG A CA    1 
ATOM   11647 C  C     . ARG D 3 402 ? 149.973 162.602 101.057 1.00 57.12  ? 402  ARG A C     1 
ATOM   11648 O  O     . ARG D 3 402 ? 149.138 162.438 101.947 1.00 58.18  ? 402  ARG A O     1 
ATOM   11649 C  CB    . ARG D 3 402 ? 149.964 160.097 100.788 1.00 56.71  ? 402  ARG A CB    1 
ATOM   11650 C  CG    . ARG D 3 402 ? 148.602 159.727 100.251 1.00 62.37  ? 402  ARG A CG    1 
ATOM   11651 C  CD    . ARG D 3 402 ? 148.594 158.296 99.768  1.00 61.96  ? 402  ARG A CD    1 
ATOM   11652 N  NE    . ARG D 3 402 ? 149.483 158.118 98.627  1.00 61.16  ? 402  ARG A NE    1 
ATOM   11653 C  CZ    . ARG D 3 402 ? 149.555 157.014 97.898  1.00 62.22  ? 402  ARG A CZ    1 
ATOM   11654 N  NH1   . ARG D 3 402 ? 148.787 155.967 98.151  1.00 61.84  ? 402  ARG A NH1   1 
ATOM   11655 N  NH2   . ARG D 3 402 ? 150.419 156.958 96.890  1.00 61.32  ? 402  ARG A NH2   1 
ATOM   11656 N  N     . ALA D 3 403 ? 150.455 163.798 100.743 1.00 51.00  ? 403  ALA A N     1 
ATOM   11657 C  CA    . ALA D 3 403 ? 150.051 164.991 101.466 1.00 45.68  ? 403  ALA A CA    1 
ATOM   11658 C  C     . ALA D 3 403 ? 148.840 165.636 100.807 1.00 50.81  ? 403  ALA A C     1 
ATOM   11659 O  O     . ALA D 3 403 ? 148.690 165.616 99.583  1.00 61.79  ? 403  ALA A O     1 
ATOM   11660 C  CB    . ALA D 3 403 ? 151.203 165.992 101.533 1.00 47.41  ? 403  ALA A CB    1 
ATOM   11661 N  N     . PHE D 3 404 ? 147.961 166.186 101.642 1.00 51.11  ? 404  PHE A N     1 
ATOM   11662 C  CA    . PHE D 3 404 ? 146.757 166.907 101.237 1.00 50.18  ? 404  PHE A CA    1 
ATOM   11663 C  C     . PHE D 3 404 ? 145.724 166.012 100.569 1.00 52.18  ? 404  PHE A C     1 
ATOM   11664 O  O     . PHE D 3 404 ? 144.657 166.495 100.176 1.00 54.59  ? 404  PHE A O     1 
ATOM   11665 C  CB    . PHE D 3 404 ? 147.087 168.078 100.308 1.00 53.67  ? 404  PHE A CB    1 
ATOM   11666 C  CG    . PHE D 3 404 ? 148.132 169.001 100.844 1.00 52.57  ? 404  PHE A CG    1 
ATOM   11667 C  CD1   . PHE D 3 404 ? 147.822 169.928 101.816 1.00 47.80  ? 404  PHE A CD1   1 
ATOM   11668 C  CD2   . PHE D 3 404 ? 149.427 168.942 100.372 1.00 59.49  ? 404  PHE A CD2   1 
ATOM   11669 C  CE1   . PHE D 3 404 ? 148.783 170.776 102.305 1.00 51.34  ? 404  PHE A CE1   1 
ATOM   11670 C  CE2   . PHE D 3 404 ? 150.392 169.788 100.860 1.00 58.08  ? 404  PHE A CE2   1 
ATOM   11671 C  CZ    . PHE D 3 404 ? 150.070 170.705 101.828 1.00 56.41  ? 404  PHE A CZ    1 
ATOM   11672 N  N     . VAL D 3 405 ? 146.011 164.718 100.425 1.00 54.01  ? 405  VAL A N     1 
ATOM   11673 C  CA    . VAL D 3 405 ? 145.119 163.836 99.680  1.00 47.07  ? 405  VAL A CA    1 
ATOM   11674 C  C     . VAL D 3 405 ? 143.795 163.673 100.412 1.00 49.84  ? 405  VAL A C     1 
ATOM   11675 O  O     . VAL D 3 405 ? 142.739 163.520 99.787  1.00 59.75  ? 405  VAL A O     1 
ATOM   11676 C  CB    . VAL D 3 405 ? 145.804 162.483 99.418  1.00 48.23  ? 405  VAL A CB    1 
ATOM   11677 C  CG1   . VAL D 3 405 ? 144.906 161.579 98.607  1.00 53.63  ? 405  VAL A CG1   1 
ATOM   11678 C  CG2   . VAL D 3 405 ? 147.113 162.696 98.692  1.00 53.46  ? 405  VAL A CG2   1 
ATOM   11679 N  N     . HIS D 3 406 ? 143.823 163.722 101.744 1.00 52.79  ? 406  HIS A N     1 
ATOM   11680 C  CA    . HIS D 3 406 ? 142.600 163.533 102.514 1.00 53.58  ? 406  HIS A CA    1 
ATOM   11681 C  C     . HIS D 3 406 ? 141.579 164.631 102.240 1.00 58.86  ? 406  HIS A C     1 
ATOM   11682 O  O     . HIS D 3 406 ? 140.371 164.375 102.287 1.00 62.16  ? 406  HIS A O     1 
ATOM   11683 C  CB    . HIS D 3 406 ? 142.923 163.469 104.004 1.00 50.79  ? 406  HIS A CB    1 
ATOM   11684 C  CG    . HIS D 3 406 ? 143.336 164.781 104.587 1.00 53.89  ? 406  HIS A CG    1 
ATOM   11685 N  ND1   . HIS D 3 406 ? 144.623 165.262 104.500 1.00 58.56  ? 406  HIS A ND1   1 
ATOM   11686 C  CD2   . HIS D 3 406 ? 142.630 165.717 105.262 1.00 53.12  ? 406  HIS A CD2   1 
ATOM   11687 C  CE1   . HIS D 3 406 ? 144.693 166.437 105.098 1.00 58.20  ? 406  HIS A CE1   1 
ATOM   11688 N  NE2   . HIS D 3 406 ? 143.497 166.736 105.570 1.00 56.39  ? 406  HIS A NE2   1 
ATOM   11689 N  N     . TRP D 3 407 ? 142.036 165.855 101.965 1.00 56.77  ? 407  TRP A N     1 
ATOM   11690 C  CA    . TRP D 3 407 ? 141.107 166.921 101.604 1.00 48.99  ? 407  TRP A CA    1 
ATOM   11691 C  C     . TRP D 3 407 ? 140.383 166.599 100.304 1.00 50.49  ? 407  TRP A C     1 
ATOM   11692 O  O     . TRP D 3 407 ? 139.169 166.798 100.195 1.00 59.93  ? 407  TRP A O     1 
ATOM   11693 C  CB    . TRP D 3 407 ? 141.847 168.251 101.477 1.00 44.26  ? 407  TRP A CB    1 
ATOM   11694 C  CG    . TRP D 3 407 ? 142.188 168.899 102.775 1.00 44.94  ? 407  TRP A CG    1 
ATOM   11695 C  CD1   . TRP D 3 407 ? 143.416 168.970 103.350 1.00 49.78  ? 407  TRP A CD1   1 
ATOM   11696 C  CD2   . TRP D 3 407 ? 141.291 169.580 103.656 1.00 48.31  ? 407  TRP A CD2   1 
ATOM   11697 N  NE1   . TRP D 3 407 ? 143.344 169.649 104.538 1.00 52.23  ? 407  TRP A NE1   1 
ATOM   11698 C  CE2   . TRP D 3 407 ? 142.047 170.032 104.750 1.00 50.06  ? 407  TRP A CE2   1 
ATOM   11699 C  CE3   . TRP D 3 407 ? 139.920 169.846 103.629 1.00 54.86  ? 407  TRP A CE3   1 
ATOM   11700 C  CZ2   . TRP D 3 407 ? 141.483 170.738 105.805 1.00 50.89  ? 407  TRP A CZ2   1 
ATOM   11701 C  CZ3   . TRP D 3 407 ? 139.361 170.547 104.679 1.00 54.99  ? 407  TRP A CZ3   1 
ATOM   11702 C  CH2   . TRP D 3 407 ? 140.141 170.985 105.751 1.00 52.04  ? 407  TRP A CH2   1 
ATOM   11703 N  N     . TYR D 3 408 ? 141.114 166.100 99.307  1.00 52.34  ? 408  TYR A N     1 
ATOM   11704 C  CA    . TYR D 3 408 ? 140.496 165.761 98.030  1.00 53.77  ? 408  TYR A CA    1 
ATOM   11705 C  C     . TYR D 3 408 ? 139.618 164.525 98.154  1.00 52.72  ? 408  TYR A C     1 
ATOM   11706 O  O     . TYR D 3 408 ? 138.510 164.485 97.610  1.00 58.82  ? 408  TYR A O     1 
ATOM   11707 C  CB    . TYR D 3 408 ? 141.573 165.542 96.971  1.00 53.68  ? 408  TYR A CB    1 
ATOM   11708 C  CG    . TYR D 3 408 ? 142.254 166.807 96.517  1.00 50.83  ? 408  TYR A CG    1 
ATOM   11709 C  CD1   . TYR D 3 408 ? 143.280 167.366 97.259  1.00 51.97  ? 408  TYR A CD1   1 
ATOM   11710 C  CD2   . TYR D 3 408 ? 141.873 167.442 95.350  1.00 48.08  ? 408  TYR A CD2   1 
ATOM   11711 C  CE1   . TYR D 3 408 ? 143.905 168.519 96.852  1.00 51.96  ? 408  TYR A CE1   1 
ATOM   11712 C  CE2   . TYR D 3 408 ? 142.493 168.593 94.936  1.00 52.49  ? 408  TYR A CE2   1 
ATOM   11713 C  CZ    . TYR D 3 408 ? 143.508 169.128 95.690  1.00 54.65  ? 408  TYR A CZ    1 
ATOM   11714 O  OH    . TYR D 3 408 ? 144.132 170.282 95.280  1.00 59.74  ? 408  TYR A OH    1 
ATOM   11715 N  N     . VAL D 3 409 ? 140.102 163.505 98.863  1.00 50.25  ? 409  VAL A N     1 
ATOM   11716 C  CA    . VAL D 3 409 ? 139.360 162.259 99.002  1.00 45.54  ? 409  VAL A CA    1 
ATOM   11717 C  C     . VAL D 3 409 ? 138.077 162.474 99.792  1.00 47.74  ? 409  VAL A C     1 
ATOM   11718 O  O     . VAL D 3 409 ? 137.067 161.803 99.548  1.00 55.32  ? 409  VAL A O     1 
ATOM   11719 C  CB    . VAL D 3 409 ? 140.265 161.192 99.643  1.00 44.01  ? 409  VAL A CB    1 
ATOM   11720 C  CG1   . VAL D 3 409 ? 139.482 159.956 99.975  1.00 47.87  ? 409  VAL A CG1   1 
ATOM   11721 C  CG2   . VAL D 3 409 ? 141.394 160.837 98.702  1.00 51.60  ? 409  VAL A CG2   1 
ATOM   11722 N  N     . GLY D 3 410 ? 138.075 163.425 100.719 1.00 49.95  ? 410  GLY A N     1 
ATOM   11723 C  CA    . GLY D 3 410 ? 136.928 163.682 101.556 1.00 51.21  ? 410  GLY A CA    1 
ATOM   11724 C  C     . GLY D 3 410 ? 135.810 164.465 100.913 1.00 52.48  ? 410  GLY A C     1 
ATOM   11725 O  O     . GLY D 3 410 ? 134.860 164.842 101.602 1.00 58.09  ? 410  GLY A O     1 
ATOM   11726 N  N     . GLU D 3 411 ? 135.886 164.728 99.613  1.00 57.62  ? 411  GLU A N     1 
ATOM   11727 C  CA    . GLU D 3 411 ? 134.842 165.451 98.899  1.00 62.19  ? 411  GLU A CA    1 
ATOM   11728 C  C     . GLU D 3 411 ? 134.502 164.755 97.590  1.00 67.13  ? 411  GLU A C     1 
ATOM   11729 O  O     . GLU D 3 411 ? 134.257 165.396 96.566  1.00 72.18  ? 411  GLU A O     1 
ATOM   11730 C  CB    . GLU D 3 411 ? 135.252 166.901 98.665  1.00 59.29  ? 411  GLU A CB    1 
ATOM   11731 C  CG    . GLU D 3 411 ? 134.966 167.795 99.858  1.00 62.42  ? 411  GLU A CG    1 
ATOM   11732 C  CD    . GLU D 3 411 ? 136.069 168.794 100.122 1.00 72.36  ? 411  GLU A CD    1 
ATOM   11733 O  OE1   . GLU D 3 411 ? 137.158 168.648 99.531  1.00 74.00  ? 411  GLU A OE1   1 
ATOM   11734 O  OE2   . GLU D 3 411 ? 135.850 169.724 100.926 1.00 75.27  ? 411  GLU A OE2   1 
ATOM   11735 N  N     . GLY D 3 412 ? 134.477 163.425 97.612  1.00 64.68  ? 412  GLY A N     1 
ATOM   11736 C  CA    . GLY D 3 412 ? 134.050 162.649 96.467  1.00 63.28  ? 412  GLY A CA    1 
ATOM   11737 C  C     . GLY D 3 412 ? 135.112 162.456 95.407  1.00 67.57  ? 412  GLY A C     1 
ATOM   11738 O  O     . GLY D 3 412 ? 134.912 162.835 94.250  1.00 75.23  ? 412  GLY A O     1 
ATOM   11739 N  N     . MET D 3 413 ? 136.244 161.869 95.782  1.00 62.08  ? 413  MET A N     1 
ATOM   11740 C  CA    . MET D 3 413 ? 137.302 161.595 94.822  1.00 62.21  ? 413  MET A CA    1 
ATOM   11741 C  C     . MET D 3 413 ? 138.096 160.382 95.272  1.00 66.48  ? 413  MET A C     1 
ATOM   11742 O  O     . MET D 3 413 ? 138.705 160.398 96.345  1.00 70.74  ? 413  MET A O     1 
ATOM   11743 C  CB    . MET D 3 413 ? 138.228 162.800 94.654  1.00 62.87  ? 413  MET A CB    1 
ATOM   11744 C  CG    . MET D 3 413 ? 139.479 162.490 93.869  1.00 65.71  ? 413  MET A CG    1 
ATOM   11745 S  SD    . MET D 3 413 ? 139.892 163.781 92.692  1.00 73.19  ? 413  MET A SD    1 
ATOM   11746 C  CE    . MET D 3 413 ? 139.672 165.233 93.708  1.00 66.67  ? 413  MET A CE    1 
ATOM   11747 N  N     . GLU D 3 414 ? 138.092 159.344 94.446  1.00 78.42  ? 414  GLU A N     1 
ATOM   11748 C  CA    . GLU D 3 414 ? 138.850 158.140 94.735  1.00 76.46  ? 414  GLU A CA    1 
ATOM   11749 C  C     . GLU D 3 414 ? 140.344 158.429 94.689  1.00 76.33  ? 414  GLU A C     1 
ATOM   11750 O  O     . GLU D 3 414 ? 140.813 159.279 93.927  1.00 79.51  ? 414  GLU A O     1 
ATOM   11751 C  CB    . GLU D 3 414 ? 138.501 157.034 93.740  1.00 76.37  ? 414  GLU A CB    1 
ATOM   11752 C  CG    . GLU D 3 414 ? 138.946 155.645 94.165  1.00 80.36  ? 414  GLU A CG    1 
ATOM   11753 C  CD    . GLU D 3 414 ? 138.801 154.622 93.055  1.00 84.03  ? 414  GLU A CD    1 
ATOM   11754 O  OE1   . GLU D 3 414 ? 138.911 155.008 91.873  1.00 81.95  ? 414  GLU A OE1   1 
ATOM   11755 O  OE2   . GLU D 3 414 ? 138.579 153.433 93.364  1.00 84.04  ? 414  GLU A OE2   1 
ATOM   11756 N  N     . GLU D 3 415 ? 141.093 157.714 95.528  1.00 74.30  ? 415  GLU A N     1 
ATOM   11757 C  CA    . GLU D 3 415 ? 142.543 157.843 95.545  1.00 73.93  ? 415  GLU A CA    1 
ATOM   11758 C  C     . GLU D 3 415 ? 143.177 157.453 94.218  1.00 77.79  ? 415  GLU A C     1 
ATOM   11759 O  O     . GLU D 3 415 ? 144.252 157.961 93.886  1.00 81.96  ? 415  GLU A O     1 
ATOM   11760 C  CB    . GLU D 3 415 ? 143.120 156.986 96.670  1.00 77.45  ? 415  GLU A CB    1 
ATOM   11761 C  CG    . GLU D 3 415 ? 144.569 157.266 97.002  1.00 79.14  ? 415  GLU A CG    1 
ATOM   11762 C  CD    . GLU D 3 415 ? 145.049 156.448 98.180  1.00 80.76  ? 415  GLU A CD    1 
ATOM   11763 O  OE1   . GLU D 3 415 ? 144.303 155.551 98.625  1.00 80.26  ? 415  GLU A OE1   1 
ATOM   11764 O  OE2   . GLU D 3 415 ? 146.171 156.697 98.662  1.00 78.89  ? 415  GLU A OE2   1 
ATOM   11765 N  N     . GLY D 3 416 ? 142.537 156.566 93.453  1.00 75.65  ? 416  GLY A N     1 
ATOM   11766 C  CA    . GLY D 3 416 ? 143.093 156.144 92.182  1.00 72.40  ? 416  GLY A CA    1 
ATOM   11767 C  C     . GLY D 3 416 ? 142.983 157.169 91.077  1.00 74.44  ? 416  GLY A C     1 
ATOM   11768 O  O     . GLY D 3 416 ? 143.645 157.022 90.044  1.00 77.79  ? 416  GLY A O     1 
ATOM   11769 N  N     . GLU D 3 417 ? 142.161 158.202 91.268  1.00 74.06  ? 417  GLU A N     1 
ATOM   11770 C  CA    . GLU D 3 417 ? 142.056 159.248 90.259  1.00 71.15  ? 417  GLU A CA    1 
ATOM   11771 C  C     . GLU D 3 417 ? 143.367 160.007 90.106  1.00 71.54  ? 417  GLU A C     1 
ATOM   11772 O  O     . GLU D 3 417 ? 143.715 160.421 88.995  1.00 80.63  ? 417  GLU A O     1 
ATOM   11773 C  CB    . GLU D 3 417 ? 140.914 160.200 90.607  1.00 73.08  ? 417  GLU A CB    1 
ATOM   11774 C  CG    . GLU D 3 417 ? 139.593 159.817 89.963  1.00 77.44  ? 417  GLU A CG    1 
ATOM   11775 C  CD    . GLU D 3 417 ? 138.458 160.742 90.353  1.00 81.71  ? 417  GLU A CD    1 
ATOM   11776 O  OE1   . GLU D 3 417 ? 138.115 160.791 91.553  1.00 81.61  ? 417  GLU A OE1   1 
ATOM   11777 O  OE2   . GLU D 3 417 ? 137.907 161.418 89.460  1.00 78.68  ? 417  GLU A OE2   1 
ATOM   11778 N  N     . PHE D 3 418 ? 144.110 160.183 91.199  1.00 57.34  ? 418  PHE A N     1 
ATOM   11779 C  CA    . PHE D 3 418 ? 145.416 160.826 91.109  1.00 62.80  ? 418  PHE A CA    1 
ATOM   11780 C  C     . PHE D 3 418 ? 146.368 160.011 90.246  1.00 63.74  ? 418  PHE A C     1 
ATOM   11781 O  O     . PHE D 3 418 ? 147.066 160.561 89.386  1.00 68.72  ? 418  PHE A O     1 
ATOM   11782 C  CB    . PHE D 3 418 ? 146.002 161.016 92.506  1.00 66.08  ? 418  PHE A CB    1 
ATOM   11783 C  CG    . PHE D 3 418 ? 145.283 162.037 93.333  1.00 63.93  ? 418  PHE A CG    1 
ATOM   11784 C  CD1   . PHE D 3 418 ? 144.116 161.710 93.993  1.00 67.48  ? 418  PHE A CD1   1 
ATOM   11785 C  CD2   . PHE D 3 418 ? 145.781 163.315 93.463  1.00 59.71  ? 418  PHE A CD2   1 
ATOM   11786 C  CE1   . PHE D 3 418 ? 143.457 162.640 94.755  1.00 67.02  ? 418  PHE A CE1   1 
ATOM   11787 C  CE2   . PHE D 3 418 ? 145.125 164.247 94.224  1.00 61.89  ? 418  PHE A CE2   1 
ATOM   11788 C  CZ    . PHE D 3 418 ? 143.963 163.910 94.872  1.00 64.78  ? 418  PHE A CZ    1 
ATOM   11789 N  N     . SER D 3 419 ? 146.405 158.696 90.460  1.00 64.89  ? 419  SER A N     1 
ATOM   11790 C  CA    . SER D 3 419 ? 147.273 157.838 89.662  1.00 66.98  ? 419  SER A CA    1 
ATOM   11791 C  C     . SER D 3 419 ? 146.837 157.818 88.204  1.00 70.47  ? 419  SER A C     1 
ATOM   11792 O  O     . SER D 3 419 ? 147.679 157.795 87.300  1.00 72.32  ? 419  SER A O     1 
ATOM   11793 C  CB    . SER D 3 419 ? 147.287 156.426 90.240  1.00 64.98  ? 419  SER A CB    1 
ATOM   11794 O  OG    . SER D 3 419 ? 145.982 155.879 90.271  1.00 71.25  ? 419  SER A OG    1 
ATOM   11795 N  N     . GLU D 3 420 ? 145.525 157.818 87.955  1.00 70.59  ? 420  GLU A N     1 
ATOM   11796 C  CA    . GLU D 3 420 ? 145.039 157.867 86.579  1.00 69.63  ? 420  GLU A CA    1 
ATOM   11797 C  C     . GLU D 3 420 ? 145.462 159.157 85.889  1.00 71.06  ? 420  GLU A C     1 
ATOM   11798 O  O     . GLU D 3 420 ? 145.903 159.138 84.733  1.00 74.18  ? 420  GLU A O     1 
ATOM   11799 C  CB    . GLU D 3 420 ? 143.520 157.723 86.553  1.00 68.71  ? 420  GLU A CB    1 
ATOM   11800 C  CG    . GLU D 3 420 ? 143.019 156.350 86.943  1.00 72.68  ? 420  GLU A CG    1 
ATOM   11801 C  CD    . GLU D 3 420 ? 141.537 156.187 86.690  1.00 77.07  ? 420  GLU A CD    1 
ATOM   11802 O  OE1   . GLU D 3 420 ? 140.970 157.010 85.941  1.00 76.45  ? 420  GLU A OE1   1 
ATOM   11803 O  OE2   . GLU D 3 420 ? 140.936 155.240 87.240  1.00 77.82  ? 420  GLU A OE2   1 
ATOM   11804 N  N     . ALA D 3 421 ? 145.341 160.288 86.586  1.00 64.04  ? 421  ALA A N     1 
ATOM   11805 C  CA    . ALA D 3 421 ? 145.768 161.559 86.012  1.00 63.24  ? 421  ALA A CA    1 
ATOM   11806 C  C     . ALA D 3 421 ? 147.268 161.571 85.750  1.00 64.66  ? 421  ALA A C     1 
ATOM   11807 O  O     . ALA D 3 421 ? 147.724 162.075 84.715  1.00 70.61  ? 421  ALA A O     1 
ATOM   11808 C  CB    . ALA D 3 421 ? 145.370 162.705 86.940  1.00 64.27  ? 421  ALA A CB    1 
ATOM   11809 N  N     . ARG D 3 422 ? 148.054 161.024 86.678  1.00 58.53  ? 422  ARG A N     1 
ATOM   11810 C  CA    . ARG D 3 422 ? 149.498 160.968 86.486  1.00 58.99  ? 422  ARG A CA    1 
ATOM   11811 C  C     . ARG D 3 422 ? 149.864 160.098 85.288  1.00 63.59  ? 422  ARG A C     1 
ATOM   11812 O  O     . ARG D 3 422 ? 150.766 160.441 84.514  1.00 70.57  ? 422  ARG A O     1 
ATOM   11813 C  CB    . ARG D 3 422 ? 150.171 160.454 87.756  1.00 60.75  ? 422  ARG A CB    1 
ATOM   11814 C  CG    . ARG D 3 422 ? 151.681 160.446 87.696  1.00 60.56  ? 422  ARG A CG    1 
ATOM   11815 C  CD    . ARG D 3 422 ? 152.226 161.798 87.290  1.00 56.30  ? 422  ARG A CD    1 
ATOM   11816 N  NE    . ARG D 3 422 ? 153.678 161.832 87.381  1.00 59.42  ? 422  ARG A NE    1 
ATOM   11817 C  CZ    . ARG D 3 422 ? 154.497 161.397 86.435  1.00 61.31  ? 422  ARG A CZ    1 
ATOM   11818 N  NH1   . ARG D 3 422 ? 154.038 160.914 85.293  1.00 60.71  ? 422  ARG A NH1   1 
ATOM   11819 N  NH2   . ARG D 3 422 ? 155.810 161.448 86.639  1.00 62.90  ? 422  ARG A NH2   1 
ATOM   11820 N  N     . GLU D 3 423 ? 149.180 158.964 85.124  1.00 67.93  ? 423  GLU A N     1 
ATOM   11821 C  CA    . GLU D 3 423 ? 149.423 158.109 83.967  1.00 65.42  ? 423  GLU A CA    1 
ATOM   11822 C  C     . GLU D 3 423 ? 149.056 158.815 82.669  1.00 68.45  ? 423  GLU A C     1 
ATOM   11823 O  O     . GLU D 3 423 ? 149.782 158.715 81.671  1.00 74.15  ? 423  GLU A O     1 
ATOM   11824 C  CB    . GLU D 3 423 ? 148.637 156.806 84.106  1.00 71.58  ? 423  GLU A CB    1 
ATOM   11825 C  CG    . GLU D 3 423 ? 148.934 155.783 83.019  1.00 76.67  ? 423  GLU A CG    1 
ATOM   11826 C  CD    . GLU D 3 423 ? 148.106 154.522 83.168  1.00 77.62  ? 423  GLU A CD    1 
ATOM   11827 O  OE1   . GLU D 3 423 ? 147.044 154.584 83.822  1.00 77.47  ? 423  GLU A OE1   1 
ATOM   11828 O  OE2   . GLU D 3 423 ? 148.516 153.470 82.633  1.00 73.10  ? 423  GLU A OE2   1 
ATOM   11829 N  N     . ASP D 3 424 ? 147.933 159.534 82.661  1.00 65.45  ? 424  ASP A N     1 
ATOM   11830 C  CA    . ASP D 3 424 ? 147.553 160.282 81.468  1.00 67.29  ? 424  ASP A CA    1 
ATOM   11831 C  C     . ASP D 3 424 ? 148.593 161.340 81.131  1.00 72.10  ? 424  ASP A C     1 
ATOM   11832 O  O     . ASP D 3 424 ? 148.912 161.558 79.957  1.00 74.36  ? 424  ASP A O     1 
ATOM   11833 C  CB    . ASP D 3 424 ? 146.184 160.924 81.663  1.00 65.04  ? 424  ASP A CB    1 
ATOM   11834 C  CG    . ASP D 3 424 ? 145.087 160.169 80.960  1.00 71.80  ? 424  ASP A CG    1 
ATOM   11835 O  OD1   . ASP D 3 424 ? 145.300 159.732 79.810  1.00 72.78  ? 424  ASP A OD1   1 
ATOM   11836 O  OD2   . ASP D 3 424 ? 144.007 160.012 81.560  1.00 76.30  ? 424  ASP A OD2   1 
ATOM   11837 N  N     . MET D 3 425 ? 149.132 162.011 82.150  1.00 68.01  ? 425  MET A N     1 
ATOM   11838 C  CA    . MET D 3 425 ? 150.156 163.023 81.904  1.00 65.40  ? 425  MET A CA    1 
ATOM   11839 C  C     . MET D 3 425 ? 151.446 162.406 81.382  1.00 68.07  ? 425  MET A C     1 
ATOM   11840 O  O     . MET D 3 425 ? 152.115 162.988 80.520  1.00 74.06  ? 425  MET A O     1 
ATOM   11841 C  CB    . MET D 3 425 ? 150.418 163.823 83.175  1.00 70.63  ? 425  MET A CB    1 
ATOM   11842 C  CG    . MET D 3 425 ? 150.824 165.249 82.907  1.00 69.06  ? 425  MET A CG    1 
ATOM   11843 S  SD    . MET D 3 425 ? 149.379 166.260 82.601  1.00 71.40  ? 425  MET A SD    1 
ATOM   11844 C  CE    . MET D 3 425 ? 148.143 165.364 83.537  1.00 70.90  ? 425  MET A CE    1 
ATOM   11845 N  N     . ALA D 3 426 ? 151.822 161.240 81.906  1.00 62.97  ? 426  ALA A N     1 
ATOM   11846 C  CA    . ALA D 3 426 ? 152.973 160.535 81.354  1.00 60.23  ? 426  ALA A CA    1 
ATOM   11847 C  C     . ALA D 3 426 ? 152.734 160.181 79.893  1.00 62.49  ? 426  ALA A C     1 
ATOM   11848 O  O     . ALA D 3 426 ? 153.643 160.288 79.062  1.00 68.02  ? 426  ALA A O     1 
ATOM   11849 C  CB    . ALA D 3 426 ? 153.270 159.281 82.176  1.00 63.64  ? 426  ALA A CB    1 
ATOM   11850 N  N     . ALA D 3 427 ? 151.513 159.757 79.565  1.00 58.72  ? 427  ALA A N     1 
ATOM   11851 C  CA    . ALA D 3 427 ? 151.179 159.455 78.178  1.00 59.92  ? 427  ALA A CA    1 
ATOM   11852 C  C     . ALA D 3 427 ? 151.285 160.694 77.299  1.00 61.71  ? 427  ALA A C     1 
ATOM   11853 O  O     . ALA D 3 427 ? 151.764 160.617 76.163  1.00 66.58  ? 427  ALA A O     1 
ATOM   11854 C  CB    . ALA D 3 427 ? 149.776 158.859 78.095  1.00 60.46  ? 427  ALA A CB    1 
ATOM   11855 N  N     . LEU D 3 428 ? 150.830 161.844 77.800  1.00 58.61  ? 428  LEU A N     1 
ATOM   11856 C  CA    . LEU D 3 428 ? 150.927 163.080 77.025  1.00 57.48  ? 428  LEU A CA    1 
ATOM   11857 C  C     . LEU D 3 428 ? 152.381 163.482 76.801  1.00 61.44  ? 428  LEU A C     1 
ATOM   11858 O  O     . LEU D 3 428 ? 152.759 163.907 75.699  1.00 72.80  ? 428  LEU A O     1 
ATOM   11859 C  CB    . LEU D 3 428 ? 150.165 164.201 77.729  1.00 57.86  ? 428  LEU A CB    1 
ATOM   11860 C  CG    . LEU D 3 428 ? 149.923 165.476 76.923  1.00 57.73  ? 428  LEU A CG    1 
ATOM   11861 C  CD1   . LEU D 3 428 ? 149.312 165.148 75.576  1.00 63.31  ? 428  LEU A CD1   1 
ATOM   11862 C  CD2   . LEU D 3 428 ? 149.037 166.430 77.695  1.00 58.08  ? 428  LEU A CD2   1 
ATOM   11863 N  N     . GLU D 3 429 ? 153.212 163.353 77.836  1.00 62.07  ? 429  GLU A N     1 
ATOM   11864 C  CA    . GLU D 3 429 ? 154.635 163.631 77.681  1.00 56.97  ? 429  GLU A CA    1 
ATOM   11865 C  C     . GLU D 3 429 ? 155.267 162.694 76.662  1.00 62.21  ? 429  GLU A C     1 
ATOM   11866 O  O     . GLU D 3 429 ? 156.083 163.118 75.831  1.00 69.48  ? 429  GLU A O     1 
ATOM   11867 C  CB    . GLU D 3 429 ? 155.340 163.507 79.030  1.00 63.92  ? 429  GLU A CB    1 
ATOM   11868 C  CG    . GLU D 3 429 ? 155.213 164.732 79.913  1.00 70.24  ? 429  GLU A CG    1 
ATOM   11869 C  CD    . GLU D 3 429 ? 156.429 164.941 80.791  1.00 75.68  ? 429  GLU A CD    1 
ATOM   11870 O  OE1   . GLU D 3 429 ? 157.521 165.190 80.239  1.00 75.96  ? 429  GLU A OE1   1 
ATOM   11871 O  OE2   . GLU D 3 429 ? 156.294 164.857 82.029  1.00 73.40  ? 429  GLU A OE2   1 
ATOM   11872 N  N     . LYS D 3 430 ? 154.898 161.414 76.708  1.00 63.49  ? 430  LYS A N     1 
ATOM   11873 C  CA    . LYS D 3 430 ? 155.428 160.454 75.749  1.00 64.64  ? 430  LYS A CA    1 
ATOM   11874 C  C     . LYS D 3 430 ? 154.988 160.796 74.334  1.00 63.30  ? 430  LYS A C     1 
ATOM   11875 O  O     . LYS D 3 430 ? 155.767 160.659 73.386  1.00 70.82  ? 430  LYS A O     1 
ATOM   11876 C  CB    . LYS D 3 430 ? 154.984 159.041 76.125  1.00 67.38  ? 430  LYS A CB    1 
ATOM   11877 C  CG    . LYS D 3 430 ? 155.658 157.942 75.327  1.00 68.90  ? 430  LYS A CG    1 
ATOM   11878 C  CD    . LYS D 3 430 ? 155.159 156.575 75.762  1.00 69.35  ? 430  LYS A CD    1 
ATOM   11879 C  CE    . LYS D 3 430 ? 155.502 156.305 77.218  1.00 66.27  ? 430  LYS A CE    1 
ATOM   11880 N  NZ    . LYS D 3 430 ? 155.053 154.956 77.659  1.00 69.78  ? 430  LYS A NZ    1 
ATOM   11881 N  N     . ASP D 3 431 ? 153.743 161.245 74.171  1.00 61.01  ? 431  ASP A N     1 
ATOM   11882 C  CA    . ASP D 3 431 ? 153.261 161.631 72.850  1.00 64.66  ? 431  ASP A CA    1 
ATOM   11883 C  C     . ASP D 3 431 ? 154.028 162.831 72.315  1.00 60.75  ? 431  ASP A C     1 
ATOM   11884 O  O     . ASP D 3 431 ? 154.365 162.881 71.126  1.00 65.49  ? 431  ASP A O     1 
ATOM   11885 C  CB    . ASP D 3 431 ? 151.765 161.933 72.903  1.00 66.75  ? 431  ASP A CB    1 
ATOM   11886 C  CG    . ASP D 3 431 ? 150.918 160.680 72.885  1.00 71.82  ? 431  ASP A CG    1 
ATOM   11887 O  OD1   . ASP D 3 431 ? 151.294 159.716 72.186  1.00 69.14  ? 431  ASP A OD1   1 
ATOM   11888 O  OD2   . ASP D 3 431 ? 149.876 160.656 73.571  1.00 71.78  ? 431  ASP A OD2   1 
ATOM   11889 N  N     . TYR D 3 432 ? 154.306 163.811 73.174  1.00 53.55  ? 432  TYR A N     1 
ATOM   11890 C  CA    . TYR D 3 432 ? 155.081 164.968 72.732  1.00 58.26  ? 432  TYR A CA    1 
ATOM   11891 C  C     . TYR D 3 432 ? 156.497 164.567 72.337  1.00 59.25  ? 432  TYR A C     1 
ATOM   11892 O  O     . TYR D 3 432 ? 157.025 165.036 71.321  1.00 67.53  ? 432  TYR A O     1 
ATOM   11893 C  CB    . TYR D 3 432 ? 155.104 166.035 73.823  1.00 58.33  ? 432  TYR A CB    1 
ATOM   11894 C  CG    . TYR D 3 432 ? 154.259 167.237 73.489  1.00 59.41  ? 432  TYR A CG    1 
ATOM   11895 C  CD1   . TYR D 3 432 ? 154.750 168.248 72.683  1.00 60.70  ? 432  TYR A CD1   1 
ATOM   11896 C  CD2   . TYR D 3 432 ? 152.962 167.347 73.958  1.00 61.76  ? 432  TYR A CD2   1 
ATOM   11897 C  CE1   . TYR D 3 432 ? 153.979 169.343 72.369  1.00 62.39  ? 432  TYR A CE1   1 
ATOM   11898 C  CE2   . TYR D 3 432 ? 152.185 168.436 73.648  1.00 62.27  ? 432  TYR A CE2   1 
ATOM   11899 C  CZ    . TYR D 3 432 ? 152.697 169.430 72.852  1.00 64.73  ? 432  TYR A CZ    1 
ATOM   11900 O  OH    . TYR D 3 432 ? 151.920 170.522 72.543  1.00 64.47  ? 432  TYR A OH    1 
ATOM   11901 N  N     . GLU D 3 433 ? 157.126 163.691 73.121  1.00 56.54  ? 433  GLU A N     1 
ATOM   11902 C  CA    . GLU D 3 433 ? 158.458 163.223 72.756  1.00 55.81  ? 433  GLU A CA    1 
ATOM   11903 C  C     . GLU D 3 433 ? 158.432 162.450 71.442  1.00 60.87  ? 433  GLU A C     1 
ATOM   11904 O  O     . GLU D 3 433 ? 159.339 162.591 70.613  1.00 62.76  ? 433  GLU A O     1 
ATOM   11905 C  CB    . GLU D 3 433 ? 159.041 162.363 73.876  1.00 61.20  ? 433  GLU A CB    1 
ATOM   11906 C  CG    . GLU D 3 433 ? 160.487 161.966 73.656  1.00 66.35  ? 433  GLU A CG    1 
ATOM   11907 C  CD    . GLU D 3 433 ? 161.043 161.149 74.803  1.00 68.54  ? 433  GLU A CD    1 
ATOM   11908 O  OE1   . GLU D 3 433 ? 160.264 160.789 75.710  1.00 72.38  ? 433  GLU A OE1   1 
ATOM   11909 O  OE2   . GLU D 3 433 ? 162.259 160.864 74.797  1.00 66.19  ? 433  GLU A OE2   1 
ATOM   11910 N  N     . GLU D 3 434 ? 157.406 161.623 71.238  1.00 67.56  ? 434  GLU A N     1 
ATOM   11911 C  CA    . GLU D 3 434 ? 157.306 160.843 70.009  1.00 65.28  ? 434  GLU A CA    1 
ATOM   11912 C  C     . GLU D 3 434 ? 157.117 161.745 68.798  1.00 65.13  ? 434  GLU A C     1 
ATOM   11913 O  O     . GLU D 3 434 ? 157.745 161.538 67.753  1.00 72.85  ? 434  GLU A O     1 
ATOM   11914 C  CB    . GLU D 3 434 ? 156.156 159.842 70.117  1.00 69.43  ? 434  GLU A CB    1 
ATOM   11915 C  CG    . GLU D 3 434 ? 156.448 158.649 71.013  1.00 72.20  ? 434  GLU A CG    1 
ATOM   11916 C  CD    . GLU D 3 434 ? 155.251 157.733 71.172  1.00 77.14  ? 434  GLU A CD    1 
ATOM   11917 O  OE1   . GLU D 3 434 ? 154.369 157.746 70.287  1.00 76.55  ? 434  GLU A OE1   1 
ATOM   11918 O  OE2   . GLU D 3 434 ? 155.190 157.002 72.182  1.00 75.07  ? 434  GLU A OE2   1 
ATOM   11919 N  N     . VAL D 3 435 ? 156.251 162.752 68.915  1.00 52.05  ? 435  VAL A N     1 
ATOM   11920 C  CA    . VAL D 3 435 ? 156.033 163.652 67.790  1.00 52.15  ? 435  VAL A CA    1 
ATOM   11921 C  C     . VAL D 3 435 ? 157.260 164.520 67.554  1.00 49.85  ? 435  VAL A C     1 
ATOM   11922 O  O     . VAL D 3 435 ? 157.476 165.010 66.440  1.00 45.46  ? 435  VAL A O     1 
ATOM   11923 C  CB    . VAL D 3 435 ? 154.763 164.496 68.010  1.00 51.15  ? 435  VAL A CB    1 
ATOM   11924 C  CG1   . VAL D 3 435 ? 154.994 165.563 69.051  1.00 52.29  ? 435  VAL A CG1   1 
ATOM   11925 C  CG2   . VAL D 3 435 ? 154.307 165.118 66.703  1.00 53.24  ? 435  VAL A CG2   1 
ATOM   11926 N  N     . GLY D 3 436 ? 158.083 164.727 68.582  1.00 58.53  ? 436  GLY A N     1 
ATOM   11927 C  CA    . GLY D 3 436 ? 159.312 165.476 68.381  1.00 55.29  ? 436  GLY A CA    1 
ATOM   11928 C  C     . GLY D 3 436 ? 160.287 164.777 67.451  1.00 54.21  ? 436  GLY A C     1 
ATOM   11929 O  O     . GLY D 3 436 ? 160.842 165.397 66.541  1.00 54.93  ? 436  GLY A O     1 
ATOM   11930 N  N     . VAL D 3 437 ? 160.503 163.483 67.660  1.00 63.22  ? 437  VAL A N     1 
ATOM   11931 C  CA    . VAL D 3 437 ? 161.487 162.731 66.892  1.00 62.06  ? 437  VAL A CA    1 
ATOM   11932 C  C     . VAL D 3 437 ? 161.067 162.607 65.434  1.00 66.89  ? 437  VAL A C     1 
ATOM   11933 O  O     . VAL D 3 437 ? 159.920 162.277 65.134  1.00 68.86  ? 437  VAL A O     1 
ATOM   11934 C  CB    . VAL D 3 437 ? 161.712 161.340 67.505  1.00 65.39  ? 437  VAL A CB    1 
ATOM   11935 C  CG1   . VAL D 3 437 ? 162.673 160.528 66.651  1.00 66.30  ? 437  VAL A CG1   1 
ATOM   11936 C  CG2   . VAL D 3 437 ? 162.231 161.466 68.930  1.00 63.49  ? 437  VAL A CG2   1 
ATOM   11937 N  N     A ALA E 2 918 ? 119.052 139.366 138.591 0.50 76.64  ? 918  ALA T N     1 
ATOM   11938 C  CA    A ALA E 2 918 ? 120.456 139.459 138.210 0.50 78.85  ? 918  ALA T CA    1 
ATOM   11939 C  C     A ALA E 2 918 ? 120.687 138.872 136.824 0.50 79.38  ? 918  ALA T C     1 
ATOM   11940 O  O     A ALA E 2 918 ? 119.740 138.624 136.078 0.50 78.64  ? 918  ALA T O     1 
ATOM   11941 C  CB    A ALA E 2 918 ? 121.331 138.757 139.233 0.50 78.75  ? 918  ALA T CB    1 
ATOM   11942 N  N     A GLN E 2 919 ? 121.954 138.650 136.488 0.50 75.36  ? 919  GLN T N     1 
ATOM   11943 C  CA    A GLN E 2 919 ? 122.345 138.108 135.196 0.50 75.95  ? 919  GLN T CA    1 
ATOM   11944 C  C     A GLN E 2 919 ? 123.160 136.838 135.396 0.50 80.28  ? 919  GLN T C     1 
ATOM   11945 O  O     A GLN E 2 919 ? 124.005 136.764 136.294 0.50 81.05  ? 919  GLN T O     1 
ATOM   11946 C  CB    A GLN E 2 919 ? 123.154 139.130 134.391 0.50 71.20  ? 919  GLN T CB    1 
ATOM   11947 C  CG    A GLN E 2 919 ? 124.279 139.784 135.172 0.50 72.20  ? 919  GLN T CG    1 
ATOM   11948 C  CD    A GLN E 2 919 ? 124.895 140.955 134.438 0.50 77.92  ? 919  GLN T CD    1 
ATOM   11949 O  OE1   A GLN E 2 919 ? 124.506 141.272 133.314 0.50 78.07  ? 919  GLN T OE1   1 
ATOM   11950 N  NE2   A GLN E 2 919 ? 125.863 141.607 135.070 0.50 76.79  ? 919  GLN T NE2   1 
ATOM   11951 N  N     A ILE E 2 920 ? 122.898 135.840 134.558 0.50 70.98  ? 920  ILE T N     1 
ATOM   11952 C  CA    A ILE E 2 920 ? 123.620 134.574 134.577 0.50 63.18  ? 920  ILE T CA    1 
ATOM   11953 C  C     A ILE E 2 920 ? 124.485 134.511 133.328 0.50 65.89  ? 920  ILE T C     1 
ATOM   11954 O  O     A ILE E 2 920 ? 123.966 134.522 132.205 0.50 71.24  ? 920  ILE T O     1 
ATOM   11955 C  CB    A ILE E 2 920 ? 122.665 133.374 134.640 0.50 61.49  ? 920  ILE T CB    1 
ATOM   11956 C  CG1   A ILE E 2 920 ? 121.902 133.364 135.962 0.50 66.48  ? 920  ILE T CG1   1 
ATOM   11957 C  CG2   A ILE E 2 920 ? 123.430 132.074 134.455 0.50 65.73  ? 920  ILE T CG2   1 
ATOM   11958 C  CD1   A ILE E 2 920 ? 121.001 132.164 136.125 0.50 63.91  ? 920  ILE T CD1   1 
ATOM   11959 N  N     A ALA E 2 921 ? 125.799 134.448 133.519 0.50 58.35  ? 921  ALA T N     1 
ATOM   11960 C  CA    A ALA E 2 921 ? 126.697 134.235 132.398 0.50 52.21  ? 921  ALA T CA    1 
ATOM   11961 C  C     A ALA E 2 921 ? 126.464 132.852 131.807 0.50 54.44  ? 921  ALA T C     1 
ATOM   11962 O  O     A ALA E 2 921 ? 126.017 131.927 132.491 0.50 65.61  ? 921  ALA T O     1 
ATOM   11963 C  CB    A ALA E 2 921 ? 128.152 134.388 132.834 0.50 54.99  ? 921  ALA T CB    1 
ATOM   11964 N  N     A LYS E 2 922 ? 126.770 132.712 130.519 0.50 53.61  ? 922  LYS T N     1 
ATOM   11965 C  CA    A LYS E 2 922 ? 126.444 131.507 129.758 0.50 60.73  ? 922  LYS T CA    1 
ATOM   11966 C  C     A LYS E 2 922 ? 127.719 130.911 129.178 0.50 60.65  ? 922  LYS T C     1 
ATOM   11967 O  O     A LYS E 2 922 ? 128.041 131.135 128.000 0.50 64.95  ? 922  LYS T O     1 
ATOM   11968 C  CB    A LYS E 2 922 ? 125.440 131.823 128.651 0.50 67.12  ? 922  LYS T CB    1 
ATOM   11969 C  CG    A LYS E 2 922 ? 124.332 132.778 129.060 0.50 68.66  ? 922  LYS T CG    1 
ATOM   11970 C  CD    A LYS E 2 922 ? 123.490 133.182 127.860 0.50 65.48  ? 922  LYS T CD    1 
ATOM   11971 C  CE    A LYS E 2 922 ? 122.488 134.263 128.227 0.50 65.45  ? 922  LYS T CE    1 
ATOM   11972 N  NZ    A LYS E 2 922 ? 121.705 134.713 127.044 0.50 64.89  ? 922  LYS T NZ    1 
ATOM   11973 N  N     A PRO E 2 923 ? 128.472 130.149 129.960 0.50 48.76  ? 923  PRO T N     1 
ATOM   11974 C  CA    A PRO E 2 923 ? 129.652 129.467 129.430 0.50 56.42  ? 923  PRO T CA    1 
ATOM   11975 C  C     A PRO E 2 923 ? 129.289 128.104 128.852 0.50 51.87  ? 923  PRO T C     1 
ATOM   11976 O  O     A PRO E 2 923 ? 128.207 127.564 129.087 0.50 52.54  ? 923  PRO T O     1 
ATOM   11977 C  CB    A PRO E 2 923 ? 130.546 129.323 130.665 0.50 52.78  ? 923  PRO T CB    1 
ATOM   11978 C  CG    A PRO E 2 923 ? 129.585 129.197 131.788 0.50 56.41  ? 923  PRO T CG    1 
ATOM   11979 C  CD    A PRO E 2 923 ? 128.336 129.960 131.413 0.50 53.24  ? 923  PRO T CD    1 
ATOM   11980 N  N     A ILE E 2 924 ? 130.225 127.555 128.080 0.50 52.11  ? 924  ILE T N     1 
ATOM   11981 C  CA    A ILE E 2 924 ? 130.034 126.277 127.413 0.50 44.24  ? 924  ILE T CA    1 
ATOM   11982 C  C     A ILE E 2 924 ? 131.174 125.345 127.794 0.50 50.38  ? 924  ILE T C     1 
ATOM   11983 O  O     A ILE E 2 924 ? 132.261 125.775 128.187 0.50 62.70  ? 924  ILE T O     1 
ATOM   11984 C  CB    A ILE E 2 924 ? 129.946 126.422 125.879 0.50 52.58  ? 924  ILE T CB    1 
ATOM   11985 C  CG1   A ILE E 2 924 ? 131.288 126.869 125.302 0.50 55.22  ? 924  ILE T CG1   1 
ATOM   11986 C  CG2   A ILE E 2 924 ? 128.853 127.401 125.498 0.50 56.06  ? 924  ILE T CG2   1 
ATOM   11987 C  CD1   A ILE E 2 924 ? 131.268 127.056 123.804 0.50 53.63  ? 924  ILE T CD1   1 
ATOM   11988 N  N     A ARG E 2 925 ? 130.907 124.051 127.675 0.50 60.16  ? 925  ARG T N     1 
ATOM   11989 C  CA    A ARG E 2 925 ? 131.846 123.001 128.026 0.50 62.64  ? 925  ARG T CA    1 
ATOM   11990 C  C     A ARG E 2 925 ? 131.896 121.966 126.913 0.50 66.43  ? 925  ARG T C     1 
ATOM   11991 O  O     A ARG E 2 925 ? 130.933 121.820 126.152 0.50 69.08  ? 925  ARG T O     1 
ATOM   11992 C  CB    A ARG E 2 925 ? 131.448 122.324 129.348 0.50 65.73  ? 925  ARG T CB    1 
ATOM   11993 C  CG    A ARG E 2 925 ? 130.357 121.266 129.218 0.50 66.67  ? 925  ARG T CG    1 
ATOM   11994 C  CD    A ARG E 2 925 ? 128.985 121.886 128.995 0.50 68.20  ? 925  ARG T CD    1 
ATOM   11995 N  NE    A ARG E 2 925 ? 127.993 120.895 128.595 0.50 71.02  ? 925  ARG T NE    1 
ATOM   11996 C  CZ    A ARG E 2 925 ? 126.759 121.185 128.207 0.50 72.64  ? 925  ARG T CZ    1 
ATOM   11997 N  NH1   A ARG E 2 925 ? 126.326 122.434 128.152 0.50 71.52  ? 925  ARG T NH1   1 
ATOM   11998 N  NH2   A ARG E 2 925 ? 125.938 120.196 127.865 0.50 70.26  ? 925  ARG T NH2   1 
ATOM   11999 N  N     A PRO E 2 926 ? 133.015 121.239 126.781 0.50 60.89  ? 926  PRO T N     1 
ATOM   12000 C  CA    A PRO E 2 926 ? 133.128 120.173 125.784 0.50 60.10  ? 926  PRO T CA    1 
ATOM   12001 C  C     A PRO E 2 926 ? 132.710 118.813 126.331 0.50 67.15  ? 926  PRO T C     1 
ATOM   12002 O  O     A PRO E 2 926 ? 132.207 118.751 127.453 0.50 71.91  ? 926  PRO T O     1 
ATOM   12003 C  CB    A PRO E 2 926 ? 134.617 120.181 125.429 0.50 59.27  ? 926  PRO T CB    1 
ATOM   12004 C  CG    A PRO E 2 926 ? 135.305 120.910 126.555 0.50 58.47  ? 926  PRO T CG    1 
ATOM   12005 C  CD    A PRO E 2 926 ? 134.278 121.437 127.508 0.50 59.51  ? 926  PRO T CD    1 
ATOM   12006 N  N     B ALA F 2 918 ? 134.202 119.485 125.879 0.50 48.58  ? 918  ALA t N     1 
ATOM   12007 C  CA    B ALA F 2 918 ? 134.308 120.681 126.705 0.50 55.80  ? 918  ALA t CA    1 
ATOM   12008 C  C     B ALA F 2 918 ? 132.949 121.355 126.846 0.50 61.25  ? 918  ALA t C     1 
ATOM   12009 O  O     B ALA F 2 918 ? 131.998 120.999 126.154 0.50 62.70  ? 918  ALA t O     1 
ATOM   12010 C  CB    B ALA F 2 918 ? 135.320 121.641 126.116 0.50 54.59  ? 918  ALA t CB    1 
ATOM   12011 N  N     B GLN F 2 919 ? 132.863 122.334 127.743 0.50 62.82  ? 919  GLN t N     1 
ATOM   12012 C  CA    B GLN F 2 919 ? 131.608 122.993 128.062 0.50 57.25  ? 919  GLN t CA    1 
ATOM   12013 C  C     B GLN F 2 919 ? 131.708 124.487 127.793 0.50 57.92  ? 919  GLN t C     1 
ATOM   12014 O  O     B GLN F 2 919 ? 132.792 125.075 127.842 0.50 69.99  ? 919  GLN t O     1 
ATOM   12015 C  CB    B GLN F 2 919 ? 131.215 122.756 129.524 0.50 63.27  ? 919  GLN t CB    1 
ATOM   12016 C  CG    B GLN F 2 919 ? 130.758 121.339 129.823 0.50 68.51  ? 919  GLN t CG    1 
ATOM   12017 C  CD    B GLN F 2 919 ? 129.456 120.985 129.130 0.50 73.77  ? 919  GLN t CD    1 
ATOM   12018 O  OE1   B GLN F 2 919 ? 128.610 121.847 128.893 0.50 70.20  ? 919  GLN t OE1   1 
ATOM   12019 N  NE2   B GLN F 2 919 ? 129.290 119.709 128.801 0.50 70.21  ? 919  GLN t NE2   1 
ATOM   12020 N  N     B ILE F 2 920 ? 130.561 125.095 127.509 0.50 46.37  ? 920  ILE t N     1 
ATOM   12021 C  CA    B ILE F 2 920 ? 130.450 126.525 127.253 0.50 45.59  ? 920  ILE t CA    1 
ATOM   12022 C  C     B ILE F 2 920 ? 129.505 127.114 128.288 0.50 53.11  ? 920  ILE t C     1 
ATOM   12023 O  O     B ILE F 2 920 ? 128.406 126.591 128.499 0.50 59.96  ? 920  ILE t O     1 
ATOM   12024 C  CB    B ILE F 2 920 ? 129.950 126.810 125.825 0.50 51.50  ? 920  ILE t CB    1 
ATOM   12025 C  CG1   B ILE F 2 920 ? 130.883 126.174 124.796 0.50 55.10  ? 920  ILE t CG1   1 
ATOM   12026 C  CG2   B ILE F 2 920 ? 129.842 128.305 125.587 0.50 53.74  ? 920  ILE t CG2   1 
ATOM   12027 C  CD1   B ILE F 2 920 ? 130.464 126.415 123.365 0.50 56.65  ? 920  ILE t CD1   1 
ATOM   12028 N  N     B ALA F 2 921 ? 129.930 128.197 128.929 0.50 54.47  ? 921  ALA t N     1 
ATOM   12029 C  CA    B ALA F 2 921 ? 129.212 128.782 130.052 0.50 52.18  ? 921  ALA t CA    1 
ATOM   12030 C  C     B ALA F 2 921 ? 128.663 130.149 129.676 0.50 49.06  ? 921  ALA t C     1 
ATOM   12031 O  O     B ALA F 2 921 ? 129.360 130.953 129.049 0.50 58.28  ? 921  ALA t O     1 
ATOM   12032 C  CB    B ALA F 2 921 ? 130.124 128.908 131.273 0.50 56.51  ? 921  ALA t CB    1 
ATOM   12033 N  N     B LYS F 2 922 ? 127.416 130.406 130.061 0.50 57.48  ? 922  LYS t N     1 
ATOM   12034 C  CA    B LYS F 2 922 ? 126.792 131.712 129.896 0.50 63.43  ? 922  LYS t CA    1 
ATOM   12035 C  C     B LYS F 2 922 ? 126.445 132.268 131.268 0.50 64.23  ? 922  LYS t C     1 
ATOM   12036 O  O     B LYS F 2 922 ? 125.642 131.653 131.992 0.50 69.87  ? 922  LYS t O     1 
ATOM   12037 C  CB    B LYS F 2 922 ? 125.538 131.618 129.026 0.50 69.31  ? 922  LYS t CB    1 
ATOM   12038 C  CG    B LYS F 2 922 ? 124.831 132.944 128.809 0.50 70.25  ? 922  LYS t CG    1 
ATOM   12039 C  CD    B LYS F 2 922 ? 123.651 132.790 127.864 0.50 68.94  ? 922  LYS t CD    1 
ATOM   12040 C  CE    B LYS F 2 922 ? 122.951 134.117 127.632 0.50 68.95  ? 922  LYS t CE    1 
ATOM   12041 N  NZ    B LYS F 2 922 ? 121.809 133.980 126.687 0.50 68.56  ? 922  LYS t NZ    1 
ATOM   12042 N  N     B PRO F 2 923 ? 127.019 133.396 131.679 0.50 60.14  ? 923  PRO t N     1 
ATOM   12043 C  CA    B PRO F 2 923 ? 126.690 133.952 132.996 0.50 63.68  ? 923  PRO t CA    1 
ATOM   12044 C  C     B PRO F 2 923 ? 125.212 134.292 133.104 0.50 65.94  ? 923  PRO t C     1 
ATOM   12045 O  O     B PRO F 2 923 ? 124.593 134.769 132.151 0.50 65.03  ? 923  PRO t O     1 
ATOM   12046 C  CB    B PRO F 2 923 ? 127.564 135.209 133.080 0.50 64.64  ? 923  PRO t CB    1 
ATOM   12047 C  CG    B PRO F 2 923 ? 128.662 134.978 132.100 0.50 65.57  ? 923  PRO t CG    1 
ATOM   12048 C  CD    B PRO F 2 923 ? 128.057 134.178 130.990 0.50 67.39  ? 923  PRO t CD    1 
ATOM   12049 N  N     B ILE F 2 924 ? 124.650 134.040 134.279 0.50 76.25  ? 924  ILE t N     1 
ATOM   12050 C  CA    B ILE F 2 924 ? 123.240 134.304 134.545 0.50 72.27  ? 924  ILE t CA    1 
ATOM   12051 C  C     B ILE F 2 924 ? 123.190 135.609 135.331 0.50 77.89  ? 924  ILE t C     1 
ATOM   12052 O  O     B ILE F 2 924 ? 123.255 135.629 136.560 0.50 78.10  ? 924  ILE t O     1 
ATOM   12053 C  CB    B ILE F 2 924 ? 122.571 133.150 135.286 0.50 72.99  ? 924  ILE t CB    1 
ATOM   12054 C  CG1   B ILE F 2 924 ? 122.746 131.855 134.495 0.50 77.54  ? 924  ILE t CG1   1 
ATOM   12055 C  CG2   B ILE F 2 924 ? 121.095 133.432 135.487 0.50 71.70  ? 924  ILE t CG2   1 
ATOM   12056 C  CD1   B ILE F 2 924 ? 122.368 131.989 133.038 0.50 76.14  ? 924  ILE t CD1   1 
ATOM   12057 N  N     B ARG F 2 925 ? 123.080 136.718 134.602 0.50 90.99  ? 925  ARG t N     1 
ATOM   12058 C  CA    B ARG F 2 925 ? 122.979 138.035 135.208 0.50 88.12  ? 925  ARG t CA    1 
ATOM   12059 C  C     B ARG F 2 925 ? 121.518 138.441 135.273 0.50 90.53  ? 925  ARG t C     1 
ATOM   12060 O  O     B ARG F 2 925 ? 120.860 138.509 134.223 0.50 93.23  ? 925  ARG t O     1 
ATOM   12061 C  CB    B ARG F 2 925 ? 123.776 139.057 134.406 0.50 84.70  ? 925  ARG t CB    1 
ATOM   12062 C  CG    B ARG F 2 925 ? 124.188 140.279 135.199 0.50 83.48  ? 925  ARG t CG    1 
ATOM   12063 C  CD    B ARG F 2 925 ? 125.260 141.067 134.471 0.50 86.31  ? 925  ARG t CD    1 
ATOM   12064 N  NE    B ARG F 2 925 ? 125.835 142.110 135.311 0.50 91.88  ? 925  ARG t NE    1 
ATOM   12065 C  CZ    B ARG F 2 925 ? 126.845 142.890 134.950 0.50 94.16  ? 925  ARG t CZ    1 
ATOM   12066 N  NH1   B ARG F 2 925 ? 127.418 142.774 133.763 0.50 93.46  ? 925  ARG t NH1   1 
ATOM   12067 N  NH2   B ARG F 2 925 ? 127.289 143.811 135.801 0.50 92.63  ? 925  ARG t NH2   1 
ATOM   12068 N  N     B PRO F 2 926 ? 120.965 138.708 136.464 0.50 89.83  ? 926  PRO t N     1 
ATOM   12069 C  CA    B PRO F 2 926 ? 119.558 139.085 136.645 0.50 92.12  ? 926  PRO t CA    1 
ATOM   12070 C  C     B PRO F 2 926 ? 119.164 140.324 135.847 0.50 94.48  ? 926  PRO t C     1 
ATOM   12071 O  O     B PRO F 2 926 ? 118.147 140.284 135.153 0.50 91.35  ? 926  PRO t O     1 
ATOM   12072 C  CB    B PRO F 2 926 ? 119.457 139.361 138.150 0.50 88.89  ? 926  PRO t CB    1 
ATOM   12073 C  CG    B PRO F 2 926 ? 120.859 139.557 138.609 0.50 88.57  ? 926  PRO t CG    1 
ATOM   12074 C  CD    B PRO F 2 926 ? 121.698 138.692 137.738 0.50 86.69  ? 926  PRO t CD    1 
HETATM 12075 P  PB    . GDP G 4 .   ? 139.163 179.806 133.254 1.00 25.03  ? 501  GDP B PB    1 
HETATM 12076 O  O1B   . GDP G 4 .   ? 139.035 179.469 131.789 1.00 25.03  ? 501  GDP B O1B   1 
HETATM 12077 O  O2B   . GDP G 4 .   ? 138.401 181.063 133.615 1.00 25.03  ? 501  GDP B O2B   1 
HETATM 12078 O  O3B   . GDP G 4 .   ? 138.731 178.632 134.099 1.00 25.03  ? 501  GDP B O3B   1 
HETATM 12079 O  O3A   . GDP G 4 .   ? 140.707 180.046 133.574 1.00 25.03  ? 501  GDP B O3A   1 
HETATM 12080 P  PA    . GDP G 4 .   ? 141.555 181.182 132.829 1.00 25.03  ? 501  GDP B PA    1 
HETATM 12081 O  O1A   . GDP G 4 .   ? 140.898 181.559 131.522 1.00 25.03  ? 501  GDP B O1A   1 
HETATM 12082 O  O2A   . GDP G 4 .   ? 141.681 182.361 133.762 1.00 25.03  ? 501  GDP B O2A   1 
HETATM 12083 O  "O5'" . GDP G 4 .   ? 142.983 180.487 132.546 1.00 25.03  ? 501  GDP B "O5'" 1 
HETATM 12084 C  "C5'" . GDP G 4 .   ? 144.208 181.041 133.025 1.00 25.03  ? 501  GDP B "C5'" 1 
HETATM 12085 C  "C4'" . GDP G 4 .   ? 145.186 181.358 131.898 1.00 25.03  ? 501  GDP B "C4'" 1 
HETATM 12086 O  "O4'" . GDP G 4 .   ? 144.647 182.406 131.086 1.00 25.03  ? 501  GDP B "O4'" 1 
HETATM 12087 C  "C3'" . GDP G 4 .   ? 146.488 181.901 132.452 1.00 25.03  ? 501  GDP B "C3'" 1 
HETATM 12088 O  "O3'" . GDP G 4 .   ? 147.575 181.491 131.614 1.00 25.03  ? 501  GDP B "O3'" 1 
HETATM 12089 C  "C2'" . GDP G 4 .   ? 146.302 183.406 132.399 1.00 25.03  ? 501  GDP B "C2'" 1 
HETATM 12090 O  "O2'" . GDP G 4 .   ? 147.545 184.104 132.287 1.00 25.03  ? 501  GDP B "O2'" 1 
HETATM 12091 C  "C1'" . GDP G 4 .   ? 145.445 183.596 131.163 1.00 25.03  ? 501  GDP B "C1'" 1 
HETATM 12092 N  N9    . GDP G 4 .   ? 144.543 184.772 131.234 1.00 25.03  ? 501  GDP B N9    1 
HETATM 12093 C  C8    . GDP G 4 .   ? 143.578 184.944 132.153 1.00 25.03  ? 501  GDP B C8    1 
HETATM 12094 N  N7    . GDP G 4 .   ? 142.902 186.099 131.941 1.00 25.03  ? 501  GDP B N7    1 
HETATM 12095 C  C5    . GDP G 4 .   ? 143.431 186.682 130.851 1.00 25.03  ? 501  GDP B C5    1 
HETATM 12096 C  C6    . GDP G 4 .   ? 143.179 187.924 130.085 1.00 25.03  ? 501  GDP B C6    1 
HETATM 12097 O  O6    . GDP G 4 .   ? 142.278 188.711 130.436 1.00 25.03  ? 501  GDP B O6    1 
HETATM 12098 N  N1    . GDP G 4 .   ? 143.935 188.180 129.015 1.00 25.03  ? 501  GDP B N1    1 
HETATM 12099 C  C2    . GDP G 4 .   ? 144.910 187.343 128.623 1.00 25.03  ? 501  GDP B C2    1 
HETATM 12100 N  N2    . GDP G 4 .   ? 145.633 187.672 127.526 1.00 25.03  ? 501  GDP B N2    1 
HETATM 12101 N  N3    . GDP G 4 .   ? 145.198 186.186 129.280 1.00 25.03  ? 501  GDP B N3    1 
HETATM 12102 C  C4    . GDP G 4 .   ? 144.507 185.804 130.382 1.00 25.03  ? 501  GDP B C4    1 
HETATM 12103 O  O01   . TA1 H 5 .   ? 148.148 202.796 118.547 1.00 90.90  ? 502  TA1 B O01   1 
HETATM 12104 C  C01   . TA1 H 5 .   ? 148.369 202.683 117.151 1.00 90.84  ? 502  TA1 B C01   1 
HETATM 12105 C  C02   . TA1 H 5 .   ? 149.763 201.932 117.031 1.00 91.83  ? 502  TA1 B C02   1 
HETATM 12106 O  O02   . TA1 H 5 .   ? 149.529 200.719 117.760 1.00 95.01  ? 502  TA1 B O02   1 
HETATM 12107 C  C03   . TA1 H 5 .   ? 150.080 200.495 118.956 1.00 91.82  ? 502  TA1 B C03   1 
HETATM 12108 O  O03   . TA1 H 5 .   ? 150.848 201.249 119.497 1.00 89.26  ? 502  TA1 B O03   1 
HETATM 12109 C  C04   . TA1 H 5 .   ? 149.617 199.210 119.540 1.00 91.05  ? 502  TA1 B C04   1 
HETATM 12110 C  C05   . TA1 H 5 .   ? 149.168 199.201 120.858 1.00 89.05  ? 502  TA1 B C05   1 
HETATM 12111 C  C06   . TA1 H 5 .   ? 148.726 198.024 121.436 1.00 86.90  ? 502  TA1 B C06   1 
HETATM 12112 C  C07   . TA1 H 5 .   ? 148.731 196.844 120.705 1.00 86.84  ? 502  TA1 B C07   1 
HETATM 12113 C  C08   . TA1 H 5 .   ? 149.175 196.846 119.393 1.00 86.80  ? 502  TA1 B C08   1 
HETATM 12114 C  C09   . TA1 H 5 .   ? 149.618 198.022 118.811 1.00 88.53  ? 502  TA1 B C09   1 
HETATM 12115 C  C10   . TA1 H 5 .   ? 150.344 201.549 115.614 1.00 84.95  ? 502  TA1 B C10   1 
HETATM 12116 C  C11   . TA1 H 5 .   ? 150.848 200.069 115.522 1.00 86.94  ? 502  TA1 B C11   1 
HETATM 12117 O  O04   . TA1 H 5 .   ? 149.744 199.180 115.686 1.00 92.42  ? 502  TA1 B O04   1 
HETATM 12118 C  C12   . TA1 H 5 .   ? 148.730 199.007 114.845 1.00 93.87  ? 502  TA1 B C12   1 
HETATM 12119 O  O05   . TA1 H 5 .   ? 148.590 199.623 113.826 1.00 94.71  ? 502  TA1 B O05   1 
HETATM 12120 C  C13   . TA1 H 5 .   ? 147.798 197.949 115.353 1.00 88.08  ? 502  TA1 B C13   1 
HETATM 12121 C  C14   . TA1 H 5 .   ? 152.003 199.620 116.419 1.00 86.04  ? 502  TA1 B C14   1 
HETATM 12122 O  O06   . TA1 H 5 .   ? 152.793 199.250 115.280 1.00 92.17  ? 502  TA1 B O06   1 
HETATM 12123 C  C15   . TA1 H 5 .   ? 151.784 199.699 114.343 1.00 88.58  ? 502  TA1 B C15   1 
HETATM 12124 C  C16   . TA1 H 5 .   ? 152.301 200.760 113.392 1.00 87.09  ? 502  TA1 B C16   1 
HETATM 12125 C  C17   . TA1 H 5 .   ? 151.573 202.088 113.456 1.00 87.40  ? 502  TA1 B C17   1 
HETATM 12126 O  O07   . TA1 H 5 .   ? 152.130 203.057 112.595 1.00 91.37  ? 502  TA1 B O07   1 
HETATM 12127 C  C18   . TA1 H 5 .   ? 151.406 202.570 114.946 1.00 87.04  ? 502  TA1 B C18   1 
HETATM 12128 C  C19   . TA1 H 5 .   ? 152.788 202.590 115.611 1.00 85.89  ? 502  TA1 B C19   1 
HETATM 12129 C  C20   . TA1 H 5 .   ? 150.949 204.049 114.815 1.00 92.79  ? 502  TA1 B C20   1 
HETATM 12130 O  O08   . TA1 H 5 .   ? 151.715 204.912 115.195 1.00 96.16  ? 502  TA1 B O08   1 
HETATM 12131 C  C21   . TA1 H 5 .   ? 149.624 204.619 114.256 1.00 90.78  ? 502  TA1 B C21   1 
HETATM 12132 O  O09   . TA1 H 5 .   ? 149.594 206.033 114.336 1.00 91.06  ? 502  TA1 B O09   1 
HETATM 12133 C  C22   . TA1 H 5 .   ? 149.657 206.802 113.242 1.00 89.01  ? 502  TA1 B C22   1 
HETATM 12134 O  O10   . TA1 H 5 .   ? 149.689 206.361 112.124 1.00 87.94  ? 502  TA1 B O10   1 
HETATM 12135 C  C23   . TA1 H 5 .   ? 149.675 208.253 113.607 1.00 85.15  ? 502  TA1 B C23   1 
HETATM 12136 C  C24   . TA1 H 5 .   ? 148.481 204.001 115.040 1.00 88.64  ? 502  TA1 B C24   1 
HETATM 12137 C  C25   . TA1 H 5 .   ? 147.661 203.126 114.385 1.00 86.39  ? 502  TA1 B C25   1 
HETATM 12138 C  C26   . TA1 H 5 .   ? 146.642 202.341 115.197 1.00 85.29  ? 502  TA1 B C26   1 
HETATM 12139 O  O11   . TA1 H 5 .   ? 146.041 201.214 114.531 1.00 87.39  ? 502  TA1 B O11   1 
HETATM 12140 C  C27   . TA1 H 5 .   ? 144.864 201.377 113.924 1.00 91.25  ? 502  TA1 B C27   1 
HETATM 12141 O  O12   . TA1 H 5 .   ? 144.260 202.418 113.864 1.00 90.98  ? 502  TA1 B O12   1 
HETATM 12142 C  C28   . TA1 H 5 .   ? 144.379 200.076 113.275 1.00 89.17  ? 502  TA1 B C28   1 
HETATM 12143 O  O13   . TA1 H 5 .   ? 143.143 200.261 112.658 1.00 86.96  ? 502  TA1 B O13   1 
HETATM 12144 C  C29   . TA1 H 5 .   ? 144.238 198.981 114.349 1.00 86.39  ? 502  TA1 B C29   1 
HETATM 12145 N  N01   . TA1 H 5 .   ? 143.395 199.500 115.395 1.00 86.65  ? 502  TA1 B N01   1 
HETATM 12146 C  C30   . TA1 H 5 .   ? 143.430 199.044 116.661 1.00 88.74  ? 502  TA1 B C30   1 
HETATM 12147 O  O14   . TA1 H 5 .   ? 144.182 198.153 117.016 1.00 93.02  ? 502  TA1 B O14   1 
HETATM 12148 C  C31   . TA1 H 5 .   ? 142.510 199.725 117.611 1.00 86.41  ? 502  TA1 B C31   1 
HETATM 12149 C  C32   . TA1 H 5 .   ? 141.133 199.674 117.417 1.00 84.70  ? 502  TA1 B C32   1 
HETATM 12150 C  C33   . TA1 H 5 .   ? 140.287 200.326 118.298 1.00 86.35  ? 502  TA1 B C33   1 
HETATM 12151 C  C34   . TA1 H 5 .   ? 140.806 201.038 119.371 1.00 88.85  ? 502  TA1 B C34   1 
HETATM 12152 C  C35   . TA1 H 5 .   ? 142.177 201.097 119.562 1.00 90.85  ? 502  TA1 B C35   1 
HETATM 12153 C  C36   . TA1 H 5 .   ? 143.025 200.446 118.683 1.00 88.76  ? 502  TA1 B C36   1 
HETATM 12154 C  C37   . TA1 H 5 .   ? 143.774 197.663 113.777 1.00 85.42  ? 502  TA1 B C37   1 
HETATM 12155 C  C38   . TA1 H 5 .   ? 144.713 196.731 113.349 1.00 87.27  ? 502  TA1 B C38   1 
HETATM 12156 C  C39   . TA1 H 5 .   ? 144.317 195.510 112.825 1.00 84.97  ? 502  TA1 B C39   1 
HETATM 12157 C  C40   . TA1 H 5 .   ? 142.970 195.201 112.727 1.00 85.44  ? 502  TA1 B C40   1 
HETATM 12158 C  C41   . TA1 H 5 .   ? 142.033 196.128 113.149 1.00 87.65  ? 502  TA1 B C41   1 
HETATM 12159 C  C42   . TA1 H 5 .   ? 142.429 197.347 113.679 1.00 85.88  ? 502  TA1 B C42   1 
HETATM 12160 C  C43   . TA1 H 5 .   ? 147.254 201.826 116.510 1.00 84.49  ? 502  TA1 B C43   1 
HETATM 12161 C  C44   . TA1 H 5 .   ? 147.726 202.766 112.927 1.00 85.25  ? 502  TA1 B C44   1 
HETATM 12162 C  C45   . TA1 H 5 .   ? 148.371 204.142 116.579 1.00 89.09  ? 502  TA1 B C45   1 
HETATM 12163 C  C46   . TA1 H 5 .   ? 147.086 204.953 116.929 1.00 86.82  ? 502  TA1 B C46   1 
HETATM 12164 C  C47   . TA1 H 5 .   ? 149.386 205.012 117.351 1.00 86.29  ? 502  TA1 B C47   1 
HETATM 12165 P  PG    . ANP I 6 .   ? 130.498 146.884 98.511  1.00 57.50  ? 1001 ANP K PG    1 
HETATM 12166 O  O1G   . ANP I 6 .   ? 131.955 146.843 98.828  1.00 64.68  ? 1001 ANP K O1G   1 
HETATM 12167 O  O2G   . ANP I 6 .   ? 130.135 148.251 97.842  1.00 48.62  ? 1001 ANP K O2G   1 
HETATM 12168 O  O3G   . ANP I 6 .   ? 129.644 146.662 99.808  1.00 67.31  ? 1001 ANP K O3G   1 
HETATM 12169 P  PB    . ANP I 6 .   ? 130.293 144.141 97.960  1.00 58.89  ? 1001 ANP K PB    1 
HETATM 12170 O  O1B   . ANP I 6 .   ? 131.722 143.742 97.940  1.00 58.11  ? 1001 ANP K O1B   1 
HETATM 12171 O  O2B   . ANP I 6 .   ? 129.637 143.840 99.344  1.00 63.55  ? 1001 ANP K O2B   1 
HETATM 12172 N  N3B   . ANP I 6 .   ? 130.074 145.701 97.412  1.00 54.60  ? 1001 ANP K N3B   1 
HETATM 12173 P  PA    . ANP I 6 .   ? 128.931 142.081 96.901  1.00 70.06  ? 1001 ANP K PA    1 
HETATM 12174 O  O1A   . ANP I 6 .   ? 127.732 142.019 97.769  1.00 58.81  ? 1001 ANP K O1A   1 
HETATM 12175 O  O2A   . ANP I 6 .   ? 129.771 140.840 96.580  1.00 68.37  ? 1001 ANP K O2A   1 
HETATM 12176 O  O3A   . ANP I 6 .   ? 129.607 143.433 96.796  1.00 57.65  ? 1001 ANP K O3A   1 
HETATM 12177 O  "O5'" . ANP I 6 .   ? 128.339 142.340 95.504  1.00 60.77  ? 1001 ANP K "O5'" 1 
HETATM 12178 C  "C5'" . ANP I 6 .   ? 127.413 141.382 95.489  1.00 58.08  ? 1001 ANP K "C5'" 1 
HETATM 12179 C  "C4'" . ANP I 6 .   ? 126.814 140.916 94.227  1.00 47.72  ? 1001 ANP K "C4'" 1 
HETATM 12180 O  "O4'" . ANP I 6 .   ? 127.840 140.291 93.421  1.00 44.12  ? 1001 ANP K "O4'" 1 
HETATM 12181 C  "C3'" . ANP I 6 .   ? 125.903 139.819 94.758  1.00 51.30  ? 1001 ANP K "C3'" 1 
HETATM 12182 O  "O3'" . ANP I 6 .   ? 124.519 139.868 94.446  1.00 55.17  ? 1001 ANP K "O3'" 1 
HETATM 12183 C  "C2'" . ANP I 6 .   ? 126.643 138.520 94.455  1.00 55.44  ? 1001 ANP K "C2'" 1 
HETATM 12184 O  "O2'" . ANP I 6 .   ? 125.783 137.469 94.044  1.00 63.50  ? 1001 ANP K "O2'" 1 
HETATM 12185 C  "C1'" . ANP I 6 .   ? 127.640 138.890 93.361  1.00 54.67  ? 1001 ANP K "C1'" 1 
HETATM 12186 N  N9    . ANP I 6 .   ? 128.867 138.147 93.624  1.00 51.23  ? 1001 ANP K N9    1 
HETATM 12187 C  C8    . ANP I 6 .   ? 129.946 138.509 94.386  1.00 54.57  ? 1001 ANP K C8    1 
HETATM 12188 N  N7    . ANP I 6 .   ? 130.846 137.563 94.517  1.00 55.67  ? 1001 ANP K N7    1 
HETATM 12189 C  C5    . ANP I 6 .   ? 130.295 136.486 93.836  1.00 50.88  ? 1001 ANP K C5    1 
HETATM 12190 C  C6    . ANP I 6 .   ? 130.757 135.173 93.603  1.00 56.07  ? 1001 ANP K C6    1 
HETATM 12191 N  N6    . ANP I 6 .   ? 131.922 134.706 94.058  1.00 60.45  ? 1001 ANP K N6    1 
HETATM 12192 N  N1    . ANP I 6 .   ? 129.963 134.343 92.884  1.00 55.32  ? 1001 ANP K N1    1 
HETATM 12193 C  C2    . ANP I 6 .   ? 128.794 134.805 92.431  1.00 56.19  ? 1001 ANP K C2    1 
HETATM 12194 N  N3    . ANP I 6 .   ? 128.261 136.021 92.590  1.00 56.20  ? 1001 ANP K N3    1 
HETATM 12195 C  C4    . ANP I 6 .   ? 129.065 136.821 93.305  1.00 49.21  ? 1001 ANP K C4    1 
HETATM 12196 MG MG    . MG  J 7 .   ? 128.877 145.117 100.789 1.00 54.89  ? 1002 MG  K MG    1 
HETATM 12197 MG MG    . MG  K 7 .   ? 112.625 105.016 146.862 1.00 65.05  ? 1001 MG  L MG    1 
HETATM 12198 P  PG    . ANP L 6 .   ? 112.856 102.563 148.565 1.00 105.19 ? 1002 ANP L PG    1 
HETATM 12199 O  O1G   . ANP L 6 .   ? 112.532 101.276 147.879 1.00 106.42 ? 1002 ANP L O1G   1 
HETATM 12200 O  O2G   . ANP L 6 .   ? 113.625 103.493 147.584 1.00 99.88  ? 1002 ANP L O2G   1 
HETATM 12201 O  O3G   . ANP L 6 .   ? 113.784 102.249 149.796 1.00 106.90 ? 1002 ANP L O3G   1 
HETATM 12202 P  PB    . ANP L 6 .   ? 111.141 104.878 149.298 1.00 105.47 ? 1002 ANP L PB    1 
HETATM 12203 O  O1B   . ANP L 6 .   ? 111.752 105.880 148.398 1.00 100.30 ? 1002 ANP L O1B   1 
HETATM 12204 O  O2B   . ANP L 6 .   ? 110.866 105.204 150.775 1.00 108.76 ? 1002 ANP L O2B   1 
HETATM 12205 N  N3B   . ANP L 6 .   ? 111.379 103.270 148.951 1.00 101.95 ? 1002 ANP L N3B   1 
HETATM 12206 P  PA    . ANP L 6 .   ? 109.082 105.932 147.746 1.00 110.65 ? 1002 ANP L PA    1 
HETATM 12207 O  O1A   . ANP L 6 .   ? 108.995 105.360 146.390 1.00 104.63 ? 1002 ANP L O1A   1 
HETATM 12208 O  O2A   . ANP L 6 .   ? 109.024 107.415 148.087 1.00 102.33 ? 1002 ANP L O2A   1 
HETATM 12209 O  O3A   . ANP L 6 .   ? 109.677 104.992 148.870 1.00 107.39 ? 1002 ANP L O3A   1 
HETATM 12210 O  "O5'" . ANP L 6 .   ? 107.600 105.738 147.988 1.00 106.83 ? 1002 ANP L "O5'" 1 
HETATM 12211 C  "C5'" . ANP L 6 .   ? 106.929 104.891 148.891 1.00 105.68 ? 1002 ANP L "C5'" 1 
HETATM 12212 C  "C4'" . ANP L 6 .   ? 105.565 104.709 148.254 1.00 104.00 ? 1002 ANP L "C4'" 1 
HETATM 12213 O  "O4'" . ANP L 6 .   ? 104.570 105.436 149.008 1.00 106.77 ? 1002 ANP L "O4'" 1 
HETATM 12214 C  "C3'" . ANP L 6 .   ? 105.417 105.232 146.827 1.00 103.56 ? 1002 ANP L "C3'" 1 
HETATM 12215 O  "O3'" . ANP L 6 .   ? 104.403 104.506 146.139 1.00 102.70 ? 1002 ANP L "O3'" 1 
HETATM 12216 C  "C2'" . ANP L 6 .   ? 105.039 106.702 147.054 1.00 104.13 ? 1002 ANP L "C2'" 1 
HETATM 12217 O  "O2'" . ANP L 6 .   ? 104.343 107.272 145.950 1.00 103.48 ? 1002 ANP L "O2'" 1 
HETATM 12218 C  "C1'" . ANP L 6 .   ? 104.172 106.610 148.315 1.00 106.40 ? 1002 ANP L "C1'" 1 
HETATM 12219 N  N9    . ANP L 6 .   ? 104.287 107.756 149.226 1.00 106.94 ? 1002 ANP L N9    1 
HETATM 12220 C  C8    . ANP L 6 .   ? 105.322 108.038 150.078 1.00 105.70 ? 1002 ANP L C8    1 
HETATM 12221 N  N7    . ANP L 6 .   ? 105.150 109.129 150.788 1.00 106.01 ? 1002 ANP L N7    1 
HETATM 12222 C  C5    . ANP L 6 .   ? 103.912 109.597 150.376 1.00 103.85 ? 1002 ANP L C5    1 
HETATM 12223 C  C6    . ANP L 6 .   ? 103.149 110.721 150.751 1.00 103.28 ? 1002 ANP L C6    1 
HETATM 12224 N  N6    . ANP L 6 .   ? 103.539 111.616 151.662 1.00 103.89 ? 1002 ANP L N6    1 
HETATM 12225 N  N1    . ANP L 6 .   ? 101.952 110.896 150.144 1.00 105.18 ? 1002 ANP L N1    1 
HETATM 12226 C  C2    . ANP L 6 .   ? 101.554 110.003 149.231 1.00 105.29 ? 1002 ANP L C2    1 
HETATM 12227 N  N3    . ANP L 6 .   ? 102.186 108.909 148.800 1.00 104.06 ? 1002 ANP L N3    1 
HETATM 12228 C  C4    . ANP L 6 .   ? 103.366 108.760 149.416 1.00 104.70 ? 1002 ANP L C4    1 
HETATM 12229 P  PG    . GTP M 8 .   ? 138.533 179.317 94.246  1.00 68.28  ? 501  GTP A PG    1 
HETATM 12230 O  O1G   . GTP M 8 .   ? 139.341 178.353 95.076  1.00 60.91  ? 501  GTP A O1G   1 
HETATM 12231 O  O2G   . GTP M 8 .   ? 137.058 178.992 94.297  1.00 75.38  ? 501  GTP A O2G   1 
HETATM 12232 O  O3G   . GTP M 8 .   ? 138.808 180.748 94.639  1.00 65.64  ? 501  GTP A O3G   1 
HETATM 12233 O  O3B   . GTP M 8 .   ? 138.997 179.050 92.744  1.00 58.56  ? 501  GTP A O3B   1 
HETATM 12234 P  PB    . GTP M 8 .   ? 139.521 180.214 91.784  1.00 67.13  ? 501  GTP A PB    1 
HETATM 12235 O  O1B   . GTP M 8 .   ? 138.723 181.485 91.975  1.00 69.59  ? 501  GTP A O1B   1 
HETATM 12236 O  O2B   . GTP M 8 .   ? 139.480 179.673 90.379  1.00 64.22  ? 501  GTP A O2B   1 
HETATM 12237 O  O3A   . GTP M 8 .   ? 141.032 180.448 92.248  1.00 54.94  ? 501  GTP A O3A   1 
HETATM 12238 P  PA    . GTP M 8 .   ? 142.013 181.384 91.399  1.00 59.20  ? 501  GTP A PA    1 
HETATM 12239 O  O1A   . GTP M 8 .   ? 142.200 182.666 92.177  1.00 64.41  ? 501  GTP A O1A   1 
HETATM 12240 O  O2A   . GTP M 8 .   ? 141.485 181.578 89.997  1.00 64.34  ? 501  GTP A O2A   1 
HETATM 12241 O  "O5'" . GTP M 8 .   ? 143.353 180.494 91.360  1.00 62.22  ? 501  GTP A "O5'" 1 
HETATM 12242 C  "C5'" . GTP M 8 .   ? 144.621 180.874 91.851  1.00 56.56  ? 501  GTP A "C5'" 1 
HETATM 12243 C  "C4'" . GTP M 8 .   ? 145.597 180.891 90.681  1.00 55.78  ? 501  GTP A "C4'" 1 
HETATM 12244 O  "O4'" . GTP M 8 .   ? 145.116 181.835 89.746  1.00 57.91  ? 501  GTP A "O4'" 1 
HETATM 12245 C  "C3'" . GTP M 8 .   ? 147.001 181.331 91.059  1.00 61.18  ? 501  GTP A "C3'" 1 
HETATM 12246 O  "O3'" . GTP M 8 .   ? 147.926 180.648 90.239  1.00 69.01  ? 501  GTP A "O3'" 1 
HETATM 12247 C  "C2'" . GTP M 8 .   ? 146.997 182.808 90.729  1.00 63.88  ? 501  GTP A "C2'" 1 
HETATM 12248 O  "O2'" . GTP M 8 .   ? 148.272 183.316 90.397  1.00 66.48  ? 501  GTP A "O2'" 1 
HETATM 12249 C  "C1'" . GTP M 8 .   ? 146.044 182.888 89.552  1.00 62.69  ? 501  GTP A "C1'" 1 
HETATM 12250 N  N9    . GTP M 8 .   ? 145.315 184.167 89.552  1.00 59.05  ? 501  GTP A N9    1 
HETATM 12251 C  C8    . GTP M 8 .   ? 144.457 184.583 90.523  1.00 58.50  ? 501  GTP A C8    1 
HETATM 12252 N  N7    . GTP M 8 .   ? 143.963 185.794 90.187  1.00 62.71  ? 501  GTP A N7    1 
HETATM 12253 C  C5    . GTP M 8 .   ? 144.486 186.165 88.999  1.00 56.12  ? 501  GTP A C5    1 
HETATM 12254 C  C6    . GTP M 8 .   ? 144.324 187.301 88.197  1.00 53.16  ? 501  GTP A C6    1 
HETATM 12255 O  O6    . GTP M 8 .   ? 143.583 188.232 88.517  1.00 60.98  ? 501  GTP A O6    1 
HETATM 12256 N  N1    . GTP M 8 .   ? 145.012 187.387 87.015  1.00 55.47  ? 501  GTP A N1    1 
HETATM 12257 C  C2    . GTP M 8 .   ? 145.846 186.368 86.629  1.00 65.36  ? 501  GTP A C2    1 
HETATM 12258 N  N2    . GTP M 8 .   ? 146.499 186.474 85.479  1.00 68.27  ? 501  GTP A N2    1 
HETATM 12259 N  N3    . GTP M 8 .   ? 146.007 185.249 87.417  1.00 65.43  ? 501  GTP A N3    1 
HETATM 12260 C  C4    . GTP M 8 .   ? 145.339 185.142 88.589  1.00 58.89  ? 501  GTP A C4    1 
HETATM 12261 MG MG    . MG  N 7 .   ? 138.018 182.460 94.220  1.00 60.85  ? 502  MG  A MG    1 
# 
