data_8KDO
# 
_entry.id   8KDO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8KDO         pdb_00008kdo 10.2210/pdb8kdo/pdb 
WWPDB D_1300040175 ?            ?                   
EMDB  EMD-37141    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-02-12 ? 
2  'EM metadata'     1 0 2025-02-12 ? 
3  FSC               1 0 2025-02-12 ? 
4  'Half map'        1 0 2025-02-12 1 
5  'Half map'        1 0 2025-02-12 2 
6  Image             1 0 2025-02-12 ? 
7  Mask              1 0 2025-02-12 ? 
8  'Primary map'     1 0 2025-02-12 ? 
9  'Structure model' 1 1 2025-02-26 ? 
10 'EM metadata'     1 1 2025-02-26 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 9  'Structure model' 'Data collection'      
2 9  'Structure model' 'Database references'  
3 10 'EM metadata'     'Database references'  
4 10 'EM metadata'     'Experimental summary' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 9  'Structure model' citation        
2 9  'Structure model' citation_author 
3 9  'Structure model' em_admin        
4 10 'EM metadata'     citation        
5 10 'EM metadata'     citation_author 
6 10 'EM metadata'     em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  9  'Structure model' '_citation.country'                 
2  9  'Structure model' '_citation.journal_abbrev'          
3  9  'Structure model' '_citation.journal_id_CSD'          
4  9  'Structure model' '_citation.journal_id_ISSN'         
5  9  'Structure model' '_citation.journal_volume'          
6  9  'Structure model' '_citation.page_first'              
7  9  'Structure model' '_citation.page_last'               
8  9  'Structure model' '_citation.pdbx_database_id_DOI'    
9  9  'Structure model' '_citation.pdbx_database_id_PubMed' 
10 9  'Structure model' '_citation.title'                   
11 9  'Structure model' '_citation.year'                    
12 9  'Structure model' '_em_admin.last_update'             
13 10 'EM metadata'     '_citation.country'                 
14 10 'EM metadata'     '_citation.journal_abbrev'          
15 10 'EM metadata'     '_citation.journal_id_CSD'          
16 10 'EM metadata'     '_citation.journal_id_ISSN'         
17 10 'EM metadata'     '_citation.journal_volume'          
18 10 'EM metadata'     '_citation.page_first'              
19 10 'EM metadata'     '_citation.page_last'               
20 10 'EM metadata'     '_citation.pdbx_database_id_DOI'    
21 10 'EM metadata'     '_citation.pdbx_database_id_PubMed' 
22 10 'EM metadata'     '_citation.title'                   
23 10 'EM metadata'     '_citation.year'                    
24 10 'EM metadata'     '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8KDO 
_pdbx_database_status.recvd_initial_deposition_date   2023-08-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Structure of LAT1-CD98hc in complex with melphalan, focused on TMD' 
_pdbx_database_related.db_id          EMD-37141 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ri.yon.df@yokohama-cu.ac.jp 
_pdbx_contact_author.name_first         Yongchan 
_pdbx_contact_author.name_last          Lee 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1507-805X 
# 
_audit_author.name               'Lee, Y.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1635 
_citation.page_last                 1635 
_citation.title                     'Structural basis of anticancer drug recognition and amino acid transport by LAT1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-56903-w 
_citation.pdbx_database_id_PubMed   39952931 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, Y.'          1  0000-0002-1507-805X 
primary 'Jin, C.'          2  ?                   
primary 'Ohgaki, R.'       3  0000-0002-6894-7239 
primary 'Xu, M.'           4  ?                   
primary 'Ogasawara, S.'    5  0000-0001-6908-9953 
primary 'Warshamanage, R.' 6  ?                   
primary 'Yamashita, K.'    7  0000-0002-5442-7582 
primary 'Murshudov, G.'    8  ?                   
primary 'Nureki, O.'       9  0000-0003-1813-7008 
primary 'Murata, T.'       10 0000-0002-5748-4670 
primary 'Kanai, Y.'        11 0000-0001-8126-286X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '4F2 cell-surface antigen heavy chain'                                 68069.625 1 ? ? ? ? 
2 polymer     man 'Large neutral amino acids transporter small subunit 1'                56043.746 1 ? ? ? ? 
3 non-polymer syn '(2~{S})-2-azanyl-3-[4-[bis(2-chloroethyl)amino]phenyl]propanoic acid' 305.200   1 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Glycoprotein, 4F2hc,4F2 heavy chain antigen,Lymphocyte activation antigen 4F2 large subunit,Solute carrier family 3 member 2' 
2 
;4F2 light chain,4F2LC,CD98 light chain,Integral membrane protein E16,L-type amino acid transporter 1,hLAT1,Solute carrier family 7 member 5,y+ system cationic amino acid transporter
;
# 
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 
;GSELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAG
LQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAA
KFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAG
NLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWF
STQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLL
LTSSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAAL
PGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQ
NERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
;
;GSELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAG
LQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAA
KFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAG
NLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWF
STQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLL
LTSSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAAL
PGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQ
NERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
;
A ? 
2 'polypeptide(L)' no no 
;MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAG
SPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPL
FPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDV
GNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHL
GVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFF
SFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKN
KPKWLLQGIFSTTVLCQKLMQVVPQETDYKDDDDK
;
;MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAG
SPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPL
FPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDV
GNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHL
GVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFF
SFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKN
KPKWLLQGIFSTTVLCQKLMQVVPQETDYKDDDDK
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        '(2~{S})-2-azanyl-3-[4-[bis(2-chloroethyl)amino]phenyl]propanoic acid' 
_pdbx_entity_nonpoly.comp_id     VUC 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   GLU n 
1 4   LEU n 
1 5   GLN n 
1 6   PRO n 
1 7   PRO n 
1 8   GLU n 
1 9   ALA n 
1 10  SER n 
1 11  ILE n 
1 12  ALA n 
1 13  VAL n 
1 14  VAL n 
1 15  SER n 
1 16  ILE n 
1 17  PRO n 
1 18  ARG n 
1 19  GLN n 
1 20  LEU n 
1 21  PRO n 
1 22  GLY n 
1 23  SER n 
1 24  HIS n 
1 25  SER n 
1 26  GLU n 
1 27  ALA n 
1 28  GLY n 
1 29  VAL n 
1 30  GLN n 
1 31  GLY n 
1 32  LEU n 
1 33  SER n 
1 34  ALA n 
1 35  GLY n 
1 36  ASP n 
1 37  ASP n 
1 38  SER n 
1 39  GLU n 
1 40  LEU n 
1 41  GLY n 
1 42  SER n 
1 43  HIS n 
1 44  CYS n 
1 45  VAL n 
1 46  ALA n 
1 47  GLN n 
1 48  THR n 
1 49  GLY n 
1 50  LEU n 
1 51  GLU n 
1 52  LEU n 
1 53  LEU n 
1 54  ALA n 
1 55  SER n 
1 56  GLY n 
1 57  ASP n 
1 58  PRO n 
1 59  LEU n 
1 60  PRO n 
1 61  SER n 
1 62  ALA n 
1 63  SER n 
1 64  GLN n 
1 65  ASN n 
1 66  ALA n 
1 67  GLU n 
1 68  MET n 
1 69  ILE n 
1 70  GLU n 
1 71  THR n 
1 72  GLY n 
1 73  SER n 
1 74  ASP n 
1 75  CYS n 
1 76  VAL n 
1 77  THR n 
1 78  GLN n 
1 79  ALA n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  LEU n 
1 84  LEU n 
1 85  ALA n 
1 86  SER n 
1 87  SER n 
1 88  ASP n 
1 89  PRO n 
1 90  PRO n 
1 91  ALA n 
1 92  LEU n 
1 93  ALA n 
1 94  SER n 
1 95  LYS n 
1 96  ASN n 
1 97  ALA n 
1 98  GLU n 
1 99  VAL n 
1 100 THR n 
1 101 GLY n 
1 102 THR n 
1 103 MET n 
1 104 SER n 
1 105 GLN n 
1 106 ASP n 
1 107 THR n 
1 108 GLU n 
1 109 VAL n 
1 110 ASP n 
1 111 MET n 
1 112 LYS n 
1 113 GLU n 
1 114 VAL n 
1 115 GLU n 
1 116 LEU n 
1 117 ASN n 
1 118 GLU n 
1 119 LEU n 
1 120 GLU n 
1 121 PRO n 
1 122 GLU n 
1 123 LYS n 
1 124 GLN n 
1 125 PRO n 
1 126 MET n 
1 127 ASN n 
1 128 ALA n 
1 129 ALA n 
1 130 SER n 
1 131 GLY n 
1 132 ALA n 
1 133 ALA n 
1 134 MET n 
1 135 SER n 
1 136 LEU n 
1 137 ALA n 
1 138 GLY n 
1 139 ALA n 
1 140 GLU n 
1 141 LYS n 
1 142 ASN n 
1 143 GLY n 
1 144 LEU n 
1 145 VAL n 
1 146 LYS n 
1 147 ILE n 
1 148 LYS n 
1 149 VAL n 
1 150 ALA n 
1 151 GLU n 
1 152 ASP n 
1 153 GLU n 
1 154 ALA n 
1 155 GLU n 
1 156 ALA n 
1 157 ALA n 
1 158 ALA n 
1 159 ALA n 
1 160 ALA n 
1 161 LYS n 
1 162 PHE n 
1 163 THR n 
1 164 GLY n 
1 165 LEU n 
1 166 SER n 
1 167 LYS n 
1 168 GLU n 
1 169 GLU n 
1 170 LEU n 
1 171 LEU n 
1 172 LYS n 
1 173 VAL n 
1 174 ALA n 
1 175 GLY n 
1 176 SER n 
1 177 PRO n 
1 178 GLY n 
1 179 TRP n 
1 180 VAL n 
1 181 ARG n 
1 182 THR n 
1 183 ARG n 
1 184 TRP n 
1 185 ALA n 
1 186 LEU n 
1 187 LEU n 
1 188 LEU n 
1 189 LEU n 
1 190 PHE n 
1 191 TRP n 
1 192 LEU n 
1 193 GLY n 
1 194 TRP n 
1 195 LEU n 
1 196 GLY n 
1 197 MET n 
1 198 LEU n 
1 199 ALA n 
1 200 GLY n 
1 201 ALA n 
1 202 VAL n 
1 203 VAL n 
1 204 ILE n 
1 205 ILE n 
1 206 VAL n 
1 207 ARG n 
1 208 ALA n 
1 209 PRO n 
1 210 ARG n 
1 211 CYS n 
1 212 ARG n 
1 213 GLU n 
1 214 LEU n 
1 215 PRO n 
1 216 ALA n 
1 217 GLN n 
1 218 LYS n 
1 219 TRP n 
1 220 TRP n 
1 221 HIS n 
1 222 THR n 
1 223 GLY n 
1 224 ALA n 
1 225 LEU n 
1 226 TYR n 
1 227 ARG n 
1 228 ILE n 
1 229 GLY n 
1 230 ASP n 
1 231 LEU n 
1 232 GLN n 
1 233 ALA n 
1 234 PHE n 
1 235 GLN n 
1 236 GLY n 
1 237 HIS n 
1 238 GLY n 
1 239 ALA n 
1 240 GLY n 
1 241 ASN n 
1 242 LEU n 
1 243 ALA n 
1 244 GLY n 
1 245 LEU n 
1 246 LYS n 
1 247 GLY n 
1 248 ARG n 
1 249 LEU n 
1 250 ASP n 
1 251 TYR n 
1 252 LEU n 
1 253 SER n 
1 254 SER n 
1 255 LEU n 
1 256 LYS n 
1 257 VAL n 
1 258 LYS n 
1 259 GLY n 
1 260 LEU n 
1 261 VAL n 
1 262 LEU n 
1 263 GLY n 
1 264 PRO n 
1 265 ILE n 
1 266 HIS n 
1 267 LYS n 
1 268 ASN n 
1 269 GLN n 
1 270 LYS n 
1 271 ASP n 
1 272 ASP n 
1 273 VAL n 
1 274 ALA n 
1 275 GLN n 
1 276 THR n 
1 277 ASP n 
1 278 LEU n 
1 279 LEU n 
1 280 GLN n 
1 281 ILE n 
1 282 ASP n 
1 283 PRO n 
1 284 ASN n 
1 285 PHE n 
1 286 GLY n 
1 287 SER n 
1 288 LYS n 
1 289 GLU n 
1 290 ASP n 
1 291 PHE n 
1 292 ASP n 
1 293 SER n 
1 294 LEU n 
1 295 LEU n 
1 296 GLN n 
1 297 SER n 
1 298 ALA n 
1 299 LYS n 
1 300 LYS n 
1 301 LYS n 
1 302 SER n 
1 303 ILE n 
1 304 ARG n 
1 305 VAL n 
1 306 ILE n 
1 307 LEU n 
1 308 ASP n 
1 309 LEU n 
1 310 THR n 
1 311 PRO n 
1 312 ASN n 
1 313 TYR n 
1 314 ARG n 
1 315 GLY n 
1 316 GLU n 
1 317 ASN n 
1 318 SER n 
1 319 TRP n 
1 320 PHE n 
1 321 SER n 
1 322 THR n 
1 323 GLN n 
1 324 VAL n 
1 325 ASP n 
1 326 THR n 
1 327 VAL n 
1 328 ALA n 
1 329 THR n 
1 330 LYS n 
1 331 VAL n 
1 332 LYS n 
1 333 ASP n 
1 334 ALA n 
1 335 LEU n 
1 336 GLU n 
1 337 PHE n 
1 338 TRP n 
1 339 LEU n 
1 340 GLN n 
1 341 ALA n 
1 342 GLY n 
1 343 VAL n 
1 344 ASP n 
1 345 GLY n 
1 346 PHE n 
1 347 GLN n 
1 348 VAL n 
1 349 ARG n 
1 350 ASP n 
1 351 ILE n 
1 352 GLU n 
1 353 ASN n 
1 354 LEU n 
1 355 LYS n 
1 356 ASP n 
1 357 ALA n 
1 358 SER n 
1 359 SER n 
1 360 PHE n 
1 361 LEU n 
1 362 ALA n 
1 363 GLU n 
1 364 TRP n 
1 365 GLN n 
1 366 ASN n 
1 367 ILE n 
1 368 THR n 
1 369 LYS n 
1 370 GLY n 
1 371 PHE n 
1 372 SER n 
1 373 GLU n 
1 374 ASP n 
1 375 ARG n 
1 376 LEU n 
1 377 LEU n 
1 378 ILE n 
1 379 ALA n 
1 380 GLY n 
1 381 THR n 
1 382 ASN n 
1 383 SER n 
1 384 SER n 
1 385 ASP n 
1 386 LEU n 
1 387 GLN n 
1 388 GLN n 
1 389 ILE n 
1 390 LEU n 
1 391 SER n 
1 392 LEU n 
1 393 LEU n 
1 394 GLU n 
1 395 SER n 
1 396 ASN n 
1 397 LYS n 
1 398 ASP n 
1 399 LEU n 
1 400 LEU n 
1 401 LEU n 
1 402 THR n 
1 403 SER n 
1 404 SER n 
1 405 TYR n 
1 406 LEU n 
1 407 SER n 
1 408 ASP n 
1 409 SER n 
1 410 GLY n 
1 411 SER n 
1 412 THR n 
1 413 GLY n 
1 414 GLU n 
1 415 HIS n 
1 416 THR n 
1 417 LYS n 
1 418 SER n 
1 419 LEU n 
1 420 VAL n 
1 421 THR n 
1 422 GLN n 
1 423 TYR n 
1 424 LEU n 
1 425 ASN n 
1 426 ALA n 
1 427 THR n 
1 428 GLY n 
1 429 ASN n 
1 430 ARG n 
1 431 TRP n 
1 432 CYS n 
1 433 SER n 
1 434 TRP n 
1 435 SER n 
1 436 LEU n 
1 437 SER n 
1 438 GLN n 
1 439 ALA n 
1 440 ARG n 
1 441 LEU n 
1 442 LEU n 
1 443 THR n 
1 444 SER n 
1 445 PHE n 
1 446 LEU n 
1 447 PRO n 
1 448 ALA n 
1 449 GLN n 
1 450 LEU n 
1 451 LEU n 
1 452 ARG n 
1 453 LEU n 
1 454 TYR n 
1 455 GLN n 
1 456 LEU n 
1 457 MET n 
1 458 LEU n 
1 459 PHE n 
1 460 THR n 
1 461 LEU n 
1 462 PRO n 
1 463 GLY n 
1 464 THR n 
1 465 PRO n 
1 466 VAL n 
1 467 PHE n 
1 468 SER n 
1 469 TYR n 
1 470 GLY n 
1 471 ASP n 
1 472 GLU n 
1 473 ILE n 
1 474 GLY n 
1 475 LEU n 
1 476 ASP n 
1 477 ALA n 
1 478 ALA n 
1 479 ALA n 
1 480 LEU n 
1 481 PRO n 
1 482 GLY n 
1 483 GLN n 
1 484 PRO n 
1 485 MET n 
1 486 GLU n 
1 487 ALA n 
1 488 PRO n 
1 489 VAL n 
1 490 MET n 
1 491 LEU n 
1 492 TRP n 
1 493 ASP n 
1 494 GLU n 
1 495 SER n 
1 496 SER n 
1 497 PHE n 
1 498 PRO n 
1 499 ASP n 
1 500 ILE n 
1 501 PRO n 
1 502 GLY n 
1 503 ALA n 
1 504 VAL n 
1 505 SER n 
1 506 ALA n 
1 507 ASN n 
1 508 MET n 
1 509 THR n 
1 510 VAL n 
1 511 LYS n 
1 512 GLY n 
1 513 GLN n 
1 514 SER n 
1 515 GLU n 
1 516 ASP n 
1 517 PRO n 
1 518 GLY n 
1 519 SER n 
1 520 LEU n 
1 521 LEU n 
1 522 SER n 
1 523 LEU n 
1 524 PHE n 
1 525 ARG n 
1 526 ARG n 
1 527 LEU n 
1 528 SER n 
1 529 ASP n 
1 530 GLN n 
1 531 ARG n 
1 532 SER n 
1 533 LYS n 
1 534 GLU n 
1 535 ARG n 
1 536 SER n 
1 537 LEU n 
1 538 LEU n 
1 539 HIS n 
1 540 GLY n 
1 541 ASP n 
1 542 PHE n 
1 543 HIS n 
1 544 ALA n 
1 545 PHE n 
1 546 SER n 
1 547 ALA n 
1 548 GLY n 
1 549 PRO n 
1 550 GLY n 
1 551 LEU n 
1 552 PHE n 
1 553 SER n 
1 554 TYR n 
1 555 ILE n 
1 556 ARG n 
1 557 HIS n 
1 558 TRP n 
1 559 ASP n 
1 560 GLN n 
1 561 ASN n 
1 562 GLU n 
1 563 ARG n 
1 564 PHE n 
1 565 LEU n 
1 566 VAL n 
1 567 VAL n 
1 568 LEU n 
1 569 ASN n 
1 570 PHE n 
1 571 GLY n 
1 572 ASP n 
1 573 VAL n 
1 574 GLY n 
1 575 LEU n 
1 576 SER n 
1 577 ALA n 
1 578 GLY n 
1 579 LEU n 
1 580 GLN n 
1 581 ALA n 
1 582 SER n 
1 583 ASP n 
1 584 LEU n 
1 585 PRO n 
1 586 ALA n 
1 587 SER n 
1 588 ALA n 
1 589 SER n 
1 590 LEU n 
1 591 PRO n 
1 592 ALA n 
1 593 LYS n 
1 594 ALA n 
1 595 ASP n 
1 596 LEU n 
1 597 LEU n 
1 598 LEU n 
1 599 SER n 
1 600 THR n 
1 601 GLN n 
1 602 PRO n 
1 603 GLY n 
1 604 ARG n 
1 605 GLU n 
1 606 GLU n 
1 607 GLY n 
1 608 SER n 
1 609 PRO n 
1 610 LEU n 
1 611 GLU n 
1 612 LEU n 
1 613 GLU n 
1 614 ARG n 
1 615 LEU n 
1 616 LYS n 
1 617 LEU n 
1 618 GLU n 
1 619 PRO n 
1 620 HIS n 
1 621 GLU n 
1 622 GLY n 
1 623 LEU n 
1 624 LEU n 
1 625 LEU n 
1 626 ARG n 
1 627 PHE n 
1 628 PRO n 
1 629 TYR n 
1 630 ALA n 
1 631 ALA n 
2 1   MET n 
2 2   ALA n 
2 3   GLY n 
2 4   ALA n 
2 5   GLY n 
2 6   PRO n 
2 7   LYS n 
2 8   ARG n 
2 9   ARG n 
2 10  ALA n 
2 11  LEU n 
2 12  ALA n 
2 13  ALA n 
2 14  PRO n 
2 15  ALA n 
2 16  ALA n 
2 17  GLU n 
2 18  GLU n 
2 19  LYS n 
2 20  GLU n 
2 21  GLU n 
2 22  ALA n 
2 23  ARG n 
2 24  GLU n 
2 25  LYS n 
2 26  MET n 
2 27  LEU n 
2 28  ALA n 
2 29  ALA n 
2 30  LYS n 
2 31  SER n 
2 32  ALA n 
2 33  ASP n 
2 34  GLY n 
2 35  SER n 
2 36  ALA n 
2 37  PRO n 
2 38  ALA n 
2 39  GLY n 
2 40  GLU n 
2 41  GLY n 
2 42  GLU n 
2 43  GLY n 
2 44  VAL n 
2 45  THR n 
2 46  LEU n 
2 47  GLN n 
2 48  ARG n 
2 49  ASN n 
2 50  ILE n 
2 51  THR n 
2 52  LEU n 
2 53  LEU n 
2 54  ASN n 
2 55  GLY n 
2 56  VAL n 
2 57  ALA n 
2 58  ILE n 
2 59  ILE n 
2 60  VAL n 
2 61  GLY n 
2 62  THR n 
2 63  ILE n 
2 64  ILE n 
2 65  GLY n 
2 66  SER n 
2 67  GLY n 
2 68  ILE n 
2 69  PHE n 
2 70  VAL n 
2 71  THR n 
2 72  PRO n 
2 73  THR n 
2 74  GLY n 
2 75  VAL n 
2 76  LEU n 
2 77  LYS n 
2 78  GLU n 
2 79  ALA n 
2 80  GLY n 
2 81  SER n 
2 82  PRO n 
2 83  GLY n 
2 84  LEU n 
2 85  ALA n 
2 86  LEU n 
2 87  VAL n 
2 88  VAL n 
2 89  TRP n 
2 90  ALA n 
2 91  ALA n 
2 92  CYS n 
2 93  GLY n 
2 94  VAL n 
2 95  PHE n 
2 96  SER n 
2 97  ILE n 
2 98  VAL n 
2 99  GLY n 
2 100 ALA n 
2 101 LEU n 
2 102 CYS n 
2 103 TYR n 
2 104 ALA n 
2 105 GLU n 
2 106 LEU n 
2 107 GLY n 
2 108 THR n 
2 109 THR n 
2 110 ILE n 
2 111 SER n 
2 112 LYS n 
2 113 SER n 
2 114 GLY n 
2 115 GLY n 
2 116 ASP n 
2 117 TYR n 
2 118 ALA n 
2 119 TYR n 
2 120 MET n 
2 121 LEU n 
2 122 GLU n 
2 123 VAL n 
2 124 TYR n 
2 125 GLY n 
2 126 SER n 
2 127 LEU n 
2 128 PRO n 
2 129 ALA n 
2 130 PHE n 
2 131 LEU n 
2 132 LYS n 
2 133 LEU n 
2 134 TRP n 
2 135 ILE n 
2 136 GLU n 
2 137 LEU n 
2 138 LEU n 
2 139 ILE n 
2 140 ILE n 
2 141 ARG n 
2 142 PRO n 
2 143 SER n 
2 144 SER n 
2 145 GLN n 
2 146 TYR n 
2 147 ILE n 
2 148 VAL n 
2 149 ALA n 
2 150 LEU n 
2 151 VAL n 
2 152 PHE n 
2 153 ALA n 
2 154 THR n 
2 155 TYR n 
2 156 LEU n 
2 157 LEU n 
2 158 LYS n 
2 159 PRO n 
2 160 LEU n 
2 161 PHE n 
2 162 PRO n 
2 163 THR n 
2 164 CYS n 
2 165 PRO n 
2 166 VAL n 
2 167 PRO n 
2 168 GLU n 
2 169 GLU n 
2 170 ALA n 
2 171 ALA n 
2 172 LYS n 
2 173 LEU n 
2 174 VAL n 
2 175 ALA n 
2 176 CYS n 
2 177 LEU n 
2 178 CYS n 
2 179 VAL n 
2 180 LEU n 
2 181 LEU n 
2 182 LEU n 
2 183 THR n 
2 184 ALA n 
2 185 VAL n 
2 186 ASN n 
2 187 CYS n 
2 188 TYR n 
2 189 SER n 
2 190 VAL n 
2 191 LYS n 
2 192 ALA n 
2 193 ALA n 
2 194 THR n 
2 195 ARG n 
2 196 VAL n 
2 197 GLN n 
2 198 ASP n 
2 199 ALA n 
2 200 PHE n 
2 201 ALA n 
2 202 ALA n 
2 203 ALA n 
2 204 LYS n 
2 205 LEU n 
2 206 LEU n 
2 207 ALA n 
2 208 LEU n 
2 209 ALA n 
2 210 LEU n 
2 211 ILE n 
2 212 ILE n 
2 213 LEU n 
2 214 LEU n 
2 215 GLY n 
2 216 PHE n 
2 217 VAL n 
2 218 GLN n 
2 219 ILE n 
2 220 GLY n 
2 221 LYS n 
2 222 GLY n 
2 223 ASP n 
2 224 VAL n 
2 225 SER n 
2 226 ASN n 
2 227 LEU n 
2 228 ASP n 
2 229 PRO n 
2 230 ASN n 
2 231 PHE n 
2 232 SER n 
2 233 PHE n 
2 234 GLU n 
2 235 GLY n 
2 236 THR n 
2 237 LYS n 
2 238 LEU n 
2 239 ASP n 
2 240 VAL n 
2 241 GLY n 
2 242 ASN n 
2 243 ILE n 
2 244 VAL n 
2 245 LEU n 
2 246 ALA n 
2 247 LEU n 
2 248 TYR n 
2 249 SER n 
2 250 GLY n 
2 251 LEU n 
2 252 PHE n 
2 253 ALA n 
2 254 TYR n 
2 255 GLY n 
2 256 GLY n 
2 257 TRP n 
2 258 ASN n 
2 259 TYR n 
2 260 LEU n 
2 261 ASN n 
2 262 PHE n 
2 263 VAL n 
2 264 THR n 
2 265 GLU n 
2 266 GLU n 
2 267 MET n 
2 268 ILE n 
2 269 ASN n 
2 270 PRO n 
2 271 TYR n 
2 272 ARG n 
2 273 ASN n 
2 274 LEU n 
2 275 PRO n 
2 276 LEU n 
2 277 ALA n 
2 278 ILE n 
2 279 ILE n 
2 280 ILE n 
2 281 SER n 
2 282 LEU n 
2 283 PRO n 
2 284 ILE n 
2 285 VAL n 
2 286 THR n 
2 287 LEU n 
2 288 VAL n 
2 289 TYR n 
2 290 VAL n 
2 291 LEU n 
2 292 THR n 
2 293 ASN n 
2 294 LEU n 
2 295 ALA n 
2 296 TYR n 
2 297 PHE n 
2 298 THR n 
2 299 THR n 
2 300 LEU n 
2 301 SER n 
2 302 THR n 
2 303 GLU n 
2 304 GLN n 
2 305 MET n 
2 306 LEU n 
2 307 SER n 
2 308 SER n 
2 309 GLU n 
2 310 ALA n 
2 311 VAL n 
2 312 ALA n 
2 313 VAL n 
2 314 ASP n 
2 315 PHE n 
2 316 GLY n 
2 317 ASN n 
2 318 TYR n 
2 319 HIS n 
2 320 LEU n 
2 321 GLY n 
2 322 VAL n 
2 323 MET n 
2 324 SER n 
2 325 TRP n 
2 326 ILE n 
2 327 ILE n 
2 328 PRO n 
2 329 VAL n 
2 330 PHE n 
2 331 VAL n 
2 332 GLY n 
2 333 LEU n 
2 334 SER n 
2 335 CYS n 
2 336 PHE n 
2 337 GLY n 
2 338 SER n 
2 339 VAL n 
2 340 ASN n 
2 341 GLY n 
2 342 SER n 
2 343 LEU n 
2 344 PHE n 
2 345 THR n 
2 346 SER n 
2 347 SER n 
2 348 ARG n 
2 349 LEU n 
2 350 PHE n 
2 351 PHE n 
2 352 VAL n 
2 353 GLY n 
2 354 SER n 
2 355 ARG n 
2 356 GLU n 
2 357 GLY n 
2 358 HIS n 
2 359 LEU n 
2 360 PRO n 
2 361 SER n 
2 362 ILE n 
2 363 LEU n 
2 364 SER n 
2 365 MET n 
2 366 ILE n 
2 367 HIS n 
2 368 PRO n 
2 369 GLN n 
2 370 LEU n 
2 371 LEU n 
2 372 THR n 
2 373 PRO n 
2 374 VAL n 
2 375 PRO n 
2 376 SER n 
2 377 LEU n 
2 378 VAL n 
2 379 PHE n 
2 380 THR n 
2 381 CYS n 
2 382 VAL n 
2 383 MET n 
2 384 THR n 
2 385 LEU n 
2 386 LEU n 
2 387 TYR n 
2 388 ALA n 
2 389 PHE n 
2 390 SER n 
2 391 LYS n 
2 392 ASP n 
2 393 ILE n 
2 394 PHE n 
2 395 SER n 
2 396 VAL n 
2 397 ILE n 
2 398 ASN n 
2 399 PHE n 
2 400 PHE n 
2 401 SER n 
2 402 PHE n 
2 403 PHE n 
2 404 ASN n 
2 405 TRP n 
2 406 LEU n 
2 407 CYS n 
2 408 VAL n 
2 409 ALA n 
2 410 LEU n 
2 411 ALA n 
2 412 ILE n 
2 413 ILE n 
2 414 GLY n 
2 415 MET n 
2 416 ILE n 
2 417 TRP n 
2 418 LEU n 
2 419 ARG n 
2 420 HIS n 
2 421 ARG n 
2 422 LYS n 
2 423 PRO n 
2 424 GLU n 
2 425 LEU n 
2 426 GLU n 
2 427 ARG n 
2 428 PRO n 
2 429 ILE n 
2 430 LYS n 
2 431 VAL n 
2 432 ASN n 
2 433 LEU n 
2 434 ALA n 
2 435 LEU n 
2 436 PRO n 
2 437 VAL n 
2 438 PHE n 
2 439 PHE n 
2 440 ILE n 
2 441 LEU n 
2 442 ALA n 
2 443 CYS n 
2 444 LEU n 
2 445 PHE n 
2 446 LEU n 
2 447 ILE n 
2 448 ALA n 
2 449 VAL n 
2 450 SER n 
2 451 PHE n 
2 452 TRP n 
2 453 LYS n 
2 454 THR n 
2 455 PRO n 
2 456 VAL n 
2 457 GLU n 
2 458 CYS n 
2 459 GLY n 
2 460 ILE n 
2 461 GLY n 
2 462 PHE n 
2 463 THR n 
2 464 ILE n 
2 465 ILE n 
2 466 LEU n 
2 467 SER n 
2 468 GLY n 
2 469 LEU n 
2 470 PRO n 
2 471 VAL n 
2 472 TYR n 
2 473 PHE n 
2 474 PHE n 
2 475 GLY n 
2 476 VAL n 
2 477 TRP n 
2 478 TRP n 
2 479 LYS n 
2 480 ASN n 
2 481 LYS n 
2 482 PRO n 
2 483 LYS n 
2 484 TRP n 
2 485 LEU n 
2 486 LEU n 
2 487 GLN n 
2 488 GLY n 
2 489 ILE n 
2 490 PHE n 
2 491 SER n 
2 492 THR n 
2 493 THR n 
2 494 VAL n 
2 495 LEU n 
2 496 CYS n 
2 497 GLN n 
2 498 LYS n 
2 499 LEU n 
2 500 MET n 
2 501 GLN n 
2 502 VAL n 
2 503 VAL n 
2 504 PRO n 
2 505 GLN n 
2 506 GLU n 
2 507 THR n 
2 508 ASP n 
2 509 TYR n 
2 510 LYS n 
2 511 ASP n 
2 512 ASP n 
2 513 ASP n 
2 514 ASP n 
2 515 LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 631 human ? 'SLC3A2, MDU1'                ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? HEK293 ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 515 human ? 'SLC7A5, CD98LC, LAT1, MPE16' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? HEK293 ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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  
ARG 'L-peptide linking' y ARGININE                                                               ?         'C6 H15 N4 O2 1'    
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                             ?         'C4 H8 N2 O3'       
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                        ?         'C4 H7 N O4'        
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                               ?         'C3 H7 N O2 S'      
121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                              ?         'C5 H10 N2 O3'      
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                        ?         'C5 H9 N O4'        
147.129 
GLY 'peptide linking'   y GLYCINE                                                                ?         'C2 H5 N O2'        
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                              ?         'C6 H10 N3 O2 1'    
156.162 
ILE 'L-peptide linking' y ISOLEUCINE                                                             ?         'C6 H13 N O2'       
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                ?         'C6 H13 N O2'       
131.173 
LYS 'L-peptide linking' y LYSINE                                                                 ?         'C6 H15 N2 O2 1'    
147.195 
MET 'L-peptide linking' y METHIONINE                                                             ?         'C5 H11 N O2 S'     
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                          ?         'C9 H11 N O2'       
165.189 
PRO 'L-peptide linking' y PROLINE                                                                ?         'C5 H9 N O2'        
115.130 
SER 'L-peptide linking' y SERINE                                                                 ?         'C3 H7 N O3'        
105.093 
THR 'L-peptide linking' y THREONINE                                                              ?         'C4 H9 N O3'        
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                             ?         'C11 H12 N2 O2'     
204.225 
TYR 'L-peptide linking' y TYROSINE                                                               ?         'C9 H11 N O3'       
181.189 
VAL 'L-peptide linking' y VALINE                                                                 ?         'C5 H11 N O2'       
117.146 
VUC non-polymer         . '(2~{S})-2-azanyl-3-[4-[bis(2-chloroethyl)amino]phenyl]propanoic acid' melphalan 'C13 H18 Cl2 N2 O2' 
305.200 
# 
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   GLY 1   0   ?   ?   ?   A . n 
A 1 2   SER 2   1   ?   ?   ?   A . n 
A 1 3   GLU 3   2   ?   ?   ?   A . n 
A 1 4   LEU 4   3   ?   ?   ?   A . n 
A 1 5   GLN 5   4   ?   ?   ?   A . n 
A 1 6   PRO 6   5   ?   ?   ?   A . n 
A 1 7   PRO 7   6   ?   ?   ?   A . n 
A 1 8   GLU 8   7   ?   ?   ?   A . n 
A 1 9   ALA 9   8   ?   ?   ?   A . n 
A 1 10  SER 10  9   ?   ?   ?   A . n 
A 1 11  ILE 11  10  ?   ?   ?   A . n 
A 1 12  ALA 12  11  ?   ?   ?   A . n 
A 1 13  VAL 13  12  ?   ?   ?   A . n 
A 1 14  VAL 14  13  ?   ?   ?   A . n 
A 1 15  SER 15  14  ?   ?   ?   A . n 
A 1 16  ILE 16  15  ?   ?   ?   A . n 
A 1 17  PRO 17  16  ?   ?   ?   A . n 
A 1 18  ARG 18  17  ?   ?   ?   A . n 
A 1 19  GLN 19  18  ?   ?   ?   A . n 
A 1 20  LEU 20  19  ?   ?   ?   A . n 
A 1 21  PRO 21  20  ?   ?   ?   A . n 
A 1 22  GLY 22  21  ?   ?   ?   A . n 
A 1 23  SER 23  22  ?   ?   ?   A . n 
A 1 24  HIS 24  23  ?   ?   ?   A . n 
A 1 25  SER 25  24  ?   ?   ?   A . n 
A 1 26  GLU 26  25  ?   ?   ?   A . n 
A 1 27  ALA 27  26  ?   ?   ?   A . n 
A 1 28  GLY 28  27  ?   ?   ?   A . n 
A 1 29  VAL 29  28  ?   ?   ?   A . n 
A 1 30  GLN 30  29  ?   ?   ?   A . n 
A 1 31  GLY 31  30  ?   ?   ?   A . n 
A 1 32  LEU 32  31  ?   ?   ?   A . n 
A 1 33  SER 33  32  ?   ?   ?   A . n 
A 1 34  ALA 34  33  ?   ?   ?   A . n 
A 1 35  GLY 35  34  ?   ?   ?   A . n 
A 1 36  ASP 36  35  ?   ?   ?   A . n 
A 1 37  ASP 37  36  ?   ?   ?   A . n 
A 1 38  SER 38  37  ?   ?   ?   A . n 
A 1 39  GLU 39  38  ?   ?   ?   A . n 
A 1 40  LEU 40  39  ?   ?   ?   A . n 
A 1 41  GLY 41  40  ?   ?   ?   A . n 
A 1 42  SER 42  41  ?   ?   ?   A . n 
A 1 43  HIS 43  42  ?   ?   ?   A . n 
A 1 44  CYS 44  43  ?   ?   ?   A . n 
A 1 45  VAL 45  44  ?   ?   ?   A . n 
A 1 46  ALA 46  45  ?   ?   ?   A . n 
A 1 47  GLN 47  46  ?   ?   ?   A . n 
A 1 48  THR 48  47  ?   ?   ?   A . n 
A 1 49  GLY 49  48  ?   ?   ?   A . n 
A 1 50  LEU 50  49  ?   ?   ?   A . n 
A 1 51  GLU 51  50  ?   ?   ?   A . n 
A 1 52  LEU 52  51  ?   ?   ?   A . n 
A 1 53  LEU 53  52  ?   ?   ?   A . n 
A 1 54  ALA 54  53  ?   ?   ?   A . n 
A 1 55  SER 55  54  ?   ?   ?   A . n 
A 1 56  GLY 56  55  ?   ?   ?   A . n 
A 1 57  ASP 57  56  ?   ?   ?   A . n 
A 1 58  PRO 58  57  ?   ?   ?   A . n 
A 1 59  LEU 59  58  ?   ?   ?   A . n 
A 1 60  PRO 60  59  ?   ?   ?   A . n 
A 1 61  SER 61  60  ?   ?   ?   A . n 
A 1 62  ALA 62  61  ?   ?   ?   A . n 
A 1 63  SER 63  62  ?   ?   ?   A . n 
A 1 64  GLN 64  63  ?   ?   ?   A . n 
A 1 65  ASN 65  64  ?   ?   ?   A . n 
A 1 66  ALA 66  65  ?   ?   ?   A . n 
A 1 67  GLU 67  66  ?   ?   ?   A . n 
A 1 68  MET 68  67  ?   ?   ?   A . n 
A 1 69  ILE 69  68  ?   ?   ?   A . n 
A 1 70  GLU 70  69  ?   ?   ?   A . n 
A 1 71  THR 71  70  ?   ?   ?   A . n 
A 1 72  GLY 72  71  ?   ?   ?   A . n 
A 1 73  SER 73  72  ?   ?   ?   A . n 
A 1 74  ASP 74  73  ?   ?   ?   A . n 
A 1 75  CYS 75  74  ?   ?   ?   A . n 
A 1 76  VAL 76  75  ?   ?   ?   A . n 
A 1 77  THR 77  76  ?   ?   ?   A . n 
A 1 78  GLN 78  77  ?   ?   ?   A . n 
A 1 79  ALA 79  78  ?   ?   ?   A . n 
A 1 80  GLY 80  79  ?   ?   ?   A . n 
A 1 81  LEU 81  80  ?   ?   ?   A . n 
A 1 82  GLN 82  81  ?   ?   ?   A . n 
A 1 83  LEU 83  82  ?   ?   ?   A . n 
A 1 84  LEU 84  83  ?   ?   ?   A . n 
A 1 85  ALA 85  84  ?   ?   ?   A . n 
A 1 86  SER 86  85  ?   ?   ?   A . n 
A 1 87  SER 87  86  ?   ?   ?   A . n 
A 1 88  ASP 88  87  ?   ?   ?   A . n 
A 1 89  PRO 89  88  ?   ?   ?   A . n 
A 1 90  PRO 90  89  ?   ?   ?   A . n 
A 1 91  ALA 91  90  ?   ?   ?   A . n 
A 1 92  LEU 92  91  ?   ?   ?   A . n 
A 1 93  ALA 93  92  ?   ?   ?   A . n 
A 1 94  SER 94  93  ?   ?   ?   A . n 
A 1 95  LYS 95  94  ?   ?   ?   A . n 
A 1 96  ASN 96  95  ?   ?   ?   A . n 
A 1 97  ALA 97  96  ?   ?   ?   A . n 
A 1 98  GLU 98  97  ?   ?   ?   A . n 
A 1 99  VAL 99  98  ?   ?   ?   A . n 
A 1 100 THR 100 99  ?   ?   ?   A . n 
A 1 101 GLY 101 100 ?   ?   ?   A . n 
A 1 102 THR 102 101 ?   ?   ?   A . n 
A 1 103 MET 103 102 ?   ?   ?   A . n 
A 1 104 SER 104 103 ?   ?   ?   A . n 
A 1 105 GLN 105 104 ?   ?   ?   A . n 
A 1 106 ASP 106 105 ?   ?   ?   A . n 
A 1 107 THR 107 106 ?   ?   ?   A . n 
A 1 108 GLU 108 107 ?   ?   ?   A . n 
A 1 109 VAL 109 108 ?   ?   ?   A . n 
A 1 110 ASP 110 109 ?   ?   ?   A . n 
A 1 111 MET 111 110 ?   ?   ?   A . n 
A 1 112 LYS 112 111 ?   ?   ?   A . n 
A 1 113 GLU 113 112 ?   ?   ?   A . n 
A 1 114 VAL 114 113 ?   ?   ?   A . n 
A 1 115 GLU 115 114 ?   ?   ?   A . n 
A 1 116 LEU 116 115 ?   ?   ?   A . n 
A 1 117 ASN 117 116 ?   ?   ?   A . n 
A 1 118 GLU 118 117 ?   ?   ?   A . n 
A 1 119 LEU 119 118 ?   ?   ?   A . n 
A 1 120 GLU 120 119 ?   ?   ?   A . n 
A 1 121 PRO 121 120 ?   ?   ?   A . n 
A 1 122 GLU 122 121 ?   ?   ?   A . n 
A 1 123 LYS 123 122 ?   ?   ?   A . n 
A 1 124 GLN 124 123 ?   ?   ?   A . n 
A 1 125 PRO 125 124 ?   ?   ?   A . n 
A 1 126 MET 126 125 ?   ?   ?   A . n 
A 1 127 ASN 127 126 ?   ?   ?   A . n 
A 1 128 ALA 128 127 ?   ?   ?   A . n 
A 1 129 ALA 129 128 ?   ?   ?   A . n 
A 1 130 SER 130 129 ?   ?   ?   A . n 
A 1 131 GLY 131 130 ?   ?   ?   A . n 
A 1 132 ALA 132 131 ?   ?   ?   A . n 
A 1 133 ALA 133 132 ?   ?   ?   A . n 
A 1 134 MET 134 133 ?   ?   ?   A . n 
A 1 135 SER 135 134 ?   ?   ?   A . n 
A 1 136 LEU 136 135 ?   ?   ?   A . n 
A 1 137 ALA 137 136 ?   ?   ?   A . n 
A 1 138 GLY 138 137 ?   ?   ?   A . n 
A 1 139 ALA 139 138 ?   ?   ?   A . n 
A 1 140 GLU 140 139 ?   ?   ?   A . n 
A 1 141 LYS 141 140 ?   ?   ?   A . n 
A 1 142 ASN 142 141 ?   ?   ?   A . n 
A 1 143 GLY 143 142 ?   ?   ?   A . n 
A 1 144 LEU 144 143 ?   ?   ?   A . n 
A 1 145 VAL 145 144 ?   ?   ?   A . n 
A 1 146 LYS 146 145 ?   ?   ?   A . n 
A 1 147 ILE 147 146 ?   ?   ?   A . n 
A 1 148 LYS 148 147 ?   ?   ?   A . n 
A 1 149 VAL 149 148 ?   ?   ?   A . n 
A 1 150 ALA 150 149 ?   ?   ?   A . n 
A 1 151 GLU 151 150 ?   ?   ?   A . n 
A 1 152 ASP 152 151 ?   ?   ?   A . n 
A 1 153 GLU 153 152 ?   ?   ?   A . n 
A 1 154 ALA 154 153 ?   ?   ?   A . n 
A 1 155 GLU 155 154 ?   ?   ?   A . n 
A 1 156 ALA 156 155 ?   ?   ?   A . n 
A 1 157 ALA 157 156 ?   ?   ?   A . n 
A 1 158 ALA 158 157 ?   ?   ?   A . n 
A 1 159 ALA 159 158 ?   ?   ?   A . n 
A 1 160 ALA 160 159 ?   ?   ?   A . n 
A 1 161 LYS 161 160 ?   ?   ?   A . n 
A 1 162 PHE 162 161 ?   ?   ?   A . n 
A 1 163 THR 163 162 162 THR THR A . n 
A 1 164 GLY 164 163 163 GLY GLY A . n 
A 1 165 LEU 165 164 164 LEU LEU A . n 
A 1 166 SER 166 165 165 SER SER A . n 
A 1 167 LYS 167 166 166 LYS LYS A . n 
A 1 168 GLU 168 167 167 GLU GLU A . n 
A 1 169 GLU 169 168 168 GLU GLU A . n 
A 1 170 LEU 170 169 169 LEU LEU A . n 
A 1 171 LEU 171 170 170 LEU LEU A . n 
A 1 172 LYS 172 171 171 LYS LYS A . n 
A 1 173 VAL 173 172 172 VAL VAL A . n 
A 1 174 ALA 174 173 173 ALA ALA A . n 
A 1 175 GLY 175 174 174 GLY GLY A . n 
A 1 176 SER 176 175 175 SER SER A . n 
A 1 177 PRO 177 176 176 PRO PRO A . n 
A 1 178 GLY 178 177 177 GLY GLY A . n 
A 1 179 TRP 179 178 178 TRP TRP A . n 
A 1 180 VAL 180 179 179 VAL VAL A . n 
A 1 181 ARG 181 180 180 ARG ARG A . n 
A 1 182 THR 182 181 181 THR THR A . n 
A 1 183 ARG 183 182 182 ARG ARG A . n 
A 1 184 TRP 184 183 183 TRP TRP A . n 
A 1 185 ALA 185 184 184 ALA ALA A . n 
A 1 186 LEU 186 185 185 LEU LEU A . n 
A 1 187 LEU 187 186 186 LEU LEU A . n 
A 1 188 LEU 188 187 187 LEU LEU A . n 
A 1 189 LEU 189 188 188 LEU LEU A . n 
A 1 190 PHE 190 189 189 PHE PHE A . n 
A 1 191 TRP 191 190 190 TRP TRP A . n 
A 1 192 LEU 192 191 191 LEU LEU A . n 
A 1 193 GLY 193 192 192 GLY GLY A . n 
A 1 194 TRP 194 193 193 TRP TRP A . n 
A 1 195 LEU 195 194 194 LEU LEU A . n 
A 1 196 GLY 196 195 195 GLY GLY A . n 
A 1 197 MET 197 196 196 MET MET A . n 
A 1 198 LEU 198 197 197 LEU LEU A . n 
A 1 199 ALA 199 198 198 ALA ALA A . n 
A 1 200 GLY 200 199 199 GLY GLY A . n 
A 1 201 ALA 201 200 200 ALA ALA A . n 
A 1 202 VAL 202 201 201 VAL VAL A . n 
A 1 203 VAL 203 202 202 VAL VAL A . n 
A 1 204 ILE 204 203 203 ILE ILE A . n 
A 1 205 ILE 205 204 204 ILE ILE A . n 
A 1 206 VAL 206 205 205 VAL VAL A . n 
A 1 207 ARG 207 206 206 ARG ARG A . n 
A 1 208 ALA 208 207 207 ALA ALA A . n 
A 1 209 PRO 209 208 208 PRO PRO A . n 
A 1 210 ARG 210 209 209 ARG ARG A . n 
A 1 211 CYS 211 210 210 CYS CYS A . n 
A 1 212 ARG 212 211 211 ARG ARG A . n 
A 1 213 GLU 213 212 212 GLU GLU A . n 
A 1 214 LEU 214 213 213 LEU LEU A . n 
A 1 215 PRO 215 214 ?   ?   ?   A . n 
A 1 216 ALA 216 215 ?   ?   ?   A . n 
A 1 217 GLN 217 216 ?   ?   ?   A . n 
A 1 218 LYS 218 217 ?   ?   ?   A . n 
A 1 219 TRP 219 218 ?   ?   ?   A . n 
A 1 220 TRP 220 219 ?   ?   ?   A . n 
A 1 221 HIS 221 220 ?   ?   ?   A . n 
A 1 222 THR 222 221 ?   ?   ?   A . n 
A 1 223 GLY 223 222 ?   ?   ?   A . n 
A 1 224 ALA 224 223 ?   ?   ?   A . n 
A 1 225 LEU 225 224 ?   ?   ?   A . n 
A 1 226 TYR 226 225 ?   ?   ?   A . n 
A 1 227 ARG 227 226 ?   ?   ?   A . n 
A 1 228 ILE 228 227 ?   ?   ?   A . n 
A 1 229 GLY 229 228 ?   ?   ?   A . n 
A 1 230 ASP 230 229 ?   ?   ?   A . n 
A 1 231 LEU 231 230 ?   ?   ?   A . n 
A 1 232 GLN 232 231 ?   ?   ?   A . n 
A 1 233 ALA 233 232 ?   ?   ?   A . n 
A 1 234 PHE 234 233 ?   ?   ?   A . n 
A 1 235 GLN 235 234 ?   ?   ?   A . n 
A 1 236 GLY 236 235 ?   ?   ?   A . n 
A 1 237 HIS 237 236 ?   ?   ?   A . n 
A 1 238 GLY 238 237 ?   ?   ?   A . n 
A 1 239 ALA 239 238 ?   ?   ?   A . n 
A 1 240 GLY 240 239 ?   ?   ?   A . n 
A 1 241 ASN 241 240 ?   ?   ?   A . n 
A 1 242 LEU 242 241 ?   ?   ?   A . n 
A 1 243 ALA 243 242 ?   ?   ?   A . n 
A 1 244 GLY 244 243 ?   ?   ?   A . n 
A 1 245 LEU 245 244 ?   ?   ?   A . n 
A 1 246 LYS 246 245 ?   ?   ?   A . n 
A 1 247 GLY 247 246 ?   ?   ?   A . n 
A 1 248 ARG 248 247 ?   ?   ?   A . n 
A 1 249 LEU 249 248 ?   ?   ?   A . n 
A 1 250 ASP 250 249 ?   ?   ?   A . n 
A 1 251 TYR 251 250 ?   ?   ?   A . n 
A 1 252 LEU 252 251 ?   ?   ?   A . n 
A 1 253 SER 253 252 ?   ?   ?   A . n 
A 1 254 SER 254 253 ?   ?   ?   A . n 
A 1 255 LEU 255 254 ?   ?   ?   A . n 
A 1 256 LYS 256 255 ?   ?   ?   A . n 
A 1 257 VAL 257 256 ?   ?   ?   A . n 
A 1 258 LYS 258 257 ?   ?   ?   A . n 
A 1 259 GLY 259 258 ?   ?   ?   A . n 
A 1 260 LEU 260 259 ?   ?   ?   A . n 
A 1 261 VAL 261 260 ?   ?   ?   A . n 
A 1 262 LEU 262 261 ?   ?   ?   A . n 
A 1 263 GLY 263 262 ?   ?   ?   A . n 
A 1 264 PRO 264 263 ?   ?   ?   A . n 
A 1 265 ILE 265 264 ?   ?   ?   A . n 
A 1 266 HIS 266 265 ?   ?   ?   A . n 
A 1 267 LYS 267 266 ?   ?   ?   A . n 
A 1 268 ASN 268 267 ?   ?   ?   A . n 
A 1 269 GLN 269 268 ?   ?   ?   A . n 
A 1 270 LYS 270 269 ?   ?   ?   A . n 
A 1 271 ASP 271 270 ?   ?   ?   A . n 
A 1 272 ASP 272 271 ?   ?   ?   A . n 
A 1 273 VAL 273 272 ?   ?   ?   A . n 
A 1 274 ALA 274 273 ?   ?   ?   A . n 
A 1 275 GLN 275 274 ?   ?   ?   A . n 
A 1 276 THR 276 275 ?   ?   ?   A . n 
A 1 277 ASP 277 276 ?   ?   ?   A . n 
A 1 278 LEU 278 277 ?   ?   ?   A . n 
A 1 279 LEU 279 278 ?   ?   ?   A . n 
A 1 280 GLN 280 279 ?   ?   ?   A . n 
A 1 281 ILE 281 280 ?   ?   ?   A . n 
A 1 282 ASP 282 281 ?   ?   ?   A . n 
A 1 283 PRO 283 282 ?   ?   ?   A . n 
A 1 284 ASN 284 283 ?   ?   ?   A . n 
A 1 285 PHE 285 284 ?   ?   ?   A . n 
A 1 286 GLY 286 285 ?   ?   ?   A . n 
A 1 287 SER 287 286 ?   ?   ?   A . n 
A 1 288 LYS 288 287 ?   ?   ?   A . n 
A 1 289 GLU 289 288 ?   ?   ?   A . n 
A 1 290 ASP 290 289 ?   ?   ?   A . n 
A 1 291 PHE 291 290 ?   ?   ?   A . n 
A 1 292 ASP 292 291 ?   ?   ?   A . n 
A 1 293 SER 293 292 ?   ?   ?   A . n 
A 1 294 LEU 294 293 ?   ?   ?   A . n 
A 1 295 LEU 295 294 ?   ?   ?   A . n 
A 1 296 GLN 296 295 ?   ?   ?   A . n 
A 1 297 SER 297 296 ?   ?   ?   A . n 
A 1 298 ALA 298 297 ?   ?   ?   A . n 
A 1 299 LYS 299 298 ?   ?   ?   A . n 
A 1 300 LYS 300 299 ?   ?   ?   A . n 
A 1 301 LYS 301 300 ?   ?   ?   A . n 
A 1 302 SER 302 301 ?   ?   ?   A . n 
A 1 303 ILE 303 302 ?   ?   ?   A . n 
A 1 304 ARG 304 303 ?   ?   ?   A . n 
A 1 305 VAL 305 304 ?   ?   ?   A . n 
A 1 306 ILE 306 305 ?   ?   ?   A . n 
A 1 307 LEU 307 306 ?   ?   ?   A . n 
A 1 308 ASP 308 307 ?   ?   ?   A . n 
A 1 309 LEU 309 308 ?   ?   ?   A . n 
A 1 310 THR 310 309 ?   ?   ?   A . n 
A 1 311 PRO 311 310 ?   ?   ?   A . n 
A 1 312 ASN 312 311 ?   ?   ?   A . n 
A 1 313 TYR 313 312 ?   ?   ?   A . n 
A 1 314 ARG 314 313 ?   ?   ?   A . n 
A 1 315 GLY 315 314 ?   ?   ?   A . n 
A 1 316 GLU 316 315 ?   ?   ?   A . n 
A 1 317 ASN 317 316 ?   ?   ?   A . n 
A 1 318 SER 318 317 ?   ?   ?   A . n 
A 1 319 TRP 319 318 ?   ?   ?   A . n 
A 1 320 PHE 320 319 ?   ?   ?   A . n 
A 1 321 SER 321 320 ?   ?   ?   A . n 
A 1 322 THR 322 321 ?   ?   ?   A . n 
A 1 323 GLN 323 322 ?   ?   ?   A . n 
A 1 324 VAL 324 323 ?   ?   ?   A . n 
A 1 325 ASP 325 324 ?   ?   ?   A . n 
A 1 326 THR 326 325 ?   ?   ?   A . n 
A 1 327 VAL 327 326 ?   ?   ?   A . n 
A 1 328 ALA 328 327 ?   ?   ?   A . n 
A 1 329 THR 329 328 ?   ?   ?   A . n 
A 1 330 LYS 330 329 ?   ?   ?   A . n 
A 1 331 VAL 331 330 ?   ?   ?   A . n 
A 1 332 LYS 332 331 ?   ?   ?   A . n 
A 1 333 ASP 333 332 ?   ?   ?   A . n 
A 1 334 ALA 334 333 ?   ?   ?   A . n 
A 1 335 LEU 335 334 ?   ?   ?   A . n 
A 1 336 GLU 336 335 ?   ?   ?   A . n 
A 1 337 PHE 337 336 ?   ?   ?   A . n 
A 1 338 TRP 338 337 ?   ?   ?   A . n 
A 1 339 LEU 339 338 ?   ?   ?   A . n 
A 1 340 GLN 340 339 ?   ?   ?   A . n 
A 1 341 ALA 341 340 ?   ?   ?   A . n 
A 1 342 GLY 342 341 ?   ?   ?   A . n 
A 1 343 VAL 343 342 ?   ?   ?   A . n 
A 1 344 ASP 344 343 ?   ?   ?   A . n 
A 1 345 GLY 345 344 ?   ?   ?   A . n 
A 1 346 PHE 346 345 ?   ?   ?   A . n 
A 1 347 GLN 347 346 ?   ?   ?   A . n 
A 1 348 VAL 348 347 ?   ?   ?   A . n 
A 1 349 ARG 349 348 ?   ?   ?   A . n 
A 1 350 ASP 350 349 ?   ?   ?   A . n 
A 1 351 ILE 351 350 ?   ?   ?   A . n 
A 1 352 GLU 352 351 ?   ?   ?   A . n 
A 1 353 ASN 353 352 ?   ?   ?   A . n 
A 1 354 LEU 354 353 ?   ?   ?   A . n 
A 1 355 LYS 355 354 ?   ?   ?   A . n 
A 1 356 ASP 356 355 ?   ?   ?   A . n 
A 1 357 ALA 357 356 ?   ?   ?   A . n 
A 1 358 SER 358 357 ?   ?   ?   A . n 
A 1 359 SER 359 358 ?   ?   ?   A . n 
A 1 360 PHE 360 359 ?   ?   ?   A . n 
A 1 361 LEU 361 360 ?   ?   ?   A . n 
A 1 362 ALA 362 361 ?   ?   ?   A . n 
A 1 363 GLU 363 362 ?   ?   ?   A . n 
A 1 364 TRP 364 363 ?   ?   ?   A . n 
A 1 365 GLN 365 364 ?   ?   ?   A . n 
A 1 366 ASN 366 365 ?   ?   ?   A . n 
A 1 367 ILE 367 366 ?   ?   ?   A . n 
A 1 368 THR 368 367 ?   ?   ?   A . n 
A 1 369 LYS 369 368 ?   ?   ?   A . n 
A 1 370 GLY 370 369 ?   ?   ?   A . n 
A 1 371 PHE 371 370 ?   ?   ?   A . n 
A 1 372 SER 372 371 ?   ?   ?   A . n 
A 1 373 GLU 373 372 ?   ?   ?   A . n 
A 1 374 ASP 374 373 ?   ?   ?   A . n 
A 1 375 ARG 375 374 ?   ?   ?   A . n 
A 1 376 LEU 376 375 ?   ?   ?   A . n 
A 1 377 LEU 377 376 ?   ?   ?   A . n 
A 1 378 ILE 378 377 ?   ?   ?   A . n 
A 1 379 ALA 379 378 ?   ?   ?   A . n 
A 1 380 GLY 380 379 ?   ?   ?   A . n 
A 1 381 THR 381 380 ?   ?   ?   A . n 
A 1 382 ASN 382 381 ?   ?   ?   A . n 
A 1 383 SER 383 382 ?   ?   ?   A . n 
A 1 384 SER 384 383 ?   ?   ?   A . n 
A 1 385 ASP 385 384 ?   ?   ?   A . n 
A 1 386 LEU 386 385 ?   ?   ?   A . n 
A 1 387 GLN 387 386 ?   ?   ?   A . n 
A 1 388 GLN 388 387 ?   ?   ?   A . n 
A 1 389 ILE 389 388 ?   ?   ?   A . n 
A 1 390 LEU 390 389 ?   ?   ?   A . n 
A 1 391 SER 391 390 ?   ?   ?   A . n 
A 1 392 LEU 392 391 ?   ?   ?   A . n 
A 1 393 LEU 393 392 ?   ?   ?   A . n 
A 1 394 GLU 394 393 ?   ?   ?   A . n 
A 1 395 SER 395 394 ?   ?   ?   A . n 
A 1 396 ASN 396 395 ?   ?   ?   A . n 
A 1 397 LYS 397 396 ?   ?   ?   A . n 
A 1 398 ASP 398 397 ?   ?   ?   A . n 
A 1 399 LEU 399 398 ?   ?   ?   A . n 
A 1 400 LEU 400 399 ?   ?   ?   A . n 
A 1 401 LEU 401 400 ?   ?   ?   A . n 
A 1 402 THR 402 401 ?   ?   ?   A . n 
A 1 403 SER 403 402 ?   ?   ?   A . n 
A 1 404 SER 404 403 ?   ?   ?   A . n 
A 1 405 TYR 405 404 ?   ?   ?   A . n 
A 1 406 LEU 406 405 ?   ?   ?   A . n 
A 1 407 SER 407 406 ?   ?   ?   A . n 
A 1 408 ASP 408 407 ?   ?   ?   A . n 
A 1 409 SER 409 408 ?   ?   ?   A . n 
A 1 410 GLY 410 409 ?   ?   ?   A . n 
A 1 411 SER 411 410 ?   ?   ?   A . n 
A 1 412 THR 412 411 ?   ?   ?   A . n 
A 1 413 GLY 413 412 ?   ?   ?   A . n 
A 1 414 GLU 414 413 ?   ?   ?   A . n 
A 1 415 HIS 415 414 ?   ?   ?   A . n 
A 1 416 THR 416 415 ?   ?   ?   A . n 
A 1 417 LYS 417 416 ?   ?   ?   A . n 
A 1 418 SER 418 417 ?   ?   ?   A . n 
A 1 419 LEU 419 418 ?   ?   ?   A . n 
A 1 420 VAL 420 419 ?   ?   ?   A . n 
A 1 421 THR 421 420 ?   ?   ?   A . n 
A 1 422 GLN 422 421 ?   ?   ?   A . n 
A 1 423 TYR 423 422 ?   ?   ?   A . n 
A 1 424 LEU 424 423 ?   ?   ?   A . n 
A 1 425 ASN 425 424 ?   ?   ?   A . n 
A 1 426 ALA 426 425 ?   ?   ?   A . n 
A 1 427 THR 427 426 ?   ?   ?   A . n 
A 1 428 GLY 428 427 ?   ?   ?   A . n 
A 1 429 ASN 429 428 ?   ?   ?   A . n 
A 1 430 ARG 430 429 ?   ?   ?   A . n 
A 1 431 TRP 431 430 ?   ?   ?   A . n 
A 1 432 CYS 432 431 ?   ?   ?   A . n 
A 1 433 SER 433 432 ?   ?   ?   A . n 
A 1 434 TRP 434 433 ?   ?   ?   A . n 
A 1 435 SER 435 434 ?   ?   ?   A . n 
A 1 436 LEU 436 435 ?   ?   ?   A . n 
A 1 437 SER 437 436 ?   ?   ?   A . n 
A 1 438 GLN 438 437 ?   ?   ?   A . n 
A 1 439 ALA 439 438 ?   ?   ?   A . n 
A 1 440 ARG 440 439 ?   ?   ?   A . n 
A 1 441 LEU 441 440 ?   ?   ?   A . n 
A 1 442 LEU 442 441 ?   ?   ?   A . n 
A 1 443 THR 443 442 ?   ?   ?   A . n 
A 1 444 SER 444 443 ?   ?   ?   A . n 
A 1 445 PHE 445 444 ?   ?   ?   A . n 
A 1 446 LEU 446 445 ?   ?   ?   A . n 
A 1 447 PRO 447 446 ?   ?   ?   A . n 
A 1 448 ALA 448 447 ?   ?   ?   A . n 
A 1 449 GLN 449 448 ?   ?   ?   A . n 
A 1 450 LEU 450 449 ?   ?   ?   A . n 
A 1 451 LEU 451 450 ?   ?   ?   A . n 
A 1 452 ARG 452 451 ?   ?   ?   A . n 
A 1 453 LEU 453 452 ?   ?   ?   A . n 
A 1 454 TYR 454 453 ?   ?   ?   A . n 
A 1 455 GLN 455 454 ?   ?   ?   A . n 
A 1 456 LEU 456 455 ?   ?   ?   A . n 
A 1 457 MET 457 456 ?   ?   ?   A . n 
A 1 458 LEU 458 457 ?   ?   ?   A . n 
A 1 459 PHE 459 458 ?   ?   ?   A . n 
A 1 460 THR 460 459 ?   ?   ?   A . n 
A 1 461 LEU 461 460 ?   ?   ?   A . n 
A 1 462 PRO 462 461 ?   ?   ?   A . n 
A 1 463 GLY 463 462 ?   ?   ?   A . n 
A 1 464 THR 464 463 ?   ?   ?   A . n 
A 1 465 PRO 465 464 ?   ?   ?   A . n 
A 1 466 VAL 466 465 ?   ?   ?   A . n 
A 1 467 PHE 467 466 ?   ?   ?   A . n 
A 1 468 SER 468 467 ?   ?   ?   A . n 
A 1 469 TYR 469 468 ?   ?   ?   A . n 
A 1 470 GLY 470 469 ?   ?   ?   A . n 
A 1 471 ASP 471 470 ?   ?   ?   A . n 
A 1 472 GLU 472 471 ?   ?   ?   A . n 
A 1 473 ILE 473 472 ?   ?   ?   A . n 
A 1 474 GLY 474 473 ?   ?   ?   A . n 
A 1 475 LEU 475 474 ?   ?   ?   A . n 
A 1 476 ASP 476 475 ?   ?   ?   A . n 
A 1 477 ALA 477 476 ?   ?   ?   A . n 
A 1 478 ALA 478 477 ?   ?   ?   A . n 
A 1 479 ALA 479 478 ?   ?   ?   A . n 
A 1 480 LEU 480 479 ?   ?   ?   A . n 
A 1 481 PRO 481 480 ?   ?   ?   A . n 
A 1 482 GLY 482 481 ?   ?   ?   A . n 
A 1 483 GLN 483 482 ?   ?   ?   A . n 
A 1 484 PRO 484 483 ?   ?   ?   A . n 
A 1 485 MET 485 484 ?   ?   ?   A . n 
A 1 486 GLU 486 485 ?   ?   ?   A . n 
A 1 487 ALA 487 486 ?   ?   ?   A . n 
A 1 488 PRO 488 487 ?   ?   ?   A . n 
A 1 489 VAL 489 488 ?   ?   ?   A . n 
A 1 490 MET 490 489 ?   ?   ?   A . n 
A 1 491 LEU 491 490 ?   ?   ?   A . n 
A 1 492 TRP 492 491 ?   ?   ?   A . n 
A 1 493 ASP 493 492 ?   ?   ?   A . n 
A 1 494 GLU 494 493 ?   ?   ?   A . n 
A 1 495 SER 495 494 ?   ?   ?   A . n 
A 1 496 SER 496 495 ?   ?   ?   A . n 
A 1 497 PHE 497 496 ?   ?   ?   A . n 
A 1 498 PRO 498 497 ?   ?   ?   A . n 
A 1 499 ASP 499 498 ?   ?   ?   A . n 
A 1 500 ILE 500 499 ?   ?   ?   A . n 
A 1 501 PRO 501 500 ?   ?   ?   A . n 
A 1 502 GLY 502 501 ?   ?   ?   A . n 
A 1 503 ALA 503 502 ?   ?   ?   A . n 
A 1 504 VAL 504 503 ?   ?   ?   A . n 
A 1 505 SER 505 504 ?   ?   ?   A . n 
A 1 506 ALA 506 505 ?   ?   ?   A . n 
A 1 507 ASN 507 506 ?   ?   ?   A . n 
A 1 508 MET 508 507 ?   ?   ?   A . n 
A 1 509 THR 509 508 ?   ?   ?   A . n 
A 1 510 VAL 510 509 ?   ?   ?   A . n 
A 1 511 LYS 511 510 ?   ?   ?   A . n 
A 1 512 GLY 512 511 ?   ?   ?   A . n 
A 1 513 GLN 513 512 ?   ?   ?   A . n 
A 1 514 SER 514 513 ?   ?   ?   A . n 
A 1 515 GLU 515 514 ?   ?   ?   A . n 
A 1 516 ASP 516 515 ?   ?   ?   A . n 
A 1 517 PRO 517 516 ?   ?   ?   A . n 
A 1 518 GLY 518 517 ?   ?   ?   A . n 
A 1 519 SER 519 518 ?   ?   ?   A . n 
A 1 520 LEU 520 519 ?   ?   ?   A . n 
A 1 521 LEU 521 520 ?   ?   ?   A . n 
A 1 522 SER 522 521 ?   ?   ?   A . n 
A 1 523 LEU 523 522 ?   ?   ?   A . n 
A 1 524 PHE 524 523 ?   ?   ?   A . n 
A 1 525 ARG 525 524 ?   ?   ?   A . n 
A 1 526 ARG 526 525 ?   ?   ?   A . n 
A 1 527 LEU 527 526 ?   ?   ?   A . n 
A 1 528 SER 528 527 ?   ?   ?   A . n 
A 1 529 ASP 529 528 ?   ?   ?   A . n 
A 1 530 GLN 530 529 ?   ?   ?   A . n 
A 1 531 ARG 531 530 ?   ?   ?   A . n 
A 1 532 SER 532 531 ?   ?   ?   A . n 
A 1 533 LYS 533 532 ?   ?   ?   A . n 
A 1 534 GLU 534 533 ?   ?   ?   A . n 
A 1 535 ARG 535 534 ?   ?   ?   A . n 
A 1 536 SER 536 535 ?   ?   ?   A . n 
A 1 537 LEU 537 536 ?   ?   ?   A . n 
A 1 538 LEU 538 537 ?   ?   ?   A . n 
A 1 539 HIS 539 538 ?   ?   ?   A . n 
A 1 540 GLY 540 539 ?   ?   ?   A . n 
A 1 541 ASP 541 540 ?   ?   ?   A . n 
A 1 542 PHE 542 541 ?   ?   ?   A . n 
A 1 543 HIS 543 542 ?   ?   ?   A . n 
A 1 544 ALA 544 543 ?   ?   ?   A . n 
A 1 545 PHE 545 544 ?   ?   ?   A . n 
A 1 546 SER 546 545 ?   ?   ?   A . n 
A 1 547 ALA 547 546 ?   ?   ?   A . n 
A 1 548 GLY 548 547 ?   ?   ?   A . n 
A 1 549 PRO 549 548 ?   ?   ?   A . n 
A 1 550 GLY 550 549 ?   ?   ?   A . n 
A 1 551 LEU 551 550 ?   ?   ?   A . n 
A 1 552 PHE 552 551 ?   ?   ?   A . n 
A 1 553 SER 553 552 ?   ?   ?   A . n 
A 1 554 TYR 554 553 ?   ?   ?   A . n 
A 1 555 ILE 555 554 ?   ?   ?   A . n 
A 1 556 ARG 556 555 ?   ?   ?   A . n 
A 1 557 HIS 557 556 ?   ?   ?   A . n 
A 1 558 TRP 558 557 ?   ?   ?   A . n 
A 1 559 ASP 559 558 ?   ?   ?   A . n 
A 1 560 GLN 560 559 ?   ?   ?   A . n 
A 1 561 ASN 561 560 ?   ?   ?   A . n 
A 1 562 GLU 562 561 ?   ?   ?   A . n 
A 1 563 ARG 563 562 ?   ?   ?   A . n 
A 1 564 PHE 564 563 ?   ?   ?   A . n 
A 1 565 LEU 565 564 ?   ?   ?   A . n 
A 1 566 VAL 566 565 ?   ?   ?   A . n 
A 1 567 VAL 567 566 ?   ?   ?   A . n 
A 1 568 LEU 568 567 ?   ?   ?   A . n 
A 1 569 ASN 569 568 ?   ?   ?   A . n 
A 1 570 PHE 570 569 ?   ?   ?   A . n 
A 1 571 GLY 571 570 ?   ?   ?   A . n 
A 1 572 ASP 572 571 ?   ?   ?   A . n 
A 1 573 VAL 573 572 ?   ?   ?   A . n 
A 1 574 GLY 574 573 ?   ?   ?   A . n 
A 1 575 LEU 575 574 ?   ?   ?   A . n 
A 1 576 SER 576 575 ?   ?   ?   A . n 
A 1 577 ALA 577 576 ?   ?   ?   A . n 
A 1 578 GLY 578 577 ?   ?   ?   A . n 
A 1 579 LEU 579 578 ?   ?   ?   A . n 
A 1 580 GLN 580 579 ?   ?   ?   A . n 
A 1 581 ALA 581 580 ?   ?   ?   A . n 
A 1 582 SER 582 581 ?   ?   ?   A . n 
A 1 583 ASP 583 582 ?   ?   ?   A . n 
A 1 584 LEU 584 583 ?   ?   ?   A . n 
A 1 585 PRO 585 584 ?   ?   ?   A . n 
A 1 586 ALA 586 585 ?   ?   ?   A . n 
A 1 587 SER 587 586 ?   ?   ?   A . n 
A 1 588 ALA 588 587 ?   ?   ?   A . n 
A 1 589 SER 589 588 ?   ?   ?   A . n 
A 1 590 LEU 590 589 ?   ?   ?   A . n 
A 1 591 PRO 591 590 ?   ?   ?   A . n 
A 1 592 ALA 592 591 ?   ?   ?   A . n 
A 1 593 LYS 593 592 ?   ?   ?   A . n 
A 1 594 ALA 594 593 ?   ?   ?   A . n 
A 1 595 ASP 595 594 ?   ?   ?   A . n 
A 1 596 LEU 596 595 ?   ?   ?   A . n 
A 1 597 LEU 597 596 ?   ?   ?   A . n 
A 1 598 LEU 598 597 ?   ?   ?   A . n 
A 1 599 SER 599 598 ?   ?   ?   A . n 
A 1 600 THR 600 599 ?   ?   ?   A . n 
A 1 601 GLN 601 600 ?   ?   ?   A . n 
A 1 602 PRO 602 601 ?   ?   ?   A . n 
A 1 603 GLY 603 602 ?   ?   ?   A . n 
A 1 604 ARG 604 603 ?   ?   ?   A . n 
A 1 605 GLU 605 604 ?   ?   ?   A . n 
A 1 606 GLU 606 605 ?   ?   ?   A . n 
A 1 607 GLY 607 606 ?   ?   ?   A . n 
A 1 608 SER 608 607 ?   ?   ?   A . n 
A 1 609 PRO 609 608 ?   ?   ?   A . n 
A 1 610 LEU 610 609 ?   ?   ?   A . n 
A 1 611 GLU 611 610 ?   ?   ?   A . n 
A 1 612 LEU 612 611 ?   ?   ?   A . n 
A 1 613 GLU 613 612 ?   ?   ?   A . n 
A 1 614 ARG 614 613 ?   ?   ?   A . n 
A 1 615 LEU 615 614 ?   ?   ?   A . n 
A 1 616 LYS 616 615 ?   ?   ?   A . n 
A 1 617 LEU 617 616 ?   ?   ?   A . n 
A 1 618 GLU 618 617 ?   ?   ?   A . n 
A 1 619 PRO 619 618 ?   ?   ?   A . n 
A 1 620 HIS 620 619 ?   ?   ?   A . n 
A 1 621 GLU 621 620 ?   ?   ?   A . n 
A 1 622 GLY 622 621 ?   ?   ?   A . n 
A 1 623 LEU 623 622 ?   ?   ?   A . n 
A 1 624 LEU 624 623 ?   ?   ?   A . n 
A 1 625 LEU 625 624 ?   ?   ?   A . n 
A 1 626 ARG 626 625 ?   ?   ?   A . n 
A 1 627 PHE 627 626 ?   ?   ?   A . n 
A 1 628 PRO 628 627 ?   ?   ?   A . n 
A 1 629 TYR 629 628 ?   ?   ?   A . n 
A 1 630 ALA 630 629 ?   ?   ?   A . n 
A 1 631 ALA 631 630 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ALA 2   2   ?   ?   ?   B . n 
B 2 3   GLY 3   3   ?   ?   ?   B . n 
B 2 4   ALA 4   4   ?   ?   ?   B . n 
B 2 5   GLY 5   5   ?   ?   ?   B . n 
B 2 6   PRO 6   6   ?   ?   ?   B . n 
B 2 7   LYS 7   7   ?   ?   ?   B . n 
B 2 8   ARG 8   8   ?   ?   ?   B . n 
B 2 9   ARG 9   9   ?   ?   ?   B . n 
B 2 10  ALA 10  10  ?   ?   ?   B . n 
B 2 11  LEU 11  11  ?   ?   ?   B . n 
B 2 12  ALA 12  12  ?   ?   ?   B . n 
B 2 13  ALA 13  13  ?   ?   ?   B . n 
B 2 14  PRO 14  14  ?   ?   ?   B . n 
B 2 15  ALA 15  15  ?   ?   ?   B . n 
B 2 16  ALA 16  16  ?   ?   ?   B . n 
B 2 17  GLU 17  17  ?   ?   ?   B . n 
B 2 18  GLU 18  18  ?   ?   ?   B . n 
B 2 19  LYS 19  19  ?   ?   ?   B . n 
B 2 20  GLU 20  20  ?   ?   ?   B . n 
B 2 21  GLU 21  21  ?   ?   ?   B . n 
B 2 22  ALA 22  22  ?   ?   ?   B . n 
B 2 23  ARG 23  23  ?   ?   ?   B . n 
B 2 24  GLU 24  24  ?   ?   ?   B . n 
B 2 25  LYS 25  25  ?   ?   ?   B . n 
B 2 26  MET 26  26  ?   ?   ?   B . n 
B 2 27  LEU 27  27  ?   ?   ?   B . n 
B 2 28  ALA 28  28  ?   ?   ?   B . n 
B 2 29  ALA 29  29  ?   ?   ?   B . n 
B 2 30  LYS 30  30  ?   ?   ?   B . n 
B 2 31  SER 31  31  ?   ?   ?   B . n 
B 2 32  ALA 32  32  ?   ?   ?   B . n 
B 2 33  ASP 33  33  ?   ?   ?   B . n 
B 2 34  GLY 34  34  ?   ?   ?   B . n 
B 2 35  SER 35  35  ?   ?   ?   B . n 
B 2 36  ALA 36  36  ?   ?   ?   B . n 
B 2 37  PRO 37  37  ?   ?   ?   B . n 
B 2 38  ALA 38  38  ?   ?   ?   B . n 
B 2 39  GLY 39  39  ?   ?   ?   B . n 
B 2 40  GLU 40  40  ?   ?   ?   B . n 
B 2 41  GLY 41  41  ?   ?   ?   B . n 
B 2 42  GLU 42  42  ?   ?   ?   B . n 
B 2 43  GLY 43  43  ?   ?   ?   B . n 
B 2 44  VAL 44  44  44  VAL VAL B . n 
B 2 45  THR 45  45  45  THR THR B . n 
B 2 46  LEU 46  46  46  LEU LEU B . n 
B 2 47  GLN 47  47  47  GLN GLN B . n 
B 2 48  ARG 48  48  48  ARG ARG B . n 
B 2 49  ASN 49  49  49  ASN ASN B . n 
B 2 50  ILE 50  50  50  ILE ILE B . n 
B 2 51  THR 51  51  51  THR THR B . n 
B 2 52  LEU 52  52  52  LEU LEU B . n 
B 2 53  LEU 53  53  53  LEU LEU B . n 
B 2 54  ASN 54  54  54  ASN ASN B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  VAL 56  56  56  VAL VAL B . n 
B 2 57  ALA 57  57  57  ALA ALA B . n 
B 2 58  ILE 58  58  58  ILE ILE B . n 
B 2 59  ILE 59  59  59  ILE ILE B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  GLY 61  61  61  GLY GLY B . n 
B 2 62  THR 62  62  62  THR THR B . n 
B 2 63  ILE 63  63  63  ILE ILE B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  GLY 65  65  65  GLY GLY B . n 
B 2 66  SER 66  66  66  SER SER B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  ILE 68  68  68  ILE ILE B . n 
B 2 69  PHE 69  69  69  PHE PHE B . n 
B 2 70  VAL 70  70  70  VAL VAL B . n 
B 2 71  THR 71  71  71  THR THR B . n 
B 2 72  PRO 72  72  72  PRO PRO B . n 
B 2 73  THR 73  73  73  THR THR B . n 
B 2 74  GLY 74  74  74  GLY GLY B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  LEU 76  76  76  LEU LEU B . n 
B 2 77  LYS 77  77  77  LYS LYS B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ALA 79  79  79  ALA ALA B . n 
B 2 80  GLY 80  80  80  GLY GLY B . n 
B 2 81  SER 81  81  81  SER SER B . n 
B 2 82  PRO 82  82  82  PRO PRO B . n 
B 2 83  GLY 83  83  83  GLY GLY B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  ALA 85  85  85  ALA ALA B . n 
B 2 86  LEU 86  86  86  LEU LEU B . n 
B 2 87  VAL 87  87  87  VAL VAL B . n 
B 2 88  VAL 88  88  88  VAL VAL B . n 
B 2 89  TRP 89  89  89  TRP TRP B . n 
B 2 90  ALA 90  90  90  ALA ALA B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  CYS 92  92  92  CYS CYS B . n 
B 2 93  GLY 93  93  93  GLY GLY B . n 
B 2 94  VAL 94  94  94  VAL VAL B . n 
B 2 95  PHE 95  95  95  PHE PHE B . n 
B 2 96  SER 96  96  96  SER SER B . n 
B 2 97  ILE 97  97  97  ILE ILE B . n 
B 2 98  VAL 98  98  98  VAL VAL B . n 
B 2 99  GLY 99  99  99  GLY GLY B . n 
B 2 100 ALA 100 100 100 ALA ALA B . n 
B 2 101 LEU 101 101 101 LEU LEU B . n 
B 2 102 CYS 102 102 102 CYS CYS B . n 
B 2 103 TYR 103 103 103 TYR TYR B . n 
B 2 104 ALA 104 104 104 ALA ALA B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 LEU 106 106 106 LEU LEU B . n 
B 2 107 GLY 107 107 107 GLY GLY B . n 
B 2 108 THR 108 108 108 THR THR B . n 
B 2 109 THR 109 109 109 THR THR B . n 
B 2 110 ILE 110 110 110 ILE ILE B . n 
B 2 111 SER 111 111 111 SER SER B . n 
B 2 112 LYS 112 112 112 LYS LYS B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 GLY 114 114 114 GLY GLY B . n 
B 2 115 GLY 115 115 115 GLY GLY B . n 
B 2 116 ASP 116 116 116 ASP ASP B . n 
B 2 117 TYR 117 117 117 TYR TYR B . n 
B 2 118 ALA 118 118 118 ALA ALA B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 MET 120 120 120 MET MET B . n 
B 2 121 LEU 121 121 121 LEU LEU B . n 
B 2 122 GLU 122 122 122 GLU GLU B . n 
B 2 123 VAL 123 123 123 VAL VAL B . n 
B 2 124 TYR 124 124 124 TYR TYR B . n 
B 2 125 GLY 125 125 125 GLY GLY B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 LEU 127 127 127 LEU LEU B . n 
B 2 128 PRO 128 128 128 PRO PRO B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 PHE 130 130 130 PHE PHE B . n 
B 2 131 LEU 131 131 131 LEU LEU B . n 
B 2 132 LYS 132 132 132 LYS LYS B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 TRP 134 134 134 TRP TRP B . n 
B 2 135 ILE 135 135 135 ILE ILE B . n 
B 2 136 GLU 136 136 136 GLU GLU B . n 
B 2 137 LEU 137 137 137 LEU LEU B . n 
B 2 138 LEU 138 138 138 LEU LEU B . n 
B 2 139 ILE 139 139 139 ILE ILE B . n 
B 2 140 ILE 140 140 140 ILE ILE B . n 
B 2 141 ARG 141 141 141 ARG ARG B . n 
B 2 142 PRO 142 142 142 PRO PRO B . n 
B 2 143 SER 143 143 143 SER SER B . n 
B 2 144 SER 144 144 144 SER SER B . n 
B 2 145 GLN 145 145 145 GLN GLN B . n 
B 2 146 TYR 146 146 146 TYR TYR B . n 
B 2 147 ILE 147 147 147 ILE ILE B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 ALA 149 149 149 ALA ALA B . n 
B 2 150 LEU 150 150 150 LEU LEU B . n 
B 2 151 VAL 151 151 151 VAL VAL B . n 
B 2 152 PHE 152 152 152 PHE PHE B . n 
B 2 153 ALA 153 153 153 ALA ALA B . n 
B 2 154 THR 154 154 154 THR THR B . n 
B 2 155 TYR 155 155 155 TYR TYR B . n 
B 2 156 LEU 156 156 156 LEU LEU B . n 
B 2 157 LEU 157 157 157 LEU LEU B . n 
B 2 158 LYS 158 158 158 LYS LYS B . n 
B 2 159 PRO 159 159 159 PRO PRO B . n 
B 2 160 LEU 160 160 160 LEU LEU B . n 
B 2 161 PHE 161 161 161 PHE PHE B . n 
B 2 162 PRO 162 162 162 PRO PRO B . n 
B 2 163 THR 163 163 163 THR THR B . n 
B 2 164 CYS 164 164 164 CYS CYS B . n 
B 2 165 PRO 165 165 165 PRO PRO B . n 
B 2 166 VAL 166 166 166 VAL VAL B . n 
B 2 167 PRO 167 167 167 PRO PRO B . n 
B 2 168 GLU 168 168 168 GLU GLU B . n 
B 2 169 GLU 169 169 169 GLU GLU B . n 
B 2 170 ALA 170 170 170 ALA ALA B . n 
B 2 171 ALA 171 171 171 ALA ALA B . n 
B 2 172 LYS 172 172 172 LYS LYS B . n 
B 2 173 LEU 173 173 173 LEU LEU B . n 
B 2 174 VAL 174 174 174 VAL VAL B . n 
B 2 175 ALA 175 175 175 ALA ALA B . n 
B 2 176 CYS 176 176 176 CYS CYS B . n 
B 2 177 LEU 177 177 177 LEU LEU B . n 
B 2 178 CYS 178 178 178 CYS CYS B . n 
B 2 179 VAL 179 179 179 VAL VAL B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 LEU 181 181 181 LEU LEU B . n 
B 2 182 LEU 182 182 182 LEU LEU B . n 
B 2 183 THR 183 183 183 THR THR B . n 
B 2 184 ALA 184 184 184 ALA ALA B . n 
B 2 185 VAL 185 185 185 VAL VAL B . n 
B 2 186 ASN 186 186 186 ASN ASN B . n 
B 2 187 CYS 187 187 187 CYS CYS B . n 
B 2 188 TYR 188 188 188 TYR TYR B . n 
B 2 189 SER 189 189 189 SER SER B . n 
B 2 190 VAL 190 190 190 VAL VAL B . n 
B 2 191 LYS 191 191 191 LYS LYS B . n 
B 2 192 ALA 192 192 192 ALA ALA B . n 
B 2 193 ALA 193 193 193 ALA ALA B . n 
B 2 194 THR 194 194 194 THR THR B . n 
B 2 195 ARG 195 195 195 ARG ARG B . n 
B 2 196 VAL 196 196 196 VAL VAL B . n 
B 2 197 GLN 197 197 197 GLN GLN B . n 
B 2 198 ASP 198 198 198 ASP ASP B . n 
B 2 199 ALA 199 199 199 ALA ALA B . n 
B 2 200 PHE 200 200 200 PHE PHE B . n 
B 2 201 ALA 201 201 201 ALA ALA B . n 
B 2 202 ALA 202 202 202 ALA ALA B . n 
B 2 203 ALA 203 203 203 ALA ALA B . n 
B 2 204 LYS 204 204 204 LYS LYS B . n 
B 2 205 LEU 205 205 205 LEU LEU B . n 
B 2 206 LEU 206 206 206 LEU LEU B . n 
B 2 207 ALA 207 207 207 ALA ALA B . n 
B 2 208 LEU 208 208 208 LEU LEU B . n 
B 2 209 ALA 209 209 209 ALA ALA B . n 
B 2 210 LEU 210 210 210 LEU LEU B . n 
B 2 211 ILE 211 211 211 ILE ILE B . n 
B 2 212 ILE 212 212 212 ILE ILE B . n 
B 2 213 LEU 213 213 213 LEU LEU B . n 
B 2 214 LEU 214 214 214 LEU LEU B . n 
B 2 215 GLY 215 215 215 GLY GLY B . n 
B 2 216 PHE 216 216 216 PHE PHE B . n 
B 2 217 VAL 217 217 217 VAL VAL B . n 
B 2 218 GLN 218 218 218 GLN GLN B . n 
B 2 219 ILE 219 219 219 ILE ILE B . n 
B 2 220 GLY 220 220 220 GLY GLY B . n 
B 2 221 LYS 221 221 221 LYS LYS B . n 
B 2 222 GLY 222 222 222 GLY GLY B . n 
B 2 223 ASP 223 223 ?   ?   ?   B . n 
B 2 224 VAL 224 224 ?   ?   ?   B . n 
B 2 225 SER 225 225 ?   ?   ?   B . n 
B 2 226 ASN 226 226 ?   ?   ?   B . n 
B 2 227 LEU 227 227 ?   ?   ?   B . n 
B 2 228 ASP 228 228 ?   ?   ?   B . n 
B 2 229 PRO 229 229 ?   ?   ?   B . n 
B 2 230 ASN 230 230 ?   ?   ?   B . n 
B 2 231 PHE 231 231 ?   ?   ?   B . n 
B 2 232 SER 232 232 ?   ?   ?   B . n 
B 2 233 PHE 233 233 233 PHE PHE B . n 
B 2 234 GLU 234 234 234 GLU GLU B . n 
B 2 235 GLY 235 235 235 GLY GLY B . n 
B 2 236 THR 236 236 236 THR THR B . n 
B 2 237 LYS 237 237 237 LYS LYS B . n 
B 2 238 LEU 238 238 238 LEU LEU B . n 
B 2 239 ASP 239 239 239 ASP ASP B . n 
B 2 240 VAL 240 240 240 VAL VAL B . n 
B 2 241 GLY 241 241 241 GLY GLY B . n 
B 2 242 ASN 242 242 242 ASN ASN B . n 
B 2 243 ILE 243 243 243 ILE ILE B . n 
B 2 244 VAL 244 244 244 VAL VAL B . n 
B 2 245 LEU 245 245 245 LEU LEU B . n 
B 2 246 ALA 246 246 246 ALA ALA B . n 
B 2 247 LEU 247 247 247 LEU LEU B . n 
B 2 248 TYR 248 248 248 TYR TYR B . n 
B 2 249 SER 249 249 249 SER SER B . n 
B 2 250 GLY 250 250 250 GLY GLY B . n 
B 2 251 LEU 251 251 251 LEU LEU B . n 
B 2 252 PHE 252 252 252 PHE PHE B . n 
B 2 253 ALA 253 253 253 ALA ALA B . n 
B 2 254 TYR 254 254 254 TYR TYR B . n 
B 2 255 GLY 255 255 255 GLY GLY B . n 
B 2 256 GLY 256 256 256 GLY GLY B . n 
B 2 257 TRP 257 257 257 TRP TRP B . n 
B 2 258 ASN 258 258 258 ASN ASN B . n 
B 2 259 TYR 259 259 259 TYR TYR B . n 
B 2 260 LEU 260 260 260 LEU LEU B . n 
B 2 261 ASN 261 261 261 ASN ASN B . n 
B 2 262 PHE 262 262 262 PHE PHE B . n 
B 2 263 VAL 263 263 263 VAL VAL B . n 
B 2 264 THR 264 264 264 THR THR B . n 
B 2 265 GLU 265 265 265 GLU GLU B . n 
B 2 266 GLU 266 266 266 GLU GLU B . n 
B 2 267 MET 267 267 267 MET MET B . n 
B 2 268 ILE 268 268 268 ILE ILE B . n 
B 2 269 ASN 269 269 269 ASN ASN B . n 
B 2 270 PRO 270 270 270 PRO PRO B . n 
B 2 271 TYR 271 271 271 TYR TYR B . n 
B 2 272 ARG 272 272 272 ARG ARG B . n 
B 2 273 ASN 273 273 273 ASN ASN B . n 
B 2 274 LEU 274 274 274 LEU LEU B . n 
B 2 275 PRO 275 275 275 PRO PRO B . n 
B 2 276 LEU 276 276 276 LEU LEU B . n 
B 2 277 ALA 277 277 277 ALA ALA B . n 
B 2 278 ILE 278 278 278 ILE ILE B . n 
B 2 279 ILE 279 279 279 ILE ILE B . n 
B 2 280 ILE 280 280 280 ILE ILE B . n 
B 2 281 SER 281 281 281 SER SER B . n 
B 2 282 LEU 282 282 282 LEU LEU B . n 
B 2 283 PRO 283 283 283 PRO PRO B . n 
B 2 284 ILE 284 284 284 ILE ILE B . n 
B 2 285 VAL 285 285 285 VAL VAL B . n 
B 2 286 THR 286 286 286 THR THR B . n 
B 2 287 LEU 287 287 287 LEU LEU B . n 
B 2 288 VAL 288 288 288 VAL VAL B . n 
B 2 289 TYR 289 289 289 TYR TYR B . n 
B 2 290 VAL 290 290 290 VAL VAL B . n 
B 2 291 LEU 291 291 291 LEU LEU B . n 
B 2 292 THR 292 292 292 THR THR B . n 
B 2 293 ASN 293 293 293 ASN ASN B . n 
B 2 294 LEU 294 294 294 LEU LEU B . n 
B 2 295 ALA 295 295 295 ALA ALA B . n 
B 2 296 TYR 296 296 296 TYR TYR B . n 
B 2 297 PHE 297 297 297 PHE PHE B . n 
B 2 298 THR 298 298 298 THR THR B . n 
B 2 299 THR 299 299 299 THR THR B . n 
B 2 300 LEU 300 300 300 LEU LEU B . n 
B 2 301 SER 301 301 301 SER SER B . n 
B 2 302 THR 302 302 302 THR THR B . n 
B 2 303 GLU 303 303 303 GLU GLU B . n 
B 2 304 GLN 304 304 304 GLN GLN B . n 
B 2 305 MET 305 305 305 MET MET B . n 
B 2 306 LEU 306 306 306 LEU LEU B . n 
B 2 307 SER 307 307 307 SER SER B . n 
B 2 308 SER 308 308 308 SER SER B . n 
B 2 309 GLU 309 309 309 GLU GLU B . n 
B 2 310 ALA 310 310 310 ALA ALA B . n 
B 2 311 VAL 311 311 311 VAL VAL B . n 
B 2 312 ALA 312 312 312 ALA ALA B . n 
B 2 313 VAL 313 313 313 VAL VAL B . n 
B 2 314 ASP 314 314 314 ASP ASP B . n 
B 2 315 PHE 315 315 315 PHE PHE B . n 
B 2 316 GLY 316 316 316 GLY GLY B . n 
B 2 317 ASN 317 317 317 ASN ASN B . n 
B 2 318 TYR 318 318 318 TYR TYR B . n 
B 2 319 HIS 319 319 319 HIS HIS B . n 
B 2 320 LEU 320 320 320 LEU LEU B . n 
B 2 321 GLY 321 321 321 GLY GLY B . n 
B 2 322 VAL 322 322 322 VAL VAL B . n 
B 2 323 MET 323 323 323 MET MET B . n 
B 2 324 SER 324 324 324 SER SER B . n 
B 2 325 TRP 325 325 325 TRP TRP B . n 
B 2 326 ILE 326 326 326 ILE ILE B . n 
B 2 327 ILE 327 327 327 ILE ILE B . n 
B 2 328 PRO 328 328 328 PRO PRO B . n 
B 2 329 VAL 329 329 329 VAL VAL B . n 
B 2 330 PHE 330 330 330 PHE PHE B . n 
B 2 331 VAL 331 331 331 VAL VAL B . n 
B 2 332 GLY 332 332 332 GLY GLY B . n 
B 2 333 LEU 333 333 333 LEU LEU B . n 
B 2 334 SER 334 334 334 SER SER B . n 
B 2 335 CYS 335 335 335 CYS CYS B . n 
B 2 336 PHE 336 336 336 PHE PHE B . n 
B 2 337 GLY 337 337 337 GLY GLY B . n 
B 2 338 SER 338 338 338 SER SER B . n 
B 2 339 VAL 339 339 339 VAL VAL B . n 
B 2 340 ASN 340 340 340 ASN ASN B . n 
B 2 341 GLY 341 341 341 GLY GLY B . n 
B 2 342 SER 342 342 342 SER SER B . n 
B 2 343 LEU 343 343 343 LEU LEU B . n 
B 2 344 PHE 344 344 344 PHE PHE B . n 
B 2 345 THR 345 345 345 THR THR B . n 
B 2 346 SER 346 346 346 SER SER B . n 
B 2 347 SER 347 347 347 SER SER B . n 
B 2 348 ARG 348 348 348 ARG ARG B . n 
B 2 349 LEU 349 349 349 LEU LEU B . n 
B 2 350 PHE 350 350 350 PHE PHE B . n 
B 2 351 PHE 351 351 351 PHE PHE B . n 
B 2 352 VAL 352 352 352 VAL VAL B . n 
B 2 353 GLY 353 353 353 GLY GLY B . n 
B 2 354 SER 354 354 354 SER SER B . n 
B 2 355 ARG 355 355 355 ARG ARG B . n 
B 2 356 GLU 356 356 356 GLU GLU B . n 
B 2 357 GLY 357 357 357 GLY GLY B . n 
B 2 358 HIS 358 358 358 HIS HIS B . n 
B 2 359 LEU 359 359 359 LEU LEU B . n 
B 2 360 PRO 360 360 360 PRO PRO B . n 
B 2 361 SER 361 361 361 SER SER B . n 
B 2 362 ILE 362 362 362 ILE ILE B . n 
B 2 363 LEU 363 363 363 LEU LEU B . n 
B 2 364 SER 364 364 364 SER SER B . n 
B 2 365 MET 365 365 365 MET MET B . n 
B 2 366 ILE 366 366 366 ILE ILE B . n 
B 2 367 HIS 367 367 367 HIS HIS B . n 
B 2 368 PRO 368 368 368 PRO PRO B . n 
B 2 369 GLN 369 369 369 GLN GLN B . n 
B 2 370 LEU 370 370 370 LEU LEU B . n 
B 2 371 LEU 371 371 371 LEU LEU B . n 
B 2 372 THR 372 372 372 THR THR B . n 
B 2 373 PRO 373 373 373 PRO PRO B . n 
B 2 374 VAL 374 374 374 VAL VAL B . n 
B 2 375 PRO 375 375 375 PRO PRO B . n 
B 2 376 SER 376 376 376 SER SER B . n 
B 2 377 LEU 377 377 377 LEU LEU B . n 
B 2 378 VAL 378 378 378 VAL VAL B . n 
B 2 379 PHE 379 379 379 PHE PHE B . n 
B 2 380 THR 380 380 380 THR THR B . n 
B 2 381 CYS 381 381 381 CYS CYS B . n 
B 2 382 VAL 382 382 382 VAL VAL B . n 
B 2 383 MET 383 383 383 MET MET B . n 
B 2 384 THR 384 384 384 THR THR B . n 
B 2 385 LEU 385 385 385 LEU LEU B . n 
B 2 386 LEU 386 386 386 LEU LEU B . n 
B 2 387 TYR 387 387 387 TYR TYR B . n 
B 2 388 ALA 388 388 388 ALA ALA B . n 
B 2 389 PHE 389 389 389 PHE PHE B . n 
B 2 390 SER 390 390 390 SER SER B . n 
B 2 391 LYS 391 391 391 LYS LYS B . n 
B 2 392 ASP 392 392 392 ASP ASP B . n 
B 2 393 ILE 393 393 393 ILE ILE B . n 
B 2 394 PHE 394 394 394 PHE PHE B . n 
B 2 395 SER 395 395 395 SER SER B . n 
B 2 396 VAL 396 396 396 VAL VAL B . n 
B 2 397 ILE 397 397 397 ILE ILE B . n 
B 2 398 ASN 398 398 398 ASN ASN B . n 
B 2 399 PHE 399 399 399 PHE PHE B . n 
B 2 400 PHE 400 400 400 PHE PHE B . n 
B 2 401 SER 401 401 401 SER SER B . n 
B 2 402 PHE 402 402 402 PHE PHE B . n 
B 2 403 PHE 403 403 403 PHE PHE B . n 
B 2 404 ASN 404 404 404 ASN ASN B . n 
B 2 405 TRP 405 405 405 TRP TRP B . n 
B 2 406 LEU 406 406 406 LEU LEU B . n 
B 2 407 CYS 407 407 407 CYS CYS B . n 
B 2 408 VAL 408 408 408 VAL VAL B . n 
B 2 409 ALA 409 409 409 ALA ALA B . n 
B 2 410 LEU 410 410 410 LEU LEU B . n 
B 2 411 ALA 411 411 411 ALA ALA B . n 
B 2 412 ILE 412 412 412 ILE ILE B . n 
B 2 413 ILE 413 413 413 ILE ILE B . n 
B 2 414 GLY 414 414 414 GLY GLY B . n 
B 2 415 MET 415 415 415 MET MET B . n 
B 2 416 ILE 416 416 416 ILE ILE B . n 
B 2 417 TRP 417 417 417 TRP TRP B . n 
B 2 418 LEU 418 418 418 LEU LEU B . n 
B 2 419 ARG 419 419 419 ARG ARG B . n 
B 2 420 HIS 420 420 420 HIS HIS B . n 
B 2 421 ARG 421 421 421 ARG ARG B . n 
B 2 422 LYS 422 422 422 LYS LYS B . n 
B 2 423 PRO 423 423 423 PRO PRO B . n 
B 2 424 GLU 424 424 424 GLU GLU B . n 
B 2 425 LEU 425 425 425 LEU LEU B . n 
B 2 426 GLU 426 426 426 GLU GLU B . n 
B 2 427 ARG 427 427 427 ARG ARG B . n 
B 2 428 PRO 428 428 428 PRO PRO B . n 
B 2 429 ILE 429 429 429 ILE ILE B . n 
B 2 430 LYS 430 430 430 LYS LYS B . n 
B 2 431 VAL 431 431 431 VAL VAL B . n 
B 2 432 ASN 432 432 432 ASN ASN B . n 
B 2 433 LEU 433 433 433 LEU LEU B . n 
B 2 434 ALA 434 434 434 ALA ALA B . n 
B 2 435 LEU 435 435 435 LEU LEU B . n 
B 2 436 PRO 436 436 436 PRO PRO B . n 
B 2 437 VAL 437 437 437 VAL VAL B . n 
B 2 438 PHE 438 438 438 PHE PHE B . n 
B 2 439 PHE 439 439 439 PHE PHE B . n 
B 2 440 ILE 440 440 440 ILE ILE B . n 
B 2 441 LEU 441 441 441 LEU LEU B . n 
B 2 442 ALA 442 442 442 ALA ALA B . n 
B 2 443 CYS 443 443 443 CYS CYS B . n 
B 2 444 LEU 444 444 444 LEU LEU B . n 
B 2 445 PHE 445 445 445 PHE PHE B . n 
B 2 446 LEU 446 446 446 LEU LEU B . n 
B 2 447 ILE 447 447 447 ILE ILE B . n 
B 2 448 ALA 448 448 448 ALA ALA B . n 
B 2 449 VAL 449 449 449 VAL VAL B . n 
B 2 450 SER 450 450 450 SER SER B . n 
B 2 451 PHE 451 451 451 PHE PHE B . n 
B 2 452 TRP 452 452 452 TRP TRP B . n 
B 2 453 LYS 453 453 453 LYS LYS B . n 
B 2 454 THR 454 454 454 THR THR B . n 
B 2 455 PRO 455 455 455 PRO PRO B . n 
B 2 456 VAL 456 456 456 VAL VAL B . n 
B 2 457 GLU 457 457 457 GLU GLU B . n 
B 2 458 CYS 458 458 458 CYS CYS B . n 
B 2 459 GLY 459 459 459 GLY GLY B . n 
B 2 460 ILE 460 460 460 ILE ILE B . n 
B 2 461 GLY 461 461 461 GLY GLY B . n 
B 2 462 PHE 462 462 462 PHE PHE B . n 
B 2 463 THR 463 463 463 THR THR B . n 
B 2 464 ILE 464 464 464 ILE ILE B . n 
B 2 465 ILE 465 465 465 ILE ILE B . n 
B 2 466 LEU 466 466 466 LEU LEU B . n 
B 2 467 SER 467 467 467 SER SER B . n 
B 2 468 GLY 468 468 468 GLY GLY B . n 
B 2 469 LEU 469 469 469 LEU LEU B . n 
B 2 470 PRO 470 470 470 PRO PRO B . n 
B 2 471 VAL 471 471 471 VAL VAL B . n 
B 2 472 TYR 472 472 472 TYR TYR B . n 
B 2 473 PHE 473 473 473 PHE PHE B . n 
B 2 474 PHE 474 474 474 PHE PHE B . n 
B 2 475 GLY 475 475 475 GLY GLY B . n 
B 2 476 VAL 476 476 476 VAL VAL B . n 
B 2 477 TRP 477 477 477 TRP TRP B . n 
B 2 478 TRP 478 478 478 TRP TRP B . n 
B 2 479 LYS 479 479 479 LYS LYS B . n 
B 2 480 ASN 480 480 480 ASN ASN B . n 
B 2 481 LYS 481 481 481 LYS LYS B . n 
B 2 482 PRO 482 482 482 PRO PRO B . n 
B 2 483 LYS 483 483 483 LYS LYS B . n 
B 2 484 TRP 484 484 484 TRP TRP B . n 
B 2 485 LEU 485 485 485 LEU LEU B . n 
B 2 486 LEU 486 486 486 LEU LEU B . n 
B 2 487 GLN 487 487 487 GLN GLN B . n 
B 2 488 GLY 488 488 488 GLY GLY B . n 
B 2 489 ILE 489 489 489 ILE ILE B . n 
B 2 490 PHE 490 490 490 PHE PHE B . n 
B 2 491 SER 491 491 491 SER SER B . n 
B 2 492 THR 492 492 492 THR THR B . n 
B 2 493 THR 493 493 493 THR THR B . n 
B 2 494 VAL 494 494 494 VAL VAL B . n 
B 2 495 LEU 495 495 495 LEU LEU B . n 
B 2 496 CYS 496 496 496 CYS CYS B . n 
B 2 497 GLN 497 497 497 GLN GLN B . n 
B 2 498 LYS 498 498 498 LYS LYS B . n 
B 2 499 LEU 499 499 499 LEU LEU B . n 
B 2 500 MET 500 500 500 MET MET B . n 
B 2 501 GLN 501 501 501 GLN GLN B . n 
B 2 502 VAL 502 502 502 VAL VAL B . n 
B 2 503 VAL 503 503 503 VAL VAL B . n 
B 2 504 PRO 504 504 504 PRO PRO B . n 
B 2 505 GLN 505 505 505 GLN GLN B . n 
B 2 506 GLU 506 506 506 GLU GLU B . n 
B 2 507 THR 507 507 507 THR THR B . n 
B 2 508 ASP 508 508 ?   ?   ?   B . n 
B 2 509 TYR 509 509 ?   ?   ?   B . n 
B 2 510 LYS 510 510 ?   ?   ?   B . n 
B 2 511 ASP 511 511 ?   ?   ?   B . n 
B 2 512 ASP 512 512 ?   ?   ?   B . n 
B 2 513 ASP 513 513 ?   ?   ?   B . n 
B 2 514 ASP 514 514 ?   ?   ?   B . n 
B 2 515 LYS 515 515 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        VUC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VUC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_nonpoly_scheme.asym_id         C 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          VUC 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     601 
_pdbx_nonpoly_scheme.auth_seq_num    601 
_pdbx_nonpoly_scheme.pdb_mon_id      VUC 
_pdbx_nonpoly_scheme.auth_mon_id     PAM 
_pdbx_nonpoly_scheme.pdb_strand_id   B 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_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                     8KDO 
_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                         8KDO 
_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                   8KDO 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               237.656 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.926 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8KDO 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            4.12 
_refine.ls_d_res_low                             4.12 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     22201 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.31766 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.31766 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'PARAMETERS FOR MASK CACLULATION' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD WITH PHASES' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.993 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             18.459 
_refine.overall_SU_ML                            0.258 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'ELECTRON MICROSCOPY' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       . 
_refine_hist.d_res_low                        . 
_refine_hist.number_atoms_solvent             ? 
_refine_hist.number_atoms_total               3937 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        ? 
_refine_hist.pdbx_number_atoms_nucleic_acid   ? 
_refine_hist.pdbx_number_atoms_ligand         ? 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.010  0.011  4041  ? r_bond_refined_d             ? ? 
'ELECTRON MICROSCOPY' ? 0.000  0.016  4033  ? r_bond_other_d               ? ? 
'ELECTRON MICROSCOPY' ? 1.854  1.624  5516  ? r_angle_refined_deg          ? ? 
'ELECTRON MICROSCOPY' ? 0.617  1.554  9242  ? r_angle_other_deg            ? ? 
'ELECTRON MICROSCOPY' ? 7.540  5.000  503   ? r_dihedral_angle_1_deg       ? ? 
'ELECTRON MICROSCOPY' ? 20.227 5.333  15    ? r_dihedral_angle_2_deg       ? ? 
'ELECTRON MICROSCOPY' ? 15.063 10.000 651   ? r_dihedral_angle_3_deg       ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'ELECTRON MICROSCOPY' ? 0.083  0.200  665   ? r_chiral_restr               ? ? 
'ELECTRON MICROSCOPY' ? 0.004  0.020  4569  ? r_gen_planes_refined         ? ? 
'ELECTRON MICROSCOPY' ? 0.001  0.020  923   ? r_gen_planes_other           ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'ELECTRON MICROSCOPY' ? 43.267 20.146 2021  ? r_mcbond_it                  ? ? 
'ELECTRON MICROSCOPY' ? 43.263 20.145 2021  ? r_mcbond_other               ? ? 
'ELECTRON MICROSCOPY' ? 58.024 36.383 2521  ? r_mcangle_it                 ? ? 
'ELECTRON MICROSCOPY' ? 58.019 36.396 2522  ? r_mcangle_other              ? ? 
'ELECTRON MICROSCOPY' ? 53.831 25.678 2020  ? r_scbond_it                  ? ? 
'ELECTRON MICROSCOPY' ? 53.821 25.683 2021  ? r_scbond_other               ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'ELECTRON MICROSCOPY' ? 78.708 44.991 2996  ? r_scangle_other              ? ? 
'ELECTRON MICROSCOPY' ? 78.399 251.96 16225 ? r_long_range_B_refined       ? ? 
'ELECTRON MICROSCOPY' ? 78.402 251.95 16226 ? r_long_range_B_other         ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'ELECTRON MICROSCOPY' 
_refine_ls_shell.d_res_high                       4.000 
_refine_ls_shell.d_res_low                        4.104 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             0 
_refine_ls_shell.number_reflns_R_work             1616 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  1.095 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.000 
# 
_struct.entry_id                     8KDO 
_struct.title                        'Structure of LAT1-CD98hc in complex with melphalan, focused on TMD' 
_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        8KDO 
_struct_keywords.text            'Transporter, Amino acid, Complex, Cancer, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT 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 3 ? 
# 
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 4F2_HUMAN  P08195 ? 1 
;ELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAGLQ
LLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKF
TGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGNL
AGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFST
QVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLT
SSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAALPG
QPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNE
RFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA
;
2 
2 UNP LAT1_HUMAN Q01650 ? 2 
;MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAG
SPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPL
FPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDV
GNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHL
GVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFF
SFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKN
KPKWLLQGIFSTTVLCQKLMQVVPQET
;
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 8KDO A 3 ? 631 ? P08195 2 ? 630 ? 2 630 
2 2 8KDO B 1 ? 507 ? Q01650 1 ? 507 ? 1 507 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8KDO GLY A 1   ? UNP P08195 ? ? 'expression tag' 0   1  
1 8KDO SER A 2   ? UNP P08195 ? ? 'expression tag' 1   2  
2 8KDO ASP B 508 ? UNP Q01650 ? ? 'expression tag' 508 3  
2 8KDO TYR B 509 ? UNP Q01650 ? ? 'expression tag' 509 4  
2 8KDO LYS B 510 ? UNP Q01650 ? ? 'expression tag' 510 5  
2 8KDO ASP B 511 ? UNP Q01650 ? ? 'expression tag' 511 6  
2 8KDO ASP B 512 ? UNP Q01650 ? ? 'expression tag' 512 7  
2 8KDO ASP B 513 ? UNP Q01650 ? ? 'expression tag' 513 8  
2 8KDO ASP B 514 ? UNP Q01650 ? ? 'expression tag' 514 9  
2 8KDO LYS B 515 ? UNP Q01650 ? ? 'expression tag' 515 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 166 ? GLY A 175 ? SER A 165 GLY A 174 1 ? 10 
HELX_P HELX_P2  AA2 SER A 176 ? ARG A 207 ? SER A 175 ARG A 206 1 ? 32 
HELX_P HELX_P3  AA3 THR B 51  ? ILE B 64  ? THR B 51  ILE B 64  1 ? 14 
HELX_P HELX_P4  AA4 SER B 66  ? THR B 71  ? SER B 66  THR B 71  1 ? 6  
HELX_P HELX_P5  AA5 THR B 71  ? GLY B 80  ? THR B 71  GLY B 80  1 ? 10 
HELX_P HELX_P6  AA6 SER B 81  ? SER B 111 ? SER B 81  SER B 111 1 ? 31 
HELX_P HELX_P7  AA7 GLY B 114 ? GLU B 122 ? GLY B 114 GLU B 122 1 ? 9  
HELX_P HELX_P8  AA8 GLY B 125 ? ILE B 139 ? GLY B 125 ILE B 139 1 ? 15 
HELX_P HELX_P9  AA9 ILE B 139 ? LEU B 157 ? ILE B 139 LEU B 157 1 ? 19 
HELX_P HELX_P10 AB1 LYS B 158 ? PHE B 161 ? LYS B 158 PHE B 161 5 ? 4  
HELX_P HELX_P11 AB2 PRO B 167 ? SER B 189 ? PRO B 167 SER B 189 1 ? 23 
HELX_P HELX_P12 AB3 SER B 189 ? GLY B 222 ? SER B 189 GLY B 222 1 ? 34 
HELX_P HELX_P13 AB4 ASP B 239 ? SER B 249 ? ASP B 239 SER B 249 1 ? 11 
HELX_P HELX_P14 AB5 SER B 249 ? TYR B 254 ? SER B 249 TYR B 254 1 ? 6  
HELX_P HELX_P15 AB6 ASN B 258 ? MET B 267 ? ASN B 258 MET B 267 5 ? 10 
HELX_P HELX_P16 AB7 ASN B 269 ? LEU B 300 ? ASN B 269 LEU B 300 1 ? 32 
HELX_P HELX_P17 AB8 SER B 301 ? SER B 308 ? SER B 301 SER B 308 1 ? 8  
HELX_P HELX_P18 AB9 ALA B 310 ? LEU B 320 ? ALA B 310 LEU B 320 1 ? 11 
HELX_P HELX_P19 AC1 TRP B 325 ? GLU B 356 ? TRP B 325 GLU B 356 1 ? 32 
HELX_P HELX_P20 AC2 PRO B 373 ? LEU B 386 ? PRO B 373 LEU B 386 1 ? 14 
HELX_P HELX_P21 AC3 ASP B 392 ? PHE B 400 ? ASP B 392 PHE B 400 1 ? 9  
HELX_P HELX_P22 AC4 PHE B 400 ? LYS B 422 ? PHE B 400 LYS B 422 1 ? 23 
HELX_P HELX_P23 AC5 LEU B 433 ? THR B 454 ? LEU B 433 THR B 454 1 ? 22 
HELX_P HELX_P24 AC6 GLU B 457 ? SER B 467 ? GLU B 457 SER B 467 1 ? 11 
HELX_P HELX_P25 AC7 SER B 467 ? VAL B 476 ? SER B 467 VAL B 476 1 ? 10 
HELX_P HELX_P26 AC8 PRO B 482 ? GLN B 501 ? PRO B 482 GLN B 501 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            211 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            164 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             210 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             164 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.097 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       211 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      164 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        210 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       164 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_pdbx_entry_details.entry_id                   8KDO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 206 ? ? -87.48  48.89  
2  1 GLU B 122 ? ? -69.36  1.38   
3  1 VAL B 123 ? ? -133.95 -69.53 
4  1 ILE B 139 ? ? -125.86 -65.12 
5  1 LEU B 238 ? ? -65.03  7.86   
6  1 ASN B 269 ? ? -151.27 78.99  
7  1 LEU B 320 ? ? -102.25 50.12  
8  1 ASP B 392 ? ? -98.98  43.44  
9  1 THR B 454 ? ? -149.43 58.30  
10 1 VAL B 476 ? ? -132.55 -47.92 
11 1 GLN B 501 ? ? 61.24   70.03  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    251 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    252 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.88 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     348 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.114 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8KDO 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8KDO 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  4.12 
_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               146704 
_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       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 LAT1-CD98hc-Fab170 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        8KDO 
_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             800 
_em_imaging.nominal_defocus_max             2000 
_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_vitrification.entry_id              8KDO 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8KDO 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_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 A GLY 0   ? A GLY 1   
2   1 Y 1 A SER 1   ? A SER 2   
3   1 Y 1 A GLU 2   ? A GLU 3   
4   1 Y 1 A LEU 3   ? A LEU 4   
5   1 Y 1 A GLN 4   ? A GLN 5   
6   1 Y 1 A PRO 5   ? A PRO 6   
7   1 Y 1 A PRO 6   ? A PRO 7   
8   1 Y 1 A GLU 7   ? A GLU 8   
9   1 Y 1 A ALA 8   ? A ALA 9   
10  1 Y 1 A SER 9   ? A SER 10  
11  1 Y 1 A ILE 10  ? A ILE 11  
12  1 Y 1 A ALA 11  ? A ALA 12  
13  1 Y 1 A VAL 12  ? A VAL 13  
14  1 Y 1 A VAL 13  ? A VAL 14  
15  1 Y 1 A SER 14  ? A SER 15  
16  1 Y 1 A ILE 15  ? A ILE 16  
17  1 Y 1 A PRO 16  ? A PRO 17  
18  1 Y 1 A ARG 17  ? A ARG 18  
19  1 Y 1 A GLN 18  ? A GLN 19  
20  1 Y 1 A LEU 19  ? A LEU 20  
21  1 Y 1 A PRO 20  ? A PRO 21  
22  1 Y 1 A GLY 21  ? A GLY 22  
23  1 Y 1 A SER 22  ? A SER 23  
24  1 Y 1 A HIS 23  ? A HIS 24  
25  1 Y 1 A SER 24  ? A SER 25  
26  1 Y 1 A GLU 25  ? A GLU 26  
27  1 Y 1 A ALA 26  ? A ALA 27  
28  1 Y 1 A GLY 27  ? A GLY 28  
29  1 Y 1 A VAL 28  ? A VAL 29  
30  1 Y 1 A GLN 29  ? A GLN 30  
31  1 Y 1 A GLY 30  ? A GLY 31  
32  1 Y 1 A LEU 31  ? A LEU 32  
33  1 Y 1 A SER 32  ? A SER 33  
34  1 Y 1 A ALA 33  ? A ALA 34  
35  1 Y 1 A GLY 34  ? A GLY 35  
36  1 Y 1 A ASP 35  ? A ASP 36  
37  1 Y 1 A ASP 36  ? A ASP 37  
38  1 Y 1 A SER 37  ? A SER 38  
39  1 Y 1 A GLU 38  ? A GLU 39  
40  1 Y 1 A LEU 39  ? A LEU 40  
41  1 Y 1 A GLY 40  ? A GLY 41  
42  1 Y 1 A SER 41  ? A SER 42  
43  1 Y 1 A HIS 42  ? A HIS 43  
44  1 Y 1 A CYS 43  ? A CYS 44  
45  1 Y 1 A VAL 44  ? A VAL 45  
46  1 Y 1 A ALA 45  ? A ALA 46  
47  1 Y 1 A GLN 46  ? A GLN 47  
48  1 Y 1 A THR 47  ? A THR 48  
49  1 Y 1 A GLY 48  ? A GLY 49  
50  1 Y 1 A LEU 49  ? A LEU 50  
51  1 Y 1 A GLU 50  ? A GLU 51  
52  1 Y 1 A LEU 51  ? A LEU 52  
53  1 Y 1 A LEU 52  ? A LEU 53  
54  1 Y 1 A ALA 53  ? A ALA 54  
55  1 Y 1 A SER 54  ? A SER 55  
56  1 Y 1 A GLY 55  ? A GLY 56  
57  1 Y 1 A ASP 56  ? A ASP 57  
58  1 Y 1 A PRO 57  ? A PRO 58  
59  1 Y 1 A LEU 58  ? A LEU 59  
60  1 Y 1 A PRO 59  ? A PRO 60  
61  1 Y 1 A SER 60  ? A SER 61  
62  1 Y 1 A ALA 61  ? A ALA 62  
63  1 Y 1 A SER 62  ? A SER 63  
64  1 Y 1 A GLN 63  ? A GLN 64  
65  1 Y 1 A ASN 64  ? A ASN 65  
66  1 Y 1 A ALA 65  ? A ALA 66  
67  1 Y 1 A GLU 66  ? A GLU 67  
68  1 Y 1 A MET 67  ? A MET 68  
69  1 Y 1 A ILE 68  ? A ILE 69  
70  1 Y 1 A GLU 69  ? A GLU 70  
71  1 Y 1 A THR 70  ? A THR 71  
72  1 Y 1 A GLY 71  ? A GLY 72  
73  1 Y 1 A SER 72  ? A SER 73  
74  1 Y 1 A ASP 73  ? A ASP 74  
75  1 Y 1 A CYS 74  ? A CYS 75  
76  1 Y 1 A VAL 75  ? A VAL 76  
77  1 Y 1 A THR 76  ? A THR 77  
78  1 Y 1 A GLN 77  ? A GLN 78  
79  1 Y 1 A ALA 78  ? A ALA 79  
80  1 Y 1 A GLY 79  ? A GLY 80  
81  1 Y 1 A LEU 80  ? A LEU 81  
82  1 Y 1 A GLN 81  ? A GLN 82  
83  1 Y 1 A LEU 82  ? A LEU 83  
84  1 Y 1 A LEU 83  ? A LEU 84  
85  1 Y 1 A ALA 84  ? A ALA 85  
86  1 Y 1 A SER 85  ? A SER 86  
87  1 Y 1 A SER 86  ? A SER 87  
88  1 Y 1 A ASP 87  ? A ASP 88  
89  1 Y 1 A PRO 88  ? A PRO 89  
90  1 Y 1 A PRO 89  ? A PRO 90  
91  1 Y 1 A ALA 90  ? A ALA 91  
92  1 Y 1 A LEU 91  ? A LEU 92  
93  1 Y 1 A ALA 92  ? A ALA 93  
94  1 Y 1 A SER 93  ? A SER 94  
95  1 Y 1 A LYS 94  ? A LYS 95  
96  1 Y 1 A ASN 95  ? A ASN 96  
97  1 Y 1 A ALA 96  ? A ALA 97  
98  1 Y 1 A GLU 97  ? A GLU 98  
99  1 Y 1 A VAL 98  ? A VAL 99  
100 1 Y 1 A THR 99  ? A THR 100 
101 1 Y 1 A GLY 100 ? A GLY 101 
102 1 Y 1 A THR 101 ? A THR 102 
103 1 Y 1 A MET 102 ? A MET 103 
104 1 Y 1 A SER 103 ? A SER 104 
105 1 Y 1 A GLN 104 ? A GLN 105 
106 1 Y 1 A ASP 105 ? A ASP 106 
107 1 Y 1 A THR 106 ? A THR 107 
108 1 Y 1 A GLU 107 ? A GLU 108 
109 1 Y 1 A VAL 108 ? A VAL 109 
110 1 Y 1 A ASP 109 ? A ASP 110 
111 1 Y 1 A MET 110 ? A MET 111 
112 1 Y 1 A LYS 111 ? A LYS 112 
113 1 Y 1 A GLU 112 ? A GLU 113 
114 1 Y 1 A VAL 113 ? A VAL 114 
115 1 Y 1 A GLU 114 ? A GLU 115 
116 1 Y 1 A LEU 115 ? A LEU 116 
117 1 Y 1 A ASN 116 ? A ASN 117 
118 1 Y 1 A GLU 117 ? A GLU 118 
119 1 Y 1 A LEU 118 ? A LEU 119 
120 1 Y 1 A GLU 119 ? A GLU 120 
121 1 Y 1 A PRO 120 ? A PRO 121 
122 1 Y 1 A GLU 121 ? A GLU 122 
123 1 Y 1 A LYS 122 ? A LYS 123 
124 1 Y 1 A GLN 123 ? A GLN 124 
125 1 Y 1 A PRO 124 ? A PRO 125 
126 1 Y 1 A MET 125 ? A MET 126 
127 1 Y 1 A ASN 126 ? A ASN 127 
128 1 Y 1 A ALA 127 ? A ALA 128 
129 1 Y 1 A ALA 128 ? A ALA 129 
130 1 Y 1 A SER 129 ? A SER 130 
131 1 Y 1 A GLY 130 ? A GLY 131 
132 1 Y 1 A ALA 131 ? A ALA 132 
133 1 Y 1 A ALA 132 ? A ALA 133 
134 1 Y 1 A MET 133 ? A MET 134 
135 1 Y 1 A SER 134 ? A SER 135 
136 1 Y 1 A LEU 135 ? A LEU 136 
137 1 Y 1 A ALA 136 ? A ALA 137 
138 1 Y 1 A GLY 137 ? A GLY 138 
139 1 Y 1 A ALA 138 ? A ALA 139 
140 1 Y 1 A GLU 139 ? A GLU 140 
141 1 Y 1 A LYS 140 ? A LYS 141 
142 1 Y 1 A ASN 141 ? A ASN 142 
143 1 Y 1 A GLY 142 ? A GLY 143 
144 1 Y 1 A LEU 143 ? A LEU 144 
145 1 Y 1 A VAL 144 ? A VAL 145 
146 1 Y 1 A LYS 145 ? A LYS 146 
147 1 Y 1 A ILE 146 ? A ILE 147 
148 1 Y 1 A LYS 147 ? A LYS 148 
149 1 Y 1 A VAL 148 ? A VAL 149 
150 1 Y 1 A ALA 149 ? A ALA 150 
151 1 Y 1 A GLU 150 ? A GLU 151 
152 1 Y 1 A ASP 151 ? A ASP 152 
153 1 Y 1 A GLU 152 ? A GLU 153 
154 1 Y 1 A ALA 153 ? A ALA 154 
155 1 Y 1 A GLU 154 ? A GLU 155 
156 1 Y 1 A ALA 155 ? A ALA 156 
157 1 Y 1 A ALA 156 ? A ALA 157 
158 1 Y 1 A ALA 157 ? A ALA 158 
159 1 Y 1 A ALA 158 ? A ALA 159 
160 1 Y 1 A ALA 159 ? A ALA 160 
161 1 Y 1 A LYS 160 ? A LYS 161 
162 1 Y 1 A PHE 161 ? A PHE 162 
163 1 Y 1 A PRO 214 ? A PRO 215 
164 1 Y 1 A ALA 215 ? A ALA 216 
165 1 Y 1 A GLN 216 ? A GLN 217 
166 1 Y 1 A LYS 217 ? A LYS 218 
167 1 Y 1 A TRP 218 ? A TRP 219 
168 1 Y 1 A TRP 219 ? A TRP 220 
169 1 Y 1 A HIS 220 ? A HIS 221 
170 1 Y 1 A THR 221 ? A THR 222 
171 1 Y 1 A GLY 222 ? A GLY 223 
172 1 Y 1 A ALA 223 ? A ALA 224 
173 1 Y 1 A LEU 224 ? A LEU 225 
174 1 Y 1 A TYR 225 ? A TYR 226 
175 1 Y 1 A ARG 226 ? A ARG 227 
176 1 Y 1 A ILE 227 ? A ILE 228 
177 1 Y 1 A GLY 228 ? A GLY 229 
178 1 Y 1 A ASP 229 ? A ASP 230 
179 1 Y 1 A LEU 230 ? A LEU 231 
180 1 Y 1 A GLN 231 ? A GLN 232 
181 1 Y 1 A ALA 232 ? A ALA 233 
182 1 Y 1 A PHE 233 ? A PHE 234 
183 1 Y 1 A GLN 234 ? A GLN 235 
184 1 Y 1 A GLY 235 ? A GLY 236 
185 1 Y 1 A HIS 236 ? A HIS 237 
186 1 Y 1 A GLY 237 ? A GLY 238 
187 1 Y 1 A ALA 238 ? A ALA 239 
188 1 Y 1 A GLY 239 ? A GLY 240 
189 1 Y 1 A ASN 240 ? A ASN 241 
190 1 Y 1 A LEU 241 ? A LEU 242 
191 1 Y 1 A ALA 242 ? A ALA 243 
192 1 Y 1 A GLY 243 ? A GLY 244 
193 1 Y 1 A LEU 244 ? A LEU 245 
194 1 Y 1 A LYS 245 ? A LYS 246 
195 1 Y 1 A GLY 246 ? A GLY 247 
196 1 Y 1 A ARG 247 ? A ARG 248 
197 1 Y 1 A LEU 248 ? A LEU 249 
198 1 Y 1 A ASP 249 ? A ASP 250 
199 1 Y 1 A TYR 250 ? A TYR 251 
200 1 Y 1 A LEU 251 ? A LEU 252 
201 1 Y 1 A SER 252 ? A SER 253 
202 1 Y 1 A SER 253 ? A SER 254 
203 1 Y 1 A LEU 254 ? A LEU 255 
204 1 Y 1 A LYS 255 ? A LYS 256 
205 1 Y 1 A VAL 256 ? A VAL 257 
206 1 Y 1 A LYS 257 ? A LYS 258 
207 1 Y 1 A GLY 258 ? A GLY 259 
208 1 Y 1 A LEU 259 ? A LEU 260 
209 1 Y 1 A VAL 260 ? A VAL 261 
210 1 Y 1 A LEU 261 ? A LEU 262 
211 1 Y 1 A GLY 262 ? A GLY 263 
212 1 Y 1 A PRO 263 ? A PRO 264 
213 1 Y 1 A ILE 264 ? A ILE 265 
214 1 Y 1 A HIS 265 ? A HIS 266 
215 1 Y 1 A LYS 266 ? A LYS 267 
216 1 Y 1 A ASN 267 ? A ASN 268 
217 1 Y 1 A GLN 268 ? A GLN 269 
218 1 Y 1 A LYS 269 ? A LYS 270 
219 1 Y 1 A ASP 270 ? A ASP 271 
220 1 Y 1 A ASP 271 ? A ASP 272 
221 1 Y 1 A VAL 272 ? A VAL 273 
222 1 Y 1 A ALA 273 ? A ALA 274 
223 1 Y 1 A GLN 274 ? A GLN 275 
224 1 Y 1 A THR 275 ? A THR 276 
225 1 Y 1 A ASP 276 ? A ASP 277 
226 1 Y 1 A LEU 277 ? A LEU 278 
227 1 Y 1 A LEU 278 ? A LEU 279 
228 1 Y 1 A GLN 279 ? A GLN 280 
229 1 Y 1 A ILE 280 ? A ILE 281 
230 1 Y 1 A ASP 281 ? A ASP 282 
231 1 Y 1 A PRO 282 ? A PRO 283 
232 1 Y 1 A ASN 283 ? A ASN 284 
233 1 Y 1 A PHE 284 ? A PHE 285 
234 1 Y 1 A GLY 285 ? A GLY 286 
235 1 Y 1 A SER 286 ? A SER 287 
236 1 Y 1 A LYS 287 ? A LYS 288 
237 1 Y 1 A GLU 288 ? A GLU 289 
238 1 Y 1 A ASP 289 ? A ASP 290 
239 1 Y 1 A PHE 290 ? A PHE 291 
240 1 Y 1 A ASP 291 ? A ASP 292 
241 1 Y 1 A SER 292 ? A SER 293 
242 1 Y 1 A LEU 293 ? A LEU 294 
243 1 Y 1 A LEU 294 ? A LEU 295 
244 1 Y 1 A GLN 295 ? A GLN 296 
245 1 Y 1 A SER 296 ? A SER 297 
246 1 Y 1 A ALA 297 ? A ALA 298 
247 1 Y 1 A LYS 298 ? A LYS 299 
248 1 Y 1 A LYS 299 ? A LYS 300 
249 1 Y 1 A LYS 300 ? A LYS 301 
250 1 Y 1 A SER 301 ? A SER 302 
251 1 Y 1 A ILE 302 ? A ILE 303 
252 1 Y 1 A ARG 303 ? A ARG 304 
253 1 Y 1 A VAL 304 ? A VAL 305 
254 1 Y 1 A ILE 305 ? A ILE 306 
255 1 Y 1 A LEU 306 ? A LEU 307 
256 1 Y 1 A ASP 307 ? A ASP 308 
257 1 Y 1 A LEU 308 ? A LEU 309 
258 1 Y 1 A THR 309 ? A THR 310 
259 1 Y 1 A PRO 310 ? A PRO 311 
260 1 Y 1 A ASN 311 ? A ASN 312 
261 1 Y 1 A TYR 312 ? A TYR 313 
262 1 Y 1 A ARG 313 ? A ARG 314 
263 1 Y 1 A GLY 314 ? A GLY 315 
264 1 Y 1 A GLU 315 ? A GLU 316 
265 1 Y 1 A ASN 316 ? A ASN 317 
266 1 Y 1 A SER 317 ? A SER 318 
267 1 Y 1 A TRP 318 ? A TRP 319 
268 1 Y 1 A PHE 319 ? A PHE 320 
269 1 Y 1 A SER 320 ? A SER 321 
270 1 Y 1 A THR 321 ? A THR 322 
271 1 Y 1 A GLN 322 ? A GLN 323 
272 1 Y 1 A VAL 323 ? A VAL 324 
273 1 Y 1 A ASP 324 ? A ASP 325 
274 1 Y 1 A THR 325 ? A THR 326 
275 1 Y 1 A VAL 326 ? A VAL 327 
276 1 Y 1 A ALA 327 ? A ALA 328 
277 1 Y 1 A THR 328 ? A THR 329 
278 1 Y 1 A LYS 329 ? A LYS 330 
279 1 Y 1 A VAL 330 ? A VAL 331 
280 1 Y 1 A LYS 331 ? A LYS 332 
281 1 Y 1 A ASP 332 ? A ASP 333 
282 1 Y 1 A ALA 333 ? A ALA 334 
283 1 Y 1 A LEU 334 ? A LEU 335 
284 1 Y 1 A GLU 335 ? A GLU 336 
285 1 Y 1 A PHE 336 ? A PHE 337 
286 1 Y 1 A TRP 337 ? A TRP 338 
287 1 Y 1 A LEU 338 ? A LEU 339 
288 1 Y 1 A GLN 339 ? A GLN 340 
289 1 Y 1 A ALA 340 ? A ALA 341 
290 1 Y 1 A GLY 341 ? A GLY 342 
291 1 Y 1 A VAL 342 ? A VAL 343 
292 1 Y 1 A ASP 343 ? A ASP 344 
293 1 Y 1 A GLY 344 ? A GLY 345 
294 1 Y 1 A PHE 345 ? A PHE 346 
295 1 Y 1 A GLN 346 ? A GLN 347 
296 1 Y 1 A VAL 347 ? A VAL 348 
297 1 Y 1 A ARG 348 ? A ARG 349 
298 1 Y 1 A ASP 349 ? A ASP 350 
299 1 Y 1 A ILE 350 ? A ILE 351 
300 1 Y 1 A GLU 351 ? A GLU 352 
301 1 Y 1 A ASN 352 ? A ASN 353 
302 1 Y 1 A LEU 353 ? A LEU 354 
303 1 Y 1 A LYS 354 ? A LYS 355 
304 1 Y 1 A ASP 355 ? A ASP 356 
305 1 Y 1 A ALA 356 ? A ALA 357 
306 1 Y 1 A SER 357 ? A SER 358 
307 1 Y 1 A SER 358 ? A SER 359 
308 1 Y 1 A PHE 359 ? A PHE 360 
309 1 Y 1 A LEU 360 ? A LEU 361 
310 1 Y 1 A ALA 361 ? A ALA 362 
311 1 Y 1 A GLU 362 ? A GLU 363 
312 1 Y 1 A TRP 363 ? A TRP 364 
313 1 Y 1 A GLN 364 ? A GLN 365 
314 1 Y 1 A ASN 365 ? A ASN 366 
315 1 Y 1 A ILE 366 ? A ILE 367 
316 1 Y 1 A THR 367 ? A THR 368 
317 1 Y 1 A LYS 368 ? A LYS 369 
318 1 Y 1 A GLY 369 ? A GLY 370 
319 1 Y 1 A PHE 370 ? A PHE 371 
320 1 Y 1 A SER 371 ? A SER 372 
321 1 Y 1 A GLU 372 ? A GLU 373 
322 1 Y 1 A ASP 373 ? A ASP 374 
323 1 Y 1 A ARG 374 ? A ARG 375 
324 1 Y 1 A LEU 375 ? A LEU 376 
325 1 Y 1 A LEU 376 ? A LEU 377 
326 1 Y 1 A ILE 377 ? A ILE 378 
327 1 Y 1 A ALA 378 ? A ALA 379 
328 1 Y 1 A GLY 379 ? A GLY 380 
329 1 Y 1 A THR 380 ? A THR 381 
330 1 Y 1 A ASN 381 ? A ASN 382 
331 1 Y 1 A SER 382 ? A SER 383 
332 1 Y 1 A SER 383 ? A SER 384 
333 1 Y 1 A ASP 384 ? A ASP 385 
334 1 Y 1 A LEU 385 ? A LEU 386 
335 1 Y 1 A GLN 386 ? A GLN 387 
336 1 Y 1 A GLN 387 ? A GLN 388 
337 1 Y 1 A ILE 388 ? A ILE 389 
338 1 Y 1 A LEU 389 ? A LEU 390 
339 1 Y 1 A SER 390 ? A SER 391 
340 1 Y 1 A LEU 391 ? A LEU 392 
341 1 Y 1 A LEU 392 ? A LEU 393 
342 1 Y 1 A GLU 393 ? A GLU 394 
343 1 Y 1 A SER 394 ? A SER 395 
344 1 Y 1 A ASN 395 ? A ASN 396 
345 1 Y 1 A LYS 396 ? A LYS 397 
346 1 Y 1 A ASP 397 ? A ASP 398 
347 1 Y 1 A LEU 398 ? A LEU 399 
348 1 Y 1 A LEU 399 ? A LEU 400 
349 1 Y 1 A LEU 400 ? A LEU 401 
350 1 Y 1 A THR 401 ? A THR 402 
351 1 Y 1 A SER 402 ? A SER 403 
352 1 Y 1 A SER 403 ? A SER 404 
353 1 Y 1 A TYR 404 ? A TYR 405 
354 1 Y 1 A LEU 405 ? A LEU 406 
355 1 Y 1 A SER 406 ? A SER 407 
356 1 Y 1 A ASP 407 ? A ASP 408 
357 1 Y 1 A SER 408 ? A SER 409 
358 1 Y 1 A GLY 409 ? A GLY 410 
359 1 Y 1 A SER 410 ? A SER 411 
360 1 Y 1 A THR 411 ? A THR 412 
361 1 Y 1 A GLY 412 ? A GLY 413 
362 1 Y 1 A GLU 413 ? A GLU 414 
363 1 Y 1 A HIS 414 ? A HIS 415 
364 1 Y 1 A THR 415 ? A THR 416 
365 1 Y 1 A LYS 416 ? A LYS 417 
366 1 Y 1 A SER 417 ? A SER 418 
367 1 Y 1 A LEU 418 ? A LEU 419 
368 1 Y 1 A VAL 419 ? A VAL 420 
369 1 Y 1 A THR 420 ? A THR 421 
370 1 Y 1 A GLN 421 ? A GLN 422 
371 1 Y 1 A TYR 422 ? A TYR 423 
372 1 Y 1 A LEU 423 ? A LEU 424 
373 1 Y 1 A ASN 424 ? A ASN 425 
374 1 Y 1 A ALA 425 ? A ALA 426 
375 1 Y 1 A THR 426 ? A THR 427 
376 1 Y 1 A GLY 427 ? A GLY 428 
377 1 Y 1 A ASN 428 ? A ASN 429 
378 1 Y 1 A ARG 429 ? A ARG 430 
379 1 Y 1 A TRP 430 ? A TRP 431 
380 1 Y 1 A CYS 431 ? A CYS 432 
381 1 Y 1 A SER 432 ? A SER 433 
382 1 Y 1 A TRP 433 ? A TRP 434 
383 1 Y 1 A SER 434 ? A SER 435 
384 1 Y 1 A LEU 435 ? A LEU 436 
385 1 Y 1 A SER 436 ? A SER 437 
386 1 Y 1 A GLN 437 ? A GLN 438 
387 1 Y 1 A ALA 438 ? A ALA 439 
388 1 Y 1 A ARG 439 ? A ARG 440 
389 1 Y 1 A LEU 440 ? A LEU 441 
390 1 Y 1 A LEU 441 ? A LEU 442 
391 1 Y 1 A THR 442 ? A THR 443 
392 1 Y 1 A SER 443 ? A SER 444 
393 1 Y 1 A PHE 444 ? A PHE 445 
394 1 Y 1 A LEU 445 ? A LEU 446 
395 1 Y 1 A PRO 446 ? A PRO 447 
396 1 Y 1 A ALA 447 ? A ALA 448 
397 1 Y 1 A GLN 448 ? A GLN 449 
398 1 Y 1 A LEU 449 ? A LEU 450 
399 1 Y 1 A LEU 450 ? A LEU 451 
400 1 Y 1 A ARG 451 ? A ARG 452 
401 1 Y 1 A LEU 452 ? A LEU 453 
402 1 Y 1 A TYR 453 ? A TYR 454 
403 1 Y 1 A GLN 454 ? A GLN 455 
404 1 Y 1 A LEU 455 ? A LEU 456 
405 1 Y 1 A MET 456 ? A MET 457 
406 1 Y 1 A LEU 457 ? A LEU 458 
407 1 Y 1 A PHE 458 ? A PHE 459 
408 1 Y 1 A THR 459 ? A THR 460 
409 1 Y 1 A LEU 460 ? A LEU 461 
410 1 Y 1 A PRO 461 ? A PRO 462 
411 1 Y 1 A GLY 462 ? A GLY 463 
412 1 Y 1 A THR 463 ? A THR 464 
413 1 Y 1 A PRO 464 ? A PRO 465 
414 1 Y 1 A VAL 465 ? A VAL 466 
415 1 Y 1 A PHE 466 ? A PHE 467 
416 1 Y 1 A SER 467 ? A SER 468 
417 1 Y 1 A TYR 468 ? A TYR 469 
418 1 Y 1 A GLY 469 ? A GLY 470 
419 1 Y 1 A ASP 470 ? A ASP 471 
420 1 Y 1 A GLU 471 ? A GLU 472 
421 1 Y 1 A ILE 472 ? A ILE 473 
422 1 Y 1 A GLY 473 ? A GLY 474 
423 1 Y 1 A LEU 474 ? A LEU 475 
424 1 Y 1 A ASP 475 ? A ASP 476 
425 1 Y 1 A ALA 476 ? A ALA 477 
426 1 Y 1 A ALA 477 ? A ALA 478 
427 1 Y 1 A ALA 478 ? A ALA 479 
428 1 Y 1 A LEU 479 ? A LEU 480 
429 1 Y 1 A PRO 480 ? A PRO 481 
430 1 Y 1 A GLY 481 ? A GLY 482 
431 1 Y 1 A GLN 482 ? A GLN 483 
432 1 Y 1 A PRO 483 ? A PRO 484 
433 1 Y 1 A MET 484 ? A MET 485 
434 1 Y 1 A GLU 485 ? A GLU 486 
435 1 Y 1 A ALA 486 ? A ALA 487 
436 1 Y 1 A PRO 487 ? A PRO 488 
437 1 Y 1 A VAL 488 ? A VAL 489 
438 1 Y 1 A MET 489 ? A MET 490 
439 1 Y 1 A LEU 490 ? A LEU 491 
440 1 Y 1 A TRP 491 ? A TRP 492 
441 1 Y 1 A ASP 492 ? A ASP 493 
442 1 Y 1 A GLU 493 ? A GLU 494 
443 1 Y 1 A SER 494 ? A SER 495 
444 1 Y 1 A SER 495 ? A SER 496 
445 1 Y 1 A PHE 496 ? A PHE 497 
446 1 Y 1 A PRO 497 ? A PRO 498 
447 1 Y 1 A ASP 498 ? A ASP 499 
448 1 Y 1 A ILE 499 ? A ILE 500 
449 1 Y 1 A PRO 500 ? A PRO 501 
450 1 Y 1 A GLY 501 ? A GLY 502 
451 1 Y 1 A ALA 502 ? A ALA 503 
452 1 Y 1 A VAL 503 ? A VAL 504 
453 1 Y 1 A SER 504 ? A SER 505 
454 1 Y 1 A ALA 505 ? A ALA 506 
455 1 Y 1 A ASN 506 ? A ASN 507 
456 1 Y 1 A MET 507 ? A MET 508 
457 1 Y 1 A THR 508 ? A THR 509 
458 1 Y 1 A VAL 509 ? A VAL 510 
459 1 Y 1 A LYS 510 ? A LYS 511 
460 1 Y 1 A GLY 511 ? A GLY 512 
461 1 Y 1 A GLN 512 ? A GLN 513 
462 1 Y 1 A SER 513 ? A SER 514 
463 1 Y 1 A GLU 514 ? A GLU 515 
464 1 Y 1 A ASP 515 ? A ASP 516 
465 1 Y 1 A PRO 516 ? A PRO 517 
466 1 Y 1 A GLY 517 ? A GLY 518 
467 1 Y 1 A SER 518 ? A SER 519 
468 1 Y 1 A LEU 519 ? A LEU 520 
469 1 Y 1 A LEU 520 ? A LEU 521 
470 1 Y 1 A SER 521 ? A SER 522 
471 1 Y 1 A LEU 522 ? A LEU 523 
472 1 Y 1 A PHE 523 ? A PHE 524 
473 1 Y 1 A ARG 524 ? A ARG 525 
474 1 Y 1 A ARG 525 ? A ARG 526 
475 1 Y 1 A LEU 526 ? A LEU 527 
476 1 Y 1 A SER 527 ? A SER 528 
477 1 Y 1 A ASP 528 ? A ASP 529 
478 1 Y 1 A GLN 529 ? A GLN 530 
479 1 Y 1 A ARG 530 ? A ARG 531 
480 1 Y 1 A SER 531 ? A SER 532 
481 1 Y 1 A LYS 532 ? A LYS 533 
482 1 Y 1 A GLU 533 ? A GLU 534 
483 1 Y 1 A ARG 534 ? A ARG 535 
484 1 Y 1 A SER 535 ? A SER 536 
485 1 Y 1 A LEU 536 ? A LEU 537 
486 1 Y 1 A LEU 537 ? A LEU 538 
487 1 Y 1 A HIS 538 ? A HIS 539 
488 1 Y 1 A GLY 539 ? A GLY 540 
489 1 Y 1 A ASP 540 ? A ASP 541 
490 1 Y 1 A PHE 541 ? A PHE 542 
491 1 Y 1 A HIS 542 ? A HIS 543 
492 1 Y 1 A ALA 543 ? A ALA 544 
493 1 Y 1 A PHE 544 ? A PHE 545 
494 1 Y 1 A SER 545 ? A SER 546 
495 1 Y 1 A ALA 546 ? A ALA 547 
496 1 Y 1 A GLY 547 ? A GLY 548 
497 1 Y 1 A PRO 548 ? A PRO 549 
498 1 Y 1 A GLY 549 ? A GLY 550 
499 1 Y 1 A LEU 550 ? A LEU 551 
500 1 Y 1 A PHE 551 ? A PHE 552 
501 1 Y 1 A SER 552 ? A SER 553 
502 1 Y 1 A TYR 553 ? A TYR 554 
503 1 Y 1 A ILE 554 ? A ILE 555 
504 1 Y 1 A ARG 555 ? A ARG 556 
505 1 Y 1 A HIS 556 ? A HIS 557 
506 1 Y 1 A TRP 557 ? A TRP 558 
507 1 Y 1 A ASP 558 ? A ASP 559 
508 1 Y 1 A GLN 559 ? A GLN 560 
509 1 Y 1 A ASN 560 ? A ASN 561 
510 1 Y 1 A GLU 561 ? A GLU 562 
511 1 Y 1 A ARG 562 ? A ARG 563 
512 1 Y 1 A PHE 563 ? A PHE 564 
513 1 Y 1 A LEU 564 ? A LEU 565 
514 1 Y 1 A VAL 565 ? A VAL 566 
515 1 Y 1 A VAL 566 ? A VAL 567 
516 1 Y 1 A LEU 567 ? A LEU 568 
517 1 Y 1 A ASN 568 ? A ASN 569 
518 1 Y 1 A PHE 569 ? A PHE 570 
519 1 Y 1 A GLY 570 ? A GLY 571 
520 1 Y 1 A ASP 571 ? A ASP 572 
521 1 Y 1 A VAL 572 ? A VAL 573 
522 1 Y 1 A GLY 573 ? A GLY 574 
523 1 Y 1 A LEU 574 ? A LEU 575 
524 1 Y 1 A SER 575 ? A SER 576 
525 1 Y 1 A ALA 576 ? A ALA 577 
526 1 Y 1 A GLY 577 ? A GLY 578 
527 1 Y 1 A LEU 578 ? A LEU 579 
528 1 Y 1 A GLN 579 ? A GLN 580 
529 1 Y 1 A ALA 580 ? A ALA 581 
530 1 Y 1 A SER 581 ? A SER 582 
531 1 Y 1 A ASP 582 ? A ASP 583 
532 1 Y 1 A LEU 583 ? A LEU 584 
533 1 Y 1 A PRO 584 ? A PRO 585 
534 1 Y 1 A ALA 585 ? A ALA 586 
535 1 Y 1 A SER 586 ? A SER 587 
536 1 Y 1 A ALA 587 ? A ALA 588 
537 1 Y 1 A SER 588 ? A SER 589 
538 1 Y 1 A LEU 589 ? A LEU 590 
539 1 Y 1 A PRO 590 ? A PRO 591 
540 1 Y 1 A ALA 591 ? A ALA 592 
541 1 Y 1 A LYS 592 ? A LYS 593 
542 1 Y 1 A ALA 593 ? A ALA 594 
543 1 Y 1 A ASP 594 ? A ASP 595 
544 1 Y 1 A LEU 595 ? A LEU 596 
545 1 Y 1 A LEU 596 ? A LEU 597 
546 1 Y 1 A LEU 597 ? A LEU 598 
547 1 Y 1 A SER 598 ? A SER 599 
548 1 Y 1 A THR 599 ? A THR 600 
549 1 Y 1 A GLN 600 ? A GLN 601 
550 1 Y 1 A PRO 601 ? A PRO 602 
551 1 Y 1 A GLY 602 ? A GLY 603 
552 1 Y 1 A ARG 603 ? A ARG 604 
553 1 Y 1 A GLU 604 ? A GLU 605 
554 1 Y 1 A GLU 605 ? A GLU 606 
555 1 Y 1 A GLY 606 ? A GLY 607 
556 1 Y 1 A SER 607 ? A SER 608 
557 1 Y 1 A PRO 608 ? A PRO 609 
558 1 Y 1 A LEU 609 ? A LEU 610 
559 1 Y 1 A GLU 610 ? A GLU 611 
560 1 Y 1 A LEU 611 ? A LEU 612 
561 1 Y 1 A GLU 612 ? A GLU 613 
562 1 Y 1 A ARG 613 ? A ARG 614 
563 1 Y 1 A LEU 614 ? A LEU 615 
564 1 Y 1 A LYS 615 ? A LYS 616 
565 1 Y 1 A LEU 616 ? A LEU 617 
566 1 Y 1 A GLU 617 ? A GLU 618 
567 1 Y 1 A PRO 618 ? A PRO 619 
568 1 Y 1 A HIS 619 ? A HIS 620 
569 1 Y 1 A GLU 620 ? A GLU 621 
570 1 Y 1 A GLY 621 ? A GLY 622 
571 1 Y 1 A LEU 622 ? A LEU 623 
572 1 Y 1 A LEU 623 ? A LEU 624 
573 1 Y 1 A LEU 624 ? A LEU 625 
574 1 Y 1 A ARG 625 ? A ARG 626 
575 1 Y 1 A PHE 626 ? A PHE 627 
576 1 Y 1 A PRO 627 ? A PRO 628 
577 1 Y 1 A TYR 628 ? A TYR 629 
578 1 Y 1 A ALA 629 ? A ALA 630 
579 1 Y 1 A ALA 630 ? A ALA 631 
580 1 Y 1 B MET 1   ? B MET 1   
581 1 Y 1 B ALA 2   ? B ALA 2   
582 1 Y 1 B GLY 3   ? B GLY 3   
583 1 Y 1 B ALA 4   ? B ALA 4   
584 1 Y 1 B GLY 5   ? B GLY 5   
585 1 Y 1 B PRO 6   ? B PRO 6   
586 1 Y 1 B LYS 7   ? B LYS 7   
587 1 Y 1 B ARG 8   ? B ARG 8   
588 1 Y 1 B ARG 9   ? B ARG 9   
589 1 Y 1 B ALA 10  ? B ALA 10  
590 1 Y 1 B LEU 11  ? B LEU 11  
591 1 Y 1 B ALA 12  ? B ALA 12  
592 1 Y 1 B ALA 13  ? B ALA 13  
593 1 Y 1 B PRO 14  ? B PRO 14  
594 1 Y 1 B ALA 15  ? B ALA 15  
595 1 Y 1 B ALA 16  ? B ALA 16  
596 1 Y 1 B GLU 17  ? B GLU 17  
597 1 Y 1 B GLU 18  ? B GLU 18  
598 1 Y 1 B LYS 19  ? B LYS 19  
599 1 Y 1 B GLU 20  ? B GLU 20  
600 1 Y 1 B GLU 21  ? B GLU 21  
601 1 Y 1 B ALA 22  ? B ALA 22  
602 1 Y 1 B ARG 23  ? B ARG 23  
603 1 Y 1 B GLU 24  ? B GLU 24  
604 1 Y 1 B LYS 25  ? B LYS 25  
605 1 Y 1 B MET 26  ? B MET 26  
606 1 Y 1 B LEU 27  ? B LEU 27  
607 1 Y 1 B ALA 28  ? B ALA 28  
608 1 Y 1 B ALA 29  ? B ALA 29  
609 1 Y 1 B LYS 30  ? B LYS 30  
610 1 Y 1 B SER 31  ? B SER 31  
611 1 Y 1 B ALA 32  ? B ALA 32  
612 1 Y 1 B ASP 33  ? B ASP 33  
613 1 Y 1 B GLY 34  ? B GLY 34  
614 1 Y 1 B SER 35  ? B SER 35  
615 1 Y 1 B ALA 36  ? B ALA 36  
616 1 Y 1 B PRO 37  ? B PRO 37  
617 1 Y 1 B ALA 38  ? B ALA 38  
618 1 Y 1 B GLY 39  ? B GLY 39  
619 1 Y 1 B GLU 40  ? B GLU 40  
620 1 Y 1 B GLY 41  ? B GLY 41  
621 1 Y 1 B GLU 42  ? B GLU 42  
622 1 Y 1 B GLY 43  ? B GLY 43  
623 1 Y 1 B ASP 223 ? B ASP 223 
624 1 Y 1 B VAL 224 ? B VAL 224 
625 1 Y 1 B SER 225 ? B SER 225 
626 1 Y 1 B ASN 226 ? B ASN 226 
627 1 Y 1 B LEU 227 ? B LEU 227 
628 1 Y 1 B ASP 228 ? B ASP 228 
629 1 Y 1 B PRO 229 ? B PRO 229 
630 1 Y 1 B ASN 230 ? B ASN 230 
631 1 Y 1 B PHE 231 ? B PHE 231 
632 1 Y 1 B SER 232 ? B SER 232 
633 1 Y 1 B ASP 508 ? B ASP 508 
634 1 Y 1 B TYR 509 ? B TYR 509 
635 1 Y 1 B LYS 510 ? B LYS 510 
636 1 Y 1 B ASP 511 ? B ASP 511 
637 1 Y 1 B ASP 512 ? B ASP 512 
638 1 Y 1 B ASP 513 ? B ASP 513 
639 1 Y 1 B ASP 514 ? B ASP 514 
640 1 Y 1 B LYS 515 ? B LYS 515 
# 
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  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
ILE N    N  N N 158 
ILE CA   C  N S 159 
ILE C    C  N N 160 
ILE O    O  N N 161 
ILE CB   C  N S 162 
ILE CG1  C  N N 163 
ILE CG2  C  N N 164 
ILE CD1  C  N N 165 
ILE OXT  O  N N 166 
ILE H    H  N N 167 
ILE H2   H  N N 168 
ILE HA   H  N N 169 
ILE HB   H  N N 170 
ILE HG12 H  N N 171 
ILE HG13 H  N N 172 
ILE HG21 H  N N 173 
ILE HG22 H  N N 174 
ILE HG23 H  N N 175 
ILE HD11 H  N N 176 
ILE HD12 H  N N 177 
ILE HD13 H  N N 178 
ILE HXT  H  N N 179 
LEU N    N  N N 180 
LEU CA   C  N S 181 
LEU C    C  N N 182 
LEU O    O  N N 183 
LEU CB   C  N N 184 
LEU CG   C  N N 185 
LEU CD1  C  N N 186 
LEU CD2  C  N N 187 
LEU OXT  O  N N 188 
LEU H    H  N N 189 
LEU H2   H  N N 190 
LEU HA   H  N N 191 
LEU HB2  H  N N 192 
LEU HB3  H  N N 193 
LEU HG   H  N N 194 
LEU HD11 H  N N 195 
LEU HD12 H  N N 196 
LEU HD13 H  N N 197 
LEU HD21 H  N N 198 
LEU HD22 H  N N 199 
LEU HD23 H  N N 200 
LEU HXT  H  N N 201 
LYS N    N  N N 202 
LYS CA   C  N S 203 
LYS C    C  N N 204 
LYS O    O  N N 205 
LYS CB   C  N N 206 
LYS CG   C  N N 207 
LYS CD   C  N N 208 
LYS CE   C  N N 209 
LYS NZ   N  N N 210 
LYS OXT  O  N N 211 
LYS H    H  N N 212 
LYS H2   H  N N 213 
LYS HA   H  N N 214 
LYS HB2  H  N N 215 
LYS HB3  H  N N 216 
LYS HG2  H  N N 217 
LYS HG3  H  N N 218 
LYS HD2  H  N N 219 
LYS HD3  H  N N 220 
LYS HE2  H  N N 221 
LYS HE3  H  N N 222 
LYS HZ1  H  N N 223 
LYS HZ2  H  N N 224 
LYS HZ3  H  N N 225 
LYS HXT  H  N N 226 
MET N    N  N N 227 
MET CA   C  N S 228 
MET C    C  N N 229 
MET O    O  N N 230 
MET CB   C  N N 231 
MET CG   C  N N 232 
MET SD   S  N N 233 
MET CE   C  N N 234 
MET OXT  O  N N 235 
MET H    H  N N 236 
MET H2   H  N N 237 
MET HA   H  N N 238 
MET HB2  H  N N 239 
MET HB3  H  N N 240 
MET HG2  H  N N 241 
MET HG3  H  N N 242 
MET HE1  H  N N 243 
MET HE2  H  N N 244 
MET HE3  H  N N 245 
MET HXT  H  N N 246 
PHE N    N  N N 247 
PHE CA   C  N S 248 
PHE C    C  N N 249 
PHE O    O  N N 250 
PHE CB   C  N N 251 
PHE CG   C  Y N 252 
PHE CD1  C  Y N 253 
PHE CD2  C  Y N 254 
PHE CE1  C  Y N 255 
PHE CE2  C  Y N 256 
PHE CZ   C  Y N 257 
PHE OXT  O  N N 258 
PHE H    H  N N 259 
PHE H2   H  N N 260 
PHE HA   H  N N 261 
PHE HB2  H  N N 262 
PHE HB3  H  N N 263 
PHE HD1  H  N N 264 
PHE HD2  H  N N 265 
PHE HE1  H  N N 266 
PHE HE2  H  N N 267 
PHE HZ   H  N N 268 
PHE HXT  H  N N 269 
PRO N    N  N N 270 
PRO CA   C  N S 271 
PRO C    C  N N 272 
PRO O    O  N N 273 
PRO CB   C  N N 274 
PRO CG   C  N N 275 
PRO CD   C  N N 276 
PRO OXT  O  N N 277 
PRO H    H  N N 278 
PRO HA   H  N N 279 
PRO HB2  H  N N 280 
PRO HB3  H  N N 281 
PRO HG2  H  N N 282 
PRO HG3  H  N N 283 
PRO HD2  H  N N 284 
PRO HD3  H  N N 285 
PRO HXT  H  N N 286 
SER N    N  N N 287 
SER CA   C  N S 288 
SER C    C  N N 289 
SER O    O  N N 290 
SER CB   C  N N 291 
SER OG   O  N N 292 
SER OXT  O  N N 293 
SER H    H  N N 294 
SER H2   H  N N 295 
SER HA   H  N N 296 
SER HB2  H  N N 297 
SER HB3  H  N N 298 
SER HG   H  N N 299 
SER HXT  H  N N 300 
THR N    N  N N 301 
THR CA   C  N S 302 
THR C    C  N N 303 
THR O    O  N N 304 
THR CB   C  N R 305 
THR OG1  O  N N 306 
THR CG2  C  N N 307 
THR OXT  O  N N 308 
THR H    H  N N 309 
THR H2   H  N N 310 
THR HA   H  N N 311 
THR HB   H  N N 312 
THR HG1  H  N N 313 
THR HG21 H  N N 314 
THR HG22 H  N N 315 
THR HG23 H  N N 316 
THR HXT  H  N N 317 
TRP N    N  N N 318 
TRP CA   C  N S 319 
TRP C    C  N N 320 
TRP O    O  N N 321 
TRP CB   C  N N 322 
TRP CG   C  Y N 323 
TRP CD1  C  Y N 324 
TRP CD2  C  Y N 325 
TRP NE1  N  Y N 326 
TRP CE2  C  Y N 327 
TRP CE3  C  Y N 328 
TRP CZ2  C  Y N 329 
TRP CZ3  C  Y N 330 
TRP CH2  C  Y N 331 
TRP OXT  O  N N 332 
TRP H    H  N N 333 
TRP H2   H  N N 334 
TRP HA   H  N N 335 
TRP HB2  H  N N 336 
TRP HB3  H  N N 337 
TRP HD1  H  N N 338 
TRP HE1  H  N N 339 
TRP HE3  H  N N 340 
TRP HZ2  H  N N 341 
TRP HZ3  H  N N 342 
TRP HH2  H  N N 343 
TRP HXT  H  N N 344 
TYR N    N  N N 345 
TYR CA   C  N S 346 
TYR C    C  N N 347 
TYR O    O  N N 348 
TYR CB   C  N N 349 
TYR CG   C  Y N 350 
TYR CD1  C  Y N 351 
TYR CD2  C  Y N 352 
TYR CE1  C  Y N 353 
TYR CE2  C  Y N 354 
TYR CZ   C  Y N 355 
TYR OH   O  N N 356 
TYR OXT  O  N N 357 
TYR H    H  N N 358 
TYR H2   H  N N 359 
TYR HA   H  N N 360 
TYR HB2  H  N N 361 
TYR HB3  H  N N 362 
TYR HD1  H  N N 363 
TYR HD2  H  N N 364 
TYR HE1  H  N N 365 
TYR HE2  H  N N 366 
TYR HH   H  N N 367 
TYR HXT  H  N N 368 
VAL N    N  N N 369 
VAL CA   C  N S 370 
VAL C    C  N N 371 
VAL O    O  N N 372 
VAL CB   C  N N 373 
VAL CG1  C  N N 374 
VAL CG2  C  N N 375 
VAL OXT  O  N N 376 
VAL H    H  N N 377 
VAL H2   H  N N 378 
VAL HA   H  N N 379 
VAL HB   H  N N 380 
VAL HG11 H  N N 381 
VAL HG12 H  N N 382 
VAL HG13 H  N N 383 
VAL HG21 H  N N 384 
VAL HG22 H  N N 385 
VAL HG23 H  N N 386 
VAL HXT  H  N N 387 
VUC C1   C  Y N 388 
VUC O1   O  N N 389 
VUC O2   O  N N 390 
VUC C2   C  Y N 391 
VUC C3   C  Y N 392 
VUC C4   C  Y N 393 
VUC C5   C  Y N 394 
VUC C6   C  Y N 395 
VUC C7   C  N N 396 
VUC C8   C  N S 397 
VUC C9   C  N N 398 
VUC C10  C  N N 399 
VUC C11  C  N N 400 
VUC C12  C  N N 401 
VUC C13  C  N N 402 
VUC N1   N  N N 403 
VUC N2   N  N N 404 
VUC CL1  CL N N 405 
VUC CL2  CL N N 406 
VUC H1   H  N N 407 
VUC H2   H  N N 408 
VUC H3   H  N N 409 
VUC H4   H  N N 410 
VUC H5   H  N N 411 
VUC H6   H  N N 412 
VUC H7   H  N N 413 
VUC H8   H  N N 414 
VUC H9   H  N N 415 
VUC H10  H  N N 416 
VUC H11  H  N N 417 
VUC H12  H  N N 418 
VUC H13  H  N N 419 
VUC H14  H  N N 420 
VUC H15  H  N N 421 
VUC H16  H  N N 422 
VUC H17  H  N N 423 
VUC H18  H  N N 424 
# 
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  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
VUC CL1 C11  sing N N 374 
VUC C11 C10  sing N N 375 
VUC C10 N2   sing N N 376 
VUC N2  C12  sing N N 377 
VUC N2  C3   sing N N 378 
VUC C12 C13  sing N N 379 
VUC C3  C2   doub Y N 380 
VUC C3  C4   sing Y N 381 
VUC C2  C1   sing Y N 382 
VUC C4  C5   doub Y N 383 
VUC N1  C8   sing N N 384 
VUC C1  C6   doub Y N 385 
VUC C5  C6   sing Y N 386 
VUC C13 CL2  sing N N 387 
VUC C6  C7   sing N N 388 
VUC C8  C7   sing N N 389 
VUC C8  C9   sing N N 390 
VUC C9  O2   doub N N 391 
VUC C9  O1   sing N N 392 
VUC C1  H1   sing N N 393 
VUC O1  H2   sing N N 394 
VUC C2  H3   sing N N 395 
VUC C4  H4   sing N N 396 
VUC C5  H5   sing N N 397 
VUC C7  H6   sing N N 398 
VUC C7  H7   sing N N 399 
VUC C8  H8   sing N N 400 
VUC C10 H9   sing N N 401 
VUC C10 H10  sing N N 402 
VUC C11 H11  sing N N 403 
VUC C11 H12  sing N N 404 
VUC C12 H13  sing N N 405 
VUC C12 H14  sing N N 406 
VUC C13 H15  sing N N 407 
VUC C13 H16  sing N N 408 
VUC N1  H17  sing N N 409 
VUC N1  H18  sing N N 410 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-08-09 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8KDO 
_em_admin.last_update        2025-02-26 
_em_admin.map_release_date   2025-02-12 
_em_admin.title              'Structure of LAT1-CD98hc in complex with melphalan, focused on TMD' 
# 
_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                MEGADALTONS 
_em_entity_assembly_molwt.value                0.173 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_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         51 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (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 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'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           ? 
_em_specimen.details                 ? 
_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 
# 
_pdbx_audit_support.funding_organization   'Max Planck Society' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8KDO 
_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  
CL 
N  
O  
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   . THR A 1 163 ? 73.762  90.524  31.986 1.00 274.61 ? 162 THR A N   1 
ATOM   2    C  CA  . THR A 1 163 ? 74.488  89.335  31.454 1.00 322.79 ? 162 THR A CA  1 
ATOM   3    C  C   . THR A 1 163 ? 75.973  89.676  31.315 1.00 264.36 ? 162 THR A C   1 
ATOM   4    O  O   . THR A 1 163 ? 76.341  90.839  31.191 1.00 213.09 ? 162 THR A O   1 
ATOM   5    C  CB  . THR A 1 163 ? 73.858  88.846  30.139 1.00 352.49 ? 162 THR A CB  1 
ATOM   6    O  OG1 . THR A 1 163 ? 72.459  88.703  30.379 1.00 393.54 ? 162 THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 163 ? 74.393  87.527  29.619 1.00 273.20 ? 162 THR A CG2 1 
ATOM   8    N  N   . GLY A 1 164 ? 76.819  88.640  31.341 1.00 256.14 ? 163 GLY A N   1 
ATOM   9    C  CA  . GLY A 1 164 ? 78.269  88.790  31.330 1.00 239.45 ? 163 GLY A CA  1 
ATOM   10   C  C   . GLY A 1 164 ? 78.907  88.547  29.959 1.00 262.63 ? 163 GLY A C   1 
ATOM   11   O  O   . GLY A 1 164 ? 78.237  88.571  28.915 1.00 214.11 ? 163 GLY A O   1 
ATOM   12   N  N   . LEU A 1 165 ? 80.232  88.299  30.000 1.00 258.23 ? 164 LEU A N   1 
ATOM   13   C  CA  . LEU A 1 165 ? 81.109  88.327  28.832 1.00 260.59 ? 164 LEU A CA  1 
ATOM   14   C  C   . LEU A 1 165 ? 80.882  87.116  27.913 1.00 256.92 ? 164 LEU A C   1 
ATOM   15   O  O   . LEU A 1 165 ? 80.522  86.026  28.346 1.00 272.90 ? 164 LEU A O   1 
ATOM   16   C  CB  . LEU A 1 165 ? 82.565  88.379  29.322 1.00 238.58 ? 164 LEU A CB  1 
ATOM   17   C  CG  . LEU A 1 165 ? 83.617  88.879  28.333 1.00 262.49 ? 164 LEU A CG  1 
ATOM   18   C  CD1 . LEU A 1 165 ? 83.391  90.347  28.003 1.00 301.36 ? 164 LEU A CD1 1 
ATOM   19   C  CD2 . LEU A 1 165 ? 85.021  88.677  28.886 1.00 241.02 ? 164 LEU A CD2 1 
ATOM   20   N  N   . SER A 1 166 ? 81.113  87.331  26.610 1.00 303.82 ? 165 SER A N   1 
ATOM   21   C  CA  . SER A 1 166 ? 81.107  86.284  25.593 1.00 327.08 ? 165 SER A CA  1 
ATOM   22   C  C   . SER A 1 166 ? 82.221  85.244  25.819 1.00 292.36 ? 165 SER A C   1 
ATOM   23   O  O   . SER A 1 166 ? 83.303  85.575  26.324 1.00 172.65 ? 165 SER A O   1 
ATOM   24   C  CB  . SER A 1 166 ? 81.175  86.947  24.214 1.00 356.49 ? 165 SER A CB  1 
ATOM   25   O  OG  . SER A 1 166 ? 81.953  86.217  23.290 1.00 369.00 ? 165 SER A OG  1 
ATOM   26   N  N   . LYS A 1 167 ? 81.955  83.984  25.406 1.00 267.37 ? 166 LYS A N   1 
ATOM   27   C  CA  . LYS A 1 167 ? 82.950  82.912  25.329 1.00 237.68 ? 166 LYS A CA  1 
ATOM   28   C  C   . LYS A 1 167 ? 84.116  83.285  24.397 1.00 273.34 ? 166 LYS A C   1 
ATOM   29   O  O   . LYS A 1 167 ? 85.259  83.330  24.828 1.00 213.16 ? 166 LYS A O   1 
ATOM   30   C  CB  . LYS A 1 167 ? 82.289  81.609  24.855 1.00 196.98 ? 166 LYS A CB  1 
ATOM   31   C  CG  . LYS A 1 167 ? 83.245  80.416  24.630 1.00 175.96 ? 166 LYS A CG  1 
ATOM   32   C  CD  . LYS A 1 167 ? 82.586  79.221  23.990 1.00 276.44 ? 166 LYS A CD  1 
ATOM   33   C  CE  . LYS A 1 167 ? 82.084  79.484  22.578 1.00 415.36 ? 166 LYS A CE  1 
ATOM   34   N  NZ  . LYS A 1 167 ? 81.479  78.279  21.953 1.00 449.06 ? 166 LYS A NZ  1 
ATOM   35   N  N   . GLU A 1 168 ? 83.826  83.556  23.117 1.00 325.13 ? 167 GLU A N   1 
ATOM   36   C  CA  . GLU A 1 168 ? 84.842  83.866  22.109 1.00 314.81 ? 167 GLU A CA  1 
ATOM   37   C  C   . GLU A 1 168 ? 85.531  85.217  22.370 1.00 306.08 ? 167 GLU A C   1 
ATOM   38   O  O   . GLU A 1 168 ? 86.674  85.397  21.929 1.00 360.19 ? 167 GLU A O   1 
ATOM   39   C  CB  . GLU A 1 168 ? 84.279  83.783  20.678 1.00 328.87 ? 167 GLU A CB  1 
ATOM   40   C  CG  . GLU A 1 168 ? 83.121  84.720  20.336 1.00 322.45 ? 167 GLU A CG  1 
ATOM   41   C  CD  . GLU A 1 168 ? 81.774  84.376  20.953 1.00 377.67 ? 167 GLU A CD  1 
ATOM   42   O  OE1 . GLU A 1 168 ? 81.577  83.199  21.356 1.00 438.65 ? 167 GLU A OE1 1 
ATOM   43   O  OE2 . GLU A 1 168 ? 80.928  85.290  21.060 1.00 408.07 ? 167 GLU A OE2 1 
ATOM   44   N  N   . GLU A 1 169 ? 84.876  86.157  23.081 1.00 280.76 ? 168 GLU A N   1 
ATOM   45   C  CA  . GLU A 1 169 ? 85.532  87.365  23.572 1.00 314.19 ? 168 GLU A CA  1 
ATOM   46   C  C   . GLU A 1 169 ? 86.565  86.997  24.643 1.00 284.34 ? 168 GLU A C   1 
ATOM   47   O  O   . GLU A 1 169 ? 87.710  87.464  24.602 1.00 351.87 ? 168 GLU A O   1 
ATOM   48   C  CB  . GLU A 1 169 ? 84.490  88.363  24.093 1.00 365.33 ? 168 GLU A CB  1 
ATOM   49   C  CG  . GLU A 1 169 ? 85.072  89.657  24.668 1.00 432.24 ? 168 GLU A CG  1 
ATOM   50   C  CD  . GLU A 1 169 ? 85.916  90.506  23.727 1.00 458.42 ? 168 GLU A CD  1 
ATOM   51   O  OE1 . GLU A 1 169 ? 85.685  90.452  22.496 1.00 480.70 ? 168 GLU A OE1 1 
ATOM   52   O  OE2 . GLU A 1 169 ? 86.810  91.227  24.228 1.00 430.75 ? 168 GLU A OE2 1 
ATOM   53   N  N   . LEU A 1 170 ? 86.169  86.155  25.609 1.00 255.06 ? 169 LEU A N   1 
ATOM   54   C  CA  . LEU A 1 170 ? 87.061  85.741  26.685 1.00 283.11 ? 169 LEU A CA  1 
ATOM   55   C  C   . LEU A 1 170 ? 88.315  85.051  26.128 1.00 289.21 ? 169 LEU A C   1 
ATOM   56   O  O   . LEU A 1 170 ? 89.380  85.219  26.704 1.00 290.12 ? 169 LEU A O   1 
ATOM   57   C  CB  . LEU A 1 170 ? 86.269  84.876  27.672 1.00 266.59 ? 169 LEU A CB  1 
ATOM   58   C  CG  . LEU A 1 170 ? 87.080  84.241  28.795 1.00 298.11 ? 169 LEU A CG  1 
ATOM   59   C  CD1 . LEU A 1 170 ? 86.271  84.251  30.075 1.00 309.50 ? 169 LEU A CD1 1 
ATOM   60   C  CD2 . LEU A 1 170 ? 87.489  82.806  28.460 1.00 361.15 ? 169 LEU A CD2 1 
ATOM   61   N  N   . LEU A 1 171 ? 88.233  84.307  25.013 1.00 237.63 ? 170 LEU A N   1 
ATOM   62   C  CA  . LEU A 1 171 ? 89.411  83.684  24.402 1.00 328.81 ? 170 LEU A CA  1 
ATOM   63   C  C   . LEU A 1 171 ? 90.520  84.693  24.057 1.00 378.00 ? 170 LEU A C   1 
ATOM   64   O  O   . LEU A 1 171 ? 91.692  84.299  24.012 1.00 362.96 ? 170 LEU A O   1 
ATOM   65   C  CB  . LEU A 1 171 ? 89.007  82.923  23.130 1.00 360.53 ? 170 LEU A CB  1 
ATOM   66   C  CG  . LEU A 1 171 ? 88.063  81.730  23.298 1.00 402.39 ? 170 LEU A CG  1 
ATOM   67   C  CD1 . LEU A 1 171 ? 87.800  81.082  21.945 1.00 420.03 ? 170 LEU A CD1 1 
ATOM   68   C  CD2 . LEU A 1 171 ? 88.593  80.697  24.296 1.00 388.24 ? 170 LEU A CD2 1 
ATOM   69   N  N   . LYS A 1 172 ? 90.170  85.972  23.815 1.00 410.57 ? 171 LYS A N   1 
ATOM   70   C  CA  . LYS A 1 172 ? 91.137  87.008  23.455 1.00 409.80 ? 171 LYS A CA  1 
ATOM   71   C  C   . LYS A 1 172 ? 91.988  87.465  24.650 1.00 363.19 ? 171 LYS A C   1 
ATOM   72   O  O   . LYS A 1 172 ? 93.114  87.925  24.449 1.00 349.10 ? 171 LYS A O   1 
ATOM   73   C  CB  . LYS A 1 172 ? 90.412  88.216  22.844 1.00 426.30 ? 171 LYS A CB  1 
ATOM   74   C  CG  . LYS A 1 172 ? 89.449  87.916  21.696 1.00 403.02 ? 171 LYS A CG  1 
ATOM   75   C  CD  . LYS A 1 172 ? 90.070  87.196  20.515 1.00 365.40 ? 171 LYS A CD  1 
ATOM   76   C  CE  . LYS A 1 172 ? 89.121  87.057  19.341 1.00 326.77 ? 171 LYS A CE  1 
ATOM   77   N  NZ  . LYS A 1 172 ? 88.143  85.962  19.529 1.00 352.91 ? 171 LYS A NZ  1 
ATOM   78   N  N   . VAL A 1 173 ? 91.456  87.352  25.884 1.00 343.67 ? 172 VAL A N   1 
ATOM   79   C  CA  . VAL A 1 173 ? 92.108  87.814  27.111 1.00 331.71 ? 172 VAL A CA  1 
ATOM   80   C  C   . VAL A 1 173 ? 92.652  86.647  27.939 1.00 286.28 ? 172 VAL A C   1 
ATOM   81   O  O   . VAL A 1 173 ? 93.761  86.742  28.460 1.00 275.79 ? 172 VAL A O   1 
ATOM   82   C  CB  . VAL A 1 173 ? 91.142  88.681  27.951 1.00 282.62 ? 172 VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 173 ? 91.729  89.107  29.298 1.00 242.51 ? 172 VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 173 ? 90.666  89.901  27.168 1.00 275.72 ? 172 VAL A CG2 1 
ATOM   85   N  N   . ALA A 1 174 ? 91.888  85.554  28.063 1.00 308.07 ? 173 ALA A N   1 
ATOM   86   C  CA  . ALA A 1 174 ? 92.100  84.548  29.097 1.00 369.21 ? 173 ALA A CA  1 
ATOM   87   C  C   . ALA A 1 174 ? 93.419  83.772  28.948 1.00 373.83 ? 173 ALA A C   1 
ATOM   88   O  O   . ALA A 1 174 ? 93.903  83.227  29.952 1.00 393.34 ? 173 ALA A O   1 
ATOM   89   C  CB  . ALA A 1 174 ? 90.909  83.611  29.114 1.00 386.87 ? 173 ALA A CB  1 
ATOM   90   N  N   . GLY A 1 175 ? 93.987  83.722  27.723 1.00 311.60 ? 174 GLY A N   1 
ATOM   91   C  CA  . GLY A 1 175 ? 95.276  83.095  27.455 1.00 323.95 ? 174 GLY A CA  1 
ATOM   92   C  C   . GLY A 1 175 ? 96.501  83.999  27.655 1.00 351.83 ? 174 GLY A C   1 
ATOM   93   O  O   . GLY A 1 175 ? 97.625  83.524  27.453 1.00 356.75 ? 174 GLY A O   1 
ATOM   94   N  N   . SER A 1 176 ? 96.315  85.279  28.043 1.00 306.45 ? 175 SER A N   1 
ATOM   95   C  CA  . SER A 1 176 ? 97.419  86.201  28.306 1.00 296.90 ? 175 SER A CA  1 
ATOM   96   C  C   . SER A 1 176 ? 98.314  85.678  29.433 1.00 303.23 ? 175 SER A C   1 
ATOM   97   O  O   . SER A 1 176 ? 97.790  85.267  30.464 1.00 382.08 ? 175 SER A O   1 
ATOM   98   C  CB  . SER A 1 176 ? 96.913  87.587  28.630 1.00 269.26 ? 175 SER A CB  1 
ATOM   99   O  OG  . SER A 1 176 ? 97.960  88.456  29.053 1.00 210.77 ? 175 SER A OG  1 
ATOM   100  N  N   . PRO A 1 177 ? 99.666  85.659  29.286 1.00 319.67 ? 176 PRO A N   1 
ATOM   101  C  CA  . PRO A 1 177 ? 100.569 85.163  30.332 1.00 333.27 ? 176 PRO A CA  1 
ATOM   102  C  C   . PRO A 1 177 ? 100.322 85.721  31.736 1.00 359.73 ? 176 PRO A C   1 
ATOM   103  O  O   . PRO A 1 177 ? 100.437 84.953  32.683 1.00 387.61 ? 176 PRO A O   1 
ATOM   104  C  CB  . PRO A 1 177 ? 101.970 85.545  29.822 1.00 364.43 ? 176 PRO A CB  1 
ATOM   105  C  CG  . PRO A 1 177 ? 101.807 85.526  28.327 1.00 381.68 ? 176 PRO A CG  1 
ATOM   106  C  CD  . PRO A 1 177 ? 100.414 86.076  28.093 1.00 378.50 ? 176 PRO A CD  1 
ATOM   107  N  N   . GLY A 1 178 ? 99.966  87.013  31.870 1.00 307.15 ? 177 GLY A N   1 
ATOM   108  C  CA  . GLY A 1 178 ? 99.598  87.615  33.149 1.00 311.72 ? 177 GLY A CA  1 
ATOM   109  C  C   . GLY A 1 178 ? 98.501  86.842  33.891 1.00 278.09 ? 177 GLY A C   1 
ATOM   110  O  O   . GLY A 1 178 ? 98.645  86.504  35.069 1.00 186.85 ? 177 GLY A O   1 
ATOM   111  N  N   . TRP A 1 179 ? 97.400  86.554  33.187 1.00 261.95 ? 178 TRP A N   1 
ATOM   112  C  CA  . TRP A 1 179 ? 96.293  85.790  33.747 1.00 218.34 ? 178 TRP A CA  1 
ATOM   113  C  C   . TRP A 1 179 ? 96.656  84.314  33.970 1.00 191.58 ? 178 TRP A C   1 
ATOM   114  O  O   . TRP A 1 179 ? 96.248  83.760  34.987 1.00 309.99 ? 178 TRP A O   1 
ATOM   115  C  CB  . TRP A 1 179 ? 95.046  85.943  32.872 1.00 254.55 ? 178 TRP A CB  1 
ATOM   116  C  CG  . TRP A 1 179 ? 94.425  87.317  32.895 1.00 250.68 ? 178 TRP A CG  1 
ATOM   117  C  CD1 . TRP A 1 179 ? 94.386  88.165  31.836 1.00 297.28 ? 178 TRP A CD1 1 
ATOM   118  C  CD2 . TRP A 1 179 ? 93.747  88.009  33.976 1.00 245.76 ? 178 TRP A CD2 1 
ATOM   119  N  NE1 . TRP A 1 179 ? 93.743  89.328  32.169 1.00 305.74 ? 178 TRP A NE1 1 
ATOM   120  C  CE2 . TRP A 1 179 ? 93.334  89.268  33.479 1.00 252.76 ? 178 TRP A CE2 1 
ATOM   121  C  CE3 . TRP A 1 179 ? 93.444  87.698  35.308 1.00 369.24 ? 178 TRP A CE3 1 
ATOM   122  C  CZ2 . TRP A 1 179 ? 92.642  90.203  34.263 1.00 255.39 ? 178 TRP A CZ2 1 
ATOM   123  C  CZ3 . TRP A 1 179 ? 92.760  88.619  36.084 1.00 411.09 ? 178 TRP A CZ3 1 
ATOM   124  C  CH2 . TRP A 1 179 ? 92.363  89.856  35.566 1.00 304.99 ? 178 TRP A CH2 1 
ATOM   125  N  N   . VAL A 1 180 ? 97.419  83.662  33.080 1.00 161.12 ? 179 VAL A N   1 
ATOM   126  C  CA  . VAL A 1 180 ? 97.842  82.268  33.277 1.00 199.21 ? 179 VAL A CA  1 
ATOM   127  C  C   . VAL A 1 180 ? 98.772  82.147  34.497 1.00 224.72 ? 179 VAL A C   1 
ATOM   128  O  O   . VAL A 1 180 ? 98.598  81.224  35.305 1.00 301.72 ? 179 VAL A O   1 
ATOM   129  C  CB  . VAL A 1 180 ? 98.503  81.679  32.015 1.00 318.97 ? 179 VAL A CB  1 
ATOM   130  C  CG1 . VAL A 1 180 ? 99.056  80.268  32.239 1.00 294.04 ? 179 VAL A CG1 1 
ATOM   131  C  CG2 . VAL A 1 180 ? 97.537  81.687  30.837 1.00 397.02 ? 179 VAL A CG2 1 
ATOM   132  N  N   . ARG A 1 181 ? 99.724  83.085  34.649 1.00 194.93 ? 180 ARG A N   1 
ATOM   133  C  CA  . ARG A 1 181 ? 100.554 83.185  35.841 1.00 243.54 ? 180 ARG A CA  1 
ATOM   134  C  C   . ARG A 1 181 ? 99.701  83.438  37.093 1.00 238.80 ? 180 ARG A C   1 
ATOM   135  O  O   . ARG A 1 181 ? 99.966  82.845  38.139 1.00 202.48 ? 180 ARG A O   1 
ATOM   136  C  CB  . ARG A 1 181 ? 101.613 84.278  35.641 1.00 342.59 ? 180 ARG A CB  1 
ATOM   137  C  CG  . ARG A 1 181 ? 102.709 83.913  34.649 1.00 382.22 ? 180 ARG A CG  1 
ATOM   138  C  CD  . ARG A 1 181 ? 103.555 85.109  34.226 1.00 381.18 ? 180 ARG A CD  1 
ATOM   139  N  NE  . ARG A 1 181 ? 104.371 85.700  35.299 1.00 391.92 ? 180 ARG A NE  1 
ATOM   140  C  CZ  . ARG A 1 181 ? 105.572 85.274  35.727 1.00 351.68 ? 180 ARG A CZ  1 
ATOM   141  N  NH1 . ARG A 1 181 ? 106.160 85.860  36.762 1.00 255.88 ? 180 ARG A NH1 1 
ATOM   142  N  NH2 . ARG A 1 181 ? 106.190 84.264  35.133 1.00 345.85 ? 180 ARG A NH2 1 
ATOM   143  N  N   . THR A 1 182 ? 98.676  84.304  37.003 1.00 233.93 ? 181 THR A N   1 
ATOM   144  C  CA  . THR A 1 182 ? 97.740  84.562  38.099 1.00 258.23 ? 181 THR A CA  1 
ATOM   145  C  C   . THR A 1 182 ? 97.034  83.273  38.553 1.00 155.33 ? 181 THR A C   1 
ATOM   146  O  O   . THR A 1 182 ? 97.004  82.959  39.726 1.00 149.97 ? 181 THR A O   1 
ATOM   147  C  CB  . THR A 1 182 ? 96.724  85.668  37.742 1.00 246.02 ? 181 THR A CB  1 
ATOM   148  O  OG1 . THR A 1 182 ? 97.424  86.874  37.437 1.00 267.86 ? 181 THR A OG1 1 
ATOM   149  C  CG2 . THR A 1 182 ? 95.739  85.982  38.846 1.00 259.43 ? 181 THR A CG2 1 
ATOM   150  N  N   . ARG A 1 183 ? 96.452  82.507  37.644 1.00 169.91 ? 182 ARG A N   1 
ATOM   151  C  CA  . ARG A 1 183 ? 95.829  81.240  37.998 1.00 195.62 ? 182 ARG A CA  1 
ATOM   152  C  C   . ARG A 1 183 ? 96.839  80.251  38.587 1.00 157.37 ? 182 ARG A C   1 
ATOM   153  O  O   . ARG A 1 183 ? 96.489  79.590  39.578 1.00 326.10 ? 182 ARG A O   1 
ATOM   154  C  CB  . ARG A 1 183 ? 95.094  80.638  36.796 1.00 244.41 ? 182 ARG A CB  1 
ATOM   155  C  CG  . ARG A 1 183 ? 93.869  81.462  36.410 1.00 228.90 ? 182 ARG A CG  1 
ATOM   156  C  CD  . ARG A 1 183 ? 93.139  80.837  35.227 1.00 273.02 ? 182 ARG A CD  1 
ATOM   157  N  NE  . ARG A 1 183 ? 92.560  81.865  34.363 1.00 254.29 ? 182 ARG A NE  1 
ATOM   158  C  CZ  . ARG A 1 183 ? 92.948  82.161  33.117 1.00 270.24 ? 182 ARG A CZ  1 
ATOM   159  N  NH1 . ARG A 1 183 ? 92.471  83.251  32.546 1.00 273.65 ? 182 ARG A NH1 1 
ATOM   160  N  NH2 . ARG A 1 183 ? 93.817  81.416  32.440 1.00 257.79 ? 182 ARG A NH2 1 
ATOM   161  N  N   . TRP A 1 184 ? 98.044  80.129  38.025 1.00 159.90 ? 183 TRP A N   1 
ATOM   162  C  CA  . TRP A 1 184 ? 99.079  79.265  38.580 1.00 200.32 ? 183 TRP A CA  1 
ATOM   163  C  C   . TRP A 1 184 ? 99.395  79.646  40.023 1.00 196.09 ? 183 TRP A C   1 
ATOM   164  O  O   . TRP A 1 184 ? 99.480  78.772  40.884 1.00 239.39 ? 183 TRP A O   1 
ATOM   165  C  CB  . TRP A 1 184 ? 100.347 79.339  37.723 1.00 288.55 ? 183 TRP A CB  1 
ATOM   166  C  CG  . TRP A 1 184 ? 101.523 78.612  38.319 1.00 314.62 ? 183 TRP A CG  1 
ATOM   167  C  CD1 . TRP A 1 184 ? 102.547 79.173  39.026 1.00 254.40 ? 183 TRP A CD1 1 
ATOM   168  C  CD2 . TRP A 1 184 ? 101.798 77.188  38.257 1.00 345.89 ? 183 TRP A CD2 1 
ATOM   169  N  NE1 . TRP A 1 184 ? 103.439 78.203  39.403 1.00 267.80 ? 183 TRP A NE1 1 
ATOM   170  C  CE2 . TRP A 1 184 ? 103.016 76.974  38.949 1.00 331.68 ? 183 TRP A CE2 1 
ATOM   171  C  CE3 . TRP A 1 184 ? 101.148 76.076  37.687 1.00 344.59 ? 183 TRP A CE3 1 
ATOM   172  C  CZ2 . TRP A 1 184 ? 103.580 75.693  39.080 1.00 373.25 ? 183 TRP A CZ2 1 
ATOM   173  C  CZ3 . TRP A 1 184 ? 101.704 74.817  37.816 1.00 356.82 ? 183 TRP A CZ3 1 
ATOM   174  C  CH2 . TRP A 1 184 ? 102.908 74.631  38.503 1.00 375.78 ? 183 TRP A CH2 1 
ATOM   175  N  N   . ALA A 1 185 ? 99.554  80.950  40.288 1.00 192.17 ? 184 ALA A N   1 
ATOM   176  C  CA  . ALA A 1 185 ? 99.808  81.459  41.631 1.00 299.71 ? 184 ALA A CA  1 
ATOM   177  C  C   . ALA A 1 185 ? 98.640  81.127  42.569 1.00 228.55 ? 184 ALA A C   1 
ATOM   178  O  O   . ALA A 1 185 ? 98.853  80.603  43.657 1.00 183.83 ? 184 ALA A O   1 
ATOM   179  C  CB  . ALA A 1 185 ? 100.091 82.952  41.580 1.00 304.76 ? 184 ALA A CB  1 
ATOM   180  N  N   . LEU A 1 186 ? 97.400  81.402  42.175 1.00 153.01 ? 185 LEU A N   1 
ATOM   181  C  CA  . LEU A 1 186 ? 96.275  81.198  43.073 1.00 169.55 ? 185 LEU A CA  1 
ATOM   182  C  C   . LEU A 1 186 ? 96.029  79.711  43.340 1.00 124.90 ? 185 LEU A C   1 
ATOM   183  O  O   . LEU A 1 186 ? 95.727  79.340  44.470 1.00 204.57 ? 185 LEU A O   1 
ATOM   184  C  CB  . LEU A 1 186 ? 95.031  81.919  42.518 1.00 166.31 ? 185 LEU A CB  1 
ATOM   185  C  CG  . LEU A 1 186 ? 95.123  83.449  42.591 1.00 199.45 ? 185 LEU A CG  1 
ATOM   186  C  CD1 . LEU A 1 186 ? 93.984  84.085  41.854 1.00 227.44 ? 185 LEU A CD1 1 
ATOM   187  C  CD2 . LEU A 1 186 ? 95.130  84.006  44.003 1.00 222.39 ? 185 LEU A CD2 1 
ATOM   188  N  N   . LEU A 1 187 ? 96.084  78.840  42.339 1.00 163.45 ? 186 LEU A N   1 
ATOM   189  C  CA  . LEU A 1 187 ? 95.899  77.404  42.564 1.00 197.52 ? 186 LEU A CA  1 
ATOM   190  C  C   . LEU A 1 187 ? 97.091  76.801  43.322 1.00 224.78 ? 186 LEU A C   1 
ATOM   191  O  O   . LEU A 1 187 ? 96.973  75.687  43.817 1.00 260.11 ? 186 LEU A O   1 
ATOM   192  C  CB  . LEU A 1 187 ? 95.636  76.670  41.241 1.00 252.26 ? 186 LEU A CB  1 
ATOM   193  C  CG  . LEU A 1 187 ? 94.162  76.574  40.839 1.00 246.51 ? 186 LEU A CG  1 
ATOM   194  C  CD1 . LEU A 1 187 ? 93.467  77.935  40.759 1.00 275.16 ? 186 LEU A CD1 1 
ATOM   195  C  CD2 . LEU A 1 187 ? 94.032  75.837  39.509 1.00 359.69 ? 186 LEU A CD2 1 
ATOM   196  N  N   . LEU A 1 188 ? 98.223  77.516  43.450 1.00 142.33 ? 187 LEU A N   1 
ATOM   197  C  CA  . LEU A 1 188 ? 99.235  77.155  44.437 1.00 212.83 ? 187 LEU A CA  1 
ATOM   198  C  C   . LEU A 1 188 ? 98.841  77.707  45.818 1.00 209.03 ? 187 LEU A C   1 
ATOM   199  O  O   . LEU A 1 188 ? 98.867  76.957  46.787 1.00 244.59 ? 187 LEU A O   1 
ATOM   200  C  CB  . LEU A 1 188 ? 100.607 77.644  43.961 1.00 282.33 ? 187 LEU A CB  1 
ATOM   201  C  CG  . LEU A 1 188 ? 101.763 77.340  44.910 1.00 392.64 ? 187 LEU A CG  1 
ATOM   202  C  CD1 . LEU A 1 188 ? 101.884 75.841  45.185 1.00 378.51 ? 187 LEU A CD1 1 
ATOM   203  C  CD2 . LEU A 1 188 ? 103.066 77.886  44.341 1.00 446.70 ? 187 LEU A CD2 1 
ATOM   204  N  N   . LEU A 1 189 ? 98.479  78.995  45.923 1.00 139.52 ? 188 LEU A N   1 
ATOM   205  C  CA  . LEU A 1 189 ? 98.139  79.635  47.202 1.00 198.71 ? 188 LEU A CA  1 
ATOM   206  C  C   . LEU A 1 189 ? 96.939  79.004  47.917 1.00 172.82 ? 188 LEU A C   1 
ATOM   207  O  O   . LEU A 1 189 ? 96.934  78.933  49.138 1.00 204.52 ? 188 LEU A O   1 
ATOM   208  C  CB  . LEU A 1 189 ? 97.883  81.142  47.000 1.00 195.32 ? 188 LEU A CB  1 
ATOM   209  C  CG  . LEU A 1 189 ? 99.044  82.032  47.415 1.00 299.16 ? 188 LEU A CG  1 
ATOM   210  C  CD1 . LEU A 1 189 ? 100.262 81.804  46.528 1.00 366.98 ? 188 LEU A CD1 1 
ATOM   211  C  CD2 . LEU A 1 189 ? 98.607  83.486  47.416 1.00 332.75 ? 188 LEU A CD2 1 
ATOM   212  N  N   . PHE A 1 190 ? 95.914  78.560  47.200 1.00 181.45 ? 189 PHE A N   1 
ATOM   213  C  CA  . PHE A 1 190 ? 94.809  77.831  47.815 1.00 158.84 ? 189 PHE A CA  1 
ATOM   214  C  C   . PHE A 1 190 ? 95.323  76.534  48.439 1.00 142.63 ? 189 PHE A C   1 
ATOM   215  O  O   . PHE A 1 190 ? 95.046  76.305  49.618 1.00 269.36 ? 189 PHE A O   1 
ATOM   216  C  CB  . PHE A 1 190 ? 93.750  77.506  46.781 1.00 224.95 ? 189 PHE A CB  1 
ATOM   217  C  CG  . PHE A 1 190 ? 92.763  76.434  47.180 1.00 224.84 ? 189 PHE A CG  1 
ATOM   218  C  CD1 . PHE A 1 190 ? 91.580  76.846  47.740 1.00 230.52 ? 189 PHE A CD1 1 
ATOM   219  C  CD2 . PHE A 1 190 ? 92.987  75.053  46.996 1.00 144.70 ? 189 PHE A CD2 1 
ATOM   220  C  CE1 . PHE A 1 190 ? 90.604  75.914  48.094 1.00 271.03 ? 189 PHE A CE1 1 
ATOM   221  C  CE2 . PHE A 1 190 ? 92.033  74.128  47.370 1.00 203.67 ? 189 PHE A CE2 1 
ATOM   222  C  CZ  . PHE A 1 190 ? 90.836  74.560  47.914 1.00 275.22 ? 189 PHE A CZ  1 
ATOM   223  N  N   . TRP A 1 191 ? 96.081  75.706  47.697 1.00 131.31 ? 190 TRP A N   1 
ATOM   224  C  CA  . TRP A 1 191 ? 96.551  74.435  48.209 1.00 178.38 ? 190 TRP A CA  1 
ATOM   225  C  C   . TRP A 1 191 ? 97.523  74.642  49.386 1.00 213.20 ? 190 TRP A C   1 
ATOM   226  O  O   . TRP A 1 191 ? 97.480  73.921  50.389 1.00 171.70 ? 190 TRP A O   1 
ATOM   227  C  CB  . TRP A 1 191 ? 97.181  73.652  47.064 1.00 221.82 ? 190 TRP A CB  1 
ATOM   228  C  CG  . TRP A 1 191 ? 97.169  72.166  47.232 1.00 333.59 ? 190 TRP A CG  1 
ATOM   229  C  CD1 . TRP A 1 191 ? 98.212  71.364  47.595 1.00 392.49 ? 190 TRP A CD1 1 
ATOM   230  C  CD2 . TRP A 1 191 ? 96.032  71.296  47.009 1.00 300.97 ? 190 TRP A CD2 1 
ATOM   231  N  NE1 . TRP A 1 191 ? 97.811  70.047  47.618 1.00 303.62 ? 190 TRP A NE1 1 
ATOM   232  C  CE2 . TRP A 1 191 ? 96.480  69.963  47.266 1.00 328.11 ? 190 TRP A CE2 1 
ATOM   233  C  CE3 . TRP A 1 191 ? 94.698  71.524  46.628 1.00 145.80 ? 190 TRP A CE3 1 
ATOM   234  C  CZ2 . TRP A 1 191 ? 95.630  68.851  47.149 1.00 255.63 ? 190 TRP A CZ2 1 
ATOM   235  C  CZ3 . TRP A 1 191 ? 93.864  70.428  46.503 1.00 268.20 ? 190 TRP A CZ3 1 
ATOM   236  C  CH2 . TRP A 1 191 ? 94.326  69.115  46.759 1.00 314.72 ? 190 TRP A CH2 1 
ATOM   237  N  N   . LEU A 1 192 ? 98.392  75.653  49.283 1.00 165.88 ? 191 LEU A N   1 
ATOM   238  C  CA  . LEU A 1 192 ? 99.290  76.066  50.349 1.00 256.33 ? 191 LEU A CA  1 
ATOM   239  C  C   . LEU A 1 192 ? 98.497  76.514  51.584 1.00 209.58 ? 191 LEU A C   1 
ATOM   240  O  O   . LEU A 1 192 ? 98.839  76.143  52.701 1.00 207.06 ? 191 LEU A O   1 
ATOM   241  C  CB  . LEU A 1 192 ? 100.195 77.177  49.785 1.00 312.87 ? 191 LEU A CB  1 
ATOM   242  C  CG  . LEU A 1 192 ? 101.146 77.859  50.767 1.00 423.52 ? 191 LEU A CG  1 
ATOM   243  C  CD1 . LEU A 1 192 ? 102.176 76.879  51.311 1.00 496.75 ? 191 LEU A CD1 1 
ATOM   244  C  CD2 . LEU A 1 192 ? 101.837 79.034  50.101 1.00 438.83 ? 191 LEU A CD2 1 
ATOM   245  N  N   . GLY A 1 193 ? 97.456  77.331  51.407 1.00 159.39 ? 192 GLY A N   1 
ATOM   246  C  CA  . GLY A 1 193 ? 96.626  77.822  52.504 1.00 214.38 ? 192 GLY A CA  1 
ATOM   247  C  C   . GLY A 1 193 ? 95.812  76.729  53.194 1.00 157.45 ? 192 GLY A C   1 
ATOM   248  O  O   . GLY A 1 193 ? 95.675  76.750  54.403 1.00 198.98 ? 192 GLY A O   1 
ATOM   249  N  N   . TRP A 1 194 ? 95.294  75.768  52.439 1.00 145.42 ? 193 TRP A N   1 
ATOM   250  C  CA  . TRP A 1 194 ? 94.691  74.553  52.979 1.00 151.60 ? 193 TRP A CA  1 
ATOM   251  C  C   . TRP A 1 194 ? 95.723  73.782  53.791 1.00 167.31 ? 193 TRP A C   1 
ATOM   252  O  O   . TRP A 1 194 ? 95.430  73.454  54.941 1.00 258.02 ? 193 TRP A O   1 
ATOM   253  C  CB  . TRP A 1 194 ? 94.182  73.718  51.815 1.00 241.55 ? 193 TRP A CB  1 
ATOM   254  C  CG  . TRP A 1 194 ? 93.441  72.453  52.103 1.00 136.36 ? 193 TRP A CG  1 
ATOM   255  C  CD1 . TRP A 1 194 ? 92.089  72.384  52.053 1.00 135.03 ? 193 TRP A CD1 1 
ATOM   256  C  CD2 . TRP A 1 194 ? 93.912  71.128  52.386 1.00 127.66 ? 193 TRP A CD2 1 
ATOM   257  N  NE1 . TRP A 1 194 ? 91.657  71.117  52.290 1.00 135.61 ? 193 TRP A NE1 1 
ATOM   258  C  CE2 . TRP A 1 194 ? 92.751  70.307  52.503 1.00 181.18 ? 193 TRP A CE2 1 
ATOM   259  C  CE3 . TRP A 1 194 ? 95.159  70.527  52.550 1.00 130.14 ? 193 TRP A CE3 1 
ATOM   260  C  CZ2 . TRP A 1 194 ? 92.828  68.928  52.792 1.00 201.01 ? 193 TRP A CZ2 1 
ATOM   261  C  CZ3 . TRP A 1 194 ? 95.239  69.174  52.836 1.00 257.99 ? 193 TRP A CZ3 1 
ATOM   262  C  CH2 . TRP A 1 194 ? 94.083  68.376  52.946 1.00 224.68 ? 193 TRP A CH2 1 
ATOM   263  N  N   . LEU A 1 195 ? 96.932  73.539  53.253 1.00 131.12 ? 194 LEU A N   1 
ATOM   264  C  CA  . LEU A 1 195 ? 97.984  72.900  54.038 1.00 202.92 ? 194 LEU A CA  1 
ATOM   265  C  C   . LEU A 1 195 ? 98.375  73.704  55.293 1.00 226.59 ? 194 LEU A C   1 
ATOM   266  O  O   . LEU A 1 195 ? 98.724  73.124  56.321 1.00 161.92 ? 194 LEU A O   1 
ATOM   267  C  CB  . LEU A 1 195 ? 99.177  72.655  53.117 1.00 192.49 ? 194 LEU A CB  1 
ATOM   268  C  CG  . LEU A 1 195 ? 98.975  71.495  52.155 1.00 210.20 ? 194 LEU A CG  1 
ATOM   269  C  CD1 . LEU A 1 195 ? 100.052 71.513  51.079 1.00 335.70 ? 194 LEU A CD1 1 
ATOM   270  C  CD2 . LEU A 1 195 ? 98.970  70.141  52.910 1.00 173.90 ? 194 LEU A CD2 1 
ATOM   271  N  N   . GLY A 1 196 ? 98.311  75.034  55.231 1.00 191.07 ? 195 GLY A N   1 
ATOM   272  C  CA  . GLY A 1 196 ? 98.479  75.889  56.391 1.00 229.95 ? 195 GLY A CA  1 
ATOM   273  C  C   . GLY A 1 196 ? 97.461  75.598  57.490 1.00 177.30 ? 195 GLY A C   1 
ATOM   274  O  O   . GLY A 1 196 ? 97.844  75.432  58.642 1.00 211.76 ? 195 GLY A O   1 
ATOM   275  N  N   . MET A 1 197 ? 96.176  75.539  57.147 1.00 141.71 ? 196 MET A N   1 
ATOM   276  C  CA  . MET A 1 197 ? 95.135  75.171  58.095 1.00 181.07 ? 196 MET A CA  1 
ATOM   277  C  C   . MET A 1 197 ? 95.350  73.745  58.613 1.00 159.20 ? 196 MET A C   1 
ATOM   278  O  O   . MET A 1 197 ? 95.078  73.495  59.781 1.00 154.86 ? 196 MET A O   1 
ATOM   279  C  CB  . MET A 1 197 ? 93.739  75.322  57.465 1.00 170.36 ? 196 MET A CB  1 
ATOM   280  C  CG  . MET A 1 197 ? 93.272  76.760  57.427 1.00 182.27 ? 196 MET A CG  1 
ATOM   281  S  SD  . MET A 1 197 ? 91.811  76.994  56.355 1.00 341.90 ? 196 MET A SD  1 
ATOM   282  C  CE  . MET A 1 197 ? 90.563  76.034  57.214 1.00 205.62 ? 196 MET A CE  1 
ATOM   283  N  N   . LEU A 1 198 ? 95.835  72.818  57.776 1.00 140.83 ? 197 LEU A N   1 
ATOM   284  C  CA  . LEU A 1 198 ? 96.055  71.439  58.178 1.00 169.55 ? 197 LEU A CA  1 
ATOM   285  C  C   . LEU A 1 198 ? 97.156  71.394  59.236 1.00 166.44 ? 197 LEU A C   1 
ATOM   286  O  O   . LEU A 1 198 ? 96.955  70.833  60.310 1.00 202.52 ? 197 LEU A O   1 
ATOM   287  C  CB  . LEU A 1 198 ? 96.357  70.591  56.932 1.00 155.76 ? 197 LEU A CB  1 
ATOM   288  C  CG  . LEU A 1 198 ? 96.421  69.059  57.097 1.00 165.15 ? 197 LEU A CG  1 
ATOM   289  C  CD1 . LEU A 1 198 ? 97.644  68.583  57.891 1.00 174.43 ? 197 LEU A CD1 1 
ATOM   290  C  CD2 . LEU A 1 198 ? 95.157  68.491  57.716 1.00 194.60 ? 197 LEU A CD2 1 
ATOM   291  N  N   . ALA A 1 199 ? 98.301  71.998  58.960 1.00 137.01 ? 198 ALA A N   1 
ATOM   292  C  CA  . ALA A 1 199 ? 99.360  72.095  59.952 1.00 228.74 ? 198 ALA A CA  1 
ATOM   293  C  C   . ALA A 1 199 ? 98.880  72.804  61.229 1.00 229.08 ? 198 ALA A C   1 
ATOM   294  O  O   . ALA A 1 199 ? 99.219  72.374  62.341 1.00 285.63 ? 198 ALA A O   1 
ATOM   295  C  CB  . ALA A 1 199 ? 100.551 72.789  59.324 1.00 327.10 ? 198 ALA A CB  1 
ATOM   296  N  N   . GLY A 1 200 ? 98.097  73.886  61.091 1.00 192.63 ? 199 GLY A N   1 
ATOM   297  C  CA  . GLY A 1 200 ? 97.463  74.579  62.204 1.00 254.23 ? 199 GLY A CA  1 
ATOM   298  C  C   . GLY A 1 200 ? 96.635  73.644  63.084 1.00 221.11 ? 199 GLY A C   1 
ATOM   299  O  O   . GLY A 1 200 ? 96.835  73.585  64.290 1.00 195.30 ? 199 GLY A O   1 
ATOM   300  N  N   . ALA A 1 201 ? 95.719  72.894  62.469 1.00 199.84 ? 200 ALA A N   1 
ATOM   301  C  CA  . ALA A 1 201 ? 94.881  71.938  63.173 1.00 248.50 ? 200 ALA A CA  1 
ATOM   302  C  C   . ALA A 1 201 ? 95.743  70.905  63.904 1.00 247.19 ? 200 ALA A C   1 
ATOM   303  O  O   . ALA A 1 201 ? 95.475  70.624  65.069 1.00 259.71 ? 200 ALA A O   1 
ATOM   304  C  CB  . ALA A 1 201 ? 93.907  71.318  62.194 1.00 254.45 ? 200 ALA A CB  1 
ATOM   305  N  N   . VAL A 1 202 ? 96.784  70.347  63.262 1.00 146.60 ? 201 VAL A N   1 
ATOM   306  C  CA  . VAL A 1 202 ? 97.654  69.375  63.912 1.00 191.53 ? 201 VAL A CA  1 
ATOM   307  C  C   . VAL A 1 202 ? 98.358  70.013  65.108 1.00 175.70 ? 201 VAL A C   1 
ATOM   308  O  O   . VAL A 1 202 ? 98.469  69.355  66.151 1.00 230.55 ? 201 VAL A O   1 
ATOM   309  C  CB  . VAL A 1 202 ? 98.621  68.725  62.905 1.00 274.65 ? 201 VAL A CB  1 
ATOM   310  C  CG1 . VAL A 1 202 ? 99.760  67.933  63.544 1.00 369.54 ? 201 VAL A CG1 1 
ATOM   311  C  CG2 . VAL A 1 202 ? 97.826  67.824  61.976 1.00 309.10 ? 201 VAL A CG2 1 
ATOM   312  N  N   . VAL A 1 203 ? 98.805  71.263  64.979 1.00 156.02 ? 202 VAL A N   1 
ATOM   313  C  CA  . VAL A 1 203 ? 99.394  71.992  66.102 1.00 225.65 ? 202 VAL A CA  1 
ATOM   314  C  C   . VAL A 1 203 ? 98.393  72.141  67.255 1.00 225.51 ? 202 VAL A C   1 
ATOM   315  O  O   . VAL A 1 203 ? 98.821  71.946  68.402 1.00 263.38 ? 202 VAL A O   1 
ATOM   316  C  CB  . VAL A 1 203 ? 99.996  73.336  65.637 1.00 301.63 ? 202 VAL A CB  1 
ATOM   317  C  CG1 . VAL A 1 203 ? 100.165 74.388  66.740 1.00 272.13 ? 202 VAL A CG1 1 
ATOM   318  C  CG2 . VAL A 1 203 ? 101.310 73.074  64.912 1.00 346.54 ? 202 VAL A CG2 1 
ATOM   319  N  N   . ILE A 1 204 ? 97.105  72.453  66.988 1.00 179.36 ? 203 ILE A N   1 
ATOM   320  C  CA  . ILE A 1 204 ? 96.107  72.535  68.052 1.00 182.40 ? 203 ILE A CA  1 
ATOM   321  C  C   . ILE A 1 204 ? 95.967  71.185  68.760 1.00 155.54 ? 203 ILE A C   1 
ATOM   322  O  O   . ILE A 1 204 ? 95.961  71.148  69.999 1.00 169.76 ? 203 ILE A O   1 
ATOM   323  C  CB  . ILE A 1 204 ? 94.738  73.062  67.573 1.00 182.89 ? 203 ILE A CB  1 
ATOM   324  C  CG1 . ILE A 1 204 ? 94.840  74.445  66.914 1.00 245.07 ? 203 ILE A CG1 1 
ATOM   325  C  CG2 . ILE A 1 204 ? 93.740  73.101  68.723 1.00 205.42 ? 203 ILE A CG2 1 
ATOM   326  C  CD1 . ILE A 1 204 ? 95.444  75.557  67.774 1.00 324.72 ? 203 ILE A CD1 1 
ATOM   327  N  N   . ILE A 1 205 ? 95.870  70.105  67.982 1.00 114.56 ? 204 ILE A N   1 
ATOM   328  C  CA  . ILE A 1 205 ? 95.750  68.756  68.540 1.00 196.51 ? 204 ILE A CA  1 
ATOM   329  C  C   . ILE A 1 205 ? 96.966  68.335  69.402 1.00 213.85 ? 204 ILE A C   1 
ATOM   330  O  O   . ILE A 1 205 ? 96.790  67.632  70.402 1.00 253.32 ? 204 ILE A O   1 
ATOM   331  C  CB  . ILE A 1 205 ? 95.427  67.774  67.388 1.00 223.21 ? 204 ILE A CB  1 
ATOM   332  C  CG1 . ILE A 1 205 ? 94.041  68.082  66.776 1.00 169.78 ? 204 ILE A CG1 1 
ATOM   333  C  CG2 . ILE A 1 205 ? 95.580  66.298  67.778 1.00 241.24 ? 204 ILE A CG2 1 
ATOM   334  C  CD1 . ILE A 1 205 ? 92.804  67.813  67.620 1.00 130.12 ? 204 ILE A CD1 1 
ATOM   335  N  N   . VAL A 1 206 ? 98.184  68.753  69.049 1.00 179.34 ? 205 VAL A N   1 
ATOM   336  C  CA  . VAL A 1 206 ? 99.356  68.551  69.895 1.00 217.85 ? 205 VAL A CA  1 
ATOM   337  C  C   . VAL A 1 206 ? 99.298  69.441  71.145 1.00 225.95 ? 205 VAL A C   1 
ATOM   338  O  O   . VAL A 1 206 ? 99.492  68.941  72.259 1.00 197.84 ? 205 VAL A O   1 
ATOM   339  C  CB  . VAL A 1 206 ? 100.646 68.797  69.082 1.00 358.37 ? 205 VAL A CB  1 
ATOM   340  C  CG1 . VAL A 1 206 ? 101.909 68.978  69.931 1.00 417.36 ? 205 VAL A CG1 1 
ATOM   341  C  CG2 . VAL A 1 206 ? 100.844 67.669  68.078 1.00 384.93 ? 205 VAL A CG2 1 
ATOM   342  N  N   . ARG A 1 207 ? 99.038  70.751  70.953 1.00 237.03 ? 206 ARG A N   1 
ATOM   343  C  CA  . ARG A 1 207 ? 99.080  71.770  72.000 1.00 288.43 ? 206 ARG A CA  1 
ATOM   344  C  C   . ARG A 1 207 ? 97.720  71.873  72.719 1.00 328.13 ? 206 ARG A C   1 
ATOM   345  O  O   . ARG A 1 207 ? 97.200  72.981  72.917 1.00 379.77 ? 206 ARG A O   1 
ATOM   346  C  CB  . ARG A 1 207 ? 99.558  73.089  71.363 1.00 325.55 ? 206 ARG A CB  1 
ATOM   347  C  CG  . ARG A 1 207 ? 100.020 74.176  72.330 1.00 357.12 ? 206 ARG A CG  1 
ATOM   348  C  CD  . ARG A 1 207 ? 100.625 75.405  71.657 1.00 342.68 ? 206 ARG A CD  1 
ATOM   349  N  NE  . ARG A 1 207 ? 99.762  76.082  70.683 1.00 381.88 ? 206 ARG A NE  1 
ATOM   350  C  CZ  . ARG A 1 207 ? 98.729  76.888  70.959 1.00 375.77 ? 206 ARG A CZ  1 
ATOM   351  N  NH1 . ARG A 1 207 ? 97.983  77.370  69.975 1.00 349.61 ? 206 ARG A NH1 1 
ATOM   352  N  NH2 . ARG A 1 207 ? 98.429  77.211  72.207 1.00 377.31 ? 206 ARG A NH2 1 
ATOM   353  N  N   . ALA A 1 208 ? 97.148  70.725  73.142 1.00 277.69 ? 207 ALA A N   1 
ATOM   354  C  CA  . ALA A 1 208 ? 95.918  70.693  73.921 1.00 248.35 ? 207 ALA A CA  1 
ATOM   355  C  C   . ALA A 1 208 ? 95.946  69.572  74.978 1.00 266.74 ? 207 ALA A C   1 
ATOM   356  O  O   . ALA A 1 208 ? 96.527  68.507  74.763 1.00 195.46 ? 207 ALA A O   1 
ATOM   357  C  CB  . ALA A 1 208 ? 94.767  70.575  72.971 1.00 192.01 ? 207 ALA A CB  1 
ATOM   358  N  N   . PRO A 1 209 ? 95.322  69.785  76.167 1.00 243.10 ? 208 PRO A N   1 
ATOM   359  C  CA  . PRO A 1 209 ? 95.393  68.816  77.266 1.00 217.68 ? 208 PRO A CA  1 
ATOM   360  C  C   . PRO A 1 209 ? 94.489  67.603  77.064 1.00 196.74 ? 208 PRO A C   1 
ATOM   361  O  O   . PRO A 1 209 ? 93.286  67.773  76.887 1.00 192.37 ? 208 PRO A O   1 
ATOM   362  C  CB  . PRO A 1 209 ? 94.889  69.629  78.470 1.00 293.12 ? 208 PRO A CB  1 
ATOM   363  C  CG  . PRO A 1 209 ? 93.952  70.681  77.879 1.00 276.18 ? 208 PRO A CG  1 
ATOM   364  C  CD  . PRO A 1 209 ? 94.514  70.974  76.507 1.00 226.84 ? 208 PRO A CD  1 
ATOM   365  N  N   . ARG A 1 210 ? 95.070  66.392  77.093 1.00 194.30 ? 209 ARG A N   1 
ATOM   366  C  CA  . ARG A 1 210 ? 94.326  65.149  76.875 1.00 230.69 ? 209 ARG A CA  1 
ATOM   367  C  C   . ARG A 1 210 ? 93.383  64.849  78.053 1.00 237.26 ? 209 ARG A C   1 
ATOM   368  O  O   . ARG A 1 210 ? 93.701  65.207  79.194 1.00 233.26 ? 209 ARG A O   1 
ATOM   369  C  CB  . ARG A 1 210 ? 95.296  63.980  76.661 1.00 238.71 ? 209 ARG A CB  1 
ATOM   370  C  CG  . ARG A 1 210 ? 96.381  64.205  75.611 1.00 292.41 ? 209 ARG A CG  1 
ATOM   371  C  CD  . ARG A 1 210 ? 95.832  64.415  74.212 1.00 338.50 ? 209 ARG A CD  1 
ATOM   372  N  NE  . ARG A 1 210 ? 96.838  64.649  73.171 1.00 370.96 ? 209 ARG A NE  1 
ATOM   373  C  CZ  . ARG A 1 210 ? 97.626  63.736  72.582 1.00 346.19 ? 209 ARG A CZ  1 
ATOM   374  N  NH1 . ARG A 1 210 ? 98.467  64.134  71.643 1.00 357.19 ? 209 ARG A NH1 1 
ATOM   375  N  NH2 . ARG A 1 210 ? 97.592  62.446  72.892 1.00 253.28 ? 209 ARG A NH2 1 
ATOM   376  N  N   . CYS A 1 211 ? 92.230  64.200  77.776 1.00 251.64 ? 210 CYS A N   1 
ATOM   377  C  CA  . CYS A 1 211 ? 91.285  63.820  78.823 1.00 280.01 ? 210 CYS A CA  1 
ATOM   378  C  C   . CYS A 1 211 ? 91.940  62.861  79.830 1.00 270.10 ? 210 CYS A C   1 
ATOM   379  O  O   . CYS A 1 211 ? 92.595  61.899  79.420 1.00 257.15 ? 210 CYS A O   1 
ATOM   380  C  CB  . CYS A 1 211 ? 90.021  63.118  78.307 1.00 256.03 ? 210 CYS A CB  1 
ATOM   381  S  SG  . CYS A 1 211 ? 89.155  63.829  76.886 1.00 247.09 ? 210 CYS A SG  1 
ATOM   382  N  N   . ARG A 1 212 ? 91.750  63.102  81.149 1.00 269.52 ? 211 ARG A N   1 
ATOM   383  C  CA  . ARG A 1 212 ? 92.228  62.193  82.186 1.00 268.39 ? 211 ARG A CA  1 
ATOM   384  C  C   . ARG A 1 212 ? 91.435  60.883  82.141 1.00 213.38 ? 211 ARG A C   1 
ATOM   385  O  O   . ARG A 1 212 ? 90.213  60.897  81.998 1.00 227.68 ? 211 ARG A O   1 
ATOM   386  C  CB  . ARG A 1 212 ? 92.100  62.844  83.566 1.00 292.98 ? 211 ARG A CB  1 
ATOM   387  C  CG  . ARG A 1 212 ? 92.788  62.077  84.684 1.00 307.30 ? 211 ARG A CG  1 
ATOM   388  C  CD  . ARG A 1 212 ? 92.504  62.723  86.026 1.00 358.88 ? 211 ARG A CD  1 
ATOM   389  N  NE  . ARG A 1 212 ? 93.162  64.021  86.134 1.00 441.42 ? 211 ARG A NE  1 
ATOM   390  C  CZ  . ARG A 1 212 ? 93.004  64.883  87.138 1.00 524.38 ? 211 ARG A CZ  1 
ATOM   391  N  NH1 . ARG A 1 212 ? 93.684  66.019  87.152 1.00 571.79 ? 211 ARG A NH1 1 
ATOM   392  N  NH2 . ARG A 1 212 ? 92.170  64.611  88.128 1.00 532.41 ? 211 ARG A NH2 1 
ATOM   393  N  N   . GLU A 1 213 ? 92.125  59.739  82.270 1.00 168.98 ? 212 GLU A N   1 
ATOM   394  C  CA  . GLU A 1 213 ? 91.445  58.448  82.246 1.00 210.48 ? 212 GLU A CA  1 
ATOM   395  C  C   . GLU A 1 213 ? 90.570  58.263  83.495 1.00 209.33 ? 212 GLU A C   1 
ATOM   396  O  O   . GLU A 1 213 ? 90.790  58.876  84.536 1.00 231.03 ? 212 GLU A O   1 
ATOM   397  C  CB  . GLU A 1 213 ? 92.462  57.311  82.081 1.00 267.41 ? 212 GLU A CB  1 
ATOM   398  C  CG  . GLU A 1 213 ? 93.375  57.075  83.274 1.00 348.11 ? 212 GLU A CG  1 
ATOM   399  C  CD  . GLU A 1 213 ? 94.504  56.092  83.000 1.00 421.11 ? 212 GLU A CD  1 
ATOM   400  O  OE1 . GLU A 1 213 ? 94.424  55.344  81.997 1.00 421.92 ? 212 GLU A OE1 1 
ATOM   401  O  OE2 . GLU A 1 213 ? 95.466  56.078  83.789 1.00 488.93 ? 212 GLU A OE2 1 
ATOM   402  N  N   . LEU A 1 214 ? 89.573  57.376  83.392 1.00 231.26 ? 213 LEU A N   1 
ATOM   403  C  CA  . LEU A 1 214 ? 88.595  57.151  84.452 1.00 270.89 ? 213 LEU A CA  1 
ATOM   404  C  C   . LEU A 1 214 ? 89.231  56.442  85.664 1.00 282.36 ? 213 LEU A C   1 
ATOM   405  O  O   . LEU A 1 214 ? 89.652  55.271  85.526 1.00 253.37 ? 213 LEU A O   1 
ATOM   406  C  CB  . LEU A 1 214 ? 87.439  56.325  83.875 1.00 262.60 ? 213 LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 214 ? 86.709  56.932  82.676 1.00 221.67 ? 213 LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 214 ? 85.634  55.992  82.187 1.00 300.90 ? 213 LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 214 ? 86.089  58.269  83.026 1.00 256.30 ? 213 LEU A CD2 1 
ATOM   410  N  N   . VAL B 2 44  ? 80.041  75.563  25.890 1.00 265.69 ? 44  VAL B N   1 
ATOM   411  C  CA  . VAL B 2 44  ? 80.071  74.202  26.515 1.00 285.80 ? 44  VAL B CA  1 
ATOM   412  C  C   . VAL B 2 44  ? 78.739  73.913  27.206 1.00 301.30 ? 44  VAL B C   1 
ATOM   413  O  O   . VAL B 2 44  ? 77.920  74.818  27.344 1.00 259.30 ? 44  VAL B O   1 
ATOM   414  C  CB  . VAL B 2 44  ? 81.247  74.044  27.504 1.00 319.81 ? 44  VAL B CB  1 
ATOM   415  C  CG1 . VAL B 2 44  ? 82.577  74.134  26.773 1.00 420.19 ? 44  VAL B CG1 1 
ATOM   416  C  CG2 . VAL B 2 44  ? 81.219  75.008  28.697 1.00 276.35 ? 44  VAL B CG2 1 
ATOM   417  N  N   . THR B 2 45  ? 78.545  72.639  27.620 1.00 309.36 ? 45  THR B N   1 
ATOM   418  C  CA  . THR B 2 45  ? 77.347  72.154  28.303 1.00 312.68 ? 45  THR B CA  1 
ATOM   419  C  C   . THR B 2 45  ? 77.722  71.121  29.378 1.00 225.20 ? 45  THR B C   1 
ATOM   420  O  O   . THR B 2 45  ? 78.611  70.327  29.155 1.00 192.41 ? 45  THR B O   1 
ATOM   421  C  CB  . THR B 2 45  ? 76.360  71.542  27.286 1.00 422.17 ? 45  THR B CB  1 
ATOM   422  O  OG1 . THR B 2 45  ? 76.260  72.318  26.089 1.00 453.66 ? 45  THR B OG1 1 
ATOM   423  C  CG2 . THR B 2 45  ? 74.949  71.406  27.812 1.00 456.19 ? 45  THR B CG2 1 
ATOM   424  N  N   . LEU B 2 46  ? 77.040  71.088  30.535 1.00 207.53 ? 46  LEU B N   1 
ATOM   425  C  CA  . LEU B 2 46  ? 77.319  70.107  31.600 1.00 232.91 ? 46  LEU B CA  1 
ATOM   426  C  C   . LEU B 2 46  ? 76.944  68.673  31.202 1.00 230.69 ? 46  LEU B C   1 
ATOM   427  O  O   . LEU B 2 46  ? 75.746  68.397  31.120 1.00 167.83 ? 46  LEU B O   1 
ATOM   428  C  CB  . LEU B 2 46  ? 76.518  70.468  32.863 1.00 203.16 ? 46  LEU B CB  1 
ATOM   429  C  CG  . LEU B 2 46  ? 76.860  71.801  33.537 1.00 223.05 ? 46  LEU B CG  1 
ATOM   430  C  CD1 . LEU B 2 46  ? 75.961  72.057  34.738 1.00 156.51 ? 46  LEU B CD1 1 
ATOM   431  C  CD2 . LEU B 2 46  ? 78.315  71.827  34.000 1.00 291.85 ? 46  LEU B CD2 1 
ATOM   432  N  N   . GLN B 2 47  ? 77.936  67.781  30.973 1.00 236.49 ? 47  GLN B N   1 
ATOM   433  C  CA  . GLN B 2 47  ? 77.645  66.410  30.547 1.00 263.05 ? 47  GLN B CA  1 
ATOM   434  C  C   . GLN B 2 47  ? 77.031  65.563  31.669 1.00 184.20 ? 47  GLN B C   1 
ATOM   435  O  O   . GLN B 2 47  ? 77.364  65.717  32.838 1.00 234.43 ? 47  GLN B O   1 
ATOM   436  C  CB  . GLN B 2 47  ? 78.886  65.681  30.006 1.00 290.26 ? 47  GLN B CB  1 
ATOM   437  C  CG  . GLN B 2 47  ? 79.371  66.165  28.641 1.00 304.69 ? 47  GLN B CG  1 
ATOM   438  C  CD  . GLN B 2 47  ? 80.285  67.361  28.703 1.00 346.32 ? 47  GLN B CD  1 
ATOM   439  O  OE1 . GLN B 2 47  ? 80.528  67.924  29.769 1.00 418.37 ? 47  GLN B OE1 1 
ATOM   440  N  NE2 . GLN B 2 47  ? 80.806  67.763  27.552 1.00 363.70 ? 47  GLN B NE2 1 
ATOM   441  N  N   . ARG B 2 48  ? 76.161  64.621  31.263 1.00 191.27 ? 48  ARG B N   1 
ATOM   442  C  CA  . ARG B 2 48  ? 75.257  63.870  32.130 1.00 201.60 ? 48  ARG B CA  1 
ATOM   443  C  C   . ARG B 2 48  ? 75.968  62.647  32.724 1.00 207.21 ? 48  ARG B C   1 
ATOM   444  O  O   . ARG B 2 48  ? 75.691  61.517  32.360 1.00 145.73 ? 48  ARG B O   1 
ATOM   445  C  CB  . ARG B 2 48  ? 74.005  63.466  31.343 1.00 204.44 ? 48  ARG B CB  1 
ATOM   446  C  CG  . ARG B 2 48  ? 73.368  64.616  30.569 1.00 178.77 ? 48  ARG B CG  1 
ATOM   447  C  CD  . ARG B 2 48  ? 72.097  64.156  29.858 1.00 234.31 ? 48  ARG B CD  1 
ATOM   448  N  NE  . ARG B 2 48  ? 70.937  64.221  30.737 1.00 246.37 ? 48  ARG B NE  1 
ATOM   449  C  CZ  . ARG B 2 48  ? 70.002  65.171  30.711 1.00 275.19 ? 48  ARG B CZ  1 
ATOM   450  N  NH1 . ARG B 2 48  ? 68.924  65.044  31.463 1.00 317.28 ? 48  ARG B NH1 1 
ATOM   451  N  NH2 . ARG B 2 48  ? 70.126  66.240  29.938 1.00 250.32 ? 48  ARG B NH2 1 
ATOM   452  N  N   . ASN B 2 49  ? 76.883  62.874  33.679 1.00 215.17 ? 49  ASN B N   1 
ATOM   453  C  CA  . ASN B 2 49  ? 77.780  61.835  34.165 1.00 193.07 ? 49  ASN B CA  1 
ATOM   454  C  C   . ASN B 2 49  ? 77.198  60.921  35.259 1.00 212.38 ? 49  ASN B C   1 
ATOM   455  O  O   . ASN B 2 49  ? 77.832  59.909  35.568 1.00 223.19 ? 49  ASN B O   1 
ATOM   456  C  CB  . ASN B 2 49  ? 79.093  62.471  34.608 1.00 199.74 ? 49  ASN B CB  1 
ATOM   457  C  CG  . ASN B 2 49  ? 80.050  62.646  33.446 1.00 247.05 ? 49  ASN B CG  1 
ATOM   458  O  OD1 . ASN B 2 49  ? 80.698  61.687  33.026 1.00 339.78 ? 49  ASN B OD1 1 
ATOM   459  N  ND2 . ASN B 2 49  ? 80.165  63.853  32.940 1.00 233.33 ? 49  ASN B ND2 1 
ATOM   460  N  N   . ILE B 2 50  ? 76.028  61.217  35.853 1.00 191.25 ? 50  ILE B N   1 
ATOM   461  C  CA  . ILE B 2 50  ? 75.520  60.426  36.982 1.00 190.10 ? 50  ILE B CA  1 
ATOM   462  C  C   . ILE B 2 50  ? 74.807  59.162  36.491 1.00 172.98 ? 50  ILE B C   1 
ATOM   463  O  O   . ILE B 2 50  ? 73.749  59.239  35.850 1.00 126.38 ? 50  ILE B O   1 
ATOM   464  C  CB  . ILE B 2 50  ? 74.603  61.261  37.903 1.00 212.70 ? 50  ILE B CB  1 
ATOM   465  C  CG1 . ILE B 2 50  ? 75.312  62.525  38.398 1.00 231.75 ? 50  ILE B CG1 1 
ATOM   466  C  CG2 . ILE B 2 50  ? 74.093  60.422  39.081 1.00 239.25 ? 50  ILE B CG2 1 
ATOM   467  C  CD1 . ILE B 2 50  ? 74.444  63.419  39.233 1.00 250.60 ? 50  ILE B CD1 1 
ATOM   468  N  N   . THR B 2 51  ? 75.410  57.997  36.820 1.00 173.69 ? 51  THR B N   1 
ATOM   469  C  CA  . THR B 2 51  ? 74.850  56.684  36.501 1.00 207.40 ? 51  THR B CA  1 
ATOM   470  C  C   . THR B 2 51  ? 73.690  56.322  37.430 1.00 154.19 ? 51  THR B C   1 
ATOM   471  O  O   . THR B 2 51  ? 73.393  57.058  38.350 1.00 210.58 ? 51  THR B O   1 
ATOM   472  C  CB  . THR B 2 51  ? 75.927  55.595  36.553 1.00 213.46 ? 51  THR B CB  1 
ATOM   473  O  OG1 . THR B 2 51  ? 76.355  55.451  37.900 1.00 164.57 ? 51  THR B OG1 1 
ATOM   474  C  CG2 . THR B 2 51  ? 77.121  55.901  35.674 1.00 286.85 ? 51  THR B CG2 1 
ATOM   475  N  N   . LEU B 2 52  ? 73.036  55.168  37.226 1.00 208.43 ? 52  LEU B N   1 
ATOM   476  C  CA  . LEU B 2 52  ? 72.019  54.669  38.153 1.00 239.80 ? 52  LEU B CA  1 
ATOM   477  C  C   . LEU B 2 52  ? 72.648  54.446  39.537 1.00 226.75 ? 52  LEU B C   1 
ATOM   478  O  O   . LEU B 2 52  ? 72.108  54.904  40.548 1.00 171.83 ? 52  LEU B O   1 
ATOM   479  C  CB  . LEU B 2 52  ? 71.405  53.384  37.570 1.00 271.49 ? 52  LEU B CB  1 
ATOM   480  C  CG  . LEU B 2 52  ? 70.267  52.686  38.330 1.00 289.00 ? 52  LEU B CG  1 
ATOM   481  C  CD1 . LEU B 2 52  ? 70.760  51.893  39.548 1.00 344.88 ? 52  LEU B CD1 1 
ATOM   482  C  CD2 . LEU B 2 52  ? 69.180  53.667  38.736 1.00 232.83 ? 52  LEU B CD2 1 
ATOM   483  N  N   . LEU B 2 53  ? 73.801  53.765  39.592 1.00 208.92 ? 53  LEU B N   1 
ATOM   484  C  CA  . LEU B 2 53  ? 74.477  53.507  40.857 1.00 200.57 ? 53  LEU B CA  1 
ATOM   485  C  C   . LEU B 2 53  ? 74.899  54.820  41.529 1.00 145.52 ? 53  LEU B C   1 
ATOM   486  O  O   . LEU B 2 53  ? 74.621  54.996  42.708 1.00 125.21 ? 53  LEU B O   1 
ATOM   487  C  CB  . LEU B 2 53  ? 75.656  52.556  40.578 1.00 248.88 ? 53  LEU B CB  1 
ATOM   488  C  CG  . LEU B 2 53  ? 76.512  52.079  41.758 1.00 266.91 ? 53  LEU B CG  1 
ATOM   489  C  CD1 . LEU B 2 53  ? 77.522  53.136  42.204 1.00 220.70 ? 53  LEU B CD1 1 
ATOM   490  C  CD2 . LEU B 2 53  ? 75.649  51.622  42.932 1.00 301.29 ? 53  LEU B CD2 1 
ATOM   491  N  N   . ASN B 2 54  ? 75.560  55.746  40.811 1.00 195.36 ? 54  ASN B N   1 
ATOM   492  C  CA  . ASN B 2 54  ? 75.973  57.033  41.391 1.00 194.02 ? 54  ASN B CA  1 
ATOM   493  C  C   . ASN B 2 54  ? 74.737  57.821  41.830 1.00 103.95 ? 54  ASN B C   1 
ATOM   494  O  O   . ASN B 2 54  ? 74.790  58.495  42.838 1.00 152.12 ? 54  ASN B O   1 
ATOM   495  C  CB  . ASN B 2 54  ? 76.883  57.857  40.465 1.00 181.98 ? 54  ASN B CB  1 
ATOM   496  C  CG  . ASN B 2 54  ? 78.196  57.152  40.181 1.00 311.39 ? 54  ASN B CG  1 
ATOM   497  O  OD1 . ASN B 2 54  ? 78.517  56.160  40.833 1.00 254.32 ? 54  ASN B OD1 1 
ATOM   498  N  ND2 . ASN B 2 54  ? 78.959  57.649  39.216 1.00 399.38 ? 54  ASN B ND2 1 
ATOM   499  N  N   . GLY B 2 55  ? 73.632  57.715  41.116 1.00 167.16 ? 55  GLY B N   1 
ATOM   500  C  CA  . GLY B 2 55  ? 72.376  58.301  41.540 1.00 166.53 ? 55  GLY B CA  1 
ATOM   501  C  C   . GLY B 2 55  ? 71.913  57.748  42.867 1.00 112.80 ? 55  GLY B C   1 
ATOM   502  O  O   . GLY B 2 55  ? 71.457  58.549  43.664 1.00 121.94 ? 55  GLY B O   1 
ATOM   503  N  N   . VAL B 2 56  ? 72.029  56.423  43.098 1.00 119.54 ? 56  VAL B N   1 
ATOM   504  C  CA  . VAL B 2 56  ? 71.773  55.848  44.423 1.00 142.57 ? 56  VAL B CA  1 
ATOM   505  C  C   . VAL B 2 56  ? 72.736  56.402  45.472 1.00 109.32 ? 56  VAL B C   1 
ATOM   506  O  O   . VAL B 2 56  ? 72.302  56.840  46.514 1.00 110.35 ? 56  VAL B O   1 
ATOM   507  C  CB  . VAL B 2 56  ? 71.816  54.318  44.393 1.00 169.55 ? 56  VAL B CB  1 
ATOM   508  C  CG1 . VAL B 2 56  ? 71.903  53.705  45.795 1.00 193.12 ? 56  VAL B CG1 1 
ATOM   509  C  CG2 . VAL B 2 56  ? 70.616  53.791  43.608 1.00 232.00 ? 56  VAL B CG2 1 
ATOM   510  N  N   . ALA B 2 57  ? 74.026  56.449  45.189 1.00 137.65 ? 57  ALA B N   1 
ATOM   511  C  CA  . ALA B 2 57  ? 75.023  56.928  46.146 1.00 131.32 ? 57  ALA B CA  1 
ATOM   512  C  C   . ALA B 2 57  ? 74.839  58.404  46.526 1.00 88.51  ? 57  ALA B C   1 
ATOM   513  O  O   . ALA B 2 57  ? 75.197  58.783  47.623 1.00 145.87 ? 57  ALA B O   1 
ATOM   514  C  CB  . ALA B 2 57  ? 76.403  56.684  45.567 1.00 180.31 ? 57  ALA B CB  1 
ATOM   515  N  N   . ILE B 2 58  ? 74.275  59.249  45.644 1.00 114.13 ? 58  ILE B N   1 
ATOM   516  C  CA  . ILE B 2 58  ? 73.915  60.634  45.923 1.00 139.86 ? 58  ILE B CA  1 
ATOM   517  C  C   . ILE B 2 58  ? 72.840  60.656  47.000 1.00 131.87 ? 58  ILE B C   1 
ATOM   518  O  O   . ILE B 2 58  ? 72.896  61.529  47.864 1.00 122.21 ? 58  ILE B O   1 
ATOM   519  C  CB  . ILE B 2 58  ? 73.497  61.373  44.615 1.00 146.44 ? 58  ILE B CB  1 
ATOM   520  C  CG1 . ILE B 2 58  ? 74.723  61.669  43.747 1.00 220.95 ? 58  ILE B CG1 1 
ATOM   521  C  CG2 . ILE B 2 58  ? 72.687  62.639  44.840 1.00 138.09 ? 58  ILE B CG2 1 
ATOM   522  C  CD1 . ILE B 2 58  ? 75.589  62.858  44.200 1.00 261.90 ? 58  ILE B CD1 1 
ATOM   523  N  N   . ILE B 2 59  ? 71.847  59.755  46.915 1.00 99.68  ? 59  ILE B N   1 
ATOM   524  C  CA  . ILE B 2 59  ? 70.697  59.804  47.805 1.00 107.36 ? 59  ILE B CA  1 
ATOM   525  C  C   . ILE B 2 59  ? 71.021  58.989  49.072 1.00 119.89 ? 59  ILE B C   1 
ATOM   526  O  O   . ILE B 2 59  ? 71.024  59.561  50.145 1.00 163.78 ? 59  ILE B O   1 
ATOM   527  C  CB  . ILE B 2 59  ? 69.354  59.493  47.077 1.00 108.40 ? 59  ILE B CB  1 
ATOM   528  C  CG1 . ILE B 2 59  ? 68.194  59.538  48.063 1.00 132.18 ? 59  ILE B CG1 1 
ATOM   529  C  CG2 . ILE B 2 59  ? 69.359  58.159  46.318 1.00 151.92 ? 59  ILE B CG2 1 
ATOM   530  C  CD1 . ILE B 2 59  ? 66.834  59.474  47.430 1.00 185.76 ? 59  ILE B CD1 1 
ATOM   531  N  N   . VAL B 2 60  ? 71.258  57.678  49.012 1.00 146.70 ? 60  VAL B N   1 
ATOM   532  C  CA  . VAL B 2 60  ? 71.515  56.869  50.204 1.00 146.20 ? 60  VAL B CA  1 
ATOM   533  C  C   . VAL B 2 60  ? 72.731  57.412  50.958 1.00 144.02 ? 60  VAL B C   1 
ATOM   534  O  O   . VAL B 2 60  ? 72.797  57.331  52.178 1.00 233.28 ? 60  VAL B O   1 
ATOM   535  C  CB  . VAL B 2 60  ? 71.710  55.364  49.864 1.00 206.78 ? 60  VAL B CB  1 
ATOM   536  C  CG1 . VAL B 2 60  ? 73.065  55.003  49.260 1.00 242.36 ? 60  VAL B CG1 1 
ATOM   537  C  CG2 . VAL B 2 60  ? 71.530  54.475  51.069 1.00 235.99 ? 60  VAL B CG2 1 
ATOM   538  N  N   . GLY B 2 61  ? 73.707  57.959  50.242 1.00 158.67 ? 61  GLY B N   1 
ATOM   539  C  CA  . GLY B 2 61  ? 74.904  58.517  50.845 1.00 184.41 ? 61  GLY B CA  1 
ATOM   540  C  C   . GLY B 2 61  ? 74.719  59.871  51.516 1.00 176.46 ? 61  GLY B C   1 
ATOM   541  O  O   . GLY B 2 61  ? 75.689  60.347  52.096 1.00 168.95 ? 61  GLY B O   1 
ATOM   542  N  N   . THR B 2 62  ? 73.526  60.483  51.458 1.00 125.77 ? 62  THR B N   1 
ATOM   543  C  CA  . THR B 2 62  ? 73.270  61.782  52.069 1.00 143.17 ? 62  THR B CA  1 
ATOM   544  C  C   . THR B 2 62  ? 72.070  61.755  52.991 1.00 105.28 ? 62  THR B C   1 
ATOM   545  O  O   . THR B 2 62  ? 71.944  62.653  53.803 1.00 133.74 ? 62  THR B O   1 
ATOM   546  C  CB  . THR B 2 62  ? 73.036  62.905  51.035 1.00 191.09 ? 62  THR B CB  1 
ATOM   547  O  OG1 . THR B 2 62  ? 71.957  62.590  50.162 1.00 199.59 ? 62  THR B OG1 1 
ATOM   548  C  CG2 . THR B 2 62  ? 74.215  63.194  50.135 1.00 198.99 ? 62  THR B CG2 1 
ATOM   549  N  N   . ILE B 2 63  ? 71.165  60.770  52.870 1.00 173.69 ? 63  ILE B N   1 
ATOM   550  C  CA  . ILE B 2 63  ? 70.076  60.563  53.825 1.00 191.50 ? 63  ILE B CA  1 
ATOM   551  C  C   . ILE B 2 63  ? 70.661  60.238  55.194 1.00 181.15 ? 63  ILE B C   1 
ATOM   552  O  O   . ILE B 2 63  ? 70.281  60.837  56.207 1.00 190.57 ? 63  ILE B O   1 
ATOM   553  C  CB  . ILE B 2 63  ? 69.086  59.469  53.363 1.00 124.69 ? 63  ILE B CB  1 
ATOM   554  C  CG1 . ILE B 2 63  ? 68.283  60.006  52.175 1.00 173.12 ? 63  ILE B CG1 1 
ATOM   555  C  CG2 . ILE B 2 63  ? 68.165  59.095  54.498 1.00 117.60 ? 63  ILE B CG2 1 
ATOM   556  C  CD1 . ILE B 2 63  ? 67.543  58.960  51.399 1.00 237.57 ? 63  ILE B CD1 1 
ATOM   557  N  N   . ILE B 2 64  ? 71.586  59.273  55.196 1.00 119.53 ? 64  ILE B N   1 
ATOM   558  C  CA  . ILE B 2 64  ? 71.947  58.583  56.419 1.00 138.46 ? 64  ILE B CA  1 
ATOM   559  C  C   . ILE B 2 64  ? 72.848  59.433  57.332 1.00 159.52 ? 64  ILE B C   1 
ATOM   560  O  O   . ILE B 2 64  ? 72.623  59.459  58.543 1.00 200.40 ? 64  ILE B O   1 
ATOM   561  C  CB  . ILE B 2 64  ? 72.501  57.200  56.043 1.00 131.13 ? 64  ILE B CB  1 
ATOM   562  C  CG1 . ILE B 2 64  ? 71.326  56.298  55.651 1.00 138.62 ? 64  ILE B CG1 1 
ATOM   563  C  CG2 . ILE B 2 64  ? 73.314  56.594  57.143 1.00 144.69 ? 64  ILE B CG2 1 
ATOM   564  C  CD1 . ILE B 2 64  ? 71.719  54.891  55.243 1.00 227.23 ? 64  ILE B CD1 1 
ATOM   565  N  N   . GLY B 2 65  ? 73.849  60.115  56.786 1.00 155.46 ? 65  GLY B N   1 
ATOM   566  C  CA  . GLY B 2 65  ? 74.698  61.096  57.479 1.00 188.62 ? 65  GLY B CA  1 
ATOM   567  C  C   . GLY B 2 65  ? 74.970  60.850  58.974 1.00 190.34 ? 65  GLY B C   1 
ATOM   568  O  O   . GLY B 2 65  ? 75.470  59.784  59.361 1.00 135.22 ? 65  GLY B O   1 
ATOM   569  N  N   . SER B 2 66  ? 74.654  61.863  59.808 1.00 231.85 ? 66  SER B N   1 
ATOM   570  C  CA  . SER B 2 66  ? 74.778  61.759  61.256 1.00 189.70 ? 66  SER B CA  1 
ATOM   571  C  C   . SER B 2 66  ? 73.523  61.189  61.891 1.00 110.93 ? 66  SER B C   1 
ATOM   572  O  O   . SER B 2 66  ? 73.620  60.651  62.970 1.00 104.37 ? 66  SER B O   1 
ATOM   573  C  CB  . SER B 2 66  ? 75.079  63.112  61.851 1.00 228.31 ? 66  SER B CB  1 
ATOM   574  O  OG  . SER B 2 66  ? 73.977  64.015  61.795 1.00 138.19 ? 66  SER B OG  1 
ATOM   575  N  N   . GLY B 2 67  ? 72.359  61.351  61.228 1.00 160.08 ? 67  GLY B N   1 
ATOM   576  C  CA  . GLY B 2 67  ? 71.025  61.148  61.791 1.00 180.26 ? 67  GLY B CA  1 
ATOM   577  C  C   . GLY B 2 67  ? 70.912  59.869  62.634 1.00 144.82 ? 67  GLY B C   1 
ATOM   578  O  O   . GLY B 2 67  ? 70.720  59.927  63.843 1.00 115.61 ? 67  GLY B O   1 
ATOM   579  N  N   . ILE B 2 68  ? 71.073  58.711  62.007 1.00 144.95 ? 68  ILE B N   1 
ATOM   580  C  CA  . ILE B 2 68  ? 70.834  57.439  62.682 1.00 175.89 ? 68  ILE B CA  1 
ATOM   581  C  C   . ILE B 2 68  ? 71.779  57.168  63.861 1.00 194.77 ? 68  ILE B C   1 
ATOM   582  O  O   . ILE B 2 68  ? 71.381  56.512  64.822 1.00 166.95 ? 68  ILE B O   1 
ATOM   583  C  CB  . ILE B 2 68  ? 70.904  56.288  61.658 1.00 180.70 ? 68  ILE B CB  1 
ATOM   584  C  CG1 . ILE B 2 68  ? 70.326  54.990  62.231 1.00 166.49 ? 68  ILE B CG1 1 
ATOM   585  C  CG2 . ILE B 2 68  ? 72.299  56.116  61.065 1.00 133.76 ? 68  ILE B CG2 1 
ATOM   586  C  CD1 . ILE B 2 68  ? 68.900  55.179  62.794 1.00 159.44 ? 68  ILE B CD1 1 
ATOM   587  N  N   . PHE B 2 69  ? 73.013  57.668  63.814 1.00 179.20 ? 69  PHE B N   1 
ATOM   588  C  CA  . PHE B 2 69  ? 73.984  57.390  64.850 1.00 145.84 ? 69  PHE B CA  1 
ATOM   589  C  C   . PHE B 2 69  ? 73.867  58.313  66.068 1.00 160.53 ? 69  PHE B C   1 
ATOM   590  O  O   . PHE B 2 69  ? 74.538  58.030  67.044 1.00 205.06 ? 69  PHE B O   1 
ATOM   591  C  CB  . PHE B 2 69  ? 75.369  57.590  64.268 1.00 189.59 ? 69  PHE B CB  1 
ATOM   592  C  CG  . PHE B 2 69  ? 75.720  56.793  63.046 1.00 151.39 ? 69  PHE B CG  1 
ATOM   593  C  CD1 . PHE B 2 69  ? 76.032  55.461  63.163 1.00 159.39 ? 69  PHE B CD1 1 
ATOM   594  C  CD2 . PHE B 2 69  ? 75.769  57.386  61.804 1.00 158.07 ? 69  PHE B CD2 1 
ATOM   595  C  CE1 . PHE B 2 69  ? 76.424  54.719  62.064 1.00 178.90 ? 69  PHE B CE1 1 
ATOM   596  C  CE2 . PHE B 2 69  ? 76.145  56.637  60.710 1.00 242.10 ? 69  PHE B CE2 1 
ATOM   597  C  CZ  . PHE B 2 69  ? 76.469  55.309  60.847 1.00 196.69 ? 69  PHE B CZ  1 
ATOM   598  N  N   . VAL B 2 70  ? 73.084  59.411  66.012 1.00 143.72 ? 70  VAL B N   1 
ATOM   599  C  CA  . VAL B 2 70  ? 72.950  60.356  67.123 1.00 166.18 ? 70  VAL B CA  1 
ATOM   600  C  C   . VAL B 2 70  ? 71.474  60.628  67.525 1.00 143.35 ? 70  VAL B C   1 
ATOM   601  O  O   . VAL B 2 70  ? 71.181  60.982  68.667 1.00 110.50 ? 70  VAL B O   1 
ATOM   602  C  CB  . VAL B 2 70  ? 73.756  61.636  66.806 1.00 152.13 ? 70  VAL B CB  1 
ATOM   603  C  CG1 . VAL B 2 70  ? 73.051  62.522  65.806 1.00 185.68 ? 70  VAL B CG1 1 
ATOM   604  C  CG2 . VAL B 2 70  ? 74.052  62.426  68.066 1.00 242.44 ? 70  VAL B CG2 1 
ATOM   605  N  N   . THR B 2 71  ? 70.509  60.471  66.611 1.00 152.66 ? 71  THR B N   1 
ATOM   606  C  CA  . THR B 2 71  ? 69.098  60.813  66.832 1.00 182.87 ? 71  THR B CA  1 
ATOM   607  C  C   . THR B 2 71  ? 68.302  59.876  67.764 1.00 188.04 ? 71  THR B C   1 
ATOM   608  O  O   . THR B 2 71  ? 67.397  60.373  68.424 1.00 148.90 ? 71  THR B O   1 
ATOM   609  C  CB  . THR B 2 71  ? 68.308  60.837  65.506 1.00 189.00 ? 71  THR B CB  1 
ATOM   610  O  OG1 . THR B 2 71  ? 68.955  61.739  64.616 1.00 192.07 ? 71  THR B OG1 1 
ATOM   611  C  CG2 . THR B 2 71  ? 66.855  61.265  65.621 1.00 184.33 ? 71  THR B CG2 1 
ATOM   612  N  N   . PRO B 2 72  ? 68.520  58.535  67.857 1.00 148.17 ? 72  PRO B N   1 
ATOM   613  C  CA  . PRO B 2 72  ? 67.569  57.640  68.545 1.00 156.83 ? 72  PRO B CA  1 
ATOM   614  C  C   . PRO B 2 72  ? 67.112  58.044  69.948 1.00 148.76 ? 72  PRO B C   1 
ATOM   615  O  O   . PRO B 2 72  ? 65.947  57.855  70.263 1.00 153.86 ? 72  PRO B O   1 
ATOM   616  C  CB  . PRO B 2 72  ? 68.340  56.297  68.614 1.00 215.61 ? 72  PRO B CB  1 
ATOM   617  C  CG  . PRO B 2 72  ? 69.218  56.340  67.386 1.00 185.75 ? 72  PRO B CG  1 
ATOM   618  C  CD  . PRO B 2 72  ? 69.644  57.786  67.288 1.00 111.31 ? 72  PRO B CD  1 
ATOM   619  N  N   . THR B 2 73  ? 68.015  58.615  70.765 1.00 173.03 ? 73  THR B N   1 
ATOM   620  C  CA  . THR B 2 73  ? 67.689  59.195  72.062 1.00 174.20 ? 73  THR B CA  1 
ATOM   621  C  C   . THR B 2 73  ? 66.494  60.171  71.965 1.00 155.94 ? 73  THR B C   1 
ATOM   622  O  O   . THR B 2 73  ? 65.605  60.148  72.822 1.00 170.76 ? 73  THR B O   1 
ATOM   623  C  CB  . THR B 2 73  ? 68.951  59.828  72.693 1.00 262.99 ? 73  THR B CB  1 
ATOM   624  O  OG1 . THR B 2 73  ? 68.695  60.020  74.087 1.00 419.66 ? 73  THR B OG1 1 
ATOM   625  C  CG2 . THR B 2 73  ? 69.411  61.144  72.087 1.00 240.10 ? 73  THR B CG2 1 
ATOM   626  N  N   . GLY B 2 74  ? 66.477  61.034  70.936 1.00 196.56 ? 74  GLY B N   1 
ATOM   627  C  CA  . GLY B 2 74  ? 65.445  62.036  70.700 1.00 238.61 ? 74  GLY B CA  1 
ATOM   628  C  C   . GLY B 2 74  ? 64.146  61.494  70.100 1.00 196.22 ? 74  GLY B C   1 
ATOM   629  O  O   . GLY B 2 74  ? 63.124  62.175  70.197 1.00 238.77 ? 74  GLY B O   1 
ATOM   630  N  N   . VAL B 2 75  ? 64.173  60.293  69.502 1.00 132.84 ? 75  VAL B N   1 
ATOM   631  C  CA  . VAL B 2 75  ? 62.939  59.545  69.245 1.00 209.70 ? 75  VAL B CA  1 
ATOM   632  C  C   . VAL B 2 75  ? 62.366  58.958  70.542 1.00 251.59 ? 75  VAL B C   1 
ATOM   633  O  O   . VAL B 2 75  ? 61.192  59.136  70.868 1.00 188.37 ? 75  VAL B O   1 
ATOM   634  C  CB  . VAL B 2 75  ? 63.152  58.422  68.216 1.00 227.05 ? 75  VAL B CB  1 
ATOM   635  C  CG1 . VAL B 2 75  ? 61.835  57.838  67.750 1.00 188.67 ? 75  VAL B CG1 1 
ATOM   636  C  CG2 . VAL B 2 75  ? 63.936  58.911  67.018 1.00 280.14 ? 75  VAL B CG2 1 
ATOM   637  N  N   . LEU B 2 76  ? 63.225  58.253  71.283 1.00 266.67 ? 76  LEU B N   1 
ATOM   638  C  CA  . LEU B 2 76  ? 62.839  57.498  72.464 1.00 210.01 ? 76  LEU B CA  1 
ATOM   639  C  C   . LEU B 2 76  ? 62.356  58.419  73.593 1.00 182.18 ? 76  LEU B C   1 
ATOM   640  O  O   . LEU B 2 76  ? 61.512  58.014  74.367 1.00 183.21 ? 76  LEU B O   1 
ATOM   641  C  CB  . LEU B 2 76  ? 64.049  56.649  72.865 1.00 206.58 ? 76  LEU B CB  1 
ATOM   642  C  CG  . LEU B 2 76  ? 63.846  55.658  74.002 1.00 220.55 ? 76  LEU B CG  1 
ATOM   643  C  CD1 . LEU B 2 76  ? 62.806  54.627  73.645 1.00 210.22 ? 76  LEU B CD1 1 
ATOM   644  C  CD2 . LEU B 2 76  ? 65.147  54.987  74.351 1.00 245.93 ? 76  LEU B CD2 1 
ATOM   645  N  N   . LYS B 2 77  ? 62.838  59.662  73.697 1.00 172.97 ? 77  LYS B N   1 
ATOM   646  C  CA  . LYS B 2 77  ? 62.353  60.614  74.691 1.00 190.78 ? 77  LYS B CA  1 
ATOM   647  C  C   . LYS B 2 77  ? 60.856  60.919  74.536 1.00 199.64 ? 77  LYS B C   1 
ATOM   648  O  O   . LYS B 2 77  ? 60.148  61.054  75.539 1.00 225.75 ? 77  LYS B O   1 
ATOM   649  C  CB  . LYS B 2 77  ? 63.199  61.891  74.616 1.00 242.32 ? 77  LYS B CB  1 
ATOM   650  C  CG  . LYS B 2 77  ? 63.030  62.826  75.798 1.00 317.35 ? 77  LYS B CG  1 
ATOM   651  C  CD  . LYS B 2 77  ? 64.116  63.899  75.885 1.00 299.97 ? 77  LYS B CD  1 
ATOM   652  C  CE  . LYS B 2 77  ? 64.005  64.984  74.834 1.00 312.65 ? 77  LYS B CE  1 
ATOM   653  N  NZ  . LYS B 2 77  ? 62.800  65.842  75.015 1.00 361.67 ? 77  LYS B NZ  1 
ATOM   654  N  N   . GLU B 2 78  ? 60.368  61.021  73.287 1.00 216.25 ? 78  GLU B N   1 
ATOM   655  C  CA  . GLU B 2 78  ? 58.973  61.322  72.993 1.00 245.98 ? 78  GLU B CA  1 
ATOM   656  C  C   . GLU B 2 78  ? 58.130  60.057  72.782 1.00 263.02 ? 78  GLU B C   1 
ATOM   657  O  O   . GLU B 2 78  ? 56.926  60.094  73.029 1.00 313.14 ? 78  GLU B O   1 
ATOM   658  C  CB  . GLU B 2 78  ? 58.913  62.252  71.780 1.00 297.62 ? 78  GLU B CB  1 
ATOM   659  C  CG  . GLU B 2 78  ? 59.739  63.526  71.913 1.00 359.86 ? 78  GLU B CG  1 
ATOM   660  C  CD  . GLU B 2 78  ? 59.621  64.272  73.236 1.00 372.01 ? 78  GLU B CD  1 
ATOM   661  O  OE1 . GLU B 2 78  ? 58.506  64.354  73.785 1.00 376.20 ? 78  GLU B OE1 1 
ATOM   662  O  OE2 . GLU B 2 78  ? 60.643  64.777  73.715 1.00 353.74 ? 78  GLU B OE2 1 
ATOM   663  N  N   . ALA B 2 79  ? 58.731  58.944  72.336 1.00 204.64 ? 79  ALA B N   1 
ATOM   664  C  CA  . ALA B 2 79  ? 58.069  57.642  72.284 1.00 246.49 ? 79  ALA B CA  1 
ATOM   665  C  C   . ALA B 2 79  ? 57.900  57.010  73.675 1.00 251.77 ? 79  ALA B C   1 
ATOM   666  O  O   . ALA B 2 79  ? 56.916  56.316  73.936 1.00 254.30 ? 79  ALA B O   1 
ATOM   667  C  CB  . ALA B 2 79  ? 58.868  56.743  71.375 1.00 240.57 ? 79  ALA B CB  1 
ATOM   668  N  N   . GLY B 2 80  ? 58.880  57.226  74.568 1.00 231.86 ? 80  GLY B N   1 
ATOM   669  C  CA  . GLY B 2 80  ? 58.902  56.721  75.938 1.00 252.58 ? 80  GLY B CA  1 
ATOM   670  C  C   . GLY B 2 80  ? 59.006  55.196  76.092 1.00 241.51 ? 80  GLY B C   1 
ATOM   671  O  O   . GLY B 2 80  ? 58.928  54.705  77.215 1.00 247.94 ? 80  GLY B O   1 
ATOM   672  N  N   . SER B 2 81  ? 59.182  54.438  74.993 1.00 213.66 ? 81  SER B N   1 
ATOM   673  C  CA  . SER B 2 81  ? 59.137  52.981  75.035 1.00 209.23 ? 81  SER B CA  1 
ATOM   674  C  C   . SER B 2 81  ? 59.886  52.347  73.872 1.00 183.73 ? 81  SER B C   1 
ATOM   675  O  O   . SER B 2 81  ? 59.702  52.798  72.749 1.00 196.26 ? 81  SER B O   1 
ATOM   676  C  CB  . SER B 2 81  ? 57.725  52.495  75.008 1.00 240.52 ? 81  SER B CB  1 
ATOM   677  O  OG  . SER B 2 81  ? 57.677  51.081  75.160 1.00 320.22 ? 81  SER B OG  1 
ATOM   678  N  N   . PRO B 2 82  ? 60.715  51.286  74.069 1.00 229.45 ? 82  PRO B N   1 
ATOM   679  C  CA  . PRO B 2 82  ? 61.414  50.628  72.959 1.00 223.72 ? 82  PRO B CA  1 
ATOM   680  C  C   . PRO B 2 82  ? 60.485  49.904  71.981 1.00 194.01 ? 82  PRO B C   1 
ATOM   681  O  O   . PRO B 2 82  ? 60.904  49.635  70.859 1.00 196.20 ? 82  PRO B O   1 
ATOM   682  C  CB  . PRO B 2 82  ? 62.386  49.645  73.643 1.00 221.79 ? 82  PRO B CB  1 
ATOM   683  C  CG  . PRO B 2 82  ? 61.726  49.345  74.964 1.00 236.47 ? 82  PRO B CG  1 
ATOM   684  C  CD  . PRO B 2 82  ? 61.026  50.637  75.352 1.00 251.81 ? 82  PRO B CD  1 
ATOM   685  N  N   . GLY B 2 83  ? 59.237  49.608  72.385 1.00 220.39 ? 83  GLY B N   1 
ATOM   686  C  CA  . GLY B 2 83  ? 58.200  49.125  71.481 1.00 283.44 ? 83  GLY B CA  1 
ATOM   687  C  C   . GLY B 2 83  ? 57.799  50.183  70.452 1.00 206.72 ? 83  GLY B C   1 
ATOM   688  O  O   . GLY B 2 83  ? 57.992  49.954  69.239 1.00 124.45 ? 83  GLY B O   1 
ATOM   689  N  N   . LEU B 2 84  ? 57.252  51.319  70.952 1.00 146.20 ? 84  LEU B N   1 
ATOM   690  C  CA  . LEU B 2 84  ? 56.703  52.342  70.066 1.00 235.33 ? 84  LEU B CA  1 
ATOM   691  C  C   . LEU B 2 84  ? 57.810  53.058  69.267 1.00 210.60 ? 84  LEU B C   1 
ATOM   692  O  O   . LEU B 2 84  ? 57.576  53.505  68.139 1.00 136.56 ? 84  LEU B O   1 
ATOM   693  C  CB  . LEU B 2 84  ? 55.825  53.325  70.851 1.00 250.71 ? 84  LEU B CB  1 
ATOM   694  C  CG  . LEU B 2 84  ? 55.060  54.315  69.959 1.00 260.37 ? 84  LEU B CG  1 
ATOM   695  C  CD1 . LEU B 2 84  ? 53.633  54.537  70.437 1.00 332.54 ? 84  LEU B CD1 1 
ATOM   696  C  CD2 . LEU B 2 84  ? 55.758  55.662  69.893 1.00 237.54 ? 84  LEU B CD2 1 
ATOM   697  N  N   . ALA B 2 85  ? 59.030  53.158  69.801 1.00 216.99 ? 85  ALA B N   1 
ATOM   698  C  CA  . ALA B 2 85  ? 60.136  53.725  69.035 1.00 244.26 ? 85  ALA B CA  1 
ATOM   699  C  C   . ALA B 2 85  ? 60.341  52.960  67.719 1.00 184.43 ? 85  ALA B C   1 
ATOM   700  O  O   . ALA B 2 85  ? 60.442  53.570  66.655 1.00 255.67 ? 85  ALA B O   1 
ATOM   701  C  CB  . ALA B 2 85  ? 61.384  53.741  69.893 1.00 330.94 ? 85  ALA B CB  1 
ATOM   702  N  N   . LEU B 2 86  ? 60.394  51.623  67.763 1.00 139.29 ? 86  LEU B N   1 
ATOM   703  C  CA  . LEU B 2 86  ? 60.521  50.833  66.548 1.00 185.99 ? 86  LEU B CA  1 
ATOM   704  C  C   . LEU B 2 86  ? 59.279  50.934  65.641 1.00 203.27 ? 86  LEU B C   1 
ATOM   705  O  O   . LEU B 2 86  ? 59.365  50.569  64.464 1.00 190.50 ? 86  LEU B O   1 
ATOM   706  C  CB  . LEU B 2 86  ? 60.827  49.381  66.936 1.00 221.14 ? 86  LEU B CB  1 
ATOM   707  C  CG  . LEU B 2 86  ? 62.198  49.134  67.570 1.00 175.91 ? 86  LEU B CG  1 
ATOM   708  C  CD1 . LEU B 2 86  ? 62.410  47.661  67.890 1.00 210.11 ? 86  LEU B CD1 1 
ATOM   709  C  CD2 . LEU B 2 86  ? 63.315  49.575  66.664 1.00 167.22 ? 86  LEU B CD2 1 
ATOM   710  N  N   . VAL B 2 87  ? 58.133  51.417  66.147 1.00 187.40 ? 87  VAL B N   1 
ATOM   711  C  CA  . VAL B 2 87  ? 56.994  51.741  65.297 1.00 206.04 ? 87  VAL B CA  1 
ATOM   712  C  C   . VAL B 2 87  ? 57.266  53.041  64.538 1.00 201.14 ? 87  VAL B C   1 
ATOM   713  O  O   . VAL B 2 87  ? 57.156  53.024  63.311 1.00 272.06 ? 87  VAL B O   1 
ATOM   714  C  CB  . VAL B 2 87  ? 55.663  51.768  66.084 1.00 284.40 ? 87  VAL B CB  1 
ATOM   715  C  CG1 . VAL B 2 87  ? 54.479  52.346  65.312 1.00 308.69 ? 87  VAL B CG1 1 
ATOM   716  C  CG2 . VAL B 2 87  ? 55.335  50.368  66.589 1.00 374.51 ? 87  VAL B CG2 1 
ATOM   717  N  N   . VAL B 2 88  ? 57.597  54.163  65.207 1.00 192.37 ? 88  VAL B N   1 
ATOM   718  C  CA  . VAL B 2 88  ? 57.744  55.449  64.505 1.00 214.81 ? 88  VAL B CA  1 
ATOM   719  C  C   . VAL B 2 88  ? 58.908  55.417  63.516 1.00 182.20 ? 88  VAL B C   1 
ATOM   720  O  O   . VAL B 2 88  ? 58.841  56.087  62.501 1.00 190.38 ? 88  VAL B O   1 
ATOM   721  C  CB  . VAL B 2 88  ? 57.850  56.672  65.438 1.00 204.04 ? 88  VAL B CB  1 
ATOM   722  C  CG1 . VAL B 2 88  ? 56.589  56.829  66.255 1.00 298.23 ? 88  VAL B CG1 1 
ATOM   723  C  CG2 . VAL B 2 88  ? 59.037  56.618  66.362 1.00 229.37 ? 88  VAL B CG2 1 
ATOM   724  N  N   . TRP B 2 89  ? 59.950  54.635  63.765 1.00 182.18 ? 89  TRP B N   1 
ATOM   725  C  CA  . TRP B 2 89  ? 61.008  54.436  62.782 1.00 216.18 ? 89  TRP B CA  1 
ATOM   726  C  C   . TRP B 2 89  ? 60.529  53.812  61.468 1.00 223.10 ? 89  TRP B C   1 
ATOM   727  O  O   . TRP B 2 89  ? 61.072  54.147  60.420 1.00 205.62 ? 89  TRP B O   1 
ATOM   728  C  CB  . TRP B 2 89  ? 62.127  53.589  63.394 1.00 235.68 ? 89  TRP B CB  1 
ATOM   729  C  CG  . TRP B 2 89  ? 63.084  54.388  64.232 1.00 246.80 ? 89  TRP B CG  1 
ATOM   730  C  CD1 . TRP B 2 89  ? 63.304  54.264  65.573 1.00 266.92 ? 89  TRP B CD1 1 
ATOM   731  C  CD2 . TRP B 2 89  ? 63.980  55.433  63.782 1.00 168.90 ? 89  TRP B CD2 1 
ATOM   732  N  NE1 . TRP B 2 89  ? 64.264  55.150  65.985 1.00 207.71 ? 89  TRP B NE1 1 
ATOM   733  C  CE2 . TRP B 2 89  ? 64.692  55.879  64.903 1.00 162.14 ? 89  TRP B CE2 1 
ATOM   734  C  CE3 . TRP B 2 89  ? 64.241  56.025  62.553 1.00 199.48 ? 89  TRP B CE3 1 
ATOM   735  C  CZ2 . TRP B 2 89  ? 65.649  56.882  64.807 1.00 189.26 ? 89  TRP B CZ2 1 
ATOM   736  C  CZ3 . TRP B 2 89  ? 65.177  57.027  62.462 1.00 240.27 ? 89  TRP B CZ3 1 
ATOM   737  C  CH2 . TRP B 2 89  ? 65.876  57.448  63.579 1.00 220.88 ? 89  TRP B CH2 1 
ATOM   738  N  N   . ALA B 2 90  ? 59.539  52.906  61.512 1.00 205.58 ? 90  ALA B N   1 
ATOM   739  C  CA  . ALA B 2 90  ? 58.930  52.341  60.311 1.00 182.37 ? 90  ALA B CA  1 
ATOM   740  C  C   . ALA B 2 90  ? 57.924  53.314  59.698 1.00 171.37 ? 90  ALA B C   1 
ATOM   741  O  O   . ALA B 2 90  ? 57.949  53.534  58.482 1.00 232.35 ? 90  ALA B O   1 
ATOM   742  C  CB  . ALA B 2 90  ? 58.289  51.018  60.651 1.00 231.66 ? 90  ALA B CB  1 
ATOM   743  N  N   . ALA B 2 91  ? 57.047  53.906  60.524 1.00 175.77 ? 91  ALA B N   1 
ATOM   744  C  CA  . ALA B 2 91  ? 55.977  54.795  60.071 1.00 241.72 ? 91  ALA B CA  1 
ATOM   745  C  C   . ALA B 2 91  ? 56.516  56.072  59.400 1.00 224.55 ? 91  ALA B C   1 
ATOM   746  O  O   . ALA B 2 91  ? 56.036  56.477  58.352 1.00 263.98 ? 91  ALA B O   1 
ATOM   747  C  CB  . ALA B 2 91  ? 55.066  55.112  61.238 1.00 285.50 ? 91  ALA B CB  1 
ATOM   748  N  N   . CYS B 2 92  ? 57.522  56.713  59.983 1.00 140.85 ? 92  CYS B N   1 
ATOM   749  C  CA  . CYS B 2 92  ? 58.221  57.807  59.324 1.00 191.90 ? 92  CYS B CA  1 
ATOM   750  C  C   . CYS B 2 92  ? 58.938  57.366  58.036 1.00 171.02 ? 92  CYS B C   1 
ATOM   751  O  O   . CYS B 2 92  ? 59.060  58.149  57.091 1.00 148.22 ? 92  CYS B O   1 
ATOM   752  C  CB  . CYS B 2 92  ? 59.207  58.431  60.298 1.00 269.36 ? 92  CYS B CB  1 
ATOM   753  S  SG  . CYS B 2 92  ? 59.830  60.002  59.666 1.00 237.94 ? 92  CYS B SG  1 
ATOM   754  N  N   . GLY B 2 93  ? 59.381  56.107  57.962 1.00 171.16 ? 93  GLY B N   1 
ATOM   755  C  CA  . GLY B 2 93  ? 59.877  55.532  56.720 1.00 183.11 ? 93  GLY B CA  1 
ATOM   756  C  C   . GLY B 2 93  ? 58.805  55.524  55.634 1.00 187.82 ? 93  GLY B C   1 
ATOM   757  O  O   . GLY B 2 93  ? 59.061  56.018  54.541 1.00 153.19 ? 93  GLY B O   1 
ATOM   758  N  N   . VAL B 2 94  ? 57.606  54.996  55.948 1.00 173.40 ? 94  VAL B N   1 
ATOM   759  C  CA  . VAL B 2 94  ? 56.473  54.982  55.029 1.00 141.62 ? 94  VAL B CA  1 
ATOM   760  C  C   . VAL B 2 94  ? 56.177  56.405  54.541 1.00 183.32 ? 94  VAL B C   1 
ATOM   761  O  O   . VAL B 2 94  ? 56.066  56.584  53.330 1.00 241.26 ? 94  VAL B O   1 
ATOM   762  C  CB  . VAL B 2 94  ? 55.242  54.313  55.663 1.00 232.37 ? 94  VAL B CB  1 
ATOM   763  C  CG1 . VAL B 2 94  ? 53.948  54.542  54.884 1.00 332.99 ? 94  VAL B CG1 1 
ATOM   764  C  CG2 . VAL B 2 94  ? 55.500  52.823  55.841 1.00 335.66 ? 94  VAL B CG2 1 
ATOM   765  N  N   . PHE B 2 95  ? 56.056  57.402  55.442 1.00 123.04 ? 95  PHE B N   1 
ATOM   766  C  CA  . PHE B 2 95  ? 55.902  58.803  55.032 1.00 165.45 ? 95  PHE B CA  1 
ATOM   767  C  C   . PHE B 2 95  ? 56.987  59.255  54.033 1.00 137.09 ? 95  PHE B C   1 
ATOM   768  O  O   . PHE B 2 95  ? 56.705  59.912  53.026 1.00 138.04 ? 95  PHE B O   1 
ATOM   769  C  CB  . PHE B 2 95  ? 55.850  59.718  56.260 1.00 179.10 ? 95  PHE B CB  1 
ATOM   770  C  CG  . PHE B 2 95  ? 55.891  61.211  55.974 1.00 215.24 ? 95  PHE B CG  1 
ATOM   771  C  CD1 . PHE B 2 95  ? 57.105  61.872  55.858 1.00 250.05 ? 95  PHE B CD1 1 
ATOM   772  C  CD2 . PHE B 2 95  ? 54.742  61.984  55.798 1.00 257.32 ? 95  PHE B CD2 1 
ATOM   773  C  CE1 . PHE B 2 95  ? 57.180  63.239  55.600 1.00 197.23 ? 95  PHE B CE1 1 
ATOM   774  C  CE2 . PHE B 2 95  ? 54.822  63.355  55.536 1.00 235.58 ? 95  PHE B CE2 1 
ATOM   775  C  CZ  . PHE B 2 95  ? 56.040  63.991  55.445 1.00 164.80 ? 95  PHE B CZ  1 
ATOM   776  N  N   . SER B 2 96  ? 58.231  58.870  54.290 1.00 127.38 ? 96  SER B N   1 
ATOM   777  C  CA  . SER B 2 96  ? 59.339  59.172  53.390 1.00 206.67 ? 96  SER B CA  1 
ATOM   778  C  C   . SER B 2 96  ? 59.178  58.543  51.998 1.00 214.05 ? 96  SER B C   1 
ATOM   779  O  O   . SER B 2 96  ? 59.350  59.241  50.994 1.00 180.98 ? 96  SER B O   1 
ATOM   780  C  CB  . SER B 2 96  ? 60.656  58.768  54.005 1.00 219.76 ? 96  SER B CB  1 
ATOM   781  O  OG  . SER B 2 96  ? 60.770  59.356  55.282 1.00 149.91 ? 96  SER B OG  1 
ATOM   782  N  N   . ILE B 2 97  ? 58.851  57.245  51.903 1.00 149.87 ? 97  ILE B N   1 
ATOM   783  C  CA  . ILE B 2 97  ? 58.634  56.612  50.607 1.00 154.00 ? 97  ILE B CA  1 
ATOM   784  C  C   . ILE B 2 97  ? 57.535  57.358  49.864 1.00 162.92 ? 97  ILE B C   1 
ATOM   785  O  O   . ILE B 2 97  ? 57.782  57.691  48.709 1.00 205.04 ? 97  ILE B O   1 
ATOM   786  C  CB  . ILE B 2 97  ? 58.360  55.092  50.711 1.00 226.47 ? 97  ILE B CB  1 
ATOM   787  C  CG1 . ILE B 2 97  ? 59.672  54.312  50.833 1.00 204.99 ? 97  ILE B CG1 1 
ATOM   788  C  CG2 . ILE B 2 97  ? 57.529  54.526  49.562 1.00 249.58 ? 97  ILE B CG2 1 
ATOM   789  C  CD1 . ILE B 2 97  ? 60.242  54.319  52.218 1.00 231.20 ? 97  ILE B CD1 1 
ATOM   790  N  N   . VAL B 2 98  ? 56.366  57.617  50.480 1.00 117.25 ? 98  VAL B N   1 
ATOM   791  C  CA  . VAL B 2 98  ? 55.285  58.232  49.713 1.00 159.49 ? 98  VAL B CA  1 
ATOM   792  C  C   . VAL B 2 98  ? 55.657  59.647  49.282 1.00 170.70 ? 98  VAL B C   1 
ATOM   793  O  O   . VAL B 2 98  ? 55.309  60.038  48.164 1.00 252.75 ? 98  VAL B O   1 
ATOM   794  C  CB  . VAL B 2 98  ? 53.915  58.171  50.406 1.00 208.80 ? 98  VAL B CB  1 
ATOM   795  C  CG1 . VAL B 2 98  ? 53.524  56.719  50.674 1.00 289.02 ? 98  VAL B CG1 1 
ATOM   796  C  CG2 . VAL B 2 98  ? 53.845  58.976  51.668 1.00 166.66 ? 98  VAL B CG2 1 
ATOM   797  N  N   . GLY B 2 99  ? 56.382  60.378  50.122 1.00 117.75 ? 99  GLY B N   1 
ATOM   798  C  CA  . GLY B 2 99  ? 56.909  61.677  49.719 1.00 189.54 ? 99  GLY B CA  1 
ATOM   799  C  C   . GLY B 2 99  ? 57.831  61.660  48.493 1.00 225.47 ? 99  GLY B C   1 
ATOM   800  O  O   . GLY B 2 99  ? 57.591  62.362  47.493 1.00 116.82 ? 99  GLY B O   1 
ATOM   801  N  N   . ALA B 2 100 ? 58.871  60.818  48.574 1.00 151.36 ? 100 ALA B N   1 
ATOM   802  C  CA  . ALA B 2 100 ? 59.808  60.647  47.473 1.00 157.36 ? 100 ALA B CA  1 
ATOM   803  C  C   . ALA B 2 100 ? 59.125  60.125  46.199 1.00 181.92 ? 100 ALA B C   1 
ATOM   804  O  O   . ALA B 2 100 ? 59.499  60.553  45.104 1.00 110.38 ? 100 ALA B O   1 
ATOM   805  C  CB  . ALA B 2 100 ? 60.912  59.735  47.921 1.00 169.33 ? 100 ALA B CB  1 
ATOM   806  N  N   . LEU B 2 101 ? 58.115  59.240  46.327 1.00 191.67 ? 101 LEU B N   1 
ATOM   807  C  CA  . LEU B 2 101 ? 57.350  58.768  45.176 1.00 144.54 ? 101 LEU B CA  1 
ATOM   808  C  C   . LEU B 2 101 ? 56.548  59.889  44.526 1.00 128.25 ? 101 LEU B C   1 
ATOM   809  O  O   . LEU B 2 101 ? 56.400  59.858  43.289 1.00 189.94 ? 101 LEU B O   1 
ATOM   810  C  CB  . LEU B 2 101 ? 56.455  57.623  45.623 1.00 137.53 ? 101 LEU B CB  1 
ATOM   811  C  CG  . LEU B 2 101 ? 57.224  56.305  45.797 1.00 272.14 ? 101 LEU B CG  1 
ATOM   812  C  CD1 . LEU B 2 101 ? 56.268  55.207  46.238 1.00 397.08 ? 101 LEU B CD1 1 
ATOM   813  C  CD2 . LEU B 2 101 ? 57.965  55.872  44.529 1.00 297.32 ? 101 LEU B CD2 1 
ATOM   814  N  N   . CYS B 2 102 ? 56.095  60.884  45.298 1.00 131.35 ? 102 CYS B N   1 
ATOM   815  C  CA  . CYS B 2 102 ? 55.527  62.094  44.701 1.00 218.24 ? 102 CYS B CA  1 
ATOM   816  C  C   . CYS B 2 102 ? 56.598  62.879  43.927 1.00 173.10 ? 102 CYS B C   1 
ATOM   817  O  O   . CYS B 2 102 ? 56.313  63.437  42.865 1.00 142.28 ? 102 CYS B O   1 
ATOM   818  C  CB  . CYS B 2 102 ? 54.808  62.914  45.768 1.00 183.71 ? 102 CYS B CB  1 
ATOM   819  S  SG  . CYS B 2 102 ? 53.423  61.982  46.476 1.00 265.54 ? 102 CYS B SG  1 
ATOM   820  N  N   . TYR B 2 103 ? 57.827  62.940  44.452 1.00 129.40 ? 103 TYR B N   1 
ATOM   821  C  CA  . TYR B 2 103 ? 58.933  63.620  43.782 1.00 170.21 ? 103 TYR B CA  1 
ATOM   822  C  C   . TYR B 2 103 ? 59.455  62.870  42.556 1.00 156.21 ? 103 TYR B C   1 
ATOM   823  O  O   . TYR B 2 103 ? 59.949  63.499  41.626 1.00 245.04 ? 103 TYR B O   1 
ATOM   824  C  CB  . TYR B 2 103 ? 60.052  63.892  44.789 1.00 155.08 ? 103 TYR B CB  1 
ATOM   825  C  CG  . TYR B 2 103 ? 59.982  65.314  45.331 1.00 156.95 ? 103 TYR B CG  1 
ATOM   826  C  CD1 . TYR B 2 103 ? 58.915  65.708  46.115 1.00 177.63 ? 103 TYR B CD1 1 
ATOM   827  C  CD2 . TYR B 2 103 ? 60.976  66.257  45.055 1.00 156.32 ? 103 TYR B CD2 1 
ATOM   828  C  CE1 . TYR B 2 103 ? 58.839  66.999  46.613 1.00 164.96 ? 103 TYR B CE1 1 
ATOM   829  C  CE2 . TYR B 2 103 ? 60.928  67.540  45.570 1.00 134.09 ? 103 TYR B CE2 1 
ATOM   830  C  CZ  . TYR B 2 103 ? 59.841  67.909  46.339 1.00 167.81 ? 103 TYR B CZ  1 
ATOM   831  O  OH  . TYR B 2 103 ? 59.742  69.155  46.880 1.00 247.91 ? 103 TYR B OH  1 
ATOM   832  N  N   . ALA B 2 104 ? 59.380  61.546  42.532 1.00 170.50 ? 104 ALA B N   1 
ATOM   833  C  CA  . ALA B 2 104 ? 59.725  60.757  41.354 1.00 185.64 ? 104 ALA B CA  1 
ATOM   834  C  C   . ALA B 2 104 ? 58.861  61.155  40.148 1.00 214.72 ? 104 ALA B C   1 
ATOM   835  O  O   . ALA B 2 104 ? 59.411  61.353  39.044 1.00 172.23 ? 104 ALA B O   1 
ATOM   836  C  CB  . ALA B 2 104 ? 59.560  59.310  41.742 1.00 232.72 ? 104 ALA B CB  1 
ATOM   837  N  N   . GLU B 2 105 ? 57.525  61.271  40.372 1.00 241.31 ? 105 GLU B N   1 
ATOM   838  C  CA  . GLU B 2 105 ? 56.615  61.851  39.393 1.00 213.53 ? 105 GLU B CA  1 
ATOM   839  C  C   . GLU B 2 105 ? 57.036  63.286  39.084 1.00 157.08 ? 105 GLU B C   1 
ATOM   840  O  O   . GLU B 2 105 ? 57.396  63.592  37.942 1.00 160.82 ? 105 GLU B O   1 
ATOM   841  C  CB  . GLU B 2 105 ? 55.152  61.821  39.850 1.00 203.04 ? 105 GLU B CB  1 
ATOM   842  C  CG  . GLU B 2 105 ? 54.204  62.575  38.918 1.00 279.28 ? 105 GLU B CG  1 
ATOM   843  C  CD  . GLU B 2 105 ? 52.714  62.284  39.035 1.00 362.21 ? 105 GLU B CD  1 
ATOM   844  O  OE1 . GLU B 2 105 ? 52.324  61.397  39.799 1.00 339.42 ? 105 GLU B OE1 1 
ATOM   845  O  OE2 . GLU B 2 105 ? 51.922  62.953  38.348 1.00 435.18 ? 105 GLU B OE2 1 
ATOM   846  N  N   . LEU B 2 106 ? 56.993  64.165  40.079 1.00 136.68 ? 106 LEU B N   1 
ATOM   847  C  CA  . LEU B 2 106 ? 57.093  65.596  39.809 1.00 226.16 ? 106 LEU B CA  1 
ATOM   848  C  C   . LEU B 2 106 ? 58.365  65.893  39.002 1.00 166.42 ? 106 LEU B C   1 
ATOM   849  O  O   . LEU B 2 106 ? 58.324  66.592  37.987 1.00 214.73 ? 106 LEU B O   1 
ATOM   850  C  CB  . LEU B 2 106 ? 57.015  66.356  41.142 1.00 242.37 ? 106 LEU B CB  1 
ATOM   851  C  CG  . LEU B 2 106 ? 57.102  67.878  41.084 1.00 191.44 ? 106 LEU B CG  1 
ATOM   852  C  CD1 . LEU B 2 106 ? 56.141  68.531  40.113 1.00 208.97 ? 106 LEU B CD1 1 
ATOM   853  C  CD2 . LEU B 2 106 ? 56.804  68.441  42.434 1.00 165.89 ? 106 LEU B CD2 1 
ATOM   854  N  N   . GLY B 2 107 ? 59.485  65.338  39.420 1.00 177.48 ? 107 GLY B N   1 
ATOM   855  C  CA  . GLY B 2 107 ? 60.736  65.527  38.708 1.00 232.92 ? 107 GLY B CA  1 
ATOM   856  C  C   . GLY B 2 107 ? 60.762  65.033  37.261 1.00 187.72 ? 107 GLY B C   1 
ATOM   857  O  O   . GLY B 2 107 ? 61.432  65.647  36.455 1.00 177.42 ? 107 GLY B O   1 
ATOM   858  N  N   . THR B 2 108 ? 60.053  63.952  36.923 1.00 153.72 ? 108 THR B N   1 
ATOM   859  C  CA  . THR B 2 108 ? 59.978  63.480  35.542 1.00 188.73 ? 108 THR B CA  1 
ATOM   860  C  C   . THR B 2 108 ? 58.861  64.168  34.736 1.00 186.90 ? 108 THR B C   1 
ATOM   861  O  O   . THR B 2 108 ? 58.925  64.126  33.508 1.00 161.82 ? 108 THR B O   1 
ATOM   862  C  CB  . THR B 2 108 ? 59.850  61.956  35.463 1.00 202.78 ? 108 THR B CB  1 
ATOM   863  O  OG1 . THR B 2 108 ? 58.732  61.473  36.211 1.00 210.61 ? 108 THR B OG1 1 
ATOM   864  C  CG2 . THR B 2 108 ? 61.108  61.295  35.964 1.00 248.89 ? 108 THR B CG2 1 
ATOM   865  N  N   . THR B 2 109 ? 57.865  64.810  35.373 1.00 161.69 ? 109 THR B N   1 
ATOM   866  C  CA  . THR B 2 109 ? 56.942  65.681  34.646 1.00 178.05 ? 109 THR B CA  1 
ATOM   867  C  C   . THR B 2 109 ? 57.636  66.967  34.159 1.00 179.88 ? 109 THR B C   1 
ATOM   868  O  O   . THR B 2 109 ? 57.505  67.337  32.993 1.00 167.99 ? 109 THR B O   1 
ATOM   869  C  CB  . THR B 2 109 ? 55.682  66.059  35.452 1.00 206.42 ? 109 THR B CB  1 
ATOM   870  O  OG1 . THR B 2 109 ? 55.979  66.910  36.550 1.00 179.95 ? 109 THR B OG1 1 
ATOM   871  C  CG2 . THR B 2 109 ? 54.943  64.877  36.037 1.00 268.64 ? 109 THR B CG2 1 
ATOM   872  N  N   . ILE B 2 110 ? 58.360  67.660  35.047 1.00 202.42 ? 110 ILE B N   1 
ATOM   873  C  CA  . ILE B 2 110 ? 59.065  68.893  34.707 1.00 174.99 ? 110 ILE B CA  1 
ATOM   874  C  C   . ILE B 2 110 ? 60.365  68.584  33.956 1.00 169.43 ? 110 ILE B C   1 
ATOM   875  O  O   . ILE B 2 110 ? 60.705  69.296  33.003 1.00 271.00 ? 110 ILE B O   1 
ATOM   876  C  CB  . ILE B 2 110 ? 59.334  69.764  35.960 1.00 200.22 ? 110 ILE B CB  1 
ATOM   877  C  CG1 . ILE B 2 110 ? 58.104  70.015  36.856 1.00 203.31 ? 110 ILE B CG1 1 
ATOM   878  C  CG2 . ILE B 2 110 ? 59.953  71.084  35.499 1.00 172.56 ? 110 ILE B CG2 1 
ATOM   879  C  CD1 . ILE B 2 110 ? 57.000  70.839  36.254 1.00 222.34 ? 110 ILE B CD1 1 
ATOM   880  N  N   . SER B 2 111 ? 61.092  67.544  34.394 1.00 219.22 ? 111 SER B N   1 
ATOM   881  C  CA  . SER B 2 111 ? 62.350  67.064  33.810 1.00 303.32 ? 111 SER B CA  1 
ATOM   882  C  C   . SER B 2 111 ? 63.430  68.164  33.767 1.00 253.46 ? 111 SER B C   1 
ATOM   883  O  O   . SER B 2 111 ? 63.989  68.492  32.720 1.00 250.22 ? 111 SER B O   1 
ATOM   884  C  CB  . SER B 2 111 ? 62.095  66.380  32.468 1.00 353.04 ? 111 SER B CB  1 
ATOM   885  O  OG  . SER B 2 111 ? 63.182  65.534  32.133 1.00 412.72 ? 111 SER B OG  1 
ATOM   886  N  N   . LYS B 2 112 ? 63.726  68.726  34.952 1.00 209.39 ? 112 LYS B N   1 
ATOM   887  C  CA  . LYS B 2 112 ? 64.579  69.899  35.118 1.00 266.87 ? 112 LYS B CA  1 
ATOM   888  C  C   . LYS B 2 112 ? 65.387  69.787  36.416 1.00 235.32 ? 112 LYS B C   1 
ATOM   889  O  O   . LYS B 2 112 ? 64.934  69.142  37.355 1.00 273.73 ? 112 LYS B O   1 
ATOM   890  C  CB  . LYS B 2 112 ? 63.678  71.137  35.086 1.00 255.58 ? 112 LYS B CB  1 
ATOM   891  C  CG  . LYS B 2 112 ? 64.366  72.489  34.902 1.00 250.94 ? 112 LYS B CG  1 
ATOM   892  C  CD  . LYS B 2 112 ? 63.425  73.656  34.705 1.00 272.90 ? 112 LYS B CD  1 
ATOM   893  C  CE  . LYS B 2 112 ? 62.429  73.560  33.552 1.00 281.44 ? 112 LYS B CE  1 
ATOM   894  N  NZ  . LYS B 2 112 ? 63.015  73.404  32.187 1.00 270.24 ? 112 LYS B NZ  1 
ATOM   895  N  N   . SER B 2 113 ? 66.573  70.421  36.479 1.00 199.10 ? 113 SER B N   1 
ATOM   896  C  CA  . SER B 2 113 ? 67.548  70.181  37.539 1.00 191.45 ? 113 SER B CA  1 
ATOM   897  C  C   . SER B 2 113 ? 67.350  71.055  38.788 1.00 216.43 ? 113 SER B C   1 
ATOM   898  O  O   . SER B 2 113 ? 67.946  70.744  39.828 1.00 134.88 ? 113 SER B O   1 
ATOM   899  C  CB  . SER B 2 113 ? 68.953  70.342  37.040 1.00 204.61 ? 113 SER B CB  1 
ATOM   900  O  OG  . SER B 2 113 ? 69.086  71.575  36.343 1.00 352.98 ? 113 SER B OG  1 
ATOM   901  N  N   . GLY B 2 114 ? 66.549  72.127  38.766 1.00 222.59 ? 114 GLY B N   1 
ATOM   902  C  CA  . GLY B 2 114 ? 66.485  73.004  39.934 1.00 251.69 ? 114 GLY B CA  1 
ATOM   903  C  C   . GLY B 2 114 ? 65.739  72.482  41.167 1.00 202.50 ? 114 GLY B C   1 
ATOM   904  O  O   . GLY B 2 114 ? 65.445  73.273  42.057 1.00 176.23 ? 114 GLY B O   1 
ATOM   905  N  N   . GLY B 2 115 ? 65.410  71.186  41.221 1.00 138.43 ? 115 GLY B N   1 
ATOM   906  C  CA  . GLY B 2 115 ? 64.678  70.557  42.303 1.00 166.88 ? 115 GLY B CA  1 
ATOM   907  C  C   . GLY B 2 115 ? 63.469  71.362  42.797 1.00 245.74 ? 115 GLY B C   1 
ATOM   908  O  O   . GLY B 2 115 ? 62.690  71.927  42.051 1.00 150.85 ? 115 GLY B O   1 
ATOM   909  N  N   . ASP B 2 116 ? 63.336  71.436  44.119 1.00 248.44 ? 116 ASP B N   1 
ATOM   910  C  CA  . ASP B 2 116 ? 62.174  72.002  44.785 1.00 174.92 ? 116 ASP B CA  1 
ATOM   911  C  C   . ASP B 2 116 ? 62.031  73.496  44.536 1.00 155.01 ? 116 ASP B C   1 
ATOM   912  O  O   . ASP B 2 116 ? 61.016  74.053  44.951 1.00 222.97 ? 116 ASP B O   1 
ATOM   913  C  CB  . ASP B 2 116 ? 62.337  71.820  46.308 1.00 286.90 ? 116 ASP B CB  1 
ATOM   914  C  CG  . ASP B 2 116 ? 62.715  70.426  46.806 1.00 324.48 ? 116 ASP B CG  1 
ATOM   915  O  OD1 . ASP B 2 116 ? 63.580  69.801  46.182 1.00 391.48 ? 116 ASP B OD1 1 
ATOM   916  O  OD2 . ASP B 2 116 ? 62.135  69.971  47.806 1.00 164.61 ? 116 ASP B OD2 1 
ATOM   917  N  N   . TYR B 2 117 ? 63.041  74.166  43.928 1.00 168.89 ? 117 TYR B N   1 
ATOM   918  C  CA  . TYR B 2 117 ? 62.934  75.552  43.476 1.00 171.59 ? 117 TYR B CA  1 
ATOM   919  C  C   . TYR B 2 117 ? 62.336  75.577  42.073 1.00 151.52 ? 117 TYR B C   1 
ATOM   920  O  O   . TYR B 2 117 ? 61.301  76.229  41.880 1.00 247.54 ? 117 TYR B O   1 
ATOM   921  C  CB  . TYR B 2 117 ? 64.295  76.220  43.556 1.00 188.54 ? 117 TYR B CB  1 
ATOM   922  C  CG  . TYR B 2 117 ? 64.492  77.406  42.630 1.00 169.44 ? 117 TYR B CG  1 
ATOM   923  C  CD1 . TYR B 2 117 ? 63.995  78.651  42.980 1.00 153.97 ? 117 TYR B CD1 1 
ATOM   924  C  CD2 . TYR B 2 117 ? 65.183  77.268  41.413 1.00 145.34 ? 117 TYR B CD2 1 
ATOM   925  C  CE1 . TYR B 2 117 ? 64.180  79.747  42.145 1.00 183.06 ? 117 TYR B CE1 1 
ATOM   926  C  CE2 . TYR B 2 117 ? 65.395  78.361  40.590 1.00 145.24 ? 117 TYR B CE2 1 
ATOM   927  C  CZ  . TYR B 2 117 ? 64.880  79.598  40.951 1.00 191.38 ? 117 TYR B CZ  1 
ATOM   928  O  OH  . TYR B 2 117 ? 65.048  80.693  40.146 1.00 246.87 ? 117 TYR B OH  1 
ATOM   929  N  N   . ALA B 2 118 ? 62.928  74.855  41.121 1.00 99.78  ? 118 ALA B N   1 
ATOM   930  C  CA  . ALA B 2 118 ? 62.353  74.727  39.787 1.00 149.38 ? 118 ALA B CA  1 
ATOM   931  C  C   . ALA B 2 118 ? 60.883  74.313  39.869 1.00 173.74 ? 118 ALA B C   1 
ATOM   932  O  O   . ALA B 2 118 ? 60.031  74.912  39.191 1.00 173.65 ? 118 ALA B O   1 
ATOM   933  C  CB  . ALA B 2 118 ? 63.131  73.717  38.909 1.00 132.66 ? 118 ALA B CB  1 
ATOM   934  N  N   . TYR B 2 119 ? 60.578  73.279  40.677 1.00 124.46 ? 119 TYR B N   1 
ATOM   935  C  CA  . TYR B 2 119 ? 59.240  72.723  40.682 1.00 162.29 ? 119 TYR B CA  1 
ATOM   936  C  C   . TYR B 2 119 ? 58.197  73.672  41.262 1.00 178.65 ? 119 TYR B C   1 
ATOM   937  O  O   . TYR B 2 119 ? 57.019  73.368  41.146 1.00 230.01 ? 119 TYR B O   1 
ATOM   938  C  CB  . TYR B 2 119 ? 59.202  71.400  41.435 1.00 180.24 ? 119 TYR B CB  1 
ATOM   939  C  CG  . TYR B 2 119 ? 60.200  70.355  40.973 1.00 135.91 ? 119 TYR B CG  1 
ATOM   940  C  CD1 . TYR B 2 119 ? 60.742  70.364  39.703 1.00 139.38 ? 119 TYR B CD1 1 
ATOM   941  C  CD2 . TYR B 2 119 ? 60.599  69.351  41.843 1.00 197.18 ? 119 TYR B CD2 1 
ATOM   942  C  CE1 . TYR B 2 119 ? 61.670  69.414  39.311 1.00 225.36 ? 119 TYR B CE1 1 
ATOM   943  C  CE2 . TYR B 2 119 ? 61.524  68.392  41.474 1.00 226.67 ? 119 TYR B CE2 1 
ATOM   944  C  CZ  . TYR B 2 119 ? 62.071  68.436  40.204 1.00 247.60 ? 119 TYR B CZ  1 
ATOM   945  O  OH  . TYR B 2 119 ? 63.009  67.516  39.802 1.00 228.80 ? 119 TYR B OH  1 
ATOM   946  N  N   . MET B 2 120 ? 58.590  74.793  41.865 1.00 153.79 ? 120 MET B N   1 
ATOM   947  C  CA  . MET B 2 120 ? 57.642  75.834  42.228 1.00 196.04 ? 120 MET B CA  1 
ATOM   948  C  C   . MET B 2 120 ? 57.771  77.068  41.323 1.00 190.38 ? 120 MET B C   1 
ATOM   949  O  O   . MET B 2 120 ? 56.790  77.811  41.182 1.00 293.36 ? 120 MET B O   1 
ATOM   950  C  CB  . MET B 2 120 ? 57.775  76.210  43.715 1.00 178.14 ? 120 MET B CB  1 
ATOM   951  C  CG  . MET B 2 120 ? 59.040  76.893  44.128 1.00 193.11 ? 120 MET B CG  1 
ATOM   952  S  SD  . MET B 2 120 ? 58.764  77.668  45.735 1.00 226.02 ? 120 MET B SD  1 
ATOM   953  C  CE  . MET B 2 120 ? 58.359  76.186  46.675 1.00 203.55 ? 120 MET B CE  1 
ATOM   954  N  N   . LEU B 2 121 ? 58.924  77.303  40.685 1.00 130.01 ? 121 LEU B N   1 
ATOM   955  C  CA  . LEU B 2 121 ? 59.058  78.365  39.695 1.00 198.66 ? 121 LEU B CA  1 
ATOM   956  C  C   . LEU B 2 121 ? 58.110  78.129  38.513 1.00 223.74 ? 121 LEU B C   1 
ATOM   957  O  O   . LEU B 2 121 ? 57.502  79.078  38.000 1.00 170.51 ? 121 LEU B O   1 
ATOM   958  C  CB  . LEU B 2 121 ? 60.528  78.409  39.267 1.00 195.41 ? 121 LEU B CB  1 
ATOM   959  C  CG  . LEU B 2 121 ? 60.882  79.451  38.217 1.00 277.61 ? 121 LEU B CG  1 
ATOM   960  C  CD1 . LEU B 2 121 ? 60.621  80.876  38.737 1.00 207.10 ? 121 LEU B CD1 1 
ATOM   961  C  CD2 . LEU B 2 121 ? 62.323  79.230  37.765 1.00 236.48 ? 121 LEU B CD2 1 
ATOM   962  N  N   . GLU B 2 122 ? 57.979  76.856  38.094 1.00 205.73 ? 122 GLU B N   1 
ATOM   963  C  CA  . GLU B 2 122 ? 57.074  76.445  37.022 1.00 227.35 ? 122 GLU B CA  1 
ATOM   964  C  C   . GLU B 2 122 ? 55.585  76.546  37.384 1.00 210.99 ? 122 GLU B C   1 
ATOM   965  O  O   . GLU B 2 122 ? 54.743  76.183  36.551 1.00 178.08 ? 122 GLU B O   1 
ATOM   966  C  CB  . GLU B 2 122 ? 57.404  75.002  36.630 1.00 253.29 ? 122 GLU B CB  1 
ATOM   967  C  CG  . GLU B 2 122 ? 58.787  74.840  36.001 1.00 350.79 ? 122 GLU B CG  1 
ATOM   968  C  CD  . GLU B 2 122 ? 59.035  75.595  34.701 1.00 465.69 ? 122 GLU B CD  1 
ATOM   969  O  OE1 . GLU B 2 122 ? 58.090  75.712  33.891 1.00 543.84 ? 122 GLU B OE1 1 
ATOM   970  O  OE2 . GLU B 2 122 ? 60.185  76.057  34.495 1.00 485.15 ? 122 GLU B OE2 1 
ATOM   971  N  N   . VAL B 2 123 ? 55.242  77.014  38.601 1.00 209.56 ? 123 VAL B N   1 
ATOM   972  C  CA  . VAL B 2 123 ? 53.884  76.992  39.138 1.00 218.91 ? 123 VAL B CA  1 
ATOM   973  C  C   . VAL B 2 123 ? 53.526  78.342  39.767 1.00 206.43 ? 123 VAL B C   1 
ATOM   974  O  O   . VAL B 2 123 ? 52.670  79.068  39.236 1.00 293.67 ? 123 VAL B O   1 
ATOM   975  C  CB  . VAL B 2 123 ? 53.689  75.834  40.143 1.00 167.91 ? 123 VAL B CB  1 
ATOM   976  C  CG1 . VAL B 2 123 ? 52.342  75.893  40.850 1.00 204.39 ? 123 VAL B CG1 1 
ATOM   977  C  CG2 . VAL B 2 123 ? 53.836  74.492  39.461 1.00 222.02 ? 123 VAL B CG2 1 
ATOM   978  N  N   . TYR B 2 124 ? 54.166  78.653  40.900 1.00 151.12 ? 124 TYR B N   1 
ATOM   979  C  CA  . TYR B 2 124 ? 53.856  79.840  41.682 1.00 234.65 ? 124 TYR B CA  1 
ATOM   980  C  C   . TYR B 2 124 ? 54.535  81.098  41.111 1.00 282.48 ? 124 TYR B C   1 
ATOM   981  O  O   . TYR B 2 124 ? 54.185  82.220  41.478 1.00 252.50 ? 124 TYR B O   1 
ATOM   982  C  CB  . TYR B 2 124 ? 54.305  79.588  43.117 1.00 230.85 ? 124 TYR B CB  1 
ATOM   983  C  CG  . TYR B 2 124 ? 53.692  78.411  43.858 1.00 230.55 ? 124 TYR B CG  1 
ATOM   984  C  CD1 . TYR B 2 124 ? 54.088  77.090  43.616 1.00 232.77 ? 124 TYR B CD1 1 
ATOM   985  C  CD2 . TYR B 2 124 ? 52.732  78.617  44.834 1.00 247.54 ? 124 TYR B CD2 1 
ATOM   986  C  CE1 . TYR B 2 124 ? 53.521  76.014  44.296 1.00 159.05 ? 124 TYR B CE1 1 
ATOM   987  C  CE2 . TYR B 2 124 ? 52.177  77.547  45.528 1.00 317.94 ? 124 TYR B CE2 1 
ATOM   988  C  CZ  . TYR B 2 124 ? 52.573  76.241  45.258 1.00 206.55 ? 124 TYR B CZ  1 
ATOM   989  O  OH  . TYR B 2 124 ? 52.056  75.184  45.942 1.00 229.65 ? 124 TYR B OH  1 
ATOM   990  N  N   . GLY B 2 125 ? 55.518  80.935  40.218 1.00 278.36 ? 125 GLY B N   1 
ATOM   991  C  CA  . GLY B 2 125 ? 56.160  82.052  39.536 1.00 291.87 ? 125 GLY B CA  1 
ATOM   992  C  C   . GLY B 2 125 ? 57.319  82.670  40.313 1.00 215.98 ? 125 GLY B C   1 
ATOM   993  O  O   . GLY B 2 125 ? 57.787  82.119  41.302 1.00 271.48 ? 125 GLY B O   1 
ATOM   994  N  N   . SER B 2 126 ? 57.755  83.852  39.855 1.00 251.28 ? 126 SER B N   1 
ATOM   995  C  CA  . SER B 2 126 ? 59.081  84.397  40.118 1.00 252.49 ? 126 SER B CA  1 
ATOM   996  C  C   . SER B 2 126 ? 59.347  84.640  41.601 1.00 214.01 ? 126 SER B C   1 
ATOM   997  O  O   . SER B 2 126 ? 60.287  84.066  42.166 1.00 272.63 ? 126 SER B O   1 
ATOM   998  C  CB  . SER B 2 126 ? 59.301  85.688  39.351 1.00 289.55 ? 126 SER B CB  1 
ATOM   999  O  OG  . SER B 2 126 ? 60.636  86.172  39.515 1.00 246.41 ? 126 SER B OG  1 
ATOM   1000 N  N   . LEU B 2 127 ? 58.528  85.484  42.249 1.00 146.25 ? 127 LEU B N   1 
ATOM   1001 C  CA  . LEU B 2 127 ? 58.841  85.876  43.628 1.00 162.44 ? 127 LEU B CA  1 
ATOM   1002 C  C   . LEU B 2 127 ? 58.667  84.698  44.604 1.00 166.91 ? 127 LEU B C   1 
ATOM   1003 O  O   . LEU B 2 127 ? 59.565  84.486  45.411 1.00 113.89 ? 127 LEU B O   1 
ATOM   1004 C  CB  . LEU B 2 127 ? 58.007  87.095  44.036 1.00 222.83 ? 127 LEU B CB  1 
ATOM   1005 C  CG  . LEU B 2 127 ? 58.016  87.465  45.512 1.00 229.96 ? 127 LEU B CG  1 
ATOM   1006 C  CD1 . LEU B 2 127 ? 59.414  87.849  45.962 1.00 227.99 ? 127 LEU B CD1 1 
ATOM   1007 C  CD2 . LEU B 2 127 ? 57.024  88.586  45.776 1.00 266.77 ? 127 LEU B CD2 1 
ATOM   1008 N  N   . PRO B 2 128 ? 57.569  83.886  44.605 1.00 202.17 ? 128 PRO B N   1 
ATOM   1009 C  CA  . PRO B 2 128 ? 57.503  82.701  45.487 1.00 223.44 ? 128 PRO B CA  1 
ATOM   1010 C  C   . PRO B 2 128 ? 58.703  81.753  45.389 1.00 130.92 ? 128 PRO B C   1 
ATOM   1011 O  O   . PRO B 2 128 ? 59.226  81.330  46.384 1.00 148.34 ? 128 PRO B O   1 
ATOM   1012 C  CB  . PRO B 2 128 ? 56.205  82.006  45.058 1.00 228.97 ? 128 PRO B CB  1 
ATOM   1013 C  CG  . PRO B 2 128 ? 55.367  83.170  44.553 1.00 254.49 ? 128 PRO B CG  1 
ATOM   1014 C  CD  . PRO B 2 128 ? 56.343  84.054  43.800 1.00 148.35 ? 128 PRO B CD  1 
ATOM   1015 N  N   . ALA B 2 129 ? 59.181  81.475  44.190 1.00 190.85 ? 129 ALA B N   1 
ATOM   1016 C  CA  . ALA B 2 129 ? 60.414  80.726  44.010 1.00 161.92 ? 129 ALA B CA  1 
ATOM   1017 C  C   . ALA B 2 129 ? 61.629  81.474  44.563 1.00 123.40 ? 129 ALA B C   1 
ATOM   1018 O  O   . ALA B 2 129 ? 62.505  80.851  45.159 1.00 209.07 ? 129 ALA B O   1 
ATOM   1019 C  CB  . ALA B 2 129 ? 60.591  80.442  42.527 1.00 251.76 ? 129 ALA B CB  1 
ATOM   1020 N  N   . PHE B 2 130 ? 61.722  82.801  44.386 1.00 108.64 ? 130 PHE B N   1 
ATOM   1021 C  CA  . PHE B 2 130 ? 62.839  83.562  44.920 1.00 124.99 ? 130 PHE B CA  1 
ATOM   1022 C  C   . PHE B 2 130 ? 62.870  83.500  46.446 1.00 126.11 ? 130 PHE B C   1 
ATOM   1023 O  O   . PHE B 2 130 ? 63.960  83.374  46.995 1.00 102.34 ? 130 PHE B O   1 
ATOM   1024 C  CB  . PHE B 2 130 ? 62.826  85.007  44.440 1.00 129.35 ? 130 PHE B CB  1 
ATOM   1025 C  CG  . PHE B 2 130 ? 64.017  85.798  44.926 1.00 145.42 ? 130 PHE B CG  1 
ATOM   1026 C  CD1 . PHE B 2 130 ? 63.978  86.475  46.169 1.00 153.85 ? 130 PHE B CD1 1 
ATOM   1027 C  CD2 . PHE B 2 130 ? 65.179  85.873  44.135 1.00 116.80 ? 130 PHE B CD2 1 
ATOM   1028 C  CE1 . PHE B 2 130 ? 65.082  87.216  46.593 1.00 169.10 ? 130 PHE B CE1 1 
ATOM   1029 C  CE2 . PHE B 2 130 ? 66.278  86.632  44.550 1.00 185.37 ? 130 PHE B CE2 1 
ATOM   1030 C  CZ  . PHE B 2 130 ? 66.224  87.292  45.784 1.00 228.44 ? 130 PHE B CZ  1 
ATOM   1031 N  N   . LEU B 2 131 ? 61.729  83.589  47.145 1.00 131.54 ? 131 LEU B N   1 
ATOM   1032 C  CA  . LEU B 2 131 ? 61.754  83.560  48.604 1.00 176.53 ? 131 LEU B CA  1 
ATOM   1033 C  C   . LEU B 2 131 ? 62.405  82.273  49.105 1.00 177.80 ? 131 LEU B C   1 
ATOM   1034 O  O   . LEU B 2 131 ? 63.234  82.327  50.030 1.00 205.53 ? 131 LEU B O   1 
ATOM   1035 C  CB  . LEU B 2 131 ? 60.335  83.740  49.173 1.00 166.00 ? 131 LEU B CB  1 
ATOM   1036 C  CG  . LEU B 2 131 ? 59.715  85.116  48.924 1.00 254.43 ? 131 LEU B CG  1 
ATOM   1037 C  CD1 . LEU B 2 131 ? 58.368  85.179  49.641 1.00 334.14 ? 131 LEU B CD1 1 
ATOM   1038 C  CD2 . LEU B 2 131 ? 60.642  86.314  49.323 1.00 189.71 ? 131 LEU B CD2 1 
ATOM   1039 N  N   . LYS B 2 132 ? 62.024  81.131  48.506 1.00 146.28 ? 132 LYS B N   1 
ATOM   1040 C  CA  . LYS B 2 132 ? 62.683  79.862  48.776 1.00 151.61 ? 132 LYS B CA  1 
ATOM   1041 C  C   . LYS B 2 132 ? 64.170  79.958  48.428 1.00 136.77 ? 132 LYS B C   1 
ATOM   1042 O  O   . LYS B 2 132 ? 64.999  79.595  49.245 1.00 149.02 ? 132 LYS B O   1 
ATOM   1043 C  CB  . LYS B 2 132 ? 61.996  78.709  48.050 1.00 151.14 ? 132 LYS B CB  1 
ATOM   1044 C  CG  . LYS B 2 132 ? 62.795  77.411  48.029 1.00 167.68 ? 132 LYS B CG  1 
ATOM   1045 C  CD  . LYS B 2 132 ? 61.943  76.255  47.621 1.00 194.33 ? 132 LYS B CD  1 
ATOM   1046 C  CE  . LYS B 2 132 ? 62.655  74.924  47.822 1.00 201.97 ? 132 LYS B CE  1 
ATOM   1047 N  NZ  . LYS B 2 132 ? 62.812  74.527  49.242 1.00 261.13 ? 132 LYS B NZ  1 
ATOM   1048 N  N   . LEU B 2 133 ? 64.518  80.433  47.245 1.00 136.39 ? 133 LEU B N   1 
ATOM   1049 C  CA  . LEU B 2 133 ? 65.905  80.414  46.838 1.00 155.08 ? 133 LEU B CA  1 
ATOM   1050 C  C   . LEU B 2 133 ? 66.771  81.267  47.765 1.00 160.88 ? 133 LEU B C   1 
ATOM   1051 O  O   . LEU B 2 133 ? 67.852  80.836  48.130 1.00 220.34 ? 133 LEU B O   1 
ATOM   1052 C  CB  . LEU B 2 133 ? 66.007  80.939  45.405 1.00 173.05 ? 133 LEU B CB  1 
ATOM   1053 C  CG  . LEU B 2 133 ? 67.388  80.867  44.810 1.00 146.62 ? 133 LEU B CG  1 
ATOM   1054 C  CD1 . LEU B 2 133 ? 67.753  79.399  44.730 1.00 111.09 ? 133 LEU B CD1 1 
ATOM   1055 C  CD2 . LEU B 2 133 ? 67.402  81.577  43.481 1.00 160.31 ? 133 LEU B CD2 1 
ATOM   1056 N  N   . TRP B 2 134 ? 66.315  82.455  48.142 1.00 130.66 ? 134 TRP B N   1 
ATOM   1057 C  CA  . TRP B 2 134 ? 67.032  83.309  49.061 1.00 145.14 ? 134 TRP B CA  1 
ATOM   1058 C  C   . TRP B 2 134 ? 67.307  82.599  50.389 1.00 193.74 ? 134 TRP B C   1 
ATOM   1059 O  O   . TRP B 2 134 ? 68.434  82.623  50.890 1.00 254.16 ? 134 TRP B O   1 
ATOM   1060 C  CB  . TRP B 2 134 ? 66.183  84.563  49.282 1.00 199.85 ? 134 TRP B CB  1 
ATOM   1061 C  CG  . TRP B 2 134 ? 66.786  85.552  50.238 1.00 226.81 ? 134 TRP B CG  1 
ATOM   1062 C  CD1 . TRP B 2 134 ? 66.342  85.832  51.498 1.00 224.77 ? 134 TRP B CD1 1 
ATOM   1063 C  CD2 . TRP B 2 134 ? 67.958  86.376  50.012 1.00 159.44 ? 134 TRP B CD2 1 
ATOM   1064 N  NE1 . TRP B 2 134 ? 67.151  86.782  52.066 1.00 233.56 ? 134 TRP B NE1 1 
ATOM   1065 C  CE2 . TRP B 2 134 ? 68.154  87.134  51.189 1.00 199.16 ? 134 TRP B CE2 1 
ATOM   1066 C  CE3 . TRP B 2 134 ? 68.856  86.526  48.951 1.00 157.65 ? 134 TRP B CE3 1 
ATOM   1067 C  CZ2 . TRP B 2 134 ? 69.218  88.038  51.316 1.00 186.92 ? 134 TRP B CZ2 1 
ATOM   1068 C  CZ3 . TRP B 2 134 ? 69.909  87.409  49.078 1.00 263.64 ? 134 TRP B CZ3 1 
ATOM   1069 C  CH2 . TRP B 2 134 ? 70.090  88.150  50.252 1.00 247.47 ? 134 TRP B CH2 1 
ATOM   1070 N  N   . ILE B 2 135 ? 66.282  81.952  50.957 1.00 167.65 ? 135 ILE B N   1 
ATOM   1071 C  CA  . ILE B 2 135 ? 66.416  81.197  52.197 1.00 172.41 ? 135 ILE B CA  1 
ATOM   1072 C  C   . ILE B 2 135 ? 67.346  79.986  52.029 1.00 173.86 ? 135 ILE B C   1 
ATOM   1073 O  O   . ILE B 2 135 ? 68.146  79.708  52.912 1.00 167.96 ? 135 ILE B O   1 
ATOM   1074 C  CB  . ILE B 2 135 ? 65.000  80.817  52.679 1.00 179.19 ? 135 ILE B CB  1 
ATOM   1075 C  CG1 . ILE B 2 135 ? 64.275  82.043  53.220 1.00 206.62 ? 135 ILE B CG1 1 
ATOM   1076 C  CG2 . ILE B 2 135 ? 64.968  79.665  53.697 1.00 190.66 ? 135 ILE B CG2 1 
ATOM   1077 C  CD1 . ILE B 2 135 ? 64.852  82.576  54.522 1.00 322.79 ? 135 ILE B CD1 1 
ATOM   1078 N  N   . GLU B 2 136 ? 67.264  79.264  50.904 1.00 144.84 ? 136 GLU B N   1 
ATOM   1079 C  CA  . GLU B 2 136 ? 68.145  78.131  50.626 1.00 168.65 ? 136 GLU B CA  1 
ATOM   1080 C  C   . GLU B 2 136 ? 69.598  78.561  50.415 1.00 137.81 ? 136 GLU B C   1 
ATOM   1081 O  O   . GLU B 2 136 ? 70.502  77.824  50.767 1.00 187.44 ? 136 GLU B O   1 
ATOM   1082 C  CB  . GLU B 2 136 ? 67.649  77.363  49.406 1.00 215.87 ? 136 GLU B CB  1 
ATOM   1083 C  CG  . GLU B 2 136 ? 66.244  76.769  49.560 1.00 276.28 ? 136 GLU B CG  1 
ATOM   1084 C  CD  . GLU B 2 136 ? 66.123  75.300  49.924 1.00 284.46 ? 136 GLU B CD  1 
ATOM   1085 O  OE1 . GLU B 2 136 ? 66.977  74.503  49.474 1.00 324.66 ? 136 GLU B OE1 1 
ATOM   1086 O  OE2 . GLU B 2 136 ? 65.145  74.945  50.628 1.00 255.67 ? 136 GLU B OE2 1 
ATOM   1087 N  N   . LEU B 2 137 ? 69.810  79.755  49.861 1.00 143.01 ? 137 LEU B N   1 
ATOM   1088 C  CA  . LEU B 2 137 ? 71.128  80.303  49.579 1.00 179.37 ? 137 LEU B CA  1 
ATOM   1089 C  C   . LEU B 2 137 ? 71.790  80.908  50.814 1.00 144.55 ? 137 LEU B C   1 
ATOM   1090 O  O   . LEU B 2 137 ? 72.989  80.734  51.005 1.00 144.02 ? 137 LEU B O   1 
ATOM   1091 C  CB  . LEU B 2 137 ? 70.965  81.338  48.465 1.00 181.30 ? 137 LEU B CB  1 
ATOM   1092 C  CG  . LEU B 2 137 ? 72.214  82.114  48.094 1.00 193.91 ? 137 LEU B CG  1 
ATOM   1093 C  CD1 . LEU B 2 137 ? 72.264  82.271  46.582 1.00 264.01 ? 137 LEU B CD1 1 
ATOM   1094 C  CD2 . LEU B 2 137 ? 72.223  83.498  48.757 1.00 263.20 ? 137 LEU B CD2 1 
ATOM   1095 N  N   . LEU B 2 138 ? 71.027  81.619  51.634 1.00 149.61 ? 138 LEU B N   1 
ATOM   1096 C  CA  . LEU B 2 138 ? 71.596  82.365  52.744 1.00 191.94 ? 138 LEU B CA  1 
ATOM   1097 C  C   . LEU B 2 138 ? 71.629  81.534  54.024 1.00 183.53 ? 138 LEU B C   1 
ATOM   1098 O  O   . LEU B 2 138 ? 72.528  81.734  54.830 1.00 175.57 ? 138 LEU B O   1 
ATOM   1099 C  CB  . LEU B 2 138 ? 70.779  83.644  52.951 1.00 245.06 ? 138 LEU B CB  1 
ATOM   1100 C  CG  . LEU B 2 138 ? 71.315  84.594  54.024 1.00 314.84 ? 138 LEU B CG  1 
ATOM   1101 C  CD1 . LEU B 2 138 ? 72.728  85.093  53.723 1.00 265.79 ? 138 LEU B CD1 1 
ATOM   1102 C  CD2 . LEU B 2 138 ? 70.374  85.773  54.181 1.00 448.75 ? 138 LEU B CD2 1 
ATOM   1103 N  N   . ILE B 2 139 ? 70.663  80.627  54.233 1.00 187.06 ? 139 ILE B N   1 
ATOM   1104 C  CA  . ILE B 2 139 ? 70.496  79.966  55.522 1.00 187.23 ? 139 ILE B CA  1 
ATOM   1105 C  C   . ILE B 2 139 ? 70.499  78.453  55.384 1.00 160.48 ? 139 ILE B C   1 
ATOM   1106 O  O   . ILE B 2 139 ? 71.397  77.828  55.925 1.00 169.83 ? 139 ILE B O   1 
ATOM   1107 C  CB  . ILE B 2 139 ? 69.207  80.433  56.232 1.00 189.04 ? 139 ILE B CB  1 
ATOM   1108 C  CG1 . ILE B 2 139 ? 69.186  81.952  56.448 1.00 273.55 ? 139 ILE B CG1 1 
ATOM   1109 C  CG2 . ILE B 2 139 ? 69.008  79.669  57.529 1.00 130.38 ? 139 ILE B CG2 1 
ATOM   1110 C  CD1 . ILE B 2 139 ? 70.260  82.501  57.394 1.00 267.99 ? 139 ILE B CD1 1 
ATOM   1111 N  N   . ILE B 2 140 ? 69.500  77.870  54.703 1.00 117.63 ? 140 ILE B N   1 
ATOM   1112 C  CA  . ILE B 2 140 ? 69.218  76.447  54.884 1.00 134.72 ? 140 ILE B CA  1 
ATOM   1113 C  C   . ILE B 2 140 ? 70.440  75.603  54.513 1.00 138.15 ? 140 ILE B C   1 
ATOM   1114 O  O   . ILE B 2 140 ? 70.828  74.713  55.257 1.00 196.12 ? 140 ILE B O   1 
ATOM   1115 C  CB  . ILE B 2 140 ? 67.971  75.966  54.131 1.00 125.12 ? 140 ILE B CB  1 
ATOM   1116 C  CG1 . ILE B 2 140 ? 66.760  76.795  54.493 1.00 140.46 ? 140 ILE B CG1 1 
ATOM   1117 C  CG2 . ILE B 2 140 ? 67.678  74.478  54.353 1.00 215.78 ? 140 ILE B CG2 1 
ATOM   1118 C  CD1 . ILE B 2 140 ? 66.304  76.562  55.874 1.00 164.91 ? 140 ILE B CD1 1 
ATOM   1119 N  N   . ARG B 2 141 ? 71.042  75.898  53.384 1.00 126.33 ? 141 ARG B N   1 
ATOM   1120 C  CA  . ARG B 2 141 ? 72.069  75.032  52.847 1.00 145.62 ? 141 ARG B CA  1 
ATOM   1121 C  C   . ARG B 2 141 ? 73.454  75.368  53.419 1.00 155.53 ? 141 ARG B C   1 
ATOM   1122 O  O   . ARG B 2 141 ? 74.157  74.433  53.741 1.00 131.62 ? 141 ARG B O   1 
ATOM   1123 C  CB  . ARG B 2 141 ? 72.002  75.137  51.323 1.00 195.51 ? 141 ARG B CB  1 
ATOM   1124 C  CG  . ARG B 2 141 ? 72.720  74.025  50.593 1.00 220.17 ? 141 ARG B CG  1 
ATOM   1125 C  CD  . ARG B 2 141 ? 72.262  72.630  50.933 1.00 211.88 ? 141 ARG B CD  1 
ATOM   1126 N  NE  . ARG B 2 141 ? 70.822  72.499  51.010 1.00 216.13 ? 141 ARG B NE  1 
ATOM   1127 C  CZ  . ARG B 2 141 ? 69.940  72.639  50.029 1.00 233.25 ? 141 ARG B CZ  1 
ATOM   1128 N  NH1 . ARG B 2 141 ? 68.662  72.618  50.342 1.00 307.62 ? 141 ARG B NH1 1 
ATOM   1129 N  NH2 . ARG B 2 141 ? 70.287  72.783  48.766 1.00 189.11 ? 141 ARG B NH2 1 
ATOM   1130 N  N   . PRO B 2 142 ? 73.924  76.639  53.585 1.00 156.77 ? 142 PRO B N   1 
ATOM   1131 C  CA  . PRO B 2 142 ? 75.181  76.898  54.281 1.00 144.03 ? 142 PRO B CA  1 
ATOM   1132 C  C   . PRO B 2 142 ? 75.192  76.384  55.717 1.00 160.38 ? 142 PRO B C   1 
ATOM   1133 O  O   . PRO B 2 142 ? 76.186  75.802  56.126 1.00 213.45 ? 142 PRO B O   1 
ATOM   1134 C  CB  . PRO B 2 142 ? 75.299  78.418  54.268 1.00 154.66 ? 142 PRO B CB  1 
ATOM   1135 C  CG  . PRO B 2 142 ? 74.511  78.820  53.051 1.00 162.42 ? 142 PRO B CG  1 
ATOM   1136 C  CD  . PRO B 2 142 ? 73.332  77.902  53.119 1.00 127.77 ? 142 PRO B CD  1 
ATOM   1137 N  N   . SER B 2 143 ? 74.095  76.553  56.472 1.00 150.10 ? 143 SER B N   1 
ATOM   1138 C  CA  . SER B 2 143 ? 74.036  76.031  57.825 1.00 159.28 ? 143 SER B CA  1 
ATOM   1139 C  C   . SER B 2 143 ? 74.111  74.520  57.846 1.00 119.29 ? 143 SER B C   1 
ATOM   1140 O  O   . SER B 2 143 ? 74.913  73.987  58.570 1.00 116.98 ? 143 SER B O   1 
ATOM   1141 C  CB  . SER B 2 143 ? 72.800  76.530  58.554 1.00 238.85 ? 143 SER B CB  1 
ATOM   1142 O  OG  . SER B 2 143 ? 71.598  76.108  57.965 1.00 185.33 ? 143 SER B OG  1 
ATOM   1143 N  N   . SER B 2 144 ? 73.294  73.835  57.040 1.00 106.92 ? 144 SER B N   1 
ATOM   1144 C  CA  . SER B 2 144 ? 73.310  72.376  56.967 1.00 139.53 ? 144 SER B CA  1 
ATOM   1145 C  C   . SER B 2 144 ? 74.688  71.821  56.578 1.00 114.64 ? 144 SER B C   1 
ATOM   1146 O  O   . SER B 2 144 ? 75.158  70.855  57.134 1.00 114.81 ? 144 SER B O   1 
ATOM   1147 C  CB  . SER B 2 144 ? 72.251  71.862  56.018 1.00 126.34 ? 144 SER B CB  1 
ATOM   1148 O  OG  . SER B 2 144 ? 70.985  72.274  56.496 1.00 148.48 ? 144 SER B OG  1 
ATOM   1149 N  N   . GLN B 2 145 ? 75.367  72.415  55.609 1.00 107.18 ? 145 GLN B N   1 
ATOM   1150 C  CA  . GLN B 2 145 ? 76.695  71.979  55.265 1.00 115.93 ? 145 GLN B CA  1 
ATOM   1151 C  C   . GLN B 2 145 ? 77.585  72.184  56.469 1.00 103.02 ? 145 GLN B C   1 
ATOM   1152 O  O   . GLN B 2 145 ? 78.312  71.281  56.826 1.00 120.48 ? 145 GLN B O   1 
ATOM   1153 C  CB  . GLN B 2 145 ? 77.237  72.751  54.047 1.00 137.38 ? 145 GLN B CB  1 
ATOM   1154 C  CG  . GLN B 2 145 ? 76.624  72.303  52.740 1.00 128.16 ? 145 GLN B CG  1 
ATOM   1155 C  CD  . GLN B 2 145 ? 77.242  72.909  51.516 1.00 193.08 ? 145 GLN B CD  1 
ATOM   1156 O  OE1 . GLN B 2 145 ? 76.518  73.389  50.629 1.00 331.57 ? 145 GLN B OE1 1 
ATOM   1157 N  NE2 . GLN B 2 145 ? 78.576  72.882  51.459 1.00 151.09 ? 145 GLN B NE2 1 
ATOM   1158 N  N   . TYR B 2 146 ? 77.578  73.371  57.072 1.00 123.55 ? 146 TYR B N   1 
ATOM   1159 C  CA  . TYR B 2 146 ? 78.541  73.701  58.107 1.00 152.66 ? 146 TYR B CA  1 
ATOM   1160 C  C   . TYR B 2 146 ? 78.337  72.759  59.291 1.00 100.27 ? 146 TYR B C   1 
ATOM   1161 O  O   . TYR B 2 146 ? 79.313  72.169  59.752 1.00 133.10 ? 146 TYR B O   1 
ATOM   1162 C  CB  . TYR B 2 146 ? 78.520  75.208  58.499 1.00 249.21 ? 146 TYR B CB  1 
ATOM   1163 C  CG  . TYR B 2 146 ? 79.312  75.305  59.779 1.00 189.54 ? 146 TYR B CG  1 
ATOM   1164 C  CD1 . TYR B 2 146 ? 80.703  75.059  59.756 1.00 128.26 ? 146 TYR B CD1 1 
ATOM   1165 C  CD2 . TYR B 2 146 ? 78.643  75.567  60.974 1.00 139.02 ? 146 TYR B CD2 1 
ATOM   1166 C  CE1 . TYR B 2 146 ? 81.423  75.072  60.923 1.00 132.62 ? 146 TYR B CE1 1 
ATOM   1167 C  CE2 . TYR B 2 146 ? 79.375  75.571  62.143 1.00 195.08 ? 146 TYR B CE2 1 
ATOM   1168 C  CZ  . TYR B 2 146 ? 80.746  75.323  62.114 1.00 166.43 ? 146 TYR B CZ  1 
ATOM   1169 O  OH  . TYR B 2 146 ? 81.372  75.352  63.327 1.00 152.38 ? 146 TYR B OH  1 
ATOM   1170 N  N   . ILE B 2 147 ? 77.123  72.629  59.832 1.00 116.61 ? 147 ILE B N   1 
ATOM   1171 C  CA  . ILE B 2 147 ? 76.945  71.770  60.995 1.00 171.02 ? 147 ILE B CA  1 
ATOM   1172 C  C   . ILE B 2 147 ? 77.322  70.322  60.685 1.00 146.08 ? 147 ILE B C   1 
ATOM   1173 O  O   . ILE B 2 147 ? 77.897  69.661  61.557 1.00 164.63 ? 147 ILE B O   1 
ATOM   1174 C  CB  . ILE B 2 147 ? 75.539  71.902  61.640 1.00 163.11 ? 147 ILE B CB  1 
ATOM   1175 C  CG1 . ILE B 2 147 ? 74.415  71.174  60.897 1.00 119.15 ? 147 ILE B CG1 1 
ATOM   1176 C  CG2 . ILE B 2 147 ? 75.185  73.381  61.903 1.00 109.73 ? 147 ILE B CG2 1 
ATOM   1177 C  CD1 . ILE B 2 147 ? 73.136  71.120  61.691 1.00 185.00 ? 147 ILE B CD1 1 
ATOM   1178 N  N   . VAL B 2 148 ? 77.028  69.819  59.479 1.00 89.04  ? 148 VAL B N   1 
ATOM   1179 C  CA  . VAL B 2 148 ? 77.381  68.452  59.206 1.00 94.67  ? 148 VAL B CA  1 
ATOM   1180 C  C   . VAL B 2 148 ? 78.880  68.331  59.044 1.00 84.45  ? 148 VAL B C   1 
ATOM   1181 O  O   . VAL B 2 148 ? 79.464  67.308  59.386 1.00 163.26 ? 148 VAL B O   1 
ATOM   1182 C  CB  . VAL B 2 148 ? 76.569  67.842  58.069 1.00 148.70 ? 148 VAL B CB  1 
ATOM   1183 C  CG1 . VAL B 2 148 ? 76.958  66.388  57.808 1.00 147.59 ? 148 VAL B CG1 1 
ATOM   1184 C  CG2 . VAL B 2 148 ? 75.089  67.862  58.418 1.00 268.00 ? 148 VAL B CG2 1 
ATOM   1185 N  N   . ALA B 2 149 ? 79.551  69.337  58.539 1.00 111.58 ? 149 ALA B N   1 
ATOM   1186 C  CA  . ALA B 2 149 ? 81.019  69.358  58.542 1.00 147.00 ? 149 ALA B CA  1 
ATOM   1187 C  C   . ALA B 2 149 ? 81.576  69.382  59.957 1.00 95.49  ? 149 ALA B C   1 
ATOM   1188 O  O   . ALA B 2 149 ? 82.659  68.847  60.201 1.00 88.87  ? 149 ALA B O   1 
ATOM   1189 C  CB  . ALA B 2 149 ? 81.543  70.535  57.721 1.00 140.93 ? 149 ALA B CB  1 
ATOM   1190 N  N   . LEU B 2 150 ? 80.850  70.016  60.885 1.00 133.35 ? 150 LEU B N   1 
ATOM   1191 C  CA  . LEU B 2 150 ? 81.244  70.040  62.283 1.00 168.50 ? 150 LEU B CA  1 
ATOM   1192 C  C   . LEU B 2 150 ? 81.053  68.665  62.911 1.00 128.77 ? 150 LEU B C   1 
ATOM   1193 O  O   . LEU B 2 150 ? 81.901  68.264  63.724 1.00 105.82 ? 150 LEU B O   1 
ATOM   1194 C  CB  . LEU B 2 150 ? 80.452  71.133  63.010 1.00 160.14 ? 150 LEU B CB  1 
ATOM   1195 C  CG  . LEU B 2 150 ? 81.021  71.461  64.369 1.00 219.09 ? 150 LEU B CG  1 
ATOM   1196 C  CD1 . LEU B 2 150 ? 82.433  72.054  64.249 1.00 122.33 ? 150 LEU B CD1 1 
ATOM   1197 C  CD2 . LEU B 2 150 ? 80.088  72.425  65.082 1.00 307.84 ? 150 LEU B CD2 1 
ATOM   1198 N  N   . VAL B 2 151 ? 79.966  67.975  62.535 1.00 98.13  ? 151 VAL B N   1 
ATOM   1199 C  CA  . VAL B 2 151 ? 79.746  66.601  62.976 1.00 126.84 ? 151 VAL B CA  1 
ATOM   1200 C  C   . VAL B 2 151 ? 80.862  65.690  62.482 1.00 90.45  ? 151 VAL B C   1 
ATOM   1201 O  O   . VAL B 2 151 ? 81.373  64.858  63.256 1.00 129.65 ? 151 VAL B O   1 
ATOM   1202 C  CB  . VAL B 2 151 ? 78.364  66.036  62.615 1.00 115.09 ? 151 VAL B CB  1 
ATOM   1203 C  CG1 . VAL B 2 151 ? 78.282  64.558  63.049 1.00 112.99 ? 151 VAL B CG1 1 
ATOM   1204 C  CG2 . VAL B 2 151 ? 77.216  66.824  63.233 1.00 250.31 ? 151 VAL B CG2 1 
ATOM   1205 N  N   . PHE B 2 152 ? 81.296  65.867  61.254 1.00 116.23 ? 152 PHE B N   1 
ATOM   1206 C  CA  . PHE B 2 152 ? 82.476  65.166  60.788 1.00 183.64 ? 152 PHE B CA  1 
ATOM   1207 C  C   . PHE B 2 152 ? 83.675  65.392  61.735 1.00 149.97 ? 152 PHE B C   1 
ATOM   1208 O  O   . PHE B 2 152 ? 84.293  64.439  62.204 1.00 134.46 ? 152 PHE B O   1 
ATOM   1209 C  CB  . PHE B 2 152 ? 82.779  65.553  59.325 1.00 170.14 ? 152 PHE B CB  1 
ATOM   1210 C  CG  . PHE B 2 152 ? 84.220  65.330  58.926 1.00 135.96 ? 152 PHE B CG  1 
ATOM   1211 C  CD1 . PHE B 2 152 ? 84.678  64.073  58.565 1.00 118.33 ? 152 PHE B CD1 1 
ATOM   1212 C  CD2 . PHE B 2 152 ? 85.117  66.382  58.974 1.00 167.99 ? 152 PHE B CD2 1 
ATOM   1213 C  CE1 . PHE B 2 152 ? 85.988  63.881  58.229 1.00 157.21 ? 152 PHE B CE1 1 
ATOM   1214 C  CE2 . PHE B 2 152 ? 86.441  66.205  58.622 1.00 207.81 ? 152 PHE B CE2 1 
ATOM   1215 C  CZ  . PHE B 2 152 ? 86.865  64.950  58.249 1.00 253.53 ? 152 PHE B CZ  1 
ATOM   1216 N  N   . ALA B 2 153 ? 84.010  66.645  62.008 1.00 107.05 ? 153 ALA B N   1 
ATOM   1217 C  CA  . ALA B 2 153 ? 85.173  66.948  62.804 1.00 152.00 ? 153 ALA B CA  1 
ATOM   1218 C  C   . ALA B 2 153 ? 85.050  66.384  64.227 1.00 140.85 ? 153 ALA B C   1 
ATOM   1219 O  O   . ALA B 2 153 ? 85.973  65.741  64.743 1.00 129.63 ? 153 ALA B O   1 
ATOM   1220 C  CB  . ALA B 2 153 ? 85.391  68.455  62.818 1.00 182.24 ? 153 ALA B CB  1 
ATOM   1221 N  N   . THR B 2 154 ? 83.932  66.646  64.904 1.00 112.24 ? 154 THR B N   1 
ATOM   1222 C  CA  . THR B 2 154 ? 83.854  66.348  66.320 1.00 156.84 ? 154 THR B CA  1 
ATOM   1223 C  C   . THR B 2 154 ? 83.868  64.836  66.541 1.00 131.43 ? 154 THR B C   1 
ATOM   1224 O  O   . THR B 2 154 ? 84.423  64.387  67.548 1.00 131.31 ? 154 THR B O   1 
ATOM   1225 C  CB  . THR B 2 154 ? 82.675  67.101  66.977 1.00 199.58 ? 154 THR B CB  1 
ATOM   1226 O  OG1 . THR B 2 154 ? 82.800  66.994  68.394 1.00 302.67 ? 154 THR B OG1 1 
ATOM   1227 C  CG2 . THR B 2 154 ? 81.313  66.565  66.612 1.00 236.46 ? 154 THR B CG2 1 
ATOM   1228 N  N   . TYR B 2 155 ? 83.239  64.046  65.659 1.00 135.40 ? 155 TYR B N   1 
ATOM   1229 C  CA  . TYR B 2 155 ? 83.295  62.595  65.783 1.00 131.49 ? 155 TYR B CA  1 
ATOM   1230 C  C   . TYR B 2 155 ? 84.635  62.053  65.306 1.00 105.93 ? 155 TYR B C   1 
ATOM   1231 O  O   . TYR B 2 155 ? 85.128  61.104  65.916 1.00 161.29 ? 155 TYR B O   1 
ATOM   1232 C  CB  . TYR B 2 155 ? 82.165  61.871  65.068 1.00 99.42  ? 155 TYR B CB  1 
ATOM   1233 C  CG  . TYR B 2 155 ? 80.862  61.876  65.824 1.00 122.70 ? 155 TYR B CG  1 
ATOM   1234 C  CD1 . TYR B 2 155 ? 80.080  63.020  65.881 1.00 182.38 ? 155 TYR B CD1 1 
ATOM   1235 C  CD2 . TYR B 2 155 ? 80.409  60.752  66.473 1.00 159.98 ? 155 TYR B CD2 1 
ATOM   1236 C  CE1 . TYR B 2 155 ? 78.875  63.055  66.560 1.00 241.06 ? 155 TYR B CE1 1 
ATOM   1237 C  CE2 . TYR B 2 155 ? 79.205  60.767  67.167 1.00 223.97 ? 155 TYR B CE2 1 
ATOM   1238 C  CZ  . TYR B 2 155 ? 78.434  61.918  67.215 1.00 244.22 ? 155 TYR B CZ  1 
ATOM   1239 O  OH  . TYR B 2 155 ? 77.242  61.941  67.882 1.00 255.71 ? 155 TYR B OH  1 
ATOM   1240 N  N   . LEU B 2 156 ? 85.255  62.632  64.279 1.00 108.48 ? 156 LEU B N   1 
ATOM   1241 C  CA  . LEU B 2 156 ? 86.518  62.090  63.782 1.00 166.19 ? 156 LEU B CA  1 
ATOM   1242 C  C   . LEU B 2 156 ? 87.634  62.249  64.817 1.00 147.66 ? 156 LEU B C   1 
ATOM   1243 O  O   . LEU B 2 156 ? 88.479  61.365  64.955 1.00 177.12 ? 156 LEU B O   1 
ATOM   1244 C  CB  . LEU B 2 156 ? 86.898  62.780  62.461 1.00 171.55 ? 156 LEU B CB  1 
ATOM   1245 C  CG  . LEU B 2 156 ? 88.109  62.166  61.789 1.00 203.03 ? 156 LEU B CG  1 
ATOM   1246 C  CD1 . LEU B 2 156 ? 87.724  60.783  61.270 1.00 204.96 ? 156 LEU B CD1 1 
ATOM   1247 C  CD2 . LEU B 2 156 ? 88.668  63.087  60.730 1.00 222.69 ? 156 LEU B CD2 1 
ATOM   1248 N  N   . LEU B 2 157 ? 87.629  63.364  65.534 1.00 111.94 ? 157 LEU B N   1 
ATOM   1249 C  CA  . LEU B 2 157 ? 88.601  63.593  66.577 1.00 130.72 ? 157 LEU B CA  1 
ATOM   1250 C  C   . LEU B 2 157 ? 88.294  62.835  67.875 1.00 146.77 ? 157 LEU B C   1 
ATOM   1251 O  O   . LEU B 2 157 ? 89.183  62.744  68.713 1.00 179.78 ? 157 LEU B O   1 
ATOM   1252 C  CB  . LEU B 2 157 ? 88.597  65.103  66.842 1.00 167.46 ? 157 LEU B CB  1 
ATOM   1253 C  CG  . LEU B 2 157 ? 89.217  65.946  65.743 1.00 142.05 ? 157 LEU B CG  1 
ATOM   1254 C  CD1 . LEU B 2 157 ? 89.038  67.458  66.116 1.00 95.19  ? 157 LEU B CD1 1 
ATOM   1255 C  CD2 . LEU B 2 157 ? 90.670  65.441  65.451 1.00 95.34  ? 157 LEU B CD2 1 
ATOM   1256 N  N   . LYS B 2 158 ? 87.076  62.308  68.076 1.00 153.95 ? 158 LYS B N   1 
ATOM   1257 C  CA  . LYS B 2 158 ? 86.593  61.819  69.368 1.00 133.26 ? 158 LYS B CA  1 
ATOM   1258 C  C   . LYS B 2 158 ? 87.527  60.799  70.013 1.00 134.50 ? 158 LYS B C   1 
ATOM   1259 O  O   . LYS B 2 158 ? 87.749  60.917  71.209 1.00 213.86 ? 158 LYS B O   1 
ATOM   1260 C  CB  . LYS B 2 158 ? 85.176  61.248  69.216 1.00 185.50 ? 158 LYS B CB  1 
ATOM   1261 C  CG  . LYS B 2 158 ? 84.377  61.044  70.505 1.00 184.04 ? 158 LYS B CG  1 
ATOM   1262 C  CD  . LYS B 2 158 ? 84.098  62.332  71.251 1.00 239.85 ? 158 LYS B CD  1 
ATOM   1263 C  CE  . LYS B 2 158 ? 82.915  62.267  72.205 1.00 286.14 ? 158 LYS B CE  1 
ATOM   1264 N  NZ  . LYS B 2 158 ? 81.573  62.343  71.540 1.00 256.95 ? 158 LYS B NZ  1 
ATOM   1265 N  N   . PRO B 2 159 ? 88.134  59.797  69.343 1.00 112.80 ? 159 PRO B N   1 
ATOM   1266 C  CA  . PRO B 2 159 ? 89.072  58.894  70.010 1.00 171.32 ? 159 PRO B CA  1 
ATOM   1267 C  C   . PRO B 2 159 ? 90.417  59.492  70.473 1.00 166.81 ? 159 PRO B C   1 
ATOM   1268 O  O   . PRO B 2 159 ? 91.115  58.839  71.251 1.00 191.58 ? 159 PRO B O   1 
ATOM   1269 C  CB  . PRO B 2 159 ? 89.316  57.799  68.969 1.00 188.49 ? 159 PRO B CB  1 
ATOM   1270 C  CG  . PRO B 2 159 ? 89.152  58.507  67.699 1.00 200.53 ? 159 PRO B CG  1 
ATOM   1271 C  CD  . PRO B 2 159 ? 87.998  59.459  67.950 1.00 124.83 ? 159 PRO B CD  1 
ATOM   1272 N  N   . LEU B 2 160 ? 90.777  60.719  70.067 1.00 151.33 ? 160 LEU B N   1 
ATOM   1273 C  CA  . LEU B 2 160 ? 91.872  61.443  70.723 1.00 172.67 ? 160 LEU B CA  1 
ATOM   1274 C  C   . LEU B 2 160 ? 91.430  62.217  71.971 1.00 151.73 ? 160 LEU B C   1 
ATOM   1275 O  O   . LEU B 2 160 ? 92.303  62.721  72.676 1.00 141.29 ? 160 LEU B O   1 
ATOM   1276 C  CB  . LEU B 2 160 ? 92.537  62.405  69.737 1.00 173.04 ? 160 LEU B CB  1 
ATOM   1277 C  CG  . LEU B 2 160 ? 93.041  61.756  68.445 1.00 331.51 ? 160 LEU B CG  1 
ATOM   1278 C  CD1 . LEU B 2 160 ? 93.798  62.781  67.617 1.00 417.96 ? 160 LEU B CD1 1 
ATOM   1279 C  CD2 . LEU B 2 160 ? 93.939  60.544  68.686 1.00 364.45 ? 160 LEU B CD2 1 
ATOM   1280 N  N   . PHE B 2 161 ? 90.108  62.288  72.238 1.00 126.20 ? 161 PHE B N   1 
ATOM   1281 C  CA  . PHE B 2 161 ? 89.541  62.925  73.408 1.00 159.00 ? 161 PHE B CA  1 
ATOM   1282 C  C   . PHE B 2 161 ? 88.358  62.115  73.951 1.00 164.65 ? 161 PHE B C   1 
ATOM   1283 O  O   . PHE B 2 161 ? 87.239  62.623  74.012 1.00 246.50 ? 161 PHE B O   1 
ATOM   1284 C  CB  . PHE B 2 161 ? 89.145  64.358  73.027 1.00 168.38 ? 161 PHE B CB  1 
ATOM   1285 C  CG  . PHE B 2 161 ? 90.280  65.258  72.598 1.00 161.25 ? 161 PHE B CG  1 
ATOM   1286 C  CD1 . PHE B 2 161 ? 90.752  65.247  71.299 1.00 174.35 ? 161 PHE B CD1 1 
ATOM   1287 C  CD2 . PHE B 2 161 ? 90.875  66.108  73.508 1.00 193.98 ? 161 PHE B CD2 1 
ATOM   1288 C  CE1 . PHE B 2 161 ? 91.796  66.070  70.914 1.00 208.25 ? 161 PHE B CE1 1 
ATOM   1289 C  CE2 . PHE B 2 161 ? 91.926  66.916  73.127 1.00 222.80 ? 161 PHE B CE2 1 
ATOM   1290 C  CZ  . PHE B 2 161 ? 92.377  66.901  71.832 1.00 225.90 ? 161 PHE B CZ  1 
ATOM   1291 N  N   . PRO B 2 162 ? 88.540  60.844  74.378 1.00 146.47 ? 162 PRO B N   1 
ATOM   1292 C  CA  . PRO B 2 162 ? 87.408  59.937  74.599 1.00 200.96 ? 162 PRO B CA  1 
ATOM   1293 C  C   . PRO B 2 162 ? 86.349  60.357  75.622 1.00 226.74 ? 162 PRO B C   1 
ATOM   1294 O  O   . PRO B 2 162 ? 85.196  59.936  75.488 1.00 269.85 ? 162 PRO B O   1 
ATOM   1295 C  CB  . PRO B 2 162 ? 88.089  58.638  75.073 1.00 236.99 ? 162 PRO B CB  1 
ATOM   1296 C  CG  . PRO B 2 162 ? 89.484  58.736  74.493 1.00 228.19 ? 162 PRO B CG  1 
ATOM   1297 C  CD  . PRO B 2 162 ? 89.829  60.200  74.639 1.00 171.81 ? 162 PRO B CD  1 
ATOM   1298 N  N   . THR B 2 163 ? 86.741  61.163  76.638 1.00 183.97 ? 163 THR B N   1 
ATOM   1299 C  CA  . THR B 2 163 ? 85.906  61.401  77.814 1.00 225.43 ? 163 THR B CA  1 
ATOM   1300 C  C   . THR B 2 163 ? 85.631  62.882  78.071 1.00 196.15 ? 163 THR B C   1 
ATOM   1301 O  O   . THR B 2 163 ? 85.051  63.221  79.099 1.00 268.86 ? 163 THR B O   1 
ATOM   1302 C  CB  . THR B 2 163 ? 86.546  60.763  79.057 1.00 326.00 ? 163 THR B CB  1 
ATOM   1303 O  OG1 . THR B 2 163 ? 87.875  61.264  79.203 1.00 299.15 ? 163 THR B OG1 1 
ATOM   1304 C  CG2 . THR B 2 163 ? 86.583  59.252  78.992 1.00 391.92 ? 163 THR B CG2 1 
ATOM   1305 N  N   . CYS B 2 164 ? 86.023  63.763  77.145 1.00 174.29 ? 164 CYS B N   1 
ATOM   1306 C  CA  . CYS B 2 164 ? 85.889  65.208  77.334 1.00 188.05 ? 164 CYS B CA  1 
ATOM   1307 C  C   . CYS B 2 164 ? 85.673  65.900  75.990 1.00 192.85 ? 164 CYS B C   1 
ATOM   1308 O  O   . CYS B 2 164 ? 86.051  65.349  74.953 1.00 303.58 ? 164 CYS B O   1 
ATOM   1309 C  CB  . CYS B 2 164 ? 87.091  65.771  78.090 1.00 211.90 ? 164 CYS B CB  1 
ATOM   1310 S  SG  . CYS B 2 164 ? 88.664  65.845  77.190 1.00 221.52 ? 164 CYS B SG  1 
ATOM   1311 N  N   . PRO B 2 165 ? 85.050  67.103  75.927 1.00 172.16 ? 165 PRO B N   1 
ATOM   1312 C  CA  . PRO B 2 165 ? 84.830  67.761  74.642 1.00 222.88 ? 165 PRO B CA  1 
ATOM   1313 C  C   . PRO B 2 165 ? 86.134  68.037  73.891 1.00 226.73 ? 165 PRO B C   1 
ATOM   1314 O  O   . PRO B 2 165 ? 87.130  68.459  74.482 1.00 225.24 ? 165 PRO B O   1 
ATOM   1315 C  CB  . PRO B 2 165 ? 84.136  69.077  75.023 1.00 286.38 ? 165 PRO B CB  1 
ATOM   1316 C  CG  . PRO B 2 165 ? 83.473  68.759  76.345 1.00 297.88 ? 165 PRO B CG  1 
ATOM   1317 C  CD  . PRO B 2 165 ? 84.492  67.881  77.042 1.00 206.79 ? 165 PRO B CD  1 
ATOM   1318 N  N   . VAL B 2 166 ? 86.115  67.811  72.566 1.00 187.97 ? 166 VAL B N   1 
ATOM   1319 C  CA  . VAL B 2 166 ? 87.239  68.129  71.697 1.00 139.80 ? 166 VAL B CA  1 
ATOM   1320 C  C   . VAL B 2 166 ? 87.402  69.647  71.616 1.00 189.91 ? 166 VAL B C   1 
ATOM   1321 O  O   . VAL B 2 166 ? 86.417  70.405  71.659 1.00 166.41 ? 166 VAL B O   1 
ATOM   1322 C  CB  . VAL B 2 166 ? 87.030  67.560  70.286 1.00 194.07 ? 166 VAL B CB  1 
ATOM   1323 C  CG1 . VAL B 2 166 ? 87.009  66.059  70.295 1.00 190.57 ? 166 VAL B CG1 1 
ATOM   1324 C  CG2 . VAL B 2 166 ? 85.756  68.045  69.590 1.00 255.54 ? 166 VAL B CG2 1 
ATOM   1325 N  N   . PRO B 2 167 ? 88.657  70.157  71.509 1.00 194.38 ? 167 PRO B N   1 
ATOM   1326 C  CA  . PRO B 2 167 ? 88.880  71.604  71.542 1.00 216.47 ? 167 PRO B CA  1 
ATOM   1327 C  C   . PRO B 2 167 ? 88.273  72.296  70.315 1.00 179.55 ? 167 PRO B C   1 
ATOM   1328 O  O   . PRO B 2 167 ? 88.422  71.833  69.177 1.00 157.55 ? 167 PRO B O   1 
ATOM   1329 C  CB  . PRO B 2 167 ? 90.410  71.715  71.659 1.00 236.03 ? 167 PRO B CB  1 
ATOM   1330 C  CG  . PRO B 2 167 ? 90.944  70.367  71.176 1.00 213.56 ? 167 PRO B CG  1 
ATOM   1331 C  CD  . PRO B 2 167 ? 89.870  69.341  71.429 1.00 126.86 ? 167 PRO B CD  1 
ATOM   1332 N  N   . GLU B 2 168 ? 87.609  73.427  70.574 1.00 180.59 ? 168 GLU B N   1 
ATOM   1333 C  CA  . GLU B 2 168 ? 86.761  74.124  69.606 1.00 247.77 ? 168 GLU B CA  1 
ATOM   1334 C  C   . GLU B 2 168 ? 87.515  74.566  68.338 1.00 213.27 ? 168 GLU B C   1 
ATOM   1335 O  O   . GLU B 2 168 ? 87.024  74.388  67.224 1.00 122.76 ? 168 GLU B O   1 
ATOM   1336 C  CB  . GLU B 2 168 ? 86.118  75.364  70.236 1.00 291.86 ? 168 GLU B CB  1 
ATOM   1337 C  CG  . GLU B 2 168 ? 85.318  75.087  71.503 1.00 390.41 ? 168 GLU B CG  1 
ATOM   1338 C  CD  . GLU B 2 168 ? 86.062  75.269  72.821 1.00 483.06 ? 168 GLU B CD  1 
ATOM   1339 O  OE1 . GLU B 2 168 ? 87.110  74.613  73.006 1.00 459.54 ? 168 GLU B OE1 1 
ATOM   1340 O  OE2 . GLU B 2 168 ? 85.595  76.066  73.664 1.00 580.55 ? 168 GLU B OE2 1 
ATOM   1341 N  N   . GLU B 2 169 ? 88.709  75.146  68.479 1.00 196.61 ? 169 GLU B N   1 
ATOM   1342 C  CA  . GLU B 2 169 ? 89.513  75.521  67.331 1.00 180.72 ? 169 GLU B CA  1 
ATOM   1343 C  C   . GLU B 2 169 ? 89.843  74.310  66.442 1.00 122.13 ? 169 GLU B C   1 
ATOM   1344 O  O   . GLU B 2 169 ? 89.829  74.401  65.216 1.00 165.34 ? 169 GLU B O   1 
ATOM   1345 C  CB  . GLU B 2 169 ? 90.785  76.221  67.828 1.00 253.14 ? 169 GLU B CB  1 
ATOM   1346 C  CG  . GLU B 2 169 ? 90.524  77.653  68.318 1.00 362.66 ? 169 GLU B CG  1 
ATOM   1347 C  CD  . GLU B 2 169 ? 90.275  78.749  67.276 1.00 414.08 ? 169 GLU B CD  1 
ATOM   1348 O  OE1 . GLU B 2 169 ? 89.452  78.539  66.351 1.00 346.30 ? 169 GLU B OE1 1 
ATOM   1349 O  OE2 . GLU B 2 169 ? 90.902  79.840  67.385 1.00 411.69 ? 169 GLU B OE2 1 
ATOM   1350 N  N   . ALA B 2 170 ? 90.196  73.168  67.033 1.00 155.83 ? 170 ALA B N   1 
ATOM   1351 C  CA  . ALA B 2 170 ? 90.513  71.971  66.263 1.00 165.36 ? 170 ALA B CA  1 
ATOM   1352 C  C   . ALA B 2 170 ? 89.267  71.492  65.524 1.00 133.98 ? 170 ALA B C   1 
ATOM   1353 O  O   . ALA B 2 170 ? 89.327  71.130  64.366 1.00 128.43 ? 170 ALA B O   1 
ATOM   1354 C  CB  . ALA B 2 170 ? 91.108  70.905  67.167 1.00 171.78 ? 170 ALA B CB  1 
ATOM   1355 N  N   . ALA B 2 171 ? 88.118  71.504  66.181 1.00 136.89 ? 171 ALA B N   1 
ATOM   1356 C  CA  . ALA B 2 171 ? 86.875  71.138  65.530 1.00 139.60 ? 171 ALA B CA  1 
ATOM   1357 C  C   . ALA B 2 171 ? 86.610  72.091  64.383 1.00 113.56 ? 171 ALA B C   1 
ATOM   1358 O  O   . ALA B 2 171 ? 86.396  71.608  63.272 1.00 171.83 ? 171 ALA B O   1 
ATOM   1359 C  CB  . ALA B 2 171 ? 85.723  71.153  66.518 1.00 213.55 ? 171 ALA B CB  1 
ATOM   1360 N  N   . LYS B 2 172 ? 86.613  73.419  64.598 1.00 73.69  ? 172 LYS B N   1 
ATOM   1361 C  CA  . LYS B 2 172 ? 86.312  74.323  63.490 1.00 138.40 ? 172 LYS B CA  1 
ATOM   1362 C  C   . LYS B 2 172 ? 87.333  74.271  62.339 1.00 119.42 ? 172 LYS B C   1 
ATOM   1363 O  O   . LYS B 2 172 ? 86.940  74.296  61.181 1.00 98.70  ? 172 LYS B O   1 
ATOM   1364 C  CB  . LYS B 2 172 ? 86.094  75.739  63.996 1.00 148.96 ? 172 LYS B CB  1 
ATOM   1365 C  CG  . LYS B 2 172 ? 84.720  75.920  64.636 1.00 131.48 ? 172 LYS B CG  1 
ATOM   1366 C  CD  . LYS B 2 172 ? 84.459  77.420  64.945 1.00 219.03 ? 172 LYS B CD  1 
ATOM   1367 C  CE  . LYS B 2 172 ? 83.028  77.744  65.347 1.00 192.36 ? 172 LYS B CE  1 
ATOM   1368 N  NZ  . LYS B 2 172 ? 82.630  77.156  66.650 1.00 248.98 ? 172 LYS B NZ  1 
ATOM   1369 N  N   . LEU B 2 173 ? 88.614  74.135  62.610 1.00 117.81 ? 173 LEU B N   1 
ATOM   1370 C  CA  . LEU B 2 173 ? 89.584  73.957  61.540 1.00 145.12 ? 173 LEU B CA  1 
ATOM   1371 C  C   . LEU B 2 173 ? 89.279  72.677  60.783 1.00 90.87  ? 173 LEU B C   1 
ATOM   1372 O  O   . LEU B 2 173 ? 89.243  72.713  59.553 1.00 143.18 ? 173 LEU B O   1 
ATOM   1373 C  CB  . LEU B 2 173 ? 91.055  73.915  62.022 1.00 131.75 ? 173 LEU B CB  1 
ATOM   1374 C  CG  . LEU B 2 173 ? 91.619  75.226  62.571 1.00 172.18 ? 173 LEU B CG  1 
ATOM   1375 C  CD1 . LEU B 2 173 ? 93.077  74.964  62.789 1.00 156.44 ? 173 LEU B CD1 1 
ATOM   1376 C  CD2 . LEU B 2 173 ? 91.370  76.520  61.751 1.00 177.97 ? 173 LEU B CD2 1 
ATOM   1377 N  N   . VAL B 2 174 ? 89.105  71.556  61.473 1.00 91.27  ? 174 VAL B N   1 
ATOM   1378 C  CA  . VAL B 2 174 ? 88.928  70.295  60.786 1.00 127.80 ? 174 VAL B CA  1 
ATOM   1379 C  C   . VAL B 2 174 ? 87.630  70.330  59.989 1.00 100.70 ? 174 VAL B C   1 
ATOM   1380 O  O   . VAL B 2 174 ? 87.587  69.749  58.892 1.00 194.14 ? 174 VAL B O   1 
ATOM   1381 C  CB  . VAL B 2 174 ? 89.077  69.100  61.742 1.00 152.77 ? 174 VAL B CB  1 
ATOM   1382 C  CG1 . VAL B 2 174 ? 88.638  67.788  61.117 1.00 229.30 ? 174 VAL B CG1 1 
ATOM   1383 C  CG2 . VAL B 2 174 ? 90.535  68.975  62.161 1.00 164.77 ? 174 VAL B CG2 1 
ATOM   1384 N  N   . ALA B 2 175 ? 86.601  70.994  60.494 1.00 99.12  ? 175 ALA B N   1 
ATOM   1385 C  CA  . ALA B 2 175 ? 85.346  71.145  59.763 1.00 135.32 ? 175 ALA B CA  1 
ATOM   1386 C  C   . ALA B 2 175 ? 85.600  71.911  58.489 1.00 114.94 ? 175 ALA B C   1 
ATOM   1387 O  O   . ALA B 2 175 ? 85.109  71.520  57.407 1.00 158.29 ? 175 ALA B O   1 
ATOM   1388 C  CB  . ALA B 2 175 ? 84.291  71.827  60.602 1.00 151.35 ? 175 ALA B CB  1 
ATOM   1389 N  N   . CYS B 2 176 ? 86.331  73.033  58.594 1.00 74.34  ? 176 CYS B N   1 
ATOM   1390 C  CA  . CYS B 2 176 ? 86.524  73.862  57.416 1.00 113.95 ? 176 CYS B CA  1 
ATOM   1391 C  C   . CYS B 2 176 ? 87.481  73.236  56.390 1.00 108.93 ? 176 CYS B C   1 
ATOM   1392 O  O   . CYS B 2 176 ? 87.288  73.401  55.179 1.00 125.80 ? 176 CYS B O   1 
ATOM   1393 C  CB  . CYS B 2 176 ? 86.846  75.243  57.907 1.00 134.05 ? 176 CYS B CB  1 
ATOM   1394 S  SG  . CYS B 2 176 ? 85.370  75.761  58.838 1.00 197.38 ? 176 CYS B SG  1 
ATOM   1395 N  N   . LEU B 2 177 ? 88.484  72.521  56.854 1.00 107.02 ? 177 LEU B N   1 
ATOM   1396 C  CA  . LEU B 2 177 ? 89.372  71.789  55.964 1.00 124.56 ? 177 LEU B CA  1 
ATOM   1397 C  C   . LEU B 2 177 ? 88.588  70.792  55.129 1.00 112.98 ? 177 LEU B C   1 
ATOM   1398 O  O   . LEU B 2 177 ? 88.941  70.604  53.955 1.00 208.92 ? 177 LEU B O   1 
ATOM   1399 C  CB  . LEU B 2 177 ? 90.440  71.067  56.792 1.00 182.74 ? 177 LEU B CB  1 
ATOM   1400 C  CG  . LEU B 2 177 ? 91.560  72.000  57.263 1.00 193.23 ? 177 LEU B CG  1 
ATOM   1401 C  CD1 . LEU B 2 177 ? 92.366  71.372  58.389 1.00 230.06 ? 177 LEU B CD1 1 
ATOM   1402 C  CD2 . LEU B 2 177 ? 92.471  72.391  56.104 1.00 188.15 ? 177 LEU B CD2 1 
ATOM   1403 N  N   . CYS B 2 178 ? 87.555  70.168  55.712 1.00 90.23  ? 178 CYS B N   1 
ATOM   1404 C  CA  . CYS B 2 178 ? 86.634  69.319  54.968 1.00 176.59 ? 178 CYS B CA  1 
ATOM   1405 C  C   . CYS B 2 178 ? 85.876  70.099  53.872 1.00 134.86 ? 178 CYS B C   1 
ATOM   1406 O  O   . CYS B 2 178 ? 85.890  69.707  52.694 1.00 132.30 ? 178 CYS B O   1 
ATOM   1407 C  CB  . CYS B 2 178 ? 85.691  68.617  55.938 1.00 215.28 ? 178 CYS B CB  1 
ATOM   1408 S  SG  . CYS B 2 178 ? 84.180  67.999  55.155 1.00 198.96 ? 178 CYS B SG  1 
ATOM   1409 N  N   . VAL B 2 179 ? 85.237  71.204  54.229 1.00 79.66  ? 179 VAL B N   1 
ATOM   1410 C  CA  . VAL B 2 179 ? 84.530  71.964  53.221 1.00 116.33 ? 179 VAL B CA  1 
ATOM   1411 C  C   . VAL B 2 179 ? 85.459  72.471  52.101 1.00 114.02 ? 179 VAL B C   1 
ATOM   1412 O  O   . VAL B 2 179 ? 85.096  72.416  50.932 1.00 127.27 ? 179 VAL B O   1 
ATOM   1413 C  CB  . VAL B 2 179 ? 83.718  73.104  53.866 1.00 158.21 ? 179 VAL B CB  1 
ATOM   1414 C  CG1 . VAL B 2 179 ? 83.027  74.018  52.859 1.00 191.01 ? 179 VAL B CG1 1 
ATOM   1415 C  CG2 . VAL B 2 179 ? 82.656  72.514  54.790 1.00 170.90 ? 179 VAL B CG2 1 
ATOM   1416 N  N   . LEU B 2 180 ? 86.644  72.978  52.408 1.00 129.47 ? 180 LEU B N   1 
ATOM   1417 C  CA  . LEU B 2 180 ? 87.600  73.392  51.380 1.00 120.43 ? 180 LEU B CA  1 
ATOM   1418 C  C   . LEU B 2 180 ? 88.033  72.238  50.480 1.00 107.43 ? 180 LEU B C   1 
ATOM   1419 O  O   . LEU B 2 180 ? 88.002  72.389  49.250 1.00 140.94 ? 180 LEU B O   1 
ATOM   1420 C  CB  . LEU B 2 180 ? 88.855  73.945  52.046 1.00 127.99 ? 180 LEU B CB  1 
ATOM   1421 C  CG  . LEU B 2 180 ? 88.700  75.300  52.708 1.00 196.59 ? 180 LEU B CG  1 
ATOM   1422 C  CD1 . LEU B 2 180 ? 89.883  75.568  53.631 1.00 298.40 ? 180 LEU B CD1 1 
ATOM   1423 C  CD2 . LEU B 2 180 ? 88.570  76.386  51.662 1.00 181.32 ? 180 LEU B CD2 1 
ATOM   1424 N  N   . LEU B 2 181 ? 88.458  71.109  51.068 1.00 87.71  ? 181 LEU B N   1 
ATOM   1425 C  CA  . LEU B 2 181 ? 88.892  69.978  50.260 1.00 93.60  ? 181 LEU B CA  1 
ATOM   1426 C  C   . LEU B 2 181 ? 87.750  69.445  49.372 1.00 110.08 ? 181 LEU B C   1 
ATOM   1427 O  O   . LEU B 2 181 ? 87.958  69.193  48.182 1.00 131.10 ? 181 LEU B O   1 
ATOM   1428 C  CB  . LEU B 2 181 ? 89.414  68.872  51.146 1.00 103.10 ? 181 LEU B CB  1 
ATOM   1429 C  CG  . LEU B 2 181 ? 89.677  67.550  50.442 1.00 139.45 ? 181 LEU B CG  1 
ATOM   1430 C  CD1 . LEU B 2 181 ? 90.847  67.735  49.519 1.00 213.99 ? 181 LEU B CD1 1 
ATOM   1431 C  CD2 . LEU B 2 181 ? 89.962  66.437  51.433 1.00 291.91 ? 181 LEU B CD2 1 
ATOM   1432 N  N   . LEU B 2 182 ? 86.539  69.310  49.890 1.00 88.69  ? 182 LEU B N   1 
ATOM   1433 C  CA  . LEU B 2 182 ? 85.449  68.841  49.057 1.00 156.34 ? 182 LEU B CA  1 
ATOM   1434 C  C   . LEU B 2 182 ? 85.093  69.835  47.959 1.00 142.61 ? 182 LEU B C   1 
ATOM   1435 O  O   . LEU B 2 182 ? 84.711  69.411  46.855 1.00 199.34 ? 182 LEU B O   1 
ATOM   1436 C  CB  . LEU B 2 182 ? 84.230  68.584  49.941 1.00 187.97 ? 182 LEU B CB  1 
ATOM   1437 C  CG  . LEU B 2 182 ? 84.383  67.344  50.792 1.00 221.27 ? 182 LEU B CG  1 
ATOM   1438 C  CD1 . LEU B 2 182 ? 83.199  67.273  51.720 1.00 235.70 ? 182 LEU B CD1 1 
ATOM   1439 C  CD2 . LEU B 2 182 ? 84.553  66.085  49.917 1.00 176.79 ? 182 LEU B CD2 1 
ATOM   1440 N  N   . THR B 2 183 ? 85.208  71.136  48.225 1.00 85.65  ? 183 THR B N   1 
ATOM   1441 C  CA  . THR B 2 183 ? 84.967  72.091  47.172 1.00 102.62 ? 183 THR B CA  1 
ATOM   1442 C  C   . THR B 2 183 ? 85.961  71.871  46.040 1.00 105.00 ? 183 THR B C   1 
ATOM   1443 O  O   . THR B 2 183 ? 85.592  71.941  44.871 1.00 127.86 ? 183 THR B O   1 
ATOM   1444 C  CB  . THR B 2 183 ? 85.022  73.532  47.690 1.00 170.15 ? 183 THR B CB  1 
ATOM   1445 O  OG1 . THR B 2 183 ? 84.057  73.689  48.720 1.00 108.52 ? 183 THR B OG1 1 
ATOM   1446 C  CG2 . THR B 2 183 ? 84.728  74.567  46.623 1.00 224.96 ? 183 THR B CG2 1 
ATOM   1447 N  N   . ALA B 2 184 ? 87.239  71.667  46.351 1.00 133.27 ? 184 ALA B N   1 
ATOM   1448 C  CA  . ALA B 2 184 ? 88.243  71.479  45.321 1.00 163.05 ? 184 ALA B CA  1 
ATOM   1449 C  C   . ALA B 2 184 ? 87.909  70.212  44.537 1.00 108.47 ? 184 ALA B C   1 
ATOM   1450 O  O   . ALA B 2 184 ? 87.974  70.217  43.297 1.00 205.92 ? 184 ALA B O   1 
ATOM   1451 C  CB  . ALA B 2 184 ? 89.628  71.448  45.921 1.00 216.43 ? 184 ALA B CB  1 
ATOM   1452 N  N   . VAL B 2 185 ? 87.569  69.123  45.215 1.00 83.20  ? 185 VAL B N   1 
ATOM   1453 C  CA  . VAL B 2 185 ? 87.248  67.894  44.506 1.00 144.33 ? 185 VAL B CA  1 
ATOM   1454 C  C   . VAL B 2 185 ? 86.065  68.084  43.564 1.00 111.28 ? 185 VAL B C   1 
ATOM   1455 O  O   . VAL B 2 185 ? 86.070  67.548  42.450 1.00 186.03 ? 185 VAL B O   1 
ATOM   1456 C  CB  . VAL B 2 185 ? 87.018  66.729  45.465 1.00 212.98 ? 185 VAL B CB  1 
ATOM   1457 C  CG1 . VAL B 2 185 ? 86.416  65.527  44.738 1.00 158.26 ? 185 VAL B CG1 1 
ATOM   1458 C  CG2 . VAL B 2 185 ? 88.332  66.366  46.151 1.00 266.76 ? 185 VAL B CG2 1 
ATOM   1459 N  N   . ASN B 2 186 ? 85.088  68.863  43.975 1.00 116.87 ? 186 ASN B N   1 
ATOM   1460 C  CA  . ASN B 2 186 ? 83.930  69.149  43.140 1.00 158.41 ? 186 ASN B CA  1 
ATOM   1461 C  C   . ASN B 2 186 ? 84.291  70.074  41.984 1.00 140.98 ? 186 ASN B C   1 
ATOM   1462 O  O   . ASN B 2 186 ? 83.619  70.001  40.944 1.00 224.11 ? 186 ASN B O   1 
ATOM   1463 C  CB  . ASN B 2 186 ? 82.754  69.666  43.979 1.00 150.01 ? 186 ASN B CB  1 
ATOM   1464 C  CG  . ASN B 2 186 ? 82.058  68.537  44.679 1.00 173.25 ? 186 ASN B CG  1 
ATOM   1465 O  OD1 . ASN B 2 186 ? 81.067  68.063  44.180 1.00 200.28 ? 186 ASN B OD1 1 
ATOM   1466 N  ND2 . ASN B 2 186 ? 82.583  68.055  45.790 1.00 205.92 ? 186 ASN B ND2 1 
ATOM   1467 N  N   . CYS B 2 187 ? 85.318  70.931  42.143 1.00 105.42 ? 187 CYS B N   1 
ATOM   1468 C  CA  . CYS B 2 187 ? 85.761  71.807  41.059 1.00 181.55 ? 187 CYS B CA  1 
ATOM   1469 C  C   . CYS B 2 187 ? 86.532  71.054  39.982 1.00 141.85 ? 187 CYS B C   1 
ATOM   1470 O  O   . CYS B 2 187 ? 86.352  71.406  38.814 1.00 170.19 ? 187 CYS B O   1 
ATOM   1471 C  CB  . CYS B 2 187 ? 86.579  72.978  41.580 1.00 217.22 ? 187 CYS B CB  1 
ATOM   1472 S  SG  . CYS B 2 187 ? 85.524  74.126  42.505 1.00 288.60 ? 187 CYS B SG  1 
ATOM   1473 N  N   . TYR B 2 188 ? 87.340  70.050  40.347 1.00 111.70 ? 188 TYR B N   1 
ATOM   1474 C  CA  . TYR B 2 188 ? 88.221  69.357  39.395 1.00 156.46 ? 188 TYR B CA  1 
ATOM   1475 C  C   . TYR B 2 188 ? 87.435  68.452  38.459 1.00 136.75 ? 188 TYR B C   1 
ATOM   1476 O  O   . TYR B 2 188 ? 87.746  68.443  37.245 1.00 278.95 ? 188 TYR B O   1 
ATOM   1477 C  CB  . TYR B 2 188 ? 89.434  68.574  39.965 1.00 115.90 ? 188 TYR B CB  1 
ATOM   1478 C  CG  . TYR B 2 188 ? 90.463  69.601  40.481 1.00 281.20 ? 188 TYR B CG  1 
ATOM   1479 C  CD1 . TYR B 2 188 ? 90.986  70.583  39.614 1.00 235.03 ? 188 TYR B CD1 1 
ATOM   1480 C  CD2 . TYR B 2 188 ? 90.905  69.628  41.818 1.00 412.21 ? 188 TYR B CD2 1 
ATOM   1481 C  CE1 . TYR B 2 188 ? 91.902  71.531  40.042 1.00 175.29 ? 188 TYR B CE1 1 
ATOM   1482 C  CE2 . TYR B 2 188 ? 91.836  70.569  42.241 1.00 372.73 ? 188 TYR B CE2 1 
ATOM   1483 C  CZ  . TYR B 2 188 ? 92.330  71.520  41.358 1.00 296.18 ? 188 TYR B CZ  1 
ATOM   1484 O  OH  . TYR B 2 188 ? 93.237  72.445  41.794 1.00 403.17 ? 188 TYR B OH  1 
ATOM   1485 N  N   . SER B 2 189 ? 86.454  67.731  38.989 1.00 167.92 ? 189 SER B N   1 
ATOM   1486 C  CA  . SER B 2 189 ? 85.830  66.719  38.162 1.00 222.37 ? 189 SER B CA  1 
ATOM   1487 C  C   . SER B 2 189 ? 84.513  66.199  38.737 1.00 178.52 ? 189 SER B C   1 
ATOM   1488 O  O   . SER B 2 189 ? 84.515  65.670  39.849 1.00 232.26 ? 189 SER B O   1 
ATOM   1489 C  CB  . SER B 2 189 ? 86.834  65.585  37.949 1.00 190.71 ? 189 SER B CB  1 
ATOM   1490 O  OG  . SER B 2 189 ? 86.230  64.507  37.246 1.00 164.33 ? 189 SER B OG  1 
ATOM   1491 N  N   . VAL B 2 190 ? 83.425  66.270  37.955 1.00 138.09 ? 190 VAL B N   1 
ATOM   1492 C  CA  . VAL B 2 190 ? 82.188  65.567  38.291 1.00 189.19 ? 190 VAL B CA  1 
ATOM   1493 C  C   . VAL B 2 190 ? 82.432  64.055  38.471 1.00 174.80 ? 190 VAL B C   1 
ATOM   1494 O  O   . VAL B 2 190 ? 81.835  63.393  39.334 1.00 152.33 ? 190 VAL B O   1 
ATOM   1495 C  CB  . VAL B 2 190 ? 81.064  65.828  37.265 1.00 184.40 ? 190 VAL B CB  1 
ATOM   1496 C  CG1 . VAL B 2 190 ? 79.770  65.058  37.631 1.00 148.73 ? 190 VAL B CG1 1 
ATOM   1497 C  CG2 . VAL B 2 190 ? 80.803  67.327  37.135 1.00 219.38 ? 190 VAL B CG2 1 
ATOM   1498 N  N   . LYS B 2 191 ? 83.311  63.498  37.643 1.00 165.63 ? 191 LYS B N   1 
ATOM   1499 C  CA  . LYS B 2 191 ? 83.681  62.107  37.721 1.00 186.81 ? 191 LYS B CA  1 
ATOM   1500 C  C   . LYS B 2 191 ? 84.362  61.848  39.063 1.00 185.62 ? 191 LYS B C   1 
ATOM   1501 O  O   . LYS B 2 191 ? 84.032  60.848  39.715 1.00 271.61 ? 191 LYS B O   1 
ATOM   1502 C  CB  . LYS B 2 191 ? 84.566  61.741  36.522 1.00 284.37 ? 191 LYS B CB  1 
ATOM   1503 C  CG  . LYS B 2 191 ? 84.265  60.374  35.936 1.00 287.06 ? 191 LYS B CG  1 
ATOM   1504 C  CD  . LYS B 2 191 ? 82.937  60.308  35.229 1.00 224.52 ? 191 LYS B CD  1 
ATOM   1505 C  CE  . LYS B 2 191 ? 82.742  58.980  34.532 1.00 381.11 ? 191 LYS B CE  1 
ATOM   1506 N  NZ  . LYS B 2 191 ? 81.478  58.915  33.763 1.00 460.40 ? 191 LYS B NZ  1 
ATOM   1507 N  N   . ALA B 2 192 ? 85.287  62.721  39.497 1.00 134.89 ? 192 ALA B N   1 
ATOM   1508 C  CA  . ALA B 2 192 ? 85.937  62.555  40.793 1.00 239.45 ? 192 ALA B CA  1 
ATOM   1509 C  C   . ALA B 2 192 ? 84.914  62.656  41.929 1.00 203.56 ? 192 ALA B C   1 
ATOM   1510 O  O   . ALA B 2 192 ? 84.850  61.772  42.779 1.00 186.72 ? 192 ALA B O   1 
ATOM   1511 C  CB  . ALA B 2 192 ? 87.068  63.543  40.971 1.00 303.24 ? 192 ALA B CB  1 
ATOM   1512 N  N   . ALA B 2 193 ? 84.089  63.697  41.954 1.00 172.18 ? 193 ALA B N   1 
ATOM   1513 C  CA  . ALA B 2 193 ? 83.154  63.876  43.052 1.00 169.48 ? 193 ALA B CA  1 
ATOM   1514 C  C   . ALA B 2 193 ? 82.156  62.717  43.129 1.00 192.41 ? 193 ALA B C   1 
ATOM   1515 O  O   . ALA B 2 193 ? 81.826  62.278  44.228 1.00 239.16 ? 193 ALA B O   1 
ATOM   1516 C  CB  . ALA B 2 193 ? 82.471  65.223  42.938 1.00 149.38 ? 193 ALA B CB  1 
ATOM   1517 N  N   . THR B 2 194 ? 81.668  62.185  41.998 1.00 150.34 ? 194 THR B N   1 
ATOM   1518 C  CA  . THR B 2 194 ? 80.731  61.071  42.030 1.00 151.87 ? 194 THR B CA  1 
ATOM   1519 C  C   . THR B 2 194 ? 81.412  59.770  42.444 1.00 131.58 ? 194 THR B C   1 
ATOM   1520 O  O   . THR B 2 194 ? 80.795  58.971  43.158 1.00 191.17 ? 194 THR B O   1 
ATOM   1521 C  CB  . THR B 2 194 ? 79.956  60.925  40.724 1.00 177.07 ? 194 THR B CB  1 
ATOM   1522 O  OG1 . THR B 2 194 ? 80.878  60.871  39.634 1.00 150.21 ? 194 THR B OG1 1 
ATOM   1523 C  CG2 . THR B 2 194 ? 78.971  62.061  40.542 1.00 220.05 ? 194 THR B CG2 1 
ATOM   1524 N  N   . ARG B 2 195 ? 82.664  59.551  42.041 1.00 155.08 ? 195 ARG B N   1 
ATOM   1525 C  CA  . ARG B 2 195 ? 83.419  58.376  42.488 1.00 218.19 ? 195 ARG B CA  1 
ATOM   1526 C  C   . ARG B 2 195 ? 83.816  58.495  43.964 1.00 190.39 ? 195 ARG B C   1 
ATOM   1527 O  O   . ARG B 2 195 ? 83.950  57.477  44.633 1.00 157.53 ? 195 ARG B O   1 
ATOM   1528 C  CB  . ARG B 2 195 ? 84.620  58.134  41.564 1.00 276.80 ? 195 ARG B CB  1 
ATOM   1529 C  CG  . ARG B 2 195 ? 84.194  57.568  40.215 1.00 265.39 ? 195 ARG B CG  1 
ATOM   1530 C  CD  . ARG B 2 195 ? 85.250  57.688  39.134 1.00 274.52 ? 195 ARG B CD  1 
ATOM   1531 N  NE  . ARG B 2 195 ? 86.415  56.849  39.367 1.00 319.40 ? 195 ARG B NE  1 
ATOM   1532 C  CZ  . ARG B 2 195 ? 87.559  56.917  38.682 1.00 366.48 ? 195 ARG B CZ  1 
ATOM   1533 N  NH1 . ARG B 2 195 ? 88.519  56.033  38.904 1.00 410.34 ? 195 ARG B NH1 1 
ATOM   1534 N  NH2 . ARG B 2 195 ? 87.748  57.862  37.773 1.00 330.50 ? 195 ARG B NH2 1 
ATOM   1535 N  N   . VAL B 2 196 ? 83.991  59.716  44.494 1.00 153.53 ? 196 VAL B N   1 
ATOM   1536 C  CA  . VAL B 2 196 ? 84.089  59.942  45.937 1.00 192.29 ? 196 VAL B CA  1 
ATOM   1537 C  C   . VAL B 2 196 ? 82.778  59.592  46.631 1.00 138.18 ? 196 VAL B C   1 
ATOM   1538 O  O   . VAL B 2 196 ? 82.769  58.982  47.681 1.00 130.35 ? 196 VAL B O   1 
ATOM   1539 C  CB  . VAL B 2 196 ? 84.549  61.372  46.279 1.00 159.21 ? 196 VAL B CB  1 
ATOM   1540 C  CG1 . VAL B 2 196 ? 84.395  61.743  47.750 1.00 116.05 ? 196 VAL B CG1 1 
ATOM   1541 C  CG2 . VAL B 2 196 ? 86.014  61.527  45.907 1.00 257.25 ? 196 VAL B CG2 1 
ATOM   1542 N  N   . GLN B 2 197 ? 81.674  59.965  46.062 1.00 141.42 ? 197 GLN B N   1 
ATOM   1543 C  CA  . GLN B 2 197 ? 80.389  59.714  46.691 1.00 190.41 ? 197 GLN B CA  1 
ATOM   1544 C  C   . GLN B 2 197 ? 80.074  58.217  46.840 1.00 175.33 ? 197 GLN B C   1 
ATOM   1545 O  O   . GLN B 2 197 ? 79.448  57.854  47.832 1.00 227.85 ? 197 GLN B O   1 
ATOM   1546 C  CB  . GLN B 2 197 ? 79.294  60.464  45.913 1.00 248.80 ? 197 GLN B CB  1 
ATOM   1547 C  CG  . GLN B 2 197 ? 77.970  60.511  46.648 1.00 187.80 ? 197 GLN B CG  1 
ATOM   1548 C  CD  . GLN B 2 197 ? 78.021  61.245  47.960 1.00 170.05 ? 197 GLN B CD  1 
ATOM   1549 O  OE1 . GLN B 2 197 ? 78.973  61.966  48.255 1.00 117.11 ? 197 GLN B OE1 1 
ATOM   1550 N  NE2 . GLN B 2 197 ? 76.991  61.062  48.781 1.00 221.69 ? 197 GLN B NE2 1 
ATOM   1551 N  N   . ASP B 2 198 ? 80.503  57.349  45.921 1.00 151.03 ? 198 ASP B N   1 
ATOM   1552 C  CA  . ASP B 2 198 ? 80.439  55.904  46.121 1.00 285.06 ? 198 ASP B CA  1 
ATOM   1553 C  C   . ASP B 2 198 ? 81.125  55.530  47.438 1.00 227.28 ? 198 ASP B C   1 
ATOM   1554 O  O   . ASP B 2 198 ? 80.526  54.866  48.292 1.00 214.99 ? 198 ASP B O   1 
ATOM   1555 C  CB  . ASP B 2 198 ? 81.049  55.125  44.938 1.00 455.79 ? 198 ASP B CB  1 
ATOM   1556 C  CG  . ASP B 2 198 ? 81.274  53.623  45.154 1.00 481.35 ? 198 ASP B CG  1 
ATOM   1557 O  OD1 . ASP B 2 198 ? 80.395  52.987  45.770 1.00 442.66 ? 198 ASP B OD1 1 
ATOM   1558 O  OD2 . ASP B 2 198 ? 82.328  53.076  44.710 1.00 323.24 ? 198 ASP B OD2 1 
ATOM   1559 N  N   . ALA B 2 199 ? 82.389  55.953  47.616 1.00 119.68 ? 199 ALA B N   1 
ATOM   1560 C  CA  . ALA B 2 199 ? 83.207  55.478  48.722 1.00 229.48 ? 199 ALA B CA  1 
ATOM   1561 C  C   . ALA B 2 199 ? 82.488  55.752  50.045 1.00 179.91 ? 199 ALA B C   1 
ATOM   1562 O  O   . ALA B 2 199 ? 82.420  54.901  50.939 1.00 157.78 ? 199 ALA B O   1 
ATOM   1563 C  CB  . ALA B 2 199 ? 84.594  56.101  48.659 1.00 222.88 ? 199 ALA B CB  1 
ATOM   1564 N  N   . PHE B 2 200 ? 81.947  56.968  50.193 1.00 177.43 ? 200 PHE B N   1 
ATOM   1565 C  CA  . PHE B 2 200 ? 81.329  57.384  51.445 1.00 174.87 ? 200 PHE B CA  1 
ATOM   1566 C  C   . PHE B 2 200 ? 79.840  57.081  51.514 1.00 157.53 ? 200 PHE B C   1 
ATOM   1567 O  O   . PHE B 2 200 ? 79.247  57.282  52.573 1.00 218.53 ? 200 PHE B O   1 
ATOM   1568 C  CB  . PHE B 2 200 ? 81.696  58.836  51.738 1.00 156.71 ? 200 PHE B CB  1 
ATOM   1569 C  CG  . PHE B 2 200 ? 83.192  59.030  51.870 1.00 161.56 ? 200 PHE B CG  1 
ATOM   1570 C  CD1 . PHE B 2 200 ? 83.929  58.316  52.817 1.00 172.13 ? 200 PHE B CD1 1 
ATOM   1571 C  CD2 . PHE B 2 200 ? 83.877  59.876  51.016 1.00 172.13 ? 200 PHE B CD2 1 
ATOM   1572 C  CE1 . PHE B 2 200 ? 85.298  58.429  52.919 1.00 155.09 ? 200 PHE B CE1 1 
ATOM   1573 C  CE2 . PHE B 2 200 ? 85.255  60.016  51.130 1.00 185.17 ? 200 PHE B CE2 1 
ATOM   1574 C  CZ  . PHE B 2 200 ? 85.957  59.297  52.081 1.00 232.12 ? 200 PHE B CZ  1 
ATOM   1575 N  N   . ALA B 2 201 ? 79.222  56.592  50.439 1.00 174.83 ? 201 ALA B N   1 
ATOM   1576 C  CA  . ALA B 2 201 ? 77.944  55.905  50.535 1.00 191.23 ? 201 ALA B CA  1 
ATOM   1577 C  C   . ALA B 2 201 ? 78.199  54.525  51.122 1.00 163.19 ? 201 ALA B C   1 
ATOM   1578 O  O   . ALA B 2 201 ? 77.487  54.107  52.040 1.00 166.66 ? 201 ALA B O   1 
ATOM   1579 C  CB  . ALA B 2 201 ? 77.270  55.848  49.186 1.00 240.45 ? 201 ALA B CB  1 
ATOM   1580 N  N   . ALA B 2 202 ? 79.215  53.824  50.604 1.00 121.29 ? 202 ALA B N   1 
ATOM   1581 C  CA  . ALA B 2 202 ? 79.553  52.493  51.050 1.00 214.95 ? 202 ALA B CA  1 
ATOM   1582 C  C   . ALA B 2 202 ? 79.892  52.567  52.527 1.00 182.88 ? 202 ALA B C   1 
ATOM   1583 O  O   . ALA B 2 202 ? 79.394  51.714  53.267 1.00 145.02 ? 202 ALA B O   1 
ATOM   1584 C  CB  . ALA B 2 202 ? 80.674  51.927  50.189 1.00 302.44 ? 202 ALA B CB  1 
ATOM   1585 N  N   . ALA B 2 203 ? 80.720  53.540  52.953 1.00 180.22 ? 203 ALA B N   1 
ATOM   1586 C  CA  . ALA B 2 203 ? 81.178  53.693  54.339 1.00 219.02 ? 203 ALA B CA  1 
ATOM   1587 C  C   . ALA B 2 203 ? 80.032  53.677  55.344 1.00 127.10 ? 203 ALA B C   1 
ATOM   1588 O  O   . ALA B 2 203 ? 80.141  52.991  56.383 1.00 199.28 ? 203 ALA B O   1 
ATOM   1589 C  CB  . ALA B 2 203 ? 82.037  54.917  54.525 1.00 200.50 ? 203 ALA B CB  1 
ATOM   1590 N  N   . LYS B 2 204 ? 78.948  54.366  55.027 1.00 108.94 ? 204 LYS B N   1 
ATOM   1591 C  CA  . LYS B 2 204 ? 77.755  54.325  55.883 1.00 190.12 ? 204 LYS B CA  1 
ATOM   1592 C  C   . LYS B 2 204 ? 77.099  52.948  55.969 1.00 218.72 ? 204 LYS B C   1 
ATOM   1593 O  O   . LYS B 2 204 ? 76.793  52.489  57.061 1.00 173.13 ? 204 LYS B O   1 
ATOM   1594 C  CB  . LYS B 2 204 ? 76.665  55.244  55.361 1.00 188.42 ? 204 LYS B CB  1 
ATOM   1595 C  CG  . LYS B 2 204 ? 77.100  56.680  55.333 1.00 179.20 ? 204 LYS B CG  1 
ATOM   1596 C  CD  . LYS B 2 204 ? 76.105  57.610  54.849 1.00 176.88 ? 204 LYS B CD  1 
ATOM   1597 C  CE  . LYS B 2 204 ? 76.599  59.031  54.803 1.00 164.55 ? 204 LYS B CE  1 
ATOM   1598 N  NZ  . LYS B 2 204 ? 77.607  59.275  53.739 1.00 169.44 ? 204 LYS B NZ  1 
ATOM   1599 N  N   . LEU B 2 205 ? 76.894  52.304  54.817 1.00 196.97 ? 205 LEU B N   1 
ATOM   1600 C  CA  . LEU B 2 205 ? 76.232  51.010  54.759 1.00 198.70 ? 205 LEU B CA  1 
ATOM   1601 C  C   . LEU B 2 205 ? 77.101  49.953  55.441 1.00 206.70 ? 205 LEU B C   1 
ATOM   1602 O  O   . LEU B 2 205 ? 76.549  49.083  56.106 1.00 205.77 ? 205 LEU B O   1 
ATOM   1603 C  CB  . LEU B 2 205 ? 75.887  50.706  53.303 1.00 168.71 ? 205 LEU B CB  1 
ATOM   1604 C  CG  . LEU B 2 205 ? 74.857  51.677  52.705 1.00 228.65 ? 205 LEU B CG  1 
ATOM   1605 C  CD1 . LEU B 2 205 ? 74.759  51.496  51.201 1.00 339.46 ? 205 LEU B CD1 1 
ATOM   1606 C  CD2 . LEU B 2 205 ? 73.469  51.518  53.330 1.00 243.35 ? 205 LEU B CD2 1 
ATOM   1607 N  N   . LEU B 2 206 ? 78.441  50.061  55.333 1.00 170.73 ? 206 LEU B N   1 
ATOM   1608 C  CA  . LEU B 2 206 ? 79.383  49.212  56.065 1.00 165.02 ? 206 LEU B CA  1 
ATOM   1609 C  C   . LEU B 2 206 ? 79.293  49.442  57.563 1.00 160.35 ? 206 LEU B C   1 
ATOM   1610 O  O   . LEU B 2 206 ? 79.230  48.463  58.319 1.00 168.55 ? 206 LEU B O   1 
ATOM   1611 C  CB  . LEU B 2 206 ? 80.801  49.467  55.548 1.00 205.02 ? 206 LEU B CB  1 
ATOM   1612 C  CG  . LEU B 2 206 ? 81.067  48.882  54.151 1.00 366.03 ? 206 LEU B CG  1 
ATOM   1613 C  CD1 . LEU B 2 206 ? 82.374  49.402  53.566 1.00 422.76 ? 206 LEU B CD1 1 
ATOM   1614 C  CD2 . LEU B 2 206 ? 81.086  47.353  54.157 1.00 442.83 ? 206 LEU B CD2 1 
ATOM   1615 N  N   . ALA B 2 207 ? 79.261  50.709  57.992 1.00 208.29 ? 207 ALA B N   1 
ATOM   1616 C  CA  . ALA B 2 207 ? 79.114  51.050  59.412 1.00 233.55 ? 207 ALA B CA  1 
ATOM   1617 C  C   . ALA B 2 207 ? 77.798  50.540  60.017 1.00 214.31 ? 207 ALA B C   1 
ATOM   1618 O  O   . ALA B 2 207 ? 77.797  49.898  61.062 1.00 214.66 ? 207 ALA B O   1 
ATOM   1619 C  CB  . ALA B 2 207 ? 79.220  52.529  59.581 1.00 216.19 ? 207 ALA B CB  1 
ATOM   1620 N  N   . LEU B 2 208 ? 76.680  50.780  59.341 1.00 139.43 ? 208 LEU B N   1 
ATOM   1621 C  CA  . LEU B 2 208 ? 75.396  50.281  59.800 1.00 147.14 ? 208 LEU B CA  1 
ATOM   1622 C  C   . LEU B 2 208 ? 75.311  48.751  59.700 1.00 197.12 ? 208 LEU B C   1 
ATOM   1623 O  O   . LEU B 2 208 ? 74.642  48.128  60.532 1.00 212.94 ? 208 LEU B O   1 
ATOM   1624 C  CB  . LEU B 2 208 ? 74.309  50.976  58.988 1.00 140.62 ? 208 LEU B CB  1 
ATOM   1625 C  CG  . LEU B 2 208 ? 74.265  52.465  59.239 1.00 154.96 ? 208 LEU B CG  1 
ATOM   1626 C  CD1 . LEU B 2 208 ? 73.364  53.131  58.235 1.00 201.96 ? 208 LEU B CD1 1 
ATOM   1627 C  CD2 . LEU B 2 208 ? 73.765  52.729  60.644 1.00 224.63 ? 208 LEU B CD2 1 
ATOM   1628 N  N   . ALA B 2 209 ? 75.992  48.131  58.723 1.00 159.78 ? 209 ALA B N   1 
ATOM   1629 C  CA  . ALA B 2 209 ? 76.141  46.688  58.704 1.00 197.83 ? 209 ALA B CA  1 
ATOM   1630 C  C   . ALA B 2 209 ? 76.882  46.219  59.950 1.00 141.13 ? 209 ALA B C   1 
ATOM   1631 O  O   . ALA B 2 209 ? 76.480  45.210  60.540 1.00 187.42 ? 209 ALA B O   1 
ATOM   1632 C  CB  . ALA B 2 209 ? 76.824  46.227  57.430 1.00 287.47 ? 209 ALA B CB  1 
ATOM   1633 N  N   . LEU B 2 210 ? 77.949  46.918  60.353 1.00 141.71 ? 210 LEU B N   1 
ATOM   1634 C  CA  . LEU B 2 210 ? 78.656  46.586  61.592 1.00 180.74 ? 210 LEU B CA  1 
ATOM   1635 C  C   . LEU B 2 210 ? 77.755  46.709  62.834 1.00 144.10 ? 210 LEU B C   1 
ATOM   1636 O  O   . LEU B 2 210 ? 77.772  45.828  63.673 1.00 155.60 ? 210 LEU B O   1 
ATOM   1637 C  CB  . LEU B 2 210 ? 79.912  47.448  61.701 1.00 160.52 ? 210 LEU B CB  1 
ATOM   1638 C  CG  . LEU B 2 210 ? 80.824  47.169  62.872 1.00 199.98 ? 210 LEU B CG  1 
ATOM   1639 C  CD1 . LEU B 2 210 ? 81.329  45.737  62.863 1.00 286.06 ? 210 LEU B CD1 1 
ATOM   1640 C  CD2 . LEU B 2 210 ? 81.996  48.115  62.785 1.00 256.80 ? 210 LEU B CD2 1 
ATOM   1641 N  N   . ILE B 2 211 ? 76.937  47.745  62.935 1.00 164.12 ? 211 ILE B N   1 
ATOM   1642 C  CA  . ILE B 2 211 ? 75.929  47.843  63.991 1.00 186.21 ? 211 ILE B CA  1 
ATOM   1643 C  C   . ILE B 2 211 ? 74.960  46.646  63.951 1.00 173.51 ? 211 ILE B C   1 
ATOM   1644 O  O   . ILE B 2 211 ? 74.744  46.013  64.984 1.00 204.74 ? 211 ILE B O   1 
ATOM   1645 C  CB  . ILE B 2 211 ? 75.162  49.195  63.942 1.00 198.99 ? 211 ILE B CB  1 
ATOM   1646 C  CG1 . ILE B 2 211 ? 76.102  50.422  64.020 1.00 163.11 ? 211 ILE B CG1 1 
ATOM   1647 C  CG2 . ILE B 2 211 ? 74.055  49.229  65.017 1.00 135.15 ? 211 ILE B CG2 1 
ATOM   1648 C  CD1 . ILE B 2 211 ? 76.974  50.513  65.291 1.00 180.92 ? 211 ILE B CD1 1 
ATOM   1649 N  N   . ILE B 2 212 ? 74.373  46.326  62.785 1.00 152.44 ? 212 ILE B N   1 
ATOM   1650 C  CA  . ILE B 2 212 ? 73.423  45.218  62.679 1.00 184.52 ? 212 ILE B CA  1 
ATOM   1651 C  C   . ILE B 2 212 ? 74.083  43.863  62.995 1.00 204.28 ? 212 ILE B C   1 
ATOM   1652 O  O   . ILE B 2 212 ? 73.480  43.035  63.697 1.00 243.89 ? 212 ILE B O   1 
ATOM   1653 C  CB  . ILE B 2 212 ? 72.746  45.222  61.302 1.00 206.10 ? 212 ILE B CB  1 
ATOM   1654 C  CG1 . ILE B 2 212 ? 71.809  46.418  61.181 1.00 242.29 ? 212 ILE B CG1 1 
ATOM   1655 C  CG2 . ILE B 2 212 ? 72.003  43.915  61.016 1.00 277.81 ? 212 ILE B CG2 1 
ATOM   1656 C  CD1 . ILE B 2 212 ? 71.376  46.691  59.748 1.00 332.81 ? 212 ILE B CD1 1 
ATOM   1657 N  N   . LEU B 2 213 ? 75.309  43.648  62.496 1.00 165.38 ? 213 LEU B N   1 
ATOM   1658 C  CA  . LEU B 2 213 ? 76.102  42.465  62.814 1.00 202.14 ? 213 LEU B CA  1 
ATOM   1659 C  C   . LEU B 2 213 ? 76.274  42.282  64.337 1.00 214.11 ? 213 LEU B C   1 
ATOM   1660 O  O   . LEU B 2 213 ? 75.980  41.212  64.870 1.00 206.64 ? 213 LEU B O   1 
ATOM   1661 C  CB  . LEU B 2 213 ? 77.446  42.592  62.084 1.00 209.18 ? 213 LEU B CB  1 
ATOM   1662 C  CG  . LEU B 2 213 ? 78.513  41.544  62.388 1.00 275.58 ? 213 LEU B CG  1 
ATOM   1663 C  CD1 . LEU B 2 213 ? 78.084  40.182  61.866 1.00 402.39 ? 213 LEU B CD1 1 
ATOM   1664 C  CD2 . LEU B 2 213 ? 79.841  41.963  61.794 1.00 239.16 ? 213 LEU B CD2 1 
ATOM   1665 N  N   . LEU B 2 214 ? 76.741  43.316  65.049 1.00 206.70 ? 214 LEU B N   1 
ATOM   1666 C  CA  . LEU B 2 214 ? 76.877  43.239  66.495 1.00 176.41 ? 214 LEU B CA  1 
ATOM   1667 C  C   . LEU B 2 214 ? 75.517  42.968  67.150 1.00 164.12 ? 214 LEU B C   1 
ATOM   1668 O  O   . LEU B 2 214 ? 75.448  42.185  68.097 1.00 251.96 ? 214 LEU B O   1 
ATOM   1669 C  CB  . LEU B 2 214 ? 77.513  44.537  67.030 1.00 229.64 ? 214 LEU B CB  1 
ATOM   1670 C  CG  . LEU B 2 214 ? 79.038  44.592  67.161 1.00 259.33 ? 214 LEU B CG  1 
ATOM   1671 C  CD1 . LEU B 2 214 ? 79.558  43.463  68.044 1.00 399.34 ? 214 LEU B CD1 1 
ATOM   1672 C  CD2 . LEU B 2 214 ? 79.729  44.538  65.819 1.00 193.29 ? 214 LEU B CD2 1 
ATOM   1673 N  N   . GLY B 2 215 ? 74.430  43.600  66.680 1.00 157.74 ? 215 GLY B N   1 
ATOM   1674 C  CA  . GLY B 2 215 ? 73.084  43.365  67.203 1.00 209.19 ? 215 GLY B CA  1 
ATOM   1675 C  C   . GLY B 2 215 ? 72.641  41.903  67.110 1.00 193.71 ? 215 GLY B C   1 
ATOM   1676 O  O   . GLY B 2 215 ? 72.230  41.308  68.115 1.00 244.66 ? 215 GLY B O   1 
ATOM   1677 N  N   . PHE B 2 216 ? 72.750  41.321  65.915 1.00 165.61 ? 216 PHE B N   1 
ATOM   1678 C  CA  . PHE B 2 216 ? 72.433  39.912  65.724 1.00 242.55 ? 216 PHE B CA  1 
ATOM   1679 C  C   . PHE B 2 216 ? 73.342  38.998  66.556 1.00 246.66 ? 216 PHE B C   1 
ATOM   1680 O  O   . PHE B 2 216 ? 72.838  37.999  67.082 1.00 286.47 ? 216 PHE B O   1 
ATOM   1681 C  CB  . PHE B 2 216 ? 72.456  39.575  64.228 1.00 325.26 ? 216 PHE B CB  1 
ATOM   1682 C  CG  . PHE B 2 216 ? 71.234  39.980  63.424 1.00 367.43 ? 216 PHE B CG  1 
ATOM   1683 C  CD1 . PHE B 2 216 ? 70.204  40.776  63.936 1.00 359.52 ? 216 PHE B CD1 1 
ATOM   1684 C  CD2 . PHE B 2 216 ? 71.097  39.515  62.115 1.00 385.71 ? 216 PHE B CD2 1 
ATOM   1685 C  CE1 . PHE B 2 216 ? 69.098  41.105  63.162 1.00 398.30 ? 216 PHE B CE1 1 
ATOM   1686 C  CE2 . PHE B 2 216 ? 69.990  39.845  61.342 1.00 369.79 ? 216 PHE B CE2 1 
ATOM   1687 C  CZ  . PHE B 2 216 ? 68.993  40.640  61.867 1.00 402.91 ? 216 PHE B CZ  1 
ATOM   1688 N  N   . VAL B 2 217 ? 74.641  39.324  66.690 1.00 212.52 ? 217 VAL B N   1 
ATOM   1689 C  CA  . VAL B 2 217 ? 75.543  38.567  67.559 1.00 242.79 ? 217 VAL B CA  1 
ATOM   1690 C  C   . VAL B 2 217 ? 75.061  38.591  69.018 1.00 197.64 ? 217 VAL B C   1 
ATOM   1691 O  O   . VAL B 2 217 ? 75.061  37.541  69.662 1.00 235.84 ? 217 VAL B O   1 
ATOM   1692 C  CB  . VAL B 2 217 ? 77.012  39.023  67.406 1.00 290.55 ? 217 VAL B CB  1 
ATOM   1693 C  CG1 . VAL B 2 217 ? 77.932  38.584  68.547 1.00 313.44 ? 217 VAL B CG1 1 
ATOM   1694 C  CG2 . VAL B 2 217 ? 77.568  38.548  66.074 1.00 358.89 ? 217 VAL B CG2 1 
ATOM   1695 N  N   . GLN B 2 218 ? 74.631  39.744  69.546 1.00 220.80 ? 218 GLN B N   1 
ATOM   1696 C  CA  . GLN B 2 218 ? 74.110  39.778  70.907 1.00 271.59 ? 218 GLN B CA  1 
ATOM   1697 C  C   . GLN B 2 218 ? 72.787  38.992  71.045 1.00 296.81 ? 218 GLN B C   1 
ATOM   1698 O  O   . GLN B 2 218 ? 72.580  38.354  72.096 1.00 419.22 ? 218 GLN B O   1 
ATOM   1699 C  CB  . GLN B 2 218 ? 73.986  41.210  71.437 1.00 243.63 ? 218 GLN B CB  1 
ATOM   1700 C  CG  . GLN B 2 218 ? 73.578  41.226  72.910 1.00 268.21 ? 218 GLN B CG  1 
ATOM   1701 C  CD  . GLN B 2 218 ? 74.011  42.421  73.711 1.00 296.25 ? 218 GLN B CD  1 
ATOM   1702 O  OE1 . GLN B 2 218 ? 74.247  43.483  73.155 1.00 222.31 ? 218 GLN B OE1 1 
ATOM   1703 N  NE2 . GLN B 2 218 ? 74.104  42.256  75.024 1.00 366.58 ? 218 GLN B NE2 1 
ATOM   1704 N  N   . ILE B 2 219 ? 71.901  38.991  70.026 1.00 194.16 ? 219 ILE B N   1 
ATOM   1705 C  CA  . ILE B 2 219 ? 70.716  38.132  70.068 1.00 219.42 ? 219 ILE B CA  1 
ATOM   1706 C  C   . ILE B 2 219 ? 71.126  36.645  70.080 1.00 355.23 ? 219 ILE B C   1 
ATOM   1707 O  O   . ILE B 2 219 ? 70.516  35.851  70.797 1.00 423.61 ? 219 ILE B O   1 
ATOM   1708 C  CB  . ILE B 2 219 ? 69.744  38.470  68.919 1.00 344.69 ? 219 ILE B CB  1 
ATOM   1709 C  CG1 . ILE B 2 219 ? 69.137  39.859  69.117 1.00 416.13 ? 219 ILE B CG1 1 
ATOM   1710 C  CG2 . ILE B 2 219 ? 68.642  37.418  68.763 1.00 381.19 ? 219 ILE B CG2 1 
ATOM   1711 C  CD1 . ILE B 2 219 ? 68.590  40.499  67.851 1.00 456.78 ? 219 ILE B CD1 1 
ATOM   1712 N  N   . GLY B 2 220 ? 72.153  36.251  69.304 1.00 382.30 ? 220 GLY B N   1 
ATOM   1713 C  CA  . GLY B 2 220 ? 72.686  34.888  69.298 1.00 360.71 ? 220 GLY B CA  1 
ATOM   1714 C  C   . GLY B 2 220 ? 73.331  34.454  70.622 1.00 390.60 ? 220 GLY B C   1 
ATOM   1715 O  O   . GLY B 2 220 ? 73.154  33.306  71.030 1.00 387.94 ? 220 GLY B O   1 
ATOM   1716 N  N   . LYS B 2 221 ? 74.066  35.364  71.286 1.00 387.66 ? 221 LYS B N   1 
ATOM   1717 C  CA  . LYS B 2 221 ? 74.695  35.108  72.584 1.00 355.69 ? 221 LYS B CA  1 
ATOM   1718 C  C   . LYS B 2 221 ? 73.708  35.166  73.760 1.00 343.41 ? 221 LYS B C   1 
ATOM   1719 O  O   . LYS B 2 221 ? 73.916  34.474  74.762 1.00 364.13 ? 221 LYS B O   1 
ATOM   1720 C  CB  . LYS B 2 221 ? 75.832  36.107  72.817 1.00 341.63 ? 221 LYS B CB  1 
ATOM   1721 C  CG  . LYS B 2 221 ? 77.038  35.890  71.918 1.00 409.47 ? 221 LYS B CG  1 
ATOM   1722 C  CD  . LYS B 2 221 ? 78.168  36.881  72.146 1.00 457.11 ? 221 LYS B CD  1 
ATOM   1723 C  CE  . LYS B 2 221 ? 78.849  36.753  73.492 1.00 497.04 ? 221 LYS B CE  1 
ATOM   1724 N  NZ  . LYS B 2 221 ? 80.004  37.675  73.607 1.00 503.97 ? 221 LYS B NZ  1 
ATOM   1725 N  N   . GLY B 2 222 ? 72.651  35.992  73.656 1.00 334.13 ? 222 GLY B N   1 
ATOM   1726 C  CA  . GLY B 2 222 ? 71.686  36.191  74.734 1.00 284.93 ? 222 GLY B CA  1 
ATOM   1727 C  C   . GLY B 2 222 ? 72.242  36.962  75.925 1.00 286.50 ? 222 GLY B C   1 
ATOM   1728 O  O   . GLY B 2 222 ? 73.302  37.633  75.792 1.00 307.61 ? 222 GLY B O   1 
ATOM   1729 N  N   . PHE B 2 233 ? 57.143  47.644  74.566 1.00 238.37 ? 233 PHE B N   1 
ATOM   1730 C  CA  . PHE B 2 233 ? 55.807  48.316  74.603 1.00 328.62 ? 233 PHE B CA  1 
ATOM   1731 C  C   . PHE B 2 233 ? 55.434  48.864  75.991 1.00 316.69 ? 233 PHE B C   1 
ATOM   1732 O  O   . PHE B 2 233 ? 54.524  49.694  76.102 1.00 168.80 ? 233 PHE B O   1 
ATOM   1733 C  CB  . PHE B 2 233 ? 54.743  47.346  74.083 1.00 370.21 ? 233 PHE B CB  1 
ATOM   1734 C  CG  . PHE B 2 233 ? 54.932  46.930  72.642 1.00 388.69 ? 233 PHE B CG  1 
ATOM   1735 C  CD1 . PHE B 2 233 ? 55.774  45.872  72.303 1.00 396.96 ? 233 PHE B CD1 1 
ATOM   1736 C  CD2 . PHE B 2 233 ? 54.266  47.602  71.623 1.00 331.16 ? 233 PHE B CD2 1 
ATOM   1737 C  CE1 . PHE B 2 233 ? 55.941  45.492  70.976 1.00 403.62 ? 233 PHE B CE1 1 
ATOM   1738 C  CE2 . PHE B 2 233 ? 54.433  47.221  70.295 1.00 368.39 ? 233 PHE B CE2 1 
ATOM   1739 C  CZ  . PHE B 2 233 ? 55.272  46.168  69.974 1.00 400.55 ? 233 PHE B CZ  1 
ATOM   1740 N  N   . GLU B 2 234 ? 56.131  48.407  77.042 1.00 364.09 ? 234 GLU B N   1 
ATOM   1741 C  CA  . GLU B 2 234 ? 55.992  48.898  78.411 1.00 374.77 ? 234 GLU B CA  1 
ATOM   1742 C  C   . GLU B 2 234 ? 56.253  50.411  78.532 1.00 313.30 ? 234 GLU B C   1 
ATOM   1743 O  O   . GLU B 2 234 ? 57.028  50.995  77.781 1.00 282.84 ? 234 GLU B O   1 
ATOM   1744 C  CB  . GLU B 2 234 ? 56.916  48.103  79.348 1.00 413.19 ? 234 GLU B CB  1 
ATOM   1745 C  CG  . GLU B 2 234 ? 58.378  48.022  78.911 1.00 412.52 ? 234 GLU B CG  1 
ATOM   1746 C  CD  . GLU B 2 234 ? 58.774  46.767  78.138 1.00 374.37 ? 234 GLU B CD  1 
ATOM   1747 O  OE1 . GLU B 2 234 ? 58.112  46.465  77.107 1.00 272.48 ? 234 GLU B OE1 1 
ATOM   1748 O  OE2 . GLU B 2 234 ? 59.733  46.096  78.552 1.00 364.35 ? 234 GLU B OE2 1 
ATOM   1749 N  N   . GLY B 2 235 ? 55.582  51.056  79.496 1.00 355.59 ? 235 GLY B N   1 
ATOM   1750 C  CA  . GLY B 2 235 ? 55.826  52.454  79.843 1.00 370.24 ? 235 GLY B CA  1 
ATOM   1751 C  C   . GLY B 2 235 ? 55.336  53.499  78.829 1.00 341.59 ? 235 GLY B C   1 
ATOM   1752 O  O   . GLY B 2 235 ? 55.579  54.691  79.041 1.00 279.74 ? 235 GLY B O   1 
ATOM   1753 N  N   . THR B 2 236 ? 54.644  53.084  77.746 1.00 315.05 ? 236 THR B N   1 
ATOM   1754 C  CA  . THR B 2 236 ? 54.433  53.952  76.585 1.00 293.95 ? 236 THR B CA  1 
ATOM   1755 C  C   . THR B 2 236 ? 53.531  55.160  76.899 1.00 307.08 ? 236 THR B C   1 
ATOM   1756 O  O   . THR B 2 236 ? 52.449  55.016  77.463 1.00 361.12 ? 236 THR B O   1 
ATOM   1757 C  CB  . THR B 2 236 ? 53.844  53.203  75.382 1.00 275.55 ? 236 THR B CB  1 
ATOM   1758 O  OG1 . THR B 2 236 ? 54.670  52.100  75.031 1.00 218.63 ? 236 THR B OG1 1 
ATOM   1759 C  CG2 . THR B 2 236 ? 53.738  54.062  74.140 1.00 341.29 ? 236 THR B CG2 1 
ATOM   1760 N  N   . LYS B 2 237 ? 53.995  56.358  76.502 1.00 288.83 ? 237 LYS B N   1 
ATOM   1761 C  CA  . LYS B 2 237 ? 53.286  57.629  76.659 1.00 316.17 ? 237 LYS B CA  1 
ATOM   1762 C  C   . LYS B 2 237 ? 52.380  57.866  75.437 1.00 292.66 ? 237 LYS B C   1 
ATOM   1763 O  O   . LYS B 2 237 ? 52.629  58.771  74.625 1.00 257.30 ? 237 LYS B O   1 
ATOM   1764 C  CB  . LYS B 2 237 ? 54.288  58.766  76.939 1.00 336.38 ? 237 LYS B CB  1 
ATOM   1765 C  CG  . LYS B 2 237 ? 55.530  58.834  76.052 1.00 351.40 ? 237 LYS B CG  1 
ATOM   1766 C  CD  . LYS B 2 237 ? 56.427  60.032  76.295 1.00 350.13 ? 237 LYS B CD  1 
ATOM   1767 C  CE  . LYS B 2 237 ? 57.077  60.052  77.663 1.00 360.05 ? 237 LYS B CE  1 
ATOM   1768 N  NZ  . LYS B 2 237 ? 58.065  61.154  77.782 1.00 376.08 ? 237 LYS B NZ  1 
ATOM   1769 N  N   . LEU B 2 238 ? 51.297  57.054  75.355 1.00 317.40 ? 238 LEU B N   1 
ATOM   1770 C  CA  . LEU B 2 238 ? 50.409  56.867  74.198 1.00 322.96 ? 238 LEU B CA  1 
ATOM   1771 C  C   . LEU B 2 238 ? 49.587  58.103  73.772 1.00 262.26 ? 238 LEU B C   1 
ATOM   1772 O  O   . LEU B 2 238 ? 48.721  57.972  72.892 1.00 201.18 ? 238 LEU B O   1 
ATOM   1773 C  CB  . LEU B 2 238 ? 49.442  55.716  74.544 1.00 366.63 ? 238 LEU B CB  1 
ATOM   1774 C  CG  . LEU B 2 238 ? 50.048  54.313  74.633 1.00 349.83 ? 238 LEU B CG  1 
ATOM   1775 C  CD1 . LEU B 2 238 ? 49.166  53.353  75.427 1.00 321.26 ? 238 LEU B CD1 1 
ATOM   1776 C  CD2 . LEU B 2 238 ? 50.301  53.761  73.237 1.00 359.39 ? 238 LEU B CD2 1 
ATOM   1777 N  N   . ASP B 2 239 ? 49.840  59.288  74.357 1.00 207.84 ? 239 ASP B N   1 
ATOM   1778 C  CA  . ASP B 2 239 ? 48.965  60.448  74.221 1.00 306.95 ? 239 ASP B CA  1 
ATOM   1779 C  C   . ASP B 2 239 ? 48.909  60.929  72.763 1.00 345.39 ? 239 ASP B C   1 
ATOM   1780 O  O   . ASP B 2 239 ? 49.951  61.172  72.140 1.00 384.19 ? 239 ASP B O   1 
ATOM   1781 C  CB  . ASP B 2 239 ? 49.415  61.610  75.119 1.00 338.58 ? 239 ASP B CB  1 
ATOM   1782 C  CG  . ASP B 2 239 ? 49.625  61.329  76.600 1.00 373.79 ? 239 ASP B CG  1 
ATOM   1783 O  OD1 . ASP B 2 239 ? 49.143  60.286  77.091 1.00 435.11 ? 239 ASP B OD1 1 
ATOM   1784 O  OD2 . ASP B 2 239 ? 50.280  62.171  77.258 1.00 371.83 ? 239 ASP B OD2 1 
ATOM   1785 N  N   . VAL B 2 240 ? 47.690  61.102  72.217 1.00 372.74 ? 240 VAL B N   1 
ATOM   1786 C  CA  . VAL B 2 240 ? 47.482  61.473  70.814 1.00 374.99 ? 240 VAL B CA  1 
ATOM   1787 C  C   . VAL B 2 240 ? 48.145  62.817  70.452 1.00 363.08 ? 240 VAL B C   1 
ATOM   1788 O  O   . VAL B 2 240 ? 48.542  63.012  69.298 1.00 241.98 ? 240 VAL B O   1 
ATOM   1789 C  CB  . VAL B 2 240 ? 45.978  61.465  70.450 1.00 362.81 ? 240 VAL B CB  1 
ATOM   1790 C  CG1 . VAL B 2 240 ? 45.396  60.064  70.575 1.00 330.46 ? 240 VAL B CG1 1 
ATOM   1791 C  CG2 . VAL B 2 240 ? 45.123  62.454  71.245 1.00 318.58 ? 240 VAL B CG2 1 
ATOM   1792 N  N   . GLY B 2 241 ? 48.267  63.740  71.428 1.00 354.76 ? 241 GLY B N   1 
ATOM   1793 C  CA  . GLY B 2 241 ? 48.977  65.007  71.268 1.00 276.50 ? 241 GLY B CA  1 
ATOM   1794 C  C   . GLY B 2 241 ? 50.495  64.923  71.470 1.00 229.32 ? 241 GLY B C   1 
ATOM   1795 O  O   . GLY B 2 241 ? 51.165  65.926  71.283 1.00 305.00 ? 241 GLY B O   1 
ATOM   1796 N  N   . ASN B 2 242 ? 51.040  63.759  71.854 1.00 231.22 ? 242 ASN B N   1 
ATOM   1797 C  CA  . ASN B 2 242 ? 52.465  63.522  72.054 1.00 289.16 ? 242 ASN B CA  1 
ATOM   1798 C  C   . ASN B 2 242 ? 53.061  62.718  70.894 1.00 273.49 ? 242 ASN B C   1 
ATOM   1799 O  O   . ASN B 2 242 ? 54.126  63.062  70.380 1.00 243.96 ? 242 ASN B O   1 
ATOM   1800 C  CB  . ASN B 2 242 ? 52.710  62.785  73.375 1.00 334.96 ? 242 ASN B CB  1 
ATOM   1801 C  CG  . ASN B 2 242 ? 54.146  62.345  73.541 1.00 303.59 ? 242 ASN B CG  1 
ATOM   1802 O  OD1 . ASN B 2 242 ? 55.057  63.167  73.492 1.00 280.67 ? 242 ASN B OD1 1 
ATOM   1803 N  ND2 . ASN B 2 242 ? 54.370  61.057  73.720 1.00 247.34 ? 242 ASN B ND2 1 
ATOM   1804 N  N   . ILE B 2 243 ? 52.385  61.642  70.456 1.00 260.08 ? 243 ILE B N   1 
ATOM   1805 C  CA  . ILE B 2 243 ? 52.963  60.700  69.497 1.00 203.62 ? 243 ILE B CA  1 
ATOM   1806 C  C   . ILE B 2 243 ? 53.224  61.405  68.164 1.00 215.87 ? 243 ILE B C   1 
ATOM   1807 O  O   . ILE B 2 243 ? 54.169  61.027  67.481 1.00 238.77 ? 243 ILE B O   1 
ATOM   1808 C  CB  . ILE B 2 243 ? 52.078  59.439  69.354 1.00 264.65 ? 243 ILE B CB  1 
ATOM   1809 C  CG1 . ILE B 2 243 ? 51.979  58.671  70.676 1.00 354.40 ? 243 ILE B CG1 1 
ATOM   1810 C  CG2 . ILE B 2 243 ? 52.537  58.518  68.231 1.00 267.77 ? 243 ILE B CG2 1 
ATOM   1811 C  CD1 . ILE B 2 243 ? 53.306  58.245  71.277 1.00 307.86 ? 243 ILE B CD1 1 
ATOM   1812 N  N   . VAL B 2 244 ? 52.454  62.436  67.774 1.00 241.89 ? 244 VAL B N   1 
ATOM   1813 C  CA  . VAL B 2 244 ? 52.778  63.197  66.564 1.00 219.42 ? 244 VAL B CA  1 
ATOM   1814 C  C   . VAL B 2 244 ? 54.162  63.860  66.664 1.00 205.73 ? 244 VAL B C   1 
ATOM   1815 O  O   . VAL B 2 244 ? 54.892  63.899  65.664 1.00 265.83 ? 244 VAL B O   1 
ATOM   1816 C  CB  . VAL B 2 244 ? 51.666  64.204  66.194 1.00 268.57 ? 244 VAL B CB  1 
ATOM   1817 C  CG1 . VAL B 2 244 ? 51.567  65.387  67.150 1.00 312.61 ? 244 VAL B CG1 1 
ATOM   1818 C  CG2 . VAL B 2 244 ? 51.849  64.672  64.764 1.00 256.29 ? 244 VAL B CG2 1 
ATOM   1819 N  N   . LEU B 2 245 ? 54.547  64.364  67.851 1.00 203.51 ? 245 LEU B N   1 
ATOM   1820 C  CA  . LEU B 2 245 ? 55.899  64.889  68.071 1.00 229.07 ? 245 LEU B CA  1 
ATOM   1821 C  C   . LEU B 2 245 ? 56.974  63.784  68.008 1.00 226.27 ? 245 LEU B C   1 
ATOM   1822 O  O   . LEU B 2 245 ? 58.093  64.036  67.549 1.00 149.19 ? 245 LEU B O   1 
ATOM   1823 C  CB  . LEU B 2 245 ? 55.930  65.651  69.400 1.00 199.28 ? 245 LEU B CB  1 
ATOM   1824 C  CG  . LEU B 2 245 ? 57.272  66.286  69.778 1.00 295.63 ? 245 LEU B CG  1 
ATOM   1825 C  CD1 . LEU B 2 245 ? 57.807  67.285  68.743 1.00 287.33 ? 245 LEU B CD1 1 
ATOM   1826 C  CD2 . LEU B 2 245 ? 57.123  66.976  71.120 1.00 385.45 ? 245 LEU B CD2 1 
ATOM   1827 N  N   . ALA B 2 246 ? 56.654  62.557  68.442 1.00 233.28 ? 246 ALA B N   1 
ATOM   1828 C  CA  . ALA B 2 246 ? 57.542  61.414  68.243 1.00 207.40 ? 246 ALA B CA  1 
ATOM   1829 C  C   . ALA B 2 246 ? 57.760  61.142  66.746 1.00 206.22 ? 246 ALA B C   1 
ATOM   1830 O  O   . ALA B 2 246 ? 58.910  60.961  66.344 1.00 158.29 ? 246 ALA B O   1 
ATOM   1831 C  CB  . ALA B 2 246 ? 57.014  60.195  68.986 1.00 270.73 ? 246 ALA B CB  1 
ATOM   1832 N  N   . LEU B 2 247 ? 56.700  61.139  65.910 1.00 224.18 ? 247 LEU B N   1 
ATOM   1833 C  CA  . LEU B 2 247 ? 56.867  60.973  64.467 1.00 217.06 ? 247 LEU B CA  1 
ATOM   1834 C  C   . LEU B 2 247 ? 57.720  62.091  63.846 1.00 154.35 ? 247 LEU B C   1 
ATOM   1835 O  O   . LEU B 2 247 ? 58.488  61.801  62.933 1.00 134.94 ? 247 LEU B O   1 
ATOM   1836 C  CB  . LEU B 2 247 ? 55.507  60.864  63.758 1.00 235.21 ? 247 LEU B CB  1 
ATOM   1837 C  CG  . LEU B 2 247 ? 54.951  59.441  63.634 1.00 286.35 ? 247 LEU B CG  1 
ATOM   1838 C  CD1 . LEU B 2 247 ? 54.050  59.106  64.812 1.00 339.87 ? 247 LEU B CD1 1 
ATOM   1839 C  CD2 . LEU B 2 247 ? 54.204  59.236  62.320 1.00 348.29 ? 247 LEU B CD2 1 
ATOM   1840 N  N   . TYR B 2 248 ? 57.629  63.339  64.321 1.00 175.22 ? 248 TYR B N   1 
ATOM   1841 C  CA  . TYR B 2 248 ? 58.433  64.448  63.794 1.00 243.36 ? 248 TYR B CA  1 
ATOM   1842 C  C   . TYR B 2 248 ? 59.951  64.181  63.948 1.00 231.65 ? 248 TYR B C   1 
ATOM   1843 O  O   . TYR B 2 248 ? 60.756  64.625  63.107 1.00 268.58 ? 248 TYR B O   1 
ATOM   1844 C  CB  . TYR B 2 248 ? 58.065  65.852  64.349 1.00 178.32 ? 248 TYR B CB  1 
ATOM   1845 C  CG  . TYR B 2 248 ? 58.777  66.884  63.466 1.00 185.06 ? 248 TYR B CG  1 
ATOM   1846 C  CD1 . TYR B 2 248 ? 58.334  67.148  62.164 1.00 237.17 ? 248 TYR B CD1 1 
ATOM   1847 C  CD2 . TYR B 2 248 ? 59.934  67.555  63.889 1.00 224.43 ? 248 TYR B CD2 1 
ATOM   1848 C  CE1 . TYR B 2 248 ? 58.992  68.039  61.329 1.00 251.18 ? 248 TYR B CE1 1 
ATOM   1849 C  CE2 . TYR B 2 248 ? 60.599  68.463  63.073 1.00 171.33 ? 248 TYR B CE2 1 
ATOM   1850 C  CZ  . TYR B 2 248 ? 60.121  68.709  61.795 1.00 259.35 ? 248 TYR B CZ  1 
ATOM   1851 O  OH  . TYR B 2 248 ? 60.763  69.610  60.991 1.00 370.85 ? 248 TYR B OH  1 
ATOM   1852 N  N   . SER B 2 249 ? 60.369  63.460  64.994 1.00 143.01 ? 249 SER B N   1 
ATOM   1853 C  CA  . SER B 2 249 ? 61.788  63.259  65.251 1.00 183.01 ? 249 SER B CA  1 
ATOM   1854 C  C   . SER B 2 249 ? 62.509  62.515  64.111 1.00 260.70 ? 249 SER B C   1 
ATOM   1855 O  O   . SER B 2 249 ? 63.709  62.705  63.930 1.00 283.83 ? 249 SER B O   1 
ATOM   1856 C  CB  . SER B 2 249 ? 61.947  62.506  66.552 1.00 286.73 ? 249 SER B CB  1 
ATOM   1857 O  OG  . SER B 2 249 ? 61.461  61.174  66.417 1.00 354.82 ? 249 SER B OG  1 
ATOM   1858 N  N   . GLY B 2 250 ? 61.805  61.652  63.349 1.00 247.20 ? 250 GLY B N   1 
ATOM   1859 C  CA  . GLY B 2 250 ? 62.374  60.953  62.205 1.00 252.21 ? 250 GLY B CA  1 
ATOM   1860 C  C   . GLY B 2 250 ? 62.589  61.840  60.975 1.00 245.65 ? 250 GLY B C   1 
ATOM   1861 O  O   . GLY B 2 250 ? 63.295  61.442  60.047 1.00 215.03 ? 250 GLY B O   1 
ATOM   1862 N  N   . LEU B 2 251 ? 62.013  63.054  60.939 1.00 255.83 ? 251 LEU B N   1 
ATOM   1863 C  CA  . LEU B 2 251 ? 62.157  63.944  59.782 1.00 234.53 ? 251 LEU B CA  1 
ATOM   1864 C  C   . LEU B 2 251 ? 63.393  64.856  59.876 1.00 235.00 ? 251 LEU B C   1 
ATOM   1865 O  O   . LEU B 2 251 ? 63.480  65.898  59.227 1.00 272.58 ? 251 LEU B O   1 
ATOM   1866 C  CB  . LEU B 2 251 ? 60.837  64.721  59.619 1.00 246.56 ? 251 LEU B CB  1 
ATOM   1867 C  CG  . LEU B 2 251 ? 59.656  63.796  59.314 1.00 238.74 ? 251 LEU B CG  1 
ATOM   1868 C  CD1 . LEU B 2 251 ? 58.364  64.579  59.159 1.00 366.14 ? 251 LEU B CD1 1 
ATOM   1869 C  CD2 . LEU B 2 251 ? 59.928  62.991  58.054 1.00 259.05 ? 251 LEU B CD2 1 
ATOM   1870 N  N   . PHE B 2 252 ? 64.371  64.463  60.692 1.00 165.54 ? 252 PHE B N   1 
ATOM   1871 C  CA  . PHE B 2 252 ? 65.767  64.769  60.480 1.00 152.31 ? 252 PHE B CA  1 
ATOM   1872 C  C   . PHE B 2 252 ? 66.458  63.544  59.890 1.00 169.18 ? 252 PHE B C   1 
ATOM   1873 O  O   . PHE B 2 252 ? 67.278  63.672  58.960 1.00 263.32 ? 252 PHE B O   1 
ATOM   1874 C  CB  . PHE B 2 252 ? 66.421  65.201  61.804 1.00 237.05 ? 252 PHE B CB  1 
ATOM   1875 C  CG  . PHE B 2 252 ? 67.849  65.653  61.618 1.00 254.35 ? 252 PHE B CG  1 
ATOM   1876 C  CD1 . PHE B 2 252 ? 68.125  66.974  61.265 1.00 324.84 ? 252 PHE B CD1 1 
ATOM   1877 C  CD2 . PHE B 2 252 ? 68.909  64.753  61.749 1.00 177.12 ? 252 PHE B CD2 1 
ATOM   1878 C  CE1 . PHE B 2 252 ? 69.436  67.394  61.060 1.00 375.61 ? 252 PHE B CE1 1 
ATOM   1879 C  CE2 . PHE B 2 252 ? 70.210  65.181  61.553 1.00 326.38 ? 252 PHE B CE2 1 
ATOM   1880 C  CZ  . PHE B 2 252 ? 70.475  66.496  61.207 1.00 403.70 ? 252 PHE B CZ  1 
ATOM   1881 N  N   . ALA B 2 253 ? 66.138  62.352  60.430 1.00 158.63 ? 253 ALA B N   1 
ATOM   1882 C  CA  . ALA B 2 253 ? 66.844  61.116  60.112 1.00 206.04 ? 253 ALA B CA  1 
ATOM   1883 C  C   . ALA B 2 253 ? 66.613  60.651  58.668 1.00 141.84 ? 253 ALA B C   1 
ATOM   1884 O  O   . ALA B 2 253 ? 67.564  60.203  58.013 1.00 116.83 ? 253 ALA B O   1 
ATOM   1885 C  CB  . ALA B 2 253 ? 66.448  60.065  61.109 1.00 207.38 ? 253 ALA B CB  1 
ATOM   1886 N  N   . TYR B 2 254 ? 65.373  60.756  58.161 1.00 151.41 ? 254 TYR B N   1 
ATOM   1887 C  CA  . TYR B 2 254 ? 65.066  60.410  56.777 1.00 179.32 ? 254 TYR B CA  1 
ATOM   1888 C  C   . TYR B 2 254 ? 65.248  61.551  55.778 1.00 136.93 ? 254 TYR B C   1 
ATOM   1889 O  O   . TYR B 2 254 ? 65.294  61.280  54.566 1.00 97.73  ? 254 TYR B O   1 
ATOM   1890 C  CB  . TYR B 2 254 ? 63.610  59.956  56.730 1.00 210.27 ? 254 TYR B CB  1 
ATOM   1891 C  CG  . TYR B 2 254 ? 63.394  58.527  57.196 1.00 179.83 ? 254 TYR B CG  1 
ATOM   1892 C  CD1 . TYR B 2 254 ? 63.757  57.462  56.384 1.00 169.24 ? 254 TYR B CD1 1 
ATOM   1893 C  CD2 . TYR B 2 254 ? 62.831  58.259  58.429 1.00 158.86 ? 254 TYR B CD2 1 
ATOM   1894 C  CE1 . TYR B 2 254 ? 63.560  56.158  56.794 1.00 182.06 ? 254 TYR B CE1 1 
ATOM   1895 C  CE2 . TYR B 2 254 ? 62.623  56.954  58.843 1.00 173.29 ? 254 TYR B CE2 1 
ATOM   1896 C  CZ  . TYR B 2 254 ? 62.983  55.900  58.023 1.00 200.97 ? 254 TYR B CZ  1 
ATOM   1897 O  OH  . TYR B 2 254 ? 62.768  54.614  58.425 1.00 284.23 ? 254 TYR B OH  1 
ATOM   1898 N  N   . GLY B 2 255 ? 65.322  62.796  56.282 1.00 157.08 ? 255 GLY B N   1 
ATOM   1899 C  CA  . GLY B 2 255 ? 65.360  63.990  55.447 1.00 231.96 ? 255 GLY B CA  1 
ATOM   1900 C  C   . GLY B 2 255 ? 66.556  64.008  54.498 1.00 208.61 ? 255 GLY B C   1 
ATOM   1901 O  O   . GLY B 2 255 ? 67.670  63.684  54.889 1.00 161.02 ? 255 GLY B O   1 
ATOM   1902 N  N   . GLY B 2 256 ? 66.292  64.385  53.240 1.00 190.78 ? 256 GLY B N   1 
ATOM   1903 C  CA  . GLY B 2 256 ? 67.308  64.387  52.189 1.00 218.61 ? 256 GLY B CA  1 
ATOM   1904 C  C   . GLY B 2 256 ? 66.914  63.556  50.966 1.00 190.60 ? 256 GLY B C   1 
ATOM   1905 O  O   . GLY B 2 256 ? 67.603  63.611  49.950 1.00 300.20 ? 256 GLY B O   1 
ATOM   1906 N  N   . TRP B 2 257 ? 65.802  62.811  51.028 1.00 133.36 ? 257 TRP B N   1 
ATOM   1907 C  CA  . TRP B 2 257 ? 65.350  62.041  49.872 1.00 158.26 ? 257 TRP B CA  1 
ATOM   1908 C  C   . TRP B 2 257 ? 65.020  62.901  48.632 1.00 123.01 ? 257 TRP B C   1 
ATOM   1909 O  O   . TRP B 2 257 ? 64.993  62.387  47.512 1.00 119.94 ? 257 TRP B O   1 
ATOM   1910 C  CB  . TRP B 2 257 ? 64.187  61.103  50.252 1.00 122.84 ? 257 TRP B CB  1 
ATOM   1911 C  CG  . TRP B 2 257 ? 63.017  61.738  50.949 1.00 143.73 ? 257 TRP B CG  1 
ATOM   1912 C  CD1 . TRP B 2 257 ? 62.711  61.574  52.274 1.00 269.21 ? 257 TRP B CD1 1 
ATOM   1913 C  CD2 . TRP B 2 257 ? 61.995  62.611  50.412 1.00 149.93 ? 257 TRP B CD2 1 
ATOM   1914 N  NE1 . TRP B 2 257 ? 61.570  62.272  52.596 1.00 237.42 ? 257 TRP B NE1 1 
ATOM   1915 C  CE2 . TRP B 2 257 ? 61.109  62.921  51.469 1.00 197.45 ? 257 TRP B CE2 1 
ATOM   1916 C  CE3 . TRP B 2 257 ? 61.718  63.149  49.150 1.00 167.65 ? 257 TRP B CE3 1 
ATOM   1917 C  CZ2 . TRP B 2 257 ? 59.998  63.750  51.266 1.00 204.59 ? 257 TRP B CZ2 1 
ATOM   1918 C  CZ3 . TRP B 2 257 ? 60.623  63.962  48.945 1.00 171.84 ? 257 TRP B CZ3 1 
ATOM   1919 C  CH2 . TRP B 2 257 ? 59.782  64.253  50.000 1.00 170.06 ? 257 TRP B CH2 1 
ATOM   1920 N  N   . ASN B 2 258 ? 64.780  64.193  48.806 1.00 111.32 ? 258 ASN B N   1 
ATOM   1921 C  CA  . ASN B 2 258 ? 64.587  65.078  47.673 1.00 134.43 ? 258 ASN B CA  1 
ATOM   1922 C  C   . ASN B 2 258 ? 65.881  65.479  46.970 1.00 151.06 ? 258 ASN B C   1 
ATOM   1923 O  O   . ASN B 2 258 ? 65.776  66.070  45.895 1.00 253.76 ? 258 ASN B O   1 
ATOM   1924 C  CB  . ASN B 2 258 ? 63.831  66.344  48.096 1.00 193.28 ? 258 ASN B CB  1 
ATOM   1925 C  CG  . ASN B 2 258 ? 64.553  67.161  49.168 1.00 230.00 ? 258 ASN B CG  1 
ATOM   1926 O  OD1 . ASN B 2 258 ? 65.446  66.704  49.894 1.00 202.98 ? 258 ASN B OD1 1 
ATOM   1927 N  ND2 . ASN B 2 258 ? 64.152  68.413  49.291 1.00 302.30 ? 258 ASN B ND2 1 
ATOM   1928 N  N   . TYR B 2 259 ? 67.074  65.179  47.506 1.00 168.66 ? 259 TYR B N   1 
ATOM   1929 C  CA  . TYR B 2 259 ? 68.315  65.718  46.968 1.00 206.61 ? 259 TYR B CA  1 
ATOM   1930 C  C   . TYR B 2 259 ? 68.564  65.300  45.521 1.00 154.31 ? 259 TYR B C   1 
ATOM   1931 O  O   . TYR B 2 259 ? 69.075  66.139  44.762 1.00 100.30 ? 259 TYR B O   1 
ATOM   1932 C  CB  . TYR B 2 259 ? 69.542  65.319  47.794 1.00 235.84 ? 259 TYR B CB  1 
ATOM   1933 C  CG  . TYR B 2 259 ? 69.765  66.091  49.095 1.00 196.67 ? 259 TYR B CG  1 
ATOM   1934 C  CD1 . TYR B 2 259 ? 69.627  67.480  49.196 1.00 138.51 ? 259 TYR B CD1 1 
ATOM   1935 C  CD2 . TYR B 2 259 ? 70.104  65.402  50.241 1.00 175.49 ? 259 TYR B CD2 1 
ATOM   1936 C  CE1 . TYR B 2 259 ? 69.830  68.146  50.372 1.00 137.01 ? 259 TYR B CE1 1 
ATOM   1937 C  CE2 . TYR B 2 259 ? 70.316  66.060  51.441 1.00 297.45 ? 259 TYR B CE2 1 
ATOM   1938 C  CZ  . TYR B 2 259 ? 70.187  67.438  51.512 1.00 321.32 ? 259 TYR B CZ  1 
ATOM   1939 O  OH  . TYR B 2 259 ? 70.423  68.016  52.735 1.00 417.41 ? 259 TYR B OH  1 
ATOM   1940 N  N   . LEU B 2 260 ? 68.170  64.069  45.143 1.00 148.97 ? 260 LEU B N   1 
ATOM   1941 C  CA  . LEU B 2 260 ? 68.402  63.583  43.776 1.00 157.50 ? 260 LEU B CA  1 
ATOM   1942 C  C   . LEU B 2 260 ? 67.678  64.390  42.681 1.00 118.28 ? 260 LEU B C   1 
ATOM   1943 O  O   . LEU B 2 260 ? 68.101  64.434  41.552 1.00 73.17  ? 260 LEU B O   1 
ATOM   1944 C  CB  . LEU B 2 260 ? 68.019  62.107  43.717 1.00 188.51 ? 260 LEU B CB  1 
ATOM   1945 C  CG  . LEU B 2 260 ? 68.531  61.345  42.494 1.00 175.02 ? 260 LEU B CG  1 
ATOM   1946 C  CD1 . LEU B 2 260 ? 70.057  61.535  42.211 1.00 110.56 ? 260 LEU B CD1 1 
ATOM   1947 C  CD2 . LEU B 2 260 ? 68.157  59.873  42.704 1.00 164.74 ? 260 LEU B CD2 1 
ATOM   1948 N  N   . ASN B 2 261 ? 66.607  65.105  43.016 1.00 187.81 ? 261 ASN B N   1 
ATOM   1949 C  CA  . ASN B 2 261 ? 65.915  66.006  42.087 1.00 148.30 ? 261 ASN B CA  1 
ATOM   1950 C  C   . ASN B 2 261 ? 66.707  67.273  41.740 1.00 115.44 ? 261 ASN B C   1 
ATOM   1951 O  O   . ASN B 2 261 ? 66.669  67.692  40.603 1.00 172.37 ? 261 ASN B O   1 
ATOM   1952 C  CB  . ASN B 2 261 ? 64.552  66.369  42.638 1.00 151.45 ? 261 ASN B CB  1 
ATOM   1953 C  CG  . ASN B 2 261 ? 63.635  65.171  42.571 1.00 197.21 ? 261 ASN B CG  1 
ATOM   1954 O  OD1 . ASN B 2 261 ? 63.718  64.243  43.380 1.00 181.99 ? 261 ASN B OD1 1 
ATOM   1955 N  ND2 . ASN B 2 261 ? 62.738  65.185  41.600 1.00 258.44 ? 261 ASN B ND2 1 
ATOM   1956 N  N   . PHE B 2 262 ? 67.484  67.831  42.656 1.00 104.01 ? 262 PHE B N   1 
ATOM   1957 C  CA  . PHE B 2 262 ? 68.371  68.939  42.366 1.00 134.98 ? 262 PHE B CA  1 
ATOM   1958 C  C   . PHE B 2 262 ? 69.522  68.628  41.389 1.00 116.67 ? 262 PHE B C   1 
ATOM   1959 O  O   . PHE B 2 262 ? 70.276  69.554  41.037 1.00 132.31 ? 262 PHE B O   1 
ATOM   1960 C  CB  . PHE B 2 262 ? 69.000  69.438  43.665 1.00 198.44 ? 262 PHE B CB  1 
ATOM   1961 C  CG  . PHE B 2 262 ? 68.155  70.210  44.647 1.00 239.14 ? 262 PHE B CG  1 
ATOM   1962 C  CD1 . PHE B 2 262 ? 67.606  71.450  44.321 1.00 258.77 ? 262 PHE B CD1 1 
ATOM   1963 C  CD2 . PHE B 2 262 ? 67.958  69.699  45.923 1.00 194.47 ? 262 PHE B CD2 1 
ATOM   1964 C  CE1 . PHE B 2 262 ? 66.843  72.157  45.241 1.00 181.23 ? 262 PHE B CE1 1 
ATOM   1965 C  CE2 . PHE B 2 262 ? 67.202  70.405  46.844 1.00 268.53 ? 262 PHE B CE2 1 
ATOM   1966 C  CZ  . PHE B 2 262 ? 66.637  71.625  46.498 1.00 290.11 ? 262 PHE B CZ  1 
ATOM   1967 N  N   . VAL B 2 263 ? 69.692  67.370  40.931 1.00 79.13  ? 263 VAL B N   1 
ATOM   1968 C  CA  . VAL B 2 263 ? 70.702  67.035  39.945 1.00 104.00 ? 263 VAL B CA  1 
ATOM   1969 C  C   . VAL B 2 263 ? 70.121  66.299  38.731 1.00 161.18 ? 263 VAL B C   1 
ATOM   1970 O  O   . VAL B 2 263 ? 70.856  65.664  37.980 1.00 225.54 ? 263 VAL B O   1 
ATOM   1971 C  CB  . VAL B 2 263 ? 71.864  66.243  40.589 1.00 138.42 ? 263 VAL B CB  1 
ATOM   1972 C  CG1 . VAL B 2 263 ? 72.484  67.060  41.719 1.00 171.53 ? 263 VAL B CG1 1 
ATOM   1973 C  CG2 . VAL B 2 263 ? 71.505  64.806  41.019 1.00 108.30 ? 263 VAL B CG2 1 
ATOM   1974 N  N   . THR B 2 264 ? 68.819  66.410  38.481 1.00 153.56 ? 264 THR B N   1 
ATOM   1975 C  CA  . THR B 2 264 ? 68.134  65.652  37.445 1.00 148.34 ? 264 THR B CA  1 
ATOM   1976 C  C   . THR B 2 264 ? 68.837  65.723  36.082 1.00 245.29 ? 264 THR B C   1 
ATOM   1977 O  O   . THR B 2 264 ? 69.036  64.668  35.473 1.00 216.23 ? 264 THR B O   1 
ATOM   1978 C  CB  . THR B 2 264 ? 66.683  66.142  37.300 1.00 159.74 ? 264 THR B CB  1 
ATOM   1979 O  OG1 . THR B 2 264 ? 66.044  65.931  38.557 1.00 210.57 ? 264 THR B OG1 1 
ATOM   1980 C  CG2 . THR B 2 264 ? 65.894  65.390  36.244 1.00 296.21 ? 264 THR B CG2 1 
ATOM   1981 N  N   . GLU B 2 265 ? 69.208  66.929  35.590 1.00 264.82 ? 265 GLU B N   1 
ATOM   1982 C  CA  . GLU B 2 265 ? 69.805  67.100  34.268 1.00 280.35 ? 265 GLU B CA  1 
ATOM   1983 C  C   . GLU B 2 265 ? 71.196  66.475  34.149 1.00 179.61 ? 265 GLU B C   1 
ATOM   1984 O  O   . GLU B 2 265 ? 71.737  66.487  33.043 1.00 166.85 ? 265 GLU B O   1 
ATOM   1985 C  CB  . GLU B 2 265 ? 69.917  68.560  33.828 1.00 293.13 ? 265 GLU B CB  1 
ATOM   1986 C  CG  . GLU B 2 265 ? 68.577  69.211  33.464 1.00 408.42 ? 265 GLU B CG  1 
ATOM   1987 C  CD  . GLU B 2 265 ? 68.705  70.331  32.437 1.00 441.07 ? 265 GLU B CD  1 
ATOM   1988 O  OE1 . GLU B 2 265 ? 68.866  70.018  31.250 1.00 510.27 ? 265 GLU B OE1 1 
ATOM   1989 O  OE2 . GLU B 2 265 ? 68.650  71.504  32.821 1.00 342.28 ? 265 GLU B OE2 1 
ATOM   1990 N  N   . GLU B 2 266 ? 71.758  65.918  35.235 1.00 142.38 ? 266 GLU B N   1 
ATOM   1991 C  CA  . GLU B 2 266 ? 73.077  65.301  35.181 1.00 200.31 ? 266 GLU B CA  1 
ATOM   1992 C  C   . GLU B 2 266 ? 73.013  63.774  35.205 1.00 165.29 ? 266 GLU B C   1 
ATOM   1993 O  O   . GLU B 2 266 ? 74.072  63.156  35.112 1.00 209.53 ? 266 GLU B O   1 
ATOM   1994 C  CB  . GLU B 2 266 ? 73.966  65.912  36.268 1.00 226.59 ? 266 GLU B CB  1 
ATOM   1995 C  CG  . GLU B 2 266 ? 74.388  67.315  35.866 1.00 279.21 ? 266 GLU B CG  1 
ATOM   1996 C  CD  . GLU B 2 266 ? 75.117  68.096  36.930 1.00 319.64 ? 266 GLU B CD  1 
ATOM   1997 O  OE1 . GLU B 2 266 ? 76.238  67.697  37.299 1.00 386.98 ? 266 GLU B OE1 1 
ATOM   1998 O  OE2 . GLU B 2 266 ? 74.558  69.107  37.398 1.00 374.00 ? 266 GLU B OE2 1 
ATOM   1999 N  N   . MET B 2 267 ? 71.815  63.171  35.289 1.00 131.67 ? 267 MET B N   1 
ATOM   2000 C  CA  . MET B 2 267 ? 71.705  61.727  35.124 1.00 228.38 ? 267 MET B CA  1 
ATOM   2001 C  C   . MET B 2 267 ? 71.655  61.296  33.644 1.00 239.95 ? 267 MET B C   1 
ATOM   2002 O  O   . MET B 2 267 ? 71.080  61.983  32.796 1.00 230.13 ? 267 MET B O   1 
ATOM   2003 C  CB  . MET B 2 267 ? 70.468  61.228  35.876 1.00 246.42 ? 267 MET B CB  1 
ATOM   2004 C  CG  . MET B 2 267 ? 70.785  61.039  37.354 1.00 242.46 ? 267 MET B CG  1 
ATOM   2005 S  SD  . MET B 2 267 ? 69.436  60.350  38.315 1.00 182.50 ? 267 MET B SD  1 
ATOM   2006 C  CE  . MET B 2 267 ? 68.454  61.852  38.409 1.00 172.34 ? 267 MET B CE  1 
ATOM   2007 N  N   . ILE B 2 268 ? 72.249  60.115  33.355 1.00 184.12 ? 268 ILE B N   1 
ATOM   2008 C  CA  . ILE B 2 268 ? 72.410  59.612  31.993 1.00 180.89 ? 268 ILE B CA  1 
ATOM   2009 C  C   . ILE B 2 268 ? 71.073  59.423  31.260 1.00 239.45 ? 268 ILE B C   1 
ATOM   2010 O  O   . ILE B 2 268 ? 70.997  59.695  30.057 1.00 298.18 ? 268 ILE B O   1 
ATOM   2011 C  CB  . ILE B 2 268 ? 73.230  58.300  31.960 1.00 250.80 ? 268 ILE B CB  1 
ATOM   2012 C  CG1 . ILE B 2 268 ? 72.622  57.135  32.774 1.00 288.97 ? 268 ILE B CG1 1 
ATOM   2013 C  CG2 . ILE B 2 268 ? 74.670  58.617  32.351 1.00 214.06 ? 268 ILE B CG2 1 
ATOM   2014 C  CD1 . ILE B 2 268 ? 73.183  55.747  32.457 1.00 290.62 ? 268 ILE B CD1 1 
ATOM   2015 N  N   . ASN B 2 269 ? 70.019  58.966  31.971 1.00 196.89 ? 269 ASN B N   1 
ATOM   2016 C  CA  . ASN B 2 269 ? 68.686  58.751  31.409 1.00 249.08 ? 269 ASN B CA  1 
ATOM   2017 C  C   . ASN B 2 269 ? 67.645  58.939  32.511 1.00 171.05 ? 269 ASN B C   1 
ATOM   2018 O  O   . ASN B 2 269 ? 67.141  57.956  33.060 1.00 175.99 ? 269 ASN B O   1 
ATOM   2019 C  CB  . ASN B 2 269 ? 68.543  57.392  30.717 1.00 297.73 ? 269 ASN B CB  1 
ATOM   2020 C  CG  . ASN B 2 269 ? 67.207  57.201  30.003 1.00 322.06 ? 269 ASN B CG  1 
ATOM   2021 O  OD1 . ASN B 2 269 ? 66.298  58.044  30.041 1.00 204.83 ? 269 ASN B OD1 1 
ATOM   2022 N  ND2 . ASN B 2 269 ? 67.067  56.071  29.327 1.00 367.29 ? 269 ASN B ND2 1 
ATOM   2023 N  N   . PRO B 2 270 ? 67.289  60.199  32.873 1.00 148.27 ? 270 PRO B N   1 
ATOM   2024 C  CA  . PRO B 2 270 ? 66.553  60.464  34.106 1.00 190.21 ? 270 PRO B CA  1 
ATOM   2025 C  C   . PRO B 2 270 ? 65.178  59.806  34.129 1.00 173.56 ? 270 PRO B C   1 
ATOM   2026 O  O   . PRO B 2 270 ? 64.739  59.408  35.200 1.00 190.79 ? 270 PRO B O   1 
ATOM   2027 C  CB  . PRO B 2 270 ? 66.439  61.996  34.167 1.00 252.26 ? 270 PRO B CB  1 
ATOM   2028 C  CG  . PRO B 2 270 ? 66.598  62.432  32.736 1.00 238.55 ? 270 PRO B CG  1 
ATOM   2029 C  CD  . PRO B 2 270 ? 67.567  61.439  32.140 1.00 166.99 ? 270 PRO B CD  1 
ATOM   2030 N  N   . TYR B 2 271 ? 64.515  59.666  32.977 1.00 163.15 ? 271 TYR B N   1 
ATOM   2031 C  CA  . TYR B 2 271 ? 63.170  59.119  32.933 1.00 188.83 ? 271 TYR B CA  1 
ATOM   2032 C  C   . TYR B 2 271 ? 63.114  57.696  33.492 1.00 165.25 ? 271 TYR B C   1 
ATOM   2033 O  O   . TYR B 2 271 ? 62.041  57.276  33.935 1.00 173.18 ? 271 TYR B O   1 
ATOM   2034 C  CB  . TYR B 2 271 ? 62.698  59.176  31.481 1.00 240.10 ? 271 TYR B CB  1 
ATOM   2035 C  CG  . TYR B 2 271 ? 62.739  60.583  30.919 1.00 219.79 ? 271 TYR B CG  1 
ATOM   2036 C  CD1 . TYR B 2 271 ? 61.768  61.506  31.275 1.00 243.42 ? 271 TYR B CD1 1 
ATOM   2037 C  CD2 . TYR B 2 271 ? 63.752  60.980  30.048 1.00 257.86 ? 271 TYR B CD2 1 
ATOM   2038 C  CE1 . TYR B 2 271 ? 61.786  62.794  30.765 1.00 306.19 ? 271 TYR B CE1 1 
ATOM   2039 C  CE2 . TYR B 2 271 ? 63.784  62.273  29.538 1.00 337.95 ? 271 TYR B CE2 1 
ATOM   2040 C  CZ  . TYR B 2 271 ? 62.796  63.183  29.899 1.00 395.21 ? 271 TYR B CZ  1 
ATOM   2041 O  OH  . TYR B 2 271 ? 62.785  64.472  29.425 1.00 487.78 ? 271 TYR B OH  1 
ATOM   2042 N  N   . ARG B 2 272 ? 64.236  56.951  33.431 1.00 155.85 ? 272 ARG B N   1 
ATOM   2043 C  CA  . ARG B 2 272 ? 64.394  55.711  34.173 1.00 223.34 ? 272 ARG B CA  1 
ATOM   2044 C  C   . ARG B 2 272 ? 65.093  55.997  35.506 1.00 194.01 ? 272 ARG B C   1 
ATOM   2045 O  O   . ARG B 2 272 ? 64.600  55.586  36.555 1.00 200.00 ? 272 ARG B O   1 
ATOM   2046 C  CB  . ARG B 2 272 ? 65.164  54.668  33.357 1.00 257.65 ? 272 ARG B CB  1 
ATOM   2047 C  CG  . ARG B 2 272 ? 65.151  53.293  34.011 1.00 238.93 ? 272 ARG B CG  1 
ATOM   2048 C  CD  . ARG B 2 272 ? 65.911  52.225  33.248 1.00 258.46 ? 272 ARG B CD  1 
ATOM   2049 N  NE  . ARG B 2 272 ? 65.779  50.917  33.901 1.00 306.27 ? 272 ARG B NE  1 
ATOM   2050 C  CZ  . ARG B 2 272 ? 66.700  49.942  33.923 1.00 319.67 ? 272 ARG B CZ  1 
ATOM   2051 N  NH1 . ARG B 2 272 ? 66.459  48.818  34.589 1.00 233.99 ? 272 ARG B NH1 1 
ATOM   2052 N  NH2 . ARG B 2 272 ? 67.857  50.082  33.291 1.00 329.02 ? 272 ARG B NH2 1 
ATOM   2053 N  N   . ASN B 2 273 ? 66.248  56.668  35.484 1.00 214.21 ? 273 ASN B N   1 
ATOM   2054 C  CA  . ASN B 2 273 ? 67.157  56.651  36.621 1.00 244.50 ? 273 ASN B CA  1 
ATOM   2055 C  C   . ASN B 2 273 ? 66.550  57.343  37.847 1.00 151.36 ? 273 ASN B C   1 
ATOM   2056 O  O   . ASN B 2 273 ? 66.732  56.865  38.957 1.00 182.04 ? 273 ASN B O   1 
ATOM   2057 C  CB  . ASN B 2 273 ? 68.530  57.265  36.294 1.00 330.54 ? 273 ASN B CB  1 
ATOM   2058 C  CG  . ASN B 2 273 ? 69.270  56.701  35.093 1.00 315.40 ? 273 ASN B CG  1 
ATOM   2059 O  OD1 . ASN B 2 273 ? 69.855  57.483  34.338 1.00 347.45 ? 273 ASN B OD1 1 
ATOM   2060 N  ND2 . ASN B 2 273 ? 69.268  55.388  34.910 1.00 238.27 ? 273 ASN B ND2 1 
ATOM   2061 N  N   . LEU B 2 274 ? 65.855  58.474  37.702 1.00 125.07 ? 274 LEU B N   1 
ATOM   2062 C  CA  . LEU B 2 274 ? 65.383  59.228  38.866 1.00 173.74 ? 274 LEU B CA  1 
ATOM   2063 C  C   . LEU B 2 274 ? 64.331  58.437  39.660 1.00 149.20 ? 274 LEU B C   1 
ATOM   2064 O  O   . LEU B 2 274 ? 64.519  58.265  40.862 1.00 168.88 ? 274 LEU B O   1 
ATOM   2065 C  CB  . LEU B 2 274 ? 64.867  60.613  38.431 1.00 200.77 ? 274 LEU B CB  1 
ATOM   2066 C  CG  . LEU B 2 274 ? 64.147  61.460  39.485 1.00 190.20 ? 274 LEU B CG  1 
ATOM   2067 C  CD1 . LEU B 2 274 ? 65.030  61.758  40.686 1.00 180.98 ? 274 LEU B CD1 1 
ATOM   2068 C  CD2 . LEU B 2 274 ? 63.641  62.741  38.861 1.00 202.49 ? 274 LEU B CD2 1 
ATOM   2069 N  N   . PRO B 2 275 ? 63.205  57.946  39.092 1.00 117.14 ? 275 PRO B N   1 
ATOM   2070 C  CA  . PRO B 2 275 ? 62.275  57.145  39.842 1.00 135.72 ? 275 PRO B CA  1 
ATOM   2071 C  C   . PRO B 2 275 ? 62.907  55.817  40.284 1.00 161.40 ? 275 PRO B C   1 
ATOM   2072 O  O   . PRO B 2 275 ? 62.627  55.362  41.384 1.00 187.50 ? 275 PRO B O   1 
ATOM   2073 C  CB  . PRO B 2 275 ? 61.091  56.974  38.879 1.00 181.68 ? 275 PRO B CB  1 
ATOM   2074 C  CG  . PRO B 2 275 ? 61.675  57.061  37.539 1.00 186.83 ? 275 PRO B CG  1 
ATOM   2075 C  CD  . PRO B 2 275 ? 62.742  58.104  37.719 1.00 185.55 ? 275 PRO B CD  1 
ATOM   2076 N  N   . LEU B 2 276 ? 63.769  55.198  39.480 1.00 145.18 ? 276 LEU B N   1 
ATOM   2077 C  CA  . LEU B 2 276 ? 64.329  53.915  39.870 1.00 171.26 ? 276 LEU B CA  1 
ATOM   2078 C  C   . LEU B 2 276 ? 65.308  54.082  41.042 1.00 195.64 ? 276 LEU B C   1 
ATOM   2079 O  O   . LEU B 2 276 ? 65.284  53.247  41.945 1.00 231.42 ? 276 LEU B O   1 
ATOM   2080 C  CB  . LEU B 2 276 ? 64.996  53.242  38.666 1.00 190.67 ? 276 LEU B CB  1 
ATOM   2081 C  CG  . LEU B 2 276 ? 65.539  51.839  38.900 1.00 232.06 ? 276 LEU B CG  1 
ATOM   2082 C  CD1 . LEU B 2 276 ? 64.441  50.897  39.381 1.00 274.42 ? 276 LEU B CD1 1 
ATOM   2083 C  CD2 . LEU B 2 276 ? 66.160  51.303  37.613 1.00 348.34 ? 276 LEU B CD2 1 
ATOM   2084 N  N   . ALA B 2 277 ? 66.157  55.121  41.061 1.00 190.33 ? 277 ALA B N   1 
ATOM   2085 C  CA  . ALA B 2 277 ? 67.116  55.330  42.146 1.00 198.41 ? 277 ALA B CA  1 
ATOM   2086 C  C   . ALA B 2 277 ? 66.392  55.646  43.451 1.00 154.69 ? 277 ALA B C   1 
ATOM   2087 O  O   . ALA B 2 277 ? 66.858  55.199  44.499 1.00 156.78 ? 277 ALA B O   1 
ATOM   2088 C  CB  . ALA B 2 277 ? 68.120  56.410  41.774 1.00 238.14 ? 277 ALA B CB  1 
ATOM   2089 N  N   . ILE B 2 278 ? 65.277  56.402  43.403 1.00 109.34 ? 278 ILE B N   1 
ATOM   2090 C  CA  . ILE B 2 278 ? 64.410  56.569  44.580 1.00 158.15 ? 278 ILE B CA  1 
ATOM   2091 C  C   . ILE B 2 278 ? 63.847  55.244  45.096 1.00 142.07 ? 278 ILE B C   1 
ATOM   2092 O  O   . ILE B 2 278 ? 63.958  54.986  46.291 1.00 124.34 ? 278 ILE B O   1 
ATOM   2093 C  CB  . ILE B 2 278 ? 63.307  57.612  44.307 1.00 117.91 ? 278 ILE B CB  1 
ATOM   2094 C  CG1 . ILE B 2 278 ? 63.983  58.998  44.348 1.00 112.52 ? 278 ILE B CG1 1 
ATOM   2095 C  CG2 . ILE B 2 278 ? 62.048  57.451  45.216 1.00 89.77  ? 278 ILE B CG2 1 
ATOM   2096 C  CD1 . ILE B 2 278 ? 63.062  60.179  44.018 1.00 168.03 ? 278 ILE B CD1 1 
ATOM   2097 N  N   . ILE B 2 279 ? 63.286  54.427  44.208 1.00 121.81 ? 279 ILE B N   1 
ATOM   2098 C  CA  . ILE B 2 279 ? 62.681  53.160  44.599 1.00 162.21 ? 279 ILE B CA  1 
ATOM   2099 C  C   . ILE B 2 279 ? 63.745  52.134  45.047 1.00 178.66 ? 279 ILE B C   1 
ATOM   2100 O  O   . ILE B 2 279 ? 63.465  51.331  45.929 1.00 223.53 ? 279 ILE B O   1 
ATOM   2101 C  CB  . ILE B 2 279 ? 61.797  52.637  43.452 1.00 271.43 ? 279 ILE B CB  1 
ATOM   2102 C  CG1 . ILE B 2 279 ? 60.608  53.572  43.216 1.00 251.08 ? 279 ILE B CG1 1 
ATOM   2103 C  CG2 . ILE B 2 279 ? 61.337  51.194  43.701 1.00 352.55 ? 279 ILE B CG2 1 
ATOM   2104 C  CD1 . ILE B 2 279 ? 59.912  53.405  41.870 1.00 300.99 ? 279 ILE B CD1 1 
ATOM   2105 N  N   . ILE B 2 280 ? 64.962  52.130  44.481 1.00 142.82 ? 280 ILE B N   1 
ATOM   2106 C  CA  . ILE B 2 280 ? 66.049  51.300  44.990 1.00 164.50 ? 280 ILE B CA  1 
ATOM   2107 C  C   . ILE B 2 280 ? 66.524  51.790  46.372 1.00 224.67 ? 280 ILE B C   1 
ATOM   2108 O  O   . ILE B 2 280 ? 66.737  50.974  47.261 1.00 150.31 ? 280 ILE B O   1 
ATOM   2109 C  CB  . ILE B 2 280 ? 67.217  51.247  43.975 1.00 219.86 ? 280 ILE B CB  1 
ATOM   2110 C  CG1 . ILE B 2 280 ? 66.840  50.440  42.720 1.00 353.07 ? 280 ILE B CG1 1 
ATOM   2111 C  CG2 . ILE B 2 280 ? 68.533  50.741  44.596 1.00 230.55 ? 280 ILE B CG2 1 
ATOM   2112 C  CD1 . ILE B 2 280 ? 66.708  48.931  42.919 1.00 419.66 ? 280 ILE B CD1 1 
ATOM   2113 N  N   . SER B 2 281 ? 66.708  53.109  46.547 1.00 251.97 ? 281 SER B N   1 
ATOM   2114 C  CA  . SER B 2 281 ? 67.341  53.705  47.724 1.00 269.60 ? 281 SER B CA  1 
ATOM   2115 C  C   . SER B 2 281 ? 66.440  53.714  48.952 1.00 210.83 ? 281 SER B C   1 
ATOM   2116 O  O   . SER B 2 281 ? 66.775  53.123  49.990 1.00 216.57 ? 281 SER B O   1 
ATOM   2117 C  CB  . SER B 2 281 ? 67.803  55.138  47.458 1.00 222.50 ? 281 SER B CB  1 
ATOM   2118 O  OG  . SER B 2 281 ? 68.372  55.724  48.646 1.00 197.42 ? 281 SER B OG  1 
ATOM   2119 N  N   . LEU B 2 282 ? 65.316  54.429  48.861 1.00 133.81 ? 282 LEU B N   1 
ATOM   2120 C  CA  . LEU B 2 282 ? 64.663  54.852  50.088 1.00 188.78 ? 282 LEU B CA  1 
ATOM   2121 C  C   . LEU B 2 282 ? 64.036  53.680  50.901 1.00 194.25 ? 282 LEU B C   1 
ATOM   2122 O  O   . LEU B 2 282 ? 64.079  53.692  52.142 1.00 212.17 ? 282 LEU B O   1 
ATOM   2123 C  CB  . LEU B 2 282 ? 63.756  56.013  49.680 1.00 157.06 ? 282 LEU B CB  1 
ATOM   2124 C  CG  . LEU B 2 282 ? 63.054  56.698  50.856 1.00 215.92 ? 282 LEU B CG  1 
ATOM   2125 C  CD1 . LEU B 2 282 ? 63.997  57.217  51.922 1.00 260.25 ? 282 LEU B CD1 1 
ATOM   2126 C  CD2 . LEU B 2 282 ? 62.264  57.854  50.374 1.00 186.45 ? 282 LEU B CD2 1 
ATOM   2127 N  N   . PRO B 2 283 ? 63.456  52.623  50.300 1.00 130.94 ? 283 PRO B N   1 
ATOM   2128 C  CA  . PRO B 2 283 ? 63.138  51.395  51.017 1.00 170.04 ? 283 PRO B CA  1 
ATOM   2129 C  C   . PRO B 2 283 ? 64.336  50.691  51.667 1.00 216.36 ? 283 PRO B C   1 
ATOM   2130 O  O   . PRO B 2 283 ? 64.183  50.165  52.772 1.00 307.30 ? 283 PRO B O   1 
ATOM   2131 C  CB  . PRO B 2 283 ? 62.523  50.488  49.941 1.00 268.97 ? 283 PRO B CB  1 
ATOM   2132 C  CG  . PRO B 2 283 ? 61.987  51.468  48.936 1.00 311.28 ? 283 PRO B CG  1 
ATOM   2133 C  CD  . PRO B 2 283 ? 63.044  52.548  48.917 1.00 197.32 ? 283 PRO B CD  1 
ATOM   2134 N  N   . ILE B 2 284 ? 65.518  50.684  51.031 1.00 165.04 ? 284 ILE B N   1 
ATOM   2135 C  CA  . ILE B 2 284 ? 66.715  50.112  51.646 1.00 211.38 ? 284 ILE B CA  1 
ATOM   2136 C  C   . ILE B 2 284 ? 67.059  50.881  52.925 1.00 205.17 ? 284 ILE B C   1 
ATOM   2137 O  O   . ILE B 2 284 ? 67.341  50.250  53.947 1.00 193.68 ? 284 ILE B O   1 
ATOM   2138 C  CB  . ILE B 2 284 ? 67.901  50.021  50.656 1.00 247.59 ? 284 ILE B CB  1 
ATOM   2139 C  CG1 . ILE B 2 284 ? 67.631  48.924  49.625 1.00 347.71 ? 284 ILE B CG1 1 
ATOM   2140 C  CG2 . ILE B 2 284 ? 69.238  49.787  51.353 1.00 271.66 ? 284 ILE B CG2 1 
ATOM   2141 C  CD1 . ILE B 2 284 ? 68.699  48.768  48.560 1.00 389.04 ? 284 ILE B CD1 1 
ATOM   2142 N  N   . VAL B 2 285 ? 67.026  52.222  52.886 1.00 186.50 ? 285 VAL B N   1 
ATOM   2143 C  CA  . VAL B 2 285 ? 67.256  53.031  54.080 1.00 192.82 ? 285 VAL B CA  1 
ATOM   2144 C  C   . VAL B 2 285 ? 66.269  52.679  55.198 1.00 167.43 ? 285 VAL B C   1 
ATOM   2145 O  O   . VAL B 2 285 ? 66.656  52.491  56.351 1.00 182.16 ? 285 VAL B O   1 
ATOM   2146 C  CB  . VAL B 2 285 ? 67.175  54.533  53.797 1.00 187.72 ? 285 VAL B CB  1 
ATOM   2147 C  CG1 . VAL B 2 285 ? 67.305  55.339  55.094 1.00 189.86 ? 285 VAL B CG1 1 
ATOM   2148 C  CG2 . VAL B 2 285 ? 68.209  54.968  52.769 1.00 244.20 ? 285 VAL B CG2 1 
ATOM   2149 N  N   . THR B 2 286 ? 64.992  52.566  54.853 1.00 131.93 ? 286 THR B N   1 
ATOM   2150 C  CA  . THR B 2 286 ? 63.972  52.193  55.812 1.00 164.07 ? 286 THR B CA  1 
ATOM   2151 C  C   . THR B 2 286 ? 64.302  50.864  56.503 1.00 136.64 ? 286 THR B C   1 
ATOM   2152 O  O   . THR B 2 286 ? 64.216  50.759  57.731 1.00 165.65 ? 286 THR B O   1 
ATOM   2153 C  CB  . THR B 2 286 ? 62.584  52.171  55.151 1.00 198.37 ? 286 THR B CB  1 
ATOM   2154 O  OG1 . THR B 2 286 ? 62.333  53.471  54.623 1.00 185.55 ? 286 THR B OG1 1 
ATOM   2155 C  CG2 . THR B 2 286 ? 61.456  51.797  56.095 1.00 209.15 ? 286 THR B CG2 1 
ATOM   2156 N  N   . LEU B 2 287 ? 64.669  49.845  55.732 1.00 126.49 ? 287 LEU B N   1 
ATOM   2157 C  CA  . LEU B 2 287 ? 65.031  48.554  56.292 1.00 203.09 ? 287 LEU B CA  1 
ATOM   2158 C  C   . LEU B 2 287 ? 66.228  48.697  57.236 1.00 177.48 ? 287 LEU B C   1 
ATOM   2159 O  O   . LEU B 2 287 ? 66.222  48.141  58.350 1.00 209.49 ? 287 LEU B O   1 
ATOM   2160 C  CB  . LEU B 2 287 ? 65.334  47.591  55.135 1.00 286.13 ? 287 LEU B CB  1 
ATOM   2161 C  CG  . LEU B 2 287 ? 65.832  46.199  55.526 1.00 374.14 ? 287 LEU B CG  1 
ATOM   2162 C  CD1 . LEU B 2 287 ? 64.757  45.431  56.282 1.00 418.13 ? 287 LEU B CD1 1 
ATOM   2163 C  CD2 . LEU B 2 287 ? 66.282  45.424  54.298 1.00 421.48 ? 287 LEU B CD2 1 
ATOM   2164 N  N   . VAL B 2 288 ? 67.256  49.433  56.789 1.00 139.75 ? 288 VAL B N   1 
ATOM   2165 C  CA  . VAL B 2 288 ? 68.485  49.590  57.549 1.00 169.26 ? 288 VAL B CA  1 
ATOM   2166 C  C   . VAL B 2 288 ? 68.190  50.281  58.878 1.00 136.49 ? 288 VAL B C   1 
ATOM   2167 O  O   . VAL B 2 288 ? 68.761  49.900  59.899 1.00 177.80 ? 288 VAL B O   1 
ATOM   2168 C  CB  . VAL B 2 288 ? 69.584  50.298  56.718 1.00 191.16 ? 288 VAL B CB  1 
ATOM   2169 C  CG1 . VAL B 2 288 ? 70.755  50.800  57.543 1.00 161.09 ? 288 VAL B CG1 1 
ATOM   2170 C  CG2 . VAL B 2 288 ? 70.117  49.378  55.636 1.00 282.71 ? 288 VAL B CG2 1 
ATOM   2171 N  N   . TYR B 2 289 ? 67.318  51.291  58.897 1.00 137.33 ? 289 TYR B N   1 
ATOM   2172 C  CA  . TYR B 2 289 ? 67.005  51.992  60.140 1.00 185.52 ? 289 TYR B CA  1 
ATOM   2173 C  C   . TYR B 2 289 ? 66.295  51.122  61.172 1.00 169.08 ? 289 TYR B C   1 
ATOM   2174 O  O   . TYR B 2 289 ? 66.684  51.124  62.341 1.00 121.21 ? 289 TYR B O   1 
ATOM   2175 C  CB  . TYR B 2 289 ? 66.172  53.230  59.827 1.00 169.30 ? 289 TYR B CB  1 
ATOM   2176 C  CG  . TYR B 2 289 ? 66.959  54.448  59.371 1.00 198.38 ? 289 TYR B CG  1 
ATOM   2177 C  CD1 . TYR B 2 289 ? 68.342  54.429  59.121 1.00 185.47 ? 289 TYR B CD1 1 
ATOM   2178 C  CD2 . TYR B 2 289 ? 66.291  55.652  59.210 1.00 202.79 ? 289 TYR B CD2 1 
ATOM   2179 C  CE1 . TYR B 2 289 ? 69.016  55.571  58.727 1.00 164.55 ? 289 TYR B CE1 1 
ATOM   2180 C  CE2 . TYR B 2 289 ? 66.950  56.802  58.823 1.00 183.03 ? 289 TYR B CE2 1 
ATOM   2181 C  CZ  . TYR B 2 289 ? 68.317  56.764  58.582 1.00 181.13 ? 289 TYR B CZ  1 
ATOM   2182 O  OH  . TYR B 2 289 ? 68.967  57.908  58.212 1.00 100.14 ? 289 TYR B OH  1 
ATOM   2183 N  N   . VAL B 2 290 ? 65.268  50.373  60.772 1.00 184.91 ? 290 VAL B N   1 
ATOM   2184 C  CA  . VAL B 2 290 ? 64.578  49.537  61.741 1.00 193.63 ? 290 VAL B CA  1 
ATOM   2185 C  C   . VAL B 2 290 ? 65.522  48.451  62.263 1.00 141.02 ? 290 VAL B C   1 
ATOM   2186 O  O   . VAL B 2 290 ? 65.497  48.175  63.463 1.00 194.21 ? 290 VAL B O   1 
ATOM   2187 C  CB  . VAL B 2 290 ? 63.237  48.994  61.210 1.00 232.16 ? 290 VAL B CB  1 
ATOM   2188 C  CG1 . VAL B 2 290 ? 62.298  50.154  60.936 1.00 205.91 ? 290 VAL B CG1 1 
ATOM   2189 C  CG2 . VAL B 2 290 ? 63.370  48.084  59.990 1.00 299.26 ? 290 VAL B CG2 1 
ATOM   2190 N  N   . LEU B 2 291 ? 66.355  47.842  61.417 1.00 145.83 ? 291 LEU B N   1 
ATOM   2191 C  CA  . LEU B 2 291 ? 67.338  46.871  61.884 1.00 185.08 ? 291 LEU B CA  1 
ATOM   2192 C  C   . LEU B 2 291 ? 68.396  47.532  62.768 1.00 186.77 ? 291 LEU B C   1 
ATOM   2193 O  O   . LEU B 2 291 ? 68.841  46.901  63.737 1.00 249.00 ? 291 LEU B O   1 
ATOM   2194 C  CB  . LEU B 2 291 ? 67.991  46.178  60.685 1.00 202.93 ? 291 LEU B CB  1 
ATOM   2195 C  CG  . LEU B 2 291 ? 67.093  45.237  59.900 1.00 292.06 ? 291 LEU B CG  1 
ATOM   2196 C  CD1 . LEU B 2 291 ? 67.833  44.721  58.668 1.00 315.07 ? 291 LEU B CD1 1 
ATOM   2197 C  CD2 . LEU B 2 291 ? 66.609  44.088  60.790 1.00 302.52 ? 291 LEU B CD2 1 
ATOM   2198 N  N   . THR B 2 292 ? 68.795  48.780  62.469 1.00 129.54 ? 292 THR B N   1 
ATOM   2199 C  CA  . THR B 2 292 ? 69.808  49.453  63.276 1.00 173.88 ? 292 THR B CA  1 
ATOM   2200 C  C   . THR B 2 292 ? 69.265  49.780  64.670 1.00 145.75 ? 292 THR B C   1 
ATOM   2201 O  O   . THR B 2 292 ? 69.949  49.565  65.671 1.00 158.41 ? 292 THR B O   1 
ATOM   2202 C  CB  . THR B 2 292 ? 70.324  50.714  62.583 1.00 213.88 ? 292 THR B CB  1 
ATOM   2203 O  OG1 . THR B 2 292 ? 70.930  50.367  61.345 1.00 141.65 ? 292 THR B OG1 1 
ATOM   2204 C  CG2 . THR B 2 292 ? 71.364  51.466  63.379 1.00 244.07 ? 292 THR B CG2 1 
ATOM   2205 N  N   . ASN B 2 293 ? 68.043  50.293  64.768 1.00 99.67  ? 293 ASN B N   1 
ATOM   2206 C  CA  . ASN B 2 293 ? 67.458  50.556  66.073 1.00 148.14 ? 293 ASN B CA  1 
ATOM   2207 C  C   . ASN B 2 293 ? 67.219  49.265  66.859 1.00 194.20 ? 293 ASN B C   1 
ATOM   2208 O  O   . ASN B 2 293 ? 67.473  49.236  68.060 1.00 185.07 ? 293 ASN B O   1 
ATOM   2209 C  CB  . ASN B 2 293 ? 66.155  51.334  65.932 1.00 169.43 ? 293 ASN B CB  1 
ATOM   2210 C  CG  . ASN B 2 293 ? 66.409  52.773  65.631 1.00 173.30 ? 293 ASN B CG  1 
ATOM   2211 O  OD1 . ASN B 2 293 ? 66.651  53.538  66.556 1.00 210.10 ? 293 ASN B OD1 1 
ATOM   2212 N  ND2 . ASN B 2 293 ? 66.351  53.149  64.359 1.00 195.52 ? 293 ASN B ND2 1 
ATOM   2213 N  N   . LEU B 2 294 ? 66.731  48.201  66.194 1.00 181.37 ? 294 LEU B N   1 
ATOM   2214 C  CA  . LEU B 2 294 ? 66.573  46.894  66.815 1.00 154.08 ? 294 LEU B CA  1 
ATOM   2215 C  C   . LEU B 2 294 ? 67.926  46.497  67.408 1.00 152.94 ? 294 LEU B C   1 
ATOM   2216 O  O   . LEU B 2 294 ? 67.974  46.096  68.568 1.00 214.82 ? 294 LEU B O   1 
ATOM   2217 C  CB  . LEU B 2 294 ? 66.030  45.909  65.764 1.00 245.59 ? 294 LEU B CB  1 
ATOM   2218 C  CG  . LEU B 2 294 ? 65.837  44.430  66.132 1.00 357.13 ? 294 LEU B CG  1 
ATOM   2219 C  CD1 . LEU B 2 294 ? 67.151  43.633  66.144 1.00 341.39 ? 294 LEU B CD1 1 
ATOM   2220 C  CD2 . LEU B 2 294 ? 65.104  44.281  67.463 1.00 437.77 ? 294 LEU B CD2 1 
ATOM   2221 N  N   . ALA B 2 295 ? 69.022  46.627  66.645 1.00 124.34 ? 295 ALA B N   1 
ATOM   2222 C  CA  . ALA B 2 295 ? 70.363  46.341  67.142 1.00 177.94 ? 295 ALA B CA  1 
ATOM   2223 C  C   . ALA B 2 295 ? 70.700  47.164  68.397 1.00 180.21 ? 295 ALA B C   1 
ATOM   2224 O  O   . ALA B 2 295 ? 71.139  46.581  69.381 1.00 177.60 ? 295 ALA B O   1 
ATOM   2225 C  CB  . ALA B 2 295 ? 71.371  46.515  66.024 1.00 194.29 ? 295 ALA B CB  1 
ATOM   2226 N  N   . TYR B 2 296 ? 70.488  48.483  68.415 1.00 183.32 ? 296 TYR B N   1 
ATOM   2227 C  CA  . TYR B 2 296 ? 70.751  49.289  69.605 1.00 202.72 ? 296 TYR B CA  1 
ATOM   2228 C  C   . TYR B 2 296 ? 69.983  48.774  70.826 1.00 196.67 ? 296 TYR B C   1 
ATOM   2229 O  O   . TYR B 2 296 ? 70.559  48.650  71.905 1.00 255.61 ? 296 TYR B O   1 
ATOM   2230 C  CB  . TYR B 2 296 ? 70.376  50.765  69.414 1.00 230.51 ? 296 TYR B CB  1 
ATOM   2231 C  CG  . TYR B 2 296 ? 71.179  51.558  68.398 1.00 240.40 ? 296 TYR B CG  1 
ATOM   2232 C  CD1 . TYR B 2 296 ? 72.553  51.350  68.234 1.00 177.64 ? 296 TYR B CD1 1 
ATOM   2233 C  CD2 . TYR B 2 296 ? 70.557  52.538  67.619 1.00 205.04 ? 296 TYR B CD2 1 
ATOM   2234 C  CE1 . TYR B 2 296 ? 73.271  52.080  67.304 1.00 218.13 ? 296 TYR B CE1 1 
ATOM   2235 C  CE2 . TYR B 2 296 ? 71.275  53.266  66.682 1.00 217.59 ? 296 TYR B CE2 1 
ATOM   2236 C  CZ  . TYR B 2 296 ? 72.638  53.044  66.530 1.00 231.67 ? 296 TYR B CZ  1 
ATOM   2237 O  OH  . TYR B 2 296 ? 73.359  53.761  65.609 1.00 181.12 ? 296 TYR B OH  1 
ATOM   2238 N  N   . PHE B 2 297 ? 68.691  48.465  70.673 1.00 167.44 ? 297 PHE B N   1 
ATOM   2239 C  CA  . PHE B 2 297 ? 67.878  47.974  71.779 1.00 197.87 ? 297 PHE B CA  1 
ATOM   2240 C  C   . PHE B 2 297 ? 68.275  46.578  72.285 1.00 207.81 ? 297 PHE B C   1 
ATOM   2241 O  O   . PHE B 2 297 ? 67.800  46.191  73.350 1.00 218.39 ? 297 PHE B O   1 
ATOM   2242 C  CB  . PHE B 2 297 ? 66.399  48.032  71.387 1.00 193.28 ? 297 PHE B CB  1 
ATOM   2243 C  CG  . PHE B 2 297 ? 65.813  49.419  71.312 1.00 164.52 ? 297 PHE B CG  1 
ATOM   2244 C  CD1 . PHE B 2 297 ? 65.901  50.282  72.389 1.00 211.58 ? 297 PHE B CD1 1 
ATOM   2245 C  CD2 . PHE B 2 297 ? 65.150  49.871  70.182 1.00 237.37 ? 297 PHE B CD2 1 
ATOM   2246 C  CE1 . PHE B 2 297 ? 65.355  51.558  72.336 1.00 224.70 ? 297 PHE B CE1 1 
ATOM   2247 C  CE2 . PHE B 2 297 ? 64.602  51.148  70.132 1.00 257.07 ? 297 PHE B CE2 1 
ATOM   2248 C  CZ  . PHE B 2 297 ? 64.705  51.985  71.206 1.00 210.66 ? 297 PHE B CZ  1 
ATOM   2249 N  N   . THR B 2 298 ? 69.130  45.819  71.575 1.00 184.77 ? 298 THR B N   1 
ATOM   2250 C  CA  . THR B 2 298 ? 69.712  44.608  72.149 1.00 228.16 ? 298 THR B CA  1 
ATOM   2251 C  C   . THR B 2 298 ? 70.714  44.924  73.262 1.00 224.08 ? 298 THR B C   1 
ATOM   2252 O  O   . THR B 2 298 ? 70.878  44.115  74.175 1.00 288.06 ? 298 THR B O   1 
ATOM   2253 C  CB  . THR B 2 298 ? 70.424  43.703  71.128 1.00 229.36 ? 298 THR B CB  1 
ATOM   2254 O  OG1 . THR B 2 298 ? 71.619  44.303  70.643 1.00 168.41 ? 298 THR B OG1 1 
ATOM   2255 C  CG2 . THR B 2 298 ? 69.565  43.366  69.930 1.00 296.91 ? 298 THR B CG2 1 
ATOM   2256 N  N   . THR B 2 299 ? 71.394  46.078  73.180 1.00 180.93 ? 299 THR B N   1 
ATOM   2257 C  CA  . THR B 2 299 ? 72.584  46.361  73.978 1.00 239.75 ? 299 THR B CA  1 
ATOM   2258 C  C   . THR B 2 299 ? 72.327  47.400  75.065 1.00 215.26 ? 299 THR B C   1 
ATOM   2259 O  O   . THR B 2 299 ? 72.784  47.233  76.198 1.00 256.47 ? 299 THR B O   1 
ATOM   2260 C  CB  . THR B 2 299 ? 73.734  46.853  73.090 1.00 271.83 ? 299 THR B CB  1 
ATOM   2261 O  OG1 . THR B 2 299 ? 74.025  45.872  72.091 1.00 218.95 ? 299 THR B OG1 1 
ATOM   2262 C  CG2 . THR B 2 299 ? 75.002  47.129  73.867 1.00 232.53 ? 299 THR B CG2 1 
ATOM   2263 N  N   . LEU B 2 300 ? 71.621  48.483  74.713 1.00 205.17 ? 300 LEU B N   1 
ATOM   2264 C  CA  . LEU B 2 300 ? 71.430  49.608  75.611 1.00 253.10 ? 300 LEU B CA  1 
ATOM   2265 C  C   . LEU B 2 300 ? 70.001  49.590  76.162 1.00 249.21 ? 300 LEU B C   1 
ATOM   2266 O  O   . LEU B 2 300 ? 69.026  49.486  75.435 1.00 225.35 ? 300 LEU B O   1 
ATOM   2267 C  CB  . LEU B 2 300 ? 71.747  50.911  74.865 1.00 281.10 ? 300 LEU B CB  1 
ATOM   2268 C  CG  . LEU B 2 300 ? 73.192  51.066  74.366 1.00 257.25 ? 300 LEU B CG  1 
ATOM   2269 C  CD1 . LEU B 2 300 ? 73.366  52.366  73.610 1.00 228.81 ? 300 LEU B CD1 1 
ATOM   2270 C  CD2 . LEU B 2 300 ? 74.219  51.022  75.490 1.00 285.44 ? 300 LEU B CD2 1 
ATOM   2271 N  N   . SER B 2 301 ? 69.882  49.704  77.488 1.00 268.03 ? 301 SER B N   1 
ATOM   2272 C  CA  . SER B 2 301 ? 68.612  49.911  78.171 1.00 257.16 ? 301 SER B CA  1 
ATOM   2273 C  C   . SER B 2 301 ? 68.029  51.290  77.873 1.00 192.24 ? 301 SER B C   1 
ATOM   2274 O  O   . SER B 2 301 ? 68.752  52.208  77.496 1.00 188.88 ? 301 SER B O   1 
ATOM   2275 C  CB  . SER B 2 301 ? 68.788  49.746  79.658 1.00 334.76 ? 301 SER B CB  1 
ATOM   2276 O  OG  . SER B 2 301 ? 69.665  50.737  80.171 1.00 303.65 ? 301 SER B OG  1 
ATOM   2277 N  N   . THR B 2 302 ? 66.710  51.444  78.066 1.00 204.08 ? 302 THR B N   1 
ATOM   2278 C  CA  . THR B 2 302 ? 66.021  52.727  77.908 1.00 296.50 ? 302 THR B CA  1 
ATOM   2279 C  C   . THR B 2 302 ? 66.711  53.857  78.688 1.00 322.43 ? 302 THR B C   1 
ATOM   2280 O  O   . THR B 2 302 ? 66.898  54.956  78.162 1.00 317.01 ? 302 THR B O   1 
ATOM   2281 C  CB  . THR B 2 302 ? 64.543  52.621  78.320 1.00 292.36 ? 302 THR B CB  1 
ATOM   2282 O  OG1 . THR B 2 302 ? 63.954  51.559  77.568 1.00 270.14 ? 302 THR B OG1 1 
ATOM   2283 C  CG2 . THR B 2 302 ? 63.734  53.882  78.087 1.00 267.92 ? 302 THR B CG2 1 
ATOM   2284 N  N   . GLU B 2 303 ? 67.101  53.584  79.937 1.00 300.05 ? 303 GLU B N   1 
ATOM   2285 C  CA  . GLU B 2 303 ? 67.741  54.573  80.800 1.00 305.03 ? 303 GLU B CA  1 
ATOM   2286 C  C   . GLU B 2 303 ? 69.120  55.007  80.269 1.00 274.14 ? 303 GLU B C   1 
ATOM   2287 O  O   . GLU B 2 303 ? 69.461  56.196  80.374 1.00 270.47 ? 303 GLU B O   1 
ATOM   2288 C  CB  . GLU B 2 303 ? 67.778  54.054  82.247 1.00 411.58 ? 303 GLU B CB  1 
ATOM   2289 C  CG  . GLU B 2 303 ? 68.502  52.715  82.473 1.00 432.14 ? 303 GLU B CG  1 
ATOM   2290 C  CD  . GLU B 2 303 ? 68.555  52.219  83.910 1.00 491.99 ? 303 GLU B CD  1 
ATOM   2291 O  OE1 . GLU B 2 303 ? 67.526  52.328  84.608 1.00 540.66 ? 303 GLU B OE1 1 
ATOM   2292 O  OE2 . GLU B 2 303 ? 69.626  51.707  84.336 1.00 511.68 ? 303 GLU B OE2 1 
ATOM   2293 N  N   . GLN B 2 304 ? 69.915  54.067  79.712 1.00 224.79 ? 304 GLN B N   1 
ATOM   2294 C  CA  . GLN B 2 304 ? 71.159  54.415  79.030 1.00 252.64 ? 304 GLN B CA  1 
ATOM   2295 C  C   . GLN B 2 304 ? 70.869  55.255  77.789 1.00 234.86 ? 304 GLN B C   1 
ATOM   2296 O  O   . GLN B 2 304 ? 71.418  56.332  77.620 1.00 188.91 ? 304 GLN B O   1 
ATOM   2297 C  CB  . GLN B 2 304 ? 71.947  53.169  78.625 1.00 215.38 ? 304 GLN B CB  1 
ATOM   2298 C  CG  . GLN B 2 304 ? 72.644  52.500  79.798 1.00 317.95 ? 304 GLN B CG  1 
ATOM   2299 C  CD  . GLN B 2 304 ? 73.012  51.055  79.552 1.00 348.34 ? 304 GLN B CD  1 
ATOM   2300 O  OE1 . GLN B 2 304 ? 72.144  50.229  79.278 1.00 346.43 ? 304 GLN B OE1 1 
ATOM   2301 N  NE2 . GLN B 2 304 ? 74.294  50.727  79.658 1.00 352.51 ? 304 GLN B NE2 1 
ATOM   2302 N  N   . MET B 2 305 ? 69.992  54.766  76.921 1.00 242.60 ? 305 MET B N   1 
ATOM   2303 C  CA  . MET B 2 305 ? 69.819  55.358  75.610 1.00 229.27 ? 305 MET B CA  1 
ATOM   2304 C  C   . MET B 2 305 ? 69.207  56.762  75.731 1.00 223.32 ? 305 MET B C   1 
ATOM   2305 O  O   . MET B 2 305 ? 69.651  57.680  75.017 1.00 265.15 ? 305 MET B O   1 
ATOM   2306 C  CB  . MET B 2 305 ? 68.966  54.438  74.733 1.00 216.64 ? 305 MET B CB  1 
ATOM   2307 C  CG  . MET B 2 305 ? 69.073  54.796  73.251 1.00 222.21 ? 305 MET B CG  1 
ATOM   2308 S  SD  . MET B 2 305 ? 68.174  53.701  72.120 1.00 275.34 ? 305 MET B SD  1 
ATOM   2309 C  CE  . MET B 2 305 ? 68.936  52.121  72.471 1.00 206.70 ? 305 MET B CE  1 
ATOM   2310 N  N   . LEU B 2 306 ? 68.225  56.955  76.637 1.00 186.91 ? 306 LEU B N   1 
ATOM   2311 C  CA  . LEU B 2 306 ? 67.530  58.232  76.783 1.00 229.72 ? 306 LEU B CA  1 
ATOM   2312 C  C   . LEU B 2 306 ? 68.400  59.335  77.421 1.00 238.40 ? 306 LEU B C   1 
ATOM   2313 O  O   . LEU B 2 306 ? 68.058  60.530  77.329 1.00 183.93 ? 306 LEU B O   1 
ATOM   2314 C  CB  . LEU B 2 306 ? 66.228  57.993  77.550 1.00 214.59 ? 306 LEU B CB  1 
ATOM   2315 C  CG  . LEU B 2 306 ? 65.205  59.135  77.485 1.00 229.07 ? 306 LEU B CG  1 
ATOM   2316 C  CD1 . LEU B 2 306 ? 63.819  58.542  77.399 1.00 247.70 ? 306 LEU B CD1 1 
ATOM   2317 C  CD2 . LEU B 2 306 ? 65.230  60.053  78.711 1.00 307.10 ? 306 LEU B CD2 1 
ATOM   2318 N  N   . SER B 2 307 ? 69.537  58.958  78.037 1.00 181.73 ? 307 SER B N   1 
ATOM   2319 C  CA  . SER B 2 307 ? 70.458  59.899  78.672 1.00 249.77 ? 307 SER B CA  1 
ATOM   2320 C  C   . SER B 2 307 ? 71.753  60.139  77.885 1.00 255.86 ? 307 SER B C   1 
ATOM   2321 O  O   . SER B 2 307 ? 72.335  61.214  77.995 1.00 281.64 ? 307 SER B O   1 
ATOM   2322 C  CB  . SER B 2 307 ? 70.764  59.435  80.077 1.00 304.47 ? 307 SER B CB  1 
ATOM   2323 O  OG  . SER B 2 307 ? 71.390  58.162  80.084 1.00 292.62 ? 307 SER B OG  1 
ATOM   2324 N  N   . SER B 2 308 ? 72.210  59.159  77.089 1.00 256.12 ? 308 SER B N   1 
ATOM   2325 C  CA  . SER B 2 308 ? 73.531  59.148  76.458 1.00 269.87 ? 308 SER B CA  1 
ATOM   2326 C  C   . SER B 2 308 ? 73.689  60.174  75.332 1.00 204.28 ? 308 SER B C   1 
ATOM   2327 O  O   . SER B 2 308 ? 72.715  60.585  74.698 1.00 232.88 ? 308 SER B O   1 
ATOM   2328 C  CB  . SER B 2 308 ? 73.843  57.777  75.941 1.00 295.23 ? 308 SER B CB  1 
ATOM   2329 O  OG  . SER B 2 308 ? 73.936  56.852  77.015 1.00 335.58 ? 308 SER B OG  1 
ATOM   2330 N  N   . GLU B 2 309 ? 74.953  60.580  75.087 1.00 193.51 ? 309 GLU B N   1 
ATOM   2331 C  CA  . GLU B 2 309 ? 75.284  61.755  74.269 1.00 302.19 ? 309 GLU B CA  1 
ATOM   2332 C  C   . GLU B 2 309 ? 75.268  61.386  72.782 1.00 298.97 ? 309 GLU B C   1 
ATOM   2333 O  O   . GLU B 2 309 ? 74.818  62.183  71.953 1.00 209.26 ? 309 GLU B O   1 
ATOM   2334 C  CB  . GLU B 2 309 ? 76.636  62.333  74.719 1.00 369.78 ? 309 GLU B CB  1 
ATOM   2335 C  CG  . GLU B 2 309 ? 77.149  63.542  73.928 1.00 436.58 ? 309 GLU B CG  1 
ATOM   2336 C  CD  . GLU B 2 309 ? 78.224  63.309  72.864 1.00 552.08 ? 309 GLU B CD  1 
ATOM   2337 O  OE1 . GLU B 2 309 ? 79.178  62.541  73.118 1.00 596.89 ? 309 GLU B OE1 1 
ATOM   2338 O  OE2 . GLU B 2 309 ? 78.129  63.922  71.774 1.00 631.01 ? 309 GLU B OE2 1 
ATOM   2339 N  N   . ALA B 2 310 ? 75.777  60.178  72.469 1.00 311.66 ? 310 ALA B N   1 
ATOM   2340 C  CA  . ALA B 2 310 ? 75.978  59.663  71.121 1.00 267.25 ? 310 ALA B CA  1 
ATOM   2341 C  C   . ALA B 2 310 ? 75.841  58.141  71.144 1.00 168.38 ? 310 ALA B C   1 
ATOM   2342 O  O   . ALA B 2 310 ? 76.812  57.406  71.371 1.00 137.74 ? 310 ALA B O   1 
ATOM   2343 C  CB  . ALA B 2 310 ? 77.339  60.097  70.658 1.00 335.47 ? 310 ALA B CB  1 
ATOM   2344 N  N   . VAL B 2 311 ? 74.618  57.655  70.921 1.00 158.37 ? 311 VAL B N   1 
ATOM   2345 C  CA  . VAL B 2 311 ? 74.228  56.307  71.328 1.00 192.06 ? 311 VAL B CA  1 
ATOM   2346 C  C   . VAL B 2 311 ? 75.128  55.257  70.674 1.00 139.81 ? 311 VAL B C   1 
ATOM   2347 O  O   . VAL B 2 311 ? 75.487  54.260  71.310 1.00 150.90 ? 311 VAL B O   1 
ATOM   2348 C  CB  . VAL B 2 311 ? 72.722  56.043  71.070 1.00 200.93 ? 311 VAL B CB  1 
ATOM   2349 C  CG1 . VAL B 2 311 ? 71.821  57.070  71.745 1.00 203.39 ? 311 VAL B CG1 1 
ATOM   2350 C  CG2 . VAL B 2 311 ? 72.371  55.965  69.611 1.00 167.14 ? 311 VAL B CG2 1 
ATOM   2351 N  N   . ALA B 2 312 ? 75.494  55.490  69.409 1.00 150.81 ? 312 ALA B N   1 
ATOM   2352 C  CA  . ALA B 2 312 ? 76.319  54.572  68.645 1.00 185.64 ? 312 ALA B CA  1 
ATOM   2353 C  C   . ALA B 2 312 ? 77.738  54.453  69.214 1.00 155.27 ? 312 ALA B C   1 
ATOM   2354 O  O   . ALA B 2 312 ? 78.344  53.389  69.092 1.00 226.31 ? 312 ALA B O   1 
ATOM   2355 C  CB  . ALA B 2 312 ? 76.314  55.000  67.205 1.00 178.07 ? 312 ALA B CB  1 
ATOM   2356 N  N   . VAL B 2 313 ? 78.277  55.497  69.847 1.00 107.52 ? 313 VAL B N   1 
ATOM   2357 C  CA  . VAL B 2 313 ? 79.619  55.444  70.404 1.00 150.96 ? 313 VAL B CA  1 
ATOM   2358 C  C   . VAL B 2 313 ? 79.609  54.570  71.660 1.00 191.96 ? 313 VAL B C   1 
ATOM   2359 O  O   . VAL B 2 313 ? 80.520  53.750  71.835 1.00 161.38 ? 313 VAL B O   1 
ATOM   2360 C  CB  . VAL B 2 313 ? 80.157  56.863  70.672 1.00 196.55 ? 313 VAL B CB  1 
ATOM   2361 C  CG1 . VAL B 2 313 ? 81.473  56.907  71.450 1.00 159.32 ? 313 VAL B CG1 1 
ATOM   2362 C  CG2 . VAL B 2 313 ? 80.278  57.625  69.357 1.00 244.74 ? 313 VAL B CG2 1 
ATOM   2363 N  N   . ASP B 2 314 ? 78.599  54.728  72.530 1.00 190.74 ? 314 ASP B N   1 
ATOM   2364 C  CA  . ASP B 2 314 ? 78.463  53.887  73.717 1.00 242.76 ? 314 ASP B CA  1 
ATOM   2365 C  C   . ASP B 2 314 ? 78.210  52.423  73.353 1.00 187.20 ? 314 ASP B C   1 
ATOM   2366 O  O   . ASP B 2 314 ? 78.785  51.527  73.982 1.00 182.82 ? 314 ASP B O   1 
ATOM   2367 C  CB  . ASP B 2 314 ? 77.396  54.468  74.652 1.00 304.08 ? 314 ASP B CB  1 
ATOM   2368 C  CG  . ASP B 2 314 ? 77.810  55.811  75.232 1.00 399.78 ? 314 ASP B CG  1 
ATOM   2369 O  OD1 . ASP B 2 314 ? 78.983  55.938  75.623 1.00 460.31 ? 314 ASP B OD1 1 
ATOM   2370 O  OD2 . ASP B 2 314 ? 76.970  56.722  75.294 1.00 432.85 ? 314 ASP B OD2 1 
ATOM   2371 N  N   . PHE B 2 315 ? 77.361  52.176  72.353 1.00 155.16 ? 315 PHE B N   1 
ATOM   2372 C  CA  . PHE B 2 315 ? 77.214  50.854  71.745 1.00 176.88 ? 315 PHE B CA  1 
ATOM   2373 C  C   . PHE B 2 315 ? 78.568  50.292  71.266 1.00 156.20 ? 315 PHE B C   1 
ATOM   2374 O  O   . PHE B 2 315 ? 78.882  49.131  71.501 1.00 214.37 ? 315 PHE B O   1 
ATOM   2375 C  CB  . PHE B 2 315 ? 76.167  50.948  70.629 1.00 177.29 ? 315 PHE B CB  1 
ATOM   2376 C  CG  . PHE B 2 315 ? 75.914  49.681  69.851 1.00 163.29 ? 315 PHE B CG  1 
ATOM   2377 C  CD1 . PHE B 2 315 ? 76.791  49.248  68.852 1.00 199.43 ? 315 PHE B CD1 1 
ATOM   2378 C  CD2 . PHE B 2 315 ? 74.788  48.908  70.125 1.00 183.92 ? 315 PHE B CD2 1 
ATOM   2379 C  CE1 . PHE B 2 315 ? 76.525  48.077  68.146 1.00 281.75 ? 315 PHE B CE1 1 
ATOM   2380 C  CE2 . PHE B 2 315 ? 74.532  47.730  69.429 1.00 195.14 ? 315 PHE B CE2 1 
ATOM   2381 C  CZ  . PHE B 2 315 ? 75.397  47.316  68.439 1.00 232.57 ? 315 PHE B CZ  1 
ATOM   2382 N  N   . GLY B 2 316 ? 79.379  51.111  70.604 1.00 150.57 ? 316 GLY B N   1 
ATOM   2383 C  CA  . GLY B 2 316 ? 80.725  50.737  70.210 1.00 235.74 ? 316 GLY B CA  1 
ATOM   2384 C  C   . GLY B 2 316 ? 81.639  50.380  71.381 1.00 233.10 ? 316 GLY B C   1 
ATOM   2385 O  O   . GLY B 2 316 ? 82.337  49.376  71.328 1.00 229.96 ? 316 GLY B O   1 
ATOM   2386 N  N   . ASN B 2 317 ? 81.628  51.190  72.443 1.00 187.71 ? 317 ASN B N   1 
ATOM   2387 C  CA  . ASN B 2 317 ? 82.386  50.906  73.655 1.00 258.44 ? 317 ASN B CA  1 
ATOM   2388 C  C   . ASN B 2 317 ? 81.939  49.608  74.348 1.00 249.57 ? 317 ASN B C   1 
ATOM   2389 O  O   . ASN B 2 317 ? 82.779  48.898  74.910 1.00 250.62 ? 317 ASN B O   1 
ATOM   2390 C  CB  . ASN B 2 317 ? 82.297  52.090  74.622 1.00 280.94 ? 317 ASN B CB  1 
ATOM   2391 C  CG  . ASN B 2 317 ? 83.035  53.334  74.161 1.00 291.65 ? 317 ASN B CG  1 
ATOM   2392 O  OD1 . ASN B 2 317 ? 83.795  53.326  73.194 1.00 202.96 ? 317 ASN B OD1 1 
ATOM   2393 N  ND2 . ASN B 2 317 ? 82.820  54.432  74.866 1.00 346.48 ? 317 ASN B ND2 1 
ATOM   2394 N  N   . TYR B 2 318 ? 80.631  49.299  74.319 1.00 198.68 ? 318 TYR B N   1 
ATOM   2395 C  CA  . TYR B 2 318 ? 80.089  48.116  74.976 1.00 181.11 ? 318 TYR B CA  1 
ATOM   2396 C  C   . TYR B 2 318 ? 80.639  46.816  74.378 1.00 220.89 ? 318 TYR B C   1 
ATOM   2397 O  O   . TYR B 2 318 ? 80.958  45.895  75.132 1.00 283.36 ? 318 TYR B O   1 
ATOM   2398 C  CB  . TYR B 2 318 ? 78.563  48.139  74.888 1.00 209.73 ? 318 TYR B CB  1 
ATOM   2399 C  CG  . TYR B 2 318 ? 77.893  47.043  75.702 1.00 264.87 ? 318 TYR B CG  1 
ATOM   2400 C  CD1 . TYR B 2 318 ? 77.763  45.747  75.212 1.00 245.32 ? 318 TYR B CD1 1 
ATOM   2401 C  CD2 . TYR B 2 318 ? 77.404  47.305  76.981 1.00 385.68 ? 318 TYR B CD2 1 
ATOM   2402 C  CE1 . TYR B 2 318 ? 77.153  44.749  75.964 1.00 330.82 ? 318 TYR B CE1 1 
ATOM   2403 C  CE2 . TYR B 2 318 ? 76.789  46.315  77.739 1.00 406.10 ? 318 TYR B CE2 1 
ATOM   2404 C  CZ  . TYR B 2 318 ? 76.662  45.030  77.232 1.00 375.57 ? 318 TYR B CZ  1 
ATOM   2405 O  OH  . TYR B 2 318 ? 76.057  44.066  77.997 1.00 356.90 ? 318 TYR B OH  1 
ATOM   2406 N  N   . HIS B 2 319 ? 80.754  46.731  73.041 1.00 206.44 ? 319 HIS B N   1 
ATOM   2407 C  CA  . HIS B 2 319 ? 81.187  45.513  72.360 1.00 223.26 ? 319 HIS B CA  1 
ATOM   2408 C  C   . HIS B 2 319 ? 82.672  45.492  71.982 1.00 248.67 ? 319 HIS B C   1 
ATOM   2409 O  O   . HIS B 2 319 ? 83.337  44.465  72.174 1.00 249.21 ? 319 HIS B O   1 
ATOM   2410 C  CB  . HIS B 2 319 ? 80.356  45.312  71.100 1.00 198.79 ? 319 HIS B CB  1 
ATOM   2411 C  CG  . HIS B 2 319 ? 78.935  44.978  71.399 1.00 248.31 ? 319 HIS B CG  1 
ATOM   2412 N  ND1 . HIS B 2 319 ? 78.505  43.812  71.999 1.00 245.44 ? 319 HIS B ND1 1 
ATOM   2413 C  CD2 . HIS B 2 319 ? 77.838  45.705  71.146 1.00 237.42 ? 319 HIS B CD2 1 
ATOM   2414 C  CE1 . HIS B 2 319 ? 77.186  43.852  72.100 1.00 239.13 ? 319 HIS B CE1 1 
ATOM   2415 N  NE2 . HIS B 2 319 ? 76.756  44.995  71.587 1.00 200.06 ? 319 HIS B NE2 1 
ATOM   2416 N  N   . LEU B 2 320 ? 83.188  46.610  71.442 1.00 222.46 ? 320 LEU B N   1 
ATOM   2417 C  CA  . LEU B 2 320 ? 84.449  46.604  70.702 1.00 275.45 ? 320 LEU B CA  1 
ATOM   2418 C  C   . LEU B 2 320 ? 85.614  47.148  71.541 1.00 251.37 ? 320 LEU B C   1 
ATOM   2419 O  O   . LEU B 2 320 ? 86.362  47.987  71.060 1.00 194.60 ? 320 LEU B O   1 
ATOM   2420 C  CB  . LEU B 2 320 ? 84.241  47.412  69.408 1.00 253.63 ? 320 LEU B CB  1 
ATOM   2421 C  CG  . LEU B 2 320 ? 83.070  46.979  68.515 1.00 241.36 ? 320 LEU B CG  1 
ATOM   2422 C  CD1 . LEU B 2 320 ? 82.969  47.877  67.301 1.00 303.89 ? 320 LEU B CD1 1 
ATOM   2423 C  CD2 . LEU B 2 320 ? 83.204  45.542  68.067 1.00 260.02 ? 320 LEU B CD2 1 
ATOM   2424 N  N   . GLY B 2 321 ? 85.806  46.654  72.775 1.00 265.14 ? 321 GLY B N   1 
ATOM   2425 C  CA  . GLY B 2 321 ? 86.663  47.291  73.779 1.00 285.44 ? 321 GLY B CA  1 
ATOM   2426 C  C   . GLY B 2 321 ? 88.111  47.605  73.354 1.00 261.84 ? 321 GLY B C   1 
ATOM   2427 O  O   . GLY B 2 321 ? 88.699  48.596  73.805 1.00 145.15 ? 321 GLY B O   1 
ATOM   2428 N  N   . VAL B 2 322 ? 88.704  46.773  72.483 1.00 272.53 ? 322 VAL B N   1 
ATOM   2429 C  CA  . VAL B 2 322 ? 90.086  46.945  72.030 1.00 292.71 ? 322 VAL B CA  1 
ATOM   2430 C  C   . VAL B 2 322 ? 90.163  48.027  70.946 1.00 220.28 ? 322 VAL B C   1 
ATOM   2431 O  O   . VAL B 2 322 ? 91.189  48.727  70.855 1.00 186.27 ? 322 VAL B O   1 
ATOM   2432 C  CB  . VAL B 2 322 ? 90.671  45.602  71.522 1.00 417.53 ? 322 VAL B CB  1 
ATOM   2433 C  CG1 . VAL B 2 322 ? 92.116  45.725  71.037 1.00 435.13 ? 322 VAL B CG1 1 
ATOM   2434 C  CG2 . VAL B 2 322 ? 90.569  44.493  72.565 1.00 448.64 ? 322 VAL B CG2 1 
ATOM   2435 N  N   . MET B 2 323 ? 89.086  48.131  70.121 1.00 211.09 ? 323 MET B N   1 
ATOM   2436 C  CA  . MET B 2 323 ? 89.055  48.962  68.916 1.00 232.45 ? 323 MET B CA  1 
ATOM   2437 C  C   . MET B 2 323 ? 87.813  49.867  68.879 1.00 238.33 ? 323 MET B C   1 
ATOM   2438 O  O   . MET B 2 323 ? 87.210  50.078  67.834 1.00 266.32 ? 323 MET B O   1 
ATOM   2439 C  CB  . MET B 2 323 ? 89.113  48.063  67.673 1.00 230.32 ? 323 MET B CB  1 
ATOM   2440 C  CG  . MET B 2 323 ? 90.461  47.402  67.469 1.00 308.14 ? 323 MET B CG  1 
ATOM   2441 S  SD  . MET B 2 323 ? 91.765  48.578  66.990 1.00 449.47 ? 323 MET B SD  1 
ATOM   2442 C  CE  . MET B 2 323 ? 93.146  47.475  66.689 1.00 364.29 ? 323 MET B CE  1 
ATOM   2443 N  N   . SER B 2 324 ? 87.427  50.442  70.025 1.00 278.39 ? 324 SER B N   1 
ATOM   2444 C  CA  . SER B 2 324 ? 86.129  51.095  70.176 1.00 242.48 ? 324 SER B CA  1 
ATOM   2445 C  C   . SER B 2 324 ? 86.029  52.353  69.328 1.00 214.53 ? 324 SER B C   1 
ATOM   2446 O  O   . SER B 2 324 ? 84.924  52.871  69.165 1.00 227.13 ? 324 SER B O   1 
ATOM   2447 C  CB  . SER B 2 324 ? 85.852  51.426  71.628 1.00 284.29 ? 324 SER B CB  1 
ATOM   2448 O  OG  . SER B 2 324 ? 86.249  50.363  72.475 1.00 351.75 ? 324 SER B OG  1 
ATOM   2449 N  N   . TRP B 2 325 ? 87.177  52.843  68.828 1.00 204.27 ? 325 TRP B N   1 
ATOM   2450 C  CA  . TRP B 2 325 ? 87.240  54.010  67.959 1.00 258.33 ? 325 TRP B CA  1 
ATOM   2451 C  C   . TRP B 2 325 ? 86.634  53.760  66.573 1.00 183.85 ? 325 TRP B C   1 
ATOM   2452 O  O   . TRP B 2 325 ? 86.355  54.747  65.855 1.00 103.63 ? 325 TRP B O   1 
ATOM   2453 C  CB  . TRP B 2 325 ? 88.693  54.503  67.871 1.00 291.21 ? 325 TRP B CB  1 
ATOM   2454 C  CG  . TRP B 2 325 ? 89.685  53.492  67.357 1.00 219.84 ? 325 TRP B CG  1 
ATOM   2455 C  CD1 . TRP B 2 325 ? 90.513  52.757  68.141 1.00 250.97 ? 325 TRP B CD1 1 
ATOM   2456 C  CD2 . TRP B 2 325 ? 89.979  53.124  65.986 1.00 170.33 ? 325 TRP B CD2 1 
ATOM   2457 N  NE1 . TRP B 2 325 ? 91.292  51.951  67.360 1.00 286.26 ? 325 TRP B NE1 1 
ATOM   2458 C  CE2 . TRP B 2 325 ? 90.993  52.150  66.035 1.00 250.64 ? 325 TRP B CE2 1 
ATOM   2459 C  CE3 . TRP B 2 325 ? 89.490  53.519  64.734 1.00 219.40 ? 325 TRP B CE3 1 
ATOM   2460 C  CZ2 . TRP B 2 325 ? 91.524  51.566  64.877 1.00 349.18 ? 325 TRP B CZ2 1 
ATOM   2461 C  CZ3 . TRP B 2 325 ? 90.011  52.944  63.591 1.00 315.18 ? 325 TRP B CZ3 1 
ATOM   2462 C  CH2 . TRP B 2 325 ? 91.018  51.981  63.662 1.00 353.06 ? 325 TRP B CH2 1 
ATOM   2463 N  N   . ILE B 2 326 ? 86.410  52.489  66.204 1.00 157.83 ? 326 ILE B N   1 
ATOM   2464 C  CA  . ILE B 2 326 ? 85.824  52.143  64.916 1.00 195.09 ? 326 ILE B CA  1 
ATOM   2465 C  C   . ILE B 2 326 ? 84.524  52.911  64.651 1.00 164.15 ? 326 ILE B C   1 
ATOM   2466 O  O   . ILE B 2 326 ? 84.451  53.585  63.586 1.00 136.10 ? 326 ILE B O   1 
ATOM   2467 C  CB  . ILE B 2 326 ? 85.655  50.616  64.795 1.00 223.17 ? 326 ILE B CB  1 
ATOM   2468 C  CG1 . ILE B 2 326 ? 87.025  49.922  64.641 1.00 298.04 ? 326 ILE B CG1 1 
ATOM   2469 C  CG2 . ILE B 2 326 ? 84.688  50.207  63.680 1.00 176.27 ? 326 ILE B CG2 1 
ATOM   2470 C  CD1 . ILE B 2 326 ? 87.711  50.029  63.285 1.00 262.97 ? 326 ILE B CD1 1 
ATOM   2471 N  N   . ILE B 2 327 ? 83.531  52.802  65.569 1.00 104.90 ? 327 ILE B N   1 
ATOM   2472 C  CA  . ILE B 2 327 ? 82.265  53.488  65.325 1.00 150.52 ? 327 ILE B CA  1 
ATOM   2473 C  C   . ILE B 2 327 ? 82.415  55.023  65.318 1.00 165.06 ? 327 ILE B C   1 
ATOM   2474 O  O   . ILE B 2 327 ? 81.927  55.644  64.375 1.00 203.45 ? 327 ILE B O   1 
ATOM   2475 C  CB  . ILE B 2 327 ? 81.138  53.001  66.262 1.00 166.28 ? 327 ILE B CB  1 
ATOM   2476 C  CG1 . ILE B 2 327 ? 80.854  51.507  66.094 1.00 180.90 ? 327 ILE B CG1 1 
ATOM   2477 C  CG2 . ILE B 2 327 ? 79.869  53.823  66.081 1.00 126.00 ? 327 ILE B CG2 1 
ATOM   2478 C  CD1 . ILE B 2 327 ? 80.402  51.074  64.719 1.00 201.29 ? 327 ILE B CD1 1 
ATOM   2479 N  N   . PRO B 2 328 ? 83.057  55.697  66.304 1.00 136.27 ? 328 PRO B N   1 
ATOM   2480 C  CA  . PRO B 2 328 ? 83.364  57.128  66.209 1.00 163.54 ? 328 PRO B CA  1 
ATOM   2481 C  C   . PRO B 2 328 ? 83.929  57.575  64.859 1.00 179.52 ? 328 PRO B C   1 
ATOM   2482 O  O   . PRO B 2 328 ? 83.424  58.543  64.290 1.00 147.15 ? 328 PRO B O   1 
ATOM   2483 C  CB  . PRO B 2 328 ? 84.401  57.355  67.318 1.00 202.28 ? 328 PRO B CB  1 
ATOM   2484 C  CG  . PRO B 2 328 ? 83.981  56.343  68.368 1.00 220.12 ? 328 PRO B CG  1 
ATOM   2485 C  CD  . PRO B 2 328 ? 83.502  55.146  67.573 1.00 140.23 ? 328 PRO B CD  1 
ATOM   2486 N  N   . VAL B 2 329 ? 84.942  56.865  64.327 1.00 165.97 ? 329 VAL B N   1 
ATOM   2487 C  CA  . VAL B 2 329 ? 85.490  57.212  63.018 1.00 159.58 ? 329 VAL B CA  1 
ATOM   2488 C  C   . VAL B 2 329 ? 84.477  56.945  61.888 1.00 192.47 ? 329 VAL B C   1 
ATOM   2489 O  O   . VAL B 2 329 ? 84.364  57.750  60.978 1.00 186.25 ? 329 VAL B O   1 
ATOM   2490 C  CB  . VAL B 2 329 ? 86.813  56.495  62.776 1.00 167.68 ? 329 VAL B CB  1 
ATOM   2491 C  CG1 . VAL B 2 329 ? 87.321  56.614  61.350 1.00 224.41 ? 329 VAL B CG1 1 
ATOM   2492 C  CG2 . VAL B 2 329 ? 87.855  57.031  63.726 1.00 208.21 ? 329 VAL B CG2 1 
ATOM   2493 N  N   . PHE B 2 330 ? 83.717  55.855  61.919 1.00 181.88 ? 330 PHE B N   1 
ATOM   2494 C  CA  . PHE B 2 330 ? 82.680  55.648  60.917 1.00 200.88 ? 330 PHE B CA  1 
ATOM   2495 C  C   . PHE B 2 330 ? 81.553  56.696  60.938 1.00 148.93 ? 330 PHE B C   1 
ATOM   2496 O  O   . PHE B 2 330 ? 81.086  57.097  59.882 1.00 170.50 ? 330 PHE B O   1 
ATOM   2497 C  CB  . PHE B 2 330 ? 82.112  54.242  61.103 1.00 253.58 ? 330 PHE B CB  1 
ATOM   2498 C  CG  . PHE B 2 330 ? 82.837  53.102  60.421 1.00 242.54 ? 330 PHE B CG  1 
ATOM   2499 C  CD1 . PHE B 2 330 ? 83.989  53.252  59.650 1.00 284.18 ? 330 PHE B CD1 1 
ATOM   2500 C  CD2 . PHE B 2 330 ? 82.302  51.832  60.558 1.00 150.58 ? 330 PHE B CD2 1 
ATOM   2501 C  CE1 . PHE B 2 330 ? 84.575  52.149  59.038 1.00 307.49 ? 330 PHE B CE1 1 
ATOM   2502 C  CE2 . PHE B 2 330 ? 82.879  50.731  59.953 1.00 206.80 ? 330 PHE B CE2 1 
ATOM   2503 C  CZ  . PHE B 2 330 ? 84.019  50.892  59.189 1.00 280.50 ? 330 PHE B CZ  1 
ATOM   2504 N  N   . VAL B 2 331 ? 81.101  57.152  62.101 1.00 128.60 ? 331 VAL B N   1 
ATOM   2505 C  CA  . VAL B 2 331 ? 80.179  58.276  62.127 1.00 157.02 ? 331 VAL B CA  1 
ATOM   2506 C  C   . VAL B 2 331 ? 80.855  59.523  61.524 1.00 141.95 ? 331 VAL B C   1 
ATOM   2507 O  O   . VAL B 2 331 ? 80.216  60.333  60.848 1.00 201.20 ? 331 VAL B O   1 
ATOM   2508 C  CB  . VAL B 2 331 ? 79.669  58.579  63.551 1.00 194.17 ? 331 VAL B CB  1 
ATOM   2509 C  CG1 . VAL B 2 331 ? 78.748  59.818  63.619 1.00 143.52 ? 331 VAL B CG1 1 
ATOM   2510 C  CG2 . VAL B 2 331 ? 79.006  57.328  64.101 1.00 154.11 ? 331 VAL B CG2 1 
ATOM   2511 N  N   . GLY B 2 332 ? 82.140  59.715  61.750 1.00 96.35  ? 332 GLY B N   1 
ATOM   2512 C  CA  . GLY B 2 332 ? 82.845  60.793  61.098 1.00 176.02 ? 332 GLY B CA  1 
ATOM   2513 C  C   . GLY B 2 332 ? 82.834  60.655  59.590 1.00 146.43 ? 332 GLY B C   1 
ATOM   2514 O  O   . GLY B 2 332 ? 82.409  61.581  58.926 1.00 165.77 ? 332 GLY B O   1 
ATOM   2515 N  N   . LEU B 2 333 ? 83.287  59.512  59.053 1.00 133.42 ? 333 LEU B N   1 
ATOM   2516 C  CA  . LEU B 2 333 ? 83.359  59.312  57.619 1.00 152.00 ? 333 LEU B CA  1 
ATOM   2517 C  C   . LEU B 2 333 ? 81.973  59.336  56.975 1.00 176.54 ? 333 LEU B C   1 
ATOM   2518 O  O   . LEU B 2 333 ? 81.842  59.759  55.813 1.00 151.57 ? 333 LEU B O   1 
ATOM   2519 C  CB  . LEU B 2 333 ? 84.097  57.997  57.385 1.00 146.08 ? 333 LEU B CB  1 
ATOM   2520 C  CG  . LEU B 2 333 ? 85.580  58.114  57.704 1.00 247.55 ? 333 LEU B CG  1 
ATOM   2521 C  CD1 . LEU B 2 333 ? 86.255  56.764  57.504 1.00 370.96 ? 333 LEU B CD1 1 
ATOM   2522 C  CD2 . LEU B 2 333 ? 86.246  59.231  56.859 1.00 234.83 ? 333 LEU B CD2 1 
ATOM   2523 N  N   . SER B 2 334 ? 80.945  58.885  57.708 1.00 157.23 ? 334 SER B N   1 
ATOM   2524 C  CA  . SER B 2 334 ? 79.577  59.029  57.251 1.00 151.22 ? 334 SER B CA  1 
ATOM   2525 C  C   . SER B 2 334 ? 79.305  60.487  56.898 1.00 109.27 ? 334 SER B C   1 
ATOM   2526 O  O   . SER B 2 334 ? 78.801  60.796  55.839 1.00 140.37 ? 334 SER B O   1 
ATOM   2527 C  CB  . SER B 2 334 ? 78.619  58.517  58.294 1.00 200.23 ? 334 SER B CB  1 
ATOM   2528 O  OG  . SER B 2 334 ? 77.291  58.739  57.895 1.00 196.83 ? 334 SER B OG  1 
ATOM   2529 N  N   . CYS B 2 335 ? 79.607  61.402  57.806 1.00 125.43 ? 335 CYS B N   1 
ATOM   2530 C  CA  . CYS B 2 335 ? 79.330  62.814  57.634 1.00 175.25 ? 335 CYS B CA  1 
ATOM   2531 C  C   . CYS B 2 335 ? 80.115  63.397  56.462 1.00 144.47 ? 335 CYS B C   1 
ATOM   2532 O  O   . CYS B 2 335 ? 79.586  64.214  55.720 1.00 109.91 ? 335 CYS B O   1 
ATOM   2533 C  CB  . CYS B 2 335 ? 79.629  63.545  58.934 1.00 231.84 ? 335 CYS B CB  1 
ATOM   2534 S  SG  . CYS B 2 335 ? 78.514  62.940  60.212 1.00 198.03 ? 335 CYS B SG  1 
ATOM   2535 N  N   . PHE B 2 336 ? 81.353  62.971  56.253 1.00 162.14 ? 336 PHE B N   1 
ATOM   2536 C  CA  . PHE B 2 336 ? 82.147  63.478  55.148 1.00 176.19 ? 336 PHE B CA  1 
ATOM   2537 C  C   . PHE B 2 336 ? 81.444  63.274  53.806 1.00 124.24 ? 336 PHE B C   1 
ATOM   2538 O  O   . PHE B 2 336 ? 81.431  64.160  52.958 1.00 111.95 ? 336 PHE B O   1 
ATOM   2539 C  CB  . PHE B 2 336 ? 83.515  62.796  55.168 1.00 210.64 ? 336 PHE B CB  1 
ATOM   2540 C  CG  . PHE B 2 336 ? 84.531  63.458  54.285 1.00 175.73 ? 336 PHE B CG  1 
ATOM   2541 C  CD1 . PHE B 2 336 ? 85.152  64.657  54.667 1.00 153.55 ? 336 PHE B CD1 1 
ATOM   2542 C  CD2 . PHE B 2 336 ? 84.846  62.882  53.074 1.00 149.26 ? 336 PHE B CD2 1 
ATOM   2543 C  CE1 . PHE B 2 336 ? 86.095  65.254  53.841 1.00 161.94 ? 336 PHE B CE1 1 
ATOM   2544 C  CE2 . PHE B 2 336 ? 85.790  63.484  52.244 1.00 250.76 ? 336 PHE B CE2 1 
ATOM   2545 C  CZ  . PHE B 2 336 ? 86.408  64.663  52.626 1.00 251.71 ? 336 PHE B CZ  1 
ATOM   2546 N  N   . GLY B 2 337 ? 80.817  62.126  53.604 1.00 123.70 ? 337 GLY B N   1 
ATOM   2547 C  CA  . GLY B 2 337 ? 79.989  61.897  52.420 1.00 193.27 ? 337 GLY B CA  1 
ATOM   2548 C  C   . GLY B 2 337 ? 78.680  62.691  52.368 1.00 120.73 ? 337 GLY B C   1 
ATOM   2549 O  O   . GLY B 2 337 ? 78.153  62.990  51.308 1.00 111.34 ? 337 GLY B O   1 
ATOM   2550 N  N   . SER B 2 338 ? 78.134  63.039  53.506 1.00 85.04  ? 338 SER B N   1 
ATOM   2551 C  CA  . SER B 2 338 ? 76.925  63.813  53.529 1.00 109.49 ? 338 SER B CA  1 
ATOM   2552 C  C   . SER B 2 338 ? 77.294  65.208  53.106 1.00 99.53  ? 338 SER B C   1 
ATOM   2553 O  O   . SER B 2 338 ? 76.493  65.861  52.425 1.00 180.37 ? 338 SER B O   1 
ATOM   2554 C  CB  . SER B 2 338 ? 76.222  63.769  54.936 1.00 192.26 ? 338 SER B CB  1 
ATOM   2555 O  OG  . SER B 2 338 ? 75.000  64.547  54.941 1.00 103.25 ? 338 SER B OG  1 
ATOM   2556 N  N   . VAL B 2 339 ? 78.451  65.734  53.557 1.00 70.28  ? 339 VAL B N   1 
ATOM   2557 C  CA  . VAL B 2 339 ? 78.814  67.090  53.181 1.00 96.96  ? 339 VAL B CA  1 
ATOM   2558 C  C   . VAL B 2 339 ? 79.045  67.091  51.686 1.00 117.82 ? 339 VAL B C   1 
ATOM   2559 O  O   . VAL B 2 339 ? 78.517  67.990  51.014 1.00 158.52 ? 339 VAL B O   1 
ATOM   2560 C  CB  . VAL B 2 339 ? 80.037  67.645  53.899 1.00 130.09 ? 339 VAL B CB  1 
ATOM   2561 C  CG1 . VAL B 2 339 ? 80.530  69.011  53.303 1.00 99.05  ? 339 VAL B CG1 1 
ATOM   2562 C  CG2 . VAL B 2 339 ? 79.722  67.722  55.375 1.00 141.04 ? 339 VAL B CG2 1 
ATOM   2563 N  N   . ASN B 2 340 ? 79.816  66.129  51.176 1.00 98.89  ? 340 ASN B N   1 
ATOM   2564 C  CA  . ASN B 2 340 ? 80.124  66.112  49.764 1.00 132.40 ? 340 ASN B CA  1 
ATOM   2565 C  C   . ASN B 2 340 ? 78.816  66.189  48.956 1.00 116.55 ? 340 ASN B C   1 
ATOM   2566 O  O   . ASN B 2 340 ? 78.627  67.033  48.096 1.00 112.05 ? 340 ASN B O   1 
ATOM   2567 C  CB  . ASN B 2 340 ? 80.980  64.887  49.451 1.00 108.20 ? 340 ASN B CB  1 
ATOM   2568 C  CG  . ASN B 2 340 ? 81.253  64.814  47.978 1.00 137.88 ? 340 ASN B CG  1 
ATOM   2569 O  OD1 . ASN B 2 340 ? 81.847  65.759  47.459 1.00 173.63 ? 340 ASN B OD1 1 
ATOM   2570 N  ND2 . ASN B 2 340 ? 80.792  63.758  47.310 1.00 125.85 ? 340 ASN B ND2 1 
ATOM   2571 N  N   . GLY B 2 341 ? 77.897  65.281  49.186 1.00 93.17  ? 341 GLY B N   1 
ATOM   2572 C  CA  . GLY B 2 341 ? 76.666  65.270  48.447 1.00 113.90 ? 341 GLY B CA  1 
ATOM   2573 C  C   . GLY B 2 341 ? 75.875  66.550  48.617 1.00 113.38 ? 341 GLY B C   1 
ATOM   2574 O  O   . GLY B 2 341 ? 75.258  66.991  47.647 1.00 226.76 ? 341 GLY B O   1 
ATOM   2575 N  N   . SER B 2 342 ? 75.839  67.139  49.823 1.00 133.51 ? 342 SER B N   1 
ATOM   2576 C  CA  . SER B 2 342 ? 75.055  68.348  50.093 1.00 157.62 ? 342 SER B CA  1 
ATOM   2577 C  C   . SER B 2 342 ? 75.650  69.521  49.349 1.00 124.45 ? 342 SER B C   1 
ATOM   2578 O  O   . SER B 2 342 ? 74.886  70.403  48.950 1.00 160.24 ? 342 SER B O   1 
ATOM   2579 C  CB  . SER B 2 342 ? 74.957  68.680  51.575 1.00 190.73 ? 342 SER B CB  1 
ATOM   2580 O  OG  . SER B 2 342 ? 74.374  67.636  52.328 1.00 200.99 ? 342 SER B OG  1 
ATOM   2581 N  N   . LEU B 2 343 ? 76.989  69.521  49.180 1.00 105.61 ? 343 LEU B N   1 
ATOM   2582 C  CA  . LEU B 2 343 ? 77.752  70.568  48.496 1.00 133.81 ? 343 LEU B CA  1 
ATOM   2583 C  C   . LEU B 2 343 ? 77.608  70.425  46.982 1.00 144.19 ? 343 LEU B C   1 
ATOM   2584 O  O   . LEU B 2 343 ? 77.342  71.403  46.287 1.00 141.34 ? 343 LEU B O   1 
ATOM   2585 C  CB  . LEU B 2 343 ? 79.200  70.425  48.978 1.00 143.11 ? 343 LEU B CB  1 
ATOM   2586 C  CG  . LEU B 2 343 ? 80.242  71.404  48.480 1.00 156.83 ? 343 LEU B CG  1 
ATOM   2587 C  CD1 . LEU B 2 343 ? 81.419  71.392  49.418 1.00 231.67 ? 343 LEU B CD1 1 
ATOM   2588 C  CD2 . LEU B 2 343 ? 80.738  71.078  47.083 1.00 211.69 ? 343 LEU B CD2 1 
ATOM   2589 N  N   . PHE B 2 344 ? 77.807  69.223  46.448 1.00 121.07 ? 344 PHE B N   1 
ATOM   2590 C  CA  . PHE B 2 344 ? 77.582  68.936  45.042 1.00 124.24 ? 344 PHE B CA  1 
ATOM   2591 C  C   . PHE B 2 344 ? 76.194  69.373  44.630 1.00 106.87 ? 344 PHE B C   1 
ATOM   2592 O  O   . PHE B 2 344 ? 76.025  70.133  43.696 1.00 96.56  ? 344 PHE B O   1 
ATOM   2593 C  CB  . PHE B 2 344 ? 77.751  67.435  44.814 1.00 184.48 ? 344 PHE B CB  1 
ATOM   2594 C  CG  . PHE B 2 344 ? 77.494  66.967  43.409 1.00 188.72 ? 344 PHE B CG  1 
ATOM   2595 C  CD1 . PHE B 2 344 ? 78.408  67.192  42.397 1.00 209.36 ? 344 PHE B CD1 1 
ATOM   2596 C  CD2 . PHE B 2 344 ? 76.341  66.308  43.103 1.00 156.34 ? 344 PHE B CD2 1 
ATOM   2597 C  CE1 . PHE B 2 344 ? 78.184  66.748  41.110 1.00 183.88 ? 344 PHE B CE1 1 
ATOM   2598 C  CE2 . PHE B 2 344 ? 76.100  65.879  41.818 1.00 223.71 ? 344 PHE B CE2 1 
ATOM   2599 C  CZ  . PHE B 2 344 ? 77.020  66.091  40.827 1.00 229.41 ? 344 PHE B CZ  1 
ATOM   2600 N  N   . THR B 2 345 ? 75.198  68.907  45.376 1.00 136.16 ? 345 THR B N   1 
ATOM   2601 C  CA  . THR B 2 345 ? 73.795  69.195  45.111 1.00 144.20 ? 345 THR B CA  1 
ATOM   2602 C  C   . THR B 2 345 ? 73.415  70.670  45.307 1.00 104.78 ? 345 THR B C   1 
ATOM   2603 O  O   . THR B 2 345 ? 72.684  71.216  44.495 1.00 109.63 ? 345 THR B O   1 
ATOM   2604 C  CB  . THR B 2 345 ? 72.924  68.312  45.982 1.00 159.44 ? 345 THR B CB  1 
ATOM   2605 O  OG1 . THR B 2 345 ? 73.277  66.953  45.776 1.00 101.96 ? 345 THR B OG1 1 
ATOM   2606 C  CG2 . THR B 2 345 ? 71.483  68.375  45.603 1.00 190.87 ? 345 THR B CG2 1 
ATOM   2607 N  N   . SER B 2 346 ? 73.919  71.333  46.324 1.00 99.74  ? 346 SER B N   1 
ATOM   2608 C  CA  . SER B 2 346 ? 73.690  72.761  46.471 1.00 171.44 ? 346 SER B CA  1 
ATOM   2609 C  C   . SER B 2 346 ? 74.246  73.580  45.316 1.00 122.46 ? 346 SER B C   1 
ATOM   2610 O  O   . SER B 2 346 ? 73.627  74.543  44.892 1.00 124.19 ? 346 SER B O   1 
ATOM   2611 C  CB  . SER B 2 346 ? 74.245  73.307  47.776 1.00 269.29 ? 346 SER B CB  1 
ATOM   2612 O  OG  . SER B 2 346 ? 75.655  73.295  47.833 1.00 172.00 ? 346 SER B OG  1 
ATOM   2613 N  N   . SER B 2 347 ? 75.407  73.219  44.808 1.00 96.76  ? 347 SER B N   1 
ATOM   2614 C  CA  . SER B 2 347 ? 76.005  73.987  43.724 1.00 135.11 ? 347 SER B CA  1 
ATOM   2615 C  C   . SER B 2 347 ? 75.058  74.118  42.546 1.00 100.08 ? 347 SER B C   1 
ATOM   2616 O  O   . SER B 2 347 ? 75.059  75.163  41.889 1.00 102.76 ? 347 SER B O   1 
ATOM   2617 C  CB  . SER B 2 347 ? 77.334  73.410  43.305 1.00 115.26 ? 347 SER B CB  1 
ATOM   2618 O  OG  . SER B 2 347 ? 77.124  72.201  42.632 1.00 115.99 ? 347 SER B OG  1 
ATOM   2619 N  N   . ARG B 2 348 ? 74.280  73.069  42.288 1.00 101.41 ? 348 ARG B N   1 
ATOM   2620 C  CA  . ARG B 2 348 ? 73.382  73.043  41.145 1.00 149.59 ? 348 ARG B CA  1 
ATOM   2621 C  C   . ARG B 2 348 ? 72.217  73.992  41.386 1.00 134.03 ? 348 ARG B C   1 
ATOM   2622 O  O   . ARG B 2 348 ? 71.789  74.639  40.444 1.00 182.22 ? 348 ARG B O   1 
ATOM   2623 C  CB  . ARG B 2 348 ? 72.925  71.608  40.829 1.00 165.02 ? 348 ARG B CB  1 
ATOM   2624 C  CG  . ARG B 2 348 ? 74.044  70.588  40.584 1.00 113.14 ? 348 ARG B CG  1 
ATOM   2625 C  CD  . ARG B 2 348 ? 75.251  71.117  39.838 1.00 136.62 ? 348 ARG B CD  1 
ATOM   2626 N  NE  . ARG B 2 348 ? 76.105  69.989  39.482 1.00 170.40 ? 348 ARG B NE  1 
ATOM   2627 C  CZ  . ARG B 2 348 ? 77.444  69.929  39.560 1.00 170.49 ? 348 ARG B CZ  1 
ATOM   2628 N  NH1 . ARG B 2 348 ? 78.117  69.094  38.786 1.00 211.08 ? 348 ARG B NH1 1 
ATOM   2629 N  NH2 . ARG B 2 348 ? 78.147  70.683  40.367 1.00 166.66 ? 348 ARG B NH2 1 
ATOM   2630 N  N   . LEU B 2 349 ? 71.700  74.093  42.608 1.00 115.18 ? 349 LEU B N   1 
ATOM   2631 C  CA  . LEU B 2 349 ? 70.614  75.019  42.884 1.00 158.53 ? 349 LEU B CA  1 
ATOM   2632 C  C   . LEU B 2 349 ? 71.007  76.460  42.555 1.00 144.39 ? 349 LEU B C   1 
ATOM   2633 O  O   . LEU B 2 349 ? 70.284  77.121  41.818 1.00 195.98 ? 349 LEU B O   1 
ATOM   2634 C  CB  . LEU B 2 349 ? 70.192  74.898  44.350 1.00 179.92 ? 349 LEU B CB  1 
ATOM   2635 C  CG  . LEU B 2 349 ? 69.180  75.932  44.838 1.00 119.77 ? 349 LEU B CG  1 
ATOM   2636 C  CD1 . LEU B 2 349 ? 67.914  75.796  44.036 1.00 185.98 ? 349 LEU B CD1 1 
ATOM   2637 C  CD2 . LEU B 2 349 ? 68.881  75.698  46.300 1.00 230.69 ? 349 LEU B CD2 1 
ATOM   2638 N  N   . PHE B 2 350 ? 72.121  76.954  43.086 1.00 132.18 ? 350 PHE B N   1 
ATOM   2639 C  CA  . PHE B 2 350 ? 72.544  78.342  42.885 1.00 195.16 ? 350 PHE B CA  1 
ATOM   2640 C  C   . PHE B 2 350 ? 72.865  78.623  41.414 1.00 148.43 ? 350 PHE B C   1 
ATOM   2641 O  O   . PHE B 2 350 ? 72.528  79.692  40.896 1.00 129.66 ? 350 PHE B O   1 
ATOM   2642 C  CB  . PHE B 2 350 ? 73.700  78.684  43.831 1.00 207.48 ? 350 PHE B CB  1 
ATOM   2643 C  CG  . PHE B 2 350 ? 73.479  78.203  45.249 1.00 211.66 ? 350 PHE B CG  1 
ATOM   2644 C  CD1 . PHE B 2 350 ? 72.258  78.412  45.897 1.00 177.57 ? 350 PHE B CD1 1 
ATOM   2645 C  CD2 . PHE B 2 350 ? 74.481  77.518  45.935 1.00 213.51 ? 350 PHE B CD2 1 
ATOM   2646 C  CE1 . PHE B 2 350 ? 72.051  77.960  47.195 1.00 186.81 ? 350 PHE B CE1 1 
ATOM   2647 C  CE2 . PHE B 2 350 ? 74.282  77.060  47.231 1.00 196.99 ? 350 PHE B CE2 1 
ATOM   2648 C  CZ  . PHE B 2 350 ? 73.065  77.278  47.855 1.00 248.81 ? 350 PHE B CZ  1 
ATOM   2649 N  N   . PHE B 2 351 ? 73.480  77.651  40.749 1.00 123.31 ? 351 PHE B N   1 
ATOM   2650 C  CA  . PHE B 2 351 ? 73.637  77.671  39.298 1.00 162.40 ? 351 PHE B CA  1 
ATOM   2651 C  C   . PHE B 2 351 ? 72.299  77.802  38.552 1.00 155.84 ? 351 PHE B C   1 
ATOM   2652 O  O   . PHE B 2 351 ? 72.111  78.761  37.792 1.00 117.41 ? 351 PHE B O   1 
ATOM   2653 C  CB  . PHE B 2 351 ? 74.430  76.426  38.902 1.00 205.46 ? 351 PHE B CB  1 
ATOM   2654 C  CG  . PHE B 2 351 ? 74.435  76.085  37.436 1.00 183.25 ? 351 PHE B CG  1 
ATOM   2655 C  CD1 . PHE B 2 351 ? 75.332  76.717  36.563 1.00 184.84 ? 351 PHE B CD1 1 
ATOM   2656 C  CD2 . PHE B 2 351 ? 73.553  75.122  36.971 1.00 146.86 ? 351 PHE B CD2 1 
ATOM   2657 C  CE1 . PHE B 2 351 ? 75.307  76.396  35.229 1.00 182.92 ? 351 PHE B CE1 1 
ATOM   2658 C  CE2 . PHE B 2 351 ? 73.528  74.802  35.635 1.00 206.08 ? 351 PHE B CE2 1 
ATOM   2659 C  CZ  . PHE B 2 351 ? 74.407  75.442  34.772 1.00 295.35 ? 351 PHE B CZ  1 
ATOM   2660 N  N   . VAL B 2 352 ? 71.359  76.877  38.777 1.00 133.21 ? 352 VAL B N   1 
ATOM   2661 C  CA  . VAL B 2 352 ? 70.058  76.943  38.122 1.00 129.16 ? 352 VAL B CA  1 
ATOM   2662 C  C   . VAL B 2 352 ? 69.348  78.264  38.411 1.00 141.83 ? 352 VAL B C   1 
ATOM   2663 O  O   . VAL B 2 352 ? 68.851  78.866  37.452 1.00 222.18 ? 352 VAL B O   1 
ATOM   2664 C  CB  . VAL B 2 352 ? 69.161  75.751  38.486 1.00 145.02 ? 352 VAL B CB  1 
ATOM   2665 C  CG1 . VAL B 2 352 ? 67.696  75.934  38.095 1.00 163.77 ? 352 VAL B CG1 1 
ATOM   2666 C  CG2 . VAL B 2 352 ? 69.751  74.510  37.846 1.00 151.48 ? 352 VAL B CG2 1 
ATOM   2667 N  N   . GLY B 2 353 ? 69.314  78.715  39.673 1.00 129.79 ? 353 GLY B N   1 
ATOM   2668 C  CA  . GLY B 2 353 ? 68.704  79.994  40.021 1.00 179.68 ? 353 GLY B CA  1 
ATOM   2669 C  C   . GLY B 2 353 ? 69.201  81.145  39.137 1.00 184.88 ? 353 GLY B C   1 
ATOM   2670 O  O   . GLY B 2 353 ? 68.405  81.991  38.733 1.00 183.59 ? 353 GLY B O   1 
ATOM   2671 N  N   . SER B 2 354 ? 70.499  81.152  38.805 1.00 168.71 ? 354 SER B N   1 
ATOM   2672 C  CA  . SER B 2 354 ? 71.080  82.190  37.966 1.00 174.34 ? 354 SER B CA  1 
ATOM   2673 C  C   . SER B 2 354 ? 70.652  82.067  36.510 1.00 155.21 ? 354 SER B C   1 
ATOM   2674 O  O   . SER B 2 354 ? 70.527  83.107  35.854 1.00 192.02 ? 354 SER B O   1 
ATOM   2675 C  CB  . SER B 2 354 ? 72.578  82.219  38.088 1.00 202.56 ? 354 SER B CB  1 
ATOM   2676 O  OG  . SER B 2 354 ? 73.144  81.126  37.393 1.00 160.91 ? 354 SER B OG  1 
ATOM   2677 N  N   . ARG B 2 355 ? 70.428  80.846  35.984 1.00 156.38 ? 355 ARG B N   1 
ATOM   2678 C  CA  . ARG B 2 355 ? 69.938  80.708  34.619 1.00 230.10 ? 355 ARG B CA  1 
ATOM   2679 C  C   . ARG B 2 355 ? 68.578  81.396  34.482 1.00 186.87 ? 355 ARG B C   1 
ATOM   2680 O  O   . ARG B 2 355 ? 68.338  82.149  33.527 1.00 183.54 ? 355 ARG B O   1 
ATOM   2681 C  CB  . ARG B 2 355 ? 69.734  79.256  34.175 1.00 210.72 ? 355 ARG B CB  1 
ATOM   2682 C  CG  . ARG B 2 355 ? 70.936  78.323  34.156 1.00 205.54 ? 355 ARG B CG  1 
ATOM   2683 C  CD  . ARG B 2 355 ? 70.669  77.101  33.243 1.00 229.83 ? 355 ARG B CD  1 
ATOM   2684 N  NE  . ARG B 2 355 ? 69.268  76.609  33.226 1.00 294.89 ? 355 ARG B NE  1 
ATOM   2685 C  CZ  . ARG B 2 355 ? 68.844  75.331  33.236 1.00 347.11 ? 355 ARG B CZ  1 
ATOM   2686 N  NH1 . ARG B 2 355 ? 67.544  75.124  33.361 1.00 344.73 ? 355 ARG B NH1 1 
ATOM   2687 N  NH2 . ARG B 2 355 ? 69.669  74.291  33.138 1.00 290.35 ? 355 ARG B NH2 1 
ATOM   2688 N  N   . GLU B 2 356 ? 67.696  81.119  35.451 1.00 148.53 ? 356 GLU B N   1 
ATOM   2689 C  CA  . GLU B 2 356 ? 66.306  81.551  35.401 1.00 217.38 ? 356 GLU B CA  1 
ATOM   2690 C  C   . GLU B 2 356 ? 66.138  82.992  35.893 1.00 201.52 ? 356 GLU B C   1 
ATOM   2691 O  O   . GLU B 2 356 ? 64.996  83.420  36.087 1.00 226.99 ? 356 GLU B O   1 
ATOM   2692 C  CB  . GLU B 2 356 ? 65.410  80.578  36.184 1.00 263.85 ? 356 GLU B CB  1 
ATOM   2693 C  CG  . GLU B 2 356 ? 65.649  79.075  35.928 1.00 330.89 ? 356 GLU B CG  1 
ATOM   2694 C  CD  . GLU B 2 356 ? 65.880  78.599  34.497 1.00 363.28 ? 356 GLU B CD  1 
ATOM   2695 O  OE1 . GLU B 2 356 ? 65.296  79.208  33.583 1.00 465.43 ? 356 GLU B OE1 1 
ATOM   2696 O  OE2 . GLU B 2 356 ? 66.637  77.609  34.290 1.00 188.45 ? 356 GLU B OE2 1 
ATOM   2697 N  N   . GLY B 2 357 ? 67.246  83.736  36.078 1.00 161.29 ? 357 GLY B N   1 
ATOM   2698 C  CA  . GLY B 2 357 ? 67.220  85.191  36.202 1.00 237.24 ? 357 GLY B CA  1 
ATOM   2699 C  C   . GLY B 2 357 ? 67.151  85.682  37.646 1.00 214.03 ? 357 GLY B C   1 
ATOM   2700 O  O   . GLY B 2 357 ? 67.056  86.888  37.862 1.00 289.87 ? 357 GLY B O   1 
ATOM   2701 N  N   . HIS B 2 358 ? 67.213  84.763  38.620 1.00 176.29 ? 358 HIS B N   1 
ATOM   2702 C  CA  . HIS B 2 358 ? 67.062  85.111  40.023 1.00 179.67 ? 358 HIS B CA  1 
ATOM   2703 C  C   . HIS B 2 358 ? 68.378  85.564  40.676 1.00 164.55 ? 358 HIS B C   1 
ATOM   2704 O  O   . HIS B 2 358 ? 68.300  86.145  41.773 1.00 192.21 ? 358 HIS B O   1 
ATOM   2705 C  CB  . HIS B 2 358 ? 66.425  83.918  40.745 1.00 194.15 ? 358 HIS B CB  1 
ATOM   2706 C  CG  . HIS B 2 358 ? 64.954  83.830  40.552 1.00 211.77 ? 358 HIS B CG  1 
ATOM   2707 N  ND1 . HIS B 2 358 ? 64.295  84.069  39.367 1.00 273.95 ? 358 HIS B ND1 1 
ATOM   2708 C  CD2 . HIS B 2 358 ? 64.001  83.546  41.450 1.00 176.00 ? 358 HIS B CD2 1 
ATOM   2709 C  CE1 . HIS B 2 358 ? 62.994  83.922  39.556 1.00 358.17 ? 358 HIS B CE1 1 
ATOM   2710 N  NE2 . HIS B 2 358 ? 62.789  83.607  40.812 1.00 255.44 ? 358 HIS B NE2 1 
ATOM   2711 N  N   . LEU B 2 359 ? 69.563  85.280  40.076 1.00 121.21 ? 359 LEU B N   1 
ATOM   2712 C  CA  . LEU B 2 359 ? 70.848  85.512  40.731 1.00 174.93 ? 359 LEU B CA  1 
ATOM   2713 C  C   . LEU B 2 359 ? 71.902  86.048  39.767 1.00 203.53 ? 359 LEU B C   1 
ATOM   2714 O  O   . LEU B 2 359 ? 71.767  85.853  38.568 1.00 291.13 ? 359 LEU B O   1 
ATOM   2715 C  CB  . LEU B 2 359 ? 71.347  84.224  41.384 1.00 173.04 ? 359 LEU B CB  1 
ATOM   2716 C  CG  . LEU B 2 359 ? 70.634  83.746  42.643 1.00 228.86 ? 359 LEU B CG  1 
ATOM   2717 C  CD1 . LEU B 2 359 ? 71.200  82.393  43.052 1.00 233.83 ? 359 LEU B CD1 1 
ATOM   2718 C  CD2 . LEU B 2 359 ? 70.774  84.723  43.820 1.00 309.36 ? 359 LEU B CD2 1 
ATOM   2719 N  N   . PRO B 2 360 ? 72.968  86.756  40.252 1.00 190.47 ? 360 PRO B N   1 
ATOM   2720 C  CA  . PRO B 2 360 ? 73.956  87.387  39.363 1.00 204.81 ? 360 PRO B CA  1 
ATOM   2721 C  C   . PRO B 2 360 ? 74.618  86.430  38.379 1.00 195.43 ? 360 PRO B C   1 
ATOM   2722 O  O   . PRO B 2 360 ? 74.929  85.285  38.730 1.00 124.02 ? 360 PRO B O   1 
ATOM   2723 C  CB  . PRO B 2 360 ? 75.000  87.952  40.323 1.00 228.57 ? 360 PRO B CB  1 
ATOM   2724 C  CG  . PRO B 2 360 ? 74.172  88.272  41.554 1.00 294.68 ? 360 PRO B CG  1 
ATOM   2725 C  CD  . PRO B 2 360 ? 73.279  87.051  41.667 1.00 201.79 ? 360 PRO B CD  1 
ATOM   2726 N  N   . SER B 2 361 ? 74.811  86.919  37.144 1.00 213.90 ? 361 SER B N   1 
ATOM   2727 C  CA  . SER B 2 361 ? 75.150  86.062  36.006 1.00 254.81 ? 361 SER B CA  1 
ATOM   2728 C  C   . SER B 2 361 ? 76.609  85.587  36.047 1.00 194.44 ? 361 SER B C   1 
ATOM   2729 O  O   . SER B 2 361 ? 77.114  85.043  35.073 1.00 164.50 ? 361 SER B O   1 
ATOM   2730 C  CB  . SER B 2 361 ? 74.817  86.786  34.712 1.00 294.38 ? 361 SER B CB  1 
ATOM   2731 O  OG  . SER B 2 361 ? 75.546  88.002  34.596 1.00 291.29 ? 361 SER B OG  1 
ATOM   2732 N  N   . ILE B 2 362 ? 77.307  85.788  37.166 1.00 160.34 ? 362 ILE B N   1 
ATOM   2733 C  CA  . ILE B 2 362 ? 78.574  85.113  37.391 1.00 159.99 ? 362 ILE B CA  1 
ATOM   2734 C  C   . ILE B 2 362 ? 78.291  83.631  37.676 1.00 190.01 ? 362 ILE B C   1 
ATOM   2735 O  O   . ILE B 2 362 ? 79.024  82.773  37.226 1.00 159.72 ? 362 ILE B O   1 
ATOM   2736 C  CB  . ILE B 2 362 ? 79.374  85.722  38.561 1.00 177.13 ? 362 ILE B CB  1 
ATOM   2737 C  CG1 . ILE B 2 362 ? 79.283  87.245  38.763 1.00 254.16 ? 362 ILE B CG1 1 
ATOM   2738 C  CG2 . ILE B 2 362 ? 80.813  85.273  38.398 1.00 159.26 ? 362 ILE B CG2 1 
ATOM   2739 C  CD1 . ILE B 2 362 ? 79.610  87.698  40.195 1.00 276.74 ? 362 ILE B CD1 1 
ATOM   2740 N  N   . LEU B 2 363 ? 77.234  83.300  38.418 1.00 209.97 ? 363 LEU B N   1 
ATOM   2741 C  CA  . LEU B 2 363 ? 77.026  81.947  38.940 1.00 189.15 ? 363 LEU B CA  1 
ATOM   2742 C  C   . LEU B 2 363 ? 76.476  80.986  37.885 1.00 236.19 ? 363 LEU B C   1 
ATOM   2743 O  O   . LEU B 2 363 ? 76.470  79.781  38.171 1.00 318.41 ? 363 LEU B O   1 
ATOM   2744 C  CB  . LEU B 2 363 ? 76.062  81.961  40.139 1.00 174.29 ? 363 LEU B CB  1 
ATOM   2745 C  CG  . LEU B 2 363 ? 76.433  82.872  41.308 1.00 226.64 ? 363 LEU B CG  1 
ATOM   2746 C  CD1 . LEU B 2 363 ? 75.401  82.733  42.432 1.00 168.16 ? 363 LEU B CD1 1 
ATOM   2747 C  CD2 . LEU B 2 363 ? 77.865  82.612  41.798 1.00 205.43 ? 363 LEU B CD2 1 
ATOM   2748 N  N   . SER B 2 364 ? 76.033  81.483  36.709 1.00 175.71 ? 364 SER B N   1 
ATOM   2749 C  CA  . SER B 2 364 ? 75.624  80.613  35.604 1.00 255.16 ? 364 SER B CA  1 
ATOM   2750 C  C   . SER B 2 364 ? 76.797  80.041  34.806 1.00 205.09 ? 364 SER B C   1 
ATOM   2751 O  O   . SER B 2 364 ? 76.611  79.161  33.981 1.00 129.25 ? 364 SER B O   1 
ATOM   2752 C  CB  . SER B 2 364 ? 74.710  81.355  34.658 1.00 338.23 ? 364 SER B CB  1 
ATOM   2753 O  OG  . SER B 2 364 ? 75.377  82.440  34.047 1.00 343.06 ? 364 SER B OG  1 
ATOM   2754 N  N   . MET B 2 365 ? 78.001  80.556  35.036 1.00 175.69 ? 365 MET B N   1 
ATOM   2755 C  CA  . MET B 2 365 ? 79.154  80.291  34.211 1.00 179.15 ? 365 MET B CA  1 
ATOM   2756 C  C   . MET B 2 365 ? 79.749  78.928  34.565 1.00 127.54 ? 365 MET B C   1 
ATOM   2757 O  O   . MET B 2 365 ? 79.653  78.443  35.714 1.00 174.69 ? 365 MET B O   1 
ATOM   2758 C  CB  . MET B 2 365 ? 80.197  81.400  34.432 1.00 192.19 ? 365 MET B CB  1 
ATOM   2759 C  CG  . MET B 2 365 ? 79.666  82.774  34.087 1.00 205.89 ? 365 MET B CG  1 
ATOM   2760 S  SD  . MET B 2 365 ? 79.761  83.203  32.373 1.00 225.36 ? 365 MET B SD  1 
ATOM   2761 C  CE  . MET B 2 365 ? 78.858  84.752  32.395 1.00 379.42 ? 365 MET B CE  1 
ATOM   2762 N  N   . ILE B 2 366 ? 80.410  78.341  33.557 1.00 92.32  ? 366 ILE B N   1 
ATOM   2763 C  CA  . ILE B 2 366 ? 81.079  77.061  33.653 1.00 114.76 ? 366 ILE B CA  1 
ATOM   2764 C  C   . ILE B 2 366 ? 82.537  77.211  33.222 1.00 113.41 ? 366 ILE B C   1 
ATOM   2765 O  O   . ILE B 2 366 ? 82.826  77.984  32.326 1.00 183.92 ? 366 ILE B O   1 
ATOM   2766 C  CB  . ILE B 2 366 ? 80.312  76.056  32.765 1.00 142.68 ? 366 ILE B CB  1 
ATOM   2767 C  CG1 . ILE B 2 366 ? 78.850  75.883  33.221 1.00 121.07 ? 366 ILE B CG1 1 
ATOM   2768 C  CG2 . ILE B 2 366 ? 81.073  74.718  32.623 1.00 108.77 ? 366 ILE B CG2 1 
ATOM   2769 C  CD1 . ILE B 2 366 ? 77.946  75.184  32.210 1.00 226.85 ? 366 ILE B CD1 1 
ATOM   2770 N  N   . HIS B 2 367 ? 83.459  76.437  33.780 1.00 140.67 ? 367 HIS B N   1 
ATOM   2771 C  CA  . HIS B 2 367 ? 84.849  76.406  33.352 1.00 168.35 ? 367 HIS B CA  1 
ATOM   2772 C  C   . HIS B 2 367 ? 85.051  75.496  32.141 1.00 203.81 ? 367 HIS B C   1 
ATOM   2773 O  O   . HIS B 2 367 ? 84.925  74.295  32.299 1.00 148.74 ? 367 HIS B O   1 
ATOM   2774 C  CB  . HIS B 2 367 ? 85.672  75.895  34.522 1.00 214.01 ? 367 HIS B CB  1 
ATOM   2775 C  CG  . HIS B 2 367 ? 87.159  75.930  34.347 1.00 180.18 ? 367 HIS B CG  1 
ATOM   2776 N  ND1 . HIS B 2 367 ? 87.933  77.044  34.091 1.00 173.06 ? 367 HIS B ND1 1 
ATOM   2777 C  CD2 . HIS B 2 367 ? 88.005  74.926  34.477 1.00 168.36 ? 367 HIS B CD2 1 
ATOM   2778 C  CE1 . HIS B 2 367 ? 89.213  76.682  34.054 1.00 301.65 ? 367 HIS B CE1 1 
ATOM   2779 N  NE2 . HIS B 2 367 ? 89.277  75.394  34.285 1.00 328.20 ? 367 HIS B NE2 1 
ATOM   2780 N  N   . PRO B 2 368 ? 85.355  76.004  30.918 1.00 215.67 ? 368 PRO B N   1 
ATOM   2781 C  CA  . PRO B 2 368 ? 85.381  75.186  29.701 1.00 207.63 ? 368 PRO B CA  1 
ATOM   2782 C  C   . PRO B 2 368 ? 86.282  73.948  29.702 1.00 224.12 ? 368 PRO B C   1 
ATOM   2783 O  O   . PRO B 2 368 ? 85.911  72.930  29.139 1.00 224.96 ? 368 PRO B O   1 
ATOM   2784 C  CB  . PRO B 2 368 ? 85.938  76.124  28.632 1.00 209.75 ? 368 PRO B CB  1 
ATOM   2785 C  CG  . PRO B 2 368 ? 85.558  77.478  29.132 1.00 207.68 ? 368 PRO B CG  1 
ATOM   2786 C  CD  . PRO B 2 368 ? 85.712  77.394  30.627 1.00 192.34 ? 368 PRO B CD  1 
ATOM   2787 N  N   . GLN B 2 369 ? 87.441  74.019  30.351 1.00 210.66 ? 369 GLN B N   1 
ATOM   2788 C  CA  . GLN B 2 369 ? 88.382  72.910  30.311 1.00 246.33 ? 369 GLN B CA  1 
ATOM   2789 C  C   . GLN B 2 369 ? 87.885  71.709  31.131 1.00 274.05 ? 369 GLN B C   1 
ATOM   2790 O  O   . GLN B 2 369 ? 88.135  70.565  30.724 1.00 297.72 ? 369 GLN B O   1 
ATOM   2791 C  CB  . GLN B 2 369 ? 89.733  73.417  30.823 1.00 377.29 ? 369 GLN B CB  1 
ATOM   2792 C  CG  . GLN B 2 369 ? 90.895  72.433  30.704 1.00 464.00 ? 369 GLN B CG  1 
ATOM   2793 C  CD  . GLN B 2 369 ? 91.396  72.230  29.291 1.00 543.73 ? 369 GLN B CD  1 
ATOM   2794 O  OE1 . GLN B 2 369 ? 90.888  72.807  28.330 1.00 566.89 ? 369 GLN B OE1 1 
ATOM   2795 N  NE2 . GLN B 2 369 ? 92.417  71.397  29.150 1.00 587.63 ? 369 GLN B NE2 1 
ATOM   2796 N  N   . LEU B 2 370 ? 87.199  71.954  32.272 1.00 225.57 ? 370 LEU B N   1 
ATOM   2797 C  CA  . LEU B 2 370 ? 86.850  70.910  33.244 1.00 245.03 ? 370 LEU B CA  1 
ATOM   2798 C  C   . LEU B 2 370 ? 85.342  70.715  33.462 1.00 208.71 ? 370 LEU B C   1 
ATOM   2799 O  O   . LEU B 2 370 ? 84.966  69.725  34.099 1.00 198.72 ? 370 LEU B O   1 
ATOM   2800 C  CB  . LEU B 2 370 ? 87.536  71.191  34.585 1.00 215.36 ? 370 LEU B CB  1 
ATOM   2801 C  CG  . LEU B 2 370 ? 89.051  71.417  34.536 1.00 320.97 ? 370 LEU B CG  1 
ATOM   2802 C  CD1 . LEU B 2 370 ? 89.555  71.779  35.940 1.00 368.46 ? 370 LEU B CD1 1 
ATOM   2803 C  CD2 . LEU B 2 370 ? 89.829  70.219  33.982 1.00 395.75 ? 370 LEU B CD2 1 
ATOM   2804 N  N   . LEU B 2 371 ? 84.506  71.626  32.934 1.00 181.55 ? 371 LEU B N   1 
ATOM   2805 C  CA  . LEU B 2 371 ? 83.065  71.466  32.752 1.00 198.37 ? 371 LEU B CA  1 
ATOM   2806 C  C   . LEU B 2 371 ? 82.344  71.369  34.104 1.00 198.38 ? 371 LEU B C   1 
ATOM   2807 O  O   . LEU B 2 371 ? 81.438  70.548  34.288 1.00 314.41 ? 371 LEU B O   1 
ATOM   2808 C  CB  . LEU B 2 371 ? 82.813  70.273  31.819 1.00 228.65 ? 371 LEU B CB  1 
ATOM   2809 C  CG  . LEU B 2 371 ? 83.391  70.450  30.417 1.00 326.16 ? 371 LEU B CG  1 
ATOM   2810 C  CD1 . LEU B 2 371 ? 83.799  69.109  29.835 1.00 368.55 ? 371 LEU B CD1 1 
ATOM   2811 C  CD2 . LEU B 2 371 ? 82.391  71.166  29.532 1.00 400.39 ? 371 LEU B CD2 1 
ATOM   2812 N  N   . THR B 2 372 ? 82.735  72.251  35.038 1.00 147.83 ? 372 THR B N   1 
ATOM   2813 C  CA  . THR B 2 372 ? 82.141  72.361  36.365 1.00 154.35 ? 372 THR B CA  1 
ATOM   2814 C  C   . THR B 2 372 ? 81.746  73.796  36.654 1.00 119.14 ? 372 THR B C   1 
ATOM   2815 O  O   . THR B 2 372 ? 82.379  74.705  36.120 1.00 186.52 ? 372 THR B O   1 
ATOM   2816 C  CB  . THR B 2 372 ? 83.091  71.891  37.475 1.00 232.69 ? 372 THR B CB  1 
ATOM   2817 O  OG1 . THR B 2 372 ? 84.320  72.588  37.373 1.00 175.94 ? 372 THR B OG1 1 
ATOM   2818 C  CG2 . THR B 2 372 ? 83.374  70.405  37.414 1.00 246.71 ? 372 THR B CG2 1 
ATOM   2819 N  N   . PRO B 2 373 ? 80.630  74.047  37.388 1.00 174.46 ? 373 PRO B N   1 
ATOM   2820 C  CA  . PRO B 2 373 ? 80.156  75.412  37.641 1.00 178.24 ? 373 PRO B CA  1 
ATOM   2821 C  C   . PRO B 2 373 ? 80.983  76.060  38.720 1.00 120.65 ? 373 PRO B C   1 
ATOM   2822 O  O   . PRO B 2 373 ? 80.405  76.450  39.703 1.00 170.16 ? 373 PRO B O   1 
ATOM   2823 C  CB  . PRO B 2 373 ? 78.666  75.198  38.016 1.00 211.13 ? 373 PRO B CB  1 
ATOM   2824 C  CG  . PRO B 2 373 ? 78.635  73.815  38.678 1.00 139.58 ? 373 PRO B CG  1 
ATOM   2825 C  CD  . PRO B 2 373 ? 79.709  73.037  37.946 1.00 179.68 ? 373 PRO B CD  1 
ATOM   2826 N  N   . VAL B 2 374 ? 82.311  76.175  38.506 1.00 99.27  ? 374 VAL B N   1 
ATOM   2827 C  CA  . VAL B 2 374 ? 83.275  76.743  39.437 1.00 147.15 ? 374 VAL B CA  1 
ATOM   2828 C  C   . VAL B 2 374 ? 82.792  77.958  40.255 1.00 138.96 ? 374 VAL B C   1 
ATOM   2829 O  O   . VAL B 2 374 ? 82.885  77.834  41.476 1.00 254.72 ? 374 VAL B O   1 
ATOM   2830 C  CB  . VAL B 2 374 ? 84.581  77.021  38.692 1.00 150.50 ? 374 VAL B CB  1 
ATOM   2831 C  CG1 . VAL B 2 374 ? 85.613  77.970  39.392 1.00 143.37 ? 374 VAL B CG1 1 
ATOM   2832 C  CG2 . VAL B 2 374 ? 85.107  75.609  38.370 1.00 168.32 ? 374 VAL B CG2 1 
ATOM   2833 N  N   . PRO B 2 375 ? 82.248  79.057  39.722 1.00 90.87  ? 375 PRO B N   1 
ATOM   2834 C  CA  . PRO B 2 375 ? 81.778  80.131  40.566 1.00 149.49 ? 375 PRO B CA  1 
ATOM   2835 C  C   . PRO B 2 375 ? 80.696  79.719  41.566 1.00 158.79 ? 375 PRO B C   1 
ATOM   2836 O  O   . PRO B 2 375 ? 80.688  80.232  42.671 1.00 163.62 ? 375 PRO B O   1 
ATOM   2837 C  CB  . PRO B 2 375 ? 81.193  81.152  39.566 1.00 220.77 ? 375 PRO B CB  1 
ATOM   2838 C  CG  . PRO B 2 375 ? 81.936  80.856  38.321 1.00 225.36 ? 375 PRO B CG  1 
ATOM   2839 C  CD  . PRO B 2 375 ? 81.982  79.342  38.326 1.00 170.27 ? 375 PRO B CD  1 
ATOM   2840 N  N   . SER B 2 376 ? 79.785  78.813  41.202 1.00 137.99 ? 376 SER B N   1 
ATOM   2841 C  CA  . SER B 2 376 ? 78.787  78.335  42.141 1.00 172.29 ? 376 SER B CA  1 
ATOM   2842 C  C   . SER B 2 376 ? 79.408  77.549  43.299 1.00 108.48 ? 376 SER B C   1 
ATOM   2843 O  O   . SER B 2 376 ? 79.028  77.732  44.446 1.00 141.33 ? 376 SER B O   1 
ATOM   2844 C  CB  . SER B 2 376 ? 77.750  77.516  41.429 1.00 223.57 ? 376 SER B CB  1 
ATOM   2845 O  OG  . SER B 2 376 ? 76.783  77.072  42.356 1.00 215.74 ? 376 SER B OG  1 
ATOM   2846 N  N   . LEU B 2 377 ? 80.347  76.660  43.019 1.00 114.87 ? 377 LEU B N   1 
ATOM   2847 C  CA  . LEU B 2 377 ? 81.051  75.912  44.061 1.00 138.01 ? 377 LEU B CA  1 
ATOM   2848 C  C   . LEU B 2 377 ? 81.884  76.829  44.957 1.00 155.53 ? 377 LEU B C   1 
ATOM   2849 O  O   . LEU B 2 377 ? 81.830  76.667  46.184 1.00 184.86 ? 377 LEU B O   1 
ATOM   2850 C  CB  . LEU B 2 377 ? 81.950  74.855  43.423 1.00 152.28 ? 377 LEU B CB  1 
ATOM   2851 C  CG  . LEU B 2 377 ? 81.182  73.724  42.739 1.00 123.13 ? 377 LEU B CG  1 
ATOM   2852 C  CD1 . LEU B 2 377 ? 82.113  72.963  41.808 1.00 185.56 ? 377 LEU B CD1 1 
ATOM   2853 C  CD2 . LEU B 2 377 ? 80.653  72.756  43.736 1.00 157.21 ? 377 LEU B CD2 1 
ATOM   2854 N  N   . VAL B 2 378 ? 82.617  77.793  44.380 1.00 104.88 ? 378 VAL B N   1 
ATOM   2855 C  CA  . VAL B 2 378 ? 83.365  78.747  45.178 1.00 101.15 ? 378 VAL B CA  1 
ATOM   2856 C  C   . VAL B 2 378 ? 82.402  79.544  46.032 1.00 85.89  ? 378 VAL B C   1 
ATOM   2857 O  O   . VAL B 2 378 ? 82.695  79.744  47.215 1.00 194.95 ? 378 VAL B O   1 
ATOM   2858 C  CB  . VAL B 2 378 ? 84.248  79.634  44.286 1.00 220.24 ? 378 VAL B CB  1 
ATOM   2859 C  CG1 . VAL B 2 378 ? 84.749  80.925  44.935 1.00 267.11 ? 378 VAL B CG1 1 
ATOM   2860 C  CG2 . VAL B 2 378 ? 85.403  78.790  43.768 1.00 331.89 ? 378 VAL B CG2 1 
ATOM   2861 N  N   . PHE B 2 379 ? 81.258  79.973  45.486 1.00 82.84  ? 379 PHE B N   1 
ATOM   2862 C  CA  . PHE B 2 379 ? 80.257  80.693  46.275 1.00 139.88 ? 379 PHE B CA  1 
ATOM   2863 C  C   . PHE B 2 379 ? 79.682  79.865  47.421 1.00 91.83  ? 379 PHE B C   1 
ATOM   2864 O  O   . PHE B 2 379 ? 79.660  80.348  48.568 1.00 142.86 ? 379 PHE B O   1 
ATOM   2865 C  CB  . PHE B 2 379 ? 79.130  81.182  45.381 1.00 162.62 ? 379 PHE B CB  1 
ATOM   2866 C  CG  . PHE B 2 379 ? 77.989  81.801  46.139 1.00 148.85 ? 379 PHE B CG  1 
ATOM   2867 C  CD1 . PHE B 2 379 ? 78.023  83.142  46.541 1.00 170.69 ? 379 PHE B CD1 1 
ATOM   2868 C  CD2 . PHE B 2 379 ? 76.890  81.019  46.440 1.00 106.14 ? 379 PHE B CD2 1 
ATOM   2869 C  CE1 . PHE B 2 379 ? 76.962  83.699  47.229 1.00 160.00 ? 379 PHE B CE1 1 
ATOM   2870 C  CE2 . PHE B 2 379 ? 75.821  81.574  47.130 1.00 180.71 ? 379 PHE B CE2 1 
ATOM   2871 C  CZ  . PHE B 2 379 ? 75.866  82.901  47.521 1.00 210.39 ? 379 PHE B CZ  1 
ATOM   2872 N  N   . THR B 2 380 ? 79.279  78.636  47.113 1.00 96.24  ? 380 THR B N   1 
ATOM   2873 C  CA  . THR B 2 380 ? 78.829  77.658  48.108 1.00 171.55 ? 380 THR B CA  1 
ATOM   2874 C  C   . THR B 2 380 ? 79.796  77.547  49.298 1.00 141.59 ? 380 THR B C   1 
ATOM   2875 O  O   . THR B 2 380 ? 79.383  77.607  50.463 1.00 75.86  ? 380 THR B O   1 
ATOM   2876 C  CB  . THR B 2 380 ? 78.688  76.269  47.454 1.00 211.99 ? 380 THR B CB  1 
ATOM   2877 O  OG1 . THR B 2 380 ? 77.689  76.403  46.446 1.00 257.66 ? 380 THR B OG1 1 
ATOM   2878 C  CG2 . THR B 2 380 ? 78.336  75.127  48.376 1.00 225.25 ? 380 THR B CG2 1 
ATOM   2879 N  N   . CYS B 2 381 ? 81.078  77.358  48.979 1.00 130.02 ? 381 CYS B N   1 
ATOM   2880 C  CA  . CYS B 2 381 ? 82.109  77.193  49.959 1.00 142.29 ? 381 CYS B CA  1 
ATOM   2881 C  C   . CYS B 2 381 ? 82.261  78.470  50.803 1.00 119.01 ? 381 CYS B C   1 
ATOM   2882 O  O   . CYS B 2 381 ? 82.203  78.402  52.029 1.00 151.57 ? 381 CYS B O   1 
ATOM   2883 C  CB  . CYS B 2 381 ? 83.399  76.840  49.244 1.00 172.50 ? 381 CYS B CB  1 
ATOM   2884 S  SG  . CYS B 2 381 ? 84.804  76.659  50.385 1.00 203.50 ? 381 CYS B SG  1 
ATOM   2885 N  N   . VAL B 2 382 ? 82.491  79.618  50.183 1.00 115.89 ? 382 VAL B N   1 
ATOM   2886 C  CA  . VAL B 2 382 ? 82.715  80.843  50.915 1.00 171.42 ? 382 VAL B CA  1 
ATOM   2887 C  C   . VAL B 2 382 ? 81.509  81.116  51.807 1.00 149.19 ? 382 VAL B C   1 
ATOM   2888 O  O   . VAL B 2 382 ? 81.684  81.454  52.986 1.00 247.80 ? 382 VAL B O   1 
ATOM   2889 C  CB  . VAL B 2 382 ? 83.056  82.008  49.957 1.00 283.04 ? 382 VAL B CB  1 
ATOM   2890 C  CG1 . VAL B 2 382 ? 82.826  83.412  50.523 1.00 341.94 ? 382 VAL B CG1 1 
ATOM   2891 C  CG2 . VAL B 2 382 ? 84.496  81.846  49.488 1.00 338.48 ? 382 VAL B CG2 1 
ATOM   2892 N  N   . MET B 2 383 ? 80.303  81.016  51.277 1.00 124.93 ? 383 MET B N   1 
ATOM   2893 C  CA  . MET B 2 383 ? 79.117  81.264  52.077 1.00 146.73 ? 383 MET B CA  1 
ATOM   2894 C  C   . MET B 2 383 ? 78.994  80.273  53.245 1.00 164.19 ? 383 MET B C   1 
ATOM   2895 O  O   . MET B 2 383 ? 78.512  80.671  54.294 1.00 220.75 ? 383 MET B O   1 
ATOM   2896 C  CB  . MET B 2 383 ? 77.906  81.154  51.143 1.00 228.10 ? 383 MET B CB  1 
ATOM   2897 C  CG  . MET B 2 383 ? 76.599  81.460  51.770 1.00 218.75 ? 383 MET B CG  1 
ATOM   2898 S  SD  . MET B 2 383 ? 76.666  83.122  52.378 1.00 233.80 ? 383 MET B SD  1 
ATOM   2899 C  CE  . MET B 2 383 ? 76.218  84.014  50.896 1.00 283.55 ? 383 MET B CE  1 
ATOM   2900 N  N   . THR B 2 384 ? 79.393  78.994  53.098 1.00 149.83 ? 384 THR B N   1 
ATOM   2901 C  CA  . THR B 2 384 ? 79.399  78.016  54.195 1.00 128.58 ? 384 THR B CA  1 
ATOM   2902 C  C   . THR B 2 384 ? 80.473  78.332  55.239 1.00 115.07 ? 384 THR B C   1 
ATOM   2903 O  O   . THR B 2 384 ? 80.194  78.304  56.420 1.00 127.30 ? 384 THR B O   1 
ATOM   2904 C  CB  . THR B 2 384 ? 79.684  76.600  53.704 1.00 157.79 ? 384 THR B CB  1 
ATOM   2905 O  OG1 . THR B 2 384 ? 78.652  76.288  52.769 1.00 222.29 ? 384 THR B OG1 1 
ATOM   2906 C  CG2 . THR B 2 384 ? 79.803  75.559  54.808 1.00 117.69 ? 384 THR B CG2 1 
ATOM   2907 N  N   . LEU B 2 385 ? 81.698  78.667  54.821 1.00 98.08  ? 385 LEU B N   1 
ATOM   2908 C  CA  . LEU B 2 385 ? 82.748  78.993  55.766 1.00 120.21 ? 385 LEU B CA  1 
ATOM   2909 C  C   . LEU B 2 385 ? 82.454  80.285  56.532 1.00 131.07 ? 385 LEU B C   1 
ATOM   2910 O  O   . LEU B 2 385 ? 82.735  80.344  57.726 1.00 152.59 ? 385 LEU B O   1 
ATOM   2911 C  CB  . LEU B 2 385 ? 84.064  79.061  55.010 1.00 163.99 ? 385 LEU B CB  1 
ATOM   2912 C  CG  . LEU B 2 385 ? 84.509  77.723  54.400 1.00 218.71 ? 385 LEU B CG  1 
ATOM   2913 C  CD1 . LEU B 2 385 ? 85.775  77.945  53.599 1.00 338.64 ? 385 LEU B CD1 1 
ATOM   2914 C  CD2 . LEU B 2 385 ? 84.732  76.646  55.462 1.00 131.80 ? 385 LEU B CD2 1 
ATOM   2915 N  N   . LEU B 2 386 ? 81.841  81.285  55.889 1.00 139.91 ? 386 LEU B N   1 
ATOM   2916 C  CA  . LEU B 2 386 ? 81.325  82.469  56.585 1.00 179.85 ? 386 LEU B CA  1 
ATOM   2917 C  C   . LEU B 2 386 ? 80.247  82.161  57.641 1.00 128.97 ? 386 LEU B C   1 
ATOM   2918 O  O   . LEU B 2 386 ? 80.005  82.973  58.527 1.00 215.70 ? 386 LEU B O   1 
ATOM   2919 C  CB  . LEU B 2 386 ? 80.765  83.471  55.570 1.00 212.89 ? 386 LEU B CB  1 
ATOM   2920 C  CG  . LEU B 2 386 ? 81.822  84.238  54.781 1.00 370.38 ? 386 LEU B CG  1 
ATOM   2921 C  CD1 . LEU B 2 386 ? 81.174  85.016  53.647 1.00 492.57 ? 386 LEU B CD1 1 
ATOM   2922 C  CD2 . LEU B 2 386 ? 82.619  85.183  55.679 1.00 377.52 ? 386 LEU B CD2 1 
ATOM   2923 N  N   . TYR B 2 387 ? 79.607  81.019  57.568 1.00 113.67 ? 387 TYR B N   1 
ATOM   2924 C  CA  . TYR B 2 387 ? 78.623  80.632  58.553 1.00 154.56 ? 387 TYR B CA  1 
ATOM   2925 C  C   . TYR B 2 387 ? 79.269  80.072  59.835 1.00 164.58 ? 387 TYR B C   1 
ATOM   2926 O  O   . TYR B 2 387 ? 78.633  80.013  60.887 1.00 197.64 ? 387 TYR B O   1 
ATOM   2927 C  CB  . TYR B 2 387 ? 77.725  79.552  57.920 1.00 191.04 ? 387 TYR B CB  1 
ATOM   2928 C  CG  . TYR B 2 387 ? 76.271  79.765  58.248 1.00 106.34 ? 387 TYR B CG  1 
ATOM   2929 C  CD1 . TYR B 2 387 ? 75.734  79.230  59.392 1.00 129.77 ? 387 TYR B CD1 1 
ATOM   2930 C  CD2 . TYR B 2 387 ? 75.478  80.520  57.437 1.00 154.47 ? 387 TYR B CD2 1 
ATOM   2931 C  CE1 . TYR B 2 387 ? 74.409  79.447  59.740 1.00 195.74 ? 387 TYR B CE1 1 
ATOM   2932 C  CE2 . TYR B 2 387 ? 74.143  80.732  57.746 1.00 230.38 ? 387 TYR B CE2 1 
ATOM   2933 C  CZ  . TYR B 2 387 ? 73.603  80.184  58.893 1.00 202.89 ? 387 TYR B CZ  1 
ATOM   2934 O  OH  . TYR B 2 387 ? 72.303  80.392  59.210 1.00 208.04 ? 387 TYR B OH  1 
ATOM   2935 N  N   . ALA B 2 388 ? 80.522  79.636  59.785 1.00 107.49 ? 388 ALA B N   1 
ATOM   2936 C  CA  . ALA B 2 388 ? 81.057  78.779  60.807 1.00 133.19 ? 388 ALA B CA  1 
ATOM   2937 C  C   . ALA B 2 388 ? 81.179  79.510  62.145 1.00 208.53 ? 388 ALA B C   1 
ATOM   2938 O  O   . ALA B 2 388 ? 81.127  78.863  63.192 1.00 298.85 ? 388 ALA B O   1 
ATOM   2939 C  CB  . ALA B 2 388 ? 82.431  78.341  60.347 1.00 220.41 ? 388 ALA B CB  1 
ATOM   2940 N  N   . PHE B 2 389 ? 81.386  80.844  62.154 1.00 191.03 ? 389 PHE B N   1 
ATOM   2941 C  CA  . PHE B 2 389 ? 81.689  81.537  63.402 1.00 211.73 ? 389 PHE B CA  1 
ATOM   2942 C  C   . PHE B 2 389 ? 80.443  82.038  64.149 1.00 193.87 ? 389 PHE B C   1 
ATOM   2943 O  O   . PHE B 2 389 ? 80.623  82.645  65.213 1.00 303.12 ? 389 PHE B O   1 
ATOM   2944 C  CB  . PHE B 2 389 ? 82.742  82.617  63.155 1.00 257.95 ? 389 PHE B CB  1 
ATOM   2945 C  CG  . PHE B 2 389 ? 82.466  83.579  62.032 1.00 242.93 ? 389 PHE B CG  1 
ATOM   2946 C  CD1 . PHE B 2 389 ? 81.372  84.436  62.063 1.00 266.10 ? 389 PHE B CD1 1 
ATOM   2947 C  CD2 . PHE B 2 389 ? 83.336  83.641  60.952 1.00 308.54 ? 389 PHE B CD2 1 
ATOM   2948 C  CE1 . PHE B 2 389 ? 81.143  85.323  61.018 1.00 400.76 ? 389 PHE B CE1 1 
ATOM   2949 C  CE2 . PHE B 2 389 ? 83.106  84.531  59.909 1.00 387.96 ? 389 PHE B CE2 1 
ATOM   2950 C  CZ  . PHE B 2 389 ? 82.009  85.367  59.943 1.00 430.26 ? 389 PHE B CZ  1 
ATOM   2951 N  N   . SER B 2 390 ? 79.215  81.784  63.661 1.00 189.68 ? 390 SER B N   1 
ATOM   2952 C  CA  . SER B 2 390 ? 78.005  82.029  64.454 1.00 294.81 ? 390 SER B CA  1 
ATOM   2953 C  C   . SER B 2 390 ? 77.851  80.998  65.590 1.00 218.75 ? 390 SER B C   1 
ATOM   2954 O  O   . SER B 2 390 ? 78.326  79.881  65.502 1.00 213.60 ? 390 SER B O   1 
ATOM   2955 C  CB  . SER B 2 390 ? 76.763  82.141  63.569 1.00 306.53 ? 390 SER B CB  1 
ATOM   2956 O  OG  . SER B 2 390 ? 76.682  83.436  62.973 1.00 228.55 ? 390 SER B OG  1 
ATOM   2957 N  N   . LYS B 2 391 ? 77.178  81.394  66.689 1.00 239.97 ? 391 LYS B N   1 
ATOM   2958 C  CA  . LYS B 2 391 ? 77.231  80.685  67.970 1.00 272.23 ? 391 LYS B CA  1 
ATOM   2959 C  C   . LYS B 2 391 ? 76.083  79.681  68.163 1.00 288.33 ? 391 LYS B C   1 
ATOM   2960 O  O   . LYS B 2 391 ? 76.338  78.519  68.500 1.00 217.55 ? 391 LYS B O   1 
ATOM   2961 C  CB  . LYS B 2 391 ? 77.209  81.706  69.111 1.00 371.99 ? 391 LYS B CB  1 
ATOM   2962 C  CG  . LYS B 2 391 ? 78.457  82.578  69.221 1.00 371.33 ? 391 LYS B CG  1 
ATOM   2963 C  CD  . LYS B 2 391 ? 78.400  83.633  70.313 1.00 358.35 ? 391 LYS B CD  1 
ATOM   2964 C  CE  . LYS B 2 391 ? 78.495  83.058  71.713 1.00 426.23 ? 391 LYS B CE  1 
ATOM   2965 N  NZ  . LYS B 2 391 ? 78.331  84.093  72.763 1.00 449.32 ? 391 LYS B NZ  1 
ATOM   2966 N  N   . ASP B 2 392 ? 74.821  80.115  67.960 1.00 305.30 ? 392 ASP B N   1 
ATOM   2967 C  CA  . ASP B 2 392 ? 73.627  79.386  68.393 1.00 345.14 ? 392 ASP B CA  1 
ATOM   2968 C  C   . ASP B 2 392 ? 72.990  78.580  67.245 1.00 313.58 ? 392 ASP B C   1 
ATOM   2969 O  O   . ASP B 2 392 ? 71.753  78.534  67.088 1.00 174.64 ? 392 ASP B O   1 
ATOM   2970 C  CB  . ASP B 2 392 ? 72.632  80.372  69.020 1.00 410.25 ? 392 ASP B CB  1 
ATOM   2971 C  CG  . ASP B 2 392 ? 73.119  81.120  70.254 1.00 408.26 ? 392 ASP B CG  1 
ATOM   2972 O  OD1 . ASP B 2 392 ? 74.083  80.657  70.905 1.00 451.63 ? 392 ASP B OD1 1 
ATOM   2973 O  OD2 . ASP B 2 392 ? 72.520  82.173  70.563 1.00 392.82 ? 392 ASP B OD2 1 
ATOM   2974 N  N   . ILE B 2 393 ? 73.827  77.893  66.444 1.00 333.18 ? 393 ILE B N   1 
ATOM   2975 C  CA  . ILE B 2 393 ? 73.403  77.323  65.166 1.00 267.91 ? 393 ILE B CA  1 
ATOM   2976 C  C   . ILE B 2 393 ? 72.246  76.340  65.376 1.00 224.92 ? 393 ILE B C   1 
ATOM   2977 O  O   . ILE B 2 393 ? 71.339  76.247  64.550 1.00 174.22 ? 393 ILE B O   1 
ATOM   2978 C  CB  . ILE B 2 393 ? 74.561  76.625  64.401 1.00 279.08 ? 393 ILE B CB  1 
ATOM   2979 C  CG1 . ILE B 2 393 ? 75.853  77.433  64.295 1.00 227.32 ? 393 ILE B CG1 1 
ATOM   2980 C  CG2 . ILE B 2 393 ? 74.106  76.278  63.002 1.00 365.28 ? 393 ILE B CG2 1 
ATOM   2981 C  CD1 . ILE B 2 393 ? 75.679  78.784  63.600 1.00 275.94 ? 393 ILE B CD1 1 
ATOM   2982 N  N   . PHE B 2 394 ? 72.283  75.559  66.465 1.00 246.03 ? 394 PHE B N   1 
ATOM   2983 C  CA  . PHE B 2 394 ? 71.315  74.486  66.684 1.00 273.39 ? 394 PHE B CA  1 
ATOM   2984 C  C   . PHE B 2 394 ? 69.943  75.026  67.112 1.00 247.58 ? 394 PHE B C   1 
ATOM   2985 O  O   . PHE B 2 394 ? 68.977  74.253  67.155 1.00 222.89 ? 394 PHE B O   1 
ATOM   2986 C  CB  . PHE B 2 394 ? 71.935  73.443  67.622 1.00 319.88 ? 394 PHE B CB  1 
ATOM   2987 C  CG  . PHE B 2 394 ? 73.168  72.793  67.021 1.00 321.47 ? 394 PHE B CG  1 
ATOM   2988 C  CD1 . PHE B 2 394 ? 73.065  71.700  66.156 1.00 221.99 ? 394 PHE B CD1 1 
ATOM   2989 C  CD2 . PHE B 2 394 ? 74.444  73.306  67.287 1.00 349.25 ? 394 PHE B CD2 1 
ATOM   2990 C  CE1 . PHE B 2 394 ? 74.210  71.128  65.608 1.00 279.53 ? 394 PHE B CE1 1 
ATOM   2991 C  CE2 . PHE B 2 394 ? 75.587  72.735  66.732 1.00 305.39 ? 394 PHE B CE2 1 
ATOM   2992 C  CZ  . PHE B 2 394 ? 75.468  71.643  65.892 1.00 306.72 ? 394 PHE B CZ  1 
ATOM   2993 N  N   . SER B 2 395 ? 69.826  76.336  67.404 1.00 233.11 ? 395 SER B N   1 
ATOM   2994 C  CA  . SER B 2 395 ? 68.527  77.022  67.392 1.00 308.10 ? 395 SER B CA  1 
ATOM   2995 C  C   . SER B 2 395 ? 68.068  77.266  65.949 1.00 298.59 ? 395 SER B C   1 
ATOM   2996 O  O   . SER B 2 395 ? 66.942  76.911  65.597 1.00 226.14 ? 395 SER B O   1 
ATOM   2997 C  CB  . SER B 2 395 ? 68.568  78.312  68.177 1.00 352.22 ? 395 SER B CB  1 
ATOM   2998 O  OG  . SER B 2 395 ? 68.923  78.083  69.533 1.00 381.07 ? 395 SER B OG  1 
ATOM   2999 N  N   . VAL B 2 396 ? 68.963  77.850  65.123 1.00 288.63 ? 396 VAL B N   1 
ATOM   3000 C  CA  . VAL B 2 396 ? 68.718  78.299  63.746 1.00 242.37 ? 396 VAL B CA  1 
ATOM   3001 C  C   . VAL B 2 396 ? 68.116  77.193  62.884 1.00 184.02 ? 396 VAL B C   1 
ATOM   3002 O  O   . VAL B 2 396 ? 67.017  77.303  62.350 1.00 99.59  ? 396 VAL B O   1 
ATOM   3003 C  CB  . VAL B 2 396 ? 69.999  78.858  63.081 1.00 189.48 ? 396 VAL B CB  1 
ATOM   3004 C  CG1 . VAL B 2 396 ? 69.771  79.232  61.622 1.00 235.89 ? 396 VAL B CG1 1 
ATOM   3005 C  CG2 . VAL B 2 396 ? 70.548  80.056  63.853 1.00 254.54 ? 396 VAL B CG2 1 
ATOM   3006 N  N   . ILE B 2 397 ? 68.864  76.100  62.765 1.00 213.50 ? 397 ILE B N   1 
ATOM   3007 C  CA  . ILE B 2 397 ? 68.483  74.988  61.910 1.00 231.63 ? 397 ILE B CA  1 
ATOM   3008 C  C   . ILE B 2 397 ? 67.227  74.278  62.432 1.00 216.18 ? 397 ILE B C   1 
ATOM   3009 O  O   . ILE B 2 397 ? 66.632  73.515  61.670 1.00 320.23 ? 397 ILE B O   1 
ATOM   3010 C  CB  . ILE B 2 397 ? 69.678  74.022  61.754 1.00 240.05 ? 397 ILE B CB  1 
ATOM   3011 C  CG1 . ILE B 2 397 ? 70.125  73.348  63.069 1.00 176.94 ? 397 ILE B CG1 1 
ATOM   3012 C  CG2 . ILE B 2 397 ? 70.815  74.744  61.072 1.00 182.92 ? 397 ILE B CG2 1 
ATOM   3013 C  CD1 . ILE B 2 397 ? 69.632  71.928  63.279 1.00 188.12 ? 397 ILE B CD1 1 
ATOM   3014 N  N   . ASN B 2 398 ? 66.829  74.496  63.697 1.00 140.55 ? 398 ASN B N   1 
ATOM   3015 C  CA  . ASN B 2 398 ? 65.599  73.940  64.230 1.00 208.47 ? 398 ASN B CA  1 
ATOM   3016 C  C   . ASN B 2 398 ? 64.439  74.863  63.861 1.00 175.57 ? 398 ASN B C   1 
ATOM   3017 O  O   . ASN B 2 398 ? 63.439  74.384  63.342 1.00 260.17 ? 398 ASN B O   1 
ATOM   3018 C  CB  . ASN B 2 398 ? 65.742  73.644  65.728 1.00 266.91 ? 398 ASN B CB  1 
ATOM   3019 C  CG  . ASN B 2 398 ? 64.778  72.585  66.239 1.00 319.15 ? 398 ASN B CG  1 
ATOM   3020 O  OD1 . ASN B 2 398 ? 63.567  72.641  65.991 1.00 209.74 ? 398 ASN B OD1 1 
ATOM   3021 N  ND2 . ASN B 2 398 ? 65.300  71.601  66.959 1.00 356.04 ? 398 ASN B ND2 1 
ATOM   3022 N  N   . PHE B 2 399 ? 64.535  76.181  64.088 1.00 192.90 ? 399 PHE B N   1 
ATOM   3023 C  CA  . PHE B 2 399 ? 63.394  77.047  63.787 1.00 293.23 ? 399 PHE B CA  1 
ATOM   3024 C  C   . PHE B 2 399 ? 63.126  77.197  62.278 1.00 221.29 ? 399 PHE B C   1 
ATOM   3025 O  O   . PHE B 2 399 ? 61.996  77.482  61.886 1.00 207.47 ? 399 PHE B O   1 
ATOM   3026 C  CB  . PHE B 2 399 ? 63.510  78.357  64.569 1.00 382.25 ? 399 PHE B CB  1 
ATOM   3027 C  CG  . PHE B 2 399 ? 64.658  79.328  64.407 1.00 243.42 ? 399 PHE B CG  1 
ATOM   3028 C  CD1 . PHE B 2 399 ? 64.831  80.052  63.243 1.00 157.41 ? 399 PHE B CD1 1 
ATOM   3029 C  CD2 . PHE B 2 399 ? 65.535  79.574  65.466 1.00 188.45 ? 399 PHE B CD2 1 
ATOM   3030 C  CE1 . PHE B 2 399 ? 65.846  80.993  63.128 1.00 231.39 ? 399 PHE B CE1 1 
ATOM   3031 C  CE2 . PHE B 2 399 ? 66.552  80.513  65.346 1.00 236.48 ? 399 PHE B CE2 1 
ATOM   3032 C  CZ  . PHE B 2 399 ? 66.714  81.222  64.172 1.00 255.48 ? 399 PHE B CZ  1 
ATOM   3033 N  N   . PHE B 2 400 ? 64.136  76.966  61.436 1.00 202.52 ? 400 PHE B N   1 
ATOM   3034 C  CA  . PHE B 2 400 ? 63.937  76.772  59.999 1.00 188.80 ? 400 PHE B CA  1 
ATOM   3035 C  C   . PHE B 2 400 ? 63.699  75.316  59.567 1.00 184.84 ? 400 PHE B C   1 
ATOM   3036 O  O   . PHE B 2 400 ? 63.466  75.098  58.388 1.00 195.94 ? 400 PHE B O   1 
ATOM   3037 C  CB  . PHE B 2 400 ? 65.172  77.293  59.266 1.00 197.79 ? 400 PHE B CB  1 
ATOM   3038 C  CG  . PHE B 2 400 ? 65.221  78.784  59.055 1.00 186.04 ? 400 PHE B CG  1 
ATOM   3039 C  CD1 . PHE B 2 400 ? 64.420  79.354  58.086 1.00 132.39 ? 400 PHE B CD1 1 
ATOM   3040 C  CD2 . PHE B 2 400 ? 66.081  79.610  59.795 1.00 248.38 ? 400 PHE B CD2 1 
ATOM   3041 C  CE1 . PHE B 2 400 ? 64.456  80.732  57.885 1.00 225.22 ? 400 PHE B CE1 1 
ATOM   3042 C  CE2 . PHE B 2 400 ? 66.138  80.989  59.571 1.00 157.02 ? 400 PHE B CE2 1 
ATOM   3043 C  CZ  . PHE B 2 400 ? 65.300  81.543  58.628 1.00 205.88 ? 400 PHE B CZ  1 
ATOM   3044 N  N   . SER B 2 401 ? 63.729  74.318  60.470 1.00 216.53 ? 401 SER B N   1 
ATOM   3045 C  CA  . SER B 2 401 ? 63.544  72.903  60.134 1.00 213.45 ? 401 SER B CA  1 
ATOM   3046 C  C   . SER B 2 401 ? 62.264  72.693  59.321 1.00 198.77 ? 401 SER B C   1 
ATOM   3047 O  O   . SER B 2 401 ? 62.258  71.966  58.328 1.00 194.53 ? 401 SER B O   1 
ATOM   3048 C  CB  . SER B 2 401 ? 63.525  72.040  61.388 1.00 248.58 ? 401 SER B CB  1 
ATOM   3049 O  OG  . SER B 2 401 ? 63.391  70.654  61.085 1.00 263.39 ? 401 SER B OG  1 
ATOM   3050 N  N   . PHE B 2 402 ? 61.191  73.361  59.758 1.00 205.43 ? 402 PHE B N   1 
ATOM   3051 C  CA  . PHE B 2 402 ? 59.850  73.230  59.203 1.00 231.69 ? 402 PHE B CA  1 
ATOM   3052 C  C   . PHE B 2 402 ? 59.728  73.839  57.801 1.00 183.73 ? 402 PHE B C   1 
ATOM   3053 O  O   . PHE B 2 402 ? 58.870  73.401  57.031 1.00 143.18 ? 402 PHE B O   1 
ATOM   3054 C  CB  . PHE B 2 402 ? 58.856  73.828  60.213 1.00 253.89 ? 402 PHE B CB  1 
ATOM   3055 C  CG  . PHE B 2 402 ? 59.020  73.224  61.597 1.00 222.69 ? 402 PHE B CG  1 
ATOM   3056 C  CD1 . PHE B 2 402 ? 58.536  71.955  61.917 1.00 239.36 ? 402 PHE B CD1 1 
ATOM   3057 C  CD2 . PHE B 2 402 ? 59.703  73.914  62.581 1.00 184.94 ? 402 PHE B CD2 1 
ATOM   3058 C  CE1 . PHE B 2 402 ? 58.713  71.413  63.185 1.00 180.41 ? 402 PHE B CE1 1 
ATOM   3059 C  CE2 . PHE B 2 402 ? 59.880  73.359  63.843 1.00 235.69 ? 402 PHE B CE2 1 
ATOM   3060 C  CZ  . PHE B 2 402 ? 59.385  72.110  64.139 1.00 174.05 ? 402 PHE B CZ  1 
ATOM   3061 N  N   . PHE B 2 403 ? 60.568  74.824  57.457 1.00 203.30 ? 403 PHE B N   1 
ATOM   3062 C  CA  . PHE B 2 403 ? 60.498  75.477  56.153 1.00 225.54 ? 403 PHE B CA  1 
ATOM   3063 C  C   . PHE B 2 403 ? 60.781  74.501  54.990 1.00 179.30 ? 403 PHE B C   1 
ATOM   3064 O  O   . PHE B 2 403 ? 60.219  74.646  53.895 1.00 241.44 ? 403 PHE B O   1 
ATOM   3065 C  CB  . PHE B 2 403 ? 61.443  76.682  56.139 1.00 234.24 ? 403 PHE B CB  1 
ATOM   3066 C  CG  . PHE B 2 403 ? 61.378  77.465  54.852 1.00 255.56 ? 403 PHE B CG  1 
ATOM   3067 C  CD1 . PHE B 2 403 ? 60.411  78.444  54.686 1.00 323.58 ? 403 PHE B CD1 1 
ATOM   3068 C  CD2 . PHE B 2 403 ? 62.257  77.196  53.794 1.00 212.73 ? 403 PHE B CD2 1 
ATOM   3069 C  CE1 . PHE B 2 403 ? 60.335  79.160  53.502 1.00 398.48 ? 403 PHE B CE1 1 
ATOM   3070 C  CE2 . PHE B 2 403 ? 62.179  77.905  52.610 1.00 221.51 ? 403 PHE B CE2 1 
ATOM   3071 C  CZ  . PHE B 2 403 ? 61.216  78.888  52.478 1.00 348.28 ? 403 PHE B CZ  1 
ATOM   3072 N  N   . ASN B 2 404 ? 61.627  73.497  55.193 1.00 105.94 ? 404 ASN B N   1 
ATOM   3073 C  CA  . ASN B 2 404 ? 61.854  72.475  54.204 1.00 129.04 ? 404 ASN B CA  1 
ATOM   3074 C  C   . ASN B 2 404 ? 60.539  71.715  53.950 1.00 133.70 ? 404 ASN B C   1 
ATOM   3075 O  O   . ASN B 2 404 ? 60.177  71.483  52.781 1.00 170.86 ? 404 ASN B O   1 
ATOM   3076 C  CB  . ASN B 2 404 ? 63.008  71.587  54.683 1.00 193.39 ? 404 ASN B CB  1 
ATOM   3077 C  CG  . ASN B 2 404 ? 63.334  70.438  53.749 1.00 240.55 ? 404 ASN B CG  1 
ATOM   3078 O  OD1 . ASN B 2 404 ? 63.834  70.712  52.661 1.00 295.62 ? 404 ASN B OD1 1 
ATOM   3079 N  ND2 . ASN B 2 404 ? 63.081  69.179  54.138 1.00 170.55 ? 404 ASN B ND2 1 
ATOM   3080 N  N   . TRP B 2 405 ? 59.828  71.301  55.023 1.00 126.47 ? 405 TRP B N   1 
ATOM   3081 C  CA  . TRP B 2 405 ? 58.606  70.498  54.915 1.00 136.60 ? 405 TRP B CA  1 
ATOM   3082 C  C   . TRP B 2 405 ? 57.512  71.322  54.274 1.00 129.02 ? 405 TRP B C   1 
ATOM   3083 O  O   . TRP B 2 405 ? 56.702  70.779  53.512 1.00 156.28 ? 405 TRP B O   1 
ATOM   3084 C  CB  . TRP B 2 405 ? 58.191  69.865  56.276 1.00 169.11 ? 405 TRP B CB  1 
ATOM   3085 C  CG  . TRP B 2 405 ? 59.320  68.979  56.691 1.00 225.17 ? 405 TRP B CG  1 
ATOM   3086 C  CD1 . TRP B 2 405 ? 60.244  69.166  57.676 1.00 248.27 ? 405 TRP B CD1 1 
ATOM   3087 C  CD2 . TRP B 2 405 ? 59.686  67.756  56.018 1.00 186.52 ? 405 TRP B CD2 1 
ATOM   3088 N  NE1 . TRP B 2 405 ? 61.153  68.133  57.683 1.00 196.68 ? 405 TRP B NE1 1 
ATOM   3089 C  CE2 . TRP B 2 405 ? 60.841  67.251  56.673 1.00 204.74 ? 405 TRP B CE2 1 
ATOM   3090 C  CE3 . TRP B 2 405 ? 59.143  67.039  54.947 1.00 138.59 ? 405 TRP B CE3 1 
ATOM   3091 C  CZ2 . TRP B 2 405 ? 61.457  66.060  56.270 1.00 271.38 ? 405 TRP B CZ2 1 
ATOM   3092 C  CZ3 . TRP B 2 405 ? 59.769  65.875  54.545 1.00 290.60 ? 405 TRP B CZ3 1 
ATOM   3093 C  CH2 . TRP B 2 405 ? 60.908  65.391  55.197 1.00 290.89 ? 405 TRP B CH2 1 
ATOM   3094 N  N   . LEU B 2 406 ? 57.468  72.615  54.602 1.00 166.18 ? 406 LEU B N   1 
ATOM   3095 C  CA  . LEU B 2 406 ? 56.518  73.523  53.979 1.00 204.37 ? 406 LEU B CA  1 
ATOM   3096 C  C   . LEU B 2 406 ? 56.720  73.537  52.463 1.00 155.93 ? 406 LEU B C   1 
ATOM   3097 O  O   . LEU B 2 406 ? 55.761  73.365  51.717 1.00 119.78 ? 406 LEU B O   1 
ATOM   3098 C  CB  . LEU B 2 406 ? 56.712  74.906  54.603 1.00 209.58 ? 406 LEU B CB  1 
ATOM   3099 C  CG  . LEU B 2 406 ? 55.771  75.966  54.093 1.00 230.26 ? 406 LEU B CG  1 
ATOM   3100 C  CD1 . LEU B 2 406 ? 54.335  75.584  54.502 1.00 201.39 ? 406 LEU B CD1 1 
ATOM   3101 C  CD2 . LEU B 2 406 ? 56.227  77.324  54.626 1.00 282.14 ? 406 LEU B CD2 1 
ATOM   3102 N  N   . CYS B 2 407 ? 57.952  73.736  52.000 1.00 123.38 ? 407 CYS B N   1 
ATOM   3103 C  CA  . CYS B 2 407 ? 58.239  73.753  50.575 1.00 146.17 ? 407 CYS B CA  1 
ATOM   3104 C  C   . CYS B 2 407 ? 57.969  72.425  49.868 1.00 129.48 ? 407 CYS B C   1 
ATOM   3105 O  O   . CYS B 2 407 ? 57.446  72.433  48.759 1.00 163.61 ? 407 CYS B O   1 
ATOM   3106 C  CB  . CYS B 2 407 ? 59.677  74.170  50.358 1.00 208.48 ? 407 CYS B CB  1 
ATOM   3107 S  SG  . CYS B 2 407 ? 59.953  75.872  50.919 1.00 272.84 ? 407 CYS B SG  1 
ATOM   3108 N  N   . VAL B 2 408 ? 58.305  71.293  50.484 1.00 160.69 ? 408 VAL B N   1 
ATOM   3109 C  CA  . VAL B 2 408 ? 57.973  69.979  49.940 1.00 176.22 ? 408 VAL B CA  1 
ATOM   3110 C  C   . VAL B 2 408 ? 56.450  69.853  49.779 1.00 174.49 ? 408 VAL B C   1 
ATOM   3111 O  O   . VAL B 2 408 ? 55.981  69.313  48.780 1.00 153.34 ? 408 VAL B O   1 
ATOM   3112 C  CB  . VAL B 2 408 ? 58.593  68.850  50.816 1.00 169.43 ? 408 VAL B CB  1 
ATOM   3113 C  CG1 . VAL B 2 408 ? 58.025  67.454  50.616 1.00 117.91 ? 408 VAL B CG1 1 
ATOM   3114 C  CG2 . VAL B 2 408 ? 60.070  68.736  50.617 1.00 158.41 ? 408 VAL B CG2 1 
ATOM   3115 N  N   . ALA B 2 409 ? 55.663  70.326  50.756 1.00 126.72 ? 409 ALA B N   1 
ATOM   3116 C  CA  . ALA B 2 409 ? 54.225  70.331  50.628 1.00 166.36 ? 409 ALA B CA  1 
ATOM   3117 C  C   . ALA B 2 409 ? 53.788  71.243  49.472 1.00 201.40 ? 409 ALA B C   1 
ATOM   3118 O  O   . ALA B 2 409 ? 52.992  70.818  48.632 1.00 242.32 ? 409 ALA B O   1 
ATOM   3119 C  CB  . ALA B 2 409 ? 53.611  70.745  51.942 1.00 244.25 ? 409 ALA B CB  1 
ATOM   3120 N  N   . LEU B 2 410 ? 54.274  72.492  49.395 1.00 152.06 ? 410 LEU B N   1 
ATOM   3121 C  CA  . LEU B 2 410 ? 53.903  73.386  48.295 1.00 158.04 ? 410 LEU B CA  1 
ATOM   3122 C  C   . LEU B 2 410 ? 54.249  72.771  46.942 1.00 162.27 ? 410 LEU B C   1 
ATOM   3123 O  O   . LEU B 2 410 ? 53.512  72.986  45.993 1.00 183.51 ? 410 LEU B O   1 
ATOM   3124 C  CB  . LEU B 2 410 ? 54.639  74.725  48.412 1.00 189.50 ? 410 LEU B CB  1 
ATOM   3125 C  CG  . LEU B 2 410 ? 54.253  75.638  49.556 1.00 245.38 ? 410 LEU B CG  1 
ATOM   3126 C  CD1 . LEU B 2 410 ? 55.194  76.851  49.549 1.00 227.51 ? 410 LEU B CD1 1 
ATOM   3127 C  CD2 . LEU B 2 410 ? 52.780  76.021  49.450 1.00 259.27 ? 410 LEU B CD2 1 
ATOM   3128 N  N   . ALA B 2 411 ? 55.351  72.010  46.836 1.00 158.55 ? 411 ALA B N   1 
ATOM   3129 C  CA  . ALA B 2 411 ? 55.738  71.373  45.594 1.00 161.68 ? 411 ALA B CA  1 
ATOM   3130 C  C   . ALA B 2 411 ? 54.715  70.323  45.173 1.00 164.12 ? 411 ALA B C   1 
ATOM   3131 O  O   . ALA B 2 411 ? 54.251  70.373  44.024 1.00 221.79 ? 411 ALA B O   1 
ATOM   3132 C  CB  . ALA B 2 411 ? 57.097  70.785  45.740 1.00 227.26 ? 411 ALA B CB  1 
ATOM   3133 N  N   . ILE B 2 412 ? 54.330  69.412  46.074 1.00 118.52 ? 412 ILE B N   1 
ATOM   3134 C  CA  . ILE B 2 412 ? 53.340  68.401  45.674 1.00 210.19 ? 412 ILE B CA  1 
ATOM   3135 C  C   . ILE B 2 412 ? 51.922  69.011  45.492 1.00 215.07 ? 412 ILE B C   1 
ATOM   3136 O  O   . ILE B 2 412 ? 51.171  68.542  44.616 1.00 121.44 ? 412 ILE B O   1 
ATOM   3137 C  CB  . ILE B 2 412 ? 53.416  67.170  46.614 1.00 227.37 ? 412 ILE B CB  1 
ATOM   3138 C  CG1 . ILE B 2 412 ? 54.817  66.556  46.658 1.00 158.16 ? 412 ILE B CG1 1 
ATOM   3139 C  CG2 . ILE B 2 412 ? 52.372  66.117  46.247 1.00 215.93 ? 412 ILE B CG2 1 
ATOM   3140 C  CD1 . ILE B 2 412 ? 55.407  66.306  45.329 1.00 237.53 ? 412 ILE B CD1 1 
ATOM   3141 N  N   . ILE B 2 413 ? 51.543  70.062  46.253 1.00 170.60 ? 413 ILE B N   1 
ATOM   3142 C  CA  . ILE B 2 413 ? 50.348  70.853  45.962 1.00 192.54 ? 413 ILE B CA  1 
ATOM   3143 C  C   . ILE B 2 413 ? 50.404  71.410  44.529 1.00 190.33 ? 413 ILE B C   1 
ATOM   3144 O  O   . ILE B 2 413 ? 49.430  71.323  43.772 1.00 252.07 ? 413 ILE B O   1 
ATOM   3145 C  CB  . ILE B 2 413 ? 50.138  71.965  47.014 1.00 220.18 ? 413 ILE B CB  1 
ATOM   3146 C  CG1 . ILE B 2 413 ? 49.750  71.389  48.371 1.00 306.33 ? 413 ILE B CG1 1 
ATOM   3147 C  CG2 . ILE B 2 413 ? 49.099  73.000  46.572 1.00 318.03 ? 413 ILE B CG2 1 
ATOM   3148 C  CD1 . ILE B 2 413 ? 49.903  72.363  49.528 1.00 379.90 ? 413 ILE B CD1 1 
ATOM   3149 N  N   . GLY B 2 414 ? 51.547  71.974  44.150 1.00 218.35 ? 414 GLY B N   1 
ATOM   3150 C  CA  . GLY B 2 414 ? 51.785  72.435  42.796 1.00 229.08 ? 414 GLY B CA  1 
ATOM   3151 C  C   . GLY B 2 414 ? 51.642  71.324  41.763 1.00 191.60 ? 414 GLY B C   1 
ATOM   3152 O  O   . GLY B 2 414 ? 51.138  71.593  40.681 1.00 231.13 ? 414 GLY B O   1 
ATOM   3153 N  N   . MET B 2 415 ? 52.064  70.093  42.089 1.00 139.50 ? 415 MET B N   1 
ATOM   3154 C  CA  . MET B 2 415 ? 51.935  68.968  41.181 1.00 213.78 ? 415 MET B CA  1 
ATOM   3155 C  C   . MET B 2 415 ? 50.457  68.647  40.871 1.00 238.63 ? 415 MET B C   1 
ATOM   3156 O  O   . MET B 2 415 ? 50.102  68.448  39.706 1.00 268.60 ? 415 MET B O   1 
ATOM   3157 C  CB  . MET B 2 415 ? 52.676  67.754  41.749 1.00 202.63 ? 415 MET B CB  1 
ATOM   3158 C  CG  . MET B 2 415 ? 52.845  66.637  40.731 1.00 253.79 ? 415 MET B CG  1 
ATOM   3159 S  SD  . MET B 2 415 ? 51.725  65.272  40.962 1.00 299.89 ? 415 MET B SD  1 
ATOM   3160 C  CE  . MET B 2 415 ? 52.607  64.352  42.224 1.00 244.74 ? 415 MET B CE  1 
ATOM   3161 N  N   . ILE B 2 416 ? 49.589  68.620  41.887 1.00 181.32 ? 416 ILE B N   1 
ATOM   3162 C  CA  . ILE B 2 416 ? 48.155  68.396  41.686 1.00 186.20 ? 416 ILE B CA  1 
ATOM   3163 C  C   . ILE B 2 416 ? 47.479  69.577  40.970 1.00 200.31 ? 416 ILE B C   1 
ATOM   3164 O  O   . ILE B 2 416 ? 46.617  69.354  40.116 1.00 308.21 ? 416 ILE B O   1 
ATOM   3165 C  CB  . ILE B 2 416 ? 47.487  68.066  43.039 1.00 296.53 ? 416 ILE B CB  1 
ATOM   3166 C  CG1 . ILE B 2 416 ? 48.066  66.776  43.636 1.00 372.89 ? 416 ILE B CG1 1 
ATOM   3167 C  CG2 . ILE B 2 416 ? 45.961  68.011  42.939 1.00 371.30 ? 416 ILE B CG2 1 
ATOM   3168 C  CD1 . ILE B 2 416 ? 48.054  65.560  42.700 1.00 353.35 ? 416 ILE B CD1 1 
ATOM   3169 N  N   . TRP B 2 417 ? 47.861  70.819  41.289 1.00 222.15 ? 417 TRP B N   1 
ATOM   3170 C  CA  . TRP B 2 417 ? 47.386  72.016  40.591 1.00 241.33 ? 417 TRP B CA  1 
ATOM   3171 C  C   . TRP B 2 417 ? 47.767  72.006  39.106 1.00 198.37 ? 417 TRP B C   1 
ATOM   3172 O  O   . TRP B 2 417 ? 46.946  72.360  38.266 1.00 172.27 ? 417 TRP B O   1 
ATOM   3173 C  CB  . TRP B 2 417 ? 47.970  73.202  41.346 1.00 283.21 ? 417 TRP B CB  1 
ATOM   3174 C  CG  . TRP B 2 417 ? 47.649  74.612  40.943 1.00 256.61 ? 417 TRP B CG  1 
ATOM   3175 C  CD1 . TRP B 2 417 ? 46.742  75.411  41.569 1.00 275.02 ? 417 TRP B CD1 1 
ATOM   3176 C  CD2 . TRP B 2 417 ? 48.275  75.425  39.920 1.00 242.32 ? 417 TRP B CD2 1 
ATOM   3177 N  NE1 . TRP B 2 417 ? 46.736  76.652  40.994 1.00 305.64 ? 417 TRP B NE1 1 
ATOM   3178 C  CE2 . TRP B 2 417 ? 47.664  76.704  39.978 1.00 293.11 ? 417 TRP B CE2 1 
ATOM   3179 C  CE3 . TRP B 2 417 ? 49.267  75.209  38.954 1.00 282.11 ? 417 TRP B CE3 1 
ATOM   3180 C  CZ2 . TRP B 2 417 ? 48.025  77.754  39.116 1.00 327.00 ? 417 TRP B CZ2 1 
ATOM   3181 C  CZ3 . TRP B 2 417 ? 49.623  76.247  38.103 1.00 405.92 ? 417 TRP B CZ3 1 
ATOM   3182 C  CH2 . TRP B 2 417 ? 49.029  77.511  38.197 1.00 410.59 ? 417 TRP B CH2 1 
ATOM   3183 N  N   . LEU B 2 418 ? 48.985  71.536  38.785 1.00 182.47 ? 418 LEU B N   1 
ATOM   3184 C  CA  . LEU B 2 418 ? 49.386  71.253  37.407 1.00 200.37 ? 418 LEU B CA  1 
ATOM   3185 C  C   . LEU B 2 418 ? 48.605  70.088  36.778 1.00 196.49 ? 418 LEU B C   1 
ATOM   3186 O  O   . LEU B 2 418 ? 48.277  70.178  35.598 1.00 261.73 ? 418 LEU B O   1 
ATOM   3187 C  CB  . LEU B 2 418 ? 50.886  70.960  37.334 1.00 210.15 ? 418 LEU B CB  1 
ATOM   3188 C  CG  . LEU B 2 418 ? 51.829  72.164  37.412 1.00 248.91 ? 418 LEU B CG  1 
ATOM   3189 C  CD1 . LEU B 2 418 ? 53.262  71.655  37.450 1.00 334.19 ? 418 LEU B CD1 1 
ATOM   3190 C  CD2 . LEU B 2 418 ? 51.672  73.138  36.248 1.00 272.79 ? 418 LEU B CD2 1 
ATOM   3191 N  N   . ARG B 2 419 ? 48.286  69.006  37.496 1.00 155.76 ? 419 ARG B N   1 
ATOM   3192 C  CA  . ARG B 2 419 ? 47.500  67.929  36.880 1.00 245.18 ? 419 ARG B CA  1 
ATOM   3193 C  C   . ARG B 2 419 ? 46.071  68.395  36.509 1.00 293.35 ? 419 ARG B C   1 
ATOM   3194 O  O   . ARG B 2 419 ? 45.489  67.852  35.563 1.00 294.64 ? 419 ARG B O   1 
ATOM   3195 C  CB  . ARG B 2 419 ? 47.511  66.642  37.723 1.00 283.90 ? 419 ARG B CB  1 
ATOM   3196 C  CG  . ARG B 2 419 ? 47.272  65.430  36.817 1.00 286.98 ? 419 ARG B CG  1 
ATOM   3197 C  CD  . ARG B 2 419 ? 47.040  64.089  37.474 1.00 288.48 ? 419 ARG B CD  1 
ATOM   3198 N  NE  . ARG B 2 419 ? 48.265  63.417  37.862 1.00 253.64 ? 419 ARG B NE  1 
ATOM   3199 C  CZ  . ARG B 2 419 ? 48.334  62.320  38.628 1.00 272.17 ? 419 ARG B CZ  1 
ATOM   3200 N  NH1 . ARG B 2 419 ? 49.506  61.838  38.970 1.00 212.08 ? 419 ARG B NH1 1 
ATOM   3201 N  NH2 . ARG B 2 419 ? 47.253  61.702  39.076 1.00 332.08 ? 419 ARG B NH2 1 
ATOM   3202 N  N   . HIS B 2 420 ? 45.506  69.395  37.220 1.00 322.73 ? 420 HIS B N   1 
ATOM   3203 C  CA  . HIS B 2 420 ? 44.294  70.095  36.790 1.00 306.17 ? 420 HIS B CA  1 
ATOM   3204 C  C   . HIS B 2 420 ? 44.545  71.021  35.592 1.00 249.70 ? 420 HIS B C   1 
ATOM   3205 O  O   . HIS B 2 420 ? 43.852  70.890  34.579 1.00 293.92 ? 420 HIS B O   1 
ATOM   3206 C  CB  . HIS B 2 420 ? 43.663  70.903  37.935 1.00 311.89 ? 420 HIS B CB  1 
ATOM   3207 C  CG  . HIS B 2 420 ? 43.031  70.091  39.027 1.00 361.08 ? 420 HIS B CG  1 
ATOM   3208 N  ND1 . HIS B 2 420 ? 43.693  69.315  39.960 1.00 426.17 ? 420 HIS B ND1 1 
ATOM   3209 C  CD2 . HIS B 2 420 ? 41.726  69.975  39.317 1.00 319.09 ? 420 HIS B CD2 1 
ATOM   3210 C  CE1 . HIS B 2 420 ? 42.803  68.749  40.773 1.00 383.66 ? 420 HIS B CE1 1 
ATOM   3211 N  NE2 . HIS B 2 420 ? 41.599  69.136  40.402 1.00 298.36 ? 420 HIS B NE2 1 
ATOM   3212 N  N   . ARG B 2 421 ? 45.508  71.955  35.699 1.00 226.55 ? 421 ARG B N   1 
ATOM   3213 C  CA  . ARG B 2 421 ? 45.650  73.045  34.735 1.00 251.19 ? 421 ARG B CA  1 
ATOM   3214 C  C   . ARG B 2 421 ? 46.344  72.615  33.428 1.00 230.69 ? 421 ARG B C   1 
ATOM   3215 O  O   . ARG B 2 421 ? 46.081  73.223  32.380 1.00 304.38 ? 421 ARG B O   1 
ATOM   3216 C  CB  . ARG B 2 421 ? 46.392  74.219  35.384 1.00 241.85 ? 421 ARG B CB  1 
ATOM   3217 C  CG  . ARG B 2 421 ? 46.357  75.504  34.560 1.00 222.13 ? 421 ARG B CG  1 
ATOM   3218 C  CD  . ARG B 2 421 ? 46.795  76.724  35.352 1.00 311.93 ? 421 ARG B CD  1 
ATOM   3219 N  NE  . ARG B 2 421 ? 45.957  76.987  36.527 1.00 376.79 ? 421 ARG B NE  1 
ATOM   3220 C  CZ  . ARG B 2 421 ? 44.777  77.616  36.508 1.00 340.88 ? 421 ARG B CZ  1 
ATOM   3221 N  NH1 . ARG B 2 421 ? 44.116  77.817  37.637 1.00 365.43 ? 421 ARG B NH1 1 
ATOM   3222 N  NH2 . ARG B 2 421 ? 44.257  78.055  35.375 1.00 310.62 ? 421 ARG B NH2 1 
ATOM   3223 N  N   . LYS B 2 422 ? 47.223  71.597  33.473 1.00 176.29 ? 422 LYS B N   1 
ATOM   3224 C  CA  . LYS B 2 422 ? 48.024  71.175  32.324 1.00 235.73 ? 422 LYS B CA  1 
ATOM   3225 C  C   . LYS B 2 422 ? 48.064  69.641  32.229 1.00 267.53 ? 422 LYS B C   1 
ATOM   3226 O  O   . LYS B 2 422 ? 49.081  68.991  32.490 1.00 301.83 ? 422 LYS B O   1 
ATOM   3227 C  CB  . LYS B 2 422 ? 49.436  71.774  32.366 1.00 230.55 ? 422 LYS B CB  1 
ATOM   3228 C  CG  . LYS B 2 422 ? 49.496  73.298  32.376 1.00 252.76 ? 422 LYS B CG  1 
ATOM   3229 C  CD  . LYS B 2 422 ? 50.895  73.868  32.402 1.00 309.17 ? 422 LYS B CD  1 
ATOM   3230 C  CE  . LYS B 2 422 ? 50.945  75.346  32.766 1.00 332.87 ? 422 LYS B CE  1 
ATOM   3231 N  NZ  . LYS B 2 422 ? 50.438  76.245  31.701 1.00 365.49 ? 422 LYS B NZ  1 
ATOM   3232 N  N   . PRO B 2 423 ? 46.955  69.002  31.782 1.00 292.30 ? 423 PRO B N   1 
ATOM   3233 C  CA  . PRO B 2 423 ? 47.000  67.613  31.310 1.00 355.78 ? 423 PRO B CA  1 
ATOM   3234 C  C   . PRO B 2 423 ? 47.817  67.478  30.013 1.00 299.33 ? 423 PRO B C   1 
ATOM   3235 O  O   . PRO B 2 423 ? 48.174  66.359  29.623 1.00 174.41 ? 423 PRO B O   1 
ATOM   3236 C  CB  . PRO B 2 423 ? 45.520  67.243  31.119 1.00 389.56 ? 423 PRO B CB  1 
ATOM   3237 C  CG  . PRO B 2 423 ? 44.858  68.560  30.819 1.00 387.09 ? 423 PRO B CG  1 
ATOM   3238 C  CD  . PRO B 2 423 ? 45.610  69.572  31.657 1.00 282.07 ? 423 PRO B CD  1 
ATOM   3239 N  N   . GLU B 2 424 ? 48.114  68.626  29.367 1.00 273.73 ? 424 GLU B N   1 
ATOM   3240 C  CA  . GLU B 2 424 ? 48.942  68.754  28.168 1.00 312.61 ? 424 GLU B CA  1 
ATOM   3241 C  C   . GLU B 2 424 ? 50.382  68.239  28.343 1.00 362.61 ? 424 GLU B C   1 
ATOM   3242 O  O   . GLU B 2 424 ? 50.981  67.757  27.370 1.00 412.38 ? 424 GLU B O   1 
ATOM   3243 C  CB  . GLU B 2 424 ? 49.027  70.233  27.753 1.00 376.65 ? 424 GLU B CB  1 
ATOM   3244 C  CG  . GLU B 2 424 ? 47.697  70.967  27.538 1.00 444.53 ? 424 GLU B CG  1 
ATOM   3245 C  CD  . GLU B 2 424 ? 46.906  70.623  26.286 1.00 539.93 ? 424 GLU B CD  1 
ATOM   3246 O  OE1 . GLU B 2 424 ? 46.859  69.437  25.905 1.00 609.69 ? 424 GLU B OE1 1 
ATOM   3247 O  OE2 . GLU B 2 424 ? 46.321  71.557  25.687 1.00 569.65 ? 424 GLU B OE2 1 
ATOM   3248 N  N   . LEU B 2 425 ? 50.954  68.354  29.561 1.00 346.04 ? 425 LEU B N   1 
ATOM   3249 C  CA  . LEU B 2 425 ? 52.338  67.965  29.844 1.00 299.74 ? 425 LEU B CA  1 
ATOM   3250 C  C   . LEU B 2 425 ? 52.503  66.444  29.834 1.00 256.54 ? 425 LEU B C   1 
ATOM   3251 O  O   . LEU B 2 425 ? 51.646  65.714  30.336 1.00 224.64 ? 425 LEU B O   1 
ATOM   3252 C  CB  . LEU B 2 425 ? 52.763  68.517  31.208 1.00 297.79 ? 425 LEU B CB  1 
ATOM   3253 C  CG  . LEU B 2 425 ? 52.928  70.034  31.295 1.00 352.77 ? 425 LEU B CG  1 
ATOM   3254 C  CD1 . LEU B 2 425 ? 53.089  70.483  32.738 1.00 358.04 ? 425 LEU B CD1 1 
ATOM   3255 C  CD2 . LEU B 2 425 ? 54.124  70.500  30.475 1.00 418.97 ? 425 LEU B CD2 1 
ATOM   3256 N  N   . GLU B 2 426 ? 53.616  65.954  29.264 1.00 237.47 ? 426 GLU B N   1 
ATOM   3257 C  CA  . GLU B 2 426 ? 53.876  64.510  29.256 1.00 266.16 ? 426 GLU B CA  1 
ATOM   3258 C  C   . GLU B 2 426 ? 54.299  64.069  30.661 1.00 274.98 ? 426 GLU B C   1 
ATOM   3259 O  O   . GLU B 2 426 ? 54.940  64.825  31.393 1.00 336.87 ? 426 GLU B O   1 
ATOM   3260 C  CB  . GLU B 2 426 ? 54.901  64.112  28.187 1.00 303.02 ? 426 GLU B CB  1 
ATOM   3261 C  CG  . GLU B 2 426 ? 56.303  64.669  28.400 1.00 399.66 ? 426 GLU B CG  1 
ATOM   3262 C  CD  . GLU B 2 426 ? 57.215  64.592  27.183 1.00 449.89 ? 426 GLU B CD  1 
ATOM   3263 O  OE1 . GLU B 2 426 ? 57.291  63.506  26.574 1.00 472.60 ? 426 GLU B OE1 1 
ATOM   3264 O  OE2 . GLU B 2 426 ? 57.853  65.618  26.847 1.00 485.14 ? 426 GLU B OE2 1 
ATOM   3265 N  N   . ARG B 2 427 ? 53.933  62.827  31.045 1.00 285.59 ? 427 ARG B N   1 
ATOM   3266 C  CA  . ARG B 2 427 ? 54.165  62.277  32.383 1.00 261.00 ? 427 ARG B CA  1 
ATOM   3267 C  C   . ARG B 2 427 ? 54.559  60.799  32.237 1.00 243.50 ? 427 ARG B C   1 
ATOM   3268 O  O   . ARG B 2 427 ? 53.720  59.913  32.369 1.00 262.77 ? 427 ARG B O   1 
ATOM   3269 C  CB  . ARG B 2 427 ? 52.922  62.491  33.260 1.00 235.92 ? 427 ARG B CB  1 
ATOM   3270 C  CG  . ARG B 2 427 ? 52.498  63.941  33.471 1.00 213.12 ? 427 ARG B CG  1 
ATOM   3271 C  CD  . ARG B 2 427 ? 51.308  64.085  34.407 1.00 226.00 ? 427 ARG B CD  1 
ATOM   3272 N  NE  . ARG B 2 427 ? 51.074  65.406  34.985 1.00 256.06 ? 427 ARG B NE  1 
ATOM   3273 C  CZ  . ARG B 2 427 ? 50.517  66.449  34.363 1.00 246.96 ? 427 ARG B CZ  1 
ATOM   3274 N  NH1 . ARG B 2 427 ? 50.476  67.640  34.941 1.00 226.42 ? 427 ARG B NH1 1 
ATOM   3275 N  NH2 . ARG B 2 427 ? 50.010  66.329  33.150 1.00 252.84 ? 427 ARG B NH2 1 
ATOM   3276 N  N   . PRO B 2 428 ? 55.840  60.483  31.920 1.00 301.90 ? 428 PRO B N   1 
ATOM   3277 C  CA  . PRO B 2 428 ? 56.315  59.101  31.742 1.00 307.43 ? 428 PRO B CA  1 
ATOM   3278 C  C   . PRO B 2 428 ? 56.066  58.121  32.896 1.00 285.71 ? 428 PRO B C   1 
ATOM   3279 O  O   . PRO B 2 428 ? 56.078  56.916  32.651 1.00 227.28 ? 428 PRO B O   1 
ATOM   3280 C  CB  . PRO B 2 428 ? 57.833  59.276  31.520 1.00 349.83 ? 428 PRO B CB  1 
ATOM   3281 C  CG  . PRO B 2 428 ? 57.945  60.652  30.913 1.00 399.46 ? 428 PRO B CG  1 
ATOM   3282 C  CD  . PRO B 2 428 ? 56.910  61.460  31.665 1.00 368.73 ? 428 PRO B CD  1 
ATOM   3283 N  N   . ILE B 2 429 ? 55.847  58.631  34.126 1.00 284.59 ? 429 ILE B N   1 
ATOM   3284 C  CA  . ILE B 2 429 ? 55.230  57.862  35.207 1.00 286.85 ? 429 ILE B CA  1 
ATOM   3285 C  C   . ILE B 2 429 ? 54.264  58.764  35.984 1.00 275.40 ? 429 ILE B C   1 
ATOM   3286 O  O   . ILE B 2 429 ? 54.520  59.963  36.120 1.00 194.54 ? 429 ILE B O   1 
ATOM   3287 C  CB  . ILE B 2 429 ? 56.290  57.198  36.119 1.00 276.29 ? 429 ILE B CB  1 
ATOM   3288 C  CG1 . ILE B 2 429 ? 55.636  56.233  37.118 1.00 246.44 ? 429 ILE B CG1 1 
ATOM   3289 C  CG2 . ILE B 2 429 ? 57.172  58.244  36.804 1.00 265.95 ? 429 ILE B CG2 1 
ATOM   3290 C  CD1 . ILE B 2 429 ? 56.588  55.284  37.800 1.00 306.57 ? 429 ILE B CD1 1 
ATOM   3291 N  N   . LYS B 2 430 ? 53.157  58.166  36.485 1.00 278.64 ? 430 LYS B N   1 
ATOM   3292 C  CA  . LYS B 2 430 ? 52.145  58.855  37.281 1.00 247.66 ? 430 LYS B CA  1 
ATOM   3293 C  C   . LYS B 2 430 ? 51.792  58.050  38.531 1.00 271.75 ? 430 LYS B C   1 
ATOM   3294 O  O   . LYS B 2 430 ? 51.811  56.811  38.510 1.00 240.74 ? 430 LYS B O   1 
ATOM   3295 C  CB  . LYS B 2 430 ? 50.883  59.074  36.455 1.00 213.73 ? 430 LYS B CB  1 
ATOM   3296 C  CG  . LYS B 2 430 ? 51.035  60.101  35.355 1.00 283.03 ? 430 LYS B CG  1 
ATOM   3297 C  CD  . LYS B 2 430 ? 49.710  60.506  34.714 1.00 384.83 ? 430 LYS B CD  1 
ATOM   3298 C  CE  . LYS B 2 430 ? 48.987  59.380  34.000 1.00 432.38 ? 430 LYS B CE  1 
ATOM   3299 N  NZ  . LYS B 2 430 ? 47.723  59.849  33.384 1.00 447.99 ? 430 LYS B NZ  1 
ATOM   3300 N  N   . VAL B 2 431 ? 51.465  58.788  39.612 1.00 227.65 ? 431 VAL B N   1 
ATOM   3301 C  CA  . VAL B 2 431 ? 51.046  58.221  40.888 1.00 257.02 ? 431 VAL B CA  1 
ATOM   3302 C  C   . VAL B 2 431 ? 49.558  58.517  41.093 1.00 285.25 ? 431 VAL B C   1 
ATOM   3303 O  O   . VAL B 2 431 ? 49.072  59.593  40.721 1.00 251.31 ? 431 VAL B O   1 
ATOM   3304 C  CB  . VAL B 2 431 ? 51.935  58.718  42.048 1.00 295.51 ? 431 VAL B CB  1 
ATOM   3305 C  CG1 . VAL B 2 431 ? 51.450  58.239  43.400 1.00 353.12 ? 431 VAL B CG1 1 
ATOM   3306 C  CG2 . VAL B 2 431 ? 53.389  58.283  41.876 1.00 385.34 ? 431 VAL B CG2 1 
ATOM   3307 N  N   . ASN B 2 432 ? 48.856  57.535  41.695 1.00 316.66 ? 432 ASN B N   1 
ATOM   3308 C  CA  . ASN B 2 432 ? 47.421  57.587  41.967 1.00 260.22 ? 432 ASN B CA  1 
ATOM   3309 C  C   . ASN B 2 432 ? 47.163  58.698  42.994 1.00 232.45 ? 432 ASN B C   1 
ATOM   3310 O  O   . ASN B 2 432 ? 47.808  58.730  44.057 1.00 240.92 ? 432 ASN B O   1 
ATOM   3311 C  CB  . ASN B 2 432 ? 46.903  56.233  42.467 1.00 314.10 ? 432 ASN B CB  1 
ATOM   3312 C  CG  . ASN B 2 432 ? 47.363  55.027  41.661 1.00 351.21 ? 432 ASN B CG  1 
ATOM   3313 O  OD1 . ASN B 2 432 ? 47.692  55.146  40.483 1.00 367.58 ? 432 ASN B OD1 1 
ATOM   3314 N  ND2 . ASN B 2 432 ? 47.390  53.855  42.283 1.00 341.53 ? 432 ASN B ND2 1 
ATOM   3315 N  N   . LEU B 2 433 ? 46.230  59.619  42.688 1.00 211.62 ? 433 LEU B N   1 
ATOM   3316 C  CA  . LEU B 2 433 ? 46.180  60.948  43.314 1.00 247.07 ? 433 LEU B CA  1 
ATOM   3317 C  C   . LEU B 2 433 ? 45.966  60.898  44.838 1.00 266.69 ? 433 LEU B C   1 
ATOM   3318 O  O   . LEU B 2 433 ? 46.291  61.865  45.534 1.00 234.57 ? 433 LEU B O   1 
ATOM   3319 C  CB  . LEU B 2 433 ? 45.093  61.742  42.575 1.00 299.01 ? 433 LEU B CB  1 
ATOM   3320 C  CG  . LEU B 2 433 ? 44.888  63.198  42.996 1.00 336.42 ? 433 LEU B CG  1 
ATOM   3321 C  CD1 . LEU B 2 433 ? 44.665  64.083  41.780 1.00 411.62 ? 433 LEU B CD1 1 
ATOM   3322 C  CD2 . LEU B 2 433 ? 43.711  63.353  43.955 1.00 339.31 ? 433 LEU B CD2 1 
ATOM   3323 N  N   . ALA B 2 434 ? 45.431  59.786  45.376 1.00 277.62 ? 434 ALA B N   1 
ATOM   3324 C  CA  . ALA B 2 434 ? 45.296  59.566  46.814 1.00 270.34 ? 434 ALA B CA  1 
ATOM   3325 C  C   . ALA B 2 434 ? 46.624  59.723  47.568 1.00 267.85 ? 434 ALA B C   1 
ATOM   3326 O  O   . ALA B 2 434 ? 46.606  60.248  48.681 1.00 256.84 ? 434 ALA B O   1 
ATOM   3327 C  CB  . ALA B 2 434 ? 44.685  58.200  47.048 1.00 311.53 ? 434 ALA B CB  1 
ATOM   3328 N  N   . LEU B 2 435 ? 47.764  59.272  46.993 1.00 250.59 ? 435 LEU B N   1 
ATOM   3329 C  CA  . LEU B 2 435 ? 49.056  59.309  47.686 1.00 234.02 ? 435 LEU B CA  1 
ATOM   3330 C  C   . LEU B 2 435 ? 49.502  60.755  47.909 1.00 175.08 ? 435 LEU B C   1 
ATOM   3331 O  O   . LEU B 2 435 ? 49.777  61.115  49.044 1.00 155.56 ? 435 LEU B O   1 
ATOM   3332 C  CB  . LEU B 2 435 ? 50.115  58.463  46.958 1.00 175.72 ? 435 LEU B CB  1 
ATOM   3333 C  CG  . LEU B 2 435 ? 50.097  56.971  47.296 1.00 246.00 ? 435 LEU B CG  1 
ATOM   3334 C  CD1 . LEU B 2 435 ? 48.832  56.291  46.767 1.00 283.89 ? 435 LEU B CD1 1 
ATOM   3335 C  CD2 . LEU B 2 435 ? 51.352  56.285  46.760 1.00 264.10 ? 435 LEU B CD2 1 
ATOM   3336 N  N   . PRO B 2 436 ? 49.586  61.628  46.878 1.00 196.30 ? 436 PRO B N   1 
ATOM   3337 C  CA  . PRO B 2 436 ? 49.737  63.068  47.092 1.00 228.11 ? 436 PRO B CA  1 
ATOM   3338 C  C   . PRO B 2 436 ? 48.819  63.674  48.147 1.00 224.24 ? 436 PRO B C   1 
ATOM   3339 O  O   . PRO B 2 436 ? 49.321  64.406  48.993 1.00 253.33 ? 436 PRO B O   1 
ATOM   3340 C  CB  . PRO B 2 436 ? 49.447  63.668  45.718 1.00 260.31 ? 436 PRO B CB  1 
ATOM   3341 C  CG  . PRO B 2 436 ? 49.946  62.606  44.773 1.00 280.09 ? 436 PRO B CG  1 
ATOM   3342 C  CD  . PRO B 2 436 ? 49.596  61.299  45.448 1.00 235.65 ? 436 PRO B CD  1 
ATOM   3343 N  N   . VAL B 2 437 ? 47.518  63.353  48.135 1.00 209.97 ? 437 VAL B N   1 
ATOM   3344 C  CA  . VAL B 2 437 ? 46.580  63.963  49.078 1.00 290.36 ? 437 VAL B CA  1 
ATOM   3345 C  C   . VAL B 2 437 ? 46.861  63.496  50.516 1.00 262.77 ? 437 VAL B C   1 
ATOM   3346 O  O   . VAL B 2 437 ? 46.817  64.326  51.447 1.00 177.05 ? 437 VAL B O   1 
ATOM   3347 C  CB  . VAL B 2 437 ? 45.120  63.724  48.637 1.00 410.22 ? 437 VAL B CB  1 
ATOM   3348 C  CG1 . VAL B 2 437 ? 44.084  64.135  49.684 1.00 439.20 ? 437 VAL B CG1 1 
ATOM   3349 C  CG2 . VAL B 2 437 ? 44.840  64.444  47.331 1.00 473.88 ? 437 VAL B CG2 1 
ATOM   3350 N  N   . PHE B 2 438 ? 47.147  62.190  50.690 1.00 222.48 ? 438 PHE B N   1 
ATOM   3351 C  CA  . PHE B 2 438 ? 47.618  61.597  51.944 1.00 295.35 ? 438 PHE B CA  1 
ATOM   3352 C  C   . PHE B 2 438 ? 48.889  62.298  52.439 1.00 307.61 ? 438 PHE B C   1 
ATOM   3353 O  O   . PHE B 2 438 ? 49.006  62.631  53.613 1.00 327.29 ? 438 PHE B O   1 
ATOM   3354 C  CB  . PHE B 2 438 ? 47.800  60.088  51.715 1.00 261.96 ? 438 PHE B CB  1 
ATOM   3355 C  CG  . PHE B 2 438 ? 48.490  59.268  52.782 1.00 323.36 ? 438 PHE B CG  1 
ATOM   3356 C  CD1 . PHE B 2 438 ? 49.875  59.306  52.956 1.00 355.30 ? 438 PHE B CD1 1 
ATOM   3357 C  CD2 . PHE B 2 438 ? 47.752  58.429  53.609 1.00 370.21 ? 438 PHE B CD2 1 
ATOM   3358 C  CE1 . PHE B 2 438 ? 50.499  58.546  53.938 1.00 384.64 ? 438 PHE B CE1 1 
ATOM   3359 C  CE2 . PHE B 2 438 ? 48.378  57.666  54.589 1.00 460.07 ? 438 PHE B CE2 1 
ATOM   3360 C  CZ  . PHE B 2 438 ? 49.749  57.724  54.752 1.00 458.53 ? 438 PHE B CZ  1 
ATOM   3361 N  N   . PHE B 2 439 ? 49.840  62.523  51.530 1.00 253.77 ? 439 PHE B N   1 
ATOM   3362 C  CA  . PHE B 2 439 ? 51.120  63.145  51.846 1.00 186.29 ? 439 PHE B CA  1 
ATOM   3363 C  C   . PHE B 2 439 ? 50.962  64.626  52.210 1.00 148.25 ? 439 PHE B C   1 
ATOM   3364 O  O   . PHE B 2 439 ? 51.542  65.069  53.182 1.00 202.60 ? 439 PHE B O   1 
ATOM   3365 C  CB  . PHE B 2 439 ? 52.068  62.912  50.671 1.00 188.87 ? 439 PHE B CB  1 
ATOM   3366 C  CG  . PHE B 2 439 ? 53.467  63.427  50.889 1.00 149.16 ? 439 PHE B CG  1 
ATOM   3367 C  CD1 . PHE B 2 439 ? 54.293  62.851  51.823 1.00 155.33 ? 439 PHE B CD1 1 
ATOM   3368 C  CD2 . PHE B 2 439 ? 53.954  64.510  50.172 1.00 186.79 ? 439 PHE B CD2 1 
ATOM   3369 C  CE1 . PHE B 2 439 ? 55.577  63.333  52.038 1.00 194.48 ? 439 PHE B CE1 1 
ATOM   3370 C  CE2 . PHE B 2 439 ? 55.238  64.996  50.377 1.00 156.98 ? 439 PHE B CE2 1 
ATOM   3371 C  CZ  . PHE B 2 439 ? 56.055  64.405  51.305 1.00 170.63 ? 439 PHE B CZ  1 
ATOM   3372 N  N   . ILE B 2 440 ? 50.171  65.410  51.479 1.00 166.95 ? 440 ILE B N   1 
ATOM   3373 C  CA  . ILE B 2 440 ? 49.932  66.816  51.835 1.00 241.96 ? 440 ILE B CA  1 
ATOM   3374 C  C   . ILE B 2 440 ? 49.177  66.967  53.166 1.00 229.35 ? 440 ILE B C   1 
ATOM   3375 O  O   . ILE B 2 440 ? 49.498  67.865  53.945 1.00 200.88 ? 440 ILE B O   1 
ATOM   3376 C  CB  . ILE B 2 440 ? 49.201  67.568  50.705 1.00 287.87 ? 440 ILE B CB  1 
ATOM   3377 C  CG1 . ILE B 2 440 ? 50.058  67.637  49.435 1.00 254.61 ? 440 ILE B CG1 1 
ATOM   3378 C  CG2 . ILE B 2 440 ? 48.745  68.963  51.180 1.00 203.20 ? 440 ILE B CG2 1 
ATOM   3379 C  CD1 . ILE B 2 440 ? 51.400  68.269  49.642 1.00 226.83 ? 440 ILE B CD1 1 
ATOM   3380 N  N   . LEU B 2 441 ? 48.205  66.095  53.456 1.00 201.96 ? 441 LEU B N   1 
ATOM   3381 C  CA  . LEU B 2 441 ? 47.593  66.085  54.778 1.00 307.97 ? 441 LEU B CA  1 
ATOM   3382 C  C   . LEU B 2 441 ? 48.676  65.865  55.852 1.00 279.00 ? 441 LEU B C   1 
ATOM   3383 O  O   . LEU B 2 441 ? 48.778  66.650  56.801 1.00 218.74 ? 441 LEU B O   1 
ATOM   3384 C  CB  . LEU B 2 441 ? 46.481  65.024  54.825 1.00 403.75 ? 441 LEU B CB  1 
ATOM   3385 C  CG  . LEU B 2 441 ? 45.789  64.826  56.178 1.00 484.12 ? 441 LEU B CG  1 
ATOM   3386 C  CD1 . LEU B 2 441 ? 44.998  66.064  56.579 1.00 517.06 ? 441 LEU B CD1 1 
ATOM   3387 C  CD2 . LEU B 2 441 ? 44.885  63.604  56.154 1.00 481.84 ? 441 LEU B CD2 1 
ATOM   3388 N  N   . ALA B 2 442 ? 49.493  64.813  55.699 1.00 216.47 ? 442 ALA B N   1 
ATOM   3389 C  CA  . ALA B 2 442 ? 50.555  64.477  56.636 1.00 238.59 ? 442 ALA B CA  1 
ATOM   3390 C  C   . ALA B 2 442 ? 51.564  65.622  56.786 1.00 168.34 ? 442 ALA B C   1 
ATOM   3391 O  O   . ALA B 2 442 ? 52.032  65.886  57.890 1.00 247.53 ? 442 ALA B O   1 
ATOM   3392 C  CB  . ALA B 2 442 ? 51.202  63.167  56.201 1.00 234.97 ? 442 ALA B CB  1 
ATOM   3393 N  N   . CYS B 2 443 ? 51.935  66.303  55.702 1.00 163.86 ? 443 CYS B N   1 
ATOM   3394 C  CA  . CYS B 2 443 ? 52.840  67.443  55.778 1.00 262.57 ? 443 CYS B CA  1 
ATOM   3395 C  C   . CYS B 2 443 ? 52.226  68.596  56.575 1.00 171.32 ? 443 CYS B C   1 
ATOM   3396 O  O   . CYS B 2 443 ? 52.833  69.029  57.549 1.00 247.78 ? 443 CYS B O   1 
ATOM   3397 C  CB  . CYS B 2 443 ? 53.229  67.923  54.385 1.00 310.98 ? 443 CYS B CB  1 
ATOM   3398 S  SG  . CYS B 2 443 ? 54.274  66.752  53.486 1.00 171.55 ? 443 CYS B SG  1 
ATOM   3399 N  N   . LEU B 2 444 ? 51.050  69.081  56.188 1.00 151.48 ? 444 LEU B N   1 
ATOM   3400 C  CA  . LEU B 2 444 ? 50.480  70.276  56.786 1.00 218.66 ? 444 LEU B CA  1 
ATOM   3401 C  C   . LEU B 2 444 ? 50.086  70.037  58.249 1.00 308.36 ? 444 LEU B C   1 
ATOM   3402 O  O   . LEU B 2 444 ? 50.158  70.979  59.034 1.00 387.27 ? 444 LEU B O   1 
ATOM   3403 C  CB  . LEU B 2 444 ? 49.299  70.744  55.926 1.00 303.27 ? 444 LEU B CB  1 
ATOM   3404 C  CG  . LEU B 2 444 ? 49.680  71.254  54.537 1.00 362.40 ? 444 LEU B CG  1 
ATOM   3405 C  CD1 . LEU B 2 444 ? 48.432  71.563  53.725 1.00 423.65 ? 444 LEU B CD1 1 
ATOM   3406 C  CD2 . LEU B 2 444 ? 50.583  72.485  54.604 1.00 385.91 ? 444 LEU B CD2 1 
ATOM   3407 N  N   . PHE B 2 445 ? 49.689  68.805  58.614 1.00 305.85 ? 445 PHE B N   1 
ATOM   3408 C  CA  . PHE B 2 445 ? 49.556  68.361  60.003 1.00 313.64 ? 445 PHE B CA  1 
ATOM   3409 C  C   . PHE B 2 445 ? 50.866  68.577  60.775 1.00 240.08 ? 445 PHE B C   1 
ATOM   3410 O  O   . PHE B 2 445 ? 50.869  69.183  61.843 1.00 230.43 ? 445 PHE B O   1 
ATOM   3411 C  CB  . PHE B 2 445 ? 49.101  66.895  60.007 1.00 257.61 ? 445 PHE B CB  1 
ATOM   3412 C  CG  . PHE B 2 445 ? 48.863  66.218  61.339 1.00 285.70 ? 445 PHE B CG  1 
ATOM   3413 C  CD1 . PHE B 2 445 ? 48.580  66.935  62.502 1.00 311.92 ? 445 PHE B CD1 1 
ATOM   3414 C  CD2 . PHE B 2 445 ? 48.921  64.828  61.422 1.00 304.35 ? 445 PHE B CD2 1 
ATOM   3415 C  CE1 . PHE B 2 445 ? 48.357  66.279  63.707 1.00 344.17 ? 445 PHE B CE1 1 
ATOM   3416 C  CE2 . PHE B 2 445 ? 48.701  64.172  62.628 1.00 332.53 ? 445 PHE B CE2 1 
ATOM   3417 C  CZ  . PHE B 2 445 ? 48.420  64.899  63.769 1.00 371.55 ? 445 PHE B CZ  1 
ATOM   3418 N  N   . LEU B 2 446 ? 51.992  68.107  60.229 1.00 225.70 ? 446 LEU B N   1 
ATOM   3419 C  CA  . LEU B 2 446 ? 53.287  68.233  60.895 1.00 249.61 ? 446 LEU B CA  1 
ATOM   3420 C  C   . LEU B 2 446 ? 53.815  69.679  60.920 1.00 238.83 ? 446 LEU B C   1 
ATOM   3421 O  O   . LEU B 2 446 ? 54.504  70.033  61.870 1.00 237.29 ? 446 LEU B O   1 
ATOM   3422 C  CB  . LEU B 2 446 ? 54.269  67.248  60.247 1.00 221.97 ? 446 LEU B CB  1 
ATOM   3423 C  CG  . LEU B 2 446 ? 53.920  65.775  60.517 1.00 215.76 ? 446 LEU B CG  1 
ATOM   3424 C  CD1 . LEU B 2 446 ? 54.742  64.839  59.655 1.00 255.08 ? 446 LEU B CD1 1 
ATOM   3425 C  CD2 . LEU B 2 446 ? 54.117  65.384  61.983 1.00 303.24 ? 446 LEU B CD2 1 
ATOM   3426 N  N   . ILE B 2 447 ? 53.500  70.535  59.935 1.00 238.10 ? 447 ILE B N   1 
ATOM   3427 C  CA  . ILE B 2 447 ? 53.842  71.952  60.053 1.00 210.23 ? 447 ILE B CA  1 
ATOM   3428 C  C   . ILE B 2 447 ? 53.126  72.548  61.271 1.00 206.40 ? 447 ILE B C   1 
ATOM   3429 O  O   . ILE B 2 447 ? 53.746  73.275  62.042 1.00 234.14 ? 447 ILE B O   1 
ATOM   3430 C  CB  . ILE B 2 447 ? 53.529  72.799  58.794 1.00 259.75 ? 447 ILE B CB  1 
ATOM   3431 C  CG1 . ILE B 2 447 ? 54.013  72.216  57.462 1.00 238.57 ? 447 ILE B CG1 1 
ATOM   3432 C  CG2 . ILE B 2 447 ? 54.092  74.215  58.985 1.00 220.62 ? 447 ILE B CG2 1 
ATOM   3433 C  CD1 . ILE B 2 447 ? 55.473  71.917  57.428 1.00 327.52 ? 447 ILE B CD1 1 
ATOM   3434 N  N   . ALA B 2 448 ? 51.833  72.252  61.451 1.00 249.64 ? 448 ALA B N   1 
ATOM   3435 C  CA  . ALA B 2 448 ? 51.021  72.809  62.537 1.00 348.31 ? 448 ALA B CA  1 
ATOM   3436 C  C   . ALA B 2 448 ? 51.583  72.463  63.926 1.00 340.66 ? 448 ALA B C   1 
ATOM   3437 O  O   . ALA B 2 448 ? 51.492  73.301  64.831 1.00 449.93 ? 448 ALA B O   1 
ATOM   3438 C  CB  . ALA B 2 448 ? 49.571  72.372  62.376 1.00 340.48 ? 448 ALA B CB  1 
ATOM   3439 N  N   . VAL B 2 449 ? 52.182  71.269  64.103 1.00 195.83 ? 449 VAL B N   1 
ATOM   3440 C  CA  . VAL B 2 449 ? 52.798  70.855  65.366 1.00 220.63 ? 449 VAL B CA  1 
ATOM   3441 C  C   . VAL B 2 449 ? 53.837  71.867  65.853 1.00 224.91 ? 449 VAL B C   1 
ATOM   3442 O  O   . VAL B 2 449 ? 53.880  72.156  67.047 1.00 283.78 ? 449 VAL B O   1 
ATOM   3443 C  CB  . VAL B 2 449 ? 53.404  69.442  65.238 1.00 277.25 ? 449 VAL B CB  1 
ATOM   3444 C  CG1 . VAL B 2 449 ? 54.314  69.019  66.393 1.00 294.09 ? 449 VAL B CG1 1 
ATOM   3445 C  CG2 . VAL B 2 449 ? 52.274  68.449  65.058 1.00 336.59 ? 449 VAL B CG2 1 
ATOM   3446 N  N   . SER B 2 450 ? 54.657  72.407  64.940 1.00 228.49 ? 450 SER B N   1 
ATOM   3447 C  CA  . SER B 2 450 ? 55.700  73.369  65.280 1.00 200.50 ? 450 SER B CA  1 
ATOM   3448 C  C   . SER B 2 450 ? 55.160  74.551  66.083 1.00 207.80 ? 450 SER B C   1 
ATOM   3449 O  O   . SER B 2 450 ? 55.749  74.938  67.091 1.00 253.51 ? 450 SER B O   1 
ATOM   3450 C  CB  . SER B 2 450 ? 56.390  73.866  64.039 1.00 214.15 ? 450 SER B CB  1 
ATOM   3451 O  OG  . SER B 2 450 ? 55.567  74.720  63.283 1.00 150.60 ? 450 SER B OG  1 
ATOM   3452 N  N   . PHE B 2 451 ? 54.020  75.102  65.661 1.00 223.72 ? 451 PHE B N   1 
ATOM   3453 C  CA  . PHE B 2 451 ? 53.404  76.280  66.269 1.00 349.54 ? 451 PHE B CA  1 
ATOM   3454 C  C   . PHE B 2 451 ? 52.632  75.958  67.562 1.00 372.77 ? 451 PHE B C   1 
ATOM   3455 O  O   . PHE B 2 451 ? 52.247  76.886  68.278 1.00 373.02 ? 451 PHE B O   1 
ATOM   3456 C  CB  . PHE B 2 451 ? 52.539  76.959  65.198 1.00 369.86 ? 451 PHE B CB  1 
ATOM   3457 C  CG  . PHE B 2 451 ? 53.237  77.179  63.866 1.00 360.98 ? 451 PHE B CG  1 
ATOM   3458 C  CD1 . PHE B 2 451 ? 54.555  77.656  63.799 1.00 247.79 ? 451 PHE B CD1 1 
ATOM   3459 C  CD2 . PHE B 2 451 ? 52.585  76.896  62.662 1.00 408.00 ? 451 PHE B CD2 1 
ATOM   3460 C  CE1 . PHE B 2 451 ? 55.188  77.847  62.578 1.00 267.97 ? 451 PHE B CE1 1 
ATOM   3461 C  CE2 . PHE B 2 451 ? 53.224  77.091  61.439 1.00 404.41 ? 451 PHE B CE2 1 
ATOM   3462 C  CZ  . PHE B 2 451 ? 54.522  77.572  61.400 1.00 358.89 ? 451 PHE B CZ  1 
ATOM   3463 N  N   . TRP B 2 452 ? 52.394  74.671  67.874 1.00 317.81 ? 452 TRP B N   1 
ATOM   3464 C  CA  . TRP B 2 452 ? 51.854  74.257  69.164 1.00 239.30 ? 452 TRP B CA  1 
ATOM   3465 C  C   . TRP B 2 452 ? 52.982  74.034  70.171 1.00 270.26 ? 452 TRP B C   1 
ATOM   3466 O  O   . TRP B 2 452 ? 52.944  74.595  71.263 1.00 405.52 ? 452 TRP B O   1 
ATOM   3467 C  CB  . TRP B 2 452 ? 50.997  72.993  68.988 1.00 315.93 ? 452 TRP B CB  1 
ATOM   3468 C  CG  . TRP B 2 452 ? 50.278  72.494  70.223 1.00 385.10 ? 452 TRP B CG  1 
ATOM   3469 C  CD1 . TRP B 2 452 ? 50.027  73.184  71.375 1.00 362.09 ? 452 TRP B CD1 1 
ATOM   3470 C  CD2 . TRP B 2 452 ? 49.709  71.167  70.430 1.00 443.42 ? 452 TRP B CD2 1 
ATOM   3471 N  NE1 . TRP B 2 452 ? 49.351  72.392  72.272 1.00 333.55 ? 452 TRP B NE1 1 
ATOM   3472 C  CE2 . TRP B 2 452 ? 49.139  71.147  71.729 1.00 384.77 ? 452 TRP B CE2 1 
ATOM   3473 C  CE3 . TRP B 2 452 ? 49.620  69.992  69.656 1.00 462.17 ? 452 TRP B CE3 1 
ATOM   3474 C  CZ2 . TRP B 2 452 ? 48.505  70.004  72.250 1.00 384.21 ? 452 TRP B CZ2 1 
ATOM   3475 C  CZ3 . TRP B 2 452 ? 48.997  68.866  70.170 1.00 438.87 ? 452 TRP B CZ3 1 
ATOM   3476 C  CH2 . TRP B 2 452 ? 48.448  68.871  71.456 1.00 411.79 ? 452 TRP B CH2 1 
ATOM   3477 N  N   . LYS B 2 453 ? 53.990  73.219  69.820 1.00 302.15 ? 453 LYS B N   1 
ATOM   3478 C  CA  . LYS B 2 453 ? 55.026  72.764  70.755 1.00 307.14 ? 453 LYS B CA  1 
ATOM   3479 C  C   . LYS B 2 453 ? 56.206  73.737  70.885 1.00 276.33 ? 453 LYS B C   1 
ATOM   3480 O  O   . LYS B 2 453 ? 56.810  73.782  71.964 1.00 286.25 ? 453 LYS B O   1 
ATOM   3481 C  CB  . LYS B 2 453 ? 55.574  71.395  70.339 1.00 300.83 ? 453 LYS B CB  1 
ATOM   3482 C  CG  . LYS B 2 453 ? 54.528  70.321  70.063 1.00 325.94 ? 453 LYS B CG  1 
ATOM   3483 C  CD  . LYS B 2 453 ? 53.557  70.062  71.187 1.00 236.89 ? 453 LYS B CD  1 
ATOM   3484 C  CE  . LYS B 2 453 ? 52.712  68.848  70.897 1.00 231.18 ? 453 LYS B CE  1 
ATOM   3485 N  NZ  . LYS B 2 453 ? 51.749  68.596  72.001 1.00 299.49 ? 453 LYS B NZ  1 
ATOM   3486 N  N   . THR B 2 454 ? 56.526  74.493  69.811 1.00 199.62 ? 454 THR B N   1 
ATOM   3487 C  CA  . THR B 2 454 ? 57.695  75.372  69.748 1.00 243.60 ? 454 THR B CA  1 
ATOM   3488 C  C   . THR B 2 454 ? 57.467  76.607  68.849 1.00 288.35 ? 454 THR B C   1 
ATOM   3489 O  O   . THR B 2 454 ? 58.207  76.822  67.883 1.00 231.11 ? 454 THR B O   1 
ATOM   3490 C  CB  . THR B 2 454 ? 58.915  74.567  69.278 1.00 296.41 ? 454 THR B CB  1 
ATOM   3491 O  OG1 . THR B 2 454 ? 58.601  73.957  68.028 1.00 335.32 ? 454 THR B OG1 1 
ATOM   3492 C  CG2 . THR B 2 454 ? 59.345  73.459  70.213 1.00 298.27 ? 454 THR B CG2 1 
ATOM   3493 N  N   . PRO B 2 455 ? 56.453  77.478  69.108 1.00 394.35 ? 455 PRO B N   1 
ATOM   3494 C  CA  . PRO B 2 455 ? 56.245  78.706  68.328 1.00 409.73 ? 455 PRO B CA  1 
ATOM   3495 C  C   . PRO B 2 455 ? 57.208  79.853  68.638 1.00 402.14 ? 455 PRO B C   1 
ATOM   3496 O  O   . PRO B 2 455 ? 57.321  80.781  67.841 1.00 399.79 ? 455 PRO B O   1 
ATOM   3497 C  CB  . PRO B 2 455 ? 54.827  79.169  68.726 1.00 331.61 ? 455 PRO B CB  1 
ATOM   3498 C  CG  . PRO B 2 455 ? 54.678  78.680  70.140 1.00 340.37 ? 455 PRO B CG  1 
ATOM   3499 C  CD  . PRO B 2 455 ? 55.435  77.362  70.161 1.00 422.71 ? 455 PRO B CD  1 
ATOM   3500 N  N   . VAL B 2 456 ? 57.916  79.771  69.780 1.00 477.76 ? 456 VAL B N   1 
ATOM   3501 C  CA  . VAL B 2 456 ? 58.531  80.910  70.465 1.00 532.99 ? 456 VAL B CA  1 
ATOM   3502 C  C   . VAL B 2 456 ? 59.617  81.567  69.595 1.00 481.31 ? 456 VAL B C   1 
ATOM   3503 O  O   . VAL B 2 456 ? 59.757  82.798  69.605 1.00 488.66 ? 456 VAL B O   1 
ATOM   3504 C  CB  . VAL B 2 456 ? 59.091  80.492  71.847 1.00 575.36 ? 456 VAL B CB  1 
ATOM   3505 C  CG1 . VAL B 2 456 ? 59.519  81.695  72.688 1.00 563.88 ? 456 VAL B CG1 1 
ATOM   3506 C  CG2 . VAL B 2 456 ? 58.107  79.644  72.656 1.00 580.87 ? 456 VAL B CG2 1 
ATOM   3507 N  N   . GLU B 2 457 ? 60.368  80.750  68.838 1.00 363.02 ? 457 GLU B N   1 
ATOM   3508 C  CA  . GLU B 2 457 ? 61.480  81.201  68.009 1.00 258.74 ? 457 GLU B CA  1 
ATOM   3509 C  C   . GLU B 2 457 ? 61.020  81.839  66.693 1.00 253.48 ? 457 GLU B C   1 
ATOM   3510 O  O   . GLU B 2 457 ? 61.794  82.580  66.075 1.00 243.50 ? 457 GLU B O   1 
ATOM   3511 C  CB  . GLU B 2 457 ? 62.377  80.008  67.655 1.00 264.36 ? 457 GLU B CB  1 
ATOM   3512 C  CG  . GLU B 2 457 ? 62.978  79.258  68.837 1.00 333.38 ? 457 GLU B CG  1 
ATOM   3513 C  CD  . GLU B 2 457 ? 62.105  78.213  69.525 1.00 408.25 ? 457 GLU B CD  1 
ATOM   3514 O  OE1 . GLU B 2 457 ? 60.915  78.099  69.203 1.00 248.92 ? 457 GLU B OE1 1 
ATOM   3515 O  OE2 . GLU B 2 457 ? 62.639  77.491  70.401 1.00 502.98 ? 457 GLU B OE2 1 
ATOM   3516 N  N   . CYS B 2 458 ? 59.782  81.549  66.257 1.00 291.39 ? 458 CYS B N   1 
ATOM   3517 C  CA  . CYS B 2 458 ? 59.390  81.558  64.851 1.00 304.55 ? 458 CYS B CA  1 
ATOM   3518 C  C   . CYS B 2 458 ? 59.622  82.922  64.192 1.00 287.90 ? 458 CYS B C   1 
ATOM   3519 O  O   . CYS B 2 458 ? 60.070  82.953  63.038 1.00 326.46 ? 458 CYS B O   1 
ATOM   3520 C  CB  . CYS B 2 458 ? 57.939  81.097  64.750 1.00 369.50 ? 458 CYS B CB  1 
ATOM   3521 S  SG  . CYS B 2 458 ? 57.374  80.949  63.038 1.00 530.55 ? 458 CYS B SG  1 
ATOM   3522 N  N   . GLY B 2 459 ? 59.339  84.032  64.912 1.00 260.97 ? 459 GLY B N   1 
ATOM   3523 C  CA  . GLY B 2 459 ? 59.519  85.403  64.426 1.00 284.24 ? 459 GLY B CA  1 
ATOM   3524 C  C   . GLY B 2 459 ? 60.937  85.735  63.933 1.00 314.06 ? 459 GLY B C   1 
ATOM   3525 O  O   . GLY B 2 459 ? 61.093  86.499  62.981 1.00 293.80 ? 459 GLY B O   1 
ATOM   3526 N  N   . ILE B 2 460 ? 61.970  85.165  64.572 1.00 299.34 ? 460 ILE B N   1 
ATOM   3527 C  CA  . ILE B 2 460 ? 63.368  85.371  64.190 1.00 234.88 ? 460 ILE B CA  1 
ATOM   3528 C  C   . ILE B 2 460 ? 63.619  84.752  62.810 1.00 225.96 ? 460 ILE B C   1 
ATOM   3529 O  O   . ILE B 2 460 ? 64.290  85.376  62.000 1.00 171.66 ? 460 ILE B O   1 
ATOM   3530 C  CB  . ILE B 2 460 ? 64.326  84.816  65.275 1.00 279.81 ? 460 ILE B CB  1 
ATOM   3531 C  CG1 . ILE B 2 460 ? 64.101  85.482  66.639 1.00 342.12 ? 460 ILE B CG1 1 
ATOM   3532 C  CG2 . ILE B 2 460 ? 65.794  84.917  64.854 1.00 274.08 ? 460 ILE B CG2 1 
ATOM   3533 C  CD1 . ILE B 2 460 ? 64.685  84.727  67.827 1.00 341.07 ? 460 ILE B CD1 1 
ATOM   3534 N  N   . GLY B 2 461 ? 63.082  83.536  62.537 1.00 271.97 ? 461 GLY B N   1 
ATOM   3535 C  CA  . GLY B 2 461 ? 63.147  82.893  61.209 1.00 318.05 ? 461 GLY B CA  1 
ATOM   3536 C  C   . GLY B 2 461 ? 62.285  83.618  60.181 1.00 274.59 ? 461 GLY B C   1 
ATOM   3537 O  O   . GLY B 2 461 ? 62.766  83.954  59.106 1.00 243.34 ? 461 GLY B O   1 
ATOM   3538 N  N   . PHE B 2 462 ? 61.019  83.887  60.520 1.00 243.81 ? 462 PHE B N   1 
ATOM   3539 C  CA  . PHE B 2 462 ? 60.070  84.538  59.619 1.00 242.33 ? 462 PHE B CA  1 
ATOM   3540 C  C   . PHE B 2 462 ? 60.514  85.951  59.187 1.00 224.18 ? 462 PHE B C   1 
ATOM   3541 O  O   . PHE B 2 462 ? 60.212  86.371  58.062 1.00 304.05 ? 462 PHE B O   1 
ATOM   3542 C  CB  . PHE B 2 462 ? 58.670  84.538  60.243 1.00 261.60 ? 462 PHE B CB  1 
ATOM   3543 C  CG  . PHE B 2 462 ? 57.562  84.499  59.222 1.00 277.35 ? 462 PHE B CG  1 
ATOM   3544 C  CD1 . PHE B 2 462 ? 57.083  85.674  58.648 1.00 373.79 ? 462 PHE B CD1 1 
ATOM   3545 C  CD2 . PHE B 2 462 ? 57.012  83.287  58.812 1.00 259.47 ? 462 PHE B CD2 1 
ATOM   3546 C  CE1 . PHE B 2 462 ? 56.065  85.636  57.702 1.00 418.21 ? 462 PHE B CE1 1 
ATOM   3547 C  CE2 . PHE B 2 462 ? 55.996  83.250  57.866 1.00 350.97 ? 462 PHE B CE2 1 
ATOM   3548 C  CZ  . PHE B 2 462 ? 55.524  84.425  57.311 1.00 424.05 ? 462 PHE B CZ  1 
ATOM   3549 N  N   . THR B 2 463 ? 61.252  86.678  60.034 1.00 161.30 ? 463 THR B N   1 
ATOM   3550 C  CA  . THR B 2 463 ? 61.903  87.924  59.651 1.00 199.48 ? 463 THR B CA  1 
ATOM   3551 C  C   . THR B 2 463 ? 62.799  87.758  58.421 1.00 215.12 ? 463 THR B C   1 
ATOM   3552 O  O   . THR B 2 463 ? 62.817  88.655  57.578 1.00 228.89 ? 463 THR B O   1 
ATOM   3553 C  CB  . THR B 2 463 ? 62.733  88.505  60.815 1.00 263.64 ? 463 THR B CB  1 
ATOM   3554 O  OG1 . THR B 2 463 ? 61.817  88.853  61.853 1.00 280.69 ? 463 THR B OG1 1 
ATOM   3555 C  CG2 . THR B 2 463 ? 63.576  89.724  60.486 1.00 236.98 ? 463 THR B CG2 1 
ATOM   3556 N  N   . ILE B 2 464 ? 63.548  86.644  58.307 1.00 177.38 ? 464 ILE B N   1 
ATOM   3557 C  CA  . ILE B 2 464 ? 64.472  86.458  57.196 1.00 211.67 ? 464 ILE B CA  1 
ATOM   3558 C  C   . ILE B 2 464 ? 63.674  86.156  55.926 1.00 187.11 ? 464 ILE B C   1 
ATOM   3559 O  O   . ILE B 2 464 ? 64.029  86.659  54.847 1.00 172.12 ? 464 ILE B O   1 
ATOM   3560 C  CB  . ILE B 2 464 ? 65.557  85.391  57.463 1.00 172.57 ? 464 ILE B CB  1 
ATOM   3561 C  CG1 . ILE B 2 464 ? 66.178  85.470  58.862 1.00 196.72 ? 464 ILE B CG1 1 
ATOM   3562 C  CG2 . ILE B 2 464 ? 66.650  85.485  56.395 1.00 234.85 ? 464 ILE B CG2 1 
ATOM   3563 C  CD1 . ILE B 2 464 ? 66.807  86.834  59.197 1.00 269.71 ? 464 ILE B CD1 1 
ATOM   3564 N  N   . ILE B 2 465 ? 62.605  85.352  56.044 1.00 133.35 ? 465 ILE B N   1 
ATOM   3565 C  CA  . ILE B 2 465 ? 61.734  85.063  54.903 1.00 174.06 ? 465 ILE B CA  1 
ATOM   3566 C  C   . ILE B 2 465 ? 61.222  86.386  54.337 1.00 168.57 ? 465 ILE B C   1 
ATOM   3567 O  O   . ILE B 2 465 ? 61.375  86.627  53.144 1.00 172.79 ? 465 ILE B O   1 
ATOM   3568 C  CB  . ILE B 2 465 ? 60.601  84.081  55.282 1.00 239.69 ? 465 ILE B CB  1 
ATOM   3569 C  CG1 . ILE B 2 465 ? 61.146  82.705  55.695 1.00 226.61 ? 465 ILE B CG1 1 
ATOM   3570 C  CG2 . ILE B 2 465 ? 59.575  83.951  54.151 1.00 221.18 ? 465 ILE B CG2 1 
ATOM   3571 C  CD1 . ILE B 2 465 ? 60.157  81.827  56.446 1.00 289.35 ? 465 ILE B CD1 1 
ATOM   3572 N  N   . LEU B 2 466 ? 60.629  87.240  55.179 1.00 214.52 ? 466 LEU B N   1 
ATOM   3573 C  CA  . LEU B 2 466 ? 60.153  88.553  54.747 1.00 267.47 ? 466 LEU B CA  1 
ATOM   3574 C  C   . LEU B 2 466 ? 61.294  89.455  54.237 1.00 259.03 ? 466 LEU B C   1 
ATOM   3575 O  O   . LEU B 2 466 ? 61.095  90.233  53.317 1.00 316.36 ? 466 LEU B O   1 
ATOM   3576 C  CB  . LEU B 2 466 ? 59.369  89.213  55.887 1.00 298.55 ? 466 LEU B CB  1 
ATOM   3577 C  CG  . LEU B 2 466 ? 58.062  88.520  56.297 1.00 293.92 ? 466 LEU B CG  1 
ATOM   3578 C  CD1 . LEU B 2 466 ? 57.436  89.259  57.472 1.00 359.48 ? 466 LEU B CD1 1 
ATOM   3579 C  CD2 . LEU B 2 466 ? 57.063  88.420  55.145 1.00 308.11 ? 466 LEU B CD2 1 
ATOM   3580 N  N   . SER B 2 467 ? 62.508  89.356  54.791 1.00 178.44 ? 467 SER B N   1 
ATOM   3581 C  CA  . SER B 2 467 ? 63.683  90.058  54.274 1.00 233.28 ? 467 SER B CA  1 
ATOM   3582 C  C   . SER B 2 467 ? 64.114  89.605  52.863 1.00 204.17 ? 467 SER B C   1 
ATOM   3583 O  O   . SER B 2 467 ? 64.958  90.254  52.243 1.00 194.61 ? 467 SER B O   1 
ATOM   3584 C  CB  . SER B 2 467 ? 64.839  89.972  55.247 1.00 297.71 ? 467 SER B CB  1 
ATOM   3585 O  OG  . SER B 2 467 ? 64.472  90.513  56.508 1.00 298.89 ? 467 SER B OG  1 
ATOM   3586 N  N   . GLY B 2 468 ? 63.538  88.519  52.331 1.00 201.64 ? 468 GLY B N   1 
ATOM   3587 C  CA  . GLY B 2 468 ? 63.655  88.147  50.923 1.00 282.04 ? 468 GLY B CA  1 
ATOM   3588 C  C   . GLY B 2 468 ? 62.972  89.094  49.936 1.00 264.33 ? 468 GLY B C   1 
ATOM   3589 O  O   . GLY B 2 468 ? 63.446  89.228  48.803 1.00 277.20 ? 468 GLY B O   1 
ATOM   3590 N  N   . LEU B 2 469 ? 61.883  89.765  50.356 1.00 187.23 ? 469 LEU B N   1 
ATOM   3591 C  CA  . LEU B 2 469 ? 61.139  90.656  49.470 1.00 176.54 ? 469 LEU B CA  1 
ATOM   3592 C  C   . LEU B 2 469 ? 61.972  91.888  49.046 1.00 185.63 ? 469 LEU B C   1 
ATOM   3593 O  O   . LEU B 2 469 ? 62.085  92.132  47.840 1.00 155.39 ? 469 LEU B O   1 
ATOM   3594 C  CB  . LEU B 2 469 ? 59.791  91.031  50.113 1.00 179.63 ? 469 LEU B CB  1 
ATOM   3595 C  CG  . LEU B 2 469 ? 58.699  89.944  50.074 1.00 242.52 ? 469 LEU B CG  1 
ATOM   3596 C  CD1 . LEU B 2 469 ? 58.743  89.040  51.279 1.00 223.97 ? 469 LEU B CD1 1 
ATOM   3597 C  CD2 . LEU B 2 469 ? 57.291  90.539  49.983 1.00 277.54 ? 469 LEU B CD2 1 
ATOM   3598 N  N   . PRO B 2 470 ? 62.574  92.709  49.952 1.00 163.71 ? 470 PRO B N   1 
ATOM   3599 C  CA  . PRO B 2 470 ? 63.445  93.830  49.586 1.00 221.93 ? 470 PRO B CA  1 
ATOM   3600 C  C   . PRO B 2 470 ? 64.515  93.528  48.553 1.00 194.91 ? 470 PRO B C   1 
ATOM   3601 O  O   . PRO B 2 470 ? 64.681  94.270  47.582 1.00 297.30 ? 470 PRO B O   1 
ATOM   3602 C  CB  . PRO B 2 470 ? 64.157  94.182  50.904 1.00 264.06 ? 470 PRO B CB  1 
ATOM   3603 C  CG  . PRO B 2 470 ? 63.039  93.963  51.900 1.00 320.54 ? 470 PRO B CG  1 
ATOM   3604 C  CD  . PRO B 2 470 ? 62.460  92.652  51.402 1.00 210.17 ? 470 PRO B CD  1 
ATOM   3605 N  N   . VAL B 2 471 ? 65.228  92.425  48.777 1.00 188.39 ? 471 VAL B N   1 
ATOM   3606 C  CA  . VAL B 2 471 ? 66.323  92.026  47.894 1.00 244.61 ? 471 VAL B CA  1 
ATOM   3607 C  C   . VAL B 2 471 ? 65.781  91.588  46.525 1.00 183.29 ? 471 VAL B C   1 
ATOM   3608 O  O   . VAL B 2 471 ? 66.443  91.832  45.516 1.00 215.19 ? 471 VAL B O   1 
ATOM   3609 C  CB  . VAL B 2 471 ? 67.207  90.953  48.550 1.00 307.23 ? 471 VAL B CB  1 
ATOM   3610 C  CG1 . VAL B 2 471 ? 68.367  90.561  47.639 1.00 282.97 ? 471 VAL B CG1 1 
ATOM   3611 C  CG2 . VAL B 2 471 ? 67.708  91.438  49.912 1.00 371.82 ? 471 VAL B CG2 1 
ATOM   3612 N  N   . TYR B 2 472 ? 64.593  90.978  46.466 1.00 136.94 ? 472 TYR B N   1 
ATOM   3613 C  CA  . TYR B 2 472 ? 63.957  90.675  45.192 1.00 217.64 ? 472 TYR B CA  1 
ATOM   3614 C  C   . TYR B 2 472 ? 63.717  91.941  44.356 1.00 218.02 ? 472 TYR B C   1 
ATOM   3615 O  O   . TYR B 2 472 ? 64.017  91.987  43.157 1.00 170.27 ? 472 TYR B O   1 
ATOM   3616 C  CB  . TYR B 2 472 ? 62.636  89.926  45.397 1.00 226.41 ? 472 TYR B CB  1 
ATOM   3617 C  CG  . TYR B 2 472 ? 61.981  89.603  44.064 1.00 239.48 ? 472 TYR B CG  1 
ATOM   3618 C  CD1 . TYR B 2 472 ? 62.486  88.590  43.237 1.00 263.77 ? 472 TYR B CD1 1 
ATOM   3619 C  CD2 . TYR B 2 472 ? 60.880  90.325  43.625 1.00 253.86 ? 472 TYR B CD2 1 
ATOM   3620 C  CE1 . TYR B 2 472 ? 61.891  88.303  42.018 1.00 178.31 ? 472 TYR B CE1 1 
ATOM   3621 C  CE2 . TYR B 2 472 ? 60.289  90.049  42.402 1.00 317.18 ? 472 TYR B CE2 1 
ATOM   3622 C  CZ  . TYR B 2 472 ? 60.791  89.030  41.604 1.00 273.11 ? 472 TYR B CZ  1 
ATOM   3623 O  OH  . TYR B 2 472 ? 60.223  88.729  40.397 1.00 346.62 ? 472 TYR B OH  1 
ATOM   3624 N  N   . PHE B 2 473 ? 63.166  92.981  44.986 1.00 201.58 ? 473 PHE B N   1 
ATOM   3625 C  CA  . PHE B 2 473 ? 62.851  94.198  44.249 1.00 231.40 ? 473 PHE B CA  1 
ATOM   3626 C  C   . PHE B 2 473 ? 64.122  94.845  43.686 1.00 267.30 ? 473 PHE B C   1 
ATOM   3627 O  O   . PHE B 2 473 ? 64.204  95.036  42.474 1.00 369.36 ? 473 PHE B O   1 
ATOM   3628 C  CB  . PHE B 2 473 ? 62.003  95.140  45.107 1.00 235.80 ? 473 PHE B CB  1 
ATOM   3629 C  CG  . PHE B 2 473 ? 60.592  94.638  45.312 1.00 273.78 ? 473 PHE B CG  1 
ATOM   3630 C  CD1 . PHE B 2 473 ? 59.745  94.424  44.225 1.00 301.98 ? 473 PHE B CD1 1 
ATOM   3631 C  CD2 . PHE B 2 473 ? 60.099  94.378  46.587 1.00 327.71 ? 473 PHE B CD2 1 
ATOM   3632 C  CE1 . PHE B 2 473 ? 58.447  93.960  44.413 1.00 338.07 ? 473 PHE B CE1 1 
ATOM   3633 C  CE2 . PHE B 2 473 ? 58.799  93.919  46.771 1.00 310.57 ? 473 PHE B CE2 1 
ATOM   3634 C  CZ  . PHE B 2 473 ? 57.975  93.710  45.685 1.00 309.89 ? 473 PHE B CZ  1 
ATOM   3635 N  N   . PHE B 2 474 ? 65.101  95.164  44.543 1.00 214.34 ? 474 PHE B N   1 
ATOM   3636 C  CA  . PHE B 2 474 ? 66.353  95.794  44.129 1.00 242.13 ? 474 PHE B CA  1 
ATOM   3637 C  C   . PHE B 2 474 ? 67.201  94.916  43.185 1.00 170.66 ? 474 PHE B C   1 
ATOM   3638 O  O   . PHE B 2 474 ? 67.849  95.430  42.270 1.00 248.72 ? 474 PHE B O   1 
ATOM   3639 C  CB  . PHE B 2 474 ? 67.149  96.188  45.376 1.00 274.69 ? 474 PHE B CB  1 
ATOM   3640 C  CG  . PHE B 2 474 ? 68.545  96.709  45.119 1.00 304.14 ? 474 PHE B CG  1 
ATOM   3641 C  CD1 . PHE B 2 474 ? 68.745  97.961  44.548 1.00 330.47 ? 474 PHE B CD1 1 
ATOM   3642 C  CD2 . PHE B 2 474 ? 69.667  95.948  45.441 1.00 320.27 ? 474 PHE B CD2 1 
ATOM   3643 C  CE1 . PHE B 2 474 ? 70.029  98.438  44.310 1.00 368.92 ? 474 PHE B CE1 1 
ATOM   3644 C  CE2 . PHE B 2 474 ? 70.950  96.426  45.205 1.00 282.28 ? 474 PHE B CE2 1 
ATOM   3645 C  CZ  . PHE B 2 474 ? 71.128  97.669  44.640 1.00 347.97 ? 474 PHE B CZ  1 
ATOM   3646 N  N   . GLY B 2 475 ? 67.211  93.606  43.390 1.00 203.99 ? 475 GLY B N   1 
ATOM   3647 C  CA  . GLY B 2 475 ? 68.080  92.710  42.636 1.00 319.36 ? 475 GLY B CA  1 
ATOM   3648 C  C   . GLY B 2 475 ? 67.500  92.185  41.319 1.00 298.71 ? 475 GLY B C   1 
ATOM   3649 O  O   . GLY B 2 475 ? 68.282  91.820  40.433 1.00 288.99 ? 475 GLY B O   1 
ATOM   3650 N  N   . VAL B 2 476 ? 66.153  92.114  41.200 1.00 239.39 ? 476 VAL B N   1 
ATOM   3651 C  CA  . VAL B 2 476 ? 65.519  91.299  40.160 1.00 279.60 ? 476 VAL B CA  1 
ATOM   3652 C  C   . VAL B 2 476 ? 64.419  92.069  39.421 1.00 273.76 ? 476 VAL B C   1 
ATOM   3653 O  O   . VAL B 2 476 ? 64.406  92.045  38.184 1.00 363.12 ? 476 VAL B O   1 
ATOM   3654 C  CB  . VAL B 2 476 ? 65.018  89.949  40.719 1.00 306.58 ? 476 VAL B CB  1 
ATOM   3655 C  CG1 . VAL B 2 476 ? 64.381  89.092  39.630 1.00 365.17 ? 476 VAL B CG1 1 
ATOM   3656 C  CG2 . VAL B 2 476 ? 66.147  89.169  41.407 1.00 336.16 ? 476 VAL B CG2 1 
ATOM   3657 N  N   . TRP B 2 477 ? 63.511  92.740  40.140 1.00 231.04 ? 477 TRP B N   1 
ATOM   3658 C  CA  . TRP B 2 477 ? 62.425  93.500  39.512 1.00 287.67 ? 477 TRP B CA  1 
ATOM   3659 C  C   . TRP B 2 477 ? 62.849  94.883  38.960 1.00 307.49 ? 477 TRP B C   1 
ATOM   3660 O  O   . TRP B 2 477 ? 62.336  95.334  37.932 1.00 219.91 ? 477 TRP B O   1 
ATOM   3661 C  CB  . TRP B 2 477 ? 61.297  93.602  40.547 1.00 262.55 ? 477 TRP B CB  1 
ATOM   3662 C  CG  . TRP B 2 477 ? 60.113  94.452  40.162 1.00 299.94 ? 477 TRP B CG  1 
ATOM   3663 C  CD1 . TRP B 2 477 ? 58.943  94.008  39.613 1.00 293.78 ? 477 TRP B CD1 1 
ATOM   3664 C  CD2 . TRP B 2 477 ? 59.973  95.890  40.315 1.00 326.99 ? 477 TRP B CD2 1 
ATOM   3665 N  NE1 . TRP B 2 477 ? 58.092  95.061  39.406 1.00 296.52 ? 477 TRP B NE1 1 
ATOM   3666 C  CE2 . TRP B 2 477 ? 58.691  96.230  39.822 1.00 358.28 ? 477 TRP B CE2 1 
ATOM   3667 C  CE3 . TRP B 2 477 ? 60.799  96.922  40.804 1.00 313.35 ? 477 TRP B CE3 1 
ATOM   3668 C  CZ2 . TRP B 2 477 ? 58.229  97.556  39.819 1.00 417.55 ? 477 TRP B CZ2 1 
ATOM   3669 C  CZ3 . TRP B 2 477 ? 60.345  98.227  40.798 1.00 350.28 ? 477 TRP B CZ3 1 
ATOM   3670 C  CH2 . TRP B 2 477 ? 59.072  98.537  40.312 1.00 401.72 ? 477 TRP B CH2 1 
ATOM   3671 N  N   . TRP B 2 478 ? 63.786  95.558  39.640 1.00 314.54 ? 478 TRP B N   1 
ATOM   3672 C  CA  . TRP B 2 478 ? 64.270  96.906  39.319 1.00 244.27 ? 478 TRP B CA  1 
ATOM   3673 C  C   . TRP B 2 478 ? 65.005  97.034  37.977 1.00 280.27 ? 478 TRP B C   1 
ATOM   3674 O  O   . TRP B 2 478 ? 64.948  98.090  37.365 1.00 268.52 ? 478 TRP B O   1 
ATOM   3675 C  CB  . TRP B 2 478 ? 65.202  97.305  40.469 1.00 326.90 ? 478 TRP B CB  1 
ATOM   3676 C  CG  . TRP B 2 478 ? 65.947  98.614  40.402 1.00 324.57 ? 478 TRP B CG  1 
ATOM   3677 C  CD1 . TRP B 2 478 ? 67.306  98.738  40.391 1.00 315.26 ? 478 TRP B CD1 1 
ATOM   3678 C  CD2 . TRP B 2 478 ? 65.418  99.968  40.395 1.00 387.45 ? 478 TRP B CD2 1 
ATOM   3679 N  NE1 . TRP B 2 478 ? 67.659  100.062 40.361 1.00 348.34 ? 478 TRP B NE1 1 
ATOM   3680 C  CE2 . TRP B 2 478 ? 66.531  100.847 40.363 1.00 417.61 ? 478 TRP B CE2 1 
ATOM   3681 C  CE3 . TRP B 2 478 ? 64.126  100.522 40.411 1.00 391.57 ? 478 TRP B CE3 1 
ATOM   3682 C  CZ2 . TRP B 2 478 ? 66.373  102.245 40.346 1.00 451.75 ? 478 TRP B CZ2 1 
ATOM   3683 C  CZ3 . TRP B 2 478 ? 63.971  101.897 40.394 1.00 401.79 ? 478 TRP B CZ3 1 
ATOM   3684 C  CH2 . TRP B 2 478 ? 65.083  102.746 40.363 1.00 433.90 ? 478 TRP B CH2 1 
ATOM   3685 N  N   . LYS B 2 479 ? 65.701  95.972  37.531 1.00 418.34 ? 479 LYS B N   1 
ATOM   3686 C  CA  . LYS B 2 479 ? 66.519  95.926  36.309 1.00 456.41 ? 479 LYS B CA  1 
ATOM   3687 C  C   . LYS B 2 479 ? 67.593  97.033  36.248 1.00 437.81 ? 479 LYS B C   1 
ATOM   3688 O  O   . LYS B 2 479 ? 67.836  97.600  35.182 1.00 317.78 ? 479 LYS B O   1 
ATOM   3689 C  CB  . LYS B 2 479 ? 65.612  95.880  35.062 1.00 430.05 ? 479 LYS B CB  1 
ATOM   3690 C  CG  . LYS B 2 479 ? 64.755  94.620  34.920 1.00 478.25 ? 479 LYS B CG  1 
ATOM   3691 C  CD  . LYS B 2 479 ? 65.549  93.323  34.854 1.00 534.28 ? 479 LYS B CD  1 
ATOM   3692 C  CE  . LYS B 2 479 ? 64.739  92.116  34.425 1.00 559.66 ? 479 LYS B CE  1 
ATOM   3693 N  NZ  . LYS B 2 479 ? 63.714  91.737  35.427 1.00 576.02 ? 479 LYS B NZ  1 
ATOM   3694 N  N   . ASN B 2 480 ? 68.238  97.305  37.401 1.00 459.63 ? 480 ASN B N   1 
ATOM   3695 C  CA  . ASN B 2 480 ? 69.512  98.020  37.529 1.00 440.55 ? 480 ASN B CA  1 
ATOM   3696 C  C   . ASN B 2 480 ? 69.551  99.357  36.766 1.00 338.64 ? 480 ASN B C   1 
ATOM   3697 O  O   . ASN B 2 480 ? 70.480  99.613  35.997 1.00 250.58 ? 480 ASN B O   1 
ATOM   3698 C  CB  . ASN B 2 480 ? 70.675  97.094  37.138 1.00 532.44 ? 480 ASN B CB  1 
ATOM   3699 C  CG  . ASN B 2 480 ? 70.679  95.785  37.904 1.00 603.35 ? 480 ASN B CG  1 
ATOM   3700 O  OD1 . ASN B 2 480 ? 70.459  95.773  39.113 1.00 616.13 ? 480 ASN B OD1 1 
ATOM   3701 N  ND2 . ASN B 2 480 ? 70.925  94.679  37.220 1.00 615.98 ? 480 ASN B ND2 1 
ATOM   3702 N  N   . LYS B 2 481 ? 68.551  100.228 36.997 1.00 301.07 ? 481 LYS B N   1 
ATOM   3703 C  CA  . LYS B 2 481 ? 68.384  101.448 36.209 1.00 263.71 ? 481 LYS B CA  1 
ATOM   3704 C  C   . LYS B 2 481 ? 69.633  102.348 36.220 1.00 324.57 ? 481 LYS B C   1 
ATOM   3705 O  O   . LYS B 2 481 ? 69.978  102.856 35.152 1.00 383.90 ? 481 LYS B O   1 
ATOM   3706 C  CB  . LYS B 2 481 ? 67.143  102.228 36.670 1.00 264.92 ? 481 LYS B CB  1 
ATOM   3707 C  CG  . LYS B 2 481 ? 65.801  101.495 36.609 1.00 308.71 ? 481 LYS B CG  1 
ATOM   3708 C  CD  . LYS B 2 481 ? 65.501  100.850 35.259 1.00 316.27 ? 481 LYS B CD  1 
ATOM   3709 C  CE  . LYS B 2 481 ? 64.028  100.641 34.948 1.00 321.91 ? 481 LYS B CE  1 
ATOM   3710 N  NZ  . LYS B 2 481 ? 63.296  99.864  35.975 1.00 308.23 ? 481 LYS B NZ  1 
ATOM   3711 N  N   . PRO B 2 482 ? 70.339  102.612 37.360 1.00 360.68 ? 482 PRO B N   1 
ATOM   3712 C  CA  . PRO B 2 482 ? 71.557  103.434 37.356 1.00 325.08 ? 482 PRO B CA  1 
ATOM   3713 C  C   . PRO B 2 482 ? 72.732  102.764 36.641 1.00 278.79 ? 482 PRO B C   1 
ATOM   3714 O  O   . PRO B 2 482 ? 73.226  101.724 37.060 1.00 264.93 ? 482 PRO B O   1 
ATOM   3715 C  CB  . PRO B 2 482 ? 71.880  103.675 38.847 1.00 326.80 ? 482 PRO B CB  1 
ATOM   3716 C  CG  . PRO B 2 482 ? 70.592  103.319 39.565 1.00 389.67 ? 482 PRO B CG  1 
ATOM   3717 C  CD  . PRO B 2 482 ? 70.012  102.193 38.732 1.00 397.17 ? 482 PRO B CD  1 
ATOM   3718 N  N   . LYS B 2 483 ? 73.196  103.397 35.555 1.00 352.44 ? 483 LYS B N   1 
ATOM   3719 C  CA  . LYS B 2 483 ? 74.197  102.812 34.662 1.00 396.44 ? 483 LYS B CA  1 
ATOM   3720 C  C   . LYS B 2 483 ? 75.571  102.680 35.340 1.00 356.15 ? 483 LYS B C   1 
ATOM   3721 O  O   . LYS B 2 483 ? 76.374  101.841 34.924 1.00 359.25 ? 483 LYS B O   1 
ATOM   3722 C  CB  . LYS B 2 483 ? 74.275  103.617 33.355 1.00 419.84 ? 483 LYS B CB  1 
ATOM   3723 C  CG  . LYS B 2 483 ? 72.946  103.823 32.626 1.00 437.16 ? 483 LYS B CG  1 
ATOM   3724 C  CD  . LYS B 2 483 ? 72.162  102.551 32.341 1.00 434.92 ? 483 LYS B CD  1 
ATOM   3725 C  CE  . LYS B 2 483 ? 70.889  102.773 31.543 1.00 372.38 ? 483 LYS B CE  1 
ATOM   3726 N  NZ  . LYS B 2 483 ? 69.881  103.556 32.297 1.00 310.39 ? 483 LYS B NZ  1 
ATOM   3727 N  N   . TRP B 2 484 ? 75.844  103.473 36.386 1.00 313.52 ? 484 TRP B N   1 
ATOM   3728 C  CA  . TRP B 2 484 ? 77.070  103.338 37.162 1.00 355.70 ? 484 TRP B CA  1 
ATOM   3729 C  C   . TRP B 2 484 ? 77.093  102.039 37.979 1.00 379.79 ? 484 TRP B C   1 
ATOM   3730 O  O   . TRP B 2 484 ? 78.128  101.373 38.041 1.00 335.33 ? 484 TRP B O   1 
ATOM   3731 C  CB  . TRP B 2 484 ? 77.277  104.585 38.032 1.00 382.97 ? 484 TRP B CB  1 
ATOM   3732 C  CG  . TRP B 2 484 ? 76.397  104.732 39.250 1.00 386.68 ? 484 TRP B CG  1 
ATOM   3733 C  CD1 . TRP B 2 484 ? 75.115  105.204 39.299 1.00 308.67 ? 484 TRP B CD1 1 
ATOM   3734 C  CD2 . TRP B 2 484 ? 76.758  104.412 40.620 1.00 404.74 ? 484 TRP B CD2 1 
ATOM   3735 N  NE1 . TRP B 2 484 ? 74.657  105.200 40.593 1.00 299.57 ? 484 TRP B NE1 1 
ATOM   3736 C  CE2 . TRP B 2 484 ? 75.638  104.722 41.434 1.00 378.16 ? 484 TRP B CE2 1 
ATOM   3737 C  CE3 . TRP B 2 484 ? 77.913  103.899 41.239 1.00 358.51 ? 484 TRP B CE3 1 
ATOM   3738 C  CZ2 . TRP B 2 484 ? 75.653  104.529 42.826 1.00 385.28 ? 484 TRP B CZ2 1 
ATOM   3739 C  CZ3 . TRP B 2 484 ? 77.930  103.713 42.611 1.00 339.05 ? 484 TRP B CZ3 1 
ATOM   3740 C  CH2 . TRP B 2 484 ? 76.811  104.026 43.392 1.00 380.03 ? 484 TRP B CH2 1 
ATOM   3741 N  N   . LEU B 2 485 ? 75.957  101.648 38.579 1.00 391.93 ? 485 LEU B N   1 
ATOM   3742 C  CA  . LEU B 2 485 ? 75.832  100.349 39.246 1.00 346.86 ? 485 LEU B CA  1 
ATOM   3743 C  C   . LEU B 2 485 ? 75.966  99.202  38.241 1.00 310.63 ? 485 LEU B C   1 
ATOM   3744 O  O   . LEU B 2 485 ? 76.669  98.239  38.520 1.00 329.16 ? 485 LEU B O   1 
ATOM   3745 C  CB  . LEU B 2 485 ? 74.493  100.257 39.993 1.00 391.61 ? 485 LEU B CB  1 
ATOM   3746 C  CG  . LEU B 2 485 ? 74.310  101.196 41.188 1.00 476.82 ? 485 LEU B CG  1 
ATOM   3747 C  CD1 . LEU B 2 485 ? 72.922  101.024 41.785 1.00 492.18 ? 485 LEU B CD1 1 
ATOM   3748 C  CD2 . LEU B 2 485 ? 75.372  100.975 42.267 1.00 499.43 ? 485 LEU B CD2 1 
ATOM   3749 N  N   . LEU B 2 486 ? 75.310  99.302  37.076 1.00 343.35 ? 486 LEU B N   1 
ATOM   3750 C  CA  . LEU B 2 486 ? 75.427  98.303  36.016 1.00 349.63 ? 486 LEU B CA  1 
ATOM   3751 C  C   . LEU B 2 486 ? 76.885  98.131  35.561 1.00 326.70 ? 486 LEU B C   1 
ATOM   3752 O  O   . LEU B 2 486 ? 77.332  97.001  35.384 1.00 275.36 ? 486 LEU B O   1 
ATOM   3753 C  CB  . LEU B 2 486 ? 74.506  98.688  34.850 1.00 375.58 ? 486 LEU B CB  1 
ATOM   3754 C  CG  . LEU B 2 486 ? 74.554  97.784  33.617 1.00 434.92 ? 486 LEU B CG  1 
ATOM   3755 C  CD1 . LEU B 2 486 ? 74.130  96.361  33.950 1.00 481.63 ? 486 LEU B CD1 1 
ATOM   3756 C  CD2 . LEU B 2 486 ? 73.678  98.344  32.514 1.00 474.79 ? 486 LEU B CD2 1 
ATOM   3757 N  N   . GLN B 2 487 ? 77.634  99.229  35.392 1.00 348.88 ? 487 GLN B N   1 
ATOM   3758 C  CA  . GLN B 2 487 ? 79.052  99.175  35.045 1.00 347.16 ? 487 GLN B CA  1 
ATOM   3759 C  C   . GLN B 2 487 ? 79.868  98.509  36.167 1.00 368.93 ? 487 GLN B C   1 
ATOM   3760 O  O   . GLN B 2 487 ? 80.773  97.722  35.864 1.00 373.35 ? 487 GLN B O   1 
ATOM   3761 C  CB  . GLN B 2 487 ? 79.545  100.582 34.679 1.00 374.75 ? 487 GLN B CB  1 
ATOM   3762 C  CG  . GLN B 2 487 ? 80.985  100.639 34.161 1.00 426.95 ? 487 GLN B CG  1 
ATOM   3763 C  CD  . GLN B 2 487 ? 82.065  100.895 35.192 1.00 456.95 ? 487 GLN B CD  1 
ATOM   3764 O  OE1 . GLN B 2 487 ? 81.830  100.943 36.398 1.00 470.18 ? 487 GLN B OE1 1 
ATOM   3765 N  NE2 . GLN B 2 487 ? 83.292  101.071 34.720 1.00 427.25 ? 487 GLN B NE2 1 
ATOM   3766 N  N   . GLY B 2 488 ? 79.561  98.786  37.450 1.00 370.73 ? 488 GLY B N   1 
ATOM   3767 C  CA  . GLY B 2 488 ? 80.186  98.109  38.585 1.00 350.48 ? 488 GLY B CA  1 
ATOM   3768 C  C   . GLY B 2 488 ? 79.926  96.598  38.613 1.00 298.72 ? 488 GLY B C   1 
ATOM   3769 O  O   . GLY B 2 488 ? 80.842  95.816  38.860 1.00 283.51 ? 488 GLY B O   1 
ATOM   3770 N  N   . ILE B 2 489 ? 78.673  96.192  38.353 1.00 293.50 ? 489 ILE B N   1 
ATOM   3771 C  CA  . ILE B 2 489 ? 78.266  94.794  38.214 1.00 295.02 ? 489 ILE B CA  1 
ATOM   3772 C  C   . ILE B 2 489 ? 79.026  94.145  37.059 1.00 260.91 ? 489 ILE B C   1 
ATOM   3773 O  O   . ILE B 2 489 ? 79.547  93.042  37.219 1.00 203.77 ? 489 ILE B O   1 
ATOM   3774 C  CB  . ILE B 2 489 ? 76.729  94.678  38.042 1.00 296.53 ? 489 ILE B CB  1 
ATOM   3775 C  CG1 . ILE B 2 489 ? 76.004  95.017  39.350 1.00 403.73 ? 489 ILE B CG1 1 
ATOM   3776 C  CG2 . ILE B 2 489 ? 76.290  93.312  37.504 1.00 208.49 ? 489 ILE B CG2 1 
ATOM   3777 C  CD1 . ILE B 2 489 ? 74.543  95.399  39.182 1.00 495.41 ? 489 ILE B CD1 1 
ATOM   3778 N  N   . PHE B 2 490 ? 79.085  94.815  35.904 1.00 279.52 ? 490 PHE B N   1 
ATOM   3779 C  CA  . PHE B 2 490 ? 79.750  94.276  34.729 1.00 303.78 ? 490 PHE B CA  1 
ATOM   3780 C  C   . PHE B 2 490 ? 81.260  94.147  34.971 1.00 218.63 ? 490 PHE B C   1 
ATOM   3781 O  O   . PHE B 2 490 ? 81.836  93.101  34.685 1.00 210.40 ? 490 PHE B O   1 
ATOM   3782 C  CB  . PHE B 2 490 ? 79.422  95.106  33.484 1.00 324.13 ? 490 PHE B CB  1 
ATOM   3783 C  CG  . PHE B 2 490 ? 79.731  94.347  32.218 1.00 300.73 ? 490 PHE B CG  1 
ATOM   3784 C  CD1 . PHE B 2 490 ? 78.796  93.484  31.660 1.00 242.38 ? 490 PHE B CD1 1 
ATOM   3785 C  CD2 . PHE B 2 490 ? 80.970  94.474  31.602 1.00 339.55 ? 490 PHE B CD2 1 
ATOM   3786 C  CE1 . PHE B 2 490 ? 79.095  92.775  30.503 1.00 311.60 ? 490 PHE B CE1 1 
ATOM   3787 C  CE2 . PHE B 2 490 ? 81.267  93.763  30.446 1.00 351.03 ? 490 PHE B CE2 1 
ATOM   3788 C  CZ  . PHE B 2 490 ? 80.331  92.914  29.900 1.00 319.52 ? 490 PHE B CZ  1 
ATOM   3789 N  N   . SER B 2 491 ? 81.886  95.189  35.525 1.00 198.09 ? 491 SER B N   1 
ATOM   3790 C  CA  . SER B 2 491 ? 83.291  95.165  35.931 1.00 312.92 ? 491 SER B CA  1 
ATOM   3791 C  C   . SER B 2 491 ? 83.597  93.976  36.856 1.00 288.51 ? 491 SER B C   1 
ATOM   3792 O  O   . SER B 2 491 ? 84.504  93.189  36.595 1.00 166.62 ? 491 SER B O   1 
ATOM   3793 C  CB  . SER B 2 491 ? 83.659  96.497  36.574 1.00 379.34 ? 491 SER B CB  1 
ATOM   3794 O  OG  . SER B 2 491 ? 85.019  96.525  36.998 1.00 315.25 ? 491 SER B OG  1 
ATOM   3795 N  N   . THR B 2 492 ? 82.828  93.844  37.944 1.00 281.35 ? 492 THR B N   1 
ATOM   3796 C  CA  . THR B 2 492 ? 82.933  92.730  38.884 1.00 275.03 ? 492 THR B CA  1 
ATOM   3797 C  C   . THR B 2 492 ? 82.802  91.385  38.168 1.00 180.81 ? 492 THR B C   1 
ATOM   3798 O  O   . THR B 2 492 ? 83.584  90.462  38.401 1.00 154.63 ? 492 THR B O   1 
ATOM   3799 C  CB  . THR B 2 492 ? 81.877  92.844  39.996 1.00 343.83 ? 492 THR B CB  1 
ATOM   3800 O  OG1 . THR B 2 492 ? 82.065  94.091  40.667 1.00 430.13 ? 492 THR B OG1 1 
ATOM   3801 C  CG2 . THR B 2 492 ? 81.928  91.737  41.029 1.00 382.13 ? 492 THR B CG2 1 
ATOM   3802 N  N   . THR B 2 493 ? 81.809  91.276  37.287 1.00 182.17 ? 493 THR B N   1 
ATOM   3803 C  CA  . THR B 2 493 ? 81.601  90.074  36.495 1.00 220.49 ? 493 THR B CA  1 
ATOM   3804 C  C   . THR B 2 493 ? 82.844  89.745  35.666 1.00 188.71 ? 493 THR B C   1 
ATOM   3805 O  O   . THR B 2 493 ? 83.399  88.660  35.814 1.00 137.50 ? 493 THR B O   1 
ATOM   3806 C  CB  . THR B 2 493 ? 80.352  90.187  35.603 1.00 232.04 ? 493 THR B CB  1 
ATOM   3807 O  OG1 . THR B 2 493 ? 79.216  90.411  36.442 1.00 196.88 ? 493 THR B OG1 1 
ATOM   3808 C  CG2 . THR B 2 493 ? 80.106  88.961  34.744 1.00 210.37 ? 493 THR B CG2 1 
ATOM   3809 N  N   . VAL B 2 494 ? 83.290  90.664  34.796 1.00 192.51 ? 494 VAL B N   1 
ATOM   3810 C  CA  . VAL B 2 494 ? 84.360  90.338  33.872 1.00 198.30 ? 494 VAL B CA  1 
ATOM   3811 C  C   . VAL B 2 494 ? 85.656  90.034  34.625 1.00 207.79 ? 494 VAL B C   1 
ATOM   3812 O  O   . VAL B 2 494 ? 86.456  89.254  34.102 1.00 138.83 ? 494 VAL B O   1 
ATOM   3813 C  CB  . VAL B 2 494 ? 84.552  91.410  32.775 1.00 281.38 ? 494 VAL B CB  1 
ATOM   3814 C  CG1 . VAL B 2 494 ? 83.287  91.531  31.927 1.00 270.50 ? 494 VAL B CG1 1 
ATOM   3815 C  CG2 . VAL B 2 494 ? 84.996  92.784  33.287 1.00 272.29 ? 494 VAL B CG2 1 
ATOM   3816 N  N   . LEU B 2 495 ? 85.892  90.618  35.817 1.00 208.12 ? 495 LEU B N   1 
ATOM   3817 C  CA  . LEU B 2 495 ? 87.028  90.221  36.645 1.00 247.52 ? 495 LEU B CA  1 
ATOM   3818 C  C   . LEU B 2 495 ? 86.936  88.734  36.977 1.00 206.93 ? 495 LEU B C   1 
ATOM   3819 O  O   . LEU B 2 495 ? 87.914  88.009  36.805 1.00 160.77 ? 495 LEU B O   1 
ATOM   3820 C  CB  . LEU B 2 495 ? 87.087  91.093  37.906 1.00 215.80 ? 495 LEU B CB  1 
ATOM   3821 C  CG  . LEU B 2 495 ? 87.587  92.516  37.665 1.00 333.16 ? 495 LEU B CG  1 
ATOM   3822 C  CD1 . LEU B 2 495 ? 87.279  93.409  38.855 1.00 384.44 ? 495 LEU B CD1 1 
ATOM   3823 C  CD2 . LEU B 2 495 ? 89.083  92.542  37.369 1.00 397.15 ? 495 LEU B CD2 1 
ATOM   3824 N  N   . CYS B 2 496 ? 85.768  88.273  37.434 1.00 198.62 ? 496 CYS B N   1 
ATOM   3825 C  CA  . CYS B 2 496 ? 85.585  86.860  37.731 1.00 299.53 ? 496 CYS B CA  1 
ATOM   3826 C  C   . CYS B 2 496 ? 85.776  85.995  36.480 1.00 264.20 ? 496 CYS B C   1 
ATOM   3827 O  O   . CYS B 2 496 ? 86.425  84.938  36.537 1.00 146.07 ? 496 CYS B O   1 
ATOM   3828 C  CB  . CYS B 2 496 ? 84.216  86.628  38.341 1.00 280.13 ? 496 CYS B CB  1 
ATOM   3829 S  SG  . CYS B 2 496 ? 83.932  87.573  39.850 1.00 279.50 ? 496 CYS B SG  1 
ATOM   3830 N  N   . GLN B 2 497 ? 85.239  86.444  35.335 1.00 223.38 ? 497 GLN B N   1 
ATOM   3831 C  CA  . GLN B 2 497 ? 85.373  85.732  34.078 1.00 178.60 ? 497 GLN B CA  1 
ATOM   3832 C  C   . GLN B 2 497 ? 86.840  85.499  33.769 1.00 187.60 ? 497 GLN B C   1 
ATOM   3833 O  O   . GLN B 2 497 ? 87.204  84.347  33.572 1.00 144.55 ? 497 GLN B O   1 
ATOM   3834 C  CB  . GLN B 2 497 ? 84.740  86.524  32.927 1.00 248.93 ? 497 GLN B CB  1 
ATOM   3835 C  CG  . GLN B 2 497 ? 83.246  86.781  33.037 1.00 273.49 ? 497 GLN B CG  1 
ATOM   3836 C  CD  . GLN B 2 497 ? 82.449  85.517  32.941 1.00 260.21 ? 497 GLN B CD  1 
ATOM   3837 O  OE1 . GLN B 2 497 ? 82.083  84.936  33.958 1.00 251.44 ? 497 GLN B OE1 1 
ATOM   3838 N  NE2 . GLN B 2 497 ? 82.168  85.079  31.719 1.00 236.88 ? 497 GLN B NE2 1 
ATOM   3839 N  N   . LYS B 2 498 ? 87.646  86.589  33.701 1.00 226.24 ? 498 LYS B N   1 
ATOM   3840 C  CA  . LYS B 2 498 ? 89.068  86.579  33.353 1.00 281.47 ? 498 LYS B CA  1 
ATOM   3841 C  C   . LYS B 2 498 ? 89.842  85.701  34.334 1.00 259.27 ? 498 LYS B C   1 
ATOM   3842 O  O   . LYS B 2 498 ? 90.677  84.881  33.937 1.00 230.63 ? 498 LYS B O   1 
ATOM   3843 C  CB  . LYS B 2 498 ? 89.645  88.006  33.357 1.00 212.18 ? 498 LYS B CB  1 
ATOM   3844 C  CG  . LYS B 2 498 ? 89.128  88.924  32.263 1.00 289.77 ? 498 LYS B CG  1 
ATOM   3845 C  CD  . LYS B 2 498 ? 89.522  90.377  32.475 1.00 320.67 ? 498 LYS B CD  1 
ATOM   3846 C  CE  . LYS B 2 498 ? 88.913  91.336  31.469 1.00 330.35 ? 498 LYS B CE  1 
ATOM   3847 N  NZ  . LYS B 2 498 ? 89.204  92.752  31.814 1.00 301.36 ? 498 LYS B NZ  1 
ATOM   3848 N  N   . LEU B 2 499 ? 89.537  85.885  35.623 1.00 213.54 ? 499 LEU B N   1 
ATOM   3849 C  CA  . LEU B 2 499 ? 90.230  85.206  36.702 1.00 234.95 ? 499 LEU B CA  1 
ATOM   3850 C  C   . LEU B 2 499 ? 89.990  83.697  36.659 1.00 256.50 ? 499 LEU B C   1 
ATOM   3851 O  O   . LEU B 2 499 ? 90.955  82.948  36.512 1.00 278.40 ? 499 LEU B O   1 
ATOM   3852 C  CB  . LEU B 2 499 ? 89.752  85.853  38.005 1.00 188.76 ? 499 LEU B CB  1 
ATOM   3853 C  CG  . LEU B 2 499 ? 90.314  85.315  39.301 1.00 223.87 ? 499 LEU B CG  1 
ATOM   3854 C  CD1 . LEU B 2 499 ? 91.835  85.270  39.289 1.00 329.54 ? 499 LEU B CD1 1 
ATOM   3855 C  CD2 . LEU B 2 499 ? 89.833  86.233  40.420 1.00 256.54 ? 499 LEU B CD2 1 
ATOM   3856 N  N   . MET B 2 500 ? 88.723  83.265  36.779 1.00 200.24 ? 500 MET B N   1 
ATOM   3857 C  CA  . MET B 2 500 ? 88.387  81.849  36.904 1.00 245.63 ? 500 MET B CA  1 
ATOM   3858 C  C   . MET B 2 500 ? 88.371  81.096  35.558 1.00 248.57 ? 500 MET B C   1 
ATOM   3859 O  O   . MET B 2 500 ? 88.374  79.856  35.542 1.00 243.03 ? 500 MET B O   1 
ATOM   3860 C  CB  . MET B 2 500 ? 87.020  81.714  37.580 1.00 289.69 ? 500 MET B CB  1 
ATOM   3861 C  CG  . MET B 2 500 ? 87.029  82.190  39.021 1.00 291.95 ? 500 MET B CG  1 
ATOM   3862 S  SD  . MET B 2 500 ? 85.404  81.992  39.820 1.00 282.70 ? 500 MET B SD  1 
ATOM   3863 C  CE  . MET B 2 500 ? 85.690  82.744  41.424 1.00 344.33 ? 500 MET B CE  1 
ATOM   3864 N  N   . GLN B 2 501 ? 88.343  81.827  34.433 1.00 171.50 ? 501 GLN B N   1 
ATOM   3865 C  CA  . GLN B 2 501 ? 88.235  81.279  33.083 1.00 222.69 ? 501 GLN B CA  1 
ATOM   3866 C  C   . GLN B 2 501 ? 86.914  80.510  32.952 1.00 200.05 ? 501 GLN B C   1 
ATOM   3867 O  O   . GLN B 2 501 ? 86.898  79.293  32.857 1.00 157.18 ? 501 GLN B O   1 
ATOM   3868 C  CB  . GLN B 2 501 ? 89.506  80.496  32.717 1.00 269.90 ? 501 GLN B CB  1 
ATOM   3869 C  CG  . GLN B 2 501 ? 89.579  80.050  31.260 1.00 324.70 ? 501 GLN B CG  1 
ATOM   3870 C  CD  . GLN B 2 501 ? 90.794  79.215  30.921 1.00 369.27 ? 501 GLN B CD  1 
ATOM   3871 O  OE1 . GLN B 2 501 ? 91.654  78.943  31.760 1.00 348.85 ? 501 GLN B OE1 1 
ATOM   3872 N  NE2 . GLN B 2 501 ? 90.875  78.799  29.664 1.00 422.37 ? 501 GLN B NE2 1 
ATOM   3873 N  N   . VAL B 2 502 ? 85.787  81.245  32.948 1.00 193.86 ? 502 VAL B N   1 
ATOM   3874 C  CA  . VAL B 2 502 ? 84.448  80.657  32.905 1.00 199.08 ? 502 VAL B CA  1 
ATOM   3875 C  C   . VAL B 2 502 ? 83.545  81.411  31.927 1.00 198.66 ? 502 VAL B C   1 
ATOM   3876 O  O   . VAL B 2 502 ? 83.732  82.599  31.684 1.00 160.43 ? 502 VAL B O   1 
ATOM   3877 C  CB  . VAL B 2 502 ? 83.825  80.584  34.302 1.00 164.51 ? 502 VAL B CB  1 
ATOM   3878 C  CG1 . VAL B 2 502 ? 84.666  79.726  35.229 1.00 187.76 ? 502 VAL B CG1 1 
ATOM   3879 C  CG2 . VAL B 2 502 ? 83.657  81.977  34.897 1.00 283.99 ? 502 VAL B CG2 1 
ATOM   3880 N  N   . VAL B 2 503 ? 82.563  80.683  31.356 1.00 210.35 ? 503 VAL B N   1 
ATOM   3881 C  CA  . VAL B 2 503 ? 81.779  81.142  30.211 1.00 145.77 ? 503 VAL B CA  1 
ATOM   3882 C  C   . VAL B 2 503 ? 80.326  80.680  30.338 1.00 160.98 ? 503 VAL B C   1 
ATOM   3883 O  O   . VAL B 2 503 ? 80.060  79.663  31.013 1.00 294.23 ? 503 VAL B O   1 
ATOM   3884 C  CB  . VAL B 2 503 ? 82.378  80.568  28.924 1.00 205.86 ? 503 VAL B CB  1 
ATOM   3885 C  CG1 . VAL B 2 503 ? 83.843  80.968  28.764 1.00 218.53 ? 503 VAL B CG1 1 
ATOM   3886 C  CG2 . VAL B 2 503 ? 82.215  79.043  28.824 1.00 174.57 ? 503 VAL B CG2 1 
ATOM   3887 N  N   . PRO B 2 504 ? 79.321  81.361  29.748 1.00 144.80 ? 504 PRO B N   1 
ATOM   3888 C  CA  . PRO B 2 504 ? 77.933  80.880  29.856 1.00 186.95 ? 504 PRO B CA  1 
ATOM   3889 C  C   . PRO B 2 504 ? 77.721  79.499  29.216 1.00 219.94 ? 504 PRO B C   1 
ATOM   3890 O  O   . PRO B 2 504 ? 78.481  79.037  28.360 1.00 138.88 ? 504 PRO B O   1 
ATOM   3891 C  CB  . PRO B 2 504 ? 77.065  81.945  29.174 1.00 174.18 ? 504 PRO B CB  1 
ATOM   3892 C  CG  . PRO B 2 504 ? 78.003  83.142  28.989 1.00 239.28 ? 504 PRO B CG  1 
ATOM   3893 C  CD  . PRO B 2 504 ? 79.431  82.602  28.981 1.00 206.69 ? 504 PRO B CD  1 
ATOM   3894 N  N   . GLN B 2 505 ? 76.649  78.835  29.650 1.00 243.53 ? 505 GLN B N   1 
ATOM   3895 C  CA  . GLN B 2 505 ? 76.243  77.584  29.036 1.00 250.92 ? 505 GLN B CA  1 
ATOM   3896 C  C   . GLN B 2 505 ? 75.547  77.821  27.687 1.00 289.88 ? 505 GLN B C   1 
ATOM   3897 O  O   . GLN B 2 505 ? 74.793  78.776  27.519 1.00 254.09 ? 505 GLN B O   1 
ATOM   3898 C  CB  . GLN B 2 505 ? 75.335  76.790  29.979 1.00 257.65 ? 505 GLN B CB  1 
ATOM   3899 C  CG  . GLN B 2 505 ? 75.082  75.392  29.439 1.00 284.94 ? 505 GLN B CG  1 
ATOM   3900 C  CD  . GLN B 2 505 ? 74.594  74.383  30.451 1.00 298.86 ? 505 GLN B CD  1 
ATOM   3901 O  OE1 . GLN B 2 505 ? 75.267  73.373  30.704 1.00 175.68 ? 505 GLN B OE1 1 
ATOM   3902 N  NE2 . GLN B 2 505 ? 73.420  74.652  31.017 1.00 293.89 ? 505 GLN B NE2 1 
ATOM   3903 N  N   . GLU B 2 506 ? 75.799  76.914  26.722 1.00 297.91 ? 506 GLU B N   1 
ATOM   3904 C  CA  . GLU B 2 506 ? 75.014  76.790  25.498 1.00 254.45 ? 506 GLU B CA  1 
ATOM   3905 C  C   . GLU B 2 506 ? 74.114  75.552  25.594 1.00 399.33 ? 506 GLU B C   1 
ATOM   3906 O  O   . GLU B 2 506 ? 74.585  74.454  25.950 1.00 511.23 ? 506 GLU B O   1 
ATOM   3907 C  CB  . GLU B 2 506 ? 75.952  76.680  24.305 1.00 313.46 ? 506 GLU B CB  1 
ATOM   3908 C  CG  . GLU B 2 506 ? 76.768  77.946  24.060 1.00 423.86 ? 506 GLU B CG  1 
ATOM   3909 C  CD  . GLU B 2 506 ? 78.113  77.732  23.385 1.00 505.27 ? 506 GLU B CD  1 
ATOM   3910 O  OE1 . GLU B 2 506 ? 78.844  76.811  23.815 1.00 499.92 ? 506 GLU B OE1 1 
ATOM   3911 O  OE2 . GLU B 2 506 ? 78.442  78.489  22.437 1.00 552.50 ? 506 GLU B OE2 1 
ATOM   3912 N  N   . THR B 2 507 ? 72.814  75.736  25.268 1.00 415.40 ? 507 THR B N   1 
ATOM   3913 C  CA  . THR B 2 507 ? 71.780  74.721  25.463 1.00 431.85 ? 507 THR B CA  1 
ATOM   3914 C  C   . THR B 2 507 ? 71.993  73.562  24.478 1.00 467.30 ? 507 THR B C   1 
ATOM   3915 O  O   . THR B 2 507 ? 71.918  72.383  24.924 1.00 440.08 ? 507 THR B O   1 
ATOM   3916 C  CB  . THR B 2 507 ? 70.369  75.320  25.319 1.00 383.52 ? 507 THR B CB  1 
ATOM   3917 O  OG1 . THR B 2 507 ? 70.231  76.444  26.192 1.00 263.58 ? 507 THR B OG1 1 
ATOM   3918 C  CG2 . THR B 2 507 ? 69.262  74.327  25.614 1.00 393.15 ? 507 THR B CG2 1 
HETATM 3919 C  C1  . VUC C 3 .   ? 70.085  67.721  56.732 1.00 306.13 ? 601 VUC B C1  1 
HETATM 3920 O  O1  . VUC C 3 .   ? 71.852  62.869  58.547 1.00 179.22 ? 601 VUC B O1  1 
HETATM 3921 O  O2  . VUC C 3 .   ? 72.948  64.050  56.986 1.00 336.94 ? 601 VUC B O2  1 
HETATM 3922 C  C2  . VUC C 3 .   ? 69.378  68.697  56.048 1.00 310.13 ? 601 VUC B C2  1 
HETATM 3923 C  C3  . VUC C 3 .   ? 68.016  68.514  55.729 1.00 242.81 ? 601 VUC B C3  1 
HETATM 3924 C  C4  . VUC C 3 .   ? 67.412  67.308  56.121 1.00 182.96 ? 601 VUC B C4  1 
HETATM 3925 C  C5  . VUC C 3 .   ? 68.138  66.347  56.809 1.00 246.49 ? 601 VUC B C5  1 
HETATM 3926 C  C6  . VUC C 3 .   ? 69.476  66.537  57.127 1.00 319.68 ? 601 VUC B C6  1 
HETATM 3927 C  C7  . VUC C 3 .   ? 70.247  65.487  57.879 1.00 326.82 ? 601 VUC B C7  1 
HETATM 3928 C  C8  . VUC C 3 .   ? 70.563  64.247  57.049 1.00 265.00 ? 601 VUC B C8  1 
HETATM 3929 C  C9  . VUC C 3 .   ? 71.885  63.661  57.576 1.00 290.47 ? 601 VUC B C9  1 
HETATM 3930 C  C10 . VUC C 3 .   ? 66.916  69.345  53.681 1.00 316.29 ? 601 VUC B C10 1 
HETATM 3931 C  C11 . VUC C 3 .   ? 67.327  70.502  52.815 1.00 395.28 ? 601 VUC B C11 1 
HETATM 3932 C  C12 . VUC C 3 .   ? 66.905  70.731  55.787 1.00 376.67 ? 601 VUC B C12 1 
HETATM 3933 C  C13 . VUC C 3 .   ? 66.644  70.601  57.295 1.00 374.59 ? 601 VUC B C13 1 
HETATM 3934 N  N1  . VUC C 3 .   ? 69.417  63.279  57.053 1.00 157.40 ? 601 VUC B N1  1 
HETATM 3935 N  N2  . VUC C 3 .   ? 67.309  69.490  55.085 1.00 302.75 ? 601 VUC B N2  1 
HETATM 3936 CL CL1 . VUC C 3 .   ? 69.073  70.918  53.035 1.00 656.79 ? 601 VUC B CL1 1 
HETATM 3937 CL CL2 . VUC C 3 .   ? 68.120  70.971  58.285 1.00 259.92 ? 601 VUC B CL2 1 
# 
