data_8KDH
# 
_entry.id   8KDH 
# 
_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   8KDH         pdb_00008kdh 10.2210/pdb8kdh/pdb 
WWPDB D_1300040168 ?            ?                   
EMDB  EMD-37136    ?            ?                   
# 
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                        8KDH 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB 'Structure of LAT1-CD98hc in complex with BCH, focused on TMD'       EMD-37136 'associated EM volume' 
EMDB 'Structure of LAT1-CD98hc-Fab170 in complex with BCH, consensus map' EMD-37135 'consensus 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 CHOLESTEROL                                                           386.654   2 ? ? ? ? 
4 non-polymer syn 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine                      760.076   1 ? ? ? ? 
5 non-polymer syn '(1~{S},2~{R},4~{R})-2-azanylbicyclo[2.2.1]heptane-2-carboxylic acid' 155.194   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 ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 CHOLESTEROL                                                           CLR 
4 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine                      LBN 
5 '(1~{S},2~{R},4~{R})-2-azanylbicyclo[2.2.1]heptane-2-carboxylic acid' VU0 
# 
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 
CLR non-polymer         . CHOLESTEROL                                                           ? 'C27 H46 O'      386.654 
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 
LBN non-polymer         . 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine                      
'(2R)-2-[(9Z)-9-Octadecenoyloxy]-3-(palmitoyloxy)propyl 2-(trimethylammonio)ethyl phosphate' 'C42 H82 N O8 P' 760.076 
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 
VU0 non-polymer         . '(1~{S},2~{R},4~{R})-2-azanylbicyclo[2.2.1]heptane-2-carboxylic acid' ? 'C8 H13 N O2'    155.194 
# 
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        VU0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VU0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CLR 1 601 601 CLR CRL B . 
D 3 CLR 1 602 602 CLR CRL B . 
E 4 LBN 1 603 603 LBN POV B . 
F 5 VU0 1 604 1   VU0 BCH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 N 1 B LBN 603 ? C5  ? E LBN 1 C5  
2  1 N 1 B LBN 603 ? C7  ? E LBN 1 C7  
3  1 N 1 B LBN 603 ? C8  ? E LBN 1 C8  
4  1 N 1 B LBN 603 ? C10 ? E LBN 1 C10 
5  1 N 1 B LBN 603 ? C11 ? E LBN 1 C11 
6  1 N 1 B LBN 603 ? C13 ? E LBN 1 C13 
7  1 N 1 B LBN 603 ? C14 ? E LBN 1 C14 
8  1 N 1 B LBN 603 ? C16 ? E LBN 1 C16 
9  1 N 1 B LBN 603 ? C17 ? E LBN 1 C17 
10 1 N 1 B LBN 603 ? C19 ? E LBN 1 C19 
11 1 N 1 B LBN 603 ? C20 ? E LBN 1 C20 
12 1 N 1 B LBN 603 ? C21 ? E LBN 1 C21 
13 1 N 1 B LBN 603 ? C22 ? E LBN 1 C22 
14 1 N 1 B LBN 603 ? C23 ? E LBN 1 C23 
15 1 N 1 B LBN 603 ? C24 ? E LBN 1 C24 
# 
_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                     8KDH 
_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                         8KDH 
_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                   8KDH 
_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                               195.528 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.900 
_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                                 8KDH 
_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                            3.78 
_refine.ls_d_res_low                             3.78 
_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                     26217 
_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                          0.34261 
_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                       0.34261 
_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                       0.799 
_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                             16.325 
_refine.overall_SU_ML                            0.236 
_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               4022 
_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' ? 0.009  0.012  4132  ? r_bond_refined_d             ? ? 
'ELECTRON MICROSCOPY' ? 0.000  0.016  4166  ? r_bond_other_d               ? ? 
'ELECTRON MICROSCOPY' ? 1.865  1.625  5651  ? r_angle_refined_deg          ? ? 
'ELECTRON MICROSCOPY' ? 0.632  1.552  9564  ? r_angle_other_deg            ? ? 
'ELECTRON MICROSCOPY' ? 7.473  5.000  503   ? r_dihedral_angle_1_deg       ? ? 
'ELECTRON MICROSCOPY' ? 8.441  6.111  18    ? r_dihedral_angle_2_deg       ? ? 
'ELECTRON MICROSCOPY' ? 14.572 10.000 651   ? r_dihedral_angle_3_deg       ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'ELECTRON MICROSCOPY' ? 0.087  0.200  687   ? r_chiral_restr               ? ? 
'ELECTRON MICROSCOPY' ? 0.004  0.020  4579  ? r_gen_planes_refined         ? ? 
'ELECTRON MICROSCOPY' ? 0.001  0.020  921   ? 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' ? 32.620 16.494 2021  ? r_mcbond_it                  ? ? 
'ELECTRON MICROSCOPY' ? 32.578 16.498 2021  ? r_mcbond_other               ? ? 
'ELECTRON MICROSCOPY' ? 44.289 29.903 2521  ? r_mcangle_it                 ? ? 
'ELECTRON MICROSCOPY' ? 44.289 29.910 2522  ? r_mcangle_other              ? ? 
'ELECTRON MICROSCOPY' ? 39.773 21.131 2111  ? r_scbond_it                  ? ? 
'ELECTRON MICROSCOPY' ? 39.765 21.135 2110  ? r_scbond_other               ? ? 
'ELECTRON MICROSCOPY' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'ELECTRON MICROSCOPY' ? 59.396 37.175 3131  ? r_scangle_other              ? ? 
'ELECTRON MICROSCOPY' ? 60.533 208.86 16596 ? r_long_range_B_refined       ? ? 
'ELECTRON MICROSCOPY' ? 60.533 208.85 16597 ? 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                       3.700 
_refine_ls_shell.d_res_low                        3.796 
_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             1949 
_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                  2.014 
_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                     8KDH 
_struct.title                        'Structure of LAT1-CD98hc in complex with BCH, 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        8KDH 
_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 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
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 8KDH A 3 ? 631 ? P08195 2 ? 630 ? 2 630 
2 2 8KDH 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 8KDH GLY A 1   ? UNP P08195 ? ? 'expression tag' 0   1  
1 8KDH SER A 2   ? UNP P08195 ? ? 'expression tag' 1   2  
2 8KDH ASP B 508 ? UNP Q01650 ? ? 'expression tag' 508 3  
2 8KDH TYR B 509 ? UNP Q01650 ? ? 'expression tag' 509 4  
2 8KDH LYS B 510 ? UNP Q01650 ? ? 'expression tag' 510 5  
2 8KDH ASP B 511 ? UNP Q01650 ? ? 'expression tag' 511 6  
2 8KDH ASP B 512 ? UNP Q01650 ? ? 'expression tag' 512 7  
2 8KDH ASP B 513 ? UNP Q01650 ? ? 'expression tag' 513 8  
2 8KDH ASP B 514 ? UNP Q01650 ? ? 'expression tag' 514 9  
2 8KDH 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,D,E,F 
# 
_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 ? ALA A 208 ? SER A 175 ALA A 207 1 ? 33 
HELX_P HELX_P3  AA3 THR B 51  ? GLY B 65  ? THR B 51  GLY B 65  1 ? 15 
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 ? GLY B 125 ? GLY B 114 GLY B 125 1 ? 12 
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 ? LYS B 158 ? ILE B 139 LYS B 158 1 ? 20 
HELX_P HELX_P10 AB1 PRO B 159 ? PHE B 161 ? PRO B 159 PHE B 161 5 ? 3  
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 ? GLY B 255 ? ASP B 239 GLY B 255 1 ? 17 
HELX_P HELX_P14 AB5 TYR B 259 ? VAL B 263 ? TYR B 259 VAL B 263 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 269 ? LEU B 300 ? ASN B 269 LEU B 300 1 ? 32 
HELX_P HELX_P16 AB7 SER B 301 ? SER B 308 ? SER B 301 SER B 308 1 ? 8  
HELX_P HELX_P17 AB8 ALA B 310 ? GLY B 321 ? ALA B 310 GLY B 321 1 ? 12 
HELX_P HELX_P18 AB9 VAL B 322 ? SER B 324 ? VAL B 322 SER B 324 5 ? 3  
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 360 ? MET B 365 ? PRO B 360 MET B 365 5 ? 6  
HELX_P HELX_P21 AC3 PRO B 373 ? LEU B 386 ? PRO B 373 LEU B 386 1 ? 14 
HELX_P HELX_P22 AC4 TYR B 387 ? SER B 390 ? TYR B 387 SER B 390 5 ? 4  
HELX_P HELX_P23 AC5 ASP B 392 ? PHE B 394 ? ASP B 392 PHE B 394 5 ? 3  
HELX_P HELX_P24 AC6 SER B 395 ? LYS B 422 ? SER B 395 LYS B 422 1 ? 28 
HELX_P HELX_P25 AC7 LEU B 433 ? THR B 454 ? LEU B 433 THR B 454 1 ? 22 
HELX_P HELX_P26 AC8 THR B 454 ? SER B 467 ? THR B 454 SER B 467 1 ? 14 
HELX_P HELX_P27 AC9 SER B 467 ? VAL B 476 ? SER B 467 VAL B 476 1 ? 10 
HELX_P HELX_P28 AD1 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               2.100 
_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                   8KDH 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 211 ? ? CZ A ARG 211 ? ? NH1 A ARG 211 ? ? 116.23 120.30 -4.07 0.50 N 
2 1 NE A ARG 211 ? ? CZ A ARG 211 ? ? NH2 A ARG 211 ? ? 124.39 120.30 4.09  0.50 N 
3 1 CB B TYR 188 ? ? CG B TYR 188 ? ? CD1 B TYR 188 ? ? 124.72 121.00 3.72  0.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 172 ? ? -128.08 -55.80 
2  1 ASN B 49  ? ? -151.13 3.61   
3  1 ILE B 139 ? ? -131.20 -50.84 
4  1 PHE B 161 ? ? -142.60 59.00  
5  1 SER B 189 ? ? -174.57 129.78 
6  1 ASN B 269 ? ? -153.60 79.72  
7  1 ALA B 310 ? ? -157.68 88.89  
8  1 LYS B 391 ? ? -82.52  -72.92 
9  1 TRP B 477 ? ? -128.83 -55.99 
10 1 LYS B 481 ? ? -145.85 57.71  
# 
_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     355 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.103 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8KDH 
_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                    8KDH 
_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                  3.78 
_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               170853 
_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                        8KDH 
_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              8KDH 
_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                8KDH 
_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  
CLR C1   C N N 74  
CLR C2   C N N 75  
CLR C3   C N S 76  
CLR C4   C N N 77  
CLR C5   C N N 78  
CLR C6   C N N 79  
CLR C7   C N N 80  
CLR C8   C N S 81  
CLR C9   C N S 82  
CLR C10  C N R 83  
CLR C11  C N N 84  
CLR C12  C N N 85  
CLR C13  C N R 86  
CLR C14  C N S 87  
CLR C15  C N N 88  
CLR C16  C N N 89  
CLR C17  C N R 90  
CLR C18  C N N 91  
CLR C19  C N N 92  
CLR C20  C N R 93  
CLR C21  C N N 94  
CLR C22  C N N 95  
CLR C23  C N N 96  
CLR C24  C N N 97  
CLR C25  C N N 98  
CLR C26  C N N 99  
CLR C27  C N N 100 
CLR O1   O N N 101 
CLR H11  H N N 102 
CLR H12  H N N 103 
CLR H21  H N N 104 
CLR H22  H N N 105 
CLR H3   H N N 106 
CLR H41  H N N 107 
CLR H42  H N N 108 
CLR H6   H N N 109 
CLR H71  H N N 110 
CLR H72  H N N 111 
CLR H8   H N N 112 
CLR H9   H N N 113 
CLR H111 H N N 114 
CLR H112 H N N 115 
CLR H121 H N N 116 
CLR H122 H N N 117 
CLR H14  H N N 118 
CLR H151 H N N 119 
CLR H152 H N N 120 
CLR H161 H N N 121 
CLR H162 H N N 122 
CLR H17  H N N 123 
CLR H181 H N N 124 
CLR H182 H N N 125 
CLR H183 H N N 126 
CLR H191 H N N 127 
CLR H192 H N N 128 
CLR H193 H N N 129 
CLR H20  H N N 130 
CLR H211 H N N 131 
CLR H212 H N N 132 
CLR H213 H N N 133 
CLR H221 H N N 134 
CLR H222 H N N 135 
CLR H231 H N N 136 
CLR H232 H N N 137 
CLR H241 H N N 138 
CLR H242 H N N 139 
CLR H25  H N N 140 
CLR H261 H N N 141 
CLR H262 H N N 142 
CLR H263 H N N 143 
CLR H271 H N N 144 
CLR H272 H N N 145 
CLR H273 H N N 146 
CLR H1   H N N 147 
CYS N    N N N 148 
CYS CA   C N R 149 
CYS C    C N N 150 
CYS O    O N N 151 
CYS CB   C N N 152 
CYS SG   S N N 153 
CYS OXT  O N N 154 
CYS H    H N N 155 
CYS H2   H N N 156 
CYS HA   H N N 157 
CYS HB2  H N N 158 
CYS HB3  H N N 159 
CYS HG   H N N 160 
CYS HXT  H N N 161 
GLN N    N N N 162 
GLN CA   C N S 163 
GLN C    C N N 164 
GLN O    O N N 165 
GLN CB   C N N 166 
GLN CG   C N N 167 
GLN CD   C N N 168 
GLN OE1  O N N 169 
GLN NE2  N N N 170 
GLN OXT  O N N 171 
GLN H    H N N 172 
GLN H2   H N N 173 
GLN HA   H N N 174 
GLN HB2  H N N 175 
GLN HB3  H N N 176 
GLN HG2  H N N 177 
GLN HG3  H N N 178 
GLN HE21 H N N 179 
GLN HE22 H N N 180 
GLN HXT  H N N 181 
GLU N    N N N 182 
GLU CA   C N S 183 
GLU C    C N N 184 
GLU O    O N N 185 
GLU CB   C N N 186 
GLU CG   C N N 187 
GLU CD   C N N 188 
GLU OE1  O N N 189 
GLU OE2  O N N 190 
GLU OXT  O N N 191 
GLU H    H N N 192 
GLU H2   H N N 193 
GLU HA   H N N 194 
GLU HB2  H N N 195 
GLU HB3  H N N 196 
GLU HG2  H N N 197 
GLU HG3  H N N 198 
GLU HE2  H N N 199 
GLU HXT  H N N 200 
GLY N    N N N 201 
GLY CA   C N N 202 
GLY C    C N N 203 
GLY O    O N N 204 
GLY OXT  O N N 205 
GLY H    H N N 206 
GLY H2   H N N 207 
GLY HA2  H N N 208 
GLY HA3  H N N 209 
GLY HXT  H N N 210 
HIS N    N N N 211 
HIS CA   C N S 212 
HIS C    C N N 213 
HIS O    O N N 214 
HIS CB   C N N 215 
HIS CG   C Y N 216 
HIS ND1  N Y N 217 
HIS CD2  C Y N 218 
HIS CE1  C Y N 219 
HIS NE2  N Y N 220 
HIS OXT  O N N 221 
HIS H    H N N 222 
HIS H2   H N N 223 
HIS HA   H N N 224 
HIS HB2  H N N 225 
HIS HB3  H N N 226 
HIS HD1  H N N 227 
HIS HD2  H N N 228 
HIS HE1  H N N 229 
HIS HE2  H N N 230 
HIS HXT  H N N 231 
ILE N    N N N 232 
ILE CA   C N S 233 
ILE C    C N N 234 
ILE O    O N N 235 
ILE CB   C N S 236 
ILE CG1  C N N 237 
ILE CG2  C N N 238 
ILE CD1  C N N 239 
ILE OXT  O N N 240 
ILE H    H N N 241 
ILE H2   H N N 242 
ILE HA   H N N 243 
ILE HB   H N N 244 
ILE HG12 H N N 245 
ILE HG13 H N N 246 
ILE HG21 H N N 247 
ILE HG22 H N N 248 
ILE HG23 H N N 249 
ILE HD11 H N N 250 
ILE HD12 H N N 251 
ILE HD13 H N N 252 
ILE HXT  H N N 253 
LBN C1   C N N 254 
LBN N1   N N N 255 
LBN P1   P N N 256 
LBN C2   C N R 257 
LBN C3   C N N 258 
LBN C4   C N N 259 
LBN C5   C N N 260 
LBN C6   C N N 261 
LBN O1   O N N 262 
LBN C7   C N N 263 
LBN C8   C N N 264 
LBN C9   C N N 265 
LBN O2   O N N 266 
LBN C10  C N N 267 
LBN C11  C N N 268 
LBN C12  C N N 269 
LBN O3   O N N 270 
LBN C13  C N N 271 
LBN C14  C N N 272 
LBN C15  C N N 273 
LBN O4   O N N 274 
LBN C16  C N N 275 
LBN C17  C N N 276 
LBN C18  C N N 277 
LBN C19  C N N 278 
LBN C20  C N N 279 
LBN C21  C N N 280 
LBN C22  C N N 281 
LBN C23  C N N 282 
LBN C24  C N N 283 
LBN C25  C N N 284 
LBN O5   O N N 285 
LBN C26  C N N 286 
LBN O6   O N N 287 
LBN C27  C N N 288 
LBN C28  C N N 289 
LBN C29  C N N 290 
LBN C30  C N N 291 
LBN C31  C N N 292 
LBN C32  C N N 293 
LBN C33  C N N 294 
LBN C34  C N N 295 
LBN O7   O N N 296 
LBN C35  C N N 297 
LBN O8   O N N 298 
LBN C36  C N N 299 
LBN C37  C N N 300 
LBN C38  C N N 301 
LBN C39  C N N 302 
LBN C40  C N N 303 
LBN C41  C N N 304 
LBN C42  C N N 305 
LBN H1   H N N 306 
LBN H2   H N N 307 
LBN H3   H N N 308 
LBN H4   H N N 309 
LBN H5   H N N 310 
LBN H6   H N N 311 
LBN H7   H N N 312 
LBN H8   H N N 313 
LBN H9   H N N 314 
LBN H10  H N N 315 
LBN H11  H N N 316 
LBN H12  H N N 317 
LBN H13  H N N 318 
LBN H14  H N N 319 
LBN H15  H N N 320 
LBN H16  H N N 321 
LBN H17  H N N 322 
LBN H18  H N N 323 
LBN H19  H N N 324 
LBN H20  H N N 325 
LBN H21  H N N 326 
LBN H22  H N N 327 
LBN H23  H N N 328 
LBN H24  H N N 329 
LBN H25  H N N 330 
LBN H26  H N N 331 
LBN H27  H N N 332 
LBN H28  H N N 333 
LBN H30  H N N 334 
LBN H31  H N N 335 
LBN H32  H N N 336 
LBN H33  H N N 337 
LBN H34  H N N 338 
LBN H35  H N N 339 
LBN H36  H N N 340 
LBN H37  H N N 341 
LBN H38  H N N 342 
LBN H39  H N N 343 
LBN H40  H N N 344 
LBN H41  H N N 345 
LBN H42  H N N 346 
LBN H43  H N N 347 
LBN H44  H N N 348 
LBN H45  H N N 349 
LBN H46  H N N 350 
LBN H47  H N N 351 
LBN H48  H N N 352 
LBN H49  H N N 353 
LBN H50  H N N 354 
LBN H51  H N N 355 
LBN H52  H N N 356 
LBN H53  H N N 357 
LBN H54  H N N 358 
LBN H55  H N N 359 
LBN H56  H N N 360 
LBN H57  H N N 361 
LBN H58  H N N 362 
LBN H59  H N N 363 
LBN H60  H N N 364 
LBN H61  H N N 365 
LBN H62  H N N 366 
LBN H63  H N N 367 
LBN H64  H N N 368 
LBN H65  H N N 369 
LBN H66  H N N 370 
LBN H67  H N N 371 
LBN H68  H N N 372 
LBN H69  H N N 373 
LBN H70  H N N 374 
LBN H71  H N N 375 
LBN H72  H N N 376 
LBN H73  H N N 377 
LBN H74  H N N 378 
LBN H75  H N N 379 
LBN H76  H N N 380 
LBN H77  H N N 381 
LBN H78  H N N 382 
LBN H79  H N N 383 
LBN H80  H N N 384 
LBN H81  H N N 385 
LBN H82  H N N 386 
LBN H83  H N N 387 
LEU N    N N N 388 
LEU CA   C N S 389 
LEU C    C N N 390 
LEU O    O N N 391 
LEU CB   C N N 392 
LEU CG   C N N 393 
LEU CD1  C N N 394 
LEU CD2  C N N 395 
LEU OXT  O N N 396 
LEU H    H N N 397 
LEU H2   H N N 398 
LEU HA   H N N 399 
LEU HB2  H N N 400 
LEU HB3  H N N 401 
LEU HG   H N N 402 
LEU HD11 H N N 403 
LEU HD12 H N N 404 
LEU HD13 H N N 405 
LEU HD21 H N N 406 
LEU HD22 H N N 407 
LEU HD23 H N N 408 
LEU HXT  H N N 409 
LYS N    N N N 410 
LYS CA   C N S 411 
LYS C    C N N 412 
LYS O    O N N 413 
LYS CB   C N N 414 
LYS CG   C N N 415 
LYS CD   C N N 416 
LYS CE   C N N 417 
LYS NZ   N N N 418 
LYS OXT  O N N 419 
LYS H    H N N 420 
LYS H2   H N N 421 
LYS HA   H N N 422 
LYS HB2  H N N 423 
LYS HB3  H N N 424 
LYS HG2  H N N 425 
LYS HG3  H N N 426 
LYS HD2  H N N 427 
LYS HD3  H N N 428 
LYS HE2  H N N 429 
LYS HE3  H N N 430 
LYS HZ1  H N N 431 
LYS HZ2  H N N 432 
LYS HZ3  H N N 433 
LYS HXT  H N N 434 
MET N    N N N 435 
MET CA   C N S 436 
MET C    C N N 437 
MET O    O N N 438 
MET CB   C N N 439 
MET CG   C N N 440 
MET SD   S N N 441 
MET CE   C N N 442 
MET OXT  O N N 443 
MET H    H N N 444 
MET H2   H N N 445 
MET HA   H N N 446 
MET HB2  H N N 447 
MET HB3  H N N 448 
MET HG2  H N N 449 
MET HG3  H N N 450 
MET HE1  H N N 451 
MET HE2  H N N 452 
MET HE3  H N N 453 
MET HXT  H N N 454 
PHE N    N N N 455 
PHE CA   C N S 456 
PHE C    C N N 457 
PHE O    O N N 458 
PHE CB   C N N 459 
PHE CG   C Y N 460 
PHE CD1  C Y N 461 
PHE CD2  C Y N 462 
PHE CE1  C Y N 463 
PHE CE2  C Y N 464 
PHE CZ   C Y N 465 
PHE OXT  O N N 466 
PHE H    H N N 467 
PHE H2   H N N 468 
PHE HA   H N N 469 
PHE HB2  H N N 470 
PHE HB3  H N N 471 
PHE HD1  H N N 472 
PHE HD2  H N N 473 
PHE HE1  H N N 474 
PHE HE2  H N N 475 
PHE HZ   H N N 476 
PHE HXT  H N N 477 
PRO N    N N N 478 
PRO CA   C N S 479 
PRO C    C N N 480 
PRO O    O N N 481 
PRO CB   C N N 482 
PRO CG   C N N 483 
PRO CD   C N N 484 
PRO OXT  O N N 485 
PRO H    H N N 486 
PRO HA   H N N 487 
PRO HB2  H N N 488 
PRO HB3  H N N 489 
PRO HG2  H N N 490 
PRO HG3  H N N 491 
PRO HD2  H N N 492 
PRO HD3  H N N 493 
PRO HXT  H N N 494 
SER N    N N N 495 
SER CA   C N S 496 
SER C    C N N 497 
SER O    O N N 498 
SER CB   C N N 499 
SER OG   O N N 500 
SER OXT  O N N 501 
SER H    H N N 502 
SER H2   H N N 503 
SER HA   H N N 504 
SER HB2  H N N 505 
SER HB3  H N N 506 
SER HG   H N N 507 
SER HXT  H N N 508 
THR N    N N N 509 
THR CA   C N S 510 
THR C    C N N 511 
THR O    O N N 512 
THR CB   C N R 513 
THR OG1  O N N 514 
THR CG2  C N N 515 
THR OXT  O N N 516 
THR H    H N N 517 
THR H2   H N N 518 
THR HA   H N N 519 
THR HB   H N N 520 
THR HG1  H N N 521 
THR HG21 H N N 522 
THR HG22 H N N 523 
THR HG23 H N N 524 
THR HXT  H N N 525 
TRP N    N N N 526 
TRP CA   C N S 527 
TRP C    C N N 528 
TRP O    O N N 529 
TRP CB   C N N 530 
TRP CG   C Y N 531 
TRP CD1  C Y N 532 
TRP CD2  C Y N 533 
TRP NE1  N Y N 534 
TRP CE2  C Y N 535 
TRP CE3  C Y N 536 
TRP CZ2  C Y N 537 
TRP CZ3  C Y N 538 
TRP CH2  C Y N 539 
TRP OXT  O N N 540 
TRP H    H N N 541 
TRP H2   H N N 542 
TRP HA   H N N 543 
TRP HB2  H N N 544 
TRP HB3  H N N 545 
TRP HD1  H N N 546 
TRP HE1  H N N 547 
TRP HE3  H N N 548 
TRP HZ2  H N N 549 
TRP HZ3  H N N 550 
TRP HH2  H N N 551 
TRP HXT  H N N 552 
TYR N    N N N 553 
TYR CA   C N S 554 
TYR C    C N N 555 
TYR O    O N N 556 
TYR CB   C N N 557 
TYR CG   C Y N 558 
TYR CD1  C Y N 559 
TYR CD2  C Y N 560 
TYR CE1  C Y N 561 
TYR CE2  C Y N 562 
TYR CZ   C Y N 563 
TYR OH   O N N 564 
TYR OXT  O N N 565 
TYR H    H N N 566 
TYR H2   H N N 567 
TYR HA   H N N 568 
TYR HB2  H N N 569 
TYR HB3  H N N 570 
TYR HD1  H N N 571 
TYR HD2  H N N 572 
TYR HE1  H N N 573 
TYR HE2  H N N 574 
TYR HH   H N N 575 
TYR HXT  H N N 576 
VAL N    N N N 577 
VAL CA   C N S 578 
VAL C    C N N 579 
VAL O    O N N 580 
VAL CB   C N N 581 
VAL CG1  C N N 582 
VAL CG2  C N N 583 
VAL OXT  O N N 584 
VAL H    H N N 585 
VAL H2   H N N 586 
VAL HA   H N N 587 
VAL HB   H N N 588 
VAL HG11 H N N 589 
VAL HG12 H N N 590 
VAL HG13 H N N 591 
VAL HG21 H N N 592 
VAL HG22 H N N 593 
VAL HG23 H N N 594 
VAL HXT  H N N 595 
VU0 N1   N N N 596 
VU0 C1   C N R 597 
VU0 C2   C N N 598 
VU0 C3   C N R 599 
VU0 C4   C N N 600 
VU0 C5   C N N 601 
VU0 C6   C N S 602 
VU0 C7   C N N 603 
VU0 C8   C N N 604 
VU0 O1   O N N 605 
VU0 O2   O N N 606 
VU0 H1   H N N 607 
VU0 H2   H N N 608 
VU0 H4   H N N 609 
VU0 H5   H N N 610 
VU0 H6   H N N 611 
VU0 H7   H N N 612 
VU0 H8   H N N 613 
VU0 H9   H N N 614 
VU0 H10  H N N 615 
VU0 H11  H N N 616 
VU0 H12  H N N 617 
VU0 H13  H N N 618 
VU0 H14  H N N 619 
# 
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  
CLR C1  C2   sing N N 70  
CLR C1  C10  sing N N 71  
CLR C1  H11  sing N N 72  
CLR C1  H12  sing N N 73  
CLR C2  C3   sing N N 74  
CLR C2  H21  sing N N 75  
CLR C2  H22  sing N N 76  
CLR C3  C4   sing N N 77  
CLR C3  O1   sing N N 78  
CLR C3  H3   sing N N 79  
CLR C4  C5   sing N N 80  
CLR C4  H41  sing N N 81  
CLR C4  H42  sing N N 82  
CLR C5  C6   doub N N 83  
CLR C5  C10  sing N N 84  
CLR C6  C7   sing N N 85  
CLR C6  H6   sing N N 86  
CLR C7  C8   sing N N 87  
CLR C7  H71  sing N N 88  
CLR C7  H72  sing N N 89  
CLR C8  C9   sing N N 90  
CLR C8  C14  sing N N 91  
CLR C8  H8   sing N N 92  
CLR C9  C10  sing N N 93  
CLR C9  C11  sing N N 94  
CLR C9  H9   sing N N 95  
CLR C10 C19  sing N N 96  
CLR C11 C12  sing N N 97  
CLR C11 H111 sing N N 98  
CLR C11 H112 sing N N 99  
CLR C12 C13  sing N N 100 
CLR C12 H121 sing N N 101 
CLR C12 H122 sing N N 102 
CLR C13 C14  sing N N 103 
CLR C13 C17  sing N N 104 
CLR C13 C18  sing N N 105 
CLR C14 C15  sing N N 106 
CLR C14 H14  sing N N 107 
CLR C15 C16  sing N N 108 
CLR C15 H151 sing N N 109 
CLR C15 H152 sing N N 110 
CLR C16 C17  sing N N 111 
CLR C16 H161 sing N N 112 
CLR C16 H162 sing N N 113 
CLR C17 C20  sing N N 114 
CLR C17 H17  sing N N 115 
CLR C18 H181 sing N N 116 
CLR C18 H182 sing N N 117 
CLR C18 H183 sing N N 118 
CLR C19 H191 sing N N 119 
CLR C19 H192 sing N N 120 
CLR C19 H193 sing N N 121 
CLR C20 C21  sing N N 122 
CLR C20 C22  sing N N 123 
CLR C20 H20  sing N N 124 
CLR C21 H211 sing N N 125 
CLR C21 H212 sing N N 126 
CLR C21 H213 sing N N 127 
CLR C22 C23  sing N N 128 
CLR C22 H221 sing N N 129 
CLR C22 H222 sing N N 130 
CLR C23 C24  sing N N 131 
CLR C23 H231 sing N N 132 
CLR C23 H232 sing N N 133 
CLR C24 C25  sing N N 134 
CLR C24 H241 sing N N 135 
CLR C24 H242 sing N N 136 
CLR C25 C26  sing N N 137 
CLR C25 C27  sing N N 138 
CLR C25 H25  sing N N 139 
CLR C26 H261 sing N N 140 
CLR C26 H262 sing N N 141 
CLR C26 H263 sing N N 142 
CLR C27 H271 sing N N 143 
CLR C27 H272 sing N N 144 
CLR C27 H273 sing N N 145 
CLR O1  H1   sing N N 146 
CYS N   CA   sing N N 147 
CYS N   H    sing N N 148 
CYS N   H2   sing N N 149 
CYS CA  C    sing N N 150 
CYS CA  CB   sing N N 151 
CYS CA  HA   sing N N 152 
CYS C   O    doub N N 153 
CYS C   OXT  sing N N 154 
CYS CB  SG   sing N N 155 
CYS CB  HB2  sing N N 156 
CYS CB  HB3  sing N N 157 
CYS SG  HG   sing N N 158 
CYS OXT HXT  sing N N 159 
GLN N   CA   sing N N 160 
GLN N   H    sing N N 161 
GLN N   H2   sing N N 162 
GLN CA  C    sing N N 163 
GLN CA  CB   sing N N 164 
GLN CA  HA   sing N N 165 
GLN C   O    doub N N 166 
GLN C   OXT  sing N N 167 
GLN CB  CG   sing N N 168 
GLN CB  HB2  sing N N 169 
GLN CB  HB3  sing N N 170 
GLN CG  CD   sing N N 171 
GLN CG  HG2  sing N N 172 
GLN CG  HG3  sing N N 173 
GLN CD  OE1  doub N N 174 
GLN CD  NE2  sing N N 175 
GLN NE2 HE21 sing N N 176 
GLN NE2 HE22 sing N N 177 
GLN OXT HXT  sing N N 178 
GLU N   CA   sing N N 179 
GLU N   H    sing N N 180 
GLU N   H2   sing N N 181 
GLU CA  C    sing N N 182 
GLU CA  CB   sing N N 183 
GLU CA  HA   sing N N 184 
GLU C   O    doub N N 185 
GLU C   OXT  sing N N 186 
GLU CB  CG   sing N N 187 
GLU CB  HB2  sing N N 188 
GLU CB  HB3  sing N N 189 
GLU CG  CD   sing N N 190 
GLU CG  HG2  sing N N 191 
GLU CG  HG3  sing N N 192 
GLU CD  OE1  doub N N 193 
GLU CD  OE2  sing N N 194 
GLU OE2 HE2  sing N N 195 
GLU OXT HXT  sing N N 196 
GLY N   CA   sing N N 197 
GLY N   H    sing N N 198 
GLY N   H2   sing N N 199 
GLY CA  C    sing N N 200 
GLY CA  HA2  sing N N 201 
GLY CA  HA3  sing N N 202 
GLY C   O    doub N N 203 
GLY C   OXT  sing N N 204 
GLY OXT HXT  sing N N 205 
HIS N   CA   sing N N 206 
HIS N   H    sing N N 207 
HIS N   H2   sing N N 208 
HIS CA  C    sing N N 209 
HIS CA  CB   sing N N 210 
HIS CA  HA   sing N N 211 
HIS C   O    doub N N 212 
HIS C   OXT  sing N N 213 
HIS CB  CG   sing N N 214 
HIS CB  HB2  sing N N 215 
HIS CB  HB3  sing N N 216 
HIS CG  ND1  sing Y N 217 
HIS CG  CD2  doub Y N 218 
HIS ND1 CE1  doub Y N 219 
HIS ND1 HD1  sing N N 220 
HIS CD2 NE2  sing Y N 221 
HIS CD2 HD2  sing N N 222 
HIS CE1 NE2  sing Y N 223 
HIS CE1 HE1  sing N N 224 
HIS NE2 HE2  sing N N 225 
HIS OXT HXT  sing N N 226 
ILE N   CA   sing N N 227 
ILE N   H    sing N N 228 
ILE N   H2   sing N N 229 
ILE CA  C    sing N N 230 
ILE CA  CB   sing N N 231 
ILE CA  HA   sing N N 232 
ILE C   O    doub N N 233 
ILE C   OXT  sing N N 234 
ILE CB  CG1  sing N N 235 
ILE CB  CG2  sing N N 236 
ILE CB  HB   sing N N 237 
ILE CG1 CD1  sing N N 238 
ILE CG1 HG12 sing N N 239 
ILE CG1 HG13 sing N N 240 
ILE CG2 HG21 sing N N 241 
ILE CG2 HG22 sing N N 242 
ILE CG2 HG23 sing N N 243 
ILE CD1 HD11 sing N N 244 
ILE CD1 HD12 sing N N 245 
ILE CD1 HD13 sing N N 246 
ILE OXT HXT  sing N N 247 
LBN C12 N1   sing N N 248 
LBN O3  P1   sing N N 249 
LBN O2  C9   sing N N 250 
LBN O2  P1   sing N N 251 
LBN C9  C6   sing N N 252 
LBN O4  P1   doub N N 253 
LBN P1  O1   sing N N 254 
LBN C6  N1   sing N N 255 
LBN N1  C15  sing N N 256 
LBN N1  C18  sing N N 257 
LBN O1  C1   sing N N 258 
LBN C2  C1   sing N N 259 
LBN C2  C3   sing N N 260 
LBN C2  O7   sing N N 261 
LBN C3  O5   sing N N 262 
LBN O6  C25  doub N N 263 
LBN O5  C25  sing N N 264 
LBN O7  C34  sing N N 265 
LBN C25 C26  sing N N 266 
LBN C34 C35  sing N N 267 
LBN C34 O8   doub N N 268 
LBN C26 C27  sing N N 269 
LBN C35 C36  sing N N 270 
LBN C27 C28  sing N N 271 
LBN C36 C37  sing N N 272 
LBN C28 C29  sing N N 273 
LBN C37 C38  sing N N 274 
LBN C29 C30  sing N N 275 
LBN C39 C38  sing N N 276 
LBN C39 C40  sing N N 277 
LBN C41 C40  sing N N 278 
LBN C41 C42  sing N N 279 
LBN C30 C31  sing N N 280 
LBN C42 C5   doub N Z 281 
LBN C31 C32  sing N N 282 
LBN C5  C8   sing N N 283 
LBN C8  C11  sing N N 284 
LBN C32 C33  sing N N 285 
LBN C11 C14  sing N N 286 
LBN C33 C4   sing N N 287 
LBN C14 C17  sing N N 288 
LBN C4  C7   sing N N 289 
LBN C17 C20  sing N N 290 
LBN C7  C10  sing N N 291 
LBN C20 C22  sing N N 292 
LBN C10 C13  sing N N 293 
LBN C22 C23  sing N N 294 
LBN C13 C16  sing N N 295 
LBN C23 C24  sing N N 296 
LBN C16 C19  sing N N 297 
LBN C19 C21  sing N N 298 
LBN C1  H1   sing N N 299 
LBN C1  H2   sing N N 300 
LBN C2  H3   sing N N 301 
LBN C3  H4   sing N N 302 
LBN C3  H5   sing N N 303 
LBN C4  H6   sing N N 304 
LBN C4  H7   sing N N 305 
LBN C5  H8   sing N N 306 
LBN C6  H9   sing N N 307 
LBN C6  H10  sing N N 308 
LBN C7  H11  sing N N 309 
LBN C7  H12  sing N N 310 
LBN C8  H13  sing N N 311 
LBN C8  H14  sing N N 312 
LBN C9  H15  sing N N 313 
LBN C9  H16  sing N N 314 
LBN C10 H17  sing N N 315 
LBN C10 H18  sing N N 316 
LBN C11 H19  sing N N 317 
LBN C12 H20  sing N N 318 
LBN C12 H21  sing N N 319 
LBN C12 H22  sing N N 320 
LBN C13 H23  sing N N 321 
LBN C13 H24  sing N N 322 
LBN C14 H25  sing N N 323 
LBN C15 H26  sing N N 324 
LBN C15 H27  sing N N 325 
LBN C15 H28  sing N N 326 
LBN C16 H30  sing N N 327 
LBN C16 H31  sing N N 328 
LBN C17 H32  sing N N 329 
LBN C17 H33  sing N N 330 
LBN C18 H34  sing N N 331 
LBN C18 H35  sing N N 332 
LBN C18 H36  sing N N 333 
LBN C19 H37  sing N N 334 
LBN C19 H38  sing N N 335 
LBN C20 H39  sing N N 336 
LBN C20 H40  sing N N 337 
LBN C21 H41  sing N N 338 
LBN C21 H42  sing N N 339 
LBN C21 H43  sing N N 340 
LBN C22 H44  sing N N 341 
LBN C22 H45  sing N N 342 
LBN C23 H46  sing N N 343 
LBN C23 H47  sing N N 344 
LBN C24 H48  sing N N 345 
LBN C24 H49  sing N N 346 
LBN C24 H50  sing N N 347 
LBN C26 H51  sing N N 348 
LBN C26 H52  sing N N 349 
LBN C27 H53  sing N N 350 
LBN C27 H54  sing N N 351 
LBN C28 H55  sing N N 352 
LBN C28 H56  sing N N 353 
LBN C29 H57  sing N N 354 
LBN C29 H58  sing N N 355 
LBN C30 H59  sing N N 356 
LBN C30 H60  sing N N 357 
LBN C31 H61  sing N N 358 
LBN C31 H62  sing N N 359 
LBN C32 H63  sing N N 360 
LBN C32 H64  sing N N 361 
LBN C33 H65  sing N N 362 
LBN C33 H66  sing N N 363 
LBN C35 H67  sing N N 364 
LBN C35 H68  sing N N 365 
LBN C36 H69  sing N N 366 
LBN C36 H70  sing N N 367 
LBN C37 H71  sing N N 368 
LBN C37 H72  sing N N 369 
LBN C38 H73  sing N N 370 
LBN C38 H74  sing N N 371 
LBN C39 H75  sing N N 372 
LBN C40 H76  sing N N 373 
LBN C41 H77  sing N N 374 
LBN C41 H78  sing N N 375 
LBN C42 H79  sing N N 376 
LBN C11 H80  sing N N 377 
LBN C14 H81  sing N N 378 
LBN C39 H82  sing N N 379 
LBN C40 H83  sing N N 380 
LEU N   CA   sing N N 381 
LEU N   H    sing N N 382 
LEU N   H2   sing N N 383 
LEU CA  C    sing N N 384 
LEU CA  CB   sing N N 385 
LEU CA  HA   sing N N 386 
LEU C   O    doub N N 387 
LEU C   OXT  sing N N 388 
LEU CB  CG   sing N N 389 
LEU CB  HB2  sing N N 390 
LEU CB  HB3  sing N N 391 
LEU CG  CD1  sing N N 392 
LEU CG  CD2  sing N N 393 
LEU CG  HG   sing N N 394 
LEU CD1 HD11 sing N N 395 
LEU CD1 HD12 sing N N 396 
LEU CD1 HD13 sing N N 397 
LEU CD2 HD21 sing N N 398 
LEU CD2 HD22 sing N N 399 
LEU CD2 HD23 sing N N 400 
LEU OXT HXT  sing N N 401 
LYS N   CA   sing N N 402 
LYS N   H    sing N N 403 
LYS N   H2   sing N N 404 
LYS CA  C    sing N N 405 
LYS CA  CB   sing N N 406 
LYS CA  HA   sing N N 407 
LYS C   O    doub N N 408 
LYS C   OXT  sing N N 409 
LYS CB  CG   sing N N 410 
LYS CB  HB2  sing N N 411 
LYS CB  HB3  sing N N 412 
LYS CG  CD   sing N N 413 
LYS CG  HG2  sing N N 414 
LYS CG  HG3  sing N N 415 
LYS CD  CE   sing N N 416 
LYS CD  HD2  sing N N 417 
LYS CD  HD3  sing N N 418 
LYS CE  NZ   sing N N 419 
LYS CE  HE2  sing N N 420 
LYS CE  HE3  sing N N 421 
LYS NZ  HZ1  sing N N 422 
LYS NZ  HZ2  sing N N 423 
LYS NZ  HZ3  sing N N 424 
LYS OXT HXT  sing N N 425 
MET N   CA   sing N N 426 
MET N   H    sing N N 427 
MET N   H2   sing N N 428 
MET CA  C    sing N N 429 
MET CA  CB   sing N N 430 
MET CA  HA   sing N N 431 
MET C   O    doub N N 432 
MET C   OXT  sing N N 433 
MET CB  CG   sing N N 434 
MET CB  HB2  sing N N 435 
MET CB  HB3  sing N N 436 
MET CG  SD   sing N N 437 
MET CG  HG2  sing N N 438 
MET CG  HG3  sing N N 439 
MET SD  CE   sing N N 440 
MET CE  HE1  sing N N 441 
MET CE  HE2  sing N N 442 
MET CE  HE3  sing N N 443 
MET OXT HXT  sing N N 444 
PHE N   CA   sing N N 445 
PHE N   H    sing N N 446 
PHE N   H2   sing N N 447 
PHE CA  C    sing N N 448 
PHE CA  CB   sing N N 449 
PHE CA  HA   sing N N 450 
PHE C   O    doub N N 451 
PHE C   OXT  sing N N 452 
PHE CB  CG   sing N N 453 
PHE CB  HB2  sing N N 454 
PHE CB  HB3  sing N N 455 
PHE CG  CD1  doub Y N 456 
PHE CG  CD2  sing Y N 457 
PHE CD1 CE1  sing Y N 458 
PHE CD1 HD1  sing N N 459 
PHE CD2 CE2  doub Y N 460 
PHE CD2 HD2  sing N N 461 
PHE CE1 CZ   doub Y N 462 
PHE CE1 HE1  sing N N 463 
PHE CE2 CZ   sing Y N 464 
PHE CE2 HE2  sing N N 465 
PHE CZ  HZ   sing N N 466 
PHE OXT HXT  sing N N 467 
PRO N   CA   sing N N 468 
PRO N   CD   sing N N 469 
PRO N   H    sing N N 470 
PRO CA  C    sing N N 471 
PRO CA  CB   sing N N 472 
PRO CA  HA   sing N N 473 
PRO C   O    doub N N 474 
PRO C   OXT  sing N N 475 
PRO CB  CG   sing N N 476 
PRO CB  HB2  sing N N 477 
PRO CB  HB3  sing N N 478 
PRO CG  CD   sing N N 479 
PRO CG  HG2  sing N N 480 
PRO CG  HG3  sing N N 481 
PRO CD  HD2  sing N N 482 
PRO CD  HD3  sing N N 483 
PRO OXT HXT  sing N N 484 
SER N   CA   sing N N 485 
SER N   H    sing N N 486 
SER N   H2   sing N N 487 
SER CA  C    sing N N 488 
SER CA  CB   sing N N 489 
SER CA  HA   sing N N 490 
SER C   O    doub N N 491 
SER C   OXT  sing N N 492 
SER CB  OG   sing N N 493 
SER CB  HB2  sing N N 494 
SER CB  HB3  sing N N 495 
SER OG  HG   sing N N 496 
SER OXT HXT  sing N N 497 
THR N   CA   sing N N 498 
THR N   H    sing N N 499 
THR N   H2   sing N N 500 
THR CA  C    sing N N 501 
THR CA  CB   sing N N 502 
THR CA  HA   sing N N 503 
THR C   O    doub N N 504 
THR C   OXT  sing N N 505 
THR CB  OG1  sing N N 506 
THR CB  CG2  sing N N 507 
THR CB  HB   sing N N 508 
THR OG1 HG1  sing N N 509 
THR CG2 HG21 sing N N 510 
THR CG2 HG22 sing N N 511 
THR CG2 HG23 sing N N 512 
THR OXT HXT  sing N N 513 
TRP N   CA   sing N N 514 
TRP N   H    sing N N 515 
TRP N   H2   sing N N 516 
TRP CA  C    sing N N 517 
TRP CA  CB   sing N N 518 
TRP CA  HA   sing N N 519 
TRP C   O    doub N N 520 
TRP C   OXT  sing N N 521 
TRP CB  CG   sing N N 522 
TRP CB  HB2  sing N N 523 
TRP CB  HB3  sing N N 524 
TRP CG  CD1  doub Y N 525 
TRP CG  CD2  sing Y N 526 
TRP CD1 NE1  sing Y N 527 
TRP CD1 HD1  sing N N 528 
TRP CD2 CE2  doub Y N 529 
TRP CD2 CE3  sing Y N 530 
TRP NE1 CE2  sing Y N 531 
TRP NE1 HE1  sing N N 532 
TRP CE2 CZ2  sing Y N 533 
TRP CE3 CZ3  doub Y N 534 
TRP CE3 HE3  sing N N 535 
TRP CZ2 CH2  doub Y N 536 
TRP CZ2 HZ2  sing N N 537 
TRP CZ3 CH2  sing Y N 538 
TRP CZ3 HZ3  sing N N 539 
TRP CH2 HH2  sing N N 540 
TRP OXT HXT  sing N N 541 
TYR N   CA   sing N N 542 
TYR N   H    sing N N 543 
TYR N   H2   sing N N 544 
TYR CA  C    sing N N 545 
TYR CA  CB   sing N N 546 
TYR CA  HA   sing N N 547 
TYR C   O    doub N N 548 
TYR C   OXT  sing N N 549 
TYR CB  CG   sing N N 550 
TYR CB  HB2  sing N N 551 
TYR CB  HB3  sing N N 552 
TYR CG  CD1  doub Y N 553 
TYR CG  CD2  sing Y N 554 
TYR CD1 CE1  sing Y N 555 
TYR CD1 HD1  sing N N 556 
TYR CD2 CE2  doub Y N 557 
TYR CD2 HD2  sing N N 558 
TYR CE1 CZ   doub Y N 559 
TYR CE1 HE1  sing N N 560 
TYR CE2 CZ   sing Y N 561 
TYR CE2 HE2  sing N N 562 
TYR CZ  OH   sing N N 563 
TYR OH  HH   sing N N 564 
TYR OXT HXT  sing N N 565 
VAL N   CA   sing N N 566 
VAL N   H    sing N N 567 
VAL N   H2   sing N N 568 
VAL CA  C    sing N N 569 
VAL CA  CB   sing N N 570 
VAL CA  HA   sing N N 571 
VAL C   O    doub N N 572 
VAL C   OXT  sing N N 573 
VAL CB  CG1  sing N N 574 
VAL CB  CG2  sing N N 575 
VAL CB  HB   sing N N 576 
VAL CG1 HG11 sing N N 577 
VAL CG1 HG12 sing N N 578 
VAL CG1 HG13 sing N N 579 
VAL CG2 HG21 sing N N 580 
VAL CG2 HG22 sing N N 581 
VAL CG2 HG23 sing N N 582 
VAL OXT HXT  sing N N 583 
VU0 C5  C4   sing N N 584 
VU0 C5  C6   sing N N 585 
VU0 C4  C3   sing N N 586 
VU0 N1  C1   sing N N 587 
VU0 C6  C1   sing N N 588 
VU0 C6  C7   sing N N 589 
VU0 C3  C7   sing N N 590 
VU0 C3  C2   sing N N 591 
VU0 C1  C2   sing N N 592 
VU0 C1  C8   sing N N 593 
VU0 C8  O2   doub N N 594 
VU0 C8  O1   sing N N 595 
VU0 N1  H1   sing N N 596 
VU0 N1  H2   sing N N 597 
VU0 C2  H4   sing N N 598 
VU0 C2  H5   sing N N 599 
VU0 C3  H6   sing N N 600 
VU0 C4  H7   sing N N 601 
VU0 C4  H8   sing N N 602 
VU0 C5  H9   sing N N 603 
VU0 C5  H10  sing N N 604 
VU0 C6  H11  sing N N 605 
VU0 C7  H12  sing N N 606 
VU0 C7  H13  sing N N 607 
VU0 O1  H14  sing N N 608 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-08-09 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8KDH 
_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 BCH, 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                    8KDH 
_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 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . THR A 1 163 ? 74.802  86.920  29.873 1.00 221.69 ? 162 THR A N   1 
ATOM   2    C CA  . THR A 1 163 ? 75.173  88.366  29.932 1.00 277.56 ? 162 THR A CA  1 
ATOM   3    C C   . THR A 1 163 ? 76.642  88.559  30.335 1.00 249.59 ? 162 THR A C   1 
ATOM   4    O O   . THR A 1 163 ? 76.894  89.066  31.426 1.00 120.64 ? 162 THR A O   1 
ATOM   5    C CB  . THR A 1 163 ? 74.245  89.151  30.881 1.00 331.88 ? 162 THR A CB  1 
ATOM   6    O OG1 . THR A 1 163 ? 74.337  88.682  32.230 1.00 339.34 ? 162 THR A OG1 1 
ATOM   7    C CG2 . THR A 1 163 ? 72.791  89.084  30.461 1.00 359.20 ? 162 THR A CG2 1 
ATOM   8    N N   . GLY A 1 164 ? 77.555  88.164  29.420 1.00 279.61 ? 163 GLY A N   1 
ATOM   9    C CA  . GLY A 1 164 ? 79.004  88.112  29.590 1.00 221.17 ? 163 GLY A CA  1 
ATOM   10   C C   . GLY A 1 164 ? 79.688  87.610  28.311 1.00 201.94 ? 163 GLY A C   1 
ATOM   11   O O   . GLY A 1 164 ? 79.072  87.549  27.246 1.00 257.16 ? 163 GLY A O   1 
ATOM   12   N N   . LEU A 1 165 ? 80.966  87.236  28.419 1.00 197.19 ? 164 LEU A N   1 
ATOM   13   C CA  . LEU A 1 165 ? 81.760  86.760  27.284 1.00 181.43 ? 164 LEU A CA  1 
ATOM   14   C C   . LEU A 1 165 ? 81.295  85.356  26.869 1.00 177.58 ? 164 LEU A C   1 
ATOM   15   O O   . LEU A 1 165 ? 81.025  84.517  27.726 1.00 286.12 ? 164 LEU A O   1 
ATOM   16   C CB  . LEU A 1 165 ? 83.255  86.721  27.651 1.00 164.62 ? 164 LEU A CB  1 
ATOM   17   C CG  . LEU A 1 165 ? 83.850  87.968  28.314 1.00 207.54 ? 164 LEU A CG  1 
ATOM   18   C CD1 . LEU A 1 165 ? 85.351  87.784  28.485 1.00 234.01 ? 164 LEU A CD1 1 
ATOM   19   C CD2 . LEU A 1 165 ? 83.541  89.254  27.543 1.00 219.79 ? 164 LEU A CD2 1 
ATOM   20   N N   . SER A 1 166 ? 81.219  85.085  25.556 1.00 209.12 ? 165 SER A N   1 
ATOM   21   C CA  . SER A 1 166 ? 81.095  83.730  25.009 1.00 206.44 ? 165 SER A CA  1 
ATOM   22   C C   . SER A 1 166 ? 82.380  82.914  25.205 1.00 166.97 ? 165 SER A C   1 
ATOM   23   O O   . SER A 1 166 ? 83.394  83.459  25.684 1.00 163.02 ? 165 SER A O   1 
ATOM   24   C CB  . SER A 1 166 ? 80.743  83.779  23.540 1.00 240.19 ? 165 SER A CB  1 
ATOM   25   O OG  . SER A 1 166 ? 81.861  84.189  22.752 1.00 224.15 ? 165 SER A OG  1 
ATOM   26   N N   . LYS A 1 167 ? 82.357  81.618  24.808 1.00 135.77 ? 166 LYS A N   1 
ATOM   27   C CA  . LYS A 1 167 ? 83.578  80.805  24.824 1.00 220.93 ? 166 LYS A CA  1 
ATOM   28   C C   . LYS A 1 167 ? 84.704  81.423  23.966 1.00 262.08 ? 166 LYS A C   1 
ATOM   29   O O   . LYS A 1 167 ? 85.884  81.447  24.382 1.00 224.33 ? 166 LYS A O   1 
ATOM   30   C CB  . LYS A 1 167 ? 83.312  79.355  24.393 1.00 213.24 ? 166 LYS A CB  1 
ATOM   31   C CG  . LYS A 1 167 ? 84.582  78.504  24.438 1.00 214.95 ? 166 LYS A CG  1 
ATOM   32   C CD  . LYS A 1 167 ? 84.408  77.035  24.187 1.00 234.65 ? 166 LYS A CD  1 
ATOM   33   C CE  . LYS A 1 167 ? 85.725  76.286  24.292 1.00 271.16 ? 166 LYS A CE  1 
ATOM   34   N NZ  . LYS A 1 167 ? 86.628  76.521  23.136 1.00 301.06 ? 166 LYS A NZ  1 
ATOM   35   N N   . GLU A 1 168 ? 84.316  81.908  22.773 1.00 263.07 ? 167 GLU A N   1 
ATOM   36   C CA  . GLU A 1 168 ? 85.199  82.542  21.806 1.00 263.10 ? 167 GLU A CA  1 
ATOM   37   C C   . GLU A 1 168 ? 85.818  83.810  22.398 1.00 241.84 ? 167 GLU A C   1 
ATOM   38   O O   . GLU A 1 168 ? 87.039  83.987  22.326 1.00 268.21 ? 167 GLU A O   1 
ATOM   39   C CB  . GLU A 1 168 ? 84.395  82.817  20.529 1.00 306.14 ? 167 GLU A CB  1 
ATOM   40   C CG  . GLU A 1 168 ? 85.162  83.529  19.418 1.00 378.62 ? 167 GLU A CG  1 
ATOM   41   C CD  . GLU A 1 168 ? 84.293  84.049  18.281 1.00 405.51 ? 167 GLU A CD  1 
ATOM   42   O OE1 . GLU A 1 168 ? 83.431  83.283  17.805 1.00 446.11 ? 167 GLU A OE1 1 
ATOM   43   O OE2 . GLU A 1 168 ? 84.478  85.223  17.866 1.00 390.52 ? 167 GLU A OE2 1 
ATOM   44   N N   . GLU A 1 169 ? 84.978  84.689  22.969 1.00 200.89 ? 168 GLU A N   1 
ATOM   45   C CA  . GLU A 1 169 ? 85.433  85.935  23.578 1.00 248.04 ? 168 GLU A CA  1 
ATOM   46   C C   . GLU A 1 169 ? 86.309  85.685  24.813 1.00 227.59 ? 168 GLU A C   1 
ATOM   47   O O   . GLU A 1 169 ? 87.273  86.425  25.029 1.00 217.35 ? 168 GLU A O   1 
ATOM   48   C CB  . GLU A 1 169 ? 84.238  86.812  23.944 1.00 246.71 ? 168 GLU A CB  1 
ATOM   49   C CG  . GLU A 1 169 ? 83.486  87.382  22.758 1.00 272.58 ? 168 GLU A CG  1 
ATOM   50   C CD  . GLU A 1 169 ? 82.194  88.098  23.131 1.00 329.39 ? 168 GLU A CD  1 
ATOM   51   O OE1 . GLU A 1 169 ? 81.334  87.470  23.798 1.00 385.35 ? 168 GLU A OE1 1 
ATOM   52   O OE2 . GLU A 1 169 ? 82.036  89.290  22.758 1.00 329.53 ? 168 GLU A OE2 1 
ATOM   53   N N   . LEU A 1 170 ? 85.993  84.655  25.615 1.00 189.49 ? 169 LEU A N   1 
ATOM   54   C CA  . LEU A 1 170 ? 86.801  84.334  26.781 1.00 206.76 ? 169 LEU A CA  1 
ATOM   55   C C   . LEU A 1 170 ? 88.202  83.852  26.381 1.00 254.57 ? 169 LEU A C   1 
ATOM   56   O O   . LEU A 1 170 ? 89.189  84.407  26.870 1.00 334.61 ? 169 LEU A O   1 
ATOM   57   C CB  . LEU A 1 170 ? 86.101  83.298  27.656 1.00 236.55 ? 169 LEU A CB  1 
ATOM   58   C CG  . LEU A 1 170 ? 86.898  82.910  28.912 1.00 291.12 ? 169 LEU A CG  1 
ATOM   59   C CD1 . LEU A 1 170 ? 86.872  84.024  29.947 1.00 309.45 ? 169 LEU A CD1 1 
ATOM   60   C CD2 . LEU A 1 170 ? 86.395  81.617  29.525 1.00 357.40 ? 169 LEU A CD2 1 
ATOM   61   N N   . LEU A 1 171 ? 88.315  82.837  25.513 1.00 218.71 ? 170 LEU A N   1 
ATOM   62   C CA  . LEU A 1 171 ? 89.626  82.290  25.165 1.00 277.73 ? 170 LEU A CA  1 
ATOM   63   C C   . LEU A 1 171 ? 90.515  83.327  24.439 1.00 290.43 ? 170 LEU A C   1 
ATOM   64   O O   . LEU A 1 171 ? 91.743  83.249  24.502 1.00 259.97 ? 170 LEU A O   1 
ATOM   65   C CB  . LEU A 1 171 ? 89.411  81.010  24.345 1.00 340.13 ? 170 LEU A CB  1 
ATOM   66   C CG  . LEU A 1 171 ? 90.662  80.184  24.040 1.00 413.82 ? 170 LEU A CG  1 
ATOM   67   C CD1 . LEU A 1 171 ? 91.305  79.649  25.312 1.00 420.14 ? 170 LEU A CD1 1 
ATOM   68   C CD2 . LEU A 1 171 ? 90.329  79.037  23.101 1.00 451.02 ? 170 LEU A CD2 1 
ATOM   69   N N   . LYS A 1 172 ? 89.906  84.317  23.762 1.00 287.17 ? 171 LYS A N   1 
ATOM   70   C CA  . LYS A 1 172 ? 90.599  85.449  23.147 1.00 306.01 ? 171 LYS A CA  1 
ATOM   71   C C   . LYS A 1 172 ? 91.163  86.467  24.162 1.00 279.40 ? 171 LYS A C   1 
ATOM   72   O O   . LYS A 1 172 ? 91.896  87.371  23.752 1.00 331.84 ? 171 LYS A O   1 
ATOM   73   C CB  . LYS A 1 172 ? 89.624  86.100  22.153 1.00 313.79 ? 171 LYS A CB  1 
ATOM   74   C CG  . LYS A 1 172 ? 90.227  87.102  21.175 1.00 335.60 ? 171 LYS A CG  1 
ATOM   75   C CD  . LYS A 1 172 ? 89.385  87.338  19.928 1.00 351.44 ? 171 LYS A CD  1 
ATOM   76   C CE  . LYS A 1 172 ? 88.001  87.909  20.180 1.00 380.38 ? 171 LYS A CE  1 
ATOM   77   N NZ  . LYS A 1 172 ? 88.029  89.321  20.638 1.00 394.37 ? 171 LYS A NZ  1 
ATOM   78   N N   . VAL A 1 173 ? 90.851  86.352  25.472 1.00 229.58 ? 172 VAL A N   1 
ATOM   79   C CA  . VAL A 1 173 ? 91.309  87.283  26.511 1.00 256.42 ? 172 VAL A CA  1 
ATOM   80   C C   . VAL A 1 173 ? 91.972  86.547  27.688 1.00 224.34 ? 172 VAL A C   1 
ATOM   81   O O   . VAL A 1 173 ? 93.122  86.839  28.032 1.00 223.30 ? 172 VAL A O   1 
ATOM   82   C CB  . VAL A 1 173 ? 90.147  88.185  26.992 1.00 245.80 ? 172 VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 173 ? 90.528  89.080  28.176 1.00 231.41 ? 172 VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 173 ? 89.588  89.019  25.845 1.00 262.36 ? 172 VAL A CG2 1 
ATOM   85   N N   . ALA A 1 174 ? 91.246  85.598  28.296 1.00 250.05 ? 173 ALA A N   1 
ATOM   86   C CA  . ALA A 1 174 ? 91.639  84.934  29.535 1.00 270.66 ? 173 ALA A CA  1 
ATOM   87   C C   . ALA A 1 174 ? 92.749  83.881  29.349 1.00 242.97 ? 173 ALA A C   1 
ATOM   88   O O   . ALA A 1 174 ? 93.229  83.338  30.346 1.00 264.66 ? 173 ALA A O   1 
ATOM   89   C CB  . ALA A 1 174 ? 90.386  84.329  30.142 1.00 302.59 ? 173 ALA A CB  1 
ATOM   90   N N   . GLY A 1 175 ? 93.154  83.583  28.098 1.00 208.97 ? 174 GLY A N   1 
ATOM   91   C CA  . GLY A 1 175 ? 94.334  82.781  27.794 1.00 243.29 ? 174 GLY A CA  1 
ATOM   92   C C   . GLY A 1 175 ? 95.667  83.546  27.789 1.00 269.04 ? 174 GLY A C   1 
ATOM   93   O O   . GLY A 1 175 ? 96.710  82.930  27.551 1.00 266.28 ? 174 GLY A O   1 
ATOM   94   N N   . SER A 1 176 ? 95.653  84.871  28.052 1.00 251.46 ? 175 SER A N   1 
ATOM   95   C CA  . SER A 1 176 ? 96.854  85.705  28.128 1.00 246.44 ? 175 SER A CA  1 
ATOM   96   C C   . SER A 1 176 ? 97.805  85.239  29.236 1.00 255.12 ? 175 SER A C   1 
ATOM   97   O O   . SER A 1 176 ? 97.326  84.937  30.326 1.00 324.46 ? 175 SER A O   1 
ATOM   98   C CB  . SER A 1 176 ? 96.506  87.156  28.368 1.00 245.18 ? 175 SER A CB  1 
ATOM   99   O OG  . SER A 1 176 ? 95.627  87.659  27.371 1.00 297.03 ? 175 SER A OG  1 
ATOM   100  N N   . PRO A 1 177 ? 99.150  85.172  29.031 1.00 276.93 ? 176 PRO A N   1 
ATOM   101  C CA  . PRO A 1 177 ? 100.089 84.721  30.071 1.00 277.45 ? 176 PRO A CA  1 
ATOM   102  C C   . PRO A 1 177 ? 99.957  85.378  31.452 1.00 279.70 ? 176 PRO A C   1 
ATOM   103  O O   . PRO A 1 177 ? 100.202 84.694  32.445 1.00 239.75 ? 176 PRO A O   1 
ATOM   104  C CB  . PRO A 1 177 ? 101.473 85.015  29.458 1.00 327.41 ? 176 PRO A CB  1 
ATOM   105  C CG  . PRO A 1 177 ? 101.234 84.919  27.975 1.00 336.05 ? 176 PRO A CG  1 
ATOM   106  C CD  . PRO A 1 177 ? 99.849  85.500  27.780 1.00 318.04 ? 176 PRO A CD  1 
ATOM   107  N N   . GLY A 1 178 ? 99.557  86.666  31.523 1.00 288.96 ? 177 GLY A N   1 
ATOM   108  C CA  . GLY A 1 178 ? 99.253  87.349  32.780 1.00 315.33 ? 177 GLY A CA  1 
ATOM   109  C C   . GLY A 1 178 ? 98.088  86.720  33.560 1.00 280.72 ? 177 GLY A C   1 
ATOM   110  O O   . GLY A 1 178 ? 98.179  86.493  34.772 1.00 232.35 ? 177 GLY A O   1 
ATOM   111  N N   . TRP A 1 179 ? 96.982  86.428  32.866 1.00 234.85 ? 178 TRP A N   1 
ATOM   112  C CA  . TRP A 1 179 ? 95.869  85.696  33.464 1.00 163.27 ? 178 TRP A CA  1 
ATOM   113  C C   . TRP A 1 179 ? 96.247  84.246  33.778 1.00 139.23 ? 178 TRP A C   1 
ATOM   114  O O   . TRP A 1 179 ? 95.844  83.767  34.830 1.00 233.37 ? 178 TRP A O   1 
ATOM   115  C CB  . TRP A 1 179 ? 94.616  85.761  32.586 1.00 153.52 ? 178 TRP A CB  1 
ATOM   116  C CG  . TRP A 1 179 ? 93.933  87.105  32.589 1.00 204.79 ? 178 TRP A CG  1 
ATOM   117  C CD1 . TRP A 1 179 ? 93.735  87.883  31.486 1.00 295.22 ? 178 TRP A CD1 1 
ATOM   118  C CD2 . TRP A 1 179 ? 93.349  87.833  33.701 1.00 169.60 ? 178 TRP A CD2 1 
ATOM   119  N NE1 . TRP A 1 179 ? 93.080  89.039  31.831 1.00 289.90 ? 178 TRP A NE1 1 
ATOM   120  C CE2 . TRP A 1 179 ? 92.826  89.041  33.183 1.00 228.26 ? 178 TRP A CE2 1 
ATOM   121  C CE3 . TRP A 1 179 ? 93.218  87.587  35.073 1.00 242.37 ? 178 TRP A CE3 1 
ATOM   122  C CZ2 . TRP A 1 179 ? 92.185  89.989  33.996 1.00 234.79 ? 178 TRP A CZ2 1 
ATOM   123  C CZ3 . TRP A 1 179 ? 92.585  88.520  35.876 1.00 279.67 ? 178 TRP A CZ3 1 
ATOM   124  C CH2 . TRP A 1 179 ? 92.075  89.705  35.341 1.00 261.50 ? 178 TRP A CH2 1 
ATOM   125  N N   . VAL A 1 180 ? 97.020  83.549  32.935 1.00 131.27 ? 179 VAL A N   1 
ATOM   126  C CA  . VAL A 1 180 ? 97.476  82.186  33.225 1.00 167.60 ? 179 VAL A CA  1 
ATOM   127  C C   . VAL A 1 180 ? 98.318  82.148  34.511 1.00 179.13 ? 179 VAL A C   1 
ATOM   128  O O   . VAL A 1 180 ? 98.078  81.295  35.366 1.00 219.02 ? 179 VAL A O   1 
ATOM   129  C CB  . VAL A 1 180 ? 98.240  81.559  32.040 1.00 236.38 ? 179 VAL A CB  1 
ATOM   130  C CG1 . VAL A 1 180 ? 98.854  80.195  32.374 1.00 243.71 ? 179 VAL A CG1 1 
ATOM   131  C CG2 . VAL A 1 180 ? 97.345  81.432  30.814 1.00 287.10 ? 179 VAL A CG2 1 
ATOM   132  N N   . ARG A 1 181 ? 99.279  83.066  34.668 1.00 191.48 ? 180 ARG A N   1 
ATOM   133  C CA  . ARG A 1 181 ? 100.090 83.151  35.876 1.00 243.56 ? 180 ARG A CA  1 
ATOM   134  C C   . ARG A 1 181 ? 99.245  83.569  37.089 1.00 223.04 ? 180 ARG A C   1 
ATOM   135  O O   . ARG A 1 181 ? 99.441  83.033  38.184 1.00 263.45 ? 180 ARG A O   1 
ATOM   136  C CB  . ARG A 1 181 ? 101.280 84.090  35.642 1.00 299.08 ? 180 ARG A CB  1 
ATOM   137  C CG  . ARG A 1 181 ? 102.339 83.513  34.715 1.00 307.64 ? 180 ARG A CG  1 
ATOM   138  C CD  . ARG A 1 181 ? 103.373 84.561  34.329 1.00 343.84 ? 180 ARG A CD  1 
ATOM   139  N NE  . ARG A 1 181 ? 104.253 84.919  35.446 1.00 372.08 ? 180 ARG A NE  1 
ATOM   140  C CZ  . ARG A 1 181 ? 105.198 85.863  35.419 1.00 362.74 ? 180 ARG A CZ  1 
ATOM   141  N NH1 . ARG A 1 181 ? 105.951 86.089  36.486 1.00 285.01 ? 180 ARG A NH1 1 
ATOM   142  N NH2 . ARG A 1 181 ? 105.389 86.581  34.324 1.00 389.10 ? 180 ARG A NH2 1 
ATOM   143  N N   . THR A 1 182 ? 98.302  84.510  36.926 1.00 169.17 ? 181 THR A N   1 
ATOM   144  C CA  . THR A 1 182 ? 97.381  84.880  37.999 1.00 184.47 ? 181 THR A CA  1 
ATOM   145  C C   . THR A 1 182 ? 96.554  83.674  38.459 1.00 143.71 ? 181 THR A C   1 
ATOM   146  O O   . THR A 1 182 ? 96.422  83.429  39.650 1.00 152.73 ? 181 THR A O   1 
ATOM   147  C CB  . THR A 1 182 ? 96.453  86.036  37.586 1.00 229.89 ? 181 THR A CB  1 
ATOM   148  O OG1 . THR A 1 182 ? 97.258  87.161  37.226 1.00 259.65 ? 181 THR A OG1 1 
ATOM   149  C CG2 . THR A 1 182 ? 95.478  86.464  38.669 1.00 190.86 ? 181 THR A CG2 1 
ATOM   150  N N   . ARG A 1 183 ? 95.988  82.915  37.525 1.00 161.73 ? 182 ARG A N   1 
ATOM   151  C CA  . ARG A 1 183 ? 95.180  81.739  37.812 1.00 172.68 ? 182 ARG A CA  1 
ATOM   152  C C   . ARG A 1 183 ? 96.012  80.640  38.486 1.00 160.14 ? 182 ARG A C   1 
ATOM   153  O O   . ARG A 1 183 ? 95.531  80.020  39.435 1.00 281.46 ? 182 ARG A O   1 
ATOM   154  C CB  . ARG A 1 183 ? 94.527  81.265  36.512 1.00 198.63 ? 182 ARG A CB  1 
ATOM   155  C CG  . ARG A 1 183 ? 93.439  80.216  36.683 1.00 232.64 ? 182 ARG A CG  1 
ATOM   156  C CD  . ARG A 1 183 ? 92.835  79.833  35.345 1.00 241.67 ? 182 ARG A CD  1 
ATOM   157  N NE  . ARG A 1 183 ? 92.305  81.025  34.687 1.00 219.37 ? 182 ARG A NE  1 
ATOM   158  C CZ  . ARG A 1 183 ? 92.579  81.421  33.443 1.00 201.77 ? 182 ARG A CZ  1 
ATOM   159  N NH1 . ARG A 1 183 ? 92.147  82.600  33.033 1.00 164.89 ? 182 ARG A NH1 1 
ATOM   160  N NH2 . ARG A 1 183 ? 93.285  80.651  32.622 1.00 205.61 ? 182 ARG A NH2 1 
ATOM   161  N N   . TRP A 1 184 ? 97.243  80.395  38.044 1.00 131.22 ? 183 TRP A N   1 
ATOM   162  C CA  . TRP A 1 184 ? 98.164  79.519  38.758 1.00 189.58 ? 183 TRP A CA  1 
ATOM   163  C C   . TRP A 1 184 ? 98.437  79.994  40.194 1.00 164.10 ? 183 TRP A C   1 
ATOM   164  O O   . TRP A 1 184 ? 98.400  79.200  41.137 1.00 203.44 ? 183 TRP A O   1 
ATOM   165  C CB  . TRP A 1 184 ? 99.477  79.411  37.982 1.00 249.33 ? 183 TRP A CB  1 
ATOM   166  C CG  . TRP A 1 184 ? 100.493 78.529  38.654 1.00 242.59 ? 183 TRP A CG  1 
ATOM   167  C CD1 . TRP A 1 184 ? 101.550 78.946  39.407 1.00 184.24 ? 183 TRP A CD1 1 
ATOM   168  C CD2 . TRP A 1 184 ? 100.539 77.079  38.632 1.00 247.40 ? 183 TRP A CD2 1 
ATOM   169  N NE1 . TRP A 1 184 ? 102.260 77.858  39.841 1.00 209.79 ? 183 TRP A NE1 1 
ATOM   170  C CE2 . TRP A 1 184 ? 101.670 76.697  39.391 1.00 251.72 ? 183 TRP A CE2 1 
ATOM   171  C CE3 . TRP A 1 184 ? 99.747  76.072  38.051 1.00 258.86 ? 183 TRP A CE3 1 
ATOM   172  C CZ2 . TRP A 1 184 ? 102.014 75.347  39.577 1.00 315.86 ? 183 TRP A CZ2 1 
ATOM   173  C CZ3 . TRP A 1 184 ? 100.084 74.744  38.237 1.00 292.29 ? 183 TRP A CZ3 1 
ATOM   174  C CH2 . TRP A 1 184 ? 101.208 74.389  38.990 1.00 329.47 ? 183 TRP A CH2 1 
ATOM   175  N N   . ALA A 1 185 ? 98.697  81.287  40.370 1.00 139.70 ? 184 ALA A N   1 
ATOM   176  C CA  . ALA A 1 185 ? 98.894  81.853  41.695 1.00 233.05 ? 184 ALA A CA  1 
ATOM   177  C C   . ALA A 1 185 ? 97.664  81.638  42.592 1.00 171.22 ? 184 ALA A C   1 
ATOM   178  O O   . ALA A 1 185 ? 97.830  81.172  43.708 1.00 139.79 ? 184 ALA A O   1 
ATOM   179  C CB  . ALA A 1 185 ? 99.283  83.317  41.582 1.00 327.63 ? 184 ALA A CB  1 
ATOM   180  N N   . LEU A 1 186 ? 96.441  81.947  42.136 1.00 150.39 ? 185 LEU A N   1 
ATOM   181  C CA  . LEU A 1 186 ? 95.229  81.732  42.924 1.00 155.78 ? 185 LEU A CA  1 
ATOM   182  C C   . LEU A 1 186 ? 95.045  80.269  43.303 1.00 134.93 ? 185 LEU A C   1 
ATOM   183  O O   . LEU A 1 186 ? 94.673  80.000  44.466 1.00 240.49 ? 185 LEU A O   1 
ATOM   184  C CB  . LEU A 1 186 ? 93.980  82.230  42.176 1.00 121.77 ? 185 LEU A CB  1 
ATOM   185  C CG  . LEU A 1 186 ? 93.845  83.746  42.104 1.00 180.58 ? 185 LEU A CG  1 
ATOM   186  C CD1 . LEU A 1 186 ? 92.663  84.108  41.220 1.00 239.35 ? 185 LEU A CD1 1 
ATOM   187  C CD2 . LEU A 1 186 ? 93.702  84.384  43.492 1.00 156.07 ? 185 LEU A CD2 1 
ATOM   188  N N   . LEU A 1 187 ? 95.298  79.356  42.369 1.00 109.93 ? 186 LEU A N   1 
ATOM   189  C CA  . LEU A 1 187 ? 95.193  77.934  42.646 1.00 164.36 ? 186 LEU A CA  1 
ATOM   190  C C   . LEU A 1 187 ? 96.165  77.536  43.775 1.00 151.02 ? 186 LEU A C   1 
ATOM   191  O O   . LEU A 1 187 ? 95.725  76.917  44.760 1.00 186.91 ? 186 LEU A O   1 
ATOM   192  C CB  . LEU A 1 187 ? 95.437  77.166  41.336 1.00 227.98 ? 186 LEU A CB  1 
ATOM   193  C CG  . LEU A 1 187 ? 95.135  75.667  41.277 1.00 222.70 ? 186 LEU A CG  1 
ATOM   194  C CD1 . LEU A 1 187 ? 96.107  74.816  42.135 1.00 207.87 ? 186 LEU A CD1 1 
ATOM   195  C CD2 . LEU A 1 187 ? 93.676  75.441  41.637 1.00 212.77 ? 186 LEU A CD2 1 
ATOM   196  N N   . LEU A 1 188 ? 97.454  77.891  43.668 1.00 127.14 ? 187 LEU A N   1 
ATOM   197  C CA  . LEU A 1 188 ? 98.421  77.480  44.670 1.00 176.82 ? 187 LEU A CA  1 
ATOM   198  C C   . LEU A 1 188 ? 98.210  78.250  45.980 1.00 154.63 ? 187 LEU A C   1 
ATOM   199  O O   . LEU A 1 188 ? 98.431  77.667  47.049 1.00 190.19 ? 187 LEU A O   1 
ATOM   200  C CB  . LEU A 1 188 ? 99.844  77.641  44.123 1.00 221.33 ? 187 LEU A CB  1 
ATOM   201  C CG  . LEU A 1 188 ? 100.950 77.157  45.059 1.00 224.00 ? 187 LEU A CG  1 
ATOM   202  C CD1 . LEU A 1 188 ? 100.784 75.671  45.386 1.00 189.66 ? 187 LEU A CD1 1 
ATOM   203  C CD2 . LEU A 1 188 ? 102.324 77.430  44.470 1.00 279.63 ? 187 LEU A CD2 1 
ATOM   204  N N   . LEU A 1 189 ? 97.765  79.517  45.920 1.00 130.74 ? 188 LEU A N   1 
ATOM   205  C CA  . LEU A 1 189 ? 97.451  80.308  47.110 1.00 167.00 ? 188 LEU A CA  1 
ATOM   206  C C   . LEU A 1 189 ? 96.346  79.641  47.930 1.00 168.30 ? 188 LEU A C   1 
ATOM   207  O O   . LEU A 1 189 ? 96.490  79.509  49.161 1.00 190.00 ? 188 LEU A O   1 
ATOM   208  C CB  . LEU A 1 189 ? 97.059  81.734  46.698 1.00 174.92 ? 188 LEU A CB  1 
ATOM   209  C CG  . LEU A 1 189 ? 96.534  82.643  47.811 1.00 235.88 ? 188 LEU A CG  1 
ATOM   210  C CD1 . LEU A 1 189 ? 97.570  82.860  48.907 1.00 298.97 ? 188 LEU A CD1 1 
ATOM   211  C CD2 . LEU A 1 189 ? 96.100  83.975  47.227 1.00 311.89 ? 188 LEU A CD2 1 
ATOM   212  N N   . PHE A 1 190 ? 95.261  79.222  47.252 1.00 163.76 ? 189 PHE A N   1 
ATOM   213  C CA  . PHE A 1 190 ? 94.204  78.468  47.897 1.00 125.89 ? 189 PHE A CA  1 
ATOM   214  C C   . PHE A 1 190 ? 94.767  77.179  48.487 1.00 106.40 ? 189 PHE A C   1 
ATOM   215  O O   . PHE A 1 190 ? 94.495  76.873  49.654 1.00 149.43 ? 189 PHE A O   1 
ATOM   216  C CB  . PHE A 1 190 ? 93.065  78.170  46.920 1.00 147.57 ? 189 PHE A CB  1 
ATOM   217  C CG  . PHE A 1 190 ? 92.045  77.170  47.435 1.00 139.26 ? 189 PHE A CG  1 
ATOM   218  C CD1 . PHE A 1 190 ? 92.263  75.815  47.182 1.00 95.59  ? 189 PHE A CD1 1 
ATOM   219  C CD2 . PHE A 1 190 ? 90.895  77.551  48.158 1.00 152.43 ? 189 PHE A CD2 1 
ATOM   220  C CE1 . PHE A 1 190 ? 91.362  74.873  47.635 1.00 122.74 ? 189 PHE A CE1 1 
ATOM   221  C CE2 . PHE A 1 190 ? 90.031  76.577  48.623 1.00 148.32 ? 189 PHE A CE2 1 
ATOM   222  C CZ  . PHE A 1 190 ? 90.260  75.249  48.352 1.00 180.82 ? 189 PHE A CZ  1 
ATOM   223  N N   . TRP A 1 191 ? 95.528  76.406  47.707 1.00 96.36  ? 190 TRP A N   1 
ATOM   224  C CA  . TRP A 1 191 ? 95.885  75.071  48.149 1.00 125.55 ? 190 TRP A CA  1 
ATOM   225  C C   . TRP A 1 191 ? 96.902  75.085  49.309 1.00 138.51 ? 190 TRP A C   1 
ATOM   226  O O   . TRP A 1 191 ? 96.801  74.263  50.233 1.00 143.38 ? 190 TRP A O   1 
ATOM   227  C CB  . TRP A 1 191 ? 96.353  74.286  46.939 1.00 156.71 ? 190 TRP A CB  1 
ATOM   228  C CG  . TRP A 1 191 ? 96.282  72.815  47.162 1.00 195.43 ? 190 TRP A CG  1 
ATOM   229  C CD1 . TRP A 1 191 ? 97.313  71.974  47.472 1.00 292.66 ? 190 TRP A CD1 1 
ATOM   230  C CD2 . TRP A 1 191 ? 95.092  72.016  47.083 1.00 146.84 ? 190 TRP A CD2 1 
ATOM   231  N NE1 . TRP A 1 191 ? 96.844  70.688  47.579 1.00 275.42 ? 190 TRP A NE1 1 
ATOM   232  C CE2 . TRP A 1 191 ? 95.483  70.674  47.349 1.00 244.94 ? 190 TRP A CE2 1 
ATOM   233  C CE3 . TRP A 1 191 ? 93.759  72.288  46.812 1.00 115.58 ? 190 TRP A CE3 1 
ATOM   234  C CZ2 . TRP A 1 191 ? 94.561  69.614  47.351 1.00 266.93 ? 190 TRP A CZ2 1 
ATOM   235  C CZ3 . TRP A 1 191 ? 92.851  71.243  46.809 1.00 220.21 ? 190 TRP A CZ3 1 
ATOM   236  C CH2 . TRP A 1 191 ? 93.244  69.925  47.074 1.00 274.92 ? 190 TRP A CH2 1 
ATOM   237  N N   . LEU A 1 192 ? 97.871  76.014  49.295 1.00 153.92 ? 191 LEU A N   1 
ATOM   238  C CA  . LEU A 1 192 ? 98.714  76.233  50.462 1.00 192.42 ? 191 LEU A CA  1 
ATOM   239  C C   . LEU A 1 192 ? 97.896  76.793  51.630 1.00 169.61 ? 191 LEU A C   1 
ATOM   240  O O   . LEU A 1 192 ? 98.181  76.492  52.782 1.00 182.79 ? 191 LEU A O   1 
ATOM   241  C CB  . LEU A 1 192 ? 99.871  77.177  50.112 1.00 248.59 ? 191 LEU A CB  1 
ATOM   242  C CG  . LEU A 1 192 ? 100.934 76.640  49.150 1.00 268.42 ? 191 LEU A CG  1 
ATOM   243  C CD1 . LEU A 1 192 ? 101.972 77.723  48.903 1.00 340.47 ? 191 LEU A CD1 1 
ATOM   244  C CD2 . LEU A 1 192 ? 101.619 75.353  49.620 1.00 224.17 ? 191 LEU A CD2 1 
ATOM   245  N N   . GLY A 1 193 ? 96.887  77.621  51.368 1.00 129.59 ? 192 GLY A N   1 
ATOM   246  C CA  . GLY A 1 193 ? 95.992  78.079  52.419 1.00 169.40 ? 192 GLY A CA  1 
ATOM   247  C C   . GLY A 1 193 ? 95.239  76.941  53.114 1.00 154.87 ? 192 GLY A C   1 
ATOM   248  O O   . GLY A 1 193 ? 95.120  76.943  54.327 1.00 156.16 ? 192 GLY A O   1 
ATOM   249  N N   . TRP A 1 194 ? 94.723  75.961  52.364 1.00 164.20 ? 193 TRP A N   1 
ATOM   250  C CA  . TRP A 1 194 ? 94.077  74.780  52.927 1.00 133.98 ? 193 TRP A CA  1 
ATOM   251  C C   . TRP A 1 194 ? 95.090  73.927  53.684 1.00 113.51 ? 193 TRP A C   1 
ATOM   252  O O   . TRP A 1 194 ? 94.783  73.513  54.804 1.00 170.03 ? 193 TRP A O   1 
ATOM   253  C CB  . TRP A 1 194 ? 93.427  73.997  51.800 1.00 183.76 ? 193 TRP A CB  1 
ATOM   254  C CG  . TRP A 1 194 ? 92.692  72.742  52.161 1.00 155.27 ? 193 TRP A CG  1 
ATOM   255  C CD1 . TRP A 1 194 ? 91.342  72.689  52.252 1.00 132.54 ? 193 TRP A CD1 1 
ATOM   256  C CD2 . TRP A 1 194 ? 93.187  71.402  52.419 1.00 115.10 ? 193 TRP A CD2 1 
ATOM   257  N NE1 . TRP A 1 194 ? 90.941  71.406  52.549 1.00 119.77 ? 193 TRP A NE1 1 
ATOM   258  C CE2 . TRP A 1 194 ? 92.047  70.593  52.662 1.00 123.90 ? 193 TRP A CE2 1 
ATOM   259  C CE3 . TRP A 1 194 ? 94.447  70.799  52.464 1.00 82.64  ? 193 TRP A CE3 1 
ATOM   260  C CZ2 . TRP A 1 194 ? 92.165  69.227  52.952 1.00 127.67 ? 193 TRP A CZ2 1 
ATOM   261  C CZ3 . TRP A 1 194 ? 94.573  69.456  52.755 1.00 142.98 ? 193 TRP A CZ3 1 
ATOM   262  C CH2 . TRP A 1 194 ? 93.439  68.672  52.991 1.00 147.38 ? 193 TRP A CH2 1 
ATOM   263  N N   . LEU A 1 195 ? 96.312  73.702  53.150 1.00 123.56 ? 194 LEU A N   1 
ATOM   264  C CA  . LEU A 1 195 ? 97.359  73.002  53.897 1.00 148.46 ? 194 LEU A CA  1 
ATOM   265  C C   . LEU A 1 195 ? 97.774  73.750  55.166 1.00 169.49 ? 194 LEU A C   1 
ATOM   266  O O   . LEU A 1 195 ? 98.061  73.093  56.174 1.00 187.47 ? 194 LEU A O   1 
ATOM   267  C CB  . LEU A 1 195 ? 98.562  72.725  52.993 1.00 149.43 ? 194 LEU A CB  1 
ATOM   268  C CG  . LEU A 1 195 ? 98.362  71.521  52.079 1.00 214.29 ? 194 LEU A CG  1 
ATOM   269  C CD1 . LEU A 1 195 ? 99.431  71.449  50.987 1.00 301.36 ? 194 LEU A CD1 1 
ATOM   270  C CD2 . LEU A 1 195 ? 98.322  70.224  52.910 1.00 160.14 ? 194 LEU A CD2 1 
ATOM   271  N N   . GLY A 1 196 ? 97.791  75.084  55.128 1.00 124.74 ? 195 GLY A N   1 
ATOM   272  C CA  . GLY A 1 196 ? 97.986  75.895  56.317 1.00 185.63 ? 195 GLY A CA  1 
ATOM   273  C C   . GLY A 1 196 ? 96.875  75.730  57.357 1.00 170.64 ? 195 GLY A C   1 
ATOM   274  O O   . GLY A 1 196 ? 97.160  75.581  58.535 1.00 133.13 ? 195 GLY A O   1 
ATOM   275  N N   . MET A 1 197 ? 95.608  75.750  56.929 1.00 174.20 ? 196 MET A N   1 
ATOM   276  C CA  . MET A 1 197 ? 94.455  75.553  57.799 1.00 147.53 ? 196 MET A CA  1 
ATOM   277  C C   . MET A 1 197 ? 94.506  74.146  58.424 1.00 94.12  ? 196 MET A C   1 
ATOM   278  O O   . MET A 1 197 ? 94.170  74.013  59.588 1.00 123.55 ? 196 MET A O   1 
ATOM   279  C CB  . MET A 1 197 ? 93.157  75.824  57.007 1.00 134.14 ? 196 MET A CB  1 
ATOM   280  C CG  . MET A 1 197 ? 91.856  75.539  57.780 1.00 157.53 ? 196 MET A CG  1 
ATOM   281  S SD  . MET A 1 197 ? 90.220  75.795  56.953 1.00 143.71 ? 196 MET A SD  1 
ATOM   282  C CE  . MET A 1 197 ? 90.277  77.585  56.896 1.00 190.34 ? 196 MET A CE  1 
ATOM   283  N N   . LEU A 1 198 ? 94.934  73.098  57.708 1.00 96.70  ? 197 LEU A N   1 
ATOM   284  C CA  . LEU A 1 198 ? 95.124  71.784  58.305 1.00 105.62 ? 197 LEU A CA  1 
ATOM   285  C C   . LEU A 1 198 ? 96.297  71.794  59.284 1.00 138.80 ? 197 LEU A C   1 
ATOM   286  O O   . LEU A 1 198 ? 96.162  71.224  60.369 1.00 167.15 ? 197 LEU A O   1 
ATOM   287  C CB  . LEU A 1 198 ? 95.305  70.707  57.241 1.00 120.42 ? 197 LEU A CB  1 
ATOM   288  C CG  . LEU A 1 198 ? 95.501  69.288  57.819 1.00 120.48 ? 197 LEU A CG  1 
ATOM   289  C CD1 . LEU A 1 198 ? 94.714  68.226  57.041 1.00 161.16 ? 197 LEU A CD1 1 
ATOM   290  C CD2 . LEU A 1 198 ? 96.994  68.914  57.852 1.00 147.65 ? 197 LEU A CD2 1 
ATOM   291  N N   . ALA A 1 199 ? 97.417  72.446  58.972 1.00 120.55 ? 198 ALA A N   1 
ATOM   292  C CA  . ALA A 1 199 ? 98.488  72.570  59.953 1.00 162.36 ? 198 ALA A CA  1 
ATOM   293  C C   . ALA A 1 199 ? 97.991  73.288  61.219 1.00 149.81 ? 198 ALA A C   1 
ATOM   294  O O   . ALA A 1 199 ? 98.345  72.885  62.333 1.00 190.93 ? 198 ALA A O   1 
ATOM   295  C CB  . ALA A 1 199 ? 99.682  73.256  59.325 1.00 230.79 ? 198 ALA A CB  1 
ATOM   296  N N   . GLY A 1 200 ? 97.170  74.342  61.077 1.00 128.96 ? 199 GLY A N   1 
ATOM   297  C CA  . GLY A 1 200 ? 96.537  75.025  62.201 1.00 167.51 ? 199 GLY A CA  1 
ATOM   298  C C   . GLY A 1 200 ? 95.683  74.094  63.064 1.00 124.93 ? 199 GLY A C   1 
ATOM   299  O O   . GLY A 1 200 ? 95.777  74.099  64.267 1.00 131.41 ? 199 GLY A O   1 
ATOM   300  N N   . ALA A 1 201 ? 94.843  73.277  62.456 1.00 149.45 ? 200 ALA A N   1 
ATOM   301  C CA  . ALA A 1 201 ? 94.054  72.293  63.169 1.00 166.72 ? 200 ALA A CA  1 
ATOM   302  C C   . ALA A 1 201 ? 94.972  71.267  63.842 1.00 150.86 ? 200 ALA A C   1 
ATOM   303  O O   . ALA A 1 201 ? 94.754  70.938  64.995 1.00 212.77 ? 200 ALA A O   1 
ATOM   304  C CB  . ALA A 1 201 ? 93.039  71.671  62.217 1.00 149.34 ? 200 ALA A CB  1 
ATOM   305  N N   . VAL A 1 202 ? 95.997  70.733  63.177 1.00 104.05 ? 201 VAL A N   1 
ATOM   306  C CA  . VAL A 1 202 ? 96.874  69.751  63.802 1.00 138.37 ? 201 VAL A CA  1 
ATOM   307  C C   . VAL A 1 202 ? 97.625  70.354  64.985 1.00 153.78 ? 201 VAL A C   1 
ATOM   308  O O   . VAL A 1 202 ? 97.834  69.649  65.980 1.00 192.93 ? 201 VAL A O   1 
ATOM   309  C CB  . VAL A 1 202 ? 97.826  69.109  62.783 1.00 202.12 ? 201 VAL A CB  1 
ATOM   310  C CG1 . VAL A 1 202 ? 98.910  68.240  63.433 1.00 186.11 ? 201 VAL A CG1 1 
ATOM   311  C CG2 . VAL A 1 202 ? 97.047  68.259  61.798 1.00 273.10 ? 201 VAL A CG2 1 
ATOM   312  N N   . VAL A 1 203 ? 98.020  71.631  64.916 1.00 137.95 ? 202 VAL A N   1 
ATOM   313  C CA  . VAL A 1 203 ? 98.583  72.320  66.075 1.00 151.63 ? 202 VAL A CA  1 
ATOM   314  C C   . VAL A 1 203 ? 97.573  72.402  67.222 1.00 167.50 ? 202 VAL A C   1 
ATOM   315  O O   . VAL A 1 203 ? 97.960  72.016  68.334 1.00 207.07 ? 202 VAL A O   1 
ATOM   316  C CB  . VAL A 1 203 ? 99.161  73.693  65.699 1.00 169.68 ? 202 VAL A CB  1 
ATOM   317  C CG1 . VAL A 1 203 ? 99.337  74.657  66.882 1.00 217.80 ? 202 VAL A CG1 1 
ATOM   318  C CG2 . VAL A 1 203 ? 100.467 73.463  64.948 1.00 225.92 ? 202 VAL A CG2 1 
ATOM   319  N N   . ILE A 1 204 ? 96.323  72.862  66.996 1.00 126.90 ? 203 ILE A N   1 
ATOM   320  C CA  . ILE A 1 204 ? 95.347  72.990  68.079 1.00 143.43 ? 203 ILE A CA  1 
ATOM   321  C C   . ILE A 1 204 ? 95.130  71.621  68.737 1.00 122.89 ? 203 ILE A C   1 
ATOM   322  O O   . ILE A 1 204 ? 95.095  71.533  69.963 1.00 159.21 ? 203 ILE A O   1 
ATOM   323  C CB  . ILE A 1 204 ? 94.021  73.653  67.632 1.00 139.96 ? 203 ILE A CB  1 
ATOM   324  C CG1 . ILE A 1 204 ? 94.221  75.105  67.226 1.00 199.73 ? 203 ILE A CG1 1 
ATOM   325  C CG2 . ILE A 1 204 ? 92.953  73.590  68.710 1.00 171.59 ? 203 ILE A CG2 1 
ATOM   326  C CD1 . ILE A 1 204 ? 93.011  75.708  66.551 1.00 216.22 ? 203 ILE A CD1 1 
ATOM   327  N N   . ILE A 1 205 ? 95.013  70.557  67.955 1.00 76.30  ? 204 ILE A N   1 
ATOM   328  C CA  . ILE A 1 205 ? 94.756  69.228  68.487 1.00 100.07 ? 204 ILE A CA  1 
ATOM   329  C C   . ILE A 1 205 ? 95.933  68.701  69.326 1.00 133.55 ? 204 ILE A C   1 
ATOM   330  O O   . ILE A 1 205 ? 95.727  67.828  70.194 1.00 221.82 ? 204 ILE A O   1 
ATOM   331  C CB  . ILE A 1 205 ? 94.380  68.290  67.313 1.00 145.59 ? 204 ILE A CB  1 
ATOM   332  C CG1 . ILE A 1 205 ? 93.058  68.702  66.614 1.00 130.43 ? 204 ILE A CG1 1 
ATOM   333  C CG2 . ILE A 1 205 ? 94.393  66.806  67.700 1.00 135.78 ? 204 ILE A CG2 1 
ATOM   334  C CD1 . ILE A 1 205 ? 91.783  68.682  67.404 1.00 120.52 ? 204 ILE A CD1 1 
ATOM   335  N N   . VAL A 1 206 ? 97.173  69.193  69.110 1.00 145.93 ? 205 VAL A N   1 
ATOM   336  C CA  . VAL A 1 206 ? 98.311  68.872  69.979 1.00 165.50 ? 205 VAL A CA  1 
ATOM   337  C C   . VAL A 1 206 ? 98.391  69.791  71.203 1.00 167.58 ? 205 VAL A C   1 
ATOM   338  O O   . VAL A 1 206 ? 98.719  69.307  72.298 1.00 175.79 ? 205 VAL A O   1 
ATOM   339  C CB  . VAL A 1 206 ? 99.620  68.855  69.176 1.00 197.51 ? 205 VAL A CB  1 
ATOM   340  C CG1 . VAL A 1 206 ? 100.881 68.885  70.038 1.00 262.16 ? 205 VAL A CG1 1 
ATOM   341  C CG2 . VAL A 1 206 ? 99.636  67.629  68.266 1.00 207.70 ? 205 VAL A CG2 1 
ATOM   342  N N   . ARG A 1 207 ? 98.091  71.087  71.026 1.00 148.66 ? 206 ARG A N   1 
ATOM   343  C CA  . ARG A 1 207 ? 98.167  72.072  72.101 1.00 205.15 ? 206 ARG A CA  1 
ATOM   344  C C   . ARG A 1 207 ? 97.020  71.959  73.116 1.00 211.54 ? 206 ARG A C   1 
ATOM   345  O O   . ARG A 1 207 ? 97.171  72.433  74.244 1.00 252.11 ? 206 ARG A O   1 
ATOM   346  C CB  . ARG A 1 207 ? 98.221  73.479  71.493 1.00 232.50 ? 206 ARG A CB  1 
ATOM   347  C CG  . ARG A 1 207 ? 99.499  73.784  70.710 1.00 290.80 ? 206 ARG A CG  1 
ATOM   348  C CD  . ARG A 1 207 ? 100.736 73.943  71.599 1.00 304.57 ? 206 ARG A CD  1 
ATOM   349  N NE  . ARG A 1 207 ? 101.981 74.157  70.862 1.00 315.55 ? 206 ARG A NE  1 
ATOM   350  C CZ  . ARG A 1 207 ? 102.408 75.323  70.366 1.00 328.40 ? 206 ARG A CZ  1 
ATOM   351  N NH1 . ARG A 1 207 ? 103.473 75.357  69.577 1.00 293.03 ? 206 ARG A NH1 1 
ATOM   352  N NH2 . ARG A 1 207 ? 101.776 76.454  70.643 1.00 318.85 ? 206 ARG A NH2 1 
ATOM   353  N N   . ALA A 1 208 ? 95.885  71.346  72.740 1.00 194.46 ? 207 ALA A N   1 
ATOM   354  C CA  . ALA A 1 208 ? 94.731  71.179  73.619 1.00 246.80 ? 207 ALA A CA  1 
ATOM   355  C C   . ALA A 1 208 ? 95.020  70.270  74.819 1.00 213.41 ? 207 ALA A C   1 
ATOM   356  O O   . ALA A 1 208 ? 95.723  69.268  74.670 1.00 152.17 ? 207 ALA A O   1 
ATOM   357  C CB  . ALA A 1 208 ? 93.571  70.637  72.819 1.00 287.82 ? 207 ALA A CB  1 
ATOM   358  N N   . PRO A 1 209 ? 94.490  70.596  76.036 1.00 190.73 ? 208 PRO A N   1 
ATOM   359  C CA  . PRO A 1 209 ? 94.639  69.741  77.213 1.00 175.52 ? 208 PRO A CA  1 
ATOM   360  C C   . PRO A 1 209 ? 94.084  68.348  76.972 1.00 161.19 ? 208 PRO A C   1 
ATOM   361  O O   . PRO A 1 209 ? 92.896  68.237  76.679 1.00 172.54 ? 208 PRO A O   1 
ATOM   362  C CB  . PRO A 1 209 ? 93.808  70.456  78.289 1.00 219.66 ? 208 PRO A CB  1 
ATOM   363  C CG  . PRO A 1 209 ? 93.843  71.910  77.869 1.00 252.51 ? 208 PRO A CG  1 
ATOM   364  C CD  . PRO A 1 209 ? 93.746  71.829  76.361 1.00 205.63 ? 208 PRO A CD  1 
ATOM   365  N N   . ARG A 1 210 ? 94.934  67.304  77.080 1.00 178.24 ? 209 ARG A N   1 
ATOM   366  C CA  . ARG A 1 210 ? 94.479  65.932  76.866 1.00 194.01 ? 209 ARG A CA  1 
ATOM   367  C C   . ARG A 1 210 ? 93.576  65.464  78.010 1.00 176.10 ? 209 ARG A C   1 
ATOM   368  O O   . ARG A 1 210 ? 93.664  65.938  79.138 1.00 192.19 ? 209 ARG A O   1 
ATOM   369  C CB  . ARG A 1 210 ? 95.662  64.992  76.588 1.00 202.56 ? 209 ARG A CB  1 
ATOM   370  C CG  . ARG A 1 210 ? 96.188  65.142  75.165 1.00 254.88 ? 209 ARG A CG  1 
ATOM   371  C CD  . ARG A 1 210 ? 95.232  64.736  74.030 1.00 237.24 ? 209 ARG A CD  1 
ATOM   372  N NE  . ARG A 1 210 ? 95.659  65.213  72.710 1.00 292.88 ? 209 ARG A NE  1 
ATOM   373  C CZ  . ARG A 1 210 ? 96.551  64.610  71.922 1.00 341.84 ? 209 ARG A CZ  1 
ATOM   374  N NH1 . ARG A 1 210 ? 96.962  65.213  70.822 1.00 382.06 ? 209 ARG A NH1 1 
ATOM   375  N NH2 . ARG A 1 210 ? 97.043  63.418  72.229 1.00 299.43 ? 209 ARG A NH2 1 
ATOM   376  N N   . CYS A 1 211 ? 92.713  64.505  77.658 1.00 181.51 ? 210 CYS A N   1 
ATOM   377  C CA  . CYS A 1 211 ? 91.579  64.080  78.466 1.00 213.66 ? 210 CYS A CA  1 
ATOM   378  C C   . CYS A 1 211 ? 92.047  63.429  79.777 1.00 218.51 ? 210 CYS A C   1 
ATOM   379  O O   . CYS A 1 211 ? 93.080  62.751  79.818 1.00 192.50 ? 210 CYS A O   1 
ATOM   380  C CB  . CYS A 1 211 ? 90.699  63.121  77.653 1.00 207.70 ? 210 CYS A CB  1 
ATOM   381  S SG  . CYS A 1 211 ? 88.917  63.341  77.917 1.00 193.91 ? 210 CYS A SG  1 
ATOM   382  N N   . ARG A 1 212 ? 91.283  63.636  80.868 1.00 234.59 ? 211 ARG A N   1 
ATOM   383  C CA  . ARG A 1 212 ? 91.551  62.984  82.149 1.00 240.91 ? 211 ARG A CA  1 
ATOM   384  C C   . ARG A 1 212 ? 91.415  61.471  81.959 1.00 212.96 ? 211 ARG A C   1 
ATOM   385  O O   . ARG A 1 212 ? 90.436  61.028  81.347 1.00 273.85 ? 211 ARG A O   1 
ATOM   386  C CB  . ARG A 1 212 ? 90.554  63.485  83.220 1.00 357.38 ? 211 ARG A CB  1 
ATOM   387  C CG  . ARG A 1 212 ? 90.884  63.088  84.649 1.00 378.35 ? 211 ARG A CG  1 
ATOM   388  C CD  . ARG A 1 212 ? 89.967  63.784  85.657 1.00 384.29 ? 211 ARG A CD  1 
ATOM   389  N NE  . ARG A 1 212 ? 88.645  63.160  85.690 1.00 307.02 ? 211 ARG A NE  1 
ATOM   390  C CZ  . ARG A 1 212 ? 87.447  63.757  85.765 1.00 214.53 ? 211 ARG A CZ  1 
ATOM   391  N NH1 . ARG A 1 212 ? 86.408  62.962  86.003 1.00 152.21 ? 211 ARG A NH1 1 
ATOM   392  N NH2 . ARG A 1 212 ? 87.250  65.085  85.650 1.00 135.42 ? 211 ARG A NH2 1 
ATOM   393  N N   . GLU A 1 213 ? 92.349  60.661  82.485 1.00 157.45 ? 212 GLU A N   1 
ATOM   394  C CA  . GLU A 1 213 ? 92.195  59.198  82.422 1.00 181.16 ? 212 GLU A CA  1 
ATOM   395  C C   . GLU A 1 213 ? 91.079  58.690  83.356 1.00 187.35 ? 212 GLU A C   1 
ATOM   396  O O   . GLU A 1 213 ? 90.711  59.366  84.323 1.00 271.23 ? 212 GLU A O   1 
ATOM   397  C CB  . GLU A 1 213 ? 93.511  58.491  82.767 1.00 234.67 ? 212 GLU A CB  1 
ATOM   398  C CG  . GLU A 1 213 ? 94.238  57.921  81.562 1.00 300.70 ? 212 GLU A CG  1 
ATOM   399  C CD  . GLU A 1 213 ? 93.645  56.629  81.016 1.00 343.66 ? 212 GLU A CD  1 
ATOM   400  O OE1 . GLU A 1 213 ? 92.483  56.315  81.360 1.00 317.72 ? 212 GLU A OE1 1 
ATOM   401  O OE2 . GLU A 1 213 ? 94.347  55.934  80.248 1.00 383.69 ? 212 GLU A OE2 1 
ATOM   402  N N   . LEU A 1 214 ? 90.541  57.485  83.072 1.00 151.53 ? 213 LEU A N   1 
ATOM   403  C CA  . LEU A 1 214 ? 89.549  56.840  83.932 1.00 204.74 ? 213 LEU A CA  1 
ATOM   404  C C   . LEU A 1 214 ? 90.110  55.544  84.554 1.00 274.14 ? 213 LEU A C   1 
ATOM   405  O O   . LEU A 1 214 ? 90.081  55.465  85.820 1.00 201.00 ? 213 LEU A O   1 
ATOM   406  C CB  . LEU A 1 214 ? 88.285  56.590  83.095 1.00 164.25 ? 213 LEU A CB  1 
ATOM   407  C CG  . LEU A 1 214 ? 87.484  57.838  82.752 1.00 163.26 ? 213 LEU A CG  1 
ATOM   408  C CD1 . LEU A 1 214 ? 86.254  57.467  81.944 1.00 200.08 ? 213 LEU A CD1 1 
ATOM   409  C CD2 . LEU A 1 214 ? 87.054  58.599  84.004 1.00 204.34 ? 213 LEU A CD2 1 
ATOM   410  N N   . VAL B 2 44  ? 79.752  72.738  25.452 1.00 197.52 ? 44  VAL B N   1 
ATOM   411  C CA  . VAL B 2 44  ? 80.224  73.262  26.779 1.00 212.04 ? 44  VAL B CA  1 
ATOM   412  C C   . VAL B 2 44  ? 79.333  72.789  27.931 1.00 233.93 ? 44  VAL B C   1 
ATOM   413  O O   . VAL B 2 44  ? 79.830  72.640  29.044 1.00 270.51 ? 44  VAL B O   1 
ATOM   414  C CB  . VAL B 2 44  ? 80.352  74.802  26.828 1.00 264.55 ? 44  VAL B CB  1 
ATOM   415  C CG1 . VAL B 2 44  ? 81.258  75.322  25.719 1.00 357.62 ? 44  VAL B CG1 1 
ATOM   416  C CG2 . VAL B 2 44  ? 79.019  75.551  26.813 1.00 255.27 ? 44  VAL B CG2 1 
ATOM   417  N N   . THR B 2 45  ? 78.031  72.562  27.695 1.00 239.46 ? 45  THR B N   1 
ATOM   418  C CA  . THR B 2 45  ? 77.081  72.181  28.749 1.00 213.66 ? 45  THR B CA  1 
ATOM   419  C C   . THR B 2 45  ? 77.427  70.823  29.394 1.00 219.19 ? 45  THR B C   1 
ATOM   420  O O   . THR B 2 45  ? 78.029  69.958  28.746 1.00 191.57 ? 45  THR B O   1 
ATOM   421  C CB  . THR B 2 45  ? 75.651  72.226  28.196 1.00 266.62 ? 45  THR B CB  1 
ATOM   422  O OG1 . THR B 2 45  ? 75.445  73.549  27.695 1.00 305.63 ? 45  THR B OG1 1 
ATOM   423  C CG2 . THR B 2 45  ? 74.572  71.889  29.206 1.00 260.81 ? 45  THR B CG2 1 
ATOM   424  N N   . LEU B 2 46  ? 77.035  70.657  30.686 1.00 205.41 ? 46  LEU B N   1 
ATOM   425  C CA  . LEU B 2 46  ? 77.369  69.521  31.560 1.00 172.46 ? 46  LEU B CA  1 
ATOM   426  C C   . LEU B 2 46  ? 77.073  68.176  30.909 1.00 180.68 ? 46  LEU B C   1 
ATOM   427  O O   . LEU B 2 46  ? 75.939  67.965  30.458 1.00 230.90 ? 46  LEU B O   1 
ATOM   428  C CB  . LEU B 2 46  ? 76.533  69.593  32.842 1.00 168.41 ? 46  LEU B CB  1 
ATOM   429  C CG  . LEU B 2 46  ? 77.041  70.438  34.009 1.00 191.09 ? 46  LEU B CG  1 
ATOM   430  C CD1 . LEU B 2 46  ? 77.445  71.820  33.601 1.00 236.41 ? 46  LEU B CD1 1 
ATOM   431  C CD2 . LEU B 2 46  ? 75.954  70.599  35.043 1.00 193.88 ? 46  LEU B CD2 1 
ATOM   432  N N   . GLN B 2 47  ? 78.072  67.277  30.886 1.00 158.97 ? 47  GLN B N   1 
ATOM   433  C CA  . GLN B 2 47  ? 77.847  65.916  30.405 1.00 208.10 ? 47  GLN B CA  1 
ATOM   434  C C   . GLN B 2 47  ? 76.993  65.094  31.378 1.00 184.27 ? 47  GLN B C   1 
ATOM   435  O O   . GLN B 2 47  ? 77.197  65.198  32.580 1.00 180.54 ? 47  GLN B O   1 
ATOM   436  C CB  . GLN B 2 47  ? 79.174  65.197  30.149 1.00 225.26 ? 47  GLN B CB  1 
ATOM   437  C CG  . GLN B 2 47  ? 79.742  65.496  28.764 1.00 280.24 ? 47  GLN B CG  1 
ATOM   438  C CD  . GLN B 2 47  ? 80.938  64.646  28.392 1.00 333.73 ? 47  GLN B CD  1 
ATOM   439  O OE1 . GLN B 2 47  ? 81.500  63.931  29.222 1.00 307.23 ? 47  GLN B OE1 1 
ATOM   440  N NE2 . GLN B 2 47  ? 81.341  64.723  27.130 1.00 360.97 ? 47  GLN B NE2 1 
ATOM   441  N N   . ARG B 2 48  ? 76.062  64.276  30.834 1.00 159.91 ? 48  ARG B N   1 
ATOM   442  C CA  . ARG B 2 48  ? 75.379  63.236  31.583 1.00 135.18 ? 48  ARG B CA  1 
ATOM   443  C C   . ARG B 2 48  ? 76.366  62.109  31.890 1.00 177.59 ? 48  ARG B C   1 
ATOM   444  O O   . ARG B 2 48  ? 76.942  61.545  30.955 1.00 208.99 ? 48  ARG B O   1 
ATOM   445  C CB  . ARG B 2 48  ? 74.181  62.650  30.817 1.00 146.94 ? 48  ARG B CB  1 
ATOM   446  C CG  . ARG B 2 48  ? 73.034  63.627  30.631 1.00 173.29 ? 48  ARG B CG  1 
ATOM   447  C CD  . ARG B 2 48  ? 71.905  63.043  29.797 1.00 175.93 ? 48  ARG B CD  1 
ATOM   448  N NE  . ARG B 2 48  ? 70.808  63.996  29.645 1.00 179.03 ? 48  ARG B NE  1 
ATOM   449  C CZ  . ARG B 2 48  ? 69.812  64.183  30.502 1.00 191.38 ? 48  ARG B CZ  1 
ATOM   450  N NH1 . ARG B 2 48  ? 68.903  65.114  30.263 1.00 230.94 ? 48  ARG B NH1 1 
ATOM   451  N NH2 . ARG B 2 48  ? 69.705  63.453  31.601 1.00 234.91 ? 48  ARG B NH2 1 
ATOM   452  N N   . ASN B 2 49  ? 76.555  61.772  33.186 1.00 161.12 ? 49  ASN B N   1 
ATOM   453  C CA  . ASN B 2 49  ? 77.401  60.631  33.549 1.00 212.96 ? 49  ASN B CA  1 
ATOM   454  C C   . ASN B 2 49  ? 77.012  59.938  34.864 1.00 164.55 ? 49  ASN B C   1 
ATOM   455  O O   . ASN B 2 49  ? 77.696  58.980  35.254 1.00 151.09 ? 49  ASN B O   1 
ATOM   456  C CB  . ASN B 2 49  ? 78.893  61.007  33.531 1.00 240.44 ? 49  ASN B CB  1 
ATOM   457  C CG  . ASN B 2 49  ? 79.270  62.116  34.486 1.00 215.73 ? 49  ASN B CG  1 
ATOM   458  O OD1 . ASN B 2 49  ? 78.824  62.131  35.635 1.00 157.64 ? 49  ASN B OD1 1 
ATOM   459  N ND2 . ASN B 2 49  ? 80.085  63.050  34.012 1.00 250.10 ? 49  ASN B ND2 1 
ATOM   460  N N   . ILE B 2 50  ? 75.924  60.355  35.529 1.00 159.94 ? 50  ILE B N   1 
ATOM   461  C CA  . ILE B 2 50  ? 75.449  59.660  36.721 1.00 181.97 ? 50  ILE B CA  1 
ATOM   462  C C   . ILE B 2 50  ? 74.681  58.397  36.291 1.00 155.35 ? 50  ILE B C   1 
ATOM   463  O O   . ILE B 2 50  ? 73.619  58.469  35.651 1.00 151.89 ? 50  ILE B O   1 
ATOM   464  C CB  . ILE B 2 50  ? 74.613  60.609  37.613 1.00 171.41 ? 50  ILE B CB  1 
ATOM   465  C CG1 . ILE B 2 50  ? 75.387  61.865  38.021 1.00 152.40 ? 50  ILE B CG1 1 
ATOM   466  C CG2 . ILE B 2 50  ? 74.080  59.898  38.838 1.00 121.56 ? 50  ILE B CG2 1 
ATOM   467  C CD1 . ILE B 2 50  ? 74.476  62.908  38.663 1.00 103.47 ? 50  ILE B CD1 1 
ATOM   468  N N   . THR B 2 51  ? 75.233  57.227  36.650 1.00 127.03 ? 51  THR B N   1 
ATOM   469  C CA  . THR B 2 51  ? 74.610  55.933  36.388 1.00 180.49 ? 51  THR B CA  1 
ATOM   470  C C   . THR B 2 51  ? 73.493  55.655  37.394 1.00 152.75 ? 51  THR B C   1 
ATOM   471  O O   . THR B 2 51  ? 73.288  56.437  38.308 1.00 227.36 ? 51  THR B O   1 
ATOM   472  C CB  . THR B 2 51  ? 75.658  54.809  36.408 1.00 203.37 ? 51  THR B CB  1 
ATOM   473  O OG1 . THR B 2 51  ? 76.213  54.700  37.712 1.00 126.46 ? 51  THR B OG1 1 
ATOM   474  C CG2 . THR B 2 51  ? 76.795  55.038  35.435 1.00 276.70 ? 51  THR B CG2 1 
ATOM   475  N N   . LEU B 2 52  ? 72.784  54.524  37.285 1.00 165.43 ? 52  LEU B N   1 
ATOM   476  C CA  . LEU B 2 52  ? 71.886  54.099  38.358 1.00 155.13 ? 52  LEU B CA  1 
ATOM   477  C C   . LEU B 2 52  ? 72.667  53.960  39.668 1.00 161.20 ? 52  LEU B C   1 
ATOM   478  O O   . LEU B 2 52  ? 72.213  54.469  40.696 1.00 125.00 ? 52  LEU B O   1 
ATOM   479  C CB  . LEU B 2 52  ? 71.215  52.758  38.026 1.00 197.91 ? 52  LEU B CB  1 
ATOM   480  C CG  . LEU B 2 52  ? 70.412  52.134  39.170 1.00 167.73 ? 52  LEU B CG  1 
ATOM   481  C CD1 . LEU B 2 52  ? 69.235  53.014  39.469 1.00 135.39 ? 52  LEU B CD1 1 
ATOM   482  C CD2 . LEU B 2 52  ? 69.968  50.720  38.844 1.00 234.16 ? 52  LEU B CD2 1 
ATOM   483  N N   . LEU B 2 53  ? 73.821  53.272  39.642 1.00 158.52 ? 53  LEU B N   1 
ATOM   484  C CA  . LEU B 2 53  ? 74.554  52.980  40.863 1.00 160.39 ? 53  LEU B CA  1 
ATOM   485  C C   . LEU B 2 53  ? 75.061  54.267  41.504 1.00 114.64 ? 53  LEU B C   1 
ATOM   486  O O   . LEU B 2 53  ? 74.988  54.394  42.719 1.00 165.48 ? 53  LEU B O   1 
ATOM   487  C CB  . LEU B 2 53  ? 75.695  52.009  40.552 1.00 222.30 ? 53  LEU B CB  1 
ATOM   488  C CG  . LEU B 2 53  ? 76.510  51.561  41.760 1.00 312.92 ? 53  LEU B CG  1 
ATOM   489  C CD1 . LEU B 2 53  ? 75.627  50.801  42.743 1.00 350.99 ? 53  LEU B CD1 1 
ATOM   490  C CD2 . LEU B 2 53  ? 77.697  50.724  41.316 1.00 394.63 ? 53  LEU B CD2 1 
ATOM   491  N N   . ASN B 2 54  ? 75.558  55.232  40.728 1.00 125.15 ? 54  ASN B N   1 
ATOM   492  C CA  . ASN B 2 54  ? 75.997  56.513  41.283 1.00 126.38 ? 54  ASN B CA  1 
ATOM   493  C C   . ASN B 2 54  ? 74.813  57.356  41.758 1.00 85.77  ? 54  ASN B C   1 
ATOM   494  O O   . ASN B 2 54  ? 74.954  58.148  42.673 1.00 142.46 ? 54  ASN B O   1 
ATOM   495  C CB  . ASN B 2 54  ? 76.945  57.231  40.326 1.00 137.70 ? 54  ASN B CB  1 
ATOM   496  C CG  . ASN B 2 54  ? 78.247  56.461  40.106 1.00 211.89 ? 54  ASN B CG  1 
ATOM   497  O OD1 . ASN B 2 54  ? 78.579  55.495  40.809 1.00 167.97 ? 54  ASN B OD1 1 
ATOM   498  N ND2 . ASN B 2 54  ? 79.018  56.878  39.115 1.00 246.70 ? 54  ASN B ND2 1 
ATOM   499  N N   . GLY B 2 55  ? 73.625  57.198  41.199 1.00 130.01 ? 55  GLY B N   1 
ATOM   500  C CA  . GLY B 2 55  ? 72.438  57.849  41.742 1.00 106.28 ? 55  GLY B CA  1 
ATOM   501  C C   . GLY B 2 55  ? 71.982  57.208  43.022 1.00 101.60 ? 55  GLY B C   1 
ATOM   502  O O   . GLY B 2 55  ? 71.638  57.940  43.923 1.00 117.08 ? 55  GLY B O   1 
ATOM   503  N N   . VAL B 2 56  ? 72.000  55.868  43.141 1.00 102.03 ? 56  VAL B N   1 
ATOM   504  C CA  . VAL B 2 56  ? 71.747  55.215  44.424 1.00 126.19 ? 56  VAL B CA  1 
ATOM   505  C C   . VAL B 2 56  ? 72.779  55.672  45.452 1.00 120.47 ? 56  VAL B C   1 
ATOM   506  O O   . VAL B 2 56  ? 72.419  55.969  46.582 1.00 101.48 ? 56  VAL B O   1 
ATOM   507  C CB  . VAL B 2 56  ? 71.729  53.692  44.292 1.00 124.66 ? 56  VAL B CB  1 
ATOM   508  C CG1 . VAL B 2 56  ? 71.805  52.959  45.635 1.00 155.51 ? 56  VAL B CG1 1 
ATOM   509  C CG2 . VAL B 2 56  ? 70.488  53.284  43.535 1.00 172.57 ? 56  VAL B CG2 1 
ATOM   510  N N   . ALA B 2 57  ? 74.050  55.768  45.074 1.00 114.99 ? 57  ALA B N   1 
ATOM   511  C CA  . ALA B 2 57  ? 75.077  56.285  45.960 1.00 104.63 ? 57  ALA B CA  1 
ATOM   512  C C   . ALA B 2 57  ? 74.792  57.730  46.352 1.00 73.36  ? 57  ALA B C   1 
ATOM   513  O O   . ALA B 2 57  ? 75.089  58.080  47.478 1.00 145.59 ? 57  ALA B O   1 
ATOM   514  C CB  . ALA B 2 57  ? 76.445  56.110  45.341 1.00 98.69  ? 57  ALA B CB  1 
ATOM   515  N N   . ILE B 2 58  ? 74.234  58.573  45.493 1.00 85.82  ? 58  ILE B N   1 
ATOM   516  C CA  . ILE B 2 58  ? 73.853  59.925  45.867 1.00 109.88 ? 58  ILE B CA  1 
ATOM   517  C C   . ILE B 2 58  ? 72.773  59.840  46.923 1.00 99.67  ? 58  ILE B C   1 
ATOM   518  O O   . ILE B 2 58  ? 72.917  60.535  47.921 1.00 118.92 ? 58  ILE B O   1 
ATOM   519  C CB  . ILE B 2 58  ? 73.453  60.824  44.662 1.00 129.02 ? 58  ILE B CB  1 
ATOM   520  C CG1 . ILE B 2 58  ? 74.709  61.264  43.900 1.00 108.01 ? 58  ILE B CG1 1 
ATOM   521  C CG2 . ILE B 2 58  ? 72.590  62.040  45.097 1.00 128.53 ? 58  ILE B CG2 1 
ATOM   522  C CD1 . ILE B 2 58  ? 74.461  61.825  42.572 1.00 103.33 ? 58  ILE B CD1 1 
ATOM   523  N N   . ILE B 2 59  ? 71.705  59.043  46.741 1.00 82.33  ? 59  ILE B N   1 
ATOM   524  C CA  . ILE B 2 59  ? 70.617  59.088  47.704 1.00 99.12  ? 59  ILE B CA  1 
ATOM   525  C C   . ILE B 2 59  ? 71.030  58.377  48.996 1.00 109.37 ? 59  ILE B C   1 
ATOM   526  O O   . ILE B 2 59  ? 70.973  58.982  50.048 1.00 135.54 ? 59  ILE B O   1 
ATOM   527  C CB  . ILE B 2 59  ? 69.273  58.586  47.151 1.00 103.94 ? 59  ILE B CB  1 
ATOM   528  C CG1 . ILE B 2 59  ? 68.842  59.332  45.898 1.00 139.77 ? 59  ILE B CG1 1 
ATOM   529  C CG2 . ILE B 2 59  ? 68.192  58.755  48.190 1.00 108.90 ? 59  ILE B CG2 1 
ATOM   530  C CD1 . ILE B 2 59  ? 67.507  58.915  45.376 1.00 124.88 ? 59  ILE B CD1 1 
ATOM   531  N N   . VAL B 2 60  ? 71.438  57.119  48.973 1.00 94.32  ? 60  VAL B N   1 
ATOM   532  C CA  . VAL B 2 60  ? 71.793  56.424  50.212 1.00 90.34  ? 60  VAL B CA  1 
ATOM   533  C C   . VAL B 2 60  ? 73.006  57.105  50.845 1.00 80.16  ? 60  VAL B C   1 
ATOM   534  O O   . VAL B 2 60  ? 73.049  57.259  52.045 1.00 183.12 ? 60  VAL B O   1 
ATOM   535  C CB  . VAL B 2 60  ? 72.077  54.922  49.995 1.00 119.35 ? 60  VAL B CB  1 
ATOM   536  C CG1 . VAL B 2 60  ? 72.396  54.187  51.272 1.00 125.12 ? 60  VAL B CG1 1 
ATOM   537  C CG2 . VAL B 2 60  ? 70.919  54.206  49.344 1.00 167.96 ? 60  VAL B CG2 1 
ATOM   538  N N   . GLY B 2 61  ? 73.982  57.541  50.075 1.00 111.23 ? 61  GLY B N   1 
ATOM   539  C CA  . GLY B 2 61  ? 75.088  58.340  50.584 1.00 134.40 ? 61  GLY B CA  1 
ATOM   540  C C   . GLY B 2 61  ? 74.673  59.650  51.254 1.00 108.13 ? 61  GLY B C   1 
ATOM   541  O O   . GLY B 2 61  ? 75.125  59.897  52.346 1.00 136.99 ? 61  GLY B O   1 
ATOM   542  N N   . THR B 2 62  ? 73.802  60.443  50.630 1.00 95.97  ? 62  THR B N   1 
ATOM   543  C CA  . THR B 2 62  ? 73.417  61.752  51.156 1.00 110.88 ? 62  THR B CA  1 
ATOM   544  C C   . THR B 2 62  ? 72.363  61.673  52.262 1.00 103.96 ? 62  THR B C   1 
ATOM   545  O O   . THR B 2 62  ? 72.348  62.550  53.111 1.00 114.15 ? 62  THR B O   1 
ATOM   546  C CB  . THR B 2 62  ? 72.937  62.720  50.065 1.00 131.34 ? 62  THR B CB  1 
ATOM   547  O OG1 . THR B 2 62  ? 73.050  64.055  50.548 1.00 91.73  ? 62  THR B OG1 1 
ATOM   548  C CG2 . THR B 2 62  ? 71.494  62.557  49.650 1.00 186.83 ? 62  THR B CG2 1 
ATOM   549  N N   . ILE B 2 63  ? 71.489  60.654  52.283 1.00 121.06 ? 63  ILE B N   1 
ATOM   550  C CA  . ILE B 2 63  ? 70.512  60.495  53.357 1.00 110.88 ? 63  ILE B CA  1 
ATOM   551  C C   . ILE B 2 63  ? 71.191  59.940  54.603 1.00 110.01 ? 63  ILE B C   1 
ATOM   552  O O   . ILE B 2 63  ? 71.066  60.545  55.666 1.00 119.21 ? 63  ILE B O   1 
ATOM   553  C CB  . ILE B 2 63  ? 69.302  59.641  52.935 1.00 89.44  ? 63  ILE B CB  1 
ATOM   554  C CG1 . ILE B 2 63  ? 68.498  60.351  51.855 1.00 144.80 ? 63  ILE B CG1 1 
ATOM   555  C CG2 . ILE B 2 63  ? 68.425  59.384  54.099 1.00 120.57 ? 63  ILE B CG2 1 
ATOM   556  C CD1 . ILE B 2 63  ? 67.268  59.614  51.378 1.00 182.30 ? 63  ILE B CD1 1 
ATOM   557  N N   . ILE B 2 64  ? 71.875  58.791  54.491 1.00 118.55 ? 64  ILE B N   1 
ATOM   558  C CA  . ILE B 2 64  ? 72.282  58.012  55.653 1.00 110.10 ? 64  ILE B CA  1 
ATOM   559  C C   . ILE B 2 64  ? 73.090  58.896  56.597 1.00 146.67 ? 64  ILE B C   1 
ATOM   560  O O   . ILE B 2 64  ? 72.825  58.828  57.808 1.00 192.42 ? 64  ILE B O   1 
ATOM   561  C CB  . ILE B 2 64  ? 73.028  56.733  55.253 1.00 109.38 ? 64  ILE B CB  1 
ATOM   562  C CG1 . ILE B 2 64  ? 72.070  55.734  54.618 1.00 168.74 ? 64  ILE B CG1 1 
ATOM   563  C CG2 . ILE B 2 64  ? 73.766  56.072  56.375 1.00 105.31 ? 64  ILE B CG2 1 
ATOM   564  C CD1 . ILE B 2 64  ? 71.156  55.056  55.547 1.00 158.33 ? 64  ILE B CD1 1 
ATOM   565  N N   . GLY B 2 65  ? 74.032  59.682  56.060 1.00 100.65 ? 65  GLY B N   1 
ATOM   566  C CA  . GLY B 2 65  ? 74.475  60.922  56.697 1.00 144.14 ? 65  GLY B CA  1 
ATOM   567  C C   . GLY B 2 65  ? 74.850  60.862  58.193 1.00 132.83 ? 65  GLY B C   1 
ATOM   568  O O   . GLY B 2 65  ? 75.569  59.961  58.627 1.00 106.03 ? 65  GLY B O   1 
ATOM   569  N N   . SER B 2 66  ? 74.377  61.859  58.963 1.00 118.60 ? 66  SER B N   1 
ATOM   570  C CA  . SER B 2 66  ? 74.648  62.012  60.380 1.00 136.84 ? 66  SER B CA  1 
ATOM   571  C C   . SER B 2 66  ? 73.475  61.582  61.252 1.00 149.64 ? 66  SER B C   1 
ATOM   572  O O   . SER B 2 66  ? 73.709  61.177  62.390 1.00 165.11 ? 66  SER B O   1 
ATOM   573  C CB  . SER B 2 66  ? 74.964  63.457  60.710 1.00 156.01 ? 66  SER B CB  1 
ATOM   574  O OG  . SER B 2 66  ? 73.821  64.293  60.581 1.00 107.68 ? 66  SER B OG  1 
ATOM   575  N N   . GLY B 2 67  ? 72.244  61.693  60.735 1.00 133.32 ? 67  GLY B N   1 
ATOM   576  C CA  . GLY B 2 67  ? 71.054  61.619  61.557 1.00 154.84 ? 67  GLY B CA  1 
ATOM   577  C C   . GLY B 2 67  ? 70.949  60.337  62.377 1.00 138.52 ? 67  GLY B C   1 
ATOM   578  O O   . GLY B 2 67  ? 70.502  60.390  63.516 1.00 119.05 ? 67  GLY B O   1 
ATOM   579  N N   . ILE B 2 68  ? 71.365  59.194  61.822 1.00 137.33 ? 68  ILE B N   1 
ATOM   580  C CA  . ILE B 2 68  ? 71.293  57.921  62.543 1.00 112.40 ? 68  ILE B CA  1 
ATOM   581  C C   . ILE B 2 68  ? 72.374  57.754  63.632 1.00 117.12 ? 68  ILE B C   1 
ATOM   582  O O   . ILE B 2 68  ? 72.360  56.780  64.399 1.00 141.27 ? 68  ILE B O   1 
ATOM   583  C CB  . ILE B 2 68  ? 71.312  56.792  61.517 1.00 105.69 ? 68  ILE B CB  1 
ATOM   584  C CG1 . ILE B 2 68  ? 70.850  55.472  62.111 1.00 141.96 ? 68  ILE B CG1 1 
ATOM   585  C CG2 . ILE B 2 68  ? 72.669  56.658  60.861 1.00 131.75 ? 68  ILE B CG2 1 
ATOM   586  C CD1 . ILE B 2 68  ? 69.476  55.522  62.768 1.00 161.74 ? 68  ILE B CD1 1 
ATOM   587  N N   . PHE B 2 69  ? 73.299  58.715  63.744 1.00 102.80 ? 69  PHE B N   1 
ATOM   588  C CA  . PHE B 2 69  ? 74.315  58.713  64.780 1.00 139.45 ? 69  PHE B CA  1 
ATOM   589  C C   . PHE B 2 69  ? 74.110  59.858  65.784 1.00 180.23 ? 69  PHE B C   1 
ATOM   590  O O   . PHE B 2 69  ? 74.290  59.641  66.984 1.00 170.96 ? 69  PHE B O   1 
ATOM   591  C CB  . PHE B 2 69  ? 75.676  58.770  64.086 1.00 124.30 ? 69  PHE B CB  1 
ATOM   592  C CG  . PHE B 2 69  ? 75.878  57.712  63.033 1.00 129.93 ? 69  PHE B CG  1 
ATOM   593  C CD1 . PHE B 2 69  ? 75.976  56.358  63.367 1.00 169.86 ? 69  PHE B CD1 1 
ATOM   594  C CD2 . PHE B 2 69  ? 75.985  58.055  61.697 1.00 147.39 ? 69  PHE B CD2 1 
ATOM   595  C CE1 . PHE B 2 69  ? 76.175  55.369  62.404 1.00 191.13 ? 69  PHE B CE1 1 
ATOM   596  C CE2 . PHE B 2 69  ? 76.178  57.062  60.740 1.00 178.31 ? 69  PHE B CE2 1 
ATOM   597  C CZ  . PHE B 2 69  ? 76.282  55.723  61.080 1.00 163.35 ? 69  PHE B CZ  1 
ATOM   598  N N   . VAL B 2 70  ? 73.733  61.059  65.303 1.00 150.52 ? 70  VAL B N   1 
ATOM   599  C CA  . VAL B 2 70  ? 73.627  62.255  66.132 1.00 152.26 ? 70  VAL B CA  1 
ATOM   600  C C   . VAL B 2 70  ? 72.210  62.480  66.691 1.00 148.92 ? 70  VAL B C   1 
ATOM   601  O O   . VAL B 2 70  ? 72.055  63.257  67.634 1.00 176.01 ? 70  VAL B O   1 
ATOM   602  C CB  . VAL B 2 70  ? 74.164  63.471  65.338 1.00 172.00 ? 70  VAL B CB  1 
ATOM   603  C CG1 . VAL B 2 70  ? 73.182  64.014  64.308 1.00 204.75 ? 70  VAL B CG1 1 
ATOM   604  C CG2 . VAL B 2 70  ? 74.617  64.622  66.227 1.00 227.41 ? 70  VAL B CG2 1 
ATOM   605  N N   . THR B 2 71  ? 71.175  61.838  66.118 1.00 163.46 ? 71  THR B N   1 
ATOM   606  C CA  . THR B 2 71  ? 69.766  62.100  66.457 1.00 160.31 ? 71  THR B CA  1 
ATOM   607  C C   . THR B 2 71  ? 68.967  60.912  67.044 1.00 127.01 ? 71  THR B C   1 
ATOM   608  O O   . THR B 2 71  ? 67.846  61.146  67.463 1.00 117.60 ? 71  THR B O   1 
ATOM   609  C CB  . THR B 2 71  ? 69.076  62.725  65.229 1.00 173.79 ? 71  THR B CB  1 
ATOM   610  O OG1 . THR B 2 71  ? 69.713  63.984  64.982 1.00 239.52 ? 71  THR B OG1 1 
ATOM   611  C CG2 . THR B 2 71  ? 67.592  62.925  65.348 1.00 185.26 ? 71  THR B CG2 1 
ATOM   612  N N   . PRO B 2 72  ? 69.427  59.638  67.207 1.00 130.14 ? 72  PRO B N   1 
ATOM   613  C CA  . PRO B 2 72  ? 68.660  58.620  67.950 1.00 131.69 ? 72  PRO B CA  1 
ATOM   614  C C   . PRO B 2 72  ? 68.181  59.008  69.363 1.00 167.43 ? 72  PRO B C   1 
ATOM   615  O O   . PRO B 2 72  ? 67.117  58.570  69.767 1.00 149.97 ? 72  PRO B O   1 
ATOM   616  C CB  . PRO B 2 72  ? 69.656  57.454  68.058 1.00 152.66 ? 72  PRO B CB  1 
ATOM   617  C CG  . PRO B 2 72  ? 70.498  57.601  66.830 1.00 153.36 ? 72  PRO B CG  1 
ATOM   618  C CD  . PRO B 2 72  ? 70.694  59.086  66.727 1.00 150.41 ? 72  PRO B CD  1 
ATOM   619  N N   . THR B 2 73  ? 68.944  59.830  70.105 1.00 158.10 ? 73  THR B N   1 
ATOM   620  C CA  . THR B 2 73  ? 68.484  60.432  71.352 1.00 147.11 ? 73  THR B CA  1 
ATOM   621  C C   . THR B 2 73  ? 67.294  61.381  71.158 1.00 129.20 ? 73  THR B C   1 
ATOM   622  O O   . THR B 2 73  ? 66.406  61.463  72.013 1.00 130.56 ? 73  THR B O   1 
ATOM   623  C CB  . THR B 2 73  ? 69.597  61.254  72.013 1.00 189.43 ? 73  THR B CB  1 
ATOM   624  O OG1 . THR B 2 73  ? 70.652  60.368  72.342 1.00 220.23 ? 73  THR B OG1 1 
ATOM   625  C CG2 . THR B 2 73  ? 69.186  61.948  73.293 1.00 228.73 ? 73  THR B CG2 1 
ATOM   626  N N   . GLY B 2 74  ? 67.296  62.113  70.039 1.00 156.89 ? 74  GLY B N   1 
ATOM   627  C CA  . GLY B 2 74  ? 66.389  63.215  69.778 1.00 181.42 ? 74  GLY B CA  1 
ATOM   628  C C   . GLY B 2 74  ? 64.940  62.751  69.706 1.00 159.81 ? 74  GLY B C   1 
ATOM   629  O O   . GLY B 2 74  ? 64.073  63.405  70.278 1.00 205.37 ? 74  GLY B O   1 
ATOM   630  N N   . VAL B 2 75  ? 64.685  61.614  69.048 1.00 97.57  ? 75  VAL B N   1 
ATOM   631  C CA  . VAL B 2 75  ? 63.332  61.099  69.018 1.00 129.26 ? 75  VAL B CA  1 
ATOM   632  C C   . VAL B 2 75  ? 62.955  60.559  70.396 1.00 168.66 ? 75  VAL B C   1 
ATOM   633  O O   . VAL B 2 75  ? 61.833  60.804  70.835 1.00 215.40 ? 75  VAL B O   1 
ATOM   634  C CB  . VAL B 2 75  ? 63.052  60.065  67.905 1.00 166.08 ? 75  VAL B CB  1 
ATOM   635  C CG1 . VAL B 2 75  ? 63.487  60.575  66.537 1.00 187.27 ? 75  VAL B CG1 1 
ATOM   636  C CG2 . VAL B 2 75  ? 63.612  58.682  68.192 1.00 168.78 ? 75  VAL B CG2 1 
ATOM   637  N N   . LEU B 2 76  ? 63.862  59.848  71.083 1.00 160.83 ? 76  LEU B N   1 
ATOM   638  C CA  . LEU B 2 76  ? 63.544  59.195  72.356 1.00 153.27 ? 76  LEU B CA  1 
ATOM   639  C C   . LEU B 2 76  ? 63.221  60.195  73.474 1.00 122.76 ? 76  LEU B C   1 
ATOM   640  O O   . LEU B 2 76  ? 62.354  59.914  74.292 1.00 110.26 ? 76  LEU B O   1 
ATOM   641  C CB  . LEU B 2 76  ? 64.714  58.290  72.722 1.00 143.42 ? 76  LEU B CB  1 
ATOM   642  C CG  . LEU B 2 76  ? 64.562  57.488  73.997 1.00 136.31 ? 76  LEU B CG  1 
ATOM   643  C CD1 . LEU B 2 76  ? 63.433  56.479  73.860 1.00 110.38 ? 76  LEU B CD1 1 
ATOM   644  C CD2 . LEU B 2 76  ? 65.905  56.839  74.340 1.00 150.77 ? 76  LEU B CD2 1 
ATOM   645  N N   . LYS B 2 77  ? 63.870  61.362  73.486 1.00 150.07 ? 77  LYS B N   1 
ATOM   646  C CA  . LYS B 2 77  ? 63.565  62.438  74.423 1.00 178.54 ? 77  LYS B CA  1 
ATOM   647  C C   . LYS B 2 77  ? 62.146  63.006  74.256 1.00 199.55 ? 77  LYS B C   1 
ATOM   648  O O   . LYS B 2 77  ? 61.593  63.512  75.235 1.00 227.86 ? 77  LYS B O   1 
ATOM   649  C CB  . LYS B 2 77  ? 64.643  63.516  74.283 1.00 219.23 ? 77  LYS B CB  1 
ATOM   650  C CG  . LYS B 2 77  ? 64.536  64.665  75.276 1.00 267.71 ? 77  LYS B CG  1 
ATOM   651  C CD  . LYS B 2 77  ? 65.834  65.425  75.465 1.00 332.37 ? 77  LYS B CD  1 
ATOM   652  C CE  . LYS B 2 77  ? 66.358  66.064  74.195 1.00 381.29 ? 77  LYS B CE  1 
ATOM   653  N NZ  . LYS B 2 77  ? 67.595  66.843  74.448 1.00 412.19 ? 77  LYS B NZ  1 
ATOM   654  N N   . GLU B 2 78  ? 61.553  62.921  73.047 1.00 164.06 ? 78  GLU B N   1 
ATOM   655  C CA  . GLU B 2 78  ? 60.181  63.357  72.804 1.00 209.87 ? 78  GLU B CA  1 
ATOM   656  C C   . GLU B 2 78  ? 59.174  62.194  72.870 1.00 199.01 ? 78  GLU B C   1 
ATOM   657  O O   . GLU B 2 78  ? 58.042  62.382  73.332 1.00 252.88 ? 78  GLU B O   1 
ATOM   658  C CB  . GLU B 2 78  ? 60.101  64.089  71.455 1.00 196.83 ? 78  GLU B CB  1 
ATOM   659  C CG  . GLU B 2 78  ? 61.081  65.244  71.238 1.00 197.51 ? 78  GLU B CG  1 
ATOM   660  C CD  . GLU B 2 78  ? 61.228  66.292  72.333 1.00 255.58 ? 78  GLU B CD  1 
ATOM   661  O OE1 . GLU B 2 78  ? 60.306  66.435  73.175 1.00 331.27 ? 78  GLU B OE1 1 
ATOM   662  O OE2 . GLU B 2 78  ? 62.278  66.977  72.343 1.00 272.02 ? 78  GLU B OE2 1 
ATOM   663  N N   . ALA B 2 79  ? 59.578  61.004  72.405 1.00 183.72 ? 79  ALA B N   1 
ATOM   664  C CA  . ALA B 2 79  ? 58.728  59.817  72.355 1.00 232.44 ? 79  ALA B CA  1 
ATOM   665  C C   . ALA B 2 79  ? 58.688  59.051  73.688 1.00 236.87 ? 79  ALA B C   1 
ATOM   666  O O   . ALA B 2 79  ? 57.783  58.234  73.905 1.00 202.22 ? 79  ALA B O   1 
ATOM   667  C CB  . ALA B 2 79  ? 59.208  58.939  71.227 1.00 215.06 ? 79  ALA B CB  1 
ATOM   668  N N   . GLY B 2 80  ? 59.655  59.275  74.592 1.00 194.61 ? 80  GLY B N   1 
ATOM   669  C CA  . GLY B 2 80  ? 59.593  58.763  75.956 1.00 220.27 ? 80  GLY B CA  1 
ATOM   670  C C   . GLY B 2 80  ? 59.995  57.290  76.113 1.00 212.40 ? 80  GLY B C   1 
ATOM   671  O O   . GLY B 2 80  ? 60.625  56.952  77.132 1.00 233.47 ? 80  GLY B O   1 
ATOM   672  N N   . SER B 2 81  ? 59.644  56.413  75.134 1.00 125.61 ? 81  SER B N   1 
ATOM   673  C CA  . SER B 2 81  ? 59.919  54.981  75.285 1.00 157.61 ? 81  SER B CA  1 
ATOM   674  C C   . SER B 2 81  ? 60.310  54.301  73.986 1.00 132.33 ? 81  SER B C   1 
ATOM   675  O O   . SER B 2 81  ? 59.948  54.786  72.923 1.00 162.15 ? 81  SER B O   1 
ATOM   676  C CB  . SER B 2 81  ? 58.763  54.254  75.894 1.00 217.42 ? 81  SER B CB  1 
ATOM   677  O OG  . SER B 2 81  ? 57.727  54.047  74.945 1.00 156.97 ? 81  SER B OG  1 
ATOM   678  N N   . PRO B 2 82  ? 61.088  53.181  74.025 1.00 147.86 ? 82  PRO B N   1 
ATOM   679  C CA  . PRO B 2 82  ? 61.559  52.509  72.809 1.00 156.69 ? 82  PRO B CA  1 
ATOM   680  C C   . PRO B 2 82  ? 60.409  52.082  71.892 1.00 168.57 ? 82  PRO B C   1 
ATOM   681  O O   . PRO B 2 82  ? 60.549  52.119  70.682 1.00 151.00 ? 82  PRO B O   1 
ATOM   682  C CB  . PRO B 2 82  ? 62.338  51.285  73.312 1.00 170.05 ? 82  PRO B CB  1 
ATOM   683  C CG  . PRO B 2 82  ? 62.774  51.714  74.701 1.00 208.60 ? 82  PRO B CG  1 
ATOM   684  C CD  . PRO B 2 82  ? 61.592  52.505  75.232 1.00 185.26 ? 82  PRO B CD  1 
ATOM   685  N N   . GLY B 2 83  ? 59.267  51.685  72.443 1.00 206.34 ? 83  GLY B N   1 
ATOM   686  C CA  . GLY B 2 83  ? 58.152  51.248  71.611 1.00 270.06 ? 83  GLY B CA  1 
ATOM   687  C C   . GLY B 2 83  ? 57.527  52.326  70.722 1.00 171.16 ? 83  GLY B C   1 
ATOM   688  O O   . GLY B 2 83  ? 57.007  51.993  69.679 1.00 193.47 ? 83  GLY B O   1 
ATOM   689  N N   . LEU B 2 84  ? 57.543  53.597  71.143 1.00 177.38 ? 84  LEU B N   1 
ATOM   690  C CA  . LEU B 2 84  ? 57.114  54.707  70.304 1.00 182.40 ? 84  LEU B CA  1 
ATOM   691  C C   . LEU B 2 84  ? 58.302  55.273  69.523 1.00 169.39 ? 84  LEU B C   1 
ATOM   692  O O   . LEU B 2 84  ? 58.144  55.634  68.352 1.00 147.61 ? 84  LEU B O   1 
ATOM   693  C CB  . LEU B 2 84  ? 56.433  55.790  71.148 1.00 185.91 ? 84  LEU B CB  1 
ATOM   694  C CG  . LEU B 2 84  ? 55.884  56.967  70.346 1.00 173.99 ? 84  LEU B CG  1 
ATOM   695  C CD1 . LEU B 2 84  ? 54.827  56.477  69.357 1.00 213.10 ? 84  LEU B CD1 1 
ATOM   696  C CD2 . LEU B 2 84  ? 55.302  58.047  71.241 1.00 177.58 ? 84  LEU B CD2 1 
ATOM   697  N N   . ALA B 2 85  ? 59.495  55.353  70.127 1.00 151.47 ? 85  ALA B N   1 
ATOM   698  C CA  . ALA B 2 85  ? 60.676  55.851  69.446 1.00 140.78 ? 85  ALA B CA  1 
ATOM   699  C C   . ALA B 2 85  ? 60.989  55.014  68.202 1.00 148.88 ? 85  ALA B C   1 
ATOM   700  O O   . ALA B 2 85  ? 61.172  55.571  67.124 1.00 204.02 ? 85  ALA B O   1 
ATOM   701  C CB  . ALA B 2 85  ? 61.836  55.848  70.421 1.00 229.26 ? 85  ALA B CB  1 
ATOM   702  N N   . LEU B 2 86  ? 61.051  53.680  68.332 1.00 130.31 ? 86  LEU B N   1 
ATOM   703  C CA  . LEU B 2 86  ? 61.327  52.803  67.207 1.00 120.60 ? 86  LEU B CA  1 
ATOM   704  C C   . LEU B 2 86  ? 60.173  52.839  66.195 1.00 140.84 ? 86  LEU B C   1 
ATOM   705  O O   . LEU B 2 86  ? 60.388  52.505  65.024 1.00 197.56 ? 86  LEU B O   1 
ATOM   706  C CB  . LEU B 2 86  ? 61.626  51.396  67.734 1.00 131.05 ? 86  LEU B CB  1 
ATOM   707  C CG  . LEU B 2 86  ? 62.287  50.465  66.718 1.00 201.76 ? 86  LEU B CG  1 
ATOM   708  C CD1 . LEU B 2 86  ? 63.532  49.746  67.274 1.00 144.45 ? 86  LEU B CD1 1 
ATOM   709  C CD2 . LEU B 2 86  ? 61.249  49.478  66.196 1.00 294.53 ? 86  LEU B CD2 1 
ATOM   710  N N   . VAL B 2 87  ? 58.964  53.277  66.598 1.00 134.18 ? 87  VAL B N   1 
ATOM   711  C CA  . VAL B 2 87  ? 57.829  53.477  65.696 1.00 151.21 ? 87  VAL B CA  1 
ATOM   712  C C   . VAL B 2 87  ? 57.962  54.776  64.908 1.00 131.48 ? 87  VAL B C   1 
ATOM   713  O O   . VAL B 2 87  ? 57.729  54.707  63.699 1.00 160.37 ? 87  VAL B O   1 
ATOM   714  C CB  . VAL B 2 87  ? 56.475  53.343  66.414 1.00 209.60 ? 87  VAL B CB  1 
ATOM   715  C CG1 . VAL B 2 87  ? 55.306  54.031  65.717 1.00 263.09 ? 87  VAL B CG1 1 
ATOM   716  C CG2 . VAL B 2 87  ? 56.171  51.860  66.605 1.00 272.82 ? 87  VAL B CG2 1 
ATOM   717  N N   . VAL B 2 88  ? 58.333  55.922  65.498 1.00 127.55 ? 88  VAL B N   1 
ATOM   718  C CA  . VAL B 2 88  ? 58.506  57.144  64.686 1.00 175.01 ? 88  VAL B CA  1 
ATOM   719  C C   . VAL B 2 88  ? 59.647  56.986  63.666 1.00 148.83 ? 88  VAL B C   1 
ATOM   720  O O   . VAL B 2 88  ? 59.585  57.610  62.610 1.00 202.25 ? 88  VAL B O   1 
ATOM   721  C CB  . VAL B 2 88  ? 58.670  58.467  65.476 1.00 162.94 ? 88  VAL B CB  1 
ATOM   722  C CG1 . VAL B 2 88  ? 57.414  58.799  66.232 1.00 188.52 ? 88  VAL B CG1 1 
ATOM   723  C CG2 . VAL B 2 88  ? 59.839  58.474  66.430 1.00 177.39 ? 88  VAL B CG2 1 
ATOM   724  N N   . TRP B 2 89  ? 60.667  56.167  63.940 1.00 124.01 ? 89  TRP B N   1 
ATOM   725  C CA  . TRP B 2 89  ? 61.682  55.826  62.949 1.00 144.81 ? 89  TRP B CA  1 
ATOM   726  C C   . TRP B 2 89  ? 61.110  55.116  61.726 1.00 124.01 ? 89  TRP B C   1 
ATOM   727  O O   . TRP B 2 89  ? 61.596  55.348  60.614 1.00 211.09 ? 89  TRP B O   1 
ATOM   728  C CB  . TRP B 2 89  ? 62.824  54.994  63.557 1.00 153.51 ? 89  TRP B CB  1 
ATOM   729  C CG  . TRP B 2 89  ? 63.805  55.870  64.295 1.00 168.06 ? 89  TRP B CG  1 
ATOM   730  C CD1 . TRP B 2 89  ? 64.033  55.885  65.638 1.00 174.40 ? 89  TRP B CD1 1 
ATOM   731  C CD2 . TRP B 2 89  ? 64.699  56.855  63.724 1.00 146.02 ? 89  TRP B CD2 1 
ATOM   732  N NE1 . TRP B 2 89  ? 64.998  56.807  65.929 1.00 184.80 ? 89  TRP B NE1 1 
ATOM   733  C CE2 . TRP B 2 89  ? 65.430  57.425  64.777 1.00 174.95 ? 89  TRP B CE2 1 
ATOM   734  C CE3 . TRP B 2 89  ? 64.961  57.301  62.434 1.00 158.68 ? 89  TRP B CE3 1 
ATOM   735  C CZ2 . TRP B 2 89  ? 66.402  58.415  64.570 1.00 209.51 ? 89  TRP B CZ2 1 
ATOM   736  C CZ3 . TRP B 2 89  ? 65.923  58.262  62.229 1.00 220.93 ? 89  TRP B CZ3 1 
ATOM   737  C CH2 . TRP B 2 89  ? 66.636  58.824  63.283 1.00 211.09 ? 89  TRP B CH2 1 
ATOM   738  N N   . ALA B 2 90  ? 60.114  54.252  61.917 1.00 119.56 ? 90  ALA B N   1 
ATOM   739  C CA  . ALA B 2 90  ? 59.426  53.613  60.805 1.00 151.12 ? 90  ALA B CA  1 
ATOM   740  C C   . ALA B 2 90  ? 58.446  54.594  60.147 1.00 141.12 ? 90  ALA B C   1 
ATOM   741  O O   . ALA B 2 90  ? 58.389  54.660  58.925 1.00 177.69 ? 90  ALA B O   1 
ATOM   742  C CB  . ALA B 2 90  ? 58.742  52.359  61.297 1.00 205.20 ? 90  ALA B CB  1 
ATOM   743  N N   . ALA B 2 91  ? 57.674  55.356  60.934 1.00 114.34 ? 91  ALA B N   1 
ATOM   744  C CA  . ALA B 2 91  ? 56.690  56.298  60.422 1.00 140.43 ? 91  ALA B CA  1 
ATOM   745  C C   . ALA B 2 91  ? 57.321  57.363  59.521 1.00 147.26 ? 91  ALA B C   1 
ATOM   746  O O   . ALA B 2 91  ? 56.795  57.652  58.444 1.00 150.58 ? 91  ALA B O   1 
ATOM   747  C CB  . ALA B 2 91  ? 55.933  56.924  61.580 1.00 157.36 ? 91  ALA B CB  1 
ATOM   748  N N   . CYS B 2 92  ? 58.448  57.958  59.932 1.00 178.36 ? 92  CYS B N   1 
ATOM   749  C CA  . CYS B 2 92  ? 59.199  58.888  59.088 1.00 157.70 ? 92  CYS B CA  1 
ATOM   750  C C   . CYS B 2 92  ? 59.691  58.206  57.818 1.00 138.34 ? 92  CYS B C   1 
ATOM   751  O O   . CYS B 2 92  ? 59.705  58.867  56.777 1.00 127.06 ? 92  CYS B O   1 
ATOM   752  C CB  . CYS B 2 92  ? 60.368  59.495  59.841 1.00 144.01 ? 92  CYS B CB  1 
ATOM   753  S SG  . CYS B 2 92  ? 59.743  60.439  61.250 1.00 212.11 ? 92  CYS B SG  1 
ATOM   754  N N   . GLY B 2 93  ? 60.051  56.910  57.899 1.00 110.88 ? 93  GLY B N   1 
ATOM   755  C CA  . GLY B 2 93  ? 60.389  56.115  56.734 1.00 115.22 ? 93  GLY B CA  1 
ATOM   756  C C   . GLY B 2 93  ? 59.227  56.073  55.739 1.00 128.32 ? 93  GLY B C   1 
ATOM   757  O O   . GLY B 2 93  ? 59.422  56.335  54.550 1.00 134.80 ? 93  GLY B O   1 
ATOM   758  N N   . VAL B 2 94  ? 58.013  55.758  56.206 1.00 126.83 ? 94  VAL B N   1 
ATOM   759  C CA  . VAL B 2 94  ? 56.825  55.681  55.372 1.00 135.02 ? 94  VAL B CA  1 
ATOM   760  C C   . VAL B 2 94  ? 56.531  57.048  54.766 1.00 103.44 ? 94  VAL B C   1 
ATOM   761  O O   . VAL B 2 94  ? 56.331  57.137  53.547 1.00 158.00 ? 94  VAL B O   1 
ATOM   762  C CB  . VAL B 2 94  ? 55.631  55.103  56.161 1.00 149.29 ? 94  VAL B CB  1 
ATOM   763  C CG1 . VAL B 2 94  ? 54.256  55.375  55.561 1.00 190.67 ? 94  VAL B CG1 1 
ATOM   764  C CG2 . VAL B 2 94  ? 55.877  53.609  56.349 1.00 200.34 ? 94  VAL B CG2 1 
ATOM   765  N N   . PHE B 2 95  ? 56.480  58.094  55.572 1.00 80.30  ? 95  PHE B N   1 
ATOM   766  C CA  . PHE B 2 95  ? 56.193  59.413  55.032 1.00 96.66  ? 95  PHE B CA  1 
ATOM   767  C C   . PHE B 2 95  ? 57.221  59.820  53.974 1.00 97.07  ? 95  PHE B C   1 
ATOM   768  O O   . PHE B 2 95  ? 56.854  60.426  52.965 1.00 135.83 ? 95  PHE B O   1 
ATOM   769  C CB  . PHE B 2 95  ? 56.173  60.394  56.186 1.00 138.47 ? 95  PHE B CB  1 
ATOM   770  C CG  . PHE B 2 95  ? 56.028  61.865  55.866 1.00 112.46 ? 95  PHE B CG  1 
ATOM   771  C CD1 . PHE B 2 95  ? 57.118  62.639  55.434 1.00 133.28 ? 95  PHE B CD1 1 
ATOM   772  C CD2 . PHE B 2 95  ? 54.810  62.477  56.043 1.00 129.44 ? 95  PHE B CD2 1 
ATOM   773  C CE1 . PHE B 2 95  ? 56.992  63.997  55.191 1.00 130.38 ? 95  PHE B CE1 1 
ATOM   774  C CE2 . PHE B 2 95  ? 54.676  63.830  55.800 1.00 163.93 ? 95  PHE B CE2 1 
ATOM   775  C CZ  . PHE B 2 95  ? 55.763  64.588  55.385 1.00 171.89 ? 95  PHE B CZ  1 
ATOM   776  N N   . SER B 2 96  ? 58.498  59.475  54.186 1.00 106.24 ? 96  SER B N   1 
ATOM   777  C CA  . SER B 2 96  ? 59.546  59.673  53.202 1.00 120.06 ? 96  SER B CA  1 
ATOM   778  C C   . SER B 2 96  ? 59.295  58.841  51.950 1.00 114.32 ? 96  SER B C   1 
ATOM   779  O O   . SER B 2 96  ? 59.367  59.401  50.862 1.00 116.01 ? 96  SER B O   1 
ATOM   780  C CB  . SER B 2 96  ? 60.899  59.365  53.776 1.00 164.64 ? 96  SER B CB  1 
ATOM   781  O OG  . SER B 2 96  ? 61.129  60.118  54.958 1.00 167.00 ? 96  SER B OG  1 
ATOM   782  N N   . ILE B 2 97  ? 59.005  57.536  52.069 1.00 107.93 ? 97  ILE B N   1 
ATOM   783  C CA  . ILE B 2 97  ? 58.754  56.683  50.905 1.00 124.20 ? 97  ILE B CA  1 
ATOM   784  C C   . ILE B 2 97  ? 57.613  57.214  50.043 1.00 108.34 ? 97  ILE B C   1 
ATOM   785  O O   . ILE B 2 97  ? 57.826  57.323  48.828 1.00 162.57 ? 97  ILE B O   1 
ATOM   786  C CB  . ILE B 2 97  ? 58.538  55.221  51.326 1.00 135.41 ? 97  ILE B CB  1 
ATOM   787  C CG1 . ILE B 2 97  ? 59.919  54.571  51.548 1.00 125.45 ? 97  ILE B CG1 1 
ATOM   788  C CG2 . ILE B 2 97  ? 57.631  54.428  50.359 1.00 135.48 ? 97  ILE B CG2 1 
ATOM   789  C CD1 . ILE B 2 97  ? 59.856  53.304  52.411 1.00 164.67 ? 97  ILE B CD1 1 
ATOM   790  N N   . VAL B 2 98  ? 56.460  57.560  50.626 1.00 87.28  ? 98  VAL B N   1 
ATOM   791  C CA  . VAL B 2 98  ? 55.359  58.061  49.812 1.00 134.51 ? 98  VAL B CA  1 
ATOM   792  C C   . VAL B 2 98  ? 55.663  59.451  49.227 1.00 130.01 ? 98  VAL B C   1 
ATOM   793  O O   . VAL B 2 98  ? 55.286  59.724  48.091 1.00 168.77 ? 98  VAL B O   1 
ATOM   794  C CB  . VAL B 2 98  ? 54.006  58.016  50.545 1.00 132.36 ? 98  VAL B CB  1 
ATOM   795  C CG1 . VAL B 2 98  ? 53.756  56.576  51.032 1.00 144.86 ? 98  VAL B CG1 1 
ATOM   796  C CG2 . VAL B 2 98  ? 53.860  59.045  51.647 1.00 114.91 ? 98  VAL B CG2 1 
ATOM   797  N N   . GLY B 2 99  ? 56.361  60.309  49.953 1.00 96.26  ? 99  GLY B N   1 
ATOM   798  C CA  . GLY B 2 99  ? 56.847  61.559  49.409 1.00 112.03 ? 99  GLY B CA  1 
ATOM   799  C C   . GLY B 2 99  ? 57.875  61.398  48.294 1.00 116.86 ? 99  GLY B C   1 
ATOM   800  O O   . GLY B 2 99  ? 57.840  62.148  47.317 1.00 201.44 ? 99  GLY B O   1 
ATOM   801  N N   . ALA B 2 100 ? 58.761  60.410  48.413 1.00 97.88  ? 100 ALA B N   1 
ATOM   802  C CA  . ALA B 2 100 ? 59.808  60.173  47.426 1.00 138.73 ? 100 ALA B CA  1 
ATOM   803  C C   . ALA B 2 100 ? 59.250  59.571  46.133 1.00 154.91 ? 100 ALA B C   1 
ATOM   804  O O   . ALA B 2 100 ? 59.589  60.021  45.033 1.00 145.96 ? 100 ALA B O   1 
ATOM   805  C CB  . ALA B 2 100 ? 60.858  59.302  48.041 1.00 135.62 ? 100 ALA B CB  1 
ATOM   806  N N   . LEU B 2 101 ? 58.371  58.577  46.237 1.00 152.07 ? 101 LEU B N   1 
ATOM   807  C CA  . LEU B 2 101 ? 57.639  58.115  45.069 1.00 135.20 ? 101 LEU B CA  1 
ATOM   808  C C   . LEU B 2 101 ? 56.859  59.266  44.427 1.00 119.60 ? 101 LEU B C   1 
ATOM   809  O O   . LEU B 2 101 ? 56.807  59.367  43.204 1.00 173.47 ? 101 LEU B O   1 
ATOM   810  C CB  . LEU B 2 101 ? 56.686  56.992  45.477 1.00 136.65 ? 101 LEU B CB  1 
ATOM   811  C CG  . LEU B 2 101 ? 57.367  55.639  45.592 1.00 189.91 ? 101 LEU B CG  1 
ATOM   812  C CD1 . LEU B 2 101 ? 56.372  54.667  46.225 1.00 289.97 ? 101 LEU B CD1 1 
ATOM   813  C CD2 . LEU B 2 101 ? 57.880  55.165  44.225 1.00 189.45 ? 101 LEU B CD2 1 
ATOM   814  N N   . CYS B 2 102 ? 56.242  60.127  45.217 1.00 85.41  ? 102 CYS B N   1 
ATOM   815  C CA  . CYS B 2 102 ? 55.566  61.278  44.680 1.00 116.46 ? 102 CYS B CA  1 
ATOM   816  C C   . CYS B 2 102 ? 56.544  62.155  43.896 1.00 106.65 ? 102 CYS B C   1 
ATOM   817  O O   . CYS B 2 102 ? 56.196  62.708  42.854 1.00 178.60 ? 102 CYS B O   1 
ATOM   818  C CB  . CYS B 2 102 ? 54.835  61.995  45.810 1.00 155.84 ? 102 CYS B CB  1 
ATOM   819  S SG  . CYS B 2 102 ? 53.505  63.039  45.191 1.00 210.89 ? 102 CYS B SG  1 
ATOM   820  N N   . TYR B 2 103 ? 57.771  62.299  44.374 1.00 113.48 ? 103 TYR B N   1 
ATOM   821  C CA  . TYR B 2 103 ? 58.841  62.985  43.651 1.00 147.51 ? 103 TYR B CA  1 
ATOM   822  C C   . TYR B 2 103 ? 59.308  62.225  42.401 1.00 131.71 ? 103 TYR B C   1 
ATOM   823  O O   . TYR B 2 103 ? 59.780  62.855  41.464 1.00 147.20 ? 103 TYR B O   1 
ATOM   824  C CB  . TYR B 2 103 ? 59.996  63.297  44.610 1.00 158.37 ? 103 TYR B CB  1 
ATOM   825  C CG  . TYR B 2 103 ? 59.955  64.754  45.039 1.00 124.82 ? 103 TYR B CG  1 
ATOM   826  C CD1 . TYR B 2 103 ? 58.862  65.248  45.724 1.00 154.88 ? 103 TYR B CD1 1 
ATOM   827  C CD2 . TYR B 2 103 ? 60.985  65.628  44.744 1.00 114.42 ? 103 TYR B CD2 1 
ATOM   828  C CE1 . TYR B 2 103 ? 58.800  66.573  46.119 1.00 155.35 ? 103 TYR B CE1 1 
ATOM   829  C CE2 . TYR B 2 103 ? 60.947  66.956  45.143 1.00 139.27 ? 103 TYR B CE2 1 
ATOM   830  C CZ  . TYR B 2 103 ? 59.843  67.431  45.836 1.00 130.83 ? 103 TYR B CZ  1 
ATOM   831  O OH  . TYR B 2 103 ? 59.768  68.737  46.231 1.00 138.70 ? 103 TYR B OH  1 
ATOM   832  N N   . ALA B 2 104 ? 59.184  60.907  42.340 1.00 121.53 ? 104 ALA B N   1 
ATOM   833  C CA  . ALA B 2 104 ? 59.455  60.175  41.105 1.00 178.37 ? 104 ALA B CA  1 
ATOM   834  C C   . ALA B 2 104 ? 58.412  60.457  40.000 1.00 166.83 ? 104 ALA B C   1 
ATOM   835  O O   . ALA B 2 104 ? 58.776  60.581  38.823 1.00 148.98 ? 104 ALA B O   1 
ATOM   836  C CB  . ALA B 2 104 ? 59.544  58.715  41.448 1.00 228.10 ? 104 ALA B CB  1 
ATOM   837  N N   . GLU B 2 105 ? 57.117  60.576  40.355 1.00 148.39 ? 105 GLU B N   1 
ATOM   838  C CA  . GLU B 2 105 ? 56.092  61.024  39.427 1.00 184.98 ? 105 GLU B CA  1 
ATOM   839  C C   . GLU B 2 105 ? 56.400  62.437  38.939 1.00 125.19 ? 105 GLU B C   1 
ATOM   840  O O   . GLU B 2 105 ? 56.435  62.689  37.731 1.00 145.42 ? 105 GLU B O   1 
ATOM   841  C CB  . GLU B 2 105 ? 54.689  60.970  40.054 1.00 222.18 ? 105 GLU B CB  1 
ATOM   842  C CG  . GLU B 2 105 ? 54.165  59.569  40.347 1.00 320.72 ? 105 GLU B CG  1 
ATOM   843  C CD  . GLU B 2 105 ? 52.725  59.564  40.839 1.00 318.96 ? 105 GLU B CD  1 
ATOM   844  O OE1 . GLU B 2 105 ? 52.518  59.786  42.042 1.00 316.07 ? 105 GLU B OE1 1 
ATOM   845  O OE2 . GLU B 2 105 ? 51.809  59.346  40.019 1.00 296.18 ? 105 GLU B OE2 1 
ATOM   846  N N   . LEU B 2 106 ? 56.610  63.361  39.870 1.00 129.29 ? 106 LEU B N   1 
ATOM   847  C CA  . LEU B 2 106 ? 56.822  64.775  39.542 1.00 158.41 ? 106 LEU B CA  1 
ATOM   848  C C   . LEU B 2 106 ? 58.101  64.986  38.730 1.00 102.51 ? 106 LEU B C   1 
ATOM   849  O O   . LEU B 2 106 ? 58.112  65.761  37.771 1.00 108.04 ? 106 LEU B O   1 
ATOM   850  C CB  . LEU B 2 106 ? 56.835  65.590  40.840 1.00 171.24 ? 106 LEU B CB  1 
ATOM   851  C CG  . LEU B 2 106 ? 56.904  67.104  40.691 1.00 142.31 ? 106 LEU B CG  1 
ATOM   852  C CD1 . LEU B 2 106 ? 55.765  67.700  39.893 1.00 164.64 ? 106 LEU B CD1 1 
ATOM   853  C CD2 . LEU B 2 106 ? 56.878  67.710  42.082 1.00 209.34 ? 106 LEU B CD2 1 
ATOM   854  N N   . GLY B 2 107 ? 59.148  64.243  39.069 1.00 120.48 ? 107 GLY B N   1 
ATOM   855  C CA  . GLY B 2 107 ? 60.413  64.346  38.376 1.00 159.31 ? 107 GLY B CA  1 
ATOM   856  C C   . GLY B 2 107 ? 60.411  63.773  36.959 1.00 150.91 ? 107 GLY B C   1 
ATOM   857  O O   . GLY B 2 107 ? 60.920  64.402  36.036 1.00 134.10 ? 107 GLY B O   1 
ATOM   858  N N   . THR B 2 108 ? 59.837  62.591  36.758 1.00 138.60 ? 108 THR B N   1 
ATOM   859  C CA  . THR B 2 108 ? 59.725  62.050  35.409 1.00 159.10 ? 108 THR B CA  1 
ATOM   860  C C   . THR B 2 108 ? 58.703  62.830  34.573 1.00 149.53 ? 108 THR B C   1 
ATOM   861  O O   . THR B 2 108 ? 58.792  62.786  33.340 1.00 148.01 ? 108 THR B O   1 
ATOM   862  C CB  . THR B 2 108 ? 59.394  60.553  35.407 1.00 200.42 ? 108 THR B CB  1 
ATOM   863  O OG1 . THR B 2 108 ? 58.218  60.307  36.186 1.00 191.60 ? 108 THR B OG1 1 
ATOM   864  C CG2 . THR B 2 108 ? 60.553  59.726  35.914 1.00 193.81 ? 108 THR B CG2 1 
ATOM   865  N N   . THR B 2 109 ? 57.734  63.518  35.199 1.00 143.72 ? 109 THR B N   1 
ATOM   866  C CA  . THR B 2 109 ? 56.843  64.432  34.493 1.00 146.71 ? 109 THR B CA  1 
ATOM   867  C C   . THR B 2 109 ? 57.625  65.590  33.870 1.00 142.91 ? 109 THR B C   1 
ATOM   868  O O   . THR B 2 109 ? 57.559  65.780  32.656 1.00 146.46 ? 109 THR B O   1 
ATOM   869  C CB  . THR B 2 109 ? 55.734  64.979  35.425 1.00 161.53 ? 109 THR B CB  1 
ATOM   870  O OG1 . THR B 2 109 ? 54.910  63.909  35.901 1.00 136.59 ? 109 THR B OG1 1 
ATOM   871  C CG2 . THR B 2 109 ? 54.811  66.015  34.817 1.00 134.59 ? 109 THR B CG2 1 
ATOM   872  N N   . ILE B 2 110 ? 58.326  66.395  34.697 1.00 134.78 ? 110 ILE B N   1 
ATOM   873  C CA  . ILE B 2 110 ? 58.835  67.696  34.276 1.00 140.88 ? 110 ILE B CA  1 
ATOM   874  C C   . ILE B 2 110 ? 60.273  67.574  33.756 1.00 161.33 ? 110 ILE B C   1 
ATOM   875  O O   . ILE B 2 110 ? 60.630  68.306  32.821 1.00 245.19 ? 110 ILE B O   1 
ATOM   876  C CB  . ILE B 2 110 ? 58.653  68.749  35.394 1.00 159.63 ? 110 ILE B CB  1 
ATOM   877  C CG1 . ILE B 2 110 ? 57.175  68.889  35.788 1.00 182.54 ? 110 ILE B CG1 1 
ATOM   878  C CG2 . ILE B 2 110 ? 59.227  70.108  34.995 1.00 137.85 ? 110 ILE B CG2 1 
ATOM   879  C CD1 . ILE B 2 110 ? 56.881  69.827  36.938 1.00 214.06 ? 110 ILE B CD1 1 
ATOM   880  N N   . SER B 2 111 ? 61.102  66.697  34.351 1.00 142.96 ? 111 SER B N   1 
ATOM   881  C CA  . SER B 2 111 ? 62.440  66.306  33.858 1.00 225.11 ? 111 SER B CA  1 
ATOM   882  C C   . SER B 2 111 ? 63.493  67.441  33.739 1.00 177.90 ? 111 SER B C   1 
ATOM   883  O O   . SER B 2 111 ? 64.607  67.193  33.283 1.00 170.92 ? 111 SER B O   1 
ATOM   884  C CB  . SER B 2 111 ? 62.360  65.508  32.550 1.00 286.23 ? 111 SER B CB  1 
ATOM   885  O OG  . SER B 2 111 ? 63.616  64.902  32.252 1.00 239.29 ? 111 SER B OG  1 
ATOM   886  N N   . LYS B 2 112 ? 63.210  68.683  34.156 1.00 165.96 ? 112 LYS B N   1 
ATOM   887  C CA  . LYS B 2 112 ? 64.253  69.650  34.465 1.00 180.61 ? 112 LYS B CA  1 
ATOM   888  C C   . LYS B 2 112 ? 65.032  69.214  35.715 1.00 188.44 ? 112 LYS B C   1 
ATOM   889  O O   . LYS B 2 112 ? 64.500  68.547  36.608 1.00 152.07 ? 112 LYS B O   1 
ATOM   890  C CB  . LYS B 2 112 ? 63.664  71.040  34.719 1.00 197.63 ? 112 LYS B CB  1 
ATOM   891  C CG  . LYS B 2 112 ? 63.150  71.747  33.485 1.00 264.63 ? 112 LYS B CG  1 
ATOM   892  C CD  . LYS B 2 112 ? 62.455  73.058  33.808 1.00 307.42 ? 112 LYS B CD  1 
ATOM   893  C CE  . LYS B 2 112 ? 61.950  73.802  32.586 1.00 358.42 ? 112 LYS B CE  1 
ATOM   894  N NZ  . LYS B 2 112 ? 63.044  74.415  31.787 1.00 367.94 ? 112 LYS B NZ  1 
ATOM   895  N N   . SER B 2 113 ? 66.314  69.612  35.773 1.00 189.67 ? 113 SER B N   1 
ATOM   896  C CA  . SER B 2 113 ? 67.111  69.623  36.997 1.00 165.48 ? 113 SER B CA  1 
ATOM   897  C C   . SER B 2 113 ? 66.678  70.822  37.839 1.00 159.78 ? 113 SER B C   1 
ATOM   898  O O   . SER B 2 113 ? 65.793  71.587  37.446 1.00 148.00 ? 113 SER B O   1 
ATOM   899  C CB  . SER B 2 113 ? 68.593  69.622  36.706 1.00 159.32 ? 113 SER B CB  1 
ATOM   900  O OG  . SER B 2 113 ? 68.996  70.757  35.971 1.00 232.87 ? 113 SER B OG  1 
ATOM   901  N N   . GLY B 2 114 ? 67.274  70.985  39.028 1.00 145.02 ? 114 GLY B N   1 
ATOM   902  C CA  . GLY B 2 114 ? 66.801  71.973  39.980 1.00 185.18 ? 114 GLY B CA  1 
ATOM   903  C C   . GLY B 2 114 ? 65.541  71.569  40.755 1.00 143.21 ? 114 GLY B C   1 
ATOM   904  O O   . GLY B 2 114 ? 65.028  72.384  41.508 1.00 134.03 ? 114 GLY B O   1 
ATOM   905  N N   . GLY B 2 115 ? 65.068  70.332  40.610 1.00 97.60  ? 115 GLY B N   1 
ATOM   906  C CA  . GLY B 2 115 ? 64.229  69.669  41.594 1.00 126.09 ? 115 GLY B CA  1 
ATOM   907  C C   . GLY B 2 115 ? 63.017  70.472  42.058 1.00 144.90 ? 115 GLY B C   1 
ATOM   908  O O   . GLY B 2 115 ? 62.286  71.025  41.256 1.00 166.57 ? 115 GLY B O   1 
ATOM   909  N N   . ASP B 2 116 ? 62.818  70.515  43.373 1.00 127.21 ? 116 ASP B N   1 
ATOM   910  C CA  . ASP B 2 116 ? 61.718  71.202  44.030 1.00 136.71 ? 116 ASP B CA  1 
ATOM   911  C C   . ASP B 2 116 ? 61.530  72.615  43.477 1.00 143.04 ? 116 ASP B C   1 
ATOM   912  O O   . ASP B 2 116 ? 60.419  72.993  43.111 1.00 171.24 ? 116 ASP B O   1 
ATOM   913  C CB  . ASP B 2 116 ? 62.050  71.165  45.532 1.00 245.71 ? 116 ASP B CB  1 
ATOM   914  C CG  . ASP B 2 116 ? 61.115  71.871  46.497 1.00 257.60 ? 116 ASP B CG  1 
ATOM   915  O OD1 . ASP B 2 116 ? 60.168  72.526  46.030 1.00 195.74 ? 116 ASP B OD1 1 
ATOM   916  O OD2 . ASP B 2 116 ? 61.372  71.766  47.724 1.00 183.01 ? 116 ASP B OD2 1 
ATOM   917  N N   . TYR B 2 117 ? 62.615  73.411  43.403 1.00 169.89 ? 117 TYR B N   1 
ATOM   918  C CA  . TYR B 2 117 ? 62.590  74.758  42.820 1.00 164.82 ? 117 TYR B CA  1 
ATOM   919  C C   . TYR B 2 117 ? 62.075  74.798  41.371 1.00 142.29 ? 117 TYR B C   1 
ATOM   920  O O   . TYR B 2 117 ? 61.191  75.599  41.070 1.00 138.33 ? 117 TYR B O   1 
ATOM   921  C CB  . TYR B 2 117 ? 63.989  75.344  42.907 1.00 150.42 ? 117 TYR B CB  1 
ATOM   922  C CG  . TYR B 2 117 ? 64.210  76.519  41.978 1.00 158.95 ? 117 TYR B CG  1 
ATOM   923  C CD1 . TYR B 2 117 ? 63.626  77.740  42.270 1.00 144.38 ? 117 TYR B CD1 1 
ATOM   924  C CD2 . TYR B 2 117 ? 64.994  76.416  40.825 1.00 158.08 ? 117 TYR B CD2 1 
ATOM   925  C CE1 . TYR B 2 117 ? 63.827  78.851  41.461 1.00 136.60 ? 117 TYR B CE1 1 
ATOM   926  C CE2 . TYR B 2 117 ? 65.184  77.519  40.005 1.00 126.09 ? 117 TYR B CE2 1 
ATOM   927  C CZ  . TYR B 2 117 ? 64.608  78.734  40.327 1.00 142.87 ? 117 TYR B CZ  1 
ATOM   928  O OH  . TYR B 2 117 ? 64.800  79.807  39.507 1.00 205.74 ? 117 TYR B OH  1 
ATOM   929  N N   . ALA B 2 118 ? 62.586  73.929  40.489 1.00 117.08 ? 118 ALA B N   1 
ATOM   930  C CA  . ALA B 2 118 ? 62.128  73.866  39.109 1.00 147.55 ? 118 ALA B CA  1 
ATOM   931  C C   . ALA B 2 118 ? 60.648  73.482  39.025 1.00 120.37 ? 118 ALA B C   1 
ATOM   932  O O   . ALA B 2 118 ? 59.874  74.104  38.296 1.00 195.79 ? 118 ALA B O   1 
ATOM   933  C CB  . ALA B 2 118 ? 62.980  72.892  38.326 1.00 167.83 ? 118 ALA B CB  1 
ATOM   934  N N   . TYR B 2 119 ? 60.245  72.455  39.766 1.00 104.41 ? 119 TYR B N   1 
ATOM   935  C CA  . TYR B 2 119 ? 58.875  71.974  39.759 1.00 120.22 ? 119 TYR B CA  1 
ATOM   936  C C   . TYR B 2 119 ? 57.916  73.011  40.338 1.00 126.01 ? 119 TYR B C   1 
ATOM   937  O O   . TYR B 2 119 ? 56.763  73.063  39.935 1.00 175.92 ? 119 TYR B O   1 
ATOM   938  C CB  . TYR B 2 119 ? 58.781  70.646  40.529 1.00 120.61 ? 119 TYR B CB  1 
ATOM   939  C CG  . TYR B 2 119 ? 59.783  69.596  40.090 1.00 130.69 ? 119 TYR B CG  1 
ATOM   940  C CD1 . TYR B 2 119 ? 60.349  69.595  38.798 1.00 167.12 ? 119 TYR B CD1 1 
ATOM   941  C CD2 . TYR B 2 119 ? 60.173  68.611  40.987 1.00 123.80 ? 119 TYR B CD2 1 
ATOM   942  C CE1 . TYR B 2 119 ? 61.277  68.629  38.433 1.00 201.44 ? 119 TYR B CE1 1 
ATOM   943  C CE2 . TYR B 2 119 ? 61.090  67.638  40.620 1.00 154.60 ? 119 TYR B CE2 1 
ATOM   944  C CZ  . TYR B 2 119 ? 61.652  67.653  39.347 1.00 180.72 ? 119 TYR B CZ  1 
ATOM   945  O OH  . TYR B 2 119 ? 62.580  66.715  38.973 1.00 111.13 ? 119 TYR B OH  1 
ATOM   946  N N   . MET B 2 120 ? 58.377  73.826  41.283 1.00 149.44 ? 120 MET B N   1 
ATOM   947  C CA  . MET B 2 120 ? 57.600  74.930  41.800 1.00 155.29 ? 120 MET B CA  1 
ATOM   948  C C   . MET B 2 120 ? 57.484  76.015  40.733 1.00 143.85 ? 120 MET B C   1 
ATOM   949  O O   . MET B 2 120 ? 56.391  76.564  40.591 1.00 234.15 ? 120 MET B O   1 
ATOM   950  C CB  . MET B 2 120 ? 58.224  75.501  43.079 1.00 157.91 ? 120 MET B CB  1 
ATOM   951  C CG  . MET B 2 120 ? 57.406  76.642  43.664 1.00 144.43 ? 120 MET B CG  1 
ATOM   952  S SD  . MET B 2 120 ? 57.866  77.099  45.325 1.00 215.10 ? 120 MET B SD  1 
ATOM   953  C CE  . MET B 2 120 ? 57.365  75.561  46.105 1.00 157.16 ? 120 MET B CE  1 
ATOM   954  N N   . LEU B 2 121 ? 58.545  76.343  39.985 1.00 137.46 ? 121 LEU B N   1 
ATOM   955  C CA  . LEU B 2 121 ? 58.464  77.394  38.969 1.00 179.19 ? 121 LEU B CA  1 
ATOM   956  C C   . LEU B 2 121 ? 57.442  77.054  37.866 1.00 177.53 ? 121 LEU B C   1 
ATOM   957  O O   . LEU B 2 121 ? 56.713  77.933  37.413 1.00 119.34 ? 121 LEU B O   1 
ATOM   958  C CB  . LEU B 2 121 ? 59.875  77.638  38.414 1.00 172.03 ? 121 LEU B CB  1 
ATOM   959  C CG  . LEU B 2 121 ? 60.018  78.707  37.343 1.00 186.93 ? 121 LEU B CG  1 
ATOM   960  C CD1 . LEU B 2 121 ? 59.454  80.041  37.802 1.00 178.56 ? 121 LEU B CD1 1 
ATOM   961  C CD2 . LEU B 2 121 ? 61.482  78.873  36.979 1.00 202.71 ? 121 LEU B CD2 1 
ATOM   962  N N   . GLU B 2 122 ? 57.367  75.785  37.443 1.00 186.08 ? 122 GLU B N   1 
ATOM   963  C CA  . GLU B 2 122 ? 56.413  75.323  36.439 1.00 158.23 ? 122 GLU B CA  1 
ATOM   964  C C   . GLU B 2 122 ? 54.956  75.340  36.904 1.00 170.41 ? 122 GLU B C   1 
ATOM   965  O O   . GLU B 2 122 ? 54.078  75.109  36.068 1.00 218.54 ? 122 GLU B O   1 
ATOM   966  C CB  . GLU B 2 122 ? 56.771  73.899  35.997 1.00 204.91 ? 122 GLU B CB  1 
ATOM   967  C CG  . GLU B 2 122 ? 58.059  73.828  35.180 1.00 302.04 ? 122 GLU B CG  1 
ATOM   968  C CD  . GLU B 2 122 ? 58.070  74.643  33.899 1.00 395.47 ? 122 GLU B CD  1 
ATOM   969  O OE1 . GLU B 2 122 ? 56.978  74.870  33.332 1.00 443.67 ? 122 GLU B OE1 1 
ATOM   970  O OE2 . GLU B 2 122 ? 59.163  75.061  33.480 1.00 433.85 ? 122 GLU B OE2 1 
ATOM   971  N N   . VAL B 2 123 ? 54.676  75.598  38.200 1.00 156.50 ? 123 VAL B N   1 
ATOM   972  C CA  . VAL B 2 123 ? 53.319  75.585  38.746 1.00 174.59 ? 123 VAL B CA  1 
ATOM   973  C C   . VAL B 2 123 ? 52.935  76.920  39.388 1.00 137.31 ? 123 VAL B C   1 
ATOM   974  O O   . VAL B 2 123 ? 51.861  77.469  39.094 1.00 187.33 ? 123 VAL B O   1 
ATOM   975  C CB  . VAL B 2 123 ? 53.142  74.420  39.728 1.00 192.85 ? 123 VAL B CB  1 
ATOM   976  C CG1 . VAL B 2 123 ? 51.817  74.508  40.472 1.00 215.95 ? 123 VAL B CG1 1 
ATOM   977  C CG2 . VAL B 2 123 ? 53.258  73.093  38.995 1.00 213.30 ? 123 VAL B CG2 1 
ATOM   978  N N   . TYR B 2 124 ? 53.795  77.440  40.262 1.00 106.34 ? 124 TYR B N   1 
ATOM   979  C CA  . TYR B 2 124 ? 53.511  78.658  41.023 1.00 160.15 ? 124 TYR B CA  1 
ATOM   980  C C   . TYR B 2 124 ? 54.131  79.925  40.406 1.00 186.87 ? 124 TYR B C   1 
ATOM   981  O O   . TYR B 2 124 ? 53.800  81.025  40.834 1.00 215.82 ? 124 TYR B O   1 
ATOM   982  C CB  . TYR B 2 124 ? 53.996  78.450  42.465 1.00 167.15 ? 124 TYR B CB  1 
ATOM   983  C CG  . TYR B 2 124 ? 53.303  77.315  43.203 1.00 174.57 ? 124 TYR B CG  1 
ATOM   984  C CD1 . TYR B 2 124 ? 53.736  75.993  43.075 1.00 203.27 ? 124 TYR B CD1 1 
ATOM   985  C CD2 . TYR B 2 124 ? 52.207  77.566  44.024 1.00 210.13 ? 124 TYR B CD2 1 
ATOM   986  C CE1 . TYR B 2 124 ? 53.091  74.958  43.734 1.00 189.81 ? 124 TYR B CE1 1 
ATOM   987  C CE2 . TYR B 2 124 ? 51.558  76.534  44.687 1.00 233.89 ? 124 TYR B CE2 1 
ATOM   988  C CZ  . TYR B 2 124 ? 52.001  75.228  44.542 1.00 178.19 ? 124 TYR B CZ  1 
ATOM   989  O OH  . TYR B 2 124 ? 51.373  74.203  45.185 1.00 144.59 ? 124 TYR B OH  1 
ATOM   990  N N   . GLY B 2 125 ? 55.019  79.802  39.414 1.00 151.48 ? 125 GLY B N   1 
ATOM   991  C CA  . GLY B 2 125 ? 55.603  80.961  38.752 1.00 205.10 ? 125 GLY B CA  1 
ATOM   992  C C   . GLY B 2 125 ? 56.730  81.648  39.531 1.00 168.48 ? 125 GLY B C   1 
ATOM   993  O O   . GLY B 2 125 ? 57.229  81.137  40.523 1.00 146.03 ? 125 GLY B O   1 
ATOM   994  N N   . SER B 2 126 ? 57.116  82.841  39.059 1.00 175.59 ? 126 SER B N   1 
ATOM   995  C CA  . SER B 2 126 ? 58.416  83.437  39.335 1.00 169.30 ? 126 SER B CA  1 
ATOM   996  C C   . SER B 2 126 ? 58.623  83.747  40.824 1.00 156.47 ? 126 SER B C   1 
ATOM   997  O O   . SER B 2 126 ? 59.592  83.265  41.414 1.00 186.48 ? 126 SER B O   1 
ATOM   998  C CB  . SER B 2 126 ? 58.629  84.656  38.457 1.00 183.98 ? 126 SER B CB  1 
ATOM   999  O OG  . SER B 2 126 ? 59.853  85.318  38.752 1.00 176.15 ? 126 SER B OG  1 
ATOM   1000 N N   . LEU B 2 127 ? 57.747  84.539  41.463 1.00 161.90 ? 127 LEU B N   1 
ATOM   1001 C CA  . LEU B 2 127 ? 58.018  84.983  42.830 1.00 144.50 ? 127 LEU B CA  1 
ATOM   1002 C C   . LEU B 2 127 ? 58.008  83.797  43.788 1.00 115.80 ? 127 LEU B C   1 
ATOM   1003 O O   . LEU B 2 127 ? 58.944  83.694  44.580 1.00 134.95 ? 127 LEU B O   1 
ATOM   1004 C CB  . LEU B 2 127 ? 57.061  86.120  43.239 1.00 179.97 ? 127 LEU B CB  1 
ATOM   1005 C CG  . LEU B 2 127 ? 57.033  86.492  44.721 1.00 223.49 ? 127 LEU B CG  1 
ATOM   1006 C CD1 . LEU B 2 127 ? 58.385  87.009  45.201 1.00 203.75 ? 127 LEU B CD1 1 
ATOM   1007 C CD2 . LEU B 2 127 ? 55.948  87.520  44.986 1.00 294.73 ? 127 LEU B CD2 1 
ATOM   1008 N N   . PRO B 2 128 ? 56.998  82.891  43.821 1.00 134.02 ? 128 PRO B N   1 
ATOM   1009 C CA  . PRO B 2 128 ? 57.061  81.709  44.692 1.00 186.89 ? 128 PRO B CA  1 
ATOM   1010 C C   . PRO B 2 128 ? 58.328  80.872  44.549 1.00 130.99 ? 128 PRO B C   1 
ATOM   1011 O O   . PRO B 2 128 ? 58.944  80.520  45.545 1.00 143.03 ? 128 PRO B O   1 
ATOM   1012 C CB  . PRO B 2 128 ? 55.805  80.924  44.319 1.00 196.41 ? 128 PRO B CB  1 
ATOM   1013 C CG  . PRO B 2 128 ? 54.857  82.020  43.890 1.00 225.32 ? 128 PRO B CG  1 
ATOM   1014 C CD  . PRO B 2 128 ? 55.729  82.963  43.097 1.00 136.43 ? 128 PRO B CD  1 
ATOM   1015 N N   . ALA B 2 129 ? 58.738  80.600  43.323 1.00 148.03 ? 129 ALA B N   1 
ATOM   1016 C CA  . ALA B 2 129 ? 59.967  79.867  43.077 1.00 136.12 ? 129 ALA B CA  1 
ATOM   1017 C C   . ALA B 2 129 ? 61.196  80.641  43.568 1.00 117.59 ? 129 ALA B C   1 
ATOM   1018 O O   . ALA B 2 129 ? 62.117  80.029  44.107 1.00 177.03 ? 129 ALA B O   1 
ATOM   1019 C CB  . ALA B 2 129 ? 60.038  79.545  41.604 1.00 162.30 ? 129 ALA B CB  1 
ATOM   1020 N N   . PHE B 2 130 ? 61.261  81.968  43.398 1.00 107.02 ? 130 PHE B N   1 
ATOM   1021 C CA  . PHE B 2 130 ? 62.405  82.710  43.898 1.00 106.01 ? 130 PHE B CA  1 
ATOM   1022 C C   . PHE B 2 130 ? 62.436  82.637  45.424 1.00 119.66 ? 130 PHE B C   1 
ATOM   1023 O O   . PHE B 2 130 ? 63.519  82.415  45.969 1.00 161.52 ? 130 PHE B O   1 
ATOM   1024 C CB  . PHE B 2 130 ? 62.413  84.172  43.448 1.00 125.69 ? 130 PHE B CB  1 
ATOM   1025 C CG  . PHE B 2 130 ? 63.550  84.941  44.076 1.00 117.41 ? 130 PHE B CG  1 
ATOM   1026 C CD1 . PHE B 2 130 ? 64.803  84.952  43.479 1.00 111.61 ? 130 PHE B CD1 1 
ATOM   1027 C CD2 . PHE B 2 130 ? 63.380  85.645  45.281 1.00 99.32  ? 130 PHE B CD2 1 
ATOM   1028 C CE1 . PHE B 2 130 ? 65.870  85.655  44.036 1.00 146.40 ? 130 PHE B CE1 1 
ATOM   1029 C CE2 . PHE B 2 130 ? 64.456  86.333  45.846 1.00 132.32 ? 130 PHE B CE2 1 
ATOM   1030 C CZ  . PHE B 2 130 ? 65.699  86.336  45.226 1.00 136.16 ? 130 PHE B CZ  1 
ATOM   1031 N N   . LEU B 2 131 ? 61.310  82.833  46.136 1.00 122.59 ? 131 LEU B N   1 
ATOM   1032 C CA  . LEU B 2 131 ? 61.353  82.783  47.590 1.00 136.15 ? 131 LEU B CA  1 
ATOM   1033 C C   . LEU B 2 131 ? 61.829  81.406  48.036 1.00 134.60 ? 131 LEU B C   1 
ATOM   1034 O O   . LEU B 2 131 ? 62.627  81.319  48.969 1.00 192.88 ? 131 LEU B O   1 
ATOM   1035 C CB  . LEU B 2 131 ? 59.983  83.124  48.202 1.00 136.96 ? 131 LEU B CB  1 
ATOM   1036 C CG  . LEU B 2 131 ? 59.515  84.552  47.973 1.00 189.63 ? 131 LEU B CG  1 
ATOM   1037 C CD1 . LEU B 2 131 ? 58.188  84.757  48.703 1.00 240.38 ? 131 LEU B CD1 1 
ATOM   1038 C CD2 . LEU B 2 131 ? 60.575  85.588  48.391 1.00 145.09 ? 131 LEU B CD2 1 
ATOM   1039 N N   . LYS B 2 132 ? 61.346  80.337  47.393 1.00 127.09 ? 132 LYS B N   1 
ATOM   1040 C CA  . LYS B 2 132 ? 61.816  78.979  47.637 1.00 128.74 ? 132 LYS B CA  1 
ATOM   1041 C C   . LYS B 2 132 ? 63.334  78.910  47.520 1.00 95.57  ? 132 LYS B C   1 
ATOM   1042 O O   . LYS B 2 132 ? 63.993  78.357  48.404 1.00 125.70 ? 132 LYS B O   1 
ATOM   1043 C CB  . LYS B 2 132 ? 61.106  78.009  46.692 1.00 126.28 ? 132 LYS B CB  1 
ATOM   1044 C CG  . LYS B 2 132 ? 61.794  76.679  46.432 1.00 103.14 ? 132 LYS B CG  1 
ATOM   1045 C CD  . LYS B 2 132 ? 61.845  75.821  47.625 1.00 157.99 ? 132 LYS B CD  1 
ATOM   1046 C CE  . LYS B 2 132 ? 62.843  74.702  47.440 1.00 198.74 ? 132 LYS B CE  1 
ATOM   1047 N NZ  . LYS B 2 132 ? 62.894  73.792  48.617 1.00 255.61 ? 132 LYS B NZ  1 
ATOM   1048 N N   . LEU B 2 133 ? 63.897  79.435  46.444 1.00 95.13  ? 133 LEU B N   1 
ATOM   1049 C CA  . LEU B 2 133 ? 65.334  79.345  46.253 1.00 113.11 ? 133 LEU B CA  1 
ATOM   1050 C C   . LEU B 2 133 ? 66.084  80.273  47.222 1.00 106.81 ? 133 LEU B C   1 
ATOM   1051 O O   . LEU B 2 133 ? 67.138  79.881  47.697 1.00 179.05 ? 133 LEU B O   1 
ATOM   1052 C CB  . LEU B 2 133 ? 65.659  79.620  44.787 1.00 105.00 ? 133 LEU B CB  1 
ATOM   1053 C CG  . LEU B 2 133 ? 67.121  79.511  44.439 1.00 120.24 ? 133 LEU B CG  1 
ATOM   1054 C CD1 . LEU B 2 133 ? 67.317  78.901  43.085 1.00 105.63 ? 133 LEU B CD1 1 
ATOM   1055 C CD2 . LEU B 2 133 ? 67.754  80.907  44.457 1.00 166.04 ? 133 LEU B CD2 1 
ATOM   1056 N N   . TRP B 2 134 ? 65.566  81.448  47.546 1.00 101.21 ? 134 TRP B N   1 
ATOM   1057 C CA  . TRP B 2 134 ? 66.217  82.357  48.470 1.00 124.28 ? 134 TRP B CA  1 
ATOM   1058 C C   . TRP B 2 134 ? 66.362  81.758  49.884 1.00 157.13 ? 134 TRP B C   1 
ATOM   1059 O O   . TRP B 2 134 ? 67.389  81.939  50.539 1.00 177.21 ? 134 TRP B O   1 
ATOM   1060 C CB  . TRP B 2 134 ? 65.397  83.650  48.507 1.00 150.86 ? 134 TRP B CB  1 
ATOM   1061 C CG  . TRP B 2 134 ? 65.956  84.744  49.371 1.00 131.17 ? 134 TRP B CG  1 
ATOM   1062 C CD1 . TRP B 2 134 ? 65.402  85.220  50.526 1.00 144.94 ? 134 TRP B CD1 1 
ATOM   1063 C CD2 . TRP B 2 134 ? 67.183  85.481  49.150 1.00 111.28 ? 134 TRP B CD2 1 
ATOM   1064 N NE1 . TRP B 2 134 ? 66.202  86.217  51.035 1.00 171.45 ? 134 TRP B NE1 1 
ATOM   1065 C CE2 . TRP B 2 134 ? 67.305  86.401  50.225 1.00 139.76 ? 134 TRP B CE2 1 
ATOM   1066 C CE3 . TRP B 2 134 ? 68.180  85.444  48.164 1.00 118.27 ? 134 TRP B CE3 1 
ATOM   1067 C CZ2 . TRP B 2 134 ? 68.392  87.288  50.326 1.00 138.36 ? 134 TRP B CZ2 1 
ATOM   1068 C CZ3 . TRP B 2 134 ? 69.260  86.311  48.271 1.00 172.52 ? 134 TRP B CZ3 1 
ATOM   1069 C CH2 . TRP B 2 134 ? 69.360  87.222  49.337 1.00 174.30 ? 134 TRP B CH2 1 
ATOM   1070 N N   . ILE B 2 135 ? 65.360  81.022  50.372 1.00 141.09 ? 135 ILE B N   1 
ATOM   1071 C CA  . ILE B 2 135 ? 65.471  80.261  51.605 1.00 151.14 ? 135 ILE B CA  1 
ATOM   1072 C C   . ILE B 2 135 ? 66.592  79.216  51.459 1.00 142.08 ? 135 ILE B C   1 
ATOM   1073 O O   . ILE B 2 135 ? 67.373  79.028  52.379 1.00 171.94 ? 135 ILE B O   1 
ATOM   1074 C CB  . ILE B 2 135 ? 64.104  79.618  51.957 1.00 180.97 ? 135 ILE B CB  1 
ATOM   1075 C CG1 . ILE B 2 135 ? 63.017  80.658  52.230 1.00 249.64 ? 135 ILE B CG1 1 
ATOM   1076 C CG2 . ILE B 2 135 ? 64.162  78.656  53.127 1.00 194.61 ? 135 ILE B CG2 1 
ATOM   1077 C CD1 . ILE B 2 135 ? 61.611  80.113  52.010 1.00 301.13 ? 135 ILE B CD1 1 
ATOM   1078 N N   . GLU B 2 136 ? 66.705  78.497  50.340 1.00 108.84 ? 136 GLU B N   1 
ATOM   1079 C CA  . GLU B 2 136 ? 67.767  77.495  50.180 1.00 121.18 ? 136 GLU B CA  1 
ATOM   1080 C C   . GLU B 2 136 ? 69.169  78.088  49.956 1.00 93.37  ? 136 GLU B C   1 
ATOM   1081 O O   . GLU B 2 136 ? 70.157  77.469  50.272 1.00 85.82  ? 136 GLU B O   1 
ATOM   1082 C CB  . GLU B 2 136 ? 67.405  76.502  49.081 1.00 99.17  ? 136 GLU B CB  1 
ATOM   1083 C CG  . GLU B 2 136 ? 66.255  75.650  49.503 1.00 136.92 ? 136 GLU B CG  1 
ATOM   1084 C CD  . GLU B 2 136 ? 65.939  74.491  48.579 1.00 253.03 ? 136 GLU B CD  1 
ATOM   1085 O OE1 . GLU B 2 136 ? 66.017  74.676  47.358 1.00 341.96 ? 136 GLU B OE1 1 
ATOM   1086 O OE2 . GLU B 2 136 ? 65.569  73.401  49.081 1.00 303.54 ? 136 GLU B OE2 1 
ATOM   1087 N N   . LEU B 2 137 ? 69.248  79.275  49.400 1.00 108.03 ? 137 LEU B N   1 
ATOM   1088 C CA  . LEU B 2 137 ? 70.482  79.994  49.181 1.00 113.66 ? 137 LEU B CA  1 
ATOM   1089 C C   . LEU B 2 137 ? 71.006  80.509  50.509 1.00 117.03 ? 137 LEU B C   1 
ATOM   1090 O O   . LEU B 2 137 ? 72.193  80.414  50.745 1.00 123.25 ? 137 LEU B O   1 
ATOM   1091 C CB  . LEU B 2 137 ? 70.152  81.132  48.205 1.00 157.65 ? 137 LEU B CB  1 
ATOM   1092 C CG  . LEU B 2 137 ? 71.338  81.908  47.662 1.00 164.65 ? 137 LEU B CG  1 
ATOM   1093 C CD1 . LEU B 2 137 ? 71.800  81.312  46.375 1.00 164.48 ? 137 LEU B CD1 1 
ATOM   1094 C CD2 . LEU B 2 137 ? 71.006  83.357  47.390 1.00 256.96 ? 137 LEU B CD2 1 
ATOM   1095 N N   . LEU B 2 138 ? 70.134  81.069  51.368 1.00 118.66 ? 138 LEU B N   1 
ATOM   1096 C CA  . LEU B 2 138 ? 70.578  81.684  52.606 1.00 146.66 ? 138 LEU B CA  1 
ATOM   1097 C C   . LEU B 2 138 ? 70.711  80.670  53.741 1.00 150.05 ? 138 LEU B C   1 
ATOM   1098 O O   . LEU B 2 138 ? 71.636  80.833  54.544 1.00 205.27 ? 138 LEU B O   1 
ATOM   1099 C CB  . LEU B 2 138 ? 69.581  82.749  53.069 1.00 207.05 ? 138 LEU B CB  1 
ATOM   1100 C CG  . LEU B 2 138 ? 69.545  84.073  52.323 1.00 203.55 ? 138 LEU B CG  1 
ATOM   1101 C CD1 . LEU B 2 138 ? 68.759  85.076  53.173 1.00 259.83 ? 138 LEU B CD1 1 
ATOM   1102 C CD2 . LEU B 2 138 ? 70.933  84.599  51.976 1.00 154.12 ? 138 LEU B CD2 1 
ATOM   1103 N N   . ILE B 2 139 ? 69.808  79.678  53.859 1.00 103.34 ? 139 ILE B N   1 
ATOM   1104 C CA  . ILE B 2 139 ? 69.759  78.918  55.105 1.00 110.30 ? 139 ILE B CA  1 
ATOM   1105 C C   . ILE B 2 139 ? 69.751  77.399  54.884 1.00 138.61 ? 139 ILE B C   1 
ATOM   1106 O O   . ILE B 2 139 ? 70.590  76.749  55.493 1.00 202.55 ? 139 ILE B O   1 
ATOM   1107 C CB  . ILE B 2 139 ? 68.684  79.429  56.089 1.00 118.96 ? 139 ILE B CB  1 
ATOM   1108 C CG1 . ILE B 2 139 ? 68.810  78.730  57.444 1.00 227.19 ? 139 ILE B CG1 1 
ATOM   1109 C CG2 . ILE B 2 139 ? 67.290  79.209  55.580 1.00 128.36 ? 139 ILE B CG2 1 
ATOM   1110 C CD1 . ILE B 2 139 ? 67.991  79.376  58.549 1.00 241.94 ? 139 ILE B CD1 1 
ATOM   1111 N N   . ILE B 2 140 ? 68.902  76.806  54.052 1.00 90.56  ? 140 ILE B N   1 
ATOM   1112 C CA  . ILE B 2 140 ? 68.774  75.357  54.085 1.00 98.19  ? 140 ILE B CA  1 
ATOM   1113 C C   . ILE B 2 140 ? 70.073  74.626  53.656 1.00 80.19  ? 140 ILE B C   1 
ATOM   1114 O O   . ILE B 2 140 ? 70.555  73.781  54.390 1.00 124.53 ? 140 ILE B O   1 
ATOM   1115 C CB  . ILE B 2 140 ? 67.596  74.859  53.233 1.00 117.18 ? 140 ILE B CB  1 
ATOM   1116 C CG1 . ILE B 2 140 ? 66.329  75.659  53.524 1.00 132.06 ? 140 ILE B CG1 1 
ATOM   1117 C CG2 . ILE B 2 140 ? 67.350  73.349  53.364 1.00 123.73 ? 140 ILE B CG2 1 
ATOM   1118 C CD1 . ILE B 2 140 ? 65.838  75.563  54.919 1.00 172.21 ? 140 ILE B CD1 1 
ATOM   1119 N N   . ARG B 2 141 ? 70.628  74.892  52.489 1.00 63.51  ? 141 ARG B N   1 
ATOM   1120 C CA  . ARG B 2 141 ? 71.732  74.094  51.990 1.00 80.93  ? 141 ARG B CA  1 
ATOM   1121 C C   . ARG B 2 141 ? 73.046  74.536  52.621 1.00 93.94  ? 141 ARG B C   1 
ATOM   1122 O O   . ARG B 2 141 ? 73.881  73.674  52.862 1.00 157.64 ? 141 ARG B O   1 
ATOM   1123 C CB  . ARG B 2 141 ? 71.785  74.089  50.461 1.00 112.13 ? 141 ARG B CB  1 
ATOM   1124 C CG  . ARG B 2 141 ? 70.463  73.755  49.777 1.00 110.44 ? 141 ARG B CG  1 
ATOM   1125 C CD  . ARG B 2 141 ? 69.823  72.468  50.157 1.00 116.64 ? 141 ARG B CD  1 
ATOM   1126 N NE  . ARG B 2 141 ? 70.779  71.397  49.851 1.00 163.14 ? 141 ARG B NE  1 
ATOM   1127 C CZ  . ARG B 2 141 ? 70.842  70.662  48.732 1.00 177.98 ? 141 ARG B CZ  1 
ATOM   1128 N NH1 . ARG B 2 141 ? 71.751  69.718  48.620 1.00 198.30 ? 141 ARG B NH1 1 
ATOM   1129 N NH2 . ARG B 2 141 ? 70.030  70.883  47.725 1.00 155.51 ? 141 ARG B NH2 1 
ATOM   1130 N N   . PRO B 2 142 ? 73.312  75.818  52.929 1.00 87.28  ? 142 PRO B N   1 
ATOM   1131 C CA  . PRO B 2 142 ? 74.430  76.158  53.803 1.00 108.14 ? 142 PRO B CA  1 
ATOM   1132 C C   . PRO B 2 142 ? 74.364  75.519  55.189 1.00 127.62 ? 142 PRO B C   1 
ATOM   1133 O O   . PRO B 2 142 ? 75.300  74.792  55.555 1.00 91.63  ? 142 PRO B O   1 
ATOM   1134 C CB  . PRO B 2 142 ? 74.361  77.679  53.924 1.00 140.84 ? 142 PRO B CB  1 
ATOM   1135 C CG  . PRO B 2 142 ? 73.702  78.075  52.612 1.00 189.74 ? 142 PRO B CG  1 
ATOM   1136 C CD  . PRO B 2 142 ? 72.644  77.002  52.426 1.00 109.15 ? 142 PRO B CD  1 
ATOM   1137 N N   . SER B 2 143 ? 73.288  75.756  55.963 1.00 104.69 ? 143 SER B N   1 
ATOM   1138 C CA  . SER B 2 143 ? 73.256  75.265  57.309 1.00 96.16  ? 143 SER B CA  1 
ATOM   1139 C C   . SER B 2 143 ? 73.331  73.727  57.383 1.00 87.77  ? 143 SER B C   1 
ATOM   1140 O O   . SER B 2 143 ? 74.097  73.223  58.208 1.00 131.44 ? 143 SER B O   1 
ATOM   1141 C CB  . SER B 2 143 ? 72.067  75.818  58.011 1.00 107.65 ? 143 SER B CB  1 
ATOM   1142 O OG  . SER B 2 143 ? 70.870  75.178  57.593 1.00 105.21 ? 143 SER B OG  1 
ATOM   1143 N N   . SER B 2 144 ? 72.544  72.968  56.613 1.00 76.12  ? 144 SER B N   1 
ATOM   1144 C CA  . SER B 2 144 ? 72.657  71.503  56.632 1.00 98.71  ? 144 SER B CA  1 
ATOM   1145 C C   . SER B 2 144 ? 74.050  70.968  56.257 1.00 82.42  ? 144 SER B C   1 
ATOM   1146 O O   . SER B 2 144 ? 74.511  69.995  56.866 1.00 110.19 ? 144 SER B O   1 
ATOM   1147 C CB  . SER B 2 144 ? 71.635  70.855  55.770 1.00 134.01 ? 144 SER B CB  1 
ATOM   1148 O OG  . SER B 2 144 ? 71.783  71.218  54.421 1.00 136.31 ? 144 SER B OG  1 
ATOM   1149 N N   . GLN B 2 145 ? 74.750  71.593  55.308 1.00 75.49  ? 145 GLN B N   1 
ATOM   1150 C CA  . GLN B 2 145 ? 76.134  71.243  55.014 1.00 88.14  ? 145 GLN B CA  1 
ATOM   1151 C C   . GLN B 2 145 ? 77.036  71.527  56.201 1.00 79.10  ? 145 GLN B C   1 
ATOM   1152 O O   . GLN B 2 145 ? 77.868  70.674  56.520 1.00 69.78  ? 145 GLN B O   1 
ATOM   1153 C CB  . GLN B 2 145 ? 76.652  71.958  53.771 1.00 120.02 ? 145 GLN B CB  1 
ATOM   1154 C CG  . GLN B 2 145 ? 76.044  71.326  52.544 1.00 166.25 ? 145 GLN B CG  1 
ATOM   1155 C CD  . GLN B 2 145 ? 76.127  72.071  51.244 1.00 159.96 ? 145 GLN B CD  1 
ATOM   1156 O OE1 . GLN B 2 145 ? 75.607  71.601  50.237 1.00 207.90 ? 145 GLN B OE1 1 
ATOM   1157 N NE2 . GLN B 2 145 ? 76.771  73.218  51.236 1.00 152.27 ? 145 GLN B NE2 1 
ATOM   1158 N N   . TYR B 2 146 ? 76.873  72.671  56.876 1.00 69.70  ? 146 TYR B N   1 
ATOM   1159 C CA  . TYR B 2 146 ? 77.754  72.946  58.018 1.00 86.06  ? 146 TYR B CA  1 
ATOM   1160 C C   . TYR B 2 146 ? 77.441  72.090  59.223 1.00 68.91  ? 146 TYR B C   1 
ATOM   1161 O O   . TYR B 2 146 ? 78.343  71.729  59.970 1.00 87.27  ? 146 TYR B O   1 
ATOM   1162 C CB  . TYR B 2 146 ? 77.702  74.410  58.426 1.00 109.08 ? 146 TYR B CB  1 
ATOM   1163 C CG  . TYR B 2 146 ? 78.886  74.735  59.309 1.00 92.53  ? 146 TYR B CG  1 
ATOM   1164 C CD1 . TYR B 2 146 ? 80.188  74.609  58.816 1.00 144.06 ? 146 TYR B CD1 1 
ATOM   1165 C CD2 . TYR B 2 146 ? 78.687  75.141  60.609 1.00 91.07  ? 146 TYR B CD2 1 
ATOM   1166 C CE1 . TYR B 2 146 ? 81.270  74.893  59.613 1.00 185.64 ? 146 TYR B CE1 1 
ATOM   1167 C CE2 . TYR B 2 146 ? 79.765  75.434  61.421 1.00 129.06 ? 146 TYR B CE2 1 
ATOM   1168 C CZ  . TYR B 2 146 ? 81.051  75.300  60.918 1.00 198.11 ? 146 TYR B CZ  1 
ATOM   1169 O OH  . TYR B 2 146 ? 82.123  75.570  61.698 1.00 220.50 ? 146 TYR B OH  1 
ATOM   1170 N N   . ILE B 2 147 ? 76.171  71.726  59.379 1.00 81.15  ? 147 ILE B N   1 
ATOM   1171 C CA  . ILE B 2 147 ? 75.756  70.747  60.372 1.00 103.11 ? 147 ILE B CA  1 
ATOM   1172 C C   . ILE B 2 147 ? 76.412  69.384  60.133 1.00 69.90  ? 147 ILE B C   1 
ATOM   1173 O O   . ILE B 2 147 ? 77.030  68.890  61.099 1.00 124.18 ? 147 ILE B O   1 
ATOM   1174 C CB  . ILE B 2 147 ? 74.220  70.758  60.455 1.00 109.68 ? 147 ILE B CB  1 
ATOM   1175 C CG1 . ILE B 2 147 ? 73.861  72.032  61.265 1.00 93.31  ? 147 ILE B CG1 1 
ATOM   1176 C CG2 . ILE B 2 147 ? 73.636  69.404  60.913 1.00 90.10  ? 147 ILE B CG2 1 
ATOM   1177 C CD1 . ILE B 2 147 ? 72.369  72.419  61.214 1.00 123.68 ? 147 ILE B CD1 1 
ATOM   1178 N N   . VAL B 2 148 ? 76.347  68.801  58.948 1.00 43.96  ? 148 VAL B N   1 
ATOM   1179 C CA  . VAL B 2 148 ? 77.001  67.496  58.795 1.00 75.50  ? 148 VAL B CA  1 
ATOM   1180 C C   . VAL B 2 148 ? 78.522  67.640  58.763 1.00 66.04  ? 148 VAL B C   1 
ATOM   1181 O O   . VAL B 2 148 ? 79.222  66.669  59.081 1.00 94.81  ? 148 VAL B O   1 
ATOM   1182 C CB  . VAL B 2 148 ? 76.491  66.583  57.662 1.00 78.31  ? 148 VAL B CB  1 
ATOM   1183 C CG1 . VAL B 2 148 ? 75.006  66.420  57.818 1.00 143.27 ? 148 VAL B CG1 1 
ATOM   1184 C CG2 . VAL B 2 148 ? 76.765  67.149  56.330 1.00 96.88  ? 148 VAL B CG2 1 
ATOM   1185 N N   . ALA B 2 149 ? 79.064  68.809  58.452 1.00 53.46  ? 149 ALA B N   1 
ATOM   1186 C CA  . ALA B 2 149 ? 80.507  68.996  58.554 1.00 68.90  ? 149 ALA B CA  1 
ATOM   1187 C C   . ALA B 2 149 ? 80.970  69.059  59.995 1.00 81.20  ? 149 ALA B C   1 
ATOM   1188 O O   . ALA B 2 149 ? 82.046  68.530  60.293 1.00 123.59 ? 149 ALA B O   1 
ATOM   1189 C CB  . ALA B 2 149 ? 80.912  70.227  57.780 1.00 84.07  ? 149 ALA B CB  1 
ATOM   1190 N N   . LEU B 2 150 ? 80.216  69.703  60.901 1.00 98.35  ? 150 LEU B N   1 
ATOM   1191 C CA  . LEU B 2 150 ? 80.611  69.752  62.312 1.00 84.41  ? 150 LEU B CA  1 
ATOM   1192 C C   . LEU B 2 150 ? 80.558  68.381  62.917 1.00 68.28  ? 150 LEU B C   1 
ATOM   1193 O O   . LEU B 2 150 ? 81.410  68.087  63.769 1.00 120.63 ? 150 LEU B O   1 
ATOM   1194 C CB  . LEU B 2 150 ? 79.718  70.683  63.132 1.00 98.73  ? 150 LEU B CB  1 
ATOM   1195 C CG  . LEU B 2 150 ? 80.359  72.040  63.369 1.00 131.06 ? 150 LEU B CG  1 
ATOM   1196 C CD1 . LEU B 2 150 ? 79.330  73.041  63.849 1.00 196.88 ? 150 LEU B CD1 1 
ATOM   1197 C CD2 . LEU B 2 150 ? 81.464  71.931  64.380 1.00 138.95 ? 150 LEU B CD2 1 
ATOM   1198 N N   . VAL B 2 151 ? 79.560  67.582  62.531 1.00 55.52  ? 151 VAL B N   1 
ATOM   1199 C CA  . VAL B 2 151 ? 79.511  66.205  63.005 1.00 89.09  ? 151 VAL B CA  1 
ATOM   1200 C C   . VAL B 2 151 ? 80.691  65.377  62.460 1.00 90.01  ? 151 VAL B C   1 
ATOM   1201 O O   . VAL B 2 151 ? 81.249  64.554  63.192 1.00 82.42  ? 151 VAL B O   1 
ATOM   1202 C CB  . VAL B 2 151 ? 78.140  65.571  62.743 1.00 84.67  ? 151 VAL B CB  1 
ATOM   1203 C CG1 . VAL B 2 151 ? 78.068  64.106  63.175 1.00 110.75 ? 151 VAL B CG1 1 
ATOM   1204 C CG2 . VAL B 2 151 ? 77.094  66.351  63.477 1.00 85.50  ? 151 VAL B CG2 1 
ATOM   1205 N N   . PHE B 2 152 ? 81.104  65.579  61.210 1.00 91.87  ? 152 PHE B N   1 
ATOM   1206 C CA  . PHE B 2 152 ? 82.291  64.911  60.717 1.00 91.57  ? 152 PHE B CA  1 
ATOM   1207 C C   . PHE B 2 152 ? 83.475  65.254  61.603 1.00 85.25  ? 152 PHE B C   1 
ATOM   1208 O O   . PHE B 2 152 ? 84.159  64.355  62.081 1.00 122.54 ? 152 PHE B O   1 
ATOM   1209 C CB  . PHE B 2 152 ? 82.597  65.339  59.287 1.00 103.73 ? 152 PHE B CB  1 
ATOM   1210 C CG  . PHE B 2 152 ? 84.018  65.105  58.845 1.00 89.15  ? 152 PHE B CG  1 
ATOM   1211 C CD1 . PHE B 2 152 ? 84.470  63.848  58.521 1.00 84.63  ? 152 PHE B CD1 1 
ATOM   1212 C CD2 . PHE B 2 152 ? 84.898  66.166  58.762 1.00 97.44  ? 152 PHE B CD2 1 
ATOM   1213 C CE1 . PHE B 2 152 ? 85.769  63.634  58.102 1.00 125.93 ? 152 PHE B CE1 1 
ATOM   1214 C CE2 . PHE B 2 152 ? 86.197  65.965  58.345 1.00 108.75 ? 152 PHE B CE2 1 
ATOM   1215 C CZ  . PHE B 2 152 ? 86.634  64.699  58.020 1.00 114.34 ? 152 PHE B CZ  1 
ATOM   1216 N N   . ALA B 2 153 ? 83.726  66.544  61.833 1.00 71.26  ? 153 ALA B N   1 
ATOM   1217 C CA  . ALA B 2 153 ? 84.869  66.939  62.630 1.00 129.79 ? 153 ALA B CA  1 
ATOM   1218 C C   . ALA B 2 153 ? 84.802  66.372  64.062 1.00 123.94 ? 153 ALA B C   1 
ATOM   1219 O O   . ALA B 2 153 ? 85.763  65.812  64.598 1.00 103.11 ? 153 ALA B O   1 
ATOM   1220 C CB  . ALA B 2 153 ? 84.947  68.436  62.629 1.00 159.22 ? 153 ALA B CB  1 
ATOM   1221 N N   . THR B 2 154 ? 83.664  66.516  64.715 1.00 78.21  ? 154 THR B N   1 
ATOM   1222 C CA  . THR B 2 154 ? 83.505  66.042  66.062 1.00 69.29  ? 154 THR B CA  1 
ATOM   1223 C C   . THR B 2 154 ? 83.749  64.536  66.158 1.00 75.17  ? 154 THR B C   1 
ATOM   1224 O O   . THR B 2 154 ? 84.546  64.117  67.004 1.00 144.40 ? 154 THR B O   1 
ATOM   1225 C CB  . THR B 2 154 ? 82.105  66.427  66.573 1.00 93.83  ? 154 THR B CB  1 
ATOM   1226 O OG1 . THR B 2 154 ? 82.101  67.861  66.637 1.00 80.50  ? 154 THR B OG1 1 
ATOM   1227 C CG2 . THR B 2 154 ? 81.700  65.851  67.915 1.00 138.63 ? 154 THR B CG2 1 
ATOM   1228 N N   . TYR B 2 155 ? 83.077  63.704  65.374 1.00 78.13  ? 155 TYR B N   1 
ATOM   1229 C CA  . TYR B 2 155 ? 83.197  62.270  65.569 1.00 103.23 ? 155 TYR B CA  1 
ATOM   1230 C C   . TYR B 2 155 ? 84.557  61.758  65.060 1.00 90.17  ? 155 TYR B C   1 
ATOM   1231 O O   . TYR B 2 155 ? 85.036  60.744  65.547 1.00 83.86  ? 155 TYR B O   1 
ATOM   1232 C CB  . TYR B 2 155 ? 82.032  61.519  64.902 1.00 114.67 ? 155 TYR B CB  1 
ATOM   1233 C CG  . TYR B 2 155 ? 80.786  61.565  65.741 1.00 99.41  ? 155 TYR B CG  1 
ATOM   1234 C CD1 . TYR B 2 155 ? 80.098  62.753  65.901 1.00 109.83 ? 155 TYR B CD1 1 
ATOM   1235 C CD2 . TYR B 2 155 ? 80.313  60.433  66.368 1.00 114.91 ? 155 TYR B CD2 1 
ATOM   1236 C CE1 . TYR B 2 155 ? 78.932  62.812  66.650 1.00 147.41 ? 155 TYR B CE1 1 
ATOM   1237 C CE2 . TYR B 2 155 ? 79.149  60.488  67.129 1.00 163.74 ? 155 TYR B CE2 1 
ATOM   1238 C CZ  . TYR B 2 155 ? 78.448  61.674  67.265 1.00 138.31 ? 155 TYR B CZ  1 
ATOM   1239 O OH  . TYR B 2 155 ? 77.314  61.720  68.039 1.00 154.31 ? 155 TYR B OH  1 
ATOM   1240 N N   . LEU B 2 156 ? 85.187  62.410  64.080 1.00 98.63  ? 156 LEU B N   1 
ATOM   1241 C CA  . LEU B 2 156 ? 86.492  61.998  63.601 1.00 110.19 ? 156 LEU B CA  1 
ATOM   1242 C C   . LEU B 2 156 ? 87.546  62.285  64.651 1.00 118.95 ? 156 LEU B C   1 
ATOM   1243 O O   . LEU B 2 156 ? 88.458  61.479  64.809 1.00 174.37 ? 156 LEU B O   1 
ATOM   1244 C CB  . LEU B 2 156 ? 86.828  62.766  62.319 1.00 115.84 ? 156 LEU B CB  1 
ATOM   1245 C CG  . LEU B 2 156 ? 88.185  62.465  61.758 1.00 134.37 ? 156 LEU B CG  1 
ATOM   1246 C CD1 . LEU B 2 156 ? 88.185  60.987  61.345 1.00 162.43 ? 156 LEU B CD1 1 
ATOM   1247 C CD2 . LEU B 2 156 ? 88.482  63.442  60.660 1.00 140.95 ? 156 LEU B CD2 1 
ATOM   1248 N N   . LEU B 2 157 ? 87.445  63.413  65.359 1.00 107.13 ? 157 LEU B N   1 
ATOM   1249 C CA  . LEU B 2 157 ? 88.418  63.742  66.391 1.00 116.07 ? 157 LEU B CA  1 
ATOM   1250 C C   . LEU B 2 157 ? 88.151  63.044  67.725 1.00 121.71 ? 157 LEU B C   1 
ATOM   1251 O O   . LEU B 2 157 ? 89.075  62.970  68.530 1.00 176.94 ? 157 LEU B O   1 
ATOM   1252 C CB  . LEU B 2 157 ? 88.388  65.249  66.579 1.00 110.39 ? 157 LEU B CB  1 
ATOM   1253 C CG  . LEU B 2 157 ? 89.003  66.036  65.441 1.00 107.02 ? 157 LEU B CG  1 
ATOM   1254 C CD1 . LEU B 2 157 ? 88.711  67.538  65.648 1.00 107.90 ? 157 LEU B CD1 1 
ATOM   1255 C CD2 . LEU B 2 157 ? 90.485  65.739  65.374 1.00 78.82  ? 157 LEU B CD2 1 
ATOM   1256 N N   . LYS B 2 158 ? 86.949  62.517  67.973 1.00 110.07 ? 158 LYS B N   1 
ATOM   1257 C CA  . LYS B 2 158 ? 86.536  61.964  69.260 1.00 114.72 ? 158 LYS B CA  1 
ATOM   1258 C C   . LYS B 2 158 ? 87.509  60.945  69.859 1.00 109.75 ? 158 LYS B C   1 
ATOM   1259 O O   . LYS B 2 158 ? 87.735  61.006  71.053 1.00 144.79 ? 158 LYS B O   1 
ATOM   1260 C CB  . LYS B 2 158 ? 85.150  61.329  69.145 1.00 140.79 ? 158 LYS B CB  1 
ATOM   1261 C CG  . LYS B 2 158 ? 84.418  61.192  70.482 1.00 122.89 ? 158 LYS B CG  1 
ATOM   1262 C CD  . LYS B 2 158 ? 83.791  62.484  70.877 1.00 138.98 ? 158 LYS B CD  1 
ATOM   1263 C CE  . LYS B 2 158 ? 82.677  62.369  71.897 1.00 192.55 ? 158 LYS B CE  1 
ATOM   1264 N NZ  . LYS B 2 158 ? 81.830  63.593  71.903 1.00 219.66 ? 158 LYS B NZ  1 
ATOM   1265 N N   . PRO B 2 159 ? 88.151  59.996  69.143 1.00 88.26  ? 159 PRO B N   1 
ATOM   1266 C CA  . PRO B 2 159 ? 89.145  59.113  69.753 1.00 122.64 ? 159 PRO B CA  1 
ATOM   1267 C C   . PRO B 2 159 ? 90.449  59.768  70.246 1.00 113.63 ? 159 PRO B C   1 
ATOM   1268 O O   . PRO B 2 159 ? 91.224  59.095  70.931 1.00 169.54 ? 159 PRO B O   1 
ATOM   1269 C CB  . PRO B 2 159 ? 89.434  58.052  68.669 1.00 153.23 ? 159 PRO B CB  1 
ATOM   1270 C CG  . PRO B 2 159 ? 89.136  58.792  67.411 1.00 152.71 ? 159 PRO B CG  1 
ATOM   1271 C CD  . PRO B 2 159 ? 87.956  59.676  67.755 1.00 89.82  ? 159 PRO B CD  1 
ATOM   1272 N N   . LEU B 2 160 ? 90.687  61.053  69.973 1.00 102.79 ? 160 LEU B N   1 
ATOM   1273 C CA  . LEU B 2 160 ? 91.746  61.808  70.658 1.00 131.48 ? 160 LEU B CA  1 
ATOM   1274 C C   . LEU B 2 160 ? 91.286  62.459  71.975 1.00 137.66 ? 160 LEU B C   1 
ATOM   1275 O O   . LEU B 2 160 ? 92.136  62.907  72.753 1.00 133.16 ? 160 LEU B O   1 
ATOM   1276 C CB  . LEU B 2 160 ? 92.268  62.925  69.756 1.00 104.54 ? 160 LEU B CB  1 
ATOM   1277 C CG  . LEU B 2 160 ? 92.670  62.561  68.347 1.00 157.93 ? 160 LEU B CG  1 
ATOM   1278 C CD1 . LEU B 2 160 ? 93.206  63.834  67.716 1.00 146.53 ? 160 LEU B CD1 1 
ATOM   1279 C CD2 . LEU B 2 160 ? 93.706  61.433  68.296 1.00 219.76 ? 160 LEU B CD2 1 
ATOM   1280 N N   . PHE B 2 161 ? 89.960  62.518  72.219 1.00 94.75  ? 161 PHE B N   1 
ATOM   1281 C CA  . PHE B 2 161 ? 89.376  63.168  73.376 1.00 106.15 ? 161 PHE B CA  1 
ATOM   1282 C C   . PHE B 2 161 ? 88.165  62.381  73.890 1.00 115.04 ? 161 PHE B C   1 
ATOM   1283 O O   . PHE B 2 161 ? 87.043  62.896  73.984 1.00 156.62 ? 161 PHE B O   1 
ATOM   1284 C CB  . PHE B 2 161 ? 88.958  64.595  72.988 1.00 136.77 ? 161 PHE B CB  1 
ATOM   1285 C CG  . PHE B 2 161 ? 90.074  65.504  72.566 1.00 105.10 ? 161 PHE B CG  1 
ATOM   1286 C CD1 . PHE B 2 161 ? 90.785  66.234  73.467 1.00 141.09 ? 161 PHE B CD1 1 
ATOM   1287 C CD2 . PHE B 2 161 ? 90.402  65.618  71.250 1.00 123.36 ? 161 PHE B CD2 1 
ATOM   1288 C CE1 . PHE B 2 161 ? 91.812  67.057  73.045 1.00 205.24 ? 161 PHE B CE1 1 
ATOM   1289 C CE2 . PHE B 2 161 ? 91.427  66.431  70.818 1.00 135.95 ? 161 PHE B CE2 1 
ATOM   1290 C CZ  . PHE B 2 161 ? 92.127  67.154  71.717 1.00 160.90 ? 161 PHE B CZ  1 
ATOM   1291 N N   . PRO B 2 162 ? 88.311  61.101  74.279 1.00 114.33 ? 162 PRO B N   1 
ATOM   1292 C CA  . PRO B 2 162 ? 87.157  60.384  74.819 1.00 135.26 ? 162 PRO B CA  1 
ATOM   1293 C C   . PRO B 2 162 ? 86.876  60.932  76.220 1.00 133.82 ? 162 PRO B C   1 
ATOM   1294 O O   . PRO B 2 162 ? 87.806  61.126  77.006 1.00 134.72 ? 162 PRO B O   1 
ATOM   1295 C CB  . PRO B 2 162 ? 87.643  58.920  74.841 1.00 197.34 ? 162 PRO B CB  1 
ATOM   1296 C CG  . PRO B 2 162 ? 89.179  59.032  74.957 1.00 188.82 ? 162 PRO B CG  1 
ATOM   1297 C CD  . PRO B 2 162 ? 89.565  60.315  74.245 1.00 117.76 ? 162 PRO B CD  1 
ATOM   1298 N N   . THR B 2 163 ? 85.598  61.155  76.542 1.00 154.48 ? 163 THR B N   1 
ATOM   1299 C CA  . THR B 2 163 ? 85.109  61.496  77.888 1.00 215.17 ? 163 THR B CA  1 
ATOM   1300 C C   . THR B 2 163 ? 85.525  62.918  78.314 1.00 158.58 ? 163 THR B C   1 
ATOM   1301 O O   . THR B 2 163 ? 85.617  63.255  79.505 1.00 214.33 ? 163 THR B O   1 
ATOM   1302 C CB  . THR B 2 163 ? 85.415  60.409  78.952 1.00 275.54 ? 163 THR B CB  1 
ATOM   1303 O OG1 . THR B 2 163 ? 86.809  60.310  79.271 1.00 215.08 ? 163 THR B OG1 1 
ATOM   1304 C CG2 . THR B 2 163 ? 84.893  59.043  78.548 1.00 333.89 ? 163 THR B CG2 1 
ATOM   1305 N N   . CYS B 2 164 ? 85.753  63.792  77.317 1.00 127.73 ? 164 CYS B N   1 
ATOM   1306 C CA  . CYS B 2 164 ? 85.702  65.241  77.494 1.00 155.74 ? 164 CYS B CA  1 
ATOM   1307 C C   . CYS B 2 164 ? 85.271  65.933  76.196 1.00 149.12 ? 164 CYS B C   1 
ATOM   1308 O O   . CYS B 2 164 ? 85.314  65.334  75.127 1.00 191.40 ? 164 CYS B O   1 
ATOM   1309 C CB  . CYS B 2 164 ? 87.035  65.780  77.999 1.00 156.27 ? 164 CYS B CB  1 
ATOM   1310 S SG  . CYS B 2 164 ? 88.491  65.221  77.084 1.00 173.85 ? 164 CYS B SG  1 
ATOM   1311 N N   . PRO B 2 165 ? 84.836  67.213  76.216 1.00 157.62 ? 165 PRO B N   1 
ATOM   1312 C CA  . PRO B 2 165 ? 84.559  67.934  74.985 1.00 166.84 ? 165 PRO B CA  1 
ATOM   1313 C C   . PRO B 2 165 ? 85.782  68.017  74.070 1.00 173.09 ? 165 PRO B C   1 
ATOM   1314 O O   . PRO B 2 165 ? 86.908  68.265  74.508 1.00 152.71 ? 165 PRO B O   1 
ATOM   1315 C CB  . PRO B 2 165 ? 84.161  69.344  75.464 1.00 242.44 ? 165 PRO B CB  1 
ATOM   1316 C CG  . PRO B 2 165 ? 83.641  69.117  76.860 1.00 287.97 ? 165 PRO B CG  1 
ATOM   1317 C CD  . PRO B 2 165 ? 84.564  68.042  77.401 1.00 263.47 ? 165 PRO B CD  1 
ATOM   1318 N N   . VAL B 2 166 ? 85.528  67.824  72.768 1.00 175.90 ? 166 VAL B N   1 
ATOM   1319 C CA  . VAL B 2 166 ? 86.516  68.006  71.713 1.00 142.64 ? 166 VAL B CA  1 
ATOM   1320 C C   . VAL B 2 166 ? 86.769  69.513  71.509 1.00 144.54 ? 166 VAL B C   1 
ATOM   1321 O O   . VAL B 2 166 ? 85.836  70.323  71.560 1.00 118.36 ? 166 VAL B O   1 
ATOM   1322 C CB  . VAL B 2 166 ? 85.999  67.289  70.458 1.00 129.88 ? 166 VAL B CB  1 
ATOM   1323 C CG1 . VAL B 2 166 ? 84.693  67.921  69.937 1.00 128.79 ? 166 VAL B CG1 1 
ATOM   1324 C CG2 . VAL B 2 166 ? 87.081  67.193  69.394 1.00 107.93 ? 166 VAL B CG2 1 
ATOM   1325 N N   . PRO B 2 167 ? 88.030  69.976  71.302 1.00 136.10 ? 167 PRO B N   1 
ATOM   1326 C CA  . PRO B 2 167 ? 88.301  71.436  71.304 1.00 137.19 ? 167 PRO B CA  1 
ATOM   1327 C C   . PRO B 2 167 ? 87.539  72.185  70.213 1.00 131.33 ? 167 PRO B C   1 
ATOM   1328 O O   . PRO B 2 167 ? 87.693  71.888  69.016 1.00 175.58 ? 167 PRO B O   1 
ATOM   1329 C CB  . PRO B 2 167 ? 89.822  71.533  71.099 1.00 163.98 ? 167 PRO B CB  1 
ATOM   1330 C CG  . PRO B 2 167 ? 90.342  70.116  71.460 1.00 150.61 ? 167 PRO B CG  1 
ATOM   1331 C CD  . PRO B 2 167 ? 89.233  69.135  71.125 1.00 80.01  ? 167 PRO B CD  1 
ATOM   1332 N N   . GLU B 2 168 ? 86.693  73.146  70.620 1.00 178.12 ? 168 GLU B N   1 
ATOM   1333 C CA  . GLU B 2 168 ? 85.698  73.752  69.724 1.00 193.92 ? 168 GLU B CA  1 
ATOM   1334 C C   . GLU B 2 168 ? 86.319  74.352  68.449 1.00 160.40 ? 168 GLU B C   1 
ATOM   1335 O O   . GLU B 2 168 ? 85.751  74.190  67.364 1.00 123.13 ? 168 GLU B O   1 
ATOM   1336 C CB  . GLU B 2 168 ? 84.887  74.848  70.425 1.00 189.96 ? 168 GLU B CB  1 
ATOM   1337 C CG  . GLU B 2 168 ? 83.969  74.332  71.499 1.00 279.01 ? 168 GLU B CG  1 
ATOM   1338 C CD  . GLU B 2 168 ? 83.161  75.429  72.174 1.00 398.19 ? 168 GLU B CD  1 
ATOM   1339 O OE1 . GLU B 2 168 ? 82.365  76.095  71.473 1.00 472.02 ? 168 GLU B OE1 1 
ATOM   1340 O OE2 . GLU B 2 168 ? 83.323  75.623  73.397 1.00 451.97 ? 168 GLU B OE2 1 
ATOM   1341 N N   . GLU B 2 169 ? 87.467  75.042  68.565 1.00 132.04 ? 169 GLU B N   1 
ATOM   1342 C CA  . GLU B 2 169 ? 88.100  75.667  67.420 1.00 143.74 ? 169 GLU B CA  1 
ATOM   1343 C C   . GLU B 2 169 ? 88.661  74.622  66.447 1.00 100.58 ? 169 GLU B C   1 
ATOM   1344 O O   . GLU B 2 169 ? 88.656  74.855  65.231 1.00 154.80 ? 169 GLU B O   1 
ATOM   1345 C CB  . GLU B 2 169 ? 89.145  76.671  67.917 1.00 228.01 ? 169 GLU B CB  1 
ATOM   1346 C CG  . GLU B 2 169 ? 88.516  77.895  68.576 1.00 265.25 ? 169 GLU B CG  1 
ATOM   1347 C CD  . GLU B 2 169 ? 87.499  78.650  67.723 1.00 294.93 ? 169 GLU B CD  1 
ATOM   1348 O OE1 . GLU B 2 169 ? 87.870  79.110  66.619 1.00 313.95 ? 169 GLU B OE1 1 
ATOM   1349 O OE2 . GLU B 2 169 ? 86.322  78.762  68.147 1.00 243.60 ? 169 GLU B OE2 1 
ATOM   1350 N N   . ALA B 2 170 ? 89.156  73.490  66.935 1.00 96.09  ? 170 ALA B N   1 
ATOM   1351 C CA  . ALA B 2 170 ? 89.578  72.402  66.060 1.00 124.93 ? 170 ALA B CA  1 
ATOM   1352 C C   . ALA B 2 170 ? 88.368  71.739  65.385 1.00 109.51 ? 170 ALA B C   1 
ATOM   1353 O O   . ALA B 2 170 ? 88.416  71.345  64.223 1.00 100.34 ? 170 ALA B O   1 
ATOM   1354 C CB  . ALA B 2 170 ? 90.414  71.395  66.818 1.00 125.43 ? 170 ALA B CB  1 
ATOM   1355 N N   . ALA B 2 171 ? 87.259  71.628  66.094 1.00 100.28 ? 171 ALA B N   1 
ATOM   1356 C CA  . ALA B 2 171 ? 86.049  71.128  65.481 1.00 125.15 ? 171 ALA B CA  1 
ATOM   1357 C C   . ALA B 2 171 ? 85.517  72.101  64.413 1.00 114.46 ? 171 ALA B C   1 
ATOM   1358 O O   . ALA B 2 171 ? 84.926  71.639  63.441 1.00 145.54 ? 171 ALA B O   1 
ATOM   1359 C CB  . ALA B 2 171 ? 85.026  70.861  66.574 1.00 207.74 ? 171 ALA B CB  1 
ATOM   1360 N N   . LYS B 2 172 ? 85.652  73.431  64.546 1.00 89.10  ? 172 LYS B N   1 
ATOM   1361 C CA  . LYS B 2 172 ? 85.327  74.335  63.457 1.00 99.99  ? 172 LYS B CA  1 
ATOM   1362 C C   . LYS B 2 172 ? 86.333  74.214  62.298 1.00 89.17  ? 172 LYS B C   1 
ATOM   1363 O O   . LYS B 2 172 ? 85.919  74.130  61.153 1.00 120.63 ? 172 LYS B O   1 
ATOM   1364 C CB  . LYS B 2 172 ? 85.288  75.782  63.918 1.00 119.13 ? 172 LYS B CB  1 
ATOM   1365 C CG  . LYS B 2 172 ? 84.068  76.206  64.739 1.00 123.16 ? 172 LYS B CG  1 
ATOM   1366 C CD  . LYS B 2 172 ? 84.270  77.758  64.988 1.00 246.39 ? 172 LYS B CD  1 
ATOM   1367 C CE  . LYS B 2 172 ? 83.285  78.381  65.960 1.00 294.20 ? 172 LYS B CE  1 
ATOM   1368 N NZ  . LYS B 2 172 ? 83.692  78.111  67.355 1.00 341.91 ? 172 LYS B NZ  1 
ATOM   1369 N N   . LEU B 2 173 ? 87.625  74.200  62.521 1.00 88.44  ? 173 LEU B N   1 
ATOM   1370 C CA  . LEU B 2 173 ? 88.553  74.098  61.410 1.00 97.02  ? 173 LEU B CA  1 
ATOM   1371 C C   . LEU B 2 173 ? 88.351  72.793  60.663 1.00 89.48  ? 173 LEU B C   1 
ATOM   1372 O O   . LEU B 2 173 ? 88.357  72.814  59.433 1.00 144.21 ? 173 LEU B O   1 
ATOM   1373 C CB  . LEU B 2 173 ? 90.037  74.091  61.847 1.00 115.46 ? 173 LEU B CB  1 
ATOM   1374 C CG  . LEU B 2 173 ? 90.618  75.381  62.337 1.00 124.60 ? 173 LEU B CG  1 
ATOM   1375 C CD1 . LEU B 2 173 ? 92.129  75.141  62.311 1.00 111.43 ? 173 LEU B CD1 1 
ATOM   1376 C CD2 . LEU B 2 173 ? 90.122  76.569  61.489 1.00 109.25 ? 173 LEU B CD2 1 
ATOM   1377 N N   . VAL B 2 174 ? 88.249  71.641  61.332 1.00 81.97  ? 174 VAL B N   1 
ATOM   1378 C CA  . VAL B 2 174 ? 88.116  70.398  60.586 1.00 92.32  ? 174 VAL B CA  1 
ATOM   1379 C C   . VAL B 2 174 ? 86.750  70.326  59.899 1.00 79.82  ? 174 VAL B C   1 
ATOM   1380 O O   . VAL B 2 174 ? 86.585  69.611  58.927 1.00 85.48  ? 174 VAL B O   1 
ATOM   1381 C CB  . VAL B 2 174 ? 88.473  69.200  61.468 1.00 94.69  ? 174 VAL B CB  1 
ATOM   1382 C CG1 . VAL B 2 174 ? 88.137  67.862  60.828 1.00 99.40  ? 174 VAL B CG1 1 
ATOM   1383 C CG2 . VAL B 2 174 ? 89.954  69.290  61.787 1.00 100.65 ? 174 VAL B CG2 1 
ATOM   1384 N N   . ALA B 2 175 ? 85.752  71.075  60.349 1.00 84.43  ? 175 ALA B N   1 
ATOM   1385 C CA  . ALA B 2 175 ? 84.502  71.193  59.605 1.00 94.35  ? 175 ALA B CA  1 
ATOM   1386 C C   . ALA B 2 175 ? 84.748  71.952  58.329 1.00 81.46  ? 175 ALA B C   1 
ATOM   1387 O O   . ALA B 2 175 ? 84.226  71.558  57.297 1.00 137.53 ? 175 ALA B O   1 
ATOM   1388 C CB  . ALA B 2 175 ? 83.423  71.842  60.472 1.00 122.62 ? 175 ALA B CB  1 
ATOM   1389 N N   . CYS B 2 176 ? 85.509  73.050  58.384 1.00 86.19  ? 176 CYS B N   1 
ATOM   1390 C CA  . CYS B 2 176 ? 85.873  73.841  57.203 1.00 118.66 ? 176 CYS B CA  1 
ATOM   1391 C C   . CYS B 2 176 ? 86.812  73.105  56.234 1.00 84.74  ? 176 CYS B C   1 
ATOM   1392 O O   . CYS B 2 176 ? 86.574  73.183  55.035 1.00 115.10 ? 176 CYS B O   1 
ATOM   1393 C CB  . CYS B 2 176 ? 86.415  75.185  57.648 1.00 112.27 ? 176 CYS B CB  1 
ATOM   1394 S SG  . CYS B 2 176 ? 85.084  76.010  58.571 1.00 140.20 ? 176 CYS B SG  1 
ATOM   1395 N N   . LEU B 2 177 ? 87.815  72.400  56.722 1.00 71.72  ? 177 LEU B N   1 
ATOM   1396 C CA  . LEU B 2 177 ? 88.691  71.599  55.879 1.00 100.01 ? 177 LEU B CA  1 
ATOM   1397 C C   . LEU B 2 177 ? 87.939  70.566  55.041 1.00 100.47 ? 177 LEU B C   1 
ATOM   1398 O O   . LEU B 2 177 ? 88.328  70.326  53.897 1.00 179.11 ? 177 LEU B O   1 
ATOM   1399 C CB  . LEU B 2 177 ? 89.726  70.863  56.741 1.00 106.12 ? 177 LEU B CB  1 
ATOM   1400 C CG  . LEU B 2 177 ? 90.847  71.742  57.255 1.00 126.94 ? 177 LEU B CG  1 
ATOM   1401 C CD1 . LEU B 2 177 ? 91.579  71.077  58.379 1.00 186.75 ? 177 LEU B CD1 1 
ATOM   1402 C CD2 . LEU B 2 177 ? 91.843  72.034  56.167 1.00 100.31 ? 177 LEU B CD2 1 
ATOM   1403 N N   . CYS B 2 178 ? 86.894  69.964  55.597 1.00 95.72  ? 178 CYS B N   1 
ATOM   1404 C CA  . CYS B 2 178 ? 86.043  69.021  54.908 1.00 118.20 ? 178 CYS B CA  1 
ATOM   1405 C C   . CYS B 2 178 ? 85.303  69.706  53.757 1.00 105.76 ? 178 CYS B C   1 
ATOM   1406 O O   . CYS B 2 178 ? 85.402  69.260  52.619 1.00 156.10 ? 178 CYS B O   1 
ATOM   1407 C CB  . CYS B 2 178 ? 85.061  68.449  55.923 1.00 156.61 ? 178 CYS B CB  1 
ATOM   1408 S SG  . CYS B 2 178 ? 83.825  67.374  55.192 1.00 147.14 ? 178 CYS B SG  1 
ATOM   1409 N N   . VAL B 2 179 ? 84.588  70.790  54.035 1.00 71.61  ? 179 VAL B N   1 
ATOM   1410 C CA  . VAL B 2 179 ? 83.865  71.506  53.006 1.00 82.95  ? 179 VAL B CA  1 
ATOM   1411 C C   . VAL B 2 179 ? 84.813  72.008  51.906 1.00 80.15  ? 179 VAL B C   1 
ATOM   1412 O O   . VAL B 2 179 ? 84.484  71.938  50.734 1.00 103.29 ? 179 VAL B O   1 
ATOM   1413 C CB  . VAL B 2 179 ? 83.068  72.684  53.614 1.00 101.48 ? 179 VAL B CB  1 
ATOM   1414 C CG1 . VAL B 2 179 ? 82.546  73.705  52.622 1.00 103.38 ? 179 VAL B CG1 1 
ATOM   1415 C CG2 . VAL B 2 179 ? 81.904  72.188  54.423 1.00 133.82 ? 179 VAL B CG2 1 
ATOM   1416 N N   . LEU B 2 180 ? 85.970  72.549  52.234 1.00 81.31  ? 180 LEU B N   1 
ATOM   1417 C CA  . LEU B 2 180 ? 86.885  73.027  51.224 1.00 91.92  ? 180 LEU B CA  1 
ATOM   1418 C C   . LEU B 2 180 ? 87.404  71.888  50.350 1.00 65.37  ? 180 LEU B C   1 
ATOM   1419 O O   . LEU B 2 180 ? 87.445  72.039  49.136 1.00 120.14 ? 180 LEU B O   1 
ATOM   1420 C CB  . LEU B 2 180 ? 88.064  73.759  51.901 1.00 110.98 ? 180 LEU B CB  1 
ATOM   1421 C CG  . LEU B 2 180 ? 87.735  75.131  52.470 1.00 107.04 ? 180 LEU B CG  1 
ATOM   1422 C CD1 . LEU B 2 180 ? 88.936  75.618  53.242 1.00 170.49 ? 180 LEU B CD1 1 
ATOM   1423 C CD2 . LEU B 2 180 ? 87.406  76.122  51.385 1.00 106.98 ? 180 LEU B CD2 1 
ATOM   1424 N N   . LEU B 2 181 ? 87.863  70.793  50.919 1.00 77.90  ? 181 LEU B N   1 
ATOM   1425 C CA  . LEU B 2 181 ? 88.437  69.718  50.126 1.00 78.41  ? 181 LEU B CA  1 
ATOM   1426 C C   . LEU B 2 181 ? 87.356  69.093  49.237 1.00 76.78  ? 181 LEU B C   1 
ATOM   1427 O O   . LEU B 2 181 ? 87.644  68.838  48.075 1.00 125.99 ? 181 LEU B O   1 
ATOM   1428 C CB  . LEU B 2 181 ? 89.022  68.649  51.047 1.00 94.92  ? 181 LEU B CB  1 
ATOM   1429 C CG  . LEU B 2 181 ? 89.453  67.362  50.376 1.00 84.53  ? 181 LEU B CG  1 
ATOM   1430 C CD1 . LEU B 2 181 ? 90.598  67.693  49.480 1.00 171.66 ? 181 LEU B CD1 1 
ATOM   1431 C CD2 . LEU B 2 181 ? 89.916  66.343  51.358 1.00 145.49 ? 181 LEU B CD2 1 
ATOM   1432 N N   . LEU B 2 182 ? 86.140  68.880  49.720 1.00 68.29  ? 182 LEU B N   1 
ATOM   1433 C CA  . LEU B 2 182 ? 85.086  68.363  48.870 1.00 109.99 ? 182 LEU B CA  1 
ATOM   1434 C C   . LEU B 2 182 ? 84.582  69.381  47.822 1.00 106.65 ? 182 LEU B C   1 
ATOM   1435 O O   . LEU B 2 182 ? 84.136  68.991  46.759 1.00 150.31 ? 182 LEU B O   1 
ATOM   1436 C CB  . LEU B 2 182 ? 83.951  67.829  49.751 1.00 107.92 ? 182 LEU B CB  1 
ATOM   1437 C CG  . LEU B 2 182 ? 84.352  66.530  50.443 1.00 120.10 ? 182 LEU B CG  1 
ATOM   1438 C CD1 . LEU B 2 182 ? 83.310  66.163  51.483 1.00 162.39 ? 182 LEU B CD1 1 
ATOM   1439 C CD2 . LEU B 2 182 ? 84.611  65.382  49.488 1.00 98.35  ? 182 LEU B CD2 1 
ATOM   1440 N N   . THR B 2 183 ? 84.665  70.670  48.052 1.00 89.65  ? 183 THR B N   1 
ATOM   1441 C CA  . THR B 2 183 ? 84.466  71.630  46.982 1.00 105.63 ? 183 THR B CA  1 
ATOM   1442 C C   . THR B 2 183 ? 85.556  71.501  45.922 1.00 93.30  ? 183 THR B C   1 
ATOM   1443 O O   . THR B 2 183 ? 85.256  71.542  44.745 1.00 135.66 ? 183 THR B O   1 
ATOM   1444 C CB  . THR B 2 183 ? 84.478  73.081  47.515 1.00 127.44 ? 183 THR B CB  1 
ATOM   1445 O OG1 . THR B 2 183 ? 83.433  73.159  48.472 1.00 150.58 ? 183 THR B OG1 1 
ATOM   1446 C CG2 . THR B 2 183 ? 84.241  74.158  46.477 1.00 108.67 ? 183 THR B CG2 1 
ATOM   1447 N N   . ALA B 2 184 ? 86.823  71.407  46.289 1.00 73.65  ? 184 ALA B N   1 
ATOM   1448 C CA  . ALA B 2 184 ? 87.875  71.237  45.323 1.00 95.54  ? 184 ALA B CA  1 
ATOM   1449 C C   . ALA B 2 184 ? 87.732  69.922  44.526 1.00 97.19  ? 184 ALA B C   1 
ATOM   1450 O O   . ALA B 2 184 ? 87.884  69.940  43.299 1.00 138.61 ? 184 ALA B O   1 
ATOM   1451 C CB  . ALA B 2 184 ? 89.204  71.322  46.046 1.00 166.83 ? 184 ALA B CB  1 
ATOM   1452 N N   . VAL B 2 185 ? 87.465  68.778  45.165 1.00 86.60  ? 185 VAL B N   1 
ATOM   1453 C CA  . VAL B 2 185 ? 87.208  67.522  44.465 1.00 99.81  ? 185 VAL B CA  1 
ATOM   1454 C C   . VAL B 2 185 ? 86.033  67.682  43.505 1.00 106.80 ? 185 VAL B C   1 
ATOM   1455 O O   . VAL B 2 185 ? 86.160  67.274  42.355 1.00 136.31 ? 185 VAL B O   1 
ATOM   1456 C CB  . VAL B 2 185 ? 86.946  66.361  45.444 1.00 132.00 ? 185 VAL B CB  1 
ATOM   1457 C CG1 . VAL B 2 185 ? 86.218  65.161  44.816 1.00 121.49 ? 185 VAL B CG1 1 
ATOM   1458 C CG2 . VAL B 2 185 ? 88.251  65.951  46.113 1.00 174.74 ? 185 VAL B CG2 1 
ATOM   1459 N N   . ASN B 2 186 ? 84.929  68.298  43.950 1.00 113.51 ? 186 ASN B N   1 
ATOM   1460 C CA  . ASN B 2 186 ? 83.734  68.422  43.141 1.00 123.12 ? 186 ASN B CA  1 
ATOM   1461 C C   . ASN B 2 186 ? 83.977  69.385  41.958 1.00 108.05 ? 186 ASN B C   1 
ATOM   1462 O O   . ASN B 2 186 ? 83.345  69.230  40.908 1.00 124.02 ? 186 ASN B O   1 
ATOM   1463 C CB  . ASN B 2 186 ? 82.540  68.735  44.046 1.00 119.81 ? 186 ASN B CB  1 
ATOM   1464 C CG  . ASN B 2 186 ? 81.238  68.160  43.518 1.00 137.15 ? 186 ASN B CG  1 
ATOM   1465 O OD1 . ASN B 2 186 ? 80.741  68.547  42.466 1.00 130.45 ? 186 ASN B OD1 1 
ATOM   1466 N ND2 . ASN B 2 186 ? 80.657  67.212  44.226 1.00 122.22 ? 186 ASN B ND2 1 
ATOM   1467 N N   . CYS B 2 187 ? 84.897  70.358  42.077 1.00 81.31  ? 187 CYS B N   1 
ATOM   1468 C CA  . CYS B 2 187 ? 85.327  71.181  40.947 1.00 150.83 ? 187 CYS B CA  1 
ATOM   1469 C C   . CYS B 2 187 ? 86.255  70.499  39.931 1.00 111.57 ? 187 CYS B C   1 
ATOM   1470 O O   . CYS B 2 187 ? 86.229  70.883  38.767 1.00 129.97 ? 187 CYS B O   1 
ATOM   1471 C CB  . CYS B 2 187 ? 85.997  72.450  41.447 1.00 144.81 ? 187 CYS B CB  1 
ATOM   1472 S SG  . CYS B 2 187 ? 84.805  73.627  42.164 1.00 140.86 ? 187 CYS B SG  1 
ATOM   1473 N N   . TYR B 2 188 ? 87.048  69.524  40.317 1.00 87.41  ? 188 TYR B N   1 
ATOM   1474 C CA  . TYR B 2 188 ? 87.997  68.907  39.398 1.00 107.34 ? 188 TYR B CA  1 
ATOM   1475 C C   . TYR B 2 188 ? 87.334  67.898  38.476 1.00 102.63 ? 188 TYR B C   1 
ATOM   1476 O O   . TYR B 2 188 ? 87.801  67.816  37.325 1.00 247.72 ? 188 TYR B O   1 
ATOM   1477 C CB  . TYR B 2 188 ? 89.182  68.263  40.140 1.00 145.20 ? 188 TYR B CB  1 
ATOM   1478 C CG  . TYR B 2 188 ? 90.326  69.220  40.492 1.00 239.88 ? 188 TYR B CG  1 
ATOM   1479 C CD1 . TYR B 2 188 ? 90.266  70.624  40.368 1.00 234.89 ? 188 TYR B CD1 1 
ATOM   1480 C CD2 . TYR B 2 188 ? 91.552  68.686  40.907 1.00 308.60 ? 188 TYR B CD2 1 
ATOM   1481 C CE1 . TYR B 2 188 ? 91.357  71.436  40.685 1.00 166.69 ? 188 TYR B CE1 1 
ATOM   1482 C CE2 . TYR B 2 188 ? 92.640  69.492  41.220 1.00 294.61 ? 188 TYR B CE2 1 
ATOM   1483 C CZ  . TYR B 2 188 ? 92.544  70.870  41.103 1.00 204.63 ? 188 TYR B CZ  1 
ATOM   1484 O OH  . TYR B 2 188 ? 93.595  71.681  41.408 1.00 236.34 ? 188 TYR B OH  1 
ATOM   1485 N N   . SER B 2 189 ? 86.311  67.145  38.903 1.00 95.18  ? 189 SER B N   1 
ATOM   1486 C CA  . SER B 2 189 ? 85.749  66.118  38.038 1.00 146.14 ? 189 SER B CA  1 
ATOM   1487 C C   . SER B 2 189 ? 84.525  65.460  38.630 1.00 137.51 ? 189 SER B C   1 
ATOM   1488 O O   . SER B 2 189 ? 84.577  64.964  39.756 1.00 205.08 ? 189 SER B O   1 
ATOM   1489 C CB  . SER B 2 189 ? 86.771  65.004  37.748 1.00 181.94 ? 189 SER B CB  1 
ATOM   1490 O OG  . SER B 2 189 ? 86.186  63.913  37.033 1.00 134.00 ? 189 SER B OG  1 
ATOM   1491 N N   . VAL B 2 190 ? 83.439  65.376  37.859 1.00 115.76 ? 190 VAL B N   1 
ATOM   1492 C CA  . VAL B 2 190 ? 82.274  64.640  38.347 1.00 128.44 ? 190 VAL B CA  1 
ATOM   1493 C C   . VAL B 2 190 ? 82.557  63.124  38.479 1.00 119.98 ? 190 VAL B C   1 
ATOM   1494 O O   . VAL B 2 190 ? 81.972  62.460  39.347 1.00 127.38 ? 190 VAL B O   1 
ATOM   1495 C CB  . VAL B 2 190 ? 81.022  64.972  37.517 1.00 137.92 ? 190 VAL B CB  1 
ATOM   1496 C CG1 . VAL B 2 190 ? 79.770  64.251  38.019 1.00 139.35 ? 190 VAL B CG1 1 
ATOM   1497 C CG2 . VAL B 2 190 ? 80.809  66.474  37.514 1.00 168.22 ? 190 VAL B CG2 1 
ATOM   1498 N N   . LYS B 2 191 ? 83.458  62.577  37.658 1.00 125.28 ? 191 LYS B N   1 
ATOM   1499 C CA  . LYS B 2 191 ? 83.923  61.205  37.819 1.00 163.61 ? 191 LYS B CA  1 
ATOM   1500 C C   . LYS B 2 191 ? 84.895  61.026  38.999 1.00 194.69 ? 191 LYS B C   1 
ATOM   1501 O O   . LYS B 2 191 ? 85.187  59.882  39.358 1.00 245.36 ? 191 LYS B O   1 
ATOM   1502 C CB  . LYS B 2 191 ? 84.513  60.721  36.490 1.00 243.54 ? 191 LYS B CB  1 
ATOM   1503 C CG  . LYS B 2 191 ? 83.455  60.375  35.446 1.00 273.87 ? 191 LYS B CG  1 
ATOM   1504 C CD  . LYS B 2 191 ? 82.676  59.083  35.699 1.00 322.41 ? 191 LYS B CD  1 
ATOM   1505 C CE  . LYS B 2 191 ? 83.510  57.819  35.590 1.00 368.07 ? 191 LYS B CE  1 
ATOM   1506 N NZ  . LYS B 2 191 ? 82.683  56.594  35.713 1.00 357.85 ? 191 LYS B NZ  1 
ATOM   1507 N N   . ALA B 2 192 ? 85.394  62.113  39.617 1.00 157.97 ? 192 ALA B N   1 
ATOM   1508 C CA  . ALA B 2 192 ? 85.954  62.056  40.959 1.00 169.27 ? 192 ALA B CA  1 
ATOM   1509 C C   . ALA B 2 192 ? 84.826  62.056  41.985 1.00 136.45 ? 192 ALA B C   1 
ATOM   1510 O O   . ALA B 2 192 ? 84.718  61.132  42.788 1.00 128.49 ? 192 ALA B O   1 
ATOM   1511 C CB  . ALA B 2 192 ? 86.938  63.180  41.201 1.00 194.71 ? 192 ALA B CB  1 
ATOM   1512 N N   . ALA B 2 193 ? 83.969  63.075  41.974 1.00 131.30 ? 193 ALA B N   1 
ATOM   1513 C CA  . ALA B 2 193 ? 82.969  63.252  43.022 1.00 133.47 ? 193 ALA B CA  1 
ATOM   1514 C C   . ALA B 2 193 ? 81.974  62.094  43.111 1.00 145.73 ? 193 ALA B C   1 
ATOM   1515 O O   . ALA B 2 193 ? 81.602  61.720  44.232 1.00 262.16 ? 193 ALA B O   1 
ATOM   1516 C CB  . ALA B 2 193 ? 82.254  64.534  42.810 1.00 131.66 ? 193 ALA B CB  1 
ATOM   1517 N N   . THR B 2 194 ? 81.554  61.488  41.986 1.00 114.95 ? 194 THR B N   1 
ATOM   1518 C CA  . THR B 2 194 ? 80.717  60.287  42.046 1.00 158.00 ? 194 THR B CA  1 
ATOM   1519 C C   . THR B 2 194 ? 81.469  59.052  42.575 1.00 148.53 ? 194 THR B C   1 
ATOM   1520 O O   . THR B 2 194 ? 80.871  58.265  43.323 1.00 212.31 ? 194 THR B O   1 
ATOM   1521 C CB  . THR B 2 194 ? 80.087  59.925  40.706 1.00 190.47 ? 194 THR B CB  1 
ATOM   1522 O OG1 . THR B 2 194 ? 81.088  59.881  39.694 1.00 230.58 ? 194 THR B OG1 1 
ATOM   1523 C CG2 . THR B 2 194 ? 78.998  60.887  40.305 1.00 212.29 ? 194 THR B CG2 1 
ATOM   1524 N N   . ARG B 2 195 ? 82.754  58.869  42.234 1.00 108.34 ? 195 ARG B N   1 
ATOM   1525 C CA  . ARG B 2 195 ? 83.507  57.774  42.814 1.00 150.95 ? 195 ARG B CA  1 
ATOM   1526 C C   . ARG B 2 195 ? 83.680  57.996  44.323 1.00 145.73 ? 195 ARG B C   1 
ATOM   1527 O O   . ARG B 2 195 ? 83.620  57.047  45.100 1.00 151.69 ? 195 ARG B O   1 
ATOM   1528 C CB  . ARG B 2 195 ? 84.837  57.585  42.073 1.00 195.26 ? 195 ARG B CB  1 
ATOM   1529 C CG  . ARG B 2 195 ? 84.677  56.901  40.725 1.00 234.66 ? 195 ARG B CG  1 
ATOM   1530 C CD  . ARG B 2 195 ? 86.014  56.630  40.053 1.00 303.86 ? 195 ARG B CD  1 
ATOM   1531 N NE  . ARG B 2 195 ? 86.748  55.527  40.675 1.00 346.07 ? 195 ARG B NE  1 
ATOM   1532 C CZ  . ARG B 2 195 ? 88.037  55.241  40.470 1.00 375.39 ? 195 ARG B CZ  1 
ATOM   1533 N NH1 . ARG B 2 195 ? 88.572  54.163  41.021 1.00 359.37 ? 195 ARG B NH1 1 
ATOM   1534 N NH2 . ARG B 2 195 ? 88.792  56.025  39.714 1.00 369.30 ? 195 ARG B NH2 1 
ATOM   1535 N N   . VAL B 2 196 ? 83.919  59.228  44.768 1.00 112.73 ? 196 VAL B N   1 
ATOM   1536 C CA  . VAL B 2 196 ? 83.950  59.563  46.191 1.00 129.12 ? 196 VAL B CA  1 
ATOM   1537 C C   . VAL B 2 196 ? 82.618  59.255  46.872 1.00 110.29 ? 196 VAL B C   1 
ATOM   1538 O O   . VAL B 2 196 ? 82.594  58.728  47.980 1.00 151.71 ? 196 VAL B O   1 
ATOM   1539 C CB  . VAL B 2 196 ? 84.410  61.016  46.403 1.00 101.91 ? 196 VAL B CB  1 
ATOM   1540 C CG1 . VAL B 2 196 ? 84.132  61.538  47.805 1.00 87.24  ? 196 VAL B CG1 1 
ATOM   1541 C CG2 . VAL B 2 196 ? 85.905  61.097  46.131 1.00 157.45 ? 196 VAL B CG2 1 
ATOM   1542 N N   . GLN B 2 197 ? 81.509  59.564  46.220 1.00 111.35 ? 197 GLN B N   1 
ATOM   1543 C CA  . GLN B 2 197 ? 80.192  59.234  46.735 1.00 106.29 ? 197 GLN B CA  1 
ATOM   1544 C C   . GLN B 2 197 ? 79.997  57.718  46.840 1.00 125.66 ? 197 GLN B C   1 
ATOM   1545 O O   . GLN B 2 197 ? 79.513  57.256  47.874 1.00 132.67 ? 197 GLN B O   1 
ATOM   1546 C CB  . GLN B 2 197 ? 79.126  59.850  45.830 1.00 156.70 ? 197 GLN B CB  1 
ATOM   1547 C CG  . GLN B 2 197 ? 77.727  59.694  46.362 1.00 156.39 ? 197 GLN B CG  1 
ATOM   1548 C CD  . GLN B 2 197 ? 77.525  60.495  47.614 1.00 172.21 ? 197 GLN B CD  1 
ATOM   1549 O OE1 . GLN B 2 197 ? 77.574  59.966  48.721 1.00 185.82 ? 197 GLN B OE1 1 
ATOM   1550 N NE2 . GLN B 2 197 ? 77.290  61.783  47.439 1.00 124.52 ? 197 GLN B NE2 1 
ATOM   1551 N N   . ASP B 2 198 ? 80.386  56.937  45.818 1.00 132.22 ? 198 ASP B N   1 
ATOM   1552 C CA  . ASP B 2 198 ? 80.317  55.484  45.869 1.00 177.87 ? 198 ASP B CA  1 
ATOM   1553 C C   . ASP B 2 198 ? 81.149  54.960  47.045 1.00 140.42 ? 198 ASP B C   1 
ATOM   1554 O O   . ASP B 2 198 ? 80.673  54.159  47.859 1.00 119.83 ? 198 ASP B O   1 
ATOM   1555 C CB  . ASP B 2 198 ? 80.745  54.875  44.526 1.00 274.58 ? 198 ASP B CB  1 
ATOM   1556 C CG  . ASP B 2 198 ? 80.611  53.356  44.420 1.00 353.69 ? 198 ASP B CG  1 
ATOM   1557 O OD1 . ASP B 2 198 ? 79.762  52.768  45.135 1.00 336.11 ? 198 ASP B OD1 1 
ATOM   1558 O OD2 . ASP B 2 198 ? 81.364  52.757  43.625 1.00 383.56 ? 198 ASP B OD2 1 
ATOM   1559 N N   . ALA B 2 199 ? 82.394  55.424  47.150 1.00 109.39 ? 199 ALA B N   1 
ATOM   1560 C CA  . ALA B 2 199 ? 83.319  55.003  48.189 1.00 173.88 ? 199 ALA B CA  1 
ATOM   1561 C C   . ALA B 2 199 ? 82.719  55.175  49.587 1.00 123.60 ? 199 ALA B C   1 
ATOM   1562 O O   . ALA B 2 199 ? 82.724  54.247  50.403 1.00 183.59 ? 199 ALA B O   1 
ATOM   1563 C CB  . ALA B 2 199 ? 84.631  55.761  48.041 1.00 201.09 ? 199 ALA B CB  1 
ATOM   1564 N N   . PHE B 2 200 ? 82.224  56.356  49.893 1.00 97.69  ? 200 PHE B N   1 
ATOM   1565 C CA  . PHE B 2 200 ? 81.705  56.618  51.228 1.00 158.19 ? 200 PHE B CA  1 
ATOM   1566 C C   . PHE B 2 200 ? 80.262  56.142  51.433 1.00 112.74 ? 200 PHE B C   1 
ATOM   1567 O O   . PHE B 2 200 ? 79.880  55.904  52.575 1.00 193.90 ? 200 PHE B O   1 
ATOM   1568 C CB  . PHE B 2 200 ? 81.926  58.087  51.595 1.00 191.20 ? 200 PHE B CB  1 
ATOM   1569 C CG  . PHE B 2 200 ? 83.385  58.420  51.778 1.00 135.88 ? 200 PHE B CG  1 
ATOM   1570 C CD1 . PHE B 2 200 ? 84.106  57.841  52.806 1.00 184.42 ? 200 PHE B CD1 1 
ATOM   1571 C CD2 . PHE B 2 200 ? 84.028  59.260  50.915 1.00 121.88 ? 200 PHE B CD2 1 
ATOM   1572 C CE1 . PHE B 2 200 ? 85.450  58.112  52.981 1.00 194.17 ? 200 PHE B CE1 1 
ATOM   1573 C CE2 . PHE B 2 200 ? 85.369  59.533  51.082 1.00 189.73 ? 200 PHE B CE2 1 
ATOM   1574 C CZ  . PHE B 2 200 ? 86.076  58.960  52.116 1.00 198.98 ? 200 PHE B CZ  1 
ATOM   1575 N N   . ALA B 2 201 ? 79.464  55.961  50.387 1.00 95.02  ? 201 ALA B N   1 
ATOM   1576 C CA  . ALA B 2 201 ? 78.175  55.289  50.528 1.00 138.38 ? 201 ALA B CA  1 
ATOM   1577 C C   . ALA B 2 201 ? 78.381  53.825  50.924 1.00 151.45 ? 201 ALA B C   1 
ATOM   1578 O O   . ALA B 2 201 ? 77.586  53.307  51.721 1.00 143.37 ? 201 ALA B O   1 
ATOM   1579 C CB  . ALA B 2 201 ? 77.360  55.434  49.261 1.00 189.90 ? 201 ALA B CB  1 
ATOM   1580 N N   . ALA B 2 202 ? 79.426  53.160  50.382 1.00 137.37 ? 202 ALA B N   1 
ATOM   1581 C CA  . ALA B 2 202 ? 79.779  51.802  50.772 1.00 153.60 ? 202 ALA B CA  1 
ATOM   1582 C C   . ALA B 2 202 ? 80.240  51.784  52.224 1.00 147.92 ? 202 ALA B C   1 
ATOM   1583 O O   . ALA B 2 202 ? 79.748  50.960  53.008 1.00 162.30 ? 202 ALA B O   1 
ATOM   1584 C CB  . ALA B 2 202 ? 80.828  51.236  49.839 1.00 195.52 ? 202 ALA B CB  1 
ATOM   1585 N N   . ALA B 2 203 ? 81.171  52.677  52.586 1.00 165.37 ? 203 ALA B N   1 
ATOM   1586 C CA  . ALA B 2 203 ? 81.789  52.690  53.907 1.00 213.68 ? 203 ALA B CA  1 
ATOM   1587 C C   . ALA B 2 203 ? 80.734  52.794  55.016 1.00 154.89 ? 203 ALA B C   1 
ATOM   1588 O O   . ALA B 2 203 ? 80.739  51.975  55.951 1.00 231.44 ? 203 ALA B O   1 
ATOM   1589 C CB  . ALA B 2 203 ? 82.824  53.792  53.991 1.00 235.40 ? 203 ALA B CB  1 
ATOM   1590 N N   . LYS B 2 204 ? 79.826  53.764  54.932 1.00 96.40  ? 204 LYS B N   1 
ATOM   1591 C CA  . LYS B 2 204 ? 78.820  53.913  55.968 1.00 125.46 ? 204 LYS B CA  1 
ATOM   1592 C C   . LYS B 2 204 ? 77.844  52.730  56.071 1.00 147.92 ? 204 LYS B C   1 
ATOM   1593 O O   . LYS B 2 204 ? 77.403  52.419  57.179 1.00 192.39 ? 204 LYS B O   1 
ATOM   1594 C CB  . LYS B 2 204 ? 78.041  55.217  55.793 1.00 139.50 ? 204 LYS B CB  1 
ATOM   1595 C CG  . LYS B 2 204 ? 77.093  55.270  54.621 1.00 136.84 ? 204 LYS B CG  1 
ATOM   1596 C CD  . LYS B 2 204 ? 76.608  56.696  54.431 1.00 120.57 ? 204 LYS B CD  1 
ATOM   1597 C CE  . LYS B 2 204 ? 77.671  57.541  53.777 1.00 206.42 ? 204 LYS B CE  1 
ATOM   1598 N NZ  . LYS B 2 204 ? 77.259  58.940  53.825 1.00 215.18 ? 204 LYS B NZ  1 
ATOM   1599 N N   . LEU B 2 205 ? 77.505  52.056  54.967 1.00 133.52 ? 205 LEU B N   1 
ATOM   1600 C CA  . LEU B 2 205 ? 76.655  50.869  55.049 1.00 169.50 ? 205 LEU B CA  1 
ATOM   1601 C C   . LEU B 2 205 ? 77.396  49.700  55.702 1.00 187.44 ? 205 LEU B C   1 
ATOM   1602 O O   . LEU B 2 205 ? 76.754  48.952  56.440 1.00 218.26 ? 205 LEU B O   1 
ATOM   1603 C CB  . LEU B 2 205 ? 76.131  50.476  53.668 1.00 175.71 ? 205 LEU B CB  1 
ATOM   1604 C CG  . LEU B 2 205 ? 75.083  51.409  53.073 1.00 185.31 ? 205 LEU B CG  1 
ATOM   1605 C CD1 . LEU B 2 205 ? 74.795  50.993  51.636 1.00 259.32 ? 205 LEU B CD1 1 
ATOM   1606 C CD2 . LEU B 2 205 ? 73.798  51.435  53.896 1.00 126.59 ? 205 LEU B CD2 1 
ATOM   1607 N N   . LEU B 2 206 ? 78.713  49.539  55.475 1.00 148.37 ? 206 LEU B N   1 
ATOM   1608 C CA  . LEU B 2 206 ? 79.493  48.575  56.248 1.00 190.71 ? 206 LEU B CA  1 
ATOM   1609 C C   . LEU B 2 206 ? 79.457  48.895  57.751 1.00 180.11 ? 206 LEU B C   1 
ATOM   1610 O O   . LEU B 2 206 ? 79.262  47.985  58.578 1.00 200.88 ? 206 LEU B O   1 
ATOM   1611 C CB  . LEU B 2 206 ? 80.938  48.531  55.738 1.00 217.05 ? 206 LEU B CB  1 
ATOM   1612 C CG  . LEU B 2 206 ? 81.130  47.937  54.342 1.00 335.76 ? 206 LEU B CG  1 
ATOM   1613 C CD1 . LEU B 2 206 ? 82.580  48.076  53.907 1.00 395.19 ? 206 LEU B CD1 1 
ATOM   1614 C CD2 . LEU B 2 206 ? 80.704  46.469  54.275 1.00 394.83 ? 206 LEU B CD2 1 
ATOM   1615 N N   . ALA B 2 207 ? 79.635  50.169  58.119 1.00 138.15 ? 207 ALA B N   1 
ATOM   1616 C CA  . ALA B 2 207 ? 79.558  50.584  59.517 1.00 148.21 ? 207 ALA B CA  1 
ATOM   1617 C C   . ALA B 2 207 ? 78.183  50.293  60.128 1.00 132.63 ? 207 ALA B C   1 
ATOM   1618 O O   . ALA B 2 207 ? 78.108  49.755  61.243 1.00 183.32 ? 207 ALA B O   1 
ATOM   1619 C CB  . ALA B 2 207 ? 79.912  52.039  59.645 1.00 179.70 ? 207 ALA B CB  1 
ATOM   1620 N N   . LEU B 2 208 ? 77.102  50.628  59.413 1.00 121.60 ? 208 LEU B N   1 
ATOM   1621 C CA  . LEU B 2 208 ? 75.751  50.346  59.888 1.00 134.11 ? 208 LEU B CA  1 
ATOM   1622 C C   . LEU B 2 208 ? 75.497  48.846  59.940 1.00 160.46 ? 208 LEU B C   1 
ATOM   1623 O O   . LEU B 2 208 ? 74.788  48.404  60.854 1.00 196.13 ? 208 LEU B O   1 
ATOM   1624 C CB  . LEU B 2 208 ? 74.728  51.111  59.042 1.00 127.81 ? 208 LEU B CB  1 
ATOM   1625 C CG  . LEU B 2 208 ? 74.725  52.600  59.398 1.00 159.72 ? 208 LEU B CG  1 
ATOM   1626 C CD1 . LEU B 2 208 ? 74.271  53.470  58.254 1.00 185.26 ? 208 LEU B CD1 1 
ATOM   1627 C CD2 . LEU B 2 208 ? 73.841  52.876  60.601 1.00 153.27 ? 208 LEU B CD2 1 
ATOM   1628 N N   . ALA B 2 209 ? 76.088  48.068  59.023 1.00 144.92 ? 209 ALA B N   1 
ATOM   1629 C CA  . ALA B 2 209 ? 76.038  46.614  59.124 1.00 203.90 ? 209 ALA B CA  1 
ATOM   1630 C C   . ALA B 2 209 ? 76.689  46.120  60.420 1.00 169.57 ? 209 ALA B C   1 
ATOM   1631 O O   . ALA B 2 209 ? 76.065  45.261  61.064 1.00 123.21 ? 209 ALA B O   1 
ATOM   1632 C CB  . ALA B 2 209 ? 76.638  45.972  57.887 1.00 297.88 ? 209 ALA B CB  1 
ATOM   1633 N N   . LEU B 2 210 ? 77.878  46.644  60.812 1.00 178.24 ? 210 LEU B N   1 
ATOM   1634 C CA  . LEU B 2 210 ? 78.515  46.281  62.090 1.00 173.34 ? 210 LEU B CA  1 
ATOM   1635 C C   . LEU B 2 210 ? 77.598  46.583  63.270 1.00 139.06 ? 210 LEU B C   1 
ATOM   1636 O O   . LEU B 2 210 ? 77.430  45.729  64.140 1.00 188.44 ? 210 LEU B O   1 
ATOM   1637 C CB  . LEU B 2 210 ? 79.852  46.993  62.330 1.00 133.05 ? 210 LEU B CB  1 
ATOM   1638 C CG  . LEU B 2 210 ? 81.010  46.510  61.457 1.00 239.52 ? 210 LEU B CG  1 
ATOM   1639 C CD1 . LEU B 2 210 ? 82.241  47.363  61.674 1.00 259.29 ? 210 LEU B CD1 1 
ATOM   1640 C CD2 . LEU B 2 210 ? 81.360  45.056  61.750 1.00 300.13 ? 210 LEU B CD2 1 
ATOM   1641 N N   . ILE B 2 211 ? 77.005  47.776  63.287 1.00 111.45 ? 211 ILE B N   1 
ATOM   1642 C CA  . ILE B 2 211 ? 76.132  48.172  64.379 1.00 135.05 ? 211 ILE B CA  1 
ATOM   1643 C C   . ILE B 2 211 ? 74.904  47.243  64.449 1.00 159.98 ? 211 ILE B C   1 
ATOM   1644 O O   . ILE B 2 211 ? 74.573  46.742  65.529 1.00 211.07 ? 211 ILE B O   1 
ATOM   1645 C CB  . ILE B 2 211 ? 75.818  49.681  64.271 1.00 117.40 ? 211 ILE B CB  1 
ATOM   1646 C CG1 . ILE B 2 211 ? 77.109  50.474  64.533 1.00 114.63 ? 211 ILE B CG1 1 
ATOM   1647 C CG2 . ILE B 2 211 ? 74.707  50.103  65.235 1.00 114.66 ? 211 ILE B CG2 1 
ATOM   1648 C CD1 . ILE B 2 211 ? 77.071  51.929  64.159 1.00 146.95 ? 211 ILE B CD1 1 
ATOM   1649 N N   . ILE B 2 212 ? 74.238  46.973  63.324 1.00 122.56 ? 212 ILE B N   1 
ATOM   1650 C CA  . ILE B 2 212 ? 73.100  46.062  63.316 1.00 137.66 ? 212 ILE B CA  1 
ATOM   1651 C C   . ILE B 2 212 ? 73.532  44.645  63.725 1.00 150.23 ? 212 ILE B C   1 
ATOM   1652 O O   . ILE B 2 212 ? 72.839  43.982  64.515 1.00 195.56 ? 212 ILE B O   1 
ATOM   1653 C CB  . ILE B 2 212 ? 72.391  46.084  61.948 1.00 159.59 ? 212 ILE B CB  1 
ATOM   1654 C CG1 . ILE B 2 212 ? 71.752  47.444  61.682 1.00 168.90 ? 212 ILE B CG1 1 
ATOM   1655 C CG2 . ILE B 2 212 ? 71.348  44.966  61.831 1.00 171.15 ? 212 ILE B CG2 1 
ATOM   1656 C CD1 . ILE B 2 212 ? 71.430  47.704  60.217 1.00 242.03 ? 212 ILE B CD1 1 
ATOM   1657 N N   . LEU B 2 213 ? 74.660  44.167  63.186 1.00 125.12 ? 213 LEU B N   1 
ATOM   1658 C CA  . LEU B 2 213 ? 75.178  42.837  63.487 1.00 151.77 ? 213 LEU B CA  1 
ATOM   1659 C C   . LEU B 2 213 ? 75.464  42.666  64.983 1.00 147.35 ? 213 LEU B C   1 
ATOM   1660 O O   . LEU B 2 213 ? 75.113  41.644  65.555 1.00 164.08 ? 213 LEU B O   1 
ATOM   1661 C CB  . LEU B 2 213 ? 76.438  42.611  62.638 1.00 201.68 ? 213 LEU B CB  1 
ATOM   1662 C CG  . LEU B 2 213 ? 77.264  41.355  62.919 1.00 234.20 ? 213 LEU B CG  1 
ATOM   1663 C CD1 . LEU B 2 213 ? 76.471  40.100  62.587 1.00 290.12 ? 213 LEU B CD1 1 
ATOM   1664 C CD2 . LEU B 2 213 ? 78.567  41.403  62.143 1.00 226.83 ? 213 LEU B CD2 1 
ATOM   1665 N N   . LEU B 2 214 ? 76.117  43.640  65.626 1.00 160.99 ? 214 LEU B N   1 
ATOM   1666 C CA  . LEU B 2 214 ? 76.379  43.579  67.060 1.00 150.97 ? 214 LEU B CA  1 
ATOM   1667 C C   . LEU B 2 214 ? 75.070  43.606  67.849 1.00 145.79 ? 214 LEU B C   1 
ATOM   1668 O O   . LEU B 2 214 ? 74.980  42.946  68.881 1.00 216.97 ? 214 LEU B O   1 
ATOM   1669 C CB  . LEU B 2 214 ? 77.331  44.713  67.435 1.00 168.89 ? 214 LEU B CB  1 
ATOM   1670 C CG  . LEU B 2 214 ? 78.753  44.539  66.901 1.00 224.70 ? 214 LEU B CG  1 
ATOM   1671 C CD1 . LEU B 2 214 ? 79.531  45.852  66.942 1.00 247.23 ? 214 LEU B CD1 1 
ATOM   1672 C CD2 . LEU B 2 214 ? 79.486  43.454  67.681 1.00 257.08 ? 214 LEU B CD2 1 
ATOM   1673 N N   . GLY B 2 215 ? 74.038  44.312  67.363 1.00 145.19 ? 215 GLY B N   1 
ATOM   1674 C CA  . GLY B 2 215 ? 72.677  44.195  67.886 1.00 177.59 ? 215 GLY B CA  1 
ATOM   1675 C C   . GLY B 2 215 ? 72.103  42.772  67.801 1.00 193.12 ? 215 GLY B C   1 
ATOM   1676 O O   . GLY B 2 215 ? 71.588  42.242  68.793 1.00 234.57 ? 215 GLY B O   1 
ATOM   1677 N N   . PHE B 2 216 ? 72.207  42.144  66.621 1.00 177.57 ? 216 PHE B N   1 
ATOM   1678 C CA  . PHE B 2 216 ? 71.768  40.766  66.414 1.00 225.02 ? 216 PHE B CA  1 
ATOM   1679 C C   . PHE B 2 216 ? 72.545  39.769  67.285 1.00 197.60 ? 216 PHE B C   1 
ATOM   1680 O O   . PHE B 2 216 ? 71.928  38.857  67.841 1.00 240.73 ? 216 PHE B O   1 
ATOM   1681 C CB  . PHE B 2 216 ? 71.861  40.400  64.924 1.00 298.68 ? 216 PHE B CB  1 
ATOM   1682 C CG  . PHE B 2 216 ? 70.806  40.962  63.989 1.00 373.49 ? 216 PHE B CG  1 
ATOM   1683 C CD1 . PHE B 2 216 ? 69.761  41.792  64.413 1.00 383.53 ? 216 PHE B CD1 1 
ATOM   1684 C CD2 . PHE B 2 216 ? 70.858  40.635  62.636 1.00 367.07 ? 216 PHE B CD2 1 
ATOM   1685 C CE1 . PHE B 2 216 ? 68.815  42.274  63.513 1.00 317.50 ? 216 PHE B CE1 1 
ATOM   1686 C CE2 . PHE B 2 216 ? 69.915  41.125  61.740 1.00 352.87 ? 216 PHE B CE2 1 
ATOM   1687 C CZ  . PHE B 2 216 ? 68.894  41.940  62.180 1.00 337.15 ? 216 PHE B CZ  1 
ATOM   1688 N N   . VAL B 2 217 ? 73.874  39.931  67.406 1.00 160.19 ? 217 VAL B N   1 
ATOM   1689 C CA  . VAL B 2 217 ? 74.716  39.132  68.299 1.00 173.18 ? 217 VAL B CA  1 
ATOM   1690 C C   . VAL B 2 217 ? 74.220  39.229  69.748 1.00 160.53 ? 217 VAL B C   1 
ATOM   1691 O O   . VAL B 2 217 ? 74.060  38.200  70.414 1.00 221.77 ? 217 VAL B O   1 
ATOM   1692 C CB  . VAL B 2 217 ? 76.204  39.524  68.156 1.00 204.41 ? 217 VAL B CB  1 
ATOM   1693 C CG1 . VAL B 2 217 ? 77.090  39.069  69.313 1.00 241.17 ? 217 VAL B CG1 1 
ATOM   1694 C CG2 . VAL B 2 217 ? 76.773  39.006  66.845 1.00 255.41 ? 217 VAL B CG2 1 
ATOM   1695 N N   . GLN B 2 218 ? 73.956  40.448  70.220 1.00 150.64 ? 218 GLN B N   1 
ATOM   1696 C CA  . GLN B 2 218 ? 73.526  40.682  71.587 1.00 165.72 ? 218 GLN B CA  1 
ATOM   1697 C C   . GLN B 2 218 ? 72.141  40.086  71.884 1.00 200.55 ? 218 GLN B C   1 
ATOM   1698 O O   . GLN B 2 218 ? 72.007  39.377  72.887 1.00 309.06 ? 218 GLN B O   1 
ATOM   1699 C CB  . GLN B 2 218 ? 73.527  42.181  71.845 1.00 216.45 ? 218 GLN B CB  1 
ATOM   1700 C CG  . GLN B 2 218 ? 73.046  42.595  73.234 1.00 215.02 ? 218 GLN B CG  1 
ATOM   1701 C CD  . GLN B 2 218 ? 73.466  44.016  73.496 1.00 243.04 ? 218 GLN B CD  1 
ATOM   1702 O OE1 . GLN B 2 218 ? 74.150  44.326  74.474 1.00 265.19 ? 218 GLN B OE1 1 
ATOM   1703 N NE2 . GLN B 2 218 ? 73.088  44.899  72.588 1.00 205.55 ? 218 GLN B NE2 1 
ATOM   1704 N N   . ILE B 2 219 ? 71.115  40.343  71.055 1.00 168.02 ? 219 ILE B N   1 
ATOM   1705 C CA  . ILE B 2 219 ? 69.789  39.788  71.315 1.00 208.87 ? 219 ILE B CA  1 
ATOM   1706 C C   . ILE B 2 219 ? 69.800  38.248  71.182 1.00 275.48 ? 219 ILE B C   1 
ATOM   1707 O O   . ILE B 2 219 ? 68.991  37.576  71.827 1.00 309.55 ? 219 ILE B O   1 
ATOM   1708 C CB  . ILE B 2 219 ? 68.712  40.491  70.452 1.00 269.79 ? 219 ILE B CB  1 
ATOM   1709 C CG1 . ILE B 2 219 ? 67.303  40.223  71.006 1.00 304.78 ? 219 ILE B CG1 1 
ATOM   1710 C CG2 . ILE B 2 219 ? 68.826  40.135  68.971 1.00 286.23 ? 219 ILE B CG2 1 
ATOM   1711 C CD1 . ILE B 2 219 ? 66.192  41.009  70.342 1.00 291.69 ? 219 ILE B CD1 1 
ATOM   1712 N N   . GLY B 2 220 ? 70.716  37.674  70.374 1.00 305.87 ? 220 GLY B N   1 
ATOM   1713 C CA  . GLY B 2 220 ? 70.967  36.233  70.326 1.00 328.54 ? 220 GLY B CA  1 
ATOM   1714 C C   . GLY B 2 220 ? 71.576  35.658  71.612 1.00 339.58 ? 220 GLY B C   1 
ATOM   1715 O O   . GLY B 2 220 ? 71.187  34.569  72.036 1.00 366.47 ? 220 GLY B O   1 
ATOM   1716 N N   . LYS B 2 221 ? 72.528  36.382  72.229 1.00 344.15 ? 221 LYS B N   1 
ATOM   1717 C CA  . LYS B 2 221 ? 73.130  36.019  73.513 1.00 348.35 ? 221 LYS B CA  1 
ATOM   1718 C C   . LYS B 2 221 ? 72.177  36.198  74.709 1.00 322.83 ? 221 LYS B C   1 
ATOM   1719 O O   . LYS B 2 221 ? 72.259  35.440  75.680 1.00 333.56 ? 221 LYS B O   1 
ATOM   1720 C CB  . LYS B 2 221 ? 74.385  36.866  73.743 1.00 370.70 ? 221 LYS B CB  1 
ATOM   1721 C CG  . LYS B 2 221 ? 75.582  36.522  72.871 1.00 362.14 ? 221 LYS B CG  1 
ATOM   1722 C CD  . LYS B 2 221 ? 76.652  37.610  72.857 1.00 379.87 ? 221 LYS B CD  1 
ATOM   1723 C CE  . LYS B 2 221 ? 77.183  38.020  74.217 1.00 384.37 ? 221 LYS B CE  1 
ATOM   1724 N NZ  . LYS B 2 221 ? 78.154  39.134  74.105 1.00 376.85 ? 221 LYS B NZ  1 
ATOM   1725 N N   . GLY B 2 222 ? 71.292  37.206  74.659 1.00 297.91 ? 222 GLY B N   1 
ATOM   1726 C CA  . GLY B 2 222 ? 70.342  37.497  75.727 1.00 286.59 ? 222 GLY B CA  1 
ATOM   1727 C C   . GLY B 2 222 ? 70.988  38.033  77.002 1.00 291.95 ? 222 GLY B C   1 
ATOM   1728 O O   . GLY B 2 222 ? 71.955  38.828  76.909 1.00 233.13 ? 222 GLY B O   1 
ATOM   1729 N N   . PHE B 2 233 ? 57.395  48.280  79.639 1.00 312.61 ? 233 PHE B N   1 
ATOM   1730 C CA  . PHE B 2 233 ? 58.352  48.523  78.524 1.00 343.22 ? 233 PHE B CA  1 
ATOM   1731 C C   . PHE B 2 233 ? 58.127  49.876  77.824 1.00 341.72 ? 233 PHE B C   1 
ATOM   1732 O O   . PHE B 2 233 ? 59.057  50.385  77.190 1.00 331.99 ? 233 PHE B O   1 
ATOM   1733 C CB  . PHE B 2 233 ? 58.278  47.366  77.519 1.00 331.47 ? 233 PHE B CB  1 
ATOM   1734 C CG  . PHE B 2 233 ? 59.314  47.423  76.418 1.00 346.30 ? 233 PHE B CG  1 
ATOM   1735 C CD1 . PHE B 2 233 ? 60.676  47.347  76.721 1.00 346.30 ? 233 PHE B CD1 1 
ATOM   1736 C CD2 . PHE B 2 233 ? 58.943  47.561  75.080 1.00 293.07 ? 233 PHE B CD2 1 
ATOM   1737 C CE1 . PHE B 2 233 ? 61.646  47.396  75.724 1.00 295.87 ? 233 PHE B CE1 1 
ATOM   1738 C CE2 . PHE B 2 233 ? 59.917  47.612  74.083 1.00 318.16 ? 233 PHE B CE2 1 
ATOM   1739 C CZ  . PHE B 2 233 ? 61.265  47.535  74.403 1.00 312.68 ? 233 PHE B CZ  1 
ATOM   1740 N N   . GLU B 2 234 ? 56.918  50.473  77.921 1.00 315.35 ? 234 GLU B N   1 
ATOM   1741 C CA  . GLU B 2 234 ? 56.525  51.591  77.060 1.00 261.77 ? 234 GLU B CA  1 
ATOM   1742 C C   . GLU B 2 234 ? 55.903  52.772  77.837 1.00 244.02 ? 234 GLU B C   1 
ATOM   1743 O O   . GLU B 2 234 ? 54.931  53.374  77.367 1.00 224.72 ? 234 GLU B O   1 
ATOM   1744 C CB  . GLU B 2 234 ? 55.573  51.098  75.961 1.00 248.61 ? 234 GLU B CB  1 
ATOM   1745 C CG  . GLU B 2 234 ? 56.169  50.035  75.044 1.00 248.23 ? 234 GLU B CG  1 
ATOM   1746 C CD  . GLU B 2 234 ? 55.284  49.674  73.850 1.00 259.08 ? 234 GLU B CD  1 
ATOM   1747 O OE1 . GLU B 2 234 ? 54.494  50.550  73.351 1.00 176.39 ? 234 GLU B OE1 1 
ATOM   1748 O OE2 . GLU B 2 234 ? 55.383  48.505  73.402 1.00 245.75 ? 234 GLU B OE2 1 
ATOM   1749 N N   . GLY B 2 235 ? 56.467  53.137  79.009 1.00 210.98 ? 235 GLY B N   1 
ATOM   1750 C CA  . GLY B 2 235 ? 56.062  54.338  79.739 1.00 222.03 ? 235 GLY B CA  1 
ATOM   1751 C C   . GLY B 2 235 ? 56.264  55.614  78.909 1.00 260.26 ? 235 GLY B C   1 
ATOM   1752 O O   . GLY B 2 235 ? 57.388  56.062  78.762 1.00 204.75 ? 235 GLY B O   1 
ATOM   1753 N N   . THR B 2 236 ? 55.177  56.195  78.363 1.00 291.94 ? 236 THR B N   1 
ATOM   1754 C CA  . THR B 2 236 ? 55.219  57.105  77.212 1.00 233.25 ? 236 THR B CA  1 
ATOM   1755 C C   . THR B 2 236 ? 54.520  58.444  77.488 1.00 258.89 ? 236 THR B C   1 
ATOM   1756 O O   . THR B 2 236 ? 53.358  58.454  77.905 1.00 310.43 ? 236 THR B O   1 
ATOM   1757 C CB  . THR B 2 236 ? 54.547  56.424  76.008 1.00 233.84 ? 236 THR B CB  1 
ATOM   1758 O OG1 . THR B 2 236 ? 55.338  55.310  75.613 1.00 198.91 ? 236 THR B OG1 1 
ATOM   1759 C CG2 . THR B 2 236 ? 54.387  57.286  74.777 1.00 237.32 ? 236 THR B CG2 1 
ATOM   1760 N N   . LYS B 2 237 ? 55.212  59.574  77.224 1.00 286.95 ? 237 LYS B N   1 
ATOM   1761 C CA  . LYS B 2 237 ? 54.631  60.915  77.306 1.00 349.21 ? 237 LYS B CA  1 
ATOM   1762 C C   . LYS B 2 237 ? 53.843  61.243  76.024 1.00 319.87 ? 237 LYS B C   1 
ATOM   1763 O O   . LYS B 2 237 ? 54.233  62.101  75.214 1.00 186.16 ? 237 LYS B O   1 
ATOM   1764 C CB  . LYS B 2 237 ? 55.729  61.942  77.619 1.00 396.47 ? 237 LYS B CB  1 
ATOM   1765 C CG  . LYS B 2 237 ? 55.208  63.314  78.022 1.00 457.79 ? 237 LYS B CG  1 
ATOM   1766 C CD  . LYS B 2 237 ? 56.291  64.260  78.511 1.00 515.82 ? 237 LYS B CD  1 
ATOM   1767 C CE  . LYS B 2 237 ? 55.792  65.648  78.867 1.00 549.00 ? 237 LYS B CE  1 
ATOM   1768 N NZ  . LYS B 2 237 ? 55.349  66.448  77.698 1.00 560.43 ? 237 LYS B NZ  1 
ATOM   1769 N N   . LEU B 2 238 ? 52.699  60.549  75.858 1.00 345.25 ? 238 LEU B N   1 
ATOM   1770 C CA  . LEU B 2 238 ? 51.861  60.652  74.663 1.00 340.87 ? 238 LEU B CA  1 
ATOM   1771 C C   . LEU B 2 238 ? 51.124  61.998  74.655 1.00 313.81 ? 238 LEU B C   1 
ATOM   1772 O O   . LEU B 2 238 ? 50.248  62.242  75.489 1.00 334.22 ? 238 LEU B O   1 
ATOM   1773 C CB  . LEU B 2 238 ? 50.877  59.472  74.618 1.00 347.76 ? 238 LEU B CB  1 
ATOM   1774 C CG  . LEU B 2 238 ? 50.370  59.075  73.229 1.00 377.62 ? 238 LEU B CG  1 
ATOM   1775 C CD1 . LEU B 2 238 ? 49.567  57.783  73.308 1.00 390.81 ? 238 LEU B CD1 1 
ATOM   1776 C CD2 . LEU B 2 238 ? 49.534  60.173  72.570 1.00 362.18 ? 238 LEU B CD2 1 
ATOM   1777 N N   . ASP B 2 239 ? 51.486  62.862  73.693 1.00 284.85 ? 239 ASP B N   1 
ATOM   1778 C CA  . ASP B 2 239 ? 50.870  64.166  73.500 1.00 287.67 ? 239 ASP B CA  1 
ATOM   1779 C C   . ASP B 2 239 ? 51.043  64.593  72.039 1.00 312.07 ? 239 ASP B C   1 
ATOM   1780 O O   . ASP B 2 239 ? 52.174  64.661  71.561 1.00 353.31 ? 239 ASP B O   1 
ATOM   1781 C CB  . ASP B 2 239 ? 51.492  65.189  74.457 1.00 301.18 ? 239 ASP B CB  1 
ATOM   1782 C CG  . ASP B 2 239 ? 50.960  66.613  74.340 1.00 351.28 ? 239 ASP B CG  1 
ATOM   1783 O OD1 . ASP B 2 239 ? 49.992  66.835  73.577 1.00 368.64 ? 239 ASP B OD1 1 
ATOM   1784 O OD2 . ASP B 2 239 ? 51.524  67.501  75.013 1.00 393.72 ? 239 ASP B OD2 1 
ATOM   1785 N N   . VAL B 2 240 ? 49.938  64.912  71.336 1.00 288.41 ? 240 VAL B N   1 
ATOM   1786 C CA  . VAL B 2 240 ? 49.995  65.408  69.960 1.00 235.62 ? 240 VAL B CA  1 
ATOM   1787 C C   . VAL B 2 240 ? 50.841  66.689  69.882 1.00 196.69 ? 240 VAL B C   1 
ATOM   1788 O O   . VAL B 2 240 ? 51.491  66.933  68.871 1.00 228.80 ? 240 VAL B O   1 
ATOM   1789 C CB  . VAL B 2 240 ? 48.573  65.594  69.378 1.00 320.19 ? 240 VAL B CB  1 
ATOM   1790 C CG1 . VAL B 2 240 ? 48.547  66.295  68.016 1.00 349.59 ? 240 VAL B CG1 1 
ATOM   1791 C CG2 . VAL B 2 240 ? 47.852  64.256  69.285 1.00 351.50 ? 240 VAL B CG2 1 
ATOM   1792 N N   . GLY B 2 241 ? 50.858  67.516  70.942 1.00 263.17 ? 241 GLY B N   1 
ATOM   1793 C CA  . GLY B 2 241 ? 51.737  68.682  71.039 1.00 267.98 ? 241 GLY B CA  1 
ATOM   1794 C C   . GLY B 2 241 ? 53.231  68.399  71.275 1.00 274.27 ? 241 GLY B C   1 
ATOM   1795 O O   . GLY B 2 241 ? 54.004  69.358  71.334 1.00 191.60 ? 241 GLY B O   1 
ATOM   1796 N N   . ASN B 2 242 ? 53.642  67.119  71.409 1.00 294.49 ? 242 ASN B N   1 
ATOM   1797 C CA  . ASN B 2 242 ? 55.021  66.724  71.713 1.00 256.21 ? 242 ASN B CA  1 
ATOM   1798 C C   . ASN B 2 242 ? 55.548  65.649  70.744 1.00 211.36 ? 242 ASN B C   1 
ATOM   1799 O O   . ASN B 2 242 ? 56.695  65.747  70.325 1.00 150.99 ? 242 ASN B O   1 
ATOM   1800 C CB  . ASN B 2 242 ? 55.120  66.302  73.184 1.00 268.73 ? 242 ASN B CB  1 
ATOM   1801 C CG  . ASN B 2 242 ? 56.514  66.354  73.787 1.00 278.82 ? 242 ASN B CG  1 
ATOM   1802 O OD1 . ASN B 2 242 ? 56.657  66.385  75.003 1.00 312.66 ? 242 ASN B OD1 1 
ATOM   1803 N ND2 . ASN B 2 242 ? 57.561  66.372  72.977 1.00 287.49 ? 242 ASN B ND2 1 
ATOM   1804 N N   . ILE B 2 243 ? 54.744  64.631  70.377 1.00 234.47 ? 243 ILE B N   1 
ATOM   1805 C CA  . ILE B 2 243 ? 55.112  63.587  69.410 1.00 204.66 ? 243 ILE B CA  1 
ATOM   1806 C C   . ILE B 2 243 ? 55.515  64.164  68.045 1.00 180.68 ? 243 ILE B C   1 
ATOM   1807 O O   . ILE B 2 243 ? 56.343  63.585  67.345 1.00 204.94 ? 243 ILE B O   1 
ATOM   1808 C CB  . ILE B 2 243 ? 53.956  62.572  69.273 1.00 215.86 ? 243 ILE B CB  1 
ATOM   1809 C CG1 . ILE B 2 243 ? 54.400  61.282  68.590 1.00 212.13 ? 243 ILE B CG1 1 
ATOM   1810 C CG2 . ILE B 2 243 ? 52.742  63.176  68.571 1.00 227.41 ? 243 ILE B CG2 1 
ATOM   1811 C CD1 . ILE B 2 243 ? 53.300  60.218  68.553 1.00 215.61 ? 243 ILE B CD1 1 
ATOM   1812 N N   . VAL B 2 244 ? 54.954  65.311  67.675 1.00 164.91 ? 244 VAL B N   1 
ATOM   1813 C CA  . VAL B 2 244 ? 55.335  66.061  66.488 1.00 208.80 ? 244 VAL B CA  1 
ATOM   1814 C C   . VAL B 2 244 ? 56.821  66.440  66.489 1.00 225.68 ? 244 VAL B C   1 
ATOM   1815 O O   . VAL B 2 244 ? 57.450  66.416  65.431 1.00 264.02 ? 244 VAL B O   1 
ATOM   1816 C CB  . VAL B 2 244 ? 54.422  67.295  66.377 1.00 256.43 ? 244 VAL B CB  1 
ATOM   1817 C CG1 . VAL B 2 244 ? 54.918  68.383  65.416 1.00 291.16 ? 244 VAL B CG1 1 
ATOM   1818 C CG2 . VAL B 2 244 ? 53.019  66.840  66.002 1.00 216.89 ? 244 VAL B CG2 1 
ATOM   1819 N N   . LEU B 2 245 ? 57.392  66.784  67.653 1.00 159.38 ? 245 LEU B N   1 
ATOM   1820 C CA  . LEU B 2 245 ? 58.819  67.080  67.734 1.00 173.45 ? 245 LEU B CA  1 
ATOM   1821 C C   . LEU B 2 245 ? 59.662  65.787  67.699 1.00 162.35 ? 245 LEU B C   1 
ATOM   1822 O O   . LEU B 2 245 ? 60.830  65.843  67.321 1.00 187.75 ? 245 LEU B O   1 
ATOM   1823 C CB  . LEU B 2 245 ? 59.092  67.935  68.977 1.00 212.87 ? 245 LEU B CB  1 
ATOM   1824 C CG  . LEU B 2 245 ? 58.771  69.420  68.790 1.00 282.19 ? 245 LEU B CG  1 
ATOM   1825 C CD1 . LEU B 2 245 ? 57.265  69.692  68.712 1.00 263.54 ? 245 LEU B CD1 1 
ATOM   1826 C CD2 . LEU B 2 245 ? 59.402  70.239  69.910 1.00 359.76 ? 245 LEU B CD2 1 
ATOM   1827 N N   . ALA B 2 246 ? 59.098  64.622  68.047 1.00 148.64 ? 246 ALA B N   1 
ATOM   1828 C CA  . ALA B 2 246 ? 59.721  63.343  67.731 1.00 173.41 ? 246 ALA B CA  1 
ATOM   1829 C C   . ALA B 2 246 ? 59.813  63.179  66.217 1.00 171.16 ? 246 ALA B C   1 
ATOM   1830 O O   . ALA B 2 246 ? 60.883  62.895  65.697 1.00 177.40 ? 246 ALA B O   1 
ATOM   1831 C CB  . ALA B 2 246 ? 58.977  62.180  68.387 1.00 226.99 ? 246 ALA B CB  1 
ATOM   1832 N N   . LEU B 2 247 ? 58.695  63.368  65.503 1.00 198.43 ? 247 LEU B N   1 
ATOM   1833 C CA  . LEU B 2 247 ? 58.654  63.274  64.049 1.00 175.73 ? 247 LEU B CA  1 
ATOM   1834 C C   . LEU B 2 247 ? 59.605  64.290  63.401 1.00 140.46 ? 247 LEU B C   1 
ATOM   1835 O O   . LEU B 2 247 ? 60.391  63.900  62.548 1.00 138.70 ? 247 LEU B O   1 
ATOM   1836 C CB  . LEU B 2 247 ? 57.212  63.455  63.555 1.00 142.86 ? 247 LEU B CB  1 
ATOM   1837 C CG  . LEU B 2 247 ? 56.265  62.331  63.952 1.00 240.36 ? 247 LEU B CG  1 
ATOM   1838 C CD1 . LEU B 2 247 ? 54.822  62.732  63.696 1.00 336.95 ? 247 LEU B CD1 1 
ATOM   1839 C CD2 . LEU B 2 247 ? 56.595  61.062  63.192 1.00 234.51 ? 247 LEU B CD2 1 
ATOM   1840 N N   . TYR B 2 248 ? 59.564  65.576  63.755 1.00 125.70 ? 248 TYR B N   1 
ATOM   1841 C CA  . TYR B 2 248 ? 60.504  66.568  63.223 1.00 147.54 ? 248 TYR B CA  1 
ATOM   1842 C C   . TYR B 2 248 ? 61.972  66.212  63.497 1.00 150.84 ? 248 TYR B C   1 
ATOM   1843 O O   . TYR B 2 248 ? 62.828  66.580  62.679 1.00 153.55 ? 248 TYR B O   1 
ATOM   1844 C CB  . TYR B 2 248 ? 60.096  67.959  63.751 1.00 182.46 ? 248 TYR B CB  1 
ATOM   1845 C CG  . TYR B 2 248 ? 59.173  68.763  62.844 1.00 158.46 ? 248 TYR B CG  1 
ATOM   1846 C CD1 . TYR B 2 248 ? 58.466  68.173  61.784 1.00 197.69 ? 248 TYR B CD1 1 
ATOM   1847 C CD2 . TYR B 2 248 ? 59.039  70.144  63.024 1.00 155.11 ? 248 TYR B CD2 1 
ATOM   1848 C CE1 . TYR B 2 248 ? 57.651  68.918  60.938 1.00 209.45 ? 248 TYR B CE1 1 
ATOM   1849 C CE2 . TYR B 2 248 ? 58.220  70.896  62.188 1.00 221.81 ? 248 TYR B CE2 1 
ATOM   1850 C CZ  . TYR B 2 248 ? 57.527  70.284  61.142 1.00 250.88 ? 248 TYR B CZ  1 
ATOM   1851 O OH  . TYR B 2 248 ? 56.723  71.005  60.299 1.00 252.97 ? 248 TYR B OH  1 
ATOM   1852 N N   . SER B 2 249 ? 62.264  65.511  64.611 1.00 165.96 ? 249 SER B N   1 
ATOM   1853 C CA  . SER B 2 249 ? 63.598  64.994  64.886 1.00 190.70 ? 249 SER B CA  1 
ATOM   1854 C C   . SER B 2 249 ? 63.922  63.822  63.959 1.00 164.61 ? 249 SER B C   1 
ATOM   1855 O O   . SER B 2 249 ? 65.021  63.763  63.414 1.00 169.08 ? 249 SER B O   1 
ATOM   1856 C CB  . SER B 2 249 ? 63.768  64.619  66.345 1.00 206.44 ? 249 SER B CB  1 
ATOM   1857 O OG  . SER B 2 249 ? 63.564  65.760  67.162 1.00 266.69 ? 249 SER B OG  1 
ATOM   1858 N N   . GLY B 2 250 ? 62.989  62.883  63.784 1.00 144.37 ? 250 GLY B N   1 
ATOM   1859 C CA  . GLY B 2 250 ? 63.173  61.731  62.913 1.00 153.50 ? 250 GLY B CA  1 
ATOM   1860 C C   . GLY B 2 250 ? 63.343  62.136  61.449 1.00 116.93 ? 250 GLY B C   1 
ATOM   1861 O O   . GLY B 2 250 ? 64.255  61.698  60.767 1.00 108.33 ? 250 GLY B O   1 
ATOM   1862 N N   . LEU B 2 251 ? 62.468  62.978  60.918 1.00 116.35 ? 251 LEU B N   1 
ATOM   1863 C CA  . LEU B 2 251 ? 62.506  63.330  59.507 1.00 129.96 ? 251 LEU B CA  1 
ATOM   1864 C C   . LEU B 2 251 ? 63.844  63.991  59.129 1.00 132.06 ? 251 LEU B C   1 
ATOM   1865 O O   . LEU B 2 251 ? 64.249  63.822  57.981 1.00 122.49 ? 251 LEU B O   1 
ATOM   1866 C CB  . LEU B 2 251 ? 61.315  64.263  59.208 1.00 114.47 ? 251 LEU B CB  1 
ATOM   1867 C CG  . LEU B 2 251 ? 59.946  63.618  59.144 1.00 115.32 ? 251 LEU B CG  1 
ATOM   1868 C CD1 . LEU B 2 251 ? 58.851  64.666  59.081 1.00 163.99 ? 251 LEU B CD1 1 
ATOM   1869 C CD2 . LEU B 2 251 ? 59.826  62.733  57.930 1.00 184.49 ? 251 LEU B CD2 1 
ATOM   1870 N N   . PHE B 2 252 ? 64.501  64.772  60.032 1.00 131.20 ? 252 PHE B N   1 
ATOM   1871 C CA  . PHE B 2 252 ? 65.794  65.372  59.733 1.00 123.76 ? 252 PHE B CA  1 
ATOM   1872 C C   . PHE B 2 252 ? 66.781  64.287  59.300 1.00 104.79 ? 252 PHE B C   1 
ATOM   1873 O O   . PHE B 2 252 ? 67.664  64.537  58.469 1.00 91.70  ? 252 PHE B O   1 
ATOM   1874 C CB  . PHE B 2 252 ? 66.367  66.159  60.917 1.00 173.11 ? 252 PHE B CB  1 
ATOM   1875 C CG  . PHE B 2 252 ? 67.845  66.500  60.744 1.00 167.97 ? 252 PHE B CG  1 
ATOM   1876 C CD1 . PHE B 2 252 ? 68.255  67.455  59.809 1.00 149.42 ? 252 PHE B CD1 1 
ATOM   1877 C CD2 . PHE B 2 252 ? 68.836  65.854  61.497 1.00 152.81 ? 252 PHE B CD2 1 
ATOM   1878 C CE1 . PHE B 2 252 ? 69.598  67.748  59.638 1.00 113.04 ? 252 PHE B CE1 1 
ATOM   1879 C CE2 . PHE B 2 252 ? 70.171  66.157  61.306 1.00 169.48 ? 252 PHE B CE2 1 
ATOM   1880 C CZ  . PHE B 2 252 ? 70.541  67.087  60.368 1.00 150.34 ? 252 PHE B CZ  1 
ATOM   1881 N N   . ALA B 2 253 ? 66.650  63.069  59.841 1.00 102.28 ? 253 ALA B N   1 
ATOM   1882 C CA  . ALA B 2 253 ? 67.561  61.976  59.505 1.00 141.55 ? 253 ALA B CA  1 
ATOM   1883 C C   . ALA B 2 253 ? 67.230  61.345  58.159 1.00 111.87 ? 253 ALA B C   1 
ATOM   1884 O O   . ALA B 2 253 ? 68.096  60.731  57.561 1.00 105.69 ? 253 ALA B O   1 
ATOM   1885 C CB  . ALA B 2 253 ? 67.546  60.974  60.623 1.00 156.85 ? 253 ALA B CB  1 
ATOM   1886 N N   . TYR B 2 254 ? 65.997  61.491  57.670 1.00 129.66 ? 254 TYR B N   1 
ATOM   1887 C CA  . TYR B 2 254 ? 65.626  61.088  56.319 1.00 123.71 ? 254 TYR B CA  1 
ATOM   1888 C C   . TYR B 2 254 ? 65.755  62.201  55.286 1.00 102.91 ? 254 TYR B C   1 
ATOM   1889 O O   . TYR B 2 254 ? 65.482  61.966  54.119 1.00 145.45 ? 254 TYR B O   1 
ATOM   1890 C CB  . TYR B 2 254 ? 64.167  60.652  56.332 1.00 113.88 ? 254 TYR B CB  1 
ATOM   1891 C CG  . TYR B 2 254 ? 63.955  59.272  56.904 1.00 134.88 ? 254 TYR B CG  1 
ATOM   1892 C CD1 . TYR B 2 254 ? 64.125  58.151  56.102 1.00 118.77 ? 254 TYR B CD1 1 
ATOM   1893 C CD2 . TYR B 2 254 ? 63.561  59.110  58.227 1.00 151.57 ? 254 TYR B CD2 1 
ATOM   1894 C CE1 . TYR B 2 254 ? 63.906  56.893  56.626 1.00 134.66 ? 254 TYR B CE1 1 
ATOM   1895 C CE2 . TYR B 2 254 ? 63.348  57.849  58.758 1.00 96.80  ? 254 TYR B CE2 1 
ATOM   1896 C CZ  . TYR B 2 254 ? 63.514  56.742  57.948 1.00 125.36 ? 254 TYR B CZ  1 
ATOM   1897 O OH  . TYR B 2 254 ? 63.286  55.509  58.476 1.00 186.39 ? 254 TYR B OH  1 
ATOM   1898 N N   . GLY B 2 255 ? 66.124  63.413  55.665 1.00 92.19  ? 255 GLY B N   1 
ATOM   1899 C CA  . GLY B 2 255 ? 66.149  64.524  54.723 1.00 118.09 ? 255 GLY B CA  1 
ATOM   1900 C C   . GLY B 2 255 ? 67.173  64.238  53.639 1.00 134.61 ? 255 GLY B C   1 
ATOM   1901 O O   . GLY B 2 255 ? 68.318  63.912  53.934 1.00 116.26 ? 255 GLY B O   1 
ATOM   1902 N N   . GLY B 2 256 ? 66.733  64.335  52.379 1.00 169.62 ? 256 GLY B N   1 
ATOM   1903 C CA  . GLY B 2 256 ? 67.590  64.029  51.240 1.00 133.67 ? 256 GLY B CA  1 
ATOM   1904 C C   . GLY B 2 256 ? 66.933  63.167  50.162 1.00 121.68 ? 256 GLY B C   1 
ATOM   1905 O O   . GLY B 2 256 ? 67.544  63.002  49.121 1.00 148.27 ? 256 GLY B O   1 
ATOM   1906 N N   . TRP B 2 257 ? 65.718  62.622  50.355 1.00 118.66 ? 257 TRP B N   1 
ATOM   1907 C CA  . TRP B 2 257 ? 65.080  61.858  49.294 1.00 130.07 ? 257 TRP B CA  1 
ATOM   1908 C C   . TRP B 2 257 ? 64.828  62.724  48.044 1.00 164.57 ? 257 TRP B C   1 
ATOM   1909 O O   . TRP B 2 257 ? 64.770  62.209  46.922 1.00 131.26 ? 257 TRP B O   1 
ATOM   1910 C CB  . TRP B 2 257 ? 63.789  61.222  49.825 1.00 115.41 ? 257 TRP B CB  1 
ATOM   1911 C CG  . TRP B 2 257 ? 62.614  62.145  49.994 1.00 126.15 ? 257 TRP B CG  1 
ATOM   1912 C CD1 . TRP B 2 257 ? 61.824  62.708  49.018 1.00 166.30 ? 257 TRP B CD1 1 
ATOM   1913 C CD2 . TRP B 2 257 ? 62.063  62.592  51.234 1.00 98.72  ? 257 TRP B CD2 1 
ATOM   1914 N NE1 . TRP B 2 257 ? 60.849  63.505  49.555 1.00 119.40 ? 257 TRP B NE1 1 
ATOM   1915 C CE2 . TRP B 2 257 ? 60.961  63.438  50.919 1.00 148.99 ? 257 TRP B CE2 1 
ATOM   1916 C CE3 . TRP B 2 257 ? 62.373  62.376  52.571 1.00 135.87 ? 257 TRP B CE3 1 
ATOM   1917 C CZ2 . TRP B 2 257 ? 60.181  64.052  51.912 1.00 202.07 ? 257 TRP B CZ2 1 
ATOM   1918 C CZ3 . TRP B 2 257 ? 61.596  62.979  53.551 1.00 220.71 ? 257 TRP B CZ3 1 
ATOM   1919 C CH2 . TRP B 2 257 ? 60.509  63.804  53.228 1.00 169.75 ? 257 TRP B CH2 1 
ATOM   1920 N N   . ASN B 2 258 ? 64.662  64.045  48.238 1.00 132.68 ? 258 ASN B N   1 
ATOM   1921 C CA  . ASN B 2 258 ? 64.488  64.978  47.130 1.00 116.58 ? 258 ASN B CA  1 
ATOM   1922 C C   . ASN B 2 258 ? 65.797  65.352  46.463 1.00 101.66 ? 258 ASN B C   1 
ATOM   1923 O O   . ASN B 2 258 ? 65.759  66.086  45.477 1.00 167.36 ? 258 ASN B O   1 
ATOM   1924 C CB  . ASN B 2 258 ? 63.712  66.242  47.531 1.00 132.89 ? 258 ASN B CB  1 
ATOM   1925 C CG  . ASN B 2 258 ? 64.242  66.994  48.728 1.00 149.56 ? 258 ASN B CG  1 
ATOM   1926 O OD1 . ASN B 2 258 ? 65.023  66.476  49.516 1.00 140.53 ? 258 ASN B OD1 1 
ATOM   1927 N ND2 . ASN B 2 258 ? 63.811  68.236  48.876 1.00 186.38 ? 258 ASN B ND2 1 
ATOM   1928 N N   . TYR B 2 259 ? 66.958  64.890  46.931 1.00 90.00  ? 259 TYR B N   1 
ATOM   1929 C CA  . TYR B 2 259 ? 68.223  65.412  46.419 1.00 106.40 ? 259 TYR B CA  1 
ATOM   1930 C C   . TYR B 2 259 ? 68.553  64.907  45.008 1.00 139.15 ? 259 TYR B C   1 
ATOM   1931 O O   . TYR B 2 259 ? 69.136  65.704  44.251 1.00 130.08 ? 259 TYR B O   1 
ATOM   1932 C CB  . TYR B 2 259 ? 69.363  65.133  47.398 1.00 148.96 ? 259 TYR B CB  1 
ATOM   1933 C CG  . TYR B 2 259 ? 69.469  66.096  48.580 1.00 103.55 ? 259 TYR B CG  1 
ATOM   1934 C CD1 . TYR B 2 259 ? 68.455  66.959  48.932 1.00 130.31 ? 259 TYR B CD1 1 
ATOM   1935 C CD2 . TYR B 2 259 ? 70.622  66.126  49.343 1.00 112.44 ? 259 TYR B CD2 1 
ATOM   1936 C CE1 . TYR B 2 259 ? 68.565  67.836  49.993 1.00 160.82 ? 259 TYR B CE1 1 
ATOM   1937 C CE2 . TYR B 2 259 ? 70.745  66.981  50.413 1.00 129.67 ? 259 TYR B CE2 1 
ATOM   1938 C CZ  . TYR B 2 259 ? 69.714  67.846  50.740 1.00 151.51 ? 259 TYR B CZ  1 
ATOM   1939 O OH  . TYR B 2 259 ? 69.790  68.718  51.787 1.00 229.25 ? 259 TYR B OH  1 
ATOM   1940 N N   . LEU B 2 260 ? 68.168  63.663  44.627 1.00 120.53 ? 260 LEU B N   1 
ATOM   1941 C CA  . LEU B 2 260 ? 68.435  63.196  43.260 1.00 108.83 ? 260 LEU B CA  1 
ATOM   1942 C C   . LEU B 2 260 ? 67.648  63.963  42.200 1.00 103.99 ? 260 LEU B C   1 
ATOM   1943 O O   . LEU B 2 260 ? 68.106  64.112  41.065 1.00 107.23 ? 260 LEU B O   1 
ATOM   1944 C CB  . LEU B 2 260 ? 68.158  61.710  43.120 1.00 117.83 ? 260 LEU B CB  1 
ATOM   1945 C CG  . LEU B 2 260 ? 68.866  61.054  41.926 1.00 127.45 ? 260 LEU B CG  1 
ATOM   1946 C CD1 . LEU B 2 260 ? 70.391  60.993  42.050 1.00 92.44  ? 260 LEU B CD1 1 
ATOM   1947 C CD2 . LEU B 2 260 ? 68.379  59.633  41.741 1.00 154.34 ? 260 LEU B CD2 1 
ATOM   1948 N N   . ASN B 2 261 ? 66.510  64.529  42.574 1.00 112.91 ? 261 ASN B N   1 
ATOM   1949 C CA  . ASN B 2 261 ? 65.772  65.453  41.702 1.00 119.97 ? 261 ASN B CA  1 
ATOM   1950 C C   . ASN B 2 261 ? 66.531  66.741  41.317 1.00 112.06 ? 261 ASN B C   1 
ATOM   1951 O O   . ASN B 2 261 ? 66.112  67.412  40.389 1.00 118.74 ? 261 ASN B O   1 
ATOM   1952 C CB  . ASN B 2 261 ? 64.396  65.759  42.300 1.00 116.33 ? 261 ASN B CB  1 
ATOM   1953 C CG  . ASN B 2 261 ? 63.381  64.737  41.854 1.00 158.95 ? 261 ASN B CG  1 
ATOM   1954 O OD1 . ASN B 2 261 ? 62.779  64.914  40.805 1.00 135.48 ? 261 ASN B OD1 1 
ATOM   1955 N ND2 . ASN B 2 261 ? 63.200  63.666  42.615 1.00 215.96 ? 261 ASN B ND2 1 
ATOM   1956 N N   . PHE B 2 262 ? 67.655  67.088  41.957 1.00 96.38  ? 262 PHE B N   1 
ATOM   1957 C CA  . PHE B 2 262 ? 68.465  68.198  41.491 1.00 86.71  ? 262 PHE B CA  1 
ATOM   1958 C C   . PHE B 2 262 ? 69.439  67.800  40.385 1.00 98.28  ? 262 PHE B C   1 
ATOM   1959 O O   . PHE B 2 262 ? 70.033  68.728  39.819 1.00 152.07 ? 262 PHE B O   1 
ATOM   1960 C CB  . PHE B 2 262 ? 69.248  68.830  42.643 1.00 142.74 ? 262 PHE B CB  1 
ATOM   1961 C CG  . PHE B 2 262 ? 68.380  69.385  43.747 1.00 146.42 ? 262 PHE B CG  1 
ATOM   1962 C CD1 . PHE B 2 262 ? 67.511  70.413  43.468 1.00 120.99 ? 262 PHE B CD1 1 
ATOM   1963 C CD2 . PHE B 2 262 ? 68.428  68.880  45.043 1.00 159.41 ? 262 PHE B CD2 1 
ATOM   1964 C CE1 . PHE B 2 262 ? 66.693  70.936  44.452 1.00 154.03 ? 262 PHE B CE1 1 
ATOM   1965 C CE2 . PHE B 2 262 ? 67.610  69.406  46.027 1.00 156.66 ? 262 PHE B CE2 1 
ATOM   1966 C CZ  . PHE B 2 262 ? 66.741  70.430  45.728 1.00 185.62 ? 262 PHE B CZ  1 
ATOM   1967 N N   . VAL B 2 263 ? 69.626  66.501  40.054 1.00 95.19  ? 263 VAL B N   1 
ATOM   1968 C CA  . VAL B 2 263 ? 70.585  66.097  39.014 1.00 125.73 ? 263 VAL B CA  1 
ATOM   1969 C C   . VAL B 2 263 ? 69.983  65.291  37.838 1.00 170.03 ? 263 VAL B C   1 
ATOM   1970 O O   . VAL B 2 263 ? 70.681  64.529  37.158 1.00 181.93 ? 263 VAL B O   1 
ATOM   1971 C CB  . VAL B 2 263 ? 71.749  65.337  39.684 1.00 131.69 ? 263 VAL B CB  1 
ATOM   1972 C CG1 . VAL B 2 263 ? 72.412  66.237  40.710 1.00 146.21 ? 263 VAL B CG1 1 
ATOM   1973 C CG2 . VAL B 2 263 ? 71.358  63.992  40.299 1.00 121.48 ? 263 VAL B CG2 1 
ATOM   1974 N N   . THR B 2 264 ? 68.694  65.468  37.551 1.00 168.40 ? 264 THR B N   1 
ATOM   1975 C CA  . THR B 2 264 ? 68.002  64.753  36.486 1.00 152.69 ? 264 THR B CA  1 
ATOM   1976 C C   . THR B 2 264 ? 68.569  65.062  35.096 1.00 154.67 ? 264 THR B C   1 
ATOM   1977 O O   . THR B 2 264 ? 68.518  64.203  34.207 1.00 181.52 ? 264 THR B O   1 
ATOM   1978 C CB  . THR B 2 264 ? 66.509  65.107  36.558 1.00 176.11 ? 264 THR B CB  1 
ATOM   1979 O OG1 . THR B 2 264 ? 66.364  66.521  36.627 1.00 127.95 ? 264 THR B OG1 1 
ATOM   1980 C CG2 . THR B 2 264 ? 65.834  64.564  37.783 1.00 144.45 ? 264 THR B CG2 1 
ATOM   1981 N N   . GLU B 2 265 ? 69.092  66.285  34.885 1.00 154.29 ? 265 GLU B N   1 
ATOM   1982 C CA  . GLU B 2 265 ? 69.752  66.652  33.631 1.00 161.48 ? 265 GLU B CA  1 
ATOM   1983 C C   . GLU B 2 265 ? 71.214  66.189  33.582 1.00 183.01 ? 265 GLU B C   1 
ATOM   1984 O O   . GLU B 2 265 ? 71.960  66.624  32.692 1.00 216.01 ? 265 GLU B O   1 
ATOM   1985 C CB  . GLU B 2 265 ? 69.671  68.156  33.393 1.00 215.16 ? 265 GLU B CB  1 
ATOM   1986 C CG  . GLU B 2 265 ? 68.281  68.625  33.042 1.00 284.84 ? 265 GLU B CG  1 
ATOM   1987 C CD  . GLU B 2 265 ? 68.235  70.126  32.818 1.00 310.09 ? 265 GLU B CD  1 
ATOM   1988 O OE1 . GLU B 2 265 ? 68.752  70.618  31.794 1.00 352.87 ? 265 GLU B OE1 1 
ATOM   1989 O OE2 . GLU B 2 265 ? 67.700  70.820  33.680 1.00 296.36 ? 265 GLU B OE2 1 
ATOM   1990 N N   . GLU B 2 266 ? 71.627  65.310  34.515 1.00 147.60 ? 266 GLU B N   1 
ATOM   1991 C CA  . GLU B 2 266 ? 72.999  64.819  34.598 1.00 148.32 ? 266 GLU B CA  1 
ATOM   1992 C C   . GLU B 2 266 ? 73.065  63.279  34.726 1.00 176.98 ? 266 GLU B C   1 
ATOM   1993 O O   . GLU B 2 266 ? 74.152  62.708  34.577 1.00 125.60 ? 266 GLU B O   1 
ATOM   1994 C CB  . GLU B 2 266 ? 73.659  65.643  35.704 1.00 145.82 ? 266 GLU B CB  1 
ATOM   1995 C CG  . GLU B 2 266 ? 75.178  65.590  35.716 1.00 230.65 ? 266 GLU B CG  1 
ATOM   1996 C CD  . GLU B 2 266 ? 75.870  66.744  36.447 1.00 228.73 ? 266 GLU B CD  1 
ATOM   1997 O OE1 . GLU B 2 266 ? 75.163  67.630  36.995 1.00 188.74 ? 266 GLU B OE1 1 
ATOM   1998 O OE2 . GLU B 2 266 ? 77.132  66.787  36.490 1.00 160.55 ? 266 GLU B OE2 1 
ATOM   1999 N N   . MET B 2 267 ? 71.934  62.585  34.949 1.00 169.97 ? 267 MET B N   1 
ATOM   2000 C CA  . MET B 2 267 ? 71.839  61.134  34.834 1.00 185.33 ? 267 MET B CA  1 
ATOM   2001 C C   . MET B 2 267 ? 71.791  60.635  33.385 1.00 192.61 ? 267 MET B C   1 
ATOM   2002 O O   . MET B 2 267 ? 71.271  61.322  32.519 1.00 205.44 ? 267 MET B O   1 
ATOM   2003 C CB  . MET B 2 267 ? 70.591  60.657  35.570 1.00 168.33 ? 267 MET B CB  1 
ATOM   2004 C CG  . MET B 2 267 ? 70.841  60.521  37.061 1.00 181.42 ? 267 MET B CG  1 
ATOM   2005 S SD  . MET B 2 267 ? 69.416  59.868  37.974 1.00 159.31 ? 267 MET B SD  1 
ATOM   2006 C CE  . MET B 2 267 ? 68.421  61.357  37.973 1.00 142.43 ? 267 MET B CE  1 
ATOM   2007 N N   . ILE B 2 268 ? 72.309  59.416  33.130 1.00 150.34 ? 268 ILE B N   1 
ATOM   2008 C CA  . ILE B 2 268 ? 72.484  58.933  31.758 1.00 180.73 ? 268 ILE B CA  1 
ATOM   2009 C C   . ILE B 2 268 ? 71.161  58.514  31.103 1.00 231.19 ? 268 ILE B C   1 
ATOM   2010 O O   . ILE B 2 268 ? 71.077  58.498  29.866 1.00 315.88 ? 268 ILE B O   1 
ATOM   2011 C CB  . ILE B 2 268 ? 73.512  57.785  31.662 1.00 185.39 ? 268 ILE B CB  1 
ATOM   2012 C CG1 . ILE B 2 268 ? 73.076  56.502  32.380 1.00 218.79 ? 268 ILE B CG1 1 
ATOM   2013 C CG2 . ILE B 2 268 ? 74.877  58.274  32.122 1.00 204.75 ? 268 ILE B CG2 1 
ATOM   2014 C CD1 . ILE B 2 268 ? 73.817  55.248  31.906 1.00 252.01 ? 268 ILE B CD1 1 
ATOM   2015 N N   . ASN B 2 269 ? 70.133  58.176  31.907 1.00 169.69 ? 269 ASN B N   1 
ATOM   2016 C CA  . ASN B 2 269 ? 68.838  57.739  31.384 1.00 204.98 ? 269 ASN B CA  1 
ATOM   2017 C C   . ASN B 2 269 ? 67.748  58.062  32.414 1.00 143.15 ? 269 ASN B C   1 
ATOM   2018 O O   . ASN B 2 269 ? 67.344  57.184  33.180 1.00 144.01 ? 269 ASN B O   1 
ATOM   2019 C CB  . ASN B 2 269 ? 68.913  56.261  30.983 1.00 231.81 ? 269 ASN B CB  1 
ATOM   2020 C CG  . ASN B 2 269 ? 67.659  55.728  30.321 1.00 278.48 ? 269 ASN B CG  1 
ATOM   2021 O OD1 . ASN B 2 269 ? 66.691  56.452  30.075 1.00 248.35 ? 269 ASN B OD1 1 
ATOM   2022 N ND2 . ASN B 2 269 ? 67.677  54.439  30.021 1.00 300.20 ? 269 ASN B ND2 1 
ATOM   2023 N N   . PRO B 2 270 ? 67.269  59.321  32.499 1.00 133.53 ? 270 PRO B N   1 
ATOM   2024 C CA  . PRO B 2 270 ? 66.485  59.746  33.649 1.00 138.18 ? 270 PRO B CA  1 
ATOM   2025 C C   . PRO B 2 270 ? 65.164  59.008  33.798 1.00 141.16 ? 270 PRO B C   1 
ATOM   2026 O O   . PRO B 2 270 ? 64.780  58.745  34.940 1.00 220.02 ? 270 PRO B O   1 
ATOM   2027 C CB  . PRO B 2 270 ? 66.273  61.263  33.453 1.00 188.75 ? 270 PRO B CB  1 
ATOM   2028 C CG  . PRO B 2 270 ? 66.494  61.481  31.978 1.00 214.82 ? 270 PRO B CG  1 
ATOM   2029 C CD  . PRO B 2 270 ? 67.478  60.415  31.537 1.00 182.65 ? 270 PRO B CD  1 
ATOM   2030 N N   . TYR B 2 271 ? 64.476  58.664  32.699 1.00 167.28 ? 271 TYR B N   1 
ATOM   2031 C CA  . TYR B 2 271 ? 63.141  58.082  32.798 1.00 213.13 ? 271 TYR B CA  1 
ATOM   2032 C C   . TYR B 2 271 ? 63.158  56.690  33.446 1.00 186.67 ? 271 TYR B C   1 
ATOM   2033 O O   . TYR B 2 271 ? 62.143  56.275  34.017 1.00 159.21 ? 271 TYR B O   1 
ATOM   2034 C CB  . TYR B 2 271 ? 62.514  58.068  31.400 1.00 252.23 ? 271 TYR B CB  1 
ATOM   2035 C CG  . TYR B 2 271 ? 62.304  59.472  30.859 1.00 241.45 ? 271 TYR B CG  1 
ATOM   2036 C CD1 . TYR B 2 271 ? 61.359  60.325  31.422 1.00 223.77 ? 271 TYR B CD1 1 
ATOM   2037 C CD2 . TYR B 2 271 ? 63.066  59.956  29.800 1.00 303.67 ? 271 TYR B CD2 1 
ATOM   2038 C CE1 . TYR B 2 271 ? 61.168  61.613  30.935 1.00 327.23 ? 271 TYR B CE1 1 
ATOM   2039 C CE2 . TYR B 2 271 ? 62.882  61.244  29.304 1.00 349.50 ? 271 TYR B CE2 1 
ATOM   2040 C CZ  . TYR B 2 271 ? 61.931  62.080  29.874 1.00 353.23 ? 271 TYR B CZ  1 
ATOM   2041 O OH  . TYR B 2 271 ? 61.738  63.352  29.397 1.00 360.81 ? 271 TYR B OH  1 
ATOM   2042 N N   . ARG B 2 272 ? 64.285  55.963  33.358 1.00 151.27 ? 272 ARG B N   1 
ATOM   2043 C CA  . ARG B 2 272 ? 64.502  54.748  34.134 1.00 191.26 ? 272 ARG B CA  1 
ATOM   2044 C C   . ARG B 2 272 ? 65.153  55.080  35.484 1.00 203.09 ? 272 ARG B C   1 
ATOM   2045 O O   . ARG B 2 272 ? 64.652  54.678  36.522 1.00 167.89 ? 272 ARG B O   1 
ATOM   2046 C CB  . ARG B 2 272 ? 65.367  53.779  33.316 1.00 219.85 ? 272 ARG B CB  1 
ATOM   2047 C CG  . ARG B 2 272 ? 65.722  52.485  34.029 1.00 229.25 ? 272 ARG B CG  1 
ATOM   2048 C CD  . ARG B 2 272 ? 66.675  51.619  33.222 1.00 214.09 ? 272 ARG B CD  1 
ATOM   2049 N NE  . ARG B 2 272 ? 67.269  50.525  33.992 1.00 256.38 ? 272 ARG B NE  1 
ATOM   2050 C CZ  . ARG B 2 272 ? 66.682  49.364  34.312 1.00 282.60 ? 272 ARG B CZ  1 
ATOM   2051 N NH1 . ARG B 2 272 ? 67.308  48.506  35.105 1.00 272.47 ? 272 ARG B NH1 1 
ATOM   2052 N NH2 . ARG B 2 272 ? 65.482  49.051  33.839 1.00 248.80 ? 272 ARG B NH2 1 
ATOM   2053 N N   . ASN B 2 273 ? 66.283  55.789  35.488 1.00 184.59 ? 273 ASN B N   1 
ATOM   2054 C CA  . ASN B 2 273 ? 67.186  55.787  36.633 1.00 153.39 ? 273 ASN B CA  1 
ATOM   2055 C C   . ASN B 2 273 ? 66.723  56.725  37.749 1.00 129.40 ? 273 ASN B C   1 
ATOM   2056 O O   . ASN B 2 273 ? 67.027  56.451  38.895 1.00 206.26 ? 273 ASN B O   1 
ATOM   2057 C CB  . ASN B 2 273 ? 68.633  56.099  36.221 1.00 177.23 ? 273 ASN B CB  1 
ATOM   2058 C CG  . ASN B 2 273 ? 69.262  55.074  35.304 1.00 194.31 ? 273 ASN B CG  1 
ATOM   2059 O OD1 . ASN B 2 273 ? 68.657  54.058  34.961 1.00 153.33 ? 273 ASN B OD1 1 
ATOM   2060 N ND2 . ASN B 2 273 ? 70.497  55.345  34.909 1.00 224.13 ? 273 ASN B ND2 1 
ATOM   2061 N N   . LEU B 2 274 ? 65.999  57.810  37.493 1.00 96.44  ? 274 LEU B N   1 
ATOM   2062 C CA  . LEU B 2 274 ? 65.470  58.631  38.581 1.00 107.10 ? 274 LEU B CA  1 
ATOM   2063 C C   . LEU B 2 274 ? 64.443  57.860  39.421 1.00 128.27 ? 274 LEU B C   1 
ATOM   2064 O O   . LEU B 2 274 ? 64.632  57.763  40.629 1.00 166.16 ? 274 LEU B O   1 
ATOM   2065 C CB  . LEU B 2 274 ? 64.865  59.942  38.046 1.00 115.91 ? 274 LEU B CB  1 
ATOM   2066 C CG  . LEU B 2 274 ? 64.064  60.792  39.040 1.00 123.66 ? 274 LEU B CG  1 
ATOM   2067 C CD1 . LEU B 2 274 ? 64.949  61.392  40.123 1.00 145.19 ? 274 LEU B CD1 1 
ATOM   2068 C CD2 . LEU B 2 274 ? 63.316  61.887  38.305 1.00 170.67 ? 274 LEU B CD2 1 
ATOM   2069 N N   . PRO B 2 275 ? 63.326  57.314  38.880 1.00 114.06 ? 275 PRO B N   1 
ATOM   2070 C CA  . PRO B 2 275 ? 62.351  56.623  39.696 1.00 128.39 ? 275 PRO B CA  1 
ATOM   2071 C C   . PRO B 2 275 ? 62.903  55.316  40.264 1.00 139.83 ? 275 PRO B C   1 
ATOM   2072 O O   . PRO B 2 275 ? 62.517  54.956  41.371 1.00 151.13 ? 275 PRO B O   1 
ATOM   2073 C CB  . PRO B 2 275 ? 61.163  56.415  38.750 1.00 154.86 ? 275 PRO B CB  1 
ATOM   2074 C CG  . PRO B 2 275 ? 61.793  56.298  37.419 1.00 186.15 ? 275 PRO B CG  1 
ATOM   2075 C CD  . PRO B 2 275 ? 62.896  57.321  37.486 1.00 150.11 ? 275 PRO B CD  1 
ATOM   2076 N N   . LEU B 2 276 ? 63.796  54.631  39.544 1.00 113.31 ? 276 LEU B N   1 
ATOM   2077 C CA  . LEU B 2 276 ? 64.425  53.431  40.063 1.00 158.63 ? 276 LEU B CA  1 
ATOM   2078 C C   . LEU B 2 276 ? 65.356  53.756  41.241 1.00 155.61 ? 276 LEU B C   1 
ATOM   2079 O O   . LEU B 2 276 ? 65.310  53.072  42.251 1.00 159.53 ? 276 LEU B O   1 
ATOM   2080 C CB  . LEU B 2 276 ? 65.148  52.700  38.925 1.00 155.22 ? 276 LEU B CB  1 
ATOM   2081 C CG  . LEU B 2 276 ? 65.780  51.351  39.279 1.00 196.64 ? 276 LEU B CG  1 
ATOM   2082 C CD1 . LEU B 2 276 ? 64.785  50.355  39.853 1.00 264.69 ? 276 LEU B CD1 1 
ATOM   2083 C CD2 . LEU B 2 276 ? 66.414  50.745  38.036 1.00 224.55 ? 276 LEU B CD2 1 
ATOM   2084 N N   . ALA B 2 277 ? 66.203  54.781  41.157 1.00 161.32 ? 277 ALA B N   1 
ATOM   2085 C CA  . ALA B 2 277 ? 67.117  55.129  42.241 1.00 176.00 ? 277 ALA B CA  1 
ATOM   2086 C C   . ALA B 2 277 ? 66.372  55.522  43.508 1.00 130.73 ? 277 ALA B C   1 
ATOM   2087 O O   . ALA B 2 277 ? 66.818  55.112  44.588 1.00 144.15 ? 277 ALA B O   1 
ATOM   2088 C CB  . ALA B 2 277 ? 68.071  56.216  41.806 1.00 215.08 ? 277 ALA B CB  1 
ATOM   2089 N N   . ILE B 2 278 ? 65.260  56.271  43.378 1.00 84.81  ? 278 ILE B N   1 
ATOM   2090 C CA  . ILE B 2 278 ? 64.394  56.565  44.521 1.00 91.19  ? 278 ILE B CA  1 
ATOM   2091 C C   . ILE B 2 278 ? 63.894  55.278  45.202 1.00 105.33 ? 278 ILE B C   1 
ATOM   2092 O O   . ILE B 2 278 ? 64.107  55.107  46.397 1.00 128.24 ? 278 ILE B O   1 
ATOM   2093 C CB  . ILE B 2 278 ? 63.215  57.464  44.133 1.00 104.03 ? 278 ILE B CB  1 
ATOM   2094 C CG1 . ILE B 2 278 ? 63.657  58.872  43.723 1.00 121.75 ? 278 ILE B CG1 1 
ATOM   2095 C CG2 . ILE B 2 278 ? 62.177  57.493  45.262 1.00 76.51  ? 278 ILE B CG2 1 
ATOM   2096 C CD1 . ILE B 2 278 ? 63.802  59.826  44.856 1.00 162.52 ? 278 ILE B CD1 1 
ATOM   2097 N N   . ILE B 2 279 ? 63.234  54.383  44.470 1.00 113.03 ? 279 ILE B N   1 
ATOM   2098 C CA  . ILE B 2 279 ? 62.532  53.271  45.105 1.00 141.02 ? 279 ILE B CA  1 
ATOM   2099 C C   . ILE B 2 279 ? 63.486  52.123  45.491 1.00 114.83 ? 279 ILE B C   1 
ATOM   2100 O O   . ILE B 2 279 ? 63.128  51.324  46.355 1.00 170.78 ? 279 ILE B O   1 
ATOM   2101 C CB  . ILE B 2 279 ? 61.331  52.810  44.238 1.00 190.93 ? 279 ILE B CB  1 
ATOM   2102 C CG1 . ILE B 2 279 ? 60.319  51.938  45.001 1.00 250.05 ? 279 ILE B CG1 1 
ATOM   2103 C CG2 . ILE B 2 279 ? 61.772  52.059  42.994 1.00 223.81 ? 279 ILE B CG2 1 
ATOM   2104 C CD1 . ILE B 2 279 ? 59.758  52.511  46.292 1.00 241.65 ? 279 ILE B CD1 1 
ATOM   2105 N N   . ILE B 2 280 ? 64.675  51.999  44.888 1.00 111.31 ? 280 ILE B N   1 
ATOM   2106 C CA  . ILE B 2 280 ? 65.728  51.147  45.422 1.00 151.92 ? 280 ILE B CA  1 
ATOM   2107 C C   . ILE B 2 280 ? 66.236  51.711  46.755 1.00 178.95 ? 280 ILE B C   1 
ATOM   2108 O O   . ILE B 2 280 ? 66.422  50.971  47.717 1.00 181.45 ? 280 ILE B O   1 
ATOM   2109 C CB  . ILE B 2 280 ? 66.883  50.954  44.408 1.00 165.11 ? 280 ILE B CB  1 
ATOM   2110 C CG1 . ILE B 2 280 ? 66.426  50.200  43.150 1.00 255.01 ? 280 ILE B CG1 1 
ATOM   2111 C CG2 . ILE B 2 280 ? 68.099  50.261  45.056 1.00 125.11 ? 280 ILE B CG2 1 
ATOM   2112 C CD1 . ILE B 2 280 ? 66.048  48.735  43.366 1.00 345.97 ? 280 ILE B CD1 1 
ATOM   2113 N N   . SER B 2 281 ? 66.468  53.025  46.804 1.00 172.98 ? 281 SER B N   1 
ATOM   2114 C CA  . SER B 2 281 ? 67.136  53.668  47.921 1.00 164.27 ? 281 SER B CA  1 
ATOM   2115 C C   . SER B 2 281 ? 66.290  53.731  49.198 1.00 132.01 ? 281 SER B C   1 
ATOM   2116 O O   . SER B 2 281 ? 66.751  53.279  50.244 1.00 237.99 ? 281 SER B O   1 
ATOM   2117 C CB  . SER B 2 281 ? 67.605  55.033  47.525 1.00 159.04 ? 281 SER B CB  1 
ATOM   2118 O OG  . SER B 2 281 ? 68.199  55.684  48.637 1.00 153.45 ? 281 SER B OG  1 
ATOM   2119 N N   . LEU B 2 282 ? 65.085  54.292  49.182 1.00 93.44  ? 282 LEU B N   1 
ATOM   2120 C CA  . LEU B 2 282 ? 64.442  54.629  50.453 1.00 132.79 ? 282 LEU B CA  1 
ATOM   2121 C C   . LEU B 2 282 ? 63.971  53.424  51.298 1.00 165.42 ? 282 LEU B C   1 
ATOM   2122 O O   . LEU B 2 282 ? 64.013  53.493  52.534 1.00 176.12 ? 282 LEU B O   1 
ATOM   2123 C CB  . LEU B 2 282 ? 63.288  55.606  50.220 1.00 119.29 ? 282 LEU B CB  1 
ATOM   2124 C CG  . LEU B 2 282 ? 63.707  57.024  50.503 1.00 135.62 ? 282 LEU B CG  1 
ATOM   2125 C CD1 . LEU B 2 282 ? 64.502  57.544  49.325 1.00 104.66 ? 282 LEU B CD1 1 
ATOM   2126 C CD2 . LEU B 2 282 ? 62.466  57.817  50.866 1.00 169.02 ? 282 LEU B CD2 1 
ATOM   2127 N N   . PRO B 2 283 ? 63.500  52.299  50.726 1.00 129.94 ? 283 PRO B N   1 
ATOM   2128 C CA  . PRO B 2 283 ? 63.365  51.063  51.484 1.00 166.04 ? 283 PRO B CA  1 
ATOM   2129 C C   . PRO B 2 283 ? 64.667  50.583  52.134 1.00 148.66 ? 283 PRO B C   1 
ATOM   2130 O O   . PRO B 2 283 ? 64.609  50.140  53.278 1.00 161.00 ? 283 PRO B O   1 
ATOM   2131 C CB  . PRO B 2 283 ? 62.825  50.078  50.432 1.00 224.96 ? 283 PRO B CB  1 
ATOM   2132 C CG  . PRO B 2 283 ? 62.066  50.994  49.501 1.00 212.59 ? 283 PRO B CG  1 
ATOM   2133 C CD  . PRO B 2 283 ? 63.014  52.162  49.361 1.00 141.76 ? 283 PRO B CD  1 
ATOM   2134 N N   . ILE B 2 284 ? 65.824  50.661  51.454 1.00 104.01 ? 284 ILE B N   1 
ATOM   2135 C CA  . ILE B 2 284 ? 67.099  50.330  52.086 1.00 128.53 ? 284 ILE B CA  1 
ATOM   2136 C C   . ILE B 2 284 ? 67.354  51.227  53.308 1.00 120.74 ? 284 ILE B C   1 
ATOM   2137 O O   . ILE B 2 284 ? 67.658  50.746  54.382 1.00 123.25 ? 284 ILE B O   1 
ATOM   2138 C CB  . ILE B 2 284 ? 68.262  50.371  51.072 1.00 128.39 ? 284 ILE B CB  1 
ATOM   2139 C CG1 . ILE B 2 284 ? 68.124  49.177  50.127 1.00 216.15 ? 284 ILE B CG1 1 
ATOM   2140 C CG2 . ILE B 2 284 ? 69.643  50.436  51.730 1.00 160.89 ? 284 ILE B CG2 1 
ATOM   2141 C CD1 . ILE B 2 284 ? 69.089  49.176  48.960 1.00 302.87 ? 284 ILE B CD1 1 
ATOM   2142 N N   . VAL B 2 285 ? 67.221  52.538  53.158 1.00 139.80 ? 285 VAL B N   1 
ATOM   2143 C CA  . VAL B 2 285 ? 67.416  53.479  54.247 1.00 107.87 ? 285 VAL B CA  1 
ATOM   2144 C C   . VAL B 2 285 ? 66.483  53.157  55.403 1.00 118.12 ? 285 VAL B C   1 
ATOM   2145 O O   . VAL B 2 285 ? 66.955  53.044  56.529 1.00 161.74 ? 285 VAL B O   1 
ATOM   2146 C CB  . VAL B 2 285 ? 67.231  54.929  53.777 1.00 121.65 ? 285 VAL B CB  1 
ATOM   2147 C CG1 . VAL B 2 285 ? 67.203  55.888  54.929 1.00 149.46 ? 285 VAL B CG1 1 
ATOM   2148 C CG2 . VAL B 2 285 ? 68.332  55.361  52.801 1.00 163.71 ? 285 VAL B CG2 1 
ATOM   2149 N N   . THR B 2 286 ? 65.177  52.994  55.158 1.00 127.14 ? 286 THR B N   1 
ATOM   2150 C CA  . THR B 2 286 ? 64.222  52.729  56.236 1.00 137.38 ? 286 THR B CA  1 
ATOM   2151 C C   . THR B 2 286 ? 64.565  51.441  56.997 1.00 125.07 ? 286 THR B C   1 
ATOM   2152 O O   . THR B 2 286 ? 64.526  51.426  58.233 1.00 106.07 ? 286 THR B O   1 
ATOM   2153 C CB  . THR B 2 286 ? 62.775  52.650  55.739 1.00 153.77 ? 286 THR B CB  1 
ATOM   2154 O OG1 . THR B 2 286 ? 62.446  53.851  55.053 1.00 181.02 ? 286 THR B OG1 1 
ATOM   2155 C CG2 . THR B 2 286 ? 61.773  52.459  56.863 1.00 134.91 ? 286 THR B CG2 1 
ATOM   2156 N N   . LEU B 2 287 ? 64.908  50.367  56.272 1.00 114.72 ? 287 LEU B N   1 
ATOM   2157 C CA  . LEU B 2 287 ? 65.314  49.117  56.886 1.00 139.59 ? 287 LEU B CA  1 
ATOM   2158 C C   . LEU B 2 287 ? 66.555  49.323  57.769 1.00 148.89 ? 287 LEU B C   1 
ATOM   2159 O O   . LEU B 2 287 ? 66.559  48.912  58.939 1.00 195.54 ? 287 LEU B O   1 
ATOM   2160 C CB  . LEU B 2 287 ? 65.571  48.085  55.780 1.00 147.66 ? 287 LEU B CB  1 
ATOM   2161 C CG  . LEU B 2 287 ? 66.085  46.724  56.259 1.00 208.01 ? 287 LEU B CG  1 
ATOM   2162 C CD1 . LEU B 2 287 ? 64.998  46.011  57.053 1.00 311.29 ? 287 LEU B CD1 1 
ATOM   2163 C CD2 . LEU B 2 287 ? 66.583  45.882  55.106 1.00 244.48 ? 287 LEU B CD2 1 
ATOM   2164 N N   . VAL B 2 288 ? 67.612  49.947  57.231 1.00 118.82 ? 288 VAL B N   1 
ATOM   2165 C CA  . VAL B 2 288 ? 68.850  50.160  57.962 1.00 123.54 ? 288 VAL B CA  1 
ATOM   2166 C C   . VAL B 2 288 ? 68.578  50.963  59.232 1.00 113.12 ? 288 VAL B C   1 
ATOM   2167 O O   . VAL B 2 288 ? 69.140  50.668  60.278 1.00 140.93 ? 288 VAL B O   1 
ATOM   2168 C CB  . VAL B 2 288 ? 69.908  50.814  57.055 1.00 129.56 ? 288 VAL B CB  1 
ATOM   2169 C CG1 . VAL B 2 288 ? 71.078  51.428  57.810 1.00 150.95 ? 288 VAL B CG1 1 
ATOM   2170 C CG2 . VAL B 2 288 ? 70.408  49.793  56.057 1.00 169.94 ? 288 VAL B CG2 1 
ATOM   2171 N N   . TYR B 2 289 ? 67.719  51.975  59.155 1.00 117.72 ? 289 TYR B N   1 
ATOM   2172 C CA  . TYR B 2 289 ? 67.411  52.830  60.295 1.00 135.51 ? 289 TYR B CA  1 
ATOM   2173 C C   . TYR B 2 289 ? 66.634  52.122  61.402 1.00 118.63 ? 289 TYR B C   1 
ATOM   2174 O O   . TYR B 2 289 ? 66.990  52.313  62.562 1.00 136.06 ? 289 TYR B O   1 
ATOM   2175 C CB  . TYR B 2 289 ? 66.669  54.056  59.766 1.00 111.83 ? 289 TYR B CB  1 
ATOM   2176 C CG  . TYR B 2 289 ? 67.559  55.167  59.258 1.00 104.95 ? 289 TYR B CG  1 
ATOM   2177 C CD1 . TYR B 2 289 ? 68.915  54.969  58.939 1.00 93.49  ? 289 TYR B CD1 1 
ATOM   2178 C CD2 . TYR B 2 289 ? 67.003  56.447  59.125 1.00 131.48 ? 289 TYR B CD2 1 
ATOM   2179 C CE1 . TYR B 2 289 ? 69.680  56.050  58.515 1.00 165.56 ? 289 TYR B CE1 1 
ATOM   2180 C CE2 . TYR B 2 289 ? 67.759  57.515  58.691 1.00 126.11 ? 289 TYR B CE2 1 
ATOM   2181 C CZ  . TYR B 2 289 ? 69.106  57.318  58.394 1.00 168.45 ? 289 TYR B CZ  1 
ATOM   2182 O OH  . TYR B 2 289 ? 69.875  58.377  57.984 1.00 89.11  ? 289 TYR B OH  1 
ATOM   2183 N N   . VAL B 2 290 ? 65.602  51.323  61.099 1.00 103.70 ? 290 VAL B N   1 
ATOM   2184 C CA  . VAL B 2 290 ? 64.890  50.638  62.163 1.00 121.98 ? 290 VAL B CA  1 
ATOM   2185 C C   . VAL B 2 290 ? 65.761  49.543  62.780 1.00 113.72 ? 290 VAL B C   1 
ATOM   2186 O O   . VAL B 2 290 ? 65.758  49.428  64.023 1.00 183.59 ? 290 VAL B O   1 
ATOM   2187 C CB  . VAL B 2 290 ? 63.510  50.124  61.751 1.00 169.42 ? 290 VAL B CB  1 
ATOM   2188 C CG1 . VAL B 2 290 ? 62.633  51.323  61.386 1.00 133.45 ? 290 VAL B CG1 1 
ATOM   2189 C CG2 . VAL B 2 290 ? 63.583  49.021  60.676 1.00 210.16 ? 290 VAL B CG2 1 
ATOM   2190 N N   . LEU B 2 291 ? 66.509  48.795  61.975 1.00 85.72  ? 291 LEU B N   1 
ATOM   2191 C CA  . LEU B 2 291 ? 67.445  47.831  62.553 1.00 139.72 ? 291 LEU B CA  1 
ATOM   2192 C C   . LEU B 2 291 ? 68.578  48.481  63.384 1.00 145.36 ? 291 LEU B C   1 
ATOM   2193 O O   . LEU B 2 291 ? 69.000  47.924  64.399 1.00 151.15 ? 291 LEU B O   1 
ATOM   2194 C CB  . LEU B 2 291 ? 68.013  46.965  61.429 1.00 136.22 ? 291 LEU B CB  1 
ATOM   2195 C CG  . LEU B 2 291 ? 67.009  46.094  60.681 1.00 164.07 ? 291 LEU B CG  1 
ATOM   2196 C CD1 . LEU B 2 291 ? 67.716  45.376  59.541 1.00 255.26 ? 291 LEU B CD1 1 
ATOM   2197 C CD2 . LEU B 2 291 ? 66.361  45.070  61.584 1.00 191.41 ? 291 LEU B CD2 1 
ATOM   2198 N N   . THR B 2 292 ? 69.082  49.651  62.987 1.00 125.12 ? 292 THR B N   1 
ATOM   2199 C CA  . THR B 2 292 ? 70.095  50.352  63.763 1.00 132.54 ? 292 THR B CA  1 
ATOM   2200 C C   . THR B 2 292 ? 69.545  50.828  65.101 1.00 107.73 ? 292 THR B C   1 
ATOM   2201 O O   . THR B 2 292 ? 70.200  50.639  66.135 1.00 156.59 ? 292 THR B O   1 
ATOM   2202 C CB  . THR B 2 292 ? 70.693  51.533  62.996 1.00 150.35 ? 292 THR B CB  1 
ATOM   2203 O OG1 . THR B 2 292 ? 71.294  51.012  61.815 1.00 176.29 ? 292 THR B OG1 1 
ATOM   2204 C CG2 . THR B 2 292 ? 71.756  52.297  63.765 1.00 135.64 ? 292 THR B CG2 1 
ATOM   2205 N N   . ASN B 2 293 ? 68.362  51.419  65.113 1.00 88.46  ? 293 ASN B N   1 
ATOM   2206 C CA  . ASN B 2 293 ? 67.741  51.741  66.385 1.00 117.02 ? 293 ASN B CA  1 
ATOM   2207 C C   . ASN B 2 293 ? 67.492  50.500  67.254 1.00 132.72 ? 293 ASN B C   1 
ATOM   2208 O O   . ASN B 2 293 ? 67.749  50.547  68.460 1.00 148.71 ? 293 ASN B O   1 
ATOM   2209 C CB  . ASN B 2 293 ? 66.461  52.531  66.172 1.00 135.44 ? 293 ASN B CB  1 
ATOM   2210 C CG  . ASN B 2 293 ? 66.799  53.963  65.884 1.00 129.15 ? 293 ASN B CG  1 
ATOM   2211 O OD1 . ASN B 2 293 ? 66.968  54.733  66.812 1.00 137.69 ? 293 ASN B OD1 1 
ATOM   2212 N ND2 . ASN B 2 293 ? 66.880  54.325  64.619 1.00 175.79 ? 293 ASN B ND2 1 
ATOM   2213 N N   . LEU B 2 294 ? 67.007  49.397  66.666 1.00 139.63 ? 294 LEU B N   1 
ATOM   2214 C CA  . LEU B 2 294 ? 66.885  48.138  67.387 1.00 189.46 ? 294 LEU B CA  1 
ATOM   2215 C C   . LEU B 2 294 ? 68.219  47.793  68.069 1.00 194.32 ? 294 LEU B C   1 
ATOM   2216 O O   . LEU B 2 294 ? 68.216  47.460  69.259 1.00 188.97 ? 294 LEU B O   1 
ATOM   2217 C CB  . LEU B 2 294 ? 66.391  47.045  66.427 1.00 203.30 ? 294 LEU B CB  1 
ATOM   2218 C CG  . LEU B 2 294 ? 66.406  45.617  66.976 1.00 273.01 ? 294 LEU B CG  1 
ATOM   2219 C CD1 . LEU B 2 294 ? 65.330  45.478  68.035 1.00 354.92 ? 294 LEU B CD1 1 
ATOM   2220 C CD2 . LEU B 2 294 ? 66.247  44.584  65.880 1.00 267.39 ? 294 LEU B CD2 1 
ATOM   2221 N N   . ALA B 2 295 ? 69.352  47.888  67.346 1.00 138.11 ? 295 ALA B N   1 
ATOM   2222 C CA  . ALA B 2 295 ? 70.659  47.632  67.937 1.00 143.31 ? 295 ALA B CA  1 
ATOM   2223 C C   . ALA B 2 295 ? 70.918  48.537  69.152 1.00 134.43 ? 295 ALA B C   1 
ATOM   2224 O O   . ALA B 2 295 ? 71.204  48.016  70.230 1.00 190.58 ? 295 ALA B O   1 
ATOM   2225 C CB  . ALA B 2 295 ? 71.724  47.735  66.875 1.00 144.62 ? 295 ALA B CB  1 
ATOM   2226 N N   . TYR B 2 296 ? 70.787  49.863  69.031 1.00 144.81 ? 296 TYR B N   1 
ATOM   2227 C CA  . TYR B 2 296 ? 71.000  50.773  70.160 1.00 161.31 ? 296 TYR B CA  1 
ATOM   2228 C C   . TYR B 2 296 ? 70.138  50.404  71.375 1.00 178.63 ? 296 TYR B C   1 
ATOM   2229 O O   . TYR B 2 296 ? 70.643  50.338  72.491 1.00 192.99 ? 296 TYR B O   1 
ATOM   2230 C CB  . TYR B 2 296 ? 70.704  52.235  69.812 1.00 177.30 ? 296 TYR B CB  1 
ATOM   2231 C CG  . TYR B 2 296 ? 71.515  52.883  68.702 1.00 168.07 ? 296 TYR B CG  1 
ATOM   2232 C CD1 . TYR B 2 296 ? 72.871  52.587  68.517 1.00 134.07 ? 296 TYR B CD1 1 
ATOM   2233 C CD2 . TYR B 2 296 ? 70.912  53.809  67.852 1.00 142.48 ? 296 TYR B CD2 1 
ATOM   2234 C CE1 . TYR B 2 296 ? 73.610  53.187  67.513 1.00 125.91 ? 296 TYR B CE1 1 
ATOM   2235 C CE2 . TYR B 2 296 ? 71.652  54.410  66.846 1.00 184.00 ? 296 TYR B CE2 1 
ATOM   2236 C CZ  . TYR B 2 296 ? 72.994  54.099  66.666 1.00 179.69 ? 296 TYR B CZ  1 
ATOM   2237 O OH  . TYR B 2 296 ? 73.671  54.715  65.646 1.00 205.04 ? 296 TYR B OH  1 
ATOM   2238 N N   . PHE B 2 297 ? 68.843  50.133  71.173 1.00 153.80 ? 297 PHE B N   1 
ATOM   2239 C CA  . PHE B 2 297 ? 67.978  49.750  72.277 1.00 140.58 ? 297 PHE B CA  1 
ATOM   2240 C C   . PHE B 2 297 ? 68.247  48.334  72.835 1.00 177.05 ? 297 PHE B C   1 
ATOM   2241 O O   . PHE B 2 297 ? 67.817  48.057  73.950 1.00 212.87 ? 297 PHE B O   1 
ATOM   2242 C CB  . PHE B 2 297 ? 66.534  49.870  71.837 1.00 157.69 ? 297 PHE B CB  1 
ATOM   2243 C CG  . PHE B 2 297 ? 66.047  51.275  71.632 1.00 147.33 ? 297 PHE B CG  1 
ATOM   2244 C CD1 . PHE B 2 297 ? 66.035  52.150  72.681 1.00 141.26 ? 297 PHE B CD1 1 
ATOM   2245 C CD2 . PHE B 2 297 ? 65.544  51.706  70.400 1.00 210.37 ? 297 PHE B CD2 1 
ATOM   2246 C CE1 . PHE B 2 297 ? 65.557  53.437  72.497 1.00 168.30 ? 297 PHE B CE1 1 
ATOM   2247 C CE2 . PHE B 2 297 ? 65.067  52.998  70.216 1.00 191.94 ? 297 PHE B CE2 1 
ATOM   2248 C CZ  . PHE B 2 297 ? 65.076  53.867  71.277 1.00 177.96 ? 297 PHE B CZ  1 
ATOM   2249 N N   . THR B 2 298 ? 68.942  47.424  72.133 1.00 140.57 ? 298 THR B N   1 
ATOM   2250 C CA  . THR B 2 298 ? 69.428  46.213  72.788 1.00 148.87 ? 298 THR B CA  1 
ATOM   2251 C C   . THR B 2 298 ? 70.590  46.502  73.744 1.00 148.14 ? 298 THR B C   1 
ATOM   2252 O O   . THR B 2 298 ? 70.700  45.816  74.761 1.00 231.57 ? 298 THR B O   1 
ATOM   2253 C CB  . THR B 2 298 ? 69.849  45.095  71.817 1.00 202.86 ? 298 THR B CB  1 
ATOM   2254 O OG1 . THR B 2 298 ? 70.892  45.504  70.934 1.00 160.80 ? 298 THR B OG1 1 
ATOM   2255 C CG2 . THR B 2 298 ? 68.698  44.577  70.982 1.00 285.56 ? 298 THR B CG2 1 
ATOM   2256 N N   . THR B 2 299 ? 71.452  47.489  73.445 1.00 142.79 ? 299 THR B N   1 
ATOM   2257 C CA  . THR B 2 299 ? 72.670  47.744  74.214 1.00 154.90 ? 299 THR B CA  1 
ATOM   2258 C C   . THR B 2 299 ? 72.458  48.682  75.396 1.00 149.91 ? 299 THR B C   1 
ATOM   2259 O O   . THR B 2 299 ? 73.065  48.479  76.453 1.00 180.63 ? 299 THR B O   1 
ATOM   2260 C CB  . THR B 2 299 ? 73.785  48.330  73.344 1.00 176.43 ? 299 THR B CB  1 
ATOM   2261 O OG1 . THR B 2 299 ? 73.960  47.485  72.217 1.00 198.97 ? 299 THR B OG1 1 
ATOM   2262 C CG2 . THR B 2 299 ? 75.119  48.377  74.042 1.00 160.45 ? 299 THR B CG2 1 
ATOM   2263 N N   . LEU B 2 300 ? 71.625  49.719  75.226 1.00 137.96 ? 300 LEU B N   1 
ATOM   2264 C CA  . LEU B 2 300 ? 71.555  50.814  76.188 1.00 176.52 ? 300 LEU B CA  1 
ATOM   2265 C C   . LEU B 2 300 ? 70.166  50.918  76.829 1.00 187.04 ? 300 LEU B C   1 
ATOM   2266 O O   . LEU B 2 300 ? 69.144  50.641  76.210 1.00 258.99 ? 300 LEU B O   1 
ATOM   2267 C CB  . LEU B 2 300 ? 71.925  52.123  75.474 1.00 179.73 ? 300 LEU B CB  1 
ATOM   2268 C CG  . LEU B 2 300 ? 73.303  52.168  74.797 1.00 192.76 ? 300 LEU B CG  1 
ATOM   2269 C CD1 . LEU B 2 300 ? 73.483  53.484  74.095 1.00 200.39 ? 300 LEU B CD1 1 
ATOM   2270 C CD2 . LEU B 2 300 ? 74.470  51.959  75.747 1.00 222.84 ? 300 LEU B CD2 1 
ATOM   2271 N N   . SER B 2 301 ? 70.140  51.348  78.094 1.00 181.44 ? 301 SER B N   1 
ATOM   2272 C CA  . SER B 2 301 ? 68.924  51.779  78.776 1.00 199.86 ? 301 SER B CA  1 
ATOM   2273 C C   . SER B 2 301 ? 68.420  53.113  78.236 1.00 144.24 ? 301 SER B C   1 
ATOM   2274 O O   . SER B 2 301 ? 69.181  53.872  77.624 1.00 179.51 ? 301 SER B O   1 
ATOM   2275 C CB  . SER B 2 301 ? 69.178  51.913  80.256 1.00 279.54 ? 301 SER B CB  1 
ATOM   2276 O OG  . SER B 2 301 ? 70.145  52.928  80.509 1.00 249.81 ? 301 SER B OG  1 
ATOM   2277 N N   . THR B 2 302 ? 67.138  53.426  78.483 1.00 142.97 ? 302 THR B N   1 
ATOM   2278 C CA  . THR B 2 302 ? 66.585  54.725  78.096 1.00 191.99 ? 302 THR B CA  1 
ATOM   2279 C C   . THR B 2 302 ? 67.344  55.885  78.754 1.00 192.72 ? 302 THR B C   1 
ATOM   2280 O O   . THR B 2 302 ? 67.639  56.873  78.076 1.00 139.73 ? 302 THR B O   1 
ATOM   2281 C CB  . THR B 2 302 ? 65.077  54.831  78.374 1.00 258.43 ? 302 THR B CB  1 
ATOM   2282 O OG1 . THR B 2 302 ? 64.836  54.536  79.751 1.00 291.56 ? 302 THR B OG1 1 
ATOM   2283 C CG2 . THR B 2 302 ? 64.249  53.913  77.493 1.00 305.43 ? 302 THR B CG2 1 
ATOM   2284 N N   . GLU B 2 303 ? 67.673  55.763  80.056 1.00 231.79 ? 303 GLU B N   1 
ATOM   2285 C CA  . GLU B 2 303 ? 68.372  56.817  80.793 1.00 249.14 ? 303 GLU B CA  1 
ATOM   2286 C C   . GLU B 2 303 ? 69.788  57.064  80.237 1.00 222.60 ? 303 GLU B C   1 
ATOM   2287 O O   . GLU B 2 303 ? 70.209  58.221  80.193 1.00 208.30 ? 303 GLU B O   1 
ATOM   2288 C CB  . GLU B 2 303 ? 68.338  56.555  82.308 1.00 291.20 ? 303 GLU B CB  1 
ATOM   2289 C CG  . GLU B 2 303 ? 69.053  55.295  82.788 1.00 333.26 ? 303 GLU B CG  1 
ATOM   2290 C CD  . GLU B 2 303 ? 68.951  54.995  84.276 1.00 393.05 ? 303 GLU B CD  1 
ATOM   2291 O OE1 . GLU B 2 303 ? 68.354  55.807  85.017 1.00 432.71 ? 303 GLU B OE1 1 
ATOM   2292 O OE2 . GLU B 2 303 ? 69.472  53.942  84.695 1.00 394.58 ? 303 GLU B OE2 1 
ATOM   2293 N N   . GLN B 2 304 ? 70.517  56.025  79.785 1.00 175.60 ? 304 GLN B N   1 
ATOM   2294 C CA  . GLN B 2 304 ? 71.773  56.227  79.064 1.00 183.31 ? 304 GLN B CA  1 
ATOM   2295 C C   . GLN B 2 304 ? 71.571  57.001  77.756 1.00 190.40 ? 304 GLN B C   1 
ATOM   2296 O O   . GLN B 2 304 ? 72.242  57.998  77.518 1.00 168.03 ? 304 GLN B O   1 
ATOM   2297 C CB  . GLN B 2 304 ? 72.441  54.893  78.737 1.00 167.10 ? 304 GLN B CB  1 
ATOM   2298 C CG  . GLN B 2 304 ? 73.164  54.288  79.921 1.00 205.55 ? 304 GLN B CG  1 
ATOM   2299 C CD  . GLN B 2 304 ? 73.466  52.823  79.721 1.00 235.18 ? 304 GLN B CD  1 
ATOM   2300 O OE1 . GLN B 2 304 ? 72.550  52.015  79.591 1.00 238.85 ? 304 GLN B OE1 1 
ATOM   2301 N NE2 . GLN B 2 304 ? 74.745  52.464  79.710 1.00 240.98 ? 304 GLN B NE2 1 
ATOM   2302 N N   . MET B 2 305 ? 70.655  56.560  76.896 1.00 195.78 ? 305 MET B N   1 
ATOM   2303 C CA  . MET B 2 305 ? 70.461  57.212  75.609 1.00 175.80 ? 305 MET B CA  1 
ATOM   2304 C C   . MET B 2 305 ? 69.936  58.651  75.750 1.00 157.66 ? 305 MET B C   1 
ATOM   2305 O O   . MET B 2 305 ? 70.249  59.488  74.902 1.00 258.36 ? 305 MET B O   1 
ATOM   2306 C CB  . MET B 2 305 ? 69.509  56.385  74.742 1.00 186.68 ? 305 MET B CB  1 
ATOM   2307 C CG  . MET B 2 305 ? 70.196  55.169  74.202 1.00 165.88 ? 305 MET B CG  1 
ATOM   2308 S SD  . MET B 2 305 ? 69.151  54.148  73.144 1.00 216.98 ? 305 MET B SD  1 
ATOM   2309 C CE  . MET B 2 305 ? 68.871  55.219  71.729 1.00 226.03 ? 305 MET B CE  1 
ATOM   2310 N N   . LEU B 2 306 ? 69.161  58.940  76.802 1.00 120.73 ? 306 LEU B N   1 
ATOM   2311 C CA  . LEU B 2 306 ? 68.663  60.282  77.051 1.00 164.22 ? 306 LEU B CA  1 
ATOM   2312 C C   . LEU B 2 306 ? 69.752  61.237  77.561 1.00 162.07 ? 306 LEU B C   1 
ATOM   2313 O O   . LEU B 2 306 ? 69.576  62.458  77.420 1.00 164.87 ? 306 LEU B O   1 
ATOM   2314 C CB  . LEU B 2 306 ? 67.503  60.177  78.054 1.00 219.23 ? 306 LEU B CB  1 
ATOM   2315 C CG  . LEU B 2 306 ? 66.201  59.596  77.494 1.00 187.47 ? 306 LEU B CG  1 
ATOM   2316 C CD1 . LEU B 2 306 ? 65.252  59.142  78.583 1.00 234.52 ? 306 LEU B CD1 1 
ATOM   2317 C CD2 . LEU B 2 306 ? 65.488  60.632  76.675 1.00 190.86 ? 306 LEU B CD2 1 
ATOM   2318 N N   . SER B 2 307 ? 70.843  60.709  78.163 1.00 150.68 ? 307 SER B N   1 
ATOM   2319 C CA  . SER B 2 307 ? 71.835  61.513  78.881 1.00 224.14 ? 307 SER B CA  1 
ATOM   2320 C C   . SER B 2 307 ? 73.232  61.508  78.247 1.00 212.44 ? 307 SER B C   1 
ATOM   2321 O O   . SER B 2 307 ? 74.052  62.359  78.596 1.00 226.12 ? 307 SER B O   1 
ATOM   2322 C CB  . SER B 2 307 ? 71.910  61.078  80.325 1.00 279.27 ? 307 SER B CB  1 
ATOM   2323 O OG  . SER B 2 307 ? 72.349  59.731  80.437 1.00 266.62 ? 307 SER B OG  1 
ATOM   2324 N N   . SER B 2 308 ? 73.502  60.566  77.326 1.00 224.79 ? 308 SER B N   1 
ATOM   2325 C CA  . SER B 2 308 ? 74.755  60.493  76.580 1.00 267.30 ? 308 SER B CA  1 
ATOM   2326 C C   . SER B 2 308 ? 74.807  61.501  75.420 1.00 258.24 ? 308 SER B C   1 
ATOM   2327 O O   . SER B 2 308 ? 73.779  61.834  74.821 1.00 171.32 ? 308 SER B O   1 
ATOM   2328 C CB  . SER B 2 308 ? 74.996  59.091  76.098 1.00 252.22 ? 308 SER B CB  1 
ATOM   2329 O OG  . SER B 2 308 ? 73.875  58.569  75.412 1.00 276.66 ? 308 SER B OG  1 
ATOM   2330 N N   . GLU B 2 309 ? 76.033  61.975  75.109 1.00 286.94 ? 309 GLU B N   1 
ATOM   2331 C CA  . GLU B 2 309 ? 76.259  63.001  74.097 1.00 321.40 ? 309 GLU B CA  1 
ATOM   2332 C C   . GLU B 2 309 ? 76.313  62.405  72.684 1.00 282.99 ? 309 GLU B C   1 
ATOM   2333 O O   . GLU B 2 309 ? 76.120  63.136  71.704 1.00 302.79 ? 309 GLU B O   1 
ATOM   2334 C CB  . GLU B 2 309 ? 77.569  63.761  74.353 1.00 385.15 ? 309 GLU B CB  1 
ATOM   2335 C CG  . GLU B 2 309 ? 77.718  64.366  75.749 1.00 461.97 ? 309 GLU B CG  1 
ATOM   2336 C CD  . GLU B 2 309 ? 78.382  63.492  76.803 1.00 516.12 ? 309 GLU B CD  1 
ATOM   2337 O OE1 . GLU B 2 309 ? 78.438  62.259  76.606 1.00 532.68 ? 309 GLU B OE1 1 
ATOM   2338 O OE2 . GLU B 2 309 ? 78.844  64.049  77.819 1.00 538.75 ? 309 GLU B OE2 1 
ATOM   2339 N N   . ALA B 2 310 ? 76.585  61.092  72.561 1.00 239.40 ? 310 ALA B N   1 
ATOM   2340 C CA  . ALA B 2 310 ? 76.952  60.493  71.280 1.00 255.29 ? 310 ALA B CA  1 
ATOM   2341 C C   . ALA B 2 310 ? 76.679  58.983  71.261 1.00 164.00 ? 310 ALA B C   1 
ATOM   2342 O O   . ALA B 2 310 ? 77.545  58.185  71.577 1.00 116.33 ? 310 ALA B O   1 
ATOM   2343 C CB  . ALA B 2 310 ? 78.409  60.809  71.015 1.00 318.62 ? 310 ALA B CB  1 
ATOM   2344 N N   . VAL B 2 311 ? 75.467  58.569  70.867 1.00 129.21 ? 311 VAL B N   1 
ATOM   2345 C CA  . VAL B 2 311 ? 74.958  57.230  71.175 1.00 101.72 ? 311 VAL B CA  1 
ATOM   2346 C C   . VAL B 2 311 ? 75.832  56.143  70.555 1.00 100.83 ? 311 VAL B C   1 
ATOM   2347 O O   . VAL B 2 311 ? 76.105  55.121  71.185 1.00 121.46 ? 311 VAL B O   1 
ATOM   2348 C CB  . VAL B 2 311 ? 73.500  57.079  70.714 1.00 139.11 ? 311 VAL B CB  1 
ATOM   2349 C CG1 . VAL B 2 311 ? 72.989  55.664  70.837 1.00 115.04 ? 311 VAL B CG1 1 
ATOM   2350 C CG2 . VAL B 2 311 ? 72.571  58.002  71.471 1.00 140.12 ? 311 VAL B CG2 1 
ATOM   2351 N N   . ALA B 2 312 ? 76.308  56.365  69.330 1.00 129.53 ? 312 ALA B N   1 
ATOM   2352 C CA  . ALA B 2 312 ? 77.167  55.393  68.664 1.00 141.66 ? 312 ALA B CA  1 
ATOM   2353 C C   . ALA B 2 312 ? 78.503  55.184  69.391 1.00 144.12 ? 312 ALA B C   1 
ATOM   2354 O O   . ALA B 2 312 ? 79.075  54.101  69.312 1.00 169.54 ? 312 ALA B O   1 
ATOM   2355 C CB  . ALA B 2 312 ? 77.375  55.833  67.237 1.00 176.14 ? 312 ALA B CB  1 
ATOM   2356 N N   . VAL B 2 313 ? 79.020  56.199  70.105 1.00 143.96 ? 313 VAL B N   1 
ATOM   2357 C CA  . VAL B 2 313 ? 80.247  56.081  70.883 1.00 159.08 ? 313 VAL B CA  1 
ATOM   2358 C C   . VAL B 2 313 ? 80.031  55.158  72.086 1.00 168.14 ? 313 VAL B C   1 
ATOM   2359 O O   . VAL B 2 313 ? 80.886  54.314  72.353 1.00 144.26 ? 313 VAL B O   1 
ATOM   2360 C CB  . VAL B 2 313 ? 80.738  57.474  71.311 1.00 164.38 ? 313 VAL B CB  1 
ATOM   2361 C CG1 . VAL B 2 313 ? 82.009  57.443  72.166 1.00 213.32 ? 313 VAL B CG1 1 
ATOM   2362 C CG2 . VAL B 2 313 ? 80.907  58.360  70.073 1.00 167.78 ? 313 VAL B CG2 1 
ATOM   2363 N N   . ASP B 2 314 ? 78.900  55.311  72.806 1.00 160.96 ? 314 ASP B N   1 
ATOM   2364 C CA  . ASP B 2 314 ? 78.544  54.430  73.916 1.00 161.39 ? 314 ASP B CA  1 
ATOM   2365 C C   . ASP B 2 314 ? 78.337  52.990  73.463 1.00 124.49 ? 314 ASP B C   1 
ATOM   2366 O O   . ASP B 2 314 ? 78.809  52.057  74.121 1.00 167.71 ? 314 ASP B O   1 
ATOM   2367 C CB  . ASP B 2 314 ? 77.325  54.962  74.671 1.00 167.95 ? 314 ASP B CB  1 
ATOM   2368 C CG  . ASP B 2 314 ? 77.644  56.101  75.636 1.00 292.16 ? 314 ASP B CG  1 
ATOM   2369 O OD1 . ASP B 2 314 ? 78.772  56.644  75.615 1.00 358.21 ? 314 ASP B OD1 1 
ATOM   2370 O OD2 . ASP B 2 314 ? 76.740  56.460  76.428 1.00 346.39 ? 314 ASP B OD2 1 
ATOM   2371 N N   . PHE B 2 315 ? 77.658  52.824  72.335 1.00 115.63 ? 315 PHE B N   1 
ATOM   2372 C CA  . PHE B 2 315 ? 77.533  51.522  71.694 1.00 132.17 ? 315 PHE B CA  1 
ATOM   2373 C C   . PHE B 2 315 ? 78.908  50.899  71.356 1.00 129.73 ? 315 PHE B C   1 
ATOM   2374 O O   . PHE B 2 315 ? 79.166  49.737  71.667 1.00 161.83 ? 315 PHE B O   1 
ATOM   2375 C CB  . PHE B 2 315 ? 76.621  51.688  70.482 1.00 125.28 ? 315 PHE B CB  1 
ATOM   2376 C CG  . PHE B 2 315 ? 76.272  50.398  69.789 1.00 141.32 ? 315 PHE B CG  1 
ATOM   2377 C CD1 . PHE B 2 315 ? 77.172  49.789  68.901 1.00 141.38 ? 315 PHE B CD1 1 
ATOM   2378 C CD2 . PHE B 2 315 ? 75.045  49.797  70.035 1.00 130.31 ? 315 PHE B CD2 1 
ATOM   2379 C CE1 . PHE B 2 315 ? 76.839  48.606  68.268 1.00 169.49 ? 315 PHE B CE1 1 
ATOM   2380 C CE2 . PHE B 2 315 ? 74.723  48.603  69.409 1.00 156.23 ? 315 PHE B CE2 1 
ATOM   2381 C CZ  . PHE B 2 315 ? 75.611  48.020  68.527 1.00 193.03 ? 315 PHE B CZ  1 
ATOM   2382 N N   . GLY B 2 316 ? 79.812  51.664  70.744 1.00 138.96 ? 316 GLY B N   1 
ATOM   2383 C CA  . GLY B 2 316 ? 81.169  51.224  70.463 1.00 172.27 ? 316 GLY B CA  1 
ATOM   2384 C C   . GLY B 2 316 ? 81.925  50.807  71.723 1.00 181.04 ? 316 GLY B C   1 
ATOM   2385 O O   . GLY B 2 316 ? 82.488  49.709  71.760 1.00 212.02 ? 316 GLY B O   1 
ATOM   2386 N N   . ASN B 2 317 ? 81.925  51.679  72.743 1.00 150.45 ? 317 ASN B N   1 
ATOM   2387 C CA  . ASN B 2 317 ? 82.591  51.424  74.010 1.00 169.98 ? 317 ASN B CA  1 
ATOM   2388 C C   . ASN B 2 317 ? 82.154  50.091  74.618 1.00 186.57 ? 317 ASN B C   1 
ATOM   2389 O O   . ASN B 2 317 ? 82.999  49.332  75.107 1.00 210.13 ? 317 ASN B O   1 
ATOM   2390 C CB  . ASN B 2 317 ? 82.354  52.580  74.990 1.00 165.59 ? 317 ASN B CB  1 
ATOM   2391 C CG  . ASN B 2 317 ? 83.326  53.740  74.849 1.00 237.25 ? 317 ASN B CG  1 
ATOM   2392 O OD1 . ASN B 2 317 ? 84.466  53.588  74.407 1.00 256.20 ? 317 ASN B OD1 1 
ATOM   2393 N ND2 . ASN B 2 317 ? 82.894  54.924  75.253 1.00 263.98 ? 317 ASN B ND2 1 
ATOM   2394 N N   . TYR B 2 318 ? 80.843  49.820  74.611 1.00 175.58 ? 318 TYR B N   1 
ATOM   2395 C CA  . TYR B 2 318 ? 80.298  48.614  75.215 1.00 189.77 ? 318 TYR B CA  1 
ATOM   2396 C C   . TYR B 2 318 ? 80.706  47.346  74.460 1.00 176.37 ? 318 TYR B C   1 
ATOM   2397 O O   . TYR B 2 318 ? 81.051  46.352  75.105 1.00 260.16 ? 318 TYR B O   1 
ATOM   2398 C CB  . TYR B 2 318 ? 78.782  48.756  75.309 1.00 220.18 ? 318 TYR B CB  1 
ATOM   2399 C CG  . TYR B 2 318 ? 78.109  47.637  76.091 1.00 255.67 ? 318 TYR B CG  1 
ATOM   2400 C CD1 . TYR B 2 318 ? 77.766  46.430  75.483 1.00 226.33 ? 318 TYR B CD1 1 
ATOM   2401 C CD2 . TYR B 2 318 ? 77.817  47.788  77.445 1.00 312.86 ? 318 TYR B CD2 1 
ATOM   2402 C CE1 . TYR B 2 318 ? 77.146  45.409  76.192 1.00 277.35 ? 318 TYR B CE1 1 
ATOM   2403 C CE2 . TYR B 2 318 ? 77.200  46.773  78.165 1.00 342.59 ? 318 TYR B CE2 1 
ATOM   2404 C CZ  . TYR B 2 318 ? 76.864  45.580  77.540 1.00 341.90 ? 318 TYR B CZ  1 
ATOM   2405 O OH  . TYR B 2 318 ? 76.256  44.580  78.256 1.00 409.16 ? 318 TYR B OH  1 
ATOM   2406 N N   . HIS B 2 319 ? 80.662  47.356  73.121 1.00 171.29 ? 319 HIS B N   1 
ATOM   2407 C CA  . HIS B 2 319 ? 80.864  46.141  72.334 1.00 190.00 ? 319 HIS B CA  1 
ATOM   2408 C C   . HIS B 2 319 ? 82.327  45.848  71.987 1.00 181.96 ? 319 HIS B C   1 
ATOM   2409 O O   . HIS B 2 319 ? 82.659  44.673  71.801 1.00 208.95 ? 319 HIS B O   1 
ATOM   2410 C CB  . HIS B 2 319 ? 79.994  46.161  71.069 1.00 186.44 ? 319 HIS B CB  1 
ATOM   2411 C CG  . HIS B 2 319 ? 78.554  45.964  71.421 1.00 182.89 ? 319 HIS B CG  1 
ATOM   2412 N ND1 . HIS B 2 319 ? 78.015  44.750  71.777 1.00 207.80 ? 319 HIS B ND1 1 
ATOM   2413 C CD2 . HIS B 2 319 ? 77.543  46.851  71.495 1.00 175.27 ? 319 HIS B CD2 1 
ATOM   2414 C CE1 . HIS B 2 319 ? 76.722  44.915  72.059 1.00 255.79 ? 319 HIS B CE1 1 
ATOM   2415 N NE2 . HIS B 2 319 ? 76.411  46.183  71.892 1.00 169.84 ? 319 HIS B NE2 1 
ATOM   2416 N N   . LEU B 2 320 ? 83.195  46.871  71.880 1.00 180.38 ? 320 LEU B N   1 
ATOM   2417 C CA  . LEU B 2 320 ? 84.490  46.697  71.217 1.00 226.04 ? 320 LEU B CA  1 
ATOM   2418 C C   . LEU B 2 320 ? 85.705  46.983  72.110 1.00 242.16 ? 320 LEU B C   1 
ATOM   2419 O O   . LEU B 2 320 ? 86.813  46.596  71.730 1.00 197.37 ? 320 LEU B O   1 
ATOM   2420 C CB  . LEU B 2 320 ? 84.501  47.593  69.975 1.00 210.49 ? 320 LEU B CB  1 
ATOM   2421 C CG  . LEU B 2 320 ? 83.411  47.295  68.948 1.00 193.80 ? 320 LEU B CG  1 
ATOM   2422 C CD1 . LEU B 2 320 ? 83.367  48.372  67.881 1.00 243.70 ? 320 LEU B CD1 1 
ATOM   2423 C CD2 . LEU B 2 320 ? 83.628  45.927  68.327 1.00 215.02 ? 320 LEU B CD2 1 
ATOM   2424 N N   . GLY B 2 321 ? 85.529  47.642  73.267 1.00 251.98 ? 321 GLY B N   1 
ATOM   2425 C CA  . GLY B 2 321 ? 86.613  47.843  74.224 1.00 290.08 ? 321 GLY B CA  1 
ATOM   2426 C C   . GLY B 2 321 ? 87.857  48.495  73.610 1.00 243.85 ? 321 GLY B C   1 
ATOM   2427 O O   . GLY B 2 321 ? 87.779  49.634  73.148 1.00 286.55 ? 321 GLY B O   1 
ATOM   2428 N N   . VAL B 2 322 ? 88.985  47.757  73.587 1.00 218.20 ? 322 VAL B N   1 
ATOM   2429 C CA  . VAL B 2 322 ? 90.280  48.237  73.105 1.00 270.95 ? 322 VAL B CA  1 
ATOM   2430 C C   . VAL B 2 322 ? 90.206  48.645  71.624 1.00 239.70 ? 322 VAL B C   1 
ATOM   2431 O O   . VAL B 2 322 ? 90.994  49.485  71.182 1.00 237.49 ? 322 VAL B O   1 
ATOM   2432 C CB  . VAL B 2 322 ? 91.379  47.177  73.362 1.00 367.85 ? 322 VAL B CB  1 
ATOM   2433 C CG1 . VAL B 2 322 ? 92.759  47.583  72.838 1.00 409.86 ? 322 VAL B CG1 1 
ATOM   2434 C CG2 . VAL B 2 322 ? 91.479  46.818  74.843 1.00 389.77 ? 322 VAL B CG2 1 
ATOM   2435 N N   . MET B 2 323 ? 89.264  48.062  70.858 1.00 211.33 ? 323 MET B N   1 
ATOM   2436 C CA  . MET B 2 323 ? 89.083  48.363  69.436 1.00 218.48 ? 323 MET B CA  1 
ATOM   2437 C C   . MET B 2 323 ? 87.981  49.408  69.156 1.00 209.46 ? 323 MET B C   1 
ATOM   2438 O O   . MET B 2 323 ? 87.612  49.600  68.008 1.00 206.65 ? 323 MET B O   1 
ATOM   2439 C CB  . MET B 2 323 ? 88.758  47.047  68.714 1.00 219.52 ? 323 MET B CB  1 
ATOM   2440 C CG  . MET B 2 323 ? 89.117  46.998  67.236 1.00 256.94 ? 323 MET B CG  1 
ATOM   2441 S SD  . MET B 2 323 ? 90.879  47.251  66.859 1.00 285.17 ? 323 MET B SD  1 
ATOM   2442 C CE  . MET B 2 323 ? 90.766  47.502  65.085 1.00 332.44 ? 323 MET B CE  1 
ATOM   2443 N N   . SER B 2 324 ? 87.458  50.132  70.163 1.00 214.55 ? 324 SER B N   1 
ATOM   2444 C CA  . SER B 2 324 ? 86.255  50.956  70.010 1.00 171.35 ? 324 SER B CA  1 
ATOM   2445 C C   . SER B 2 324 ? 86.408  52.167  69.089 1.00 164.99 ? 324 SER B C   1 
ATOM   2446 O O   . SER B 2 324 ? 85.389  52.720  68.685 1.00 198.75 ? 324 SER B O   1 
ATOM   2447 C CB  . SER B 2 324 ? 85.748  51.441  71.352 1.00 195.51 ? 324 SER B CB  1 
ATOM   2448 O OG  . SER B 2 324 ? 84.561  52.219  71.200 1.00 180.08 ? 324 SER B OG  1 
ATOM   2449 N N   . TRP B 2 325 ? 87.630  52.595  68.754 1.00 159.28 ? 325 TRP B N   1 
ATOM   2450 C CA  . TRP B 2 325 ? 87.818  53.788  67.929 1.00 191.30 ? 325 TRP B CA  1 
ATOM   2451 C C   . TRP B 2 325 ? 87.222  53.666  66.510 1.00 161.19 ? 325 TRP B C   1 
ATOM   2452 O O   . TRP B 2 325 ? 86.999  54.715  65.858 1.00 104.60 ? 325 TRP B O   1 
ATOM   2453 C CB  . TRP B 2 325 ? 89.310  54.166  67.874 1.00 222.95 ? 325 TRP B CB  1 
ATOM   2454 C CG  . TRP B 2 325 ? 90.168  53.060  67.313 1.00 178.60 ? 325 TRP B CG  1 
ATOM   2455 C CD1 . TRP B 2 325 ? 90.857  52.145  68.047 1.00 215.79 ? 325 TRP B CD1 1 
ATOM   2456 C CD2 . TRP B 2 325 ? 90.442  52.748  65.928 1.00 134.48 ? 325 TRP B CD2 1 
ATOM   2457 N NE1 . TRP B 2 325 ? 91.523  51.279  67.226 1.00 245.59 ? 325 TRP B NE1 1 
ATOM   2458 C CE2 . TRP B 2 325 ? 91.296  51.626  65.915 1.00 231.93 ? 325 TRP B CE2 1 
ATOM   2459 C CE3 . TRP B 2 325 ? 90.068  53.295  64.703 1.00 159.84 ? 325 TRP B CE3 1 
ATOM   2460 C CZ2 . TRP B 2 325 ? 91.766  51.058  64.719 1.00 302.33 ? 325 TRP B CZ2 1 
ATOM   2461 C CZ3 . TRP B 2 325 ? 90.526  52.740  63.521 1.00 270.36 ? 325 TRP B CZ3 1 
ATOM   2462 C CH2 . TRP B 2 325 ? 91.367  51.629  63.529 1.00 295.10 ? 325 TRP B CH2 1 
ATOM   2463 N N   . ILE B 2 326 ? 86.934  52.436  66.028 1.00 128.93 ? 326 ILE B N   1 
ATOM   2464 C CA  . ILE B 2 326 ? 86.401  52.268  64.683 1.00 155.75 ? 326 ILE B CA  1 
ATOM   2465 C C   . ILE B 2 326 ? 85.021  52.912  64.509 1.00 171.68 ? 326 ILE B C   1 
ATOM   2466 O O   . ILE B 2 326 ? 84.745  53.437  63.414 1.00 236.62 ? 326 ILE B O   1 
ATOM   2467 C CB  . ILE B 2 326 ? 86.371  50.796  64.250 1.00 183.30 ? 326 ILE B CB  1 
ATOM   2468 C CG1 . ILE B 2 326 ? 85.304  49.973  64.997 1.00 146.20 ? 326 ILE B CG1 1 
ATOM   2469 C CG2 . ILE B 2 326 ? 87.782  50.204  64.332 1.00 237.24 ? 326 ILE B CG2 1 
ATOM   2470 C CD1 . ILE B 2 326 ? 85.136  48.556  64.453 1.00 243.09 ? 326 ILE B CD1 1 
ATOM   2471 N N   . ILE B 2 327 ? 84.170  52.884  65.555 1.00 117.30 ? 327 ILE B N   1 
ATOM   2472 C CA  . ILE B 2 327 ? 82.820  53.403  65.407 1.00 125.95 ? 327 ILE B CA  1 
ATOM   2473 C C   . ILE B 2 327 ? 82.829  54.932  65.268 1.00 105.12 ? 327 ILE B C   1 
ATOM   2474 O O   . ILE B 2 327 ? 82.208  55.436  64.319 1.00 181.04 ? 327 ILE B O   1 
ATOM   2475 C CB  . ILE B 2 327 ? 81.854  52.871  66.483 1.00 129.03 ? 327 ILE B CB  1 
ATOM   2476 C CG1 . ILE B 2 327 ? 81.649  51.358  66.333 1.00 157.16 ? 327 ILE B CG1 1 
ATOM   2477 C CG2 . ILE B 2 327 ? 80.507  53.582  66.443 1.00 110.06 ? 327 ILE B CG2 1 
ATOM   2478 C CD1 . ILE B 2 327 ? 81.079  50.878  64.985 1.00 146.70 ? 327 ILE B CD1 1 
ATOM   2479 N N   . PRO B 2 328 ? 83.480  55.726  66.133 1.00 99.66  ? 328 PRO B N   1 
ATOM   2480 C CA  . PRO B 2 328 ? 83.658  57.148  65.879 1.00 121.91 ? 328 PRO B CA  1 
ATOM   2481 C C   . PRO B 2 328 ? 84.181  57.457  64.472 1.00 136.44 ? 328 PRO B C   1 
ATOM   2482 O O   . PRO B 2 328 ? 83.610  58.318  63.798 1.00 160.33 ? 328 PRO B O   1 
ATOM   2483 C CB  . PRO B 2 328 ? 84.664  57.583  66.953 1.00 158.08 ? 328 PRO B CB  1 
ATOM   2484 C CG  . PRO B 2 328 ? 84.362  56.654  68.088 1.00 205.55 ? 328 PRO B CG  1 
ATOM   2485 C CD  . PRO B 2 328 ? 84.026  55.339  67.423 1.00 157.35 ? 328 PRO B CD  1 
ATOM   2486 N N   . VAL B 2 329 ? 85.239  56.778  63.994 1.00 92.72  ? 329 VAL B N   1 
ATOM   2487 C CA  . VAL B 2 329 ? 85.768  57.107  62.678 1.00 103.00 ? 329 VAL B CA  1 
ATOM   2488 C C   . VAL B 2 329 ? 84.732  56.837  61.582 1.00 120.16 ? 329 VAL B C   1 
ATOM   2489 O O   . VAL B 2 329 ? 84.577  57.672  60.699 1.00 156.67 ? 329 VAL B O   1 
ATOM   2490 C CB  . VAL B 2 329 ? 87.097  56.392  62.428 1.00 125.90 ? 329 VAL B CB  1 
ATOM   2491 C CG1 . VAL B 2 329 ? 87.546  56.351  60.973 1.00 157.80 ? 329 VAL B CG1 1 
ATOM   2492 C CG2 . VAL B 2 329 ? 88.163  57.060  63.290 1.00 130.13 ? 329 VAL B CG2 1 
ATOM   2493 N N   . PHE B 2 330 ? 84.005  55.725  61.620 1.00 120.83 ? 330 PHE B N   1 
ATOM   2494 C CA  . PHE B 2 330 ? 82.959  55.516  60.629 1.00 138.47 ? 330 PHE B CA  1 
ATOM   2495 C C   . PHE B 2 330 ? 81.798  56.525  60.718 1.00 131.35 ? 330 PHE B C   1 
ATOM   2496 O O   . PHE B 2 330 ? 81.237  56.872  59.687 1.00 164.17 ? 330 PHE B O   1 
ATOM   2497 C CB  . PHE B 2 330 ? 82.383  54.113  60.769 1.00 194.35 ? 330 PHE B CB  1 
ATOM   2498 C CG  . PHE B 2 330 ? 83.230  52.973  60.257 1.00 185.34 ? 330 PHE B CG  1 
ATOM   2499 C CD1 . PHE B 2 330 ? 83.853  53.034  59.024 1.00 180.68 ? 330 PHE B CD1 1 
ATOM   2500 C CD2 . PHE B 2 330 ? 83.372  51.811  61.003 1.00 222.70 ? 330 PHE B CD2 1 
ATOM   2501 C CE1 . PHE B 2 330 ? 84.616  51.972  58.552 1.00 234.90 ? 330 PHE B CE1 1 
ATOM   2502 C CE2 . PHE B 2 330 ? 84.131  50.749  60.524 1.00 268.82 ? 330 PHE B CE2 1 
ATOM   2503 C CZ  . PHE B 2 330 ? 84.752  50.830  59.300 1.00 251.51 ? 330 PHE B CZ  1 
ATOM   2504 N N   . VAL B 2 331 ? 81.395  57.017  61.898 1.00 134.17 ? 331 VAL B N   1 
ATOM   2505 C CA  . VAL B 2 331 ? 80.429  58.115  61.949 1.00 134.68 ? 331 VAL B CA  1 
ATOM   2506 C C   . VAL B 2 331 ? 80.986  59.352  61.244 1.00 99.82  ? 331 VAL B C   1 
ATOM   2507 O O   . VAL B 2 331 ? 80.246  60.077  60.573 1.00 100.17 ? 331 VAL B O   1 
ATOM   2508 C CB  . VAL B 2 331 ? 79.977  58.473  63.378 1.00 131.80 ? 331 VAL B CB  1 
ATOM   2509 C CG1 . VAL B 2 331 ? 79.035  59.673  63.390 1.00 97.21  ? 331 VAL B CG1 1 
ATOM   2510 C CG2 . VAL B 2 331 ? 79.299  57.256  64.006 1.00 181.43 ? 331 VAL B CG2 1 
ATOM   2511 N N   . GLY B 2 332 ? 82.285  59.595  61.396 1.00 115.45 ? 332 GLY B N   1 
ATOM   2512 C CA  . GLY B 2 332 ? 82.973  60.623  60.636 1.00 154.31 ? 332 GLY B CA  1 
ATOM   2513 C C   . GLY B 2 332 ? 82.861  60.419  59.128 1.00 118.80 ? 332 GLY B C   1 
ATOM   2514 O O   . GLY B 2 332 ? 82.318  61.279  58.435 1.00 122.20 ? 332 GLY B O   1 
ATOM   2515 N N   . LEU B 2 333 ? 83.329  59.269  58.638 1.00 101.99 ? 333 LEU B N   1 
ATOM   2516 C CA  . LEU B 2 333 ? 83.262  58.964  57.217 1.00 122.45 ? 333 LEU B CA  1 
ATOM   2517 C C   . LEU B 2 333 ? 81.819  58.967  56.687 1.00 105.42 ? 333 LEU B C   1 
ATOM   2518 O O   . LEU B 2 333 ? 81.612  59.267  55.508 1.00 104.35 ? 333 LEU B O   1 
ATOM   2519 C CB  . LEU B 2 333 ? 83.969  57.622  56.947 1.00 122.19 ? 333 LEU B CB  1 
ATOM   2520 C CG  . LEU B 2 333 ? 85.459  57.595  57.318 1.00 139.12 ? 333 LEU B CG  1 
ATOM   2521 C CD1 . LEU B 2 333 ? 86.093  56.321  56.786 1.00 192.79 ? 333 LEU B CD1 1 
ATOM   2522 C CD2 . LEU B 2 333 ? 86.273  58.814  56.821 1.00 151.17 ? 333 LEU B CD2 1 
ATOM   2523 N N   . SER B 2 334 ? 80.823  58.649  57.520 1.00 87.79  ? 334 SER B N   1 
ATOM   2524 C CA  . SER B 2 334 ? 79.427  58.737  57.123 1.00 102.78 ? 334 SER B CA  1 
ATOM   2525 C C   . SER B 2 334 ? 78.968  60.169  56.896 1.00 74.93  ? 334 SER B C   1 
ATOM   2526 O O   . SER B 2 334 ? 78.170  60.417  55.992 1.00 150.03 ? 334 SER B O   1 
ATOM   2527 C CB  . SER B 2 334 ? 78.524  58.067  58.100 1.00 136.44 ? 334 SER B CB  1 
ATOM   2528 O OG  . SER B 2 334 ? 77.209  58.055  57.578 1.00 129.26 ? 334 SER B OG  1 
ATOM   2529 N N   . CYS B 2 335 ? 79.450  61.108  57.676 1.00 86.91  ? 335 CYS B N   1 
ATOM   2530 C CA  . CYS B 2 335 ? 79.125  62.514  57.483 1.00 118.88 ? 335 CYS B CA  1 
ATOM   2531 C C   . CYS B 2 335 ? 79.850  63.055  56.256 1.00 107.90 ? 335 CYS B C   1 
ATOM   2532 O O   . CYS B 2 335 ? 79.260  63.819  55.495 1.00 149.55 ? 335 CYS B O   1 
ATOM   2533 C CB  . CYS B 2 335 ? 79.480  63.289  58.747 1.00 163.53 ? 335 CYS B CB  1 
ATOM   2534 S SG  . CYS B 2 335 ? 78.480  62.769  60.163 1.00 135.71 ? 335 CYS B SG  1 
ATOM   2535 N N   . PHE B 2 336 ? 81.112  62.650  56.040 1.00 97.14  ? 336 PHE B N   1 
ATOM   2536 C CA  . PHE B 2 336 ? 81.926  63.184  54.959 1.00 101.57 ? 336 PHE B CA  1 
ATOM   2537 C C   . PHE B 2 336 ? 81.266  62.960  53.609 1.00 118.30 ? 336 PHE B C   1 
ATOM   2538 O O   . PHE B 2 336 ? 81.127  63.923  52.853 1.00 99.10  ? 336 PHE B O   1 
ATOM   2539 C CB  . PHE B 2 336 ? 83.286  62.517  55.040 1.00 145.14 ? 336 PHE B CB  1 
ATOM   2540 C CG  . PHE B 2 336 ? 84.345  63.055  54.117 1.00 126.83 ? 336 PHE B CG  1 
ATOM   2541 C CD1 . PHE B 2 336 ? 85.086  64.191  54.467 1.00 91.76  ? 336 PHE B CD1 1 
ATOM   2542 C CD2 . PHE B 2 336 ? 84.605  62.388  52.930 1.00 109.59 ? 336 PHE B CD2 1 
ATOM   2543 C CE1 . PHE B 2 336 ? 86.090  64.640  53.628 1.00 137.71 ? 336 PHE B CE1 1 
ATOM   2544 C CE2 . PHE B 2 336 ? 85.607  62.853  52.084 1.00 140.67 ? 336 PHE B CE2 1 
ATOM   2545 C CZ  . PHE B 2 336 ? 86.342  63.971  52.433 1.00 167.10 ? 336 PHE B CZ  1 
ATOM   2546 N N   . GLY B 2 337 ? 80.823  61.717  53.332 1.00 119.17 ? 337 GLY B N   1 
ATOM   2547 C CA  . GLY B 2 337 ? 79.987  61.366  52.179 1.00 119.80 ? 337 GLY B CA  1 
ATOM   2548 C C   . GLY B 2 337 ? 78.737  62.235  51.910 1.00 79.61  ? 337 GLY B C   1 
ATOM   2549 O O   . GLY B 2 337 ? 78.364  62.498  50.762 1.00 156.55 ? 337 GLY B O   1 
ATOM   2550 N N   . SER B 2 338 ? 78.106  62.702  52.961 1.00 70.94  ? 338 SER B N   1 
ATOM   2551 C CA  . SER B 2 338 ? 76.944  63.560  52.855 1.00 81.46  ? 338 SER B CA  1 
ATOM   2552 C C   . SER B 2 338 ? 77.337  65.010  52.540 1.00 101.13 ? 338 SER B C   1 
ATOM   2553 O O   . SER B 2 338 ? 76.583  65.707  51.856 1.00 98.40  ? 338 SER B O   1 
ATOM   2554 C CB  . SER B 2 338 ? 76.115  63.490  54.137 1.00 112.56 ? 338 SER B CB  1 
ATOM   2555 O OG  . SER B 2 338 ? 74.973  64.370  54.065 1.00 109.41 ? 338 SER B OG  1 
ATOM   2556 N N   . VAL B 2 339 ? 78.490  65.519  53.038 1.00 81.46  ? 339 VAL B N   1 
ATOM   2557 C CA  . VAL B 2 339 ? 78.910  66.855  52.691 1.00 75.65  ? 339 VAL B CA  1 
ATOM   2558 C C   . VAL B 2 339 ? 79.124  66.858  51.185 1.00 112.49 ? 339 VAL B C   1 
ATOM   2559 O O   . VAL B 2 339 ? 78.784  67.848  50.516 1.00 149.56 ? 339 VAL B O   1 
ATOM   2560 C CB  . VAL B 2 339 ? 80.170  67.305  53.430 1.00 95.34  ? 339 VAL B CB  1 
ATOM   2561 C CG1 . VAL B 2 339 ? 80.650  68.681  52.965 1.00 141.61 ? 339 VAL B CG1 1 
ATOM   2562 C CG2 . VAL B 2 339 ? 79.996  67.371  54.902 1.00 112.33 ? 339 VAL B CG2 1 
ATOM   2563 N N   . ASN B 2 340 ? 79.712  65.781  50.634 1.00 102.53 ? 340 ASN B N   1 
ATOM   2564 C CA  . ASN B 2 340 ? 79.931  65.674  49.197 1.00 99.33  ? 340 ASN B CA  1 
ATOM   2565 C C   . ASN B 2 340 ? 78.589  65.671  48.452 1.00 92.77  ? 340 ASN B C   1 
ATOM   2566 O O   . ASN B 2 340 ? 78.362  66.465  47.552 1.00 72.87  ? 340 ASN B O   1 
ATOM   2567 C CB  . ASN B 2 340 ? 80.779  64.442  48.926 1.00 83.18  ? 340 ASN B CB  1 
ATOM   2568 C CG  . ASN B 2 340 ? 81.003  64.260  47.459 1.00 132.77 ? 340 ASN B CG  1 
ATOM   2569 O OD1 . ASN B 2 340 ? 81.208  65.260  46.769 1.00 165.06 ? 340 ASN B OD1 1 
ATOM   2570 N ND2 . ASN B 2 340 ? 80.949  63.018  46.990 1.00 120.40 ? 340 ASN B ND2 1 
ATOM   2571 N N   . GLY B 2 341 ? 77.690  64.764  48.804 1.00 101.53 ? 341 GLY B N   1 
ATOM   2572 C CA  . GLY B 2 341 ? 76.386  64.662  48.160 1.00 113.16 ? 341 GLY B CA  1 
ATOM   2573 C C   . GLY B 2 341 ? 75.563  65.946  48.214 1.00 95.30  ? 341 GLY B C   1 
ATOM   2574 O O   . GLY B 2 341 ? 74.864  66.256  47.266 1.00 123.38 ? 341 GLY B O   1 
ATOM   2575 N N   . SER B 2 342 ? 75.671  66.710  49.293 1.00 71.66  ? 342 SER B N   1 
ATOM   2576 C CA  . SER B 2 342 ? 75.018  67.984  49.339 1.00 77.23  ? 342 SER B CA  1 
ATOM   2577 C C   . SER B 2 342 ? 75.784  69.019  48.506 1.00 95.26  ? 342 SER B C   1 
ATOM   2578 O O   . SER B 2 342 ? 75.115  69.757  47.796 1.00 152.44 ? 342 SER B O   1 
ATOM   2579 C CB  . SER B 2 342 ? 74.760  68.437  50.749 1.00 143.03 ? 342 SER B CB  1 
ATOM   2580 O OG  . SER B 2 342 ? 73.939  69.607  50.699 1.00 205.21 ? 342 SER B OG  1 
ATOM   2581 N N   . LEU B 2 343 ? 77.126  69.122  48.517 1.00 98.05  ? 343 LEU B N   1 
ATOM   2582 C CA  . LEU B 2 343 ? 77.814  70.087  47.646 1.00 103.92 ? 343 LEU B CA  1 
ATOM   2583 C C   . LEU B 2 343 ? 77.532  69.803  46.181 1.00 97.50  ? 343 LEU B C   1 
ATOM   2584 O O   . LEU B 2 343 ? 77.370  70.742  45.399 1.00 110.74 ? 343 LEU B O   1 
ATOM   2585 C CB  . LEU B 2 343 ? 79.328  70.064  47.889 1.00 120.65 ? 343 LEU B CB  1 
ATOM   2586 C CG  . LEU B 2 343 ? 79.773  70.788  49.156 1.00 164.52 ? 343 LEU B CG  1 
ATOM   2587 C CD1 . LEU B 2 343 ? 81.241  70.475  49.400 1.00 217.09 ? 343 LEU B CD1 1 
ATOM   2588 C CD2 . LEU B 2 343 ? 79.535  72.317  49.091 1.00 91.27  ? 343 LEU B CD2 1 
ATOM   2589 N N   . PHE B 2 344 ? 77.480  68.520  45.815 1.00 96.84  ? 344 PHE B N   1 
ATOM   2590 C CA  . PHE B 2 344 ? 77.080  68.073  44.489 1.00 98.29  ? 344 PHE B CA  1 
ATOM   2591 C C   . PHE B 2 344 ? 75.714  68.644  44.159 1.00 86.25  ? 344 PHE B C   1 
ATOM   2592 O O   . PHE B 2 344 ? 75.595  69.431  43.253 1.00 136.96 ? 344 PHE B O   1 
ATOM   2593 C CB  . PHE B 2 344 ? 77.064  66.550  44.463 1.00 112.01 ? 344 PHE B CB  1 
ATOM   2594 C CG  . PHE B 2 344 ? 77.114  65.840  43.137 1.00 126.55 ? 344 PHE B CG  1 
ATOM   2595 C CD1 . PHE B 2 344 ? 76.210  66.102  42.139 1.00 102.84 ? 344 PHE B CD1 1 
ATOM   2596 C CD2 . PHE B 2 344 ? 78.070  64.843  42.928 1.00 184.78 ? 344 PHE B CD2 1 
ATOM   2597 C CE1 . PHE B 2 344 ? 76.288  65.410  40.944 1.00 147.29 ? 344 PHE B CE1 1 
ATOM   2598 C CE2 . PHE B 2 344 ? 78.147  64.144  41.742 1.00 172.11 ? 344 PHE B CE2 1 
ATOM   2599 C CZ  . PHE B 2 344 ? 77.244  64.432  40.751 1.00 195.54 ? 344 PHE B CZ  1 
ATOM   2600 N N   . THR B 2 345 ? 74.670  68.268  44.867 1.00 84.31  ? 345 THR B N   1 
ATOM   2601 C CA  . THR B 2 345 ? 73.324  68.597  44.462 1.00 95.51  ? 345 THR B CA  1 
ATOM   2602 C C   . THR B 2 345 ? 72.987  70.059  44.745 1.00 93.05  ? 345 THR B C   1 
ATOM   2603 O O   . THR B 2 345 ? 72.070  70.592  44.117 1.00 156.78 ? 345 THR B O   1 
ATOM   2604 C CB  . THR B 2 345 ? 72.320  67.648  45.151 1.00 138.71 ? 345 THR B CB  1 
ATOM   2605 O OG1 . THR B 2 345 ? 72.467  67.731  46.569 1.00 122.10 ? 345 THR B OG1 1 
ATOM   2606 C CG2 . THR B 2 345 ? 72.497  66.199  44.744 1.00 144.28 ? 345 THR B CG2 1 
ATOM   2607 N N   . SER B 2 346 ? 73.644  70.722  45.700 1.00 102.17 ? 346 SER B N   1 
ATOM   2608 C CA  . SER B 2 346 ? 73.412  72.126  46.010 1.00 114.02 ? 346 SER B CA  1 
ATOM   2609 C C   . SER B 2 346 ? 73.946  73.013  44.897 1.00 98.96  ? 346 SER B C   1 
ATOM   2610 O O   . SER B 2 346 ? 73.254  73.919  44.436 1.00 150.71 ? 346 SER B O   1 
ATOM   2611 C CB  . SER B 2 346 ? 74.005  72.513  47.324 1.00 126.26 ? 346 SER B CB  1 
ATOM   2612 O OG  . SER B 2 346 ? 73.760  73.883  47.590 1.00 110.39 ? 346 SER B OG  1 
ATOM   2613 N N   . SER B 2 347 ? 75.151  72.750  44.423 1.00 89.54  ? 347 SER B N   1 
ATOM   2614 C CA  . SER B 2 347 ? 75.688  73.531  43.312 1.00 134.49 ? 347 SER B CA  1 
ATOM   2615 C C   . SER B 2 347 ? 74.795  73.458  42.062 1.00 112.68 ? 347 SER B C   1 
ATOM   2616 O O   . SER B 2 347 ? 74.646  74.433  41.340 1.00 103.77 ? 347 SER B O   1 
ATOM   2617 C CB  . SER B 2 347 ? 77.124  73.113  42.982 1.00 109.59 ? 347 SER B CB  1 
ATOM   2618 O OG  . SER B 2 347 ? 77.191  71.761  42.618 1.00 130.75 ? 347 SER B OG  1 
ATOM   2619 N N   . ARG B 2 348 ? 74.216  72.300  41.757 1.00 86.50  ? 348 ARG B N   1 
ATOM   2620 C CA  . ARG B 2 348 ? 73.362  72.165  40.611 1.00 77.92  ? 348 ARG B CA  1 
ATOM   2621 C C   . ARG B 2 348 ? 72.076  72.967  40.786 1.00 88.69  ? 348 ARG B C   1 
ATOM   2622 O O   . ARG B 2 348 ? 71.574  73.483  39.790 1.00 113.78 ? 348 ARG B O   1 
ATOM   2623 C CB  . ARG B 2 348 ? 73.009  70.692  40.353 1.00 114.12 ? 348 ARG B CB  1 
ATOM   2624 C CG  . ARG B 2 348 ? 74.192  69.779  40.067 1.00 97.92  ? 348 ARG B CG  1 
ATOM   2625 C CD  . ARG B 2 348 ? 75.378  70.409  39.335 1.00 89.84  ? 348 ARG B CD  1 
ATOM   2626 N NE  . ARG B 2 348 ? 76.246  69.307  38.923 1.00 143.64 ? 348 ARG B NE  1 
ATOM   2627 C CZ  . ARG B 2 348 ? 77.433  68.951  39.421 1.00 135.86 ? 348 ARG B CZ  1 
ATOM   2628 N NH1 . ARG B 2 348 ? 78.081  67.960  38.859 1.00 117.84 ? 348 ARG B NH1 1 
ATOM   2629 N NH2 . ARG B 2 348 ? 77.979  69.572  40.442 1.00 118.16 ? 348 ARG B NH2 1 
ATOM   2630 N N   . LEU B 2 349 ? 71.494  73.066  41.989 1.00 111.75 ? 349 LEU B N   1 
ATOM   2631 C CA  . LEU B 2 349 ? 70.312  73.898  42.215 1.00 116.66 ? 349 LEU B CA  1 
ATOM   2632 C C   . LEU B 2 349 ? 70.600  75.359  41.829 1.00 92.54  ? 349 LEU B C   1 
ATOM   2633 O O   . LEU B 2 349 ? 69.853  75.929  41.056 1.00 103.44 ? 349 LEU B O   1 
ATOM   2634 C CB  . LEU B 2 349 ? 69.841  73.775  43.675 1.00 111.81 ? 349 LEU B CB  1 
ATOM   2635 C CG  . LEU B 2 349 ? 68.910  74.918  44.125 1.00 124.99 ? 349 LEU B CG  1 
ATOM   2636 C CD1 . LEU B 2 349 ? 67.576  74.758  43.432 1.00 163.92 ? 349 LEU B CD1 1 
ATOM   2637 C CD2 . LEU B 2 349 ? 68.722  74.972  45.612 1.00 118.06 ? 349 LEU B CD2 1 
ATOM   2638 N N   . PHE B 2 350 ? 71.668  75.974  42.351 1.00 105.11 ? 350 PHE B N   1 
ATOM   2639 C CA  . PHE B 2 350 ? 71.960  77.372  42.095 1.00 123.85 ? 350 PHE B CA  1 
ATOM   2640 C C   . PHE B 2 350 ? 72.282  77.598  40.619 1.00 116.99 ? 350 PHE B C   1 
ATOM   2641 O O   . PHE B 2 350 ? 71.909  78.632  40.055 1.00 95.88  ? 350 PHE B O   1 
ATOM   2642 C CB  . PHE B 2 350 ? 73.081  77.880  43.018 1.00 135.70 ? 350 PHE B CB  1 
ATOM   2643 C CG  . PHE B 2 350 ? 72.838  77.736  44.503 1.00 143.21 ? 350 PHE B CG  1 
ATOM   2644 C CD1 . PHE B 2 350 ? 71.557  77.661  45.049 1.00 163.33 ? 350 PHE B CD1 1 
ATOM   2645 C CD2 . PHE B 2 350 ? 73.898  77.664  45.381 1.00 161.05 ? 350 PHE B CD2 1 
ATOM   2646 C CE1 . PHE B 2 350 ? 71.345  77.517  46.420 1.00 132.18 ? 350 PHE B CE1 1 
ATOM   2647 C CE2 . PHE B 2 350 ? 73.687  77.533  46.749 1.00 175.98 ? 350 PHE B CE2 1 
ATOM   2648 C CZ  . PHE B 2 350 ? 72.422  77.448  47.265 1.00 183.47 ? 350 PHE B CZ  1 
ATOM   2649 N N   . PHE B 2 351 ? 72.973  76.651  39.985 1.00 101.04 ? 351 PHE B N   1 
ATOM   2650 C CA  . PHE B 2 351 ? 73.229  76.675  38.545 1.00 106.60 ? 351 PHE B CA  1 
ATOM   2651 C C   . PHE B 2 351 ? 71.944  76.753  37.747 1.00 86.21  ? 351 PHE B C   1 
ATOM   2652 O O   . PHE B 2 351 ? 71.862  77.576  36.831 1.00 141.84 ? 351 PHE B O   1 
ATOM   2653 C CB  . PHE B 2 351 ? 74.050  75.449  38.211 1.00 157.10 ? 351 PHE B CB  1 
ATOM   2654 C CG  . PHE B 2 351 ? 74.159  74.996  36.780 1.00 140.12 ? 351 PHE B CG  1 
ATOM   2655 C CD1 . PHE B 2 351 ? 75.052  75.591  35.915 1.00 140.71 ? 351 PHE B CD1 1 
ATOM   2656 C CD2 . PHE B 2 351 ? 73.414  73.918  36.336 1.00 151.01 ? 351 PHE B CD2 1 
ATOM   2657 C CE1 . PHE B 2 351 ? 75.165  75.128  34.625 1.00 187.63 ? 351 PHE B CE1 1 
ATOM   2658 C CE2 . PHE B 2 351 ? 73.535  73.469  35.039 1.00 183.73 ? 351 PHE B CE2 1 
ATOM   2659 C CZ  . PHE B 2 351 ? 74.417  74.063  34.185 1.00 219.16 ? 351 PHE B CZ  1 
ATOM   2660 N N   . VAL B 2 352 ? 70.931  75.949  38.103 1.00 74.75  ? 352 VAL B N   1 
ATOM   2661 C CA  . VAL B 2 352 ? 69.603  76.054  37.500 1.00 95.95  ? 352 VAL B CA  1 
ATOM   2662 C C   . VAL B 2 352 ? 68.912  77.392  37.814 1.00 74.88  ? 352 VAL B C   1 
ATOM   2663 O O   . VAL B 2 352 ? 68.362  78.032  36.935 1.00 121.49 ? 352 VAL B O   1 
ATOM   2664 C CB  . VAL B 2 352 ? 68.713  74.876  37.898 1.00 106.83 ? 352 VAL B CB  1 
ATOM   2665 C CG1 . VAL B 2 352 ? 67.254  75.085  37.499 1.00 126.59 ? 352 VAL B CG1 1 
ATOM   2666 C CG2 . VAL B 2 352 ? 69.280  73.591  37.292 1.00 125.39 ? 352 VAL B CG2 1 
ATOM   2667 N N   . GLY B 2 353 ? 68.958  77.849  39.037 1.00 93.67  ? 353 GLY B N   1 
ATOM   2668 C CA  . GLY B 2 353 ? 68.368  79.118  39.403 1.00 114.68 ? 353 GLY B CA  1 
ATOM   2669 C C   . GLY B 2 353 ? 68.981  80.303  38.680 1.00 117.41 ? 353 GLY B C   1 
ATOM   2670 O O   . GLY B 2 353 ? 68.309  81.301  38.490 1.00 164.43 ? 353 GLY B O   1 
ATOM   2671 N N   . SER B 2 354 ? 70.245  80.198  38.280 1.00 109.56 ? 354 SER B N   1 
ATOM   2672 C CA  . SER B 2 354 ? 70.889  81.221  37.472 1.00 149.21 ? 354 SER B CA  1 
ATOM   2673 C C   . SER B 2 354 ? 70.512  81.084  36.000 1.00 134.34 ? 354 SER B C   1 
ATOM   2674 O O   . SER B 2 354 ? 70.253  82.108  35.355 1.00 156.74 ? 354 SER B O   1 
ATOM   2675 C CB  . SER B 2 354 ? 72.379  81.181  37.699 1.00 170.90 ? 354 SER B CB  1 
ATOM   2676 O OG  . SER B 2 354 ? 73.018  82.263  37.053 1.00 152.56 ? 354 SER B OG  1 
ATOM   2677 N N   . ARG B 2 355 ? 70.483  79.850  35.472 1.00 130.86 ? 355 ARG B N   1 
ATOM   2678 C CA  . ARG B 2 355 ? 70.033  79.584  34.111 1.00 152.57 ? 355 ARG B CA  1 
ATOM   2679 C C   . ARG B 2 355 ? 68.636  80.163  33.857 1.00 144.96 ? 355 ARG B C   1 
ATOM   2680 O O   . ARG B 2 355 ? 68.421  80.810  32.833 1.00 183.13 ? 355 ARG B O   1 
ATOM   2681 C CB  . ARG B 2 355 ? 70.046  78.076  33.876 1.00 166.66 ? 355 ARG B CB  1 
ATOM   2682 C CG  . ARG B 2 355 ? 69.491  77.572  32.554 1.00 208.20 ? 355 ARG B CG  1 
ATOM   2683 C CD  . ARG B 2 355 ? 68.833  76.216  32.748 1.00 212.16 ? 355 ARG B CD  1 
ATOM   2684 N NE  . ARG B 2 355 ? 69.786  75.097  32.839 1.00 209.70 ? 355 ARG B NE  1 
ATOM   2685 C CZ  . ARG B 2 355 ? 69.406  73.832  32.889 1.00 237.62 ? 355 ARG B CZ  1 
ATOM   2686 N NH1 . ARG B 2 355 ? 70.245  72.866  32.560 1.00 255.88 ? 355 ARG B NH1 1 
ATOM   2687 N NH2 . ARG B 2 355 ? 68.157  73.543  33.215 1.00 239.60 ? 355 ARG B NH2 1 
ATOM   2688 N N   . GLU B 2 356 ? 67.702  79.953  34.784 1.00 114.25 ? 356 GLU B N   1 
ATOM   2689 C CA  . GLU B 2 356 ? 66.315  80.396  34.629 1.00 169.90 ? 356 GLU B CA  1 
ATOM   2690 C C   . GLU B 2 356 ? 66.066  81.750  35.326 1.00 181.63 ? 356 GLU B C   1 
ATOM   2691 O O   . GLU B 2 356 ? 64.934  82.033  35.779 1.00 146.92 ? 356 GLU B O   1 
ATOM   2692 C CB  . GLU B 2 356 ? 65.373  79.294  35.126 1.00 198.23 ? 356 GLU B CB  1 
ATOM   2693 C CG  . GLU B 2 356 ? 65.630  77.978  34.410 1.00 247.33 ? 356 GLU B CG  1 
ATOM   2694 C CD  . GLU B 2 356 ? 64.547  76.913  34.462 1.00 338.94 ? 356 GLU B CD  1 
ATOM   2695 O OE1 . GLU B 2 356 ? 63.973  76.697  35.546 1.00 335.79 ? 356 GLU B OE1 1 
ATOM   2696 O OE2 . GLU B 2 356 ? 64.292  76.286  33.404 1.00 408.61 ? 356 GLU B OE2 1 
ATOM   2697 N N   . GLY B 2 357 ? 67.129  82.581  35.438 1.00 146.91 ? 357 GLY B N   1 
ATOM   2698 C CA  . GLY B 2 357 ? 67.013  84.033  35.482 1.00 164.72 ? 357 GLY B CA  1 
ATOM   2699 C C   . GLY B 2 357 ? 66.788  84.640  36.862 1.00 165.06 ? 357 GLY B C   1 
ATOM   2700 O O   . GLY B 2 357 ? 66.622  85.858  36.959 1.00 180.09 ? 357 GLY B O   1 
ATOM   2701 N N   . HIS B 2 358 ? 66.788  83.818  37.923 1.00 171.92 ? 358 HIS B N   1 
ATOM   2702 C CA  . HIS B 2 358 ? 66.545  84.258  39.293 1.00 169.88 ? 358 HIS B CA  1 
ATOM   2703 C C   . HIS B 2 358 ? 67.822  84.662  40.024 1.00 156.50 ? 358 HIS B C   1 
ATOM   2704 O O   . HIS B 2 358 ? 67.713  85.386  41.020 1.00 180.65 ? 358 HIS B O   1 
ATOM   2705 C CB  . HIS B 2 358 ? 65.810  83.154  40.064 1.00 167.36 ? 358 HIS B CB  1 
ATOM   2706 C CG  . HIS B 2 358 ? 64.332  83.154  39.841 1.00 168.92 ? 358 HIS B CG  1 
ATOM   2707 N ND1 . HIS B 2 358 ? 63.467  82.161  40.228 1.00 199.18 ? 358 HIS B ND1 1 
ATOM   2708 C CD2 . HIS B 2 358 ? 63.585  84.086  39.244 1.00 188.74 ? 358 HIS B CD2 1 
ATOM   2709 C CE1 . HIS B 2 358 ? 62.241  82.499  39.867 1.00 236.82 ? 358 HIS B CE1 1 
ATOM   2710 N NE2 . HIS B 2 358 ? 62.297  83.665  39.258 1.00 215.90 ? 358 HIS B NE2 1 
ATOM   2711 N N   . LEU B 2 359 ? 68.993  84.220  39.537 1.00 136.58 ? 359 LEU B N   1 
ATOM   2712 C CA  . LEU B 2 359 ? 70.219  84.322  40.319 1.00 162.89 ? 359 LEU B CA  1 
ATOM   2713 C C   . LEU B 2 359 ? 71.391  84.788  39.439 1.00 154.21 ? 359 LEU B C   1 
ATOM   2714 O O   . LEU B 2 359 ? 71.503  84.326  38.315 1.00 164.96 ? 359 LEU B O   1 
ATOM   2715 C CB  . LEU B 2 359 ? 70.398  82.939  40.952 1.00 140.33 ? 359 LEU B CB  1 
ATOM   2716 C CG  . LEU B 2 359 ? 71.223  82.857  42.229 1.00 175.69 ? 359 LEU B CG  1 
ATOM   2717 C CD1 . LEU B 2 359 ? 70.558  83.565  43.413 1.00 190.99 ? 359 LEU B CD1 1 
ATOM   2718 C CD2 . LEU B 2 359 ? 71.442  81.409  42.588 1.00 145.62 ? 359 LEU B CD2 1 
ATOM   2719 N N   . PRO B 2 360 ? 72.266  85.734  39.893 1.00 145.48 ? 360 PRO B N   1 
ATOM   2720 C CA  . PRO B 2 360 ? 73.231  86.441  39.035 1.00 149.57 ? 360 PRO B CA  1 
ATOM   2721 C C   . PRO B 2 360 ? 74.092  85.562  38.127 1.00 151.17 ? 360 PRO B C   1 
ATOM   2722 O O   . PRO B 2 360 ? 74.466  84.450  38.487 1.00 133.22 ? 360 PRO B O   1 
ATOM   2723 C CB  . PRO B 2 360 ? 74.132  87.241  39.992 1.00 184.85 ? 360 PRO B CB  1 
ATOM   2724 C CG  . PRO B 2 360 ? 73.797  86.723  41.370 1.00 236.65 ? 360 PRO B CG  1 
ATOM   2725 C CD  . PRO B 2 360 ? 72.369  86.238  41.263 1.00 195.31 ? 360 PRO B CD  1 
ATOM   2726 N N   . SER B 2 361 ? 74.375  86.085  36.923 1.00 151.79 ? 361 SER B N   1 
ATOM   2727 C CA  . SER B 2 361 ? 74.616  85.287  35.721 1.00 160.90 ? 361 SER B CA  1 
ATOM   2728 C C   . SER B 2 361 ? 75.842  84.368  35.828 1.00 134.17 ? 361 SER B C   1 
ATOM   2729 O O   . SER B 2 361 ? 75.880  83.280  35.253 1.00 121.37 ? 361 SER B O   1 
ATOM   2730 C CB  . SER B 2 361 ? 74.742  86.160  34.505 1.00 182.28 ? 361 SER B CB  1 
ATOM   2731 O OG  . SER B 2 361 ? 74.873  85.345  33.336 1.00 270.08 ? 361 SER B OG  1 
ATOM   2732 N N   . ILE B 2 362 ? 76.854  84.789  36.592 1.00 127.75 ? 362 ILE B N   1 
ATOM   2733 C CA  . ILE B 2 362 ? 78.102  84.046  36.713 1.00 137.30 ? 362 ILE B CA  1 
ATOM   2734 C C   . ILE B 2 362 ? 77.858  82.624  37.217 1.00 132.89 ? 362 ILE B C   1 
ATOM   2735 O O   . ILE B 2 362 ? 78.582  81.723  36.819 1.00 114.74 ? 362 ILE B O   1 
ATOM   2736 C CB  . ILE B 2 362 ? 79.106  84.857  37.575 1.00 155.17 ? 362 ILE B CB  1 
ATOM   2737 C CG1 . ILE B 2 362 ? 80.466  84.161  37.735 1.00 143.72 ? 362 ILE B CG1 1 
ATOM   2738 C CG2 . ILE B 2 362 ? 78.509  85.274  38.911 1.00 151.25 ? 362 ILE B CG2 1 
ATOM   2739 C CD1 . ILE B 2 362 ? 81.173  83.891  36.427 1.00 142.30 ? 362 ILE B CD1 1 
ATOM   2740 N N   . LEU B 2 363 ? 76.850  82.409  38.080 1.00 152.40 ? 363 LEU B N   1 
ATOM   2741 C CA  . LEU B 2 363 ? 76.575  81.085  38.641 1.00 154.77 ? 363 LEU B CA  1 
ATOM   2742 C C   . LEU B 2 363 ? 76.081  80.080  37.590 1.00 140.48 ? 363 LEU B C   1 
ATOM   2743 O O   . LEU B 2 363 ? 76.179  78.868  37.849 1.00 154.74 ? 363 LEU B O   1 
ATOM   2744 C CB  . LEU B 2 363 ? 75.564  81.186  39.803 1.00 108.46 ? 363 LEU B CB  1 
ATOM   2745 C CG  . LEU B 2 363 ? 75.964  81.988  41.032 1.00 132.83 ? 363 LEU B CG  1 
ATOM   2746 C CD1 . LEU B 2 363 ? 74.960  81.678  42.143 1.00 140.38 ? 363 LEU B CD1 1 
ATOM   2747 C CD2 . LEU B 2 363 ? 77.432  81.763  41.500 1.00 121.44 ? 363 LEU B CD2 1 
ATOM   2748 N N   . SER B 2 364 ? 75.567  80.543  36.440 1.00 95.68  ? 364 SER B N   1 
ATOM   2749 C CA  . SER B 2 364 ? 75.164  79.635  35.383 1.00 128.98 ? 364 SER B CA  1 
ATOM   2750 C C   . SER B 2 364 ? 76.347  79.102  34.559 1.00 125.32 ? 364 SER B C   1 
ATOM   2751 O O   . SER B 2 364 ? 76.159  78.212  33.738 1.00 139.44 ? 364 SER B O   1 
ATOM   2752 C CB  . SER B 2 364 ? 74.149  80.324  34.480 1.00 188.63 ? 364 SER B CB  1 
ATOM   2753 O OG  . SER B 2 364 ? 74.766  81.361  33.701 1.00 236.03 ? 364 SER B OG  1 
ATOM   2754 N N   . MET B 2 365 ? 77.547  79.649  34.719 1.00 119.00 ? 365 MET B N   1 
ATOM   2755 C CA  . MET B 2 365 ? 78.653  79.372  33.813 1.00 131.16 ? 365 MET B CA  1 
ATOM   2756 C C   . MET B 2 365 ? 79.355  78.062  34.190 1.00 104.04 ? 365 MET B C   1 
ATOM   2757 O O   . MET B 2 365 ? 79.225  77.547  35.320 1.00 182.88 ? 365 MET B O   1 
ATOM   2758 C CB  . MET B 2 365 ? 79.627  80.576  33.827 1.00 120.52 ? 365 MET B CB  1 
ATOM   2759 C CG  . MET B 2 365 ? 78.906  81.846  33.403 1.00 182.59 ? 365 MET B CG  1 
ATOM   2760 S SD  . MET B 2 365 ? 79.931  83.237  32.984 1.00 235.33 ? 365 MET B SD  1 
ATOM   2761 C CE  . MET B 2 365 ? 78.694  84.451  32.521 1.00 242.34 ? 365 MET B CE  1 
ATOM   2762 N N   . ILE B 2 366 ? 80.162  77.552  33.244 1.00 90.39  ? 366 ILE B N   1 
ATOM   2763 C CA  . ILE B 2 366 ? 80.836  76.268  33.362 1.00 106.67 ? 366 ILE B CA  1 
ATOM   2764 C C   . ILE B 2 366 ? 82.313  76.405  32.961 1.00 105.44 ? 366 ILE B C   1 
ATOM   2765 O O   . ILE B 2 366 ? 82.635  77.169  32.080 1.00 126.47 ? 366 ILE B O   1 
ATOM   2766 C CB  . ILE B 2 366 ? 80.125  75.257  32.465 1.00 107.05 ? 366 ILE B CB  1 
ATOM   2767 C CG1 . ILE B 2 366 ? 78.627  75.134  32.773 1.00 125.04 ? 366 ILE B CG1 1 
ATOM   2768 C CG2 . ILE B 2 366 ? 80.837  73.904  32.505 1.00 63.52  ? 366 ILE B CG2 1 
ATOM   2769 C CD1 . ILE B 2 366 ? 77.824  74.601  31.550 1.00 254.89 ? 366 ILE B CD1 1 
ATOM   2770 N N   . HIS B 2 367 ? 83.231  75.679  33.588 1.00 120.70 ? 367 HIS B N   1 
ATOM   2771 C CA  . HIS B 2 367 ? 84.630  75.664  33.190 1.00 124.74 ? 367 HIS B CA  1 
ATOM   2772 C C   . HIS B 2 367 ? 84.831  74.670  32.053 1.00 150.15 ? 367 HIS B C   1 
ATOM   2773 O O   . HIS B 2 367 ? 84.705  73.468  32.286 1.00 110.79 ? 367 HIS B O   1 
ATOM   2774 C CB  . HIS B 2 367 ? 85.507  75.289  34.387 1.00 202.38 ? 367 HIS B CB  1 
ATOM   2775 C CG  . HIS B 2 367 ? 86.962  75.241  34.035 1.00 163.14 ? 367 HIS B CG  1 
ATOM   2776 N ND1 . HIS B 2 367 ? 87.749  76.330  33.745 1.00 145.26 ? 367 HIS B ND1 1 
ATOM   2777 C CD2 . HIS B 2 367 ? 87.744  74.197  33.932 1.00 127.10 ? 367 HIS B CD2 1 
ATOM   2778 C CE1 . HIS B 2 367 ? 88.982  75.905  33.482 1.00 229.57 ? 367 HIS B CE1 1 
ATOM   2779 N NE2 . HIS B 2 367 ? 88.997  74.610  33.583 1.00 217.81 ? 367 HIS B NE2 1 
ATOM   2780 N N   . PRO B 2 368 ? 85.131  75.125  30.804 1.00 174.45 ? 368 PRO B N   1 
ATOM   2781 C CA  . PRO B 2 368 ? 84.959  74.289  29.619 1.00 176.88 ? 368 PRO B CA  1 
ATOM   2782 C C   . PRO B 2 368 ? 85.914  73.099  29.462 1.00 180.33 ? 368 PRO B C   1 
ATOM   2783 O O   . PRO B 2 368 ? 85.549  72.153  28.775 1.00 201.40 ? 368 PRO B O   1 
ATOM   2784 C CB  . PRO B 2 368 ? 85.120  75.284  28.472 1.00 168.21 ? 368 PRO B CB  1 
ATOM   2785 C CG  . PRO B 2 368 ? 86.025  76.354  29.023 1.00 167.99 ? 368 PRO B CG  1 
ATOM   2786 C CD  . PRO B 2 368 ? 85.610  76.466  30.459 1.00 156.92 ? 368 PRO B CD  1 
ATOM   2787 N N   . GLN B 2 369 ? 87.097  73.105  30.090 1.00 154.29 ? 369 GLN B N   1 
ATOM   2788 C CA  . GLN B 2 369 ? 87.986  71.950  30.021 1.00 188.56 ? 369 GLN B CA  1 
ATOM   2789 C C   . GLN B 2 369 ? 87.535  70.779  30.917 1.00 224.53 ? 369 GLN B C   1 
ATOM   2790 O O   . GLN B 2 369 ? 87.924  69.641  30.642 1.00 250.37 ? 369 GLN B O   1 
ATOM   2791 C CB  . GLN B 2 369 ? 89.407  72.381  30.394 1.00 239.35 ? 369 GLN B CB  1 
ATOM   2792 C CG  . GLN B 2 369 ? 90.030  73.358  29.397 1.00 265.48 ? 369 GLN B CG  1 
ATOM   2793 C CD  . GLN B 2 369 ? 91.487  73.663  29.673 1.00 351.68 ? 369 GLN B CD  1 
ATOM   2794 O OE1 . GLN B 2 369 ? 92.057  73.246  30.682 1.00 396.63 ? 369 GLN B OE1 1 
ATOM   2795 N NE2 . GLN B 2 369 ? 92.112  74.406  28.770 1.00 373.24 ? 369 GLN B NE2 1 
ATOM   2796 N N   . LEU B 2 370 ? 86.747  71.034  31.987 1.00 181.38 ? 370 LEU B N   1 
ATOM   2797 C CA  . LEU B 2 370 ? 86.359  70.025  32.978 1.00 171.11 ? 370 LEU B CA  1 
ATOM   2798 C C   . LEU B 2 370 ? 84.847  69.752  33.047 1.00 179.71 ? 370 LEU B C   1 
ATOM   2799 O O   . LEU B 2 370 ? 84.438  68.700  33.589 1.00 127.75 ? 370 LEU B O   1 
ATOM   2800 C CB  . LEU B 2 370 ? 86.848  70.513  34.346 1.00 137.96 ? 370 LEU B CB  1 
ATOM   2801 C CG  . LEU B 2 370 ? 88.354  70.670  34.515 1.00 160.69 ? 370 LEU B CG  1 
ATOM   2802 C CD1 . LEU B 2 370 ? 88.639  71.222  35.906 1.00 137.87 ? 370 LEU B CD1 1 
ATOM   2803 C CD2 . LEU B 2 370 ? 89.113  69.354  34.284 1.00 221.55 ? 370 LEU B CD2 1 
ATOM   2804 N N   . LEU B 2 371 ? 84.042  70.704  32.519 1.00 155.66 ? 371 LEU B N   1 
ATOM   2805 C CA  . LEU B 2 371 ? 82.585  70.701  32.484 1.00 145.69 ? 371 LEU B CA  1 
ATOM   2806 C C   . LEU B 2 371 ? 81.962  70.690  33.899 1.00 132.33 ? 371 LEU B C   1 
ATOM   2807 O O   . LEU B 2 371 ? 80.884  70.096  34.113 1.00 220.69 ? 371 LEU B O   1 
ATOM   2808 C CB  . LEU B 2 371 ? 82.123  69.529  31.606 1.00 192.19 ? 371 LEU B CB  1 
ATOM   2809 C CG  . LEU B 2 371 ? 82.771  69.388  30.227 1.00 202.61 ? 371 LEU B CG  1 
ATOM   2810 C CD1 . LEU B 2 371 ? 82.184  68.205  29.490 1.00 298.27 ? 371 LEU B CD1 1 
ATOM   2811 C CD2 . LEU B 2 371 ? 82.608  70.640  29.405 1.00 229.70 ? 371 LEU B CD2 1 
ATOM   2812 N N   . THR B 2 372 ? 82.606  71.384  34.855 1.00 123.41 ? 372 THR B N   1 
ATOM   2813 C CA  . THR B 2 372 ? 82.126  71.529  36.230 1.00 116.41 ? 372 THR B CA  1 
ATOM   2814 C C   . THR B 2 372 ? 81.665  72.950  36.509 1.00 91.29  ? 372 THR B C   1 
ATOM   2815 O O   . THR B 2 372 ? 82.258  73.901  36.004 1.00 153.66 ? 372 THR B O   1 
ATOM   2816 C CB  . THR B 2 372 ? 83.219  71.142  37.228 1.00 162.77 ? 372 THR B CB  1 
ATOM   2817 O OG1 . THR B 2 372 ? 84.398  71.922  36.977 1.00 111.50 ? 372 THR B OG1 1 
ATOM   2818 C CG2 . THR B 2 372 ? 83.506  69.653  37.153 1.00 191.27 ? 372 THR B CG2 1 
ATOM   2819 N N   . PRO B 2 373 ? 80.565  73.142  37.261 1.00 95.36  ? 373 PRO B N   1 
ATOM   2820 C CA  . PRO B 2 373 ? 79.987  74.464  37.467 1.00 120.97 ? 373 PRO B CA  1 
ATOM   2821 C C   . PRO B 2 373 ? 80.721  75.296  38.505 1.00 121.19 ? 373 PRO B C   1 
ATOM   2822 O O   . PRO B 2 373 ? 80.088  75.716  39.463 1.00 120.18 ? 373 PRO B O   1 
ATOM   2823 C CB  . PRO B 2 373 ? 78.538  74.118  37.904 1.00 160.26 ? 373 PRO B CB  1 
ATOM   2824 C CG  . PRO B 2 373 ? 78.659  72.825  38.634 1.00 125.93 ? 373 PRO B CG  1 
ATOM   2825 C CD  . PRO B 2 373 ? 79.773  72.093  37.914 1.00 111.74 ? 373 PRO B CD  1 
ATOM   2826 N N   . VAL B 2 374 ? 82.026  75.560  38.268 1.00 109.01 ? 374 VAL B N   1 
ATOM   2827 C CA  . VAL B 2 374 ? 82.974  76.159  39.219 1.00 100.60 ? 374 VAL B CA  1 
ATOM   2828 C C   . VAL B 2 374 ? 82.456  77.359  40.014 1.00 82.98  ? 374 VAL B C   1 
ATOM   2829 O O   . VAL B 2 374 ? 82.558  77.304  41.249 1.00 139.13 ? 374 VAL B O   1 
ATOM   2830 C CB  . VAL B 2 374 ? 84.282  76.488  38.533 1.00 112.04 ? 374 VAL B CB  1 
ATOM   2831 C CG1 . VAL B 2 374 ? 85.168  77.407  39.347 1.00 130.42 ? 374 VAL B CG1 1 
ATOM   2832 C CG2 . VAL B 2 374 ? 84.974  75.152  38.263 1.00 131.69 ? 374 VAL B CG2 1 
ATOM   2833 N N   . PRO B 2 375 ? 81.826  78.383  39.429 1.00 84.95  ? 375 PRO B N   1 
ATOM   2834 C CA  . PRO B 2 375 ? 81.348  79.505  40.232 1.00 125.51 ? 375 PRO B CA  1 
ATOM   2835 C C   . PRO B 2 375 ? 80.243  79.128  41.220 1.00 120.19 ? 375 PRO B C   1 
ATOM   2836 O O   . PRO B 2 375 ? 80.219  79.671  42.320 1.00 152.66 ? 375 PRO B O   1 
ATOM   2837 C CB  . PRO B 2 375 ? 80.821  80.513  39.209 1.00 166.10 ? 375 PRO B CB  1 
ATOM   2838 C CG  . PRO B 2 375 ? 81.433  80.041  37.897 1.00 214.29 ? 375 PRO B CG  1 
ATOM   2839 C CD  . PRO B 2 375 ? 81.495  78.533  38.026 1.00 111.81 ? 375 PRO B CD  1 
ATOM   2840 N N   . SER B 2 376 ? 79.356  78.191  40.848 1.00 118.20 ? 376 SER B N   1 
ATOM   2841 C CA  . SER B 2 376 ? 78.315  77.728  41.746 1.00 135.04 ? 376 SER B CA  1 
ATOM   2842 C C   . SER B 2 376 ? 78.907  76.946  42.927 1.00 122.11 ? 376 SER B C   1 
ATOM   2843 O O   . SER B 2 376 ? 78.503  77.142  44.073 1.00 114.94 ? 376 SER B O   1 
ATOM   2844 C CB  . SER B 2 376 ? 77.300  76.930  40.985 1.00 160.83 ? 376 SER B CB  1 
ATOM   2845 O OG  . SER B 2 376 ? 76.271  76.504  41.857 1.00 228.80 ? 376 SER B OG  1 
ATOM   2846 N N   . LEU B 2 377 ? 79.854  76.036  42.671 1.00 96.28  ? 377 LEU B N   1 
ATOM   2847 C CA  . LEU B 2 377 ? 80.521  75.330  43.757 1.00 84.59  ? 377 LEU B CA  1 
ATOM   2848 C C   . LEU B 2 377 ? 81.266  76.284  44.688 1.00 91.91  ? 377 LEU B C   1 
ATOM   2849 O O   . LEU B 2 377 ? 81.153  76.166  45.898 1.00 119.70 ? 377 LEU B O   1 
ATOM   2850 C CB  . LEU B 2 377 ? 81.477  74.278  43.203 1.00 81.32  ? 377 LEU B CB  1 
ATOM   2851 C CG  . LEU B 2 377 ? 80.776  73.000  42.794 1.00 88.84  ? 377 LEU B CG  1 
ATOM   2852 C CD1 . LEU B 2 377 ? 81.694  72.141  41.959 1.00 90.46  ? 377 LEU B CD1 1 
ATOM   2853 C CD2 . LEU B 2 377 ? 80.399  72.201  44.001 1.00 147.93 ? 377 LEU B CD2 1 
ATOM   2854 N N   . VAL B 2 378 ? 82.015  77.238  44.159 1.00 99.90  ? 378 VAL B N   1 
ATOM   2855 C CA  . VAL B 2 378 ? 82.728  78.197  44.988 1.00 95.48  ? 378 VAL B CA  1 
ATOM   2856 C C   . VAL B 2 378 ? 81.757  79.046  45.791 1.00 88.72  ? 378 VAL B C   1 
ATOM   2857 O O   . VAL B 2 378 ? 82.080  79.385  46.926 1.00 157.32 ? 378 VAL B O   1 
ATOM   2858 C CB  . VAL B 2 378 ? 83.685  79.020  44.112 1.00 108.90 ? 378 VAL B CB  1 
ATOM   2859 C CG1 . VAL B 2 378 ? 84.101  80.396  44.647 1.00 108.10 ? 378 VAL B CG1 1 
ATOM   2860 C CG2 . VAL B 2 378 ? 84.875  78.106  43.798 1.00 120.55 ? 378 VAL B CG2 1 
ATOM   2861 N N   . PHE B 2 379 ? 80.585  79.367  45.267 1.00 78.03  ? 379 PHE B N   1 
ATOM   2862 C CA  . PHE B 2 379 ? 79.600  80.084  46.057 1.00 89.78  ? 379 PHE B CA  1 
ATOM   2863 C C   . PHE B 2 379 ? 79.001  79.224  47.142 1.00 79.27  ? 379 PHE B C   1 
ATOM   2864 O O   . PHE B 2 379 ? 79.007  79.681  48.296 1.00 127.11 ? 379 PHE B O   1 
ATOM   2865 C CB  . PHE B 2 379 ? 78.456  80.592  45.184 1.00 143.95 ? 379 PHE B CB  1 
ATOM   2866 C CG  . PHE B 2 379 ? 77.402  81.344  45.950 1.00 96.45  ? 379 PHE B CG  1 
ATOM   2867 C CD1 . PHE B 2 379 ? 77.586  82.671  46.296 1.00 137.06 ? 379 PHE B CD1 1 
ATOM   2868 C CD2 . PHE B 2 379 ? 76.238  80.726  46.291 1.00 92.69  ? 379 PHE B CD2 1 
ATOM   2869 C CE1 . PHE B 2 379 ? 76.605  83.378  46.975 1.00 166.99 ? 379 PHE B CE1 1 
ATOM   2870 C CE2 . PHE B 2 379 ? 75.259  81.408  46.988 1.00 157.63 ? 379 PHE B CE2 1 
ATOM   2871 C CZ  . PHE B 2 379 ? 75.441  82.737  47.334 1.00 193.63 ? 379 PHE B CZ  1 
ATOM   2872 N N   . THR B 2 380 ? 78.489  78.014  46.843 1.00 92.48  ? 380 THR B N   1 
ATOM   2873 C CA  . THR B 2 380 ? 77.835  77.214  47.891 1.00 136.87 ? 380 THR B CA  1 
ATOM   2874 C C   . THR B 2 380 ? 78.827  76.832  49.001 1.00 110.24 ? 380 THR B C   1 
ATOM   2875 O O   . THR B 2 380 ? 78.441  76.762  50.171 1.00 108.87 ? 380 THR B O   1 
ATOM   2876 C CB  . THR B 2 380 ? 77.077  75.994  47.333 1.00 130.64 ? 380 THR B CB  1 
ATOM   2877 O OG1 . THR B 2 380 ? 76.212  75.501  48.374 1.00 189.80 ? 380 THR B OG1 1 
ATOM   2878 C CG2 . THR B 2 380 ? 77.981  74.895  46.822 1.00 77.68  ? 380 THR B CG2 1 
ATOM   2879 N N   . CYS B 2 381 ? 80.082  76.582  48.645 1.00 81.82  ? 381 CYS B N   1 
ATOM   2880 C CA  . CYS B 2 381 ? 81.147  76.435  49.596 1.00 92.20  ? 381 CYS B CA  1 
ATOM   2881 C C   . CYS B 2 381 ? 81.265  77.665  50.505 1.00 84.22  ? 381 CYS B C   1 
ATOM   2882 O O   . CYS B 2 381 ? 81.126  77.562  51.698 1.00 92.21  ? 381 CYS B O   1 
ATOM   2883 C CB  . CYS B 2 381 ? 82.458  76.202  48.857 1.00 111.32 ? 381 CYS B CB  1 
ATOM   2884 S SG  . CYS B 2 381 ? 83.875  76.091  49.989 1.00 135.84 ? 381 CYS B SG  1 
ATOM   2885 N N   . VAL B 2 382 ? 81.575  78.842  49.981 1.00 117.84 ? 382 VAL B N   1 
ATOM   2886 C CA  . VAL B 2 382 ? 81.758  80.028  50.810 1.00 111.59 ? 382 VAL B CA  1 
ATOM   2887 C C   . VAL B 2 382 ? 80.510  80.275  51.643 1.00 110.33 ? 382 VAL B C   1 
ATOM   2888 O O   . VAL B 2 382 ? 80.648  80.651  52.779 1.00 142.27 ? 382 VAL B O   1 
ATOM   2889 C CB  . VAL B 2 382 ? 82.114  81.244  49.930 1.00 141.68 ? 382 VAL B CB  1 
ATOM   2890 C CG1 . VAL B 2 382 ? 81.717  82.625  50.474 1.00 162.06 ? 382 VAL B CG1 1 
ATOM   2891 C CG2 . VAL B 2 382 ? 83.595  81.139  49.640 1.00 171.09 ? 382 VAL B CG2 1 
ATOM   2892 N N   . MET B 2 383 ? 79.313  80.086  51.096 1.00 104.09 ? 383 MET B N   1 
ATOM   2893 C CA  . MET B 2 383 ? 78.091  80.317  51.828 1.00 113.03 ? 383 MET B CA  1 
ATOM   2894 C C   . MET B 2 383 ? 77.978  79.336  53.005 1.00 119.46 ? 383 MET B C   1 
ATOM   2895 O O   . MET B 2 383 ? 77.379  79.675  54.013 1.00 103.82 ? 383 MET B O   1 
ATOM   2896 C CB  . MET B 2 383 ? 76.920  80.150  50.858 1.00 136.84 ? 383 MET B CB  1 
ATOM   2897 C CG  . MET B 2 383 ? 75.662  80.795  51.340 1.00 152.28 ? 383 MET B CG  1 
ATOM   2898 S SD  . MET B 2 383 ? 75.752  82.573  51.187 1.00 198.13 ? 383 MET B SD  1 
ATOM   2899 C CE  . MET B 2 383 ? 74.159  82.988  51.909 1.00 236.80 ? 383 MET B CE  1 
ATOM   2900 N N   . THR B 2 384 ? 78.542  78.119  52.904 1.00 101.63 ? 384 THR B N   1 
ATOM   2901 C CA  . THR B 2 384 ? 78.564  77.146  53.996 1.00 88.50  ? 384 THR B CA  1 
ATOM   2902 C C   . THR B 2 384 ? 79.539  77.559  55.079 1.00 70.31  ? 384 THR B C   1 
ATOM   2903 O O   . THR B 2 384 ? 79.224  77.453  56.239 1.00 72.41  ? 384 THR B O   1 
ATOM   2904 C CB  . THR B 2 384 ? 78.989  75.746  53.528 1.00 90.02  ? 384 THR B CB  1 
ATOM   2905 O OG1 . THR B 2 384 ? 78.040  75.350  52.528 1.00 126.52 ? 384 THR B OG1 1 
ATOM   2906 C CG2 . THR B 2 384 ? 79.077  74.695  54.615 1.00 68.18  ? 384 THR B CG2 1 
ATOM   2907 N N   . LEU B 2 385 ? 80.727  78.054  54.729 1.00 73.53  ? 385 LEU B N   1 
ATOM   2908 C CA  . LEU B 2 385 ? 81.717  78.411  55.731 1.00 82.71  ? 385 LEU B CA  1 
ATOM   2909 C C   . LEU B 2 385 ? 81.266  79.601  56.584 1.00 99.14  ? 385 LEU B C   1 
ATOM   2910 O O   . LEU B 2 385 ? 81.690  79.710  57.716 1.00 122.81 ? 385 LEU B O   1 
ATOM   2911 C CB  . LEU B 2 385 ? 83.037  78.716  55.042 1.00 78.59  ? 385 LEU B CB  1 
ATOM   2912 C CG  . LEU B 2 385 ? 83.627  77.553  54.237 1.00 107.30 ? 385 LEU B CG  1 
ATOM   2913 C CD1 . LEU B 2 385 ? 84.930  77.991  53.600 1.00 150.39 ? 385 LEU B CD1 1 
ATOM   2914 C CD2 . LEU B 2 385 ? 83.785  76.319  55.115 1.00 104.03 ? 385 LEU B CD2 1 
ATOM   2915 N N   . LEU B 2 386 ? 80.387  80.472  56.108 1.00 88.22  ? 386 LEU B N   1 
ATOM   2916 C CA  . LEU B 2 386 ? 79.861  81.542  56.933 1.00 114.16 ? 386 LEU B CA  1 
ATOM   2917 C C   . LEU B 2 386 ? 79.067  81.029  58.155 1.00 114.07 ? 386 LEU B C   1 
ATOM   2918 O O   . LEU B 2 386 ? 78.949  81.771  59.148 1.00 170.49 ? 386 LEU B O   1 
ATOM   2919 C CB  . LEU B 2 386 ? 78.990  82.472  56.087 1.00 131.41 ? 386 LEU B CB  1 
ATOM   2920 C CG  . LEU B 2 386 ? 79.717  83.216  54.975 1.00 159.58 ? 386 LEU B CG  1 
ATOM   2921 C CD1 . LEU B 2 386 ? 78.723  84.101  54.235 1.00 238.77 ? 386 LEU B CD1 1 
ATOM   2922 C CD2 . LEU B 2 386 ? 80.932  84.031  55.457 1.00 183.94 ? 386 LEU B CD2 1 
ATOM   2923 N N   . TYR B 2 387 ? 78.562  79.797  58.126 1.00 72.18  ? 387 TYR B N   1 
ATOM   2924 C CA  . TYR B 2 387 ? 77.910  79.228  59.294 1.00 105.64 ? 387 TYR B CA  1 
ATOM   2925 C C   . TYR B 2 387 ? 78.892  78.862  60.418 1.00 98.84  ? 387 TYR B C   1 
ATOM   2926 O O   . TYR B 2 387 ? 78.452  78.595  61.535 1.00 97.32  ? 387 TYR B O   1 
ATOM   2927 C CB  . TYR B 2 387 ? 76.976  78.083  58.843 1.00 126.08 ? 387 TYR B CB  1 
ATOM   2928 C CG  . TYR B 2 387 ? 75.662  78.657  58.358 1.00 115.17 ? 387 TYR B CG  1 
ATOM   2929 C CD1 . TYR B 2 387 ? 75.528  79.169  57.106 1.00 148.17 ? 387 TYR B CD1 1 
ATOM   2930 C CD2 . TYR B 2 387 ? 74.582  78.752  59.201 1.00 124.59 ? 387 TYR B CD2 1 
ATOM   2931 C CE1 . TYR B 2 387 ? 74.337  79.747  56.698 1.00 216.88 ? 387 TYR B CE1 1 
ATOM   2932 C CE2 . TYR B 2 387 ? 73.392  79.321  58.815 1.00 126.54 ? 387 TYR B CE2 1 
ATOM   2933 C CZ  . TYR B 2 387 ? 73.259  79.815  57.551 1.00 179.22 ? 387 TYR B CZ  1 
ATOM   2934 O OH  . TYR B 2 387 ? 72.079  80.384  57.190 1.00 243.96 ? 387 TYR B OH  1 
ATOM   2935 N N   . ALA B 2 388 ? 80.191  78.886  60.178 1.00 80.53  ? 388 ALA B N   1 
ATOM   2936 C CA  . ALA B 2 388 ? 81.153  78.834  61.266 1.00 134.95 ? 388 ALA B CA  1 
ATOM   2937 C C   . ALA B 2 388 ? 80.999  79.963  62.309 1.00 153.57 ? 388 ALA B C   1 
ATOM   2938 O O   . ALA B 2 388 ? 81.417  79.778  63.462 1.00 230.15 ? 388 ALA B O   1 
ATOM   2939 C CB  . ALA B 2 388 ? 82.558  78.793  60.685 1.00 164.90 ? 388 ALA B CB  1 
ATOM   2940 N N   . PHE B 2 389 ? 80.428  81.113  61.943 1.00 112.75 ? 389 PHE B N   1 
ATOM   2941 C CA  . PHE B 2 389 ? 80.193  82.194  62.887 1.00 160.88 ? 389 PHE B CA  1 
ATOM   2942 C C   . PHE B 2 389 ? 78.889  81.999  63.669 1.00 201.05 ? 389 PHE B C   1 
ATOM   2943 O O   . PHE B 2 389 ? 78.307  82.991  64.126 1.00 298.63 ? 389 PHE B O   1 
ATOM   2944 C CB  . PHE B 2 389 ? 80.189  83.533  62.128 1.00 195.40 ? 389 PHE B CB  1 
ATOM   2945 C CG  . PHE B 2 389 ? 81.438  83.791  61.324 1.00 149.91 ? 389 PHE B CG  1 
ATOM   2946 C CD1 . PHE B 2 389 ? 82.681  83.591  61.899 1.00 164.39 ? 389 PHE B CD1 1 
ATOM   2947 C CD2 . PHE B 2 389 ? 81.376  84.241  60.018 1.00 191.19 ? 389 PHE B CD2 1 
ATOM   2948 C CE1 . PHE B 2 389 ? 83.846  83.831  61.186 1.00 175.18 ? 389 PHE B CE1 1 
ATOM   2949 C CE2 . PHE B 2 389 ? 82.540  84.480  59.298 1.00 257.46 ? 389 PHE B CE2 1 
ATOM   2950 C CZ  . PHE B 2 389 ? 83.772  84.277  59.885 1.00 249.08 ? 389 PHE B CZ  1 
ATOM   2951 N N   . SER B 2 390 ? 78.435  80.735  63.819 1.00 121.30 ? 390 SER B N   1 
ATOM   2952 C CA  . SER B 2 390 ? 77.244  80.417  64.588 1.00 186.94 ? 390 SER B CA  1 
ATOM   2953 C C   . SER B 2 390 ? 77.653  79.612  65.822 1.00 207.06 ? 390 SER B C   1 
ATOM   2954 O O   . SER B 2 390 ? 78.468  78.697  65.695 1.00 244.80 ? 390 SER B O   1 
ATOM   2955 C CB  . SER B 2 390 ? 76.254  79.696  63.714 1.00 176.02 ? 390 SER B CB  1 
ATOM   2956 O OG  . SER B 2 390 ? 75.013  79.529  64.383 1.00 243.34 ? 390 SER B OG  1 
ATOM   2957 N N   . LYS B 2 391 ? 77.086  79.964  66.999 1.00 202.92 ? 391 LYS B N   1 
ATOM   2958 C CA  . LYS B 2 391 ? 77.390  79.273  68.246 1.00 224.92 ? 391 LYS B CA  1 
ATOM   2959 C C   . LYS B 2 391 ? 76.541  78.000  68.352 1.00 210.08 ? 391 LYS B C   1 
ATOM   2960 O O   . LYS B 2 391 ? 77.080  76.894  68.209 1.00 212.28 ? 391 LYS B O   1 
ATOM   2961 C CB  . LYS B 2 391 ? 77.230  80.218  69.447 1.00 282.10 ? 391 LYS B CB  1 
ATOM   2962 C CG  . LYS B 2 391 ? 77.705  79.641  70.781 1.00 376.24 ? 391 LYS B CG  1 
ATOM   2963 C CD  . LYS B 2 391 ? 79.225  79.524  70.895 1.00 438.25 ? 391 LYS B CD  1 
ATOM   2964 C CE  . LYS B 2 391 ? 79.726  79.002  72.229 1.00 486.39 ? 391 LYS B CE  1 
ATOM   2965 N NZ  . LYS B 2 391 ? 79.802  77.521  72.266 1.00 514.30 ? 391 LYS B NZ  1 
ATOM   2966 N N   . ASP B 2 392 ? 75.226  78.137  68.613 1.00 225.24 ? 392 ASP B N   1 
ATOM   2967 C CA  . ASP B 2 392 ? 74.344  76.985  68.778 1.00 287.77 ? 392 ASP B CA  1 
ATOM   2968 C C   . ASP B 2 392 ? 73.712  76.634  67.430 1.00 227.79 ? 392 ASP B C   1 
ATOM   2969 O O   . ASP B 2 392 ? 72.498  76.761  67.250 1.00 278.66 ? 392 ASP B O   1 
ATOM   2970 C CB  . ASP B 2 392 ? 73.309  77.232  69.888 1.00 381.70 ? 392 ASP B CB  1 
ATOM   2971 C CG  . ASP B 2 392 ? 72.553  75.995  70.360 1.00 406.28 ? 392 ASP B CG  1 
ATOM   2972 O OD1 . ASP B 2 392 ? 72.851  74.884  69.879 1.00 358.03 ? 392 ASP B OD1 1 
ATOM   2973 O OD2 . ASP B 2 392 ? 71.661  76.154  71.217 1.00 439.06 ? 392 ASP B OD2 1 
ATOM   2974 N N   . ILE B 2 393 ? 74.546  76.163  66.489 1.00 171.11 ? 393 ILE B N   1 
ATOM   2975 C CA  . ILE B 2 393 ? 74.117  75.911  65.113 1.00 244.31 ? 393 ILE B CA  1 
ATOM   2976 C C   . ILE B 2 393 ? 73.064  74.794  65.036 1.00 265.27 ? 393 ILE B C   1 
ATOM   2977 O O   . ILE B 2 393 ? 72.188  74.828  64.170 1.00 246.58 ? 393 ILE B O   1 
ATOM   2978 C CB  . ILE B 2 393 ? 75.328  75.640  64.184 1.00 259.57 ? 393 ILE B CB  1 
ATOM   2979 C CG1 . ILE B 2 393 ? 74.943  75.378  62.719 1.00 246.13 ? 393 ILE B CG1 1 
ATOM   2980 C CG2 . ILE B 2 393 ? 76.195  74.517  64.697 1.00 243.12 ? 393 ILE B CG2 1 
ATOM   2981 C CD1 . ILE B 2 393 ? 74.185  76.507  62.073 1.00 240.03 ? 393 ILE B CD1 1 
ATOM   2982 N N   . PHE B 2 394 ? 73.125  73.795  65.930 1.00 201.35 ? 394 PHE B N   1 
ATOM   2983 C CA  . PHE B 2 394 ? 72.158  72.696  65.890 1.00 171.34 ? 394 PHE B CA  1 
ATOM   2984 C C   . PHE B 2 394 ? 70.713  73.133  66.173 1.00 147.93 ? 394 PHE B C   1 
ATOM   2985 O O   . PHE B 2 394 ? 69.803  72.361  65.821 1.00 162.92 ? 394 PHE B O   1 
ATOM   2986 C CB  . PHE B 2 394 ? 72.617  71.555  66.793 1.00 167.65 ? 394 PHE B CB  1 
ATOM   2987 C CG  . PHE B 2 394 ? 73.812  70.856  66.199 1.00 182.55 ? 394 PHE B CG  1 
ATOM   2988 C CD1 . PHE B 2 394 ? 75.089  71.358  66.427 1.00 197.17 ? 394 PHE B CD1 1 
ATOM   2989 C CD2 . PHE B 2 394 ? 73.661  69.721  65.401 1.00 169.88 ? 394 PHE B CD2 1 
ATOM   2990 C CE1 . PHE B 2 394 ? 76.202  70.729  65.892 1.00 274.58 ? 394 PHE B CE1 1 
ATOM   2991 C CE2 . PHE B 2 394 ? 74.778  69.106  64.867 1.00 218.73 ? 394 PHE B CE2 1 
ATOM   2992 C CZ  . PHE B 2 394 ? 76.039  69.617  65.111 1.00 265.79 ? 394 PHE B CZ  1 
ATOM   2993 N N   . SER B 2 395 ? 70.523  74.335  66.758 1.00 185.02 ? 395 SER B N   1 
ATOM   2994 C CA  . SER B 2 395 ? 69.227  75.005  66.833 1.00 168.12 ? 395 SER B CA  1 
ATOM   2995 C C   . SER B 2 395 ? 68.554  75.112  65.463 1.00 240.78 ? 395 SER B C   1 
ATOM   2996 O O   . SER B 2 395 ? 67.338  74.980  65.378 1.00 294.98 ? 395 SER B O   1 
ATOM   2997 C CB  . SER B 2 395 ? 69.371  76.373  67.461 1.00 195.77 ? 395 SER B CB  1 
ATOM   2998 O OG  . SER B 2 395 ? 68.107  76.981  67.672 1.00 259.88 ? 395 SER B OG  1 
ATOM   2999 N N   . VAL B 2 396 ? 69.322  75.326  64.376 1.00 251.68 ? 396 VAL B N   1 
ATOM   3000 C CA  . VAL B 2 396 ? 68.783  75.576  63.037 1.00 248.67 ? 396 VAL B CA  1 
ATOM   3001 C C   . VAL B 2 396 ? 68.049  74.347  62.467 1.00 172.01 ? 396 VAL B C   1 
ATOM   3002 O O   . VAL B 2 396 ? 67.288  74.490  61.519 1.00 168.73 ? 396 VAL B O   1 
ATOM   3003 C CB  . VAL B 2 396 ? 69.878  76.132  62.096 1.00 229.61 ? 396 VAL B CB  1 
ATOM   3004 C CG1 . VAL B 2 396 ? 69.355  76.407  60.694 1.00 284.62 ? 396 VAL B CG1 1 
ATOM   3005 C CG2 . VAL B 2 396 ? 70.474  77.420  62.655 1.00 269.75 ? 396 VAL B CG2 1 
ATOM   3006 N N   . ILE B 2 397 ? 68.214  73.152  63.041 1.00 188.16 ? 397 ILE B N   1 
ATOM   3007 C CA  . ILE B 2 397 ? 67.435  71.977  62.660 1.00 203.08 ? 397 ILE B CA  1 
ATOM   3008 C C   . ILE B 2 397 ? 65.920  72.195  62.846 1.00 189.62 ? 397 ILE B C   1 
ATOM   3009 O O   . ILE B 2 397 ? 65.156  71.627  62.069 1.00 222.66 ? 397 ILE B O   1 
ATOM   3010 C CB  . ILE B 2 397 ? 67.973  70.724  63.391 1.00 205.91 ? 397 ILE B CB  1 
ATOM   3011 C CG1 . ILE B 2 397 ? 69.386  70.391  62.938 1.00 145.20 ? 397 ILE B CG1 1 
ATOM   3012 C CG2 . ILE B 2 397 ? 67.104  69.488  63.213 1.00 200.00 ? 397 ILE B CG2 1 
ATOM   3013 C CD1 . ILE B 2 397 ? 70.073  69.380  63.849 1.00 186.52 ? 397 ILE B CD1 1 
ATOM   3014 N N   . ASN B 2 398 ? 65.441  73.006  63.803 1.00 156.15 ? 398 ASN B N   1 
ATOM   3015 C CA  . ASN B 2 398 ? 64.009  73.321  63.837 1.00 249.85 ? 398 ASN B CA  1 
ATOM   3016 C C   . ASN B 2 398 ? 63.594  74.135  62.587 1.00 289.09 ? 398 ASN B C   1 
ATOM   3017 O O   . ASN B 2 398 ? 62.637  73.730  61.906 1.00 248.22 ? 398 ASN B O   1 
ATOM   3018 C CB  . ASN B 2 398 ? 63.558  73.874  65.207 1.00 295.12 ? 398 ASN B CB  1 
ATOM   3019 C CG  . ASN B 2 398 ? 64.167  75.183  65.676 1.00 326.54 ? 398 ASN B CG  1 
ATOM   3020 O OD1 . ASN B 2 398 ? 64.531  76.047  64.886 1.00 372.54 ? 398 ASN B OD1 1 
ATOM   3021 N ND2 . ASN B 2 398 ? 64.269  75.353  66.984 1.00 335.51 ? 398 ASN B ND2 1 
ATOM   3022 N N   . PHE B 2 399 ? 64.296  75.242  62.251 1.00 289.80 ? 399 PHE B N   1 
ATOM   3023 C CA  . PHE B 2 399 ? 64.032  76.034  61.042 1.00 270.40 ? 399 PHE B CA  1 
ATOM   3024 C C   . PHE B 2 399 ? 64.141  75.186  59.764 1.00 226.72 ? 399 PHE B C   1 
ATOM   3025 O O   . PHE B 2 399 ? 63.269  75.276  58.902 1.00 136.68 ? 399 PHE B O   1 
ATOM   3026 C CB  . PHE B 2 399 ? 64.946  77.268  61.008 1.00 251.32 ? 399 PHE B CB  1 
ATOM   3027 C CG  . PHE B 2 399 ? 64.576  78.319  62.034 1.00 357.12 ? 399 PHE B CG  1 
ATOM   3028 C CD1 . PHE B 2 399 ? 63.382  79.036  61.929 1.00 393.56 ? 399 PHE B CD1 1 
ATOM   3029 C CD2 . PHE B 2 399 ? 65.403  78.591  63.123 1.00 371.13 ? 399 PHE B CD2 1 
ATOM   3030 C CE1 . PHE B 2 399 ? 63.032  79.998  62.872 1.00 379.01 ? 399 PHE B CE1 1 
ATOM   3031 C CE2 . PHE B 2 399 ? 65.052  79.556  64.067 1.00 362.37 ? 399 PHE B CE2 1 
ATOM   3032 C CZ  . PHE B 2 399 ? 63.867  80.259  63.941 1.00 343.25 ? 399 PHE B CZ  1 
ATOM   3033 N N   . PHE B 2 400 ? 65.193  74.357  59.643 1.00 238.48 ? 400 PHE B N   1 
ATOM   3034 C CA  . PHE B 2 400 ? 65.349  73.385  58.553 1.00 189.90 ? 400 PHE B CA  1 
ATOM   3035 C C   . PHE B 2 400 ? 64.110  72.494  58.417 1.00 151.36 ? 400 PHE B C   1 
ATOM   3036 O O   . PHE B 2 400 ? 63.594  72.359  57.320 1.00 173.36 ? 400 PHE B O   1 
ATOM   3037 C CB  . PHE B 2 400 ? 66.626  72.558  58.756 1.00 183.32 ? 400 PHE B CB  1 
ATOM   3038 C CG  . PHE B 2 400 ? 66.884  71.436  57.779 1.00 143.35 ? 400 PHE B CG  1 
ATOM   3039 C CD1 . PHE B 2 400 ? 66.231  70.193  57.880 1.00 203.15 ? 400 PHE B CD1 1 
ATOM   3040 C CD2 . PHE B 2 400 ? 67.811  71.603  56.768 1.00 140.89 ? 400 PHE B CD2 1 
ATOM   3041 C CE1 . PHE B 2 400 ? 66.478  69.162  56.975 1.00 189.77 ? 400 PHE B CE1 1 
ATOM   3042 C CE2 . PHE B 2 400 ? 68.050  70.569  55.850 1.00 204.97 ? 400 PHE B CE2 1 
ATOM   3043 C CZ  . PHE B 2 400 ? 67.394  69.343  55.954 1.00 153.46 ? 400 PHE B CZ  1 
ATOM   3044 N N   . SER B 2 401 ? 63.625  71.907  59.515 1.00 158.72 ? 401 SER B N   1 
ATOM   3045 C CA  . SER B 2 401 ? 62.490  70.991  59.485 1.00 203.51 ? 401 SER B CA  1 
ATOM   3046 C C   . SER B 2 401 ? 61.197  71.717  59.072 1.00 213.03 ? 401 SER B C   1 
ATOM   3047 O O   . SER B 2 401 ? 60.392  71.176  58.295 1.00 148.33 ? 401 SER B O   1 
ATOM   3048 C CB  . SER B 2 401 ? 62.347  70.265  60.811 1.00 210.59 ? 401 SER B CB  1 
ATOM   3049 O OG  . SER B 2 401 ? 61.940  71.135  61.858 1.00 228.19 ? 401 SER B OG  1 
ATOM   3050 N N   . PHE B 2 402 ? 60.975  72.944  59.574 1.00 169.60 ? 402 PHE B N   1 
ATOM   3051 C CA  . PHE B 2 402 ? 59.795  73.714  59.198 1.00 198.90 ? 402 PHE B CA  1 
ATOM   3052 C C   . PHE B 2 402 ? 59.836  74.090  57.711 1.00 219.75 ? 402 PHE B C   1 
ATOM   3053 O O   . PHE B 2 402 ? 58.886  73.806  56.986 1.00 174.01 ? 402 PHE B O   1 
ATOM   3054 C CB  . PHE B 2 402 ? 59.672  74.953  60.092 1.00 240.27 ? 402 PHE B CB  1 
ATOM   3055 C CG  . PHE B 2 402 ? 58.556  75.881  59.678 1.00 275.46 ? 402 PHE B CG  1 
ATOM   3056 C CD1 . PHE B 2 402 ? 57.233  75.619  60.031 1.00 284.87 ? 402 PHE B CD1 1 
ATOM   3057 C CD2 . PHE B 2 402 ? 58.829  77.012  58.912 1.00 262.24 ? 402 PHE B CD2 1 
ATOM   3058 C CE1 . PHE B 2 402 ? 56.217  76.479  59.639 1.00 291.35 ? 402 PHE B CE1 1 
ATOM   3059 C CE2 . PHE B 2 402 ? 57.808  77.868  58.517 1.00 257.76 ? 402 PHE B CE2 1 
ATOM   3060 C CZ  . PHE B 2 402 ? 56.505  77.597  58.881 1.00 317.50 ? 402 PHE B CZ  1 
ATOM   3061 N N   . PHE B 2 403 ? 60.931  74.741  57.271 1.00 237.36 ? 403 PHE B N   1 
ATOM   3062 C CA  . PHE B 2 403 ? 61.059  75.266  55.917 1.00 216.00 ? 403 PHE B CA  1 
ATOM   3063 C C   . PHE B 2 403 ? 61.043  74.157  54.853 1.00 147.15 ? 403 PHE B C   1 
ATOM   3064 O O   . PHE B 2 403 ? 60.435  74.324  53.813 1.00 133.08 ? 403 PHE B O   1 
ATOM   3065 C CB  . PHE B 2 403 ? 62.351  76.081  55.801 1.00 229.06 ? 403 PHE B CB  1 
ATOM   3066 C CG  . PHE B 2 403 ? 62.465  77.405  56.531 1.00 201.80 ? 403 PHE B CG  1 
ATOM   3067 C CD1 . PHE B 2 403 ? 61.424  78.316  56.578 1.00 273.76 ? 403 PHE B CD1 1 
ATOM   3068 C CD2 . PHE B 2 403 ? 63.661  77.771  57.158 1.00 206.38 ? 403 PHE B CD2 1 
ATOM   3069 C CE1 . PHE B 2 403 ? 61.579  79.528  57.249 1.00 326.58 ? 403 PHE B CE1 1 
ATOM   3070 C CE2 . PHE B 2 403 ? 63.822  78.988  57.813 1.00 158.30 ? 403 PHE B CE2 1 
ATOM   3071 C CZ  . PHE B 2 403 ? 62.779  79.868  57.858 1.00 234.74 ? 403 PHE B CZ  1 
ATOM   3072 N N   . ASN B 2 404 ? 61.701  73.027  55.100 1.00 136.33 ? 404 ASN B N   1 
ATOM   3073 C CA  . ASN B 2 404 ? 61.821  71.954  54.131 1.00 130.75 ? 404 ASN B CA  1 
ATOM   3074 C C   . ASN B 2 404 ? 60.423  71.361  53.855 1.00 143.96 ? 404 ASN B C   1 
ATOM   3075 O O   . ASN B 2 404 ? 60.013  71.385  52.686 1.00 217.77 ? 404 ASN B O   1 
ATOM   3076 C CB  . ASN B 2 404 ? 62.895  70.981  54.621 1.00 131.07 ? 404 ASN B CB  1 
ATOM   3077 C CG  . ASN B 2 404 ? 63.271  69.840  53.692 1.00 185.54 ? 404 ASN B CG  1 
ATOM   3078 O OD1 . ASN B 2 404 ? 62.608  69.565  52.701 1.00 243.34 ? 404 ASN B OD1 1 
ATOM   3079 N ND2 . ASN B 2 404 ? 64.375  69.175  53.983 1.00 200.57 ? 404 ASN B ND2 1 
ATOM   3080 N N   . TRP B 2 405 ? 59.669  70.862  54.846 1.00 130.49 ? 405 TRP B N   1 
ATOM   3081 C CA  . TRP B 2 405 ? 58.449  70.101  54.512 1.00 132.56 ? 405 TRP B CA  1 
ATOM   3082 C C   . TRP B 2 405 ? 57.334  71.036  54.028 1.00 159.16 ? 405 TRP B C   1 
ATOM   3083 O O   . TRP B 2 405 ? 56.464  70.530  53.322 1.00 143.41 ? 405 TRP B O   1 
ATOM   3084 C CB  . TRP B 2 405 ? 57.936  69.160  55.637 1.00 197.54 ? 405 TRP B CB  1 
ATOM   3085 C CG  . TRP B 2 405 ? 59.057  68.426  56.309 1.00 204.91 ? 405 TRP B CG  1 
ATOM   3086 C CD1 . TRP B 2 405 ? 59.358  68.434  57.641 1.00 259.57 ? 405 TRP B CD1 1 
ATOM   3087 C CD2 . TRP B 2 405 ? 60.086  67.650  55.661 1.00 154.43 ? 405 TRP B CD2 1 
ATOM   3088 N NE1 . TRP B 2 405 ? 60.492  67.695  57.874 1.00 234.75 ? 405 TRP B NE1 1 
ATOM   3089 C CE2 . TRP B 2 405 ? 60.971  67.207  56.679 1.00 199.98 ? 405 TRP B CE2 1 
ATOM   3090 C CE3 . TRP B 2 405 ? 60.364  67.286  54.343 1.00 154.37 ? 405 TRP B CE3 1 
ATOM   3091 C CZ2 . TRP B 2 405 ? 62.099  66.425  56.403 1.00 179.06 ? 405 TRP B CZ2 1 
ATOM   3092 C CZ3 . TRP B 2 405 ? 61.490  66.542  54.073 1.00 212.54 ? 405 TRP B CZ3 1 
ATOM   3093 C CH2 . TRP B 2 405 ? 62.353  66.131  55.084 1.00 195.23 ? 405 TRP B CH2 1 
ATOM   3094 N N   . LEU B 2 406 ? 57.348  72.350  54.355 1.00 128.73 ? 406 LEU B N   1 
ATOM   3095 C CA  . LEU B 2 406 ? 56.476  73.323  53.692 1.00 137.15 ? 406 LEU B CA  1 
ATOM   3096 C C   . LEU B 2 406 ? 56.773  73.426  52.187 1.00 141.35 ? 406 LEU B C   1 
ATOM   3097 O O   . LEU B 2 406 ? 55.852  73.455  51.377 1.00 122.62 ? 406 LEU B O   1 
ATOM   3098 C CB  . LEU B 2 406 ? 56.605  74.694  54.361 1.00 162.90 ? 406 LEU B CB  1 
ATOM   3099 C CG  . LEU B 2 406 ? 55.827  75.845  53.710 1.00 199.11 ? 406 LEU B CG  1 
ATOM   3100 C CD1 . LEU B 2 406 ? 54.315  75.609  53.759 1.00 189.86 ? 406 LEU B CD1 1 
ATOM   3101 C CD2 . LEU B 2 406 ? 56.195  77.173  54.360 1.00 232.52 ? 406 LEU B CD2 1 
ATOM   3102 N N   . CYS B 2 407 ? 58.042  73.470  51.783 1.00 148.31 ? 407 CYS B N   1 
ATOM   3103 C CA  . CYS B 2 407 ? 58.374  73.465  50.368 1.00 134.30 ? 407 CYS B CA  1 
ATOM   3104 C C   . CYS B 2 407 ? 57.972  72.145  49.705 1.00 103.05 ? 407 CYS B C   1 
ATOM   3105 O O   . CYS B 2 407 ? 57.390  72.166  48.630 1.00 186.94 ? 407 CYS B O   1 
ATOM   3106 C CB  . CYS B 2 407 ? 59.849  73.788  50.185 1.00 208.48 ? 407 CYS B CB  1 
ATOM   3107 S SG  . CYS B 2 407 ? 60.241  75.453  50.798 1.00 213.45 ? 407 CYS B SG  1 
ATOM   3108 N N   . VAL B 2 408 ? 58.218  70.990  50.313 1.00 110.61 ? 408 VAL B N   1 
ATOM   3109 C CA  . VAL B 2 408 ? 57.734  69.735  49.746 1.00 135.79 ? 408 VAL B CA  1 
ATOM   3110 C C   . VAL B 2 408 ? 56.198  69.708  49.703 1.00 126.77 ? 408 VAL B C   1 
ATOM   3111 O O   . VAL B 2 408 ? 55.633  69.243  48.725 1.00 150.23 ? 408 VAL B O   1 
ATOM   3112 C CB  . VAL B 2 408 ? 58.305  68.504  50.475 1.00 183.10 ? 408 VAL B CB  1 
ATOM   3113 C CG1 . VAL B 2 408 ? 57.890  67.191  49.816 1.00 166.69 ? 408 VAL B CG1 1 
ATOM   3114 C CG2 . VAL B 2 408 ? 59.828  68.540  50.568 1.00 191.90 ? 408 VAL B CG2 1 
ATOM   3115 N N   . ALA B 2 409 ? 55.496  70.217  50.712 1.00 140.58 ? 409 ALA B N   1 
ATOM   3116 C CA  . ALA B 2 409 ? 54.043  70.331  50.672 1.00 190.75 ? 409 ALA B CA  1 
ATOM   3117 C C   . ALA B 2 409 ? 53.580  71.107  49.439 1.00 175.50 ? 409 ALA B C   1 
ATOM   3118 O O   . ALA B 2 409 ? 52.721  70.627  48.703 1.00 192.87 ? 409 ALA B O   1 
ATOM   3119 C CB  . ALA B 2 409 ? 53.523  71.009  51.936 1.00 271.46 ? 409 ALA B CB  1 
ATOM   3120 N N   . LEU B 2 410 ? 54.138  72.308  49.212 1.00 129.32 ? 410 LEU B N   1 
ATOM   3121 C CA  . LEU B 2 410 ? 53.790  73.123  48.060 1.00 130.53 ? 410 LEU B CA  1 
ATOM   3122 C C   . LEU B 2 410 ? 54.090  72.381  46.757 1.00 117.11 ? 410 LEU B C   1 
ATOM   3123 O O   . LEU B 2 410 ? 53.294  72.449  45.830 1.00 133.92 ? 410 LEU B O   1 
ATOM   3124 C CB  . LEU B 2 410 ? 54.557  74.446  48.126 1.00 144.13 ? 410 LEU B CB  1 
ATOM   3125 C CG  . LEU B 2 410 ? 54.174  75.407  49.238 1.00 194.61 ? 410 LEU B CG  1 
ATOM   3126 C CD1 . LEU B 2 410 ? 55.232  76.498  49.348 1.00 261.93 ? 410 LEU B CD1 1 
ATOM   3127 C CD2 . LEU B 2 410 ? 52.800  76.007  48.993 1.00 270.18 ? 410 LEU B CD2 1 
ATOM   3128 N N   . ALA B 2 411 ? 55.209  71.661  46.668 1.00 110.84 ? 411 ALA B N   1 
ATOM   3129 C CA  . ALA B 2 411 ? 55.544  70.877  45.490 1.00 135.01 ? 411 ALA B CA  1 
ATOM   3130 C C   . ALA B 2 411 ? 54.511  69.790  45.201 1.00 120.99 ? 411 ALA B C   1 
ATOM   3131 O O   . ALA B 2 411 ? 54.122  69.624  44.041 1.00 154.85 ? 411 ALA B O   1 
ATOM   3132 C CB  . ALA B 2 411 ? 56.914  70.276  45.645 1.00 158.93 ? 411 ALA B CB  1 
ATOM   3133 N N   . ILE B 2 412 ? 54.041  69.061  46.223 1.00 114.73 ? 412 ILE B N   1 
ATOM   3134 C CA  . ILE B 2 412 ? 53.089  67.981  45.995 1.00 125.70 ? 412 ILE B CA  1 
ATOM   3135 C C   . ILE B 2 412 ? 51.666  68.520  45.802 1.00 148.73 ? 412 ILE B C   1 
ATOM   3136 O O   . ILE B 2 412 ? 50.916  67.920  45.023 1.00 183.26 ? 412 ILE B O   1 
ATOM   3137 C CB  . ILE B 2 412 ? 53.212  66.886  47.077 1.00 136.47 ? 412 ILE B CB  1 
ATOM   3138 C CG1 . ILE B 2 412 ? 54.628  66.300  47.111 1.00 192.19 ? 412 ILE B CG1 1 
ATOM   3139 C CG2 . ILE B 2 412 ? 52.194  65.792  46.858 1.00 157.23 ? 412 ILE B CG2 1 
ATOM   3140 C CD1 . ILE B 2 412 ? 55.214  65.948  45.709 1.00 151.23 ? 412 ILE B CD1 1 
ATOM   3141 N N   . ILE B 2 413 ? 51.276  69.627  46.445 1.00 131.94 ? 413 ILE B N   1 
ATOM   3142 C CA  . ILE B 2 413 ? 50.055  70.321  46.051 1.00 140.33 ? 413 ILE B CA  1 
ATOM   3143 C C   . ILE B 2 413 ? 50.144  70.599  44.547 1.00 140.96 ? 413 ILE B C   1 
ATOM   3144 O O   . ILE B 2 413 ? 49.192  70.350  43.803 1.00 182.49 ? 413 ILE B O   1 
ATOM   3145 C CB  . ILE B 2 413 ? 49.808  71.584  46.907 1.00 184.33 ? 413 ILE B CB  1 
ATOM   3146 C CG1 . ILE B 2 413 ? 49.513  71.238  48.366 1.00 243.95 ? 413 ILE B CG1 1 
ATOM   3147 C CG2 . ILE B 2 413 ? 48.679  72.441  46.339 1.00 254.82 ? 413 ILE B CG2 1 
ATOM   3148 C CD1 . ILE B 2 413 ? 49.742  72.378  49.346 1.00 300.77 ? 413 ILE B CD1 1 
ATOM   3149 N N   . GLY B 2 414 ? 51.289  71.112  44.095 1.00 134.97 ? 414 GLY B N   1 
ATOM   3150 C CA  . GLY B 2 414 ? 51.564  71.333  42.682 1.00 152.34 ? 414 GLY B CA  1 
ATOM   3151 C C   . GLY B 2 414 ? 51.477  70.086  41.802 1.00 132.97 ? 414 GLY B C   1 
ATOM   3152 O O   . GLY B 2 414 ? 51.006  70.190  40.684 1.00 183.51 ? 414 GLY B O   1 
ATOM   3153 N N   . MET B 2 415 ? 51.905  68.918  42.287 1.00 148.42 ? 415 MET B N   1 
ATOM   3154 C CA  . MET B 2 415 ? 51.836  67.668  41.541 1.00 144.27 ? 415 MET B CA  1 
ATOM   3155 C C   . MET B 2 415 ? 50.386  67.331  41.169 1.00 171.21 ? 415 MET B C   1 
ATOM   3156 O O   . MET B 2 415 ? 50.136  66.983  40.016 1.00 192.71 ? 415 MET B O   1 
ATOM   3157 C CB  . MET B 2 415 ? 52.461  66.532  42.374 1.00 199.53 ? 415 MET B CB  1 
ATOM   3158 C CG  . MET B 2 415 ? 52.265  65.093  41.858 1.00 157.09 ? 415 MET B CG  1 
ATOM   3159 S SD  . MET B 2 415 ? 53.115  64.856  40.292 1.00 167.27 ? 415 MET B SD  1 
ATOM   3160 C CE  . MET B 2 415 ? 52.171  63.526  39.574 1.00 220.33 ? 415 MET B CE  1 
ATOM   3161 N N   . ILE B 2 416 ? 49.437  67.428  42.120 1.00 172.27 ? 416 ILE B N   1 
ATOM   3162 C CA  . ILE B 2 416 ? 48.028  67.200  41.835 1.00 223.64 ? 416 ILE B CA  1 
ATOM   3163 C C   . ILE B 2 416 ? 47.519  68.287  40.881 1.00 223.05 ? 416 ILE B C   1 
ATOM   3164 O O   . ILE B 2 416 ? 46.888  67.984  39.868 1.00 234.91 ? 416 ILE B O   1 
ATOM   3165 C CB  . ILE B 2 416 ? 47.183  67.155  43.131 1.00 310.34 ? 416 ILE B CB  1 
ATOM   3166 C CG1 . ILE B 2 416 ? 47.683  66.086  44.105 1.00 336.65 ? 416 ILE B CG1 1 
ATOM   3167 C CG2 . ILE B 2 416 ? 45.690  66.974  42.821 1.00 410.82 ? 416 ILE B CG2 1 
ATOM   3168 C CD1 . ILE B 2 416 ? 46.887  66.006  45.390 1.00 391.49 ? 416 ILE B CD1 1 
ATOM   3169 N N   . TRP B 2 417 ? 47.782  69.555  41.216 1.00 174.88 ? 417 TRP B N   1 
ATOM   3170 C CA  . TRP B 2 417 ? 47.298  70.716  40.475 1.00 172.28 ? 417 TRP B CA  1 
ATOM   3171 C C   . TRP B 2 417 ? 47.703  70.637  39.007 1.00 142.42 ? 417 TRP B C   1 
ATOM   3172 O O   . TRP B 2 417 ? 46.865  70.828  38.138 1.00 223.28 ? 417 TRP B O   1 
ATOM   3173 C CB  . TRP B 2 417 ? 47.838  71.963  41.171 1.00 205.80 ? 417 TRP B CB  1 
ATOM   3174 C CG  . TRP B 2 417 ? 47.455  73.337  40.686 1.00 214.24 ? 417 TRP B CG  1 
ATOM   3175 C CD1 . TRP B 2 417 ? 46.580  74.165  41.326 1.00 206.80 ? 417 TRP B CD1 1 
ATOM   3176 C CD2 . TRP B 2 417 ? 47.953  74.083  39.542 1.00 278.22 ? 417 TRP B CD2 1 
ATOM   3177 N NE1 . TRP B 2 417 ? 46.478  75.356  40.657 1.00 236.74 ? 417 TRP B NE1 1 
ATOM   3178 C CE2 . TRP B 2 417 ? 47.307  75.346  39.561 1.00 295.55 ? 417 TRP B CE2 1 
ATOM   3179 C CE3 . TRP B 2 417 ? 48.862  73.824  38.498 1.00 314.35 ? 417 TRP B CE3 1 
ATOM   3180 C CZ2 . TRP B 2 417 ? 47.552  76.327  38.583 1.00 367.70 ? 417 TRP B CZ2 1 
ATOM   3181 C CZ3 . TRP B 2 417 ? 49.112  74.791  37.541 1.00 356.47 ? 417 TRP B CZ3 1 
ATOM   3182 C CH2 . TRP B 2 417 ? 48.472  76.034  37.593 1.00 391.85 ? 417 TRP B CH2 1 
ATOM   3183 N N   . LEU B 2 418 ? 48.961  70.316  38.717 1.00 133.69 ? 418 LEU B N   1 
ATOM   3184 C CA  . LEU B 2 418 ? 49.452  70.258  37.344 1.00 144.26 ? 418 LEU B CA  1 
ATOM   3185 C C   . LEU B 2 418 ? 48.875  69.052  36.585 1.00 172.20 ? 418 LEU B C   1 
ATOM   3186 O O   . LEU B 2 418 ? 48.589  69.182  35.403 1.00 193.97 ? 418 LEU B O   1 
ATOM   3187 C CB  . LEU B 2 418 ? 50.983  70.229  37.383 1.00 168.40 ? 418 LEU B CB  1 
ATOM   3188 C CG  . LEU B 2 418 ? 51.704  70.269  36.044 1.00 151.19 ? 418 LEU B CG  1 
ATOM   3189 C CD1 . LEU B 2 418 ? 51.455  71.608  35.378 1.00 181.94 ? 418 LEU B CD1 1 
ATOM   3190 C CD2 . LEU B 2 418 ? 53.203  69.986  36.205 1.00 199.75 ? 418 LEU B CD2 1 
ATOM   3191 N N   . ARG B 2 419 ? 48.677  67.894  37.230 1.00 175.21 ? 419 ARG B N   1 
ATOM   3192 C CA  . ARG B 2 419 ? 48.065  66.736  36.574 1.00 223.88 ? 419 ARG B CA  1 
ATOM   3193 C C   . ARG B 2 419 ? 46.585  66.975  36.206 1.00 251.34 ? 419 ARG B C   1 
ATOM   3194 O O   . ARG B 2 419 ? 46.103  66.406  35.225 1.00 208.64 ? 419 ARG B O   1 
ATOM   3195 C CB  . ARG B 2 419 ? 48.256  65.472  37.427 1.00 245.27 ? 419 ARG B CB  1 
ATOM   3196 C CG  . ARG B 2 419 ? 47.897  64.191  36.679 1.00 273.75 ? 419 ARG B CG  1 
ATOM   3197 C CD  . ARG B 2 419 ? 48.630  62.952  37.160 1.00 248.48 ? 419 ARG B CD  1 
ATOM   3198 N NE  . ARG B 2 419 ? 48.363  62.691  38.571 1.00 273.68 ? 419 ARG B NE  1 
ATOM   3199 C CZ  . ARG B 2 419 ? 48.978  61.790  39.332 1.00 313.68 ? 419 ARG B CZ  1 
ATOM   3200 N NH1 . ARG B 2 419 ? 48.568  61.610  40.574 1.00 286.00 ? 419 ARG B NH1 1 
ATOM   3201 N NH2 . ARG B 2 419 ? 49.993  61.074  38.874 1.00 353.01 ? 419 ARG B NH2 1 
ATOM   3202 N N   . HIS B 2 420 ? 45.859  67.808  36.970 1.00 250.30 ? 420 HIS B N   1 
ATOM   3203 C CA  . HIS B 2 420 ? 44.511  68.251  36.615 1.00 268.03 ? 420 HIS B CA  1 
ATOM   3204 C C   . HIS B 2 420 ? 44.509  69.401  35.599 1.00 225.37 ? 420 HIS B C   1 
ATOM   3205 O O   . HIS B 2 420 ? 43.689  69.392  34.679 1.00 240.89 ? 420 HIS B O   1 
ATOM   3206 C CB  . HIS B 2 420 ? 43.729  68.639  37.879 1.00 287.41 ? 420 HIS B CB  1 
ATOM   3207 C CG  . HIS B 2 420 ? 43.393  67.485  38.783 1.00 386.15 ? 420 HIS B CG  1 
ATOM   3208 N ND1 . HIS B 2 420 ? 42.710  67.603  39.980 1.00 425.68 ? 420 HIS B ND1 1 
ATOM   3209 C CD2 . HIS B 2 420 ? 43.659  66.176  38.644 1.00 421.57 ? 420 HIS B CD2 1 
ATOM   3210 C CE1 . HIS B 2 420 ? 42.574  66.404  40.532 1.00 416.87 ? 420 HIS B CE1 1 
ATOM   3211 N NE2 . HIS B 2 420 ? 43.143  65.523  39.737 1.00 416.48 ? 420 HIS B NE2 1 
ATOM   3212 N N   . ARG B 2 421 ? 45.410  70.383  35.762 1.00 217.74 ? 421 ARG B N   1 
ATOM   3213 C CA  . ARG B 2 421 ? 45.412  71.613  34.972 1.00 236.40 ? 421 ARG B CA  1 
ATOM   3214 C C   . ARG B 2 421 ? 46.012  71.436  33.566 1.00 204.76 ? 421 ARG B C   1 
ATOM   3215 O O   . ARG B 2 421 ? 45.600  72.169  32.658 1.00 276.50 ? 421 ARG B O   1 
ATOM   3216 C CB  . ARG B 2 421 ? 46.147  72.728  35.740 1.00 242.86 ? 421 ARG B CB  1 
ATOM   3217 C CG  . ARG B 2 421 ? 46.075  74.110  35.098 1.00 248.02 ? 421 ARG B CG  1 
ATOM   3218 C CD  . ARG B 2 421 ? 44.655  74.633  34.936 1.00 296.69 ? 421 ARG B CD  1 
ATOM   3219 N NE  . ARG B 2 421 ? 44.567  75.882  34.191 1.00 320.27 ? 421 ARG B NE  1 
ATOM   3220 C CZ  . ARG B 2 421 ? 44.490  75.998  32.865 1.00 373.34 ? 421 ARG B CZ  1 
ATOM   3221 N NH1 . ARG B 2 421 ? 44.393  77.198  32.319 1.00 375.19 ? 421 ARG B NH1 1 
ATOM   3222 N NH2 . ARG B 2 421 ? 44.505  74.931  32.080 1.00 416.86 ? 421 ARG B NH2 1 
ATOM   3223 N N   . LYS B 2 422 ? 46.969  70.498  33.383 1.00 181.62 ? 422 LYS B N   1 
ATOM   3224 C CA  . LYS B 2 422 ? 47.670  70.252  32.117 1.00 210.20 ? 422 LYS B CA  1 
ATOM   3225 C C   . LYS B 2 422 ? 47.815  68.741  31.879 1.00 219.69 ? 422 LYS B C   1 
ATOM   3226 O O   . LYS B 2 422 ? 48.926  68.201  31.901 1.00 222.36 ? 422 LYS B O   1 
ATOM   3227 C CB  . LYS B 2 422 ? 49.033  70.967  32.107 1.00 186.41 ? 422 LYS B CB  1 
ATOM   3228 C CG  . LYS B 2 422 ? 48.937  72.486  32.168 1.00 195.19 ? 422 LYS B CG  1 
ATOM   3229 C CD  . LYS B 2 422 ? 50.256  73.188  31.975 1.00 236.14 ? 422 LYS B CD  1 
ATOM   3230 C CE  . LYS B 2 422 ? 50.146  74.687  32.168 1.00 271.44 ? 422 LYS B CE  1 
ATOM   3231 N NZ  . LYS B 2 422 ? 51.474  75.344  32.087 1.00 308.00 ? 422 LYS B NZ  1 
ATOM   3232 N N   . PRO B 2 423 ? 46.699  68.004  31.642 1.00 233.16 ? 423 PRO B N   1 
ATOM   3233 C CA  . PRO B 2 423 ? 46.734  66.537  31.562 1.00 253.76 ? 423 PRO B CA  1 
ATOM   3234 C C   . PRO B 2 423 ? 47.427  65.956  30.322 1.00 235.87 ? 423 PRO B C   1 
ATOM   3235 O O   . PRO B 2 423 ? 47.696  64.756  30.293 1.00 213.84 ? 423 PRO B O   1 
ATOM   3236 C CB  . PRO B 2 423 ? 45.243  66.146  31.608 1.00 257.79 ? 423 PRO B CB  1 
ATOM   3237 C CG  . PRO B 2 423 ? 44.533  67.346  31.019 1.00 297.45 ? 423 PRO B CG  1 
ATOM   3238 C CD  . PRO B 2 423 ? 45.344  68.543  31.460 1.00 250.97 ? 423 PRO B CD  1 
ATOM   3239 N N   . GLU B 2 424 ? 47.726  66.795  29.317 1.00 224.07 ? 424 GLU B N   1 
ATOM   3240 C CA  . GLU B 2 424 ? 48.399  66.371  28.087 1.00 315.98 ? 424 GLU B CA  1 
ATOM   3241 C C   . GLU B 2 424 ? 49.904  66.079  28.264 1.00 331.32 ? 424 GLU B C   1 
ATOM   3242 O O   . GLU B 2 424 ? 50.491  65.415  27.402 1.00 331.31 ? 424 GLU B O   1 
ATOM   3243 C CB  . GLU B 2 424 ? 48.165  67.402  26.967 1.00 367.46 ? 424 GLU B CB  1 
ATOM   3244 C CG  . GLU B 2 424 ? 48.817  68.779  27.154 1.00 406.71 ? 424 GLU B CG  1 
ATOM   3245 C CD  . GLU B 2 424 ? 47.997  69.830  27.892 1.00 409.95 ? 424 GLU B CD  1 
ATOM   3246 O OE1 . GLU B 2 424 ? 47.344  69.477  28.894 1.00 307.91 ? 424 GLU B OE1 1 
ATOM   3247 O OE2 . GLU B 2 424 ? 48.016  71.003  27.466 1.00 465.14 ? 424 GLU B OE2 1 
ATOM   3248 N N   . LEU B 2 425 ? 50.537  66.568  29.352 1.00 317.76 ? 425 LEU B N   1 
ATOM   3249 C CA  . LEU B 2 425 ? 51.958  66.342  29.611 1.00 255.90 ? 425 LEU B CA  1 
ATOM   3250 C C   . LEU B 2 425 ? 52.205  64.869  29.947 1.00 239.51 ? 425 LEU B C   1 
ATOM   3251 O O   . LEU B 2 425 ? 51.450  64.255  30.709 1.00 189.46 ? 425 LEU B O   1 
ATOM   3252 C CB  . LEU B 2 425 ? 52.438  67.244  30.758 1.00 217.48 ? 425 LEU B CB  1 
ATOM   3253 C CG  . LEU B 2 425 ? 52.389  68.747  30.507 1.00 268.85 ? 425 LEU B CG  1 
ATOM   3254 C CD1 . LEU B 2 425 ? 52.719  69.514  31.776 1.00 283.69 ? 425 LEU B CD1 1 
ATOM   3255 C CD2 . LEU B 2 425 ? 53.343  69.132  29.387 1.00 304.07 ? 425 LEU B CD2 1 
ATOM   3256 N N   . GLU B 2 426 ? 53.290  64.324  29.367 1.00 273.68 ? 426 GLU B N   1 
ATOM   3257 C CA  . GLU B 2 426 ? 53.635  62.909  29.471 1.00 299.17 ? 426 GLU B CA  1 
ATOM   3258 C C   . GLU B 2 426 ? 53.900  62.460  30.918 1.00 268.23 ? 426 GLU B C   1 
ATOM   3259 O O   . GLU B 2 426 ? 54.381  63.229  31.744 1.00 207.22 ? 426 GLU B O   1 
ATOM   3260 C CB  . GLU B 2 426 ? 54.848  62.590  28.584 1.00 286.56 ? 426 GLU B CB  1 
ATOM   3261 C CG  . GLU B 2 426 ? 54.463  61.998  27.239 1.00 314.93 ? 426 GLU B CG  1 
ATOM   3262 C CD  . GLU B 2 426 ? 53.862  60.599  27.301 1.00 340.07 ? 426 GLU B CD  1 
ATOM   3263 O OE1 . GLU B 2 426 ? 53.679  60.067  28.412 1.00 303.42 ? 426 GLU B OE1 1 
ATOM   3264 O OE2 . GLU B 2 426 ? 53.573  60.037  26.221 1.00 381.72 ? 426 GLU B OE2 1 
ATOM   3265 N N   . ARG B 2 427 ? 53.595  61.176  31.206 1.00 259.06 ? 427 ARG B N   1 
ATOM   3266 C CA  . ARG B 2 427 ? 53.728  60.568  32.535 1.00 195.36 ? 427 ARG B CA  1 
ATOM   3267 C C   . ARG B 2 427 ? 54.447  59.219  32.405 1.00 171.13 ? 427 ARG B C   1 
ATOM   3268 O O   . ARG B 2 427 ? 53.824  58.158  32.513 1.00 217.20 ? 427 ARG B O   1 
ATOM   3269 C CB  . ARG B 2 427 ? 52.337  60.370  33.167 1.00 250.51 ? 427 ARG B CB  1 
ATOM   3270 C CG  . ARG B 2 427 ? 51.420  61.592  33.168 1.00 212.42 ? 427 ARG B CG  1 
ATOM   3271 C CD  . ARG B 2 427 ? 51.944  62.733  34.012 1.00 211.20 ? 427 ARG B CD  1 
ATOM   3272 N NE  . ARG B 2 427 ? 51.265  63.971  33.664 1.00 169.30 ? 427 ARG B NE  1 
ATOM   3273 C CZ  . ARG B 2 427 ? 51.145  65.039  34.461 1.00 201.36 ? 427 ARG B CZ  1 
ATOM   3274 N NH1 . ARG B 2 427 ? 50.533  66.113  33.977 1.00 180.27 ? 427 ARG B NH1 1 
ATOM   3275 N NH2 . ARG B 2 427 ? 51.593  65.061  35.714 1.00 184.51 ? 427 ARG B NH2 1 
ATOM   3276 N N   . PRO B 2 428 ? 55.770  59.193  32.134 1.00 175.33 ? 428 PRO B N   1 
ATOM   3277 C CA  . PRO B 2 428 ? 56.518  57.943  31.929 1.00 242.12 ? 428 PRO B CA  1 
ATOM   3278 C C   . PRO B 2 428 ? 56.432  56.940  33.081 1.00 225.21 ? 428 PRO B C   1 
ATOM   3279 O O   . PRO B 2 428 ? 56.524  55.743  32.833 1.00 236.05 ? 428 PRO B O   1 
ATOM   3280 C CB  . PRO B 2 428 ? 57.965  58.419  31.705 1.00 294.46 ? 428 PRO B CB  1 
ATOM   3281 C CG  . PRO B 2 428 ? 57.774  59.807  31.149 1.00 331.08 ? 428 PRO B CG  1 
ATOM   3282 C CD  . PRO B 2 428 ? 56.620  60.367  31.957 1.00 248.02 ? 428 PRO B CD  1 
ATOM   3283 N N   . ILE B 2 429 ? 56.249  57.433  34.318 1.00 212.49 ? 429 ILE B N   1 
ATOM   3284 C CA  . ILE B 2 429 ? 55.678  56.662  35.420 1.00 226.79 ? 429 ILE B CA  1 
ATOM   3285 C C   . ILE B 2 429 ? 54.576  57.502  36.089 1.00 212.30 ? 429 ILE B C   1 
ATOM   3286 O O   . ILE B 2 429 ? 54.709  58.702  36.304 1.00 149.30 ? 429 ILE B O   1 
ATOM   3287 C CB  . ILE B 2 429 ? 56.770  56.140  36.391 1.00 241.47 ? 429 ILE B CB  1 
ATOM   3288 C CG1 . ILE B 2 429 ? 57.584  55.023  35.716 1.00 283.22 ? 429 ILE B CG1 1 
ATOM   3289 C CG2 . ILE B 2 429 ? 56.205  55.679  37.729 1.00 253.44 ? 429 ILE B CG2 1 
ATOM   3290 C CD1 . ILE B 2 429 ? 58.588  54.287  36.606 1.00 314.61 ? 429 ILE B CD1 1 
ATOM   3291 N N   . LYS B 2 430 ? 53.463  56.822  36.401 1.00 250.03 ? 430 LYS B N   1 
ATOM   3292 C CA  . LYS B 2 430 ? 52.326  57.340  37.151 1.00 236.80 ? 430 LYS B CA  1 
ATOM   3293 C C   . LYS B 2 430 ? 51.915  56.240  38.131 1.00 298.26 ? 430 LYS B C   1 
ATOM   3294 O O   . LYS B 2 430 ? 51.831  55.062  37.750 1.00 374.83 ? 430 LYS B O   1 
ATOM   3295 C CB  . LYS B 2 430 ? 51.186  57.723  36.205 1.00 299.73 ? 430 LYS B CB  1 
ATOM   3296 C CG  . LYS B 2 430 ? 49.858  58.042  36.872 1.00 324.85 ? 430 LYS B CG  1 
ATOM   3297 C CD  . LYS B 2 430 ? 48.819  58.561  35.895 1.00 366.17 ? 430 LYS B CD  1 
ATOM   3298 C CE  . LYS B 2 430 ? 47.492  58.915  36.538 1.00 391.25 ? 430 LYS B CE  1 
ATOM   3299 N NZ  . LYS B 2 430 ? 46.741  57.720  36.999 1.00 416.77 ? 430 LYS B NZ  1 
ATOM   3300 N N   . VAL B 2 431 ? 51.652  56.625  39.394 1.00 266.49 ? 431 VAL B N   1 
ATOM   3301 C CA  . VAL B 2 431 ? 51.548  55.664  40.489 1.00 320.65 ? 431 VAL B CA  1 
ATOM   3302 C C   . VAL B 2 431 ? 50.126  55.689  41.059 1.00 270.17 ? 431 VAL B C   1 
ATOM   3303 O O   . VAL B 2 431 ? 49.447  54.655  41.026 1.00 318.27 ? 431 VAL B O   1 
ATOM   3304 C CB  . VAL B 2 431 ? 52.641  55.878  41.560 1.00 384.16 ? 431 VAL B CB  1 
ATOM   3305 C CG1 . VAL B 2 431 ? 52.499  54.902  42.722 1.00 431.88 ? 431 VAL B CG1 1 
ATOM   3306 C CG2 . VAL B 2 431 ? 54.037  55.743  40.976 1.00 377.98 ? 431 VAL B CG2 1 
ATOM   3307 N N   . ASN B 2 432 ? 49.679  56.849  41.580 1.00 182.86 ? 432 ASN B N   1 
ATOM   3308 C CA  . ASN B 2 432 ? 48.360  56.960  42.201 1.00 226.89 ? 432 ASN B CA  1 
ATOM   3309 C C   . ASN B 2 432 ? 47.967  58.431  42.389 1.00 211.45 ? 432 ASN B C   1 
ATOM   3310 O O   . ASN B 2 432 ? 48.811  59.314  42.280 1.00 256.63 ? 432 ASN B O   1 
ATOM   3311 C CB  . ASN B 2 432 ? 48.322  56.188  43.529 1.00 235.45 ? 432 ASN B CB  1 
ATOM   3312 C CG  . ASN B 2 432 ? 46.962  55.591  43.814 1.00 250.76 ? 432 ASN B CG  1 
ATOM   3313 O OD1 . ASN B 2 432 ? 46.022  56.325  44.100 1.00 252.35 ? 432 ASN B OD1 1 
ATOM   3314 N ND2 . ASN B 2 432 ? 46.842  54.275  43.741 1.00 276.94 ? 432 ASN B ND2 1 
ATOM   3315 N N   . LEU B 2 433 ? 46.679  58.706  42.681 1.00 179.73 ? 433 LEU B N   1 
ATOM   3316 C CA  . LEU B 2 433 ? 46.239  60.025  43.157 1.00 170.86 ? 433 LEU B CA  1 
ATOM   3317 C C   . LEU B 2 433 ? 46.076  60.064  44.690 1.00 207.73 ? 433 LEU B C   1 
ATOM   3318 O O   . LEU B 2 433 ? 45.925  61.155  45.223 1.00 156.95 ? 433 LEU B O   1 
ATOM   3319 C CB  . LEU B 2 433 ? 44.965  60.472  42.416 1.00 241.73 ? 433 LEU B CB  1 
ATOM   3320 C CG  . LEU B 2 433 ? 43.596  59.952  42.892 1.00 337.52 ? 433 LEU B CG  1 
ATOM   3321 C CD1 . LEU B 2 433 ? 42.467  60.726  42.227 1.00 359.38 ? 433 LEU B CD1 1 
ATOM   3322 C CD2 . LEU B 2 433 ? 43.411  58.461  42.637 1.00 351.71 ? 433 LEU B CD2 1 
ATOM   3323 N N   . ALA B 2 434 ? 46.127  58.911  45.392 1.00 225.58 ? 434 ALA B N   1 
ATOM   3324 C CA  . ALA B 2 434 ? 45.999  58.833  46.844 1.00 246.05 ? 434 ALA B CA  1 
ATOM   3325 C C   . ALA B 2 434 ? 47.289  59.247  47.561 1.00 202.24 ? 434 ALA B C   1 
ATOM   3326 O O   . ALA B 2 434 ? 47.205  59.992  48.545 1.00 185.93 ? 434 ALA B O   1 
ATOM   3327 C CB  . ALA B 2 434 ? 45.576  57.433  47.237 1.00 301.07 ? 434 ALA B CB  1 
ATOM   3328 N N   . LEU B 2 435 ? 48.471  58.783  47.096 1.00 160.76 ? 435 LEU B N   1 
ATOM   3329 C CA  . LEU B 2 435 ? 49.736  59.064  47.780 1.00 161.59 ? 435 LEU B CA  1 
ATOM   3330 C C   . LEU B 2 435 ? 49.999  60.578  47.888 1.00 168.18 ? 435 LEU B C   1 
ATOM   3331 O O   . LEU B 2 435 ? 50.338  61.043  48.981 1.00 234.63 ? 435 LEU B O   1 
ATOM   3332 C CB  . LEU B 2 435 ? 50.918  58.335  47.107 1.00 168.85 ? 435 LEU B CB  1 
ATOM   3333 C CG  . LEU B 2 435 ? 50.866  56.813  47.054 1.00 222.84 ? 435 LEU B CG  1 
ATOM   3334 C CD1 . LEU B 2 435 ? 52.194  56.297  46.508 1.00 212.52 ? 435 LEU B CD1 1 
ATOM   3335 C CD2 . LEU B 2 435 ? 50.572  56.199  48.422 1.00 273.01 ? 435 LEU B CD2 1 
ATOM   3336 N N   . PRO B 2 436 ? 49.860  61.406  46.821 1.00 125.22 ? 436 PRO B N   1 
ATOM   3337 C CA  . PRO B 2 436 ? 49.883  62.864  46.958 1.00 139.90 ? 436 PRO B CA  1 
ATOM   3338 C C   . PRO B 2 436 ? 48.926  63.415  48.024 1.00 153.73 ? 436 PRO B C   1 
ATOM   3339 O O   . PRO B 2 436 ? 49.361  64.203  48.846 1.00 164.29 ? 436 PRO B O   1 
ATOM   3340 C CB  . PRO B 2 436 ? 49.491  63.389  45.568 1.00 187.66 ? 436 PRO B CB  1 
ATOM   3341 C CG  . PRO B 2 436 ? 49.896  62.282  44.630 1.00 220.61 ? 436 PRO B CG  1 
ATOM   3342 C CD  . PRO B 2 436 ? 49.673  61.013  45.425 1.00 176.58 ? 436 PRO B CD  1 
ATOM   3343 N N   . VAL B 2 437 ? 47.654  63.004  48.049 1.00 167.12 ? 437 VAL B N   1 
ATOM   3344 C CA  . VAL B 2 437 ? 46.665  63.545  48.977 1.00 203.47 ? 437 VAL B CA  1 
ATOM   3345 C C   . VAL B 2 437 ? 47.054  63.211  50.420 1.00 198.13 ? 437 VAL B C   1 
ATOM   3346 O O   . VAL B 2 437 ? 47.017  64.101  51.282 1.00 194.55 ? 437 VAL B O   1 
ATOM   3347 C CB  . VAL B 2 437 ? 45.233  63.068  48.636 1.00 260.93 ? 437 VAL B CB  1 
ATOM   3348 C CG1 . VAL B 2 437 ? 44.194  63.392  49.711 1.00 355.79 ? 437 VAL B CG1 1 
ATOM   3349 C CG2 . VAL B 2 437 ? 44.773  63.644  47.305 1.00 242.49 ? 437 VAL B CG2 1 
ATOM   3350 N N   . PHE B 2 438 ? 47.424  61.947  50.681 1.00 175.21 ? 438 PHE B N   1 
ATOM   3351 C CA  . PHE B 2 438 ? 47.883  61.521  51.997 1.00 209.45 ? 438 PHE B CA  1 
ATOM   3352 C C   . PHE B 2 438 ? 49.122  62.316  52.432 1.00 191.96 ? 438 PHE B C   1 
ATOM   3353 O O   . PHE B 2 438 ? 49.198  62.762  53.571 1.00 170.21 ? 438 PHE B O   1 
ATOM   3354 C CB  . PHE B 2 438 ? 48.149  60.011  51.999 1.00 255.97 ? 438 PHE B CB  1 
ATOM   3355 C CG  . PHE B 2 438 ? 48.829  59.509  53.252 1.00 313.63 ? 438 PHE B CG  1 
ATOM   3356 C CD1 . PHE B 2 438 ? 48.109  59.273  54.415 1.00 320.83 ? 438 PHE B CD1 1 
ATOM   3357 C CD2 . PHE B 2 438 ? 50.202  59.290  53.285 1.00 329.47 ? 438 PHE B CD2 1 
ATOM   3358 C CE1 . PHE B 2 438 ? 48.743  58.812  55.568 1.00 304.00 ? 438 PHE B CE1 1 
ATOM   3359 C CE2 . PHE B 2 438 ? 50.840  58.833  54.437 1.00 279.80 ? 438 PHE B CE2 1 
ATOM   3360 C CZ  . PHE B 2 438 ? 50.109  58.594  55.581 1.00 265.20 ? 438 PHE B CZ  1 
ATOM   3361 N N   . PHE B 2 439 ? 50.107  62.499  51.544 1.00 189.03 ? 439 PHE B N   1 
ATOM   3362 C CA  . PHE B 2 439 ? 51.300  63.263  51.884 1.00 159.07 ? 439 PHE B CA  1 
ATOM   3363 C C   . PHE B 2 439 ? 50.942  64.728  52.174 1.00 137.47 ? 439 PHE B C   1 
ATOM   3364 O O   . PHE B 2 439 ? 51.448  65.274  53.139 1.00 176.49 ? 439 PHE B O   1 
ATOM   3365 C CB  . PHE B 2 439 ? 52.339  63.126  50.772 1.00 175.35 ? 439 PHE B CB  1 
ATOM   3366 C CG  . PHE B 2 439 ? 53.626  63.836  51.087 1.00 167.05 ? 439 PHE B CG  1 
ATOM   3367 C CD1 . PHE B 2 439 ? 53.775  65.219  50.898 1.00 188.59 ? 439 PHE B CD1 1 
ATOM   3368 C CD2 . PHE B 2 439 ? 54.678  63.114  51.590 1.00 128.61 ? 439 PHE B CD2 1 
ATOM   3369 C CE1 . PHE B 2 439 ? 54.956  65.859  51.229 1.00 173.45 ? 439 PHE B CE1 1 
ATOM   3370 C CE2 . PHE B 2 439 ? 55.870  63.742  51.902 1.00 152.11 ? 439 PHE B CE2 1 
ATOM   3371 C CZ  . PHE B 2 439 ? 56.004  65.100  51.712 1.00 202.33 ? 439 PHE B CZ  1 
ATOM   3372 N N   . ILE B 2 440 ? 50.072  65.370  51.379 1.00 126.57 ? 440 ILE B N   1 
ATOM   3373 C CA  . ILE B 2 440 ? 49.681  66.763  51.599 1.00 164.38 ? 440 ILE B CA  1 
ATOM   3374 C C   . ILE B 2 440 ? 48.984  66.934  52.958 1.00 214.07 ? 440 ILE B C   1 
ATOM   3375 O O   . ILE B 2 440 ? 49.372  67.814  53.731 1.00 149.52 ? 440 ILE B O   1 
ATOM   3376 C CB  . ILE B 2 440 ? 48.795  67.305  50.464 1.00 211.98 ? 440 ILE B CB  1 
ATOM   3377 C CG1 . ILE B 2 440 ? 49.556  67.391  49.143 1.00 217.32 ? 440 ILE B CG1 1 
ATOM   3378 C CG2 . ILE B 2 440 ? 48.199  68.666  50.827 1.00 250.21 ? 440 ILE B CG2 1 
ATOM   3379 C CD1 . ILE B 2 440 ? 48.647  67.467  47.938 1.00 215.04 ? 440 ILE B CD1 1 
ATOM   3380 N N   . LEU B 2 441 ? 47.973  66.109  53.279 1.00 232.71 ? 441 LEU B N   1 
ATOM   3381 C CA  . LEU B 2 441 ? 47.281  66.276  54.556 1.00 250.46 ? 441 LEU B CA  1 
ATOM   3382 C C   . LEU B 2 441 ? 48.237  65.969  55.723 1.00 220.48 ? 441 LEU B C   1 
ATOM   3383 O O   . LEU B 2 441 ? 48.175  66.645  56.751 1.00 230.28 ? 441 LEU B O   1 
ATOM   3384 C CB  . LEU B 2 441 ? 45.969  65.471  54.582 1.00 283.47 ? 441 LEU B CB  1 
ATOM   3385 C CG  . LEU B 2 441 ? 46.041  63.943  54.635 1.00 308.07 ? 441 LEU B CG  1 
ATOM   3386 C CD1 . LEU B 2 441 ? 46.117  63.409  56.067 1.00 311.34 ? 441 LEU B CD1 1 
ATOM   3387 C CD2 . LEU B 2 441 ? 44.833  63.331  53.943 1.00 372.68 ? 441 LEU B CD2 1 
ATOM   3388 N N   . ALA B 2 442 ? 49.134  64.984  55.576 1.00 182.89 ? 442 ALA B N   1 
ATOM   3389 C CA  . ALA B 2 442 ? 50.158  64.682  56.569 1.00 166.02 ? 442 ALA B CA  1 
ATOM   3390 C C   . ALA B 2 442 ? 51.108  65.861  56.796 1.00 126.31 ? 442 ALA B C   1 
ATOM   3391 O O   . ALA B 2 442 ? 51.275  66.305  57.927 1.00 198.98 ? 442 ALA B O   1 
ATOM   3392 C CB  . ALA B 2 442 ? 50.908  63.433  56.158 1.00 135.05 ? 442 ALA B CB  1 
ATOM   3393 N N   . CYS B 2 443 ? 51.746  66.383  55.751 1.00 155.98 ? 443 CYS B N   1 
ATOM   3394 C CA  . CYS B 2 443 ? 52.752  67.430  55.921 1.00 155.85 ? 443 CYS B CA  1 
ATOM   3395 C C   . CYS B 2 443 ? 52.067  68.709  56.420 1.00 154.03 ? 443 CYS B C   1 
ATOM   3396 O O   . CYS B 2 443 ? 52.633  69.377  57.278 1.00 169.24 ? 443 CYS B O   1 
ATOM   3397 C CB  . CYS B 2 443 ? 53.589  67.625  54.650 1.00 157.28 ? 443 CYS B CB  1 
ATOM   3398 S SG  . CYS B 2 443 ? 52.611  68.141  53.229 1.00 295.30 ? 443 CYS B SG  1 
ATOM   3399 N N   . LEU B 2 444 ? 50.861  69.051  55.924 1.00 155.32 ? 444 LEU B N   1 
ATOM   3400 C CA  . LEU B 2 444 ? 50.150  70.232  56.408 1.00 193.72 ? 444 LEU B CA  1 
ATOM   3401 C C   . LEU B 2 444 ? 49.728  70.071  57.867 1.00 182.11 ? 444 LEU B C   1 
ATOM   3402 O O   . LEU B 2 444 ? 49.737  71.069  58.589 1.00 202.47 ? 444 LEU B O   1 
ATOM   3403 C CB  . LEU B 2 444 ? 48.960  70.550  55.493 1.00 268.42 ? 444 LEU B CB  1 
ATOM   3404 C CG  . LEU B 2 444 ? 49.322  71.123  54.116 1.00 315.55 ? 444 LEU B CG  1 
ATOM   3405 C CD1 . LEU B 2 444 ? 48.075  71.301  53.264 1.00 373.93 ? 444 LEU B CD1 1 
ATOM   3406 C CD2 . LEU B 2 444 ? 50.064  72.462  54.205 1.00 283.47 ? 444 LEU B CD2 1 
ATOM   3407 N N   . PHE B 2 445 ? 49.380  68.856  58.317 1.00 188.86 ? 445 PHE B N   1 
ATOM   3408 C CA  . PHE B 2 445 ? 49.209  68.570  59.748 1.00 240.22 ? 445 PHE B CA  1 
ATOM   3409 C C   . PHE B 2 445 ? 50.502  68.885  60.517 1.00 154.96 ? 445 PHE B C   1 
ATOM   3410 O O   . PHE B 2 445 ? 50.458  69.708  61.423 1.00 132.76 ? 445 PHE B O   1 
ATOM   3411 C CB  . PHE B 2 445 ? 48.692  67.140  59.984 1.00 246.73 ? 445 PHE B CB  1 
ATOM   3412 C CG  . PHE B 2 445 ? 48.898  66.599  61.385 1.00 215.44 ? 445 PHE B CG  1 
ATOM   3413 C CD1 . PHE B 2 445 ? 48.361  67.254  62.489 1.00 297.58 ? 445 PHE B CD1 1 
ATOM   3414 C CD2 . PHE B 2 445 ? 49.628  65.440  61.613 1.00 208.90 ? 445 PHE B CD2 1 
ATOM   3415 C CE1 . PHE B 2 445 ? 48.549  66.763  63.777 1.00 309.97 ? 445 PHE B CE1 1 
ATOM   3416 C CE2 . PHE B 2 445 ? 49.819  64.951  62.897 1.00 230.95 ? 445 PHE B CE2 1 
ATOM   3417 C CZ  . PHE B 2 445 ? 49.277  65.610  63.981 1.00 254.02 ? 445 PHE B CZ  1 
ATOM   3418 N N   . LEU B 2 446 ? 51.625  68.273  60.132 1.00 141.72 ? 446 LEU B N   1 
ATOM   3419 C CA  . LEU B 2 446 ? 52.931  68.484  60.757 1.00 157.59 ? 446 LEU B CA  1 
ATOM   3420 C C   . LEU B 2 446 ? 53.311  69.973  60.825 1.00 165.45 ? 446 LEU B C   1 
ATOM   3421 O O   . LEU B 2 446 ? 53.848  70.416  61.850 1.00 256.11 ? 446 LEU B O   1 
ATOM   3422 C CB  . LEU B 2 446 ? 54.021  67.684  60.007 1.00 155.96 ? 446 LEU B CB  1 
ATOM   3423 C CG  . LEU B 2 446 ? 54.336  66.280  60.546 1.00 211.61 ? 446 LEU B CG  1 
ATOM   3424 C CD1 . LEU B 2 446 ? 54.863  66.341  61.977 1.00 274.44 ? 446 LEU B CD1 1 
ATOM   3425 C CD2 . LEU B 2 446 ? 53.136  65.330  60.506 1.00 211.02 ? 446 LEU B CD2 1 
ATOM   3426 N N   . ILE B 2 447 ? 53.048  70.746  59.763 1.00 151.98 ? 447 ILE B N   1 
ATOM   3427 C CA  . ILE B 2 447 ? 53.350  72.173  59.730 1.00 187.77 ? 447 ILE B CA  1 
ATOM   3428 C C   . ILE B 2 447 ? 52.412  72.927  60.677 1.00 199.86 ? 447 ILE B C   1 
ATOM   3429 O O   . ILE B 2 447 ? 52.893  73.674  61.531 1.00 239.73 ? 447 ILE B O   1 
ATOM   3430 C CB  . ILE B 2 447 ? 53.298  72.713  58.279 1.00 210.22 ? 447 ILE B CB  1 
ATOM   3431 C CG1 . ILE B 2 447 ? 54.351  72.048  57.382 1.00 212.79 ? 447 ILE B CG1 1 
ATOM   3432 C CG2 . ILE B 2 447 ? 53.441  74.228  58.221 1.00 178.10 ? 447 ILE B CG2 1 
ATOM   3433 C CD1 . ILE B 2 447 ? 53.988  71.993  55.901 1.00 139.11 ? 447 ILE B CD1 1 
ATOM   3434 N N   . ALA B 2 448 ? 51.089  72.749  60.531 1.00 226.49 ? 448 ALA B N   1 
ATOM   3435 C CA  . ALA B 2 448 ? 50.098  73.514  61.288 1.00 271.27 ? 448 ALA B CA  1 
ATOM   3436 C C   . ALA B 2 448 ? 50.230  73.267  62.795 1.00 234.18 ? 448 ALA B C   1 
ATOM   3437 O O   . ALA B 2 448 ? 50.166  74.219  63.584 1.00 225.66 ? 448 ALA B O   1 
ATOM   3438 C CB  . ALA B 2 448 ? 48.701  73.200  60.785 1.00 287.44 ? 448 ALA B CB  1 
ATOM   3439 N N   . VAL B 2 449 ? 50.428  71.999  63.193 1.00 222.20 ? 449 VAL B N   1 
ATOM   3440 C CA  . VAL B 2 449 ? 50.517  71.619  64.601 1.00 244.81 ? 449 VAL B CA  1 
ATOM   3441 C C   . VAL B 2 449 ? 51.833  72.114  65.235 1.00 201.88 ? 449 VAL B C   1 
ATOM   3442 O O   . VAL B 2 449 ? 51.808  72.636  66.348 1.00 244.48 ? 449 VAL B O   1 
ATOM   3443 C CB  . VAL B 2 449 ? 50.276  70.104  64.777 1.00 196.27 ? 449 VAL B CB  1 
ATOM   3444 C CG1 . VAL B 2 449 ? 51.441  69.269  64.327 1.00 174.90 ? 449 VAL B CG1 1 
ATOM   3445 C CG2 . VAL B 2 449 ? 49.931  69.752  66.212 1.00 219.05 ? 449 VAL B CG2 1 
ATOM   3446 N N   . SER B 2 450 ? 52.975  71.983  64.548 1.00 182.69 ? 450 SER B N   1 
ATOM   3447 C CA  . SER B 2 450 ? 54.243  72.471  65.077 1.00 209.98 ? 450 SER B CA  1 
ATOM   3448 C C   . SER B 2 450 ? 54.257  74.009  65.142 1.00 219.37 ? 450 SER B C   1 
ATOM   3449 O O   . SER B 2 450 ? 54.789  74.567  66.105 1.00 309.55 ? 450 SER B O   1 
ATOM   3450 C CB  . SER B 2 450 ? 55.424  71.920  64.305 1.00 264.74 ? 450 SER B CB  1 
ATOM   3451 O OG  . SER B 2 450 ? 55.400  72.357  62.955 1.00 313.71 ? 450 SER B OG  1 
ATOM   3452 N N   . PHE B 2 451 ? 53.666  74.698  64.148 1.00 215.91 ? 451 PHE B N   1 
ATOM   3453 C CA  . PHE B 2 451 ? 53.461  76.144  64.196 1.00 286.98 ? 451 PHE B CA  1 
ATOM   3454 C C   . PHE B 2 451 ? 52.642  76.554  65.431 1.00 310.17 ? 451 PHE B C   1 
ATOM   3455 O O   . PHE B 2 451 ? 53.061  77.433  66.190 1.00 298.86 ? 451 PHE B O   1 
ATOM   3456 C CB  . PHE B 2 451 ? 52.832  76.647  62.887 1.00 327.59 ? 451 PHE B CB  1 
ATOM   3457 C CG  . PHE B 2 451 ? 52.725  78.151  62.776 1.00 347.75 ? 451 PHE B CG  1 
ATOM   3458 C CD1 . PHE B 2 451 ? 51.753  78.858  63.483 1.00 401.95 ? 451 PHE B CD1 1 
ATOM   3459 C CD2 . PHE B 2 451 ? 53.599  78.869  61.967 1.00 288.97 ? 451 PHE B CD2 1 
ATOM   3460 C CE1 . PHE B 2 451 ? 51.660  80.242  63.379 1.00 413.80 ? 451 PHE B CE1 1 
ATOM   3461 C CE2 . PHE B 2 451 ? 53.512  80.254  61.869 1.00 342.12 ? 451 PHE B CE2 1 
ATOM   3462 C CZ  . PHE B 2 451 ? 52.539  80.937  62.572 1.00 398.93 ? 451 PHE B CZ  1 
ATOM   3463 N N   . TRP B 2 452 ? 51.481  75.918  65.638 1.00 289.27 ? 452 TRP B N   1 
ATOM   3464 C CA  . TRP B 2 452 ? 50.611  76.165  66.790 1.00 278.99 ? 452 TRP B CA  1 
ATOM   3465 C C   . TRP B 2 452 ? 51.344  76.021  68.136 1.00 268.42 ? 452 TRP B C   1 
ATOM   3466 O O   . TRP B 2 452 ? 51.105  76.821  69.042 1.00 281.03 ? 452 TRP B O   1 
ATOM   3467 C CB  . TRP B 2 452 ? 49.392  75.234  66.699 1.00 310.41 ? 452 TRP B CB  1 
ATOM   3468 C CG  . TRP B 2 452 ? 48.568  75.125  67.958 1.00 321.07 ? 452 TRP B CG  1 
ATOM   3469 C CD1 . TRP B 2 452 ? 47.834  76.118  68.538 1.00 335.51 ? 452 TRP B CD1 1 
ATOM   3470 C CD2 . TRP B 2 452 ? 48.395  73.948  68.797 1.00 336.78 ? 452 TRP B CD2 1 
ATOM   3471 N NE1 . TRP B 2 452 ? 47.219  75.647  69.671 1.00 377.85 ? 452 TRP B NE1 1 
ATOM   3472 C CE2 . TRP B 2 452 ? 47.539  74.320  69.862 1.00 390.56 ? 452 TRP B CE2 1 
ATOM   3473 C CE3 . TRP B 2 452 ? 48.867  72.619  68.763 1.00 317.52 ? 452 TRP B CE3 1 
ATOM   3474 C CZ2 . TRP B 2 452 ? 47.158  73.412  70.867 1.00 397.63 ? 452 TRP B CZ2 1 
ATOM   3475 C CZ3 . TRP B 2 452 ? 48.491  71.727  69.752 1.00 302.49 ? 452 TRP B CZ3 1 
ATOM   3476 C CH2 . TRP B 2 452 ? 47.647  72.121  70.792 1.00 336.50 ? 452 TRP B CH2 1 
ATOM   3477 N N   . LYS B 2 453 ? 52.237  75.027  68.271 1.00 270.67 ? 453 LYS B N   1 
ATOM   3478 C CA  . LYS B 2 453 ? 53.049  74.850  69.473 1.00 254.92 ? 453 LYS B CA  1 
ATOM   3479 C C   . LYS B 2 453 ? 54.230  75.831  69.587 1.00 272.42 ? 453 LYS B C   1 
ATOM   3480 O O   . LYS B 2 453 ? 54.741  75.981  70.699 1.00 320.98 ? 453 LYS B O   1 
ATOM   3481 C CB  . LYS B 2 453 ? 53.557  73.402  69.544 1.00 265.06 ? 453 LYS B CB  1 
ATOM   3482 C CG  . LYS B 2 453 ? 52.480  72.342  69.755 1.00 283.26 ? 453 LYS B CG  1 
ATOM   3483 C CD  . LYS B 2 453 ? 51.633  72.503  71.012 1.00 356.40 ? 453 LYS B CD  1 
ATOM   3484 C CE  . LYS B 2 453 ? 52.429  72.538  72.302 1.00 420.97 ? 453 LYS B CE  1 
ATOM   3485 N NZ  . LYS B 2 453 ? 51.545  72.615  73.492 1.00 432.69 ? 453 LYS B NZ  1 
ATOM   3486 N N   . THR B 2 454 ? 54.680  76.496  68.496 1.00 269.25 ? 454 THR B N   1 
ATOM   3487 C CA  . THR B 2 454 ? 55.864  77.369  68.519 1.00 255.60 ? 454 THR B CA  1 
ATOM   3488 C C   . THR B 2 454 ? 55.673  78.706  67.765 1.00 263.48 ? 454 THR B C   1 
ATOM   3489 O O   . THR B 2 454 ? 56.514  79.069  66.929 1.00 303.57 ? 454 THR B O   1 
ATOM   3490 C CB  . THR B 2 454 ? 57.095  76.592  67.995 1.00 277.15 ? 454 THR B CB  1 
ATOM   3491 O OG1 . THR B 2 454 ? 56.903  76.153  66.648 1.00 296.69 ? 454 THR B OG1 1 
ATOM   3492 C CG2 . THR B 2 454 ? 57.443  75.362  68.808 1.00 268.35 ? 454 THR B CG2 1 
ATOM   3493 N N   . PRO B 2 455 ? 54.603  79.520  68.013 1.00 318.19 ? 455 PRO B N   1 
ATOM   3494 C CA  . PRO B 2 455 ? 54.378  80.779  67.282 1.00 363.65 ? 455 PRO B CA  1 
ATOM   3495 C C   . PRO B 2 455 ? 55.510  81.812  67.355 1.00 398.73 ? 455 PRO B C   1 
ATOM   3496 O O   . PRO B 2 455 ? 55.716  82.535  66.385 1.00 396.33 ? 455 PRO B O   1 
ATOM   3497 C CB  . PRO B 2 455 ? 53.111  81.383  67.928 1.00 328.38 ? 455 PRO B CB  1 
ATOM   3498 C CG  . PRO B 2 455 ? 52.405  80.191  68.514 1.00 323.83 ? 455 PRO B CG  1 
ATOM   3499 C CD  . PRO B 2 455 ? 53.536  79.307  69.001 1.00 315.90 ? 455 PRO B CD  1 
ATOM   3500 N N   . VAL B 2 456 ? 56.245  81.868  68.481 1.00 413.23 ? 456 VAL B N   1 
ATOM   3501 C CA  . VAL B 2 456 ? 57.308  82.850  68.696 1.00 387.02 ? 456 VAL B CA  1 
ATOM   3502 C C   . VAL B 2 456 ? 58.476  82.585  67.733 1.00 310.42 ? 456 VAL B C   1 
ATOM   3503 O O   . VAL B 2 456 ? 58.980  83.520  67.108 1.00 316.71 ? 456 VAL B O   1 
ATOM   3504 C CB  . VAL B 2 456 ? 57.768  82.872  70.173 1.00 419.19 ? 456 VAL B CB  1 
ATOM   3505 C CG1 . VAL B 2 456 ? 58.919  83.844  70.422 1.00 421.76 ? 456 VAL B CG1 1 
ATOM   3506 C CG2 . VAL B 2 456 ? 56.616  83.189  71.122 1.00 408.90 ? 456 VAL B CG2 1 
ATOM   3507 N N   . GLU B 2 457 ? 58.887  81.313  67.606 1.00 238.12 ? 457 GLU B N   1 
ATOM   3508 C CA  . GLU B 2 457 ? 59.944  80.882  66.697 1.00 245.17 ? 457 GLU B CA  1 
ATOM   3509 C C   . GLU B 2 457 ? 59.482  80.926  65.230 1.00 294.59 ? 457 GLU B C   1 
ATOM   3510 O O   . GLU B 2 457 ? 60.220  81.408  64.362 1.00 324.77 ? 457 GLU B O   1 
ATOM   3511 C CB  . GLU B 2 457 ? 60.406  79.469  67.071 1.00 267.25 ? 457 GLU B CB  1 
ATOM   3512 C CG  . GLU B 2 457 ? 61.043  79.355  68.454 1.00 298.50 ? 457 GLU B CG  1 
ATOM   3513 C CD  . GLU B 2 457 ? 60.134  79.354  69.676 1.00 316.86 ? 457 GLU B CD  1 
ATOM   3514 O OE1 . GLU B 2 457 ? 58.899  79.283  69.524 1.00 298.38 ? 457 GLU B OE1 1 
ATOM   3515 O OE2 . GLU B 2 457 ? 60.669  79.430  70.796 1.00 330.11 ? 457 GLU B OE2 1 
ATOM   3516 N N   . CYS B 2 458 ? 58.269  80.433  64.930 1.00 319.53 ? 458 CYS B N   1 
ATOM   3517 C CA  . CYS B 2 458 ? 57.778  80.393  63.553 1.00 284.05 ? 458 CYS B CA  1 
ATOM   3518 C C   . CYS B 2 458 ? 57.552  81.798  62.975 1.00 232.37 ? 458 CYS B C   1 
ATOM   3519 O O   . CYS B 2 458 ? 57.779  82.007  61.781 1.00 180.12 ? 458 CYS B O   1 
ATOM   3520 C CB  . CYS B 2 458 ? 56.513  79.540  63.464 1.00 280.88 ? 458 CYS B CB  1 
ATOM   3521 S SG  . CYS B 2 458 ? 56.830  77.806  63.898 1.00 222.66 ? 458 CYS B SG  1 
ATOM   3522 N N   . GLY B 2 459 ? 57.121  82.757  63.814 1.00 320.29 ? 459 GLY B N   1 
ATOM   3523 C CA  . GLY B 2 459 ? 56.933  84.151  63.426 1.00 393.96 ? 459 GLY B CA  1 
ATOM   3524 C C   . GLY B 2 459 ? 58.205  84.802  62.884 1.00 421.79 ? 459 GLY B C   1 
ATOM   3525 O O   . GLY B 2 459 ? 58.178  85.363  61.790 1.00 442.84 ? 459 GLY B O   1 
ATOM   3526 N N   . ILE B 2 460 ? 59.317  84.716  63.635 1.00 386.23 ? 460 ILE B N   1 
ATOM   3527 C CA  . ILE B 2 460 ? 60.609  85.213  63.151 1.00 327.67 ? 460 ILE B CA  1 
ATOM   3528 C C   . ILE B 2 460 ? 61.043  84.411  61.911 1.00 258.23 ? 460 ILE B C   1 
ATOM   3529 O O   . ILE B 2 460 ? 61.632  84.992  61.000 1.00 216.55 ? 460 ILE B O   1 
ATOM   3530 C CB  . ILE B 2 460 ? 61.682  85.296  64.276 1.00 381.61 ? 460 ILE B CB  1 
ATOM   3531 C CG1 . ILE B 2 460 ? 62.972  85.986  63.812 1.00 370.08 ? 460 ILE B CG1 1 
ATOM   3532 C CG2 . ILE B 2 460 ? 62.004  83.952  64.918 1.00 437.23 ? 460 ILE B CG2 1 
ATOM   3533 C CD1 . ILE B 2 460 ? 62.818  87.459  63.518 1.00 387.84 ? 460 ILE B CD1 1 
ATOM   3534 N N   . GLY B 2 461 ? 60.735  83.101  61.840 1.00 310.40 ? 461 GLY B N   1 
ATOM   3535 C CA  . GLY B 2 461 ? 60.933  82.283  60.642 1.00 311.98 ? 461 GLY B CA  1 
ATOM   3536 C C   . GLY B 2 461 ? 60.330  82.884  59.362 1.00 247.20 ? 461 GLY B C   1 
ATOM   3537 O O   . GLY B 2 461 ? 60.992  82.929  58.330 1.00 154.45 ? 461 GLY B O   1 
ATOM   3538 N N   . PHE B 2 462 ? 59.085  83.373  59.414 1.00 259.56 ? 462 PHE B N   1 
ATOM   3539 C CA  . PHE B 2 462 ? 58.468  84.044  58.266 1.00 251.02 ? 462 PHE B CA  1 
ATOM   3540 C C   . PHE B 2 462 ? 59.234  85.299  57.809 1.00 208.60 ? 462 PHE B C   1 
ATOM   3541 O O   . PHE B 2 462 ? 59.145  85.639  56.632 1.00 241.92 ? 462 PHE B O   1 
ATOM   3542 C CB  . PHE B 2 462 ? 56.984  84.346  58.532 1.00 302.52 ? 462 PHE B CB  1 
ATOM   3543 C CG  . PHE B 2 462 ? 56.053  83.279  57.997 1.00 354.84 ? 462 PHE B CG  1 
ATOM   3544 C CD1 . PHE B 2 462 ? 55.664  83.284  56.660 1.00 373.42 ? 462 PHE B CD1 1 
ATOM   3545 C CD2 . PHE B 2 462 ? 55.571  82.257  58.812 1.00 368.45 ? 462 PHE B CD2 1 
ATOM   3546 C CE1 . PHE B 2 462 ? 54.812  82.306  56.154 1.00 337.17 ? 462 PHE B CE1 1 
ATOM   3547 C CE2 . PHE B 2 462 ? 54.720  81.281  58.301 1.00 343.19 ? 462 PHE B CE2 1 
ATOM   3548 C CZ  . PHE B 2 462 ? 54.343  81.303  56.974 1.00 295.13 ? 462 PHE B CZ  1 
ATOM   3549 N N   . THR B 2 463 ? 60.003  85.980  58.676 1.00 212.91 ? 463 THR B N   1 
ATOM   3550 C CA  . THR B 2 463 ? 60.827  87.115  58.241 1.00 264.73 ? 463 THR B CA  1 
ATOM   3551 C C   . THR B 2 463 ? 62.008  86.683  57.354 1.00 211.85 ? 463 THR B C   1 
ATOM   3552 O O   . THR B 2 463 ? 62.421  87.443  56.485 1.00 186.65 ? 463 THR B O   1 
ATOM   3553 C CB  . THR B 2 463 ? 61.339  87.982  59.405 1.00 353.49 ? 463 THR B CB  1 
ATOM   3554 O OG1 . THR B 2 463 ? 62.428  87.341  60.073 1.00 408.01 ? 463 THR B OG1 1 
ATOM   3555 C CG2 . THR B 2 463 ? 60.252  88.322  60.405 1.00 416.43 ? 463 THR B CG2 1 
ATOM   3556 N N   . ILE B 2 464 ? 62.542  85.469  57.530 1.00 208.96 ? 464 ILE B N   1 
ATOM   3557 C CA  . ILE B 2 464 ? 63.528  84.904  56.612 1.00 199.17 ? 464 ILE B CA  1 
ATOM   3558 C C   . ILE B 2 464 ? 62.888  84.745  55.227 1.00 209.68 ? 464 ILE B C   1 
ATOM   3559 O O   . ILE B 2 464 ? 63.484  85.143  54.234 1.00 197.45 ? 464 ILE B O   1 
ATOM   3560 C CB  . ILE B 2 464 ? 64.102  83.559  57.134 1.00 305.30 ? 464 ILE B CB  1 
ATOM   3561 C CG1 . ILE B 2 464 ? 64.744  83.690  58.523 1.00 353.40 ? 464 ILE B CG1 1 
ATOM   3562 C CG2 . ILE B 2 464 ? 65.078  82.933  56.138 1.00 350.43 ? 464 ILE B CG2 1 
ATOM   3563 C CD1 . ILE B 2 464 ? 65.912  84.668  58.611 1.00 369.05 ? 464 ILE B CD1 1 
ATOM   3564 N N   . ILE B 2 465 ? 61.670  84.179  55.158 1.00 213.06 ? 465 ILE B N   1 
ATOM   3565 C CA  . ILE B 2 465 ? 60.925  83.982  53.913 1.00 181.53 ? 465 ILE B CA  1 
ATOM   3566 C C   . ILE B 2 465 ? 60.724  85.331  53.216 1.00 187.55 ? 465 ILE B C   1 
ATOM   3567 O O   . ILE B 2 465 ? 61.146  85.513  52.073 1.00 152.22 ? 465 ILE B O   1 
ATOM   3568 C CB  . ILE B 2 465 ? 59.578  83.261  54.158 1.00 161.91 ? 465 ILE B CB  1 
ATOM   3569 C CG1 . ILE B 2 465 ? 59.761  81.902  54.845 1.00 248.08 ? 465 ILE B CG1 1 
ATOM   3570 C CG2 . ILE B 2 465 ? 58.801  83.118  52.853 1.00 195.41 ? 465 ILE B CG2 1 
ATOM   3571 C CD1 . ILE B 2 465 ? 58.488  81.141  55.152 1.00 323.99 ? 465 ILE B CD1 1 
ATOM   3572 N N   . LEU B 2 466 ? 60.094  86.278  53.931 1.00 240.26 ? 466 LEU B N   1 
ATOM   3573 C CA  . LEU B 2 466 ? 59.719  87.585  53.396 1.00 227.61 ? 466 LEU B CA  1 
ATOM   3574 C C   . LEU B 2 466 ? 60.933  88.480  53.099 1.00 178.27 ? 466 LEU B C   1 
ATOM   3575 O O   . LEU B 2 466 ? 60.794  89.416  52.328 1.00 196.65 ? 466 LEU B O   1 
ATOM   3576 C CB  . LEU B 2 466 ? 58.729  88.256  54.362 1.00 285.95 ? 466 LEU B CB  1 
ATOM   3577 C CG  . LEU B 2 466 ? 57.373  87.553  54.507 1.00 328.10 ? 466 LEU B CG  1 
ATOM   3578 C CD1 . LEU B 2 466 ? 56.604  88.089  55.707 1.00 361.40 ? 466 LEU B CD1 1 
ATOM   3579 C CD2 . LEU B 2 466 ? 56.525  87.685  53.247 1.00 336.92 ? 466 LEU B CD2 1 
ATOM   3580 N N   . SER B 2 467 ? 62.130  88.208  53.639 1.00 165.41 ? 467 SER B N   1 
ATOM   3581 C CA  . SER B 2 467 ? 63.360  88.914  53.269 1.00 183.74 ? 467 SER B CA  1 
ATOM   3582 C C   . SER B 2 467 ? 63.713  88.813  51.785 1.00 177.14 ? 467 SER B C   1 
ATOM   3583 O O   . SER B 2 467 ? 64.519  89.603  51.305 1.00 172.59 ? 467 SER B O   1 
ATOM   3584 C CB  . SER B 2 467 ? 64.551  88.424  54.069 1.00 285.21 ? 467 SER B CB  1 
ATOM   3585 O OG  . SER B 2 467 ? 65.021  87.163  53.599 1.00 316.58 ? 467 SER B OG  1 
ATOM   3586 N N   . GLY B 2 468 ? 63.122  87.857  51.056 1.00 233.19 ? 468 GLY B N   1 
ATOM   3587 C CA  . GLY B 2 468 ? 63.351  87.684  49.634 1.00 248.62 ? 468 GLY B CA  1 
ATOM   3588 C C   . GLY B 2 468 ? 62.705  88.745  48.756 1.00 209.50 ? 468 GLY B C   1 
ATOM   3589 O O   . GLY B 2 468 ? 63.228  89.012  47.683 1.00 174.17 ? 468 GLY B O   1 
ATOM   3590 N N   . LEU B 2 469 ? 61.591  89.364  49.176 1.00 164.63 ? 469 LEU B N   1 
ATOM   3591 C CA  . LEU B 2 469 ? 60.850  90.261  48.299 1.00 160.12 ? 469 LEU B CA  1 
ATOM   3592 C C   . LEU B 2 469 ? 61.691  91.484  47.918 1.00 145.31 ? 469 LEU B C   1 
ATOM   3593 O O   . LEU B 2 469 ? 61.704  91.837  46.737 1.00 188.17 ? 469 LEU B O   1 
ATOM   3594 C CB  . LEU B 2 469 ? 59.497  90.627  48.930 1.00 169.29 ? 469 LEU B CB  1 
ATOM   3595 C CG  . LEU B 2 469 ? 58.436  89.525  48.810 1.00 203.62 ? 469 LEU B CG  1 
ATOM   3596 C CD1 . LEU B 2 469 ? 58.510  88.574  49.987 1.00 208.28 ? 469 LEU B CD1 1 
ATOM   3597 C CD2 . LEU B 2 469 ? 57.024  90.098  48.689 1.00 277.50 ? 469 LEU B CD2 1 
ATOM   3598 N N   . PRO B 2 470 ? 62.396  92.189  48.831 1.00 131.02 ? 470 PRO B N   1 
ATOM   3599 C CA  . PRO B 2 470 ? 63.346  93.241  48.446 1.00 190.45 ? 470 PRO B CA  1 
ATOM   3600 C C   . PRO B 2 470 ? 64.343  92.845  47.364 1.00 175.16 ? 470 PRO B C   1 
ATOM   3601 O O   . PRO B 2 470 ? 64.509  93.590  46.405 1.00 207.48 ? 470 PRO B O   1 
ATOM   3602 C CB  . PRO B 2 470 ? 64.064  93.588  49.765 1.00 238.33 ? 470 PRO B CB  1 
ATOM   3603 C CG  . PRO B 2 470 ? 62.985  93.347  50.794 1.00 248.62 ? 470 PRO B CG  1 
ATOM   3604 C CD  . PRO B 2 470 ? 62.285  92.099  50.284 1.00 163.78 ? 470 PRO B CD  1 
ATOM   3605 N N   . VAL B 2 471 ? 64.979  91.675  47.507 1.00 182.75 ? 471 VAL B N   1 
ATOM   3606 C CA  . VAL B 2 471 ? 65.990  91.202  46.567 1.00 218.71 ? 471 VAL B CA  1 
ATOM   3607 C C   . VAL B 2 471 ? 65.340  90.793  45.240 1.00 210.11 ? 471 VAL B C   1 
ATOM   3608 O O   . VAL B 2 471 ? 65.884  91.086  44.171 1.00 258.26 ? 471 VAL B O   1 
ATOM   3609 C CB  . VAL B 2 471 ? 66.836  90.068  47.177 1.00 214.12 ? 471 VAL B CB  1 
ATOM   3610 C CG1 . VAL B 2 471 ? 67.924  89.595  46.224 1.00 287.20 ? 471 VAL B CG1 1 
ATOM   3611 C CG2 . VAL B 2 471 ? 67.469  90.511  48.485 1.00 249.50 ? 471 VAL B CG2 1 
ATOM   3612 N N   . TYR B 2 472 ? 64.176  90.142  45.299 1.00 162.83 ? 472 TYR B N   1 
ATOM   3613 C CA  . TYR B 2 472 ? 63.414  89.760  44.116 1.00 157.71 ? 472 TYR B CA  1 
ATOM   3614 C C   . TYR B 2 472 ? 63.058  90.976  43.267 1.00 183.45 ? 472 TYR B C   1 
ATOM   3615 O O   . TYR B 2 472 ? 63.350  91.022  42.085 1.00 145.00 ? 472 TYR B O   1 
ATOM   3616 C CB  . TYR B 2 472 ? 62.129  89.052  44.546 1.00 175.00 ? 472 TYR B CB  1 
ATOM   3617 C CG  . TYR B 2 472 ? 61.245  88.662  43.379 1.00 155.22 ? 472 TYR B CG  1 
ATOM   3618 C CD1 . TYR B 2 472 ? 61.564  87.576  42.576 1.00 178.61 ? 472 TYR B CD1 1 
ATOM   3619 C CD2 . TYR B 2 472 ? 60.113  89.383  43.075 1.00 186.61 ? 472 TYR B CD2 1 
ATOM   3620 C CE1 . TYR B 2 472 ? 60.770  87.203  41.500 1.00 145.08 ? 472 TYR B CE1 1 
ATOM   3621 C CE2 . TYR B 2 472 ? 59.309  89.024  41.999 1.00 237.12 ? 472 TYR B CE2 1 
ATOM   3622 C CZ  . TYR B 2 472 ? 59.633  87.928  41.212 1.00 172.63 ? 472 TYR B CZ  1 
ATOM   3623 O OH  . TYR B 2 472 ? 58.857  87.563  40.143 1.00 204.36 ? 472 TYR B OH  1 
ATOM   3624 N N   . PHE B 2 473 ? 62.426  91.985  43.864 1.00 201.28 ? 473 PHE B N   1 
ATOM   3625 C CA  . PHE B 2 473 ? 62.063  93.177  43.113 1.00 174.52 ? 473 PHE B CA  1 
ATOM   3626 C C   . PHE B 2 473 ? 63.318  93.862  42.563 1.00 172.70 ? 473 PHE B C   1 
ATOM   3627 O O   . PHE B 2 473 ? 63.340  94.186  41.377 1.00 269.30 ? 473 PHE B O   1 
ATOM   3628 C CB  . PHE B 2 473 ? 61.163  94.073  43.968 1.00 171.39 ? 473 PHE B CB  1 
ATOM   3629 C CG  . PHE B 2 473 ? 59.754  93.545  44.150 1.00 216.98 ? 473 PHE B CG  1 
ATOM   3630 C CD1 . PHE B 2 473 ? 58.992  93.095  43.068 1.00 208.20 ? 473 PHE B CD1 1 
ATOM   3631 C CD2 . PHE B 2 473 ? 59.166  93.512  45.412 1.00 296.02 ? 473 PHE B CD2 1 
ATOM   3632 C CE1 . PHE B 2 473 ? 57.695  92.622  43.246 1.00 249.47 ? 473 PHE B CE1 1 
ATOM   3633 C CE2 . PHE B 2 473 ? 57.868  93.038  45.587 1.00 327.59 ? 473 PHE B CE2 1 
ATOM   3634 C CZ  . PHE B 2 473 ? 57.134  92.592  44.505 1.00 285.74 ? 473 PHE B CZ  1 
ATOM   3635 N N   . PHE B 2 474 ? 64.350  94.080  43.391 1.00 128.86 ? 474 PHE B N   1 
ATOM   3636 C CA  . PHE B 2 474 ? 65.578  94.750  42.958 1.00 215.79 ? 474 PHE B CA  1 
ATOM   3637 C C   . PHE B 2 474 ? 66.285  94.048  41.782 1.00 209.26 ? 474 PHE B C   1 
ATOM   3638 O O   . PHE B 2 474 ? 66.725  94.731  40.838 1.00 259.39 ? 474 PHE B O   1 
ATOM   3639 C CB  . PHE B 2 474 ? 66.541  94.924  44.137 1.00 248.53 ? 474 PHE B CB  1 
ATOM   3640 C CG  . PHE B 2 474 ? 67.793  95.702  43.799 1.00 273.76 ? 474 PHE B CG  1 
ATOM   3641 C CD1 . PHE B 2 474 ? 68.887  95.076  43.200 1.00 270.85 ? 474 PHE B CD1 1 
ATOM   3642 C CD2 . PHE B 2 474 ? 67.875  97.069  44.062 1.00 335.84 ? 474 PHE B CD2 1 
ATOM   3643 C CE1 . PHE B 2 474 ? 70.036  95.793  42.885 1.00 337.15 ? 474 PHE B CE1 1 
ATOM   3644 C CE2 . PHE B 2 474 ? 69.028  97.783  43.748 1.00 384.33 ? 474 PHE B CE2 1 
ATOM   3645 C CZ  . PHE B 2 474 ? 70.104  97.145  43.157 1.00 392.95 ? 474 PHE B CZ  1 
ATOM   3646 N N   . GLY B 2 475 ? 66.385  92.710  41.824 1.00 173.72 ? 475 GLY B N   1 
ATOM   3647 C CA  . GLY B 2 475 ? 67.144  91.941  40.845 1.00 211.72 ? 475 GLY B CA  1 
ATOM   3648 C C   . GLY B 2 475 ? 66.326  91.394  39.664 1.00 236.64 ? 475 GLY B C   1 
ATOM   3649 O O   . GLY B 2 475 ? 66.839  91.358  38.543 1.00 232.06 ? 475 GLY B O   1 
ATOM   3650 N N   . VAL B 2 476 ? 65.070  90.957  39.906 1.00 191.32 ? 476 VAL B N   1 
ATOM   3651 C CA  . VAL B 2 476 ? 64.297  90.158  38.956 1.00 191.51 ? 476 VAL B CA  1 
ATOM   3652 C C   . VAL B 2 476 ? 63.276  91.011  38.196 1.00 245.15 ? 476 VAL B C   1 
ATOM   3653 O O   . VAL B 2 476 ? 63.135  90.833  36.984 1.00 304.92 ? 476 VAL B O   1 
ATOM   3654 C CB  . VAL B 2 476 ? 63.595  88.959  39.636 1.00 152.01 ? 476 VAL B CB  1 
ATOM   3655 C CG1 . VAL B 2 476 ? 62.870  88.072  38.634 1.00 191.45 ? 476 VAL B CG1 1 
ATOM   3656 C CG2 . VAL B 2 476 ? 64.575  88.106  40.429 1.00 184.74 ? 476 VAL B CG2 1 
ATOM   3657 N N   . TRP B 2 477 ? 62.552  91.911  38.878 1.00 234.22 ? 477 TRP B N   1 
ATOM   3658 C CA  . TRP B 2 477 ? 61.246  92.351  38.378 1.00 269.84 ? 477 TRP B CA  1 
ATOM   3659 C C   . TRP B 2 477 ? 61.089  93.878  38.310 1.00 238.43 ? 477 TRP B C   1 
ATOM   3660 O O   . TRP B 2 477 ? 60.776  94.398  37.235 1.00 275.39 ? 477 TRP B O   1 
ATOM   3661 C CB  . TRP B 2 477 ? 60.148  91.697  39.236 1.00 318.06 ? 477 TRP B CB  1 
ATOM   3662 C CG  . TRP B 2 477 ? 58.744  91.866  38.699 1.00 336.64 ? 477 TRP B CG  1 
ATOM   3663 C CD1 . TRP B 2 477 ? 58.075  90.948  37.941 1.00 345.09 ? 477 TRP B CD1 1 
ATOM   3664 C CD2 . TRP B 2 477 ? 57.831  92.990  38.866 1.00 327.54 ? 477 TRP B CD2 1 
ATOM   3665 N NE1 . TRP B 2 477 ? 56.826  91.416  37.621 1.00 337.19 ? 477 TRP B NE1 1 
ATOM   3666 C CE2 . TRP B 2 477 ? 56.639  92.663  38.171 1.00 352.43 ? 477 TRP B CE2 1 
ATOM   3667 C CE3 . TRP B 2 477 ? 57.890  94.234  39.527 1.00 288.80 ? 477 TRP B CE3 1 
ATOM   3668 C CZ2 . TRP B 2 477 ? 55.538  93.534  38.125 1.00 377.08 ? 477 TRP B CZ2 1 
ATOM   3669 C CZ3 . TRP B 2 477 ? 56.809  95.095  39.478 1.00 316.08 ? 477 TRP B CZ3 1 
ATOM   3670 C CH2 . TRP B 2 477 ? 55.645  94.745  38.786 1.00 369.19 ? 477 TRP B CH2 1 
ATOM   3671 N N   . TRP B 2 478 ? 61.291  94.579  39.435 1.00 268.97 ? 478 TRP B N   1 
ATOM   3672 C CA  . TRP B 2 478 ? 61.173  96.032  39.526 1.00 372.45 ? 478 TRP B CA  1 
ATOM   3673 C C   . TRP B 2 478 ? 62.385  96.685  38.851 1.00 369.77 ? 478 TRP B C   1 
ATOM   3674 O O   . TRP B 2 478 ? 62.247  97.747  38.223 1.00 403.10 ? 478 TRP B O   1 
ATOM   3675 C CB  . TRP B 2 478 ? 61.010  96.398  41.018 1.00 467.12 ? 478 TRP B CB  1 
ATOM   3676 C CG  . TRP B 2 478 ? 60.517  97.774  41.416 1.00 485.69 ? 478 TRP B CG  1 
ATOM   3677 C CD1 . TRP B 2 478 ? 60.922  98.988  40.938 1.00 462.52 ? 478 TRP B CD1 1 
ATOM   3678 C CD2 . TRP B 2 478 ? 59.513  98.061  42.436 1.00 488.72 ? 478 TRP B CD2 1 
ATOM   3679 N NE1 . TRP B 2 478 ? 60.237  99.996  41.569 1.00 466.09 ? 478 TRP B NE1 1 
ATOM   3680 C CE2 . TRP B 2 478 ? 59.366  99.468  42.496 1.00 487.39 ? 478 TRP B CE2 1 
ATOM   3681 C CE3 . TRP B 2 478 ? 58.723  97.272  43.296 1.00 444.90 ? 478 TRP B CE3 1 
ATOM   3682 C CZ2 . TRP B 2 478 ? 58.465  100.086 43.381 1.00 468.61 ? 478 TRP B CZ2 1 
ATOM   3683 C CZ3 . TRP B 2 478 ? 57.836  97.880  44.170 1.00 365.51 ? 478 TRP B CZ3 1 
ATOM   3684 C CH2 . TRP B 2 478 ? 57.712  99.273  44.210 1.00 406.92 ? 478 TRP B CH2 1 
ATOM   3685 N N   . LYS B 2 479 ? 63.564  96.033  38.995 1.00 306.13 ? 479 LYS B N   1 
ATOM   3686 C CA  . LYS B 2 479 ? 64.766  96.240  38.187 1.00 285.45 ? 479 LYS B CA  1 
ATOM   3687 C C   . LYS B 2 479 ? 65.189  97.719  38.123 1.00 293.14 ? 479 LYS B C   1 
ATOM   3688 O O   . LYS B 2 479 ? 65.140  98.369  37.077 1.00 313.95 ? 479 LYS B O   1 
ATOM   3689 C CB  . LYS B 2 479 ? 64.549  95.634  36.793 1.00 258.36 ? 479 LYS B CB  1 
ATOM   3690 C CG  . LYS B 2 479 ? 65.791  95.454  35.939 1.00 296.45 ? 479 LYS B CG  1 
ATOM   3691 C CD  . LYS B 2 479 ? 65.521  94.678  34.673 1.00 299.05 ? 479 LYS B CD  1 
ATOM   3692 C CE  . LYS B 2 479 ? 64.628  95.386  33.678 1.00 274.83 ? 479 LYS B CE  1 
ATOM   3693 N NZ  . LYS B 2 479 ? 64.437  94.563  32.460 1.00 281.27 ? 479 LYS B NZ  1 
ATOM   3694 N N   . ASN B 2 480 ? 65.640  98.260  39.261 1.00 269.38 ? 480 ASN B N   1 
ATOM   3695 C CA  . ASN B 2 480 ? 66.325  99.551  39.267 1.00 267.41 ? 480 ASN B CA  1 
ATOM   3696 C C   . ASN B 2 480 ? 67.592  99.419  38.407 1.00 286.13 ? 480 ASN B C   1 
ATOM   3697 O O   . ASN B 2 480 ? 68.379  98.494  38.616 1.00 297.10 ? 480 ASN B O   1 
ATOM   3698 C CB  . ASN B 2 480 ? 66.638  100.033 40.688 1.00 318.78 ? 480 ASN B CB  1 
ATOM   3699 C CG  . ASN B 2 480 ? 65.429  100.104 41.604 1.00 349.04 ? 480 ASN B CG  1 
ATOM   3700 O OD1 . ASN B 2 480 ? 64.996  99.077  42.124 1.00 350.84 ? 480 ASN B OD1 1 
ATOM   3701 N ND2 . ASN B 2 480 ? 64.892  101.297 41.821 1.00 353.74 ? 480 ASN B ND2 1 
ATOM   3702 N N   . LYS B 2 481 ? 67.787  100.333 37.431 1.00 297.47 ? 481 LYS B N   1 
ATOM   3703 C CA  . LYS B 2 481 ? 68.711  100.106 36.315 1.00 291.65 ? 481 LYS B CA  1 
ATOM   3704 C C   . LYS B 2 481 ? 69.426  101.387 35.825 1.00 322.56 ? 481 LYS B C   1 
ATOM   3705 O O   . LYS B 2 481 ? 69.361  101.735 34.637 1.00 310.47 ? 481 LYS B O   1 
ATOM   3706 C CB  . LYS B 2 481 ? 67.927  99.369  35.214 1.00 261.00 ? 481 LYS B CB  1 
ATOM   3707 C CG  . LYS B 2 481 ? 66.668  100.046 34.676 1.00 287.96 ? 481 LYS B CG  1 
ATOM   3708 C CD  . LYS B 2 481 ? 65.816  99.125  33.826 1.00 280.31 ? 481 LYS B CD  1 
ATOM   3709 C CE  . LYS B 2 481 ? 64.532  99.764  33.330 1.00 279.90 ? 481 LYS B CE  1 
ATOM   3710 N NZ  . LYS B 2 481 ? 63.552  99.990  34.422 1.00 263.32 ? 481 LYS B NZ  1 
ATOM   3711 N N   . PRO B 2 482 ? 70.179  102.130 36.685 1.00 334.93 ? 482 PRO B N   1 
ATOM   3712 C CA  . PRO B 2 482 ? 71.124  103.138 36.198 1.00 319.15 ? 482 PRO B CA  1 
ATOM   3713 C C   . PRO B 2 482 ? 72.178  102.450 35.335 1.00 311.37 ? 482 PRO B C   1 
ATOM   3714 O O   . PRO B 2 482 ? 72.658  101.392 35.708 1.00 312.67 ? 482 PRO B O   1 
ATOM   3715 C CB  . PRO B 2 482 ? 71.781  103.732 37.458 1.00 311.61 ? 482 PRO B CB  1 
ATOM   3716 C CG  . PRO B 2 482 ? 70.870  103.344 38.603 1.00 320.71 ? 482 PRO B CG  1 
ATOM   3717 C CD  . PRO B 2 482 ? 70.205  102.058 38.156 1.00 334.04 ? 482 PRO B CD  1 
ATOM   3718 N N   . LYS B 2 483 ? 72.557  103.020 34.185 1.00 324.95 ? 483 LYS B N   1 
ATOM   3719 C CA  . LYS B 2 483 ? 73.457  102.324 33.258 1.00 351.51 ? 483 LYS B CA  1 
ATOM   3720 C C   . LYS B 2 483 ? 74.858  102.085 33.850 1.00 306.78 ? 483 LYS B C   1 
ATOM   3721 O O   . LYS B 2 483 ? 75.539  101.155 33.406 1.00 280.84 ? 483 LYS B O   1 
ATOM   3722 C CB  . LYS B 2 483 ? 73.508  103.043 31.901 1.00 395.69 ? 483 LYS B CB  1 
ATOM   3723 C CG  . LYS B 2 483 ? 72.174  103.126 31.160 1.00 425.72 ? 483 LYS B CG  1 
ATOM   3724 C CD  . LYS B 2 483 ? 71.485  101.786 30.911 1.00 439.37 ? 483 LYS B CD  1 
ATOM   3725 C CE  . LYS B 2 483 ? 70.230  101.880 30.066 1.00 457.78 ? 483 LYS B CE  1 
ATOM   3726 N NZ  . LYS B 2 483 ? 70.534  102.125 28.636 1.00 473.60 ? 483 LYS B NZ  1 
ATOM   3727 N N   . TRP B 2 484 ? 75.288  102.871 34.854 1.00 295.56 ? 484 TRP B N   1 
ATOM   3728 C CA  . TRP B 2 484 ? 76.512  102.583 35.601 1.00 336.14 ? 484 TRP B CA  1 
ATOM   3729 C C   . TRP B 2 484 ? 76.419  101.283 36.416 1.00 317.23 ? 484 TRP B C   1 
ATOM   3730 O O   . TRP B 2 484 ? 77.426  100.578 36.550 1.00 326.50 ? 484 TRP B O   1 
ATOM   3731 C CB  . TRP B 2 484 ? 76.907  103.776 36.493 1.00 376.78 ? 484 TRP B CB  1 
ATOM   3732 C CG  . TRP B 2 484 ? 75.938  104.141 37.594 1.00 385.57 ? 484 TRP B CG  1 
ATOM   3733 C CD1 . TRP B 2 484 ? 75.051  105.176 37.545 1.00 408.65 ? 484 TRP B CD1 1 
ATOM   3734 C CD2 . TRP B 2 484 ? 75.752  103.516 38.896 1.00 362.41 ? 484 TRP B CD2 1 
ATOM   3735 N NE1 . TRP B 2 484 ? 74.326  105.238 38.706 1.00 400.95 ? 484 TRP B NE1 1 
ATOM   3736 C CE2 . TRP B 2 484 ? 74.726  104.237 39.559 1.00 373.38 ? 484 TRP B CE2 1 
ATOM   3737 C CE3 . TRP B 2 484 ? 76.335  102.427 39.571 1.00 352.57 ? 484 TRP B CE3 1 
ATOM   3738 C CZ2 . TRP B 2 484 ? 74.286  103.899 40.849 1.00 362.80 ? 484 TRP B CZ2 1 
ATOM   3739 C CZ3 . TRP B 2 484 ? 75.902  102.093 40.842 1.00 361.48 ? 484 TRP B CZ3 1 
ATOM   3740 C CH2 . TRP B 2 484 ? 74.890  102.824 41.472 1.00 360.62 ? 484 TRP B CH2 1 
ATOM   3741 N N   . LEU B 2 485 ? 75.231  100.958 36.958 1.00 274.29 ? 485 LEU B N   1 
ATOM   3742 C CA  . LEU B 2 485 ? 75.023  99.717  37.699 1.00 267.59 ? 485 LEU B CA  1 
ATOM   3743 C C   . LEU B 2 485 ? 75.172  98.517  36.757 1.00 242.33 ? 485 LEU B C   1 
ATOM   3744 O O   . LEU B 2 485 ? 75.864  97.557  37.097 1.00 235.90 ? 485 LEU B O   1 
ATOM   3745 C CB  . LEU B 2 485 ? 73.650  99.758  38.389 1.00 278.55 ? 485 LEU B CB  1 
ATOM   3746 C CG  . LEU B 2 485 ? 73.266  98.508  39.186 1.00 304.92 ? 485 LEU B CG  1 
ATOM   3747 C CD1 . LEU B 2 485 ? 74.207  98.302  40.365 1.00 355.35 ? 485 LEU B CD1 1 
ATOM   3748 C CD2 . LEU B 2 485 ? 71.828  98.582  39.662 1.00 284.86 ? 485 LEU B CD2 1 
ATOM   3749 N N   . LEU B 2 486 ? 74.541  98.577  35.574 1.00 220.96 ? 486 LEU B N   1 
ATOM   3750 C CA  . LEU B 2 486 ? 74.650  97.535  34.556 1.00 252.89 ? 486 LEU B CA  1 
ATOM   3751 C C   . LEU B 2 486 ? 76.100  97.374  34.072 1.00 228.40 ? 486 LEU B C   1 
ATOM   3752 O O   . LEU B 2 486 ? 76.560  96.238  33.915 1.00 245.12 ? 486 LEU B O   1 
ATOM   3753 C CB  . LEU B 2 486 ? 73.687  97.832  33.392 1.00 269.75 ? 486 LEU B CB  1 
ATOM   3754 C CG  . LEU B 2 486 ? 72.215  97.420  33.565 1.00 260.86 ? 486 LEU B CG  1 
ATOM   3755 C CD1 . LEU B 2 486 ? 72.076  95.913  33.754 1.00 274.89 ? 486 LEU B CD1 1 
ATOM   3756 C CD2 . LEU B 2 486 ? 71.532  98.159  34.714 1.00 220.15 ? 486 LEU B CD2 1 
ATOM   3757 N N   . GLN B 2 487 ? 76.825  98.485  33.860 1.00 229.67 ? 487 GLN B N   1 
ATOM   3758 C CA  . GLN B 2 487 ? 78.243  98.449  33.501 1.00 272.59 ? 487 GLN B CA  1 
ATOM   3759 C C   . GLN B 2 487 ? 79.089  97.781  34.601 1.00 256.83 ? 487 GLN B C   1 
ATOM   3760 O O   . GLN B 2 487 ? 80.019  97.030  34.279 1.00 239.05 ? 487 GLN B O   1 
ATOM   3761 C CB  . GLN B 2 487 ? 78.717  99.870  33.161 1.00 358.22 ? 487 GLN B CB  1 
ATOM   3762 C CG  . GLN B 2 487 ? 80.184  99.978  32.726 1.00 418.23 ? 487 GLN B CG  1 
ATOM   3763 C CD  . GLN B 2 487 ? 81.196  100.254 33.820 1.00 441.82 ? 487 GLN B CD  1 
ATOM   3764 O OE1 . GLN B 2 487 ? 80.878  100.317 35.006 1.00 461.70 ? 487 GLN B OE1 1 
ATOM   3765 N NE2 . GLN B 2 487 ? 82.449  100.432 33.426 1.00 420.92 ? 487 GLN B NE2 1 
ATOM   3766 N N   . GLY B 2 488 ? 78.772  98.038  35.886 1.00 264.48 ? 488 GLY B N   1 
ATOM   3767 C CA  . GLY B 2 488 ? 79.444  97.421  37.026 1.00 271.70 ? 488 GLY B CA  1 
ATOM   3768 C C   . GLY B 2 488 ? 79.172  95.922  37.158 1.00 231.99 ? 488 GLY B C   1 
ATOM   3769 O O   . GLY B 2 488 ? 80.101  95.146  37.371 1.00 183.25 ? 488 GLY B O   1 
ATOM   3770 N N   . ILE B 2 489 ? 77.902  95.510  37.032 1.00 196.58 ? 489 ILE B N   1 
ATOM   3771 C CA  . ILE B 2 489 ? 77.515  94.103  37.082 1.00 214.31 ? 489 ILE B CA  1 
ATOM   3772 C C   . ILE B 2 489 ? 78.201  93.332  35.949 1.00 198.01 ? 489 ILE B C   1 
ATOM   3773 O O   . ILE B 2 489 ? 78.733  92.245  36.184 1.00 174.11 ? 489 ILE B O   1 
ATOM   3774 C CB  . ILE B 2 489 ? 75.970  93.963  37.086 1.00 234.46 ? 489 ILE B CB  1 
ATOM   3775 C CG1 . ILE B 2 489 ? 75.376  94.444  38.418 1.00 274.11 ? 489 ILE B CG1 1 
ATOM   3776 C CG2 . ILE B 2 489 ? 75.488  92.550  36.749 1.00 265.75 ? 489 ILE B CG2 1 
ATOM   3777 C CD1 . ILE B 2 489 ? 75.672  93.557  39.634 1.00 289.46 ? 489 ILE B CD1 1 
ATOM   3778 N N   . PHE B 2 490 ? 78.198  93.878  34.728 1.00 220.47 ? 490 PHE B N   1 
ATOM   3779 C CA  . PHE B 2 490 ? 78.890  93.252  33.612 1.00 249.48 ? 490 PHE B CA  1 
ATOM   3780 C C   . PHE B 2 490 ? 80.398  93.153  33.885 1.00 222.50 ? 490 PHE B C   1 
ATOM   3781 O O   . PHE B 2 490 ? 80.974  92.073  33.745 1.00 229.24 ? 490 PHE B O   1 
ATOM   3782 C CB  . PHE B 2 490 ? 78.575  93.981  32.302 1.00 280.00 ? 490 PHE B CB  1 
ATOM   3783 C CG  . PHE B 2 490 ? 79.164  93.296  31.094 1.00 267.96 ? 490 PHE B CG  1 
ATOM   3784 C CD1 . PHE B 2 490 ? 80.446  93.616  30.661 1.00 283.77 ? 490 PHE B CD1 1 
ATOM   3785 C CD2 . PHE B 2 490 ? 78.452  92.317  30.402 1.00 243.73 ? 490 PHE B CD2 1 
ATOM   3786 C CE1 . PHE B 2 490 ? 80.997  92.983  29.553 1.00 299.32 ? 490 PHE B CE1 1 
ATOM   3787 C CE2 . PHE B 2 490 ? 79.008  91.684  29.299 1.00 260.04 ? 490 PHE B CE2 1 
ATOM   3788 C CZ  . PHE B 2 490 ? 80.279  92.016  28.877 1.00 286.00 ? 490 PHE B CZ  1 
ATOM   3789 N N   . SER B 2 491 ? 81.037  94.263  34.277 1.00 227.42 ? 491 SER B N   1 
ATOM   3790 C CA  . SER B 2 491 ? 82.469  94.288  34.572 1.00 263.98 ? 491 SER B CA  1 
ATOM   3791 C C   . SER B 2 491 ? 82.856  93.264  35.647 1.00 239.66 ? 491 SER B C   1 
ATOM   3792 O O   . SER B 2 491 ? 83.872  92.574  35.516 1.00 200.89 ? 491 SER B O   1 
ATOM   3793 C CB  . SER B 2 491 ? 82.924  95.677  34.970 1.00 327.67 ? 491 SER B CB  1 
ATOM   3794 O OG  . SER B 2 491 ? 82.646  96.620  33.945 1.00 356.32 ? 491 SER B OG  1 
ATOM   3795 N N   . THR B 2 492 ? 82.052  93.153  36.715 1.00 211.38 ? 492 THR B N   1 
ATOM   3796 C CA  . THR B 2 492 ? 82.275  92.181  37.777 1.00 207.88 ? 492 THR B CA  1 
ATOM   3797 C C   . THR B 2 492 ? 82.135  90.757  37.242 1.00 197.37 ? 492 THR B C   1 
ATOM   3798 O O   . THR B 2 492 ? 82.932  89.886  37.578 1.00 224.37 ? 492 THR B O   1 
ATOM   3799 C CB  . THR B 2 492 ? 81.320  92.406  38.958 1.00 243.66 ? 492 THR B CB  1 
ATOM   3800 O OG1 . THR B 2 492 ? 81.411  93.764  39.393 1.00 273.42 ? 492 THR B OG1 1 
ATOM   3801 C CG2 . THR B 2 492 ? 81.610  91.517  40.149 1.00 306.83 ? 492 THR B CG2 1 
ATOM   3802 N N   . THR B 2 493 ? 81.124  90.505  36.405 1.00 179.29 ? 493 THR B N   1 
ATOM   3803 C CA  . THR B 2 493 ? 80.892  89.178  35.842 1.00 173.44 ? 493 THR B CA  1 
ATOM   3804 C C   . THR B 2 493 ? 82.069  88.731  34.973 1.00 164.18 ? 493 THR B C   1 
ATOM   3805 O O   . THR B 2 493 ? 82.573  87.635  35.173 1.00 106.46 ? 493 THR B O   1 
ATOM   3806 C CB  . THR B 2 493 ? 79.576  89.123  35.052 1.00 191.38 ? 493 THR B CB  1 
ATOM   3807 O OG1 . THR B 2 493 ? 78.502  89.452  35.940 1.00 171.14 ? 493 THR B OG1 1 
ATOM   3808 C CG2 . THR B 2 493 ? 79.320  87.769  34.404 1.00 167.41 ? 493 THR B CG2 1 
ATOM   3809 N N   . VAL B 2 494 ? 82.521  89.570  34.031 1.00 197.06 ? 494 VAL B N   1 
ATOM   3810 C CA  . VAL B 2 494 ? 83.628  89.199  33.154 1.00 202.18 ? 494 VAL B CA  1 
ATOM   3811 C C   . VAL B 2 494 ? 84.933  89.071  33.938 1.00 185.00 ? 494 VAL B C   1 
ATOM   3812 O O   . VAL B 2 494 ? 85.751  88.232  33.575 1.00 162.08 ? 494 VAL B O   1 
ATOM   3813 C CB  . VAL B 2 494 ? 83.781  90.131  31.933 1.00 282.02 ? 494 VAL B CB  1 
ATOM   3814 C CG1 . VAL B 2 494 ? 82.512  90.152  31.097 1.00 294.14 ? 494 VAL B CG1 1 
ATOM   3815 C CG2 . VAL B 2 494 ? 84.194  91.553  32.280 1.00 297.11 ? 494 VAL B CG2 1 
ATOM   3816 N N   . LEU B 2 495 ? 85.137  89.859  35.000 1.00 180.35 ? 495 LEU B N   1 
ATOM   3817 C CA  . LEU B 2 495 ? 86.273  89.653  35.900 1.00 220.66 ? 495 LEU B CA  1 
ATOM   3818 C C   . LEU B 2 495 ? 86.240  88.236  36.497 1.00 216.02 ? 495 LEU B C   1 
ATOM   3819 O O   . LEU B 2 495 ? 87.255  87.538  36.469 1.00 204.51 ? 495 LEU B O   1 
ATOM   3820 C CB  . LEU B 2 495 ? 86.268  90.783  36.948 1.00 242.57 ? 495 LEU B CB  1 
ATOM   3821 C CG  . LEU B 2 495 ? 87.395  90.836  37.992 1.00 305.20 ? 495 LEU B CG  1 
ATOM   3822 C CD1 . LEU B 2 495 ? 87.160  89.871  39.152 1.00 340.74 ? 495 LEU B CD1 1 
ATOM   3823 C CD2 . LEU B 2 495 ? 88.772  90.582  37.379 1.00 345.09 ? 495 LEU B CD2 1 
ATOM   3824 N N   . CYS B 2 496 ? 85.085  87.783  37.007 1.00 208.36 ? 496 CYS B N   1 
ATOM   3825 C CA  . CYS B 2 496 ? 84.940  86.426  37.528 1.00 202.88 ? 496 CYS B CA  1 
ATOM   3826 C C   . CYS B 2 496 ? 85.171  85.358  36.448 1.00 200.86 ? 496 CYS B C   1 
ATOM   3827 O O   . CYS B 2 496 ? 85.791  84.322  36.728 1.00 143.05 ? 496 CYS B O   1 
ATOM   3828 C CB  . CYS B 2 496 ? 83.570  86.264  38.168 1.00 185.34 ? 496 CYS B CB  1 
ATOM   3829 S SG  . CYS B 2 496 ? 83.322  87.426  39.524 1.00 327.09 ? 496 CYS B SG  1 
ATOM   3830 N N   . GLN B 2 497 ? 84.694  85.598  35.211 1.00 177.91 ? 497 GLN B N   1 
ATOM   3831 C CA  . GLN B 2 497 ? 84.980  84.715  34.092 1.00 146.57 ? 497 GLN B CA  1 
ATOM   3832 C C   . GLN B 2 497 ? 86.480  84.592  33.880 1.00 156.72 ? 497 GLN B C   1 
ATOM   3833 O O   . GLN B 2 497 ? 86.930  83.480  33.668 1.00 135.61 ? 497 GLN B O   1 
ATOM   3834 C CB  . GLN B 2 497 ? 84.322  85.204  32.797 1.00 151.61 ? 497 GLN B CB  1 
ATOM   3835 C CG  . GLN B 2 497 ? 82.814  85.095  32.796 1.00 167.18 ? 497 GLN B CG  1 
ATOM   3836 C CD  . GLN B 2 497 ? 82.220  85.306  31.434 1.00 193.82 ? 497 GLN B CD  1 
ATOM   3837 O OE1 . GLN B 2 497 ? 81.705  86.376  31.139 1.00 261.73 ? 497 GLN B OE1 1 
ATOM   3838 N NE2 . GLN B 2 497 ? 82.288  84.293  30.581 1.00 190.44 ? 497 GLN B NE2 1 
ATOM   3839 N N   . LYS B 2 498 ? 87.240  85.706  33.923 1.00 158.20 ? 498 LYS B N   1 
ATOM   3840 C CA  . LYS B 2 498 ? 88.674  85.722  33.650 1.00 173.71 ? 498 LYS B CA  1 
ATOM   3841 C C   . LYS B 2 498 ? 89.446  84.936  34.706 1.00 179.23 ? 498 LYS B C   1 
ATOM   3842 O O   . LYS B 2 498 ? 90.362  84.190  34.333 1.00 177.77 ? 498 LYS B O   1 
ATOM   3843 C CB  . LYS B 2 498 ? 89.180  87.163  33.529 1.00 182.76 ? 498 LYS B CB  1 
ATOM   3844 C CG  . LYS B 2 498 ? 88.752  87.853  32.246 1.00 193.12 ? 498 LYS B CG  1 
ATOM   3845 C CD  . LYS B 2 498 ? 89.054  89.331  32.245 1.00 234.34 ? 498 LYS B CD  1 
ATOM   3846 C CE  . LYS B 2 498 ? 88.428  90.067  31.079 1.00 292.48 ? 498 LYS B CE  1 
ATOM   3847 N NZ  . LYS B 2 498 ? 88.913  91.468  30.977 1.00 304.46 ? 498 LYS B NZ  1 
ATOM   3848 N N   . LEU B 2 499 ? 89.076  85.085  35.994 1.00 168.15 ? 499 LEU B N   1 
ATOM   3849 C CA  . LEU B 2 499 ? 89.708  84.334  37.079 1.00 174.97 ? 499 LEU B CA  1 
ATOM   3850 C C   . LEU B 2 499 ? 89.492  82.827  36.905 1.00 185.43 ? 499 LEU B C   1 
ATOM   3851 O O   . LEU B 2 499 ? 90.465  82.065  36.813 1.00 180.06 ? 499 LEU B O   1 
ATOM   3852 C CB  . LEU B 2 499 ? 89.173  84.801  38.441 1.00 152.33 ? 499 LEU B CB  1 
ATOM   3853 C CG  . LEU B 2 499 ? 89.997  85.866  39.158 1.00 208.30 ? 499 LEU B CG  1 
ATOM   3854 C CD1 . LEU B 2 499 ? 90.049  87.186  38.384 1.00 230.55 ? 499 LEU B CD1 1 
ATOM   3855 C CD2 . LEU B 2 499 ? 89.432  86.096  40.552 1.00 220.65 ? 499 LEU B CD2 1 
ATOM   3856 N N   . MET B 2 500 ? 88.218  82.403  36.862 1.00 160.04 ? 500 MET B N   1 
ATOM   3857 C CA  . MET B 2 500 ? 87.857  80.992  36.931 1.00 180.04 ? 500 MET B CA  1 
ATOM   3858 C C   . MET B 2 500 ? 87.935  80.284  35.570 1.00 189.12 ? 500 MET B C   1 
ATOM   3859 O O   . MET B 2 500 ? 87.896  79.058  35.525 1.00 205.44 ? 500 MET B O   1 
ATOM   3860 C CB  . MET B 2 500 ? 86.442  80.874  37.505 1.00 221.40 ? 500 MET B CB  1 
ATOM   3861 C CG  . MET B 2 500 ? 86.336  81.400  38.937 1.00 193.64 ? 500 MET B CG  1 
ATOM   3862 S SD  . MET B 2 500 ? 84.619  81.405  39.559 1.00 134.92 ? 500 MET B SD  1 
ATOM   3863 C CE  . MET B 2 500 ? 84.669  82.715  40.792 1.00 214.38 ? 500 MET B CE  1 
ATOM   3864 N N   . GLN B 2 501 ? 88.032  81.044  34.465 1.00 186.71 ? 501 GLN B N   1 
ATOM   3865 C CA  . GLN B 2 501 ? 87.950  80.578  33.081 1.00 185.83 ? 501 GLN B CA  1 
ATOM   3866 C C   . GLN B 2 501 ? 86.634  79.836  32.859 1.00 166.31 ? 501 GLN B C   1 
ATOM   3867 O O   . GLN B 2 501 ? 86.621  78.631  32.674 1.00 140.45 ? 501 GLN B O   1 
ATOM   3868 C CB  . GLN B 2 501 ? 89.193  79.757  32.724 1.00 186.74 ? 501 GLN B CB  1 
ATOM   3869 C CG  . GLN B 2 501 ? 89.333  79.423  31.241 1.00 175.63 ? 501 GLN B CG  1 
ATOM   3870 C CD  . GLN B 2 501 ? 90.516  78.512  30.986 1.00 238.62 ? 501 GLN B CD  1 
ATOM   3871 O OE1 . GLN B 2 501 ? 91.398  78.354  31.833 1.00 212.90 ? 501 GLN B OE1 1 
ATOM   3872 N NE2 . GLN B 2 501 ? 90.546  77.893  29.811 1.00 290.12 ? 501 GLN B NE2 1 
ATOM   3873 N N   . VAL B 2 502 ? 85.512  80.573  32.887 1.00 166.01 ? 502 VAL B N   1 
ATOM   3874 C CA  . VAL B 2 502 ? 84.193  79.959  32.738 1.00 185.86 ? 502 VAL B CA  1 
ATOM   3875 C C   . VAL B 2 502 ? 83.365  80.646  31.648 1.00 202.45 ? 502 VAL B C   1 
ATOM   3876 O O   . VAL B 2 502 ? 83.435  81.860  31.439 1.00 182.34 ? 502 VAL B O   1 
ATOM   3877 C CB  . VAL B 2 502 ? 83.431  79.921  34.071 1.00 144.06 ? 502 VAL B CB  1 
ATOM   3878 C CG1 . VAL B 2 502 ? 84.167  79.034  35.068 1.00 157.91 ? 502 VAL B CG1 1 
ATOM   3879 C CG2 . VAL B 2 502 ? 83.207  81.307  34.662 1.00 143.50 ? 502 VAL B CG2 1 
ATOM   3880 N N   . VAL B 2 503 ? 82.558  79.826  30.955 1.00 183.15 ? 503 VAL B N   1 
ATOM   3881 C CA  . VAL B 2 503 ? 81.805  80.201  29.764 1.00 110.62 ? 503 VAL B CA  1 
ATOM   3882 C C   . VAL B 2 503 ? 80.344  79.878  30.030 1.00 117.79 ? 503 VAL B C   1 
ATOM   3883 O O   . VAL B 2 503 ? 80.035  78.909  30.756 1.00 227.62 ? 503 VAL B O   1 
ATOM   3884 C CB  . VAL B 2 503 ? 82.323  79.411  28.559 1.00 152.94 ? 503 VAL B CB  1 
ATOM   3885 C CG1 . VAL B 2 503 ? 83.800  79.669  28.360 1.00 190.51 ? 503 VAL B CG1 1 
ATOM   3886 C CG2 . VAL B 2 503 ? 82.107  77.897  28.644 1.00 181.73 ? 503 VAL B CG2 1 
ATOM   3887 N N   . PRO B 2 504 ? 79.385  80.660  29.515 1.00 104.70 ? 504 PRO B N   1 
ATOM   3888 C CA  . PRO B 2 504 ? 77.974  80.381  29.798 1.00 151.96 ? 504 PRO B CA  1 
ATOM   3889 C C   . PRO B 2 504 ? 77.491  79.103  29.098 1.00 179.53 ? 504 PRO B C   1 
ATOM   3890 O O   . PRO B 2 504 ? 78.080  78.649  28.119 1.00 151.62 ? 504 PRO B O   1 
ATOM   3891 C CB  . PRO B 2 504 ? 77.260  81.671  29.363 1.00 192.06 ? 504 PRO B CB  1 
ATOM   3892 C CG  . PRO B 2 504 ? 78.187  82.259  28.321 1.00 220.07 ? 504 PRO B CG  1 
ATOM   3893 C CD  . PRO B 2 504 ? 79.594  81.855  28.715 1.00 163.06 ? 504 PRO B CD  1 
ATOM   3894 N N   . GLN B 2 505 ? 76.405  78.538  29.651 1.00 176.15 ? 505 GLN B N   1 
ATOM   3895 C CA  . GLN B 2 505 ? 75.774  77.304  29.193 1.00 203.52 ? 505 GLN B CA  1 
ATOM   3896 C C   . GLN B 2 505 ? 75.130  77.511  27.817 1.00 260.36 ? 505 GLN B C   1 
ATOM   3897 O O   . GLN B 2 505 ? 74.567  78.580  27.559 1.00 307.95 ? 505 GLN B O   1 
ATOM   3898 C CB  . GLN B 2 505 ? 74.741  76.930  30.264 1.00 268.16 ? 505 GLN B CB  1 
ATOM   3899 C CG  . GLN B 2 505 ? 73.908  75.658  30.048 1.00 290.22 ? 505 GLN B CG  1 
ATOM   3900 C CD  . GLN B 2 505 ? 72.922  75.332  31.156 1.00 293.89 ? 505 GLN B CD  1 
ATOM   3901 O OE1 . GLN B 2 505 ? 72.178  74.356  31.087 1.00 218.76 ? 505 GLN B OE1 1 
ATOM   3902 N NE2 . GLN B 2 505 ? 72.902  76.137  32.207 1.00 338.44 ? 505 GLN B NE2 1 
ATOM   3903 N N   . GLU B 2 506 ? 75.184  76.490  26.933 1.00 266.42 ? 506 GLU B N   1 
ATOM   3904 C CA  . GLU B 2 506 ? 74.688  76.605  25.559 1.00 288.58 ? 506 GLU B CA  1 
ATOM   3905 C C   . GLU B 2 506 ? 73.685  75.499  25.186 1.00 284.40 ? 506 GLU B C   1 
ATOM   3906 O O   . GLU B 2 506 ? 73.847  74.344  25.583 1.00 341.44 ? 506 GLU B O   1 
ATOM   3907 C CB  . GLU B 2 506 ? 75.850  76.594  24.559 1.00 298.91 ? 506 GLU B CB  1 
ATOM   3908 C CG  . GLU B 2 506 ? 76.868  77.722  24.729 1.00 345.56 ? 506 GLU B CG  1 
ATOM   3909 C CD  . GLU B 2 506 ? 76.401  79.139  24.415 1.00 393.31 ? 506 GLU B CD  1 
ATOM   3910 O OE1 . GLU B 2 506 ? 75.187  79.363  24.237 1.00 438.13 ? 506 GLU B OE1 1 
ATOM   3911 O OE2 . GLU B 2 506 ? 77.270  80.037  24.334 1.00 409.85 ? 506 GLU B OE2 1 
ATOM   3912 N N   . THR B 2 507 ? 72.649  75.889  24.407 1.00 305.22 ? 507 THR B N   1 
ATOM   3913 C CA  . THR B 2 507 ? 71.681  75.015  23.730 1.00 338.70 ? 507 THR B CA  1 
ATOM   3914 C C   . THR B 2 507 ? 71.247  73.860  24.657 1.00 285.24 ? 507 THR B C   1 
ATOM   3915 O O   . THR B 2 507 ? 71.619  72.676  24.410 1.00 210.27 ? 507 THR B O   1 
ATOM   3916 C CB  . THR B 2 507 ? 72.202  74.576  22.342 1.00 371.03 ? 507 THR B CB  1 
ATOM   3917 O OG1 . THR B 2 507 ? 72.595  75.725  21.591 1.00 320.54 ? 507 THR B OG1 1 
ATOM   3918 C CG2 . THR B 2 507 ? 71.185  73.838  21.493 1.00 380.00 ? 507 THR B CG2 1 
HETATM 3919 C C1  . CLR C 3 .   ? 97.314  64.186  67.036 1.00 180.17 ? 601 CLR B C1  1 
HETATM 3920 C C2  . CLR C 3 .   ? 98.300  63.640  68.073 1.00 228.03 ? 601 CLR B C2  1 
HETATM 3921 C C3  . CLR C 3 .   ? 98.045  62.183  68.372 1.00 251.63 ? 601 CLR B C3  1 
HETATM 3922 C C4  . CLR C 3 .   ? 98.110  61.371  67.086 1.00 265.05 ? 601 CLR B C4  1 
HETATM 3923 C C5  . CLR C 3 .   ? 97.177  61.909  66.010 1.00 207.04 ? 601 CLR B C5  1 
HETATM 3924 C C6  . CLR C 3 .   ? 96.309  61.107  65.405 1.00 217.97 ? 601 CLR B C6  1 
HETATM 3925 C C7  . CLR C 3 .   ? 95.353  61.513  64.320 1.00 262.30 ? 601 CLR B C7  1 
HETATM 3926 C C8  . CLR C 3 .   ? 95.604  62.918  63.760 1.00 225.85 ? 601 CLR B C8  1 
HETATM 3927 C C9  . CLR C 3 .   ? 96.027  63.884  64.893 1.00 170.87 ? 601 CLR B C9  1 
HETATM 3928 C C10 . CLR C 3 .   ? 97.278  63.406  65.693 1.00 183.93 ? 601 CLR B C10 1 
HETATM 3929 C C11 . CLR C 3 .   ? 96.144  65.334  64.385 1.00 189.79 ? 601 CLR B C11 1 
HETATM 3930 C C12 . CLR C 3 .   ? 94.906  65.804  63.614 1.00 185.74 ? 601 CLR B C12 1 
HETATM 3931 C C13 . CLR C 3 .   ? 94.524  64.871  62.453 1.00 185.69 ? 601 CLR B C13 1 
HETATM 3932 C C14 . CLR C 3 .   ? 94.346  63.472  63.081 1.00 218.99 ? 601 CLR B C14 1 
HETATM 3933 C C15 . CLR C 3 .   ? 93.608  62.651  62.019 1.00 204.59 ? 601 CLR B C15 1 
HETATM 3934 C C16 . CLR C 3 .   ? 92.754  63.678  61.256 1.00 185.63 ? 601 CLR B C16 1 
HETATM 3935 C C17 . CLR C 3 .   ? 93.105  65.085  61.826 1.00 195.39 ? 601 CLR B C17 1 
HETATM 3936 C C18 . CLR C 3 .   ? 95.610  64.891  61.351 1.00 202.67 ? 601 CLR B C18 1 
HETATM 3937 C C19 . CLR C 3 .   ? 98.585  63.647  64.903 1.00 239.87 ? 601 CLR B C19 1 
HETATM 3938 C C20 . CLR C 3 .   ? 92.874  66.243  60.822 1.00 196.65 ? 601 CLR B C20 1 
HETATM 3939 C C21 . CLR C 3 .   ? 93.013  67.620  61.473 1.00 175.38 ? 601 CLR B C21 1 
HETATM 3940 C C22 . CLR C 3 .   ? 91.511  66.179  60.108 1.00 150.14 ? 601 CLR B C22 1 
HETATM 3941 C C23 . CLR C 3 .   ? 91.492  66.574  58.641 1.00 156.39 ? 601 CLR B C23 1 
HETATM 3942 C C24 . CLR C 3 .   ? 90.323  65.898  57.922 1.00 225.59 ? 601 CLR B C24 1 
HETATM 3943 C C25 . CLR C 3 .   ? 90.199  66.019  56.420 1.00 197.29 ? 601 CLR B C25 1 
HETATM 3944 C C26 . CLR C 3 .   ? 91.355  65.291  55.739 1.00 206.01 ? 601 CLR B C26 1 
HETATM 3945 C C27 . CLR C 3 .   ? 90.077  67.477  56.015 1.00 146.24 ? 601 CLR B C27 1 
HETATM 3946 O O1  . CLR C 3 .   ? 98.996  61.717  69.346 1.00 234.74 ? 601 CLR B O1  1 
HETATM 3947 C C1  . CLR D 3 .   ? 88.338  80.104  61.572 1.00 204.89 ? 602 CLR B C1  1 
HETATM 3948 C C2  . CLR D 3 .   ? 88.062  79.719  63.038 1.00 221.13 ? 602 CLR B C2  1 
HETATM 3949 C C3  . CLR D 3 .   ? 86.822  80.408  63.578 1.00 248.43 ? 602 CLR B C3  1 
HETATM 3950 C C4  . CLR D 3 .   ? 85.629  80.088  62.705 1.00 222.12 ? 602 CLR B C4  1 
HETATM 3951 C C5  . CLR D 3 .   ? 85.867  80.358  61.227 1.00 171.47 ? 602 CLR B C5  1 
HETATM 3952 C C6  . CLR D 3 .   ? 84.936  80.982  60.539 1.00 157.52 ? 602 CLR B C6  1 
HETATM 3953 C C7  . CLR D 3 .   ? 84.942  81.250  59.075 1.00 194.58 ? 602 CLR B C7  1 
HETATM 3954 C C8  . CLR D 3 .   ? 86.088  80.575  58.341 1.00 170.30 ? 602 CLR B C8  1 
HETATM 3955 C C9  . CLR D 3 .   ? 87.368  80.572  59.209 1.00 180.48 ? 602 CLR B C9  1 
HETATM 3956 C C10 . CLR D 3 .   ? 87.163  79.843  60.585 1.00 175.28 ? 602 CLR B C10 1 
HETATM 3957 C C11 . CLR D 3 .   ? 88.586  80.119  58.368 1.00 218.96 ? 602 CLR B C11 1 
HETATM 3958 C C12 . CLR D 3 .   ? 88.733  80.777  56.976 1.00 205.71 ? 602 CLR B C12 1 
HETATM 3959 C C13 . CLR D 3 .   ? 87.440  80.762  56.143 1.00 224.34 ? 602 CLR B C13 1 
HETATM 3960 C C14 . CLR D 3 .   ? 86.329  81.349  57.051 1.00 217.56 ? 602 CLR B C14 1 
HETATM 3961 C C15 . CLR D 3 .   ? 85.130  81.695  56.148 1.00 205.02 ? 602 CLR B C15 1 
HETATM 3962 C C16 . CLR D 3 .   ? 85.770  81.920  54.760 1.00 304.84 ? 602 CLR B C16 1 
HETATM 3963 C C17 . CLR D 3 .   ? 87.314  81.796  54.970 1.00 332.61 ? 602 CLR B C17 1 
HETATM 3964 C C18 . CLR D 3 .   ? 87.140  79.322  55.677 1.00 202.63 ? 602 CLR B C18 1 
HETATM 3965 C C19 . CLR D 3 .   ? 87.005  78.318  60.392 1.00 212.19 ? 602 CLR B C19 1 
HETATM 3966 C C20 . CLR D 3 .   ? 88.119  81.650  53.650 1.00 401.76 ? 602 CLR B C20 1 
HETATM 3967 C C21 . CLR D 3 .   ? 88.307  83.008  52.968 1.00 450.35 ? 602 CLR B C21 1 
HETATM 3968 C C22 . CLR D 3 .   ? 87.517  80.651  52.640 1.00 381.50 ? 602 CLR B C22 1 
HETATM 3969 C C23 . CLR D 3 .   ? 88.526  80.018  51.697 1.00 353.04 ? 602 CLR B C23 1 
HETATM 3970 C C24 . CLR D 3 .   ? 89.514  79.057  52.388 1.00 310.84 ? 602 CLR B C24 1 
HETATM 3971 C C25 . CLR D 3 .   ? 90.971  79.539  52.545 1.00 244.17 ? 602 CLR B C25 1 
HETATM 3972 C C26 . CLR D 3 .   ? 91.642  79.794  51.204 1.00 295.61 ? 602 CLR B C26 1 
HETATM 3973 C C27 . CLR D 3 .   ? 91.805  78.538  53.321 1.00 212.97 ? 602 CLR B C27 1 
HETATM 3974 O O1  . CLR D 3 .   ? 86.477  80.010  64.910 1.00 246.02 ? 602 CLR B O1  1 
HETATM 3975 C C1  . LBN E 4 .   ? 91.525  76.918  37.438 1.00 223.23 ? 603 LBN B C1  1 
HETATM 3976 N N1  . LBN E 4 .   ? 95.374  71.534  36.547 1.00 454.06 ? 603 LBN B N1  1 
HETATM 3977 P P1  . LBN E 4 .   ? 92.721  75.863  35.326 1.00 279.51 ? 603 LBN B P1  1 
HETATM 3978 C C2  . LBN E 4 .   ? 90.132  76.883  38.030 1.00 253.44 ? 603 LBN B C2  1 
HETATM 3979 C C3  . LBN E 4 .   ? 89.434  75.540  37.875 1.00 247.58 ? 603 LBN B C3  1 
HETATM 3980 C C4  . LBN E 4 .   ? 86.260  78.906  47.802 1.00 103.01 ? 603 LBN B C4  1 
HETATM 3981 C C6  . LBN E 4 .   ? 94.290  72.569  36.809 1.00 423.77 ? 603 LBN B C6  1 
HETATM 3982 O O1  . LBN E 4 .   ? 91.445  76.523  36.038 1.00 229.90 ? 603 LBN B O1  1 
HETATM 3983 C C9  . LBN E 4 .   ? 94.055  73.636  35.765 1.00 372.36 ? 603 LBN B C9  1 
HETATM 3984 O O2  . LBN E 4 .   ? 92.977  74.526  36.176 1.00 310.62 ? 603 LBN B O2  1 
HETATM 3985 C C12 . LBN E 4 .   ? 95.471  70.636  37.738 1.00 455.62 ? 603 LBN B C12 1 
HETATM 3986 O O3  . LBN E 4 .   ? 93.883  76.796  35.545 1.00 312.85 ? 603 LBN B O3  1 
HETATM 3987 C C15 . LBN E 4 .   ? 96.705  72.183  36.333 1.00 463.16 ? 603 LBN B C15 1 
HETATM 3988 O O4  . LBN E 4 .   ? 92.357  75.439  33.929 1.00 269.70 ? 603 LBN B O4  1 
HETATM 3989 C C18 . LBN E 4 .   ? 95.037  70.704  35.353 1.00 453.47 ? 603 LBN B C18 1 
HETATM 3990 C C25 . LBN E 4 .   ? 89.756  74.218  39.842 1.00 266.05 ? 603 LBN B C25 1 
HETATM 3991 O O5  . LBN E 4 .   ? 88.964  75.051  39.162 1.00 182.56 ? 603 LBN B O5  1 
HETATM 3992 C C26 . LBN E 4 .   ? 88.999  73.594  40.977 1.00 206.24 ? 603 LBN B C26 1 
HETATM 3993 O O6  . LBN E 4 .   ? 90.918  74.061  39.568 1.00 321.18 ? 603 LBN B O6  1 
HETATM 3994 C C27 . LBN E 4 .   ? 89.582  73.926  42.306 1.00 184.40 ? 603 LBN B C27 1 
HETATM 3995 C C28 . LBN E 4 .   ? 89.321  75.408  42.622 1.00 189.91 ? 603 LBN B C28 1 
HETATM 3996 C C29 . LBN E 4 .   ? 89.213  75.769  44.100 1.00 187.79 ? 603 LBN B C29 1 
HETATM 3997 C C30 . LBN E 4 .   ? 87.915  75.394  44.764 1.00 177.11 ? 603 LBN B C30 1 
HETATM 3998 C C31 . LBN E 4 .   ? 87.769  75.836  46.192 1.00 166.80 ? 603 LBN B C31 1 
HETATM 3999 C C32 . LBN E 4 .   ? 87.883  77.371  46.432 1.00 165.58 ? 603 LBN B C32 1 
HETATM 4000 C C33 . LBN E 4 .   ? 87.402  77.919  47.817 1.00 160.27 ? 603 LBN B C33 1 
HETATM 4001 C C34 . LBN E 4 .   ? 90.379  78.551  39.771 1.00 227.61 ? 603 LBN B C34 1 
HETATM 4002 O O7  . LBN E 4 .   ? 90.237  77.259  39.438 1.00 276.54 ? 603 LBN B O7  1 
HETATM 4003 C C35 . LBN E 4 .   ? 90.967  78.771  41.129 1.00 173.70 ? 603 LBN B C35 1 
HETATM 4004 O O8  . LBN E 4 .   ? 90.070  79.455  39.050 1.00 216.82 ? 603 LBN B O8  1 
HETATM 4005 C C36 . LBN E 4 .   ? 89.992  79.484  41.993 1.00 179.50 ? 603 LBN B C36 1 
HETATM 4006 C C37 . LBN E 4 .   ? 90.581  79.902  43.309 1.00 209.86 ? 603 LBN B C37 1 
HETATM 4007 C C38 . LBN E 4 .   ? 89.551  80.482  44.273 1.00 221.93 ? 603 LBN B C38 1 
HETATM 4008 C C39 . LBN E 4 .   ? 89.136  81.901  44.007 1.00 206.85 ? 603 LBN B C39 1 
HETATM 4009 C C40 . LBN E 4 .   ? 87.839  82.055  43.229 1.00 196.26 ? 603 LBN B C40 1 
HETATM 4010 C C41 . LBN E 4 .   ? 87.345  83.470  43.074 1.00 217.23 ? 603 LBN B C41 1 
HETATM 4011 C C42 . LBN E 4 .   ? 86.421  83.937  44.171 1.00 204.13 ? 603 LBN B C42 1 
HETATM 4012 N N1  . VU0 F 5 .   ? 70.070  63.558  55.633 1.00 180.74 ? 604 VU0 B N1  1 
HETATM 4013 C C1  . VU0 F 5 .   ? 70.994  64.626  56.160 1.00 127.59 ? 604 VU0 B C1  1 
HETATM 4014 C C2  . VU0 F 5 .   ? 70.251  65.750  56.947 1.00 106.48 ? 604 VU0 B C2  1 
HETATM 4015 C C3  . VU0 F 5 .   ? 70.476  67.001  56.090 1.00 115.49 ? 604 VU0 B C3  1 
HETATM 4016 C C4  . VU0 F 5 .   ? 69.744  66.854  54.747 1.00 182.86 ? 604 VU0 B C4  1 
HETATM 4017 C C5  . VU0 F 5 .   ? 70.736  65.962  53.925 1.00 218.73 ? 604 VU0 B C5  1 
HETATM 4018 C C6  . VU0 F 5 .   ? 71.717  65.469  55.001 1.00 139.29 ? 604 VU0 B C6  1 
HETATM 4019 C C7  . VU0 F 5 .   ? 71.951  66.816  55.657 1.00 139.51 ? 604 VU0 B C7  1 
HETATM 4020 C C8  . VU0 F 5 .   ? 71.928  63.853  57.066 1.00 107.01 ? 604 VU0 B C8  1 
HETATM 4021 O O1  . VU0 F 5 .   ? 71.495  63.192  57.984 1.00 135.51 ? 604 VU0 B O1  1 
HETATM 4022 O O2  . VU0 F 5 .   ? 73.098  63.912  56.865 1.00 153.13 ? 604 VU0 B O2  1 
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